diff --git a/.github/workflows/build.yaml b/.github/workflows/build.yaml
index 892d28ff..3328305c 100644
--- a/.github/workflows/build.yaml
+++ b/.github/workflows/build.yaml
@@ -33,7 +33,7 @@ jobs:
         uses: actions/checkout@v3
         # See: https://github.com/marketplace/actions/setup-miniconda
       - name: Setup miniconda
-        uses: conda-incubator/setup-miniconda@v2
+        uses: conda-incubator/setup-miniconda@v3
         with:
           auto-update-conda: true
           miniforge-variant: Mambaforge
@@ -48,15 +48,18 @@ jobs:
         run: conda install dssp -c salilab
       - name: Install mmseqs
         run: mamba install -c conda-forge -c bioconda mmseqs2
-      - name: Install PyTorch
-        #run: mamba install -c pytorch pytorch==${{matrix.torch}} cpuonly
-        run: pip install torch==${{matrix.torch}}+cpu -f https://download.pytorch.org/whl/torch_stable.html
+      - name: Install PyTorch (1.13.0)
+        if: matrix.torch == '1.13.0'
+        run: pip install torch==${{matrix.torch}}+cpu --extra-index-url https://download.pytorch.org/whl/cpu
+      - name: Install PyTorch (2.0+)
+        if: matrix.torch != '1.13.0'
+        run: pip install torch==${{matrix.torch}} -f https://download.pytorch.org/whl/cpu
       - name: Install PyG
         #run: mamba install -c pyg pyg
         run: pip install torch_geometric
       - name: Install torch-cluster
         #run: mamba install pytorch-cluster -c pyg
-        run: pip install pyg_lib torch_scatter torch_sparse torch_cluster torch_spline_conv -f https://data.pyg.org/whl/torch-${{matrix.torch}}+cpu.html
+        run: pip install torch_scatter torch_sparse torch_cluster torch_spline_conv -f https://data.pyg.org/whl/torch-${{matrix.torch}}+cpu.html
       - name: Install BLAST
         run: sudo apt install ncbi-blast+
       - name: Install Graphein
@@ -70,4 +73,4 @@ jobs:
       - name: Run unit tests and generate coverage report
         run: pytest .
       - name: Test notebook execution
-        run: pytest --nbval-lax notebooks/ --current-env --ignore-glob="notebooks/dataloader_tutorial.ipynb" --ignore-glob="notebooks/datasets_and_dataloaders.ipynb" --ignore-glob="notebooks/foldcomp.ipynb"
+        run: pytest --nbval-lax notebooks/ --current-env --ignore-glob="notebooks/dataloader_tutorial.ipynb" --ignore-glob="notebooks/datasets_and_dataloaders.ipynb" --ignore-glob="notebooks/foldcomp.ipynb" --ignore-glob="notebooks/grn_tutorial.ipynb"
diff --git a/.github/workflows/minimal__install.yaml b/.github/workflows/minimal__install.yaml
index 2d1f96bd..f18aca59 100644
--- a/.github/workflows/minimal__install.yaml
+++ b/.github/workflows/minimal__install.yaml
@@ -34,7 +34,7 @@ jobs:
         uses: actions/checkout@v3
         # See: https://github.com/marketplace/actions/setup-miniconda
       - name: Setup miniconda
-        uses: conda-incubator/setup-miniconda@v2
+        uses: conda-incubator/setup-miniconda@v3
         with:
           auto-update-conda: true
           miniforge-variant: Mambaforge
@@ -50,4 +50,4 @@ jobs:
       - name: Run unit tests and generate coverage report
         run: pytest . --ignore-glob="tests/protein/tensor" --ignore="tests/ml/test_conversion.py" --ignore="tests/ml/test_torch_geometric_dataset.py"
       - name: Test notebook execution
-        run: pytest --nbval-lax notebooks/ --current-env --ignore-glob="notebooks/dataloader_tutorial.ipynb" --ignore-glob="notebooks/higher_order_graphs.ipynb" --ignore-glob="notebooks/protein_graph_analytics.ipynb" --ignore-glob="notebooks/subgraphing_tutorial.ipynb" --ignore-glob="notebooks/splitting_a_dataset.ipynb" --ignore-glob="notebooks/protein_tensors.ipynb" --ignore-glob="notebooks/datasets_and_dataloaders.ipynb" --ignore-glob="notebooks/foldcomp.ipynb" --ignore-glob="notebooks/creating_datasets_from_the_pdb.ipynb"
+        run: pytest --nbval-lax notebooks/ --current-env --ignore-glob="notebooks/dataloader_tutorial.ipynb" --ignore-glob="notebooks/higher_order_graphs.ipynb" --ignore-glob="notebooks/protein_graph_analytics.ipynb" --ignore-glob="notebooks/subgraphing_tutorial.ipynb" --ignore-glob="notebooks/splitting_a_dataset.ipynb" --ignore-glob="notebooks/protein_tensors.ipynb" --ignore-glob="notebooks/datasets_and_dataloaders.ipynb" --ignore-glob="notebooks/foldcomp.ipynb" --ignore-glob="notebooks/creating_datasets_from_the_pdb.ipynb" --ignore-glob="notebooks/grn_tutorial.ipynb"
diff --git a/.requirements/base.in b/.requirements/base.in
index 8369bfd7..b25fd397 100644
--- a/.requirements/base.in
+++ b/.requirements/base.in
@@ -1,5 +1,5 @@
 pandas<2.0.0
-biopandas>=0.5.0.dev0
+biopandas>=0.5.1
 biopython
 bioservices>=1.10.0
 deepdiff
diff --git a/CHANGELOG.md b/CHANGELOG.md
index d0baa19e..37d7033c 100644
--- a/CHANGELOG.md
+++ b/CHANGELOG.md
@@ -8,6 +8,7 @@
 * Fix cluster file loading bug in `pdb_data.py` [#396](https://github.com/a-r-j/graphein/pull/396)
 
 #### Misc
+* set logging to false by default and added mmcif support [#402](https://github.com/a-r-j/graphein/pull/402)
 * add metadata options for uniprot, ecnumber and CATH code to pdb manager [#398](https://github.com/a-r-j/graphein/pull/398)
 * bumped logging level down from `INFO` to `DEBUG` at several places to reduced output length [#391](https://github.com/a-r-j/graphein/pull/391)
 * exposed `fill_value` and `bfactor` option to `protein_to_pyg` function. [#385](https://github.com/a-r-j/graphein/pull/385) and [#388](https://github.com/a-r-j/graphein/pull/388)
diff --git a/graphein/__init__.py b/graphein/__init__.py
index 0d2a5da5..1a7db64c 100644
--- a/graphein/__init__.py
+++ b/graphein/__init__.py
@@ -21,6 +21,8 @@
     ]
 )
 
+logger.disable("graphein")
+
 
 def verbose(enabled: bool = False):
     """Enable/Disable logging.
diff --git a/graphein/grn/parse_regnetwork.py b/graphein/grn/parse_regnetwork.py
index 0d7e5787..545fea5f 100644
--- a/graphein/grn/parse_regnetwork.py
+++ b/graphein/grn/parse_regnetwork.py
@@ -18,9 +18,12 @@
 import wget
 from loguru import logger as log
 
-from graphein.utils.utils import filter_dataframe, ping
+from graphein.utils.utils import deprecated, filter_dataframe, ping
 
 
+@deprecated(
+    "RegNetwork appears to be down. This warning will be removed in a future release if the service is restored."
+)
 def _download_RegNetwork(
     root_dir: Optional[Path] = None, network_type: str = "human"
 ) -> str:
@@ -86,6 +89,9 @@ def _download_RegNetwork(
     return file
 
 
+@deprecated(
+    "RegNetwork appears to be down. This warning will be removed in a future release if the service is restored."
+)
 def _download_RegNetwork_regtypes(root_dir: Optional[Path] = None) -> str:
     """
     Downloads RegNetwork regulatory interactions types to the root directory.
@@ -124,6 +130,9 @@ def _download_RegNetwork_regtypes(root_dir: Optional[Path] = None) -> str:
     return file
 
 
+@deprecated(
+    "RegNetwork appears to be down. This warning will be removed in a future release if the service is restored."
+)
 @functools.lru_cache()
 def load_RegNetwork_interactions(
     root_dir: Optional[Path] = None,
@@ -144,6 +153,9 @@ def load_RegNetwork_interactions(
     )
 
 
+@deprecated(
+    "RegNetwork appears to be down. This warning will be removed in a future release if the service is restored."
+)
 @functools.lru_cache()
 def load_RegNetwork_regulation_types(
     root_dir: Optional[Path] = None,
@@ -168,6 +180,9 @@ def load_RegNetwork_regulation_types(
     )
 
 
+@deprecated(
+    "RegNetwork appears to be down. This warning will be removed in a future release if the service is restored."
+)
 def parse_RegNetwork(
     gene_list: List[str], root_dir: Optional[Path] = None
 ) -> pd.DataFrame:
@@ -244,6 +259,9 @@ def standardise_RegNetwork(df: pd.DataFrame) -> pd.DataFrame:
     return df
 
 
+@deprecated(
+    "RegNetwork appears to be down. This warning will be removed in a future release if the service is restored."
+)
 def RegNetwork_df(
     gene_list: List[str],
     root_dir: Optional[Path] = None,
diff --git a/graphein/ml/clustering.py b/graphein/ml/clustering.py
index b6d4a49b..e0364e33 100644
--- a/graphein/ml/clustering.py
+++ b/graphein/ml/clustering.py
@@ -85,7 +85,7 @@ def get_seq_records(
             "Alphabet given. Only checking for terminating *!\n"
         )
         check_sequences = False
-    with open(filename, "rU") as handle:
+    with open(filename, "r") as handle:
         records = list(SeqIO.parse(handle, file_format, alphabet=alphabet))
     del handle
     if check_sequences:
diff --git a/graphein/ml/datasets/foldcomp_dataset.py b/graphein/ml/datasets/foldcomp_dataset.py
index 76209add..bfed70e2 100644
--- a/graphein/ml/datasets/foldcomp_dataset.py
+++ b/graphein/ml/datasets/foldcomp_dataset.py
@@ -236,10 +236,6 @@ def download(self):
                 asyncio.run(_)
             os.chdir(curr_dir)
             log.info("Download complete.")
-            # log.info("Moving files to raw directory...")
-
-            # for f in self._database_files:
-            #    shutil.move(f, self.root)
         else:
             log.info(f"FoldComp database already downloaded: {self.root}.")
 
diff --git a/graphein/ml/datasets/pdb_data.py b/graphein/ml/datasets/pdb_data.py
index 6dbb4fc4..acd6716a 100644
--- a/graphein/ml/datasets/pdb_data.py
+++ b/graphein/ml/datasets/pdb_data.py
@@ -120,6 +120,7 @@ def __init__(
         ).name
 
         self.list_columns = ["ligands"]
+        self.labels = labels
 
         # Data
         self.download_metadata()
@@ -165,9 +166,10 @@ def download_metadata(self):
         self._download_entry_metadata()
         self._download_exp_type()
         self._download_pdb_availability()
-        self._download_pdb_chain_cath_uniprot_map()
-        self._download_cath_id_cath_code_map()
-        self._download_pdb_chain_ec_number_map()
+        if self.labels:
+            self._download_pdb_chain_cath_uniprot_map()
+            self._download_cath_id_cath_code_map()
+            self._download_pdb_chain_ec_number_map()
 
     def get_unavailable_pdb_files(
         self, splits: Optional[List[str]] = None
@@ -643,15 +645,12 @@ def _parse_cath_code(self) -> Dict[str, str]:
         with gzip.open(
             self.root_dir / self.cath_id_cath_code_filename, "rt"
         ) as f:
-            print(f)
             for line in f:
-                print(line)
                 try:
                     cath_id, cath_version, cath_code, cath_segment = (
                         line.strip().split()
                     )
                     cath_mapping[cath_id] = cath_code
-                    print(cath_id, cath_code)
                 except ValueError:
                     continue
         return cath_mapping
diff --git a/graphein/protein/graphs.py b/graphein/protein/graphs.py
index dfe237f7..2417c004 100644
--- a/graphein/protein/graphs.py
+++ b/graphein/protein/graphs.py
@@ -18,6 +18,7 @@
 import networkx as nx
 import numpy as np
 import pandas as pd
+from biopandas.mmcif import PandasMmcif
 from biopandas.mmtf import PandasMmtf
 from biopandas.pdb import PandasPdb
 from loguru import logger as log
@@ -111,9 +112,16 @@ def read_pdb_to_dataframe(
             atomic_df = PandasPdb().read_pdb(path)
         elif path.endswith(".mmtf") or path.endswith(".mmtf.gz"):
             atomic_df = PandasMmtf().read_mmtf(path)
+        elif (
+            path.endswith(".cif")
+            or path.endswith(".cif.gz")
+            or path.endswith(".mmcif")
+            or path.endswith(".mmcif.gz")
+        ):
+            atomic_df = PandasMmcif().read_mmcif(path)
         else:
             raise ValueError(
-                f"File {path} must be either .pdb(.gz), .mmtf(.gz) or .ent, not {path.split('.')[-1]}"
+                f"File {path} must be either .pdb(.gz), .mmtf(.gz), .(mm)cif(.gz) or .ent, not {path.split('.')[-1]}"
             )
     elif uniprot_id is not None:
         atomic_df = PandasPdb().fetch_pdb(
@@ -121,11 +129,11 @@ def read_pdb_to_dataframe(
         )
     else:
         atomic_df = PandasPdb().fetch_pdb(pdb_code)
-
     atomic_df = atomic_df.get_model(model_index)
     if len(atomic_df.df["ATOM"]) == 0:
         raise ValueError(f"No model found for index: {model_index}")
-
+    if isinstance(atomic_df, PandasMmcif):
+        atomic_df = atomic_df.convert_to_pandas_pdb()
     return pd.concat([atomic_df.df["ATOM"], atomic_df.df["HETATM"]])
 
 
diff --git a/graphein/protein/tensor/io.py b/graphein/protein/tensor/io.py
index 58089158..e938130a 100644
--- a/graphein/protein/tensor/io.py
+++ b/graphein/protein/tensor/io.py
@@ -49,7 +49,7 @@
         conda_channel="pyg",
         pip_install=True,
     )
-    log.debug(message)
+    log.warning(message)
 
 try:
     import torch
@@ -60,7 +60,7 @@
         conda_channel="pytorch",
         pip_install=True,
     )
-    log.debug(message)
+    log.warning(message)
 
 
 def get_protein_length(df: pd.DataFrame, insertions: bool = True) -> int:
@@ -246,7 +246,9 @@ def protein_to_pyg(
 
     out = Data(
         coords=protein_df_to_tensor(
-            df, atoms_to_keep=atom_types, fill_value=fill_value_coords
+            df,
+            atoms_to_keep=atom_types,
+            fill_value=fill_value_coords,
         ),
         residues=get_sequence(
             df,
@@ -259,6 +261,7 @@ def protein_to_pyg(
         residue_type=residue_type_tensor(df),
         chains=protein_df_to_chain_tensor(df),
     )
+
     if store_het:
         out.hetatms = [het_coords]
 
@@ -360,6 +363,7 @@ def protein_df_to_tensor(
     positions[residue_indices, atom_indices] = torch.tensor(
         df[["x_coord", "y_coord", "z_coord"]].values
     ).float()
+
     return positions
 
 
diff --git a/graphein/protein/utils.py b/graphein/protein/utils.py
index c16669f1..490a9e39 100644
--- a/graphein/protein/utils.py
+++ b/graphein/protein/utils.py
@@ -11,7 +11,7 @@
 from functools import lru_cache, partial
 from multiprocessing import Pool
 from pathlib import Path
-from typing import Any, Dict, List, Optional, Tuple, Type, Union
+from typing import Any, Dict, List, Literal, Optional, Tuple, Type, Union
 from urllib.error import HTTPError
 from urllib.request import urlopen
 
@@ -96,7 +96,7 @@ def read_fasta(file_path: str) -> Dict[str, str]:
 def download_pdb_multiprocessing(
     pdb_codes: List[str],
     out_dir: Union[str, Path],  # type: ignore
-    format: str = "pdb",
+    format: Literal["pdb", "mmtf", "mmcif", "cif", "bcif"] = "pdb",
     overwrite: bool = False,
     strict: bool = False,
     max_workers: int = 16,
@@ -108,7 +108,7 @@ def download_pdb_multiprocessing(
     :type pdb_codes: List[str]
     :param out_dir: Path to directory to download PDB structures to.
     :type out_dir: Union[str, Path]
-    :param format: Filetype to download. ``pdb``, ``mmtf``, ``mmcif`` or ``bcif``.
+    :param format: Filetype to download. ``pdb``, ``mmtf``, ``mmcif``/``cif`` or ``bcif``.
     :type format: str
     :param overwrite: Whether to overwrite existing files, defaults to
         ``False``.
@@ -146,7 +146,7 @@ def download_pdb_multiprocessing(
 def download_pdb(
     pdb_code: str,
     out_dir: Optional[Union[str, Path]] = None,
-    format: str = "pdb",
+    format: Literal["pdb", "mmtf", "mmcif", "cif", "bcif"] = "pdb",
     check_obsolete: bool = False,
     overwrite: bool = False,
     strict: bool = True,
@@ -162,7 +162,7 @@ def download_pdb(
     :param out_dir: Path to directory to download PDB structure to. If ``None``,
         will download to a temporary directory.
     :type out_dir: Optional[Union[str, Path]]
-    :param format: Filetype to download. ``pdb``, ``mmtf``, ``mmcif`` or ``bcif``.
+    :param format: Filetype to download. ``pdb``, ``mmtf``, ``mmcif``/``cif`` or ``bcif``.
     :type format: str
     :param check_obsolete: Whether to check for obsolete PDB codes,
         defaults to ``False``. If an obsolete PDB code is found, the updated PDB
@@ -183,7 +183,7 @@ def download_pdb(
     elif format == "mmtf":
         BASE_URL = "https://mmtf.rcsb.org/v1.0/full/"
         extension = ".mmtf.gz"
-    elif format == "mmcif":
+    elif format == "cif" or format == "mmcif":
         BASE_URL = "https://files.rcsb.org/download/"
         extension = ".cif.gz"
     elif format == "bcif":
@@ -191,7 +191,7 @@ def download_pdb(
         extension = ".bcif.gz"
     else:
         raise ValueError(
-            f"Invalid format: {format}. Must be 'pdb', 'mmtf', 'mmcif' or 'bcif'."
+            f"Invalid format: {format}. Must be 'pdb', 'mmtf', '(mm)cif' or 'bcif'."
         )
 
     # Make output directory if it doesn't exist or set it to tempdir if None
diff --git a/graphein/utils/utils.py b/graphein/utils/utils.py
index 4234de2e..700eda56 100644
--- a/graphein/utils/utils.py
+++ b/graphein/utils/utils.py
@@ -7,11 +7,13 @@
 # Code Repository: https://github.com/a-r-j/graphein
 from __future__ import annotations
 
-import os
+import functools
+import inspect
 import platform
 import subprocess
 import sys
-from typing import Any, Callable, Iterable, List, Optional
+import warnings
+from typing import Any, Callable, Iterable, List
 
 import networkx as nx
 import numpy as np
@@ -25,10 +27,6 @@
     from typing_extensions import Literal
 
 
-AggregationType: List["sum", "mean", "max", "min", "median"]
-"""Types of aggregations for features."""
-
-
 def onek_encoding_unk(
     x: Iterable[Any], allowable_set: List[Any]
 ) -> List[bool]:
@@ -359,11 +357,13 @@ def ping(host: str) -> bool:
     return subprocess.call(command) == 0
 
 
-def parse_aggregation_type(aggregation_type: AggregationType) -> Callable:
+def parse_aggregation_type(
+    aggregation_type: Literal["sum", "mean", "max", "min", "median"]
+) -> Callable:
     """Returns an aggregation function by name
 
     :param aggregation_type: One of: ``["max", "min", "mean", "median", "sum"]``.
-    :type aggregration_type: AggregationType
+    :type aggregration_type: Literal["sum", "mean", "max", "min", "median"]
     :returns: NumPy aggregation function.
     :rtype: Callable
     :raises ValueError: if aggregation type is not supported.
@@ -384,3 +384,61 @@ def parse_aggregation_type(aggregation_type: AggregationType) -> Callable:
             f" Please use min, max, mean, median, sum"
         )
     return func
+
+
+_string_types = (type(b""), type(""))
+
+
+def deprecated(reason):
+    """
+    This is a decorator which can be used to mark functions
+    as deprecated. It will result in a warning being emitted
+    when the function is used.
+    """
+
+    if isinstance(reason, _string_types):
+
+        def decorator(func1):
+            if inspect.isclass(func1):
+                fmt1 = "Call to deprecated class {name} ({reason})."
+            else:
+                fmt1 = "Call to deprecated function {name} ({reason})."
+
+            @functools.wraps(func1)
+            def new_func1(*args, **kwargs):
+                warnings.simplefilter("always", DeprecationWarning)
+                warnings.warn(
+                    fmt1.format(name=func1.__name__, reason=reason),
+                    category=DeprecationWarning,
+                    stacklevel=2,
+                )
+                warnings.simplefilter("default", DeprecationWarning)
+                return func1(*args, **kwargs)
+
+            return new_func1
+
+        return decorator
+
+    elif inspect.isclass(reason) or inspect.isfunction(reason):
+        func2 = reason
+
+        if inspect.isclass(func2):
+            fmt2 = "Call to deprecated class {name}."
+        else:
+            fmt2 = "Call to deprecated function {name}."
+
+        @functools.wraps(func2)
+        def new_func2(*args, **kwargs):
+            warnings.simplefilter("always", DeprecationWarning)
+            warnings.warn(
+                fmt2.format(name=func2.__name__),
+                category=DeprecationWarning,
+                stacklevel=2,
+            )
+            warnings.simplefilter("default", DeprecationWarning)
+            return func2(*args, **kwargs)
+
+        return new_func2
+
+    else:
+        raise TypeError(repr(type(reason)))
diff --git a/tests/protein/nodes/features/test_geometry.py b/tests/protein/nodes/features/test_geometry.py
index 216287a4..76cb5953 100644
--- a/tests/protein/nodes/features/test_geometry.py
+++ b/tests/protein/nodes/features/test_geometry.py
@@ -84,7 +84,8 @@ def test_add_beta_carbon_vector(caplog):
 
     # Test handling of missing beta-carbons
     g = construct_graph(config=config, pdb_code="3se8")
-    assert "H:CYS:104" in caplog.text  # Test warning is raised
+
+    assert "H:CYS:104" in g.nodes
     for n, d in g.nodes(data=True):
         assert d["c_beta_vector"].shape == (3,)
         if n == "H:CYS:104":
diff --git a/tests/protein/tensor/test_io.py b/tests/protein/tensor/test_io.py
index bb1806e0..f489dac7 100644
--- a/tests/protein/tensor/test_io.py
+++ b/tests/protein/tensor/test_io.py
@@ -7,6 +7,7 @@
 # Code Repository: https://github.com/a-r-j/graphein
 
 import os
+from pathlib import Path
 
 import pytest
 from biopandas.pdb import PandasPdb
@@ -16,6 +17,7 @@
 from graphein.protein.tensor.io import (
     protein_df_to_chain_tensor,
     protein_df_to_tensor,
+    protein_to_pyg,
     to_dataframe,
     to_pdb,
 )
@@ -28,6 +30,13 @@
 except ImportError:
     TORCH_AVAIL = False
 
+PDB_DATA_PATH = (
+    Path(__file__).resolve().parent.parent / "test_data" / "4hhb.pdb"
+)
+CIF_DATA_PATH = (
+    Path(__file__).resolve().parent.parent / "test_data" / "4hhb.cif"
+)
+
 
 def get_example_df():
     p = PandasPdb().fetch_pdb("3EIY")
@@ -99,3 +108,17 @@ def test_to_pdb():
         ppdb1.df["ATOM"][["atom_name", "residue_name", "element_symbol"]][:50],
         ppdb2.df["ATOM"][["atom_name", "residue_name", "element_symbol"]][:50],
     )
+
+
+def test_pdb_to_pyg():
+    pyg_object = protein_to_pyg(PDB_DATA_PATH)
+
+
+def test_cif_to_pyg():
+    pyg_object = protein_to_pyg(CIF_DATA_PATH)
+
+
+def test_pdb_and_cif_parsing():
+    pdb_pyg = protein_to_pyg(PDB_DATA_PATH)
+    cif_pyg = protein_to_pyg(CIF_DATA_PATH)
+    assert pdb_pyg.coords.shape == cif_pyg.coords.shape
diff --git a/tests/protein/test_data/4hhb.cif b/tests/protein/test_data/4hhb.cif
new file mode 100644
index 00000000..3209ad61
--- /dev/null
+++ b/tests/protein/test_data/4hhb.cif
@@ -0,0 +1,11053 @@
+data_4HHB
+#
+_entry.id   4HHB
+#
+_audit_conform.dict_name       mmcif_pdbx.dic
+_audit_conform.dict_version    5.392
+_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic
+#
+loop_
+_database_2.database_id
+_database_2.database_code
+_database_2.pdbx_database_accession
+_database_2.pdbx_DOI
+PDB   4HHB         pdb_00004hhb 10.2210/pdb4hhb/pdb
+WWPDB D_1000179340 ?            ?
+#
+loop_
+_pdbx_audit_revision_history.ordinal
+_pdbx_audit_revision_history.data_content_type
+_pdbx_audit_revision_history.major_revision
+_pdbx_audit_revision_history.minor_revision
+_pdbx_audit_revision_history.revision_date
+1 'Structure model' 1 0 1984-07-17
+2 'Structure model' 1 1 2008-03-03
+3 'Structure model' 1 2 2011-07-13
+4 'Structure model' 2 0 2020-06-17
+5 'Structure model' 3 0 2021-03-31
+6 'Structure model' 4 0 2023-02-08
+7 'Structure model' 4 1 2023-03-15
+8 'Structure model' 4 2 2024-05-22
+#
+loop_
+_pdbx_audit_revision_details.ordinal
+_pdbx_audit_revision_details.revision_ordinal
+_pdbx_audit_revision_details.data_content_type
+_pdbx_audit_revision_details.provider
+_pdbx_audit_revision_details.type
+_pdbx_audit_revision_details.description
+_pdbx_audit_revision_details.details
+1 1 'Structure model' repository 'Initial release' ? ?
+2 6 'Structure model' repository Remediation       ?
+'Coordinates and associated ncs operations (if present) transformed into standard crystal frame'
+#
+loop_
+_pdbx_audit_revision_group.ordinal
+_pdbx_audit_revision_group.revision_ordinal
+_pdbx_audit_revision_group.data_content_type
+_pdbx_audit_revision_group.group
+1  2 'Structure model' 'Version format compliance'
+2  3 'Structure model' Advisory
+3  3 'Structure model' 'Version format compliance'
+4  4 'Structure model' Advisory
+5  4 'Structure model' 'Atomic model'
+6  4 'Structure model' 'Data collection'
+7  4 'Structure model' 'Database references'
+8  4 'Structure model' Other
+9  4 'Structure model' 'Source and taxonomy'
+10 4 'Structure model' 'Structure summary'
+11 5 'Structure model' 'Atomic model'
+12 5 'Structure model' 'Data collection'
+13 5 'Structure model' 'Derived calculations'
+14 6 'Structure model' Advisory
+15 6 'Structure model' 'Atomic model'
+16 6 'Structure model' 'Data collection'
+17 6 'Structure model' 'Database references'
+18 6 'Structure model' 'Derived calculations'
+19 6 'Structure model' Other
+20 6 'Structure model' 'Refinement description'
+21 7 'Structure model' Advisory
+22 8 'Structure model' 'Data collection'
+#
+loop_
+_pdbx_audit_revision_category.ordinal
+_pdbx_audit_revision_category.revision_ordinal
+_pdbx_audit_revision_category.data_content_type
+_pdbx_audit_revision_category.category
+1  4 'Structure model' atom_site
+2  4 'Structure model' database_PDB_caveat
+3  4 'Structure model' entity
+4  4 'Structure model' entity_name_com
+5  4 'Structure model' entity_src_gen
+6  4 'Structure model' pdbx_database_status
+7  4 'Structure model' pdbx_validate_rmsd_angle
+8  4 'Structure model' pdbx_validate_rmsd_bond
+9  4 'Structure model' struct_ref
+10 4 'Structure model' struct_ref_seq
+11 5 'Structure model' atom_site
+12 5 'Structure model' pdbx_validate_rmsd_angle
+13 5 'Structure model' pdbx_validate_rmsd_bond
+14 5 'Structure model' struct_site
+15 6 'Structure model' atom_site
+16 6 'Structure model' atom_sites
+17 6 'Structure model' database_2
+18 6 'Structure model' database_PDB_matrix
+19 6 'Structure model' pdbx_struct_conn_angle
+20 6 'Structure model' pdbx_validate_close_contact
+21 6 'Structure model' pdbx_validate_main_chain_plane
+22 6 'Structure model' pdbx_validate_peptide_omega
+23 6 'Structure model' pdbx_validate_planes
+24 6 'Structure model' pdbx_validate_polymer_linkage
+25 6 'Structure model' pdbx_validate_rmsd_angle
+26 6 'Structure model' pdbx_validate_rmsd_bond
+27 6 'Structure model' pdbx_validate_torsion
+28 6 'Structure model' struct_ncs_oper
+29 7 'Structure model' pdbx_database_remark
+30 8 'Structure model' chem_comp_atom
+31 8 'Structure model' chem_comp_bond
+#
+loop_
+_pdbx_audit_revision_item.ordinal
+_pdbx_audit_revision_item.revision_ordinal
+_pdbx_audit_revision_item.data_content_type
+_pdbx_audit_revision_item.item
+1  4 'Structure model' '_atom_site.B_iso_or_equiv'
+2  4 'Structure model' '_atom_site.Cartn_x'
+3  4 'Structure model' '_atom_site.Cartn_y'
+4  4 'Structure model' '_atom_site.Cartn_z'
+5  4 'Structure model' '_entity.pdbx_description'
+6  4 'Structure model' '_entity_src_gen.gene_src_common_name'
+7  4 'Structure model' '_entity_src_gen.pdbx_beg_seq_num'
+8  4 'Structure model' '_entity_src_gen.pdbx_end_seq_num'
+9  4 'Structure model' '_entity_src_gen.pdbx_gene_src_gene'
+10 4 'Structure model' '_entity_src_gen.pdbx_seq_type'
+11 4 'Structure model' '_pdbx_database_status.process_site'
+12 4 'Structure model' '_pdbx_validate_rmsd_angle.angle_deviation'
+13 4 'Structure model' '_pdbx_validate_rmsd_angle.angle_value'
+14 4 'Structure model' '_pdbx_validate_rmsd_bond.bond_deviation'
+15 4 'Structure model' '_pdbx_validate_rmsd_bond.bond_value'
+16 4 'Structure model' '_struct_ref.pdbx_align_begin'
+17 4 'Structure model' '_struct_ref_seq.db_align_beg'
+18 4 'Structure model' '_struct_ref_seq.db_align_end'
+19 5 'Structure model' '_atom_site.B_iso_or_equiv'
+20 5 'Structure model' '_atom_site.Cartn_x'
+21 5 'Structure model' '_atom_site.Cartn_y'
+22 5 'Structure model' '_atom_site.Cartn_z'
+23 5 'Structure model' '_pdbx_validate_rmsd_bond.bond_deviation'
+24 5 'Structure model' '_pdbx_validate_rmsd_bond.bond_value'
+25 5 'Structure model' '_struct_site.pdbx_auth_asym_id'
+26 5 'Structure model' '_struct_site.pdbx_auth_comp_id'
+27 5 'Structure model' '_struct_site.pdbx_auth_seq_id'
+28 6 'Structure model' '_atom_site.Cartn_x'
+29 6 'Structure model' '_atom_site.Cartn_y'
+30 6 'Structure model' '_atom_site.Cartn_z'
+31 6 'Structure model' '_atom_sites.fract_transf_matrix[1][1]'
+32 6 'Structure model' '_atom_sites.fract_transf_matrix[1][2]'
+33 6 'Structure model' '_atom_sites.fract_transf_matrix[1][3]'
+34 6 'Structure model' '_atom_sites.fract_transf_matrix[2][1]'
+35 6 'Structure model' '_atom_sites.fract_transf_matrix[2][2]'
+36 6 'Structure model' '_atom_sites.fract_transf_matrix[2][3]'
+37 6 'Structure model' '_atom_sites.fract_transf_matrix[3][1]'
+38 6 'Structure model' '_atom_sites.fract_transf_matrix[3][2]'
+39 6 'Structure model' '_atom_sites.fract_transf_matrix[3][3]'
+40 6 'Structure model' '_atom_sites.fract_transf_vector[1]'
+41 6 'Structure model' '_atom_sites.fract_transf_vector[2]'
+42 6 'Structure model' '_atom_sites.fract_transf_vector[3]'
+43 6 'Structure model' '_database_2.pdbx_DOI'
+44 6 'Structure model' '_database_2.pdbx_database_accession'
+45 6 'Structure model' '_database_PDB_matrix.origx[1][1]'
+46 6 'Structure model' '_database_PDB_matrix.origx[1][2]'
+47 6 'Structure model' '_database_PDB_matrix.origx[1][3]'
+48 6 'Structure model' '_database_PDB_matrix.origx[2][1]'
+49 6 'Structure model' '_database_PDB_matrix.origx[2][2]'
+50 6 'Structure model' '_database_PDB_matrix.origx[2][3]'
+51 6 'Structure model' '_database_PDB_matrix.origx[3][1]'
+52 6 'Structure model' '_database_PDB_matrix.origx[3][2]'
+53 6 'Structure model' '_database_PDB_matrix.origx[3][3]'
+54 6 'Structure model' '_database_PDB_matrix.origx_vector[1]'
+55 6 'Structure model' '_database_PDB_matrix.origx_vector[2]'
+56 6 'Structure model' '_database_PDB_matrix.origx_vector[3]'
+57 6 'Structure model' '_pdbx_struct_conn_angle.value'
+58 6 'Structure model' '_pdbx_validate_close_contact.dist'
+59 6 'Structure model' '_pdbx_validate_peptide_omega.omega'
+60 6 'Structure model' '_pdbx_validate_planes.rmsd'
+61 6 'Structure model' '_pdbx_validate_polymer_linkage.dist'
+62 6 'Structure model' '_pdbx_validate_torsion.phi'
+63 6 'Structure model' '_pdbx_validate_torsion.psi'
+64 6 'Structure model' '_struct_ncs_oper.matrix[1][1]'
+65 6 'Structure model' '_struct_ncs_oper.matrix[1][2]'
+66 6 'Structure model' '_struct_ncs_oper.matrix[1][3]'
+67 6 'Structure model' '_struct_ncs_oper.matrix[2][1]'
+68 6 'Structure model' '_struct_ncs_oper.matrix[2][2]'
+69 6 'Structure model' '_struct_ncs_oper.matrix[2][3]'
+70 6 'Structure model' '_struct_ncs_oper.matrix[3][1]'
+71 6 'Structure model' '_struct_ncs_oper.matrix[3][2]'
+72 6 'Structure model' '_struct_ncs_oper.matrix[3][3]'
+73 6 'Structure model' '_struct_ncs_oper.vector[1]'
+74 6 'Structure model' '_struct_ncs_oper.vector[2]'
+75 6 'Structure model' '_struct_ncs_oper.vector[3]'
+#
+loop_
+_database_PDB_caveat.id
+_database_PDB_caveat.text
+1  'THR A 137 HAS WRONG CHIRALITY AT ATOM CB'
+2  'THR B 12 HAS WRONG CHIRALITY AT ATOM CB'
+3  'THR B 50 HAS WRONG CHIRALITY AT ATOM CB'
+4  'ASN C 78 HAS WRONG CHIRALITY AT ATOM CA'
+5  'THR C 118 HAS WRONG CHIRALITY AT ATOM CB'
+6  'HIS D 2 HAS WRONG CHIRALITY AT ATOM CA'
+7  'SER D 72 HAS WRONG CHIRALITY AT ATOM CA'
+8  'ASP D 73 HAS WRONG CHIRALITY AT ATOM CA'
+9  'LEU D 78 HAS WRONG CHIRALITY AT ATOM CA'
+10 'LYS D 144 HAS WRONG CHIRALITY AT ATOM CA'
+#
+_pdbx_database_PDB_obs_spr.id               SPRSDE
+_pdbx_database_PDB_obs_spr.date             1984-07-17
+_pdbx_database_PDB_obs_spr.pdb_id           4HHB
+_pdbx_database_PDB_obs_spr.replace_pdb_id   1HHB
+_pdbx_database_PDB_obs_spr.details          ?
+#
+_pdbx_database_status.status_code                     REL
+_pdbx_database_status.entry_id                        4HHB
+_pdbx_database_status.recvd_initial_deposition_date   1984-03-07
+_pdbx_database_status.deposit_site                    ?
+_pdbx_database_status.process_site                    BNL
+_pdbx_database_status.SG_entry                        .
+_pdbx_database_status.pdb_format_compatible           Y
+_pdbx_database_status.status_code_mr                  ?
+_pdbx_database_status.status_code_sf                  ?
+_pdbx_database_status.status_code_cs                  ?
+_pdbx_database_status.status_code_nmr_data            ?
+_pdbx_database_status.methods_development_category    ?
+#
+loop_
+_pdbx_database_related.db_name
+_pdbx_database_related.db_id
+_pdbx_database_related.details
+_pdbx_database_related.content_type
+PDB 2HHB
+;REFINED BY THE METHOD OF JACK AND LEVITT.  THIS
+        ENTRY PRESENTS THE BEST ESTIMATE OF THE
+        COORDINATES.
+;
+unspecified
+PDB 3HHB
+;SYMMETRY AVERAGED ABOUT THE (NON-CRYSTALLOGRAPHIC)
+        MOLECULAR AXIS AND THEN RE-REGULARIZED BY THE
+        ENERGY REFINEMENT METHOD OF LEVITT.  THIS ENTRY
+        PRESENTS COORDINATES THAT ARE ADEQUATE FOR MOST
+        PURPOSES, SUCH AS COMPARISON WITH OTHER STRUCTURES.
+;
+unspecified
+PDB 1GLI . unspecified
+#
+loop_
+_audit_author.name
+_audit_author.pdbx_ordinal
+_audit_author.identifier_ORCID
+'Fermi, G.'    1 ?
+'Perutz, M.F.' 2 ?
+#
+loop_
+_citation.id
+_citation.title
+_citation.journal_abbrev
+_citation.journal_volume
+_citation.page_first
+_citation.page_last
+_citation.year
+_citation.journal_id_ASTM
+_citation.country
+_citation.journal_id_ISSN
+_citation.journal_id_CSD
+_citation.book_publisher
+_citation.pdbx_database_id_PubMed
+_citation.pdbx_database_id_DOI
+primary 'The crystal structure of human deoxyhaemoglobin at 1.74 A resolution' J.Mol.Biol. 175 159 174 1984 JMOBAK UK 0022-2836
+0070 ?                                                            6726807 '10.1016/0022-2836(84)90472-8'
+1       'Stereochemistry of Iron in Deoxyhaemoglobin' Nature                                                                295
+535 ?   1982 NATUAS UK 0028-0836     0006 ?                                                            ?       ?
+3       'Regulation of Oxygen Affinity of Hemoglobin. Influence of Structure of the Globin on the Heme Iron' Annu.Rev.Biochem. 48
+327 ?   1979 ARBOAW US 0066-4154     0413 ?                                                            ?       ?
+4       'Three-Dimensional Fourier Synthesis of Human Deoxyhemoglobin at 2.5 Angstroms Resolution, I.X-Ray Analysis' J.Mol.Biol.
+100 3   ?   1976 JMOBAK UK 0022-2836     0070 ?                                                            ?       ?
+5
+'Three-Dimensional Fourier Synthesis of Human Deoxyhaemoglobin at 2.5 Angstroms Resolution, Refinement of the Atomic Model'
+J.Mol.Biol.                                                           97  237 ?   1975 JMOBAK UK 0022-2836     0070 ? ?       ?
+6       'Three-Dimensional Fourier Synthesis of Human Deoxyhaemoglobin at 3.5 Angstroms Resolution' Nature 228 516 ?   1970 NATUAS
+UK 0028-0836     0006 ?                                                            ?       ?
+2       ? 'Haemoglobin and Myoglobin. Atlas of Molecular Structures in Biology' 2   ?   ?   1981 ?      ?  0-19-854706-4 0986
+'Oxford University Press'                                    ?       ?
+7       ? 'Atlas of Protein Sequence and Structure (Data Section)'              5   56  ?   1972 ?      ?  0-912466-02-2 0435
+'National Biomedical Research Foundation, Silver Spring,Md.' ?       ?
+8       ? 'Atlas of Protein Sequence and Structure (Data Section)'              5   64  ?   1972 ?      ?  0-912466-02-2 0435
+'National Biomedical Research Foundation, Silver Spring,Md.' ?       ?
+#
+loop_
+_citation_author.citation_id
+_citation_author.name
+_citation_author.ordinal
+_citation_author.identifier_ORCID
+primary 'Fermi, G.'     1  ?
+primary 'Perutz, M.F.'  2  ?
+primary 'Shaanan, B.'   3  ?
+primary 'Fourme, R.'    4  ?
+1       'Perutz, M.F.'  5  ?
+1       'Hasnain, S.S.' 6  ?
+1       'Duke, P.J.'    7  ?
+1       'Sessler, J.L.' 8  ?
+1       'Hahn, J.E.'    9  ?
+2       'Fermi, G.'     10 ?
+2       'Perutz, M.F.'  11 ?
+3       'Perutz, M.F.'  12 ?
+4       'Teneyck, L.F.' 13 ?
+4       'Arnone, A.'    14 ?
+5       'Fermi, G.'     15 ?
+6       'Muirhead, H.'  16 ?
+6       'Greer, J.'     17 ?
+#
+loop_
+_citation_editor.citation_id
+_citation_editor.name
+_citation_editor.ordinal
+7 'Dayhoff, M.O.' 1
+8 'Dayhoff, M.O.' 2
+#
+loop_
+_entity.id
+_entity.type
+_entity.src_method
+_entity.pdbx_description
+_entity.formula_weight
+_entity.pdbx_number_of_molecules
+_entity.pdbx_ec
+_entity.pdbx_mutation
+_entity.pdbx_fragment
+_entity.details
+1 polymer     man 'Hemoglobin subunit alpha'        15150.353 2   ? ? ? ?
+2 polymer     man 'Hemoglobin subunit beta'         15890.198 2   ? ? ? ?
+3 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   4   ? ? ? ?
+4 non-polymer syn 'PHOSPHATE ION'                   94.971    2   ? ? ? ?
+5 water       nat water                             18.015    221 ? ? ? ?
+#
+loop_
+_entity_name_com.entity_id
+_entity_name_com.name
+1 'Alpha-globin,Hemoglobin alpha chain'
+2 'Beta-globin,Hemoglobin beta chain'
+#
+loop_
+_entity_poly.entity_id
+_entity_poly.type
+_entity_poly.nstd_linkage
+_entity_poly.nstd_monomer
+_entity_poly.pdbx_seq_one_letter_code
+_entity_poly.pdbx_seq_one_letter_code_can
+_entity_poly.pdbx_strand_id
+_entity_poly.pdbx_target_identifier
+1 'polypeptide(L)' no no
+;VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL
+SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
+;
+;VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL
+SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
+;
+A,C ?
+2 'polypeptide(L)' no no
+;VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN
+LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
+;
+;VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN
+LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
+;
+B,D ?
+#
+loop_
+_pdbx_entity_nonpoly.entity_id
+_pdbx_entity_nonpoly.name
+_pdbx_entity_nonpoly.comp_id
+3 'PROTOPORPHYRIN IX CONTAINING FE' HEM
+4 'PHOSPHATE ION'                   PO4
+5 water                             HOH
+#
+loop_
+_entity_poly_seq.entity_id
+_entity_poly_seq.num
+_entity_poly_seq.mon_id
+_entity_poly_seq.hetero
+1 1   VAL n
+1 2   LEU n
+1 3   SER n
+1 4   PRO n
+1 5   ALA n
+1 6   ASP n
+1 7   LYS n
+1 8   THR n
+1 9   ASN n
+1 10  VAL n
+1 11  LYS n
+1 12  ALA n
+1 13  ALA n
+1 14  TRP n
+1 15  GLY n
+1 16  LYS n
+1 17  VAL n
+1 18  GLY n
+1 19  ALA n
+1 20  HIS n
+1 21  ALA n
+1 22  GLY n
+1 23  GLU n
+1 24  TYR n
+1 25  GLY n
+1 26  ALA n
+1 27  GLU n
+1 28  ALA n
+1 29  LEU n
+1 30  GLU n
+1 31  ARG n
+1 32  MET n
+1 33  PHE n
+1 34  LEU n
+1 35  SER n
+1 36  PHE n
+1 37  PRO n
+1 38  THR n
+1 39  THR n
+1 40  LYS n
+1 41  THR n
+1 42  TYR n
+1 43  PHE n
+1 44  PRO n
+1 45  HIS n
+1 46  PHE n
+1 47  ASP n
+1 48  LEU n
+1 49  SER n
+1 50  HIS n
+1 51  GLY n
+1 52  SER n
+1 53  ALA n
+1 54  GLN n
+1 55  VAL n
+1 56  LYS n
+1 57  GLY n
+1 58  HIS n
+1 59  GLY n
+1 60  LYS n
+1 61  LYS n
+1 62  VAL n
+1 63  ALA n
+1 64  ASP n
+1 65  ALA n
+1 66  LEU n
+1 67  THR n
+1 68  ASN n
+1 69  ALA n
+1 70  VAL n
+1 71  ALA n
+1 72  HIS n
+1 73  VAL n
+1 74  ASP n
+1 75  ASP n
+1 76  MET n
+1 77  PRO n
+1 78  ASN n
+1 79  ALA n
+1 80  LEU n
+1 81  SER n
+1 82  ALA n
+1 83  LEU n
+1 84  SER n
+1 85  ASP n
+1 86  LEU n
+1 87  HIS n
+1 88  ALA n
+1 89  HIS n
+1 90  LYS n
+1 91  LEU n
+1 92  ARG n
+1 93  VAL n
+1 94  ASP n
+1 95  PRO n
+1 96  VAL n
+1 97  ASN n
+1 98  PHE n
+1 99  LYS n
+1 100 LEU n
+1 101 LEU n
+1 102 SER n
+1 103 HIS n
+1 104 CYS n
+1 105 LEU n
+1 106 LEU n
+1 107 VAL n
+1 108 THR n
+1 109 LEU n
+1 110 ALA n
+1 111 ALA n
+1 112 HIS n
+1 113 LEU n
+1 114 PRO n
+1 115 ALA n
+1 116 GLU n
+1 117 PHE n
+1 118 THR n
+1 119 PRO n
+1 120 ALA n
+1 121 VAL n
+1 122 HIS n
+1 123 ALA n
+1 124 SER n
+1 125 LEU n
+1 126 ASP n
+1 127 LYS n
+1 128 PHE n
+1 129 LEU n
+1 130 ALA n
+1 131 SER n
+1 132 VAL n
+1 133 SER n
+1 134 THR n
+1 135 VAL n
+1 136 LEU n
+1 137 THR n
+1 138 SER n
+1 139 LYS n
+1 140 TYR n
+1 141 ARG n
+2 1   VAL n
+2 2   HIS n
+2 3   LEU n
+2 4   THR n
+2 5   PRO n
+2 6   GLU n
+2 7   GLU n
+2 8   LYS n
+2 9   SER n
+2 10  ALA n
+2 11  VAL n
+2 12  THR n
+2 13  ALA n
+2 14  LEU n
+2 15  TRP n
+2 16  GLY n
+2 17  LYS n
+2 18  VAL n
+2 19  ASN n
+2 20  VAL n
+2 21  ASP n
+2 22  GLU n
+2 23  VAL n
+2 24  GLY n
+2 25  GLY n
+2 26  GLU n
+2 27  ALA n
+2 28  LEU n
+2 29  GLY n
+2 30  ARG n
+2 31  LEU n
+2 32  LEU n
+2 33  VAL n
+2 34  VAL n
+2 35  TYR n
+2 36  PRO n
+2 37  TRP n
+2 38  THR n
+2 39  GLN n
+2 40  ARG n
+2 41  PHE n
+2 42  PHE n
+2 43  GLU n
+2 44  SER n
+2 45  PHE n
+2 46  GLY n
+2 47  ASP n
+2 48  LEU n
+2 49  SER n
+2 50  THR n
+2 51  PRO n
+2 52  ASP n
+2 53  ALA n
+2 54  VAL n
+2 55  MET n
+2 56  GLY n
+2 57  ASN n
+2 58  PRO n
+2 59  LYS n
+2 60  VAL n
+2 61  LYS n
+2 62  ALA n
+2 63  HIS n
+2 64  GLY n
+2 65  LYS n
+2 66  LYS n
+2 67  VAL n
+2 68  LEU n
+2 69  GLY n
+2 70  ALA n
+2 71  PHE n
+2 72  SER n
+2 73  ASP n
+2 74  GLY n
+2 75  LEU n
+2 76  ALA n
+2 77  HIS n
+2 78  LEU n
+2 79  ASP n
+2 80  ASN n
+2 81  LEU n
+2 82  LYS n
+2 83  GLY n
+2 84  THR n
+2 85  PHE n
+2 86  ALA n
+2 87  THR n
+2 88  LEU n
+2 89  SER n
+2 90  GLU n
+2 91  LEU n
+2 92  HIS n
+2 93  CYS n
+2 94  ASP n
+2 95  LYS n
+2 96  LEU n
+2 97  HIS n
+2 98  VAL n
+2 99  ASP n
+2 100 PRO n
+2 101 GLU n
+2 102 ASN n
+2 103 PHE n
+2 104 ARG n
+2 105 LEU n
+2 106 LEU n
+2 107 GLY n
+2 108 ASN n
+2 109 VAL n
+2 110 LEU n
+2 111 VAL n
+2 112 CYS n
+2 113 VAL n
+2 114 LEU n
+2 115 ALA n
+2 116 HIS n
+2 117 HIS n
+2 118 PHE n
+2 119 GLY n
+2 120 LYS n
+2 121 GLU n
+2 122 PHE n
+2 123 THR n
+2 124 PRO n
+2 125 PRO n
+2 126 VAL n
+2 127 GLN n
+2 128 ALA n
+2 129 ALA n
+2 130 TYR n
+2 131 GLN n
+2 132 LYS n
+2 133 VAL n
+2 134 VAL n
+2 135 ALA n
+2 136 GLY n
+2 137 VAL n
+2 138 ALA n
+2 139 ASN n
+2 140 ALA n
+2 141 LEU n
+2 142 ALA n
+2 143 HIS n
+2 144 LYS n
+2 145 TYR n
+2 146 HIS n
+#
+loop_
+_entity_src_gen.entity_id
+_entity_src_gen.pdbx_src_id
+_entity_src_gen.pdbx_alt_source_flag
+_entity_src_gen.pdbx_seq_type
+_entity_src_gen.pdbx_beg_seq_num
+_entity_src_gen.pdbx_end_seq_num
+_entity_src_gen.gene_src_common_name
+_entity_src_gen.gene_src_genus
+_entity_src_gen.pdbx_gene_src_gene
+_entity_src_gen.gene_src_species
+_entity_src_gen.gene_src_strain
+_entity_src_gen.gene_src_tissue
+_entity_src_gen.gene_src_tissue_fraction
+_entity_src_gen.gene_src_details
+_entity_src_gen.pdbx_gene_src_fragment
+_entity_src_gen.pdbx_gene_src_scientific_name
+_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id
+_entity_src_gen.pdbx_gene_src_variant
+_entity_src_gen.pdbx_gene_src_cell_line
+_entity_src_gen.pdbx_gene_src_atcc
+_entity_src_gen.pdbx_gene_src_organ
+_entity_src_gen.pdbx_gene_src_organelle
+_entity_src_gen.pdbx_gene_src_cell
+_entity_src_gen.pdbx_gene_src_cellular_location
+_entity_src_gen.host_org_common_name
+_entity_src_gen.pdbx_host_org_scientific_name
+_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id
+_entity_src_gen.host_org_genus
+_entity_src_gen.pdbx_host_org_gene
+_entity_src_gen.pdbx_host_org_organ
+_entity_src_gen.host_org_species
+_entity_src_gen.pdbx_host_org_tissue
+_entity_src_gen.pdbx_host_org_tissue_fraction
+_entity_src_gen.pdbx_host_org_strain
+_entity_src_gen.pdbx_host_org_variant
+_entity_src_gen.pdbx_host_org_cell_line
+_entity_src_gen.pdbx_host_org_atcc
+_entity_src_gen.pdbx_host_org_culture_collection
+_entity_src_gen.pdbx_host_org_cell
+_entity_src_gen.pdbx_host_org_organelle
+_entity_src_gen.pdbx_host_org_cellular_location
+_entity_src_gen.pdbx_host_org_vector_type
+_entity_src_gen.pdbx_host_org_vector
+_entity_src_gen.host_org_details
+_entity_src_gen.expression_system_id
+_entity_src_gen.plasmid_name
+_entity_src_gen.plasmid_details
+_entity_src_gen.pdbx_description
+1 1 sample 'Biological sequence' 1 141 Human Homo 'HBA1, HBA2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?
+? ? ? ? ? ? ? ? ? ? ? ? ?
+2 1 sample 'Biological sequence' 1 146 Human Homo HBB          ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ?
+? ? ? ? ? ? ? ? ? ? ? ? ?
+#
+loop_
+_chem_comp.id
+_chem_comp.type
+_chem_comp.mon_nstd_flag
+_chem_comp.name
+_chem_comp.pdbx_synonyms
+_chem_comp.formula
+_chem_comp.formula_weight
+ALA 'L-peptide linking' y ALANINE                           ?    'C3 H7 N O2'       89.093
+ARG 'L-peptide linking' y ARGININE                          ?    'C6 H15 N4 O2 1'   175.209
+ASN 'L-peptide linking' y ASPARAGINE                        ?    'C4 H8 N2 O3'      132.118
+ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ?    'C4 H7 N O4'       133.103
+CYS 'L-peptide linking' y CYSTEINE                          ?    'C3 H7 N O2 S'     121.158
+GLN 'L-peptide linking' y GLUTAMINE                         ?    'C5 H10 N2 O3'     146.144
+GLU 'L-peptide linking' y 'GLUTAMIC ACID'                   ?    'C5 H9 N O4'       147.129
+GLY 'peptide linking'   y GLYCINE                           ?    'C2 H5 N O2'       75.067
+HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487
+HIS 'L-peptide linking' y HISTIDINE                         ?    'C6 H10 N3 O2 1'   156.162
+HOH non-polymer         . WATER                             ?    'H2 O'             18.015
+LEU 'L-peptide linking' y LEUCINE                           ?    'C6 H13 N O2'      131.173
+LYS 'L-peptide linking' y LYSINE                            ?    'C6 H15 N2 O2 1'   147.195
+MET 'L-peptide linking' y METHIONINE                        ?    'C5 H11 N O2 S'    149.211
+PHE 'L-peptide linking' y PHENYLALANINE                     ?    'C9 H11 N O2'      165.189
+PO4 non-polymer         . 'PHOSPHATE ION'                   ?    'O4 P -3'          94.971
+PRO 'L-peptide linking' y PROLINE                           ?    'C5 H9 N O2'       115.130
+SER 'L-peptide linking' y SERINE                            ?    'C3 H7 N O3'       105.093
+THR 'L-peptide linking' y THREONINE                         ?    'C4 H9 N O3'       119.119
+TRP 'L-peptide linking' y TRYPTOPHAN                        ?    'C11 H12 N2 O2'    204.225
+TYR 'L-peptide linking' y TYROSINE                          ?    'C9 H11 N O3'      181.189
+VAL 'L-peptide linking' y VALINE                            ?    'C5 H11 N O2'      117.146
+#
+loop_
+_pdbx_poly_seq_scheme.asym_id
+_pdbx_poly_seq_scheme.entity_id
+_pdbx_poly_seq_scheme.seq_id
+_pdbx_poly_seq_scheme.mon_id
+_pdbx_poly_seq_scheme.ndb_seq_num
+_pdbx_poly_seq_scheme.pdb_seq_num
+_pdbx_poly_seq_scheme.auth_seq_num
+_pdbx_poly_seq_scheme.pdb_mon_id
+_pdbx_poly_seq_scheme.auth_mon_id
+_pdbx_poly_seq_scheme.pdb_strand_id
+_pdbx_poly_seq_scheme.pdb_ins_code
+_pdbx_poly_seq_scheme.hetero
+A 1 1   VAL 1   1   1   VAL VAL A . n
+A 1 2   LEU 2   2   2   LEU LEU A . n
+A 1 3   SER 3   3   3   SER SER A . n
+A 1 4   PRO 4   4   4   PRO PRO A . n
+A 1 5   ALA 5   5   5   ALA ALA A . n
+A 1 6   ASP 6   6   6   ASP ASP A . n
+A 1 7   LYS 7   7   7   LYS LYS A . n
+A 1 8   THR 8   8   8   THR THR A . n
+A 1 9   ASN 9   9   9   ASN ASN A . n
+A 1 10  VAL 10  10  10  VAL VAL A . n
+A 1 11  LYS 11  11  11  LYS LYS A . n
+A 1 12  ALA 12  12  12  ALA ALA A . n
+A 1 13  ALA 13  13  13  ALA ALA A . n
+A 1 14  TRP 14  14  14  TRP TRP A . n
+A 1 15  GLY 15  15  15  GLY GLY A . n
+A 1 16  LYS 16  16  16  LYS LYS A . n
+A 1 17  VAL 17  17  17  VAL VAL A . n
+A 1 18  GLY 18  18  18  GLY GLY A . n
+A 1 19  ALA 19  19  19  ALA ALA A . n
+A 1 20  HIS 20  20  20  HIS HIS A . n
+A 1 21  ALA 21  21  21  ALA ALA A . n
+A 1 22  GLY 22  22  22  GLY GLY A . n
+A 1 23  GLU 23  23  23  GLU GLU A . n
+A 1 24  TYR 24  24  24  TYR TYR A . n
+A 1 25  GLY 25  25  25  GLY GLY A . n
+A 1 26  ALA 26  26  26  ALA ALA A . n
+A 1 27  GLU 27  27  27  GLU GLU A . n
+A 1 28  ALA 28  28  28  ALA ALA A . n
+A 1 29  LEU 29  29  29  LEU LEU A . n
+A 1 30  GLU 30  30  30  GLU GLU A . n
+A 1 31  ARG 31  31  31  ARG ARG A . n
+A 1 32  MET 32  32  32  MET MET A . n
+A 1 33  PHE 33  33  33  PHE PHE A . n
+A 1 34  LEU 34  34  34  LEU LEU A . n
+A 1 35  SER 35  35  35  SER SER A . n
+A 1 36  PHE 36  36  36  PHE PHE A . n
+A 1 37  PRO 37  37  37  PRO PRO A . n
+A 1 38  THR 38  38  38  THR THR A . n
+A 1 39  THR 39  39  39  THR THR A . n
+A 1 40  LYS 40  40  40  LYS LYS A . n
+A 1 41  THR 41  41  41  THR THR A . n
+A 1 42  TYR 42  42  42  TYR TYR A . n
+A 1 43  PHE 43  43  43  PHE PHE A . n
+A 1 44  PRO 44  44  44  PRO PRO A . n
+A 1 45  HIS 45  45  45  HIS HIS A . n
+A 1 46  PHE 46  46  46  PHE PHE A . n
+A 1 47  ASP 47  47  47  ASP ASP A . n
+A 1 48  LEU 48  48  48  LEU LEU A . n
+A 1 49  SER 49  49  49  SER SER A . n
+A 1 50  HIS 50  50  50  HIS HIS A . n
+A 1 51  GLY 51  51  51  GLY GLY A . n
+A 1 52  SER 52  52  52  SER SER A . n
+A 1 53  ALA 53  53  53  ALA ALA A . n
+A 1 54  GLN 54  54  54  GLN GLN A . n
+A 1 55  VAL 55  55  55  VAL VAL A . n
+A 1 56  LYS 56  56  56  LYS LYS A . n
+A 1 57  GLY 57  57  57  GLY GLY A . n
+A 1 58  HIS 58  58  58  HIS HIS A . n
+A 1 59  GLY 59  59  59  GLY GLY A . n
+A 1 60  LYS 60  60  60  LYS LYS A . n
+A 1 61  LYS 61  61  61  LYS LYS A . n
+A 1 62  VAL 62  62  62  VAL VAL A . n
+A 1 63  ALA 63  63  63  ALA ALA A . n
+A 1 64  ASP 64  64  64  ASP ASP A . n
+A 1 65  ALA 65  65  65  ALA ALA A . n
+A 1 66  LEU 66  66  66  LEU LEU A . n
+A 1 67  THR 67  67  67  THR THR A . n
+A 1 68  ASN 68  68  68  ASN ASN A . n
+A 1 69  ALA 69  69  69  ALA ALA A . n
+A 1 70  VAL 70  70  70  VAL VAL A . n
+A 1 71  ALA 71  71  71  ALA ALA A . n
+A 1 72  HIS 72  72  72  HIS HIS A . n
+A 1 73  VAL 73  73  73  VAL VAL A . n
+A 1 74  ASP 74  74  74  ASP ASP A . n
+A 1 75  ASP 75  75  75  ASP ASP A . n
+A 1 76  MET 76  76  76  MET MET A . n
+A 1 77  PRO 77  77  77  PRO PRO A . n
+A 1 78  ASN 78  78  78  ASN ASN A . n
+A 1 79  ALA 79  79  79  ALA ALA A . n
+A 1 80  LEU 80  80  80  LEU LEU A . n
+A 1 81  SER 81  81  81  SER SER A . n
+A 1 82  ALA 82  82  82  ALA ALA A . n
+A 1 83  LEU 83  83  83  LEU LEU A . n
+A 1 84  SER 84  84  84  SER SER A . n
+A 1 85  ASP 85  85  85  ASP ASP A . n
+A 1 86  LEU 86  86  86  LEU LEU A . n
+A 1 87  HIS 87  87  87  HIS HIS A . n
+A 1 88  ALA 88  88  88  ALA ALA A . n
+A 1 89  HIS 89  89  89  HIS HIS A . n
+A 1 90  LYS 90  90  90  LYS LYS A . n
+A 1 91  LEU 91  91  91  LEU LEU A . n
+A 1 92  ARG 92  92  92  ARG ARG A . n
+A 1 93  VAL 93  93  93  VAL VAL A . n
+A 1 94  ASP 94  94  94  ASP ASP A . n
+A 1 95  PRO 95  95  95  PRO PRO A . n
+A 1 96  VAL 96  96  96  VAL VAL A . n
+A 1 97  ASN 97  97  97  ASN ASN A . n
+A 1 98  PHE 98  98  98  PHE PHE A . n
+A 1 99  LYS 99  99  99  LYS LYS A . n
+A 1 100 LEU 100 100 100 LEU LEU A . n
+A 1 101 LEU 101 101 101 LEU LEU A . n
+A 1 102 SER 102 102 102 SER SER A . n
+A 1 103 HIS 103 103 103 HIS HIS A . n
+A 1 104 CYS 104 104 104 CYS CYS A . n
+A 1 105 LEU 105 105 105 LEU LEU A . n
+A 1 106 LEU 106 106 106 LEU LEU A . n
+A 1 107 VAL 107 107 107 VAL VAL A . n
+A 1 108 THR 108 108 108 THR THR A . n
+A 1 109 LEU 109 109 109 LEU LEU A . n
+A 1 110 ALA 110 110 110 ALA ALA A . n
+A 1 111 ALA 111 111 111 ALA ALA A . n
+A 1 112 HIS 112 112 112 HIS HIS A . n
+A 1 113 LEU 113 113 113 LEU LEU A . n
+A 1 114 PRO 114 114 114 PRO PRO A . n
+A 1 115 ALA 115 115 115 ALA ALA A . n
+A 1 116 GLU 116 116 116 GLU GLU A . n
+A 1 117 PHE 117 117 117 PHE PHE A . n
+A 1 118 THR 118 118 118 THR THR A . n
+A 1 119 PRO 119 119 119 PRO PRO A . n
+A 1 120 ALA 120 120 120 ALA ALA A . n
+A 1 121 VAL 121 121 121 VAL VAL A . n
+A 1 122 HIS 122 122 122 HIS HIS A . n
+A 1 123 ALA 123 123 123 ALA ALA A . n
+A 1 124 SER 124 124 124 SER SER A . n
+A 1 125 LEU 125 125 125 LEU LEU A . n
+A 1 126 ASP 126 126 126 ASP ASP A . n
+A 1 127 LYS 127 127 127 LYS LYS A . n
+A 1 128 PHE 128 128 128 PHE PHE A . n
+A 1 129 LEU 129 129 129 LEU LEU A . n
+A 1 130 ALA 130 130 130 ALA ALA A . n
+A 1 131 SER 131 131 131 SER SER A . n
+A 1 132 VAL 132 132 132 VAL VAL A . n
+A 1 133 SER 133 133 133 SER SER A . n
+A 1 134 THR 134 134 134 THR THR A . n
+A 1 135 VAL 135 135 135 VAL VAL A . n
+A 1 136 LEU 136 136 136 LEU LEU A . n
+A 1 137 THR 137 137 137 THR THR A . n
+A 1 138 SER 138 138 138 SER SER A . n
+A 1 139 LYS 139 139 139 LYS LYS A . n
+A 1 140 TYR 140 140 140 TYR TYR A . n
+A 1 141 ARG 141 141 141 ARG ARG A . n
+B 2 1   VAL 1   1   1   VAL VAL B . n
+B 2 2   HIS 2   2   2   HIS HIS B . n
+B 2 3   LEU 3   3   3   LEU LEU B . n
+B 2 4   THR 4   4   4   THR THR B . n
+B 2 5   PRO 5   5   5   PRO PRO B . n
+B 2 6   GLU 6   6   6   GLU GLU B . n
+B 2 7   GLU 7   7   7   GLU GLU B . n
+B 2 8   LYS 8   8   8   LYS LYS B . n
+B 2 9   SER 9   9   9   SER SER B . n
+B 2 10  ALA 10  10  10  ALA ALA B . n
+B 2 11  VAL 11  11  11  VAL VAL B . n
+B 2 12  THR 12  12  12  THR THR B . n
+B 2 13  ALA 13  13  13  ALA ALA B . n
+B 2 14  LEU 14  14  14  LEU LEU B . n
+B 2 15  TRP 15  15  15  TRP TRP B . n
+B 2 16  GLY 16  16  16  GLY GLY B . n
+B 2 17  LYS 17  17  17  LYS LYS B . n
+B 2 18  VAL 18  18  18  VAL VAL B . n
+B 2 19  ASN 19  19  19  ASN ASN B . n
+B 2 20  VAL 20  20  20  VAL VAL B . n
+B 2 21  ASP 21  21  21  ASP ASP B . n
+B 2 22  GLU 22  22  22  GLU GLU B . n
+B 2 23  VAL 23  23  23  VAL VAL B . n
+B 2 24  GLY 24  24  24  GLY GLY B . n
+B 2 25  GLY 25  25  25  GLY GLY B . n
+B 2 26  GLU 26  26  26  GLU GLU B . n
+B 2 27  ALA 27  27  27  ALA ALA B . n
+B 2 28  LEU 28  28  28  LEU LEU B . n
+B 2 29  GLY 29  29  29  GLY GLY B . n
+B 2 30  ARG 30  30  30  ARG ARG B . n
+B 2 31  LEU 31  31  31  LEU LEU B . n
+B 2 32  LEU 32  32  32  LEU LEU B . n
+B 2 33  VAL 33  33  33  VAL VAL B . n
+B 2 34  VAL 34  34  34  VAL VAL B . n
+B 2 35  TYR 35  35  35  TYR TYR B . n
+B 2 36  PRO 36  36  36  PRO PRO B . n
+B 2 37  TRP 37  37  37  TRP TRP B . n
+B 2 38  THR 38  38  38  THR THR B . n
+B 2 39  GLN 39  39  39  GLN GLN B . n
+B 2 40  ARG 40  40  40  ARG ARG B . n
+B 2 41  PHE 41  41  41  PHE PHE B . n
+B 2 42  PHE 42  42  42  PHE PHE B . n
+B 2 43  GLU 43  43  43  GLU GLU B . n
+B 2 44  SER 44  44  44  SER SER B . n
+B 2 45  PHE 45  45  45  PHE PHE B . n
+B 2 46  GLY 46  46  46  GLY GLY B . n
+B 2 47  ASP 47  47  47  ASP ASP B . n
+B 2 48  LEU 48  48  48  LEU LEU B . n
+B 2 49  SER 49  49  49  SER SER B . n
+B 2 50  THR 50  50  50  THR THR B . n
+B 2 51  PRO 51  51  51  PRO PRO B . n
+B 2 52  ASP 52  52  52  ASP ASP B . n
+B 2 53  ALA 53  53  53  ALA ALA B . n
+B 2 54  VAL 54  54  54  VAL VAL B . n
+B 2 55  MET 55  55  55  MET MET B . n
+B 2 56  GLY 56  56  56  GLY GLY B . n
+B 2 57  ASN 57  57  57  ASN ASN B . n
+B 2 58  PRO 58  58  58  PRO PRO B . n
+B 2 59  LYS 59  59  59  LYS LYS B . n
+B 2 60  VAL 60  60  60  VAL VAL B . n
+B 2 61  LYS 61  61  61  LYS LYS B . n
+B 2 62  ALA 62  62  62  ALA ALA B . n
+B 2 63  HIS 63  63  63  HIS HIS B . n
+B 2 64  GLY 64  64  64  GLY GLY B . n
+B 2 65  LYS 65  65  65  LYS LYS B . n
+B 2 66  LYS 66  66  66  LYS LYS B . n
+B 2 67  VAL 67  67  67  VAL VAL B . n
+B 2 68  LEU 68  68  68  LEU LEU B . n
+B 2 69  GLY 69  69  69  GLY GLY B . n
+B 2 70  ALA 70  70  70  ALA ALA B . n
+B 2 71  PHE 71  71  71  PHE PHE B . n
+B 2 72  SER 72  72  72  SER SER B . n
+B 2 73  ASP 73  73  73  ASP ASP B . n
+B 2 74  GLY 74  74  74  GLY GLY B . n
+B 2 75  LEU 75  75  75  LEU LEU B . n
+B 2 76  ALA 76  76  76  ALA ALA B . n
+B 2 77  HIS 77  77  77  HIS HIS B . n
+B 2 78  LEU 78  78  78  LEU LEU B . n
+B 2 79  ASP 79  79  79  ASP ASP B . n
+B 2 80  ASN 80  80  80  ASN ASN B . n
+B 2 81  LEU 81  81  81  LEU LEU B . n
+B 2 82  LYS 82  82  82  LYS LYS B . n
+B 2 83  GLY 83  83  83  GLY GLY B . n
+B 2 84  THR 84  84  84  THR THR B . n
+B 2 85  PHE 85  85  85  PHE PHE B . n
+B 2 86  ALA 86  86  86  ALA ALA B . n
+B 2 87  THR 87  87  87  THR THR B . n
+B 2 88  LEU 88  88  88  LEU LEU B . n
+B 2 89  SER 89  89  89  SER SER B . n
+B 2 90  GLU 90  90  90  GLU GLU B . n
+B 2 91  LEU 91  91  91  LEU LEU B . n
+B 2 92  HIS 92  92  92  HIS HIS B . n
+B 2 93  CYS 93  93  93  CYS CYS B . n
+B 2 94  ASP 94  94  94  ASP ASP B . n
+B 2 95  LYS 95  95  95  LYS LYS B . n
+B 2 96  LEU 96  96  96  LEU LEU B . n
+B 2 97  HIS 97  97  97  HIS HIS B . n
+B 2 98  VAL 98  98  98  VAL VAL B . n
+B 2 99  ASP 99  99  99  ASP ASP B . n
+B 2 100 PRO 100 100 100 PRO PRO B . n
+B 2 101 GLU 101 101 101 GLU GLU B . n
+B 2 102 ASN 102 102 102 ASN ASN B . n
+B 2 103 PHE 103 103 103 PHE PHE B . n
+B 2 104 ARG 104 104 104 ARG ARG B . n
+B 2 105 LEU 105 105 105 LEU LEU B . n
+B 2 106 LEU 106 106 106 LEU LEU B . n
+B 2 107 GLY 107 107 107 GLY GLY B . n
+B 2 108 ASN 108 108 108 ASN ASN B . n
+B 2 109 VAL 109 109 109 VAL VAL B . n
+B 2 110 LEU 110 110 110 LEU LEU B . n
+B 2 111 VAL 111 111 111 VAL VAL B . n
+B 2 112 CYS 112 112 112 CYS CYS B . n
+B 2 113 VAL 113 113 113 VAL VAL B . n
+B 2 114 LEU 114 114 114 LEU LEU B . n
+B 2 115 ALA 115 115 115 ALA ALA B . n
+B 2 116 HIS 116 116 116 HIS HIS B . n
+B 2 117 HIS 117 117 117 HIS HIS B . n
+B 2 118 PHE 118 118 118 PHE PHE B . n
+B 2 119 GLY 119 119 119 GLY GLY B . n
+B 2 120 LYS 120 120 120 LYS LYS B . n
+B 2 121 GLU 121 121 121 GLU GLU B . n
+B 2 122 PHE 122 122 122 PHE PHE B . n
+B 2 123 THR 123 123 123 THR THR B . n
+B 2 124 PRO 124 124 124 PRO PRO B . n
+B 2 125 PRO 125 125 125 PRO PRO B . n
+B 2 126 VAL 126 126 126 VAL VAL B . n
+B 2 127 GLN 127 127 127 GLN GLN B . n
+B 2 128 ALA 128 128 128 ALA ALA B . n
+B 2 129 ALA 129 129 129 ALA ALA B . n
+B 2 130 TYR 130 130 130 TYR TYR B . n
+B 2 131 GLN 131 131 131 GLN GLN B . n
+B 2 132 LYS 132 132 132 LYS LYS B . n
+B 2 133 VAL 133 133 133 VAL VAL B . n
+B 2 134 VAL 134 134 134 VAL VAL B . n
+B 2 135 ALA 135 135 135 ALA ALA B . n
+B 2 136 GLY 136 136 136 GLY GLY B . n
+B 2 137 VAL 137 137 137 VAL VAL B . n
+B 2 138 ALA 138 138 138 ALA ALA B . n
+B 2 139 ASN 139 139 139 ASN ASN B . n
+B 2 140 ALA 140 140 140 ALA ALA B . n
+B 2 141 LEU 141 141 141 LEU LEU B . n
+B 2 142 ALA 142 142 142 ALA ALA B . n
+B 2 143 HIS 143 143 143 HIS HIS B . n
+B 2 144 LYS 144 144 144 LYS LYS B . n
+B 2 145 TYR 145 145 145 TYR TYR B . n
+B 2 146 HIS 146 146 146 HIS HIS B . n
+C 1 1   VAL 1   1   1   VAL VAL C . n
+C 1 2   LEU 2   2   2   LEU LEU C . n
+C 1 3   SER 3   3   3   SER SER C . n
+C 1 4   PRO 4   4   4   PRO PRO C . n
+C 1 5   ALA 5   5   5   ALA ALA C . n
+C 1 6   ASP 6   6   6   ASP ASP C . n
+C 1 7   LYS 7   7   7   LYS LYS C . n
+C 1 8   THR 8   8   8   THR THR C . n
+C 1 9   ASN 9   9   9   ASN ASN C . n
+C 1 10  VAL 10  10  10  VAL VAL C . n
+C 1 11  LYS 11  11  11  LYS LYS C . n
+C 1 12  ALA 12  12  12  ALA ALA C . n
+C 1 13  ALA 13  13  13  ALA ALA C . n
+C 1 14  TRP 14  14  14  TRP TRP C . n
+C 1 15  GLY 15  15  15  GLY GLY C . n
+C 1 16  LYS 16  16  16  LYS LYS C . n
+C 1 17  VAL 17  17  17  VAL VAL C . n
+C 1 18  GLY 18  18  18  GLY GLY C . n
+C 1 19  ALA 19  19  19  ALA ALA C . n
+C 1 20  HIS 20  20  20  HIS HIS C . n
+C 1 21  ALA 21  21  21  ALA ALA C . n
+C 1 22  GLY 22  22  22  GLY GLY C . n
+C 1 23  GLU 23  23  23  GLU GLU C . n
+C 1 24  TYR 24  24  24  TYR TYR C . n
+C 1 25  GLY 25  25  25  GLY GLY C . n
+C 1 26  ALA 26  26  26  ALA ALA C . n
+C 1 27  GLU 27  27  27  GLU GLU C . n
+C 1 28  ALA 28  28  28  ALA ALA C . n
+C 1 29  LEU 29  29  29  LEU LEU C . n
+C 1 30  GLU 30  30  30  GLU GLU C . n
+C 1 31  ARG 31  31  31  ARG ARG C . n
+C 1 32  MET 32  32  32  MET MET C . n
+C 1 33  PHE 33  33  33  PHE PHE C . n
+C 1 34  LEU 34  34  34  LEU LEU C . n
+C 1 35  SER 35  35  35  SER SER C . n
+C 1 36  PHE 36  36  36  PHE PHE C . n
+C 1 37  PRO 37  37  37  PRO PRO C . n
+C 1 38  THR 38  38  38  THR THR C . n
+C 1 39  THR 39  39  39  THR THR C . n
+C 1 40  LYS 40  40  40  LYS LYS C . n
+C 1 41  THR 41  41  41  THR THR C . n
+C 1 42  TYR 42  42  42  TYR TYR C . n
+C 1 43  PHE 43  43  43  PHE PHE C . n
+C 1 44  PRO 44  44  44  PRO PRO C . n
+C 1 45  HIS 45  45  45  HIS HIS C . n
+C 1 46  PHE 46  46  46  PHE PHE C . n
+C 1 47  ASP 47  47  47  ASP ASP C . n
+C 1 48  LEU 48  48  48  LEU LEU C . n
+C 1 49  SER 49  49  49  SER SER C . n
+C 1 50  HIS 50  50  50  HIS HIS C . n
+C 1 51  GLY 51  51  51  GLY GLY C . n
+C 1 52  SER 52  52  52  SER SER C . n
+C 1 53  ALA 53  53  53  ALA ALA C . n
+C 1 54  GLN 54  54  54  GLN GLN C . n
+C 1 55  VAL 55  55  55  VAL VAL C . n
+C 1 56  LYS 56  56  56  LYS LYS C . n
+C 1 57  GLY 57  57  57  GLY GLY C . n
+C 1 58  HIS 58  58  58  HIS HIS C . n
+C 1 59  GLY 59  59  59  GLY GLY C . n
+C 1 60  LYS 60  60  60  LYS LYS C . n
+C 1 61  LYS 61  61  61  LYS LYS C . n
+C 1 62  VAL 62  62  62  VAL VAL C . n
+C 1 63  ALA 63  63  63  ALA ALA C . n
+C 1 64  ASP 64  64  64  ASP ASP C . n
+C 1 65  ALA 65  65  65  ALA ALA C . n
+C 1 66  LEU 66  66  66  LEU LEU C . n
+C 1 67  THR 67  67  67  THR THR C . n
+C 1 68  ASN 68  68  68  ASN ASN C . n
+C 1 69  ALA 69  69  69  ALA ALA C . n
+C 1 70  VAL 70  70  70  VAL VAL C . n
+C 1 71  ALA 71  71  71  ALA ALA C . n
+C 1 72  HIS 72  72  72  HIS HIS C . n
+C 1 73  VAL 73  73  73  VAL VAL C . n
+C 1 74  ASP 74  74  74  ASP ASP C . n
+C 1 75  ASP 75  75  75  ASP ASP C . n
+C 1 76  MET 76  76  76  MET MET C . n
+C 1 77  PRO 77  77  77  PRO PRO C . n
+C 1 78  ASN 78  78  78  ASN ASN C . n
+C 1 79  ALA 79  79  79  ALA ALA C . n
+C 1 80  LEU 80  80  80  LEU LEU C . n
+C 1 81  SER 81  81  81  SER SER C . n
+C 1 82  ALA 82  82  82  ALA ALA C . n
+C 1 83  LEU 83  83  83  LEU LEU C . n
+C 1 84  SER 84  84  84  SER SER C . n
+C 1 85  ASP 85  85  85  ASP ASP C . n
+C 1 86  LEU 86  86  86  LEU LEU C . n
+C 1 87  HIS 87  87  87  HIS HIS C . n
+C 1 88  ALA 88  88  88  ALA ALA C . n
+C 1 89  HIS 89  89  89  HIS HIS C . n
+C 1 90  LYS 90  90  90  LYS LYS C . n
+C 1 91  LEU 91  91  91  LEU LEU C . n
+C 1 92  ARG 92  92  92  ARG ARG C . n
+C 1 93  VAL 93  93  93  VAL VAL C . n
+C 1 94  ASP 94  94  94  ASP ASP C . n
+C 1 95  PRO 95  95  95  PRO PRO C . n
+C 1 96  VAL 96  96  96  VAL VAL C . n
+C 1 97  ASN 97  97  97  ASN ASN C . n
+C 1 98  PHE 98  98  98  PHE PHE C . n
+C 1 99  LYS 99  99  99  LYS LYS C . n
+C 1 100 LEU 100 100 100 LEU LEU C . n
+C 1 101 LEU 101 101 101 LEU LEU C . n
+C 1 102 SER 102 102 102 SER SER C . n
+C 1 103 HIS 103 103 103 HIS HIS C . n
+C 1 104 CYS 104 104 104 CYS CYS C . n
+C 1 105 LEU 105 105 105 LEU LEU C . n
+C 1 106 LEU 106 106 106 LEU LEU C . n
+C 1 107 VAL 107 107 107 VAL VAL C . n
+C 1 108 THR 108 108 108 THR THR C . n
+C 1 109 LEU 109 109 109 LEU LEU C . n
+C 1 110 ALA 110 110 110 ALA ALA C . n
+C 1 111 ALA 111 111 111 ALA ALA C . n
+C 1 112 HIS 112 112 112 HIS HIS C . n
+C 1 113 LEU 113 113 113 LEU LEU C . n
+C 1 114 PRO 114 114 114 PRO PRO C . n
+C 1 115 ALA 115 115 115 ALA ALA C . n
+C 1 116 GLU 116 116 116 GLU GLU C . n
+C 1 117 PHE 117 117 117 PHE PHE C . n
+C 1 118 THR 118 118 118 THR THR C . n
+C 1 119 PRO 119 119 119 PRO PRO C . n
+C 1 120 ALA 120 120 120 ALA ALA C . n
+C 1 121 VAL 121 121 121 VAL VAL C . n
+C 1 122 HIS 122 122 122 HIS HIS C . n
+C 1 123 ALA 123 123 123 ALA ALA C . n
+C 1 124 SER 124 124 124 SER SER C . n
+C 1 125 LEU 125 125 125 LEU LEU C . n
+C 1 126 ASP 126 126 126 ASP ASP C . n
+C 1 127 LYS 127 127 127 LYS LYS C . n
+C 1 128 PHE 128 128 128 PHE PHE C . n
+C 1 129 LEU 129 129 129 LEU LEU C . n
+C 1 130 ALA 130 130 130 ALA ALA C . n
+C 1 131 SER 131 131 131 SER SER C . n
+C 1 132 VAL 132 132 132 VAL VAL C . n
+C 1 133 SER 133 133 133 SER SER C . n
+C 1 134 THR 134 134 134 THR THR C . n
+C 1 135 VAL 135 135 135 VAL VAL C . n
+C 1 136 LEU 136 136 136 LEU LEU C . n
+C 1 137 THR 137 137 137 THR THR C . n
+C 1 138 SER 138 138 138 SER SER C . n
+C 1 139 LYS 139 139 139 LYS LYS C . n
+C 1 140 TYR 140 140 140 TYR TYR C . n
+C 1 141 ARG 141 141 141 ARG ARG C . n
+D 2 1   VAL 1   1   1   VAL VAL D . n
+D 2 2   HIS 2   2   2   HIS HIS D . n
+D 2 3   LEU 3   3   3   LEU LEU D . n
+D 2 4   THR 4   4   4   THR THR D . n
+D 2 5   PRO 5   5   5   PRO PRO D . n
+D 2 6   GLU 6   6   6   GLU GLU D . n
+D 2 7   GLU 7   7   7   GLU GLU D . n
+D 2 8   LYS 8   8   8   LYS LYS D . n
+D 2 9   SER 9   9   9   SER SER D . n
+D 2 10  ALA 10  10  10  ALA ALA D . n
+D 2 11  VAL 11  11  11  VAL VAL D . n
+D 2 12  THR 12  12  12  THR THR D . n
+D 2 13  ALA 13  13  13  ALA ALA D . n
+D 2 14  LEU 14  14  14  LEU LEU D . n
+D 2 15  TRP 15  15  15  TRP TRP D . n
+D 2 16  GLY 16  16  16  GLY GLY D . n
+D 2 17  LYS 17  17  17  LYS LYS D . n
+D 2 18  VAL 18  18  18  VAL VAL D . n
+D 2 19  ASN 19  19  19  ASN ASN D . n
+D 2 20  VAL 20  20  20  VAL VAL D . n
+D 2 21  ASP 21  21  21  ASP ASP D . n
+D 2 22  GLU 22  22  22  GLU GLU D . n
+D 2 23  VAL 23  23  23  VAL VAL D . n
+D 2 24  GLY 24  24  24  GLY GLY D . n
+D 2 25  GLY 25  25  25  GLY GLY D . n
+D 2 26  GLU 26  26  26  GLU GLU D . n
+D 2 27  ALA 27  27  27  ALA ALA D . n
+D 2 28  LEU 28  28  28  LEU LEU D . n
+D 2 29  GLY 29  29  29  GLY GLY D . n
+D 2 30  ARG 30  30  30  ARG ARG D . n
+D 2 31  LEU 31  31  31  LEU LEU D . n
+D 2 32  LEU 32  32  32  LEU LEU D . n
+D 2 33  VAL 33  33  33  VAL VAL D . n
+D 2 34  VAL 34  34  34  VAL VAL D . n
+D 2 35  TYR 35  35  35  TYR TYR D . n
+D 2 36  PRO 36  36  36  PRO PRO D . n
+D 2 37  TRP 37  37  37  TRP TRP D . n
+D 2 38  THR 38  38  38  THR THR D . n
+D 2 39  GLN 39  39  39  GLN GLN D . n
+D 2 40  ARG 40  40  40  ARG ARG D . n
+D 2 41  PHE 41  41  41  PHE PHE D . n
+D 2 42  PHE 42  42  42  PHE PHE D . n
+D 2 43  GLU 43  43  43  GLU GLU D . n
+D 2 44  SER 44  44  44  SER SER D . n
+D 2 45  PHE 45  45  45  PHE PHE D . n
+D 2 46  GLY 46  46  46  GLY GLY D . n
+D 2 47  ASP 47  47  47  ASP ASP D . n
+D 2 48  LEU 48  48  48  LEU LEU D . n
+D 2 49  SER 49  49  49  SER SER D . n
+D 2 50  THR 50  50  50  THR THR D . n
+D 2 51  PRO 51  51  51  PRO PRO D . n
+D 2 52  ASP 52  52  52  ASP ASP D . n
+D 2 53  ALA 53  53  53  ALA ALA D . n
+D 2 54  VAL 54  54  54  VAL VAL D . n
+D 2 55  MET 55  55  55  MET MET D . n
+D 2 56  GLY 56  56  56  GLY GLY D . n
+D 2 57  ASN 57  57  57  ASN ASN D . n
+D 2 58  PRO 58  58  58  PRO PRO D . n
+D 2 59  LYS 59  59  59  LYS LYS D . n
+D 2 60  VAL 60  60  60  VAL VAL D . n
+D 2 61  LYS 61  61  61  LYS LYS D . n
+D 2 62  ALA 62  62  62  ALA ALA D . n
+D 2 63  HIS 63  63  63  HIS HIS D . n
+D 2 64  GLY 64  64  64  GLY GLY D . n
+D 2 65  LYS 65  65  65  LYS LYS D . n
+D 2 66  LYS 66  66  66  LYS LYS D . n
+D 2 67  VAL 67  67  67  VAL VAL D . n
+D 2 68  LEU 68  68  68  LEU LEU D . n
+D 2 69  GLY 69  69  69  GLY GLY D . n
+D 2 70  ALA 70  70  70  ALA ALA D . n
+D 2 71  PHE 71  71  71  PHE PHE D . n
+D 2 72  SER 72  72  72  SER SER D . n
+D 2 73  ASP 73  73  73  ASP ASP D . n
+D 2 74  GLY 74  74  74  GLY GLY D . n
+D 2 75  LEU 75  75  75  LEU LEU D . n
+D 2 76  ALA 76  76  76  ALA ALA D . n
+D 2 77  HIS 77  77  77  HIS HIS D . n
+D 2 78  LEU 78  78  78  LEU LEU D . n
+D 2 79  ASP 79  79  79  ASP ASP D . n
+D 2 80  ASN 80  80  80  ASN ASN D . n
+D 2 81  LEU 81  81  81  LEU LEU D . n
+D 2 82  LYS 82  82  82  LYS LYS D . n
+D 2 83  GLY 83  83  83  GLY GLY D . n
+D 2 84  THR 84  84  84  THR THR D . n
+D 2 85  PHE 85  85  85  PHE PHE D . n
+D 2 86  ALA 86  86  86  ALA ALA D . n
+D 2 87  THR 87  87  87  THR THR D . n
+D 2 88  LEU 88  88  88  LEU LEU D . n
+D 2 89  SER 89  89  89  SER SER D . n
+D 2 90  GLU 90  90  90  GLU GLU D . n
+D 2 91  LEU 91  91  91  LEU LEU D . n
+D 2 92  HIS 92  92  92  HIS HIS D . n
+D 2 93  CYS 93  93  93  CYS CYS D . n
+D 2 94  ASP 94  94  94  ASP ASP D . n
+D 2 95  LYS 95  95  95  LYS LYS D . n
+D 2 96  LEU 96  96  96  LEU LEU D . n
+D 2 97  HIS 97  97  97  HIS HIS D . n
+D 2 98  VAL 98  98  98  VAL VAL D . n
+D 2 99  ASP 99  99  99  ASP ASP D . n
+D 2 100 PRO 100 100 100 PRO PRO D . n
+D 2 101 GLU 101 101 101 GLU GLU D . n
+D 2 102 ASN 102 102 102 ASN ASN D . n
+D 2 103 PHE 103 103 103 PHE PHE D . n
+D 2 104 ARG 104 104 104 ARG ARG D . n
+D 2 105 LEU 105 105 105 LEU LEU D . n
+D 2 106 LEU 106 106 106 LEU LEU D . n
+D 2 107 GLY 107 107 107 GLY GLY D . n
+D 2 108 ASN 108 108 108 ASN ASN D . n
+D 2 109 VAL 109 109 109 VAL VAL D . n
+D 2 110 LEU 110 110 110 LEU LEU D . n
+D 2 111 VAL 111 111 111 VAL VAL D . n
+D 2 112 CYS 112 112 112 CYS CYS D . n
+D 2 113 VAL 113 113 113 VAL VAL D . n
+D 2 114 LEU 114 114 114 LEU LEU D . n
+D 2 115 ALA 115 115 115 ALA ALA D . n
+D 2 116 HIS 116 116 116 HIS HIS D . n
+D 2 117 HIS 117 117 117 HIS HIS D . n
+D 2 118 PHE 118 118 118 PHE PHE D . n
+D 2 119 GLY 119 119 119 GLY GLY D . n
+D 2 120 LYS 120 120 120 LYS LYS D . n
+D 2 121 GLU 121 121 121 GLU GLU D . n
+D 2 122 PHE 122 122 122 PHE PHE D . n
+D 2 123 THR 123 123 123 THR THR D . n
+D 2 124 PRO 124 124 124 PRO PRO D . n
+D 2 125 PRO 125 125 125 PRO PRO D . n
+D 2 126 VAL 126 126 126 VAL VAL D . n
+D 2 127 GLN 127 127 127 GLN GLN D . n
+D 2 128 ALA 128 128 128 ALA ALA D . n
+D 2 129 ALA 129 129 129 ALA ALA D . n
+D 2 130 TYR 130 130 130 TYR TYR D . n
+D 2 131 GLN 131 131 131 GLN GLN D . n
+D 2 132 LYS 132 132 132 LYS LYS D . n
+D 2 133 VAL 133 133 133 VAL VAL D . n
+D 2 134 VAL 134 134 134 VAL VAL D . n
+D 2 135 ALA 135 135 135 ALA ALA D . n
+D 2 136 GLY 136 136 136 GLY GLY D . n
+D 2 137 VAL 137 137 137 VAL VAL D . n
+D 2 138 ALA 138 138 138 ALA ALA D . n
+D 2 139 ASN 139 139 139 ASN ASN D . n
+D 2 140 ALA 140 140 140 ALA ALA D . n
+D 2 141 LEU 141 141 141 LEU LEU D . n
+D 2 142 ALA 142 142 142 ALA ALA D . n
+D 2 143 HIS 143 143 143 HIS HIS D . n
+D 2 144 LYS 144 144 144 LYS LYS D . n
+D 2 145 TYR 145 145 145 TYR TYR D . n
+D 2 146 HIS 146 146 146 HIS HIS D . n
+#
+loop_
+_pdbx_nonpoly_scheme.asym_id
+_pdbx_nonpoly_scheme.entity_id
+_pdbx_nonpoly_scheme.mon_id
+_pdbx_nonpoly_scheme.ndb_seq_num
+_pdbx_nonpoly_scheme.pdb_seq_num
+_pdbx_nonpoly_scheme.auth_seq_num
+_pdbx_nonpoly_scheme.pdb_mon_id
+_pdbx_nonpoly_scheme.auth_mon_id
+_pdbx_nonpoly_scheme.pdb_strand_id
+_pdbx_nonpoly_scheme.pdb_ins_code
+E 3 HEM 1  142 1   HEM HEM A .
+F 4 PO4 1  147 2   PO4 PO4 B .
+G 3 HEM 1  148 1   HEM HEM B .
+H 3 HEM 1  142 1   HEM HEM C .
+I 4 PO4 1  147 1   PO4 PO4 D .
+J 3 HEM 1  148 1   HEM HEM D .
+K 5 HOH 1  143 6   HOH HOH A .
+K 5 HOH 2  144 9   HOH HOH A .
+K 5 HOH 3  145 12  HOH HOH A .
+K 5 HOH 4  146 16  HOH HOH A .
+K 5 HOH 5  147 17  HOH HOH A .
+K 5 HOH 6  148 21  HOH HOH A .
+K 5 HOH 7  149 27  HOH HOH A .
+K 5 HOH 8  150 29  HOH HOH A .
+K 5 HOH 9  151 30  HOH HOH A .
+K 5 HOH 10 152 31  HOH HOH A .
+K 5 HOH 11 153 38  HOH HOH A .
+K 5 HOH 12 154 39  HOH HOH A .
+K 5 HOH 13 155 43  HOH HOH A .
+K 5 HOH 14 156 44  HOH HOH A .
+K 5 HOH 15 157 51  HOH HOH A .
+K 5 HOH 16 158 54  HOH HOH A .
+K 5 HOH 17 159 59  HOH HOH A .
+K 5 HOH 18 160 62  HOH HOH A .
+K 5 HOH 19 161 63  HOH HOH A .
+K 5 HOH 20 162 66  HOH HOH A .
+K 5 HOH 21 163 67  HOH HOH A .
+K 5 HOH 22 164 84  HOH HOH A .
+K 5 HOH 23 165 86  HOH HOH A .
+K 5 HOH 24 166 88  HOH HOH A .
+K 5 HOH 25 167 94  HOH HOH A .
+K 5 HOH 26 168 102 HOH HOH A .
+K 5 HOH 27 169 104 HOH HOH A .
+K 5 HOH 28 170 105 HOH HOH A .
+K 5 HOH 29 171 124 HOH HOH A .
+K 5 HOH 30 172 129 HOH HOH A .
+K 5 HOH 31 173 132 HOH HOH A .
+K 5 HOH 32 174 133 HOH HOH A .
+K 5 HOH 33 175 136 HOH HOH A .
+K 5 HOH 34 176 137 HOH HOH A .
+K 5 HOH 35 177 139 HOH HOH A .
+K 5 HOH 36 178 146 HOH HOH A .
+K 5 HOH 37 179 148 HOH HOH A .
+K 5 HOH 38 180 154 HOH HOH A .
+K 5 HOH 39 181 155 HOH HOH A .
+K 5 HOH 40 182 159 HOH HOH A .
+K 5 HOH 41 183 160 HOH HOH A .
+K 5 HOH 42 184 166 HOH HOH A .
+K 5 HOH 43 185 167 HOH HOH A .
+K 5 HOH 44 186 173 HOH HOH A .
+K 5 HOH 45 187 175 HOH HOH A .
+K 5 HOH 46 188 183 HOH HOH A .
+K 5 HOH 47 189 213 HOH HOH A .
+K 5 HOH 48 190 214 HOH HOH A .
+K 5 HOH 49 191 215 HOH HOH A .
+K 5 HOH 50 192 216 HOH HOH A .
+K 5 HOH 51 193 218 HOH HOH A .
+K 5 HOH 52 194 219 HOH HOH A .
+K 5 HOH 53 195 220 HOH HOH A .
+K 5 HOH 54 196 221 HOH HOH A .
+K 5 HOH 55 197 222 HOH HOH A .
+K 5 HOH 56 198 223 HOH HOH A .
+L 5 HOH 1  149 8   HOH HOH B .
+L 5 HOH 2  150 13  HOH HOH B .
+L 5 HOH 3  151 15  HOH HOH B .
+L 5 HOH 4  152 20  HOH HOH B .
+L 5 HOH 5  153 35  HOH HOH B .
+L 5 HOH 6  154 36  HOH HOH B .
+L 5 HOH 7  155 37  HOH HOH B .
+L 5 HOH 8  156 40  HOH HOH B .
+L 5 HOH 9  157 47  HOH HOH B .
+L 5 HOH 10 158 49  HOH HOH B .
+L 5 HOH 11 159 52  HOH HOH B .
+L 5 HOH 12 160 53  HOH HOH B .
+L 5 HOH 13 161 56  HOH HOH B .
+L 5 HOH 14 162 78  HOH HOH B .
+L 5 HOH 15 163 80  HOH HOH B .
+L 5 HOH 16 164 81  HOH HOH B .
+L 5 HOH 17 165 85  HOH HOH B .
+L 5 HOH 18 166 89  HOH HOH B .
+L 5 HOH 19 167 90  HOH HOH B .
+L 5 HOH 20 168 97  HOH HOH B .
+L 5 HOH 21 169 98  HOH HOH B .
+L 5 HOH 22 170 101 HOH HOH B .
+L 5 HOH 23 171 109 HOH HOH B .
+L 5 HOH 24 172 110 HOH HOH B .
+L 5 HOH 25 173 113 HOH HOH B .
+L 5 HOH 26 174 114 HOH HOH B .
+L 5 HOH 27 175 116 HOH HOH B .
+L 5 HOH 28 176 123 HOH HOH B .
+L 5 HOH 29 177 131 HOH HOH B .
+L 5 HOH 30 178 134 HOH HOH B .
+L 5 HOH 31 179 141 HOH HOH B .
+L 5 HOH 32 180 142 HOH HOH B .
+L 5 HOH 33 181 143 HOH HOH B .
+L 5 HOH 34 182 144 HOH HOH B .
+L 5 HOH 35 183 145 HOH HOH B .
+L 5 HOH 36 184 149 HOH HOH B .
+L 5 HOH 37 185 153 HOH HOH B .
+L 5 HOH 38 186 161 HOH HOH B .
+L 5 HOH 39 187 162 HOH HOH B .
+L 5 HOH 40 188 165 HOH HOH B .
+L 5 HOH 41 189 168 HOH HOH B .
+L 5 HOH 42 190 171 HOH HOH B .
+L 5 HOH 43 191 178 HOH HOH B .
+L 5 HOH 44 192 179 HOH HOH B .
+L 5 HOH 45 193 200 HOH HOH B .
+L 5 HOH 46 194 201 HOH HOH B .
+L 5 HOH 47 195 202 HOH HOH B .
+L 5 HOH 48 196 203 HOH HOH B .
+L 5 HOH 49 197 204 HOH HOH B .
+L 5 HOH 50 198 205 HOH HOH B .
+L 5 HOH 51 199 206 HOH HOH B .
+L 5 HOH 52 200 207 HOH HOH B .
+L 5 HOH 53 201 208 HOH HOH B .
+L 5 HOH 54 202 209 HOH HOH B .
+L 5 HOH 55 203 210 HOH HOH B .
+L 5 HOH 56 204 211 HOH HOH B .
+L 5 HOH 57 205 212 HOH HOH B .
+M 5 HOH 1  143 4   HOH HOH C .
+M 5 HOH 2  144 5   HOH HOH C .
+M 5 HOH 3  145 10  HOH HOH C .
+M 5 HOH 4  146 14  HOH HOH C .
+M 5 HOH 5  147 18  HOH HOH C .
+M 5 HOH 6  148 19  HOH HOH C .
+M 5 HOH 7  149 22  HOH HOH C .
+M 5 HOH 8  150 25  HOH HOH C .
+M 5 HOH 9  151 26  HOH HOH C .
+M 5 HOH 10 152 28  HOH HOH C .
+M 5 HOH 11 153 32  HOH HOH C .
+M 5 HOH 12 154 33  HOH HOH C .
+M 5 HOH 13 155 41  HOH HOH C .
+M 5 HOH 14 156 45  HOH HOH C .
+M 5 HOH 15 157 48  HOH HOH C .
+M 5 HOH 16 158 55  HOH HOH C .
+M 5 HOH 17 159 58  HOH HOH C .
+M 5 HOH 18 160 64  HOH HOH C .
+M 5 HOH 19 161 68  HOH HOH C .
+M 5 HOH 20 162 69  HOH HOH C .
+M 5 HOH 21 163 70  HOH HOH C .
+M 5 HOH 22 164 71  HOH HOH C .
+M 5 HOH 23 165 72  HOH HOH C .
+M 5 HOH 24 166 74  HOH HOH C .
+M 5 HOH 25 167 79  HOH HOH C .
+M 5 HOH 26 168 82  HOH HOH C .
+M 5 HOH 27 169 83  HOH HOH C .
+M 5 HOH 28 170 91  HOH HOH C .
+M 5 HOH 29 171 92  HOH HOH C .
+M 5 HOH 30 172 96  HOH HOH C .
+M 5 HOH 31 173 108 HOH HOH C .
+M 5 HOH 32 174 112 HOH HOH C .
+M 5 HOH 33 175 115 HOH HOH C .
+M 5 HOH 34 176 119 HOH HOH C .
+M 5 HOH 35 177 122 HOH HOH C .
+M 5 HOH 36 178 125 HOH HOH C .
+M 5 HOH 37 179 126 HOH HOH C .
+M 5 HOH 38 180 127 HOH HOH C .
+M 5 HOH 39 181 135 HOH HOH C .
+M 5 HOH 40 182 140 HOH HOH C .
+M 5 HOH 41 183 150 HOH HOH C .
+M 5 HOH 42 184 151 HOH HOH C .
+M 5 HOH 43 185 152 HOH HOH C .
+M 5 HOH 44 186 156 HOH HOH C .
+M 5 HOH 45 187 164 HOH HOH C .
+M 5 HOH 46 188 172 HOH HOH C .
+M 5 HOH 47 189 174 HOH HOH C .
+M 5 HOH 48 190 177 HOH HOH C .
+M 5 HOH 49 191 180 HOH HOH C .
+M 5 HOH 50 192 181 HOH HOH C .
+M 5 HOH 51 193 184 HOH HOH C .
+M 5 HOH 52 194 192 HOH HOH C .
+M 5 HOH 53 195 193 HOH HOH C .
+M 5 HOH 54 196 194 HOH HOH C .
+M 5 HOH 55 197 195 HOH HOH C .
+M 5 HOH 56 198 196 HOH HOH C .
+M 5 HOH 57 199 197 HOH HOH C .
+M 5 HOH 58 200 198 HOH HOH C .
+M 5 HOH 59 201 199 HOH HOH C .
+N 5 HOH 1  149 3   HOH HOH D .
+N 5 HOH 2  150 7   HOH HOH D .
+N 5 HOH 3  151 11  HOH HOH D .
+N 5 HOH 4  152 23  HOH HOH D .
+N 5 HOH 5  153 24  HOH HOH D .
+N 5 HOH 6  154 34  HOH HOH D .
+N 5 HOH 7  155 42  HOH HOH D .
+N 5 HOH 8  156 46  HOH HOH D .
+N 5 HOH 9  157 50  HOH HOH D .
+N 5 HOH 10 158 57  HOH HOH D .
+N 5 HOH 11 159 60  HOH HOH D .
+N 5 HOH 12 160 61  HOH HOH D .
+N 5 HOH 13 161 65  HOH HOH D .
+N 5 HOH 14 162 73  HOH HOH D .
+N 5 HOH 15 163 75  HOH HOH D .
+N 5 HOH 16 164 76  HOH HOH D .
+N 5 HOH 17 165 77  HOH HOH D .
+N 5 HOH 18 166 87  HOH HOH D .
+N 5 HOH 19 167 93  HOH HOH D .
+N 5 HOH 20 168 95  HOH HOH D .
+N 5 HOH 21 169 99  HOH HOH D .
+N 5 HOH 22 170 100 HOH HOH D .
+N 5 HOH 23 171 103 HOH HOH D .
+N 5 HOH 24 172 106 HOH HOH D .
+N 5 HOH 25 173 107 HOH HOH D .
+N 5 HOH 26 174 111 HOH HOH D .
+N 5 HOH 27 175 117 HOH HOH D .
+N 5 HOH 28 176 118 HOH HOH D .
+N 5 HOH 29 177 120 HOH HOH D .
+N 5 HOH 30 178 121 HOH HOH D .
+N 5 HOH 31 179 128 HOH HOH D .
+N 5 HOH 32 180 130 HOH HOH D .
+N 5 HOH 33 181 138 HOH HOH D .
+N 5 HOH 34 182 147 HOH HOH D .
+N 5 HOH 35 183 157 HOH HOH D .
+N 5 HOH 36 184 158 HOH HOH D .
+N 5 HOH 37 185 163 HOH HOH D .
+N 5 HOH 38 186 169 HOH HOH D .
+N 5 HOH 39 187 170 HOH HOH D .
+N 5 HOH 40 188 176 HOH HOH D .
+N 5 HOH 41 189 182 HOH HOH D .
+N 5 HOH 42 190 185 HOH HOH D .
+N 5 HOH 43 191 186 HOH HOH D .
+N 5 HOH 44 192 187 HOH HOH D .
+N 5 HOH 45 193 188 HOH HOH D .
+N 5 HOH 46 194 189 HOH HOH D .
+N 5 HOH 47 195 190 HOH HOH D .
+N 5 HOH 48 196 191 HOH HOH D .
+N 5 HOH 49 197 217 HOH HOH D .
+#
+loop_
+_pdbx_unobs_or_zero_occ_atoms.id
+_pdbx_unobs_or_zero_occ_atoms.PDB_model_num
+_pdbx_unobs_or_zero_occ_atoms.polymer_flag
+_pdbx_unobs_or_zero_occ_atoms.occupancy_flag
+_pdbx_unobs_or_zero_occ_atoms.auth_asym_id
+_pdbx_unobs_or_zero_occ_atoms.auth_comp_id
+_pdbx_unobs_or_zero_occ_atoms.auth_seq_id
+_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code
+_pdbx_unobs_or_zero_occ_atoms.auth_atom_id
+_pdbx_unobs_or_zero_occ_atoms.label_alt_id
+_pdbx_unobs_or_zero_occ_atoms.label_asym_id
+_pdbx_unobs_or_zero_occ_atoms.label_comp_id
+_pdbx_unobs_or_zero_occ_atoms.label_seq_id
+_pdbx_unobs_or_zero_occ_atoms.label_atom_id
+1 1 N 1 B PO4 147 ? O1 ? F PO4 1 O1
+2 1 N 1 B PO4 147 ? O2 ? F PO4 1 O2
+3 1 N 1 B PO4 147 ? O3 ? F PO4 1 O3
+4 1 N 1 B PO4 147 ? O4 ? F PO4 1 O4
+5 1 N 1 D PO4 147 ? O1 ? I PO4 1 O1
+6 1 N 1 D PO4 147 ? O2 ? I PO4 1 O2
+7 1 N 1 D PO4 147 ? O3 ? I PO4 1 O3
+8 1 N 1 D PO4 147 ? O4 ? I PO4 1 O4
+#
+_cell.entry_id           4HHB
+_cell.length_a           63.150
+_cell.length_b           83.590
+_cell.length_c           53.800
+_cell.angle_alpha        90.00
+_cell.angle_beta         99.34
+_cell.angle_gamma        90.00
+_cell.Z_PDB              4
+_cell.pdbx_unique_axis   ?
+#
+_symmetry.entry_id                         4HHB
+_symmetry.space_group_name_H-M             'P 1 21 1'
+_symmetry.pdbx_full_space_group_name_H-M   ?
+_symmetry.cell_setting                     ?
+_symmetry.Int_Tables_number                4
+#
+_exptl.entry_id          4HHB
+_exptl.method            'X-RAY DIFFRACTION'
+_exptl.crystals_number   ?
+#
+_exptl_crystal.id                    1
+_exptl_crystal.density_meas          ?
+_exptl_crystal.density_Matthews      2.26
+_exptl_crystal.density_percent_sol   45.48
+_exptl_crystal.description           ?
+_exptl_crystal.preparation           ?
+#
+_diffrn.id                               1
+_diffrn.crystal_id                       1
+_diffrn.ambient_temp                     ?
+_diffrn.ambient_temp_details             ?
+_diffrn.pdbx_serial_crystal_experiment   ?
+#
+_refine.entry_id                                 4HHB
+_refine.ls_number_reflns_obs                     ?
+_refine.ls_number_reflns_all                     ?
+_refine.pdbx_ls_sigma_I                          ?
+_refine.pdbx_ls_sigma_F                          ?
+_refine.pdbx_data_cutoff_high_absF               ?
+_refine.pdbx_data_cutoff_low_absF                ?
+_refine.pdbx_data_cutoff_high_rms_absF           ?
+_refine.ls_d_res_low                             ?
+_refine.ls_d_res_high                            1.74
+_refine.ls_percent_reflns_obs                    ?
+_refine.ls_R_factor_obs                          ?
+_refine.ls_R_factor_all                          ?
+_refine.ls_R_factor_R_work                       0.1350000
+_refine.ls_R_factor_R_free                       ?
+_refine.ls_R_factor_R_free_error                 ?
+_refine.ls_R_factor_R_free_error_details         ?
+_refine.ls_percent_reflns_R_free                 ?
+_refine.ls_number_reflns_R_free                  ?
+_refine.ls_number_parameters                     ?
+_refine.ls_number_restraints                     ?
+_refine.occupancy_min                            ?
+_refine.occupancy_max                            ?
+_refine.B_iso_mean                               ?
+_refine.aniso_B[1][1]                            ?
+_refine.aniso_B[2][2]                            ?
+_refine.aniso_B[3][3]                            ?
+_refine.aniso_B[1][2]                            ?
+_refine.aniso_B[1][3]                            ?
+_refine.aniso_B[2][3]                            ?
+_refine.solvent_model_details                    ?
+_refine.solvent_model_param_ksol                 ?
+_refine.solvent_model_param_bsol                 ?
+_refine.pdbx_ls_cross_valid_method               ?
+_refine.details
+;THE COORDINATES GIVEN HERE ARE IN THE ORTHOGONAL ANGSTROM
+SYSTEM STANDARD FOR HEMOGLOBINS. THE Y AXIS IS THE
+(NON CRYSTALLOGRAPHIC) MOLECULAR DIAD AND THE X AXIS IS THE
+PSEUDO DIAD WHICH RELATES THE ALPHA-1 AND BETA-1 CHAINS.
+THE TRANSFORMATION GIVEN IN THE *MTRIX* RECORDS BELOW
+WILL GENERATE COORDINATES FOR THE *C* AND *D* CHAINS FROM
+THE *A* AND *B* CHAINS RESPECTIVELY.
+;
+_refine.pdbx_starting_model                      ?
+_refine.pdbx_method_to_determine_struct          ?
+_refine.pdbx_isotropic_thermal_model             ?
+_refine.pdbx_stereochemistry_target_values       ?
+_refine.pdbx_stereochem_target_val_spec_case     ?
+_refine.pdbx_R_Free_selection_details            ?
+_refine.pdbx_overall_ESU_R                       ?
+_refine.pdbx_overall_ESU_R_Free                  ?
+_refine.overall_SU_ML                            ?
+_refine.overall_SU_B                             ?
+_refine.pdbx_refine_id                           'X-RAY DIFFRACTION'
+_refine.pdbx_diffrn_id                           1
+_refine.pdbx_TLS_residual_ADP_flag               ?
+_refine.correlation_coeff_Fo_to_Fc               ?
+_refine.correlation_coeff_Fo_to_Fc_free          ?
+_refine.pdbx_solvent_vdw_probe_radii             ?
+_refine.pdbx_solvent_ion_probe_radii             ?
+_refine.pdbx_solvent_shrinkage_radii             ?
+_refine.pdbx_overall_phase_error                 ?
+_refine.overall_SU_R_Cruickshank_DPI             ?
+_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ?
+_refine.pdbx_overall_SU_R_Blow_DPI               ?
+_refine.pdbx_overall_SU_R_free_Blow_DPI          ?
+#
+_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION'
+_refine_hist.cycle_id                         LAST
+_refine_hist.pdbx_number_atoms_protein        4384
+_refine_hist.pdbx_number_atoms_nucleic_acid   0
+_refine_hist.pdbx_number_atoms_ligand         174
+_refine_hist.number_atoms_solvent             221
+_refine_hist.number_atoms_total               4779
+_refine_hist.d_res_high                       1.74
+_refine_hist.d_res_low                        .
+#
+_struct_ncs_oper.id             1
+_struct_ncs_oper.code           given
+_struct_ncs_oper.details        ?
+_struct_ncs_oper.matrix[1][1]   -0.952899
+_struct_ncs_oper.matrix[1][2]   0.301963
+_struct_ncs_oper.matrix[1][3]   -0.028045
+_struct_ncs_oper.vector[1]      17.049680
+_struct_ncs_oper.matrix[2][1]   0.302014
+_struct_ncs_oper.matrix[2][2]   0.936202
+_struct_ncs_oper.matrix[2][3]   -0.179824
+_struct_ncs_oper.vector[2]      4.936040
+_struct_ncs_oper.matrix[3][1]   -0.028043
+_struct_ncs_oper.matrix[3][2]   -0.179784
+_struct_ncs_oper.matrix[3][3]   -0.983303
+_struct_ncs_oper.vector[3]      81.782290
+#
+_database_PDB_matrix.entry_id          4HHB
+_database_PDB_matrix.origx[1][1]       0.985646
+_database_PDB_matrix.origx[1][2]       -0.158954
+_database_PDB_matrix.origx[1][3]       -0.056388
+_database_PDB_matrix.origx_vector[1]   -5.704395
+_database_PDB_matrix.origx[2][1]       0.153472
+_database_PDB_matrix.origx[2][2]       0.983904
+_database_PDB_matrix.origx[2][3]       -0.091380
+_database_PDB_matrix.origx_vector[2]   -11.435287
+_database_PDB_matrix.origx[3][1]       0.069996
+_database_PDB_matrix.origx[3][2]       0.081402
+_database_PDB_matrix.origx[3][3]       0.994230
+_database_PDB_matrix.origx_vector[3]   -41.452811
+#
+_struct.entry_id                  4HHB
+_struct.title                     'THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS RESOLUTION'
+_struct.pdbx_model_details        ?
+_struct.pdbx_CASP_flag            ?
+_struct.pdbx_model_type_details   ?
+#
+_struct_keywords.entry_id        4HHB
+_struct_keywords.pdbx_keywords   'OXYGEN TRANSPORT'
+_struct_keywords.text            'OXYGEN TRANSPORT'
+#
+loop_
+_struct_asym.id
+_struct_asym.pdbx_blank_PDB_chainid_flag
+_struct_asym.pdbx_modified
+_struct_asym.entity_id
+_struct_asym.details
+A N N 1 ?
+B N N 2 ?
+C N N 1 ?
+D N N 2 ?
+E N N 3 ?
+F N N 4 ?
+G N N 3 ?
+H N N 3 ?
+I N N 4 ?
+J N N 3 ?
+K N N 5 ?
+L N N 5 ?
+M N N 5 ?
+N N N 5 ?
+#
+loop_
+_struct_ref.id
+_struct_ref.db_name
+_struct_ref.db_code
+_struct_ref.pdbx_db_accession
+_struct_ref.pdbx_db_isoform
+_struct_ref.entity_id
+_struct_ref.pdbx_seq_one_letter_code
+_struct_ref.pdbx_align_begin
+1 UNP HBA_HUMAN P69905 ? 1
+;VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL
+SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
+;
+2
+2 UNP HBB_HUMAN P68871 ? 2
+;VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN
+LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
+;
+2
+#
+loop_
+_struct_ref_seq.align_id
+_struct_ref_seq.ref_id
+_struct_ref_seq.pdbx_PDB_id_code
+_struct_ref_seq.pdbx_strand_id
+_struct_ref_seq.seq_align_beg
+_struct_ref_seq.pdbx_seq_align_beg_ins_code
+_struct_ref_seq.seq_align_end
+_struct_ref_seq.pdbx_seq_align_end_ins_code
+_struct_ref_seq.pdbx_db_accession
+_struct_ref_seq.db_align_beg
+_struct_ref_seq.pdbx_db_align_beg_ins_code
+_struct_ref_seq.db_align_end
+_struct_ref_seq.pdbx_db_align_end_ins_code
+_struct_ref_seq.pdbx_auth_seq_align_beg
+_struct_ref_seq.pdbx_auth_seq_align_end
+1 1 4HHB A 1 ? 141 ? P69905 2 ? 142 ? 1 141
+2 2 4HHB B 1 ? 146 ? P68871 2 ? 147 ? 1 146
+3 1 4HHB C 1 ? 141 ? P69905 2 ? 142 ? 1 141
+4 2 4HHB D 1 ? 146 ? P68871 2 ? 147 ? 1 146
+#
+_pdbx_struct_assembly.id                   1
+_pdbx_struct_assembly.details              author_and_software_defined_assembly
+_pdbx_struct_assembly.method_details       PISA
+_pdbx_struct_assembly.oligomeric_details   tetrameric
+_pdbx_struct_assembly.oligomeric_count     4
+#
+loop_
+_pdbx_struct_assembly_prop.biol_id
+_pdbx_struct_assembly_prop.type
+_pdbx_struct_assembly_prop.value
+_pdbx_struct_assembly_prop.details
+1 'ABSA (A^2)' 11630 ?
+1 MORE         -98   ?
+1 'SSA (A^2)'  24010 ?
+#
+_pdbx_struct_assembly_gen.assembly_id       1
+_pdbx_struct_assembly_gen.oper_expression   1
+_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N
+#
+_pdbx_struct_oper_list.id                   1
+_pdbx_struct_oper_list.type                 'identity operation'
+_pdbx_struct_oper_list.name                 1_555
+_pdbx_struct_oper_list.symmetry_operation   x,y,z
+_pdbx_struct_oper_list.matrix[1][1]         1.0000000000
+_pdbx_struct_oper_list.matrix[1][2]         0.0000000000
+_pdbx_struct_oper_list.matrix[1][3]         0.0000000000
+_pdbx_struct_oper_list.vector[1]            0.0000000000
+_pdbx_struct_oper_list.matrix[2][1]         0.0000000000
+_pdbx_struct_oper_list.matrix[2][2]         1.0000000000
+_pdbx_struct_oper_list.matrix[2][3]         0.0000000000
+_pdbx_struct_oper_list.vector[2]            0.0000000000
+_pdbx_struct_oper_list.matrix[3][1]         0.0000000000
+_pdbx_struct_oper_list.matrix[3][2]         0.0000000000
+_pdbx_struct_oper_list.matrix[3][3]         1.0000000000
+_pdbx_struct_oper_list.vector[3]            0.0000000000
+#
+loop_
+_struct_conf.conf_type_id
+_struct_conf.id
+_struct_conf.pdbx_PDB_helix_id
+_struct_conf.beg_label_comp_id
+_struct_conf.beg_label_asym_id
+_struct_conf.beg_label_seq_id
+_struct_conf.pdbx_beg_PDB_ins_code
+_struct_conf.end_label_comp_id
+_struct_conf.end_label_asym_id
+_struct_conf.end_label_seq_id
+_struct_conf.pdbx_end_PDB_ins_code
+_struct_conf.beg_auth_comp_id
+_struct_conf.beg_auth_asym_id
+_struct_conf.beg_auth_seq_id
+_struct_conf.end_auth_comp_id
+_struct_conf.end_auth_asym_id
+_struct_conf.end_auth_seq_id
+_struct_conf.pdbx_PDB_helix_class
+_struct_conf.details
+_struct_conf.pdbx_PDB_helix_length
+HELX_P HELX_P1  AA SER A 3   ? GLY A 18  ? SER A 3   GLY A 18  1 ?                              16
+HELX_P HELX_P2  AB HIS A 20  ? SER A 35  ? HIS A 20  SER A 35  1 ?                              16
+HELX_P HELX_P3  AC PHE A 36  ? TYR A 42  ? PHE A 36  TYR A 42  1 ?                              7
+HELX_P HELX_P4  AD HIS A 50  ? GLY A 51  ? HIS A 50  GLY A 51  1 'DEGEN 2 RES HLX RETAIN HOMOL' 2
+HELX_P HELX_P5  AE SER A 52  ? ALA A 71  ? SER A 52  ALA A 71  1 ?                              20
+HELX_P HELX_P6  AF LEU A 80  ? ALA A 88  ? LEU A 80  ALA A 88  1 ?                              9
+HELX_P HELX_P7  AG ASP A 94  ? HIS A 112 ? ASP A 94  HIS A 112 1 ?                              19
+HELX_P HELX_P8  AH THR A 118 ? SER A 138 ? THR A 118 SER A 138 1 ?                              21
+HELX_P HELX_P9  BA THR B 4   ? VAL B 18  ? THR B 4   VAL B 18  1 ?                              15
+HELX_P HELX_P10 BB ASN B 19  ? VAL B 34  ? ASN B 19  VAL B 34  1 ?                              16
+HELX_P HELX_P11 BC TYR B 35  ? PHE B 41  ? TYR B 35  PHE B 41  1 ?                              7
+HELX_P HELX_P12 BD THR B 50  ? GLY B 56  ? THR B 50  GLY B 56  1 ?                              7
+HELX_P HELX_P13 BE ASN B 57  ? ALA B 76  ? ASN B 57  ALA B 76  1 ?                              20
+HELX_P HELX_P14 BF PHE B 85  ? CYS B 93  ? PHE B 85  CYS B 93  1 ?                              9
+HELX_P HELX_P15 BG ASP B 99  ? HIS B 117 ? ASP B 99  HIS B 117 1 ?                              19
+HELX_P HELX_P16 BH THR B 123 ? HIS B 143 ? THR B 123 HIS B 143 1 ?                              21
+HELX_P HELX_P17 CA SER C 3   ? GLY C 18  ? SER C 3   GLY C 18  1 ?                              16
+HELX_P HELX_P18 CB HIS C 20  ? SER C 35  ? HIS C 20  SER C 35  1 ?                              16
+HELX_P HELX_P19 CC PHE C 36  ? TYR C 42  ? PHE C 36  TYR C 42  1 ?                              7
+HELX_P HELX_P20 CD HIS C 50  ? GLY C 51  ? HIS C 50  GLY C 51  1 'DEGEN 2 RES HLX RETAIN HOMOL' 2
+HELX_P HELX_P21 CE SER C 52  ? ALA C 71  ? SER C 52  ALA C 71  1 ?                              20
+HELX_P HELX_P22 CF LEU C 80  ? ALA C 88  ? LEU C 80  ALA C 88  1 ?                              9
+HELX_P HELX_P23 CG ASP C 94  ? HIS C 112 ? ASP C 94  HIS C 112 1 ?                              19
+HELX_P HELX_P24 CH THR C 118 ? SER C 138 ? THR C 118 SER C 138 1 ?                              21
+HELX_P HELX_P25 DA THR D 4   ? VAL D 18  ? THR D 4   VAL D 18  1 ?                              15
+HELX_P HELX_P26 DB ASN D 19  ? VAL D 34  ? ASN D 19  VAL D 34  1 ?                              16
+HELX_P HELX_P27 DC TYR D 35  ? PHE D 41  ? TYR D 35  PHE D 41  1 ?                              7
+HELX_P HELX_P28 DD THR D 50  ? GLY D 56  ? THR D 50  GLY D 56  1 ?                              7
+HELX_P HELX_P29 DE ASN D 57  ? ALA D 76  ? ASN D 57  ALA D 76  1 ?                              20
+HELX_P HELX_P30 DF PHE D 85  ? CYS D 93  ? PHE D 85  CYS D 93  1 ?                              9
+HELX_P HELX_P31 DG ASP D 99  ? HIS D 117 ? ASP D 99  HIS D 117 1 ?                              19
+HELX_P HELX_P32 DH THR D 123 ? HIS D 143 ? THR D 123 HIS D 143 1 ?                              21
+#
+_struct_conf_type.id          HELX_P
+_struct_conf_type.criteria    ?
+_struct_conf_type.reference   ?
+#
+loop_
+_struct_conn.id
+_struct_conn.conn_type_id
+_struct_conn.pdbx_leaving_atom_flag
+_struct_conn.pdbx_PDB_id
+_struct_conn.ptnr1_label_asym_id
+_struct_conn.ptnr1_label_comp_id
+_struct_conn.ptnr1_label_seq_id
+_struct_conn.ptnr1_label_atom_id
+_struct_conn.pdbx_ptnr1_label_alt_id
+_struct_conn.pdbx_ptnr1_PDB_ins_code
+_struct_conn.pdbx_ptnr1_standard_comp_id
+_struct_conn.ptnr1_symmetry
+_struct_conn.ptnr2_label_asym_id
+_struct_conn.ptnr2_label_comp_id
+_struct_conn.ptnr2_label_seq_id
+_struct_conn.ptnr2_label_atom_id
+_struct_conn.pdbx_ptnr2_label_alt_id
+_struct_conn.pdbx_ptnr2_PDB_ins_code
+_struct_conn.ptnr1_auth_asym_id
+_struct_conn.ptnr1_auth_comp_id
+_struct_conn.ptnr1_auth_seq_id
+_struct_conn.ptnr2_auth_asym_id
+_struct_conn.ptnr2_auth_comp_id
+_struct_conn.ptnr2_auth_seq_id
+_struct_conn.ptnr2_symmetry
+_struct_conn.pdbx_ptnr3_label_atom_id
+_struct_conn.pdbx_ptnr3_label_seq_id
+_struct_conn.pdbx_ptnr3_label_comp_id
+_struct_conn.pdbx_ptnr3_label_asym_id
+_struct_conn.pdbx_ptnr3_label_alt_id
+_struct_conn.pdbx_ptnr3_PDB_ins_code
+_struct_conn.details
+_struct_conn.pdbx_dist_value
+_struct_conn.pdbx_value_order
+_struct_conn.pdbx_role
+metalc1 metalc ? ? A HIS 87 NE2 ? ? ? 1_555 E HEM . FE ? ? A HIS 87 A HEM 142 1_555 ? ? ? ? ? ? ? 2.143 ? ?
+metalc2 metalc ? ? B HIS 92 NE2 ? ? ? 1_555 G HEM . FE ? ? B HIS 92 B HEM 148 1_555 ? ? ? ? ? ? ? 2.222 ? ?
+metalc3 metalc ? ? C HIS 87 NE2 ? ? ? 1_555 H HEM . FE ? ? C HIS 87 C HEM 142 1_555 ? ? ? ? ? ? ? 2.258 ? ?
+metalc4 metalc ? ? D HIS 92 NE2 ? ? ? 1_555 J HEM . FE ? ? D HIS 92 D HEM 148 1_555 ? ? ? ? ? ? ? 1.982 ? ?
+#
+_struct_conn_type.id          metalc
+_struct_conn_type.criteria    ?
+_struct_conn_type.reference   ?
+#
+loop_
+_pdbx_struct_conn_angle.id
+_pdbx_struct_conn_angle.ptnr1_label_atom_id
+_pdbx_struct_conn_angle.ptnr1_label_alt_id
+_pdbx_struct_conn_angle.ptnr1_label_asym_id
+_pdbx_struct_conn_angle.ptnr1_label_comp_id
+_pdbx_struct_conn_angle.ptnr1_label_seq_id
+_pdbx_struct_conn_angle.ptnr1_auth_atom_id
+_pdbx_struct_conn_angle.ptnr1_auth_asym_id
+_pdbx_struct_conn_angle.ptnr1_auth_comp_id
+_pdbx_struct_conn_angle.ptnr1_auth_seq_id
+_pdbx_struct_conn_angle.ptnr1_PDB_ins_code
+_pdbx_struct_conn_angle.ptnr1_symmetry
+_pdbx_struct_conn_angle.ptnr2_label_atom_id
+_pdbx_struct_conn_angle.ptnr2_label_alt_id
+_pdbx_struct_conn_angle.ptnr2_label_asym_id
+_pdbx_struct_conn_angle.ptnr2_label_comp_id
+_pdbx_struct_conn_angle.ptnr2_label_seq_id
+_pdbx_struct_conn_angle.ptnr2_auth_atom_id
+_pdbx_struct_conn_angle.ptnr2_auth_asym_id
+_pdbx_struct_conn_angle.ptnr2_auth_comp_id
+_pdbx_struct_conn_angle.ptnr2_auth_seq_id
+_pdbx_struct_conn_angle.ptnr2_PDB_ins_code
+_pdbx_struct_conn_angle.ptnr2_symmetry
+_pdbx_struct_conn_angle.ptnr3_label_atom_id
+_pdbx_struct_conn_angle.ptnr3_label_alt_id
+_pdbx_struct_conn_angle.ptnr3_label_asym_id
+_pdbx_struct_conn_angle.ptnr3_label_comp_id
+_pdbx_struct_conn_angle.ptnr3_label_seq_id
+_pdbx_struct_conn_angle.ptnr3_auth_atom_id
+_pdbx_struct_conn_angle.ptnr3_auth_asym_id
+_pdbx_struct_conn_angle.ptnr3_auth_comp_id
+_pdbx_struct_conn_angle.ptnr3_auth_seq_id
+_pdbx_struct_conn_angle.ptnr3_PDB_ins_code
+_pdbx_struct_conn_angle.ptnr3_symmetry
+_pdbx_struct_conn_angle.value
+_pdbx_struct_conn_angle.value_esd
+1  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? E HEM . ? A HEM 142 ? 1_555 NA ? E HEM . ? A HEM 142 ? 1_555 100.8 ?
+2  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? E HEM . ? A HEM 142 ? 1_555 NB ? E HEM . ? A HEM 142 ? 1_555 100.3 ?
+3  NA  ? E HEM .  ? A HEM 142 ? 1_555 FE ? E HEM . ? A HEM 142 ? 1_555 NB ? E HEM . ? A HEM 142 ? 1_555 86.2  ?
+4  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? E HEM . ? A HEM 142 ? 1_555 NC ? E HEM . ? A HEM 142 ? 1_555 104.6 ?
+5  NA  ? E HEM .  ? A HEM 142 ? 1_555 FE ? E HEM . ? A HEM 142 ? 1_555 NC ? E HEM . ? A HEM 142 ? 1_555 154.5 ?
+6  NB  ? E HEM .  ? A HEM 142 ? 1_555 FE ? E HEM . ? A HEM 142 ? 1_555 NC ? E HEM . ? A HEM 142 ? 1_555 88.3  ?
+7  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? E HEM . ? A HEM 142 ? 1_555 ND ? E HEM . ? A HEM 142 ? 1_555 106.5 ?
+8  NA  ? E HEM .  ? A HEM 142 ? 1_555 FE ? E HEM . ? A HEM 142 ? 1_555 ND ? E HEM . ? A HEM 142 ? 1_555 90.2  ?
+9  NB  ? E HEM .  ? A HEM 142 ? 1_555 FE ? E HEM . ? A HEM 142 ? 1_555 ND ? E HEM . ? A HEM 142 ? 1_555 153.2 ?
+10 NC  ? E HEM .  ? A HEM 142 ? 1_555 FE ? E HEM . ? A HEM 142 ? 1_555 ND ? E HEM . ? A HEM 142 ? 1_555 83.6  ?
+11 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? G HEM . ? B HEM 148 ? 1_555 NA ? G HEM . ? B HEM 148 ? 1_555 97.7  ?
+12 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? G HEM . ? B HEM 148 ? 1_555 NB ? G HEM . ? B HEM 148 ? 1_555 97.1  ?
+13 NA  ? G HEM .  ? B HEM 148 ? 1_555 FE ? G HEM . ? B HEM 148 ? 1_555 NB ? G HEM . ? B HEM 148 ? 1_555 88.7  ?
+14 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? G HEM . ? B HEM 148 ? 1_555 NC ? G HEM . ? B HEM 148 ? 1_555 104.0 ?
+15 NA  ? G HEM .  ? B HEM 148 ? 1_555 FE ? G HEM . ? B HEM 148 ? 1_555 NC ? G HEM . ? B HEM 148 ? 1_555 158.2 ?
+16 NB  ? G HEM .  ? B HEM 148 ? 1_555 FE ? G HEM . ? B HEM 148 ? 1_555 NC ? G HEM . ? B HEM 148 ? 1_555 90.0  ?
+17 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? G HEM . ? B HEM 148 ? 1_555 ND ? G HEM . ? B HEM 148 ? 1_555 103.6 ?
+18 NA  ? G HEM .  ? B HEM 148 ? 1_555 FE ? G HEM . ? B HEM 148 ? 1_555 ND ? G HEM . ? B HEM 148 ? 1_555 91.0  ?
+19 NB  ? G HEM .  ? B HEM 148 ? 1_555 FE ? G HEM . ? B HEM 148 ? 1_555 ND ? G HEM . ? B HEM 148 ? 1_555 159.1 ?
+20 NC  ? G HEM .  ? B HEM 148 ? 1_555 FE ? G HEM . ? B HEM 148 ? 1_555 ND ? G HEM . ? B HEM 148 ? 1_555 82.6  ?
+21 NE2 ? C HIS 87 ? C HIS 87  ? 1_555 FE ? H HEM . ? C HEM 142 ? 1_555 NA ? H HEM . ? C HEM 142 ? 1_555 92.2  ?
+22 NE2 ? C HIS 87 ? C HIS 87  ? 1_555 FE ? H HEM . ? C HEM 142 ? 1_555 NB ? H HEM . ? C HEM 142 ? 1_555 93.3  ?
+23 NA  ? H HEM .  ? C HEM 142 ? 1_555 FE ? H HEM . ? C HEM 142 ? 1_555 NB ? H HEM . ? C HEM 142 ? 1_555 83.8  ?
+24 NE2 ? C HIS 87 ? C HIS 87  ? 1_555 FE ? H HEM . ? C HEM 142 ? 1_555 NC ? H HEM . ? C HEM 142 ? 1_555 105.8 ?
+25 NA  ? H HEM .  ? C HEM 142 ? 1_555 FE ? H HEM . ? C HEM 142 ? 1_555 NC ? H HEM . ? C HEM 142 ? 1_555 162.0 ?
+26 NB  ? H HEM .  ? C HEM 142 ? 1_555 FE ? H HEM . ? C HEM 142 ? 1_555 NC ? H HEM . ? C HEM 142 ? 1_555 94.8  ?
+27 NE2 ? C HIS 87 ? C HIS 87  ? 1_555 FE ? H HEM . ? C HEM 142 ? 1_555 ND ? H HEM . ? C HEM 142 ? 1_555 103.5 ?
+28 NA  ? H HEM .  ? C HEM 142 ? 1_555 FE ? H HEM . ? C HEM 142 ? 1_555 ND ? H HEM . ? C HEM 142 ? 1_555 88.9  ?
+29 NB  ? H HEM .  ? C HEM 142 ? 1_555 FE ? H HEM . ? C HEM 142 ? 1_555 ND ? H HEM . ? C HEM 142 ? 1_555 161.9 ?
+30 NC  ? H HEM .  ? C HEM 142 ? 1_555 FE ? H HEM . ? C HEM 142 ? 1_555 ND ? H HEM . ? C HEM 142 ? 1_555 87.1  ?
+31 NE2 ? D HIS 92 ? D HIS 92  ? 1_555 FE ? J HEM . ? D HEM 148 ? 1_555 NA ? J HEM . ? D HEM 148 ? 1_555 90.2  ?
+32 NE2 ? D HIS 92 ? D HIS 92  ? 1_555 FE ? J HEM . ? D HEM 148 ? 1_555 NB ? J HEM . ? D HEM 148 ? 1_555 102.2 ?
+33 NA  ? J HEM .  ? D HEM 148 ? 1_555 FE ? J HEM . ? D HEM 148 ? 1_555 NB ? J HEM . ? D HEM 148 ? 1_555 88.3  ?
+34 NE2 ? D HIS 92 ? D HIS 92  ? 1_555 FE ? J HEM . ? D HEM 148 ? 1_555 NC ? J HEM . ? D HEM 148 ? 1_555 109.1 ?
+35 NA  ? J HEM .  ? D HEM 148 ? 1_555 FE ? J HEM . ? D HEM 148 ? 1_555 NC ? J HEM . ? D HEM 148 ? 1_555 160.5 ?
+36 NB  ? J HEM .  ? D HEM 148 ? 1_555 FE ? J HEM . ? D HEM 148 ? 1_555 NC ? J HEM . ? D HEM 148 ? 1_555 84.5  ?
+37 NE2 ? D HIS 92 ? D HIS 92  ? 1_555 FE ? J HEM . ? D HEM 148 ? 1_555 ND ? J HEM . ? D HEM 148 ? 1_555 97.8  ?
+38 NA  ? J HEM .  ? D HEM 148 ? 1_555 FE ? J HEM . ? D HEM 148 ? 1_555 ND ? J HEM . ? D HEM 148 ? 1_555 89.1  ?
+39 NB  ? J HEM .  ? D HEM 148 ? 1_555 FE ? J HEM . ? D HEM 148 ? 1_555 ND ? J HEM . ? D HEM 148 ? 1_555 159.9 ?
+40 NC  ? J HEM .  ? D HEM 148 ? 1_555 FE ? J HEM . ? D HEM 148 ? 1_555 ND ? J HEM . ? D HEM 148 ? 1_555 91.4  ?
+#
+loop_
+_struct_site.id
+_struct_site.pdbx_evidence_code
+_struct_site.pdbx_auth_asym_id
+_struct_site.pdbx_auth_comp_id
+_struct_site.pdbx_auth_seq_id
+_struct_site.pdbx_auth_ins_code
+_struct_site.pdbx_num_residues
+_struct_site.details
+AC1 Software D PO4 147 ? 1  'BINDING SITE FOR RESIDUE PO4 D 147'
+AC2 Software B PO4 147 ? 1  'BINDING SITE FOR RESIDUE PO4 B 147'
+AC3 Software A HEM 142 ? 16 'BINDING SITE FOR RESIDUE HEM A 142'
+AC4 Software B HEM 148 ? 13 'BINDING SITE FOR RESIDUE HEM B 148'
+AC5 Software C HEM 142 ? 15 'BINDING SITE FOR RESIDUE HEM C 142'
+AC6 Software D HEM 148 ? 7  'BINDING SITE FOR RESIDUE HEM D 148'
+#
+loop_
+_struct_site_gen.id
+_struct_site_gen.site_id
+_struct_site_gen.pdbx_num_res
+_struct_site_gen.label_comp_id
+_struct_site_gen.label_asym_id
+_struct_site_gen.label_seq_id
+_struct_site_gen.pdbx_auth_ins_code
+_struct_site_gen.auth_comp_id
+_struct_site_gen.auth_asym_id
+_struct_site_gen.auth_seq_id
+_struct_site_gen.label_atom_id
+_struct_site_gen.label_alt_id
+_struct_site_gen.symmetry
+_struct_site_gen.details
+1  AC1 1  VAL D 1   ? VAL D 1   . ? 1_555 ?
+2  AC2 1  HOH L .   ? HOH B 197 . ? 1_555 ?
+3  AC3 16 TYR A 42  ? TYR A 42  . ? 1_555 ?
+4  AC3 16 PHE A 43  ? PHE A 43  . ? 1_555 ?
+5  AC3 16 HIS A 45  ? HIS A 45  . ? 1_555 ?
+6  AC3 16 PHE A 46  ? PHE A 46  . ? 1_555 ?
+7  AC3 16 HIS A 58  ? HIS A 58  . ? 1_555 ?
+8  AC3 16 LYS A 61  ? LYS A 61  . ? 1_555 ?
+9  AC3 16 LEU A 86  ? LEU A 86  . ? 1_555 ?
+10 AC3 16 HIS A 87  ? HIS A 87  . ? 1_555 ?
+11 AC3 16 LEU A 91  ? LEU A 91  . ? 1_555 ?
+12 AC3 16 VAL A 93  ? VAL A 93  . ? 1_555 ?
+13 AC3 16 ASN A 97  ? ASN A 97  . ? 1_555 ?
+14 AC3 16 PHE A 98  ? PHE A 98  . ? 1_555 ?
+15 AC3 16 LEU A 101 ? LEU A 101 . ? 1_555 ?
+16 AC3 16 LEU A 136 ? LEU A 136 . ? 1_555 ?
+17 AC3 16 HOH K .   ? HOH A 144 . ? 1_555 ?
+18 AC3 16 HOH K .   ? HOH A 159 . ? 1_555 ?
+19 AC4 13 ALA A 53  ? ALA A 53  . ? 1_556 ?
+20 AC4 13 HOH K .   ? HOH A 145 . ? 1_556 ?
+21 AC4 13 PHE B 41  ? PHE B 41  . ? 1_555 ?
+22 AC4 13 HIS B 63  ? HIS B 63  . ? 1_555 ?
+23 AC4 13 LYS B 66  ? LYS B 66  . ? 1_555 ?
+24 AC4 13 VAL B 67  ? VAL B 67  . ? 1_555 ?
+25 AC4 13 HIS B 92  ? HIS B 92  . ? 1_555 ?
+26 AC4 13 LEU B 96  ? LEU B 96  . ? 1_555 ?
+27 AC4 13 ASN B 102 ? ASN B 102 . ? 1_555 ?
+28 AC4 13 PHE B 103 ? PHE B 103 . ? 1_555 ?
+29 AC4 13 LEU B 141 ? LEU B 141 . ? 1_555 ?
+30 AC4 13 HOH L .   ? HOH B 175 . ? 1_555 ?
+31 AC4 13 HOH L .   ? HOH B 193 . ? 1_555 ?
+32 AC5 15 TYR C 42  ? TYR C 42  . ? 1_555 ?
+33 AC5 15 PHE C 43  ? PHE C 43  . ? 1_555 ?
+34 AC5 15 HIS C 45  ? HIS C 45  . ? 1_555 ?
+35 AC5 15 HIS C 58  ? HIS C 58  . ? 1_555 ?
+36 AC5 15 LYS C 61  ? LYS C 61  . ? 1_555 ?
+37 AC5 15 LEU C 83  ? LEU C 83  . ? 1_555 ?
+38 AC5 15 LEU C 86  ? LEU C 86  . ? 1_555 ?
+39 AC5 15 HIS C 87  ? HIS C 87  . ? 1_555 ?
+40 AC5 15 LEU C 91  ? LEU C 91  . ? 1_555 ?
+41 AC5 15 VAL C 93  ? VAL C 93  . ? 1_555 ?
+42 AC5 15 ASN C 97  ? ASN C 97  . ? 1_555 ?
+43 AC5 15 PHE C 98  ? PHE C 98  . ? 1_555 ?
+44 AC5 15 LEU C 136 ? LEU C 136 . ? 1_555 ?
+45 AC5 15 HOH M .   ? HOH C 149 . ? 1_555 ?
+46 AC5 15 HOH M .   ? HOH C 164 . ? 1_555 ?
+47 AC6 7  HIS D 63  ? HIS D 63  . ? 1_555 ?
+48 AC6 7  LYS D 66  ? LYS D 66  . ? 1_555 ?
+49 AC6 7  VAL D 67  ? VAL D 67  . ? 1_555 ?
+50 AC6 7  HIS D 92  ? HIS D 92  . ? 1_555 ?
+51 AC6 7  LEU D 96  ? LEU D 96  . ? 1_555 ?
+52 AC6 7  ASN D 102 ? ASN D 102 . ? 1_555 ?
+53 AC6 7  LEU D 141 ? LEU D 141 . ? 1_555 ?
+#
+loop_
+_pdbx_validate_close_contact.id
+_pdbx_validate_close_contact.PDB_model_num
+_pdbx_validate_close_contact.auth_atom_id_1
+_pdbx_validate_close_contact.auth_asym_id_1
+_pdbx_validate_close_contact.auth_comp_id_1
+_pdbx_validate_close_contact.auth_seq_id_1
+_pdbx_validate_close_contact.PDB_ins_code_1
+_pdbx_validate_close_contact.label_alt_id_1
+_pdbx_validate_close_contact.auth_atom_id_2
+_pdbx_validate_close_contact.auth_asym_id_2
+_pdbx_validate_close_contact.auth_comp_id_2
+_pdbx_validate_close_contact.auth_seq_id_2
+_pdbx_validate_close_contact.PDB_ins_code_2
+_pdbx_validate_close_contact.label_alt_id_2
+_pdbx_validate_close_contact.dist
+1 1 C   B VAL 1  ? ? CA  B HIS 2   ? ? 1.64
+2 1 C   D PHE 45 ? ? CA  D GLY 46  ? ? 1.78
+3 1 CB  D THR 4  ? ? OE2 D GLU 6   ? ? 2.00
+4 1 NZ  D LYS 66 ? ? O1A D HEM 148 ? ? 2.06
+5 1 OD2 D ASP 73 ? ? O   D HOH 174 ? ? 2.10
+6 1 OG1 D THR 4  ? ? OE2 D GLU 6   ? ? 2.19
+#
+loop_
+_pdbx_validate_symm_contact.id
+_pdbx_validate_symm_contact.PDB_model_num
+_pdbx_validate_symm_contact.auth_atom_id_1
+_pdbx_validate_symm_contact.auth_asym_id_1
+_pdbx_validate_symm_contact.auth_comp_id_1
+_pdbx_validate_symm_contact.auth_seq_id_1
+_pdbx_validate_symm_contact.PDB_ins_code_1
+_pdbx_validate_symm_contact.label_alt_id_1
+_pdbx_validate_symm_contact.site_symmetry_1
+_pdbx_validate_symm_contact.auth_atom_id_2
+_pdbx_validate_symm_contact.auth_asym_id_2
+_pdbx_validate_symm_contact.auth_comp_id_2
+_pdbx_validate_symm_contact.auth_seq_id_2
+_pdbx_validate_symm_contact.PDB_ins_code_2
+_pdbx_validate_symm_contact.label_alt_id_2
+_pdbx_validate_symm_contact.site_symmetry_2
+_pdbx_validate_symm_contact.dist
+1 1 OD2 C ASP 85  ? ? 1_555 O B HOH 204 ? ? 2_657 1.41
+2 1 O   B HOH 204 ? ? 1_555 O C HOH 161 ? ? 2_647 2.02
+#
+loop_
+_pdbx_validate_rmsd_bond.id
+_pdbx_validate_rmsd_bond.PDB_model_num
+_pdbx_validate_rmsd_bond.auth_atom_id_1
+_pdbx_validate_rmsd_bond.auth_asym_id_1
+_pdbx_validate_rmsd_bond.auth_comp_id_1
+_pdbx_validate_rmsd_bond.auth_seq_id_1
+_pdbx_validate_rmsd_bond.PDB_ins_code_1
+_pdbx_validate_rmsd_bond.label_alt_id_1
+_pdbx_validate_rmsd_bond.auth_atom_id_2
+_pdbx_validate_rmsd_bond.auth_asym_id_2
+_pdbx_validate_rmsd_bond.auth_comp_id_2
+_pdbx_validate_rmsd_bond.auth_seq_id_2
+_pdbx_validate_rmsd_bond.PDB_ins_code_2
+_pdbx_validate_rmsd_bond.label_alt_id_2
+_pdbx_validate_rmsd_bond.bond_value
+_pdbx_validate_rmsd_bond.bond_target_value
+_pdbx_validate_rmsd_bond.bond_deviation
+_pdbx_validate_rmsd_bond.bond_standard_deviation
+_pdbx_validate_rmsd_bond.linker_flag
+1    1 N   A VAL 1   ? ? CA  A VAL 1   ? ? 1.164 1.459 -0.295 0.020 N
+2    1 CA  A VAL 1   ? ? CB  A VAL 1   ? ? 1.843 1.543 0.300  0.021 N
+3    1 CB  A VAL 1   ? ? CG1 A VAL 1   ? ? 1.317 1.524 -0.207 0.021 N
+4    1 CB  A VAL 1   ? ? CG2 A VAL 1   ? ? 1.241 1.524 -0.283 0.021 N
+5    1 CA  A LEU 2   ? ? C   A LEU 2   ? ? 1.774 1.525 0.249  0.026 N
+6    1 C   A LEU 2   ? ? N   A SER 3   ? ? 1.015 1.336 -0.321 0.023 Y
+7    1 N   A SER 3   ? ? CA  A SER 3   ? ? 1.627 1.459 0.168  0.020 N
+8    1 CB  A SER 3   ? ? OG  A SER 3   ? ? 1.286 1.418 -0.132 0.013 N
+9    1 C   A SER 3   ? ? N   A PRO 4   ? ? 1.620 1.338 0.282  0.019 Y
+10   1 N   A PRO 4   ? ? CA  A PRO 4   ? ? 1.319 1.468 -0.149 0.017 N
+11   1 CA  A PRO 4   ? ? CB  A PRO 4   ? ? 1.734 1.531 0.203  0.020 N
+12   1 C   A PRO 4   ? ? N   A ALA 5   ? ? 1.594 1.336 0.258  0.023 Y
+13   1 N   A ALA 5   ? ? CA  A ALA 5   ? ? 1.328 1.459 -0.131 0.020 N
+14   1 CA  A ALA 5   ? ? CB  A ALA 5   ? ? 1.767 1.520 0.247  0.021 N
+15   1 N   A LYS 7   ? ? CA  A LYS 7   ? ? 1.616 1.459 0.157  0.020 N
+16   1 C   A LYS 7   ? ? N   A THR 8   ? ? 1.593 1.336 0.257  0.023 Y
+17   1 CA  A THR 8   ? ? CB  A THR 8   ? ? 1.707 1.529 0.178  0.026 N
+18   1 CB  A THR 8   ? ? OG1 A THR 8   ? ? 1.255 1.428 -0.173 0.020 N
+19   1 CB  A THR 8   ? ? CG2 A THR 8   ? ? 1.274 1.519 -0.245 0.033 N
+20   1 CA  A THR 8   ? ? C   A THR 8   ? ? 1.351 1.525 -0.174 0.026 N
+21   1 C   A THR 8   ? ? N   A ASN 9   ? ? 1.516 1.336 0.180  0.023 Y
+22   1 CB  A VAL 10  ? ? CG2 A VAL 10  ? ? 1.346 1.524 -0.178 0.021 N
+23   1 CA  A VAL 10  ? ? C   A VAL 10  ? ? 1.685 1.525 0.160  0.026 N
+24   1 N   A LYS 11  ? ? CA  A LYS 11  ? ? 1.591 1.459 0.132  0.020 N
+25   1 CA  A LYS 11  ? ? CB  A LYS 11  ? ? 1.397 1.535 -0.138 0.022 N
+26   1 CB  A LYS 11  ? ? CG  A LYS 11  ? ? 1.325 1.521 -0.196 0.027 N
+27   1 CG  A LYS 11  ? ? CD  A LYS 11  ? ? 1.314 1.520 -0.206 0.034 N
+28   1 CD  A LYS 11  ? ? CE  A LYS 11  ? ? 1.962 1.508 0.454  0.025 N
+29   1 N   A ALA 12  ? ? CA  A ALA 12  ? ? 1.325 1.459 -0.134 0.020 N
+30   1 C   A ALA 12  ? ? O   A ALA 12  ? ? 1.454 1.229 0.225  0.019 N
+31   1 CA  A ALA 13  ? ? C   A ALA 13  ? ? 1.726 1.525 0.201  0.026 N
+32   1 CA  A TRP 14  ? ? CB  A TRP 14  ? ? 1.826 1.535 0.291  0.022 N
+33   1 CB  A TRP 14  ? ? CG  A TRP 14  ? ? 1.224 1.498 -0.274 0.018 N
+34   1 CG  A TRP 14  ? ? CD1 A TRP 14  ? ? 1.669 1.363 0.306  0.014 N
+35   1 CD1 A TRP 14  ? ? NE1 A TRP 14  ? ? 1.533 1.375 0.158  0.017 N
+36   1 NE1 A TRP 14  ? ? CE2 A TRP 14  ? ? 1.136 1.371 -0.235 0.013 N
+37   1 CE2 A TRP 14  ? ? CZ2 A TRP 14  ? ? 1.151 1.393 -0.242 0.017 N
+38   1 CE2 A TRP 14  ? ? CD2 A TRP 14  ? ? 1.630 1.409 0.221  0.012 N
+39   1 CH2 A TRP 14  ? ? CZ2 A TRP 14  ? ? 1.151 1.369 -0.218 0.019 N
+40   1 CA  A GLY 15  ? ? C   A GLY 15  ? ? 1.696 1.514 0.182  0.016 N
+41   1 C   A GLY 15  ? ? O   A GLY 15  ? ? 1.668 1.232 0.436  0.016 N
+42   1 C   A GLY 15  ? ? N   A LYS 16  ? ? 0.918 1.336 -0.418 0.023 Y
+43   1 CB  A LYS 16  ? ? CG  A LYS 16  ? ? 1.687 1.521 0.166  0.027 N
+44   1 CG  A LYS 16  ? ? CD  A LYS 16  ? ? 2.008 1.520 0.488  0.034 N
+45   1 CD  A LYS 16  ? ? CE  A LYS 16  ? ? 1.918 1.508 0.410  0.025 N
+46   1 C   A LYS 16  ? ? O   A LYS 16  ? ? 1.080 1.229 -0.149 0.019 N
+47   1 C   A LYS 16  ? ? N   A VAL 17  ? ? 1.516 1.336 0.180  0.023 Y
+48   1 N   A VAL 17  ? ? CA  A VAL 17  ? ? 1.267 1.459 -0.192 0.020 N
+49   1 CA  A VAL 17  ? ? CB  A VAL 17  ? ? 1.375 1.543 -0.168 0.021 N
+50   1 CA  A VAL 17  ? ? C   A VAL 17  ? ? 1.957 1.525 0.432  0.026 N
+51   1 C   A VAL 17  ? ? O   A VAL 17  ? ? 0.746 1.229 -0.483 0.019 N
+52   1 C   A VAL 17  ? ? N   A GLY 18  ? ? 1.595 1.336 0.259  0.023 Y
+53   1 CA  A GLY 18  ? ? C   A GLY 18  ? ? 1.861 1.514 0.347  0.016 N
+54   1 C   A GLY 18  ? ? O   A GLY 18  ? ? 1.336 1.232 0.104  0.016 N
+55   1 C   A ALA 19  ? ? O   A ALA 19  ? ? 1.465 1.229 0.236  0.019 N
+56   1 CA  A HIS 20  ? ? CB  A HIS 20  ? ? 1.367 1.535 -0.168 0.022 N
+57   1 CB  A HIS 20  ? ? CG  A HIS 20  ? ? 1.367 1.492 -0.125 0.016 N
+58   1 CG  A HIS 20  ? ? CD2 A HIS 20  ? ? 1.529 1.354 0.175  0.009 N
+59   1 CG  A HIS 20  ? ? ND1 A HIS 20  ? ? 1.705 1.383 0.322  0.022 N
+60   1 CE1 A HIS 20  ? ? NE2 A HIS 20  ? ? 1.026 1.317 -0.291 0.011 N
+61   1 NE2 A HIS 20  ? ? CD2 A HIS 20  ? ? 1.553 1.415 0.138  0.021 N
+62   1 CA  A ALA 21  ? ? C   A ALA 21  ? ? 2.086 1.525 0.561  0.026 N
+63   1 C   A ALA 21  ? ? O   A ALA 21  ? ? 1.072 1.229 -0.157 0.019 N
+64   1 CA  A GLY 22  ? ? C   A GLY 22  ? ? 1.198 1.514 -0.316 0.016 N
+65   1 C   A GLY 22  ? ? N   A GLU 23  ? ? 1.488 1.336 0.152  0.023 Y
+66   1 CG  A GLU 23  ? ? CD  A GLU 23  ? ? 2.098 1.515 0.583  0.015 N
+67   1 CD  A GLU 23  ? ? OE1 A GLU 23  ? ? 1.719 1.252 0.467  0.011 N
+68   1 CD  A GLU 23  ? ? OE2 A GLU 23  ? ? 1.415 1.252 0.163  0.011 N
+69   1 CB  A TYR 24  ? ? CG  A TYR 24  ? ? 1.694 1.512 0.182  0.015 N
+70   1 CG  A TYR 24  ? ? CD1 A TYR 24  ? ? 1.291 1.387 -0.096 0.013 N
+71   1 CE1 A TYR 24  ? ? CZ  A TYR 24  ? ? 1.129 1.381 -0.252 0.013 N
+72   1 CZ  A TYR 24  ? ? CE2 A TYR 24  ? ? 1.547 1.381 0.166  0.013 N
+73   1 CA  A GLY 25  ? ? C   A GLY 25  ? ? 1.416 1.514 -0.098 0.016 N
+74   1 N   A ALA 26  ? ? CA  A ALA 26  ? ? 1.201 1.459 -0.258 0.020 N
+75   1 C   A ALA 26  ? ? N   A GLU 27  ? ? 1.494 1.336 0.158  0.023 Y
+76   1 CG  A GLU 27  ? ? CD  A GLU 27  ? ? 1.695 1.515 0.180  0.015 N
+77   1 CD  A GLU 27  ? ? OE1 A GLU 27  ? ? 1.157 1.252 -0.095 0.011 N
+78   1 N   A LEU 29  ? ? CA  A LEU 29  ? ? 1.632 1.459 0.173  0.020 N
+79   1 CA  A LEU 29  ? ? CB  A LEU 29  ? ? 1.790 1.533 0.257  0.023 N
+80   1 CB  A GLU 30  ? ? CG  A GLU 30  ? ? 1.356 1.517 -0.161 0.019 N
+81   1 CG  A GLU 30  ? ? CD  A GLU 30  ? ? 2.002 1.515 0.487  0.015 N
+82   1 CD  A GLU 30  ? ? OE2 A GLU 30  ? ? 1.320 1.252 0.068  0.011 N
+83   1 CD  A ARG 31  ? ? NE  A ARG 31  ? ? 1.675 1.460 0.215  0.017 N
+84   1 CG  A PHE 33  ? ? CD2 A PHE 33  ? ? 1.547 1.383 0.164  0.015 N
+85   1 CG  A PHE 33  ? ? CD1 A PHE 33  ? ? 1.235 1.383 -0.148 0.015 N
+86   1 CZ  A PHE 33  ? ? CE2 A PHE 33  ? ? 1.126 1.369 -0.243 0.019 N
+87   1 CE2 A PHE 33  ? ? CD2 A PHE 33  ? ? 1.580 1.388 0.192  0.020 N
+88   1 CA  A PHE 33  ? ? C   A PHE 33  ? ? 1.298 1.525 -0.227 0.026 N
+89   1 C   A PHE 33  ? ? N   A LEU 34  ? ? 1.488 1.336 0.152  0.023 Y
+90   1 N   A SER 35  ? ? CA  A SER 35  ? ? 1.331 1.459 -0.128 0.020 N
+91   1 CG  A PHE 36  ? ? CD2 A PHE 36  ? ? 1.537 1.383 0.154  0.015 N
+92   1 N   A PRO 37  ? ? CA  A PRO 37  ? ? 1.614 1.468 0.146  0.017 N
+93   1 CD  A PRO 37  ? ? N   A PRO 37  ? ? 1.237 1.474 -0.237 0.014 N
+94   1 CA  A LYS 40  ? ? CB  A LYS 40  ? ? 1.752 1.535 0.217  0.022 N
+95   1 CD  A LYS 40  ? ? CE  A LYS 40  ? ? 1.357 1.508 -0.151 0.025 N
+96   1 C   A LYS 40  ? ? O   A LYS 40  ? ? 1.105 1.229 -0.124 0.019 N
+97   1 CA  A THR 41  ? ? C   A THR 41  ? ? 1.349 1.525 -0.176 0.026 N
+98   1 C   A THR 41  ? ? O   A THR 41  ? ? 1.354 1.229 0.125  0.019 N
+99   1 CG  A TYR 42  ? ? CD2 A TYR 42  ? ? 1.473 1.387 0.086  0.013 N
+100  1 CE1 A TYR 42  ? ? CZ  A TYR 42  ? ? 1.270 1.381 -0.111 0.013 N
+101  1 CA  A TYR 42  ? ? C   A TYR 42  ? ? 1.722 1.525 0.197  0.026 N
+102  1 CG  A PHE 43  ? ? CD2 A PHE 43  ? ? 1.268 1.383 -0.115 0.015 N
+103  1 CG  A PHE 43  ? ? CD1 A PHE 43  ? ? 1.490 1.383 0.107  0.015 N
+104  1 CA  A PRO 44  ? ? CB  A PRO 44  ? ? 1.374 1.531 -0.157 0.020 N
+105  1 CD  A PRO 44  ? ? N   A PRO 44  ? ? 1.338 1.474 -0.136 0.014 N
+106  1 CA  A PRO 44  ? ? C   A PRO 44  ? ? 1.826 1.524 0.302  0.020 N
+107  1 C   A PRO 44  ? ? N   A HIS 45  ? ? 1.190 1.336 -0.146 0.023 Y
+108  1 CA  A HIS 45  ? ? CB  A HIS 45  ? ? 1.395 1.535 -0.140 0.022 N
+109  1 CE1 A HIS 45  ? ? NE2 A HIS 45  ? ? 1.522 1.333 0.189  0.019 N
+110  1 C   A HIS 45  ? ? N   A PHE 46  ? ? 1.617 1.336 0.281  0.023 Y
+111  1 CB  A PHE 46  ? ? CG  A PHE 46  ? ? 1.301 1.509 -0.208 0.017 N
+112  1 CG  A PHE 46  ? ? CD2 A PHE 46  ? ? 1.124 1.383 -0.259 0.015 N
+113  1 CG  A PHE 46  ? ? CD1 A PHE 46  ? ? 1.473 1.383 0.090  0.015 N
+114  1 CE1 A PHE 46  ? ? CZ  A PHE 46  ? ? 1.545 1.369 0.176  0.019 N
+115  1 CE2 A PHE 46  ? ? CD2 A PHE 46  ? ? 1.557 1.388 0.169  0.020 N
+116  1 CA  A ASP 47  ? ? C   A ASP 47  ? ? 1.739 1.525 0.214  0.026 N
+117  1 C   A ASP 47  ? ? N   A LEU 48  ? ? 1.134 1.336 -0.202 0.023 Y
+118  1 CA  A LEU 48  ? ? CB  A LEU 48  ? ? 1.699 1.533 0.166  0.023 N
+119  1 CG  A LEU 48  ? ? CD2 A LEU 48  ? ? 1.254 1.514 -0.260 0.037 N
+120  1 N   A SER 49  ? ? CA  A SER 49  ? ? 1.614 1.459 0.155  0.020 N
+121  1 CA  A SER 49  ? ? CB  A SER 49  ? ? 1.367 1.525 -0.158 0.015 N
+122  1 CB  A SER 49  ? ? OG  A SER 49  ? ? 1.100 1.418 -0.318 0.013 N
+123  1 C   A SER 49  ? ? N   A HIS 50  ? ? 1.581 1.336 0.245  0.023 Y
+124  1 CA  A HIS 50  ? ? CB  A HIS 50  ? ? 2.015 1.535 0.480  0.022 N
+125  1 CB  A HIS 50  ? ? CG  A HIS 50  ? ? 1.330 1.492 -0.162 0.016 N
+126  1 CG  A HIS 50  ? ? CD2 A HIS 50  ? ? 1.609 1.354 0.255  0.009 N
+127  1 C   A HIS 50  ? ? O   A HIS 50  ? ? 1.483 1.229 0.254  0.019 N
+128  1 C   A HIS 50  ? ? N   A GLY 51  ? ? 0.959 1.336 -0.377 0.023 Y
+129  1 N   A SER 52  ? ? CA  A SER 52  ? ? 1.747 1.459 0.288  0.020 N
+130  1 CB  A SER 52  ? ? OG  A SER 52  ? ? 1.338 1.418 -0.080 0.013 N
+131  1 CA  A SER 52  ? ? C   A SER 52  ? ? 1.213 1.525 -0.312 0.026 N
+132  1 CA  A ALA 53  ? ? CB  A ALA 53  ? ? 1.680 1.520 0.160  0.021 N
+133  1 CG  A LYS 56  ? ? CD  A LYS 56  ? ? 2.058 1.520 0.538  0.034 N
+134  1 CD  A LYS 56  ? ? CE  A LYS 56  ? ? 1.842 1.508 0.334  0.025 N
+135  1 CA  A LYS 56  ? ? C   A LYS 56  ? ? 1.345 1.525 -0.180 0.026 N
+136  1 C   A LYS 56  ? ? N   A GLY 57  ? ? 1.550 1.336 0.214  0.023 Y
+137  1 CA  A GLY 57  ? ? C   A GLY 57  ? ? 1.654 1.514 0.140  0.016 N
+138  1 CB  A HIS 58  ? ? CG  A HIS 58  ? ? 1.689 1.496 0.193  0.018 N
+139  1 CE1 A HIS 58  ? ? NE2 A HIS 58  ? ? 1.186 1.317 -0.131 0.011 N
+140  1 NE2 A HIS 58  ? ? CD2 A HIS 58  ? ? 1.304 1.373 -0.069 0.011 N
+141  1 CA  A HIS 58  ? ? C   A HIS 58  ? ? 1.762 1.525 0.237  0.026 N
+142  1 N   A GLY 59  ? ? CA  A GLY 59  ? ? 1.562 1.456 0.106  0.015 N
+143  1 CA  A GLY 59  ? ? C   A GLY 59  ? ? 1.319 1.514 -0.195 0.016 N
+144  1 CA  A LYS 60  ? ? CB  A LYS 60  ? ? 1.676 1.535 0.141  0.022 N
+145  1 CB  A LYS 60  ? ? CG  A LYS 60  ? ? 1.353 1.521 -0.168 0.027 N
+146  1 CD  A LYS 60  ? ? CE  A LYS 60  ? ? 1.933 1.508 0.425  0.025 N
+147  1 CE  A LYS 60  ? ? NZ  A LYS 60  ? ? 2.685 1.486 1.199  0.025 N
+148  1 CA  A LYS 60  ? ? C   A LYS 60  ? ? 1.362 1.525 -0.163 0.026 N
+149  1 C   A LYS 60  ? ? O   A LYS 60  ? ? 1.098 1.229 -0.131 0.019 N
+150  1 C   A LYS 60  ? ? N   A LYS 61  ? ? 1.511 1.336 0.175  0.023 Y
+151  1 CD  A LYS 61  ? ? CE  A LYS 61  ? ? 0.815 1.508 -0.693 0.025 N
+152  1 CE  A LYS 61  ? ? NZ  A LYS 61  ? ? 1.742 1.486 0.256  0.025 N
+153  1 CA  A LYS 61  ? ? C   A LYS 61  ? ? 1.690 1.525 0.165  0.026 N
+154  1 N   A VAL 62  ? ? CA  A VAL 62  ? ? 1.599 1.459 0.140  0.020 N
+155  1 CA  A VAL 62  ? ? C   A VAL 62  ? ? 1.746 1.525 0.221  0.026 N
+156  1 CA  A ALA 63  ? ? C   A ALA 63  ? ? 1.360 1.525 -0.165 0.026 N
+157  1 CB  A ASP 64  ? ? CG  A ASP 64  ? ? 1.955 1.513 0.442  0.021 N
+158  1 CG  A ASP 64  ? ? OD1 A ASP 64  ? ? 1.510 1.249 0.261  0.023 N
+159  1 C   A ASP 64  ? ? N   A ALA 65  ? ? 1.501 1.336 0.165  0.023 Y
+160  1 CB  A THR 67  ? ? OG1 A THR 67  ? ? 1.089 1.428 -0.339 0.020 N
+161  1 C   A THR 67  ? ? O   A THR 67  ? ? 1.400 1.229 0.171  0.019 N
+162  1 C   A ASN 68  ? ? O   A ASN 68  ? ? 1.394 1.229 0.165  0.019 N
+163  1 C   A ASN 68  ? ? N   A ALA 69  ? ? 1.484 1.336 0.148  0.023 Y
+164  1 C   A ALA 69  ? ? O   A ALA 69  ? ? 1.093 1.229 -0.136 0.019 N
+165  1 N   A VAL 70  ? ? CA  A VAL 70  ? ? 1.586 1.459 0.127  0.020 N
+166  1 CA  A VAL 70  ? ? CB  A VAL 70  ? ? 1.370 1.543 -0.173 0.021 N
+167  1 CA  A ALA 71  ? ? CB  A ALA 71  ? ? 1.372 1.520 -0.148 0.021 N
+168  1 CA  A ALA 71  ? ? C   A ALA 71  ? ? 1.193 1.525 -0.332 0.026 N
+169  1 C   A ALA 71  ? ? O   A ALA 71  ? ? 1.444 1.229 0.215  0.019 N
+170  1 CA  A HIS 72  ? ? CB  A HIS 72  ? ? 1.779 1.535 0.244  0.022 N
+171  1 CB  A HIS 72  ? ? CG  A HIS 72  ? ? 1.323 1.492 -0.169 0.016 N
+172  1 CG  A HIS 72  ? ? CD2 A HIS 72  ? ? 1.478 1.354 0.124  0.009 N
+173  1 CG  A HIS 72  ? ? ND1 A HIS 72  ? ? 1.847 1.383 0.464  0.022 N
+174  1 NE2 A HIS 72  ? ? CD2 A HIS 72  ? ? 1.626 1.415 0.211  0.021 N
+175  1 CA  A HIS 72  ? ? C   A HIS 72  ? ? 1.359 1.525 -0.166 0.026 N
+176  1 CA  A VAL 73  ? ? CB  A VAL 73  ? ? 1.359 1.543 -0.184 0.021 N
+177  1 CB  A VAL 73  ? ? CG2 A VAL 73  ? ? 1.384 1.524 -0.140 0.021 N
+178  1 CA  A VAL 73  ? ? C   A VAL 73  ? ? 1.210 1.525 -0.315 0.026 N
+179  1 N   A ASP 74  ? ? CA  A ASP 74  ? ? 1.604 1.459 0.145  0.020 N
+180  1 CB  A ASP 74  ? ? CG  A ASP 74  ? ? 1.798 1.513 0.285  0.021 N
+181  1 CG  A ASP 74  ? ? OD1 A ASP 74  ? ? 0.797 1.249 -0.452 0.023 N
+182  1 CG  A ASP 74  ? ? OD2 A ASP 74  ? ? 1.572 1.249 0.323  0.023 N
+183  1 C   A ASP 74  ? ? O   A ASP 74  ? ? 1.351 1.229 0.122  0.019 N
+184  1 C   A ASP 74  ? ? N   A ASP 75  ? ? 0.925 1.336 -0.411 0.023 Y
+185  1 CA  A ASP 75  ? ? CB  A ASP 75  ? ? 1.973 1.535 0.438  0.022 N
+186  1 CB  A ASP 75  ? ? CG  A ASP 75  ? ? 0.678 1.513 -0.835 0.021 N
+187  1 CG  A ASP 75  ? ? OD1 A ASP 75  ? ? 1.817 1.249 0.568  0.023 N
+188  1 CG  A ASP 75  ? ? OD2 A ASP 75  ? ? 2.036 1.249 0.787  0.023 N
+189  1 N   A MET 76  ? ? CA  A MET 76  ? ? 1.605 1.459 0.146  0.020 N
+190  1 CB  A MET 76  ? ? CG  A MET 76  ? ? 1.117 1.509 -0.392 0.032 N
+191  1 CG  A MET 76  ? ? SD  A MET 76  ? ? 2.017 1.807 0.210  0.026 N
+192  1 C   A MET 76  ? ? N   A PRO 77  ? ? 1.208 1.338 -0.130 0.019 Y
+193  1 N   A PRO 77  ? ? CA  A PRO 77  ? ? 1.350 1.468 -0.118 0.017 N
+194  1 CA  A PRO 77  ? ? CB  A PRO 77  ? ? 1.720 1.531 0.189  0.020 N
+195  1 CA  A PRO 77  ? ? C   A PRO 77  ? ? 1.278 1.524 -0.246 0.020 N
+196  1 C   A PRO 77  ? ? O   A PRO 77  ? ? 1.432 1.228 0.204  0.020 N
+197  1 CB  A ASN 78  ? ? CG  A ASN 78  ? ? 0.882 1.506 -0.624 0.023 N
+198  1 CG  A ASN 78  ? ? OD1 A ASN 78  ? ? 2.069 1.235 0.834  0.022 N
+199  1 CG  A ASN 78  ? ? ND2 A ASN 78  ? ? 1.122 1.324 -0.202 0.025 N
+200  1 C   A ASN 78  ? ? O   A ASN 78  ? ? 1.394 1.229 0.165  0.019 N
+201  1 CA  A ALA 79  ? ? CB  A ALA 79  ? ? 1.371 1.520 -0.149 0.021 N
+202  1 CA  A ALA 79  ? ? C   A ALA 79  ? ? 1.701 1.525 0.176  0.026 N
+203  1 N   A LEU 80  ? ? CA  A LEU 80  ? ? 1.595 1.459 0.136  0.020 N
+204  1 CA  A SER 81  ? ? CB  A SER 81  ? ? 2.003 1.525 0.478  0.015 N
+205  1 C   A SER 81  ? ? O   A SER 81  ? ? 1.356 1.229 0.127  0.019 N
+206  1 CB  A LEU 83  ? ? CG  A LEU 83  ? ? 1.222 1.521 -0.299 0.029 N
+207  1 CA  A SER 84  ? ? CB  A SER 84  ? ? 1.819 1.525 0.294  0.015 N
+208  1 CB  A SER 84  ? ? OG  A SER 84  ? ? 1.220 1.418 -0.198 0.013 N
+209  1 N   A ASP 85  ? ? CA  A ASP 85  ? ? 1.635 1.459 0.176  0.020 N
+210  1 CG  A ASP 85  ? ? OD1 A ASP 85  ? ? 0.751 1.249 -0.498 0.023 N
+211  1 CG  A ASP 85  ? ? OD2 A ASP 85  ? ? 1.730 1.249 0.481  0.023 N
+212  1 CB  A LEU 86  ? ? CG  A LEU 86  ? ? 1.258 1.521 -0.263 0.029 N
+213  1 CB  A HIS 87  ? ? CG  A HIS 87  ? ? 1.605 1.496 0.109  0.018 N
+214  1 CA  A HIS 87  ? ? C   A HIS 87  ? ? 1.754 1.525 0.229  0.026 N
+215  1 CA  A ALA 88  ? ? C   A ALA 88  ? ? 1.733 1.525 0.208  0.026 N
+216  1 C   A ALA 88  ? ? O   A ALA 88  ? ? 1.058 1.229 -0.171 0.019 N
+217  1 CG  A HIS 89  ? ? CD2 A HIS 89  ? ? 1.532 1.354 0.178  0.009 N
+218  1 NE2 A HIS 89  ? ? CD2 A HIS 89  ? ? 1.277 1.373 -0.096 0.011 N
+219  1 N   A LYS 90  ? ? CA  A LYS 90  ? ? 1.274 1.459 -0.185 0.020 N
+220  1 CA  A LYS 90  ? ? CB  A LYS 90  ? ? 1.692 1.535 0.157  0.022 N
+221  1 CB  A LYS 90  ? ? CG  A LYS 90  ? ? 1.721 1.521 0.200  0.027 N
+222  1 CG  A LYS 90  ? ? CD  A LYS 90  ? ? 1.189 1.520 -0.331 0.034 N
+223  1 CD  A LYS 90  ? ? CE  A LYS 90  ? ? 1.839 1.508 0.331  0.025 N
+224  1 CE  A LYS 90  ? ? NZ  A LYS 90  ? ? 2.667 1.486 1.181  0.025 N
+225  1 CB  A ARG 92  ? ? CG  A ARG 92  ? ? 1.345 1.521 -0.176 0.027 N
+226  1 CG  A ARG 92  ? ? CD  A ARG 92  ? ? 2.251 1.515 0.736  0.025 N
+227  1 CD  A ARG 92  ? ? NE  A ARG 92  ? ? 1.342 1.460 -0.118 0.017 N
+228  1 NE  A ARG 92  ? ? CZ  A ARG 92  ? ? 2.569 1.326 1.243  0.013 N
+229  1 CZ  A ARG 92  ? ? NH1 A ARG 92  ? ? 1.497 1.326 0.171  0.013 N
+230  1 CZ  A ARG 92  ? ? NH2 A ARG 92  ? ? 0.853 1.326 -0.473 0.013 N
+231  1 CA  A ARG 92  ? ? C   A ARG 92  ? ? 1.368 1.525 -0.157 0.026 N
+232  1 CA  A ASP 94  ? ? C   A ASP 94  ? ? 1.691 1.525 0.166  0.026 N
+233  1 C   A PRO 95  ? ? O   A PRO 95  ? ? 1.355 1.228 0.127  0.020 N
+234  1 CA  A VAL 96  ? ? CB  A VAL 96  ? ? 1.691 1.543 0.148  0.021 N
+235  1 CB  A VAL 96  ? ? CG1 A VAL 96  ? ? 1.110 1.524 -0.414 0.021 N
+236  1 CB  A VAL 96  ? ? CG2 A VAL 96  ? ? 1.018 1.524 -0.506 0.021 N
+237  1 CG  A ASN 97  ? ? ND2 A ASN 97  ? ? 1.477 1.324 0.153  0.025 N
+238  1 CD1 A PHE 98  ? ? CE1 A PHE 98  ? ? 1.247 1.388 -0.141 0.020 N
+239  1 CZ  A PHE 98  ? ? CE2 A PHE 98  ? ? 1.238 1.369 -0.131 0.019 N
+240  1 CB  A LYS 99  ? ? CG  A LYS 99  ? ? 1.091 1.521 -0.430 0.027 N
+241  1 CG  A LYS 99  ? ? CD  A LYS 99  ? ? 0.997 1.520 -0.523 0.034 N
+242  1 CD  A LYS 99  ? ? CE  A LYS 99  ? ? 1.947 1.508 0.439  0.025 N
+243  1 CE  A LYS 99  ? ? NZ  A LYS 99  ? ? 2.201 1.486 0.715  0.025 N
+244  1 CA  A LYS 99  ? ? C   A LYS 99  ? ? 1.327 1.525 -0.198 0.026 N
+245  1 N   A CYS 104 ? ? CA  A CYS 104 ? ? 1.643 1.459 0.184  0.020 N
+246  1 CB  A LEU 105 ? ? CG  A LEU 105 ? ? 1.288 1.521 -0.233 0.029 N
+247  1 CG  A LEU 105 ? ? CD2 A LEU 105 ? ? 1.194 1.514 -0.320 0.037 N
+248  1 CB  A LEU 106 ? ? CG  A LEU 106 ? ? 1.146 1.521 -0.375 0.029 N
+249  1 CA  A LEU 106 ? ? C   A LEU 106 ? ? 1.335 1.525 -0.190 0.026 N
+250  1 C   A LEU 106 ? ? O   A LEU 106 ? ? 1.370 1.229 0.141  0.019 N
+251  1 CA  A THR 108 ? ? CB  A THR 108 ? ? 1.692 1.529 0.163  0.026 N
+252  1 CG  A LEU 109 ? ? CD2 A LEU 109 ? ? 1.250 1.514 -0.264 0.037 N
+253  1 ND1 A HIS 112 ? ? CE1 A HIS 112 ? ? 1.612 1.343 0.269  0.025 N
+254  1 CA  A LEU 113 ? ? CB  A LEU 113 ? ? 1.384 1.533 -0.149 0.023 N
+255  1 CB  A LEU 113 ? ? CG  A LEU 113 ? ? 1.711 1.521 0.190  0.029 N
+256  1 N   A PRO 114 ? ? CA  A PRO 114 ? ? 1.603 1.468 0.135  0.017 N
+257  1 CA  A PRO 114 ? ? C   A PRO 114 ? ? 1.664 1.524 0.140  0.020 N
+258  1 CD  A GLU 116 ? ? OE2 A GLU 116 ? ? 1.435 1.252 0.183  0.011 N
+259  1 CE2 A PHE 117 ? ? CD2 A PHE 117 ? ? 1.522 1.388 0.134  0.020 N
+260  1 CA  A PRO 119 ? ? C   A PRO 119 ? ? 1.387 1.524 -0.137 0.020 N
+261  1 N   A ALA 120 ? ? CA  A ALA 120 ? ? 1.326 1.459 -0.133 0.020 N
+262  1 C   A ALA 120 ? ? N   A VAL 121 ? ? 1.168 1.336 -0.168 0.023 Y
+263  1 N   A HIS 122 ? ? CA  A HIS 122 ? ? 1.657 1.459 0.198  0.020 N
+264  1 ND1 A HIS 122 ? ? CE1 A HIS 122 ? ? 1.530 1.343 0.187  0.025 N
+265  1 CB  A LYS 127 ? ? CG  A LYS 127 ? ? 0.712 1.521 -0.809 0.027 N
+266  1 CG  A LYS 127 ? ? CD  A LYS 127 ? ? 1.974 1.520 0.454  0.034 N
+267  1 C   A LYS 127 ? ? N   A PHE 128 ? ? 1.162 1.336 -0.174 0.023 Y
+268  1 CG  A PHE 128 ? ? CD2 A PHE 128 ? ? 1.218 1.383 -0.165 0.015 N
+269  1 CG  A PHE 128 ? ? CD1 A PHE 128 ? ? 1.476 1.383 0.093  0.015 N
+270  1 CE2 A PHE 128 ? ? CD2 A PHE 128 ? ? 1.512 1.388 0.124  0.020 N
+271  1 CA  A SER 131 ? ? CB  A SER 131 ? ? 1.635 1.525 0.110  0.015 N
+272  1 CB  A SER 131 ? ? OG  A SER 131 ? ? 1.216 1.418 -0.202 0.013 N
+273  1 CA  A VAL 132 ? ? CB  A VAL 132 ? ? 1.381 1.543 -0.162 0.021 N
+274  1 C   A VAL 132 ? ? O   A VAL 132 ? ? 1.379 1.229 0.150  0.019 N
+275  1 CB  A THR 134 ? ? OG1 A THR 134 ? ? 1.174 1.428 -0.254 0.020 N
+276  1 CA  A THR 134 ? ? C   A THR 134 ? ? 1.312 1.525 -0.213 0.026 N
+277  1 N   A THR 137 ? ? CA  A THR 137 ? ? 1.647 1.459 0.188  0.020 N
+278  1 CA  A THR 137 ? ? CB  A THR 137 ? ? 1.910 1.529 0.381  0.026 N
+279  1 CB  A THR 137 ? ? OG1 A THR 137 ? ? 1.663 1.428 0.235  0.020 N
+280  1 CB  A THR 137 ? ? CG2 A THR 137 ? ? 1.007 1.519 -0.512 0.033 N
+281  1 CA  A SER 138 ? ? CB  A SER 138 ? ? 2.119 1.525 0.594  0.015 N
+282  1 CB  A SER 138 ? ? OG  A SER 138 ? ? 1.304 1.418 -0.114 0.013 N
+283  1 N   A LYS 139 ? ? CA  A LYS 139 ? ? 1.592 1.459 0.133  0.020 N
+284  1 CE  A LYS 139 ? ? NZ  A LYS 139 ? ? 1.956 1.486 0.470  0.025 N
+285  1 CG  A TYR 140 ? ? CD1 A TYR 140 ? ? 1.516 1.387 0.129  0.013 N
+286  1 CE1 A TYR 140 ? ? CZ  A TYR 140 ? ? 1.219 1.381 -0.162 0.013 N
+287  1 CZ  A TYR 140 ? ? OH  A TYR 140 ? ? 1.207 1.374 -0.167 0.017 N
+288  1 N   A ARG 141 ? ? CA  A ARG 141 ? ? 1.617 1.459 0.158  0.020 N
+289  1 CA  A ARG 141 ? ? CB  A ARG 141 ? ? 1.351 1.535 -0.184 0.022 N
+290  1 CB  A ARG 141 ? ? CG  A ARG 141 ? ? 1.792 1.521 0.271  0.027 N
+291  1 NE  A ARG 141 ? ? CZ  A ARG 141 ? ? 1.466 1.326 0.140  0.013 N
+292  1 N   B VAL 1   ? ? CA  B VAL 1   ? ? 1.685 1.459 0.226  0.020 N
+293  1 CA  B VAL 1   ? ? CB  B VAL 1   ? ? 1.860 1.543 0.317  0.021 N
+294  1 CB  B VAL 1   ? ? CG1 B VAL 1   ? ? 2.028 1.524 0.504  0.021 N
+295  1 CB  B VAL 1   ? ? CG2 B VAL 1   ? ? 1.242 1.524 -0.282 0.021 N
+296  1 CA  B VAL 1   ? ? C   B VAL 1   ? ? 2.086 1.525 0.561  0.026 N
+297  1 C   B VAL 1   ? ? O   B VAL 1   ? ? 1.702 1.229 0.473  0.019 N
+298  1 C   B VAL 1   ? ? N   B HIS 2   ? ? 0.787 1.336 -0.549 0.023 Y
+299  1 CA  B HIS 2   ? ? CB  B HIS 2   ? ? 2.012 1.535 0.477  0.022 N
+300  1 CB  B HIS 2   ? ? CG  B HIS 2   ? ? 0.834 1.492 -0.658 0.016 N
+301  1 CG  B HIS 2   ? ? CD2 B HIS 2   ? ? 2.053 1.354 0.699  0.009 N
+302  1 CG  B HIS 2   ? ? ND1 B HIS 2   ? ? 1.884 1.383 0.501  0.022 N
+303  1 ND1 B HIS 2   ? ? CE1 B HIS 2   ? ? 2.177 1.343 0.834  0.025 N
+304  1 CE1 B HIS 2   ? ? NE2 B HIS 2   ? ? 1.609 1.333 0.276  0.019 N
+305  1 NE2 B HIS 2   ? ? CD2 B HIS 2   ? ? 2.087 1.415 0.672  0.021 N
+306  1 CA  B HIS 2   ? ? C   B HIS 2   ? ? 1.841 1.525 0.316  0.026 N
+307  1 C   B HIS 2   ? ? O   B HIS 2   ? ? 1.433 1.229 0.204  0.019 N
+308  1 C   B HIS 2   ? ? N   B LEU 3   ? ? 1.118 1.336 -0.218 0.023 Y
+309  1 N   B LEU 3   ? ? CA  B LEU 3   ? ? 1.590 1.459 0.131  0.020 N
+310  1 CA  B LEU 3   ? ? CB  B LEU 3   ? ? 1.771 1.533 0.238  0.023 N
+311  1 CA  B THR 4   ? ? C   B THR 4   ? ? 1.266 1.525 -0.259 0.026 N
+312  1 N   B PRO 5   ? ? CA  B PRO 5   ? ? 1.185 1.468 -0.283 0.017 N
+313  1 CD  B PRO 5   ? ? N   B PRO 5   ? ? 1.813 1.474 0.339  0.014 N
+314  1 CA  B PRO 5   ? ? C   B PRO 5   ? ? 1.783 1.524 0.259  0.020 N
+315  1 CB  B GLU 6   ? ? CG  B GLU 6   ? ? 1.037 1.517 -0.480 0.019 N
+316  1 CG  B GLU 6   ? ? CD  B GLU 6   ? ? 2.069 1.515 0.554  0.015 N
+317  1 CD  B GLU 6   ? ? OE1 B GLU 6   ? ? 1.669 1.252 0.417  0.011 N
+318  1 CD  B GLU 6   ? ? OE2 B GLU 6   ? ? 0.950 1.252 -0.302 0.011 N
+319  1 CA  B GLU 6   ? ? C   B GLU 6   ? ? 1.770 1.525 0.245  0.026 N
+320  1 C   B GLU 6   ? ? O   B GLU 6   ? ? 1.470 1.229 0.241  0.019 N
+321  1 C   B GLU 6   ? ? N   B GLU 7   ? ? 1.196 1.336 -0.140 0.023 Y
+322  1 N   B GLU 7   ? ? CA  B GLU 7   ? ? 1.619 1.459 0.160  0.020 N
+323  1 CA  B GLU 7   ? ? CB  B GLU 7   ? ? 0.983 1.535 -0.552 0.022 N
+324  1 CB  B GLU 7   ? ? CG  B GLU 7   ? ? 1.770 1.517 0.253  0.019 N
+325  1 CG  B GLU 7   ? ? CD  B GLU 7   ? ? 1.380 1.515 -0.135 0.015 N
+326  1 CD  B GLU 7   ? ? OE2 B GLU 7   ? ? 1.370 1.252 0.118  0.011 N
+327  1 N   B LYS 8   ? ? CA  B LYS 8   ? ? 1.328 1.459 -0.131 0.020 N
+328  1 CA  B LYS 8   ? ? CB  B LYS 8   ? ? 1.744 1.535 0.209  0.022 N
+329  1 CB  B LYS 8   ? ? CG  B LYS 8   ? ? 0.867 1.521 -0.654 0.027 N
+330  1 CG  B LYS 8   ? ? CD  B LYS 8   ? ? 1.784 1.520 0.264  0.034 N
+331  1 CD  B LYS 8   ? ? CE  B LYS 8   ? ? 1.349 1.508 -0.159 0.025 N
+332  1 CE  B LYS 8   ? ? NZ  B LYS 8   ? ? 2.273 1.486 0.787  0.025 N
+333  1 C   B LYS 8   ? ? O   B LYS 8   ? ? 1.465 1.229 0.236  0.019 N
+334  1 N   B SER 9   ? ? CA  B SER 9   ? ? 1.097 1.459 -0.362 0.020 N
+335  1 CA  B SER 9   ? ? CB  B SER 9   ? ? 1.788 1.525 0.263  0.015 N
+336  1 CA  B SER 9   ? ? C   B SER 9   ? ? 1.867 1.525 0.342  0.026 N
+337  1 N   B ALA 10  ? ? CA  B ALA 10  ? ? 1.289 1.459 -0.170 0.020 N
+338  1 CA  B ALA 10  ? ? C   B ALA 10  ? ? 1.779 1.525 0.254  0.026 N
+339  1 CA  B VAL 11  ? ? CB  B VAL 11  ? ? 1.393 1.543 -0.150 0.021 N
+340  1 CA  B THR 12  ? ? CB  B THR 12  ? ? 1.704 1.529 0.175  0.026 N
+341  1 CB  B THR 12  ? ? OG1 B THR 12  ? ? 1.223 1.428 -0.205 0.020 N
+342  1 CB  B THR 12  ? ? CG2 B THR 12  ? ? 0.577 1.519 -0.942 0.033 N
+343  1 N   B ALA 13  ? ? CA  B ALA 13  ? ? 1.325 1.459 -0.134 0.020 N
+344  1 CA  B ALA 13  ? ? CB  B ALA 13  ? ? 1.674 1.520 0.154  0.021 N
+345  1 C   B ALA 13  ? ? N   B LEU 14  ? ? 1.490 1.336 0.154  0.023 Y
+346  1 CB  B TRP 15  ? ? CG  B TRP 15  ? ? 1.611 1.498 0.113  0.018 N
+347  1 CG  B TRP 15  ? ? CD1 B TRP 15  ? ? 1.254 1.363 -0.109 0.014 N
+348  1 NE1 B TRP 15  ? ? CE2 B TRP 15  ? ? 1.470 1.371 0.099  0.013 N
+349  1 CE2 B TRP 15  ? ? CD2 B TRP 15  ? ? 1.494 1.409 0.085  0.012 N
+350  1 N   B GLY 16  ? ? CA  B GLY 16  ? ? 1.577 1.456 0.121  0.015 N
+351  1 CA  B GLY 16  ? ? C   B GLY 16  ? ? 1.395 1.514 -0.119 0.016 N
+352  1 CD  B LYS 17  ? ? CE  B LYS 17  ? ? 1.692 1.508 0.184  0.025 N
+353  1 C   B LYS 17  ? ? O   B LYS 17  ? ? 1.416 1.229 0.187  0.019 N
+354  1 CB  B VAL 18  ? ? CG2 B VAL 18  ? ? 1.713 1.524 0.189  0.021 N
+355  1 CG  B ASN 19  ? ? OD1 B ASN 19  ? ? 1.064 1.235 -0.171 0.022 N
+356  1 CG  B ASN 19  ? ? ND2 B ASN 19  ? ? 1.491 1.324 0.167  0.025 N
+357  1 CA  B VAL 20  ? ? C   B VAL 20  ? ? 1.304 1.525 -0.221 0.026 N
+358  1 C   B VAL 20  ? ? O   B VAL 20  ? ? 1.385 1.229 0.156  0.019 N
+359  1 CB  B ASP 21  ? ? CG  B ASP 21  ? ? 1.837 1.513 0.324  0.021 N
+360  1 CG  B ASP 21  ? ? OD2 B ASP 21  ? ? 1.459 1.249 0.210  0.023 N
+361  1 N   B GLU 22  ? ? CA  B GLU 22  ? ? 1.615 1.459 0.156  0.020 N
+362  1 CB  B GLU 22  ? ? CG  B GLU 22  ? ? 1.315 1.517 -0.202 0.019 N
+363  1 CG  B GLU 22  ? ? CD  B GLU 22  ? ? 1.854 1.515 0.339  0.015 N
+364  1 CD  B GLU 22  ? ? OE1 B GLU 22  ? ? 1.766 1.252 0.514  0.011 N
+365  1 CD  B GLU 22  ? ? OE2 B GLU 22  ? ? 2.118 1.252 0.866  0.011 N
+366  1 CB  B GLU 26  ? ? CG  B GLU 26  ? ? 1.726 1.517 0.209  0.019 N
+367  1 CG  B GLU 26  ? ? CD  B GLU 26  ? ? 1.381 1.515 -0.134 0.015 N
+368  1 CD  B GLU 26  ? ? OE1 B GLU 26  ? ? 2.826 1.252 1.574  0.011 N
+369  1 CD  B GLU 26  ? ? OE2 B GLU 26  ? ? 2.428 1.252 1.176  0.011 N
+370  1 CB  B LEU 28  ? ? CG  B LEU 28  ? ? 1.734 1.521 0.213  0.029 N
+371  1 CG  B LEU 32  ? ? CD1 B LEU 32  ? ? 1.262 1.514 -0.252 0.037 N
+372  1 N   B VAL 34  ? ? CA  B VAL 34  ? ? 1.595 1.459 0.136  0.020 N
+373  1 CG  B TYR 35  ? ? CD1 B TYR 35  ? ? 1.470 1.387 0.083  0.013 N
+374  1 CZ  B TYR 35  ? ? CE2 B TYR 35  ? ? 1.281 1.381 -0.100 0.013 N
+375  1 CE2 B TYR 35  ? ? CD2 B TYR 35  ? ? 1.288 1.389 -0.101 0.015 N
+376  1 C   B TYR 35  ? ? N   B PRO 36  ? ? 1.221 1.338 -0.117 0.019 Y
+377  1 CG  B TRP 37  ? ? CD1 B TRP 37  ? ? 1.479 1.363 0.116  0.014 N
+378  1 NE1 B TRP 37  ? ? CE2 B TRP 37  ? ? 1.253 1.371 -0.118 0.013 N
+379  1 CE2 B TRP 37  ? ? CD2 B TRP 37  ? ? 1.489 1.409 0.080  0.012 N
+380  1 CZ3 B TRP 37  ? ? CH2 B TRP 37  ? ? 1.283 1.396 -0.113 0.016 N
+381  1 N   B GLN 39  ? ? CA  B GLN 39  ? ? 1.593 1.459 0.134  0.020 N
+382  1 CD  B ARG 40  ? ? NE  B ARG 40  ? ? 1.241 1.460 -0.219 0.017 N
+383  1 NE  B ARG 40  ? ? CZ  B ARG 40  ? ? 1.530 1.326 0.204  0.013 N
+384  1 CZ  B ARG 40  ? ? NH1 B ARG 40  ? ? 1.157 1.326 -0.169 0.013 N
+385  1 CZ  B ARG 40  ? ? NH2 B ARG 40  ? ? 1.558 1.326 0.232  0.013 N
+386  1 C   B ARG 40  ? ? N   B PHE 41  ? ? 1.129 1.336 -0.207 0.023 Y
+387  1 CG  B PHE 41  ? ? CD2 B PHE 41  ? ? 1.536 1.383 0.153  0.015 N
+388  1 CE1 B PHE 41  ? ? CZ  B PHE 41  ? ? 1.238 1.369 -0.131 0.019 N
+389  1 CA  B PHE 41  ? ? C   B PHE 41  ? ? 1.773 1.525 0.248  0.026 N
+390  1 C   B PHE 41  ? ? O   B PHE 41  ? ? 1.072 1.229 -0.157 0.019 N
+391  1 CB  B PHE 42  ? ? CG  B PHE 42  ? ? 1.364 1.509 -0.145 0.017 N
+392  1 CG  B PHE 42  ? ? CD1 B PHE 42  ? ? 1.686 1.383 0.303  0.015 N
+393  1 CE1 B PHE 42  ? ? CZ  B PHE 42  ? ? 1.187 1.369 -0.182 0.019 N
+394  1 CZ  B PHE 42  ? ? CE2 B PHE 42  ? ? 1.515 1.369 0.146  0.019 N
+395  1 CA  B GLU 43  ? ? CB  B GLU 43  ? ? 1.261 1.535 -0.274 0.022 N
+396  1 CG  B GLU 43  ? ? CD  B GLU 43  ? ? 2.425 1.515 0.910  0.015 N
+397  1 CD  B GLU 43  ? ? OE1 B GLU 43  ? ? 0.848 1.252 -0.404 0.011 N
+398  1 CD  B GLU 43  ? ? OE2 B GLU 43  ? ? 1.511 1.252 0.259  0.011 N
+399  1 N   B SER 44  ? ? CA  B SER 44  ? ? 1.581 1.459 0.122  0.020 N
+400  1 CA  B SER 44  ? ? CB  B SER 44  ? ? 1.396 1.525 -0.129 0.015 N
+401  1 CB  B SER 44  ? ? OG  B SER 44  ? ? 1.176 1.418 -0.242 0.013 N
+402  1 C   B SER 44  ? ? O   B SER 44  ? ? 1.501 1.229 0.272  0.019 N
+403  1 C   B SER 44  ? ? N   B PHE 45  ? ? 1.552 1.336 0.216  0.023 Y
+404  1 CB  B PHE 45  ? ? CG  B PHE 45  ? ? 1.643 1.509 0.134  0.017 N
+405  1 CG  B PHE 45  ? ? CD2 B PHE 45  ? ? 1.045 1.383 -0.338 0.015 N
+406  1 CD1 B PHE 45  ? ? CE1 B PHE 45  ? ? 1.624 1.388 0.236  0.020 N
+407  1 CE1 B PHE 45  ? ? CZ  B PHE 45  ? ? 1.011 1.369 -0.358 0.019 N
+408  1 N   B GLY 46  ? ? CA  B GLY 46  ? ? 1.349 1.456 -0.107 0.015 N
+409  1 CA  B GLY 46  ? ? C   B GLY 46  ? ? 1.677 1.514 0.163  0.016 N
+410  1 C   B GLY 46  ? ? O   B GLY 46  ? ? 1.437 1.232 0.205  0.016 N
+411  1 C   B GLY 46  ? ? N   B ASP 47  ? ? 1.074 1.336 -0.262 0.023 Y
+412  1 N   B ASP 47  ? ? CA  B ASP 47  ? ? 1.671 1.459 0.212  0.020 N
+413  1 CG  B ASP 47  ? ? OD2 B ASP 47  ? ? 1.783 1.249 0.534  0.023 N
+414  1 CA  B ASP 47  ? ? C   B ASP 47  ? ? 1.747 1.525 0.222  0.026 N
+415  1 C   B ASP 47  ? ? N   B LEU 48  ? ? 1.487 1.336 0.151  0.023 Y
+416  1 N   B LEU 48  ? ? CA  B LEU 48  ? ? 1.588 1.459 0.129  0.020 N
+417  1 CA  B LEU 48  ? ? CB  B LEU 48  ? ? 1.390 1.533 -0.143 0.023 N
+418  1 N   B SER 49  ? ? CA  B SER 49  ? ? 1.674 1.459 0.215  0.020 N
+419  1 CA  B SER 49  ? ? CB  B SER 49  ? ? 1.834 1.525 0.309  0.015 N
+420  1 CB  B SER 49  ? ? OG  B SER 49  ? ? 1.707 1.418 0.289  0.013 N
+421  1 CA  B SER 49  ? ? C   B SER 49  ? ? 1.310 1.525 -0.215 0.026 N
+422  1 C   B SER 49  ? ? O   B SER 49  ? ? 1.789 1.229 0.560  0.019 N
+423  1 N   B THR 50  ? ? CA  B THR 50  ? ? 1.286 1.459 -0.173 0.020 N
+424  1 CA  B THR 50  ? ? CB  B THR 50  ? ? 1.277 1.529 -0.252 0.026 N
+425  1 CB  B THR 50  ? ? CG2 B THR 50  ? ? 1.749 1.519 0.230  0.033 N
+426  1 CD  B PRO 51  ? ? N   B PRO 51  ? ? 1.615 1.474 0.141  0.014 N
+427  1 C   B PRO 51  ? ? O   B PRO 51  ? ? 1.411 1.228 0.183  0.020 N
+428  1 CB  B ASP 52  ? ? CG  B ASP 52  ? ? 1.773 1.513 0.260  0.021 N
+429  1 CG  B ASP 52  ? ? OD1 B ASP 52  ? ? 1.059 1.249 -0.190 0.023 N
+430  1 CA  B ALA 53  ? ? CB  B ALA 53  ? ? 1.364 1.520 -0.156 0.021 N
+431  1 C   B ALA 53  ? ? N   B VAL 54  ? ? 1.484 1.336 0.148  0.023 Y
+432  1 CA  B VAL 54  ? ? CB  B VAL 54  ? ? 1.693 1.543 0.150  0.021 N
+433  1 CA  B VAL 54  ? ? C   B VAL 54  ? ? 1.309 1.525 -0.216 0.026 N
+434  1 C   B VAL 54  ? ? O   B VAL 54  ? ? 1.357 1.229 0.128  0.019 N
+435  1 CG  B ASN 57  ? ? OD1 B ASN 57  ? ? 1.073 1.235 -0.162 0.022 N
+436  1 CB  B PRO 58  ? ? CG  B PRO 58  ? ? 1.168 1.495 -0.327 0.050 N
+437  1 CD  B PRO 58  ? ? N   B PRO 58  ? ? 1.781 1.474 0.307  0.014 N
+438  1 CA  B LYS 59  ? ? CB  B LYS 59  ? ? 1.358 1.535 -0.177 0.022 N
+439  1 CG  B LYS 59  ? ? CD  B LYS 59  ? ? 1.003 1.520 -0.517 0.034 N
+440  1 CD  B LYS 59  ? ? CE  B LYS 59  ? ? 2.363 1.508 0.855  0.025 N
+441  1 CE  B LYS 59  ? ? NZ  B LYS 59  ? ? 1.919 1.486 0.433  0.025 N
+442  1 CB  B LYS 61  ? ? CG  B LYS 61  ? ? 1.238 1.521 -0.283 0.027 N
+443  1 CG  B LYS 61  ? ? CD  B LYS 61  ? ? 1.928 1.520 0.408  0.034 N
+444  1 CD  B LYS 61  ? ? CE  B LYS 61  ? ? 1.696 1.508 0.188  0.025 N
+445  1 CE  B LYS 61  ? ? NZ  B LYS 61  ? ? 1.746 1.486 0.260  0.025 N
+446  1 CA  B HIS 63  ? ? CB  B HIS 63  ? ? 1.390 1.535 -0.145 0.022 N
+447  1 CG  B HIS 63  ? ? CD2 B HIS 63  ? ? 1.452 1.354 0.098  0.009 N
+448  1 CG  B HIS 63  ? ? ND1 B HIS 63  ? ? 1.645 1.383 0.262  0.022 N
+449  1 ND1 B HIS 63  ? ? CE1 B HIS 63  ? ? 1.572 1.343 0.229  0.025 N
+450  1 CE1 B HIS 63  ? ? NE2 B HIS 63  ? ? 1.201 1.317 -0.116 0.011 N
+451  1 C   B GLY 64  ? ? O   B GLY 64  ? ? 1.109 1.232 -0.123 0.016 N
+452  1 CA  B LYS 65  ? ? CB  B LYS 65  ? ? 1.799 1.535 0.264  0.022 N
+453  1 CB  B LYS 65  ? ? CG  B LYS 65  ? ? 0.577 1.521 -0.944 0.027 N
+454  1 CG  B LYS 65  ? ? CD  B LYS 65  ? ? 2.492 1.520 0.972  0.034 N
+455  1 CD  B LYS 65  ? ? CE  B LYS 65  ? ? 2.349 1.508 0.841  0.025 N
+456  1 CE  B LYS 65  ? ? NZ  B LYS 65  ? ? 2.586 1.486 1.100  0.025 N
+457  1 N   B LYS 66  ? ? CA  B LYS 66  ? ? 1.182 1.459 -0.277 0.020 N
+458  1 CD  B LYS 66  ? ? CE  B LYS 66  ? ? 2.367 1.508 0.859  0.025 N
+459  1 CE  B LYS 66  ? ? NZ  B LYS 66  ? ? 1.806 1.486 0.320  0.025 N
+460  1 CA  B LYS 66  ? ? C   B LYS 66  ? ? 1.722 1.525 0.197  0.026 N
+461  1 N   B VAL 67  ? ? CA  B VAL 67  ? ? 1.594 1.459 0.135  0.020 N
+462  1 CG  B LEU 68  ? ? CD2 B LEU 68  ? ? 1.273 1.514 -0.241 0.037 N
+463  1 N   B GLY 69  ? ? CA  B GLY 69  ? ? 1.288 1.456 -0.168 0.015 N
+464  1 CA  B GLY 69  ? ? C   B GLY 69  ? ? 1.646 1.514 0.132  0.016 N
+465  1 C   B GLY 69  ? ? O   B GLY 69  ? ? 1.102 1.232 -0.130 0.016 N
+466  1 C   B GLY 69  ? ? N   B ALA 70  ? ? 1.533 1.336 0.197  0.023 Y
+467  1 CG  B PHE 71  ? ? CD2 B PHE 71  ? ? 1.496 1.383 0.113  0.015 N
+468  1 C   B PHE 71  ? ? N   B SER 72  ? ? 1.046 1.336 -0.290 0.023 Y
+469  1 N   B SER 72  ? ? CA  B SER 72  ? ? 1.606 1.459 0.147  0.020 N
+470  1 CB  B SER 72  ? ? OG  B SER 72  ? ? 1.325 1.418 -0.093 0.013 N
+471  1 N   B ASP 73  ? ? CA  B ASP 73  ? ? 1.592 1.459 0.133  0.020 N
+472  1 CA  B ASP 73  ? ? CB  B ASP 73  ? ? 1.692 1.535 0.157  0.022 N
+473  1 CB  B ASP 73  ? ? CG  B ASP 73  ? ? 1.715 1.513 0.202  0.021 N
+474  1 CG  B ASP 73  ? ? OD1 B ASP 73  ? ? 1.467 1.249 0.218  0.023 N
+475  1 CG  B ASP 73  ? ? OD2 B ASP 73  ? ? 1.008 1.249 -0.241 0.023 N
+476  1 CA  B ASP 73  ? ? C   B ASP 73  ? ? 1.197 1.525 -0.328 0.026 N
+477  1 C   B ASP 73  ? ? O   B ASP 73  ? ? 1.395 1.229 0.166  0.019 N
+478  1 N   B GLY 74  ? ? CA  B GLY 74  ? ? 1.273 1.456 -0.183 0.015 N
+479  1 CA  B GLY 74  ? ? C   B GLY 74  ? ? 1.320 1.514 -0.194 0.016 N
+480  1 CB  B LEU 75  ? ? CG  B LEU 75  ? ? 1.276 1.521 -0.245 0.029 N
+481  1 N   B ALA 76  ? ? CA  B ALA 76  ? ? 1.327 1.459 -0.132 0.020 N
+482  1 C   B ALA 76  ? ? O   B ALA 76  ? ? 0.913 1.229 -0.316 0.019 N
+483  1 C   B ALA 76  ? ? N   B HIS 77  ? ? 1.636 1.336 0.300  0.023 Y
+484  1 CA  B HIS 77  ? ? CB  B HIS 77  ? ? 1.393 1.535 -0.142 0.022 N
+485  1 CB  B HIS 77  ? ? CG  B HIS 77  ? ? 1.658 1.496 0.162  0.018 N
+486  1 CG  B HIS 77  ? ? CD2 B HIS 77  ? ? 1.835 1.354 0.481  0.009 N
+487  1 ND1 B HIS 77  ? ? CE1 B HIS 77  ? ? 1.140 1.323 -0.183 0.015 N
+488  1 N   B ASP 79  ? ? CA  B ASP 79  ? ? 1.595 1.459 0.136  0.020 N
+489  1 CB  B ASP 79  ? ? CG  B ASP 79  ? ? 1.176 1.513 -0.337 0.021 N
+490  1 CG  B ASP 79  ? ? OD2 B ASP 79  ? ? 1.671 1.249 0.422  0.023 N
+491  1 C   B ASP 79  ? ? O   B ASP 79  ? ? 1.018 1.229 -0.211 0.019 N
+492  1 N   B ASN 80  ? ? CA  B ASN 80  ? ? 1.727 1.459 0.268  0.020 N
+493  1 CA  B ASN 80  ? ? CB  B ASN 80  ? ? 1.364 1.527 -0.163 0.026 N
+494  1 CB  B ASN 80  ? ? CG  B ASN 80  ? ? 1.751 1.506 0.245  0.023 N
+495  1 CG  B ASN 80  ? ? OD1 B ASN 80  ? ? 1.507 1.235 0.272  0.022 N
+496  1 CA  B ASN 80  ? ? C   B ASN 80  ? ? 1.797 1.525 0.272  0.026 N
+497  1 C   B ASN 80  ? ? O   B ASN 80  ? ? 1.078 1.229 -0.151 0.019 N
+498  1 N   B LEU 81  ? ? CA  B LEU 81  ? ? 1.681 1.459 0.222  0.020 N
+499  1 CA  B LEU 81  ? ? C   B LEU 81  ? ? 1.320 1.525 -0.205 0.026 N
+500  1 CD  B LYS 82  ? ? CE  B LYS 82  ? ? 0.698 1.508 -0.810 0.025 N
+501  1 CE  B LYS 82  ? ? NZ  B LYS 82  ? ? 2.346 1.486 0.860  0.025 N
+502  1 CA  B LYS 82  ? ? C   B LYS 82  ? ? 1.277 1.525 -0.248 0.026 N
+503  1 N   B GLY 83  ? ? CA  B GLY 83  ? ? 1.595 1.456 0.139  0.015 N
+504  1 CA  B GLY 83  ? ? C   B GLY 83  ? ? 1.407 1.514 -0.107 0.016 N
+505  1 CB  B THR 84  ? ? OG1 B THR 84  ? ? 1.591 1.428 0.163  0.020 N
+506  1 CB  B THR 84  ? ? CG2 B THR 84  ? ? 1.250 1.519 -0.269 0.033 N
+507  1 CB  B PHE 85  ? ? CG  B PHE 85  ? ? 1.388 1.509 -0.121 0.017 N
+508  1 CA  B THR 87  ? ? CB  B THR 87  ? ? 1.948 1.529 0.419  0.026 N
+509  1 CB  B THR 87  ? ? CG2 B THR 87  ? ? 2.023 1.519 0.504  0.033 N
+510  1 CB  B SER 89  ? ? OG  B SER 89  ? ? 1.583 1.418 0.165  0.013 N
+511  1 N   B GLU 90  ? ? CA  B GLU 90  ? ? 1.337 1.459 -0.122 0.020 N
+512  1 CA  B GLU 90  ? ? CB  B GLU 90  ? ? 1.844 1.535 0.309  0.022 N
+513  1 CB  B GLU 90  ? ? CG  B GLU 90  ? ? 1.301 1.517 -0.216 0.019 N
+514  1 CG  B GLU 90  ? ? CD  B GLU 90  ? ? 2.065 1.515 0.550  0.015 N
+515  1 CD  B GLU 90  ? ? OE1 B GLU 90  ? ? 0.920 1.252 -0.332 0.011 N
+516  1 C   B GLU 90  ? ? N   B LEU 91  ? ? 1.484 1.336 0.148  0.023 Y
+517  1 CG  B LEU 91  ? ? CD2 B LEU 91  ? ? 1.287 1.514 -0.227 0.037 N
+518  1 NE2 B HIS 92  ? ? CD2 B HIS 92  ? ? 1.238 1.373 -0.135 0.011 N
+519  1 CB  B CYS 93  ? ? SG  B CYS 93  ? ? 1.957 1.818 0.139  0.017 N
+520  1 C   B CYS 93  ? ? O   B CYS 93  ? ? 1.105 1.229 -0.124 0.019 N
+521  1 CB  B ASP 94  ? ? CG  B ASP 94  ? ? 1.699 1.513 0.186  0.021 N
+522  1 CG  B ASP 94  ? ? OD2 B ASP 94  ? ? 0.974 1.249 -0.275 0.023 N
+523  1 C   B ASP 94  ? ? O   B ASP 94  ? ? 1.385 1.229 0.156  0.019 N
+524  1 CA  B LYS 95  ? ? CB  B LYS 95  ? ? 1.721 1.535 0.186  0.022 N
+525  1 CA  B LYS 95  ? ? C   B LYS 95  ? ? 1.311 1.525 -0.214 0.026 N
+526  1 C   B LYS 95  ? ? O   B LYS 95  ? ? 1.096 1.229 -0.133 0.019 N
+527  1 C   B LYS 95  ? ? N   B LEU 96  ? ? 1.514 1.336 0.178  0.023 Y
+528  1 CB  B HIS 97  ? ? CG  B HIS 97  ? ? 1.632 1.496 0.136  0.018 N
+529  1 CB  B VAL 98  ? ? CG2 B VAL 98  ? ? 1.656 1.524 0.132  0.021 N
+530  1 CA  B VAL 98  ? ? C   B VAL 98  ? ? 1.689 1.525 0.164  0.026 N
+531  1 CG  B GLU 101 ? ? CD  B GLU 101 ? ? 2.023 1.515 0.508  0.015 N
+532  1 CD  B GLU 101 ? ? OE1 B GLU 101 ? ? 1.168 1.252 -0.084 0.011 N
+533  1 C   B GLU 101 ? ? N   B ASN 102 ? ? 1.519 1.336 0.183  0.023 Y
+534  1 CG  B ASN 102 ? ? OD1 B ASN 102 ? ? 0.935 1.235 -0.300 0.022 N
+535  1 CG  B ASN 102 ? ? ND2 B ASN 102 ? ? 1.486 1.324 0.162  0.025 N
+536  1 CG  B PHE 103 ? ? CD2 B PHE 103 ? ? 1.291 1.383 -0.092 0.015 N
+537  1 CE1 B PHE 103 ? ? CZ  B PHE 103 ? ? 1.182 1.369 -0.187 0.019 N
+538  1 CA  B ARG 104 ? ? CB  B ARG 104 ? ? 1.675 1.535 0.140  0.022 N
+539  1 CG  B ARG 104 ? ? CD  B ARG 104 ? ? 1.757 1.515 0.242  0.025 N
+540  1 CD  B ARG 104 ? ? NE  B ARG 104 ? ? 1.654 1.460 0.194  0.017 N
+541  1 NE  B ARG 104 ? ? CZ  B ARG 104 ? ? 2.128 1.326 0.802  0.013 N
+542  1 CZ  B ARG 104 ? ? NH1 B ARG 104 ? ? 1.873 1.326 0.547  0.013 N
+543  1 CZ  B ARG 104 ? ? NH2 B ARG 104 ? ? 1.973 1.326 0.647  0.013 N
+544  1 CG  B LEU 106 ? ? CD2 B LEU 106 ? ? 1.285 1.514 -0.229 0.037 N
+545  1 CB  B ASN 108 ? ? CG  B ASN 108 ? ? 1.840 1.506 0.334  0.023 N
+546  1 CB  B VAL 109 ? ? CG2 B VAL 109 ? ? 1.656 1.524 0.132  0.021 N
+547  1 CA  B CYS 112 ? ? CB  B CYS 112 ? ? 1.368 1.526 -0.158 0.013 N
+548  1 CB  B CYS 112 ? ? SG  B CYS 112 ? ? 1.942 1.818 0.124  0.017 N
+549  1 C   B VAL 113 ? ? O   B VAL 113 ? ? 1.418 1.229 0.189  0.019 N
+550  1 CB  B HIS 117 ? ? CG  B HIS 117 ? ? 1.355 1.492 -0.137 0.016 N
+551  1 CG  B HIS 117 ? ? CD2 B HIS 117 ? ? 1.657 1.354 0.303  0.009 N
+552  1 CG  B HIS 117 ? ? ND1 B HIS 117 ? ? 1.942 1.383 0.559  0.022 N
+553  1 ND1 B HIS 117 ? ? CE1 B HIS 117 ? ? 1.749 1.343 0.406  0.025 N
+554  1 CE1 B HIS 117 ? ? NE2 B HIS 117 ? ? 1.529 1.333 0.196  0.019 N
+555  1 NE2 B HIS 117 ? ? CD2 B HIS 117 ? ? 2.213 1.415 0.798  0.021 N
+556  1 CB  B PHE 118 ? ? CG  B PHE 118 ? ? 1.346 1.509 -0.163 0.017 N
+557  1 CG  B PHE 118 ? ? CD2 B PHE 118 ? ? 1.548 1.383 0.165  0.015 N
+558  1 CD1 B PHE 118 ? ? CE1 B PHE 118 ? ? 1.512 1.388 0.124  0.020 N
+559  1 CE1 B PHE 118 ? ? CZ  B PHE 118 ? ? 1.522 1.369 0.153  0.019 N
+560  1 CE2 B PHE 118 ? ? CD2 B PHE 118 ? ? 1.159 1.388 -0.229 0.020 N
+561  1 C   B GLY 119 ? ? O   B GLY 119 ? ? 1.338 1.232 0.106  0.016 N
+562  1 CA  B LYS 120 ? ? CB  B LYS 120 ? ? 1.680 1.535 0.145  0.022 N
+563  1 CB  B LYS 120 ? ? CG  B LYS 120 ? ? 1.318 1.521 -0.203 0.027 N
+564  1 CD  B LYS 120 ? ? CE  B LYS 120 ? ? 1.666 1.508 0.158  0.025 N
+565  1 CE  B LYS 120 ? ? NZ  B LYS 120 ? ? 1.317 1.486 -0.169 0.025 N
+566  1 N   B GLU 121 ? ? CA  B GLU 121 ? ? 1.302 1.459 -0.157 0.020 N
+567  1 CA  B GLU 121 ? ? CB  B GLU 121 ? ? 1.684 1.535 0.149  0.022 N
+568  1 CB  B GLU 121 ? ? CG  B GLU 121 ? ? 1.082 1.517 -0.435 0.019 N
+569  1 CG  B GLU 121 ? ? CD  B GLU 121 ? ? 2.068 1.515 0.553  0.015 N
+570  1 CD  B GLU 121 ? ? OE1 B GLU 121 ? ? 1.868 1.252 0.616  0.011 N
+571  1 CD  B GLU 121 ? ? OE2 B GLU 121 ? ? 1.129 1.252 -0.123 0.011 N
+572  1 CB  B THR 123 ? ? OG1 B THR 123 ? ? 1.292 1.428 -0.136 0.020 N
+573  1 CA  B THR 123 ? ? C   B THR 123 ? ? 1.695 1.525 0.170  0.026 N
+574  1 C   B THR 123 ? ? O   B THR 123 ? ? 1.106 1.229 -0.123 0.019 N
+575  1 C   B THR 123 ? ? N   B PRO 124 ? ? 1.191 1.338 -0.147 0.019 Y
+576  1 CD  B PRO 124 ? ? N   B PRO 124 ? ? 1.699 1.474 0.225  0.014 N
+577  1 C   B PRO 124 ? ? O   B PRO 124 ? ? 1.361 1.228 0.133  0.020 N
+578  1 C   B PRO 124 ? ? N   B PRO 125 ? ? 1.199 1.338 -0.139 0.019 Y
+579  1 CD  B PRO 125 ? ? N   B PRO 125 ? ? 1.673 1.474 0.199  0.014 N
+580  1 C   B VAL 126 ? ? O   B VAL 126 ? ? 1.414 1.229 0.185  0.019 N
+581  1 CE1 B TYR 130 ? ? CZ  B TYR 130 ? ? 1.302 1.381 -0.079 0.013 N
+582  1 CE2 B TYR 130 ? ? CD2 B TYR 130 ? ? 1.594 1.389 0.205  0.015 N
+583  1 CA  B LYS 132 ? ? CB  B LYS 132 ? ? 1.319 1.535 -0.216 0.022 N
+584  1 CD  B LYS 132 ? ? CE  B LYS 132 ? ? 1.660 1.508 0.152  0.025 N
+585  1 CE  B LYS 132 ? ? NZ  B LYS 132 ? ? 1.882 1.486 0.396  0.025 N
+586  1 CB  B VAL 133 ? ? CG1 B VAL 133 ? ? 1.392 1.524 -0.132 0.021 N
+587  1 N   B VAL 134 ? ? CA  B VAL 134 ? ? 1.291 1.459 -0.168 0.020 N
+588  1 C   B VAL 134 ? ? O   B VAL 134 ? ? 1.373 1.229 0.144  0.019 N
+589  1 N   B GLY 136 ? ? CA  B GLY 136 ? ? 1.566 1.456 0.110  0.015 N
+590  1 CB  B ASN 139 ? ? CG  B ASN 139 ? ? 0.659 1.506 -0.847 0.023 N
+591  1 CG  B ASN 139 ? ? OD1 B ASN 139 ? ? 1.585 1.235 0.350  0.022 N
+592  1 CG  B ASN 139 ? ? ND2 B ASN 139 ? ? 2.013 1.324 0.689  0.025 N
+593  1 CA  B ALA 140 ? ? CB  B ALA 140 ? ? 1.653 1.520 0.133  0.021 N
+594  1 CA  B ALA 142 ? ? C   B ALA 142 ? ? 1.821 1.525 0.296  0.026 N
+595  1 C   B ALA 142 ? ? O   B ALA 142 ? ? 1.360 1.229 0.131  0.019 N
+596  1 C   B ALA 142 ? ? N   B HIS 143 ? ? 1.149 1.336 -0.187 0.023 Y
+597  1 CA  B HIS 143 ? ? CB  B HIS 143 ? ? 1.363 1.535 -0.172 0.022 N
+598  1 CB  B HIS 143 ? ? CG  B HIS 143 ? ? 1.740 1.496 0.244  0.018 N
+599  1 CG  B HIS 143 ? ? CD2 B HIS 143 ? ? 1.174 1.353 -0.179 0.017 N
+600  1 CG  B HIS 143 ? ? ND1 B HIS 143 ? ? 1.702 1.383 0.319  0.022 N
+601  1 ND1 B HIS 143 ? ? CE1 B HIS 143 ? ? 1.987 1.343 0.644  0.025 N
+602  1 CE1 B HIS 143 ? ? NE2 B HIS 143 ? ? 1.562 1.333 0.229  0.019 N
+603  1 CA  B HIS 143 ? ? C   B HIS 143 ? ? 1.764 1.525 0.239  0.026 N
+604  1 CD  B LYS 144 ? ? CE  B LYS 144 ? ? 2.006 1.508 0.498  0.025 N
+605  1 CE  B LYS 144 ? ? NZ  B LYS 144 ? ? 1.993 1.486 0.507  0.025 N
+606  1 CA  B LYS 144 ? ? C   B LYS 144 ? ? 1.354 1.525 -0.171 0.026 N
+607  1 C   B LYS 144 ? ? O   B LYS 144 ? ? 1.368 1.229 0.139  0.019 N
+608  1 CA  B TYR 145 ? ? CB  B TYR 145 ? ? 1.288 1.535 -0.247 0.022 N
+609  1 CB  B TYR 145 ? ? CG  B TYR 145 ? ? 1.622 1.512 0.110  0.015 N
+610  1 CD1 B TYR 145 ? ? CE1 B TYR 145 ? ? 1.285 1.389 -0.104 0.015 N
+611  1 CE1 B TYR 145 ? ? CZ  B TYR 145 ? ? 1.567 1.381 0.186  0.013 N
+612  1 CE2 B TYR 145 ? ? CD2 B TYR 145 ? ? 1.622 1.389 0.233  0.015 N
+613  1 CA  B TYR 145 ? ? C   B TYR 145 ? ? 1.749 1.525 0.224  0.026 N
+614  1 C   B TYR 145 ? ? O   B TYR 145 ? ? 1.349 1.229 0.120  0.019 N
+615  1 C   B TYR 145 ? ? N   B HIS 146 ? ? 0.970 1.336 -0.366 0.023 Y
+616  1 N   B HIS 146 ? ? CA  B HIS 146 ? ? 1.644 1.459 0.185  0.020 N
+617  1 CB  B HIS 146 ? ? CG  B HIS 146 ? ? 2.045 1.496 0.549  0.018 N
+618  1 CG  B HIS 146 ? ? CD2 B HIS 146 ? ? 1.626 1.354 0.272  0.009 N
+619  1 CG  B HIS 146 ? ? ND1 B HIS 146 ? ? 0.980 1.369 -0.389 0.015 N
+620  1 ND1 B HIS 146 ? ? CE1 B HIS 146 ? ? 1.840 1.343 0.497  0.025 N
+621  1 N   C VAL 1   ? ? CA  C VAL 1   ? ? 2.332 1.459 0.873  0.020 N
+622  1 CA  C VAL 1   ? ? CB  C VAL 1   ? ? 1.250 1.543 -0.293 0.021 N
+623  1 CB  C VAL 1   ? ? CG1 C VAL 1   ? ? 2.218 1.524 0.694  0.021 N
+624  1 CB  C VAL 1   ? ? CG2 C VAL 1   ? ? 2.483 1.524 0.959  0.021 N
+625  1 CA  C VAL 1   ? ? C   C VAL 1   ? ? 1.832 1.525 0.307  0.026 N
+626  1 CA  C LEU 2   ? ? CB  C LEU 2   ? ? 1.366 1.533 -0.167 0.023 N
+627  1 CG  C LEU 2   ? ? CD1 C LEU 2   ? ? 1.246 1.514 -0.268 0.037 N
+628  1 CG  C LEU 2   ? ? CD2 C LEU 2   ? ? 1.242 1.514 -0.272 0.037 N
+629  1 CA  C LEU 2   ? ? C   C LEU 2   ? ? 1.791 1.525 0.266  0.026 N
+630  1 C   C LEU 2   ? ? N   C SER 3   ? ? 1.195 1.336 -0.141 0.023 Y
+631  1 CA  C SER 3   ? ? CB  C SER 3   ? ? 1.405 1.525 -0.120 0.015 N
+632  1 N   C PRO 4   ? ? CA  C PRO 4   ? ? 1.260 1.468 -0.208 0.017 N
+633  1 CA  C PRO 4   ? ? C   C PRO 4   ? ? 1.645 1.524 0.121  0.020 N
+634  1 N   C LYS 7   ? ? CA  C LYS 7   ? ? 1.750 1.459 0.291  0.020 N
+635  1 CG  C LYS 7   ? ? CD  C LYS 7   ? ? 1.947 1.520 0.427  0.034 N
+636  1 CD  C LYS 7   ? ? CE  C LYS 7   ? ? 1.211 1.508 -0.297 0.025 N
+637  1 CE  C LYS 7   ? ? NZ  C LYS 7   ? ? 1.194 1.486 -0.292 0.025 N
+638  1 CA  C LYS 7   ? ? C   C LYS 7   ? ? 1.185 1.525 -0.340 0.026 N
+639  1 C   C LYS 7   ? ? N   C THR 8   ? ? 1.507 1.336 0.171  0.023 Y
+640  1 CA  C THR 8   ? ? CB  C THR 8   ? ? 1.839 1.529 0.310  0.026 N
+641  1 CA  C THR 8   ? ? C   C THR 8   ? ? 1.326 1.525 -0.199 0.026 N
+642  1 CB  C VAL 10  ? ? CG1 C VAL 10  ? ? 1.654 1.524 0.130  0.021 N
+643  1 CA  C VAL 10  ? ? C   C VAL 10  ? ? 1.812 1.525 0.287  0.026 N
+644  1 CD  C LYS 11  ? ? CE  C LYS 11  ? ? 1.312 1.508 -0.196 0.025 N
+645  1 CE  C LYS 11  ? ? NZ  C LYS 11  ? ? 1.913 1.486 0.427  0.025 N
+646  1 CA  C LYS 11  ? ? C   C LYS 11  ? ? 1.236 1.525 -0.289 0.026 N
+647  1 N   C ALA 12  ? ? CA  C ALA 12  ? ? 1.313 1.459 -0.146 0.020 N
+648  1 C   C ALA 12  ? ? O   C ALA 12  ? ? 1.369 1.229 0.140  0.019 N
+649  1 C   C ALA 12  ? ? N   C ALA 13  ? ? 1.547 1.336 0.211  0.023 Y
+650  1 CG  C TRP 14  ? ? CD1 C TRP 14  ? ? 1.571 1.363 0.208  0.014 N
+651  1 NE1 C TRP 14  ? ? CE2 C TRP 14  ? ? 1.240 1.371 -0.131 0.013 N
+652  1 CE2 C TRP 14  ? ? CD2 C TRP 14  ? ? 1.574 1.409 0.165  0.012 N
+653  1 CD2 C TRP 14  ? ? CE3 C TRP 14  ? ? 1.206 1.399 -0.193 0.015 N
+654  1 CZ3 C TRP 14  ? ? CH2 C TRP 14  ? ? 1.725 1.396 0.329  0.016 N
+655  1 CH2 C TRP 14  ? ? CZ2 C TRP 14  ? ? 1.198 1.369 -0.171 0.019 N
+656  1 C   C TRP 14  ? ? O   C TRP 14  ? ? 1.384 1.229 0.155  0.019 N
+657  1 C   C GLY 15  ? ? O   C GLY 15  ? ? 1.573 1.232 0.341  0.016 N
+658  1 C   C GLY 15  ? ? N   C LYS 16  ? ? 1.091 1.336 -0.245 0.023 Y
+659  1 CB  C LYS 16  ? ? CG  C LYS 16  ? ? 1.935 1.521 0.414  0.027 N
+660  1 CG  C LYS 16  ? ? CD  C LYS 16  ? ? 1.811 1.520 0.291  0.034 N
+661  1 CD  C LYS 16  ? ? CE  C LYS 16  ? ? 2.226 1.508 0.718  0.025 N
+662  1 CE  C LYS 16  ? ? NZ  C LYS 16  ? ? 1.709 1.486 0.223  0.025 N
+663  1 CA  C LYS 16  ? ? C   C LYS 16  ? ? 1.817 1.525 0.292  0.026 N
+664  1 CB  C VAL 17  ? ? CG1 C VAL 17  ? ? 1.315 1.524 -0.209 0.021 N
+665  1 CB  C VAL 17  ? ? CG2 C VAL 17  ? ? 1.655 1.524 0.131  0.021 N
+666  1 C   C VAL 17  ? ? O   C VAL 17  ? ? 1.380 1.229 0.151  0.019 N
+667  1 C   C VAL 17  ? ? N   C GLY 18  ? ? 1.506 1.336 0.170  0.023 Y
+668  1 N   C GLY 18  ? ? CA  C GLY 18  ? ? 1.569 1.456 0.113  0.015 N
+669  1 CA  C GLY 18  ? ? C   C GLY 18  ? ? 1.360 1.514 -0.154 0.016 N
+670  1 C   C GLY 18  ? ? O   C GLY 18  ? ? 1.421 1.232 0.189  0.016 N
+671  1 N   C ALA 19  ? ? CA  C ALA 19  ? ? 1.337 1.459 -0.122 0.020 N
+672  1 C   C ALA 19  ? ? O   C ALA 19  ? ? 1.437 1.229 0.208  0.019 N
+673  1 CA  C HIS 20  ? ? CB  C HIS 20  ? ? 1.380 1.535 -0.155 0.022 N
+674  1 CB  C HIS 20  ? ? CG  C HIS 20  ? ? 1.707 1.496 0.211  0.018 N
+675  1 CG  C HIS 20  ? ? ND1 C HIS 20  ? ? 1.644 1.383 0.261  0.022 N
+676  1 ND1 C HIS 20  ? ? CE1 C HIS 20  ? ? 1.786 1.343 0.443  0.025 N
+677  1 CE1 C HIS 20  ? ? NE2 C HIS 20  ? ? 1.569 1.333 0.236  0.019 N
+678  1 NE2 C HIS 20  ? ? CD2 C HIS 20  ? ? 1.167 1.373 -0.206 0.011 N
+679  1 C   C ALA 21  ? ? N   C GLY 22  ? ? 1.167 1.336 -0.169 0.023 Y
+680  1 CA  C GLY 22  ? ? C   C GLY 22  ? ? 1.202 1.514 -0.312 0.016 N
+681  1 C   C GLY 22  ? ? O   C GLY 22  ? ? 1.379 1.232 0.147  0.016 N
+682  1 N   C GLU 23  ? ? CA  C GLU 23  ? ? 1.305 1.459 -0.154 0.020 N
+683  1 CG  C GLU 23  ? ? CD  C GLU 23  ? ? 2.153 1.515 0.638  0.015 N
+684  1 CD  C GLU 23  ? ? OE1 C GLU 23  ? ? 2.374 1.252 1.122  0.011 N
+685  1 CD  C GLU 23  ? ? OE2 C GLU 23  ? ? 0.873 1.252 -0.379 0.011 N
+686  1 CA  C GLU 23  ? ? C   C GLU 23  ? ? 1.706 1.525 0.181  0.026 N
+687  1 CG  C TYR 24  ? ? CD1 C TYR 24  ? ? 1.532 1.387 0.145  0.013 N
+688  1 CD1 C TYR 24  ? ? CE1 C TYR 24  ? ? 1.502 1.389 0.113  0.015 N
+689  1 CE1 C TYR 24  ? ? CZ  C TYR 24  ? ? 1.243 1.381 -0.138 0.013 N
+690  1 CZ  C TYR 24  ? ? OH  C TYR 24  ? ? 1.547 1.374 0.173  0.017 N
+691  1 CE2 C TYR 24  ? ? CD2 C TYR 24  ? ? 1.557 1.389 0.168  0.015 N
+692  1 N   C GLY 25  ? ? CA  C GLY 25  ? ? 1.335 1.456 -0.121 0.015 N
+693  1 C   C GLY 25  ? ? O   C GLY 25  ? ? 1.469 1.232 0.237  0.016 N
+694  1 C   C ALA 26  ? ? N   C GLU 27  ? ? 1.530 1.336 0.194  0.023 Y
+695  1 CD  C GLU 27  ? ? OE2 C GLU 27  ? ? 1.323 1.252 0.071  0.011 N
+696  1 CA  C LEU 29  ? ? C   C LEU 29  ? ? 1.338 1.525 -0.187 0.026 N
+697  1 CG  C GLU 30  ? ? CD  C GLU 30  ? ? 1.958 1.515 0.443  0.015 N
+698  1 CD  C GLU 30  ? ? OE2 C GLU 30  ? ? 0.799 1.252 -0.453 0.011 N
+699  1 CD  C ARG 31  ? ? NE  C ARG 31  ? ? 1.590 1.460 0.130  0.017 N
+700  1 CG  C PHE 36  ? ? CD2 C PHE 36  ? ? 1.530 1.383 0.147  0.015 N
+701  1 CE2 C PHE 36  ? ? CD2 C PHE 36  ? ? 1.258 1.388 -0.130 0.020 N
+702  1 CD  C PRO 37  ? ? N   C PRO 37  ? ? 1.276 1.474 -0.198 0.014 N
+703  1 CA  C THR 38  ? ? CB  C THR 38  ? ? 1.806 1.529 0.277  0.026 N
+704  1 CB  C THR 38  ? ? OG1 C THR 38  ? ? 1.612 1.428 0.184  0.020 N
+705  1 CA  C THR 38  ? ? C   C THR 38  ? ? 1.350 1.525 -0.175 0.026 N
+706  1 N   C LYS 40  ? ? CA  C LYS 40  ? ? 1.596 1.459 0.137  0.020 N
+707  1 CD  C LYS 40  ? ? CE  C LYS 40  ? ? 0.851 1.508 -0.657 0.025 N
+708  1 CE  C LYS 40  ? ? NZ  C LYS 40  ? ? 1.692 1.486 0.206  0.025 N
+709  1 N   C THR 41  ? ? CA  C THR 41  ? ? 1.583 1.459 0.124  0.020 N
+710  1 C   C THR 41  ? ? O   C THR 41  ? ? 1.420 1.229 0.191  0.019 N
+711  1 CG  C TYR 42  ? ? CD1 C TYR 42  ? ? 1.505 1.387 0.118  0.013 N
+712  1 CZ  C TYR 42  ? ? CE2 C TYR 42  ? ? 1.496 1.381 0.115  0.013 N
+713  1 N   C PHE 43  ? ? CA  C PHE 43  ? ? 1.591 1.459 0.132  0.020 N
+714  1 CG  C PHE 43  ? ? CD2 C PHE 43  ? ? 1.520 1.383 0.137  0.015 N
+715  1 CA  C PRO 44  ? ? CB  C PRO 44  ? ? 1.723 1.531 0.192  0.020 N
+716  1 C   C PRO 44  ? ? N   C HIS 45  ? ? 1.109 1.336 -0.227 0.023 Y
+717  1 CB  C HIS 45  ? ? CG  C HIS 45  ? ? 1.610 1.496 0.114  0.018 N
+718  1 ND1 C HIS 45  ? ? CE1 C HIS 45  ? ? 1.144 1.323 -0.179 0.015 N
+719  1 NE2 C HIS 45  ? ? CD2 C HIS 45  ? ? 1.288 1.373 -0.085 0.011 N
+720  1 CA  C PHE 46  ? ? CB  C PHE 46  ? ? 1.677 1.535 0.142  0.022 N
+721  1 CB  C PHE 46  ? ? CG  C PHE 46  ? ? 1.348 1.509 -0.161 0.017 N
+722  1 CE1 C PHE 46  ? ? CZ  C PHE 46  ? ? 1.183 1.369 -0.186 0.019 N
+723  1 CZ  C PHE 46  ? ? CE2 C PHE 46  ? ? 1.568 1.369 0.199  0.019 N
+724  1 CE2 C PHE 46  ? ? CD2 C PHE 46  ? ? 0.917 1.388 -0.471 0.020 N
+725  1 C   C PHE 46  ? ? N   C ASP 47  ? ? 1.536 1.336 0.200  0.023 Y
+726  1 CA  C ASP 47  ? ? CB  C ASP 47  ? ? 1.720 1.535 0.185  0.022 N
+727  1 CB  C ASP 47  ? ? CG  C ASP 47  ? ? 1.721 1.513 0.208  0.021 N
+728  1 CG  C ASP 47  ? ? OD1 C ASP 47  ? ? 1.036 1.249 -0.213 0.023 N
+729  1 N   C LEU 48  ? ? CA  C LEU 48  ? ? 1.594 1.459 0.135  0.020 N
+730  1 CG  C LEU 48  ? ? CD2 C LEU 48  ? ? 1.742 1.514 0.228  0.037 N
+731  1 CA  C LEU 48  ? ? C   C LEU 48  ? ? 1.321 1.525 -0.204 0.026 N
+732  1 C   C LEU 48  ? ? O   C LEU 48  ? ? 1.398 1.229 0.169  0.019 N
+733  1 CB  C SER 49  ? ? OG  C SER 49  ? ? 1.104 1.418 -0.314 0.013 N
+734  1 CA  C SER 49  ? ? C   C SER 49  ? ? 1.325 1.525 -0.200 0.026 N
+735  1 C   C SER 49  ? ? N   C HIS 50  ? ? 1.582 1.336 0.246  0.023 Y
+736  1 CA  C HIS 50  ? ? CB  C HIS 50  ? ? 1.716 1.535 0.181  0.022 N
+737  1 CB  C HIS 50  ? ? CG  C HIS 50  ? ? 1.311 1.492 -0.181 0.016 N
+738  1 CG  C HIS 50  ? ? CD2 C HIS 50  ? ? 1.245 1.353 -0.108 0.017 N
+739  1 CG  C HIS 50  ? ? ND1 C HIS 50  ? ? 1.668 1.383 0.285  0.022 N
+740  1 CE1 C HIS 50  ? ? NE2 C HIS 50  ? ? 1.549 1.333 0.216  0.019 N
+741  1 CA  C HIS 50  ? ? C   C HIS 50  ? ? 1.710 1.525 0.185  0.026 N
+742  1 N   C GLY 51  ? ? CA  C GLY 51  ? ? 1.308 1.456 -0.148 0.015 N
+743  1 N   C SER 52  ? ? CA  C SER 52  ? ? 1.612 1.459 0.153  0.020 N
+744  1 CA  C SER 52  ? ? CB  C SER 52  ? ? 1.427 1.525 -0.098 0.015 N
+745  1 CA  C SER 52  ? ? C   C SER 52  ? ? 1.281 1.525 -0.244 0.026 N
+746  1 C   C SER 52  ? ? O   C SER 52  ? ? 1.361 1.229 0.132  0.019 N
+747  1 CA  C GLN 54  ? ? C   C GLN 54  ? ? 1.746 1.525 0.221  0.026 N
+748  1 N   C VAL 55  ? ? CA  C VAL 55  ? ? 1.610 1.459 0.151  0.020 N
+749  1 CG  C LYS 56  ? ? CD  C LYS 56  ? ? 2.268 1.520 0.748  0.034 N
+750  1 CD  C LYS 56  ? ? CE  C LYS 56  ? ? 2.393 1.508 0.885  0.025 N
+751  1 CE  C LYS 56  ? ? NZ  C LYS 56  ? ? 1.724 1.486 0.238  0.025 N
+752  1 CA  C LYS 56  ? ? C   C LYS 56  ? ? 1.294 1.525 -0.231 0.026 N
+753  1 C   C GLY 57  ? ? O   C GLY 57  ? ? 1.373 1.232 0.141  0.016 N
+754  1 CG  C HIS 58  ? ? CD2 C HIS 58  ? ? 1.218 1.353 -0.135 0.017 N
+755  1 CA  C HIS 58  ? ? C   C HIS 58  ? ? 1.692 1.525 0.167  0.026 N
+756  1 N   C GLY 59  ? ? CA  C GLY 59  ? ? 1.330 1.456 -0.126 0.015 N
+757  1 C   C GLY 59  ? ? O   C GLY 59  ? ? 1.348 1.232 0.116  0.016 N
+758  1 CD  C LYS 60  ? ? CE  C LYS 60  ? ? 1.342 1.508 -0.166 0.025 N
+759  1 CE  C LYS 60  ? ? NZ  C LYS 60  ? ? 2.015 1.486 0.529  0.025 N
+760  1 CB  C LYS 61  ? ? CG  C LYS 61  ? ? 1.332 1.521 -0.189 0.027 N
+761  1 CD  C LYS 61  ? ? CE  C LYS 61  ? ? 1.807 1.508 0.299  0.025 N
+762  1 CE  C LYS 61  ? ? NZ  C LYS 61  ? ? 1.977 1.486 0.491  0.025 N
+763  1 CA  C LYS 61  ? ? C   C LYS 61  ? ? 1.764 1.525 0.239  0.026 N
+764  1 CA  C ALA 63  ? ? C   C ALA 63  ? ? 1.361 1.525 -0.164 0.026 N
+765  1 CB  C ASP 64  ? ? CG  C ASP 64  ? ? 1.661 1.513 0.148  0.021 N
+766  1 CG  C ASP 64  ? ? OD2 C ASP 64  ? ? 1.070 1.249 -0.179 0.023 N
+767  1 C   C ALA 65  ? ? N   C LEU 66  ? ? 1.494 1.336 0.158  0.023 Y
+768  1 N   C ASN 68  ? ? CA  C ASN 68  ? ? 1.328 1.459 -0.131 0.020 N
+769  1 CG  C ASN 68  ? ? OD1 C ASN 68  ? ? 0.916 1.235 -0.319 0.022 N
+770  1 CG  C ASN 68  ? ? ND2 C ASN 68  ? ? 1.543 1.324 0.219  0.025 N
+771  1 C   C ASN 68  ? ? O   C ASN 68  ? ? 1.475 1.229 0.246  0.019 N
+772  1 N   C ALA 69  ? ? CA  C ALA 69  ? ? 1.641 1.459 0.182  0.020 N
+773  1 N   C VAL 70  ? ? CA  C VAL 70  ? ? 1.677 1.459 0.218  0.020 N
+774  1 CA  C VAL 70  ? ? C   C VAL 70  ? ? 1.741 1.525 0.216  0.026 N
+775  1 C   C VAL 70  ? ? N   C ALA 71  ? ? 0.988 1.336 -0.348 0.023 Y
+776  1 N   C ALA 71  ? ? CA  C ALA 71  ? ? 1.667 1.459 0.208  0.020 N
+777  1 CA  C ALA 71  ? ? CB  C ALA 71  ? ? 1.281 1.520 -0.239 0.021 N
+778  1 CA  C ALA 71  ? ? C   C ALA 71  ? ? 1.284 1.525 -0.241 0.026 N
+779  1 N   C HIS 72  ? ? CA  C HIS 72  ? ? 1.278 1.459 -0.181 0.020 N
+780  1 CA  C HIS 72  ? ? CB  C HIS 72  ? ? 1.855 1.535 0.320  0.022 N
+781  1 CB  C HIS 72  ? ? CG  C HIS 72  ? ? 1.216 1.492 -0.276 0.016 N
+782  1 CG  C HIS 72  ? ? CD2 C HIS 72  ? ? 1.620 1.354 0.266  0.009 N
+783  1 CG  C HIS 72  ? ? ND1 C HIS 72  ? ? 1.796 1.383 0.413  0.022 N
+784  1 ND1 C HIS 72  ? ? CE1 C HIS 72  ? ? 1.062 1.323 -0.261 0.015 N
+785  1 CA  C HIS 72  ? ? C   C HIS 72  ? ? 1.193 1.525 -0.332 0.026 N
+786  1 C   C HIS 72  ? ? O   C HIS 72  ? ? 1.452 1.229 0.223  0.019 N
+787  1 N   C VAL 73  ? ? CA  C VAL 73  ? ? 1.335 1.459 -0.124 0.020 N
+788  1 CA  C VAL 73  ? ? CB  C VAL 73  ? ? 1.799 1.543 0.256  0.021 N
+789  1 CB  C VAL 73  ? ? CG1 C VAL 73  ? ? 1.397 1.524 -0.127 0.021 N
+790  1 CA  C VAL 73  ? ? C   C VAL 73  ? ? 1.688 1.525 0.163  0.026 N
+791  1 N   C ASP 74  ? ? CA  C ASP 74  ? ? 1.598 1.459 0.139  0.020 N
+792  1 CB  C ASP 74  ? ? CG  C ASP 74  ? ? 1.349 1.513 -0.164 0.021 N
+793  1 CG  C ASP 74  ? ? OD1 C ASP 74  ? ? 1.517 1.249 0.268  0.023 N
+794  1 C   C ASP 74  ? ? O   C ASP 74  ? ? 0.907 1.229 -0.322 0.019 N
+795  1 N   C ASP 75  ? ? CA  C ASP 75  ? ? 1.707 1.459 0.248  0.020 N
+796  1 C   C ASP 75  ? ? N   C MET 76  ? ? 1.588 1.336 0.252  0.023 Y
+797  1 CG  C MET 76  ? ? SD  C MET 76  ? ? 2.052 1.807 0.245  0.026 N
+798  1 CA  C MET 76  ? ? C   C MET 76  ? ? 1.330 1.525 -0.195 0.026 N
+799  1 CA  C PRO 77  ? ? C   C PRO 77  ? ? 1.347 1.524 -0.177 0.020 N
+800  1 CA  C ASN 78  ? ? CB  C ASN 78  ? ? 1.697 1.527 0.170  0.026 N
+801  1 CB  C ASN 78  ? ? CG  C ASN 78  ? ? 1.765 1.506 0.259  0.023 N
+802  1 CA  C ASN 78  ? ? C   C ASN 78  ? ? 1.143 1.525 -0.382 0.026 N
+803  1 C   C ASN 78  ? ? N   C ALA 79  ? ? 1.501 1.336 0.165  0.023 Y
+804  1 CA  C SER 81  ? ? CB  C SER 81  ? ? 1.662 1.525 0.137  0.015 N
+805  1 CB  C SER 81  ? ? OG  C SER 81  ? ? 1.538 1.418 0.120  0.013 N
+806  1 C   C LEU 83  ? ? O   C LEU 83  ? ? 1.372 1.229 0.143  0.019 N
+807  1 CA  C SER 84  ? ? CB  C SER 84  ? ? 1.792 1.525 0.267  0.015 N
+808  1 CB  C SER 84  ? ? OG  C SER 84  ? ? 1.181 1.418 -0.237 0.013 N
+809  1 CG  C ASP 85  ? ? OD1 C ASP 85  ? ? 1.050 1.249 -0.199 0.023 N
+810  1 CG  C HIS 87  ? ? CD2 C HIS 87  ? ? 1.464 1.354 0.110  0.009 N
+811  1 CE1 C HIS 87  ? ? NE2 C HIS 87  ? ? 1.165 1.317 -0.152 0.011 N
+812  1 CA  C HIS 87  ? ? C   C HIS 87  ? ? 1.819 1.525 0.294  0.026 N
+813  1 CA  C ALA 88  ? ? C   C ALA 88  ? ? 1.682 1.525 0.157  0.026 N
+814  1 CE1 C HIS 89  ? ? NE2 C HIS 89  ? ? 1.188 1.317 -0.129 0.011 N
+815  1 N   C LYS 90  ? ? CA  C LYS 90  ? ? 1.309 1.459 -0.150 0.020 N
+816  1 CG  C LYS 90  ? ? CD  C LYS 90  ? ? 1.896 1.520 0.376  0.034 N
+817  1 CD  C LYS 90  ? ? CE  C LYS 90  ? ? 1.908 1.508 0.400  0.025 N
+818  1 CE  C LYS 90  ? ? NZ  C LYS 90  ? ? 2.063 1.486 0.577  0.025 N
+819  1 CD  C ARG 92  ? ? NE  C ARG 92  ? ? 1.076 1.460 -0.384 0.017 N
+820  1 NE  C ARG 92  ? ? CZ  C ARG 92  ? ? 2.965 1.326 1.639  0.013 N
+821  1 CZ  C ARG 92  ? ? NH1 C ARG 92  ? ? 1.869 1.326 0.543  0.013 N
+822  1 CZ  C ARG 92  ? ? NH2 C ARG 92  ? ? 0.982 1.326 -0.344 0.013 N
+823  1 C   C ARG 92  ? ? O   C ARG 92  ? ? 1.037 1.229 -0.192 0.019 N
+824  1 CG  C ASP 94  ? ? OD1 C ASP 94  ? ? 1.077 1.249 -0.172 0.023 N
+825  1 N   C PRO 95  ? ? CA  C PRO 95  ? ? 1.612 1.468 0.144  0.017 N
+826  1 CA  C PRO 95  ? ? C   C PRO 95  ? ? 1.343 1.524 -0.181 0.020 N
+827  1 C   C PRO 95  ? ? O   C PRO 95  ? ? 1.357 1.228 0.129  0.020 N
+828  1 CB  C VAL 96  ? ? CG2 C VAL 96  ? ? 1.353 1.524 -0.171 0.021 N
+829  1 CG  C PHE 98  ? ? CD2 C PHE 98  ? ? 1.282 1.383 -0.101 0.015 N
+830  1 CB  C LYS 99  ? ? CG  C LYS 99  ? ? 0.738 1.521 -0.783 0.027 N
+831  1 CG  C LYS 99  ? ? CD  C LYS 99  ? ? 1.821 1.520 0.301  0.034 N
+832  1 CD  C LYS 99  ? ? CE  C LYS 99  ? ? 2.261 1.508 0.753  0.025 N
+833  1 C   C LYS 99  ? ? O   C LYS 99  ? ? 1.111 1.229 -0.118 0.019 N
+834  1 CG  C HIS 103 ? ? ND1 C HIS 103 ? ? 1.585 1.383 0.202  0.022 N
+835  1 CG  C LEU 105 ? ? CD1 C LEU 105 ? ? 1.789 1.514 0.275  0.037 N
+836  1 CG  C LEU 105 ? ? CD2 C LEU 105 ? ? 2.119 1.514 0.605  0.037 N
+837  1 N   C LEU 106 ? ? CA  C LEU 106 ? ? 1.582 1.459 0.123  0.020 N
+838  1 CA  C LEU 106 ? ? C   C LEU 106 ? ? 1.332 1.525 -0.193 0.026 N
+839  1 C   C LEU 109 ? ? N   C ALA 110 ? ? 1.488 1.336 0.152  0.023 Y
+840  1 C   C ALA 110 ? ? O   C ALA 110 ? ? 1.359 1.229 0.130  0.019 N
+841  1 CB  C HIS 112 ? ? CG  C HIS 112 ? ? 1.311 1.492 -0.181 0.016 N
+842  1 CG  C HIS 112 ? ? ND1 C HIS 112 ? ? 1.781 1.383 0.398  0.022 N
+843  1 C   C HIS 112 ? ? N   C LEU 113 ? ? 1.168 1.336 -0.168 0.023 Y
+844  1 CA  C LEU 113 ? ? CB  C LEU 113 ? ? 1.330 1.533 -0.203 0.023 N
+845  1 CG  C LEU 113 ? ? CD1 C LEU 113 ? ? 1.750 1.514 0.236  0.037 N
+846  1 CG  C LEU 113 ? ? CD2 C LEU 113 ? ? 1.215 1.514 -0.299 0.037 N
+847  1 N   C PRO 114 ? ? CA  C PRO 114 ? ? 1.720 1.468 0.252  0.017 N
+848  1 CA  C PRO 114 ? ? CB  C PRO 114 ? ? 1.320 1.531 -0.211 0.020 N
+849  1 CD  C PRO 114 ? ? N   C PRO 114 ? ? 1.590 1.474 0.116  0.014 N
+850  1 CA  C PRO 114 ? ? C   C PRO 114 ? ? 1.905 1.524 0.381  0.020 N
+851  1 C   C PRO 114 ? ? O   C PRO 114 ? ? 1.382 1.228 0.154  0.020 N
+852  1 N   C ALA 115 ? ? CA  C ALA 115 ? ? 1.287 1.459 -0.172 0.020 N
+853  1 CA  C ALA 115 ? ? CB  C ALA 115 ? ? 1.705 1.520 0.185  0.021 N
+854  1 CA  C ALA 115 ? ? C   C ALA 115 ? ? 1.214 1.525 -0.311 0.026 N
+855  1 CB  C GLU 116 ? ? CG  C GLU 116 ? ? 2.333 1.517 0.816  0.019 N
+856  1 CD  C GLU 116 ? ? OE1 C GLU 116 ? ? 1.127 1.252 -0.125 0.011 N
+857  1 CD  C GLU 116 ? ? OE2 C GLU 116 ? ? 1.452 1.252 0.200  0.011 N
+858  1 CG  C PHE 117 ? ? CD1 C PHE 117 ? ? 1.489 1.383 0.106  0.015 N
+859  1 CD1 C PHE 117 ? ? CE1 C PHE 117 ? ? 1.599 1.388 0.211  0.020 N
+860  1 CA  C THR 118 ? ? CB  C THR 118 ? ? 1.751 1.529 0.222  0.026 N
+861  1 CB  C THR 118 ? ? CG2 C THR 118 ? ? 1.111 1.519 -0.408 0.033 N
+862  1 C   C THR 118 ? ? N   C PRO 119 ? ? 1.068 1.338 -0.270 0.019 Y
+863  1 CD  C PRO 119 ? ? N   C PRO 119 ? ? 1.632 1.474 0.158  0.014 N
+864  1 C   C ALA 120 ? ? O   C ALA 120 ? ? 1.350 1.229 0.121  0.019 N
+865  1 CA  C HIS 122 ? ? CB  C HIS 122 ? ? 1.396 1.535 -0.139 0.022 N
+866  1 CG  C HIS 122 ? ? CD2 C HIS 122 ? ? 1.474 1.354 0.120  0.009 N
+867  1 CA  C SER 124 ? ? CB  C SER 124 ? ? 1.626 1.525 0.101  0.015 N
+868  1 CB  C ASP 126 ? ? CG  C ASP 126 ? ? 1.698 1.513 0.185  0.021 N
+869  1 C   C LYS 127 ? ? O   C LYS 127 ? ? 1.421 1.229 0.192  0.019 N
+870  1 CB  C PHE 128 ? ? CG  C PHE 128 ? ? 1.678 1.509 0.169  0.017 N
+871  1 CG  C PHE 128 ? ? CD2 C PHE 128 ? ? 1.218 1.383 -0.165 0.015 N
+872  1 CE1 C PHE 128 ? ? CZ  C PHE 128 ? ? 1.252 1.369 -0.117 0.019 N
+873  1 CZ  C PHE 128 ? ? CE2 C PHE 128 ? ? 1.250 1.369 -0.119 0.019 N
+874  1 CE2 C PHE 128 ? ? CD2 C PHE 128 ? ? 1.575 1.388 0.187  0.020 N
+875  1 CA  C PHE 128 ? ? C   C PHE 128 ? ? 1.726 1.525 0.201  0.026 N
+876  1 C   C PHE 128 ? ? O   C PHE 128 ? ? 1.344 1.229 0.115  0.019 N
+877  1 CA  C ALA 130 ? ? CB  C ALA 130 ? ? 1.387 1.520 -0.133 0.021 N
+878  1 C   C ALA 130 ? ? O   C ALA 130 ? ? 1.360 1.229 0.131  0.019 N
+879  1 N   C SER 131 ? ? CA  C SER 131 ? ? 1.626 1.459 0.167  0.020 N
+880  1 CA  C SER 131 ? ? CB  C SER 131 ? ? 1.727 1.525 0.202  0.015 N
+881  1 CB  C SER 131 ? ? OG  C SER 131 ? ? 1.507 1.418 0.089  0.013 N
+882  1 CA  C SER 131 ? ? C   C SER 131 ? ? 1.756 1.525 0.231  0.026 N
+883  1 CA  C VAL 132 ? ? CB  C VAL 132 ? ? 1.400 1.543 -0.143 0.021 N
+884  1 CB  C VAL 132 ? ? CG2 C VAL 132 ? ? 1.721 1.524 0.197  0.021 N
+885  1 C   C SER 133 ? ? O   C SER 133 ? ? 1.446 1.229 0.217  0.019 N
+886  1 C   C SER 133 ? ? N   C THR 134 ? ? 1.177 1.336 -0.159 0.023 Y
+887  1 CB  C THR 137 ? ? OG1 C THR 137 ? ? 1.219 1.428 -0.209 0.020 N
+888  1 CA  C THR 137 ? ? C   C THR 137 ? ? 1.742 1.525 0.217  0.026 N
+889  1 CA  C SER 138 ? ? CB  C SER 138 ? ? 2.140 1.525 0.615  0.015 N
+890  1 CB  C SER 138 ? ? OG  C SER 138 ? ? 1.292 1.418 -0.126 0.013 N
+891  1 CG  C LYS 139 ? ? CD  C LYS 139 ? ? 1.292 1.520 -0.228 0.034 N
+892  1 CD  C LYS 139 ? ? CE  C LYS 139 ? ? 1.953 1.508 0.445  0.025 N
+893  1 CE  C LYS 139 ? ? NZ  C LYS 139 ? ? 1.840 1.486 0.354  0.025 N
+894  1 CG  C TYR 140 ? ? CD2 C TYR 140 ? ? 1.494 1.387 0.107  0.013 N
+895  1 CG  C TYR 140 ? ? CD1 C TYR 140 ? ? 1.222 1.387 -0.165 0.013 N
+896  1 CZ  C TYR 140 ? ? CE2 C TYR 140 ? ? 1.223 1.381 -0.158 0.013 N
+897  1 CZ  C ARG 141 ? ? NH2 C ARG 141 ? ? 1.441 1.326 0.115  0.013 N
+898  1 N   D VAL 1   ? ? CA  D VAL 1   ? ? 1.770 1.459 0.311  0.020 N
+899  1 CA  D VAL 1   ? ? CB  D VAL 1   ? ? 1.696 1.543 0.153  0.021 N
+900  1 CB  D VAL 1   ? ? CG1 D VAL 1   ? ? 1.729 1.524 0.205  0.021 N
+901  1 CB  D VAL 1   ? ? CG2 D VAL 1   ? ? 1.172 1.524 -0.352 0.021 N
+902  1 CA  D VAL 1   ? ? C   D VAL 1   ? ? 2.020 1.525 0.495  0.026 N
+903  1 C   D VAL 1   ? ? N   D HIS 2   ? ? 1.182 1.336 -0.154 0.023 Y
+904  1 CA  D HIS 2   ? ? CB  D HIS 2   ? ? 2.214 1.535 0.679  0.022 N
+905  1 CB  D HIS 2   ? ? CG  D HIS 2   ? ? 1.051 1.492 -0.441 0.016 N
+906  1 CG  D HIS 2   ? ? CD2 D HIS 2   ? ? 1.854 1.354 0.500  0.009 N
+907  1 CG  D HIS 2   ? ? ND1 D HIS 2   ? ? 2.479 1.383 1.096  0.022 N
+908  1 ND1 D HIS 2   ? ? CE1 D HIS 2   ? ? 1.899 1.343 0.556  0.025 N
+909  1 CE1 D HIS 2   ? ? NE2 D HIS 2   ? ? 1.905 1.333 0.572  0.019 N
+910  1 NE2 D HIS 2   ? ? CD2 D HIS 2   ? ? 1.575 1.415 0.160  0.021 N
+911  1 C   D HIS 2   ? ? O   D HIS 2   ? ? 1.540 1.229 0.311  0.019 N
+912  1 C   D LEU 3   ? ? O   D LEU 3   ? ? 1.765 1.229 0.536  0.019 N
+913  1 C   D LEU 3   ? ? N   D THR 4   ? ? 1.520 1.336 0.184  0.023 Y
+914  1 N   D THR 4   ? ? CA  D THR 4   ? ? 1.243 1.459 -0.216 0.020 N
+915  1 CA  D THR 4   ? ? CB  D THR 4   ? ? 1.817 1.529 0.288  0.026 N
+916  1 CB  D THR 4   ? ? CG2 D THR 4   ? ? 1.232 1.519 -0.287 0.033 N
+917  1 C   D THR 4   ? ? O   D THR 4   ? ? 1.412 1.229 0.183  0.019 N
+918  1 C   D THR 4   ? ? N   D PRO 5   ? ? 0.968 1.338 -0.370 0.019 Y
+919  1 N   D PRO 5   ? ? CA  D PRO 5   ? ? 1.838 1.468 0.370  0.017 N
+920  1 CA  D PRO 5   ? ? CB  D PRO 5   ? ? 2.309 1.531 0.778  0.020 N
+921  1 CB  D PRO 5   ? ? CG  D PRO 5   ? ? 1.053 1.495 -0.442 0.050 N
+922  1 CD  D PRO 5   ? ? N   D PRO 5   ? ? 1.577 1.474 0.103  0.014 N
+923  1 N   D GLU 6   ? ? CA  D GLU 6   ? ? 1.314 1.459 -0.145 0.020 N
+924  1 CA  D GLU 6   ? ? CB  D GLU 6   ? ? 1.724 1.535 0.189  0.022 N
+925  1 CB  D GLU 6   ? ? CG  D GLU 6   ? ? 0.939 1.517 -0.578 0.019 N
+926  1 CG  D GLU 6   ? ? CD  D GLU 6   ? ? 1.970 1.515 0.455  0.015 N
+927  1 CD  D GLU 6   ? ? OE1 D GLU 6   ? ? 0.938 1.252 -0.314 0.011 N
+928  1 CD  D GLU 6   ? ? OE2 D GLU 6   ? ? 2.591 1.252 1.339  0.011 N
+929  1 CA  D GLU 6   ? ? C   D GLU 6   ? ? 2.305 1.525 0.780  0.026 N
+930  1 C   D GLU 6   ? ? O   D GLU 6   ? ? 1.019 1.229 -0.210 0.019 N
+931  1 CB  D GLU 7   ? ? CG  D GLU 7   ? ? 1.876 1.517 0.359  0.019 N
+932  1 CG  D GLU 7   ? ? CD  D GLU 7   ? ? 1.349 1.515 -0.166 0.015 N
+933  1 CD  D GLU 7   ? ? OE1 D GLU 7   ? ? 1.464 1.252 0.212  0.011 N
+934  1 CD  D GLU 7   ? ? OE2 D GLU 7   ? ? 1.382 1.252 0.130  0.011 N
+935  1 CA  D GLU 7   ? ? C   D GLU 7   ? ? 1.746 1.525 0.221  0.026 N
+936  1 C   D GLU 7   ? ? N   D LYS 8   ? ? 1.179 1.336 -0.157 0.023 Y
+937  1 N   D LYS 8   ? ? CA  D LYS 8   ? ? 1.680 1.459 0.221  0.020 N
+938  1 CA  D LYS 8   ? ? CB  D LYS 8   ? ? 1.851 1.535 0.316  0.022 N
+939  1 CB  D LYS 8   ? ? CG  D LYS 8   ? ? 1.789 1.521 0.268  0.027 N
+940  1 CG  D LYS 8   ? ? CD  D LYS 8   ? ? 1.225 1.520 -0.295 0.034 N
+941  1 CD  D LYS 8   ? ? CE  D LYS 8   ? ? 2.031 1.508 0.523  0.025 N
+942  1 CE  D LYS 8   ? ? NZ  D LYS 8   ? ? 1.937 1.486 0.451  0.025 N
+943  1 CA  D LYS 8   ? ? C   D LYS 8   ? ? 1.324 1.525 -0.201 0.026 N
+944  1 CB  D SER 9   ? ? OG  D SER 9   ? ? 1.161 1.418 -0.257 0.013 N
+945  1 N   D ALA 10  ? ? CA  D ALA 10  ? ? 1.605 1.459 0.146  0.020 N
+946  1 CA  D ALA 10  ? ? CB  D ALA 10  ? ? 1.375 1.520 -0.145 0.021 N
+947  1 CA  D ALA 10  ? ? C   D ALA 10  ? ? 1.754 1.525 0.229  0.026 N
+948  1 CB  D VAL 11  ? ? CG1 D VAL 11  ? ? 1.279 1.524 -0.245 0.021 N
+949  1 CB  D VAL 11  ? ? CG2 D VAL 11  ? ? 1.695 1.524 0.171  0.021 N
+950  1 N   D THR 12  ? ? CA  D THR 12  ? ? 1.684 1.459 0.225  0.020 N
+951  1 CA  D THR 12  ? ? CB  D THR 12  ? ? 1.929 1.529 0.400  0.026 N
+952  1 CA  D THR 12  ? ? C   D THR 12  ? ? 1.368 1.525 -0.157 0.026 N
+953  1 C   D THR 12  ? ? O   D THR 12  ? ? 1.394 1.229 0.165  0.019 N
+954  1 CA  D ALA 13  ? ? CB  D ALA 13  ? ? 1.108 1.520 -0.412 0.021 N
+955  1 C   D ALA 13  ? ? O   D ALA 13  ? ? 1.101 1.229 -0.128 0.019 N
+956  1 C   D ALA 13  ? ? N   D LEU 14  ? ? 1.523 1.336 0.187  0.023 Y
+957  1 N   D LEU 14  ? ? CA  D LEU 14  ? ? 1.329 1.459 -0.130 0.020 N
+958  1 CA  D LEU 14  ? ? CB  D LEU 14  ? ? 1.721 1.533 0.188  0.023 N
+959  1 CG  D TRP 15  ? ? CD2 D TRP 15  ? ? 1.546 1.432 0.114  0.017 N
+960  1 NE1 D TRP 15  ? ? CE2 D TRP 15  ? ? 1.489 1.371 0.118  0.013 N
+961  1 CE2 D TRP 15  ? ? CD2 D TRP 15  ? ? 1.579 1.409 0.170  0.012 N
+962  1 CZ3 D TRP 15  ? ? CH2 D TRP 15  ? ? 1.545 1.396 0.149  0.016 N
+963  1 CH2 D TRP 15  ? ? CZ2 D TRP 15  ? ? 1.226 1.369 -0.143 0.019 N
+964  1 CA  D GLY 16  ? ? C   D GLY 16  ? ? 1.390 1.514 -0.124 0.016 N
+965  1 C   D GLY 16  ? ? O   D GLY 16  ? ? 1.356 1.232 0.124  0.016 N
+966  1 CB  D LYS 17  ? ? CG  D LYS 17  ? ? 1.317 1.521 -0.204 0.027 N
+967  1 CE  D LYS 17  ? ? NZ  D LYS 17  ? ? 1.982 1.486 0.496  0.025 N
+968  1 C   D LYS 17  ? ? N   D VAL 18  ? ? 1.606 1.336 0.270  0.023 Y
+969  1 N   D VAL 18  ? ? CA  D VAL 18  ? ? 1.700 1.459 0.241  0.020 N
+970  1 CA  D VAL 18  ? ? CB  D VAL 18  ? ? 1.257 1.543 -0.286 0.021 N
+971  1 CB  D VAL 18  ? ? CG1 D VAL 18  ? ? 1.294 1.524 -0.230 0.021 N
+972  1 CB  D VAL 18  ? ? CG2 D VAL 18  ? ? 1.796 1.524 0.272  0.021 N
+973  1 CA  D VAL 18  ? ? C   D VAL 18  ? ? 1.728 1.525 0.203  0.026 N
+974  1 C   D VAL 18  ? ? N   D ASN 19  ? ? 1.181 1.336 -0.155 0.023 Y
+975  1 CB  D ASN 19  ? ? CG  D ASN 19  ? ? 1.718 1.506 0.212  0.023 N
+976  1 CG  D ASN 19  ? ? OD1 D ASN 19  ? ? 1.598 1.235 0.363  0.022 N
+977  1 CG  D ASN 19  ? ? ND2 D ASN 19  ? ? 1.711 1.324 0.387  0.025 N
+978  1 CA  D ASN 19  ? ? C   D ASN 19  ? ? 1.258 1.525 -0.267 0.026 N
+979  1 C   D ASN 19  ? ? O   D ASN 19  ? ? 1.441 1.229 0.212  0.019 N
+980  1 C   D ASN 19  ? ? N   D VAL 20  ? ? 1.150 1.336 -0.186 0.023 Y
+981  1 N   D VAL 20  ? ? CA  D VAL 20  ? ? 1.632 1.459 0.173  0.020 N
+982  1 CA  D VAL 20  ? ? CB  D VAL 20  ? ? 2.095 1.543 0.552  0.021 N
+983  1 CB  D VAL 20  ? ? CG1 D VAL 20  ? ? 1.150 1.524 -0.374 0.021 N
+984  1 CB  D VAL 20  ? ? CG2 D VAL 20  ? ? 1.175 1.524 -0.349 0.021 N
+985  1 CA  D VAL 20  ? ? C   D VAL 20  ? ? 1.187 1.525 -0.338 0.026 N
+986  1 CB  D ASP 21  ? ? CG  D ASP 21  ? ? 1.779 1.513 0.266  0.021 N
+987  1 CG  D ASP 21  ? ? OD1 D ASP 21  ? ? 1.585 1.249 0.336  0.023 N
+988  1 CA  D ASP 21  ? ? C   D ASP 21  ? ? 0.967 1.525 -0.558 0.026 N
+989  1 C   D ASP 21  ? ? O   D ASP 21  ? ? 1.503 1.229 0.274  0.019 N
+990  1 CB  D GLU 22  ? ? CG  D GLU 22  ? ? 0.756 1.517 -0.761 0.019 N
+991  1 CG  D GLU 22  ? ? CD  D GLU 22  ? ? 2.386 1.515 0.871  0.015 N
+992  1 CD  D GLU 22  ? ? OE1 D GLU 22  ? ? 1.441 1.252 0.189  0.011 N
+993  1 CA  D GLU 22  ? ? C   D GLU 22  ? ? 1.826 1.525 0.301  0.026 N
+994  1 CB  D VAL 23  ? ? CG1 D VAL 23  ? ? 1.345 1.524 -0.179 0.021 N
+995  1 CA  D GLY 25  ? ? C   D GLY 25  ? ? 1.392 1.514 -0.122 0.016 N
+996  1 CB  D GLU 26  ? ? CG  D GLU 26  ? ? 2.179 1.517 0.662  0.019 N
+997  1 CG  D GLU 26  ? ? CD  D GLU 26  ? ? 1.902 1.515 0.387  0.015 N
+998  1 CD  D GLU 26  ? ? OE1 D GLU 26  ? ? 1.790 1.252 0.538  0.011 N
+999  1 CD  D GLU 26  ? ? OE2 D GLU 26  ? ? 1.706 1.252 0.454  0.011 N
+1000 1 CA  D GLU 26  ? ? C   D GLU 26  ? ? 1.707 1.525 0.182  0.026 N
+1001 1 CD  D ARG 30  ? ? NE  D ARG 30  ? ? 1.227 1.460 -0.233 0.017 N
+1002 1 CZ  D ARG 30  ? ? NH2 D ARG 30  ? ? 1.434 1.326 0.108  0.013 N
+1003 1 C   D ARG 30  ? ? N   D LEU 31  ? ? 1.193 1.336 -0.143 0.023 Y
+1004 1 CG  D LEU 32  ? ? CD2 D LEU 32  ? ? 1.274 1.514 -0.240 0.037 N
+1005 1 C   D LEU 32  ? ? O   D LEU 32  ? ? 1.357 1.229 0.128  0.019 N
+1006 1 CG  D TYR 35  ? ? CD2 D TYR 35  ? ? 1.235 1.387 -0.152 0.013 N
+1007 1 N   D PRO 36  ? ? CA  D PRO 36  ? ? 1.626 1.468 0.158  0.017 N
+1008 1 CD  D PRO 36  ? ? N   D PRO 36  ? ? 1.303 1.474 -0.171 0.014 N
+1009 1 CE2 D TRP 37  ? ? CZ2 D TRP 37  ? ? 1.561 1.393 0.168  0.017 N
+1010 1 CE2 D TRP 37  ? ? CD2 D TRP 37  ? ? 1.335 1.409 -0.074 0.012 N
+1011 1 CD  D GLN 39  ? ? OE1 D GLN 39  ? ? 1.408 1.235 0.173  0.022 N
+1012 1 CB  D ARG 40  ? ? CG  D ARG 40  ? ? 1.210 1.521 -0.311 0.027 N
+1013 1 CD  D ARG 40  ? ? NE  D ARG 40  ? ? 1.281 1.460 -0.179 0.017 N
+1014 1 NE  D ARG 40  ? ? CZ  D ARG 40  ? ? 1.467 1.326 0.141  0.013 N
+1015 1 CZ  D ARG 40  ? ? NH1 D ARG 40  ? ? 1.145 1.326 -0.181 0.013 N
+1016 1 CZ  D ARG 40  ? ? NH2 D ARG 40  ? ? 1.463 1.326 0.137  0.013 N
+1017 1 C   D ARG 40  ? ? O   D ARG 40  ? ? 1.463 1.229 0.234  0.019 N
+1018 1 CB  D PHE 41  ? ? CG  D PHE 41  ? ? 1.644 1.509 0.135  0.017 N
+1019 1 CG  D PHE 41  ? ? CD2 D PHE 41  ? ? 1.259 1.383 -0.124 0.015 N
+1020 1 CE1 D PHE 41  ? ? CZ  D PHE 41  ? ? 1.079 1.369 -0.290 0.019 N
+1021 1 CA  D PHE 41  ? ? C   D PHE 41  ? ? 1.732 1.525 0.207  0.026 N
+1022 1 CG  D PHE 42  ? ? CD1 D PHE 42  ? ? 1.684 1.383 0.301  0.015 N
+1023 1 CE1 D PHE 42  ? ? CZ  D PHE 42  ? ? 1.196 1.369 -0.173 0.019 N
+1024 1 CZ  D PHE 42  ? ? CE2 D PHE 42  ? ? 1.558 1.369 0.189  0.019 N
+1025 1 N   D GLU 43  ? ? CA  D GLU 43  ? ? 1.607 1.459 0.148  0.020 N
+1026 1 CA  D GLU 43  ? ? CB  D GLU 43  ? ? 1.182 1.535 -0.353 0.022 N
+1027 1 CB  D GLU 43  ? ? CG  D GLU 43  ? ? 0.777 1.517 -0.740 0.019 N
+1028 1 CG  D GLU 43  ? ? CD  D GLU 43  ? ? 1.918 1.515 0.403  0.015 N
+1029 1 CD  D GLU 43  ? ? OE1 D GLU 43  ? ? 1.602 1.252 0.350  0.011 N
+1030 1 CD  D GLU 43  ? ? OE2 D GLU 43  ? ? 1.586 1.252 0.334  0.011 N
+1031 1 CA  D GLU 43  ? ? C   D GLU 43  ? ? 1.937 1.525 0.412  0.026 N
+1032 1 C   D GLU 43  ? ? O   D GLU 43  ? ? 1.068 1.229 -0.161 0.019 N
+1033 1 CA  D SER 44  ? ? CB  D SER 44  ? ? 1.344 1.525 -0.181 0.015 N
+1034 1 CB  D SER 44  ? ? OG  D SER 44  ? ? 1.254 1.418 -0.164 0.013 N
+1035 1 CA  D SER 44  ? ? C   D SER 44  ? ? 1.338 1.525 -0.187 0.026 N
+1036 1 C   D SER 44  ? ? N   D PHE 45  ? ? 1.488 1.336 0.152  0.023 Y
+1037 1 CG  D PHE 45  ? ? CD2 D PHE 45  ? ? 1.225 1.383 -0.158 0.015 N
+1038 1 CD1 D PHE 45  ? ? CE1 D PHE 45  ? ? 1.605 1.388 0.217  0.020 N
+1039 1 CA  D PHE 45  ? ? C   D PHE 45  ? ? 1.724 1.525 0.199  0.026 N
+1040 1 C   D PHE 45  ? ? O   D PHE 45  ? ? 1.371 1.229 0.142  0.019 N
+1041 1 C   D PHE 45  ? ? N   D GLY 46  ? ? 0.867 1.336 -0.469 0.023 Y
+1042 1 N   D GLY 46  ? ? CA  D GLY 46  ? ? 1.314 1.456 -0.142 0.015 N
+1043 1 CA  D GLY 46  ? ? C   D GLY 46  ? ? 1.822 1.514 0.308  0.016 N
+1044 1 C   D GLY 46  ? ? O   D GLY 46  ? ? 1.401 1.232 0.169  0.016 N
+1045 1 N   D ASP 47  ? ? CA  D ASP 47  ? ? 2.088 1.459 0.629  0.020 N
+1046 1 CA  D ASP 47  ? ? CB  D ASP 47  ? ? 1.942 1.535 0.407  0.022 N
+1047 1 CB  D ASP 47  ? ? CG  D ASP 47  ? ? 1.756 1.513 0.243  0.021 N
+1048 1 CA  D ASP 47  ? ? C   D ASP 47  ? ? 2.426 1.525 0.901  0.026 N
+1049 1 C   D ASP 47  ? ? O   D ASP 47  ? ? 1.346 1.229 0.117  0.019 N
+1050 1 C   D ASP 47  ? ? N   D LEU 48  ? ? 1.186 1.336 -0.150 0.023 Y
+1051 1 N   D LEU 48  ? ? CA  D LEU 48  ? ? 1.717 1.459 0.258  0.020 N
+1052 1 CA  D LEU 48  ? ? CB  D LEU 48  ? ? 1.344 1.533 -0.189 0.023 N
+1053 1 CG  D LEU 48  ? ? CD1 D LEU 48  ? ? 1.752 1.514 0.238  0.037 N
+1054 1 CA  D LEU 48  ? ? C   D LEU 48  ? ? 1.686 1.525 0.161  0.026 N
+1055 1 C   D LEU 48  ? ? N   D SER 49  ? ? 1.512 1.336 0.176  0.023 Y
+1056 1 CA  D SER 49  ? ? C   D SER 49  ? ? 1.863 1.525 0.338  0.026 N
+1057 1 C   D SER 49  ? ? O   D SER 49  ? ? 1.400 1.229 0.171  0.019 N
+1058 1 N   D THR 50  ? ? CA  D THR 50  ? ? 1.708 1.459 0.249  0.020 N
+1059 1 CA  D THR 50  ? ? CB  D THR 50  ? ? 2.108 1.529 0.579  0.026 N
+1060 1 CA  D THR 50  ? ? C   D THR 50  ? ? 1.714 1.525 0.189  0.026 N
+1061 1 CD  D PRO 51  ? ? N   D PRO 51  ? ? 1.586 1.474 0.112  0.014 N
+1062 1 CA  D PRO 51  ? ? C   D PRO 51  ? ? 1.388 1.524 -0.136 0.020 N
+1063 1 C   D PRO 51  ? ? O   D PRO 51  ? ? 1.371 1.228 0.143  0.020 N
+1064 1 C   D PRO 51  ? ? N   D ASP 52  ? ? 1.474 1.336 0.138  0.023 Y
+1065 1 N   D ASP 52  ? ? CA  D ASP 52  ? ? 1.764 1.459 0.305  0.020 N
+1066 1 CB  D ASP 52  ? ? CG  D ASP 52  ? ? 1.753 1.513 0.240  0.021 N
+1067 1 CG  D ASP 52  ? ? OD2 D ASP 52  ? ? 2.443 1.249 1.194  0.023 N
+1068 1 CA  D ALA 53  ? ? CB  D ALA 53  ? ? 1.293 1.520 -0.227 0.021 N
+1069 1 CA  D ALA 53  ? ? C   D ALA 53  ? ? 1.762 1.525 0.237  0.026 N
+1070 1 C   D ALA 53  ? ? O   D ALA 53  ? ? 0.892 1.229 -0.337 0.019 N
+1071 1 C   D ALA 53  ? ? N   D VAL 54  ? ? 1.557 1.336 0.221  0.023 Y
+1072 1 N   D VAL 54  ? ? CA  D VAL 54  ? ? 1.615 1.459 0.156  0.020 N
+1073 1 CB  D VAL 54  ? ? CG1 D VAL 54  ? ? 1.663 1.524 0.139  0.021 N
+1074 1 CB  D VAL 54  ? ? CG2 D VAL 54  ? ? 1.264 1.524 -0.260 0.021 N
+1075 1 C   D VAL 54  ? ? O   D VAL 54  ? ? 1.381 1.229 0.152  0.019 N
+1076 1 CA  D MET 55  ? ? CB  D MET 55  ? ? 1.674 1.535 0.139  0.022 N
+1077 1 CB  D MET 55  ? ? CG  D MET 55  ? ? 1.250 1.509 -0.259 0.032 N
+1078 1 CA  D MET 55  ? ? C   D MET 55  ? ? 1.897 1.525 0.372  0.026 N
+1079 1 CB  D PRO 58  ? ? CG  D PRO 58  ? ? 2.000 1.495 0.505  0.050 N
+1080 1 CG  D PRO 58  ? ? CD  D PRO 58  ? ? 0.226 1.502 -1.276 0.033 N
+1081 1 CD  D PRO 58  ? ? N   D PRO 58  ? ? 1.710 1.474 0.236  0.014 N
+1082 1 CA  D PRO 58  ? ? C   D PRO 58  ? ? 1.686 1.524 0.162  0.020 N
+1083 1 C   D PRO 58  ? ? O   D PRO 58  ? ? 1.432 1.228 0.204  0.020 N
+1084 1 C   D PRO 58  ? ? N   D LYS 59  ? ? 1.162 1.336 -0.174 0.023 Y
+1085 1 N   D LYS 59  ? ? CA  D LYS 59  ? ? 1.336 1.459 -0.123 0.020 N
+1086 1 CG  D LYS 59  ? ? CD  D LYS 59  ? ? 0.974 1.520 -0.546 0.034 N
+1087 1 CD  D LYS 59  ? ? CE  D LYS 59  ? ? 1.880 1.508 0.372  0.025 N
+1088 1 CA  D LYS 59  ? ? C   D LYS 59  ? ? 1.757 1.525 0.232  0.026 N
+1089 1 N   D VAL 60  ? ? CA  D VAL 60  ? ? 1.665 1.459 0.206  0.020 N
+1090 1 CA  D VAL 60  ? ? C   D VAL 60  ? ? 1.329 1.525 -0.196 0.026 N
+1091 1 C   D VAL 60  ? ? N   D LYS 61  ? ? 1.476 1.336 0.140  0.023 Y
+1092 1 CG  D LYS 61  ? ? CD  D LYS 61  ? ? 1.272 1.520 -0.248 0.034 N
+1093 1 CD  D LYS 61  ? ? CE  D LYS 61  ? ? 1.726 1.508 0.218  0.025 N
+1094 1 CE  D LYS 61  ? ? NZ  D LYS 61  ? ? 1.234 1.486 -0.252 0.025 N
+1095 1 CA  D HIS 63  ? ? CB  D HIS 63  ? ? 1.270 1.535 -0.265 0.022 N
+1096 1 CB  D HIS 63  ? ? CG  D HIS 63  ? ? 1.685 1.496 0.189  0.018 N
+1097 1 CG  D HIS 63  ? ? CD2 D HIS 63  ? ? 1.440 1.354 0.086  0.009 N
+1098 1 ND1 D HIS 63  ? ? CE1 D HIS 63  ? ? 1.632 1.343 0.289  0.025 N
+1099 1 CE1 D HIS 63  ? ? NE2 D HIS 63  ? ? 1.188 1.317 -0.129 0.011 N
+1100 1 C   D GLY 64  ? ? N   D LYS 65  ? ? 1.499 1.336 0.163  0.023 Y
+1101 1 CG  D LYS 65  ? ? CD  D LYS 65  ? ? 2.266 1.520 0.746  0.034 N
+1102 1 CD  D LYS 65  ? ? CE  D LYS 65  ? ? 2.203 1.508 0.695  0.025 N
+1103 1 CB  D LYS 66  ? ? CG  D LYS 66  ? ? 1.102 1.521 -0.419 0.027 N
+1104 1 CG  D LYS 66  ? ? CD  D LYS 66  ? ? 2.063 1.520 0.543  0.034 N
+1105 1 CD  D LYS 66  ? ? CE  D LYS 66  ? ? 2.269 1.508 0.761  0.025 N
+1106 1 CE  D LYS 66  ? ? NZ  D LYS 66  ? ? 1.950 1.486 0.464  0.025 N
+1107 1 C   D LYS 66  ? ? N   D VAL 67  ? ? 1.483 1.336 0.147  0.023 Y
+1108 1 CA  D VAL 67  ? ? CB  D VAL 67  ? ? 1.760 1.543 0.217  0.021 N
+1109 1 CA  D VAL 67  ? ? C   D VAL 67  ? ? 1.339 1.525 -0.186 0.026 N
+1110 1 CB  D LEU 68  ? ? CG  D LEU 68  ? ? 1.329 1.521 -0.192 0.029 N
+1111 1 CG  D LEU 68  ? ? CD1 D LEU 68  ? ? 1.238 1.514 -0.276 0.037 N
+1112 1 C   D ALA 70  ? ? O   D ALA 70  ? ? 1.386 1.229 0.157  0.019 N
+1113 1 N   D PHE 71  ? ? CA  D PHE 71  ? ? 1.633 1.459 0.174  0.020 N
+1114 1 CE1 D PHE 71  ? ? CZ  D PHE 71  ? ? 1.248 1.369 -0.121 0.019 N
+1115 1 CA  D SER 72  ? ? CB  D SER 72  ? ? 1.667 1.525 0.142  0.015 N
+1116 1 CB  D SER 72  ? ? OG  D SER 72  ? ? 1.326 1.418 -0.092 0.013 N
+1117 1 CA  D ASP 73  ? ? CB  D ASP 73  ? ? 1.859 1.535 0.324  0.022 N
+1118 1 CB  D ASP 73  ? ? CG  D ASP 73  ? ? 1.282 1.513 -0.231 0.021 N
+1119 1 CG  D ASP 73  ? ? OD1 D ASP 73  ? ? 1.580 1.249 0.331  0.023 N
+1120 1 CG  D ASP 73  ? ? OD2 D ASP 73  ? ? 2.258 1.249 1.009  0.023 N
+1121 1 CA  D ASP 73  ? ? C   D ASP 73  ? ? 1.209 1.525 -0.316 0.026 N
+1122 1 C   D ASP 73  ? ? N   D GLY 74  ? ? 1.613 1.336 0.277  0.023 Y
+1123 1 N   D GLY 74  ? ? CA  D GLY 74  ? ? 1.366 1.456 -0.090 0.015 N
+1124 1 CA  D LEU 75  ? ? CB  D LEU 75  ? ? 1.691 1.533 0.158  0.023 N
+1125 1 CG  D LEU 75  ? ? CD2 D LEU 75  ? ? 1.238 1.514 -0.276 0.037 N
+1126 1 N   D ALA 76  ? ? CA  D ALA 76  ? ? 1.940 1.459 0.481  0.020 N
+1127 1 CA  D ALA 76  ? ? CB  D ALA 76  ? ? 1.352 1.520 -0.168 0.021 N
+1128 1 CA  D ALA 76  ? ? C   D ALA 76  ? ? 1.072 1.525 -0.453 0.026 N
+1129 1 C   D ALA 76  ? ? O   D ALA 76  ? ? 1.489 1.229 0.260  0.019 N
+1130 1 N   D HIS 77  ? ? CA  D HIS 77  ? ? 1.323 1.459 -0.136 0.020 N
+1131 1 CA  D HIS 77  ? ? CB  D HIS 77  ? ? 1.754 1.535 0.219  0.022 N
+1132 1 CG  D HIS 77  ? ? CD2 D HIS 77  ? ? 1.417 1.354 0.063  0.009 N
+1133 1 ND1 D HIS 77  ? ? CE1 D HIS 77  ? ? 1.908 1.343 0.565  0.025 N
+1134 1 CE1 D HIS 77  ? ? NE2 D HIS 77  ? ? 1.042 1.317 -0.275 0.011 N
+1135 1 NE2 D HIS 77  ? ? CD2 D HIS 77  ? ? 1.880 1.415 0.465  0.021 N
+1136 1 C   D HIS 77  ? ? N   D LEU 78  ? ? 1.549 1.336 0.213  0.023 Y
+1137 1 N   D LEU 78  ? ? CA  D LEU 78  ? ? 1.253 1.459 -0.206 0.020 N
+1138 1 CA  D LEU 78  ? ? CB  D LEU 78  ? ? 1.793 1.533 0.260  0.023 N
+1139 1 CG  D LEU 78  ? ? CD2 D LEU 78  ? ? 0.881 1.514 -0.633 0.037 N
+1140 1 C   D LEU 78  ? ? O   D LEU 78  ? ? 1.015 1.229 -0.214 0.019 N
+1141 1 C   D LEU 78  ? ? N   D ASP 79  ? ? 1.497 1.336 0.161  0.023 Y
+1142 1 CA  D ASP 79  ? ? CB  D ASP 79  ? ? 1.732 1.535 0.197  0.022 N
+1143 1 CB  D ASP 79  ? ? CG  D ASP 79  ? ? 1.225 1.513 -0.288 0.021 N
+1144 1 CG  D ASP 79  ? ? OD1 D ASP 79  ? ? 1.990 1.249 0.741  0.023 N
+1145 1 CG  D ASP 79  ? ? OD2 D ASP 79  ? ? 1.981 1.249 0.732  0.023 N
+1146 1 CA  D ASP 79  ? ? C   D ASP 79  ? ? 1.833 1.525 0.308  0.026 N
+1147 1 N   D ASN 80  ? ? CA  D ASN 80  ? ? 1.755 1.459 0.296  0.020 N
+1148 1 CA  D ASN 80  ? ? CB  D ASN 80  ? ? 1.164 1.527 -0.363 0.026 N
+1149 1 CB  D ASN 80  ? ? CG  D ASN 80  ? ? 1.263 1.506 -0.243 0.023 N
+1150 1 CG  D ASN 80  ? ? OD1 D ASN 80  ? ? 1.659 1.235 0.424  0.022 N
+1151 1 CA  D ASN 80  ? ? C   D ASN 80  ? ? 1.733 1.525 0.208  0.026 N
+1152 1 C   D ASN 80  ? ? O   D ASN 80  ? ? 1.067 1.229 -0.162 0.019 N
+1153 1 CG  D LEU 81  ? ? CD1 D LEU 81  ? ? 1.246 1.514 -0.268 0.037 N
+1154 1 CB  D LYS 82  ? ? CG  D LYS 82  ? ? 1.286 1.521 -0.235 0.027 N
+1155 1 CG  D LYS 82  ? ? CD  D LYS 82  ? ? 1.890 1.520 0.370  0.034 N
+1156 1 CD  D LYS 82  ? ? CE  D LYS 82  ? ? 2.415 1.508 0.907  0.025 N
+1157 1 CE  D LYS 82  ? ? NZ  D LYS 82  ? ? 1.943 1.486 0.457  0.025 N
+1158 1 C   D LYS 82  ? ? N   D GLY 83  ? ? 1.532 1.336 0.196  0.023 Y
+1159 1 CA  D GLY 83  ? ? C   D GLY 83  ? ? 1.411 1.514 -0.103 0.016 N
+1160 1 C   D GLY 83  ? ? O   D GLY 83  ? ? 1.499 1.232 0.267  0.016 N
+1161 1 C   D GLY 83  ? ? N   D THR 84  ? ? 1.551 1.336 0.215  0.023 Y
+1162 1 N   D THR 84  ? ? CA  D THR 84  ? ? 1.327 1.459 -0.132 0.020 N
+1163 1 CB  D THR 84  ? ? OG1 D THR 84  ? ? 1.225 1.428 -0.203 0.020 N
+1164 1 CA  D THR 84  ? ? C   D THR 84  ? ? 1.683 1.525 0.158  0.026 N
+1165 1 N   D PHE 85  ? ? CA  D PHE 85  ? ? 1.630 1.459 0.171  0.020 N
+1166 1 CE1 D PHE 85  ? ? CZ  D PHE 85  ? ? 1.487 1.369 0.118  0.019 N
+1167 1 N   D ALA 86  ? ? CA  D ALA 86  ? ? 1.596 1.459 0.137  0.020 N
+1168 1 CA  D ALA 86  ? ? CB  D ALA 86  ? ? 1.676 1.520 0.156  0.021 N
+1169 1 CG  D GLU 90  ? ? CD  D GLU 90  ? ? 2.428 1.515 0.913  0.015 N
+1170 1 CD  D GLU 90  ? ? OE1 D GLU 90  ? ? 1.639 1.252 0.387  0.011 N
+1171 1 C   D LEU 91  ? ? N   D HIS 92  ? ? 1.491 1.336 0.155  0.023 Y
+1172 1 CG  D HIS 92  ? ? ND1 D HIS 92  ? ? 1.550 1.383 0.167  0.022 N
+1173 1 CA  D HIS 92  ? ? C   D HIS 92  ? ? 1.756 1.525 0.231  0.026 N
+1174 1 N   D CYS 93  ? ? CA  D CYS 93  ? ? 1.590 1.459 0.131  0.020 N
+1175 1 CB  D CYS 93  ? ? SG  D CYS 93  ? ? 1.998 1.818 0.180  0.017 N
+1176 1 C   D CYS 93  ? ? O   D CYS 93  ? ? 1.054 1.229 -0.175 0.019 N
+1177 1 N   D ASP 94  ? ? CA  D ASP 94  ? ? 1.677 1.459 0.218  0.020 N
+1178 1 CB  D ASP 94  ? ? CG  D ASP 94  ? ? 1.654 1.513 0.141  0.021 N
+1179 1 CG  D ASP 94  ? ? OD1 D ASP 94  ? ? 1.061 1.249 -0.188 0.023 N
+1180 1 CG  D ASP 94  ? ? OD2 D ASP 94  ? ? 1.528 1.249 0.279  0.023 N
+1181 1 N   D LYS 95  ? ? CA  D LYS 95  ? ? 1.593 1.459 0.134  0.020 N
+1182 1 CG  D LYS 95  ? ? CD  D LYS 95  ? ? 2.164 1.520 0.644  0.034 N
+1183 1 CE  D LYS 95  ? ? NZ  D LYS 95  ? ? 1.985 1.486 0.499  0.025 N
+1184 1 CA  D LYS 95  ? ? C   D LYS 95  ? ? 1.366 1.525 -0.159 0.026 N
+1185 1 C   D LYS 95  ? ? N   D LEU 96  ? ? 1.637 1.336 0.301  0.023 Y
+1186 1 CB  D HIS 97  ? ? CG  D HIS 97  ? ? 1.654 1.496 0.158  0.018 N
+1187 1 ND1 D HIS 97  ? ? CE1 D HIS 97  ? ? 1.535 1.343 0.192  0.025 N
+1188 1 CB  D VAL 98  ? ? CG2 D VAL 98  ? ? 1.671 1.524 0.147  0.021 N
+1189 1 CB  D ASP 99  ? ? CG  D ASP 99  ? ? 1.661 1.513 0.148  0.021 N
+1190 1 CB  D GLU 101 ? ? CG  D GLU 101 ? ? 1.718 1.517 0.201  0.019 N
+1191 1 CG  D GLU 101 ? ? CD  D GLU 101 ? ? 2.065 1.515 0.550  0.015 N
+1192 1 CD  D GLU 101 ? ? OE2 D GLU 101 ? ? 1.450 1.252 0.198  0.011 N
+1193 1 C   D ASN 102 ? ? O   D ASN 102 ? ? 1.438 1.229 0.209  0.019 N
+1194 1 CG  D PHE 103 ? ? CD1 D PHE 103 ? ? 1.488 1.383 0.105  0.015 N
+1195 1 CG  D ARG 104 ? ? CD  D ARG 104 ? ? 1.701 1.515 0.186  0.025 N
+1196 1 CD  D ARG 104 ? ? NE  D ARG 104 ? ? 1.838 1.460 0.378  0.017 N
+1197 1 NE  D ARG 104 ? ? CZ  D ARG 104 ? ? 2.576 1.326 1.250  0.013 N
+1198 1 CZ  D ARG 104 ? ? NH1 D ARG 104 ? ? 1.481 1.326 0.155  0.013 N
+1199 1 CZ  D ARG 104 ? ? NH2 D ARG 104 ? ? 1.221 1.326 -0.105 0.013 N
+1200 1 CA  D LEU 105 ? ? CB  D LEU 105 ? ? 1.375 1.533 -0.158 0.023 N
+1201 1 CB  D ASN 108 ? ? CG  D ASN 108 ? ? 1.828 1.506 0.322  0.023 N
+1202 1 CA  D LEU 110 ? ? CB  D LEU 110 ? ? 1.379 1.533 -0.154 0.023 N
+1203 1 C   D LEU 110 ? ? N   D VAL 111 ? ? 1.526 1.336 0.190  0.023 Y
+1204 1 C   D CYS 112 ? ? O   D CYS 112 ? ? 1.111 1.229 -0.118 0.019 N
+1205 1 CB  D VAL 113 ? ? CG2 D VAL 113 ? ? 1.742 1.524 0.218  0.021 N
+1206 1 CG  D HIS 116 ? ? ND1 D HIS 116 ? ? 1.248 1.369 -0.121 0.015 N
+1207 1 CE1 D HIS 116 ? ? NE2 D HIS 116 ? ? 1.502 1.333 0.169  0.019 N
+1208 1 CB  D HIS 117 ? ? CG  D HIS 117 ? ? 1.244 1.492 -0.248 0.016 N
+1209 1 CG  D HIS 117 ? ? CD2 D HIS 117 ? ? 1.601 1.354 0.247  0.009 N
+1210 1 CG  D HIS 117 ? ? ND1 D HIS 117 ? ? 1.738 1.383 0.355  0.022 N
+1211 1 ND1 D HIS 117 ? ? CE1 D HIS 117 ? ? 1.645 1.343 0.302  0.025 N
+1212 1 CE1 D HIS 117 ? ? NE2 D HIS 117 ? ? 0.970 1.317 -0.347 0.011 N
+1213 1 NE2 D HIS 117 ? ? CD2 D HIS 117 ? ? 1.232 1.373 -0.141 0.011 N
+1214 1 CG  D PHE 118 ? ? CD2 D PHE 118 ? ? 1.475 1.383 0.092  0.015 N
+1215 1 CE1 D PHE 118 ? ? CZ  D PHE 118 ? ? 1.484 1.369 0.115  0.019 N
+1216 1 CE2 D PHE 118 ? ? CD2 D PHE 118 ? ? 1.541 1.388 0.153  0.020 N
+1217 1 CA  D GLY 119 ? ? C   D GLY 119 ? ? 1.630 1.514 0.116  0.016 N
+1218 1 CB  D LYS 120 ? ? CG  D LYS 120 ? ? 1.353 1.521 -0.168 0.027 N
+1219 1 CE  D LYS 120 ? ? NZ  D LYS 120 ? ? 2.292 1.486 0.806  0.025 N
+1220 1 N   D GLU 121 ? ? CA  D GLU 121 ? ? 1.286 1.459 -0.173 0.020 N
+1221 1 CA  D GLU 121 ? ? CB  D GLU 121 ? ? 1.792 1.535 0.257  0.022 N
+1222 1 CB  D GLU 121 ? ? CG  D GLU 121 ? ? 1.087 1.517 -0.430 0.019 N
+1223 1 CG  D GLU 121 ? ? CD  D GLU 121 ? ? 2.008 1.515 0.493  0.015 N
+1224 1 CD  D GLU 121 ? ? OE1 D GLU 121 ? ? 1.518 1.252 0.266  0.011 N
+1225 1 CG  D PHE 122 ? ? CD2 D PHE 122 ? ? 1.502 1.383 0.119  0.015 N
+1226 1 CG  D PHE 122 ? ? CD1 D PHE 122 ? ? 1.264 1.383 -0.119 0.015 N
+1227 1 CD1 D PHE 122 ? ? CE1 D PHE 122 ? ? 1.526 1.388 0.138  0.020 N
+1228 1 CB  D THR 123 ? ? CG2 D THR 123 ? ? 1.796 1.519 0.277  0.033 N
+1229 1 N   D PRO 125 ? ? CA  D PRO 125 ? ? 1.325 1.468 -0.143 0.017 N
+1230 1 CD  D PRO 125 ? ? N   D PRO 125 ? ? 1.670 1.474 0.196  0.014 N
+1231 1 CA  D VAL 126 ? ? CB  D VAL 126 ? ? 1.813 1.543 0.270  0.021 N
+1232 1 CB  D VAL 126 ? ? CG1 D VAL 126 ? ? 1.387 1.524 -0.137 0.021 N
+1233 1 C   D VAL 126 ? ? O   D VAL 126 ? ? 1.096 1.229 -0.133 0.019 N
+1234 1 C   D VAL 126 ? ? N   D GLN 127 ? ? 1.499 1.336 0.163  0.023 Y
+1235 1 CD1 D TYR 130 ? ? CE1 D TYR 130 ? ? 1.559 1.389 0.170  0.015 N
+1236 1 CE1 D TYR 130 ? ? CZ  D TYR 130 ? ? 1.581 1.381 0.200  0.013 N
+1237 1 CZ  D TYR 130 ? ? CE2 D TYR 130 ? ? 1.276 1.381 -0.105 0.013 N
+1238 1 CE2 D TYR 130 ? ? CD2 D TYR 130 ? ? 1.500 1.389 0.111  0.015 N
+1239 1 CG  D GLN 131 ? ? CD  D GLN 131 ? ? 1.768 1.506 0.262  0.023 N
+1240 1 C   D GLN 131 ? ? O   D GLN 131 ? ? 1.101 1.229 -0.128 0.019 N
+1241 1 CD  D LYS 132 ? ? CE  D LYS 132 ? ? 1.707 1.508 0.199  0.025 N
+1242 1 CE  D LYS 132 ? ? NZ  D LYS 132 ? ? 2.485 1.486 0.999  0.025 N
+1243 1 CA  D ALA 135 ? ? C   D ALA 135 ? ? 1.728 1.525 0.203  0.026 N
+1244 1 N   D GLY 136 ? ? CA  D GLY 136 ? ? 1.302 1.456 -0.154 0.015 N
+1245 1 CA  D VAL 137 ? ? CB  D VAL 137 ? ? 1.734 1.543 0.191  0.021 N
+1246 1 CA  D ASN 139 ? ? CB  D ASN 139 ? ? 1.203 1.527 -0.324 0.026 N
+1247 1 CG  D ASN 139 ? ? OD1 D ASN 139 ? ? 1.678 1.235 0.443  0.022 N
+1248 1 CG  D ASN 139 ? ? ND2 D ASN 139 ? ? 1.567 1.324 0.243  0.025 N
+1249 1 C   D ALA 140 ? ? N   D LEU 141 ? ? 1.196 1.336 -0.140 0.023 Y
+1250 1 CG  D LEU 141 ? ? CD2 D LEU 141 ? ? 1.776 1.514 0.262  0.037 N
+1251 1 CB  D HIS 143 ? ? CG  D HIS 143 ? ? 1.339 1.492 -0.153 0.016 N
+1252 1 CG  D HIS 143 ? ? CD2 D HIS 143 ? ? 1.848 1.354 0.494  0.009 N
+1253 1 CG  D HIS 143 ? ? ND1 D HIS 143 ? ? 1.230 1.369 -0.139 0.015 N
+1254 1 ND1 D HIS 143 ? ? CE1 D HIS 143 ? ? 1.620 1.343 0.277  0.025 N
+1255 1 CA  D LYS 144 ? ? CB  D LYS 144 ? ? 1.300 1.535 -0.235 0.022 N
+1256 1 CB  D LYS 144 ? ? CG  D LYS 144 ? ? 1.685 1.521 0.164  0.027 N
+1257 1 CD  D LYS 144 ? ? CE  D LYS 144 ? ? 1.101 1.508 -0.407 0.025 N
+1258 1 CE  D LYS 144 ? ? NZ  D LYS 144 ? ? 2.164 1.486 0.678  0.025 N
+1259 1 N   D TYR 145 ? ? CA  D TYR 145 ? ? 1.339 1.459 -0.120 0.020 N
+1260 1 CE1 D TYR 145 ? ? CZ  D TYR 145 ? ? 1.473 1.381 0.092  0.013 N
+1261 1 CZ  D TYR 145 ? ? CE2 D TYR 145 ? ? 1.227 1.381 -0.154 0.013 N
+1262 1 CE2 D TYR 145 ? ? CD2 D TYR 145 ? ? 1.516 1.389 0.127  0.015 N
+1263 1 N   D HIS 146 ? ? CA  D HIS 146 ? ? 1.626 1.459 0.167  0.020 N
+1264 1 CA  D HIS 146 ? ? CB  D HIS 146 ? ? 1.724 1.535 0.189  0.022 N
+1265 1 CG  D HIS 146 ? ? CD2 D HIS 146 ? ? 1.234 1.353 -0.119 0.017 N
+1266 1 CG  D HIS 146 ? ? ND1 D HIS 146 ? ? 1.849 1.383 0.466  0.022 N
+1267 1 ND1 D HIS 146 ? ? CE1 D HIS 146 ? ? 0.669 1.323 -0.654 0.015 N
+1268 1 CE1 D HIS 146 ? ? NE2 D HIS 146 ? ? 1.596 1.333 0.263  0.019 N
+1269 1 NE2 D HIS 146 ? ? CD2 D HIS 146 ? ? 1.578 1.415 0.163  0.021 N
+1270 1 C   D HIS 146 ? ? OXT D HIS 146 ? ? 1.398 1.229 0.169  0.019 N
+#
+loop_
+_pdbx_validate_rmsd_angle.id
+_pdbx_validate_rmsd_angle.PDB_model_num
+_pdbx_validate_rmsd_angle.auth_atom_id_1
+_pdbx_validate_rmsd_angle.auth_asym_id_1
+_pdbx_validate_rmsd_angle.auth_comp_id_1
+_pdbx_validate_rmsd_angle.auth_seq_id_1
+_pdbx_validate_rmsd_angle.PDB_ins_code_1
+_pdbx_validate_rmsd_angle.label_alt_id_1
+_pdbx_validate_rmsd_angle.auth_atom_id_2
+_pdbx_validate_rmsd_angle.auth_asym_id_2
+_pdbx_validate_rmsd_angle.auth_comp_id_2
+_pdbx_validate_rmsd_angle.auth_seq_id_2
+_pdbx_validate_rmsd_angle.PDB_ins_code_2
+_pdbx_validate_rmsd_angle.label_alt_id_2
+_pdbx_validate_rmsd_angle.auth_atom_id_3
+_pdbx_validate_rmsd_angle.auth_asym_id_3
+_pdbx_validate_rmsd_angle.auth_comp_id_3
+_pdbx_validate_rmsd_angle.auth_seq_id_3
+_pdbx_validate_rmsd_angle.PDB_ins_code_3
+_pdbx_validate_rmsd_angle.label_alt_id_3
+_pdbx_validate_rmsd_angle.angle_value
+_pdbx_validate_rmsd_angle.angle_target_value
+_pdbx_validate_rmsd_angle.angle_deviation
+_pdbx_validate_rmsd_angle.angle_standard_deviation
+_pdbx_validate_rmsd_angle.linker_flag
+1    1 CG1 A VAL 1   ? ? CB  A VAL 1   ? ? CG2 A VAL 1   ? ? 138.34 110.90 27.44  1.60 N
+2    1 CA  A VAL 1   ? ? CB  A VAL 1   ? ? CG2 A VAL 1   ? ? 84.94  110.90 -25.96 1.50 N
+3    1 CA  A VAL 1   ? ? C   A VAL 1   ? ? N   A LEU 2   ? ? 103.91 117.20 -13.29 2.20 Y
+4    1 O   A VAL 1   ? ? C   A VAL 1   ? ? N   A LEU 2   ? ? 135.34 122.70 12.64  1.60 Y
+5    1 C   A VAL 1   ? ? N   A LEU 2   ? ? CA  A LEU 2   ? ? 101.09 121.70 -20.61 2.50 Y
+6    1 N   A LEU 2   ? ? CA  A LEU 2   ? ? CB  A LEU 2   ? ? 92.49  110.40 -17.91 2.00 N
+7    1 CB  A LEU 2   ? ? CG  A LEU 2   ? ? CD1 A LEU 2   ? ? 124.01 111.00 13.01  1.70 N
+8    1 CA  A LEU 2   ? ? C   A LEU 2   ? ? O   A LEU 2   ? ? 98.31  120.10 -21.79 2.10 N
+9    1 O   A LEU 2   ? ? C   A LEU 2   ? ? N   A SER 3   ? ? 152.89 122.70 30.19  1.60 Y
+10   1 N   A SER 3   ? ? CA  A SER 3   ? ? CB  A SER 3   ? ? 100.76 110.50 -9.74  1.50 N
+11   1 CA  A SER 3   ? ? C   A SER 3   ? ? O   A SER 3   ? ? 136.04 120.10 15.94  2.10 N
+12   1 O   A SER 3   ? ? C   A SER 3   ? ? N   A PRO 4   ? ? 106.46 121.10 -14.64 1.90 Y
+13   1 C   A SER 3   ? ? N   A PRO 4   ? ? CA  A PRO 4   ? ? 105.24 119.30 -14.06 1.50 Y
+14   1 C   A SER 3   ? ? N   A PRO 4   ? ? CD  A PRO 4   ? ? 109.94 128.40 -18.46 2.10 Y
+15   1 CB  A PRO 4   ? ? CA  A PRO 4   ? ? C   A PRO 4   ? ? 80.99  111.70 -30.71 2.10 N
+16   1 CA  A PRO 4   ? ? CB  A PRO 4   ? ? CG  A PRO 4   ? ? 89.06  104.80 -15.74 1.90 N
+17   1 N   A PRO 4   ? ? CD  A PRO 4   ? ? CG  A PRO 4   ? ? 90.80  103.20 -12.40 1.50 N
+18   1 O   A PRO 4   ? ? C   A PRO 4   ? ? N   A ALA 5   ? ? 112.82 122.70 -9.88  1.60 Y
+19   1 CB  A ALA 5   ? ? CA  A ALA 5   ? ? C   A ALA 5   ? ? 99.28  110.10 -10.82 1.50 N
+20   1 CB  A ASP 6   ? ? CG  A ASP 6   ? ? OD1 A ASP 6   ? ? 124.77 118.30 6.47   0.90 N
+21   1 CB  A ASP 6   ? ? CG  A ASP 6   ? ? OD2 A ASP 6   ? ? 109.51 118.30 -8.79  0.90 N
+22   1 O   A ASP 6   ? ? C   A ASP 6   ? ? N   A LYS 7   ? ? 137.51 122.70 14.81  1.60 Y
+23   1 C   A ASP 6   ? ? N   A LYS 7   ? ? CA  A LYS 7   ? ? 101.41 121.70 -20.29 2.50 Y
+24   1 N   A LYS 7   ? ? CA  A LYS 7   ? ? CB  A LYS 7   ? ? 97.04  110.60 -13.56 1.80 N
+25   1 CD  A LYS 7   ? ? CE  A LYS 7   ? ? NZ  A LYS 7   ? ? 84.29  111.70 -27.41 2.30 N
+26   1 N   A LYS 7   ? ? CA  A LYS 7   ? ? C   A LYS 7   ? ? 133.07 111.00 22.07  2.70 N
+27   1 CA  A LYS 7   ? ? C   A LYS 7   ? ? N   A THR 8   ? ? 97.12  117.20 -20.08 2.20 Y
+28   1 C   A LYS 7   ? ? N   A THR 8   ? ? CA  A THR 8   ? ? 106.03 121.70 -15.67 2.50 Y
+29   1 CA  A THR 8   ? ? CB  A THR 8   ? ? CG2 A THR 8   ? ? 101.71 112.40 -10.69 1.40 N
+30   1 CA  A THR 8   ? ? C   A THR 8   ? ? O   A THR 8   ? ? 141.42 120.10 21.32  2.10 N
+31   1 O   A VAL 10  ? ? C   A VAL 10  ? ? N   A LYS 11  ? ? 134.13 122.70 11.43  1.60 Y
+32   1 C   A LYS 11  ? ? N   A ALA 12  ? ? CA  A ALA 12  ? ? 98.80  121.70 -22.90 2.50 Y
+33   1 CB  A ALA 12  ? ? CA  A ALA 12  ? ? C   A ALA 12  ? ? 80.66  110.10 -29.44 1.50 N
+34   1 N   A ALA 12  ? ? CA  A ALA 12  ? ? CB  A ALA 12  ? ? 95.63  110.10 -14.47 1.40 N
+35   1 O   A ALA 12  ? ? C   A ALA 12  ? ? N   A ALA 13  ? ? 96.83  122.70 -25.87 1.60 Y
+36   1 O   A ALA 13  ? ? C   A ALA 13  ? ? N   A TRP 14  ? ? 136.29 122.70 13.59  1.60 Y
+37   1 CA  A TRP 14  ? ? CB  A TRP 14  ? ? CG  A TRP 14  ? ? 91.35  113.70 -22.35 1.90 N
+38   1 CG  A TRP 14  ? ? CD1 A TRP 14  ? ? NE1 A TRP 14  ? ? 96.55  110.10 -13.55 1.00 N
+39   1 CD1 A TRP 14  ? ? NE1 A TRP 14  ? ? CE2 A TRP 14  ? ? 128.82 109.00 19.82  0.90 N
+40   1 NE1 A TRP 14  ? ? CE2 A TRP 14  ? ? CZ2 A TRP 14  ? ? 141.59 130.40 11.19  1.10 N
+41   1 CH2 A TRP 14  ? ? CZ2 A TRP 14  ? ? CE2 A TRP 14  ? ? 130.63 117.40 13.23  1.00 N
+42   1 C   A TRP 14  ? ? N   A GLY 15  ? ? CA  A GLY 15  ? ? 103.27 122.30 -19.03 2.10 Y
+43   1 N   A GLY 15  ? ? CA  A GLY 15  ? ? C   A GLY 15  ? ? 88.81  113.10 -24.29 2.50 N
+44   1 CA  A GLY 15  ? ? C   A GLY 15  ? ? O   A GLY 15  ? ? 99.03  120.60 -21.57 1.80 N
+45   1 CA  A GLY 15  ? ? C   A GLY 15  ? ? N   A LYS 16  ? ? 142.77 117.20 25.57  2.20 Y
+46   1 O   A GLY 15  ? ? C   A GLY 15  ? ? N   A LYS 16  ? ? 112.77 122.70 -9.93  1.60 Y
+47   1 C   A GLY 15  ? ? N   A LYS 16  ? ? CA  A LYS 16  ? ? 136.70 121.70 15.00  2.50 Y
+48   1 N   A LYS 16  ? ? CA  A LYS 16  ? ? CB  A LYS 16  ? ? 125.33 110.60 14.73  1.80 N
+49   1 CG  A LYS 16  ? ? CD  A LYS 16  ? ? CE  A LYS 16  ? ? 63.33  111.90 -48.57 3.00 N
+50   1 CD  A LYS 16  ? ? CE  A LYS 16  ? ? NZ  A LYS 16  ? ? 129.57 111.70 17.87  2.30 N
+51   1 N   A VAL 17  ? ? CA  A VAL 17  ? ? CB  A VAL 17  ? ? 126.79 111.50 15.29  2.20 N
+52   1 CA  A VAL 17  ? ? CB  A VAL 17  ? ? CG2 A VAL 17  ? ? 121.53 110.90 10.63  1.50 N
+53   1 CA  A VAL 17  ? ? C   A VAL 17  ? ? N   A GLY 18  ? ? 83.62  116.20 -32.58 2.00 Y
+54   1 O   A VAL 17  ? ? C   A VAL 17  ? ? N   A GLY 18  ? ? 153.75 123.20 30.55  1.70 Y
+55   1 C   A VAL 17  ? ? N   A GLY 18  ? ? CA  A GLY 18  ? ? 106.28 122.30 -16.02 2.10 Y
+56   1 CA  A GLY 18  ? ? C   A GLY 18  ? ? O   A GLY 18  ? ? 108.27 120.60 -12.33 1.80 N
+57   1 CA  A GLY 18  ? ? C   A GLY 18  ? ? N   A ALA 19  ? ? 103.88 117.20 -13.32 2.20 Y
+58   1 O   A GLY 18  ? ? C   A GLY 18  ? ? N   A ALA 19  ? ? 147.81 122.70 25.11  1.60 Y
+59   1 CB  A ALA 19  ? ? CA  A ALA 19  ? ? C   A ALA 19  ? ? 96.05  110.10 -14.05 1.50 N
+60   1 N   A ALA 19  ? ? CA  A ALA 19  ? ? CB  A ALA 19  ? ? 126.43 110.10 16.33  1.40 N
+61   1 N   A ALA 19  ? ? CA  A ALA 19  ? ? C   A ALA 19  ? ? 89.91  111.00 -21.09 2.70 N
+62   1 O   A ALA 19  ? ? C   A ALA 19  ? ? N   A HIS 20  ? ? 108.05 122.70 -14.65 1.60 Y
+63   1 CB  A HIS 20  ? ? CG  A HIS 20  ? ? CD2 A HIS 20  ? ? 117.48 129.70 -12.22 1.60 N
+64   1 CG  A HIS 20  ? ? ND1 A HIS 20  ? ? CE1 A HIS 20  ? ? 90.13  105.70 -15.57 1.30 N
+65   1 ND1 A HIS 20  ? ? CE1 A HIS 20  ? ? NE2 A HIS 20  ? ? 133.08 111.50 21.58  1.30 N
+66   1 CG  A HIS 20  ? ? CD2 A HIS 20  ? ? NE2 A HIS 20  ? ? 94.55  106.70 -12.15 1.20 N
+67   1 CB  A ALA 21  ? ? CA  A ALA 21  ? ? C   A ALA 21  ? ? 130.13 110.10 20.03  1.50 N
+68   1 N   A ALA 21  ? ? CA  A ALA 21  ? ? CB  A ALA 21  ? ? 121.00 110.10 10.90  1.40 N
+69   1 CA  A ALA 21  ? ? C   A ALA 21  ? ? O   A ALA 21  ? ? 95.52  120.10 -24.58 2.10 N
+70   1 CA  A ALA 21  ? ? C   A ALA 21  ? ? N   A GLY 22  ? ? 88.39  116.20 -27.81 2.00 Y
+71   1 C   A ALA 21  ? ? N   A GLY 22  ? ? CA  A GLY 22  ? ? 93.47  122.30 -28.83 2.10 Y
+72   1 N   A GLY 22  ? ? CA  A GLY 22  ? ? C   A GLY 22  ? ? 128.82 113.10 15.72  2.50 N
+73   1 CA  A GLY 22  ? ? C   A GLY 22  ? ? O   A GLY 22  ? ? 139.31 120.60 18.71  1.80 N
+74   1 O   A GLY 22  ? ? C   A GLY 22  ? ? N   A GLU 23  ? ? 94.63  122.70 -28.07 1.60 Y
+75   1 N   A GLU 23  ? ? CA  A GLU 23  ? ? CB  A GLU 23  ? ? 97.75  110.60 -12.85 1.80 N
+76   1 CG  A GLU 23  ? ? CD  A GLU 23  ? ? OE1 A GLU 23  ? ? 84.19  118.30 -34.11 2.00 N
+77   1 CG  A GLU 23  ? ? CD  A GLU 23  ? ? OE2 A GLU 23  ? ? 105.30 118.30 -13.00 2.00 N
+78   1 CA  A TYR 24  ? ? CB  A TYR 24  ? ? CG  A TYR 24  ? ? 100.84 113.40 -12.56 1.90 N
+79   1 CB  A TYR 24  ? ? CG  A TYR 24  ? ? CD1 A TYR 24  ? ? 117.27 121.00 -3.73  0.60 N
+80   1 CG  A TYR 24  ? ? CD1 A TYR 24  ? ? CE1 A TYR 24  ? ? 114.94 121.30 -6.36  0.80 N
+81   1 CG  A TYR 24  ? ? CD2 A TYR 24  ? ? CE2 A TYR 24  ? ? 128.73 121.30 7.43   0.80 N
+82   1 CD1 A TYR 24  ? ? CE1 A TYR 24  ? ? CZ  A TYR 24  ? ? 130.55 119.80 10.75  0.90 N
+83   1 CZ  A TYR 24  ? ? CE2 A TYR 24  ? ? CD2 A TYR 24  ? ? 108.52 119.80 -11.28 0.90 N
+84   1 O   A GLY 25  ? ? C   A GLY 25  ? ? N   A ALA 26  ? ? 104.87 122.70 -17.83 1.60 Y
+85   1 CB  A ALA 26  ? ? CA  A ALA 26  ? ? C   A ALA 26  ? ? 93.76  110.10 -16.34 1.50 N
+86   1 N   A ALA 26  ? ? CA  A ALA 26  ? ? CB  A ALA 26  ? ? 126.67 110.10 16.57  1.40 N
+87   1 CA  A ALA 26  ? ? C   A ALA 26  ? ? O   A ALA 26  ? ? 141.83 120.10 21.73  2.10 N
+88   1 O   A ALA 26  ? ? C   A ALA 26  ? ? N   A GLU 27  ? ? 113.10 122.70 -9.60  1.60 Y
+89   1 OE1 A GLU 27  ? ? CD  A GLU 27  ? ? OE2 A GLU 27  ? ? 132.66 123.30 9.36   1.20 N
+90   1 CA  A ALA 28  ? ? C   A ALA 28  ? ? N   A LEU 29  ? ? 100.99 117.20 -16.21 2.20 Y
+91   1 C   A ALA 28  ? ? N   A LEU 29  ? ? CA  A LEU 29  ? ? 106.27 121.70 -15.43 2.50 Y
+92   1 CB  A LEU 29  ? ? CG  A LEU 29  ? ? CD1 A LEU 29  ? ? 95.54  111.00 -15.46 1.70 N
+93   1 OE1 A GLU 30  ? ? CD  A GLU 30  ? ? OE2 A GLU 30  ? ? 144.27 123.30 20.97  1.20 N
+94   1 CG  A GLU 30  ? ? CD  A GLU 30  ? ? OE2 A GLU 30  ? ? 105.72 118.30 -12.58 2.00 N
+95   1 NE  A ARG 31  ? ? CZ  A ARG 31  ? ? NH1 A ARG 31  ? ? 128.95 120.30 8.65   0.50 N
+96   1 NE  A ARG 31  ? ? CZ  A ARG 31  ? ? NH2 A ARG 31  ? ? 107.66 120.30 -12.64 0.50 N
+97   1 O   A ARG 31  ? ? C   A ARG 31  ? ? N   A MET 32  ? ? 133.59 122.70 10.89  1.60 Y
+98   1 CB  A PHE 33  ? ? CG  A PHE 33  ? ? CD2 A PHE 33  ? ? 110.09 120.80 -10.71 0.70 N
+99   1 CB  A PHE 33  ? ? CG  A PHE 33  ? ? CD1 A PHE 33  ? ? 132.73 120.80 11.93  0.70 N
+100  1 CG  A PHE 33  ? ? CD1 A PHE 33  ? ? CE1 A PHE 33  ? ? 129.69 120.80 8.89   1.10 N
+101  1 CG  A PHE 33  ? ? CD2 A PHE 33  ? ? CE2 A PHE 33  ? ? 105.74 120.80 -15.06 1.10 N
+102  1 CD1 A PHE 33  ? ? CE1 A PHE 33  ? ? CZ  A PHE 33  ? ? 112.16 120.10 -7.94  1.20 N
+103  1 CZ  A PHE 33  ? ? CE2 A PHE 33  ? ? CD2 A PHE 33  ? ? 131.72 120.10 11.62  1.20 N
+104  1 CA  A PHE 33  ? ? C   A PHE 33  ? ? O   A PHE 33  ? ? 133.41 120.10 13.31  2.10 N
+105  1 CB  A LEU 34  ? ? CG  A LEU 34  ? ? CD1 A LEU 34  ? ? 131.84 111.00 20.84  1.70 N
+106  1 CB  A PHE 36  ? ? CG  A PHE 36  ? ? CD2 A PHE 36  ? ? 112.08 120.80 -8.72  0.70 N
+107  1 O   A PHE 36  ? ? C   A PHE 36  ? ? N   A PRO 37  ? ? 133.36 121.10 12.26  1.90 Y
+108  1 C   A PHE 36  ? ? N   A PRO 37  ? ? CA  A PRO 37  ? ? 107.91 119.30 -11.39 1.50 Y
+109  1 CA  A THR 38  ? ? CB  A THR 38  ? ? CG2 A THR 38  ? ? 99.79  112.40 -12.61 1.40 N
+110  1 O   A THR 39  ? ? C   A THR 39  ? ? N   A LYS 40  ? ? 133.86 122.70 11.16  1.60 Y
+111  1 O   A THR 41  ? ? C   A THR 41  ? ? N   A TYR 42  ? ? 105.91 122.70 -16.79 1.60 Y
+112  1 CA  A TYR 42  ? ? CB  A TYR 42  ? ? CG  A TYR 42  ? ? 99.92  113.40 -13.48 1.90 N
+113  1 CB  A TYR 42  ? ? CG  A TYR 42  ? ? CD2 A TYR 42  ? ? 116.18 121.00 -4.82  0.60 N
+114  1 CB  A TYR 42  ? ? CG  A TYR 42  ? ? CD1 A TYR 42  ? ? 127.46 121.00 6.46   0.60 N
+115  1 CG  A TYR 42  ? ? CD1 A TYR 42  ? ? CE1 A TYR 42  ? ? 113.73 121.30 -7.57  0.80 N
+116  1 CD1 A TYR 42  ? ? CE1 A TYR 42  ? ? CZ  A TYR 42  ? ? 130.60 119.80 10.80  0.90 N
+117  1 CB  A PHE 43  ? ? CG  A PHE 43  ? ? CD2 A PHE 43  ? ? 131.75 120.80 10.95  0.70 N
+118  1 CB  A PHE 43  ? ? CG  A PHE 43  ? ? CD1 A PHE 43  ? ? 113.99 120.80 -6.81  0.70 N
+119  1 CG  A PHE 43  ? ? CD1 A PHE 43  ? ? CE1 A PHE 43  ? ? 113.29 120.80 -7.51  1.10 N
+120  1 CG  A PHE 43  ? ? CD2 A PHE 43  ? ? CE2 A PHE 43  ? ? 132.26 120.80 11.46  1.10 N
+121  1 CD1 A PHE 43  ? ? CE1 A PHE 43  ? ? CZ  A PHE 43  ? ? 131.07 120.10 10.97  1.20 N
+122  1 CZ  A PHE 43  ? ? CE2 A PHE 43  ? ? CD2 A PHE 43  ? ? 107.75 120.10 -12.35 1.20 N
+123  1 CA  A HIS 45  ? ? CB  A HIS 45  ? ? CG  A HIS 45  ? ? 132.23 113.60 18.63  1.70 N
+124  1 CB  A HIS 45  ? ? CG  A HIS 45  ? ? ND1 A HIS 45  ? ? 108.15 121.40 -13.25 1.30 N
+125  1 CB  A PHE 46  ? ? CG  A PHE 46  ? ? CD2 A PHE 46  ? ? 136.54 120.80 15.74  0.70 N
+126  1 CD1 A PHE 46  ? ? CG  A PHE 46  ? ? CD2 A PHE 46  ? ? 101.88 118.30 -16.42 1.30 N
+127  1 CG  A PHE 46  ? ? CD2 A PHE 46  ? ? CE2 A PHE 46  ? ? 136.70 120.80 15.90  1.10 N
+128  1 CD1 A PHE 46  ? ? CE1 A PHE 46  ? ? CZ  A PHE 46  ? ? 127.92 120.10 7.82   1.20 N
+129  1 CE1 A PHE 46  ? ? CZ  A PHE 46  ? ? CE2 A PHE 46  ? ? 100.12 120.00 -19.88 1.80 N
+130  1 CB  A ASP 47  ? ? CG  A ASP 47  ? ? OD1 A ASP 47  ? ? 130.99 118.30 12.69  0.90 N
+131  1 CB  A ASP 47  ? ? CG  A ASP 47  ? ? OD2 A ASP 47  ? ? 96.21  118.30 -22.09 0.90 N
+132  1 O   A ASP 47  ? ? C   A ASP 47  ? ? N   A LEU 48  ? ? 141.53 122.70 18.83  1.60 Y
+133  1 CB  A LEU 48  ? ? CG  A LEU 48  ? ? CD1 A LEU 48  ? ? 98.01  111.00 -12.99 1.70 N
+134  1 CB  A LEU 48  ? ? CG  A LEU 48  ? ? CD2 A LEU 48  ? ? 132.62 111.00 21.62  1.70 N
+135  1 CB  A SER 49  ? ? CA  A SER 49  ? ? C   A SER 49  ? ? 143.95 110.10 33.85  1.90 N
+136  1 CA  A SER 49  ? ? C   A SER 49  ? ? O   A SER 49  ? ? 134.97 120.10 14.87  2.10 N
+137  1 C   A SER 49  ? ? N   A HIS 50  ? ? CA  A HIS 50  ? ? 94.82  121.70 -26.88 2.50 Y
+138  1 CB  A HIS 50  ? ? CA  A HIS 50  ? ? C   A HIS 50  ? ? 90.66  110.40 -19.74 2.00 N
+139  1 N   A HIS 50  ? ? CA  A HIS 50  ? ? CB  A HIS 50  ? ? 85.29  110.60 -25.31 1.80 N
+140  1 CB  A HIS 50  ? ? CG  A HIS 50  ? ? CD2 A HIS 50  ? ? 116.43 129.70 -13.27 1.60 N
+141  1 ND1 A HIS 50  ? ? CG  A HIS 50  ? ? CD2 A HIS 50  ? ? 96.84  106.00 -9.16  1.40 N
+142  1 ND1 A HIS 50  ? ? CE1 A HIS 50  ? ? NE2 A HIS 50  ? ? 101.55 108.50 -6.95  1.10 N
+143  1 CE1 A HIS 50  ? ? NE2 A HIS 50  ? ? CD2 A HIS 50  ? ? 113.53 109.00 4.53   0.70 N
+144  1 CG  A HIS 50  ? ? CD2 A HIS 50  ? ? NE2 A HIS 50  ? ? 92.62  106.70 -14.08 1.20 N
+145  1 CA  A HIS 50  ? ? C   A HIS 50  ? ? N   A GLY 51  ? ? 133.49 116.20 17.29  2.00 Y
+146  1 O   A HIS 50  ? ? C   A HIS 50  ? ? N   A GLY 51  ? ? 111.26 123.20 -11.94 1.70 Y
+147  1 C   A HIS 50  ? ? N   A GLY 51  ? ? CA  A GLY 51  ? ? 150.51 122.30 28.21  2.10 Y
+148  1 O   A GLY 51  ? ? C   A GLY 51  ? ? N   A SER 52  ? ? 134.96 122.70 12.26  1.60 Y
+149  1 C   A GLY 51  ? ? N   A SER 52  ? ? CA  A SER 52  ? ? 105.55 121.70 -16.15 2.50 Y
+150  1 CB  A SER 52  ? ? CA  A SER 52  ? ? C   A SER 52  ? ? 125.30 110.10 15.20  1.90 N
+151  1 CA  A SER 52  ? ? C   A SER 52  ? ? O   A SER 52  ? ? 136.93 120.10 16.83  2.10 N
+152  1 O   A SER 52  ? ? C   A SER 52  ? ? N   A ALA 53  ? ? 107.83 122.70 -14.87 1.60 Y
+153  1 CB  A ALA 53  ? ? CA  A ALA 53  ? ? C   A ALA 53  ? ? 95.09  110.10 -15.01 1.50 N
+154  1 O   A GLN 54  ? ? C   A GLN 54  ? ? N   A VAL 55  ? ? 136.03 122.70 13.33  1.60 Y
+155  1 CB  A LYS 56  ? ? CA  A LYS 56  ? ? C   A LYS 56  ? ? 122.43 110.40 12.03  2.00 N
+156  1 CB  A LYS 56  ? ? CG  A LYS 56  ? ? CD  A LYS 56  ? ? 87.40  111.60 -24.20 2.60 N
+157  1 CD  A LYS 56  ? ? CE  A LYS 56  ? ? NZ  A LYS 56  ? ? 94.04  111.70 -17.66 2.30 N
+158  1 CA  A LYS 56  ? ? C   A LYS 56  ? ? O   A LYS 56  ? ? 138.73 120.10 18.63  2.10 N
+159  1 CA  A LYS 56  ? ? C   A LYS 56  ? ? N   A GLY 57  ? ? 103.67 116.20 -12.53 2.00 Y
+160  1 O   A LYS 56  ? ? C   A LYS 56  ? ? N   A GLY 57  ? ? 108.49 123.20 -14.71 1.70 Y
+161  1 O   A GLY 57  ? ? C   A GLY 57  ? ? N   A HIS 58  ? ? 140.56 122.70 17.86  1.60 Y
+162  1 CA  A HIS 58  ? ? CB  A HIS 58  ? ? CG  A HIS 58  ? ? 101.73 113.60 -11.87 1.70 N
+163  1 CG  A HIS 58  ? ? ND1 A HIS 58  ? ? CE1 A HIS 58  ? ? 97.75  105.70 -7.95  1.30 N
+164  1 CA  A HIS 58  ? ? C   A HIS 58  ? ? N   A GLY 59  ? ? 104.10 116.20 -12.10 2.00 Y
+165  1 O   A HIS 58  ? ? C   A HIS 58  ? ? N   A GLY 59  ? ? 146.41 123.20 23.21  1.70 Y
+166  1 C   A HIS 58  ? ? N   A GLY 59  ? ? CA  A GLY 59  ? ? 104.96 122.30 -17.34 2.10 Y
+167  1 O   A GLY 59  ? ? C   A GLY 59  ? ? N   A LYS 60  ? ? 109.99 122.70 -12.71 1.60 Y
+168  1 CD  A LYS 60  ? ? CE  A LYS 60  ? ? NZ  A LYS 60  ? ? 73.74  111.70 -37.96 2.30 N
+169  1 CA  A LYS 60  ? ? C   A LYS 60  ? ? O   A LYS 60  ? ? 137.78 120.10 17.68  2.10 N
+170  1 CA  A LYS 60  ? ? C   A LYS 60  ? ? N   A LYS 61  ? ? 102.05 117.20 -15.15 2.20 Y
+171  1 CB  A LYS 61  ? ? CA  A LYS 61  ? ? C   A LYS 61  ? ? 95.46  110.40 -14.94 2.00 N
+172  1 CD  A LYS 61  ? ? CE  A LYS 61  ? ? NZ  A LYS 61  ? ? 128.54 111.70 16.84  2.30 N
+173  1 CA  A LYS 61  ? ? C   A LYS 61  ? ? N   A VAL 62  ? ? 101.97 117.20 -15.23 2.20 Y
+174  1 O   A LYS 61  ? ? C   A LYS 61  ? ? N   A VAL 62  ? ? 143.19 122.70 20.49  1.60 Y
+175  1 C   A LYS 61  ? ? N   A VAL 62  ? ? CA  A VAL 62  ? ? 104.91 121.70 -16.79 2.50 Y
+176  1 CG1 A VAL 62  ? ? CB  A VAL 62  ? ? CG2 A VAL 62  ? ? 96.57  110.90 -14.33 1.60 N
+177  1 CA  A VAL 62  ? ? C   A VAL 62  ? ? N   A ALA 63  ? ? 97.82  117.20 -19.38 2.20 Y
+178  1 O   A VAL 62  ? ? C   A VAL 62  ? ? N   A ALA 63  ? ? 145.12 122.70 22.42  1.60 Y
+179  1 C   A VAL 62  ? ? N   A ALA 63  ? ? CA  A ALA 63  ? ? 100.66 121.70 -21.04 2.50 Y
+180  1 N   A ALA 63  ? ? CA  A ALA 63  ? ? CB  A ALA 63  ? ? 99.07  110.10 -11.03 1.40 N
+181  1 O   A ALA 63  ? ? C   A ALA 63  ? ? N   A ASP 64  ? ? 109.24 122.70 -13.46 1.60 Y
+182  1 CB  A ASP 64  ? ? CA  A ASP 64  ? ? C   A ASP 64  ? ? 97.78  110.40 -12.62 2.00 N
+183  1 OD1 A ASP 64  ? ? CG  A ASP 64  ? ? OD2 A ASP 64  ? ? 145.02 123.30 21.72  1.90 N
+184  1 CB  A ASP 64  ? ? CG  A ASP 64  ? ? OD1 A ASP 64  ? ? 97.44  118.30 -20.86 0.90 N
+185  1 CB  A ASP 64  ? ? CG  A ASP 64  ? ? OD2 A ASP 64  ? ? 99.49  118.30 -18.81 0.90 N
+186  1 N   A ASP 64  ? ? CA  A ASP 64  ? ? C   A ASP 64  ? ? 127.85 111.00 16.85  2.70 N
+187  1 O   A ALA 65  ? ? C   A ALA 65  ? ? N   A LEU 66  ? ? 142.44 122.70 19.74  1.60 Y
+188  1 C   A ALA 65  ? ? N   A LEU 66  ? ? CA  A LEU 66  ? ? 103.39 121.70 -18.31 2.50 Y
+189  1 O   A ASN 68  ? ? C   A ASN 68  ? ? N   A ALA 69  ? ? 111.89 122.70 -10.81 1.60 Y
+190  1 N   A ALA 69  ? ? CA  A ALA 69  ? ? CB  A ALA 69  ? ? 99.34  110.10 -10.76 1.40 N
+191  1 CG1 A VAL 70  ? ? CB  A VAL 70  ? ? CG2 A VAL 70  ? ? 97.88  110.90 -13.02 1.60 N
+192  1 CA  A VAL 70  ? ? CB  A VAL 70  ? ? CG1 A VAL 70  ? ? 122.96 110.90 12.06  1.50 N
+193  1 CB  A ALA 71  ? ? CA  A ALA 71  ? ? C   A ALA 71  ? ? 119.91 110.10 9.81   1.50 N
+194  1 CA  A ALA 71  ? ? C   A ALA 71  ? ? N   A HIS 72  ? ? 141.47 117.20 24.27  2.20 Y
+195  1 O   A ALA 71  ? ? C   A ALA 71  ? ? N   A HIS 72  ? ? 109.30 122.70 -13.40 1.60 Y
+196  1 CA  A HIS 72  ? ? CB  A HIS 72  ? ? CG  A HIS 72  ? ? 85.01  113.60 -28.59 1.70 N
+197  1 CB  A HIS 72  ? ? CG  A HIS 72  ? ? CD2 A HIS 72  ? ? 143.44 131.40 12.04  1.20 N
+198  1 ND1 A HIS 72  ? ? CG  A HIS 72  ? ? CD2 A HIS 72  ? ? 72.06  106.00 -33.94 1.40 N
+199  1 ND1 A HIS 72  ? ? CE1 A HIS 72  ? ? NE2 A HIS 72  ? ? 95.78  108.50 -12.72 1.10 N
+200  1 CG  A HIS 72  ? ? CD2 A HIS 72  ? ? NE2 A HIS 72  ? ? 128.83 109.20 19.63  1.90 N
+201  1 O   A HIS 72  ? ? C   A HIS 72  ? ? N   A VAL 73  ? ? 109.61 122.70 -13.09 1.60 Y
+202  1 CA  A VAL 73  ? ? CB  A VAL 73  ? ? CG1 A VAL 73  ? ? 121.16 110.90 10.26  1.50 N
+203  1 CA  A VAL 73  ? ? C   A VAL 73  ? ? O   A VAL 73  ? ? 143.39 120.10 23.29  2.10 N
+204  1 O   A VAL 73  ? ? C   A VAL 73  ? ? N   A ASP 74  ? ? 104.09 122.70 -18.61 1.60 Y
+205  1 OD1 A ASP 74  ? ? CG  A ASP 74  ? ? OD2 A ASP 74  ? ? 111.26 123.30 -12.04 1.90 N
+206  1 CB  A ASP 74  ? ? CG  A ASP 74  ? ? OD1 A ASP 74  ? ? 127.38 118.30 9.08   0.90 N
+207  1 CA  A ASP 74  ? ? C   A ASP 74  ? ? O   A ASP 74  ? ? 96.46  120.10 -23.64 2.10 N
+208  1 CA  A ASP 74  ? ? C   A ASP 74  ? ? N   A ASP 75  ? ? 145.16 117.20 27.96  2.20 Y
+209  1 CB  A ASP 75  ? ? CA  A ASP 75  ? ? C   A ASP 75  ? ? 85.88  110.40 -24.52 2.00 N
+210  1 N   A ASP 75  ? ? CA  A ASP 75  ? ? CB  A ASP 75  ? ? 95.66  110.60 -14.94 1.80 N
+211  1 CA  A ASP 75  ? ? CB  A ASP 75  ? ? CG  A ASP 75  ? ? 72.53  113.40 -40.87 2.20 N
+212  1 OD1 A ASP 75  ? ? CG  A ASP 75  ? ? OD2 A ASP 75  ? ? 73.99  123.30 -49.31 1.90 N
+213  1 CB  A ASP 75  ? ? CG  A ASP 75  ? ? OD1 A ASP 75  ? ? 152.77 118.30 34.47  0.90 N
+214  1 CB  A ASP 75  ? ? CG  A ASP 75  ? ? OD2 A ASP 75  ? ? 78.85  118.30 -39.45 0.90 N
+215  1 CA  A ASP 75  ? ? C   A ASP 75  ? ? N   A MET 76  ? ? 100.32 117.20 -16.88 2.20 Y
+216  1 C   A ASP 75  ? ? N   A MET 76  ? ? CA  A MET 76  ? ? 106.26 121.70 -15.44 2.50 Y
+217  1 N   A MET 76  ? ? CA  A MET 76  ? ? CB  A MET 76  ? ? 99.04  110.60 -11.56 1.80 N
+218  1 CA  A MET 76  ? ? CB  A MET 76  ? ? CG  A MET 76  ? ? 97.04  113.30 -16.26 1.70 N
+219  1 CG  A MET 76  ? ? SD  A MET 76  ? ? CE  A MET 76  ? ? 116.04 100.20 15.84  1.60 N
+220  1 N   A PRO 77  ? ? CA  A PRO 77  ? ? CB  A PRO 77  ? ? 111.15 103.30 7.85   1.20 N
+221  1 CA  A PRO 77  ? ? CB  A PRO 77  ? ? CG  A PRO 77  ? ? 88.11  104.80 -16.69 1.90 N
+222  1 O   A PRO 77  ? ? C   A PRO 77  ? ? N   A ASN 78  ? ? 110.84 122.70 -11.86 1.60 Y
+223  1 N   A ASN 78  ? ? CA  A ASN 78  ? ? CB  A ASN 78  ? ? 127.92 110.60 17.32  1.80 N
+224  1 OD1 A ASN 78  ? ? CG  A ASN 78  ? ? ND2 A ASN 78  ? ? 84.96  121.90 -36.94 2.30 N
+225  1 CB  A ASN 78  ? ? CG  A ASN 78  ? ? ND2 A ASN 78  ? ? 138.16 116.70 21.46  2.40 N
+226  1 O   A ASN 78  ? ? C   A ASN 78  ? ? N   A ALA 79  ? ? 112.16 122.70 -10.54 1.60 Y
+227  1 O   A ALA 79  ? ? C   A ALA 79  ? ? N   A LEU 80  ? ? 132.47 122.70 9.77   1.60 Y
+228  1 N   A SER 81  ? ? CA  A SER 81  ? ? CB  A SER 81  ? ? 87.80  110.50 -22.70 1.50 N
+229  1 CA  A SER 81  ? ? CB  A SER 81  ? ? OG  A SER 81  ? ? 83.40  111.20 -27.80 2.70 N
+230  1 CA  A SER 81  ? ? C   A SER 81  ? ? N   A ALA 82  ? ? 132.46 117.20 15.26  2.20 Y
+231  1 O   A SER 81  ? ? C   A SER 81  ? ? N   A ALA 82  ? ? 110.03 122.70 -12.67 1.60 Y
+232  1 C   A SER 81  ? ? N   A ALA 82  ? ? CA  A ALA 82  ? ? 138.09 121.70 16.39  2.50 Y
+233  1 N   A ALA 82  ? ? CA  A ALA 82  ? ? CB  A ALA 82  ? ? 123.81 110.10 13.71  1.40 N
+234  1 CB  A LEU 83  ? ? CA  A LEU 83  ? ? C   A LEU 83  ? ? 97.76  110.20 -12.44 1.90 N
+235  1 CD1 A LEU 83  ? ? CG  A LEU 83  ? ? CD2 A LEU 83  ? ? 89.11  110.50 -21.39 3.00 N
+236  1 CB  A LEU 83  ? ? CG  A LEU 83  ? ? CD2 A LEU 83  ? ? 121.29 111.00 10.29  1.70 N
+237  1 O   A LEU 83  ? ? C   A LEU 83  ? ? N   A SER 84  ? ? 112.73 122.70 -9.97  1.60 Y
+238  1 CB  A SER 84  ? ? CA  A SER 84  ? ? C   A SER 84  ? ? 97.62  110.10 -12.48 1.90 N
+239  1 N   A SER 84  ? ? CA  A SER 84  ? ? CB  A SER 84  ? ? 120.23 110.50 9.73   1.50 N
+240  1 O   A SER 84  ? ? C   A SER 84  ? ? N   A ASP 85  ? ? 134.69 122.70 11.99  1.60 Y
+241  1 CA  A ASP 85  ? ? CB  A ASP 85  ? ? CG  A ASP 85  ? ? 100.18 113.40 -13.22 2.20 N
+242  1 OD1 A ASP 85  ? ? CG  A ASP 85  ? ? OD2 A ASP 85  ? ? 109.10 123.30 -14.20 1.90 N
+243  1 CB  A ASP 85  ? ? CG  A ASP 85  ? ? OD1 A ASP 85  ? ? 134.46 118.30 16.16  0.90 N
+244  1 CB  A ASP 85  ? ? CG  A ASP 85  ? ? OD2 A ASP 85  ? ? 105.45 118.30 -12.85 0.90 N
+245  1 CD1 A LEU 86  ? ? CG  A LEU 86  ? ? CD2 A LEU 86  ? ? 91.73  110.50 -18.77 3.00 N
+246  1 CB  A LEU 86  ? ? CG  A LEU 86  ? ? CD2 A LEU 86  ? ? 126.41 111.00 15.41  1.70 N
+247  1 C   A LEU 86  ? ? N   A HIS 87  ? ? CA  A HIS 87  ? ? 105.80 121.70 -15.90 2.50 Y
+248  1 CA  A HIS 87  ? ? CB  A HIS 87  ? ? CG  A HIS 87  ? ? 101.08 113.60 -12.52 1.70 N
+249  1 CB  A HIS 87  ? ? CG  A HIS 87  ? ? CD2 A HIS 87  ? ? 142.12 131.40 10.72  1.20 N
+250  1 O   A HIS 87  ? ? C   A HIS 87  ? ? N   A ALA 88  ? ? 138.85 122.70 16.15  1.60 Y
+251  1 O   A ALA 88  ? ? C   A ALA 88  ? ? N   A HIS 89  ? ? 138.43 122.70 15.73  1.60 Y
+252  1 CG  A HIS 89  ? ? ND1 A HIS 89  ? ? CE1 A HIS 89  ? ? 124.40 109.00 15.40  1.00 N
+253  1 ND1 A HIS 89  ? ? CE1 A HIS 89  ? ? NE2 A HIS 89  ? ? 82.84  108.50 -25.66 1.10 N
+254  1 CE1 A HIS 89  ? ? NE2 A HIS 89  ? ? CD2 A HIS 89  ? ? 137.38 109.00 28.38  0.70 N
+255  1 CG  A HIS 89  ? ? CD2 A HIS 89  ? ? NE2 A HIS 89  ? ? 95.32  106.70 -11.38 1.20 N
+256  1 O   A HIS 89  ? ? C   A HIS 89  ? ? N   A LYS 90  ? ? 107.46 122.70 -15.24 1.60 Y
+257  1 C   A HIS 89  ? ? N   A LYS 90  ? ? CA  A LYS 90  ? ? 136.81 121.70 15.11  2.50 Y
+258  1 CD  A LYS 90  ? ? CE  A LYS 90  ? ? NZ  A LYS 90  ? ? 68.30  111.70 -43.40 2.30 N
+259  1 N   A LYS 90  ? ? CA  A LYS 90  ? ? C   A LYS 90  ? ? 133.43 111.00 22.43  2.70 N
+260  1 CG  A ARG 92  ? ? CD  A ARG 92  ? ? NE  A ARG 92  ? ? 46.37  111.80 -65.43 2.10 N
+261  1 CD  A ARG 92  ? ? NE  A ARG 92  ? ? CZ  A ARG 92  ? ? 50.94  123.60 -72.66 1.40 N
+262  1 NH1 A ARG 92  ? ? CZ  A ARG 92  ? ? NH2 A ARG 92  ? ? 151.84 119.40 32.44  1.10 N
+263  1 NE  A ARG 92  ? ? CZ  A ARG 92  ? ? NH1 A ARG 92  ? ? 99.86  120.30 -20.44 0.50 N
+264  1 NE  A ARG 92  ? ? CZ  A ARG 92  ? ? NH2 A ARG 92  ? ? 91.72  120.30 -28.58 0.50 N
+265  1 O   A ARG 92  ? ? C   A ARG 92  ? ? N   A VAL 93  ? ? 110.41 122.70 -12.29 1.60 Y
+266  1 O   A VAL 93  ? ? C   A VAL 93  ? ? N   A ASP 94  ? ? 110.33 122.70 -12.37 1.60 Y
+267  1 CA  A VAL 96  ? ? CB  A VAL 96  ? ? CG1 A VAL 96  ? ? 120.87 110.90 9.97   1.50 N
+268  1 CA  A VAL 96  ? ? CB  A VAL 96  ? ? CG2 A VAL 96  ? ? 96.72  110.90 -14.18 1.50 N
+269  1 CA  A VAL 96  ? ? C   A VAL 96  ? ? O   A VAL 96  ? ? 132.92 120.10 12.82  2.10 N
+270  1 CB  A PHE 98  ? ? CG  A PHE 98  ? ? CD2 A PHE 98  ? ? 126.98 120.80 6.18   0.70 N
+271  1 CB  A PHE 98  ? ? CG  A PHE 98  ? ? CD1 A PHE 98  ? ? 110.02 120.80 -10.78 0.70 N
+272  1 CZ  A PHE 98  ? ? CE2 A PHE 98  ? ? CD2 A PHE 98  ? ? 110.83 120.10 -9.27  1.20 N
+273  1 CA  A LYS 99  ? ? CB  A LYS 99  ? ? CG  A LYS 99  ? ? 126.64 113.40 13.24  2.20 N
+274  1 CB  A LYS 99  ? ? CG  A LYS 99  ? ? CD  A LYS 99  ? ? 128.01 111.60 16.41  2.60 N
+275  1 CD  A LYS 99  ? ? CE  A LYS 99  ? ? NZ  A LYS 99  ? ? 97.35  111.70 -14.35 2.30 N
+276  1 O   A LEU 101 ? ? C   A LEU 101 ? ? N   A SER 102 ? ? 110.56 122.70 -12.14 1.60 Y
+277  1 ND1 A HIS 103 ? ? CE1 A HIS 103 ? ? NE2 A HIS 103 ? ? 121.08 111.50 9.58   1.30 N
+278  1 CA  A HIS 103 ? ? C   A HIS 103 ? ? O   A HIS 103 ? ? 135.13 120.10 15.03  2.10 N
+279  1 N   A LEU 105 ? ? CA  A LEU 105 ? ? CB  A LEU 105 ? ? 96.61  110.40 -13.79 2.00 N
+280  1 CB  A LEU 105 ? ? CG  A LEU 105 ? ? CD2 A LEU 105 ? ? 127.73 111.00 16.73  1.70 N
+281  1 O   A LEU 105 ? ? C   A LEU 105 ? ? N   A LEU 106 ? ? 134.49 122.70 11.79  1.60 Y
+282  1 CA  A LEU 106 ? ? CB  A LEU 106 ? ? CG  A LEU 106 ? ? 138.70 115.30 23.40  2.30 N
+283  1 CB  A LEU 106 ? ? CG  A LEU 106 ? ? CD1 A LEU 106 ? ? 125.77 111.00 14.77  1.70 N
+284  1 O   A LEU 106 ? ? C   A LEU 106 ? ? N   A VAL 107 ? ? 110.17 122.70 -12.53 1.60 Y
+285  1 CA  A THR 108 ? ? CB  A THR 108 ? ? CG2 A THR 108 ? ? 101.71 112.40 -10.69 1.40 N
+286  1 CD1 A LEU 109 ? ? CG  A LEU 109 ? ? CD2 A LEU 109 ? ? 128.56 110.50 18.06  3.00 N
+287  1 CA  A ALA 110 ? ? C   A ALA 110 ? ? O   A ALA 110 ? ? 136.69 120.10 16.59  2.10 N
+288  1 O   A ALA 110 ? ? C   A ALA 110 ? ? N   A ALA 111 ? ? 101.65 122.70 -21.05 1.60 Y
+289  1 C   A ALA 110 ? ? N   A ALA 111 ? ? CA  A ALA 111 ? ? 141.29 121.70 19.59  2.50 Y
+290  1 N   A ALA 111 ? ? CA  A ALA 111 ? ? CB  A ALA 111 ? ? 127.41 110.10 17.31  1.40 N
+291  1 CB  A HIS 112 ? ? CG  A HIS 112 ? ? ND1 A HIS 112 ? ? 107.53 121.40 -13.87 1.30 N
+292  1 CG  A HIS 112 ? ? ND1 A HIS 112 ? ? CE1 A HIS 112 ? ? 90.50  105.70 -15.20 1.30 N
+293  1 ND1 A HIS 112 ? ? CE1 A HIS 112 ? ? NE2 A HIS 112 ? ? 120.27 111.50 8.77   1.30 N
+294  1 CA  A HIS 112 ? ? C   A HIS 112 ? ? O   A HIS 112 ? ? 101.39 120.10 -18.71 2.10 N
+295  1 CB  A LEU 113 ? ? CG  A LEU 113 ? ? CD1 A LEU 113 ? ? 122.54 111.00 11.54  1.70 N
+296  1 N   A PRO 114 ? ? CA  A PRO 114 ? ? CB  A PRO 114 ? ? 93.55  103.30 -9.75  1.20 N
+297  1 CA  A PRO 114 ? ? CB  A PRO 114 ? ? CG  A PRO 114 ? ? 120.21 104.80 15.41  1.90 N
+298  1 OE1 A GLU 116 ? ? CD  A GLU 116 ? ? OE2 A GLU 116 ? ? 106.08 123.30 -17.22 1.20 N
+299  1 CG  A GLU 116 ? ? CD  A GLU 116 ? ? OE1 A GLU 116 ? ? 139.76 118.30 21.46  2.00 N
+300  1 CB  A PHE 117 ? ? CG  A PHE 117 ? ? CD2 A PHE 117 ? ? 115.04 120.80 -5.76  0.70 N
+301  1 CD1 A PHE 117 ? ? CG  A PHE 117 ? ? CD2 A PHE 117 ? ? 129.01 118.30 10.71  1.30 N
+302  1 CB  A PHE 117 ? ? CG  A PHE 117 ? ? CD1 A PHE 117 ? ? 115.33 120.80 -5.47  0.70 N
+303  1 CG  A PHE 117 ? ? CD1 A PHE 117 ? ? CE1 A PHE 117 ? ? 111.87 120.80 -8.93  1.10 N
+304  1 CZ  A PHE 117 ? ? CE2 A PHE 117 ? ? CD2 A PHE 117 ? ? 112.72 120.10 -7.38  1.20 N
+305  1 CA  A THR 118 ? ? CB  A THR 118 ? ? OG1 A THR 118 ? ? 127.94 109.00 18.94  2.10 N
+306  1 N   A ALA 120 ? ? CA  A ALA 120 ? ? CB  A ALA 120 ? ? 125.66 110.10 15.56  1.40 N
+307  1 CB  A HIS 122 ? ? CA  A HIS 122 ? ? C   A HIS 122 ? ? 131.92 110.40 21.52  2.00 N
+308  1 O   A LEU 125 ? ? C   A LEU 125 ? ? N   A ASP 126 ? ? 112.55 122.70 -10.15 1.60 Y
+309  1 CB  A ASP 126 ? ? CG  A ASP 126 ? ? OD1 A ASP 126 ? ? 110.81 118.30 -7.49  0.90 N
+310  1 CA  A ASP 126 ? ? C   A ASP 126 ? ? O   A ASP 126 ? ? 133.86 120.10 13.76  2.10 N
+311  1 O   A ASP 126 ? ? C   A ASP 126 ? ? N   A LYS 127 ? ? 106.76 122.70 -15.94 1.60 Y
+312  1 CB  A LYS 127 ? ? CA  A LYS 127 ? ? C   A LYS 127 ? ? 129.22 110.40 18.82  2.00 N
+313  1 CG  A LYS 127 ? ? CD  A LYS 127 ? ? CE  A LYS 127 ? ? 89.97  111.90 -21.93 3.00 N
+314  1 CG  A PHE 128 ? ? CD1 A PHE 128 ? ? CE1 A PHE 128 ? ? 113.97 120.80 -6.83  1.10 N
+315  1 CG  A PHE 128 ? ? CD2 A PHE 128 ? ? CE2 A PHE 128 ? ? 132.89 120.80 12.09  1.10 N
+316  1 CE1 A PHE 128 ? ? CZ  A PHE 128 ? ? CE2 A PHE 128 ? ? 135.45 120.00 15.45  1.80 N
+317  1 CZ  A PHE 128 ? ? CE2 A PHE 128 ? ? CD2 A PHE 128 ? ? 99.23  120.10 -20.87 1.20 N
+318  1 CB  A LEU 129 ? ? CG  A LEU 129 ? ? CD2 A LEU 129 ? ? 99.47  111.00 -11.53 1.70 N
+319  1 O   A SER 131 ? ? C   A SER 131 ? ? N   A VAL 132 ? ? 139.35 122.70 16.65  1.60 Y
+320  1 CG1 A VAL 132 ? ? CB  A VAL 132 ? ? CG2 A VAL 132 ? ? 98.53  110.90 -12.37 1.60 N
+321  1 CA  A VAL 132 ? ? CB  A VAL 132 ? ? CG1 A VAL 132 ? ? 120.26 110.90 9.36   1.50 N
+322  1 N   A THR 134 ? ? CA  A THR 134 ? ? CB  A THR 134 ? ? 96.73  110.30 -13.57 1.90 N
+323  1 O   A THR 134 ? ? C   A THR 134 ? ? N   A VAL 135 ? ? 108.33 122.70 -14.37 1.60 Y
+324  1 CD1 A LEU 136 ? ? CG  A LEU 136 ? ? CD2 A LEU 136 ? ? 132.30 110.50 21.80  3.00 N
+325  1 CA  A THR 137 ? ? CB  A THR 137 ? ? OG1 A THR 137 ? ? 77.88  109.00 -31.12 2.10 N
+326  1 CB  A SER 138 ? ? CA  A SER 138 ? ? C   A SER 138 ? ? 97.01  110.10 -13.09 1.90 N
+327  1 CA  A SER 138 ? ? CB  A SER 138 ? ? OG  A SER 138 ? ? 52.65  111.20 -58.55 2.70 N
+328  1 O   A SER 138 ? ? C   A SER 138 ? ? N   A LYS 139 ? ? 132.66 122.70 9.96   1.60 Y
+329  1 CB  A TYR 140 ? ? CG  A TYR 140 ? ? CD2 A TYR 140 ? ? 128.94 121.00 7.94   0.60 N
+330  1 CD1 A TYR 140 ? ? CG  A TYR 140 ? ? CD2 A TYR 140 ? ? 110.68 117.90 -7.22  1.10 N
+331  1 CD1 A TYR 140 ? ? CE1 A TYR 140 ? ? CZ  A TYR 140 ? ? 130.19 119.80 10.39  0.90 N
+332  1 CB  A ARG 141 ? ? CA  A ARG 141 ? ? C   A ARG 141 ? ? 131.01 110.40 20.61  2.00 N
+333  1 CG  A ARG 141 ? ? CD  A ARG 141 ? ? NE  A ARG 141 ? ? 87.28  111.80 -24.52 2.10 N
+334  1 CD  A ARG 141 ? ? NE  A ARG 141 ? ? CZ  A ARG 141 ? ? 106.67 123.60 -16.93 1.40 N
+335  1 NE  A ARG 141 ? ? CZ  A ARG 141 ? ? NH1 A ARG 141 ? ? 132.93 120.30 12.63  0.50 N
+336  1 NE  A ARG 141 ? ? CZ  A ARG 141 ? ? NH2 A ARG 141 ? ? 108.58 120.30 -11.72 0.50 N
+337  1 CG1 B VAL 1   ? ? CB  B VAL 1   ? ? CG2 B VAL 1   ? ? 145.45 110.90 34.55  1.60 N
+338  1 CA  B VAL 1   ? ? CB  B VAL 1   ? ? CG1 B VAL 1   ? ? 95.45  110.90 -15.45 1.50 N
+339  1 CA  B VAL 1   ? ? C   B VAL 1   ? ? O   B VAL 1   ? ? 95.31  120.10 -24.79 2.10 N
+340  1 CA  B VAL 1   ? ? C   B VAL 1   ? ? N   B HIS 2   ? ? 89.73  117.20 -27.47 2.20 Y
+341  1 C   B VAL 1   ? ? N   B HIS 2   ? ? CA  B HIS 2   ? ? 81.69  121.70 -40.01 2.50 Y
+342  1 CB  B HIS 2   ? ? CA  B HIS 2   ? ? C   B HIS 2   ? ? 76.70  110.40 -33.70 2.00 N
+343  1 N   B HIS 2   ? ? CA  B HIS 2   ? ? CB  B HIS 2   ? ? 95.80  110.60 -14.80 1.80 N
+344  1 CA  B HIS 2   ? ? CB  B HIS 2   ? ? CG  B HIS 2   ? ? 133.33 113.60 19.73  1.70 N
+345  1 CB  B HIS 2   ? ? CG  B HIS 2   ? ? CD2 B HIS 2   ? ? 115.41 129.70 -14.29 1.60 N
+346  1 ND1 B HIS 2   ? ? CG  B HIS 2   ? ? CD2 B HIS 2   ? ? 118.26 108.80 9.46   1.40 N
+347  1 CG  B HIS 2   ? ? ND1 B HIS 2   ? ? CE1 B HIS 2   ? ? 85.88  105.70 -19.82 1.30 N
+348  1 ND1 B HIS 2   ? ? CE1 B HIS 2   ? ? NE2 B HIS 2   ? ? 132.43 111.50 20.93  1.30 N
+349  1 CA  B HIS 2   ? ? C   B HIS 2   ? ? O   B HIS 2   ? ? 133.63 120.10 13.53  2.10 N
+350  1 CA  B HIS 2   ? ? C   B HIS 2   ? ? N   B LEU 3   ? ? 97.52  117.20 -19.68 2.20 Y
+351  1 N   B LEU 3   ? ? CA  B LEU 3   ? ? CB  B LEU 3   ? ? 91.79  110.40 -18.61 2.00 N
+352  1 CB  B LEU 3   ? ? CG  B LEU 3   ? ? CD2 B LEU 3   ? ? 100.06 111.00 -10.94 1.70 N
+353  1 CA  B LEU 3   ? ? C   B LEU 3   ? ? N   B THR 4   ? ? 98.24  117.20 -18.96 2.20 Y
+354  1 O   B LEU 3   ? ? C   B LEU 3   ? ? N   B THR 4   ? ? 134.59 122.70 11.89  1.60 Y
+355  1 C   B LEU 3   ? ? N   B THR 4   ? ? CA  B THR 4   ? ? 95.13  121.70 -26.57 2.50 Y
+356  1 N   B THR 4   ? ? CA  B THR 4   ? ? CB  B THR 4   ? ? 87.22  110.30 -23.08 1.90 N
+357  1 CA  B THR 4   ? ? CB  B THR 4   ? ? CG2 B THR 4   ? ? 135.83 112.40 23.43  1.40 N
+358  1 C   B THR 4   ? ? N   B PRO 5   ? ? CA  B PRO 5   ? ? 135.74 119.30 16.44  1.50 Y
+359  1 C   B THR 4   ? ? N   B PRO 5   ? ? CD  B PRO 5   ? ? 114.63 128.40 -13.77 2.10 Y
+360  1 CA  B PRO 5   ? ? N   B PRO 5   ? ? CD  B PRO 5   ? ? 93.13  111.70 -18.57 1.40 N
+361  1 N   B PRO 5   ? ? CA  B PRO 5   ? ? CB  B PRO 5   ? ? 139.23 103.30 35.93  1.20 N
+362  1 CA  B PRO 5   ? ? CB  B PRO 5   ? ? CG  B PRO 5   ? ? 83.03  104.80 -21.77 1.90 N
+363  1 N   B PRO 5   ? ? CD  B PRO 5   ? ? CG  B PRO 5   ? ? 93.71  103.20 -9.49  1.50 N
+364  1 CA  B PRO 5   ? ? C   B PRO 5   ? ? N   B GLU 6   ? ? 98.21  117.20 -18.99 2.20 Y
+365  1 O   B PRO 5   ? ? C   B PRO 5   ? ? N   B GLU 6   ? ? 136.97 122.70 14.27  1.60 Y
+366  1 CB  B GLU 6   ? ? CA  B GLU 6   ? ? C   B GLU 6   ? ? 97.81  110.40 -12.59 2.00 N
+367  1 CA  B GLU 6   ? ? CB  B GLU 6   ? ? CG  B GLU 6   ? ? 137.40 113.40 24.00  2.20 N
+368  1 OE1 B GLU 6   ? ? CD  B GLU 6   ? ? OE2 B GLU 6   ? ? 102.21 123.30 -21.09 1.20 N
+369  1 CG  B GLU 6   ? ? CD  B GLU 6   ? ? OE1 B GLU 6   ? ? 100.90 118.30 -17.40 2.00 N
+370  1 CG  B GLU 6   ? ? CD  B GLU 6   ? ? OE2 B GLU 6   ? ? 132.48 118.30 14.18  2.00 N
+371  1 CB  B GLU 7   ? ? CA  B GLU 7   ? ? C   B GLU 7   ? ? 128.08 110.40 17.68  2.00 N
+372  1 N   B GLU 7   ? ? CA  B GLU 7   ? ? C   B GLU 7   ? ? 93.45  111.00 -17.55 2.70 N
+373  1 CB  B LYS 8   ? ? CG  B LYS 8   ? ? CD  B LYS 8   ? ? 136.95 111.60 25.35  2.60 N
+374  1 CG  B LYS 8   ? ? CD  B LYS 8   ? ? CE  B LYS 8   ? ? 130.40 111.90 18.50  3.00 N
+375  1 O   B LYS 8   ? ? C   B LYS 8   ? ? N   B SER 9   ? ? 102.07 122.70 -20.63 1.60 Y
+376  1 N   B SER 9   ? ? CA  B SER 9   ? ? CB  B SER 9   ? ? 123.04 110.50 12.54  1.50 N
+377  1 CA  B SER 9   ? ? CB  B SER 9   ? ? OG  B SER 9   ? ? 80.51  111.20 -30.69 2.70 N
+378  1 CA  B SER 9   ? ? C   B SER 9   ? ? N   B ALA 10  ? ? 101.56 117.20 -15.64 2.20 Y
+379  1 CB  B ALA 10  ? ? CA  B ALA 10  ? ? C   B ALA 10  ? ? 96.29  110.10 -13.81 1.50 N
+380  1 OG1 B THR 12  ? ? CB  B THR 12  ? ? CG2 B THR 12  ? ? 163.82 110.00 53.82  2.30 N
+381  1 CA  B THR 12  ? ? CB  B THR 12  ? ? OG1 B THR 12  ? ? 94.17  109.00 -14.83 2.10 N
+382  1 CA  B THR 12  ? ? CB  B THR 12  ? ? CG2 B THR 12  ? ? 99.97  112.40 -12.43 1.40 N
+383  1 CA  B THR 12  ? ? C   B THR 12  ? ? O   B THR 12  ? ? 132.83 120.10 12.73  2.10 N
+384  1 O   B THR 12  ? ? C   B THR 12  ? ? N   B ALA 13  ? ? 110.09 122.70 -12.61 1.60 Y
+385  1 N   B ALA 13  ? ? CA  B ALA 13  ? ? C   B ALA 13  ? ? 128.10 111.00 17.10  2.70 N
+386  1 O   B ALA 13  ? ? C   B ALA 13  ? ? N   B LEU 14  ? ? 110.62 122.70 -12.08 1.60 Y
+387  1 N   B LEU 14  ? ? CA  B LEU 14  ? ? CB  B LEU 14  ? ? 98.09  110.40 -12.31 2.00 N
+388  1 CD1 B LEU 14  ? ? CG  B LEU 14  ? ? CD2 B LEU 14  ? ? 129.48 110.50 18.98  3.00 N
+389  1 CG  B TRP 15  ? ? CD1 B TRP 15  ? ? NE1 B TRP 15  ? ? 117.04 110.10 6.94   1.00 N
+390  1 NE1 B TRP 15  ? ? CE2 B TRP 15  ? ? CD2 B TRP 15  ? ? 100.45 107.30 -6.85  1.00 N
+391  1 O   B TRP 15  ? ? C   B TRP 15  ? ? N   B GLY 16  ? ? 138.52 123.20 15.32  1.70 Y
+392  1 CD  B LYS 17  ? ? CE  B LYS 17  ? ? NZ  B LYS 17  ? ? 86.13  111.70 -25.57 2.30 N
+393  1 CA  B LYS 17  ? ? C   B LYS 17  ? ? N   B VAL 18  ? ? 133.42 117.20 16.22  2.20 Y
+394  1 O   B LYS 17  ? ? C   B LYS 17  ? ? N   B VAL 18  ? ? 105.12 122.70 -17.58 1.60 Y
+395  1 C   B LYS 17  ? ? N   B VAL 18  ? ? CA  B VAL 18  ? ? 138.00 121.70 16.30  2.50 Y
+396  1 CA  B VAL 18  ? ? CB  B VAL 18  ? ? CG2 B VAL 18  ? ? 92.93  110.90 -17.97 1.50 N
+397  1 CB  B ASN 19  ? ? CG  B ASN 19  ? ? OD1 B ASN 19  ? ? 133.88 121.60 12.28  2.00 N
+398  1 CB  B ASN 19  ? ? CG  B ASN 19  ? ? ND2 B ASN 19  ? ? 97.37  116.70 -19.33 2.40 N
+399  1 CA  B VAL 20  ? ? CB  B VAL 20  ? ? CG1 B VAL 20  ? ? 100.63 110.90 -10.27 1.50 N
+400  1 CA  B VAL 20  ? ? C   B VAL 20  ? ? N   B ASP 21  ? ? 132.97 117.20 15.77  2.20 Y
+401  1 O   B VAL 20  ? ? C   B VAL 20  ? ? N   B ASP 21  ? ? 96.44  122.70 -26.26 1.60 Y
+402  1 OD1 B ASP 21  ? ? CG  B ASP 21  ? ? OD2 B ASP 21  ? ? 135.06 123.30 11.76  1.90 N
+403  1 CB  B ASP 21  ? ? CG  B ASP 21  ? ? OD1 B ASP 21  ? ? 102.85 118.30 -15.45 0.90 N
+404  1 CB  B ASP 21  ? ? CG  B ASP 21  ? ? OD2 B ASP 21  ? ? 101.24 118.30 -17.06 0.90 N
+405  1 CB  B GLU 22  ? ? CG  B GLU 22  ? ? CD  B GLU 22  ? ? 147.02 114.20 32.82  2.70 N
+406  1 OE1 B GLU 22  ? ? CD  B GLU 22  ? ? OE2 B GLU 22  ? ? 71.20  123.30 -52.10 1.20 N
+407  1 CG  B GLU 22  ? ? CD  B GLU 22  ? ? OE1 B GLU 22  ? ? 91.22  118.30 -27.08 2.00 N
+408  1 CG  B GLU 22  ? ? CD  B GLU 22  ? ? OE2 B GLU 22  ? ? 82.03  118.30 -36.27 2.00 N
+409  1 CG1 B VAL 23  ? ? CB  B VAL 23  ? ? CG2 B VAL 23  ? ? 123.94 110.90 13.04  1.60 N
+410  1 CA  B VAL 23  ? ? CB  B VAL 23  ? ? CG2 B VAL 23  ? ? 94.69  110.90 -16.21 1.50 N
+411  1 CA  B GLY 24  ? ? C   B GLY 24  ? ? O   B GLY 24  ? ? 132.25 120.60 11.65  1.80 N
+412  1 CB  B GLU 26  ? ? CG  B GLU 26  ? ? CD  B GLU 26  ? ? 170.31 114.20 56.11  2.70 N
+413  1 OE1 B GLU 26  ? ? CD  B GLU 26  ? ? OE2 B GLU 26  ? ? 62.20  123.30 -61.10 1.20 N
+414  1 CG  B GLU 26  ? ? CD  B GLU 26  ? ? OE1 B GLU 26  ? ? 90.12  118.30 -28.18 2.00 N
+415  1 CG  B GLU 26  ? ? CD  B GLU 26  ? ? OE2 B GLU 26  ? ? 53.28  118.30 -65.02 2.00 N
+416  1 O   B GLU 26  ? ? C   B GLU 26  ? ? N   B ALA 27  ? ? 135.25 122.70 12.55  1.60 Y
+417  1 N   B ALA 27  ? ? CA  B ALA 27  ? ? CB  B ALA 27  ? ? 100.99 110.10 -9.11  1.40 N
+418  1 CB  B LEU 28  ? ? CG  B LEU 28  ? ? CD2 B LEU 28  ? ? 87.71  111.00 -23.29 1.70 N
+419  1 CA  B LEU 28  ? ? C   B LEU 28  ? ? O   B LEU 28  ? ? 134.71 120.10 14.61  2.10 N
+420  1 O   B LEU 28  ? ? C   B LEU 28  ? ? N   B GLY 29  ? ? 112.02 123.20 -11.18 1.70 Y
+421  1 NH1 B ARG 30  ? ? CZ  B ARG 30  ? ? NH2 B ARG 30  ? ? 108.39 119.40 -11.01 1.10 N
+422  1 NE  B ARG 30  ? ? CZ  B ARG 30  ? ? NH1 B ARG 30  ? ? 115.33 120.30 -4.97  0.50 N
+423  1 NE  B ARG 30  ? ? CZ  B ARG 30  ? ? NH2 B ARG 30  ? ? 136.18 120.30 15.88  0.50 N
+424  1 CB  B LEU 31  ? ? CG  B LEU 31  ? ? CD1 B LEU 31  ? ? 99.02  111.00 -11.98 1.70 N
+425  1 CB  B LEU 32  ? ? CG  B LEU 32  ? ? CD1 B LEU 32  ? ? 137.61 111.00 26.61  1.70 N
+426  1 CB  B TYR 35  ? ? CG  B TYR 35  ? ? CD2 B TYR 35  ? ? 127.21 121.00 6.21   0.60 N
+427  1 CD1 B TYR 35  ? ? CG  B TYR 35  ? ? CD2 B TYR 35  ? ? 108.71 117.90 -9.19  1.10 N
+428  1 CZ  B TYR 35  ? ? CE2 B TYR 35  ? ? CD2 B TYR 35  ? ? 126.29 119.80 6.49   0.90 N
+429  1 O   B TYR 35  ? ? C   B TYR 35  ? ? N   B PRO 36  ? ? 132.74 121.10 11.64  1.90 Y
+430  1 CA  B PRO 36  ? ? N   B PRO 36  ? ? CD  B PRO 36  ? ? 101.49 111.70 -10.21 1.40 N
+431  1 N   B PRO 36  ? ? CA  B PRO 36  ? ? CB  B PRO 36  ? ? 110.86 103.30 7.56   1.20 N
+432  1 N   B PRO 36  ? ? CD  B PRO 36  ? ? CG  B PRO 36  ? ? 115.86 103.20 12.66  1.50 N
+433  1 O   B PRO 36  ? ? C   B PRO 36  ? ? N   B TRP 37  ? ? 112.99 122.70 -9.71  1.60 Y
+434  1 N   B TRP 37  ? ? CA  B TRP 37  ? ? CB  B TRP 37  ? ? 99.53  110.60 -11.07 1.80 N
+435  1 CD1 B TRP 37  ? ? CG  B TRP 37  ? ? CD2 B TRP 37  ? ? 101.26 106.30 -5.04  0.80 N
+436  1 CD1 B TRP 37  ? ? NE1 B TRP 37  ? ? CE2 B TRP 37  ? ? 122.56 109.00 13.56  0.90 N
+437  1 CD2 B TRP 37  ? ? CE3 B TRP 37  ? ? CZ3 B TRP 37  ? ? 110.43 118.80 -8.37  1.30 N
+438  1 CZ3 B TRP 37  ? ? CH2 B TRP 37  ? ? CZ2 B TRP 37  ? ? 132.31 121.60 10.71  1.20 N
+439  1 CH2 B TRP 37  ? ? CZ2 B TRP 37  ? ? CE2 B TRP 37  ? ? 104.61 117.40 -12.79 1.00 N
+440  1 N   B THR 38  ? ? CA  B THR 38  ? ? CB  B THR 38  ? ? 125.34 110.30 15.04  1.90 N
+441  1 CA  B THR 38  ? ? CB  B THR 38  ? ? CG2 B THR 38  ? ? 102.20 112.40 -10.20 1.40 N
+442  1 NH1 B ARG 40  ? ? CZ  B ARG 40  ? ? NH2 B ARG 40  ? ? 143.86 119.40 24.46  1.10 N
+443  1 NE  B ARG 40  ? ? CZ  B ARG 40  ? ? NH1 B ARG 40  ? ? 109.38 120.30 -10.92 0.50 N
+444  1 NE  B ARG 40  ? ? CZ  B ARG 40  ? ? NH2 B ARG 40  ? ? 102.52 120.30 -17.78 0.50 N
+445  1 CA  B ARG 40  ? ? C   B ARG 40  ? ? O   B ARG 40  ? ? 103.02 120.10 -17.08 2.10 N
+446  1 CA  B ARG 40  ? ? C   B ARG 40  ? ? N   B PHE 41  ? ? 136.08 117.20 18.88  2.20 Y
+447  1 CB  B PHE 41  ? ? CG  B PHE 41  ? ? CD1 B PHE 41  ? ? 115.08 120.80 -5.72  0.70 N
+448  1 CG  B PHE 41  ? ? CD1 B PHE 41  ? ? CE1 B PHE 41  ? ? 114.14 120.80 -6.66  1.10 N
+449  1 CG  B PHE 41  ? ? CD2 B PHE 41  ? ? CE2 B PHE 41  ? ? 110.90 120.80 -9.90  1.10 N
+450  1 CA  B PHE 41  ? ? C   B PHE 41  ? ? O   B PHE 41  ? ? 105.90 120.10 -14.20 2.10 N
+451  1 O   B PHE 41  ? ? C   B PHE 41  ? ? N   B PHE 42  ? ? 144.28 122.70 21.58  1.60 Y
+452  1 CB  B PHE 42  ? ? CG  B PHE 42  ? ? CD2 B PHE 42  ? ? 140.34 120.80 19.54  0.70 N
+453  1 CD1 B PHE 42  ? ? CG  B PHE 42  ? ? CD2 B PHE 42  ? ? 105.20 118.30 -13.10 1.30 N
+454  1 CB  B PHE 42  ? ? CG  B PHE 42  ? ? CD1 B PHE 42  ? ? 113.94 120.80 -6.86  0.70 N
+455  1 CG  B PHE 42  ? ? CD1 B PHE 42  ? ? CE1 B PHE 42  ? ? 108.25 120.80 -12.55 1.10 N
+456  1 CG  B PHE 42  ? ? CD2 B PHE 42  ? ? CE2 B PHE 42  ? ? 133.67 120.80 12.87  1.10 N
+457  1 CD1 B PHE 42  ? ? CE1 B PHE 42  ? ? CZ  B PHE 42  ? ? 144.95 120.10 24.85  1.20 N
+458  1 CE1 B PHE 42  ? ? CZ  B PHE 42  ? ? CE2 B PHE 42  ? ? 104.05 120.00 -15.95 1.80 N
+459  1 N   B GLU 43  ? ? CA  B GLU 43  ? ? CB  B GLU 43  ? ? 90.03  110.60 -20.57 1.80 N
+460  1 CA  B GLU 43  ? ? CB  B GLU 43  ? ? CG  B GLU 43  ? ? 137.87 113.40 24.47  2.20 N
+461  1 OE1 B GLU 43  ? ? CD  B GLU 43  ? ? OE2 B GLU 43  ? ? 161.28 123.30 37.98  1.20 N
+462  1 CG  B GLU 43  ? ? CD  B GLU 43  ? ? OE1 B GLU 43  ? ? 96.69  118.30 -21.61 2.00 N
+463  1 CG  B GLU 43  ? ? CD  B GLU 43  ? ? OE2 B GLU 43  ? ? 69.22  118.30 -49.08 2.00 N
+464  1 O   B GLU 43  ? ? C   B GLU 43  ? ? N   B SER 44  ? ? 103.49 122.70 -19.21 1.60 Y
+465  1 CB  B SER 44  ? ? CA  B SER 44  ? ? C   B SER 44  ? ? 132.63 110.10 22.53  1.90 N
+466  1 CA  B SER 44  ? ? CB  B SER 44  ? ? OG  B SER 44  ? ? 147.51 111.20 36.31  2.70 N
+467  1 CA  B SER 44  ? ? C   B SER 44  ? ? O   B SER 44  ? ? 106.18 120.10 -13.92 2.10 N
+468  1 O   B SER 44  ? ? C   B SER 44  ? ? N   B PHE 45  ? ? 81.36  122.70 -41.34 1.60 Y
+469  1 C   B SER 44  ? ? N   B PHE 45  ? ? CA  B PHE 45  ? ? 137.08 121.70 15.38  2.50 Y
+470  1 CB  B PHE 45  ? ? CG  B PHE 45  ? ? CD2 B PHE 45  ? ? 133.29 120.80 12.49  0.70 N
+471  1 CB  B PHE 45  ? ? CG  B PHE 45  ? ? CD1 B PHE 45  ? ? 111.44 120.80 -9.36  0.70 N
+472  1 CG  B PHE 45  ? ? CD1 B PHE 45  ? ? CE1 B PHE 45  ? ? 109.15 120.80 -11.65 1.10 N
+473  1 CG  B PHE 45  ? ? CD2 B PHE 45  ? ? CE2 B PHE 45  ? ? 150.53 120.80 29.73  1.10 N
+474  1 CE1 B PHE 45  ? ? CZ  B PHE 45  ? ? CE2 B PHE 45  ? ? 137.54 120.00 17.54  1.80 N
+475  1 CZ  B PHE 45  ? ? CE2 B PHE 45  ? ? CD2 B PHE 45  ? ? 91.92  120.10 -28.18 1.20 N
+476  1 CA  B PHE 45  ? ? C   B PHE 45  ? ? N   B GLY 46  ? ? 137.46 116.20 21.26  2.00 Y
+477  1 O   B PHE 45  ? ? C   B PHE 45  ? ? N   B GLY 46  ? ? 110.21 123.20 -12.99 1.70 Y
+478  1 O   B GLY 46  ? ? C   B GLY 46  ? ? N   B ASP 47  ? ? 134.54 122.70 11.84  1.60 Y
+479  1 CB  B ASP 47  ? ? CA  B ASP 47  ? ? C   B ASP 47  ? ? 92.95  110.40 -17.45 2.00 N
+480  1 N   B ASP 47  ? ? CA  B ASP 47  ? ? CB  B ASP 47  ? ? 94.70  110.60 -15.90 1.80 N
+481  1 OD1 B ASP 47  ? ? CG  B ASP 47  ? ? OD2 B ASP 47  ? ? 104.05 123.30 -19.25 1.90 N
+482  1 CA  B ASP 47  ? ? C   B ASP 47  ? ? N   B LEU 48  ? ? 96.06  117.20 -21.14 2.20 Y
+483  1 CB  B LEU 48  ? ? CA  B LEU 48  ? ? C   B LEU 48  ? ? 125.86 110.20 15.66  1.90 N
+484  1 CB  B LEU 48  ? ? CG  B LEU 48  ? ? CD2 B LEU 48  ? ? 129.15 111.00 18.15  1.70 N
+485  1 C   B LEU 48  ? ? N   B SER 49  ? ? CA  B SER 49  ? ? 100.19 121.70 -21.51 2.50 Y
+486  1 CB  B SER 49  ? ? CA  B SER 49  ? ? C   B SER 49  ? ? 84.79  110.10 -25.31 1.90 N
+487  1 N   B SER 49  ? ? CA  B SER 49  ? ? CB  B SER 49  ? ? 94.30  110.50 -16.20 1.50 N
+488  1 N   B SER 49  ? ? CA  B SER 49  ? ? C   B SER 49  ? ? 92.80  111.00 -18.20 2.70 N
+489  1 CA  B SER 49  ? ? C   B SER 49  ? ? O   B SER 49  ? ? 92.07  120.10 -28.03 2.10 N
+490  1 CA  B SER 49  ? ? C   B SER 49  ? ? N   B THR 50  ? ? 137.76 117.20 20.56  2.20 Y
+491  1 O   B SER 49  ? ? C   B SER 49  ? ? N   B THR 50  ? ? 88.45  122.70 -34.25 1.60 Y
+492  1 C   B SER 49  ? ? N   B THR 50  ? ? CA  B THR 50  ? ? 157.11 121.70 35.41  2.50 Y
+493  1 N   B THR 50  ? ? CA  B THR 50  ? ? CB  B THR 50  ? ? 94.41  110.30 -15.89 1.90 N
+494  1 CA  B THR 50  ? ? CB  B THR 50  ? ? OG1 B THR 50  ? ? 123.70 109.00 14.70  2.10 N
+495  1 CA  B THR 50  ? ? CB  B THR 50  ? ? CG2 B THR 50  ? ? 137.00 112.40 24.60  1.40 N
+496  1 N   B THR 50  ? ? CA  B THR 50  ? ? C   B THR 50  ? ? 127.36 111.00 16.36  2.70 N
+497  1 O   B PRO 51  ? ? C   B PRO 51  ? ? N   B ASP 52  ? ? 109.01 122.70 -13.69 1.60 Y
+498  1 OD1 B ASP 52  ? ? CG  B ASP 52  ? ? OD2 B ASP 52  ? ? 110.38 123.30 -12.92 1.90 N
+499  1 CB  B ASP 52  ? ? CG  B ASP 52  ? ? OD2 B ASP 52  ? ? 98.72  118.30 -19.58 0.90 N
+500  1 CA  B ALA 53  ? ? C   B ALA 53  ? ? O   B ALA 53  ? ? 145.63 120.10 25.53  2.10 N
+501  1 O   B ALA 53  ? ? C   B ALA 53  ? ? N   B VAL 54  ? ? 107.35 122.70 -15.35 1.60 Y
+502  1 CG1 B VAL 54  ? ? CB  B VAL 54  ? ? CG2 B VAL 54  ? ? 123.72 110.90 12.82  1.60 N
+503  1 O   B MET 55  ? ? C   B MET 55  ? ? N   B GLY 56  ? ? 136.15 123.20 12.95  1.70 Y
+504  1 O   B GLY 56  ? ? C   B GLY 56  ? ? N   B ASN 57  ? ? 99.20  122.70 -23.50 1.60 Y
+505  1 O   B ASN 57  ? ? C   B ASN 57  ? ? N   B PRO 58  ? ? 106.26 121.10 -14.84 1.90 Y
+506  1 C   B ASN 57  ? ? N   B PRO 58  ? ? CA  B PRO 58  ? ? 131.35 119.30 12.05  1.50 Y
+507  1 C   B ASN 57  ? ? N   B PRO 58  ? ? CD  B PRO 58  ? ? 115.20 128.40 -13.20 2.10 Y
+508  1 CB  B PRO 58  ? ? CG  B PRO 58  ? ? CD  B PRO 58  ? ? 145.32 106.50 38.82  3.90 N
+509  1 N   B PRO 58  ? ? CD  B PRO 58  ? ? CG  B PRO 58  ? ? 81.22  103.20 -21.98 1.50 N
+510  1 O   B PRO 58  ? ? C   B PRO 58  ? ? N   B LYS 59  ? ? 133.48 122.70 10.78  1.60 Y
+511  1 CG  B LYS 59  ? ? CD  B LYS 59  ? ? CE  B LYS 59  ? ? 92.60  111.90 -19.30 3.00 N
+512  1 CD  B LYS 59  ? ? CE  B LYS 59  ? ? NZ  B LYS 59  ? ? 71.60  111.70 -40.10 2.30 N
+513  1 CG1 B VAL 60  ? ? CB  B VAL 60  ? ? CG2 B VAL 60  ? ? 124.71 110.90 13.81  1.60 N
+514  1 CA  B VAL 60  ? ? C   B VAL 60  ? ? O   B VAL 60  ? ? 140.34 120.10 20.24  2.10 N
+515  1 O   B VAL 60  ? ? C   B VAL 60  ? ? N   B LYS 61  ? ? 105.35 122.70 -17.35 1.60 Y
+516  1 CB  B LYS 61  ? ? CA  B LYS 61  ? ? C   B LYS 61  ? ? 98.06  110.40 -12.34 2.00 N
+517  1 CG  B LYS 61  ? ? CD  B LYS 61  ? ? CE  B LYS 61  ? ? 93.24  111.90 -18.66 3.00 N
+518  1 CD  B LYS 61  ? ? CE  B LYS 61  ? ? NZ  B LYS 61  ? ? 89.17  111.70 -22.53 2.30 N
+519  1 O   B LYS 61  ? ? C   B LYS 61  ? ? N   B ALA 62  ? ? 111.25 122.70 -11.45 1.60 Y
+520  1 CA  B HIS 63  ? ? CB  B HIS 63  ? ? CG  B HIS 63  ? ? 124.09 113.60 10.49  1.70 N
+521  1 CE1 B HIS 63  ? ? NE2 B HIS 63  ? ? CD2 B HIS 63  ? ? 115.25 109.00 6.25   0.70 N
+522  1 CA  B GLY 64  ? ? C   B GLY 64  ? ? O   B GLY 64  ? ? 142.69 120.60 22.09  1.80 N
+523  1 O   B GLY 64  ? ? C   B GLY 64  ? ? N   B LYS 65  ? ? 110.06 122.70 -12.64 1.60 Y
+524  1 CA  B LYS 65  ? ? CB  B LYS 65  ? ? CG  B LYS 65  ? ? 99.27  113.40 -14.13 2.20 N
+525  1 CB  B LYS 65  ? ? CG  B LYS 65  ? ? CD  B LYS 65  ? ? 93.52  111.60 -18.08 2.60 N
+526  1 CG  B LYS 65  ? ? CD  B LYS 65  ? ? CE  B LYS 65  ? ? 64.38  111.90 -47.52 3.00 N
+527  1 CD  B LYS 65  ? ? CE  B LYS 65  ? ? NZ  B LYS 65  ? ? 71.25  111.70 -40.45 2.30 N
+528  1 CB  B LYS 66  ? ? CA  B LYS 66  ? ? C   B LYS 66  ? ? 97.05  110.40 -13.35 2.00 N
+529  1 CA  B LYS 66  ? ? CB  B LYS 66  ? ? CG  B LYS 66  ? ? 127.27 113.40 13.87  2.20 N
+530  1 CG  B LYS 66  ? ? CD  B LYS 66  ? ? CE  B LYS 66  ? ? 88.62  111.90 -23.28 3.00 N
+531  1 CD  B LYS 66  ? ? CE  B LYS 66  ? ? NZ  B LYS 66  ? ? 90.86  111.70 -20.84 2.30 N
+532  1 O   B LYS 66  ? ? C   B LYS 66  ? ? N   B VAL 67  ? ? 133.58 122.70 10.88  1.60 Y
+533  1 CG1 B VAL 67  ? ? CB  B VAL 67  ? ? CG2 B VAL 67  ? ? 123.93 110.90 13.03  1.60 N
+534  1 CD1 B LEU 68  ? ? CG  B LEU 68  ? ? CD2 B LEU 68  ? ? 140.82 110.50 30.32  3.00 N
+535  1 CB  B LEU 68  ? ? CG  B LEU 68  ? ? CD1 B LEU 68  ? ? 89.92  111.00 -21.08 1.70 N
+536  1 CA  B GLY 69  ? ? C   B GLY 69  ? ? N   B ALA 70  ? ? 102.13 117.20 -15.07 2.20 Y
+537  1 CG  B PHE 71  ? ? CD1 B PHE 71  ? ? CE1 B PHE 71  ? ? 127.68 120.80 6.88   1.10 N
+538  1 CG  B PHE 71  ? ? CD2 B PHE 71  ? ? CE2 B PHE 71  ? ? 112.68 120.80 -8.12  1.10 N
+539  1 CZ  B PHE 71  ? ? CE2 B PHE 71  ? ? CD2 B PHE 71  ? ? 130.29 120.10 10.19  1.20 N
+540  1 CB  B SER 72  ? ? CA  B SER 72  ? ? C   B SER 72  ? ? 130.02 110.10 19.92  1.90 N
+541  1 CB  B ASP 73  ? ? CG  B ASP 73  ? ? OD1 B ASP 73  ? ? 126.82 118.30 8.52   0.90 N
+542  1 CB  B ASP 73  ? ? CG  B ASP 73  ? ? OD2 B ASP 73  ? ? 108.10 118.30 -10.20 0.90 N
+543  1 CA  B ASP 73  ? ? C   B ASP 73  ? ? N   B GLY 74  ? ? 132.81 116.20 16.61  2.00 Y
+544  1 O   B ASP 73  ? ? C   B ASP 73  ? ? N   B GLY 74  ? ? 96.80  123.20 -26.40 1.70 Y
+545  1 C   B ASP 73  ? ? N   B GLY 74  ? ? CA  B GLY 74  ? ? 135.08 122.30 12.78  2.10 Y
+546  1 N   B GLY 74  ? ? CA  B GLY 74  ? ? C   B GLY 74  ? ? 129.54 113.10 16.44  2.50 N
+547  1 CA  B GLY 74  ? ? C   B GLY 74  ? ? O   B GLY 74  ? ? 150.49 120.60 29.89  1.80 N
+548  1 CB  B ALA 76  ? ? CA  B ALA 76  ? ? C   B ALA 76  ? ? 90.89  110.10 -19.21 1.50 N
+549  1 N   B ALA 76  ? ? CA  B ALA 76  ? ? C   B ALA 76  ? ? 127.47 111.00 16.47  2.70 N
+550  1 CA  B ALA 76  ? ? C   B ALA 76  ? ? O   B ALA 76  ? ? 134.51 120.10 14.41  2.10 N
+551  1 CB  B HIS 77  ? ? CG  B HIS 77  ? ? CD2 B HIS 77  ? ? 108.71 129.70 -20.99 1.60 N
+552  1 CB  B HIS 77  ? ? CG  B HIS 77  ? ? ND1 B HIS 77  ? ? 140.30 123.20 17.10  2.50 N
+553  1 ND1 B HIS 77  ? ? CE1 B HIS 77  ? ? NE2 B HIS 77  ? ? 126.06 111.50 14.56  1.30 N
+554  1 CE1 B HIS 77  ? ? NE2 B HIS 77  ? ? CD2 B HIS 77  ? ? 119.75 109.00 10.75  0.70 N
+555  1 CG  B HIS 77  ? ? CD2 B HIS 77  ? ? NE2 B HIS 77  ? ? 82.91  106.70 -23.79 1.20 N
+556  1 CB  B LEU 78  ? ? CA  B LEU 78  ? ? C   B LEU 78  ? ? 90.05  110.20 -20.15 1.90 N
+557  1 CA  B LEU 78  ? ? CB  B LEU 78  ? ? CG  B LEU 78  ? ? 97.25  115.30 -18.05 2.30 N
+558  1 CB  B LEU 78  ? ? CG  B LEU 78  ? ? CD2 B LEU 78  ? ? 130.65 111.00 19.65  1.70 N
+559  1 CA  B LEU 78  ? ? C   B LEU 78  ? ? O   B LEU 78  ? ? 106.89 120.10 -13.21 2.10 N
+560  1 N   B ASP 79  ? ? CA  B ASP 79  ? ? CB  B ASP 79  ? ? 96.43  110.60 -14.17 1.80 N
+561  1 OD1 B ASP 79  ? ? CG  B ASP 79  ? ? OD2 B ASP 79  ? ? 108.75 123.30 -14.55 1.90 N
+562  1 CB  B ASP 79  ? ? CG  B ASP 79  ? ? OD2 B ASP 79  ? ? 123.99 118.30 5.69   0.90 N
+563  1 O   B ASP 79  ? ? C   B ASP 79  ? ? N   B ASN 80  ? ? 103.90 122.70 -18.80 1.60 Y
+564  1 CB  B ASN 80  ? ? CG  B ASN 80  ? ? OD1 B ASN 80  ? ? 99.80  121.60 -21.80 2.00 N
+565  1 CB  B ASN 80  ? ? CG  B ASN 80  ? ? ND2 B ASN 80  ? ? 96.38  116.70 -20.32 2.40 N
+566  1 N   B ASN 80  ? ? CA  B ASN 80  ? ? C   B ASN 80  ? ? 92.62  111.00 -18.38 2.70 N
+567  1 CA  B ASN 80  ? ? C   B ASN 80  ? ? O   B ASN 80  ? ? 104.02 120.10 -16.08 2.10 N
+568  1 C   B ASN 80  ? ? N   B LEU 81  ? ? CA  B LEU 81  ? ? 105.80 121.70 -15.90 2.50 Y
+569  1 CB  B LEU 81  ? ? CA  B LEU 81  ? ? C   B LEU 81  ? ? 130.30 110.20 20.10  1.90 N
+570  1 N   B LEU 81  ? ? CA  B LEU 81  ? ? CB  B LEU 81  ? ? 90.71  110.40 -19.69 2.00 N
+571  1 CA  B LEU 81  ? ? CB  B LEU 81  ? ? CG  B LEU 81  ? ? 136.56 115.30 21.26  2.30 N
+572  1 CB  B LEU 81  ? ? CG  B LEU 81  ? ? CD1 B LEU 81  ? ? 121.89 111.00 10.89  1.70 N
+573  1 N   B LYS 82  ? ? CA  B LYS 82  ? ? CB  B LYS 82  ? ? 89.19  110.60 -21.41 1.80 N
+574  1 O   B LYS 82  ? ? C   B LYS 82  ? ? N   B GLY 83  ? ? 111.49 123.20 -11.71 1.70 Y
+575  1 N   B THR 84  ? ? CA  B THR 84  ? ? CB  B THR 84  ? ? 123.27 110.30 12.97  1.90 N
+576  1 CA  B THR 84  ? ? C   B THR 84  ? ? O   B THR 84  ? ? 135.17 120.10 15.07  2.10 N
+577  1 O   B THR 84  ? ? C   B THR 84  ? ? N   B PHE 85  ? ? 111.85 122.70 -10.85 1.60 Y
+578  1 CB  B PHE 85  ? ? CG  B PHE 85  ? ? CD2 B PHE 85  ? ? 113.11 120.80 -7.69  0.70 N
+579  1 CB  B PHE 85  ? ? CG  B PHE 85  ? ? CD1 B PHE 85  ? ? 126.62 120.80 5.82   0.70 N
+580  1 CG  B PHE 85  ? ? CD2 B PHE 85  ? ? CE2 B PHE 85  ? ? 107.55 120.80 -13.25 1.10 N
+581  1 CD1 B PHE 85  ? ? CE1 B PHE 85  ? ? CZ  B PHE 85  ? ? 132.61 120.10 12.51  1.20 N
+582  1 CE1 B PHE 85  ? ? CZ  B PHE 85  ? ? CE2 B PHE 85  ? ? 101.58 120.00 -18.42 1.80 N
+583  1 CZ  B PHE 85  ? ? CE2 B PHE 85  ? ? CD2 B PHE 85  ? ? 139.32 120.10 19.22  1.20 N
+584  1 CB  B THR 87  ? ? CA  B THR 87  ? ? C   B THR 87  ? ? 90.47  111.60 -21.13 2.70 N
+585  1 OG1 B THR 87  ? ? CB  B THR 87  ? ? CG2 B THR 87  ? ? 77.55  110.00 -32.45 2.30 N
+586  1 CA  B THR 87  ? ? CB  B THR 87  ? ? OG1 B THR 87  ? ? 88.47  109.00 -20.53 2.10 N
+587  1 CA  B THR 87  ? ? CB  B THR 87  ? ? CG2 B THR 87  ? ? 94.64  112.40 -17.76 1.40 N
+588  1 CB  B LEU 88  ? ? CG  B LEU 88  ? ? CD1 B LEU 88  ? ? 99.73  111.00 -11.27 1.70 N
+589  1 CB  B LEU 88  ? ? CG  B LEU 88  ? ? CD2 B LEU 88  ? ? 96.67  111.00 -14.33 1.70 N
+590  1 N   B SER 89  ? ? CA  B SER 89  ? ? CB  B SER 89  ? ? 98.15  110.50 -12.35 1.50 N
+591  1 CA  B GLU 90  ? ? CB  B GLU 90  ? ? CG  B GLU 90  ? ? 98.79  113.40 -14.61 2.20 N
+592  1 OE1 B GLU 90  ? ? CD  B GLU 90  ? ? OE2 B GLU 90  ? ? 130.61 123.30 7.31   1.20 N
+593  1 CG  B GLU 90  ? ? CD  B GLU 90  ? ? OE1 B GLU 90  ? ? 98.66  118.30 -19.64 2.00 N
+594  1 CG  B GLU 90  ? ? CD  B GLU 90  ? ? OE2 B GLU 90  ? ? 104.95 118.30 -13.35 2.00 N
+595  1 N   B GLU 90  ? ? CA  B GLU 90  ? ? C   B GLU 90  ? ? 138.56 111.00 27.56  2.70 N
+596  1 CA  B GLU 90  ? ? C   B GLU 90  ? ? O   B GLU 90  ? ? 133.73 120.10 13.63  2.10 N
+597  1 CA  B GLU 90  ? ? C   B GLU 90  ? ? N   B LEU 91  ? ? 97.42  117.20 -19.78 2.20 Y
+598  1 C   B LEU 91  ? ? N   B HIS 92  ? ? CA  B HIS 92  ? ? 105.54 121.70 -16.16 2.50 Y
+599  1 CE1 B HIS 92  ? ? NE2 B HIS 92  ? ? CD2 B HIS 92  ? ? 114.26 109.00 5.26   0.70 N
+600  1 O   B CYS 93  ? ? C   B CYS 93  ? ? N   B ASP 94  ? ? 132.64 122.70 9.94   1.60 Y
+601  1 OD1 B ASP 94  ? ? CG  B ASP 94  ? ? OD2 B ASP 94  ? ? 154.79 123.30 31.49  1.90 N
+602  1 CB  B ASP 94  ? ? CG  B ASP 94  ? ? OD1 B ASP 94  ? ? 97.42  118.30 -20.88 0.90 N
+603  1 CB  B ASP 94  ? ? CG  B ASP 94  ? ? OD2 B ASP 94  ? ? 105.76 118.30 -12.54 0.90 N
+604  1 CA  B ASP 94  ? ? C   B ASP 94  ? ? N   B LYS 95  ? ? 135.16 117.20 17.96  2.20 Y
+605  1 O   B ASP 94  ? ? C   B ASP 94  ? ? N   B LYS 95  ? ? 106.74 122.70 -15.96 1.60 Y
+606  1 N   B LYS 95  ? ? CA  B LYS 95  ? ? CB  B LYS 95  ? ? 97.56  110.60 -13.04 1.80 N
+607  1 N   B LYS 95  ? ? CA  B LYS 95  ? ? C   B LYS 95  ? ? 127.81 111.00 16.81  2.70 N
+608  1 O   B LYS 95  ? ? C   B LYS 95  ? ? N   B LEU 96  ? ? 112.27 122.70 -10.43 1.60 Y
+609  1 CB  B LEU 96  ? ? CG  B LEU 96  ? ? CD2 B LEU 96  ? ? 91.83  111.00 -19.17 1.70 N
+610  1 CG  B HIS 97  ? ? CD2 B HIS 97  ? ? NE2 B HIS 97  ? ? 97.74  106.70 -8.96  1.20 N
+611  1 OD1 B ASP 99  ? ? CG  B ASP 99  ? ? OD2 B ASP 99  ? ? 137.79 123.30 14.49  1.90 N
+612  1 CB  B ASP 99  ? ? CG  B ASP 99  ? ? OD1 B ASP 99  ? ? 111.27 118.30 -7.03  0.90 N
+613  1 CB  B ASP 99  ? ? CG  B ASP 99  ? ? OD2 B ASP 99  ? ? 110.87 118.30 -7.43  0.90 N
+614  1 N   B ASP 99  ? ? CA  B ASP 99  ? ? C   B ASP 99  ? ? 93.60  111.00 -17.40 2.70 N
+615  1 OE1 B GLU 101 ? ? CD  B GLU 101 ? ? OE2 B GLU 101 ? ? 178.51 123.30 55.21  1.20 N
+616  1 CG  B GLU 101 ? ? CD  B GLU 101 ? ? OE1 B GLU 101 ? ? 105.23 118.30 -13.07 2.00 N
+617  1 CG  B GLU 101 ? ? CD  B GLU 101 ? ? OE2 B GLU 101 ? ? 75.82  118.30 -42.48 2.00 N
+618  1 O   B GLU 101 ? ? C   B GLU 101 ? ? N   B ASN 102 ? ? 112.24 122.70 -10.46 1.60 Y
+619  1 N   B PHE 103 ? ? CA  B PHE 103 ? ? CB  B PHE 103 ? ? 122.38 110.60 11.78  1.80 N
+620  1 CD1 B PHE 103 ? ? CG  B PHE 103 ? ? CD2 B PHE 103 ? ? 126.29 118.30 7.99   1.30 N
+621  1 CB  B PHE 103 ? ? CG  B PHE 103 ? ? CD1 B PHE 103 ? ? 114.99 120.80 -5.81  0.70 N
+622  1 CG  B PHE 103 ? ? CD2 B PHE 103 ? ? CE2 B PHE 103 ? ? 113.88 120.80 -6.92  1.10 N
+623  1 CG  B ARG 104 ? ? CD  B ARG 104 ? ? NE  B ARG 104 ? ? 99.13  111.80 -12.67 2.10 N
+624  1 CD  B ARG 104 ? ? NE  B ARG 104 ? ? CZ  B ARG 104 ? ? 71.54  123.60 -52.06 1.40 N
+625  1 NH1 B ARG 104 ? ? CZ  B ARG 104 ? ? NH2 B ARG 104 ? ? 131.45 119.40 12.05  1.10 N
+626  1 NE  B ARG 104 ? ? CZ  B ARG 104 ? ? NH2 B ARG 104 ? ? 102.98 120.30 -17.32 0.50 N
+627  1 OD1 B ASN 108 ? ? CG  B ASN 108 ? ? ND2 B ASN 108 ? ? 164.26 121.90 42.36  2.30 N
+628  1 CB  B ASN 108 ? ? CG  B ASN 108 ? ? ND2 B ASN 108 ? ? 84.52  116.70 -32.18 2.40 N
+629  1 O   B VAL 111 ? ? C   B VAL 111 ? ? N   B CYS 112 ? ? 108.74 122.70 -13.96 1.60 Y
+630  1 N   B CYS 112 ? ? CA  B CYS 112 ? ? CB  B CYS 112 ? ? 123.02 110.80 12.22  1.50 N
+631  1 CA  B VAL 113 ? ? C   B VAL 113 ? ? N   B LEU 114 ? ? 132.06 117.20 14.86  2.20 Y
+632  1 CB  B LEU 114 ? ? CA  B LEU 114 ? ? C   B LEU 114 ? ? 125.99 110.20 15.79  1.90 N
+633  1 N   B ALA 115 ? ? CA  B ALA 115 ? ? CB  B ALA 115 ? ? 98.40  110.10 -11.70 1.40 N
+634  1 CB  B HIS 117 ? ? CG  B HIS 117 ? ? CD2 B HIS 117 ? ? 145.12 131.40 13.72  1.20 N
+635  1 ND1 B HIS 117 ? ? CG  B HIS 117 ? ? CD2 B HIS 117 ? ? 124.61 108.80 15.81  1.40 N
+636  1 CB  B HIS 117 ? ? CG  B HIS 117 ? ? ND1 B HIS 117 ? ? 90.13  121.40 -31.27 1.30 N
+637  1 CE1 B HIS 117 ? ? NE2 B HIS 117 ? ? CD2 B HIS 117 ? ? 116.65 109.00 7.65   0.70 N
+638  1 CG  B HIS 117 ? ? CD2 B HIS 117 ? ? NE2 B HIS 117 ? ? 79.80  106.70 -26.90 1.20 N
+639  1 CB  B PHE 118 ? ? CG  B PHE 118 ? ? CD2 B PHE 118 ? ? 132.09 120.80 11.29  0.70 N
+640  1 CD1 B PHE 118 ? ? CG  B PHE 118 ? ? CD2 B PHE 118 ? ? 107.83 118.30 -10.47 1.30 N
+641  1 CE1 B PHE 118 ? ? CZ  B PHE 118 ? ? CE2 B PHE 118 ? ? 103.59 120.00 -16.41 1.80 N
+642  1 CZ  B PHE 118 ? ? CE2 B PHE 118 ? ? CD2 B PHE 118 ? ? 127.80 120.10 7.70   1.20 N
+643  1 CB  B LYS 120 ? ? CA  B LYS 120 ? ? C   B LYS 120 ? ? 98.13  110.40 -12.27 2.00 N
+644  1 CG  B LYS 120 ? ? CD  B LYS 120 ? ? CE  B LYS 120 ? ? 93.53  111.90 -18.37 3.00 N
+645  1 CG  B GLU 121 ? ? CD  B GLU 121 ? ? OE1 B GLU 121 ? ? 90.94  118.30 -27.36 2.00 N
+646  1 CG  B GLU 121 ? ? CD  B GLU 121 ? ? OE2 B GLU 121 ? ? 85.18  118.30 -33.12 2.00 N
+647  1 CB  B PHE 122 ? ? CG  B PHE 122 ? ? CD2 B PHE 122 ? ? 114.14 120.80 -6.66  0.70 N
+648  1 CD1 B PHE 122 ? ? CE1 B PHE 122 ? ? CZ  B PHE 122 ? ? 110.93 120.10 -9.17  1.20 N
+649  1 C   B PRO 124 ? ? N   B PRO 125 ? ? CA  B PRO 125 ? ? 133.07 119.30 13.77  1.50 Y
+650  1 CA  B PRO 125 ? ? N   B PRO 125 ? ? CD  B PRO 125 ? ? 97.77  111.70 -13.93 1.40 N
+651  1 N   B PRO 125 ? ? CA  B PRO 125 ? ? CB  B PRO 125 ? ? 118.99 103.30 15.69  1.20 N
+652  1 CG1 B VAL 126 ? ? CB  B VAL 126 ? ? CG2 B VAL 126 ? ? 95.74  110.90 -15.16 1.60 N
+653  1 CA  B VAL 126 ? ? C   B VAL 126 ? ? N   B GLN 127 ? ? 132.33 117.20 15.13  2.20 Y
+654  1 O   B VAL 126 ? ? C   B VAL 126 ? ? N   B GLN 127 ? ? 111.24 122.70 -11.46 1.60 Y
+655  1 CA  B GLN 127 ? ? C   B GLN 127 ? ? O   B GLN 127 ? ? 137.22 120.10 17.12  2.10 N
+656  1 O   B GLN 127 ? ? C   B GLN 127 ? ? N   B ALA 128 ? ? 107.79 122.70 -14.91 1.60 Y
+657  1 CB  B TYR 130 ? ? CG  B TYR 130 ? ? CD2 B TYR 130 ? ? 116.79 121.00 -4.21  0.60 N
+658  1 CB  B TYR 130 ? ? CG  B TYR 130 ? ? CD1 B TYR 130 ? ? 126.60 121.00 5.60   0.60 N
+659  1 CD1 B TYR 130 ? ? CE1 B TYR 130 ? ? CZ  B TYR 130 ? ? 126.62 119.80 6.82   0.90 N
+660  1 CZ  B TYR 130 ? ? CE2 B TYR 130 ? ? CD2 B TYR 130 ? ? 111.95 119.80 -7.85  0.90 N
+661  1 CG  B LYS 132 ? ? CD  B LYS 132 ? ? CE  B LYS 132 ? ? 92.40  111.90 -19.50 3.00 N
+662  1 CD  B LYS 132 ? ? CE  B LYS 132 ? ? NZ  B LYS 132 ? ? 79.06  111.70 -32.64 2.30 N
+663  1 N   B VAL 134 ? ? CA  B VAL 134 ? ? CB  B VAL 134 ? ? 135.16 111.50 23.66  2.20 N
+664  1 CA  B VAL 134 ? ? CB  B VAL 134 ? ? CG1 B VAL 134 ? ? 96.72  110.90 -14.18 1.50 N
+665  1 O   B VAL 134 ? ? C   B VAL 134 ? ? N   B ALA 135 ? ? 109.92 122.70 -12.78 1.60 Y
+666  1 CA  B ALA 138 ? ? C   B ALA 138 ? ? O   B ALA 138 ? ? 133.71 120.10 13.61  2.10 N
+667  1 CB  B ASN 139 ? ? CA  B ASN 139 ? ? C   B ASN 139 ? ? 91.33  110.40 -19.07 2.00 N
+668  1 CA  B ASN 139 ? ? CB  B ASN 139 ? ? CG  B ASN 139 ? ? 98.69  113.40 -14.71 2.20 N
+669  1 OD1 B ASN 139 ? ? CG  B ASN 139 ? ? ND2 B ASN 139 ? ? 62.94  121.90 -58.96 2.30 N
+670  1 CB  B ASN 139 ? ? CG  B ASN 139 ? ? OD1 B ASN 139 ? ? 155.55 121.60 33.95  2.00 N
+671  1 O   B ALA 140 ? ? C   B ALA 140 ? ? N   B LEU 141 ? ? 110.79 122.70 -11.91 1.60 Y
+672  1 CB  B LEU 141 ? ? CA  B LEU 141 ? ? C   B LEU 141 ? ? 122.77 110.20 12.57  1.90 N
+673  1 O   B LEU 141 ? ? C   B LEU 141 ? ? N   B ALA 142 ? ? 112.25 122.70 -10.45 1.60 Y
+674  1 N   B ALA 142 ? ? CA  B ALA 142 ? ? CB  B ALA 142 ? ? 119.02 110.10 8.92   1.40 N
+675  1 CA  B ALA 142 ? ? C   B ALA 142 ? ? O   B ALA 142 ? ? 105.94 120.10 -14.16 2.10 N
+676  1 O   B ALA 142 ? ? C   B ALA 142 ? ? N   B HIS 143 ? ? 138.52 122.70 15.82  1.60 Y
+677  1 CB  B HIS 143 ? ? CG  B HIS 143 ? ? CD2 B HIS 143 ? ? 113.44 129.70 -16.26 1.60 N
+678  1 ND1 B HIS 143 ? ? CG  B HIS 143 ? ? CD2 B HIS 143 ? ? 154.78 108.80 45.98  1.40 N
+679  1 CB  B HIS 143 ? ? CG  B HIS 143 ? ? ND1 B HIS 143 ? ? 89.66  121.40 -31.74 1.30 N
+680  1 CG  B HIS 143 ? ? ND1 B HIS 143 ? ? CE1 B HIS 143 ? ? 59.66  105.70 -46.04 1.30 N
+681  1 ND1 B HIS 143 ? ? CE1 B HIS 143 ? ? NE2 B HIS 143 ? ? 121.85 111.50 10.35  1.30 N
+682  1 CG  B LYS 144 ? ? CD  B LYS 144 ? ? CE  B LYS 144 ? ? 165.57 111.90 53.67  3.00 N
+683  1 CA  B LYS 144 ? ? C   B LYS 144 ? ? N   B TYR 145 ? ? 137.95 117.20 20.75  2.20 Y
+684  1 O   B LYS 144 ? ? C   B LYS 144 ? ? N   B TYR 145 ? ? 105.00 122.70 -17.70 1.60 Y
+685  1 C   B LYS 144 ? ? N   B TYR 145 ? ? CA  B TYR 145 ? ? 144.11 121.70 22.41  2.50 Y
+686  1 N   B TYR 145 ? ? CA  B TYR 145 ? ? CB  B TYR 145 ? ? 131.06 110.60 20.46  1.80 N
+687  1 CB  B TYR 145 ? ? CG  B TYR 145 ? ? CD2 B TYR 145 ? ? 107.46 121.00 -13.54 0.60 N
+688  1 CD1 B TYR 145 ? ? CG  B TYR 145 ? ? CD2 B TYR 145 ? ? 133.07 117.90 15.17  1.10 N
+689  1 CG  B TYR 145 ? ? CD2 B TYR 145 ? ? CE2 B TYR 145 ? ? 109.69 121.30 -11.61 0.80 N
+690  1 CA  B TYR 145 ? ? C   B TYR 145 ? ? O   B TYR 145 ? ? 99.74  120.10 -20.36 2.10 N
+691  1 O   B TYR 145 ? ? C   B TYR 145 ? ? N   B HIS 146 ? ? 132.68 122.70 9.98   1.60 Y
+692  1 CA  B HIS 146 ? ? CB  B HIS 146 ? ? CG  B HIS 146 ? ? 99.50  113.60 -14.10 1.70 N
+693  1 CB  B HIS 146 ? ? CG  B HIS 146 ? ? CD2 B HIS 146 ? ? 92.07  129.70 -37.63 1.60 N
+694  1 ND1 B HIS 146 ? ? CG  B HIS 146 ? ? CD2 B HIS 146 ? ? 87.90  106.00 -18.10 1.40 N
+695  1 CB  B HIS 146 ? ? CG  B HIS 146 ? ? ND1 B HIS 146 ? ? 100.45 121.40 -20.95 1.30 N
+696  1 ND1 B HIS 146 ? ? CE1 B HIS 146 ? ? NE2 B HIS 146 ? ? 79.07  108.50 -29.43 1.10 N
+697  1 CG  B HIS 146 ? ? CD2 B HIS 146 ? ? NE2 B HIS 146 ? ? 82.55  106.70 -24.15 1.20 N
+698  1 CB  C VAL 1   ? ? CA  C VAL 1   ? ? C   C VAL 1   ? ? 99.62  111.40 -11.78 1.90 N
+699  1 N   C VAL 1   ? ? CA  C VAL 1   ? ? CB  C VAL 1   ? ? 69.02  111.50 -42.48 2.20 N
+700  1 CG1 C VAL 1   ? ? CB  C VAL 1   ? ? CG2 C VAL 1   ? ? 53.57  110.90 -57.33 1.60 N
+701  1 CA  C VAL 1   ? ? CB  C VAL 1   ? ? CG1 C VAL 1   ? ? 72.02  110.90 -38.88 1.50 N
+702  1 CA  C VAL 1   ? ? CB  C VAL 1   ? ? CG2 C VAL 1   ? ? 76.74  110.90 -34.16 1.50 N
+703  1 N   C VAL 1   ? ? CA  C VAL 1   ? ? C   C VAL 1   ? ? 87.48  111.00 -23.52 2.70 N
+704  1 CA  C VAL 1   ? ? C   C VAL 1   ? ? O   C VAL 1   ? ? 133.61 120.10 13.51  2.10 N
+705  1 CB  C LEU 2   ? ? CG  C LEU 2   ? ? CD2 C LEU 2   ? ? 121.77 111.00 10.77  1.70 N
+706  1 CA  C LEU 2   ? ? C   C LEU 2   ? ? O   C LEU 2   ? ? 96.74  120.10 -23.36 2.10 N
+707  1 O   C LEU 2   ? ? C   C LEU 2   ? ? N   C SER 3   ? ? 138.85 122.70 16.15  1.60 Y
+708  1 CB  C SER 3   ? ? CA  C SER 3   ? ? C   C SER 3   ? ? 124.60 110.10 14.50  1.90 N
+709  1 O   C SER 3   ? ? C   C SER 3   ? ? N   C PRO 4   ? ? 106.73 121.10 -14.37 1.90 Y
+710  1 C   C SER 3   ? ? N   C PRO 4   ? ? CA  C PRO 4   ? ? 128.32 119.30 9.02   1.50 Y
+711  1 C   C SER 3   ? ? N   C PRO 4   ? ? CD  C PRO 4   ? ? 110.74 128.40 -17.66 2.10 Y
+712  1 CA  C PRO 4   ? ? C   C PRO 4   ? ? N   C ALA 5   ? ? 102.44 117.20 -14.76 2.20 Y
+713  1 O   C PRO 4   ? ? C   C PRO 4   ? ? N   C ALA 5   ? ? 138.37 122.70 15.67  1.60 Y
+714  1 N   C ALA 5   ? ? CA  C ALA 5   ? ? CB  C ALA 5   ? ? 123.14 110.10 13.04  1.40 N
+715  1 CA  C ALA 5   ? ? C   C ALA 5   ? ? N   C ASP 6   ? ? 103.52 117.20 -13.68 2.20 Y
+716  1 CB  C ASP 6   ? ? CG  C ASP 6   ? ? OD2 C ASP 6   ? ? 112.39 118.30 -5.91  0.90 N
+717  1 CB  C LYS 7   ? ? CA  C LYS 7   ? ? C   C LYS 7   ? ? 126.79 110.40 16.39  2.00 N
+718  1 CD  C LYS 7   ? ? CE  C LYS 7   ? ? NZ  C LYS 7   ? ? 147.18 111.70 35.48  2.30 N
+719  1 CA  C LYS 7   ? ? C   C LYS 7   ? ? O   C LYS 7   ? ? 141.55 120.10 21.45  2.10 N
+720  1 CA  C LYS 7   ? ? C   C LYS 7   ? ? N   C THR 8   ? ? 102.62 117.20 -14.58 2.20 Y
+721  1 CG1 C VAL 10  ? ? CB  C VAL 10  ? ? CG2 C VAL 10  ? ? 100.29 110.90 -10.61 1.60 N
+722  1 O   C VAL 10  ? ? C   C VAL 10  ? ? N   C LYS 11  ? ? 139.86 122.70 17.16  1.60 Y
+723  1 CB  C LYS 11  ? ? CA  C LYS 11  ? ? C   C LYS 11  ? ? 123.13 110.40 12.73  2.00 N
+724  1 CA  C LYS 11  ? ? CB  C LYS 11  ? ? CG  C LYS 11  ? ? 132.50 113.40 19.10  2.20 N
+725  1 O   C LYS 11  ? ? C   C LYS 11  ? ? N   C ALA 12  ? ? 112.92 122.70 -9.78  1.60 Y
+726  1 CB  C ALA 12  ? ? CA  C ALA 12  ? ? C   C ALA 12  ? ? 98.31  110.10 -11.79 1.50 N
+727  1 N   C ALA 12  ? ? CA  C ALA 12  ? ? C   C ALA 12  ? ? 135.37 111.00 24.37  2.70 N
+728  1 CA  C ALA 12  ? ? C   C ALA 12  ? ? O   C ALA 12  ? ? 150.55 120.10 30.45  2.10 N
+729  1 O   C ALA 12  ? ? C   C ALA 12  ? ? N   C ALA 13  ? ? 103.92 122.70 -18.78 1.60 Y
+730  1 CB  C ALA 13  ? ? CA  C ALA 13  ? ? C   C ALA 13  ? ? 119.65 110.10 9.55   1.50 N
+731  1 CD1 C TRP 14  ? ? CG  C TRP 14  ? ? CD2 C TRP 14  ? ? 116.24 106.30 9.94   0.80 N
+732  1 CB  C TRP 14  ? ? CG  C TRP 14  ? ? CD1 C TRP 14  ? ? 110.72 127.00 -16.28 1.30 N
+733  1 CG  C TRP 14  ? ? CD1 C TRP 14  ? ? NE1 C TRP 14  ? ? 89.98  110.10 -20.12 1.00 N
+734  1 CD1 C TRP 14  ? ? NE1 C TRP 14  ? ? CE2 C TRP 14  ? ? 127.89 109.00 18.89  0.90 N
+735  1 NE1 C TRP 14  ? ? CE2 C TRP 14  ? ? CZ2 C TRP 14  ? ? 145.54 130.40 15.14  1.10 N
+736  1 CD2 C TRP 14  ? ? CE2 C TRP 14  ? ? CZ2 C TRP 14  ? ? 110.73 122.30 -11.57 1.20 N
+737  1 CE2 C TRP 14  ? ? CD2 C TRP 14  ? ? CG  C TRP 14  ? ? 101.05 107.30 -6.25  0.80 N
+738  1 CD2 C TRP 14  ? ? CE3 C TRP 14  ? ? CZ3 C TRP 14  ? ? 127.90 118.80 9.10   1.30 N
+739  1 CE3 C TRP 14  ? ? CZ3 C TRP 14  ? ? CH2 C TRP 14  ? ? 102.92 121.20 -18.28 1.10 N
+740  1 CH2 C TRP 14  ? ? CZ2 C TRP 14  ? ? CE2 C TRP 14  ? ? 129.48 117.40 12.08  1.00 N
+741  1 CA  C TRP 14  ? ? C   C TRP 14  ? ? N   C GLY 15  ? ? 137.76 116.20 21.56  2.00 Y
+742  1 O   C TRP 14  ? ? C   C TRP 14  ? ? N   C GLY 15  ? ? 95.90  123.20 -27.30 1.70 Y
+743  1 C   C TRP 14  ? ? N   C GLY 15  ? ? CA  C GLY 15  ? ? 156.60 122.30 34.30  2.10 Y
+744  1 O   C GLY 15  ? ? C   C GLY 15  ? ? N   C LYS 16  ? ? 111.03 122.70 -11.67 1.60 Y
+745  1 C   C GLY 15  ? ? N   C LYS 16  ? ? CA  C LYS 16  ? ? 153.81 121.70 32.11  2.50 Y
+746  1 N   C LYS 16  ? ? CA  C LYS 16  ? ? CB  C LYS 16  ? ? 142.40 110.60 31.80  1.80 N
+747  1 CB  C LYS 16  ? ? CG  C LYS 16  ? ? CD  C LYS 16  ? ? 76.80  111.60 -34.80 2.60 N
+748  1 CD  C LYS 16  ? ? CE  C LYS 16  ? ? NZ  C LYS 16  ? ? 84.96  111.70 -26.74 2.30 N
+749  1 N   C LYS 16  ? ? CA  C LYS 16  ? ? C   C LYS 16  ? ? 93.78  111.00 -17.22 2.70 N
+750  1 CB  C VAL 17  ? ? CA  C VAL 17  ? ? C   C VAL 17  ? ? 126.01 111.40 14.61  1.90 N
+751  1 CG1 C VAL 17  ? ? CB  C VAL 17  ? ? CG2 C VAL 17  ? ? 127.78 110.90 16.88  1.60 N
+752  1 CA  C VAL 17  ? ? C   C VAL 17  ? ? O   C VAL 17  ? ? 134.90 120.10 14.80  2.10 N
+753  1 CA  C VAL 17  ? ? C   C VAL 17  ? ? N   C GLY 18  ? ? 101.25 116.20 -14.95 2.00 Y
+754  1 C   C VAL 17  ? ? N   C GLY 18  ? ? CA  C GLY 18  ? ? 105.42 122.30 -16.88 2.10 Y
+755  1 CA  C GLY 18  ? ? C   C GLY 18  ? ? N   C ALA 19  ? ? 98.27  117.20 -18.93 2.20 Y
+756  1 C   C GLY 18  ? ? N   C ALA 19  ? ? CA  C ALA 19  ? ? 105.74 121.70 -15.96 2.50 Y
+757  1 O   C ALA 19  ? ? C   C ALA 19  ? ? N   C HIS 20  ? ? 102.16 122.70 -20.54 1.60 Y
+758  1 CB  C HIS 20  ? ? CG  C HIS 20  ? ? ND1 C HIS 20  ? ? 95.46  121.40 -25.94 1.30 N
+759  1 CG  C HIS 20  ? ? ND1 C HIS 20  ? ? CE1 C HIS 20  ? ? 89.62  105.70 -16.08 1.30 N
+760  1 ND1 C HIS 20  ? ? CE1 C HIS 20  ? ? NE2 C HIS 20  ? ? 98.37  108.50 -10.13 1.10 N
+761  1 CE1 C HIS 20  ? ? NE2 C HIS 20  ? ? CD2 C HIS 20  ? ? 116.05 109.00 7.05   0.70 N
+762  1 N   C ALA 21  ? ? CA  C ALA 21  ? ? CB  C ALA 21  ? ? 100.69 110.10 -9.41  1.40 N
+763  1 CA  C ALA 21  ? ? C   C ALA 21  ? ? N   C GLY 22  ? ? 128.44 116.20 12.24  2.00 Y
+764  1 CA  C GLY 22  ? ? C   C GLY 22  ? ? N   C GLU 23  ? ? 140.09 117.20 22.89  2.20 Y
+765  1 O   C GLY 22  ? ? C   C GLY 22  ? ? N   C GLU 23  ? ? 95.95  122.70 -26.75 1.60 Y
+766  1 C   C GLY 22  ? ? N   C GLU 23  ? ? CA  C GLU 23  ? ? 142.23 121.70 20.53  2.50 Y
+767  1 CB  C GLU 23  ? ? CG  C GLU 23  ? ? CD  C GLU 23  ? ? 93.48  114.20 -20.72 2.70 N
+768  1 OE1 C GLU 23  ? ? CD  C GLU 23  ? ? OE2 C GLU 23  ? ? 89.06  123.30 -34.24 1.20 N
+769  1 CG  C GLU 23  ? ? CD  C GLU 23  ? ? OE1 C GLU 23  ? ? 78.20  118.30 -40.10 2.00 N
+770  1 CG  C GLU 23  ? ? CD  C GLU 23  ? ? OE2 C GLU 23  ? ? 87.19  118.30 -31.11 2.00 N
+771  1 CB  C TYR 24  ? ? CG  C TYR 24  ? ? CD2 C TYR 24  ? ? 113.61 121.00 -7.39  0.60 N
+772  1 CD1 C TYR 24  ? ? CG  C TYR 24  ? ? CD2 C TYR 24  ? ? 132.59 117.90 14.69  1.10 N
+773  1 CB  C TYR 24  ? ? CG  C TYR 24  ? ? CD1 C TYR 24  ? ? 113.59 121.00 -7.41  0.60 N
+774  1 CG  C TYR 24  ? ? CD1 C TYR 24  ? ? CE1 C TYR 24  ? ? 103.50 121.30 -17.80 0.80 N
+775  1 CG  C TYR 24  ? ? CD2 C TYR 24  ? ? CE2 C TYR 24  ? ? 115.46 121.30 -5.84  0.80 N
+776  1 OH  C TYR 24  ? ? CZ  C TYR 24  ? ? CE2 C TYR 24  ? ? 100.24 120.10 -19.86 2.70 N
+777  1 CE1 C TYR 24  ? ? CZ  C TYR 24  ? ? CE2 C TYR 24  ? ? 144.85 119.80 25.05  1.60 N
+778  1 CZ  C TYR 24  ? ? CE2 C TYR 24  ? ? CD2 C TYR 24  ? ? 102.62 119.80 -17.18 0.90 N
+779  1 CA  C GLY 25  ? ? C   C GLY 25  ? ? N   C ALA 26  ? ? 135.28 117.20 18.08  2.20 Y
+780  1 O   C GLY 25  ? ? C   C GLY 25  ? ? N   C ALA 26  ? ? 100.81 122.70 -21.89 1.60 Y
+781  1 C   C GLY 25  ? ? N   C ALA 26  ? ? CA  C ALA 26  ? ? 136.86 121.70 15.16  2.50 Y
+782  1 CA  C ALA 26  ? ? C   C ALA 26  ? ? O   C ALA 26  ? ? 136.82 120.10 16.72  2.10 N
+783  1 CA  C LEU 29  ? ? C   C LEU 29  ? ? O   C LEU 29  ? ? 134.25 120.10 14.15  2.10 N
+784  1 O   C LEU 29  ? ? C   C LEU 29  ? ? N   C GLU 30  ? ? 105.17 122.70 -17.53 1.60 Y
+785  1 OE1 C GLU 30  ? ? CD  C GLU 30  ? ? OE2 C GLU 30  ? ? 162.05 123.30 38.75  1.20 N
+786  1 CG  C GLU 30  ? ? CD  C GLU 30  ? ? OE1 C GLU 30  ? ? 92.94  118.30 -25.36 2.00 N
+787  1 CG  C GLU 30  ? ? CD  C GLU 30  ? ? OE2 C GLU 30  ? ? 96.74  118.30 -21.56 2.00 N
+788  1 NH1 C ARG 31  ? ? CZ  C ARG 31  ? ? NH2 C ARG 31  ? ? 126.76 119.40 7.36   1.10 N
+789  1 NE  C ARG 31  ? ? CZ  C ARG 31  ? ? NH2 C ARG 31  ? ? 113.95 120.30 -6.35  0.50 N
+790  1 CB  C PHE 33  ? ? CG  C PHE 33  ? ? CD1 C PHE 33  ? ? 111.35 120.80 -9.45  0.70 N
+791  1 CG  C PHE 33  ? ? CD2 C PHE 33  ? ? CE2 C PHE 33  ? ? 107.05 120.80 -13.75 1.10 N
+792  1 CZ  C PHE 33  ? ? CE2 C PHE 33  ? ? CD2 C PHE 33  ? ? 128.35 120.10 8.25   1.20 N
+793  1 CG  C PHE 36  ? ? CD2 C PHE 36  ? ? CE2 C PHE 36  ? ? 111.42 120.80 -9.38  1.10 N
+794  1 C   C PHE 36  ? ? N   C PRO 37  ? ? CD  C PRO 37  ? ? 141.87 128.40 13.47  2.10 Y
+795  1 CA  C PRO 37  ? ? N   C PRO 37  ? ? CD  C PRO 37  ? ? 103.26 111.70 -8.44  1.40 N
+796  1 N   C PRO 37  ? ? CD  C PRO 37  ? ? CG  C PRO 37  ? ? 113.90 103.20 10.70  1.50 N
+797  1 CB  C THR 38  ? ? CA  C THR 38  ? ? C   C THR 38  ? ? 129.50 111.60 17.90  2.70 N
+798  1 N   C THR 38  ? ? CA  C THR 38  ? ? CB  C THR 38  ? ? 98.73  110.30 -11.57 1.90 N
+799  1 OG1 C THR 38  ? ? CB  C THR 38  ? ? CG2 C THR 38  ? ? 56.18  110.00 -53.82 2.30 N
+800  1 CA  C THR 38  ? ? CB  C THR 38  ? ? OG1 C THR 38  ? ? 89.98  109.00 -19.02 2.10 N
+801  1 CA  C THR 38  ? ? CB  C THR 38  ? ? CG2 C THR 38  ? ? 99.08  112.40 -13.32 1.40 N
+802  1 CD  C LYS 40  ? ? CE  C LYS 40  ? ? NZ  C LYS 40  ? ? 94.60  111.70 -17.10 2.30 N
+803  1 CA  C THR 41  ? ? C   C THR 41  ? ? N   C TYR 42  ? ? 141.42 117.20 24.22  2.20 Y
+804  1 O   C THR 41  ? ? C   C THR 41  ? ? N   C TYR 42  ? ? 103.89 122.70 -18.81 1.60 Y
+805  1 CA  C TYR 42  ? ? CB  C TYR 42  ? ? CG  C TYR 42  ? ? 99.10  113.40 -14.30 1.90 N
+806  1 CB  C TYR 42  ? ? CG  C TYR 42  ? ? CD2 C TYR 42  ? ? 124.92 121.00 3.92   0.60 N
+807  1 CD1 C TYR 42  ? ? CE1 C TYR 42  ? ? CZ  C TYR 42  ? ? 126.70 119.80 6.90   0.90 N
+808  1 CB  C PHE 43  ? ? CG  C PHE 43  ? ? CD2 C PHE 43  ? ? 113.84 120.80 -6.96  0.70 N
+809  1 CD1 C PHE 43  ? ? CG  C PHE 43  ? ? CD2 C PHE 43  ? ? 126.16 118.30 7.86   1.30 N
+810  1 CG  C PHE 43  ? ? CD1 C PHE 43  ? ? CE1 C PHE 43  ? ? 112.26 120.80 -8.54  1.10 N
+811  1 CG  C PHE 43  ? ? CD2 C PHE 43  ? ? CE2 C PHE 43  ? ? 105.39 120.80 -15.41 1.10 N
+812  1 CD1 C PHE 43  ? ? CE1 C PHE 43  ? ? CZ  C PHE 43  ? ? 129.62 120.10 9.52   1.20 N
+813  1 CE1 C PHE 43  ? ? CZ  C PHE 43  ? ? CE2 C PHE 43  ? ? 107.68 120.00 -12.32 1.80 N
+814  1 CZ  C PHE 43  ? ? CE2 C PHE 43  ? ? CD2 C PHE 43  ? ? 136.74 120.10 16.64  1.20 N
+815  1 C   C PHE 43  ? ? N   C PRO 44  ? ? CA  C PRO 44  ? ? 109.88 119.30 -9.42  1.50 Y
+816  1 CA  C PRO 44  ? ? N   C PRO 44  ? ? CD  C PRO 44  ? ? 124.30 111.70 12.60  1.40 N
+817  1 N   C PRO 44  ? ? CA  C PRO 44  ? ? CB  C PRO 44  ? ? 90.38  103.30 -12.92 1.20 N
+818  1 N   C PRO 44  ? ? CD  C PRO 44  ? ? CG  C PRO 44  ? ? 92.24  103.20 -10.96 1.50 N
+819  1 CA  C HIS 45  ? ? CB  C HIS 45  ? ? CG  C HIS 45  ? ? 131.99 113.60 18.39  1.70 N
+820  1 CB  C HIS 45  ? ? CG  C HIS 45  ? ? ND1 C HIS 45  ? ? 106.33 121.40 -15.07 1.30 N
+821  1 CG  C HIS 45  ? ? ND1 C HIS 45  ? ? CE1 C HIS 45  ? ? 86.09  105.70 -19.61 1.30 N
+822  1 ND1 C HIS 45  ? ? CE1 C HIS 45  ? ? NE2 C HIS 45  ? ? 134.60 111.50 23.10  1.30 N
+823  1 O   C HIS 45  ? ? C   C HIS 45  ? ? N   C PHE 46  ? ? 137.30 122.70 14.60  1.60 Y
+824  1 CB  C PHE 46  ? ? CG  C PHE 46  ? ? CD2 C PHE 46  ? ? 138.39 120.80 17.59  0.70 N
+825  1 CD1 C PHE 46  ? ? CG  C PHE 46  ? ? CD2 C PHE 46  ? ? 100.92 118.30 -17.38 1.30 N
+826  1 CD1 C PHE 46  ? ? CE1 C PHE 46  ? ? CZ  C PHE 46  ? ? 130.30 120.10 10.20  1.20 N
+827  1 CE1 C PHE 46  ? ? CZ  C PHE 46  ? ? CE2 C PHE 46  ? ? 90.65  120.00 -29.35 1.80 N
+828  1 CZ  C PHE 46  ? ? CE2 C PHE 46  ? ? CD2 C PHE 46  ? ? 147.54 120.10 27.44  1.20 N
+829  1 O   C PHE 46  ? ? C   C PHE 46  ? ? N   C ASP 47  ? ? 102.07 122.70 -20.63 1.60 Y
+830  1 N   C ASP 47  ? ? CA  C ASP 47  ? ? CB  C ASP 47  ? ? 97.88  110.60 -12.72 1.80 N
+831  1 CA  C ASP 47  ? ? CB  C ASP 47  ? ? CG  C ASP 47  ? ? 99.42  113.40 -13.98 2.20 N
+832  1 CB  C ASP 47  ? ? CG  C ASP 47  ? ? OD1 C ASP 47  ? ? 101.99 118.30 -16.31 0.90 N
+833  1 CB  C ASP 47  ? ? CG  C ASP 47  ? ? OD2 C ASP 47  ? ? 100.82 118.30 -17.48 0.90 N
+834  1 CA  C ASP 47  ? ? C   C ASP 47  ? ? N   C LEU 48  ? ? 103.45 117.20 -13.75 2.20 Y
+835  1 CB  C LEU 48  ? ? CG  C LEU 48  ? ? CD1 C LEU 48  ? ? 131.36 111.00 20.36  1.70 N
+836  1 O   C LEU 48  ? ? C   C LEU 48  ? ? N   C SER 49  ? ? 100.97 122.70 -21.73 1.60 Y
+837  1 C   C LEU 48  ? ? N   C SER 49  ? ? CA  C SER 49  ? ? 144.92 121.70 23.22  2.50 Y
+838  1 CB  C SER 49  ? ? CA  C SER 49  ? ? C   C SER 49  ? ? 131.29 110.10 21.19  1.90 N
+839  1 N   C SER 49  ? ? CA  C SER 49  ? ? CB  C SER 49  ? ? 122.41 110.50 11.91  1.50 N
+840  1 N   C SER 49  ? ? CA  C SER 49  ? ? C   C SER 49  ? ? 91.91  111.00 -19.09 2.70 N
+841  1 CA  C SER 49  ? ? C   C SER 49  ? ? O   C SER 49  ? ? 140.28 120.10 20.18  2.10 N
+842  1 O   C SER 49  ? ? C   C SER 49  ? ? N   C HIS 50  ? ? 110.63 122.70 -12.07 1.60 Y
+843  1 CA  C HIS 50  ? ? CB  C HIS 50  ? ? CG  C HIS 50  ? ? 103.09 113.60 -10.51 1.70 N
+844  1 CB  C HIS 50  ? ? CG  C HIS 50  ? ? CD2 C HIS 50  ? ? 156.98 131.40 25.58  1.20 N
+845  1 ND1 C HIS 50  ? ? CG  C HIS 50  ? ? CD2 C HIS 50  ? ? 94.41  106.00 -11.59 1.40 N
+846  1 CB  C HIS 50  ? ? CG  C HIS 50  ? ? ND1 C HIS 50  ? ? 108.47 121.40 -12.93 1.30 N
+847  1 ND1 C HIS 50  ? ? CE1 C HIS 50  ? ? NE2 C HIS 50  ? ? 121.52 111.50 10.02  1.30 N
+848  1 CE1 C HIS 50  ? ? NE2 C HIS 50  ? ? CD2 C HIS 50  ? ? 86.32  106.60 -20.28 2.50 N
+849  1 CG  C HIS 50  ? ? CD2 C HIS 50  ? ? NE2 C HIS 50  ? ? 133.13 109.20 23.93  1.90 N
+850  1 CA  C HIS 50  ? ? C   C HIS 50  ? ? O   C HIS 50  ? ? 106.90 120.10 -13.20 2.10 N
+851  1 O   C HIS 50  ? ? C   C HIS 50  ? ? N   C GLY 51  ? ? 138.12 123.20 14.92  1.70 Y
+852  1 CA  C GLY 51  ? ? C   C GLY 51  ? ? O   C GLY 51  ? ? 133.98 120.60 13.38  1.80 N
+853  1 CA  C SER 52  ? ? C   C SER 52  ? ? N   C ALA 53  ? ? 132.30 117.20 15.10  2.20 Y
+854  1 O   C SER 52  ? ? C   C SER 52  ? ? N   C ALA 53  ? ? 103.09 122.70 -19.61 1.60 Y
+855  1 CB  C ALA 53  ? ? CA  C ALA 53  ? ? C   C ALA 53  ? ? 127.99 110.10 17.89  1.50 N
+856  1 CA  C ALA 53  ? ? C   C ALA 53  ? ? N   C GLN 54  ? ? 97.92  117.20 -19.28 2.20 Y
+857  1 O   C ALA 53  ? ? C   C ALA 53  ? ? N   C GLN 54  ? ? 141.13 122.70 18.43  1.60 Y
+858  1 CA  C GLN 54  ? ? C   C GLN 54  ? ? N   C VAL 55  ? ? 103.56 117.20 -13.64 2.20 Y
+859  1 O   C GLN 54  ? ? C   C GLN 54  ? ? N   C VAL 55  ? ? 135.71 122.70 13.01  1.60 Y
+860  1 CA  C VAL 55  ? ? CB  C VAL 55  ? ? CG1 C VAL 55  ? ? 100.86 110.90 -10.04 1.50 N
+861  1 CB  C LYS 56  ? ? CG  C LYS 56  ? ? CD  C LYS 56  ? ? 86.59  111.60 -25.01 2.60 N
+862  1 CG  C LYS 56  ? ? CD  C LYS 56  ? ? CE  C LYS 56  ? ? 66.36  111.90 -45.54 3.00 N
+863  1 CD  C LYS 56  ? ? CE  C LYS 56  ? ? NZ  C LYS 56  ? ? 74.85  111.70 -36.85 2.30 N
+864  1 CA  C LYS 56  ? ? C   C LYS 56  ? ? O   C LYS 56  ? ? 135.57 120.10 15.47  2.10 N
+865  1 O   C LYS 56  ? ? C   C LYS 56  ? ? N   C GLY 57  ? ? 105.68 123.20 -17.52 1.70 Y
+866  1 CG  C HIS 58  ? ? ND1 C HIS 58  ? ? CE1 C HIS 58  ? ? 93.11  105.70 -12.59 1.30 N
+867  1 ND1 C HIS 58  ? ? CE1 C HIS 58  ? ? NE2 C HIS 58  ? ? 121.88 111.50 10.38  1.30 N
+868  1 CE1 C HIS 58  ? ? NE2 C HIS 58  ? ? CD2 C HIS 58  ? ? 90.60  106.60 -16.00 2.50 N
+869  1 CG  C HIS 58  ? ? CD2 C HIS 58  ? ? NE2 C HIS 58  ? ? 121.04 109.20 11.84  1.90 N
+870  1 O   C HIS 58  ? ? C   C HIS 58  ? ? N   C GLY 59  ? ? 134.61 123.20 11.41  1.70 Y
+871  1 CA  C LYS 60  ? ? CB  C LYS 60  ? ? CG  C LYS 60  ? ? 97.59  113.40 -15.81 2.20 N
+872  1 CD  C LYS 60  ? ? CE  C LYS 60  ? ? NZ  C LYS 60  ? ? 89.51  111.70 -22.19 2.30 N
+873  1 CD  C LYS 61  ? ? CE  C LYS 61  ? ? NZ  C LYS 61  ? ? 74.17  111.70 -37.53 2.30 N
+874  1 O   C LYS 61  ? ? C   C LYS 61  ? ? N   C VAL 62  ? ? 132.93 122.70 10.23  1.60 Y
+875  1 CA  C VAL 62  ? ? C   C VAL 62  ? ? N   C ALA 63  ? ? 98.55  117.20 -18.65 2.20 Y
+876  1 CA  C ALA 63  ? ? C   C ALA 63  ? ? O   C ALA 63  ? ? 136.06 120.10 15.96  2.10 N
+877  1 O   C ALA 63  ? ? C   C ALA 63  ? ? N   C ASP 64  ? ? 105.53 122.70 -17.17 1.60 Y
+878  1 CA  C ASP 64  ? ? CB  C ASP 64  ? ? CG  C ASP 64  ? ? 127.89 113.40 14.49  2.20 N
+879  1 OD1 C ASP 64  ? ? CG  C ASP 64  ? ? OD2 C ASP 64  ? ? 141.55 123.30 18.25  1.90 N
+880  1 CB  C ASP 64  ? ? CG  C ASP 64  ? ? OD1 C ASP 64  ? ? 106.89 118.30 -11.41 0.90 N
+881  1 CB  C ASP 64  ? ? CG  C ASP 64  ? ? OD2 C ASP 64  ? ? 103.45 118.30 -14.85 0.90 N
+882  1 CB  C ALA 65  ? ? CA  C ALA 65  ? ? C   C ALA 65  ? ? 100.70 110.10 -9.40  1.50 N
+883  1 CA  C THR 67  ? ? CB  C THR 67  ? ? CG2 C THR 67  ? ? 101.89 112.40 -10.51 1.40 N
+884  1 CB  C ALA 69  ? ? CA  C ALA 69  ? ? C   C ALA 69  ? ? 119.47 110.10 9.37   1.50 N
+885  1 O   C ALA 69  ? ? C   C ALA 69  ? ? N   C VAL 70  ? ? 136.13 122.70 13.43  1.60 Y
+886  1 CA  C VAL 70  ? ? C   C VAL 70  ? ? O   C VAL 70  ? ? 99.96  120.10 -20.14 2.10 N
+887  1 O   C VAL 70  ? ? C   C VAL 70  ? ? N   C ALA 71  ? ? 142.96 122.70 20.26  1.60 Y
+888  1 CB  C ALA 71  ? ? CA  C ALA 71  ? ? C   C ALA 71  ? ? 133.35 110.10 23.25  1.50 N
+889  1 O   C ALA 71  ? ? C   C ALA 71  ? ? N   C HIS 72  ? ? 99.80  122.70 -22.90 1.60 Y
+890  1 C   C ALA 71  ? ? N   C HIS 72  ? ? CA  C HIS 72  ? ? 146.12 121.70 24.42  2.50 Y
+891  1 CB  C HIS 72  ? ? CG  C HIS 72  ? ? CD2 C HIS 72  ? ? 145.80 131.40 14.40  1.20 N
+892  1 ND1 C HIS 72  ? ? CG  C HIS 72  ? ? CD2 C HIS 72  ? ? 85.54  106.00 -20.46 1.40 N
+893  1 ND1 C HIS 72  ? ? CE1 C HIS 72  ? ? NE2 C HIS 72  ? ? 134.89 111.50 23.39  1.30 N
+894  1 CE1 C HIS 72  ? ? NE2 C HIS 72  ? ? CD2 C HIS 72  ? ? 91.46  106.60 -15.14 2.50 N
+895  1 N   C HIS 72  ? ? CA  C HIS 72  ? ? C   C HIS 72  ? ? 139.60 111.00 28.60  2.70 N
+896  1 CA  C HIS 72  ? ? C   C HIS 72  ? ? O   C HIS 72  ? ? 135.94 120.10 15.84  2.10 N
+897  1 O   C HIS 72  ? ? C   C HIS 72  ? ? N   C VAL 73  ? ? 108.06 122.70 -14.64 1.60 Y
+898  1 CG1 C VAL 73  ? ? CB  C VAL 73  ? ? CG2 C VAL 73  ? ? 145.55 110.90 34.65  1.60 N
+899  1 CA  C VAL 73  ? ? CB  C VAL 73  ? ? CG1 C VAL 73  ? ? 88.89  110.90 -22.01 1.50 N
+900  1 O   C VAL 73  ? ? C   C VAL 73  ? ? N   C ASP 74  ? ? 139.62 122.70 16.92  1.60 Y
+901  1 N   C ASP 74  ? ? CA  C ASP 74  ? ? CB  C ASP 74  ? ? 99.47  110.60 -11.13 1.80 N
+902  1 CA  C ASP 74  ? ? CB  C ASP 74  ? ? CG  C ASP 74  ? ? 131.12 113.40 17.72  2.20 N
+903  1 OD1 C ASP 74  ? ? CG  C ASP 74  ? ? OD2 C ASP 74  ? ? 89.55  123.30 -33.75 1.90 N
+904  1 CB  C ASP 74  ? ? CG  C ASP 74  ? ? OD1 C ASP 74  ? ? 125.02 118.30 6.72   0.90 N
+905  1 CB  C ASP 74  ? ? CG  C ASP 74  ? ? OD2 C ASP 74  ? ? 141.74 118.30 23.44  0.90 N
+906  1 CA  C ASP 74  ? ? C   C ASP 74  ? ? N   C ASP 75  ? ? 101.29 117.20 -15.91 2.20 Y
+907  1 O   C ASP 74  ? ? C   C ASP 74  ? ? N   C ASP 75  ? ? 136.59 122.70 13.89  1.60 Y
+908  1 OD1 C ASP 75  ? ? CG  C ASP 75  ? ? OD2 C ASP 75  ? ? 152.64 123.30 29.34  1.90 N
+909  1 CB  C ASP 75  ? ? CG  C ASP 75  ? ? OD1 C ASP 75  ? ? 111.54 118.30 -6.76  0.90 N
+910  1 CB  C ASP 75  ? ? CG  C ASP 75  ? ? OD2 C ASP 75  ? ? 89.17  118.30 -29.13 0.90 N
+911  1 N   C MET 76  ? ? CA  C MET 76  ? ? CB  C MET 76  ? ? 98.25  110.60 -12.35 1.80 N
+912  1 C   C MET 76  ? ? N   C PRO 77  ? ? CA  C PRO 77  ? ? 109.75 119.30 -9.55  1.50 Y
+913  1 N   C PRO 77  ? ? CA  C PRO 77  ? ? C   C PRO 77  ? ? 135.04 112.10 22.94  2.60 N
+914  1 CA  C PRO 77  ? ? C   C PRO 77  ? ? O   C PRO 77  ? ? 134.83 120.20 14.63  2.40 N
+915  1 O   C PRO 77  ? ? C   C PRO 77  ? ? N   C ASN 78  ? ? 108.51 122.70 -14.19 1.60 Y
+916  1 N   C ASN 78  ? ? CA  C ASN 78  ? ? C   C ASN 78  ? ? 130.00 111.00 19.00  2.70 N
+917  1 CA  C ASN 78  ? ? C   C ASN 78  ? ? O   C ASN 78  ? ? 149.00 120.10 28.90  2.10 N
+918  1 O   C ASN 78  ? ? C   C ASN 78  ? ? N   C ALA 79  ? ? 105.51 122.70 -17.19 1.60 Y
+919  1 CB  C ALA 79  ? ? CA  C ALA 79  ? ? C   C ALA 79  ? ? 95.24  110.10 -14.86 1.50 N
+920  1 CB  C LEU 80  ? ? CG  C LEU 80  ? ? CD2 C LEU 80  ? ? 100.20 111.00 -10.80 1.70 N
+921  1 N   C SER 81  ? ? CA  C SER 81  ? ? CB  C SER 81  ? ? 93.84  110.50 -16.66 1.50 N
+922  1 CA  C SER 81  ? ? CB  C SER 81  ? ? OG  C SER 81  ? ? 88.78  111.20 -22.42 2.70 N
+923  1 CA  C ALA 82  ? ? C   C ALA 82  ? ? O   C ALA 82  ? ? 138.54 120.10 18.44  2.10 N
+924  1 CB  C LEU 83  ? ? CA  C LEU 83  ? ? C   C LEU 83  ? ? 94.59  110.20 -15.61 1.90 N
+925  1 N   C LEU 83  ? ? CA  C LEU 83  ? ? CB  C LEU 83  ? ? 97.00  110.40 -13.40 2.00 N
+926  1 CB  C SER 84  ? ? CA  C SER 84  ? ? C   C SER 84  ? ? 93.58  110.10 -16.52 1.90 N
+927  1 N   C SER 84  ? ? CA  C SER 84  ? ? CB  C SER 84  ? ? 129.28 110.50 18.78  1.50 N
+928  1 CA  C SER 84  ? ? CB  C SER 84  ? ? OG  C SER 84  ? ? 83.72  111.20 -27.48 2.70 N
+929  1 CB  C ASP 85  ? ? CG  C ASP 85  ? ? OD1 C ASP 85  ? ? 132.20 118.30 13.90  0.90 N
+930  1 CB  C ASP 85  ? ? CG  C ASP 85  ? ? OD2 C ASP 85  ? ? 106.71 118.30 -11.59 0.90 N
+931  1 CA  C LEU 86  ? ? C   C LEU 86  ? ? O   C LEU 86  ? ? 139.12 120.10 19.02  2.10 N
+932  1 CA  C LEU 86  ? ? C   C LEU 86  ? ? N   C HIS 87  ? ? 101.78 117.20 -15.42 2.20 Y
+933  1 CE1 C HIS 87  ? ? NE2 C HIS 87  ? ? CD2 C HIS 87  ? ? 117.38 109.00 8.38   0.70 N
+934  1 O   C HIS 87  ? ? C   C HIS 87  ? ? N   C ALA 88  ? ? 136.97 122.70 14.27  1.60 Y
+935  1 CB  C HIS 89  ? ? CG  C HIS 89  ? ? CD2 C HIS 89  ? ? 113.85 129.70 -15.85 1.60 N
+936  1 CG  C HIS 89  ? ? ND1 C HIS 89  ? ? CE1 C HIS 89  ? ? 90.55  105.70 -15.15 1.30 N
+937  1 ND1 C HIS 89  ? ? CE1 C HIS 89  ? ? NE2 C HIS 89  ? ? 133.90 111.50 22.40  1.30 N
+938  1 N   C LYS 90  ? ? CA  C LYS 90  ? ? CB  C LYS 90  ? ? 128.00 110.60 17.40  1.80 N
+939  1 CB  C LYS 90  ? ? CG  C LYS 90  ? ? CD  C LYS 90  ? ? 86.42  111.60 -25.18 2.60 N
+940  1 CG  C LYS 90  ? ? CD  C LYS 90  ? ? CE  C LYS 90  ? ? 87.59  111.90 -24.31 3.00 N
+941  1 CD  C LYS 90  ? ? CE  C LYS 90  ? ? NZ  C LYS 90  ? ? 86.07  111.70 -25.63 2.30 N
+942  1 N   C LEU 91  ? ? CA  C LEU 91  ? ? CB  C LEU 91  ? ? 97.68  110.40 -12.72 2.00 N
+943  1 CD  C ARG 92  ? ? NE  C ARG 92  ? ? CZ  C ARG 92  ? ? 75.38  123.60 -48.22 1.40 N
+944  1 NE  C ARG 92  ? ? CZ  C ARG 92  ? ? NH1 C ARG 92  ? ? 92.19  120.30 -28.11 0.50 N
+945  1 NE  C ARG 92  ? ? CZ  C ARG 92  ? ? NH2 C ARG 92  ? ? 37.43  120.30 -82.87 0.50 N
+946  1 CB  C ASP 94  ? ? CG  C ASP 94  ? ? OD1 C ASP 94  ? ? 124.68 118.30 6.38   0.90 N
+947  1 CB  C ASP 94  ? ? CG  C ASP 94  ? ? OD2 C ASP 94  ? ? 109.91 118.30 -8.39  0.90 N
+948  1 CA  C PRO 95  ? ? C   C PRO 95  ? ? N   C VAL 96  ? ? 135.44 117.20 18.24  2.20 Y
+949  1 O   C PRO 95  ? ? C   C PRO 95  ? ? N   C VAL 96  ? ? 110.78 122.70 -11.92 1.60 Y
+950  1 CA  C VAL 96  ? ? CB  C VAL 96  ? ? CG1 C VAL 96  ? ? 101.27 110.90 -9.63  1.50 N
+951  1 CA  C VAL 96  ? ? CB  C VAL 96  ? ? CG2 C VAL 96  ? ? 125.02 110.90 14.12  1.50 N
+952  1 CB  C PHE 98  ? ? CG  C PHE 98  ? ? CD1 C PHE 98  ? ? 116.36 120.80 -4.44  0.70 N
+953  1 CG  C PHE 98  ? ? CD2 C PHE 98  ? ? CE2 C PHE 98  ? ? 107.96 120.80 -12.84 1.10 N
+954  1 CE1 C PHE 98  ? ? CZ  C PHE 98  ? ? CE2 C PHE 98  ? ? 105.78 120.00 -14.22 1.80 N
+955  1 CZ  C PHE 98  ? ? CE2 C PHE 98  ? ? CD2 C PHE 98  ? ? 137.66 120.10 17.56  1.20 N
+956  1 CA  C LYS 99  ? ? CB  C LYS 99  ? ? CG  C LYS 99  ? ? 128.62 113.40 15.22  2.20 N
+957  1 CB  C LYS 99  ? ? CG  C LYS 99  ? ? CD  C LYS 99  ? ? 129.76 111.60 18.16  2.60 N
+958  1 CG  C LYS 99  ? ? CD  C LYS 99  ? ? CE  C LYS 99  ? ? 89.26  111.90 -22.64 3.00 N
+959  1 CA  C LYS 99  ? ? C   C LYS 99  ? ? N   C LEU 100 ? ? 101.01 117.20 -16.19 2.20 Y
+960  1 CB  C LEU 100 ? ? CA  C LEU 100 ? ? C   C LEU 100 ? ? 121.89 110.20 11.69  1.90 N
+961  1 CG  C HIS 103 ? ? ND1 C HIS 103 ? ? CE1 C HIS 103 ? ? 93.55  105.70 -12.15 1.30 N
+962  1 ND1 C HIS 103 ? ? CE1 C HIS 103 ? ? NE2 C HIS 103 ? ? 123.21 111.50 11.71  1.30 N
+963  1 O   C HIS 103 ? ? C   C HIS 103 ? ? N   C CYS 104 ? ? 112.60 122.70 -10.10 1.60 Y
+964  1 CD1 C LEU 105 ? ? CG  C LEU 105 ? ? CD2 C LEU 105 ? ? 82.32  110.50 -28.18 3.00 N
+965  1 CB  C LEU 105 ? ? CG  C LEU 105 ? ? CD2 C LEU 105 ? ? 90.12  111.00 -20.88 1.70 N
+966  1 C   C LEU 106 ? ? N   C VAL 107 ? ? CA  C VAL 107 ? ? 140.49 121.70 18.79  2.50 Y
+967  1 N   C VAL 107 ? ? CA  C VAL 107 ? ? CB  C VAL 107 ? ? 125.61 111.50 14.11  2.20 N
+968  1 CA  C VAL 107 ? ? C   C VAL 107 ? ? O   C VAL 107 ? ? 134.58 120.10 14.48  2.10 N
+969  1 O   C VAL 107 ? ? C   C VAL 107 ? ? N   C THR 108 ? ? 110.92 122.70 -11.78 1.60 Y
+970  1 CB  C LEU 109 ? ? CA  C LEU 109 ? ? C   C LEU 109 ? ? 128.23 110.20 18.03  1.90 N
+971  1 CD1 C LEU 109 ? ? CG  C LEU 109 ? ? CD2 C LEU 109 ? ? 129.40 110.50 18.90  3.00 N
+972  1 CB  C ALA 110 ? ? CA  C ALA 110 ? ? C   C ALA 110 ? ? 121.33 110.10 11.23  1.50 N
+973  1 O   C ALA 110 ? ? C   C ALA 110 ? ? N   C ALA 111 ? ? 110.16 122.70 -12.54 1.60 Y
+974  1 CA  C HIS 112 ? ? CB  C HIS 112 ? ? CG  C HIS 112 ? ? 102.81 113.60 -10.79 1.70 N
+975  1 CB  C HIS 112 ? ? CG  C HIS 112 ? ? CD2 C HIS 112 ? ? 144.61 131.40 13.21  1.20 N
+976  1 ND1 C HIS 112 ? ? CG  C HIS 112 ? ? CD2 C HIS 112 ? ? 89.66  106.00 -16.34 1.40 N
+977  1 CG  C HIS 112 ? ? CD2 C HIS 112 ? ? NE2 C HIS 112 ? ? 122.43 109.20 13.23  1.90 N
+978  1 CA  C HIS 112 ? ? C   C HIS 112 ? ? N   C LEU 113 ? ? 136.42 117.20 19.22  2.20 Y
+979  1 O   C HIS 112 ? ? C   C HIS 112 ? ? N   C LEU 113 ? ? 107.95 122.70 -14.75 1.60 Y
+980  1 C   C HIS 112 ? ? N   C LEU 113 ? ? CA  C LEU 113 ? ? 144.26 121.70 22.56  2.50 Y
+981  1 CB  C LEU 113 ? ? CG  C LEU 113 ? ? CD1 C LEU 113 ? ? 89.44  111.00 -21.56 1.70 N
+982  1 CB  C LEU 113 ? ? CG  C LEU 113 ? ? CD2 C LEU 113 ? ? 131.66 111.00 20.66  1.70 N
+983  1 CA  C LEU 113 ? ? C   C LEU 113 ? ? O   C LEU 113 ? ? 98.07  120.10 -22.03 2.10 N
+984  1 C   C LEU 113 ? ? N   C PRO 114 ? ? CA  C PRO 114 ? ? 134.97 119.30 15.67  1.50 Y
+985  1 CB  C PRO 114 ? ? CA  C PRO 114 ? ? C   C PRO 114 ? ? 140.45 111.70 28.75  2.10 N
+986  1 N   C PRO 114 ? ? CD  C PRO 114 ? ? CG  C PRO 114 ? ? 90.46  103.20 -12.74 1.50 N
+987  1 N   C PRO 114 ? ? CA  C PRO 114 ? ? C   C PRO 114 ? ? 91.63  112.10 -20.47 2.60 N
+988  1 O   C PRO 114 ? ? C   C PRO 114 ? ? N   C ALA 115 ? ? 103.75 122.70 -18.95 1.60 Y
+989  1 N   C ALA 115 ? ? CA  C ALA 115 ? ? CB  C ALA 115 ? ? 120.96 110.10 10.86  1.40 N
+990  1 O   C ALA 115 ? ? C   C ALA 115 ? ? N   C GLU 116 ? ? 105.22 122.70 -17.48 1.60 Y
+991  1 CB  C GLU 116 ? ? CA  C GLU 116 ? ? C   C GLU 116 ? ? 89.56  110.40 -20.84 2.00 N
+992  1 CB  C GLU 116 ? ? CG  C GLU 116 ? ? CD  C GLU 116 ? ? 81.86  114.20 -32.34 2.70 N
+993  1 CG  C GLU 116 ? ? CD  C GLU 116 ? ? OE1 C GLU 116 ? ? 142.07 118.30 23.77  2.00 N
+994  1 CG  C GLU 116 ? ? CD  C GLU 116 ? ? OE2 C GLU 116 ? ? 82.79  118.30 -35.51 2.00 N
+995  1 CB  C PHE 117 ? ? CG  C PHE 117 ? ? CD2 C PHE 117 ? ? 127.07 120.80 6.27   0.70 N
+996  1 CG  C PHE 117 ? ? CD2 C PHE 117 ? ? CE2 C PHE 117 ? ? 129.80 120.80 9.00   1.10 N
+997  1 CE1 C PHE 117 ? ? CZ  C PHE 117 ? ? CE2 C PHE 117 ? ? 132.90 120.00 12.90  1.80 N
+998  1 CZ  C PHE 117 ? ? CE2 C PHE 117 ? ? CD2 C PHE 117 ? ? 110.45 120.10 -9.65  1.20 N
+999  1 N   C THR 118 ? ? CA  C THR 118 ? ? CB  C THR 118 ? ? 96.88  110.30 -13.42 1.90 N
+1000 1 CA  C THR 118 ? ? CB  C THR 118 ? ? CG2 C THR 118 ? ? 128.13 112.40 15.73  1.40 N
+1001 1 O   C THR 118 ? ? C   C THR 118 ? ? N   C PRO 119 ? ? 133.03 121.10 11.93  1.90 Y
+1002 1 CB  C HIS 122 ? ? CA  C HIS 122 ? ? C   C HIS 122 ? ? 122.69 110.40 12.29  2.00 N
+1003 1 O   C SER 124 ? ? C   C SER 124 ? ? N   C LEU 125 ? ? 136.19 122.70 13.49  1.60 Y
+1004 1 CB  C ASP 126 ? ? CG  C ASP 126 ? ? OD1 C ASP 126 ? ? 107.11 118.30 -11.19 0.90 N
+1005 1 CB  C PHE 128 ? ? CG  C PHE 128 ? ? CD2 C PHE 128 ? ? 106.66 120.80 -14.14 0.70 N
+1006 1 CD1 C PHE 128 ? ? CG  C PHE 128 ? ? CD2 C PHE 128 ? ? 142.71 118.30 24.41  1.30 N
+1007 1 CB  C PHE 128 ? ? CG  C PHE 128 ? ? CD1 C PHE 128 ? ? 110.55 120.80 -10.25 0.70 N
+1008 1 CG  C PHE 128 ? ? CD1 C PHE 128 ? ? CE1 C PHE 128 ? ? 100.79 120.80 -20.01 1.10 N
+1009 1 CG  C PHE 128 ? ? CD2 C PHE 128 ? ? CE2 C PHE 128 ? ? 103.15 120.80 -17.65 1.10 N
+1010 1 CD1 C PHE 128 ? ? CE1 C PHE 128 ? ? CZ  C PHE 128 ? ? 130.66 120.10 10.56  1.20 N
+1011 1 O   C PHE 128 ? ? C   C PHE 128 ? ? N   C LEU 129 ? ? 133.62 122.70 10.92  1.60 Y
+1012 1 O   C LEU 129 ? ? C   C LEU 129 ? ? N   C ALA 130 ? ? 111.51 122.70 -11.19 1.60 Y
+1013 1 N   C ALA 130 ? ? CA  C ALA 130 ? ? CB  C ALA 130 ? ? 119.39 110.10 9.29   1.40 N
+1014 1 CB  C SER 131 ? ? CA  C SER 131 ? ? C   C SER 131 ? ? 97.25  110.10 -12.85 1.90 N
+1015 1 CA  C SER 131 ? ? C   C SER 131 ? ? O   C SER 131 ? ? 100.97 120.10 -19.13 2.10 N
+1016 1 O   C SER 131 ? ? C   C SER 131 ? ? N   C VAL 132 ? ? 138.73 122.70 16.03  1.60 Y
+1017 1 N   C SER 133 ? ? CA  C SER 133 ? ? CB  C SER 133 ? ? 120.04 110.50 9.54   1.50 N
+1018 1 OG1 C THR 137 ? ? CB  C THR 137 ? ? CG2 C THR 137 ? ? 129.84 110.00 19.84  2.30 N
+1019 1 CA  C THR 137 ? ? CB  C THR 137 ? ? CG2 C THR 137 ? ? 101.94 112.40 -10.46 1.40 N
+1020 1 CB  C SER 138 ? ? CA  C SER 138 ? ? C   C SER 138 ? ? 98.61  110.10 -11.49 1.90 N
+1021 1 N   C SER 138 ? ? CA  C SER 138 ? ? CB  C SER 138 ? ? 96.22  110.50 -14.28 1.50 N
+1022 1 CA  C SER 138 ? ? CB  C SER 138 ? ? OG  C SER 138 ? ? 53.75  111.20 -57.45 2.70 N
+1023 1 CA  C SER 138 ? ? C   C SER 138 ? ? O   C SER 138 ? ? 103.08 120.10 -17.02 2.10 N
+1024 1 O   C SER 138 ? ? C   C SER 138 ? ? N   C LYS 139 ? ? 137.89 122.70 15.19  1.60 Y
+1025 1 CA  C LYS 139 ? ? CB  C LYS 139 ? ? CG  C LYS 139 ? ? 99.02  113.40 -14.38 2.20 N
+1026 1 CD  C LYS 139 ? ? CE  C LYS 139 ? ? NZ  C LYS 139 ? ? 73.58  111.70 -38.12 2.30 N
+1027 1 CD1 C TYR 140 ? ? CG  C TYR 140 ? ? CD2 C TYR 140 ? ? 110.66 117.90 -7.24  1.10 N
+1028 1 CB  C TYR 140 ? ? CG  C TYR 140 ? ? CD1 C TYR 140 ? ? 128.75 121.00 7.75   0.60 N
+1029 1 O   C TYR 140 ? ? C   C TYR 140 ? ? N   C ARG 141 ? ? 133.11 122.70 10.41  1.60 Y
+1030 1 CB  C ARG 141 ? ? CG  C ARG 141 ? ? CD  C ARG 141 ? ? 95.55  111.60 -16.05 2.60 N
+1031 1 CG  C ARG 141 ? ? CD  C ARG 141 ? ? NE  C ARG 141 ? ? 97.56  111.80 -14.24 2.10 N
+1032 1 NH1 C ARG 141 ? ? CZ  C ARG 141 ? ? NH2 C ARG 141 ? ? 127.53 119.40 8.13   1.10 N
+1033 1 NE  C ARG 141 ? ? CZ  C ARG 141 ? ? NH2 C ARG 141 ? ? 103.00 120.30 -17.30 0.50 N
+1034 1 CA  C ARG 141 ? ? C   C ARG 141 ? ? O   C ARG 141 ? ? 103.04 120.10 -17.06 2.10 N
+1035 1 CB  D VAL 1   ? ? CA  D VAL 1   ? ? C   D VAL 1   ? ? 98.02  111.40 -13.38 1.90 N
+1036 1 CG1 D VAL 1   ? ? CB  D VAL 1   ? ? CG2 D VAL 1   ? ? 100.34 110.90 -10.56 1.60 N
+1037 1 CA  D VAL 1   ? ? C   D VAL 1   ? ? O   D VAL 1   ? ? 100.55 120.10 -19.55 2.10 N
+1038 1 CA  D VAL 1   ? ? C   D VAL 1   ? ? N   D HIS 2   ? ? 84.06  117.20 -33.14 2.20 Y
+1039 1 O   D VAL 1   ? ? C   D VAL 1   ? ? N   D HIS 2   ? ? 146.46 122.70 23.76  1.60 Y
+1040 1 C   D VAL 1   ? ? N   D HIS 2   ? ? CA  D HIS 2   ? ? 106.40 121.70 -15.30 2.50 Y
+1041 1 CB  D HIS 2   ? ? CA  D HIS 2   ? ? C   D HIS 2   ? ? 126.69 110.40 16.29  2.00 N
+1042 1 CB  D HIS 2   ? ? CG  D HIS 2   ? ? CD2 D HIS 2   ? ? 167.99 131.40 36.59  1.20 N
+1043 1 ND1 D HIS 2   ? ? CG  D HIS 2   ? ? CD2 D HIS 2   ? ? 94.29  106.00 -11.71 1.40 N
+1044 1 CB  D HIS 2   ? ? CG  D HIS 2   ? ? ND1 D HIS 2   ? ? 94.33  121.40 -27.07 1.30 N
+1045 1 ND1 D HIS 2   ? ? CE1 D HIS 2   ? ? NE2 D HIS 2   ? ? 85.03  108.50 -23.47 1.10 N
+1046 1 CE1 D HIS 2   ? ? NE2 D HIS 2   ? ? CD2 D HIS 2   ? ? 145.24 109.00 36.24  0.70 N
+1047 1 N   D HIS 2   ? ? CA  D HIS 2   ? ? C   D HIS 2   ? ? 130.99 111.00 19.99  2.70 N
+1048 1 CA  D HIS 2   ? ? C   D HIS 2   ? ? O   D HIS 2   ? ? 95.47  120.10 -24.63 2.10 N
+1049 1 O   D HIS 2   ? ? C   D HIS 2   ? ? N   D LEU 3   ? ? 144.14 122.70 21.44  1.60 Y
+1050 1 C   D HIS 2   ? ? N   D LEU 3   ? ? CA  D LEU 3   ? ? 99.56  121.70 -22.14 2.50 Y
+1051 1 N   D LEU 3   ? ? CA  D LEU 3   ? ? CB  D LEU 3   ? ? 131.21 110.40 20.81  2.00 N
+1052 1 CA  D LEU 3   ? ? CB  D LEU 3   ? ? CG  D LEU 3   ? ? 92.04  115.30 -23.26 2.30 N
+1053 1 CD1 D LEU 3   ? ? CG  D LEU 3   ? ? CD2 D LEU 3   ? ? 87.52  110.50 -22.98 3.00 N
+1054 1 CB  D LEU 3   ? ? CG  D LEU 3   ? ? CD1 D LEU 3   ? ? 98.99  111.00 -12.01 1.70 N
+1055 1 N   D LEU 3   ? ? CA  D LEU 3   ? ? C   D LEU 3   ? ? 82.71  111.00 -28.29 2.70 N
+1056 1 CA  D LEU 3   ? ? C   D LEU 3   ? ? O   D LEU 3   ? ? 98.05  120.10 -22.05 2.10 N
+1057 1 O   D LEU 3   ? ? C   D LEU 3   ? ? N   D THR 4   ? ? 76.00  122.70 -46.70 1.60 Y
+1058 1 C   D LEU 3   ? ? N   D THR 4   ? ? CA  D THR 4   ? ? 143.80 121.70 22.10  2.50 Y
+1059 1 OG1 D THR 4   ? ? CB  D THR 4   ? ? CG2 D THR 4   ? ? 125.56 110.00 15.56  2.30 N
+1060 1 CA  D THR 4   ? ? C   D THR 4   ? ? O   D THR 4   ? ? 95.46  120.10 -24.64 2.10 N
+1061 1 CA  D THR 4   ? ? C   D THR 4   ? ? N   D PRO 5   ? ? 134.66 117.10 17.56  2.80 Y
+1062 1 C   D THR 4   ? ? N   D PRO 5   ? ? CA  D PRO 5   ? ? 103.81 119.30 -15.49 1.50 Y
+1063 1 CB  D PRO 5   ? ? CA  D PRO 5   ? ? C   D PRO 5   ? ? 86.78  111.70 -24.92 2.10 N
+1064 1 N   D PRO 5   ? ? CA  D PRO 5   ? ? CB  D PRO 5   ? ? 76.49  103.30 -26.81 1.20 N
+1065 1 O   D PRO 5   ? ? C   D PRO 5   ? ? N   D GLU 6   ? ? 111.05 122.70 -11.65 1.60 Y
+1066 1 CB  D GLU 6   ? ? CA  D GLU 6   ? ? C   D GLU 6   ? ? 87.32  110.40 -23.08 2.00 N
+1067 1 N   D GLU 6   ? ? CA  D GLU 6   ? ? CB  D GLU 6   ? ? 124.93 110.60 14.33  1.80 N
+1068 1 OE1 D GLU 6   ? ? CD  D GLU 6   ? ? OE2 D GLU 6   ? ? 43.74  123.30 -79.56 1.20 N
+1069 1 CG  D GLU 6   ? ? CD  D GLU 6   ? ? OE2 D GLU 6   ? ? 87.51  118.30 -30.79 2.00 N
+1070 1 N   D GLU 6   ? ? CA  D GLU 6   ? ? C   D GLU 6   ? ? 94.16  111.00 -16.84 2.70 N
+1071 1 CA  D GLU 6   ? ? C   D GLU 6   ? ? O   D GLU 6   ? ? 99.25  120.10 -20.85 2.10 N
+1072 1 CA  D GLU 6   ? ? C   D GLU 6   ? ? N   D GLU 7   ? ? 99.10  117.20 -18.10 2.20 Y
+1073 1 O   D GLU 6   ? ? C   D GLU 6   ? ? N   D GLU 7   ? ? 158.66 122.70 35.96  1.60 Y
+1074 1 C   D GLU 6   ? ? N   D GLU 7   ? ? CA  D GLU 7   ? ? 103.43 121.70 -18.27 2.50 Y
+1075 1 CA  D GLU 7   ? ? CB  D GLU 7   ? ? CG  D GLU 7   ? ? 100.08 113.40 -13.32 2.20 N
+1076 1 CB  D GLU 7   ? ? CG  D GLU 7   ? ? CD  D GLU 7   ? ? 97.61  114.20 -16.59 2.70 N
+1077 1 OE1 D GLU 7   ? ? CD  D GLU 7   ? ? OE2 D GLU 7   ? ? 113.31 123.30 -9.99  1.20 N
+1078 1 CG  D GLU 7   ? ? CD  D GLU 7   ? ? OE1 D GLU 7   ? ? 92.96  118.30 -25.34 2.00 N
+1079 1 CG  D GLU 7   ? ? CD  D GLU 7   ? ? OE2 D GLU 7   ? ? 143.31 118.30 25.01  2.00 N
+1080 1 CA  D GLU 7   ? ? C   D GLU 7   ? ? O   D GLU 7   ? ? 104.92 120.10 -15.18 2.10 N
+1081 1 O   D GLU 7   ? ? C   D GLU 7   ? ? N   D LYS 8   ? ? 139.67 122.70 16.97  1.60 Y
+1082 1 N   D LYS 8   ? ? CA  D LYS 8   ? ? CB  D LYS 8   ? ? 92.44  110.60 -18.16 1.80 N
+1083 1 CA  D LYS 8   ? ? CB  D LYS 8   ? ? CG  D LYS 8   ? ? 77.90  113.40 -35.50 2.20 N
+1084 1 CA  D LYS 8   ? ? C   D LYS 8   ? ? O   D LYS 8   ? ? 133.86 120.10 13.76  2.10 N
+1085 1 O   D LYS 8   ? ? C   D LYS 8   ? ? N   D SER 9   ? ? 101.25 122.70 -21.45 1.60 Y
+1086 1 CA  D SER 9   ? ? CB  D SER 9   ? ? OG  D SER 9   ? ? 133.20 111.20 22.00  2.70 N
+1087 1 O   D SER 9   ? ? C   D SER 9   ? ? N   D ALA 10  ? ? 139.76 122.70 17.06  1.60 Y
+1088 1 C   D SER 9   ? ? N   D ALA 10  ? ? CA  D ALA 10  ? ? 102.20 121.70 -19.50 2.50 Y
+1089 1 CB  D ALA 10  ? ? CA  D ALA 10  ? ? C   D ALA 10  ? ? 90.12  110.10 -19.98 1.50 N
+1090 1 N   D ALA 10  ? ? CA  D ALA 10  ? ? CB  D ALA 10  ? ? 97.36  110.10 -12.74 1.40 N
+1091 1 O   D VAL 11  ? ? C   D VAL 11  ? ? N   D THR 12  ? ? 138.50 122.70 15.80  1.60 Y
+1092 1 N   D THR 12  ? ? CA  D THR 12  ? ? CB  D THR 12  ? ? 98.76  110.30 -11.54 1.90 N
+1093 1 CA  D THR 12  ? ? CB  D THR 12  ? ? OG1 D THR 12  ? ? 87.15  109.00 -21.85 2.10 N
+1094 1 CA  D THR 12  ? ? CB  D THR 12  ? ? CG2 D THR 12  ? ? 90.35  112.40 -22.05 1.40 N
+1095 1 O   D THR 12  ? ? C   D THR 12  ? ? N   D ALA 13  ? ? 105.18 122.70 -17.52 1.60 Y
+1096 1 N   D ALA 13  ? ? CA  D ALA 13  ? ? CB  D ALA 13  ? ? 132.46 110.10 22.36  1.40 N
+1097 1 CA  D ALA 13  ? ? C   D ALA 13  ? ? O   D ALA 13  ? ? 134.81 120.10 14.71  2.10 N
+1098 1 CA  D ALA 13  ? ? C   D ALA 13  ? ? N   D LEU 14  ? ? 102.72 117.20 -14.48 2.20 Y
+1099 1 CB  D LEU 14  ? ? CG  D LEU 14  ? ? CD1 D LEU 14  ? ? 94.01  111.00 -16.99 1.70 N
+1100 1 O   D LEU 14  ? ? C   D LEU 14  ? ? N   D TRP 15  ? ? 133.64 122.70 10.94  1.60 Y
+1101 1 NE1 D TRP 15  ? ? CE2 D TRP 15  ? ? CZ2 D TRP 15  ? ? 139.03 130.40 8.63   1.10 N
+1102 1 NE1 D TRP 15  ? ? CE2 D TRP 15  ? ? CD2 D TRP 15  ? ? 101.18 107.30 -6.12  1.00 N
+1103 1 CZ3 D TRP 15  ? ? CH2 D TRP 15  ? ? CZ2 D TRP 15  ? ? 129.34 121.60 7.74   1.20 N
+1104 1 CA  D GLY 16  ? ? C   D GLY 16  ? ? N   D LYS 17  ? ? 136.28 117.20 19.08  2.20 Y
+1105 1 O   D GLY 16  ? ? C   D GLY 16  ? ? N   D LYS 17  ? ? 109.80 122.70 -12.90 1.60 Y
+1106 1 C   D GLY 16  ? ? N   D LYS 17  ? ? CA  D LYS 17  ? ? 144.90 121.70 23.20  2.50 Y
+1107 1 N   D LYS 17  ? ? CA  D LYS 17  ? ? CB  D LYS 17  ? ? 121.44 110.60 10.84  1.80 N
+1108 1 CB  D LYS 17  ? ? CG  D LYS 17  ? ? CD  D LYS 17  ? ? 92.29  111.60 -19.31 2.60 N
+1109 1 CG  D LYS 17  ? ? CD  D LYS 17  ? ? CE  D LYS 17  ? ? 135.55 111.90 23.65  3.00 N
+1110 1 CD  D LYS 17  ? ? CE  D LYS 17  ? ? NZ  D LYS 17  ? ? 91.08  111.70 -20.62 2.30 N
+1111 1 CA  D LYS 17  ? ? C   D LYS 17  ? ? O   D LYS 17  ? ? 156.50 120.10 36.40  2.10 N
+1112 1 O   D LYS 17  ? ? C   D LYS 17  ? ? N   D VAL 18  ? ? 88.00  122.70 -34.70 1.60 Y
+1113 1 CG1 D VAL 18  ? ? CB  D VAL 18  ? ? CG2 D VAL 18  ? ? 100.71 110.90 -10.19 1.60 N
+1114 1 CA  D VAL 18  ? ? CB  D VAL 18  ? ? CG1 D VAL 18  ? ? 127.43 110.90 16.53  1.50 N
+1115 1 CA  D VAL 18  ? ? C   D VAL 18  ? ? O   D VAL 18  ? ? 100.12 120.10 -19.98 2.10 N
+1116 1 O   D VAL 18  ? ? C   D VAL 18  ? ? N   D ASN 19  ? ? 149.56 122.70 26.86  1.60 Y
+1117 1 CB  D ASN 19  ? ? CA  D ASN 19  ? ? C   D ASN 19  ? ? 123.78 110.40 13.38  2.00 N
+1118 1 OD1 D ASN 19  ? ? CG  D ASN 19  ? ? ND2 D ASN 19  ? ? 78.71  121.90 -43.19 2.30 N
+1119 1 CB  D ASN 19  ? ? CG  D ASN 19  ? ? OD1 D ASN 19  ? ? 102.65 121.60 -18.95 2.00 N
+1120 1 CB  D ASN 19  ? ? CG  D ASN 19  ? ? ND2 D ASN 19  ? ? 100.13 116.70 -16.57 2.40 N
+1121 1 CA  D ASN 19  ? ? C   D ASN 19  ? ? O   D ASN 19  ? ? 107.20 120.10 -12.90 2.10 N
+1122 1 CA  D ASN 19  ? ? C   D ASN 19  ? ? N   D VAL 20  ? ? 139.55 117.20 22.35  2.20 Y
+1123 1 CB  D VAL 20  ? ? CA  D VAL 20  ? ? C   D VAL 20  ? ? 126.87 111.40 15.47  1.90 N
+1124 1 CG1 D VAL 20  ? ? CB  D VAL 20  ? ? CG2 D VAL 20  ? ? 162.83 110.90 51.93  1.60 N
+1125 1 CA  D VAL 20  ? ? CB  D VAL 20  ? ? CG1 D VAL 20  ? ? 93.21  110.90 -17.69 1.50 N
+1126 1 CA  D VAL 20  ? ? CB  D VAL 20  ? ? CG2 D VAL 20  ? ? 71.55  110.90 -39.35 1.50 N
+1127 1 CA  D VAL 20  ? ? C   D VAL 20  ? ? O   D VAL 20  ? ? 149.04 120.10 28.94  2.10 N
+1128 1 O   D VAL 20  ? ? C   D VAL 20  ? ? N   D ASP 21  ? ? 102.51 122.70 -20.19 1.60 Y
+1129 1 OD1 D ASP 21  ? ? CG  D ASP 21  ? ? OD2 D ASP 21  ? ? 102.49 123.30 -20.81 1.90 N
+1130 1 CB  D ASP 21  ? ? CG  D ASP 21  ? ? OD1 D ASP 21  ? ? 127.62 118.30 9.32   0.90 N
+1131 1 CB  D ASP 21  ? ? CG  D ASP 21  ? ? OD2 D ASP 21  ? ? 107.81 118.30 -10.49 0.90 N
+1132 1 N   D ASP 21  ? ? CA  D ASP 21  ? ? C   D ASP 21  ? ? 142.79 111.00 31.79  2.70 N
+1133 1 O   D ASP 21  ? ? C   D ASP 21  ? ? N   D GLU 22  ? ? 108.45 122.70 -14.25 1.60 Y
+1134 1 CG  D GLU 22  ? ? CD  D GLU 22  ? ? OE2 D GLU 22  ? ? 91.72  118.30 -26.58 2.00 N
+1135 1 CG1 D VAL 23  ? ? CB  D VAL 23  ? ? CG2 D VAL 23  ? ? 121.43 110.90 10.53  1.60 N
+1136 1 CA  D VAL 23  ? ? CB  D VAL 23  ? ? CG2 D VAL 23  ? ? 97.04  110.90 -13.86 1.50 N
+1137 1 CA  D GLY 24  ? ? C   D GLY 24  ? ? N   D GLY 25  ? ? 128.95 116.20 12.75  2.00 Y
+1138 1 O   D GLY 24  ? ? C   D GLY 24  ? ? N   D GLY 25  ? ? 102.30 123.20 -20.90 1.70 Y
+1139 1 C   D GLY 24  ? ? N   D GLY 25  ? ? CA  D GLY 25  ? ? 135.25 122.30 12.95  2.10 Y
+1140 1 CB  D GLU 26  ? ? CG  D GLU 26  ? ? CD  D GLU 26  ? ? 46.05  114.20 -68.15 2.70 N
+1141 1 OE1 D GLU 26  ? ? CD  D GLU 26  ? ? OE2 D GLU 26  ? ? 81.99  123.30 -41.31 1.20 N
+1142 1 CG  D GLU 26  ? ? CD  D GLU 26  ? ? OE1 D GLU 26  ? ? 67.20  118.30 -51.10 2.00 N
+1143 1 CG  D GLU 26  ? ? CD  D GLU 26  ? ? OE2 D GLU 26  ? ? 74.76  118.30 -43.54 2.00 N
+1144 1 O   D GLU 26  ? ? C   D GLU 26  ? ? N   D ALA 27  ? ? 133.38 122.70 10.68  1.60 Y
+1145 1 CD  D ARG 30  ? ? NE  D ARG 30  ? ? CZ  D ARG 30  ? ? 137.27 123.60 13.67  1.40 N
+1146 1 NH1 D ARG 30  ? ? CZ  D ARG 30  ? ? NH2 D ARG 30  ? ? 103.55 119.40 -15.85 1.10 N
+1147 1 NE  D ARG 30  ? ? CZ  D ARG 30  ? ? NH1 D ARG 30  ? ? 135.26 120.30 14.96  0.50 N
+1148 1 CA  D LEU 31  ? ? C   D LEU 31  ? ? N   D LEU 32  ? ? 103.62 117.20 -13.58 2.20 Y
+1149 1 CB  D LEU 32  ? ? CG  D LEU 32  ? ? CD2 D LEU 32  ? ? 133.85 111.00 22.85  1.70 N
+1150 1 CB  D TYR 35  ? ? CG  D TYR 35  ? ? CD2 D TYR 35  ? ? 126.60 121.00 5.60   0.60 N
+1151 1 CB  D TYR 35  ? ? CG  D TYR 35  ? ? CD1 D TYR 35  ? ? 115.77 121.00 -5.23  0.60 N
+1152 1 CG  D TYR 35  ? ? CD1 D TYR 35  ? ? CE1 D TYR 35  ? ? 127.10 121.30 5.80   0.80 N
+1153 1 CD1 D TYR 35  ? ? CE1 D TYR 35  ? ? CZ  D TYR 35  ? ? 110.61 119.80 -9.19  0.90 N
+1154 1 N   D PRO 36  ? ? CD  D PRO 36  ? ? CG  D PRO 36  ? ? 114.01 103.20 10.81  1.50 N
+1155 1 CE3 D TRP 37  ? ? CZ3 D TRP 37  ? ? CH2 D TRP 37  ? ? 112.20 121.20 -9.00  1.10 N
+1156 1 CZ3 D TRP 37  ? ? CH2 D TRP 37  ? ? CZ2 D TRP 37  ? ? 137.32 121.60 15.72  1.20 N
+1157 1 CH2 D TRP 37  ? ? CZ2 D TRP 37  ? ? CE2 D TRP 37  ? ? 104.88 117.40 -12.52 1.00 N
+1158 1 CA  D THR 38  ? ? CB  D THR 38  ? ? CG2 D THR 38  ? ? 102.40 112.40 -10.00 1.40 N
+1159 1 N   D GLN 39  ? ? CA  D GLN 39  ? ? CB  D GLN 39  ? ? 99.45  110.60 -11.15 1.80 N
+1160 1 O   D GLN 39  ? ? C   D GLN 39  ? ? N   D ARG 40  ? ? 111.69 122.70 -11.01 1.60 Y
+1161 1 CA  D ARG 40  ? ? CB  D ARG 40  ? ? CG  D ARG 40  ? ? 133.93 113.40 20.53  2.20 N
+1162 1 NH1 D ARG 40  ? ? CZ  D ARG 40  ? ? NH2 D ARG 40  ? ? 126.76 119.40 7.36   1.10 N
+1163 1 NE  D ARG 40  ? ? CZ  D ARG 40  ? ? NH1 D ARG 40  ? ? 114.61 120.30 -5.69  0.50 N
+1164 1 NE  D ARG 40  ? ? CZ  D ARG 40  ? ? NH2 D ARG 40  ? ? 101.06 120.30 -19.24 0.50 N
+1165 1 CA  D ARG 40  ? ? C   D ARG 40  ? ? N   D PHE 41  ? ? 134.39 117.20 17.19  2.20 Y
+1166 1 O   D ARG 40  ? ? C   D ARG 40  ? ? N   D PHE 41  ? ? 109.00 122.70 -13.70 1.60 Y
+1167 1 CB  D PHE 41  ? ? CG  D PHE 41  ? ? CD1 D PHE 41  ? ? 116.43 120.80 -4.37  0.70 N
+1168 1 CG  D PHE 41  ? ? CD1 D PHE 41  ? ? CE1 D PHE 41  ? ? 98.15  120.80 -22.65 1.10 N
+1169 1 CD1 D PHE 41  ? ? CE1 D PHE 41  ? ? CZ  D PHE 41  ? ? 142.29 120.10 22.19  1.20 N
+1170 1 CZ  D PHE 41  ? ? CE2 D PHE 41  ? ? CD2 D PHE 41  ? ? 105.99 120.10 -14.11 1.20 N
+1171 1 CA  D PHE 41  ? ? C   D PHE 41  ? ? O   D PHE 41  ? ? 100.90 120.10 -19.20 2.10 N
+1172 1 O   D PHE 41  ? ? C   D PHE 41  ? ? N   D PHE 42  ? ? 146.41 122.70 23.71  1.60 Y
+1173 1 C   D PHE 41  ? ? N   D PHE 42  ? ? CA  D PHE 42  ? ? 105.00 121.70 -16.70 2.50 Y
+1174 1 CB  D PHE 42  ? ? CG  D PHE 42  ? ? CD2 D PHE 42  ? ? 129.33 120.80 8.53   0.70 N
+1175 1 CB  D PHE 42  ? ? CG  D PHE 42  ? ? CD1 D PHE 42  ? ? 105.47 120.80 -15.33 0.70 N
+1176 1 CG  D PHE 42  ? ? CD1 D PHE 42  ? ? CE1 D PHE 42  ? ? 100.41 120.80 -20.39 1.10 N
+1177 1 CD1 D PHE 42  ? ? CE1 D PHE 42  ? ? CZ  D PHE 42  ? ? 134.31 120.10 14.21  1.20 N
+1178 1 C   D PHE 42  ? ? N   D GLU 43  ? ? CA  D GLU 43  ? ? 104.72 121.70 -16.98 2.50 Y
+1179 1 CB  D GLU 43  ? ? CA  D GLU 43  ? ? C   D GLU 43  ? ? 87.83  110.40 -22.57 2.00 N
+1180 1 CA  D GLU 43  ? ? CB  D GLU 43  ? ? CG  D GLU 43  ? ? 165.87 113.40 52.47  2.20 N
+1181 1 CB  D GLU 43  ? ? CG  D GLU 43  ? ? CD  D GLU 43  ? ? 94.87  114.20 -19.33 2.70 N
+1182 1 OE1 D GLU 43  ? ? CD  D GLU 43  ? ? OE2 D GLU 43  ? ? 88.12  123.30 -35.18 1.20 N
+1183 1 CG  D GLU 43  ? ? CD  D GLU 43  ? ? OE2 D GLU 43  ? ? 145.80 118.30 27.50  2.00 N
+1184 1 CA  D GLU 43  ? ? C   D GLU 43  ? ? N   D SER 44  ? ? 98.30  117.20 -18.90 2.20 Y
+1185 1 O   D GLU 43  ? ? C   D GLU 43  ? ? N   D SER 44  ? ? 147.38 122.70 24.68  1.60 Y
+1186 1 CA  D SER 44  ? ? C   D SER 44  ? ? N   D PHE 45  ? ? 136.68 117.20 19.48  2.20 Y
+1187 1 O   D SER 44  ? ? C   D SER 44  ? ? N   D PHE 45  ? ? 94.75  122.70 -27.95 1.60 Y
+1188 1 CB  D PHE 45  ? ? CG  D PHE 45  ? ? CD2 D PHE 45  ? ? 135.48 120.80 14.68  0.70 N
+1189 1 CB  D PHE 45  ? ? CG  D PHE 45  ? ? CD1 D PHE 45  ? ? 113.12 120.80 -7.68  0.70 N
+1190 1 CG  D PHE 45  ? ? CD1 D PHE 45  ? ? CE1 D PHE 45  ? ? 112.91 120.80 -7.89  1.10 N
+1191 1 CG  D PHE 45  ? ? CD2 D PHE 45  ? ? CE2 D PHE 45  ? ? 134.99 120.80 14.19  1.10 N
+1192 1 CE1 D PHE 45  ? ? CZ  D PHE 45  ? ? CE2 D PHE 45  ? ? 108.62 120.00 -11.38 1.80 N
+1193 1 CA  D PHE 45  ? ? C   D PHE 45  ? ? O   D PHE 45  ? ? 96.02  120.10 -24.08 2.10 N
+1194 1 O   D PHE 45  ? ? C   D PHE 45  ? ? N   D GLY 46  ? ? 144.26 123.20 21.06  1.70 Y
+1195 1 C   D PHE 45  ? ? N   D GLY 46  ? ? CA  D GLY 46  ? ? 107.73 122.30 -14.57 2.10 Y
+1196 1 CA  D GLY 46  ? ? C   D GLY 46  ? ? O   D GLY 46  ? ? 91.84  120.60 -28.76 1.80 N
+1197 1 O   D GLY 46  ? ? C   D GLY 46  ? ? N   D ASP 47  ? ? 144.17 122.70 21.47  1.60 Y
+1198 1 C   D GLY 46  ? ? N   D ASP 47  ? ? CA  D ASP 47  ? ? 76.58  121.70 -45.12 2.50 Y
+1199 1 CB  D ASP 47  ? ? CA  D ASP 47  ? ? C   D ASP 47  ? ? 80.27  110.40 -30.13 2.00 N
+1200 1 N   D ASP 47  ? ? CA  D ASP 47  ? ? CB  D ASP 47  ? ? 67.84  110.60 -42.76 1.80 N
+1201 1 CA  D ASP 47  ? ? CB  D ASP 47  ? ? CG  D ASP 47  ? ? 95.63  113.40 -17.77 2.20 N
+1202 1 OD1 D ASP 47  ? ? CG  D ASP 47  ? ? OD2 D ASP 47  ? ? 145.42 123.30 22.12  1.90 N
+1203 1 CB  D ASP 47  ? ? CG  D ASP 47  ? ? OD1 D ASP 47  ? ? 97.68  118.30 -20.62 0.90 N
+1204 1 N   D ASP 47  ? ? CA  D ASP 47  ? ? C   D ASP 47  ? ? 69.76  111.00 -41.24 2.70 N
+1205 1 CA  D ASP 47  ? ? C   D ASP 47  ? ? N   D LEU 48  ? ? 82.02  117.20 -35.18 2.20 Y
+1206 1 O   D ASP 47  ? ? C   D ASP 47  ? ? N   D LEU 48  ? ? 163.93 122.70 41.23  1.60 Y
+1207 1 C   D ASP 47  ? ? N   D LEU 48  ? ? CA  D LEU 48  ? ? 103.31 121.70 -18.39 2.50 Y
+1208 1 CA  D LEU 48  ? ? CB  D LEU 48  ? ? CG  D LEU 48  ? ? 98.02  115.30 -17.28 2.30 N
+1209 1 CB  D LEU 48  ? ? CG  D LEU 48  ? ? CD1 D LEU 48  ? ? 100.62 111.00 -10.38 1.70 N
+1210 1 CB  D LEU 48  ? ? CG  D LEU 48  ? ? CD2 D LEU 48  ? ? 126.95 111.00 15.95  1.70 N
+1211 1 C   D LEU 48  ? ? N   D SER 49  ? ? CA  D SER 49  ? ? 104.84 121.70 -16.86 2.50 Y
+1212 1 CB  D SER 49  ? ? CA  D SER 49  ? ? C   D SER 49  ? ? 89.04  110.10 -21.06 1.90 N
+1213 1 CA  D SER 49  ? ? C   D SER 49  ? ? N   D THR 50  ? ? 103.01 117.20 -14.19 2.20 Y
+1214 1 C   D SER 49  ? ? N   D THR 50  ? ? CA  D THR 50  ? ? 90.25  121.70 -31.45 2.50 Y
+1215 1 CB  D THR 50  ? ? CA  D THR 50  ? ? C   D THR 50  ? ? 81.22  111.60 -30.38 2.70 N
+1216 1 N   D THR 50  ? ? CA  D THR 50  ? ? CB  D THR 50  ? ? 82.45  110.30 -27.85 1.90 N
+1217 1 CA  D THR 50  ? ? CB  D THR 50  ? ? OG1 D THR 50  ? ? 125.15 109.00 16.15  2.10 N
+1218 1 CA  D THR 50  ? ? CB  D THR 50  ? ? CG2 D THR 50  ? ? 101.86 112.40 -10.54 1.40 N
+1219 1 N   D PRO 51  ? ? CD  D PRO 51  ? ? CG  D PRO 51  ? ? 89.48  103.20 -13.72 1.50 N
+1220 1 CA  D PRO 51  ? ? C   D PRO 51  ? ? O   D PRO 51  ? ? 135.94 120.20 15.74  2.40 N
+1221 1 O   D PRO 51  ? ? C   D PRO 51  ? ? N   D ASP 52  ? ? 112.25 122.70 -10.45 1.60 Y
+1222 1 N   D ASP 52  ? ? CA  D ASP 52  ? ? CB  D ASP 52  ? ? 89.20  110.60 -21.40 1.80 N
+1223 1 CA  D ASP 52  ? ? CB  D ASP 52  ? ? CG  D ASP 52  ? ? 128.46 113.40 15.06  2.20 N
+1224 1 OD1 D ASP 52  ? ? CG  D ASP 52  ? ? OD2 D ASP 52  ? ? 100.45 123.30 -22.85 1.90 N
+1225 1 CB  D ASP 52  ? ? CG  D ASP 52  ? ? OD1 D ASP 52  ? ? 95.06  118.30 -23.24 0.90 N
+1226 1 CB  D ASP 52  ? ? CG  D ASP 52  ? ? OD2 D ASP 52  ? ? 89.71  118.30 -28.59 0.90 N
+1227 1 CA  D ASP 52  ? ? C   D ASP 52  ? ? O   D ASP 52  ? ? 101.31 120.10 -18.79 2.10 N
+1228 1 O   D ASP 52  ? ? C   D ASP 52  ? ? N   D ALA 53  ? ? 135.92 122.70 13.22  1.60 Y
+1229 1 CB  D ALA 53  ? ? CA  D ALA 53  ? ? C   D ALA 53  ? ? 96.69  110.10 -13.41 1.50 N
+1230 1 N   D ALA 53  ? ? CA  D ALA 53  ? ? CB  D ALA 53  ? ? 127.34 110.10 17.24  1.40 N
+1231 1 CA  D ALA 53  ? ? C   D ALA 53  ? ? O   D ALA 53  ? ? 139.33 120.10 19.23  2.10 N
+1232 1 CA  D VAL 54  ? ? CB  D VAL 54  ? ? CG1 D VAL 54  ? ? 95.21  110.90 -15.69 1.50 N
+1233 1 O   D VAL 54  ? ? C   D VAL 54  ? ? N   D MET 55  ? ? 107.33 122.70 -15.37 1.60 Y
+1234 1 CB  D MET 55  ? ? CG  D MET 55  ? ? SD  D MET 55  ? ? 137.22 112.40 24.82  3.00 N
+1235 1 CA  D MET 55  ? ? C   D MET 55  ? ? O   D MET 55  ? ? 102.10 120.10 -18.00 2.10 N
+1236 1 CA  D MET 55  ? ? C   D MET 55  ? ? N   D GLY 56  ? ? 94.18  116.20 -22.02 2.00 Y
+1237 1 O   D MET 55  ? ? C   D MET 55  ? ? N   D GLY 56  ? ? 160.37 123.20 37.17  1.70 Y
+1238 1 C   D MET 55  ? ? N   D GLY 56  ? ? CA  D GLY 56  ? ? 78.33  122.30 -43.97 2.10 Y
+1239 1 CA  D GLY 56  ? ? C   D GLY 56  ? ? O   D GLY 56  ? ? 132.91 120.60 12.31  1.80 N
+1240 1 O   D GLY 56  ? ? C   D GLY 56  ? ? N   D ASN 57  ? ? 93.29  122.70 -29.41 1.60 Y
+1241 1 CA  D ASN 57  ? ? C   D ASN 57  ? ? O   D ASN 57  ? ? 143.56 120.10 23.46  2.10 N
+1242 1 O   D ASN 57  ? ? C   D ASN 57  ? ? N   D PRO 58  ? ? 104.47 121.10 -16.63 1.90 Y
+1243 1 C   D ASN 57  ? ? N   D PRO 58  ? ? CD  D PRO 58  ? ? 143.69 128.40 15.29  2.10 Y
+1244 1 CA  D PRO 58  ? ? N   D PRO 58  ? ? CD  D PRO 58  ? ? 95.59  111.70 -16.11 1.40 N
+1245 1 CA  D PRO 58  ? ? CB  D PRO 58  ? ? CG  D PRO 58  ? ? 71.72  104.80 -33.08 1.90 N
+1246 1 CB  D PRO 58  ? ? CG  D PRO 58  ? ? CD  D PRO 58  ? ? 152.36 106.50 45.86  3.90 N
+1247 1 N   D PRO 58  ? ? CD  D PRO 58  ? ? CG  D PRO 58  ? ? 56.72  103.20 -46.48 1.50 N
+1248 1 CD  D LYS 59  ? ? CE  D LYS 59  ? ? NZ  D LYS 59  ? ? 96.99  111.70 -14.71 2.30 N
+1249 1 CA  D LYS 59  ? ? C   D LYS 59  ? ? N   D VAL 60  ? ? 98.86  117.20 -18.34 2.20 Y
+1250 1 O   D LYS 59  ? ? C   D LYS 59  ? ? N   D VAL 60  ? ? 145.89 122.70 23.19  1.60 Y
+1251 1 CB  D VAL 60  ? ? CA  D VAL 60  ? ? C   D VAL 60  ? ? 130.09 111.40 18.69  1.90 N
+1252 1 CG1 D VAL 60  ? ? CB  D VAL 60  ? ? CG2 D VAL 60  ? ? 127.31 110.90 16.41  1.60 N
+1253 1 CA  D VAL 60  ? ? CB  D VAL 60  ? ? CG1 D VAL 60  ? ? 98.44  110.90 -12.46 1.50 N
+1254 1 CA  D VAL 60  ? ? CB  D VAL 60  ? ? CG2 D VAL 60  ? ? 120.45 110.90 9.55   1.50 N
+1255 1 O   D VAL 60  ? ? C   D VAL 60  ? ? N   D LYS 61  ? ? 111.88 122.70 -10.82 1.60 Y
+1256 1 CA  D HIS 63  ? ? CB  D HIS 63  ? ? CG  D HIS 63  ? ? 133.46 113.60 19.86  1.70 N
+1257 1 CB  D HIS 63  ? ? CG  D HIS 63  ? ? CD2 D HIS 63  ? ? 116.20 129.70 -13.50 1.60 N
+1258 1 ND1 D HIS 63  ? ? CG  D HIS 63  ? ? CD2 D HIS 63  ? ? 123.36 108.80 14.56  1.40 N
+1259 1 CB  D HIS 63  ? ? CG  D HIS 63  ? ? ND1 D HIS 63  ? ? 109.17 121.40 -12.23 1.30 N
+1260 1 CG  D HIS 63  ? ? ND1 D HIS 63  ? ? CE1 D HIS 63  ? ? 91.20  105.70 -14.50 1.30 N
+1261 1 ND1 D HIS 63  ? ? CE1 D HIS 63  ? ? NE2 D HIS 63  ? ? 98.99  108.50 -9.51  1.10 N
+1262 1 CE1 D HIS 63  ? ? NE2 D HIS 63  ? ? CD2 D HIS 63  ? ? 117.62 109.00 8.62   0.70 N
+1263 1 CG  D HIS 63  ? ? CD2 D HIS 63  ? ? NE2 D HIS 63  ? ? 85.45  106.70 -21.25 1.20 N
+1264 1 O   D HIS 63  ? ? C   D HIS 63  ? ? N   D GLY 64  ? ? 136.73 123.20 13.53  1.70 Y
+1265 1 CA  D GLY 64  ? ? C   D GLY 64  ? ? O   D GLY 64  ? ? 131.98 120.60 11.38  1.80 N
+1266 1 N   D LYS 65  ? ? CA  D LYS 65  ? ? CB  D LYS 65  ? ? 97.56  110.60 -13.04 1.80 N
+1267 1 CA  D LYS 65  ? ? CB  D LYS 65  ? ? CG  D LYS 65  ? ? 92.33  113.40 -21.07 2.20 N
+1268 1 CB  D LYS 65  ? ? CG  D LYS 65  ? ? CD  D LYS 65  ? ? 79.34  111.60 -32.26 2.60 N
+1269 1 CG  D LYS 65  ? ? CD  D LYS 65  ? ? CE  D LYS 65  ? ? 76.43  111.90 -35.47 3.00 N
+1270 1 CD  D LYS 65  ? ? CE  D LYS 65  ? ? NZ  D LYS 65  ? ? 83.93  111.70 -27.77 2.30 N
+1271 1 CB  D LYS 66  ? ? CA  D LYS 66  ? ? C   D LYS 66  ? ? 123.37 110.40 12.97  2.00 N
+1272 1 CA  D LYS 66  ? ? CB  D LYS 66  ? ? CG  D LYS 66  ? ? 143.51 113.40 30.11  2.20 N
+1273 1 CG  D LYS 66  ? ? CD  D LYS 66  ? ? CE  D LYS 66  ? ? 88.63  111.90 -23.27 3.00 N
+1274 1 N   D VAL 67  ? ? CA  D VAL 67  ? ? CB  D VAL 67  ? ? 91.07  111.50 -20.43 2.20 N
+1275 1 CG1 D VAL 67  ? ? CB  D VAL 67  ? ? CG2 D VAL 67  ? ? 132.28 110.90 21.38  1.60 N
+1276 1 CA  D VAL 67  ? ? CB  D VAL 67  ? ? CG1 D VAL 67  ? ? 94.61  110.90 -16.29 1.50 N
+1277 1 CB  D LEU 68  ? ? CG  D LEU 68  ? ? CD1 D LEU 68  ? ? 124.77 111.00 13.77  1.70 N
+1278 1 CB  D PHE 71  ? ? CG  D PHE 71  ? ? CD2 D PHE 71  ? ? 110.03 120.80 -10.77 0.70 N
+1279 1 CD1 D PHE 71  ? ? CG  D PHE 71  ? ? CD2 D PHE 71  ? ? 138.37 118.30 20.07  1.30 N
+1280 1 CB  D PHE 71  ? ? CG  D PHE 71  ? ? CD1 D PHE 71  ? ? 110.75 120.80 -10.05 0.70 N
+1281 1 CG  D PHE 71  ? ? CD1 D PHE 71  ? ? CE1 D PHE 71  ? ? 106.98 120.80 -13.82 1.10 N
+1282 1 CG  D PHE 71  ? ? CD2 D PHE 71  ? ? CE2 D PHE 71  ? ? 96.62  120.80 -24.18 1.10 N
+1283 1 CD1 D PHE 71  ? ? CE1 D PHE 71  ? ? CZ  D PHE 71  ? ? 128.39 120.10 8.29   1.20 N
+1284 1 CZ  D PHE 71  ? ? CE2 D PHE 71  ? ? CD2 D PHE 71  ? ? 130.24 120.10 10.14  1.20 N
+1285 1 N   D SER 72  ? ? CA  D SER 72  ? ? CB  D SER 72  ? ? 140.43 110.50 29.93  1.50 N
+1286 1 CA  D SER 72  ? ? CB  D SER 72  ? ? OG  D SER 72  ? ? 89.98  111.20 -21.22 2.70 N
+1287 1 CA  D SER 72  ? ? C   D SER 72  ? ? O   D SER 72  ? ? 142.02 120.10 21.92  2.10 N
+1288 1 CA  D SER 72  ? ? C   D SER 72  ? ? N   D ASP 73  ? ? 100.62 117.20 -16.58 2.20 Y
+1289 1 CA  D ASP 73  ? ? CB  D ASP 73  ? ? CG  D ASP 73  ? ? 83.50  113.40 -29.90 2.20 N
+1290 1 OD1 D ASP 73  ? ? CG  D ASP 73  ? ? OD2 D ASP 73  ? ? 71.12  123.30 -52.18 1.90 N
+1291 1 CB  D ASP 73  ? ? CG  D ASP 73  ? ? OD1 D ASP 73  ? ? 157.24 118.30 38.94  0.90 N
+1292 1 CB  D ASP 73  ? ? CG  D ASP 73  ? ? OD2 D ASP 73  ? ? 89.55  118.30 -28.75 0.90 N
+1293 1 N   D ASP 73  ? ? CA  D ASP 73  ? ? C   D ASP 73  ? ? 138.43 111.00 27.43  2.70 N
+1294 1 CA  D ASP 73  ? ? C   D ASP 73  ? ? O   D ASP 73  ? ? 147.28 120.10 27.18  2.10 N
+1295 1 O   D ASP 73  ? ? C   D ASP 73  ? ? N   D GLY 74  ? ? 99.51  123.20 -23.69 1.70 Y
+1296 1 CA  D GLY 74  ? ? C   D GLY 74  ? ? O   D GLY 74  ? ? 131.94 120.60 11.34  1.80 N
+1297 1 CB  D LEU 75  ? ? CA  D LEU 75  ? ? C   D LEU 75  ? ? 122.88 110.20 12.68  1.90 N
+1298 1 CB  D LEU 75  ? ? CG  D LEU 75  ? ? CD2 D LEU 75  ? ? 131.93 111.00 20.93  1.70 N
+1299 1 CB  D ALA 76  ? ? CA  D ALA 76  ? ? C   D ALA 76  ? ? 129.70 110.10 19.60  1.50 N
+1300 1 N   D ALA 76  ? ? CA  D ALA 76  ? ? CB  D ALA 76  ? ? 80.22  110.10 -29.88 1.40 N
+1301 1 N   D ALA 76  ? ? CA  D ALA 76  ? ? C   D ALA 76  ? ? 92.58  111.00 -18.42 2.70 N
+1302 1 CA  D ALA 76  ? ? C   D ALA 76  ? ? O   D ALA 76  ? ? 105.95 120.10 -14.15 2.10 N
+1303 1 CA  D ALA 76  ? ? C   D ALA 76  ? ? N   D HIS 77  ? ? 151.45 117.20 34.25  2.20 Y
+1304 1 O   D ALA 76  ? ? C   D ALA 76  ? ? N   D HIS 77  ? ? 97.77  122.70 -24.93 1.60 Y
+1305 1 CB  D HIS 77  ? ? CA  D HIS 77  ? ? C   D HIS 77  ? ? 84.39  110.40 -26.01 2.00 N
+1306 1 ND1 D HIS 77  ? ? CG  D HIS 77  ? ? CD2 D HIS 77  ? ? 128.65 108.80 19.85  1.40 N
+1307 1 CB  D HIS 77  ? ? CG  D HIS 77  ? ? ND1 D HIS 77  ? ? 110.11 121.40 -11.29 1.30 N
+1308 1 CG  D HIS 77  ? ? ND1 D HIS 77  ? ? CE1 D HIS 77  ? ? 97.64  105.70 -8.06  1.30 N
+1309 1 ND1 D HIS 77  ? ? CE1 D HIS 77  ? ? NE2 D HIS 77  ? ? 90.43  108.50 -18.07 1.10 N
+1310 1 CE1 D HIS 77  ? ? NE2 D HIS 77  ? ? CD2 D HIS 77  ? ? 132.89 109.00 23.89  0.70 N
+1311 1 CG  D HIS 77  ? ? CD2 D HIS 77  ? ? NE2 D HIS 77  ? ? 79.89  106.70 -26.81 1.20 N
+1312 1 CA  D HIS 77  ? ? C   D HIS 77  ? ? O   D HIS 77  ? ? 145.78 120.10 25.68  2.10 N
+1313 1 CA  D HIS 77  ? ? C   D HIS 77  ? ? N   D LEU 78  ? ? 97.44  117.20 -19.76 2.20 Y
+1314 1 CB  D LEU 78  ? ? CG  D LEU 78  ? ? CD1 D LEU 78  ? ? 94.53  111.00 -16.47 1.70 N
+1315 1 CB  D LEU 78  ? ? CG  D LEU 78  ? ? CD2 D LEU 78  ? ? 142.62 111.00 31.62  1.70 N
+1316 1 N   D LEU 78  ? ? CA  D LEU 78  ? ? C   D LEU 78  ? ? 143.43 111.00 32.43  2.70 N
+1317 1 CA  D LEU 78  ? ? C   D LEU 78  ? ? O   D LEU 78  ? ? 153.76 120.10 33.66  2.10 N
+1318 1 CA  D LEU 78  ? ? C   D LEU 78  ? ? N   D ASP 79  ? ? 91.47  117.20 -25.73 2.20 Y
+1319 1 C   D LEU 78  ? ? N   D ASP 79  ? ? CA  D ASP 79  ? ? 102.38 121.70 -19.32 2.50 Y
+1320 1 CB  D ASP 79  ? ? CA  D ASP 79  ? ? C   D ASP 79  ? ? 80.94  110.40 -29.46 2.00 N
+1321 1 N   D ASP 79  ? ? CA  D ASP 79  ? ? CB  D ASP 79  ? ? 87.40  110.60 -23.20 1.80 N
+1322 1 OD1 D ASP 79  ? ? CG  D ASP 79  ? ? OD2 D ASP 79  ? ? 82.07  123.30 -41.23 1.90 N
+1323 1 CB  D ASP 79  ? ? CG  D ASP 79  ? ? OD1 D ASP 79  ? ? 109.77 118.30 -8.53  0.90 N
+1324 1 CB  D ASP 79  ? ? CG  D ASP 79  ? ? OD2 D ASP 79  ? ? 92.06  118.30 -26.24 0.90 N
+1325 1 CA  D ASP 79  ? ? C   D ASP 79  ? ? N   D ASN 80  ? ? 90.66  117.20 -26.54 2.20 Y
+1326 1 C   D ASP 79  ? ? N   D ASN 80  ? ? CA  D ASN 80  ? ? 95.02  121.70 -26.68 2.50 Y
+1327 1 CB  D ASN 80  ? ? CA  D ASN 80  ? ? C   D ASN 80  ? ? 96.34  110.40 -14.06 2.00 N
+1328 1 CA  D ASN 80  ? ? CB  D ASN 80  ? ? CG  D ASN 80  ? ? 175.84 113.40 62.44  2.20 N
+1329 1 OD1 D ASN 80  ? ? CG  D ASN 80  ? ? ND2 D ASN 80  ? ? 154.40 121.90 32.50  2.30 N
+1330 1 CB  D ASN 80  ? ? CG  D ASN 80  ? ? OD1 D ASN 80  ? ? 109.22 121.60 -12.38 2.00 N
+1331 1 CB  D ASN 80  ? ? CG  D ASN 80  ? ? ND2 D ASN 80  ? ? 91.49  116.70 -25.21 2.40 N
+1332 1 CA  D ASN 80  ? ? C   D ASN 80  ? ? N   D LEU 81  ? ? 90.94  117.20 -26.26 2.20 Y
+1333 1 C   D ASN 80  ? ? N   D LEU 81  ? ? CA  D LEU 81  ? ? 105.08 121.70 -16.62 2.50 Y
+1334 1 CB  D LEU 81  ? ? CG  D LEU 81  ? ? CD2 D LEU 81  ? ? 122.47 111.00 11.47  1.70 N
+1335 1 CG  D LYS 82  ? ? CD  D LYS 82  ? ? CE  D LYS 82  ? ? 77.80  111.90 -34.10 3.00 N
+1336 1 CD  D LYS 82  ? ? CE  D LYS 82  ? ? NZ  D LYS 82  ? ? 57.02  111.70 -54.68 2.30 N
+1337 1 O   D LYS 82  ? ? C   D LYS 82  ? ? N   D GLY 83  ? ? 106.18 123.20 -17.02 1.70 Y
+1338 1 O   D GLY 83  ? ? C   D GLY 83  ? ? N   D THR 84  ? ? 103.63 122.70 -19.07 1.60 Y
+1339 1 CA  D THR 84  ? ? CB  D THR 84  ? ? CG2 D THR 84  ? ? 126.47 112.40 14.07  1.40 N
+1340 1 CA  D THR 84  ? ? C   D THR 84  ? ? N   D PHE 85  ? ? 102.37 117.20 -14.83 2.20 Y
+1341 1 CA  D PHE 85  ? ? CB  D PHE 85  ? ? CG  D PHE 85  ? ? 98.93  113.90 -14.97 2.40 N
+1342 1 CB  D PHE 85  ? ? CG  D PHE 85  ? ? CD2 D PHE 85  ? ? 125.61 120.80 4.81   0.70 N
+1343 1 CB  D PHE 85  ? ? CG  D PHE 85  ? ? CD1 D PHE 85  ? ? 113.12 120.80 -7.68  0.70 N
+1344 1 CE1 D PHE 85  ? ? CZ  D PHE 85  ? ? CE2 D PHE 85  ? ? 107.84 120.00 -12.16 1.80 N
+1345 1 CZ  D PHE 85  ? ? CE2 D PHE 85  ? ? CD2 D PHE 85  ? ? 131.55 120.10 11.45  1.20 N
+1346 1 O   D PHE 85  ? ? C   D PHE 85  ? ? N   D ALA 86  ? ? 109.75 122.70 -12.95 1.60 Y
+1347 1 CB  D ALA 86  ? ? CA  D ALA 86  ? ? C   D ALA 86  ? ? 97.93  110.10 -12.17 1.50 N
+1348 1 CA  D SER 89  ? ? C   D SER 89  ? ? O   D SER 89  ? ? 139.75 120.10 19.65  2.10 N
+1349 1 O   D SER 89  ? ? C   D SER 89  ? ? N   D GLU 90  ? ? 110.58 122.70 -12.12 1.60 Y
+1350 1 CA  D GLU 90  ? ? CB  D GLU 90  ? ? CG  D GLU 90  ? ? 95.18  113.40 -18.22 2.20 N
+1351 1 CB  D GLU 90  ? ? CG  D GLU 90  ? ? CD  D GLU 90  ? ? 89.48  114.20 -24.72 2.70 N
+1352 1 OE1 D GLU 90  ? ? CD  D GLU 90  ? ? OE2 D GLU 90  ? ? 105.65 123.30 -17.65 1.20 N
+1353 1 CG  D GLU 90  ? ? CD  D GLU 90  ? ? OE1 D GLU 90  ? ? 74.24  118.30 -44.06 2.00 N
+1354 1 CG  D GLU 90  ? ? CD  D GLU 90  ? ? OE2 D GLU 90  ? ? 96.79  118.30 -21.51 2.00 N
+1355 1 C   D GLU 90  ? ? N   D LEU 91  ? ? CA  D LEU 91  ? ? 105.73 121.70 -15.97 2.50 Y
+1356 1 CA  D LEU 91  ? ? C   D LEU 91  ? ? O   D LEU 91  ? ? 134.05 120.10 13.95  2.10 N
+1357 1 CB  D HIS 92  ? ? CA  D HIS 92  ? ? C   D HIS 92  ? ? 94.20  110.40 -16.20 2.00 N
+1358 1 N   D HIS 92  ? ? CA  D HIS 92  ? ? CB  D HIS 92  ? ? 96.53  110.60 -14.07 1.80 N
+1359 1 CA  D HIS 92  ? ? CB  D HIS 92  ? ? CG  D HIS 92  ? ? 103.40 113.60 -10.20 1.70 N
+1360 1 CB  D HIS 92  ? ? CG  D HIS 92  ? ? CD2 D HIS 92  ? ? 150.95 131.40 19.55  1.20 N
+1361 1 CB  D HIS 92  ? ? CG  D HIS 92  ? ? ND1 D HIS 92  ? ? 110.96 121.40 -10.44 1.30 N
+1362 1 CG  D HIS 92  ? ? ND1 D HIS 92  ? ? CE1 D HIS 92  ? ? 95.92  105.70 -9.78  1.30 N
+1363 1 ND1 D HIS 92  ? ? CE1 D HIS 92  ? ? NE2 D HIS 92  ? ? 127.86 111.50 16.36  1.30 N
+1364 1 CE1 D HIS 92  ? ? NE2 D HIS 92  ? ? CD2 D HIS 92  ? ? 89.86  106.60 -16.74 2.50 N
+1365 1 CG  D HIS 92  ? ? CD2 D HIS 92  ? ? NE2 D HIS 92  ? ? 124.38 109.20 15.18  1.90 N
+1366 1 CA  D HIS 92  ? ? C   D HIS 92  ? ? O   D HIS 92  ? ? 105.28 120.10 -14.82 2.10 N
+1367 1 CB  D CYS 93  ? ? CA  D CYS 93  ? ? C   D CYS 93  ? ? 126.78 111.50 15.28  1.20 N
+1368 1 N   D CYS 93  ? ? CA  D CYS 93  ? ? CB  D CYS 93  ? ? 96.00  110.60 -14.60 1.80 N
+1369 1 CA  D CYS 93  ? ? CB  D CYS 93  ? ? SG  D CYS 93  ? ? 98.36  114.00 -15.64 1.80 N
+1370 1 CA  D CYS 93  ? ? C   D CYS 93  ? ? N   D ASP 94  ? ? 101.53 117.20 -15.67 2.20 Y
+1371 1 O   D CYS 93  ? ? C   D CYS 93  ? ? N   D ASP 94  ? ? 142.12 122.70 19.42  1.60 Y
+1372 1 C   D CYS 93  ? ? N   D ASP 94  ? ? CA  D ASP 94  ? ? 106.46 121.70 -15.24 2.50 Y
+1373 1 N   D ASP 94  ? ? CA  D ASP 94  ? ? CB  D ASP 94  ? ? 97.01  110.60 -13.59 1.80 N
+1374 1 OD1 D ASP 94  ? ? CG  D ASP 94  ? ? OD2 D ASP 94  ? ? 153.47 123.30 30.17  1.90 N
+1375 1 CB  D ASP 94  ? ? CG  D ASP 94  ? ? OD1 D ASP 94  ? ? 96.27  118.30 -22.03 0.90 N
+1376 1 CB  D ASP 94  ? ? CG  D ASP 94  ? ? OD2 D ASP 94  ? ? 101.45 118.30 -16.85 0.90 N
+1377 1 CB  D LYS 95  ? ? CG  D LYS 95  ? ? CD  D LYS 95  ? ? 89.54  111.60 -22.06 2.60 N
+1378 1 CA  D LYS 95  ? ? C   D LYS 95  ? ? O   D LYS 95  ? ? 139.19 120.10 19.09  2.10 N
+1379 1 O   D LYS 95  ? ? C   D LYS 95  ? ? N   D LEU 96  ? ? 106.92 122.70 -15.78 1.60 Y
+1380 1 O   D LEU 96  ? ? C   D LEU 96  ? ? N   D HIS 97  ? ? 132.67 122.70 9.97   1.60 Y
+1381 1 CB  D HIS 97  ? ? CG  D HIS 97  ? ? CD2 D HIS 97  ? ? 118.37 129.70 -11.33 1.60 N
+1382 1 ND1 D HIS 97  ? ? CG  D HIS 97  ? ? CD2 D HIS 97  ? ? 119.37 108.80 10.57  1.40 N
+1383 1 ND1 D HIS 97  ? ? CE1 D HIS 97  ? ? NE2 D HIS 97  ? ? 88.40  108.50 -20.10 1.10 N
+1384 1 CE1 D HIS 97  ? ? NE2 D HIS 97  ? ? CD2 D HIS 97  ? ? 134.71 109.00 25.71  0.70 N
+1385 1 CG  D HIS 97  ? ? CD2 D HIS 97  ? ? NE2 D HIS 97  ? ? 85.52  106.70 -21.18 1.20 N
+1386 1 CA  D VAL 98  ? ? CB  D VAL 98  ? ? CG2 D VAL 98  ? ? 99.74  110.90 -11.16 1.50 N
+1387 1 OD1 D ASP 99  ? ? CG  D ASP 99  ? ? OD2 D ASP 99  ? ? 141.06 123.30 17.76  1.90 N
+1388 1 CB  D ASP 99  ? ? CG  D ASP 99  ? ? OD1 D ASP 99  ? ? 106.74 118.30 -11.56 0.90 N
+1389 1 CB  D ASP 99  ? ? CG  D ASP 99  ? ? OD2 D ASP 99  ? ? 111.36 118.30 -6.94  0.90 N
+1390 1 CA  D PRO 100 ? ? N   D PRO 100 ? ? CD  D PRO 100 ? ? 102.47 111.70 -9.23  1.40 N
+1391 1 CB  D PRO 100 ? ? CA  D PRO 100 ? ? C   D PRO 100 ? ? 128.06 111.70 16.36  2.10 N
+1392 1 O   D PRO 100 ? ? C   D PRO 100 ? ? N   D GLU 101 ? ? 133.48 122.70 10.78  1.60 Y
+1393 1 OE1 D GLU 101 ? ? CD  D GLU 101 ? ? OE2 D GLU 101 ? ? 156.95 123.30 33.65  1.20 N
+1394 1 CG  D GLU 101 ? ? CD  D GLU 101 ? ? OE1 D GLU 101 ? ? 89.57  118.30 -28.73 2.00 N
+1395 1 CG  D GLU 101 ? ? CD  D GLU 101 ? ? OE2 D GLU 101 ? ? 80.87  118.30 -37.43 2.00 N
+1396 1 CA  D ASN 102 ? ? C   D ASN 102 ? ? N   D PHE 103 ? ? 130.46 117.20 13.26  2.20 Y
+1397 1 N   D PHE 103 ? ? CA  D PHE 103 ? ? CB  D PHE 103 ? ? 122.48 110.60 11.88  1.80 N
+1398 1 CG  D ARG 104 ? ? CD  D ARG 104 ? ? NE  D ARG 104 ? ? 89.31  111.80 -22.49 2.10 N
+1399 1 CD  D ARG 104 ? ? NE  D ARG 104 ? ? CZ  D ARG 104 ? ? 86.37  123.60 -37.23 1.40 N
+1400 1 NE  D ARG 104 ? ? CZ  D ARG 104 ? ? NH1 D ARG 104 ? ? 91.08  120.30 -29.22 0.50 N
+1401 1 NE  D ARG 104 ? ? CZ  D ARG 104 ? ? NH2 D ARG 104 ? ? 76.84  120.30 -43.46 0.50 N
+1402 1 CA  D LEU 105 ? ? CB  D LEU 105 ? ? CG  D LEU 105 ? ? 130.03 115.30 14.73  2.30 N
+1403 1 CB  D LEU 105 ? ? CG  D LEU 105 ? ? CD1 D LEU 105 ? ? 129.77 111.00 18.77  1.70 N
+1404 1 OD1 D ASN 108 ? ? CG  D ASN 108 ? ? ND2 D ASN 108 ? ? 141.93 121.90 20.03  2.30 N
+1405 1 CB  D ASN 108 ? ? CG  D ASN 108 ? ? ND2 D ASN 108 ? ? 97.59  116.70 -19.11 2.40 N
+1406 1 CA  D LEU 110 ? ? C   D LEU 110 ? ? O   D LEU 110 ? ? 137.02 120.10 16.92  2.10 N
+1407 1 O   D LEU 110 ? ? C   D LEU 110 ? ? N   D VAL 111 ? ? 110.91 122.70 -11.79 1.60 Y
+1408 1 CA  D CYS 112 ? ? C   D CYS 112 ? ? N   D VAL 113 ? ? 101.28 117.20 -15.92 2.20 Y
+1409 1 ND1 D HIS 116 ? ? CG  D HIS 116 ? ? CD2 D HIS 116 ? ? 121.74 108.80 12.94  1.40 N
+1410 1 CB  D HIS 117 ? ? CG  D HIS 117 ? ? CD2 D HIS 117 ? ? 147.08 131.40 15.68  1.20 N
+1411 1 ND1 D HIS 117 ? ? CG  D HIS 117 ? ? CD2 D HIS 117 ? ? 90.52  106.00 -15.48 1.40 N
+1412 1 CG  D HIS 117 ? ? ND1 D HIS 117 ? ? CE1 D HIS 117 ? ? 92.64  105.70 -13.06 1.30 N
+1413 1 ND1 D HIS 117 ? ? CE1 D HIS 117 ? ? NE2 D HIS 117 ? ? 121.46 111.50 9.96   1.30 N
+1414 1 CE1 D HIS 117 ? ? NE2 D HIS 117 ? ? CD2 D HIS 117 ? ? 115.01 109.00 6.01   0.70 N
+1415 1 O   D HIS 117 ? ? C   D HIS 117 ? ? N   D PHE 118 ? ? 110.72 122.70 -11.98 1.60 Y
+1416 1 CB  D PHE 118 ? ? CG  D PHE 118 ? ? CD2 D PHE 118 ? ? 111.97 120.80 -8.83  0.70 N
+1417 1 CB  D PHE 118 ? ? CG  D PHE 118 ? ? CD1 D PHE 118 ? ? 135.16 120.80 14.36  0.70 N
+1418 1 CG  D PHE 118 ? ? CD1 D PHE 118 ? ? CE1 D PHE 118 ? ? 141.50 120.80 20.70  1.10 N
+1419 1 CG  D PHE 118 ? ? CD2 D PHE 118 ? ? CE2 D PHE 118 ? ? 111.74 120.80 -9.06  1.10 N
+1420 1 CD1 D PHE 118 ? ? CE1 D PHE 118 ? ? CZ  D PHE 118 ? ? 104.02 120.10 -16.08 1.20 N
+1421 1 CA  D GLY 119 ? ? C   D GLY 119 ? ? O   D GLY 119 ? ? 135.81 120.60 15.21  1.80 N
+1422 1 CB  D LYS 120 ? ? CG  D LYS 120 ? ? CD  D LYS 120 ? ? 134.73 111.60 23.13  2.60 N
+1423 1 O   D LYS 120 ? ? C   D LYS 120 ? ? N   D GLU 121 ? ? 103.76 122.70 -18.94 1.60 Y
+1424 1 OE1 D GLU 121 ? ? CD  D GLU 121 ? ? OE2 D GLU 121 ? ? 105.47 123.30 -17.83 1.20 N
+1425 1 CG  D GLU 121 ? ? CD  D GLU 121 ? ? OE1 D GLU 121 ? ? 94.16  118.30 -24.14 2.00 N
+1426 1 CG  D GLU 121 ? ? CD  D GLU 121 ? ? OE2 D GLU 121 ? ? 92.17  118.30 -26.13 2.00 N
+1427 1 O   D GLU 121 ? ? C   D GLU 121 ? ? N   D PHE 122 ? ? 135.49 122.70 12.79  1.60 Y
+1428 1 N   D PHE 122 ? ? CA  D PHE 122 ? ? CB  D PHE 122 ? ? 99.11  110.60 -11.49 1.80 N
+1429 1 CD1 D PHE 122 ? ? CG  D PHE 122 ? ? CD2 D PHE 122 ? ? 108.31 118.30 -9.99  1.30 N
+1430 1 CB  D PHE 122 ? ? CG  D PHE 122 ? ? CD1 D PHE 122 ? ? 126.75 120.80 5.95   0.70 N
+1431 1 CG  D PHE 122 ? ? CD1 D PHE 122 ? ? CE1 D PHE 122 ? ? 128.68 120.80 7.88   1.10 N
+1432 1 CG  D PHE 122 ? ? CD2 D PHE 122 ? ? CE2 D PHE 122 ? ? 130.91 120.80 10.11  1.10 N
+1433 1 CD1 D PHE 122 ? ? CE1 D PHE 122 ? ? CZ  D PHE 122 ? ? 108.96 120.10 -11.14 1.20 N
+1434 1 CE1 D PHE 122 ? ? CZ  D PHE 122 ? ? CE2 D PHE 122 ? ? 135.68 120.00 15.68  1.80 N
+1435 1 CZ  D PHE 122 ? ? CE2 D PHE 122 ? ? CD2 D PHE 122 ? ? 106.81 120.10 -13.29 1.20 N
+1436 1 CA  D VAL 126 ? ? CB  D VAL 126 ? ? CG1 D VAL 126 ? ? 100.79 110.90 -10.11 1.50 N
+1437 1 CA  D VAL 126 ? ? CB  D VAL 126 ? ? CG2 D VAL 126 ? ? 94.50  110.90 -16.40 1.50 N
+1438 1 O   D VAL 126 ? ? C   D VAL 126 ? ? N   D GLN 127 ? ? 134.41 122.70 11.71  1.60 Y
+1439 1 CB  D TYR 130 ? ? CG  D TYR 130 ? ? CD2 D TYR 130 ? ? 128.33 121.00 7.33   0.60 N
+1440 1 CG  D TYR 130 ? ? CD1 D TYR 130 ? ? CE1 D TYR 130 ? ? 135.02 121.30 13.72  0.80 N
+1441 1 CD1 D TYR 130 ? ? CE1 D TYR 130 ? ? CZ  D TYR 130 ? ? 104.80 119.80 -15.00 0.90 N
+1442 1 CZ  D TYR 130 ? ? CE2 D TYR 130 ? ? CD2 D TYR 130 ? ? 126.37 119.80 6.57   0.90 N
+1443 1 OE1 D GLN 131 ? ? CD  D GLN 131 ? ? NE2 D GLN 131 ? ? 138.73 121.90 16.83  2.30 N
+1444 1 CG  D GLN 131 ? ? CD  D GLN 131 ? ? OE1 D GLN 131 ? ? 106.49 121.60 -15.11 2.00 N
+1445 1 CA  D GLN 131 ? ? C   D GLN 131 ? ? O   D GLN 131 ? ? 133.10 120.10 13.00  2.10 N
+1446 1 CD  D LYS 132 ? ? CE  D LYS 132 ? ? NZ  D LYS 132 ? ? 71.58  111.70 -40.12 2.30 N
+1447 1 CG1 D VAL 133 ? ? CB  D VAL 133 ? ? CG2 D VAL 133 ? ? 126.81 110.90 15.91  1.60 N
+1448 1 N   D ALA 135 ? ? CA  D ALA 135 ? ? CB  D ALA 135 ? ? 119.13 110.10 9.03   1.40 N
+1449 1 CB  D VAL 137 ? ? CA  D VAL 137 ? ? C   D VAL 137 ? ? 98.11  111.40 -13.29 1.90 N
+1450 1 CG1 D VAL 137 ? ? CB  D VAL 137 ? ? CG2 D VAL 137 ? ? 121.40 110.90 10.50  1.60 N
+1451 1 O   D VAL 137 ? ? C   D VAL 137 ? ? N   D ALA 138 ? ? 107.27 122.70 -15.43 1.60 Y
+1452 1 CB  D ASN 139 ? ? CG  D ASN 139 ? ? OD1 D ASN 139 ? ? 91.23  121.60 -30.37 2.00 N
+1453 1 CA  D ASN 139 ? ? C   D ASN 139 ? ? O   D ASN 139 ? ? 133.25 120.10 13.15  2.10 N
+1454 1 CD1 D LEU 141 ? ? CG  D LEU 141 ? ? CD2 D LEU 141 ? ? 91.91  110.50 -18.59 3.00 N
+1455 1 CB  D LEU 141 ? ? CG  D LEU 141 ? ? CD1 D LEU 141 ? ? 98.77  111.00 -12.23 1.70 N
+1456 1 CB  D LEU 141 ? ? CG  D LEU 141 ? ? CD2 D LEU 141 ? ? 97.96  111.00 -13.04 1.70 N
+1457 1 CB  D HIS 143 ? ? CG  D HIS 143 ? ? CD2 D HIS 143 ? ? 113.24 129.70 -16.46 1.60 N
+1458 1 ND1 D HIS 143 ? ? CG  D HIS 143 ? ? CD2 D HIS 143 ? ? 118.83 108.80 10.03  1.40 N
+1459 1 CG  D HIS 143 ? ? ND1 D HIS 143 ? ? CE1 D HIS 143 ? ? 93.37  105.70 -12.33 1.30 N
+1460 1 CE1 D HIS 143 ? ? NE2 D HIS 143 ? ? CD2 D HIS 143 ? ? 113.34 109.00 4.34   0.70 N
+1461 1 CG  D HIS 143 ? ? CD2 D HIS 143 ? ? NE2 D HIS 143 ? ? 92.99  106.70 -13.71 1.20 N
+1462 1 O   D HIS 143 ? ? C   D HIS 143 ? ? N   D LYS 144 ? ? 135.70 122.70 13.00  1.60 Y
+1463 1 CB  D LYS 144 ? ? CA  D LYS 144 ? ? C   D LYS 144 ? ? 124.69 110.40 14.29  2.00 N
+1464 1 N   D LYS 144 ? ? CA  D LYS 144 ? ? CB  D LYS 144 ? ? 122.35 110.60 11.75  1.80 N
+1465 1 CG  D LYS 144 ? ? CD  D LYS 144 ? ? CE  D LYS 144 ? ? 135.79 111.90 23.89  3.00 N
+1466 1 CD  D LYS 144 ? ? CE  D LYS 144 ? ? NZ  D LYS 144 ? ? 133.89 111.70 22.19  2.30 N
+1467 1 O   D LYS 144 ? ? C   D LYS 144 ? ? N   D TYR 145 ? ? 111.13 122.70 -11.57 1.60 Y
+1468 1 CB  D TYR 145 ? ? CG  D TYR 145 ? ? CD2 D TYR 145 ? ? 109.95 121.00 -11.05 0.60 N
+1469 1 CB  D TYR 145 ? ? CG  D TYR 145 ? ? CD1 D TYR 145 ? ? 134.82 121.00 13.82  0.60 N
+1470 1 CG  D TYR 145 ? ? CD1 D TYR 145 ? ? CE1 D TYR 145 ? ? 131.30 121.30 10.00  0.80 N
+1471 1 CG  D TYR 145 ? ? CD2 D TYR 145 ? ? CE2 D TYR 145 ? ? 113.88 121.30 -7.42  0.80 N
+1472 1 CD1 D TYR 145 ? ? CE1 D TYR 145 ? ? CZ  D TYR 145 ? ? 114.03 119.80 -5.77  0.90 N
+1473 1 N   D HIS 146 ? ? CA  D HIS 146 ? ? CB  D HIS 146 ? ? 95.37  110.60 -15.23 1.80 N
+1474 1 CB  D HIS 146 ? ? CG  D HIS 146 ? ? CD2 D HIS 146 ? ? 155.87 131.40 24.47  1.20 N
+1475 1 ND1 D HIS 146 ? ? CG  D HIS 146 ? ? CD2 D HIS 146 ? ? 73.64  106.00 -32.36 1.40 N
+1476 1 ND1 D HIS 146 ? ? CE1 D HIS 146 ? ? NE2 D HIS 146 ? ? 132.02 111.50 20.52  1.30 N
+1477 1 CE1 D HIS 146 ? ? NE2 D HIS 146 ? ? CD2 D HIS 146 ? ? 73.11  106.60 -33.49 2.50 N
+1478 1 CG  D HIS 146 ? ? CD2 D HIS 146 ? ? NE2 D HIS 146 ? ? 138.24 109.20 29.04  1.90 N
+1479 1 CA  D HIS 146 ? ? C   D HIS 146 ? ? O   D HIS 146 ? ? 136.28 120.10 16.18  2.10 N
+#
+loop_
+_pdbx_validate_torsion.id
+_pdbx_validate_torsion.PDB_model_num
+_pdbx_validate_torsion.auth_comp_id
+_pdbx_validate_torsion.auth_asym_id
+_pdbx_validate_torsion.auth_seq_id
+_pdbx_validate_torsion.PDB_ins_code
+_pdbx_validate_torsion.label_alt_id
+_pdbx_validate_torsion.phi
+_pdbx_validate_torsion.psi
+1  1 SER A 3   ? ? -60.78  -176.03
+2  1 LYS A 16  ? ? -1.55   -55.42
+3  1 ALA A 21  ? ? -47.38  -76.55
+4  1 LEU A 48  ? ? -103.92 40.81
+5  1 SER A 52  ? ? -47.77  150.86
+6  1 HIS A 122 ? ? -41.04  -70.13
+7  1 THR B 4   ? ? -55.04  -176.35
+8  1 GLU B 7   ? ? -64.23  -71.41
+9  1 PHE B 45  ? ? -52.07  -9.17
+10 1 ASN B 80  ? ? -142.39 59.75
+11 1 TYR B 145 ? ? -35.62  130.61
+12 1 SER C 3   ? ? -57.25  172.94
+13 1 VAL C 17  ? ? -65.43  -70.33
+14 1 LEU C 48  ? ? -92.57  32.02
+15 1 ASP C 75  ? ? -151.27 72.44
+16 1 LYS C 90  ? ? -122.54 -77.09
+17 1 LEU C 113 ? ? -107.89 71.19
+18 1 LEU D 3   ? ? -100.25 -163.79
+19 1 ASN D 19  ? ? -63.10  94.49
+20 1 GLN D 39  ? ? -67.48  0.49
+21 1 SER D 72  ? ? -40.75  -71.69
+22 1 ASP D 73  ? ? -22.71  -43.08
+23 1 ALA D 76  ? ? -63.28  7.67
+24 1 HIS D 77  ? ? -172.71 62.56
+25 1 LEU D 78  ? ? -25.62  -50.94
+26 1 ASN D 80  ? ? -167.02 85.07
+27 1 HIS D 97  ? ? 76.11   35.29
+#
+loop_
+_pdbx_validate_peptide_omega.id
+_pdbx_validate_peptide_omega.PDB_model_num
+_pdbx_validate_peptide_omega.auth_comp_id_1
+_pdbx_validate_peptide_omega.auth_asym_id_1
+_pdbx_validate_peptide_omega.auth_seq_id_1
+_pdbx_validate_peptide_omega.PDB_ins_code_1
+_pdbx_validate_peptide_omega.label_alt_id_1
+_pdbx_validate_peptide_omega.auth_comp_id_2
+_pdbx_validate_peptide_omega.auth_asym_id_2
+_pdbx_validate_peptide_omega.auth_seq_id_2
+_pdbx_validate_peptide_omega.PDB_ins_code_2
+_pdbx_validate_peptide_omega.label_alt_id_2
+_pdbx_validate_peptide_omega.omega
+1 1 GLY A 18 ? ? ALA A 19 ? ? -145.53
+2 1 SER B 49 ? ? THR B 50 ? ? 113.84
+3 1 LEU D 3  ? ? THR D 4  ? ? 148.66
+4 1 VAL D 18 ? ? ASN D 19 ? ? 148.41
+5 1 LEU D 48 ? ? SER D 49 ? ? -144.38
+6 1 SER D 49 ? ? THR D 50 ? ? 143.57
+#
+loop_
+_pdbx_validate_chiral.id
+_pdbx_validate_chiral.PDB_model_num
+_pdbx_validate_chiral.auth_atom_id
+_pdbx_validate_chiral.label_alt_id
+_pdbx_validate_chiral.auth_asym_id
+_pdbx_validate_chiral.auth_comp_id
+_pdbx_validate_chiral.auth_seq_id
+_pdbx_validate_chiral.PDB_ins_code
+_pdbx_validate_chiral.details
+_pdbx_validate_chiral.omega
+1  1 CB ? A THR 137 ? 'WRONG HAND' .
+2  1 CB ? B THR 12  ? PLANAR       .
+3  1 CB ? B THR 50  ? PLANAR       .
+4  1 CA ? C ASN 78  ? PLANAR       .
+5  1 CB ? C THR 118 ? 'WRONG HAND' .
+6  1 CA ? D HIS 2   ? PLANAR       .
+7  1 CA ? D SER 72  ? PLANAR       .
+8  1 CA ? D ASP 73  ? PLANAR       .
+9  1 CA ? D LEU 78  ? PLANAR       .
+10 1 CA ? D LYS 144 ? PLANAR       .
+#
+loop_
+_pdbx_validate_planes.id
+_pdbx_validate_planes.PDB_model_num
+_pdbx_validate_planes.auth_comp_id
+_pdbx_validate_planes.auth_asym_id
+_pdbx_validate_planes.auth_seq_id
+_pdbx_validate_planes.PDB_ins_code
+_pdbx_validate_planes.label_alt_id
+_pdbx_validate_planes.rmsd
+_pdbx_validate_planes.type
+1  1 HIS A 20  ? ? 0.175 'SIDE CHAIN'
+2  1 GLU A 23  ? ? 0.248 'SIDE CHAIN'
+3  1 TYR A 24  ? ? 0.104 'SIDE CHAIN'
+4  1 PHE A 36  ? ? 0.086 'SIDE CHAIN'
+5  1 HIS A 45  ? ? 0.112 'SIDE CHAIN'
+6  1 HIS A 50  ? ? 0.199 'SIDE CHAIN'
+7  1 GLN A 54  ? ? 0.099 'SIDE CHAIN'
+8  1 ASP A 64  ? ? 0.137 'SIDE CHAIN'
+9  1 HIS A 72  ? ? 0.240 'SIDE CHAIN'
+10 1 ASN A 78  ? ? 0.078 'SIDE CHAIN'
+11 1 ASP A 85  ? ? 0.088 'SIDE CHAIN'
+12 1 ARG A 92  ? ? 0.084 'SIDE CHAIN'
+13 1 ASP A 126 ? ? 0.099 'SIDE CHAIN'
+14 1 ARG A 141 ? ? 0.084 'SIDE CHAIN'
+15 1 HIS B 2   ? ? 0.161 'SIDE CHAIN'
+16 1 GLU B 6   ? ? 0.159 'SIDE CHAIN'
+17 1 ASN B 19  ? ? 0.077 'SIDE CHAIN'
+18 1 ASP B 21  ? ? 0.154 'SIDE CHAIN'
+19 1 GLU B 22  ? ? 0.514 'SIDE CHAIN'
+20 1 GLU B 26  ? ? 0.375 'SIDE CHAIN'
+21 1 ASP B 47  ? ? 0.135 'SIDE CHAIN'
+22 1 ASP B 52  ? ? 0.194 'SIDE CHAIN'
+23 1 HIS B 63  ? ? 0.110 'SIDE CHAIN'
+24 1 ASP B 79  ? ? 0.111 'SIDE CHAIN'
+25 1 ASN B 80  ? ? 0.198 'SIDE CHAIN'
+26 1 GLU B 90  ? ? 0.147 'SIDE CHAIN'
+27 1 ARG B 104 ? ? 0.386 'SIDE CHAIN'
+28 1 HIS B 117 ? ? 0.223 'SIDE CHAIN'
+29 1 PHE B 118 ? ? 0.130 'SIDE CHAIN'
+30 1 GLU B 121 ? ? 0.264 'SIDE CHAIN'
+31 1 HIS B 143 ? ? 0.095 'SIDE CHAIN'
+32 1 HIS B 146 ? ? 0.307 'SIDE CHAIN'
+33 1 ASN C 9   ? ? 0.081 'SIDE CHAIN'
+34 1 HIS C 20  ? ? 0.144 'SIDE CHAIN'
+35 1 GLU C 23  ? ? 0.301 'SIDE CHAIN'
+36 1 HIS C 45  ? ? 0.095 'SIDE CHAIN'
+37 1 PHE C 46  ? ? 0.104 'SIDE CHAIN'
+38 1 ASP C 47  ? ? 0.154 'SIDE CHAIN'
+39 1 ASP C 64  ? ? 0.079 'SIDE CHAIN'
+40 1 ASP C 75  ? ? 0.073 'SIDE CHAIN'
+41 1 ASN C 78  ? ? 0.112 'SIDE CHAIN'
+42 1 ARG C 92  ? ? 0.200 'SIDE CHAIN'
+43 1 GLU C 116 ? ? 0.093 'SIDE CHAIN'
+44 1 ASP C 126 ? ? 0.111 'SIDE CHAIN'
+45 1 ARG C 141 ? ? 0.078 'SIDE CHAIN'
+46 1 HIS D 2   ? ? 0.103 'SIDE CHAIN'
+47 1 GLU D 6   ? ? 0.165 'SIDE CHAIN'
+48 1 GLU D 7   ? ? 0.103 'SIDE CHAIN'
+49 1 ASN D 19  ? ? 0.383 'SIDE CHAIN'
+50 1 ASP D 21  ? ? 0.177 'SIDE CHAIN'
+51 1 GLU D 22  ? ? 0.211 'SIDE CHAIN'
+52 1 GLU D 26  ? ? 0.537 'SIDE CHAIN'
+53 1 ARG D 40  ? ? 0.124 'SIDE CHAIN'
+54 1 GLU D 43  ? ? 0.153 'SIDE CHAIN'
+55 1 ASP D 52  ? ? 0.332 'SIDE CHAIN'
+56 1 HIS D 63  ? ? 0.182 'SIDE CHAIN'
+57 1 HIS D 77  ? ? 0.139 'SIDE CHAIN'
+58 1 ASP D 79  ? ? 0.334 'SIDE CHAIN'
+59 1 GLU D 90  ? ? 0.345 'SIDE CHAIN'
+60 1 HIS D 92  ? ? 0.076 'SIDE CHAIN'
+61 1 ASP D 94  ? ? 0.080 'SIDE CHAIN'
+62 1 GLU D 101 ? ? 0.105 'SIDE CHAIN'
+63 1 ARG D 104 ? ? 0.295 'SIDE CHAIN'
+64 1 ASN D 108 ? ? 0.102 'SIDE CHAIN'
+65 1 HIS D 117 ? ? 0.080 'SIDE CHAIN'
+66 1 PHE D 118 ? ? 0.098 'SIDE CHAIN'
+67 1 GLU D 121 ? ? 0.317 'SIDE CHAIN'
+68 1 GLN D 127 ? ? 0.072 'SIDE CHAIN'
+69 1 ASN D 139 ? ? 0.210 'SIDE CHAIN'
+70 1 HIS D 143 ? ? 0.091 'SIDE CHAIN'
+71 1 HIS D 146 ? ? 0.100 'SIDE CHAIN'
+#
+loop_
+_pdbx_validate_main_chain_plane.id
+_pdbx_validate_main_chain_plane.PDB_model_num
+_pdbx_validate_main_chain_plane.auth_comp_id
+_pdbx_validate_main_chain_plane.auth_asym_id
+_pdbx_validate_main_chain_plane.auth_seq_id
+_pdbx_validate_main_chain_plane.PDB_ins_code
+_pdbx_validate_main_chain_plane.label_alt_id
+_pdbx_validate_main_chain_plane.improper_torsion_angle
+1   1 VAL A 1   ? ? -12.67
+2   1 SER A 3   ? ? -13.97
+3   1 PRO A 4   ? ? -17.03
+4   1 ASN A 9   ? ? 10.02
+5   1 LYS A 11  ? ? -14.61
+6   1 ALA A 12  ? ? -29.90
+7   1 GLY A 15  ? ? 25.11
+8   1 ALA A 19  ? ? -16.93
+9   1 ALA A 21  ? ? 26.58
+10  1 GLY A 22  ? ? 15.67
+11  1 THR A 41  ? ? 10.64
+12  1 PHE A 46  ? ? -11.01
+13  1 LEU A 48  ? ? -25.05
+14  1 SER A 52  ? ? -10.25
+15  1 LYS A 56  ? ? 14.68
+16  1 GLY A 59  ? ? -10.73
+17  1 LYS A 61  ? ? -11.08
+18  1 ALA A 63  ? ? -17.65
+19  1 ASP A 74  ? ? 18.33
+20  1 ASP A 75  ? ? -17.01
+21  1 MET A 76  ? ? -10.25
+22  1 ASN A 78  ? ? -10.99
+23  1 SER A 81  ? ? -10.91
+24  1 ALA A 82  ? ? 11.25
+25  1 LEU A 83  ? ? -10.57
+26  1 ASP A 85  ? ? -12.17
+27  1 ALA A 88  ? ? 11.86
+28  1 LYS A 90  ? ? -14.78
+29  1 ASN A 97  ? ? -10.44
+30  1 LYS A 99  ? ? -15.41
+31  1 LEU A 101 ? ? -11.02
+32  1 ALA A 111 ? ? 10.65
+33  1 PRO A 114 ? ? -12.35
+34  1 THR A 118 ? ? -18.84
+35  1 HIS A 122 ? ? 17.51
+36  1 VAL B 1   ? ? 34.90
+37  1 LEU B 3   ? ? 14.22
+38  1 THR B 4   ? ? -16.95
+39  1 GLU B 7   ? ? 12.88
+40  1 LEU B 14  ? ? 12.18
+41  1 ASP B 21  ? ? -10.64
+42  1 THR B 38  ? ? 14.85
+43  1 GLU B 43  ? ? -24.17
+44  1 SER B 44  ? ? 54.71
+45  1 ASP B 47  ? ? 16.36
+46  1 SER B 49  ? ? -74.48
+47  1 GLY B 56  ? ? -31.34
+48  1 LYS B 59  ? ? -12.58
+49  1 VAL B 60  ? ? 10.99
+50  1 LYS B 61  ? ? -14.98
+51  1 ALA B 62  ? ? 10.48
+52  1 HIS B 63  ? ? -10.21
+53  1 LEU B 78  ? ? -25.61
+54  1 ASP B 79  ? ? 22.49
+55  1 ASN B 80  ? ? -11.79
+56  1 THR B 84  ? ? 10.66
+57  1 GLU B 90  ? ? -10.53
+58  1 PRO B 100 ? ? -11.05
+59  1 GLU B 101 ? ? -10.34
+60  1 LEU B 114 ? ? 12.27
+61  1 THR B 123 ? ? -10.83
+62  1 VAL B 126 ? ? -11.55
+63  1 GLN B 131 ? ? -10.66
+64  1 ASN B 139 ? ? -17.45
+65  1 LEU B 141 ? ? 16.09
+66  1 SER C 3   ? ? -12.01
+67  1 ALA C 5   ? ? 12.74
+68  1 TRP C 14  ? ? -12.08
+69  1 VAL C 17  ? ? 12.35
+70  1 GLY C 18  ? ? -13.66
+71  1 ALA C 21  ? ? -14.11
+72  1 GLY C 25  ? ? -12.76
+73  1 PRO C 44  ? ? -13.48
+74  1 HIS C 45  ? ? 12.45
+75  1 PHE C 46  ? ? -11.87
+76  1 ASP C 47  ? ? 19.28
+77  1 LEU C 48  ? ? -13.66
+78  1 ALA C 69  ? ? 11.77
+79  1 ALA C 71  ? ? 22.20
+80  1 HIS C 72  ? ? 13.20
+81  1 ASP C 74  ? ? 12.28
+82  1 ASP C 75  ? ? -23.65
+83  1 LEU C 80  ? ? -11.13
+84  1 LEU C 83  ? ? -10.02
+85  1 ALA C 88  ? ? 13.90
+86  1 PRO C 95  ? ? -13.46
+87  1 LEU C 109 ? ? 16.41
+88  1 ALA C 110 ? ? 13.99
+89  1 ALA C 111 ? ? 15.44
+90  1 HIS C 112 ? ? 15.15
+91  1 LEU C 113 ? ? -20.93
+92  1 PRO C 114 ? ? -32.95
+93  1 GLU C 116 ? ? -12.28
+94  1 PRO C 119 ? ? 11.38
+95  1 LEU C 125 ? ? -10.18
+96  1 VAL C 135 ? ? 14.69
+97  1 SER C 138 ? ? 10.61
+98  1 VAL D 1   ? ? -18.81
+99  1 HIS D 2   ? ? -12.80
+100 1 LEU D 3   ? ? -69.38
+101 1 PRO D 5   ? ? -10.97
+102 1 LYS D 8   ? ? -16.55
+103 1 LYS D 17  ? ? 10.50
+104 1 ASP D 21  ? ? -17.94
+105 1 GLU D 22  ? ? 23.45
+106 1 VAL D 33  ? ? 10.98
+107 1 VAL D 34  ? ? 11.45
+108 1 PHE D 42  ? ? 10.17
+109 1 GLY D 46  ? ? -18.78
+110 1 LEU D 48  ? ? 13.68
+111 1 SER D 49  ? ? -21.45
+112 1 ASP D 52  ? ? 12.37
+113 1 GLY D 56  ? ? 17.15
+114 1 VAL D 60  ? ? 10.38
+115 1 GLY D 64  ? ? -10.32
+116 1 LYS D 66  ? ? 16.86
+117 1 ASP D 73  ? ? -11.35
+118 1 LEU D 75  ? ? 15.45
+119 1 ALA D 76  ? ? -28.03
+120 1 ASP D 79  ? ? -15.12
+121 1 ASN D 80  ? ? -17.80
+122 1 GLY D 83  ? ? -24.31
+123 1 THR D 84  ? ? 22.99
+124 1 HIS D 92  ? ? -12.20
+125 1 LEU D 96  ? ? 11.44
+126 1 HIS D 117 ? ? 12.21
+127 1 LYS D 120 ? ? -25.39
+128 1 VAL D 137 ? ? -19.80
+129 1 LYS D 144 ? ? 17.04
+#
+loop_
+_pdbx_validate_polymer_linkage.id
+_pdbx_validate_polymer_linkage.PDB_model_num
+_pdbx_validate_polymer_linkage.auth_atom_id_1
+_pdbx_validate_polymer_linkage.auth_asym_id_1
+_pdbx_validate_polymer_linkage.auth_comp_id_1
+_pdbx_validate_polymer_linkage.auth_seq_id_1
+_pdbx_validate_polymer_linkage.PDB_ins_code_1
+_pdbx_validate_polymer_linkage.label_alt_id_1
+_pdbx_validate_polymer_linkage.auth_atom_id_2
+_pdbx_validate_polymer_linkage.auth_asym_id_2
+_pdbx_validate_polymer_linkage.auth_comp_id_2
+_pdbx_validate_polymer_linkage.auth_seq_id_2
+_pdbx_validate_polymer_linkage.PDB_ins_code_2
+_pdbx_validate_polymer_linkage.label_alt_id_2
+_pdbx_validate_polymer_linkage.dist
+1  1 C A LEU 2   ? ? N A SER 3   ? ? 1.02
+2  1 C A SER 3   ? ? N A PRO 4   ? ? 1.62
+3  1 C A GLY 15  ? ? N A LYS 16  ? ? 0.92
+4  1 C A PRO 44  ? ? N A HIS 45  ? ? 1.19
+5  1 C A HIS 45  ? ? N A PHE 46  ? ? 1.62
+6  1 C A ASP 47  ? ? N A LEU 48  ? ? 1.13
+7  1 C A HIS 50  ? ? N A GLY 51  ? ? 0.96
+8  1 C A ASP 74  ? ? N A ASP 75  ? ? 0.92
+9  1 C A ALA 120 ? ? N A VAL 121 ? ? 1.17
+10 1 C A LYS 127 ? ? N A PHE 128 ? ? 1.16
+11 1 C B VAL 1   ? ? N B HIS 2   ? ? 0.79
+12 1 C B HIS 2   ? ? N B LEU 3   ? ? 1.12
+13 1 C B GLU 6   ? ? N B GLU 7   ? ? 1.20
+14 1 C B ARG 40  ? ? N B PHE 41  ? ? 1.13
+15 1 C B GLY 46  ? ? N B ASP 47  ? ? 1.07
+16 1 C B PHE 71  ? ? N B SER 72  ? ? 1.05
+17 1 C B GLY 74  ? ? N B LEU 75  ? ? 1.70
+18 1 C B ALA 76  ? ? N B HIS 77  ? ? 1.64
+19 1 C B LEU 81  ? ? N B LYS 82  ? ? 1.66
+20 1 C B THR 123 ? ? N B PRO 124 ? ? 1.19
+21 1 C B PRO 124 ? ? N B PRO 125 ? ? 1.20
+22 1 C B ALA 142 ? ? N B HIS 143 ? ? 1.15
+23 1 C B TYR 145 ? ? N B HIS 146 ? ? 0.97
+24 1 C C LEU 2   ? ? N C SER 3   ? ? 1.20
+25 1 C C GLY 15  ? ? N C LYS 16  ? ? 1.09
+26 1 C C ALA 21  ? ? N C GLY 22  ? ? 1.17
+27 1 C C PRO 44  ? ? N C HIS 45  ? ? 1.11
+28 1 C C VAL 70  ? ? N C ALA 71  ? ? 0.99
+29 1 C C ALA 82  ? ? N C LEU 83  ? ? 1.69
+30 1 C C HIS 112 ? ? N C LEU 113 ? ? 1.17
+31 1 C C THR 118 ? ? N C PRO 119 ? ? 1.07
+32 1 C C SER 133 ? ? N C THR 134 ? ? 1.18
+33 1 C D VAL 1   ? ? N D HIS 2   ? ? 1.18
+34 1 C D THR 4   ? ? N D PRO 5   ? ? 0.97
+35 1 C D GLU 7   ? ? N D LYS 8   ? ? 1.18
+36 1 C D LYS 17  ? ? N D VAL 18  ? ? 1.61
+37 1 C D VAL 18  ? ? N D ASN 19  ? ? 1.18
+38 1 C D ASN 19  ? ? N D VAL 20  ? ? 1.15
+39 1 C D ARG 30  ? ? N D LEU 31  ? ? 1.19
+40 1 C D PHE 45  ? ? N D GLY 46  ? ? 0.87
+41 1 C D ASP 47  ? ? N D LEU 48  ? ? 1.19
+42 1 C D PRO 58  ? ? N D LYS 59  ? ? 1.16
+43 1 C D ASP 73  ? ? N D GLY 74  ? ? 1.61
+44 1 C D LYS 95  ? ? N D LEU 96  ? ? 1.64
+45 1 C D ALA 140 ? ? N D LEU 141 ? ? 1.20
+#
+loop_
+_chem_comp_atom.comp_id
+_chem_comp_atom.atom_id
+_chem_comp_atom.type_symbol
+_chem_comp_atom.pdbx_aromatic_flag
+_chem_comp_atom.pdbx_stereo_config
+_chem_comp_atom.pdbx_ordinal
+ALA N    N  N N 1
+ALA CA   C  N S 2
+ALA C    C  N N 3
+ALA O    O  N N 4
+ALA CB   C  N N 5
+ALA OXT  O  N N 6
+ALA H    H  N N 7
+ALA H2   H  N N 8
+ALA HA   H  N N 9
+ALA HB1  H  N N 10
+ALA HB2  H  N N 11
+ALA HB3  H  N N 12
+ALA HXT  H  N N 13
+ARG N    N  N N 14
+ARG CA   C  N S 15
+ARG C    C  N N 16
+ARG O    O  N N 17
+ARG CB   C  N N 18
+ARG CG   C  N N 19
+ARG CD   C  N N 20
+ARG NE   N  N N 21
+ARG CZ   C  N N 22
+ARG NH1  N  N N 23
+ARG NH2  N  N N 24
+ARG OXT  O  N N 25
+ARG H    H  N N 26
+ARG H2   H  N N 27
+ARG HA   H  N N 28
+ARG HB2  H  N N 29
+ARG HB3  H  N N 30
+ARG HG2  H  N N 31
+ARG HG3  H  N N 32
+ARG HD2  H  N N 33
+ARG HD3  H  N N 34
+ARG HE   H  N N 35
+ARG HH11 H  N N 36
+ARG HH12 H  N N 37
+ARG HH21 H  N N 38
+ARG HH22 H  N N 39
+ARG HXT  H  N N 40
+ASN N    N  N N 41
+ASN CA   C  N S 42
+ASN C    C  N N 43
+ASN O    O  N N 44
+ASN CB   C  N N 45
+ASN CG   C  N N 46
+ASN OD1  O  N N 47
+ASN ND2  N  N N 48
+ASN OXT  O  N N 49
+ASN H    H  N N 50
+ASN H2   H  N N 51
+ASN HA   H  N N 52
+ASN HB2  H  N N 53
+ASN HB3  H  N N 54
+ASN HD21 H  N N 55
+ASN HD22 H  N N 56
+ASN HXT  H  N N 57
+ASP N    N  N N 58
+ASP CA   C  N S 59
+ASP C    C  N N 60
+ASP O    O  N N 61
+ASP CB   C  N N 62
+ASP CG   C  N N 63
+ASP OD1  O  N N 64
+ASP OD2  O  N N 65
+ASP OXT  O  N N 66
+ASP H    H  N N 67
+ASP H2   H  N N 68
+ASP HA   H  N N 69
+ASP HB2  H  N N 70
+ASP HB3  H  N N 71
+ASP HD2  H  N N 72
+ASP HXT  H  N N 73
+CYS N    N  N N 74
+CYS CA   C  N R 75
+CYS C    C  N N 76
+CYS O    O  N N 77
+CYS CB   C  N N 78
+CYS SG   S  N N 79
+CYS OXT  O  N N 80
+CYS H    H  N N 81
+CYS H2   H  N N 82
+CYS HA   H  N N 83
+CYS HB2  H  N N 84
+CYS HB3  H  N N 85
+CYS HG   H  N N 86
+CYS HXT  H  N N 87
+GLN N    N  N N 88
+GLN CA   C  N S 89
+GLN C    C  N N 90
+GLN O    O  N N 91
+GLN CB   C  N N 92
+GLN CG   C  N N 93
+GLN CD   C  N N 94
+GLN OE1  O  N N 95
+GLN NE2  N  N N 96
+GLN OXT  O  N N 97
+GLN H    H  N N 98
+GLN H2   H  N N 99
+GLN HA   H  N N 100
+GLN HB2  H  N N 101
+GLN HB3  H  N N 102
+GLN HG2  H  N N 103
+GLN HG3  H  N N 104
+GLN HE21 H  N N 105
+GLN HE22 H  N N 106
+GLN HXT  H  N N 107
+GLU N    N  N N 108
+GLU CA   C  N S 109
+GLU C    C  N N 110
+GLU O    O  N N 111
+GLU CB   C  N N 112
+GLU CG   C  N N 113
+GLU CD   C  N N 114
+GLU OE1  O  N N 115
+GLU OE2  O  N N 116
+GLU OXT  O  N N 117
+GLU H    H  N N 118
+GLU H2   H  N N 119
+GLU HA   H  N N 120
+GLU HB2  H  N N 121
+GLU HB3  H  N N 122
+GLU HG2  H  N N 123
+GLU HG3  H  N N 124
+GLU HE2  H  N N 125
+GLU HXT  H  N N 126
+GLY N    N  N N 127
+GLY CA   C  N N 128
+GLY C    C  N N 129
+GLY O    O  N N 130
+GLY OXT  O  N N 131
+GLY H    H  N N 132
+GLY H2   H  N N 133
+GLY HA2  H  N N 134
+GLY HA3  H  N N 135
+GLY HXT  H  N N 136
+HEM CHA  C  N N 137
+HEM CHB  C  N N 138
+HEM CHC  C  N N 139
+HEM CHD  C  N N 140
+HEM C1A  C  Y N 141
+HEM C2A  C  Y N 142
+HEM C3A  C  Y N 143
+HEM C4A  C  Y N 144
+HEM CMA  C  N N 145
+HEM CAA  C  N N 146
+HEM CBA  C  N N 147
+HEM CGA  C  N N 148
+HEM O1A  O  N N 149
+HEM O2A  O  N N 150
+HEM C1B  C  N N 151
+HEM C2B  C  N N 152
+HEM C3B  C  N N 153
+HEM C4B  C  N N 154
+HEM CMB  C  N N 155
+HEM CAB  C  N N 156
+HEM CBB  C  N N 157
+HEM C1C  C  Y N 158
+HEM C2C  C  Y N 159
+HEM C3C  C  Y N 160
+HEM C4C  C  Y N 161
+HEM CMC  C  N N 162
+HEM CAC  C  N N 163
+HEM CBC  C  N N 164
+HEM C1D  C  N N 165
+HEM C2D  C  N N 166
+HEM C3D  C  N N 167
+HEM C4D  C  N N 168
+HEM CMD  C  N N 169
+HEM CAD  C  N N 170
+HEM CBD  C  N N 171
+HEM CGD  C  N N 172
+HEM O1D  O  N N 173
+HEM O2D  O  N N 174
+HEM NA   N  Y N 175
+HEM NB   N  N N 176
+HEM NC   N  Y N 177
+HEM ND   N  N N 178
+HEM FE   FE N N 179
+HEM HHB  H  N N 180
+HEM HHC  H  N N 181
+HEM HHD  H  N N 182
+HEM HMA  H  N N 183
+HEM HMAA H  N N 184
+HEM HMAB H  N N 185
+HEM HAA  H  N N 186
+HEM HAAA H  N N 187
+HEM HBA  H  N N 188
+HEM HBAA H  N N 189
+HEM HMB  H  N N 190
+HEM HMBA H  N N 191
+HEM HMBB H  N N 192
+HEM HAB  H  N N 193
+HEM HBB  H  N N 194
+HEM HBBA H  N N 195
+HEM HMC  H  N N 196
+HEM HMCA H  N N 197
+HEM HMCB H  N N 198
+HEM HAC  H  N N 199
+HEM HBC  H  N N 200
+HEM HBCA H  N N 201
+HEM HMD  H  N N 202
+HEM HMDA H  N N 203
+HEM HMDB H  N N 204
+HEM HAD  H  N N 205
+HEM HADA H  N N 206
+HEM HBD  H  N N 207
+HEM HBDA H  N N 208
+HEM H2A  H  N N 209
+HEM H2D  H  N N 210
+HEM HHA  H  N N 211
+HIS N    N  N N 212
+HIS CA   C  N S 213
+HIS C    C  N N 214
+HIS O    O  N N 215
+HIS CB   C  N N 216
+HIS CG   C  Y N 217
+HIS ND1  N  Y N 218
+HIS CD2  C  Y N 219
+HIS CE1  C  Y N 220
+HIS NE2  N  Y N 221
+HIS OXT  O  N N 222
+HIS H    H  N N 223
+HIS H2   H  N N 224
+HIS HA   H  N N 225
+HIS HB2  H  N N 226
+HIS HB3  H  N N 227
+HIS HD1  H  N N 228
+HIS HD2  H  N N 229
+HIS HE1  H  N N 230
+HIS HE2  H  N N 231
+HIS HXT  H  N N 232
+HOH O    O  N N 233
+HOH H1   H  N N 234
+HOH H2   H  N N 235
+LEU N    N  N N 236
+LEU CA   C  N S 237
+LEU C    C  N N 238
+LEU O    O  N N 239
+LEU CB   C  N N 240
+LEU CG   C  N N 241
+LEU CD1  C  N N 242
+LEU CD2  C  N N 243
+LEU OXT  O  N N 244
+LEU H    H  N N 245
+LEU H2   H  N N 246
+LEU HA   H  N N 247
+LEU HB2  H  N N 248
+LEU HB3  H  N N 249
+LEU HG   H  N N 250
+LEU HD11 H  N N 251
+LEU HD12 H  N N 252
+LEU HD13 H  N N 253
+LEU HD21 H  N N 254
+LEU HD22 H  N N 255
+LEU HD23 H  N N 256
+LEU HXT  H  N N 257
+LYS N    N  N N 258
+LYS CA   C  N S 259
+LYS C    C  N N 260
+LYS O    O  N N 261
+LYS CB   C  N N 262
+LYS CG   C  N N 263
+LYS CD   C  N N 264
+LYS CE   C  N N 265
+LYS NZ   N  N N 266
+LYS OXT  O  N N 267
+LYS H    H  N N 268
+LYS H2   H  N N 269
+LYS HA   H  N N 270
+LYS HB2  H  N N 271
+LYS HB3  H  N N 272
+LYS HG2  H  N N 273
+LYS HG3  H  N N 274
+LYS HD2  H  N N 275
+LYS HD3  H  N N 276
+LYS HE2  H  N N 277
+LYS HE3  H  N N 278
+LYS HZ1  H  N N 279
+LYS HZ2  H  N N 280
+LYS HZ3  H  N N 281
+LYS HXT  H  N N 282
+MET N    N  N N 283
+MET CA   C  N S 284
+MET C    C  N N 285
+MET O    O  N N 286
+MET CB   C  N N 287
+MET CG   C  N N 288
+MET SD   S  N N 289
+MET CE   C  N N 290
+MET OXT  O  N N 291
+MET H    H  N N 292
+MET H2   H  N N 293
+MET HA   H  N N 294
+MET HB2  H  N N 295
+MET HB3  H  N N 296
+MET HG2  H  N N 297
+MET HG3  H  N N 298
+MET HE1  H  N N 299
+MET HE2  H  N N 300
+MET HE3  H  N N 301
+MET HXT  H  N N 302
+PHE N    N  N N 303
+PHE CA   C  N S 304
+PHE C    C  N N 305
+PHE O    O  N N 306
+PHE CB   C  N N 307
+PHE CG   C  Y N 308
+PHE CD1  C  Y N 309
+PHE CD2  C  Y N 310
+PHE CE1  C  Y N 311
+PHE CE2  C  Y N 312
+PHE CZ   C  Y N 313
+PHE OXT  O  N N 314
+PHE H    H  N N 315
+PHE H2   H  N N 316
+PHE HA   H  N N 317
+PHE HB2  H  N N 318
+PHE HB3  H  N N 319
+PHE HD1  H  N N 320
+PHE HD2  H  N N 321
+PHE HE1  H  N N 322
+PHE HE2  H  N N 323
+PHE HZ   H  N N 324
+PHE HXT  H  N N 325
+PO4 P    P  N N 326
+PO4 O1   O  N N 327
+PO4 O2   O  N N 328
+PO4 O3   O  N N 329
+PO4 O4   O  N N 330
+PRO N    N  N N 331
+PRO CA   C  N S 332
+PRO C    C  N N 333
+PRO O    O  N N 334
+PRO CB   C  N N 335
+PRO CG   C  N N 336
+PRO CD   C  N N 337
+PRO OXT  O  N N 338
+PRO H    H  N N 339
+PRO HA   H  N N 340
+PRO HB2  H  N N 341
+PRO HB3  H  N N 342
+PRO HG2  H  N N 343
+PRO HG3  H  N N 344
+PRO HD2  H  N N 345
+PRO HD3  H  N N 346
+PRO HXT  H  N N 347
+SER N    N  N N 348
+SER CA   C  N S 349
+SER C    C  N N 350
+SER O    O  N N 351
+SER CB   C  N N 352
+SER OG   O  N N 353
+SER OXT  O  N N 354
+SER H    H  N N 355
+SER H2   H  N N 356
+SER HA   H  N N 357
+SER HB2  H  N N 358
+SER HB3  H  N N 359
+SER HG   H  N N 360
+SER HXT  H  N N 361
+THR N    N  N N 362
+THR CA   C  N S 363
+THR C    C  N N 364
+THR O    O  N N 365
+THR CB   C  N R 366
+THR OG1  O  N N 367
+THR CG2  C  N N 368
+THR OXT  O  N N 369
+THR H    H  N N 370
+THR H2   H  N N 371
+THR HA   H  N N 372
+THR HB   H  N N 373
+THR HG1  H  N N 374
+THR HG21 H  N N 375
+THR HG22 H  N N 376
+THR HG23 H  N N 377
+THR HXT  H  N N 378
+TRP N    N  N N 379
+TRP CA   C  N S 380
+TRP C    C  N N 381
+TRP O    O  N N 382
+TRP CB   C  N N 383
+TRP CG   C  Y N 384
+TRP CD1  C  Y N 385
+TRP CD2  C  Y N 386
+TRP NE1  N  Y N 387
+TRP CE2  C  Y N 388
+TRP CE3  C  Y N 389
+TRP CZ2  C  Y N 390
+TRP CZ3  C  Y N 391
+TRP CH2  C  Y N 392
+TRP OXT  O  N N 393
+TRP H    H  N N 394
+TRP H2   H  N N 395
+TRP HA   H  N N 396
+TRP HB2  H  N N 397
+TRP HB3  H  N N 398
+TRP HD1  H  N N 399
+TRP HE1  H  N N 400
+TRP HE3  H  N N 401
+TRP HZ2  H  N N 402
+TRP HZ3  H  N N 403
+TRP HH2  H  N N 404
+TRP HXT  H  N N 405
+TYR N    N  N N 406
+TYR CA   C  N S 407
+TYR C    C  N N 408
+TYR O    O  N N 409
+TYR CB   C  N N 410
+TYR CG   C  Y N 411
+TYR CD1  C  Y N 412
+TYR CD2  C  Y N 413
+TYR CE1  C  Y N 414
+TYR CE2  C  Y N 415
+TYR CZ   C  Y N 416
+TYR OH   O  N N 417
+TYR OXT  O  N N 418
+TYR H    H  N N 419
+TYR H2   H  N N 420
+TYR HA   H  N N 421
+TYR HB2  H  N N 422
+TYR HB3  H  N N 423
+TYR HD1  H  N N 424
+TYR HD2  H  N N 425
+TYR HE1  H  N N 426
+TYR HE2  H  N N 427
+TYR HH   H  N N 428
+TYR HXT  H  N N 429
+VAL N    N  N N 430
+VAL CA   C  N S 431
+VAL C    C  N N 432
+VAL O    O  N N 433
+VAL CB   C  N N 434
+VAL CG1  C  N N 435
+VAL CG2  C  N N 436
+VAL OXT  O  N N 437
+VAL H    H  N N 438
+VAL H2   H  N N 439
+VAL HA   H  N N 440
+VAL HB   H  N N 441
+VAL HG11 H  N N 442
+VAL HG12 H  N N 443
+VAL HG13 H  N N 444
+VAL HG21 H  N N 445
+VAL HG22 H  N N 446
+VAL HG23 H  N N 447
+VAL HXT  H  N N 448
+#
+loop_
+_chem_comp_bond.comp_id
+_chem_comp_bond.atom_id_1
+_chem_comp_bond.atom_id_2
+_chem_comp_bond.value_order
+_chem_comp_bond.pdbx_aromatic_flag
+_chem_comp_bond.pdbx_stereo_config
+_chem_comp_bond.pdbx_ordinal
+ALA N   CA   sing N N 1
+ALA N   H    sing N N 2
+ALA N   H2   sing N N 3
+ALA CA  C    sing N N 4
+ALA CA  CB   sing N N 5
+ALA CA  HA   sing N N 6
+ALA C   O    doub N N 7
+ALA C   OXT  sing N N 8
+ALA CB  HB1  sing N N 9
+ALA CB  HB2  sing N N 10
+ALA CB  HB3  sing N N 11
+ALA OXT HXT  sing N N 12
+ARG N   CA   sing N N 13
+ARG N   H    sing N N 14
+ARG N   H2   sing N N 15
+ARG CA  C    sing N N 16
+ARG CA  CB   sing N N 17
+ARG CA  HA   sing N N 18
+ARG C   O    doub N N 19
+ARG C   OXT  sing N N 20
+ARG CB  CG   sing N N 21
+ARG CB  HB2  sing N N 22
+ARG CB  HB3  sing N N 23
+ARG CG  CD   sing N N 24
+ARG CG  HG2  sing N N 25
+ARG CG  HG3  sing N N 26
+ARG CD  NE   sing N N 27
+ARG CD  HD2  sing N N 28
+ARG CD  HD3  sing N N 29
+ARG NE  CZ   sing N N 30
+ARG NE  HE   sing N N 31
+ARG CZ  NH1  sing N N 32
+ARG CZ  NH2  doub N N 33
+ARG NH1 HH11 sing N N 34
+ARG NH1 HH12 sing N N 35
+ARG NH2 HH21 sing N N 36
+ARG NH2 HH22 sing N N 37
+ARG OXT HXT  sing N N 38
+ASN N   CA   sing N N 39
+ASN N   H    sing N N 40
+ASN N   H2   sing N N 41
+ASN CA  C    sing N N 42
+ASN CA  CB   sing N N 43
+ASN CA  HA   sing N N 44
+ASN C   O    doub N N 45
+ASN C   OXT  sing N N 46
+ASN CB  CG   sing N N 47
+ASN CB  HB2  sing N N 48
+ASN CB  HB3  sing N N 49
+ASN CG  OD1  doub N N 50
+ASN CG  ND2  sing N N 51
+ASN ND2 HD21 sing N N 52
+ASN ND2 HD22 sing N N 53
+ASN OXT HXT  sing N N 54
+ASP N   CA   sing N N 55
+ASP N   H    sing N N 56
+ASP N   H2   sing N N 57
+ASP CA  C    sing N N 58
+ASP CA  CB   sing N N 59
+ASP CA  HA   sing N N 60
+ASP C   O    doub N N 61
+ASP C   OXT  sing N N 62
+ASP CB  CG   sing N N 63
+ASP CB  HB2  sing N N 64
+ASP CB  HB3  sing N N 65
+ASP CG  OD1  doub N N 66
+ASP CG  OD2  sing N N 67
+ASP OD2 HD2  sing N N 68
+ASP OXT HXT  sing N N 69
+CYS N   CA   sing N N 70
+CYS N   H    sing N N 71
+CYS N   H2   sing N N 72
+CYS CA  C    sing N N 73
+CYS CA  CB   sing N N 74
+CYS CA  HA   sing N N 75
+CYS C   O    doub N N 76
+CYS C   OXT  sing N N 77
+CYS CB  SG   sing N N 78
+CYS CB  HB2  sing N N 79
+CYS CB  HB3  sing N N 80
+CYS SG  HG   sing N N 81
+CYS OXT HXT  sing N N 82
+GLN N   CA   sing N N 83
+GLN N   H    sing N N 84
+GLN N   H2   sing N N 85
+GLN CA  C    sing N N 86
+GLN CA  CB   sing N N 87
+GLN CA  HA   sing N N 88
+GLN C   O    doub N N 89
+GLN C   OXT  sing N N 90
+GLN CB  CG   sing N N 91
+GLN CB  HB2  sing N N 92
+GLN CB  HB3  sing N N 93
+GLN CG  CD   sing N N 94
+GLN CG  HG2  sing N N 95
+GLN CG  HG3  sing N N 96
+GLN CD  OE1  doub N N 97
+GLN CD  NE2  sing N N 98
+GLN NE2 HE21 sing N N 99
+GLN NE2 HE22 sing N N 100
+GLN OXT HXT  sing N N 101
+GLU N   CA   sing N N 102
+GLU N   H    sing N N 103
+GLU N   H2   sing N N 104
+GLU CA  C    sing N N 105
+GLU CA  CB   sing N N 106
+GLU CA  HA   sing N N 107
+GLU C   O    doub N N 108
+GLU C   OXT  sing N N 109
+GLU CB  CG   sing N N 110
+GLU CB  HB2  sing N N 111
+GLU CB  HB3  sing N N 112
+GLU CG  CD   sing N N 113
+GLU CG  HG2  sing N N 114
+GLU CG  HG3  sing N N 115
+GLU CD  OE1  doub N N 116
+GLU CD  OE2  sing N N 117
+GLU OE2 HE2  sing N N 118
+GLU OXT HXT  sing N N 119
+GLY N   CA   sing N N 120
+GLY N   H    sing N N 121
+GLY N   H2   sing N N 122
+GLY CA  C    sing N N 123
+GLY CA  HA2  sing N N 124
+GLY CA  HA3  sing N N 125
+GLY C   O    doub N N 126
+GLY C   OXT  sing N N 127
+GLY OXT HXT  sing N N 128
+HEM CHA C1A  sing N N 129
+HEM CHA C4D  doub N N 130
+HEM CHA HHA  sing N N 131
+HEM CHB C4A  sing N N 132
+HEM CHB C1B  doub N N 133
+HEM CHB HHB  sing N N 134
+HEM CHC C4B  sing N N 135
+HEM CHC C1C  doub N N 136
+HEM CHC HHC  sing N N 137
+HEM CHD C4C  doub N N 138
+HEM CHD C1D  sing N N 139
+HEM CHD HHD  sing N N 140
+HEM C1A C2A  doub Y N 141
+HEM C1A NA   sing Y N 142
+HEM C2A C3A  sing Y N 143
+HEM C2A CAA  sing N N 144
+HEM C3A C4A  doub Y N 145
+HEM C3A CMA  sing N N 146
+HEM C4A NA   sing Y N 147
+HEM CMA HMA  sing N N 148
+HEM CMA HMAA sing N N 149
+HEM CMA HMAB sing N N 150
+HEM CAA CBA  sing N N 151
+HEM CAA HAA  sing N N 152
+HEM CAA HAAA sing N N 153
+HEM CBA CGA  sing N N 154
+HEM CBA HBA  sing N N 155
+HEM CBA HBAA sing N N 156
+HEM CGA O1A  doub N N 157
+HEM CGA O2A  sing N N 158
+HEM C1B C2B  sing N N 159
+HEM C1B NB   sing N N 160
+HEM C2B C3B  doub N N 161
+HEM C2B CMB  sing N N 162
+HEM C3B C4B  sing N N 163
+HEM C3B CAB  sing N N 164
+HEM C4B NB   doub N N 165
+HEM CMB HMB  sing N N 166
+HEM CMB HMBA sing N N 167
+HEM CMB HMBB sing N N 168
+HEM CAB CBB  doub N N 169
+HEM CAB HAB  sing N N 170
+HEM CBB HBB  sing N N 171
+HEM CBB HBBA sing N N 172
+HEM C1C C2C  sing Y N 173
+HEM C1C NC   sing Y N 174
+HEM C2C C3C  doub Y N 175
+HEM C2C CMC  sing N N 176
+HEM C3C C4C  sing Y N 177
+HEM C3C CAC  sing N N 178
+HEM C4C NC   sing Y N 179
+HEM CMC HMC  sing N N 180
+HEM CMC HMCA sing N N 181
+HEM CMC HMCB sing N N 182
+HEM CAC CBC  doub N N 183
+HEM CAC HAC  sing N N 184
+HEM CBC HBC  sing N N 185
+HEM CBC HBCA sing N N 186
+HEM C1D C2D  sing N N 187
+HEM C1D ND   doub N N 188
+HEM C2D C3D  doub N N 189
+HEM C2D CMD  sing N N 190
+HEM C3D C4D  sing N N 191
+HEM C3D CAD  sing N N 192
+HEM C4D ND   sing N N 193
+HEM CMD HMD  sing N N 194
+HEM CMD HMDA sing N N 195
+HEM CMD HMDB sing N N 196
+HEM CAD CBD  sing N N 197
+HEM CAD HAD  sing N N 198
+HEM CAD HADA sing N N 199
+HEM CBD CGD  sing N N 200
+HEM CBD HBD  sing N N 201
+HEM CBD HBDA sing N N 202
+HEM CGD O1D  doub N N 203
+HEM CGD O2D  sing N N 204
+HEM O2A H2A  sing N N 205
+HEM O2D H2D  sing N N 206
+HEM FE  NA   sing N N 207
+HEM FE  NB   sing N N 208
+HEM FE  NC   sing N N 209
+HEM FE  ND   sing N N 210
+HIS N   CA   sing N N 211
+HIS N   H    sing N N 212
+HIS N   H2   sing N N 213
+HIS CA  C    sing N N 214
+HIS CA  CB   sing N N 215
+HIS CA  HA   sing N N 216
+HIS C   O    doub N N 217
+HIS C   OXT  sing N N 218
+HIS CB  CG   sing N N 219
+HIS CB  HB2  sing N N 220
+HIS CB  HB3  sing N N 221
+HIS CG  ND1  sing Y N 222
+HIS CG  CD2  doub Y N 223
+HIS ND1 CE1  doub Y N 224
+HIS ND1 HD1  sing N N 225
+HIS CD2 NE2  sing Y N 226
+HIS CD2 HD2  sing N N 227
+HIS CE1 NE2  sing Y N 228
+HIS CE1 HE1  sing N N 229
+HIS NE2 HE2  sing N N 230
+HIS OXT HXT  sing N N 231
+HOH O   H1   sing N N 232
+HOH O   H2   sing N N 233
+LEU N   CA   sing N N 234
+LEU N   H    sing N N 235
+LEU N   H2   sing N N 236
+LEU CA  C    sing N N 237
+LEU CA  CB   sing N N 238
+LEU CA  HA   sing N N 239
+LEU C   O    doub N N 240
+LEU C   OXT  sing N N 241
+LEU CB  CG   sing N N 242
+LEU CB  HB2  sing N N 243
+LEU CB  HB3  sing N N 244
+LEU CG  CD1  sing N N 245
+LEU CG  CD2  sing N N 246
+LEU CG  HG   sing N N 247
+LEU CD1 HD11 sing N N 248
+LEU CD1 HD12 sing N N 249
+LEU CD1 HD13 sing N N 250
+LEU CD2 HD21 sing N N 251
+LEU CD2 HD22 sing N N 252
+LEU CD2 HD23 sing N N 253
+LEU OXT HXT  sing N N 254
+LYS N   CA   sing N N 255
+LYS N   H    sing N N 256
+LYS N   H2   sing N N 257
+LYS CA  C    sing N N 258
+LYS CA  CB   sing N N 259
+LYS CA  HA   sing N N 260
+LYS C   O    doub N N 261
+LYS C   OXT  sing N N 262
+LYS CB  CG   sing N N 263
+LYS CB  HB2  sing N N 264
+LYS CB  HB3  sing N N 265
+LYS CG  CD   sing N N 266
+LYS CG  HG2  sing N N 267
+LYS CG  HG3  sing N N 268
+LYS CD  CE   sing N N 269
+LYS CD  HD2  sing N N 270
+LYS CD  HD3  sing N N 271
+LYS CE  NZ   sing N N 272
+LYS CE  HE2  sing N N 273
+LYS CE  HE3  sing N N 274
+LYS NZ  HZ1  sing N N 275
+LYS NZ  HZ2  sing N N 276
+LYS NZ  HZ3  sing N N 277
+LYS OXT HXT  sing N N 278
+MET N   CA   sing N N 279
+MET N   H    sing N N 280
+MET N   H2   sing N N 281
+MET CA  C    sing N N 282
+MET CA  CB   sing N N 283
+MET CA  HA   sing N N 284
+MET C   O    doub N N 285
+MET C   OXT  sing N N 286
+MET CB  CG   sing N N 287
+MET CB  HB2  sing N N 288
+MET CB  HB3  sing N N 289
+MET CG  SD   sing N N 290
+MET CG  HG2  sing N N 291
+MET CG  HG3  sing N N 292
+MET SD  CE   sing N N 293
+MET CE  HE1  sing N N 294
+MET CE  HE2  sing N N 295
+MET CE  HE3  sing N N 296
+MET OXT HXT  sing N N 297
+PHE N   CA   sing N N 298
+PHE N   H    sing N N 299
+PHE N   H2   sing N N 300
+PHE CA  C    sing N N 301
+PHE CA  CB   sing N N 302
+PHE CA  HA   sing N N 303
+PHE C   O    doub N N 304
+PHE C   OXT  sing N N 305
+PHE CB  CG   sing N N 306
+PHE CB  HB2  sing N N 307
+PHE CB  HB3  sing N N 308
+PHE CG  CD1  doub Y N 309
+PHE CG  CD2  sing Y N 310
+PHE CD1 CE1  sing Y N 311
+PHE CD1 HD1  sing N N 312
+PHE CD2 CE2  doub Y N 313
+PHE CD2 HD2  sing N N 314
+PHE CE1 CZ   doub Y N 315
+PHE CE1 HE1  sing N N 316
+PHE CE2 CZ   sing Y N 317
+PHE CE2 HE2  sing N N 318
+PHE CZ  HZ   sing N N 319
+PHE OXT HXT  sing N N 320
+PO4 P   O1   doub N N 321
+PO4 P   O2   sing N N 322
+PO4 P   O3   sing N N 323
+PO4 P   O4   sing N N 324
+PRO N   CA   sing N N 325
+PRO N   CD   sing N N 326
+PRO N   H    sing N N 327
+PRO CA  C    sing N N 328
+PRO CA  CB   sing N N 329
+PRO CA  HA   sing N N 330
+PRO C   O    doub N N 331
+PRO C   OXT  sing N N 332
+PRO CB  CG   sing N N 333
+PRO CB  HB2  sing N N 334
+PRO CB  HB3  sing N N 335
+PRO CG  CD   sing N N 336
+PRO CG  HG2  sing N N 337
+PRO CG  HG3  sing N N 338
+PRO CD  HD2  sing N N 339
+PRO CD  HD3  sing N N 340
+PRO OXT HXT  sing N N 341
+SER N   CA   sing N N 342
+SER N   H    sing N N 343
+SER N   H2   sing N N 344
+SER CA  C    sing N N 345
+SER CA  CB   sing N N 346
+SER CA  HA   sing N N 347
+SER C   O    doub N N 348
+SER C   OXT  sing N N 349
+SER CB  OG   sing N N 350
+SER CB  HB2  sing N N 351
+SER CB  HB3  sing N N 352
+SER OG  HG   sing N N 353
+SER OXT HXT  sing N N 354
+THR N   CA   sing N N 355
+THR N   H    sing N N 356
+THR N   H2   sing N N 357
+THR CA  C    sing N N 358
+THR CA  CB   sing N N 359
+THR CA  HA   sing N N 360
+THR C   O    doub N N 361
+THR C   OXT  sing N N 362
+THR CB  OG1  sing N N 363
+THR CB  CG2  sing N N 364
+THR CB  HB   sing N N 365
+THR OG1 HG1  sing N N 366
+THR CG2 HG21 sing N N 367
+THR CG2 HG22 sing N N 368
+THR CG2 HG23 sing N N 369
+THR OXT HXT  sing N N 370
+TRP N   CA   sing N N 371
+TRP N   H    sing N N 372
+TRP N   H2   sing N N 373
+TRP CA  C    sing N N 374
+TRP CA  CB   sing N N 375
+TRP CA  HA   sing N N 376
+TRP C   O    doub N N 377
+TRP C   OXT  sing N N 378
+TRP CB  CG   sing N N 379
+TRP CB  HB2  sing N N 380
+TRP CB  HB3  sing N N 381
+TRP CG  CD1  doub Y N 382
+TRP CG  CD2  sing Y N 383
+TRP CD1 NE1  sing Y N 384
+TRP CD1 HD1  sing N N 385
+TRP CD2 CE2  doub Y N 386
+TRP CD2 CE3  sing Y N 387
+TRP NE1 CE2  sing Y N 388
+TRP NE1 HE1  sing N N 389
+TRP CE2 CZ2  sing Y N 390
+TRP CE3 CZ3  doub Y N 391
+TRP CE3 HE3  sing N N 392
+TRP CZ2 CH2  doub Y N 393
+TRP CZ2 HZ2  sing N N 394
+TRP CZ3 CH2  sing Y N 395
+TRP CZ3 HZ3  sing N N 396
+TRP CH2 HH2  sing N N 397
+TRP OXT HXT  sing N N 398
+TYR N   CA   sing N N 399
+TYR N   H    sing N N 400
+TYR N   H2   sing N N 401
+TYR CA  C    sing N N 402
+TYR CA  CB   sing N N 403
+TYR CA  HA   sing N N 404
+TYR C   O    doub N N 405
+TYR C   OXT  sing N N 406
+TYR CB  CG   sing N N 407
+TYR CB  HB2  sing N N 408
+TYR CB  HB3  sing N N 409
+TYR CG  CD1  doub Y N 410
+TYR CG  CD2  sing Y N 411
+TYR CD1 CE1  sing Y N 412
+TYR CD1 HD1  sing N N 413
+TYR CD2 CE2  doub Y N 414
+TYR CD2 HD2  sing N N 415
+TYR CE1 CZ   doub Y N 416
+TYR CE1 HE1  sing N N 417
+TYR CE2 CZ   sing Y N 418
+TYR CE2 HE2  sing N N 419
+TYR CZ  OH   sing N N 420
+TYR OH  HH   sing N N 421
+TYR OXT HXT  sing N N 422
+VAL N   CA   sing N N 423
+VAL N   H    sing N N 424
+VAL N   H2   sing N N 425
+VAL CA  C    sing N N 426
+VAL CA  CB   sing N N 427
+VAL CA  HA   sing N N 428
+VAL C   O    doub N N 429
+VAL C   OXT  sing N N 430
+VAL CB  CG1  sing N N 431
+VAL CB  CG2  sing N N 432
+VAL CB  HB   sing N N 433
+VAL CG1 HG11 sing N N 434
+VAL CG1 HG12 sing N N 435
+VAL CG1 HG13 sing N N 436
+VAL CG2 HG21 sing N N 437
+VAL CG2 HG22 sing N N 438
+VAL CG2 HG23 sing N N 439
+VAL OXT HXT  sing N N 440
+#
+_atom_sites.entry_id                    4HHB
+_atom_sites.fract_transf_matrix[1][1]   0.015835
+_atom_sites.fract_transf_matrix[1][2]   0.000000
+_atom_sites.fract_transf_matrix[1][3]   0.002604
+_atom_sites.fract_transf_vector[1]      0.000000
+_atom_sites.fract_transf_matrix[2][1]   0.000000
+_atom_sites.fract_transf_matrix[2][2]   0.011963
+_atom_sites.fract_transf_matrix[2][3]   0.000000
+_atom_sites.fract_transf_vector[2]      0.000000
+_atom_sites.fract_transf_matrix[3][1]   0.000000
+_atom_sites.fract_transf_matrix[3][2]   0.000000
+_atom_sites.fract_transf_matrix[3][3]   0.018837
+_atom_sites.fract_transf_vector[3]      0.000000
+#
+_atom_sites_footnote.id     1
+_atom_sites_footnote.text   'PROBABLY PHOSPHATE GROUP.'
+#
+loop_
+_atom_type.symbol
+C
+FE
+N
+O
+P
+S
+#
+loop_
+_atom_site.group_PDB
+_atom_site.id
+_atom_site.type_symbol
+_atom_site.label_atom_id
+_atom_site.label_alt_id
+_atom_site.label_comp_id
+_atom_site.label_asym_id
+_atom_site.label_entity_id
+_atom_site.label_seq_id
+_atom_site.pdbx_PDB_ins_code
+_atom_site.Cartn_x
+_atom_site.Cartn_y
+_atom_site.Cartn_z
+_atom_site.occupancy
+_atom_site.B_iso_or_equiv
+_atom_site.pdbx_formal_charge
+_atom_site.auth_seq_id
+_atom_site.auth_comp_id
+_atom_site.auth_asym_id
+_atom_site.auth_atom_id
+_atom_site.pdbx_PDB_model_num
+ATOM   1    N  N   . VAL A 1 1   ? 19.323  29.727  42.781 1.00 49.05 ? 1   VAL A N   1
+ATOM   2    C  CA  . VAL A 1 1   ? 20.141  30.469  42.414 1.00 43.14 ? 1   VAL A CA  1
+ATOM   3    C  C   . VAL A 1 1   ? 21.664  29.857  42.548 1.00 24.80 ? 1   VAL A C   1
+ATOM   4    O  O   . VAL A 1 1   ? 21.985  29.541  43.704 1.00 37.68 ? 1   VAL A O   1
+ATOM   5    C  CB  . VAL A 1 1   ? 19.887  31.918  43.524 1.00 72.12 ? 1   VAL A CB  1
+ATOM   6    C  CG1 . VAL A 1 1   ? 20.656  32.850  42.999 1.00 61.79 ? 1   VAL A CG1 1
+ATOM   7    C  CG2 . VAL A 1 1   ? 18.692  31.583  43.506 1.00 80.12 ? 1   VAL A CG2 1
+ATOM   8    N  N   . LEU A 1 2   ? 22.284  30.338  41.520 1.00 26.44 ? 2   LEU A N   1
+ATOM   9    C  CA  . LEU A 1 2   ? 23.773  29.985  41.873 1.00 26.32 ? 2   LEU A CA  1
+ATOM   10   C  C   . LEU A 1 2   ? 24.698  31.236  42.725 1.00 32.96 ? 2   LEU A C   1
+ATOM   11   O  O   . LEU A 1 2   ? 24.359  32.232  42.013 1.00 31.90 ? 2   LEU A O   1
+ATOM   12   C  CB  . LEU A 1 2   ? 24.180  29.902  40.374 1.00 29.23 ? 2   LEU A CB  1
+ATOM   13   C  CG  . LEU A 1 2   ? 24.177  28.761  39.582 1.00 37.71 ? 2   LEU A CG  1
+ATOM   14   C  CD1 . LEU A 1 2   ? 24.140  27.432  40.098 1.00 39.10 ? 2   LEU A CD1 1
+ATOM   15   C  CD2 . LEU A 1 2   ? 24.210  28.919  37.923 1.00 37.47 ? 2   LEU A CD2 1
+ATOM   16   N  N   . SER A 1 3   ? 25.002  30.808  43.594 1.00 28.01 ? 3   SER A N   1
+ATOM   17   C  CA  . SER A 1 3   ? 25.913  31.899  44.386 1.00 26.03 ? 3   SER A CA  1
+ATOM   18   C  C   . SER A 1 3   ? 26.954  32.120  43.503 1.00 25.99 ? 3   SER A C   1
+ATOM   19   O  O   . SER A 1 3   ? 27.580  31.417  42.575 1.00 25.98 ? 3   SER A O   1
+ATOM   20   C  CB  . SER A 1 3   ? 26.339  31.102  45.563 1.00 23.41 ? 3   SER A CB  1
+ATOM   21   O  OG  . SER A 1 3   ? 27.242  30.187  45.530 1.00 30.00 ? 3   SER A OG  1
+ATOM   22   N  N   . PRO A 1 4   ? 28.057  33.118  44.145 1.00 37.49 ? 4   PRO A N   1
+ATOM   23   C  CA  . PRO A 1 4   ? 28.906  33.371  43.168 1.00 38.81 ? 4   PRO A CA  1
+ATOM   24   C  C   . PRO A 1 4   ? 30.214  32.554  43.225 1.00 25.63 ? 4   PRO A C   1
+ATOM   25   O  O   . PRO A 1 4   ? 30.831  31.987  42.344 1.00 34.38 ? 4   PRO A O   1
+ATOM   26   C  CB  . PRO A 1 4   ? 29.916  34.531  43.968 1.00 50.44 ? 4   PRO A CB  1
+ATOM   27   C  CG  . PRO A 1 4   ? 28.712  35.195  44.473 1.00 43.42 ? 4   PRO A CG  1
+ATOM   28   C  CD  . PRO A 1 4   ? 27.379  34.390  44.646 1.00 42.77 ? 4   PRO A CD  1
+ATOM   29   N  N   . ALA A 1 5   ? 30.083  31.678  44.550 1.00 24.33 ? 5   ALA A N   1
+ATOM   30   C  CA  . ALA A 1 5   ? 31.123  30.854  44.608 1.00 24.06 ? 5   ALA A CA  1
+ATOM   31   C  C   . ALA A 1 5   ? 30.675  29.484  43.759 1.00 20.01 ? 5   ALA A C   1
+ATOM   32   O  O   . ALA A 1 5   ? 31.598  28.842  43.152 1.00 24.46 ? 5   ALA A O   1
+ATOM   33   C  CB  . ALA A 1 5   ? 31.015  30.218  46.253 1.00 28.15 ? 5   ALA A CB  1
+ATOM   34   N  N   . ASP A 1 6   ? 29.272  29.194  43.577 1.00 21.19 ? 6   ASP A N   1
+ATOM   35   C  CA  . ASP A 1 6   ? 28.883  28.227  42.499 1.00 23.14 ? 6   ASP A CA  1
+ATOM   36   C  C   . ASP A 1 6   ? 29.575  28.619  41.206 1.00 15.75 ? 6   ASP A C   1
+ATOM   37   O  O   . ASP A 1 6   ? 30.048  27.586  40.573 1.00 18.92 ? 6   ASP A O   1
+ATOM   38   C  CB  . ASP A 1 6   ? 27.485  28.065  42.473 1.00 18.68 ? 6   ASP A CB  1
+ATOM   39   C  CG  . ASP A 1 6   ? 26.874  27.385  43.720 1.00 21.70 ? 6   ASP A CG  1
+ATOM   40   O  OD1 . ASP A 1 6   ? 27.375  26.460  44.316 1.00 19.76 ? 6   ASP A OD1 1
+ATOM   41   O  OD2 . ASP A 1 6   ? 25.719  27.885  43.957 1.00 21.26 ? 6   ASP A OD2 1
+ATOM   42   N  N   . LYS A 1 7   ? 29.277  29.964  40.920 1.00 15.62 ? 7   LYS A N   1
+ATOM   43   C  CA  . LYS A 1 7   ? 30.058  30.174  39.521 1.00 26.74 ? 7   LYS A CA  1
+ATOM   44   C  C   . LYS A 1 7   ? 31.481  29.979  39.107 1.00 24.82 ? 7   LYS A C   1
+ATOM   45   O  O   . LYS A 1 7   ? 31.841  29.367  38.199 1.00 21.36 ? 7   LYS A O   1
+ATOM   46   C  CB  . LYS A 1 7   ? 29.362  31.513  39.112 1.00 28.73 ? 7   LYS A CB  1
+ATOM   47   C  CG  . LYS A 1 7   ? 27.887  31.712  39.434 1.00 34.11 ? 7   LYS A CG  1
+ATOM   48   C  CD  . LYS A 1 7   ? 27.434  33.307  39.171 1.00 46.50 ? 7   LYS A CD  1
+ATOM   49   C  CE  . LYS A 1 7   ? 26.166  33.430  39.863 1.00 40.75 ? 7   LYS A CE  1
+ATOM   50   N  NZ  . LYS A 1 7   ? 26.143  34.856  39.243 1.00 50.05 ? 7   LYS A NZ  1
+ATOM   51   N  N   . THR A 1 8   ? 32.142  30.276  40.526 1.00 20.80 ? 8   THR A N   1
+ATOM   52   C  CA  . THR A 1 8   ? 33.577  29.907  40.396 1.00 23.21 ? 8   THR A CA  1
+ATOM   53   C  C   . THR A 1 8   ? 34.010  28.663  40.095 1.00 17.85 ? 8   THR A C   1
+ATOM   54   O  O   . THR A 1 8   ? 34.804  28.109  39.456 1.00 20.04 ? 8   THR A O   1
+ATOM   55   C  CB  . THR A 1 8   ? 34.201  30.764  41.734 1.00 31.90 ? 8   THR A CB  1
+ATOM   56   O  OG1 . THR A 1 8   ? 33.986  31.993  41.596 1.00 31.01 ? 8   THR A OG1 1
+ATOM   57   C  CG2 . THR A 1 8   ? 35.426  30.415  41.716 1.00 43.78 ? 8   THR A CG2 1
+ATOM   58   N  N   . ASN A 1 9   ? 33.146  27.738  40.929 1.00 16.13 ? 9   ASN A N   1
+ATOM   59   C  CA  . ASN A 1 9   ? 33.275  26.383  40.940 1.00 17.84 ? 9   ASN A CA  1
+ATOM   60   C  C   . ASN A 1 9   ? 33.113  25.658  39.458 1.00 14.45 ? 9   ASN A C   1
+ATOM   61   O  O   . ASN A 1 9   ? 33.642  24.721  39.133 1.00 21.78 ? 9   ASN A O   1
+ATOM   62   C  CB  . ASN A 1 9   ? 32.451  25.650  41.980 1.00 20.10 ? 9   ASN A CB  1
+ATOM   63   C  CG  . ASN A 1 9   ? 32.954  26.032  43.366 1.00 34.82 ? 9   ASN A CG  1
+ATOM   64   O  OD1 . ASN A 1 9   ? 34.126  26.287  43.620 1.00 26.93 ? 9   ASN A OD1 1
+ATOM   65   N  ND2 . ASN A 1 9   ? 32.273  25.663  44.310 1.00 28.08 ? 9   ASN A ND2 1
+ATOM   66   N  N   . VAL A 1 10  ? 31.933  26.055  38.904 1.00 19.64 ? 10  VAL A N   1
+ATOM   67   C  CA  . VAL A 1 10  ? 31.494  25.556  37.564 1.00 13.04 ? 10  VAL A CA  1
+ATOM   68   C  C   . VAL A 1 10  ? 32.720  26.076  36.532 1.00 18.71 ? 10  VAL A C   1
+ATOM   69   O  O   . VAL A 1 10  ? 33.036  25.252  35.673 1.00 22.34 ? 10  VAL A O   1
+ATOM   70   C  CB  . VAL A 1 10  ? 30.155  26.031  37.319 1.00 19.07 ? 10  VAL A CB  1
+ATOM   71   C  CG1 . VAL A 1 10  ? 29.865  25.687  35.930 1.00 21.59 ? 10  VAL A CG1 1
+ATOM   72   C  CG2 . VAL A 1 10  ? 29.160  25.612  38.122 1.00 22.75 ? 10  VAL A CG2 1
+ATOM   73   N  N   . LYS A 1 11  ? 32.991  27.369  36.724 1.00 18.31 ? 11  LYS A N   1
+ATOM   74   C  CA  . LYS A 1 11  ? 33.940  27.959  35.592 1.00 24.80 ? 11  LYS A CA  1
+ATOM   75   C  C   . LYS A 1 11  ? 35.319  27.185  35.909 1.00 19.51 ? 11  LYS A C   1
+ATOM   76   O  O   . LYS A 1 11  ? 36.019  26.715  34.889 1.00 22.33 ? 11  LYS A O   1
+ATOM   77   C  CB  . LYS A 1 11  ? 34.208  29.311  35.820 1.00 39.77 ? 11  LYS A CB  1
+ATOM   78   C  CG  . LYS A 1 11  ? 33.202  30.123  35.532 1.00 34.41 ? 11  LYS A CG  1
+ATOM   79   C  CD  . LYS A 1 11  ? 33.427  31.408  35.371 1.00 46.95 ? 11  LYS A CD  1
+ATOM   80   C  CE  . LYS A 1 11  ? 31.840  32.105  34.452 1.00 49.55 ? 11  LYS A CE  1
+ATOM   81   N  NZ  . LYS A 1 11  ? 31.837  33.372  34.990 1.00 78.67 ? 11  LYS A NZ  1
+ATOM   82   N  N   . ALA A 1 12  ? 35.559  26.560  37.085 1.00 20.60 ? 12  ALA A N   1
+ATOM   83   C  CA  . ALA A 1 12  ? 36.832  26.247  36.892 1.00 25.98 ? 12  ALA A CA  1
+ATOM   84   C  C   . ALA A 1 12  ? 36.793  24.842  36.939 1.00 38.04 ? 12  ALA A C   1
+ATOM   85   O  O   . ALA A 1 12  ? 37.604  24.054  36.025 1.00 31.19 ? 12  ALA A O   1
+ATOM   86   C  CB  . ALA A 1 12  ? 37.186  26.023  38.483 1.00 28.13 ? 12  ALA A CB  1
+ATOM   87   N  N   . ALA A 1 13  ? 35.697  24.001  36.953 1.00 21.69 ? 13  ALA A N   1
+ATOM   88   C  CA  . ALA A 1 13  ? 35.708  22.676  36.618 1.00 19.11 ? 13  ALA A CA  1
+ATOM   89   C  C   . ALA A 1 13  ? 35.554  22.420  34.918 1.00 22.93 ? 13  ALA A C   1
+ATOM   90   O  O   . ALA A 1 13  ? 36.099  21.504  34.436 1.00 24.98 ? 13  ALA A O   1
+ATOM   91   C  CB  . ALA A 1 13  ? 34.415  22.026  37.306 1.00 23.17 ? 13  ALA A CB  1
+ATOM   92   N  N   . TRP A 1 14  ? 34.674  23.405  34.488 1.00 22.14 ? 14  TRP A N   1
+ATOM   93   C  CA  . TRP A 1 14  ? 34.467  23.218  33.030 1.00 21.27 ? 14  TRP A CA  1
+ATOM   94   C  C   . TRP A 1 14  ? 35.810  23.715  32.187 1.00 28.97 ? 14  TRP A C   1
+ATOM   95   O  O   . TRP A 1 14  ? 36.104  23.111  31.138 1.00 27.61 ? 14  TRP A O   1
+ATOM   96   C  CB  . TRP A 1 14  ? 32.998  24.227  32.631 1.00 29.00 ? 14  TRP A CB  1
+ATOM   97   C  CG  . TRP A 1 14  ? 32.826  23.615  31.585 1.00 25.79 ? 14  TRP A CG  1
+ATOM   98   C  CD1 . TRP A 1 14  ? 32.942  24.430  30.133 1.00 22.38 ? 14  TRP A CD1 1
+ATOM   99   C  CD2 . TRP A 1 14  ? 31.864  22.532  31.263 1.00 20.46 ? 14  TRP A CD2 1
+ATOM   100  N  NE1 . TRP A 1 14  ? 32.091  23.452  29.315 1.00 29.74 ? 14  TRP A NE1 1
+ATOM   101  C  CE2 . TRP A 1 14  ? 31.537  22.524  29.666 1.00 27.75 ? 14  TRP A CE2 1
+ATOM   102  C  CE3 . TRP A 1 14  ? 31.357  21.442  31.937 1.00 34.00 ? 14  TRP A CE3 1
+ATOM   103  C  CZ2 . TRP A 1 14  ? 30.923  21.636  29.268 1.00 34.81 ? 14  TRP A CZ2 1
+ATOM   104  C  CZ3 . TRP A 1 14  ? 30.604  20.519  31.143 1.00 42.11 ? 14  TRP A CZ3 1
+ATOM   105  C  CH2 . TRP A 1 14  ? 30.479  20.726  29.816 1.00 47.54 ? 14  TRP A CH2 1
+ATOM   106  N  N   . GLY A 1 15  ? 36.554  24.532  33.024 1.00 40.92 ? 15  GLY A N   1
+ATOM   107  C  CA  . GLY A 1 15  ? 37.583  25.041  32.159 1.00 38.97 ? 15  GLY A CA  1
+ATOM   108  C  C   . GLY A 1 15  ? 38.439  23.595  32.385 1.00 34.61 ? 15  GLY A C   1
+ATOM   109  O  O   . GLY A 1 15  ? 39.292  23.569  30.952 1.00 36.24 ? 15  GLY A O   1
+ATOM   110  N  N   . LYS A 1 16  ? 38.813  23.060  33.031 1.00 35.37 ? 16  LYS A N   1
+ATOM   111  C  CA  . LYS A 1 16  ? 39.261  21.595  33.148 1.00 29.09 ? 16  LYS A CA  1
+ATOM   112  C  C   . LYS A 1 16  ? 39.041  20.671  31.899 1.00 27.28 ? 16  LYS A C   1
+ATOM   113  O  O   . LYS A 1 16  ? 39.653  19.882  31.488 1.00 36.62 ? 16  LYS A O   1
+ATOM   114  C  CB  . LYS A 1 16  ? 39.285  20.770  34.453 1.00 30.47 ? 16  LYS A CB  1
+ATOM   115  C  CG  . LYS A 1 16  ? 40.457  19.570  34.277 1.00 47.02 ? 16  LYS A CG  1
+ATOM   116  C  CD  . LYS A 1 16  ? 42.065  20.737  34.566 1.00 66.41 ? 16  LYS A CD  1
+ATOM   117  C  CE  . LYS A 1 16  ? 42.400  18.931  34.013 1.00 65.00 ? 16  LYS A CE  1
+ATOM   118  N  NZ  . LYS A 1 16  ? 42.386  17.736  34.775 1.00 69.28 ? 16  LYS A NZ  1
+ATOM   119  N  N   . VAL A 1 17  ? 37.560  20.787  31.598 1.00 40.63 ? 17  VAL A N   1
+ATOM   120  C  CA  . VAL A 1 17  ? 36.916  20.003  30.839 1.00 32.19 ? 17  VAL A CA  1
+ATOM   121  C  C   . VAL A 1 17  ? 37.714  20.042  29.052 1.00 51.53 ? 17  VAL A C   1
+ATOM   122  O  O   . VAL A 1 17  ? 38.053  19.397  28.891 1.00 36.95 ? 17  VAL A O   1
+ATOM   123  C  CB  . VAL A 1 17  ? 35.556  19.802  30.826 1.00 24.77 ? 17  VAL A CB  1
+ATOM   124  C  CG1 . VAL A 1 17  ? 34.992  19.492  29.499 1.00 21.73 ? 17  VAL A CG1 1
+ATOM   125  C  CG2 . VAL A 1 17  ? 34.793  19.260  32.089 1.00 23.90 ? 17  VAL A CG2 1
+ATOM   126  N  N   . GLY A 1 18  ? 37.672  21.623  29.262 1.00 36.07 ? 18  GLY A N   1
+ATOM   127  C  CA  . GLY A 1 18  ? 38.436  22.192  28.188 1.00 37.64 ? 18  GLY A CA  1
+ATOM   128  C  C   . GLY A 1 18  ? 37.724  21.396  26.664 1.00 27.84 ? 18  GLY A C   1
+ATOM   129  O  O   . GLY A 1 18  ? 36.434  21.732  26.580 1.00 34.16 ? 18  GLY A O   1
+ATOM   130  N  N   . ALA A 1 19  ? 38.690  20.739  26.186 1.00 35.70 ? 19  ALA A N   1
+ATOM   131  C  CA  . ALA A 1 19  ? 38.676  20.710  24.774 1.00 37.59 ? 19  ALA A CA  1
+ATOM   132  C  C   . ALA A 1 19  ? 38.192  19.125  24.814 1.00 34.69 ? 19  ALA A C   1
+ATOM   133  O  O   . ALA A 1 19  ? 37.606  18.539  23.606 1.00 48.59 ? 19  ALA A O   1
+ATOM   134  C  CB  . ALA A 1 19  ? 39.890  20.486  23.851 1.00 46.19 ? 19  ALA A CB  1
+ATOM   135  N  N   . HIS A 1 20  ? 37.787  18.414  25.852 1.00 20.24 ? 20  HIS A N   1
+ATOM   136  C  CA  . HIS A 1 20  ? 37.288  17.018  25.894 1.00 19.03 ? 20  HIS A CA  1
+ATOM   137  C  C   . HIS A 1 20  ? 35.735  17.350  25.947 1.00 17.82 ? 20  HIS A C   1
+ATOM   138  O  O   . HIS A 1 20  ? 35.006  16.255  26.085 1.00 20.59 ? 20  HIS A O   1
+ATOM   139  C  CB  . HIS A 1 20  ? 37.591  16.412  27.081 1.00 31.92 ? 20  HIS A CB  1
+ATOM   140  C  CG  . HIS A 1 20  ? 38.818  15.858  27.318 1.00 45.35 ? 20  HIS A CG  1
+ATOM   141  N  ND1 . HIS A 1 20  ? 39.616  15.003  26.078 1.00 52.86 ? 20  HIS A ND1 1
+ATOM   142  C  CD2 . HIS A 1 20  ? 39.956  16.803  27.705 1.00 43.12 ? 20  HIS A CD2 1
+ATOM   143  C  CE1 . HIS A 1 20  ? 40.744  15.113  26.724 1.00 68.75 ? 20  HIS A CE1 1
+ATOM   144  N  NE2 . HIS A 1 20  ? 41.076  15.758  27.450 1.00 55.89 ? 20  HIS A NE2 1
+ATOM   145  N  N   . ALA A 1 21  ? 35.289  18.461  25.830 1.00 29.55 ? 21  ALA A N   1
+ATOM   146  C  CA  . ALA A 1 21  ? 33.825  18.860  26.213 1.00 29.36 ? 21  ALA A CA  1
+ATOM   147  C  C   . ALA A 1 21  ? 32.921  17.251  25.240 1.00 46.23 ? 21  ALA A C   1
+ATOM   148  O  O   . ALA A 1 21  ? 32.024  17.267  25.826 1.00 27.88 ? 21  ALA A O   1
+ATOM   149  C  CB  . ALA A 1 21  ? 33.439  20.204  26.284 1.00 28.64 ? 21  ALA A CB  1
+ATOM   150  N  N   . GLY A 1 22  ? 33.121  17.872  24.106 1.00 27.74 ? 22  GLY A N   1
+ATOM   151  C  CA  . GLY A 1 22  ? 32.458  16.809  23.303 1.00 29.10 ? 22  GLY A CA  1
+ATOM   152  C  C   . GLY A 1 22  ? 32.386  15.634  23.526 1.00 40.30 ? 22  GLY A C   1
+ATOM   153  O  O   . GLY A 1 22  ? 31.679  14.644  23.206 1.00 33.08 ? 22  GLY A O   1
+ATOM   154  N  N   . GLU A 1 23  ? 33.633  14.841  23.696 1.00 22.76 ? 23  GLU A N   1
+ATOM   155  C  CA  . GLU A 1 23  ? 33.758  13.411  23.993 1.00 14.60 ? 23  GLU A CA  1
+ATOM   156  C  C   . GLU A 1 23  ? 32.902  13.122  25.335 1.00 13.41 ? 23  GLU A C   1
+ATOM   157  O  O   . GLU A 1 23  ? 32.456  12.018  25.508 1.00 16.24 ? 23  GLU A O   1
+ATOM   158  C  CB  . GLU A 1 23  ? 35.369  13.376  24.231 1.00 20.16 ? 23  GLU A CB  1
+ATOM   159  C  CG  . GLU A 1 23  ? 35.681  11.895  24.352 1.00 40.65 ? 23  GLU A CG  1
+ATOM   160  C  CD  . GLU A 1 23  ? 37.773  11.969  24.493 1.00 70.75 ? 23  GLU A CD  1
+ATOM   161  O  OE1 . GLU A 1 23  ? 37.498  11.638  26.157 1.00 57.57 ? 23  GLU A OE1 1
+ATOM   162  O  OE2 . GLU A 1 23  ? 38.146  13.187  23.876 1.00 57.46 ? 23  GLU A OE2 1
+ATOM   163  N  N   . TYR A 1 24  ? 33.071  14.032  26.284 1.00 18.60 ? 24  TYR A N   1
+ATOM   164  C  CA  . TYR A 1 24  ? 32.420  13.791  27.541 1.00 26.35 ? 24  TYR A CA  1
+ATOM   165  C  C   . TYR A 1 24  ? 30.918  13.964  27.214 1.00 17.67 ? 24  TYR A C   1
+ATOM   166  O  O   . TYR A 1 24  ? 30.168  13.175  27.952 1.00 17.15 ? 24  TYR A O   1
+ATOM   167  C  CB  . TYR A 1 24  ? 32.643  15.082  28.524 1.00 21.47 ? 24  TYR A CB  1
+ATOM   168  C  CG  . TYR A 1 24  ? 34.174  14.736  29.162 1.00 17.94 ? 24  TYR A CG  1
+ATOM   169  C  CD1 . TYR A 1 24  ? 34.650  15.558  30.037 1.00 25.54 ? 24  TYR A CD1 1
+ATOM   170  C  CD2 . TYR A 1 24  ? 34.963  13.771  28.697 1.00 18.41 ? 24  TYR A CD2 1
+ATOM   171  C  CE1 . TYR A 1 24  ? 36.047  15.300  30.438 1.00 27.77 ? 24  TYR A CE1 1
+ATOM   172  C  CE2 . TYR A 1 24  ? 36.313  13.499  29.020 1.00 24.84 ? 24  TYR A CE2 1
+ATOM   173  C  CZ  . TYR A 1 24  ? 36.761  14.482  30.127 1.00 28.92 ? 24  TYR A CZ  1
+ATOM   174  O  OH  . TYR A 1 24  ? 38.077  14.435  30.223 1.00 33.79 ? 24  TYR A OH  1
+ATOM   175  N  N   . GLY A 1 25  ? 30.384  14.912  26.506 1.00 17.58 ? 25  GLY A N   1
+ATOM   176  C  CA  . GLY A 1 25  ? 28.988  15.021  25.961 1.00 16.95 ? 25  GLY A CA  1
+ATOM   177  C  C   . GLY A 1 25  ? 28.571  13.735  25.541 1.00 12.93 ? 25  GLY A C   1
+ATOM   178  O  O   . GLY A 1 25  ? 27.456  13.128  25.739 1.00 14.53 ? 25  GLY A O   1
+ATOM   179  N  N   . ALA A 1 26  ? 29.193  13.014  24.577 1.00 15.78 ? 26  ALA A N   1
+ATOM   180  C  CA  . ALA A 1 26  ? 28.959  11.960  24.052 1.00 18.05 ? 26  ALA A CA  1
+ATOM   181  C  C   . ALA A 1 26  ? 28.684  10.573  24.956 1.00 13.38 ? 26  ALA A C   1
+ATOM   182  O  O   . ALA A 1 26  ? 27.957  9.673   25.048 1.00 13.68 ? 26  ALA A O   1
+ATOM   183  C  CB  . ALA A 1 26  ? 29.782  11.279  23.082 1.00 21.17 ? 26  ALA A CB  1
+ATOM   184  N  N   . GLU A 1 27  ? 29.803  10.526  25.945 1.00 13.26 ? 27  GLU A N   1
+ATOM   185  C  CA  . GLU A 1 27  ? 29.741  9.512   27.000 1.00 15.73 ? 27  GLU A CA  1
+ATOM   186  C  C   . GLU A 1 27  ? 28.543  9.721   27.939 1.00 9.69  ? 27  GLU A C   1
+ATOM   187  O  O   . GLU A 1 27  ? 27.997  8.693   28.213 1.00 13.70 ? 27  GLU A O   1
+ATOM   188  C  CB  . GLU A 1 27  ? 31.163  9.735   27.677 1.00 17.47 ? 27  GLU A CB  1
+ATOM   189  C  CG  . GLU A 1 27  ? 31.163  8.726   28.840 1.00 16.72 ? 27  GLU A CG  1
+ATOM   190  C  CD  . GLU A 1 27  ? 32.614  8.732   29.717 1.00 28.34 ? 27  GLU A CD  1
+ATOM   191  O  OE1 . GLU A 1 27  ? 32.419  8.475   30.828 1.00 20.53 ? 27  GLU A OE1 1
+ATOM   192  O  OE2 . GLU A 1 27  ? 33.568  9.162   29.141 1.00 20.32 ? 27  GLU A OE2 1
+ATOM   193  N  N   . ALA A 1 28  ? 28.249  10.962  28.287 1.00 11.71 ? 28  ALA A N   1
+ATOM   194  C  CA  . ALA A 1 28  ? 27.105  11.207  29.104 1.00 14.08 ? 28  ALA A CA  1
+ATOM   195  C  C   . ALA A 1 28  ? 25.796  10.535  28.544 1.00 18.50 ? 28  ALA A C   1
+ATOM   196  O  O   . ALA A 1 28  ? 24.910  10.071  29.047 1.00 12.43 ? 28  ALA A O   1
+ATOM   197  C  CB  . ALA A 1 28  ? 26.926  12.630  29.458 1.00 19.09 ? 28  ALA A CB  1
+ATOM   198  N  N   . LEU A 1 29  ? 25.767  11.063  27.208 1.00 12.19 ? 29  LEU A N   1
+ATOM   199  C  CA  . LEU A 1 29  ? 24.518  10.331  26.454 1.00 17.48 ? 29  LEU A CA  1
+ATOM   200  C  C   . LEU A 1 29  ? 24.504  8.793   26.440 1.00 9.74  ? 29  LEU A C   1
+ATOM   201  O  O   . LEU A 1 29  ? 23.456  8.214   26.652 1.00 10.80 ? 29  LEU A O   1
+ATOM   202  C  CB  . LEU A 1 29  ? 24.500  10.976  24.784 1.00 12.13 ? 29  LEU A CB  1
+ATOM   203  C  CG  . LEU A 1 29  ? 24.327  12.461  24.812 1.00 14.66 ? 29  LEU A CG  1
+ATOM   204  C  CD1 . LEU A 1 29  ? 24.649  12.677  23.315 1.00 16.80 ? 29  LEU A CD1 1
+ATOM   205  C  CD2 . LEU A 1 29  ? 22.855  12.643  25.024 1.00 18.58 ? 29  LEU A CD2 1
+ATOM   206  N  N   . GLU A 1 30  ? 25.681  8.147   26.059 1.00 9.20  ? 30  GLU A N   1
+ATOM   207  C  CA  . GLU A 1 30  ? 25.685  6.735   26.191 1.00 11.66 ? 30  GLU A CA  1
+ATOM   208  C  C   . GLU A 1 30  ? 25.276  6.128   27.538 1.00 13.48 ? 30  GLU A C   1
+ATOM   209  O  O   . GLU A 1 30  ? 24.656  5.146   27.625 1.00 17.00 ? 30  GLU A O   1
+ATOM   210  C  CB  . GLU A 1 30  ? 26.982  6.289   25.644 1.00 19.11 ? 30  GLU A CB  1
+ATOM   211  C  CG  . GLU A 1 30  ? 26.952  4.956   25.891 1.00 27.23 ? 30  GLU A CG  1
+ATOM   212  C  CD  . GLU A 1 30  ? 28.610  4.344   24.951 1.00 43.77 ? 30  GLU A CD  1
+ATOM   213  O  OE1 . GLU A 1 30  ? 29.403  5.267   24.919 1.00 45.21 ? 30  GLU A OE1 1
+ATOM   214  O  OE2 . GLU A 1 30  ? 28.312  3.169   24.429 1.00 45.13 ? 30  GLU A OE2 1
+ATOM   215  N  N   . ARG A 1 31  ? 25.849  6.862   28.541 1.00 11.70 ? 31  ARG A N   1
+ATOM   216  C  CA  . ARG A 1 31  ? 25.494  6.477   29.930 1.00 13.69 ? 31  ARG A CA  1
+ATOM   217  C  C   . ARG A 1 31  ? 23.905  6.550   30.154 1.00 13.95 ? 31  ARG A C   1
+ATOM   218  O  O   . ARG A 1 31  ? 23.431  5.543   30.810 1.00 16.42 ? 31  ARG A O   1
+ATOM   219  C  CB  . ARG A 1 31  ? 26.183  7.223   30.999 1.00 9.32  ? 31  ARG A CB  1
+ATOM   220  C  CG  . ARG A 1 31  ? 27.719  6.823   30.974 1.00 14.85 ? 31  ARG A CG  1
+ATOM   221  C  CD  . ARG A 1 31  ? 28.365  7.741   31.920 1.00 20.12 ? 31  ARG A CD  1
+ATOM   222  N  NE  . ARG A 1 31  ? 30.007  7.518   32.167 1.00 14.83 ? 31  ARG A NE  1
+ATOM   223  C  CZ  . ARG A 1 31  ? 30.374  6.442   32.782 1.00 13.22 ? 31  ARG A CZ  1
+ATOM   224  N  NH1 . ARG A 1 31  ? 29.644  5.568   33.401 1.00 11.40 ? 31  ARG A NH1 1
+ATOM   225  N  NH2 . ARG A 1 31  ? 31.719  6.304   32.607 1.00 17.34 ? 31  ARG A NH2 1
+ATOM   226  N  N   . MET A 1 32  ? 23.371  7.664   29.683 1.00 11.37 ? 32  MET A N   1
+ATOM   227  C  CA  . MET A 1 32  ? 21.971  7.778   29.854 1.00 10.16 ? 32  MET A CA  1
+ATOM   228  C  C   . MET A 1 32  ? 21.193  6.745   29.104 1.00 12.10 ? 32  MET A C   1
+ATOM   229  O  O   . MET A 1 32  ? 20.200  6.115   29.637 1.00 12.78 ? 32  MET A O   1
+ATOM   230  C  CB  . MET A 1 32  ? 21.508  9.125   29.396 1.00 12.48 ? 32  MET A CB  1
+ATOM   231  C  CG  . MET A 1 32  ? 20.069  9.586   29.508 1.00 17.73 ? 32  MET A CG  1
+ATOM   232  S  SD  . MET A 1 32  ? 19.666  11.138  28.793 1.00 15.12 ? 32  MET A SD  1
+ATOM   233  C  CE  . MET A 1 32  ? 19.832  10.587  27.075 1.00 11.32 ? 32  MET A CE  1
+ATOM   234  N  N   . PHE A 1 33  ? 21.472  6.455   27.928 1.00 13.98 ? 33  PHE A N   1
+ATOM   235  C  CA  . PHE A 1 33  ? 20.804  5.332   27.135 1.00 16.07 ? 33  PHE A CA  1
+ATOM   236  C  C   . PHE A 1 33  ? 20.756  4.094   27.521 1.00 12.29 ? 33  PHE A C   1
+ATOM   237  O  O   . PHE A 1 33  ? 19.855  3.278   27.607 1.00 14.84 ? 33  PHE A O   1
+ATOM   238  C  CB  . PHE A 1 33  ? 21.258  5.369   25.686 1.00 11.16 ? 33  PHE A CB  1
+ATOM   239  C  CG  . PHE A 1 33  ? 20.998  6.601   24.949 1.00 10.01 ? 33  PHE A CG  1
+ATOM   240  C  CD1 . PHE A 1 33  ? 20.035  7.373   24.921 1.00 13.62 ? 33  PHE A CD1 1
+ATOM   241  C  CD2 . PHE A 1 33  ? 22.144  6.872   23.946 1.00 19.46 ? 33  PHE A CD2 1
+ATOM   242  C  CE1 . PHE A 1 33  ? 19.777  8.553   24.028 1.00 17.65 ? 33  PHE A CE1 1
+ATOM   243  C  CE2 . PHE A 1 33  ? 21.824  8.278   23.299 1.00 14.83 ? 33  PHE A CE2 1
+ATOM   244  C  CZ  . PHE A 1 33  ? 20.893  8.911   23.305 1.00 12.93 ? 33  PHE A CZ  1
+ATOM   245  N  N   . LEU A 1 34  ? 21.949  3.754   28.342 1.00 16.04 ? 34  LEU A N   1
+ATOM   246  C  CA  . LEU A 1 34  ? 22.106  2.381   28.856 1.00 14.57 ? 34  LEU A CA  1
+ATOM   247  C  C   . LEU A 1 34  ? 21.389  2.378   30.261 1.00 17.64 ? 34  LEU A C   1
+ATOM   248  O  O   . LEU A 1 34  ? 20.938  1.317   30.615 1.00 18.98 ? 34  LEU A O   1
+ATOM   249  C  CB  . LEU A 1 34  ? 23.446  1.993   29.003 1.00 18.08 ? 34  LEU A CB  1
+ATOM   250  C  CG  . LEU A 1 34  ? 24.291  1.614   28.022 1.00 28.60 ? 34  LEU A CG  1
+ATOM   251  C  CD1 . LEU A 1 34  ? 25.845  1.477   27.982 1.00 25.37 ? 34  LEU A CD1 1
+ATOM   252  C  CD2 . LEU A 1 34  ? 23.655  0.958   27.004 1.00 34.83 ? 34  LEU A CD2 1
+ATOM   253  N  N   . SER A 1 35  ? 21.549  3.520   31.132 1.00 15.41 ? 35  SER A N   1
+ATOM   254  C  CA  . SER A 1 35  ? 21.173  3.290   32.388 1.00 14.95 ? 35  SER A CA  1
+ATOM   255  C  C   . SER A 1 35  ? 19.624  3.547   32.560 1.00 15.69 ? 35  SER A C   1
+ATOM   256  O  O   . SER A 1 35  ? 18.876  3.117   33.486 1.00 14.29 ? 35  SER A O   1
+ATOM   257  C  CB  . SER A 1 35  ? 21.736  4.467   33.318 1.00 13.14 ? 35  SER A CB  1
+ATOM   258  O  OG  . SER A 1 35  ? 23.055  4.020   33.621 1.00 17.78 ? 35  SER A OG  1
+ATOM   259  N  N   . PHE A 1 36  ? 19.149  4.429   31.673 1.00 13.54 ? 36  PHE A N   1
+ATOM   260  C  CA  . PHE A 1 36  ? 17.700  4.829   31.549 1.00 13.46 ? 36  PHE A CA  1
+ATOM   261  C  C   . PHE A 1 36  ? 17.241  4.706   30.110 1.00 8.62  ? 36  PHE A C   1
+ATOM   262  O  O   . PHE A 1 36  ? 17.009  5.817   29.402 1.00 14.12 ? 36  PHE A O   1
+ATOM   263  C  CB  . PHE A 1 36  ? 17.696  6.285   31.968 1.00 16.50 ? 36  PHE A CB  1
+ATOM   264  C  CG  . PHE A 1 36  ? 18.345  6.800   33.314 1.00 13.63 ? 36  PHE A CG  1
+ATOM   265  C  CD1 . PHE A 1 36  ? 19.617  7.297   33.349 1.00 11.92 ? 36  PHE A CD1 1
+ATOM   266  C  CD2 . PHE A 1 36  ? 17.711  6.142   34.550 1.00 19.28 ? 36  PHE A CD2 1
+ATOM   267  C  CE1 . PHE A 1 36  ? 20.188  7.527   34.572 1.00 15.75 ? 36  PHE A CE1 1
+ATOM   268  C  CE2 . PHE A 1 36  ? 18.366  6.356   35.744 1.00 13.78 ? 36  PHE A CE2 1
+ATOM   269  C  CZ  . PHE A 1 36  ? 19.636  6.925   35.714 1.00 15.33 ? 36  PHE A CZ  1
+ATOM   270  N  N   . PRO A 1 37  ? 16.816  3.498   30.019 1.00 14.18 ? 37  PRO A N   1
+ATOM   271  C  CA  . PRO A 1 37  ? 16.354  3.248   28.493 1.00 17.12 ? 37  PRO A CA  1
+ATOM   272  C  C   . PRO A 1 37  ? 15.213  3.919   28.007 1.00 17.85 ? 37  PRO A C   1
+ATOM   273  O  O   . PRO A 1 37  ? 15.057  4.094   26.767 1.00 18.50 ? 37  PRO A O   1
+ATOM   274  C  CB  . PRO A 1 37  ? 16.249  1.724   28.442 1.00 23.37 ? 37  PRO A CB  1
+ATOM   275  C  CG  . PRO A 1 37  ? 16.392  1.253   29.803 1.00 28.27 ? 37  PRO A CG  1
+ATOM   276  C  CD  . PRO A 1 37  ? 16.930  2.479   30.711 1.00 20.43 ? 37  PRO A CD  1
+ATOM   277  N  N   . THR A 1 38  ? 14.357  4.466   28.929 1.00 18.86 ? 38  THR A N   1
+ATOM   278  C  CA  . THR A 1 38  ? 13.157  5.139   28.339 1.00 14.66 ? 38  THR A CA  1
+ATOM   279  C  C   . THR A 1 38  ? 13.600  6.361   27.574 1.00 12.72 ? 38  THR A C   1
+ATOM   280  O  O   . THR A 1 38  ? 12.939  6.947   26.810 1.00 15.75 ? 38  THR A O   1
+ATOM   281  C  CB  . THR A 1 38  ? 12.316  5.589   29.574 1.00 19.10 ? 38  THR A CB  1
+ATOM   282  O  OG1 . THR A 1 38  ? 12.943  6.229   30.555 1.00 18.82 ? 38  THR A OG1 1
+ATOM   283  C  CG2 . THR A 1 38  ? 11.781  4.216   30.042 1.00 22.69 ? 38  THR A CG2 1
+ATOM   284  N  N   . THR A 1 39  ? 14.859  6.930   27.855 1.00 14.27 ? 39  THR A N   1
+ATOM   285  C  CA  . THR A 1 39  ? 15.238  8.149   27.103 1.00 10.19 ? 39  THR A CA  1
+ATOM   286  C  C   . THR A 1 39  ? 15.500  7.830   25.576 1.00 10.17 ? 39  THR A C   1
+ATOM   287  O  O   . THR A 1 39  ? 15.558  8.745   24.910 1.00 14.01 ? 39  THR A O   1
+ATOM   288  C  CB  . THR A 1 39  ? 16.395  8.679   27.763 1.00 15.56 ? 39  THR A CB  1
+ATOM   289  O  OG1 . THR A 1 39  ? 17.651  7.831   27.803 1.00 14.68 ? 39  THR A OG1 1
+ATOM   290  C  CG2 . THR A 1 39  ? 16.291  9.101   29.229 1.00 20.52 ? 39  THR A CG2 1
+ATOM   291  N  N   . LYS A 1 40  ? 15.588  6.638   25.375 1.00 14.72 ? 40  LYS A N   1
+ATOM   292  C  CA  . LYS A 1 40  ? 15.881  6.424   24.003 1.00 15.89 ? 40  LYS A CA  1
+ATOM   293  C  C   . LYS A 1 40  ? 14.655  6.610   23.010 1.00 21.37 ? 40  LYS A C   1
+ATOM   294  O  O   . LYS A 1 40  ? 14.649  6.682   21.907 1.00 15.72 ? 40  LYS A O   1
+ATOM   295  C  CB  . LYS A 1 40  ? 16.170  4.717   23.736 1.00 11.64 ? 40  LYS A CB  1
+ATOM   296  C  CG  . LYS A 1 40  ? 17.561  4.446   24.277 1.00 16.19 ? 40  LYS A CG  1
+ATOM   297  C  CD  . LYS A 1 40  ? 17.961  3.027   23.949 1.00 23.35 ? 40  LYS A CD  1
+ATOM   298  C  CE  . LYS A 1 40  ? 17.340  2.023   24.619 1.00 24.42 ? 40  LYS A CE  1
+ATOM   299  N  NZ  . LYS A 1 40  ? 17.779  0.582   24.380 1.00 19.04 ? 40  LYS A NZ  1
+ATOM   300  N  N   . THR A 1 41  ? 13.439  6.783   23.700 1.00 13.16 ? 41  THR A N   1
+ATOM   301  C  CA  . THR A 1 41  ? 12.175  7.074   22.983 1.00 14.78 ? 41  THR A CA  1
+ATOM   302  C  C   . THR A 1 41  ? 12.378  8.219   22.300 1.00 15.32 ? 41  THR A C   1
+ATOM   303  O  O   . THR A 1 41  ? 11.504  8.711   21.390 1.00 15.67 ? 41  THR A O   1
+ATOM   304  C  CB  . THR A 1 41  ? 10.945  7.027   24.025 1.00 15.38 ? 41  THR A CB  1
+ATOM   305  O  OG1 . THR A 1 41  ? 11.077  8.071   24.916 1.00 14.93 ? 41  THR A OG1 1
+ATOM   306  C  CG2 . THR A 1 41  ? 10.726  5.714   24.494 1.00 16.57 ? 41  THR A CG2 1
+ATOM   307  N  N   . TYR A 1 42  ? 13.250  9.259   22.591 1.00 10.46 ? 42  TYR A N   1
+ATOM   308  C  CA  . TYR A 1 42  ? 13.209  10.568  21.934 1.00 12.73 ? 42  TYR A CA  1
+ATOM   309  C  C   . TYR A 1 42  ? 14.312  10.499  20.614 1.00 7.07  ? 42  TYR A C   1
+ATOM   310  O  O   . TYR A 1 42  ? 14.483  11.535  19.973 1.00 12.11 ? 42  TYR A O   1
+ATOM   311  C  CB  . TYR A 1 42  ? 13.924  11.525  22.878 1.00 14.67 ? 42  TYR A CB  1
+ATOM   312  C  CG  . TYR A 1 42  ? 12.738  11.878  23.857 1.00 13.54 ? 42  TYR A CG  1
+ATOM   313  C  CD1 . TYR A 1 42  ? 11.677  12.803  23.635 1.00 19.68 ? 42  TYR A CD1 1
+ATOM   314  C  CD2 . TYR A 1 42  ? 12.746  11.193  25.161 1.00 18.38 ? 42  TYR A CD2 1
+ATOM   315  C  CE1 . TYR A 1 42  ? 10.720  12.820  24.659 1.00 23.98 ? 42  TYR A CE1 1
+ATOM   316  C  CE2 . TYR A 1 42  ? 11.767  11.459  26.089 1.00 13.41 ? 42  TYR A CE2 1
+ATOM   317  C  CZ  . TYR A 1 42  ? 10.738  12.296  25.816 1.00 18.96 ? 42  TYR A CZ  1
+ATOM   318  O  OH  . TYR A 1 42  ? 9.783   12.529  26.788 1.00 19.81 ? 42  TYR A OH  1
+ATOM   319  N  N   . PHE A 1 43  ? 15.042  9.334   20.605 1.00 17.11 ? 43  PHE A N   1
+ATOM   320  C  CA  . PHE A 1 43  ? 16.101  9.057   19.587 1.00 18.18 ? 43  PHE A CA  1
+ATOM   321  C  C   . PHE A 1 43  ? 15.721  7.963   18.679 1.00 24.86 ? 43  PHE A C   1
+ATOM   322  O  O   . PHE A 1 43  ? 16.638  7.262   18.347 1.00 22.13 ? 43  PHE A O   1
+ATOM   323  C  CB  . PHE A 1 43  ? 17.409  9.021   20.171 1.00 15.44 ? 43  PHE A CB  1
+ATOM   324  C  CG  . PHE A 1 43  ? 17.903  10.358  20.901 1.00 14.36 ? 43  PHE A CG  1
+ATOM   325  C  CD1 . PHE A 1 43  ? 17.434  10.488  22.309 1.00 14.47 ? 43  PHE A CD1 1
+ATOM   326  C  CD2 . PHE A 1 43  ? 18.498  11.389  20.463 1.00 16.54 ? 43  PHE A CD2 1
+ATOM   327  C  CE1 . PHE A 1 43  ? 17.873  11.597  22.912 1.00 20.56 ? 43  PHE A CE1 1
+ATOM   328  C  CE2 . PHE A 1 43  ? 18.922  12.637  21.114 1.00 17.61 ? 43  PHE A CE2 1
+ATOM   329  C  CZ  . PHE A 1 43  ? 18.577  12.548  22.483 1.00 18.88 ? 43  PHE A CZ  1
+ATOM   330  N  N   . PRO A 1 44  ? 14.492  7.767   18.271 1.00 18.09 ? 44  PRO A N   1
+ATOM   331  C  CA  . PRO A 1 44  ? 14.321  6.535   17.581 1.00 22.24 ? 44  PRO A CA  1
+ATOM   332  C  C   . PRO A 1 44  ? 14.918  6.772   15.872 1.00 24.15 ? 44  PRO A C   1
+ATOM   333  O  O   . PRO A 1 44  ? 15.206  5.837   15.268 1.00 24.01 ? 44  PRO A O   1
+ATOM   334  C  CB  . PRO A 1 44  ? 12.967  6.606   17.356 1.00 28.44 ? 44  PRO A CB  1
+ATOM   335  C  CG  . PRO A 1 44  ? 12.507  8.020   17.350 1.00 24.77 ? 44  PRO A CG  1
+ATOM   336  C  CD  . PRO A 1 44  ? 13.454  8.598   18.416 1.00 21.37 ? 44  PRO A CD  1
+ATOM   337  N  N   . HIS A 1 45  ? 15.240  7.893   15.634 1.00 22.61 ? 45  HIS A N   1
+ATOM   338  C  CA  . HIS A 1 45  ? 15.913  8.246   14.334 1.00 32.33 ? 45  HIS A CA  1
+ATOM   339  C  C   . HIS A 1 45  ? 17.383  8.157   14.233 1.00 27.50 ? 45  HIS A C   1
+ATOM   340  O  O   . HIS A 1 45  ? 18.037  8.482   13.320 1.00 22.34 ? 45  HIS A O   1
+ATOM   341  C  CB  . HIS A 1 45  ? 15.593  9.554   13.971 1.00 28.91 ? 45  HIS A CB  1
+ATOM   342  C  CG  . HIS A 1 45  ? 15.690  10.926  14.749 1.00 24.48 ? 45  HIS A CG  1
+ATOM   343  N  ND1 . HIS A 1 45  ? 15.420  10.662  16.192 1.00 28.61 ? 45  HIS A ND1 1
+ATOM   344  C  CD2 . HIS A 1 45  ? 16.610  11.875  14.613 1.00 25.11 ? 45  HIS A CD2 1
+ATOM   345  C  CE1 . HIS A 1 45  ? 15.767  11.823  16.768 1.00 26.97 ? 45  HIS A CE1 1
+ATOM   346  N  NE2 . HIS A 1 45  ? 16.593  12.571  15.731 1.00 30.40 ? 45  HIS A NE2 1
+ATOM   347  N  N   . PHE A 1 46  ? 18.207  7.804   15.579 1.00 17.28 ? 46  PHE A N   1
+ATOM   348  C  CA  . PHE A 1 46  ? 19.550  7.726   15.637 1.00 16.89 ? 46  PHE A CA  1
+ATOM   349  C  C   . PHE A 1 46  ? 19.866  6.269   15.514 1.00 16.17 ? 46  PHE A C   1
+ATOM   350  O  O   . PHE A 1 46  ? 19.344  5.340   16.122 1.00 18.14 ? 46  PHE A O   1
+ATOM   351  C  CB  . PHE A 1 46  ? 19.965  8.363   17.039 1.00 19.02 ? 46  PHE A CB  1
+ATOM   352  C  CG  . PHE A 1 46  ? 20.178  9.639   16.902 1.00 24.73 ? 46  PHE A CG  1
+ATOM   353  C  CD1 . PHE A 1 46  ? 21.089  10.369  17.801 1.00 19.60 ? 46  PHE A CD1 1
+ATOM   354  C  CD2 . PHE A 1 46  ? 19.861  10.447  16.188 1.00 32.07 ? 46  PHE A CD2 1
+ATOM   355  C  CE1 . PHE A 1 46  ? 21.279  11.655  17.858 1.00 16.62 ? 46  PHE A CE1 1
+ATOM   356  C  CE2 . PHE A 1 46  ? 20.068  11.984  16.052 1.00 32.95 ? 46  PHE A CE2 1
+ATOM   357  C  CZ  . PHE A 1 46  ? 20.756  12.736  16.886 1.00 26.82 ? 46  PHE A CZ  1
+ATOM   358  N  N   . ASP A 1 47  ? 21.231  6.185   15.016 1.00 19.28 ? 47  ASP A N   1
+ATOM   359  C  CA  . ASP A 1 47  ? 21.861  4.885   15.347 1.00 21.11 ? 47  ASP A CA  1
+ATOM   360  C  C   . ASP A 1 47  ? 22.630  5.090   16.893 1.00 19.86 ? 47  ASP A C   1
+ATOM   361  O  O   . ASP A 1 47  ? 23.376  5.998   16.879 1.00 21.26 ? 47  ASP A O   1
+ATOM   362  C  CB  . ASP A 1 47  ? 23.135  4.848   14.281 1.00 18.49 ? 47  ASP A CB  1
+ATOM   363  C  CG  . ASP A 1 47  ? 23.809  3.405   14.556 1.00 31.25 ? 47  ASP A CG  1
+ATOM   364  O  OD1 . ASP A 1 47  ? 23.644  2.649   15.396 1.00 29.75 ? 47  ASP A OD1 1
+ATOM   365  O  OD2 . ASP A 1 47  ? 24.860  3.621   13.910 1.00 43.41 ? 47  ASP A OD2 1
+ATOM   366  N  N   . LEU A 1 48  ? 22.082  4.402   17.609 1.00 24.03 ? 48  LEU A N   1
+ATOM   367  C  CA  . LEU A 1 48  ? 22.550  4.431   18.889 1.00 18.27 ? 48  LEU A CA  1
+ATOM   368  C  C   . LEU A 1 48  ? 23.448  3.263   19.460 1.00 36.02 ? 48  LEU A C   1
+ATOM   369  O  O   . LEU A 1 48  ? 23.927  3.481   20.472 1.00 39.74 ? 48  LEU A O   1
+ATOM   370  C  CB  . LEU A 1 48  ? 21.261  4.461   19.996 1.00 19.69 ? 48  LEU A CB  1
+ATOM   371  C  CG  . LEU A 1 48  ? 20.516  5.709   19.878 1.00 21.82 ? 48  LEU A CG  1
+ATOM   372  C  CD1 . LEU A 1 48  ? 19.168  5.276   20.851 1.00 33.27 ? 48  LEU A CD1 1
+ATOM   373  C  CD2 . LEU A 1 48  ? 20.850  6.912   19.997 1.00 24.10 ? 48  LEU A CD2 1
+ATOM   374  N  N   . SER A 1 49  ? 24.339  2.929   18.392 1.00 29.95 ? 49  SER A N   1
+ATOM   375  C  CA  . SER A 1 49  ? 25.535  1.858   18.561 1.00 36.57 ? 49  SER A CA  1
+ATOM   376  C  C   . SER A 1 49  ? 26.458  2.801   19.207 1.00 27.84 ? 49  SER A C   1
+ATOM   377  O  O   . SER A 1 49  ? 26.802  4.037   19.000 1.00 22.88 ? 49  SER A O   1
+ATOM   378  C  CB  . SER A 1 49  ? 25.373  1.033   17.483 1.00 37.22 ? 49  SER A CB  1
+ATOM   379  O  OG  . SER A 1 49  ? 25.921  1.581   16.702 1.00 43.53 ? 49  SER A OG  1
+ATOM   380  N  N   . HIS A 1 50  ? 27.455  1.965   20.106 1.00 28.70 ? 50  HIS A N   1
+ATOM   381  C  CA  . HIS A 1 50  ? 28.218  3.101   20.528 1.00 33.73 ? 50  HIS A CA  1
+ATOM   382  C  C   . HIS A 1 50  ? 29.310  3.619   19.727 1.00 26.32 ? 50  HIS A C   1
+ATOM   383  O  O   . HIS A 1 50  ? 29.775  2.696   18.663 1.00 31.00 ? 50  HIS A O   1
+ATOM   384  C  CB  . HIS A 1 50  ? 29.450  1.750   21.376 1.00 52.72 ? 50  HIS A CB  1
+ATOM   385  C  CG  . HIS A 1 50  ? 30.508  2.456   21.766 1.00 44.40 ? 50  HIS A CG  1
+ATOM   386  N  ND1 . HIS A 1 50  ? 30.572  3.193   22.971 1.00 33.80 ? 50  HIS A ND1 1
+ATOM   387  C  CD2 . HIS A 1 50  ? 31.879  1.639   21.968 1.00 47.43 ? 50  HIS A CD2 1
+ATOM   388  C  CE1 . HIS A 1 50  ? 31.865  3.679   23.166 1.00 41.56 ? 50  HIS A CE1 1
+ATOM   389  N  NE2 . HIS A 1 50  ? 32.604  2.825   22.372 1.00 46.05 ? 50  HIS A NE2 1
+ATOM   390  N  N   . GLY A 1 51  ? 29.701  4.489   19.628 1.00 24.77 ? 51  GLY A N   1
+ATOM   391  C  CA  . GLY A 1 51  ? 30.524  5.414   18.901 1.00 47.57 ? 51  GLY A CA  1
+ATOM   392  C  C   . GLY A 1 51  ? 29.939  6.009   17.597 1.00 38.90 ? 51  GLY A C   1
+ATOM   393  O  O   . GLY A 1 51  ? 30.692  6.324   16.802 1.00 36.29 ? 51  GLY A O   1
+ATOM   394  N  N   . SER A 1 52  ? 28.692  5.715   17.597 1.00 31.32 ? 52  SER A N   1
+ATOM   395  C  CA  . SER A 1 52  ? 28.020  6.525   16.203 1.00 26.23 ? 52  SER A CA  1
+ATOM   396  C  C   . SER A 1 52  ? 28.378  7.683   16.152 1.00 16.57 ? 52  SER A C   1
+ATOM   397  O  O   . SER A 1 52  ? 28.369  8.634   16.879 1.00 20.02 ? 52  SER A O   1
+ATOM   398  C  CB  . SER A 1 52  ? 26.583  6.055   16.229 1.00 27.24 ? 52  SER A CB  1
+ATOM   399  O  OG  . SER A 1 52  ? 25.890  7.062   16.774 1.00 23.82 ? 52  SER A OG  1
+ATOM   400  N  N   . ALA A 1 53  ? 28.439  8.171   14.779 1.00 17.74 ? 53  ALA A N   1
+ATOM   401  C  CA  . ALA A 1 53  ? 28.722  9.512   14.598 1.00 23.86 ? 53  ALA A CA  1
+ATOM   402  C  C   . ALA A 1 53  ? 27.534  10.514  14.908 1.00 16.18 ? 53  ALA A C   1
+ATOM   403  O  O   . ALA A 1 53  ? 27.765  11.610  15.323 1.00 19.42 ? 53  ALA A O   1
+ATOM   404  C  CB  . ALA A 1 53  ? 28.701  9.765   12.937 1.00 25.47 ? 53  ALA A CB  1
+ATOM   405  N  N   . GLN A 1 54  ? 26.241  9.921   15.021 1.00 20.85 ? 54  GLN A N   1
+ATOM   406  C  CA  . GLN A 1 54  ? 25.159  10.806  15.328 1.00 13.59 ? 54  GLN A CA  1
+ATOM   407  C  C   . GLN A 1 54  ? 25.363  11.099  16.958 1.00 19.26 ? 54  GLN A C   1
+ATOM   408  O  O   . GLN A 1 54  ? 24.921  12.247  17.202 1.00 20.48 ? 54  GLN A O   1
+ATOM   409  C  CB  . GLN A 1 54  ? 23.833  9.934   15.159 1.00 15.39 ? 54  GLN A CB  1
+ATOM   410  C  CG  . GLN A 1 54  ? 23.396  10.063  13.711 1.00 20.40 ? 54  GLN A CG  1
+ATOM   411  C  CD  . GLN A 1 54  ? 22.433  9.055   13.441 1.00 15.48 ? 54  GLN A CD  1
+ATOM   412  O  OE1 . GLN A 1 54  ? 22.607  7.801   13.464 1.00 23.45 ? 54  GLN A OE1 1
+ATOM   413  N  NE2 . GLN A 1 54  ? 21.468  9.362   12.404 1.00 19.86 ? 54  GLN A NE2 1
+ATOM   414  N  N   . VAL A 1 55  ? 25.628  10.046  17.643 1.00 16.87 ? 55  VAL A N   1
+ATOM   415  C  CA  . VAL A 1 55  ? 25.853  10.345  19.086 1.00 16.48 ? 55  VAL A CA  1
+ATOM   416  C  C   . VAL A 1 55  ? 26.934  11.263  19.445 1.00 17.36 ? 55  VAL A C   1
+ATOM   417  O  O   . VAL A 1 55  ? 26.957  12.206  20.118 1.00 18.40 ? 55  VAL A O   1
+ATOM   418  C  CB  . VAL A 1 55  ? 25.910  8.894   19.761 1.00 14.78 ? 55  VAL A CB  1
+ATOM   419  C  CG1 . VAL A 1 55  ? 26.329  9.077   21.197 1.00 21.77 ? 55  VAL A CG1 1
+ATOM   420  C  CG2 . VAL A 1 55  ? 24.596  8.299   19.723 1.00 16.83 ? 55  VAL A CG2 1
+ATOM   421  N  N   . LYS A 1 56  ? 28.140  10.992  18.743 1.00 16.43 ? 56  LYS A N   1
+ATOM   422  C  CA  . LYS A 1 56  ? 29.167  11.903  18.754 1.00 16.52 ? 56  LYS A CA  1
+ATOM   423  C  C   . LYS A 1 56  ? 28.842  13.208  18.768 1.00 21.58 ? 56  LYS A C   1
+ATOM   424  O  O   . LYS A 1 56  ? 29.300  14.272  19.188 1.00 20.11 ? 56  LYS A O   1
+ATOM   425  C  CB  . LYS A 1 56  ? 30.539  11.379  18.178 1.00 18.35 ? 56  LYS A CB  1
+ATOM   426  C  CG  . LYS A 1 56  ? 30.761  10.000  18.746 1.00 28.49 ? 56  LYS A CG  1
+ATOM   427  C  CD  . LYS A 1 56  ? 32.602  10.020  17.827 1.00 44.71 ? 56  LYS A CD  1
+ATOM   428  C  CE  . LYS A 1 56  ? 33.183  8.332   18.281 1.00 47.65 ? 56  LYS A CE  1
+ATOM   429  N  NZ  . LYS A 1 56  ? 34.579  8.484   17.517 1.00 52.31 ? 56  LYS A NZ  1
+ATOM   430  N  N   . GLY A 1 57  ? 28.245  13.452  17.358 1.00 17.21 ? 57  GLY A N   1
+ATOM   431  C  CA  . GLY A 1 57  ? 27.796  14.786  16.962 1.00 25.10 ? 57  GLY A CA  1
+ATOM   432  C  C   . GLY A 1 57  ? 26.736  15.547  17.979 1.00 19.44 ? 57  GLY A C   1
+ATOM   433  O  O   . GLY A 1 57  ? 27.113  16.686  18.224 1.00 20.54 ? 57  GLY A O   1
+ATOM   434  N  N   . HIS A 1 58  ? 25.914  14.696  18.379 1.00 18.79 ? 58  HIS A N   1
+ATOM   435  C  CA  . HIS A 1 58  ? 24.939  15.324  19.353 1.00 20.27 ? 58  HIS A CA  1
+ATOM   436  C  C   . HIS A 1 58  ? 25.745  15.724  20.868 1.00 13.51 ? 58  HIS A C   1
+ATOM   437  O  O   . HIS A 1 58  ? 25.371  16.810  21.249 1.00 17.47 ? 58  HIS A O   1
+ATOM   438  C  CB  . HIS A 1 58  ? 23.856  14.230  19.475 1.00 17.90 ? 58  HIS A CB  1
+ATOM   439  C  CG  . HIS A 1 58  ? 22.624  15.055  20.283 1.00 15.76 ? 58  HIS A CG  1
+ATOM   440  N  ND1 . HIS A 1 58  ? 22.013  16.251  19.904 1.00 20.40 ? 58  HIS A ND1 1
+ATOM   441  C  CD2 . HIS A 1 58  ? 22.075  14.631  21.390 1.00 20.31 ? 58  HIS A CD2 1
+ATOM   442  C  CE1 . HIS A 1 58  ? 21.283  16.447  21.027 1.00 20.13 ? 58  HIS A CE1 1
+ATOM   443  N  NE2 . HIS A 1 58  ? 21.201  15.523  21.766 1.00 21.08 ? 58  HIS A NE2 1
+ATOM   444  N  N   . GLY A 1 59  ? 26.499  14.754  21.076 1.00 14.95 ? 59  GLY A N   1
+ATOM   445  C  CA  . GLY A 1 59  ? 27.326  15.150  22.340 1.00 18.11 ? 59  GLY A CA  1
+ATOM   446  C  C   . GLY A 1 59  ? 28.073  16.237  22.353 1.00 19.85 ? 59  GLY A C   1
+ATOM   447  O  O   . GLY A 1 59  ? 28.089  17.241  23.214 1.00 15.36 ? 59  GLY A O   1
+ATOM   448  N  N   . LYS A 1 60  ? 28.653  16.636  21.141 1.00 17.17 ? 60  LYS A N   1
+ATOM   449  C  CA  . LYS A 1 60  ? 29.271  17.993  20.951 1.00 18.34 ? 60  LYS A CA  1
+ATOM   450  C  C   . LYS A 1 60  ? 28.618  19.182  21.070 1.00 18.03 ? 60  LYS A C   1
+ATOM   451  O  O   . LYS A 1 60  ? 28.786  20.158  21.544 1.00 18.72 ? 60  LYS A O   1
+ATOM   452  C  CB  . LYS A 1 60  ? 30.241  17.969  19.584 1.00 30.65 ? 60  LYS A CB  1
+ATOM   453  C  CG  . LYS A 1 60  ? 30.892  19.120  19.299 1.00 41.57 ? 60  LYS A CG  1
+ATOM   454  C  CD  . LYS A 1 60  ? 31.654  18.805  18.090 1.00 63.44 ? 60  LYS A CD  1
+ATOM   455  C  CE  . LYS A 1 60  ? 32.483  20.535  17.851 1.00 44.10 ? 60  LYS A CE  1
+ATOM   456  N  NZ  . LYS A 1 60  ? 33.349  19.000  15.825 1.00 49.08 ? 60  LYS A NZ  1
+ATOM   457  N  N   . LYS A 1 61  ? 27.305  18.891  20.381 1.00 16.33 ? 61  LYS A N   1
+ATOM   458  C  CA  . LYS A 1 61  ? 26.406  20.018  20.481 1.00 17.87 ? 61  LYS A CA  1
+ATOM   459  C  C   . LYS A 1 61  ? 25.667  20.310  21.972 1.00 14.89 ? 61  LYS A C   1
+ATOM   460  O  O   . LYS A 1 61  ? 25.719  21.471  22.204 1.00 19.71 ? 61  LYS A O   1
+ATOM   461  C  CB  . LYS A 1 61  ? 25.029  19.743  19.678 1.00 25.67 ? 61  LYS A CB  1
+ATOM   462  C  CG  . LYS A 1 61  ? 25.216  19.894  18.029 1.00 41.04 ? 61  LYS A CG  1
+ATOM   463  C  CD  . LYS A 1 61  ? 24.046  19.278  17.257 1.00 54.25 ? 61  LYS A CD  1
+ATOM   464  C  CE  . LYS A 1 61  ? 24.093  19.216  16.446 1.00 78.95 ? 61  LYS A CE  1
+ATOM   465  N  NZ  . LYS A 1 61  ? 22.888  18.634  15.330 1.00 43.58 ? 61  LYS A NZ  1
+ATOM   466  N  N   . VAL A 1 62  ? 25.705  19.160  22.515 1.00 15.10 ? 62  VAL A N   1
+ATOM   467  C  CA  . VAL A 1 62  ? 25.202  19.396  24.014 1.00 16.18 ? 62  VAL A CA  1
+ATOM   468  C  C   . VAL A 1 62  ? 26.390  20.196  25.013 1.00 18.93 ? 62  VAL A C   1
+ATOM   469  O  O   . VAL A 1 62  ? 25.976  21.171  25.503 1.00 16.64 ? 62  VAL A O   1
+ATOM   470  C  CB  . VAL A 1 62  ? 24.972  18.026  24.544 1.00 13.59 ? 62  VAL A CB  1
+ATOM   471  C  CG1 . VAL A 1 62  ? 24.531  18.041  25.998 1.00 20.28 ? 62  VAL A CG1 1
+ATOM   472  C  CG2 . VAL A 1 62  ? 23.606  17.650  23.950 1.00 17.24 ? 62  VAL A CG2 1
+ATOM   473  N  N   . ALA A 1 63  ? 27.460  19.600  24.531 1.00 18.60 ? 63  ALA A N   1
+ATOM   474  C  CA  . ALA A 1 63  ? 28.582  20.350  25.308 1.00 14.91 ? 63  ALA A CA  1
+ATOM   475  C  C   . ALA A 1 63  ? 29.003  21.573  24.888 1.00 18.47 ? 63  ALA A C   1
+ATOM   476  O  O   . ALA A 1 63  ? 29.102  22.574  25.751 1.00 18.58 ? 63  ALA A O   1
+ATOM   477  C  CB  . ALA A 1 63  ? 29.780  19.242  25.165 1.00 37.76 ? 63  ALA A CB  1
+ATOM   478  N  N   . ASP A 1 64  ? 28.781  22.101  23.577 1.00 16.80 ? 64  ASP A N   1
+ATOM   479  C  CA  . ASP A 1 64  ? 28.902  23.435  23.484 1.00 24.74 ? 64  ASP A CA  1
+ATOM   480  C  C   . ASP A 1 64  ? 27.900  24.509  23.946 1.00 17.12 ? 64  ASP A C   1
+ATOM   481  O  O   . ASP A 1 64  ? 28.207  25.466  24.430 1.00 22.08 ? 64  ASP A O   1
+ATOM   482  C  CB  . ASP A 1 64  ? 28.710  23.623  21.910 1.00 35.97 ? 64  ASP A CB  1
+ATOM   483  C  CG  . ASP A 1 64  ? 30.382  23.354  20.934 1.00 31.06 ? 64  ASP A CG  1
+ATOM   484  O  OD1 . ASP A 1 64  ? 31.160  22.706  22.054 1.00 35.72 ? 64  ASP A OD1 1
+ATOM   485  O  OD2 . ASP A 1 64  ? 29.911  23.194  19.746 1.00 43.58 ? 64  ASP A OD2 1
+ATOM   486  N  N   . ALA A 1 65  ? 26.556  23.841  23.922 1.00 13.28 ? 65  ALA A N   1
+ATOM   487  C  CA  . ALA A 1 65  ? 25.704  24.565  24.780 1.00 17.27 ? 65  ALA A CA  1
+ATOM   488  C  C   . ALA A 1 65  ? 25.941  24.743  26.360 1.00 13.03 ? 65  ALA A C   1
+ATOM   489  O  O   . ALA A 1 65  ? 25.682  25.885  26.689 1.00 17.77 ? 65  ALA A O   1
+ATOM   490  C  CB  . ALA A 1 65  ? 24.224  23.928  24.590 1.00 23.35 ? 65  ALA A CB  1
+ATOM   491  N  N   . LEU A 1 66  ? 26.522  23.690  26.759 1.00 15.51 ? 66  LEU A N   1
+ATOM   492  C  CA  . LEU A 1 66  ? 26.830  23.985  28.180 1.00 11.63 ? 66  LEU A CA  1
+ATOM   493  C  C   . LEU A 1 66  ? 27.994  24.879  28.298 1.00 19.15 ? 66  LEU A C   1
+ATOM   494  O  O   . LEU A 1 66  ? 28.003  25.809  29.226 1.00 19.52 ? 66  LEU A O   1
+ATOM   495  C  CB  . LEU A 1 66  ? 27.140  22.631  28.733 1.00 13.76 ? 66  LEU A CB  1
+ATOM   496  C  CG  . LEU A 1 66  ? 25.969  21.570  29.084 1.00 19.82 ? 66  LEU A CG  1
+ATOM   497  C  CD1 . LEU A 1 66  ? 26.451  20.266  29.375 1.00 18.79 ? 66  LEU A CD1 1
+ATOM   498  C  CD2 . LEU A 1 66  ? 24.927  22.136  29.936 1.00 21.54 ? 66  LEU A CD2 1
+ATOM   499  N  N   . THR A 1 67  ? 28.894  24.797  27.433 1.00 15.35 ? 67  THR A N   1
+ATOM   500  C  CA  . THR A 1 67  ? 29.987  25.722  27.322 1.00 19.22 ? 67  THR A CA  1
+ATOM   501  C  C   . THR A 1 67  ? 29.533  27.249  27.222 1.00 19.35 ? 67  THR A C   1
+ATOM   502  O  O   . THR A 1 67  ? 29.862  28.300  28.086 1.00 25.50 ? 67  THR A O   1
+ATOM   503  C  CB  . THR A 1 67  ? 31.052  25.304  26.397 1.00 27.92 ? 67  THR A CB  1
+ATOM   504  O  OG1 . THR A 1 67  ? 31.573  24.356  26.523 1.00 31.77 ? 67  THR A OG1 1
+ATOM   505  C  CG2 . THR A 1 67  ? 31.872  26.620  26.101 1.00 31.55 ? 67  THR A CG2 1
+ATOM   506  N  N   . ASN A 1 68  ? 28.527  27.377  26.364 1.00 18.73 ? 68  ASN A N   1
+ATOM   507  C  CA  . ASN A 1 68  ? 27.903  28.765  26.282 1.00 18.68 ? 68  ASN A CA  1
+ATOM   508  C  C   . ASN A 1 68  ? 27.199  29.150  27.441 1.00 24.52 ? 68  ASN A C   1
+ATOM   509  O  O   . ASN A 1 68  ? 27.276  30.433  27.981 1.00 25.75 ? 68  ASN A O   1
+ATOM   510  C  CB  . ASN A 1 68  ? 26.831  28.696  25.264 1.00 25.79 ? 68  ASN A CB  1
+ATOM   511  C  CG  . ASN A 1 68  ? 26.000  30.047  25.032 1.00 36.65 ? 68  ASN A CG  1
+ATOM   512  O  OD1 . ASN A 1 68  ? 26.556  31.024  25.062 1.00 38.63 ? 68  ASN A OD1 1
+ATOM   513  N  ND2 . ASN A 1 68  ? 24.805  30.037  24.375 1.00 39.67 ? 68  ASN A ND2 1
+ATOM   514  N  N   . ALA A 1 69  ? 26.532  28.200  28.365 1.00 17.85 ? 69  ALA A N   1
+ATOM   515  C  CA  . ALA A 1 69  ? 25.790  28.757  29.513 1.00 16.12 ? 69  ALA A CA  1
+ATOM   516  C  C   . ALA A 1 69  ? 26.891  29.054  30.649 1.00 15.28 ? 69  ALA A C   1
+ATOM   517  O  O   . ALA A 1 69  ? 26.657  29.867  31.341 1.00 20.90 ? 69  ALA A O   1
+ATOM   518  C  CB  . ALA A 1 69  ? 25.155  27.554  29.987 1.00 21.91 ? 69  ALA A CB  1
+ATOM   519  N  N   . VAL A 1 70  ? 28.057  28.189  30.632 1.00 18.42 ? 70  VAL A N   1
+ATOM   520  C  CA  . VAL A 1 70  ? 29.133  28.642  31.705 1.00 18.79 ? 70  VAL A CA  1
+ATOM   521  C  C   . VAL A 1 70  ? 29.720  29.997  31.369 1.00 21.40 ? 70  VAL A C   1
+ATOM   522  O  O   . VAL A 1 70  ? 29.832  30.776  32.297 1.00 22.44 ? 70  VAL A O   1
+ATOM   523  C  CB  . VAL A 1 70  ? 30.103  27.675  31.660 1.00 19.75 ? 70  VAL A CB  1
+ATOM   524  C  CG1 . VAL A 1 70  ? 31.421  27.766  32.467 1.00 24.49 ? 70  VAL A CG1 1
+ATOM   525  C  CG2 . VAL A 1 70  ? 29.603  26.303  32.220 1.00 30.23 ? 70  VAL A CG2 1
+ATOM   526  N  N   . ALA A 1 71  ? 29.816  30.392  30.095 1.00 20.17 ? 71  ALA A N   1
+ATOM   527  C  CA  . ALA A 1 71  ? 30.256  31.825  29.607 1.00 23.56 ? 71  ALA A CA  1
+ATOM   528  C  C   . ALA A 1 71  ? 29.353  32.490  30.015 1.00 25.98 ? 71  ALA A C   1
+ATOM   529  O  O   . ALA A 1 71  ? 29.851  33.820  30.274 1.00 33.09 ? 71  ALA A O   1
+ATOM   530  C  CB  . ALA A 1 71  ? 30.419  31.647  28.256 1.00 32.78 ? 71  ALA A CB  1
+ATOM   531  N  N   . HIS A 1 72  ? 28.051  32.486  30.131 1.00 23.78 ? 72  HIS A N   1
+ATOM   532  C  CA  . HIS A 1 72  ? 27.118  33.426  30.392 1.00 21.95 ? 72  HIS A CA  1
+ATOM   533  C  C   . HIS A 1 72  ? 26.318  33.218  31.471 1.00 20.17 ? 72  HIS A C   1
+ATOM   534  O  O   . HIS A 1 72  ? 25.022  33.226  31.566 1.00 23.99 ? 72  HIS A O   1
+ATOM   535  C  CB  . HIS A 1 72  ? 25.883  33.619  29.126 1.00 35.07 ? 72  HIS A CB  1
+ATOM   536  C  CG  . HIS A 1 72  ? 26.911  33.711  28.299 1.00 34.89 ? 72  HIS A CG  1
+ATOM   537  N  ND1 . HIS A 1 72  ? 27.114  35.271  27.331 1.00 43.74 ? 72  HIS A ND1 1
+ATOM   538  C  CD2 . HIS A 1 72  ? 27.382  33.349  26.946 1.00 29.96 ? 72  HIS A CD2 1
+ATOM   539  C  CE1 . HIS A 1 72  ? 28.394  35.349  26.783 1.00 41.69 ? 72  HIS A CE1 1
+ATOM   540  N  NE2 . HIS A 1 72  ? 28.236  34.244  25.890 1.00 44.85 ? 72  HIS A NE2 1
+ATOM   541  N  N   . VAL A 1 73  ? 26.878  32.677  32.654 1.00 23.31 ? 73  VAL A N   1
+ATOM   542  C  CA  . VAL A 1 73  ? 26.152  32.112  33.889 1.00 23.32 ? 73  VAL A CA  1
+ATOM   543  C  C   . VAL A 1 73  ? 25.301  32.867  34.300 1.00 32.07 ? 73  VAL A C   1
+ATOM   544  O  O   . VAL A 1 73  ? 24.197  32.912  34.748 1.00 42.18 ? 73  VAL A O   1
+ATOM   545  C  CB  . VAL A 1 73  ? 27.058  31.518  34.709 1.00 41.19 ? 73  VAL A CB  1
+ATOM   546  C  CG1 . VAL A 1 73  ? 28.147  32.256  35.265 1.00 52.76 ? 73  VAL A CG1 1
+ATOM   547  C  CG2 . VAL A 1 73  ? 26.694  30.313  35.284 1.00 47.91 ? 73  VAL A CG2 1
+ATOM   548  N  N   . ASP A 1 74  ? 25.723  34.236  34.274 1.00 30.40 ? 74  ASP A N   1
+ATOM   549  C  CA  . ASP A 1 74  ? 24.798  35.390  34.896 1.00 34.95 ? 74  ASP A CA  1
+ATOM   550  C  C   . ASP A 1 74  ? 23.635  35.478  33.755 1.00 50.97 ? 74  ASP A C   1
+ATOM   551  O  O   . ASP A 1 74  ? 22.893  36.427  34.367 1.00 49.62 ? 74  ASP A O   1
+ATOM   552  C  CB  . ASP A 1 74  ? 25.550  36.712  34.857 1.00 42.77 ? 74  ASP A CB  1
+ATOM   553  C  CG  . ASP A 1 74  ? 26.764  36.525  36.170 1.00 52.01 ? 74  ASP A CG  1
+ATOM   554  O  OD1 . ASP A 1 74  ? 26.666  36.159  36.871 1.00 49.67 ? 74  ASP A OD1 1
+ATOM   555  O  OD2 . ASP A 1 74  ? 28.285  36.614  35.781 1.00 51.46 ? 74  ASP A OD2 1
+ATOM   556  N  N   . ASP A 1 75  ? 23.431  35.326  32.866 1.00 36.55 ? 75  ASP A N   1
+ATOM   557  C  CA  . ASP A 1 75  ? 22.132  35.469  31.993 1.00 36.46 ? 75  ASP A CA  1
+ATOM   558  C  C   . ASP A 1 75  ? 22.081  34.217  30.986 1.00 19.07 ? 75  ASP A C   1
+ATOM   559  O  O   . ASP A 1 75  ? 21.728  34.406  29.722 1.00 22.77 ? 75  ASP A O   1
+ATOM   560  C  CB  . ASP A 1 75  ? 22.999  36.443  30.512 1.00 64.13 ? 75  ASP A CB  1
+ATOM   561  C  CG  . ASP A 1 75  ? 22.481  36.822  30.729 1.00 74.46 ? 75  ASP A CG  1
+ATOM   562  O  OD1 . ASP A 1 75  ? 21.068  37.933  30.461 1.00 47.43 ? 75  ASP A OD1 1
+ATOM   563  O  OD2 . ASP A 1 75  ? 22.442  37.209  28.730 1.00 60.83 ? 75  ASP A OD2 1
+ATOM   564  N  N   . MET A 1 76  ? 21.728  33.315  31.769 1.00 28.83 ? 76  MET A N   1
+ATOM   565  C  CA  . MET A 1 76  ? 21.515  32.000  30.873 1.00 25.75 ? 76  MET A CA  1
+ATOM   566  C  C   . MET A 1 76  ? 20.042  31.923  30.225 1.00 26.47 ? 76  MET A C   1
+ATOM   567  O  O   . MET A 1 76  ? 20.000  31.526  29.075 1.00 25.06 ? 76  MET A O   1
+ATOM   568  C  CB  . MET A 1 76  ? 21.373  30.888  32.076 1.00 26.87 ? 76  MET A CB  1
+ATOM   569  C  CG  . MET A 1 76  ? 22.421  30.504  32.032 1.00 44.91 ? 76  MET A CG  1
+ATOM   570  S  SD  . MET A 1 76  ? 22.668  28.752  33.000 1.00 43.69 ? 76  MET A SD  1
+ATOM   571  C  CE  . MET A 1 76  ? 22.741  28.828  34.435 1.00 47.45 ? 76  MET A CE  1
+ATOM   572  N  N   . PRO A 1 77  ? 19.180  32.562  30.779 1.00 24.72 ? 77  PRO A N   1
+ATOM   573  C  CA  . PRO A 1 77  ? 18.176  32.924  29.953 1.00 32.25 ? 77  PRO A CA  1
+ATOM   574  C  C   . PRO A 1 77  ? 18.283  33.291  28.734 1.00 33.71 ? 77  PRO A C   1
+ATOM   575  O  O   . PRO A 1 77  ? 17.566  32.773  27.608 1.00 27.50 ? 77  PRO A O   1
+ATOM   576  C  CB  . PRO A 1 77  ? 16.910  33.703  30.819 1.00 35.42 ? 77  PRO A CB  1
+ATOM   577  C  CG  . PRO A 1 77  ? 17.589  33.234  32.132 1.00 42.65 ? 77  PRO A CG  1
+ATOM   578  C  CD  . PRO A 1 77  ? 18.904  32.981  32.140 1.00 26.77 ? 77  PRO A CD  1
+ATOM   579  N  N   . ASN A 1 78  ? 18.884  34.434  28.426 1.00 28.71 ? 78  ASN A N   1
+ATOM   580  C  CA  . ASN A 1 78  ? 19.028  35.114  27.274 1.00 29.25 ? 78  ASN A CA  1
+ATOM   581  C  C   . ASN A 1 78  ? 20.042  34.292  26.488 1.00 25.30 ? 78  ASN A C   1
+ATOM   582  O  O   . ASN A 1 78  ? 19.826  33.801  25.201 1.00 31.49 ? 78  ASN A O   1
+ATOM   583  C  CB  . ASN A 1 78  ? 19.616  36.562  27.071 1.00 52.85 ? 78  ASN A CB  1
+ATOM   584  C  CG  . ASN A 1 78  ? 19.043  37.223  27.187 1.00 62.76 ? 78  ASN A CG  1
+ATOM   585  O  OD1 . ASN A 1 78  ? 18.416  38.053  28.975 1.00 71.55 ? 78  ASN A OD1 1
+ATOM   586  N  ND2 . ASN A 1 78  ? 18.035  37.532  26.804 1.00 72.60 ? 78  ASN A ND2 1
+ATOM   587  N  N   . ALA A 1 79  ? 21.001  33.685  27.082 1.00 21.06 ? 79  ALA A N   1
+ATOM   588  C  CA  . ALA A 1 79  ? 22.002  32.897  26.398 1.00 28.88 ? 79  ALA A CA  1
+ATOM   589  C  C   . ALA A 1 79  ? 21.427  31.515  25.591 1.00 27.69 ? 79  ALA A C   1
+ATOM   590  O  O   . ALA A 1 79  ? 21.833  31.257  24.500 1.00 25.51 ? 79  ALA A O   1
+ATOM   591  C  CB  . ALA A 1 79  ? 23.049  32.613  27.237 1.00 35.64 ? 79  ALA A CB  1
+ATOM   592  N  N   . LEU A 1 80  ? 20.637  30.953  26.329 1.00 22.21 ? 80  LEU A N   1
+ATOM   593  C  CA  . LEU A 1 80  ? 19.923  29.569  25.986 1.00 24.91 ? 80  LEU A CA  1
+ATOM   594  C  C   . LEU A 1 80  ? 18.656  29.915  25.159 1.00 29.49 ? 80  LEU A C   1
+ATOM   595  O  O   . LEU A 1 80  ? 17.846  28.929  25.043 1.00 21.47 ? 80  LEU A O   1
+ATOM   596  C  CB  . LEU A 1 80  ? 19.802  28.621  27.129 1.00 17.03 ? 80  LEU A CB  1
+ATOM   597  C  CG  . LEU A 1 80  ? 21.190  28.251  27.752 1.00 26.04 ? 80  LEU A CG  1
+ATOM   598  C  CD1 . LEU A 1 80  ? 20.923  27.416  28.907 1.00 30.97 ? 80  LEU A CD1 1
+ATOM   599  C  CD2 . LEU A 1 80  ? 21.925  27.484  26.552 1.00 40.31 ? 80  LEU A CD2 1
+ATOM   600  N  N   . SER A 1 81  ? 18.189  31.243  24.838 1.00 21.07 ? 81  SER A N   1
+ATOM   601  C  CA  . SER A 1 81  ? 16.735  31.300  24.540 1.00 18.09 ? 81  SER A CA  1
+ATOM   602  C  C   . SER A 1 81  ? 16.482  30.612  23.271 1.00 20.48 ? 81  SER A C   1
+ATOM   603  O  O   . SER A 1 81  ? 15.305  29.944  23.188 1.00 25.77 ? 81  SER A O   1
+ATOM   604  C  CB  . SER A 1 81  ? 17.030  33.153  23.839 1.00 32.64 ? 81  SER A CB  1
+ATOM   605  O  OG  . SER A 1 81  ? 15.549  33.222  23.885 1.00 44.30 ? 81  SER A OG  1
+ATOM   606  N  N   . ALA A 1 82  ? 17.241  30.273  22.317 1.00 23.80 ? 82  ALA A N   1
+ATOM   607  C  CA  . ALA A 1 82  ? 17.142  29.608  21.116 1.00 21.23 ? 82  ALA A CA  1
+ATOM   608  C  C   . ALA A 1 82  ? 16.699  28.277  21.510 1.00 19.91 ? 82  ALA A C   1
+ATOM   609  O  O   . ALA A 1 82  ? 15.902  27.485  20.957 1.00 24.36 ? 82  ALA A O   1
+ATOM   610  C  CB  . ALA A 1 82  ? 18.236  29.609  20.052 1.00 22.94 ? 82  ALA A CB  1
+ATOM   611  N  N   . LEU A 1 83  ? 17.653  27.657  22.340 1.00 18.35 ? 83  LEU A N   1
+ATOM   612  C  CA  . LEU A 1 83  ? 17.367  26.154  22.574 1.00 19.01 ? 83  LEU A CA  1
+ATOM   613  C  C   . LEU A 1 83  ? 16.368  25.989  23.593 1.00 18.91 ? 83  LEU A C   1
+ATOM   614  O  O   . LEU A 1 83  ? 15.610  24.935  23.499 1.00 18.17 ? 83  LEU A O   1
+ATOM   615  C  CB  . LEU A 1 83  ? 18.638  25.756  23.452 1.00 22.27 ? 83  LEU A CB  1
+ATOM   616  C  CG  . LEU A 1 83  ? 19.363  24.804  23.203 1.00 34.66 ? 83  LEU A CG  1
+ATOM   617  C  CD1 . LEU A 1 83  ? 19.584  24.723  21.636 1.00 28.24 ? 83  LEU A CD1 1
+ATOM   618  C  CD2 . LEU A 1 83  ? 21.040  24.899  23.408 1.00 38.79 ? 83  LEU A CD2 1
+ATOM   619  N  N   . SER A 1 84  ? 15.902  26.869  24.424 1.00 13.22 ? 84  SER A N   1
+ATOM   620  C  CA  . SER A 1 84  ? 14.661  26.676  25.091 1.00 14.54 ? 84  SER A CA  1
+ATOM   621  C  C   . SER A 1 84  ? 13.310  26.681  24.249 1.00 13.50 ? 84  SER A C   1
+ATOM   622  O  O   . SER A 1 84  ? 12.480  25.985  24.569 1.00 20.19 ? 84  SER A O   1
+ATOM   623  C  CB  . SER A 1 84  ? 14.135  27.827  26.398 1.00 25.45 ? 84  SER A CB  1
+ATOM   624  O  OG  . SER A 1 84  ? 14.979  28.671  26.146 1.00 36.19 ? 84  SER A OG  1
+ATOM   625  N  N   . ASP A 1 85  ? 13.484  27.575  23.204 1.00 15.99 ? 85  ASP A N   1
+ATOM   626  C  CA  . ASP A 1 85  ? 12.162  27.501  22.245 1.00 18.10 ? 85  ASP A CA  1
+ATOM   627  C  C   . ASP A 1 85  ? 12.138  26.277  21.471 1.00 20.71 ? 85  ASP A C   1
+ATOM   628  O  O   . ASP A 1 85  ? 11.231  25.609  21.457 1.00 20.01 ? 85  ASP A O   1
+ATOM   629  C  CB  . ASP A 1 85  ? 12.463  28.553  21.171 1.00 30.89 ? 85  ASP A CB  1
+ATOM   630  C  CG  . ASP A 1 85  ? 12.102  29.856  21.952 1.00 57.00 ? 85  ASP A CG  1
+ATOM   631  O  OD1 . ASP A 1 85  ? 11.504  30.086  22.343 1.00 51.34 ? 85  ASP A OD1 1
+ATOM   632  O  OD2 . ASP A 1 85  ? 12.666  31.158  20.962 1.00 50.68 ? 85  ASP A OD2 1
+ATOM   633  N  N   . LEU A 1 86  ? 13.374  25.607  21.110 1.00 20.13 ? 86  LEU A N   1
+ATOM   634  C  CA  . LEU A 1 86  ? 13.448  24.432  20.415 1.00 17.03 ? 86  LEU A CA  1
+ATOM   635  C  C   . LEU A 1 86  ? 12.876  23.268  21.176 1.00 14.48 ? 86  LEU A C   1
+ATOM   636  O  O   . LEU A 1 86  ? 12.215  22.352  20.743 1.00 18.46 ? 86  LEU A O   1
+ATOM   637  C  CB  . LEU A 1 86  ? 14.980  24.212  19.994 1.00 16.01 ? 86  LEU A CB  1
+ATOM   638  C  CG  . LEU A 1 86  ? 15.169  23.110  19.418 1.00 23.66 ? 86  LEU A CG  1
+ATOM   639  C  CD1 . LEU A 1 86  ? 14.819  23.101  17.957 1.00 40.43 ? 86  LEU A CD1 1
+ATOM   640  C  CD2 . LEU A 1 86  ? 16.643  22.388  19.121 1.00 33.72 ? 86  LEU A CD2 1
+ATOM   641  N  N   . HIS A 1 87  ? 13.369  23.355  22.561 1.00 12.17 ? 87  HIS A N   1
+ATOM   642  C  CA  . HIS A 1 87  ? 12.943  22.052  23.237 1.00 12.85 ? 87  HIS A CA  1
+ATOM   643  C  C   . HIS A 1 87  ? 11.269  22.286  23.707 1.00 15.39 ? 87  HIS A C   1
+ATOM   644  O  O   . HIS A 1 87  ? 10.689  21.261  23.717 1.00 15.03 ? 87  HIS A O   1
+ATOM   645  C  CB  . HIS A 1 87  ? 13.660  21.990  24.672 1.00 13.63 ? 87  HIS A CB  1
+ATOM   646  C  CG  . HIS A 1 87  ? 15.021  21.223  24.304 1.00 14.91 ? 87  HIS A CG  1
+ATOM   647  N  ND1 . HIS A 1 87  ? 16.112  22.133  23.814 1.00 15.35 ? 87  HIS A ND1 1
+ATOM   648  C  CD2 . HIS A 1 87  ? 15.621  20.053  24.418 1.00 17.85 ? 87  HIS A CD2 1
+ATOM   649  C  CE1 . HIS A 1 87  ? 17.080  21.246  23.554 1.00 15.29 ? 87  HIS A CE1 1
+ATOM   650  N  NE2 . HIS A 1 87  ? 16.894  20.030  24.002 1.00 15.64 ? 87  HIS A NE2 1
+ATOM   651  N  N   . ALA A 1 88  ? 11.017  23.539  23.811 1.00 19.56 ? 88  ALA A N   1
+ATOM   652  C  CA  . ALA A 1 88  ? 9.545   23.815  24.255 1.00 16.45 ? 88  ALA A CA  1
+ATOM   653  C  C   . ALA A 1 88  ? 8.528   23.379  22.921 1.00 28.29 ? 88  ALA A C   1
+ATOM   654  O  O   . ALA A 1 88  ? 7.580   23.093  23.293 1.00 25.27 ? 88  ALA A O   1
+ATOM   655  C  CB  . ALA A 1 88  ? 9.250   25.108  24.951 1.00 17.34 ? 88  ALA A CB  1
+ATOM   656  N  N   . HIS A 1 89  ? 9.023   23.978  21.881 1.00 21.56 ? 89  HIS A N   1
+ATOM   657  C  CA  . HIS A 1 89  ? 8.146   23.939  20.770 1.00 29.42 ? 89  HIS A CA  1
+ATOM   658  C  C   . HIS A 1 89  ? 8.153   22.948  19.753 1.00 27.17 ? 89  HIS A C   1
+ATOM   659  O  O   . HIS A 1 89  ? 7.206   22.405  19.052 1.00 22.35 ? 89  HIS A O   1
+ATOM   660  C  CB  . HIS A 1 89  ? 8.116   25.270  20.105 1.00 26.26 ? 89  HIS A CB  1
+ATOM   661  C  CG  . HIS A 1 89  ? 7.714   26.366  20.955 1.00 44.45 ? 89  HIS A CG  1
+ATOM   662  N  ND1 . HIS A 1 89  ? 6.646   26.385  21.884 1.00 45.59 ? 89  HIS A ND1 1
+ATOM   663  C  CD2 . HIS A 1 89  ? 8.393   27.678  21.360 1.00 45.61 ? 89  HIS A CD2 1
+ATOM   664  C  CE1 . HIS A 1 89  ? 6.507   27.346  22.939 1.00 42.72 ? 89  HIS A CE1 1
+ATOM   665  N  NE2 . HIS A 1 89  ? 7.546   27.974  22.269 1.00 43.49 ? 89  HIS A NE2 1
+ATOM   666  N  N   . LYS A 1 90  ? 9.239   22.247  19.555 1.00 18.65 ? 90  LYS A N   1
+ATOM   667  C  CA  . LYS A 1 90  ? 9.580   21.241  18.851 1.00 28.92 ? 90  LYS A CA  1
+ATOM   668  C  C   . LYS A 1 90  ? 9.844   19.831  19.166 1.00 28.09 ? 90  LYS A C   1
+ATOM   669  O  O   . LYS A 1 90  ? 9.116   18.958  19.169 1.00 25.04 ? 90  LYS A O   1
+ATOM   670  C  CB  . LYS A 1 90  ? 10.799  21.726  17.783 1.00 32.47 ? 90  LYS A CB  1
+ATOM   671  C  CG  . LYS A 1 90  ? 10.208  23.051  16.857 1.00 49.97 ? 90  LYS A CG  1
+ATOM   672  C  CD  . LYS A 1 90  ? 9.245   23.014  16.161 1.00 58.54 ? 90  LYS A CD  1
+ATOM   673  C  CE  . LYS A 1 90  ? 9.829   24.267  14.948 1.00 66.22 ? 90  LYS A CE  1
+ATOM   674  N  NZ  . LYS A 1 90  ? 7.249   23.686  14.601 1.00 63.54 ? 90  LYS A NZ  1
+ATOM   675  N  N   . LEU A 1 91  ? 10.820  19.765  20.120 1.00 17.50 ? 91  LEU A N   1
+ATOM   676  C  CA  . LEU A 1 91  ? 11.331  18.550  20.540 1.00 15.47 ? 91  LEU A CA  1
+ATOM   677  C  C   . LEU A 1 91  ? 10.393  17.922  21.662 1.00 18.54 ? 91  LEU A C   1
+ATOM   678  O  O   . LEU A 1 91  ? 10.088  16.751  21.575 1.00 17.03 ? 91  LEU A O   1
+ATOM   679  C  CB  . LEU A 1 91  ? 12.846  18.568  21.209 1.00 13.84 ? 91  LEU A CB  1
+ATOM   680  C  CG  . LEU A 1 91  ? 13.894  19.019  20.201 1.00 16.01 ? 91  LEU A CG  1
+ATOM   681  C  CD1 . LEU A 1 91  ? 15.091  19.254  20.693 1.00 18.27 ? 91  LEU A CD1 1
+ATOM   682  C  CD2 . LEU A 1 91  ? 13.860  18.151  19.034 1.00 22.12 ? 91  LEU A CD2 1
+ATOM   683  N  N   . ARG A 1 92  ? 10.096  18.794  22.561 1.00 18.03 ? 92  ARG A N   1
+ATOM   684  C  CA  . ARG A 1 92  ? 8.982   18.475  23.626 1.00 14.41 ? 92  ARG A CA  1
+ATOM   685  C  C   . ARG A 1 92  ? 9.315   17.390  24.390 1.00 15.84 ? 92  ARG A C   1
+ATOM   686  O  O   . ARG A 1 92  ? 8.545   16.391  24.699 1.00 17.92 ? 92  ARG A O   1
+ATOM   687  C  CB  . ARG A 1 92  ? 7.568   18.415  22.788 1.00 18.61 ? 92  ARG A CB  1
+ATOM   688  C  CG  . ARG A 1 92  ? 7.080   19.614  22.422 1.00 25.14 ? 92  ARG A CG  1
+ATOM   689  C  CD  . ARG A 1 92  ? 6.263   19.222  20.361 1.00 53.25 ? 92  ARG A CD  1
+ATOM   690  N  NE  . ARG A 1 92  ? 5.775   19.838  21.449 1.00 51.61 ? 92  ARG A NE  1
+ATOM   691  C  CZ  . ARG A 1 92  ? 4.678   19.502  19.150 1.00 59.18 ? 92  ARG A CZ  1
+ATOM   692  N  NH1 . ARG A 1 92  ? 5.696   18.611  18.508 1.00 31.30 ? 92  ARG A NH1 1
+ATOM   693  N  NH2 . ARG A 1 92  ? 3.901   19.647  19.471 1.00 36.70 ? 92  ARG A NH2 1
+ATOM   694  N  N   . VAL A 1 93  ? 10.450  17.265  24.950 1.00 14.32 ? 93  VAL A N   1
+ATOM   695  C  CA  . VAL A 1 93  ? 11.029  16.299  25.838 1.00 16.19 ? 93  VAL A CA  1
+ATOM   696  C  C   . VAL A 1 93  ? 10.463  16.413  27.093 1.00 13.83 ? 93  VAL A C   1
+ATOM   697  O  O   . VAL A 1 93  ? 10.481  17.529  27.810 1.00 14.88 ? 93  VAL A O   1
+ATOM   698  C  CB  . VAL A 1 93  ? 12.521  16.421  25.936 1.00 12.60 ? 93  VAL A CB  1
+ATOM   699  C  CG1 . VAL A 1 93  ? 13.018  15.448  26.927 1.00 15.68 ? 93  VAL A CG1 1
+ATOM   700  C  CG2 . VAL A 1 93  ? 13.175  16.259  24.534 1.00 15.91 ? 93  VAL A CG2 1
+ATOM   701  N  N   . ASP A 1 94  ? 9.877   15.404  27.801 1.00 14.66 ? 94  ASP A N   1
+ATOM   702  C  CA  . ASP A 1 94  ? 9.139   15.576  29.102 1.00 11.73 ? 94  ASP A CA  1
+ATOM   703  C  C   . ASP A 1 94  ? 10.382  16.098  30.122 1.00 12.54 ? 94  ASP A C   1
+ATOM   704  O  O   . ASP A 1 94  ? 11.372  15.545  30.049 1.00 16.42 ? 94  ASP A O   1
+ATOM   705  C  CB  . ASP A 1 94  ? 8.749   14.222  29.591 1.00 12.92 ? 94  ASP A CB  1
+ATOM   706  C  CG  . ASP A 1 94  ? 7.889   14.502  30.818 1.00 22.91 ? 94  ASP A CG  1
+ATOM   707  O  OD1 . ASP A 1 94  ? 6.670   14.605  30.774 1.00 22.17 ? 94  ASP A OD1 1
+ATOM   708  O  OD2 . ASP A 1 94  ? 8.490   14.600  31.919 1.00 19.01 ? 94  ASP A OD2 1
+ATOM   709  N  N   . PRO A 1 95  ? 10.036  16.903  31.026 1.00 16.46 ? 95  PRO A N   1
+ATOM   710  C  CA  . PRO A 1 95  ? 11.018  17.573  31.839 1.00 14.67 ? 95  PRO A CA  1
+ATOM   711  C  C   . PRO A 1 95  ? 11.600  16.528  32.668 1.00 17.74 ? 95  PRO A C   1
+ATOM   712  O  O   . PRO A 1 95  ? 12.831  16.813  33.158 1.00 22.38 ? 95  PRO A O   1
+ATOM   713  C  CB  . PRO A 1 95  ? 10.255  18.390  32.773 1.00 22.16 ? 95  PRO A CB  1
+ATOM   714  C  CG  . PRO A 1 95  ? 9.279   19.007  31.875 1.00 21.38 ? 95  PRO A CG  1
+ATOM   715  C  CD  . PRO A 1 95  ? 8.838   17.824  31.026 1.00 20.78 ? 95  PRO A CD  1
+ATOM   716  N  N   . VAL A 1 96  ? 11.094  15.369  32.998 1.00 13.01 ? 96  VAL A N   1
+ATOM   717  C  CA  . VAL A 1 96  ? 11.818  14.490  33.880 1.00 11.93 ? 96  VAL A CA  1
+ATOM   718  C  C   . VAL A 1 96  ? 13.110  14.055  33.442 1.00 21.27 ? 96  VAL A C   1
+ATOM   719  O  O   . VAL A 1 96  ? 14.061  13.636  34.018 1.00 16.07 ? 96  VAL A O   1
+ATOM   720  C  CB  . VAL A 1 96  ? 10.746  13.223  34.202 1.00 29.83 ? 96  VAL A CB  1
+ATOM   721  C  CG1 . VAL A 1 96  ? 10.636  12.376  33.493 1.00 48.43 ? 96  VAL A CG1 1
+ATOM   722  C  CG2 . VAL A 1 96  ? 11.211  12.884  35.042 1.00 70.91 ? 96  VAL A CG2 1
+ATOM   723  N  N   . ASN A 1 97  ? 13.198  14.031  32.013 1.00 15.63 ? 97  ASN A N   1
+ATOM   724  C  CA  . ASN A 1 97  ? 14.422  13.357  31.439 1.00 10.10 ? 97  ASN A CA  1
+ATOM   725  C  C   . ASN A 1 97  ? 15.668  14.400  31.471 1.00 4.91  ? 97  ASN A C   1
+ATOM   726  O  O   . ASN A 1 97  ? 16.742  13.804  31.479 1.00 9.67  ? 97  ASN A O   1
+ATOM   727  C  CB  . ASN A 1 97  ? 14.255  13.082  29.893 1.00 13.43 ? 97  ASN A CB  1
+ATOM   728  C  CG  . ASN A 1 97  ? 13.203  12.042  29.782 1.00 17.91 ? 97  ASN A CG  1
+ATOM   729  O  OD1 . ASN A 1 97  ? 13.400  10.905  29.862 1.00 10.92 ? 97  ASN A OD1 1
+ATOM   730  N  ND2 . ASN A 1 97  ? 11.883  12.627  29.469 1.00 21.96 ? 97  ASN A ND2 1
+ATOM   731  N  N   . PHE A 1 98  ? 15.454  15.613  31.826 1.00 9.20  ? 98  PHE A N   1
+ATOM   732  C  CA  . PHE A 1 98  ? 16.514  16.576  32.022 1.00 12.10 ? 98  PHE A CA  1
+ATOM   733  C  C   . PHE A 1 98  ? 17.359  16.153  33.342 1.00 12.02 ? 98  PHE A C   1
+ATOM   734  O  O   . PHE A 1 98  ? 18.668  16.201  33.344 1.00 11.50 ? 98  PHE A O   1
+ATOM   735  C  CB  . PHE A 1 98  ? 16.213  18.094  32.094 1.00 16.66 ? 98  PHE A CB  1
+ATOM   736  C  CG  . PHE A 1 98  ? 15.656  18.483  30.822 1.00 14.23 ? 98  PHE A CG  1
+ATOM   737  C  CD1 . PHE A 1 98  ? 16.581  19.170  30.099 1.00 16.70 ? 98  PHE A CD1 1
+ATOM   738  C  CD2 . PHE A 1 98  ? 14.368  18.262  30.377 1.00 12.76 ? 98  PHE A CD2 1
+ATOM   739  C  CE1 . PHE A 1 98  ? 16.216  19.599  28.986 1.00 23.57 ? 98  PHE A CE1 1
+ATOM   740  C  CE2 . PHE A 1 98  ? 14.023  18.675  29.011 1.00 15.74 ? 98  PHE A CE2 1
+ATOM   741  C  CZ  . PHE A 1 98  ? 14.964  19.283  28.484 1.00 17.50 ? 98  PHE A CZ  1
+ATOM   742  N  N   . LYS A 1 99  ? 16.726  15.616  34.363 1.00 13.69 ? 99  LYS A N   1
+ATOM   743  C  CA  . LYS A 1 99  ? 17.454  15.015  35.527 1.00 13.57 ? 99  LYS A CA  1
+ATOM   744  C  C   . LYS A 1 99  ? 18.070  13.857  35.323 1.00 14.35 ? 99  LYS A C   1
+ATOM   745  O  O   . LYS A 1 99  ? 19.246  13.843  35.836 1.00 13.29 ? 99  LYS A O   1
+ATOM   746  C  CB  . LYS A 1 99  ? 16.282  14.903  36.646 1.00 22.01 ? 99  LYS A CB  1
+ATOM   747  C  CG  . LYS A 1 99  ? 15.507  15.642  36.853 1.00 54.35 ? 99  LYS A CG  1
+ATOM   748  C  CD  . LYS A 1 99  ? 15.051  15.827  37.720 1.00 72.56 ? 99  LYS A CD  1
+ATOM   749  C  CE  . LYS A 1 99  ? 13.360  14.885  37.925 1.00 73.99 ? 99  LYS A CE  1
+ATOM   750  N  NZ  . LYS A 1 99  ? 12.431  16.281  39.350 1.00 80.12 ? 99  LYS A NZ  1
+ATOM   751  N  N   . LEU A 1 100 ? 17.756  13.069  34.307 1.00 9.89  ? 100 LEU A N   1
+ATOM   752  C  CA  . LEU A 1 100 ? 18.442  11.879  34.037 1.00 8.80  ? 100 LEU A CA  1
+ATOM   753  C  C   . LEU A 1 100 ? 19.685  12.195  33.255 1.00 9.28  ? 100 LEU A C   1
+ATOM   754  O  O   . LEU A 1 100 ? 20.768  11.674  33.627 1.00 12.09 ? 100 LEU A O   1
+ATOM   755  C  CB  . LEU A 1 100 ? 17.575  10.876  33.345 1.00 11.00 ? 100 LEU A CB  1
+ATOM   756  C  CG  . LEU A 1 100 ? 16.276  10.692  33.948 1.00 16.83 ? 100 LEU A CG  1
+ATOM   757  C  CD1 . LEU A 1 100 ? 15.380  9.564   33.086 1.00 20.94 ? 100 LEU A CD1 1
+ATOM   758  C  CD2 . LEU A 1 100 ? 16.543  9.775   35.154 1.00 18.49 ? 100 LEU A CD2 1
+ATOM   759  N  N   . LEU A 1 101 ? 19.694  13.056  32.271 1.00 8.39  ? 101 LEU A N   1
+ATOM   760  C  CA  . LEU A 1 101 ? 20.901  13.404  31.570 1.00 10.30 ? 101 LEU A CA  1
+ATOM   761  C  C   . LEU A 1 101 ? 21.812  14.257  32.401 1.00 14.49 ? 101 LEU A C   1
+ATOM   762  O  O   . LEU A 1 101 ? 23.089  14.040  32.549 1.00 16.14 ? 101 LEU A O   1
+ATOM   763  C  CB  . LEU A 1 101 ? 20.471  14.278  30.463 1.00 11.44 ? 101 LEU A CB  1
+ATOM   764  C  CG  . LEU A 1 101 ? 21.739  14.747  29.620 1.00 15.06 ? 101 LEU A CG  1
+ATOM   765  C  CD1 . LEU A 1 101 ? 22.668  13.778  29.142 1.00 17.72 ? 101 LEU A CD1 1
+ATOM   766  C  CD2 . LEU A 1 101 ? 21.165  15.689  28.431 1.00 19.38 ? 101 LEU A CD2 1
+ATOM   767  N  N   . SER A 1 102 ? 21.320  15.125  33.447 1.00 15.17 ? 102 SER A N   1
+ATOM   768  C  CA  . SER A 1 102 ? 22.133  15.859  34.357 1.00 9.19  ? 102 SER A CA  1
+ATOM   769  C  C   . SER A 1 102 ? 22.949  14.793  35.226 1.00 9.91  ? 102 SER A C   1
+ATOM   770  O  O   . SER A 1 102 ? 24.210  15.034  35.472 1.00 14.07 ? 102 SER A O   1
+ATOM   771  C  CB  . SER A 1 102 ? 21.243  16.667  35.243 1.00 12.36 ? 102 SER A CB  1
+ATOM   772  O  OG  . SER A 1 102 ? 20.692  17.778  34.508 1.00 16.52 ? 102 SER A OG  1
+ATOM   773  N  N   . HIS A 1 103 ? 22.269  13.787  35.810 1.00 12.27 ? 103 HIS A N   1
+ATOM   774  C  CA  . HIS A 1 103 ? 22.797  12.699  36.563 1.00 10.16 ? 103 HIS A CA  1
+ATOM   775  C  C   . HIS A 1 103 ? 24.082  12.227  35.911 1.00 13.13 ? 103 HIS A C   1
+ATOM   776  O  O   . HIS A 1 103 ? 25.238  11.935  36.322 1.00 13.37 ? 103 HIS A O   1
+ATOM   777  C  CB  . HIS A 1 103 ? 21.928  11.728  37.165 1.00 12.31 ? 103 HIS A CB  1
+ATOM   778  C  CG  . HIS A 1 103 ? 22.522  10.606  37.851 1.00 10.33 ? 103 HIS A CG  1
+ATOM   779  N  ND1 . HIS A 1 103 ? 22.512  9.312   37.327 1.00 10.01 ? 103 HIS A ND1 1
+ATOM   780  C  CD2 . HIS A 1 103 ? 23.251  10.666  39.003 1.00 9.56  ? 103 HIS A CD2 1
+ATOM   781  C  CE1 . HIS A 1 103 ? 23.268  8.706   38.293 1.00 12.63 ? 103 HIS A CE1 1
+ATOM   782  N  NE2 . HIS A 1 103 ? 23.816  9.433   39.328 1.00 10.77 ? 103 HIS A NE2 1
+ATOM   783  N  N   . CYS A 1 104 ? 23.785  11.793  34.589 1.00 11.06 ? 104 CYS A N   1
+ATOM   784  C  CA  . CYS A 1 104 ? 24.955  11.067  33.693 1.00 11.72 ? 104 CYS A CA  1
+ATOM   785  C  C   . CYS A 1 104 ? 25.930  12.114  33.326 1.00 9.58  ? 104 CYS A C   1
+ATOM   786  O  O   . CYS A 1 104 ? 27.037  11.591  33.242 1.00 14.10 ? 104 CYS A O   1
+ATOM   787  C  CB  . CYS A 1 104 ? 24.215  10.422  32.545 1.00 16.81 ? 104 CYS A CB  1
+ATOM   788  S  SG  . CYS A 1 104 ? 23.130  9.077   32.871 1.00 14.76 ? 104 CYS A SG  1
+ATOM   789  N  N   . LEU A 1 105 ? 25.686  13.340  33.245 1.00 7.99  ? 105 LEU A N   1
+ATOM   790  C  CA  . LEU A 1 105 ? 26.930  14.181  33.011 1.00 10.43 ? 105 LEU A CA  1
+ATOM   791  C  C   . LEU A 1 105 ? 27.781  14.431  34.330 1.00 11.96 ? 105 LEU A C   1
+ATOM   792  O  O   . LEU A 1 105 ? 28.916  14.332  34.133 1.00 15.19 ? 105 LEU A O   1
+ATOM   793  C  CB  . LEU A 1 105 ? 26.144  15.534  32.454 1.00 16.93 ? 105 LEU A CB  1
+ATOM   794  C  CG  . LEU A 1 105 ? 26.145  15.973  31.243 1.00 44.57 ? 105 LEU A CG  1
+ATOM   795  C  CD1 . LEU A 1 105 ? 25.187  17.180  31.028 1.00 40.98 ? 105 LEU A CD1 1
+ATOM   796  C  CD2 . LEU A 1 105 ? 27.021  15.889  30.436 1.00 33.21 ? 105 LEU A CD2 1
+ATOM   797  N  N   . LEU A 1 106 ? 27.003  14.439  35.449 1.00 10.40 ? 106 LEU A N   1
+ATOM   798  C  CA  . LEU A 1 106 ? 27.781  14.390  36.680 1.00 15.02 ? 106 LEU A CA  1
+ATOM   799  C  C   . LEU A 1 106 ? 28.498  13.290  36.921 1.00 13.79 ? 106 LEU A C   1
+ATOM   800  O  O   . LEU A 1 106 ? 29.832  13.331  37.231 1.00 13.12 ? 106 LEU A O   1
+ATOM   801  C  CB  . LEU A 1 106 ? 26.793  14.652  37.846 1.00 16.59 ? 106 LEU A CB  1
+ATOM   802  C  CG  . LEU A 1 106 ? 26.544  15.485  38.593 1.00 26.87 ? 106 LEU A CG  1
+ATOM   803  C  CD1 . LEU A 1 106 ? 25.587  15.412  39.609 1.00 28.01 ? 106 LEU A CD1 1
+ATOM   804  C  CD2 . LEU A 1 106 ? 27.348  16.855  38.542 1.00 18.73 ? 106 LEU A CD2 1
+ATOM   805  N  N   . VAL A 1 107 ? 28.140  12.045  36.588 1.00 9.58  ? 107 VAL A N   1
+ATOM   806  C  CA  . VAL A 1 107 ? 28.867  10.896  36.584 1.00 10.69 ? 107 VAL A CA  1
+ATOM   807  C  C   . VAL A 1 107 ? 29.996  10.906  35.663 1.00 12.39 ? 107 VAL A C   1
+ATOM   808  O  O   . VAL A 1 107 ? 31.155  10.432  35.980 1.00 13.09 ? 107 VAL A O   1
+ATOM   809  C  CB  . VAL A 1 107 ? 27.983  9.640   36.248 1.00 14.48 ? 107 VAL A CB  1
+ATOM   810  C  CG1 . VAL A 1 107 ? 28.786  8.493   36.042 1.00 19.64 ? 107 VAL A CG1 1
+ATOM   811  C  CG2 . VAL A 1 107 ? 26.924  9.344   37.458 1.00 13.81 ? 107 VAL A CG2 1
+ATOM   812  N  N   . THR A 1 108 ? 29.866  11.477  34.500 1.00 12.66 ? 108 THR A N   1
+ATOM   813  C  CA  . THR A 1 108 ? 30.981  11.523  33.513 1.00 11.04 ? 108 THR A CA  1
+ATOM   814  C  C   . THR A 1 108 ? 32.033  12.346  34.052 1.00 11.25 ? 108 THR A C   1
+ATOM   815  O  O   . THR A 1 108 ? 33.217  12.034  33.937 1.00 13.68 ? 108 THR A O   1
+ATOM   816  C  CB  . THR A 1 108 ? 30.229  12.009  32.077 1.00 8.55  ? 108 THR A CB  1
+ATOM   817  O  OG1 . THR A 1 108 ? 29.394  10.995  31.572 1.00 9.51  ? 108 THR A OG1 1
+ATOM   818  C  CG2 . THR A 1 108 ? 31.361  11.981  31.120 1.00 15.85 ? 108 THR A CG2 1
+ATOM   819  N  N   . LEU A 1 109 ? 31.639  13.594  34.560 1.00 11.20 ? 109 LEU A N   1
+ATOM   820  C  CA  . LEU A 1 109 ? 32.654  14.548  35.105 1.00 12.61 ? 109 LEU A CA  1
+ATOM   821  C  C   . LEU A 1 109 ? 33.444  13.819  36.314 1.00 16.09 ? 109 LEU A C   1
+ATOM   822  O  O   . LEU A 1 109 ? 34.680  13.951  36.361 1.00 14.60 ? 109 LEU A O   1
+ATOM   823  C  CB  . LEU A 1 109 ? 31.945  15.735  35.484 1.00 17.08 ? 109 LEU A CB  1
+ATOM   824  C  CG  . LEU A 1 109 ? 31.514  16.805  34.364 1.00 24.50 ? 109 LEU A CG  1
+ATOM   825  C  CD1 . LEU A 1 109 ? 30.585  17.626  34.772 1.00 22.52 ? 109 LEU A CD1 1
+ATOM   826  C  CD2 . LEU A 1 109 ? 32.083  16.763  33.252 1.00 32.08 ? 109 LEU A CD2 1
+ATOM   827  N  N   . ALA A 1 110 ? 32.593  13.124  37.089 1.00 13.55 ? 110 ALA A N   1
+ATOM   828  C  CA  . ALA A 1 110 ? 33.320  12.567  38.211 1.00 19.86 ? 110 ALA A CA  1
+ATOM   829  C  C   . ALA A 1 110 ? 34.311  11.619  37.928 1.00 18.59 ? 110 ALA A C   1
+ATOM   830  O  O   . ALA A 1 110 ? 35.463  11.335  38.363 1.00 14.76 ? 110 ALA A O   1
+ATOM   831  C  CB  . ALA A 1 110 ? 32.204  11.822  39.035 1.00 17.34 ? 110 ALA A CB  1
+ATOM   832  N  N   . ALA A 1 111 ? 34.188  10.725  36.841 1.00 15.15 ? 111 ALA A N   1
+ATOM   833  C  CA  . ALA A 1 111 ? 34.853  9.713   36.216 1.00 13.42 ? 111 ALA A CA  1
+ATOM   834  C  C   . ALA A 1 111 ? 36.249  10.312  35.639 1.00 16.84 ? 111 ALA A C   1
+ATOM   835  O  O   . ALA A 1 111 ? 37.082  9.553   35.401 1.00 21.50 ? 111 ALA A O   1
+ATOM   836  C  CB  . ALA A 1 111 ? 34.300  8.724   35.293 1.00 16.85 ? 111 ALA A CB  1
+ATOM   837  N  N   . HIS A 1 112 ? 36.122  11.507  35.127 1.00 17.71 ? 112 HIS A N   1
+ATOM   838  C  CA  . HIS A 1 112 ? 37.272  12.082  34.373 1.00 25.83 ? 112 HIS A CA  1
+ATOM   839  C  C   . HIS A 1 112 ? 37.896  13.229  35.271 1.00 21.86 ? 112 HIS A C   1
+ATOM   840  O  O   . HIS A 1 112 ? 39.065  13.433  34.663 1.00 23.07 ? 112 HIS A O   1
+ATOM   841  C  CB  . HIS A 1 112 ? 36.757  12.745  32.940 1.00 17.12 ? 112 HIS A CB  1
+ATOM   842  C  CG  . HIS A 1 112 ? 36.394  11.697  32.055 1.00 18.91 ? 112 HIS A CG  1
+ATOM   843  N  ND1 . HIS A 1 112 ? 37.514  11.389  31.288 1.00 20.25 ? 112 HIS A ND1 1
+ATOM   844  C  CD2 . HIS A 1 112 ? 35.227  11.180  31.616 1.00 13.97 ? 112 HIS A CD2 1
+ATOM   845  C  CE1 . HIS A 1 112 ? 36.653  10.329  30.431 1.00 16.16 ? 112 HIS A CE1 1
+ATOM   846  N  NE2 . HIS A 1 112 ? 35.281  10.132  30.712 1.00 16.17 ? 112 HIS A NE2 1
+ATOM   847  N  N   . LEU A 1 113 ? 37.428  13.701  36.294 1.00 16.18 ? 113 LEU A N   1
+ATOM   848  C  CA  . LEU A 1 113 ? 38.133  14.905  36.927 1.00 18.52 ? 113 LEU A CA  1
+ATOM   849  C  C   . LEU A 1 113 ? 38.386  14.437  38.302 1.00 15.09 ? 113 LEU A C   1
+ATOM   850  O  O   . LEU A 1 113 ? 37.851  15.105  39.218 1.00 22.00 ? 113 LEU A O   1
+ATOM   851  C  CB  . LEU A 1 113 ? 37.256  15.942  37.195 1.00 26.60 ? 113 LEU A CB  1
+ATOM   852  C  CG  . LEU A 1 113 ? 36.923  16.856  35.788 1.00 26.91 ? 113 LEU A CG  1
+ATOM   853  C  CD1 . LEU A 1 113 ? 36.178  18.296  35.839 1.00 38.78 ? 113 LEU A CD1 1
+ATOM   854  C  CD2 . LEU A 1 113 ? 38.017  16.930  34.744 1.00 35.29 ? 113 LEU A CD2 1
+ATOM   855  N  N   . PRO A 1 114 ? 39.101  13.423  38.641 1.00 18.92 ? 114 PRO A N   1
+ATOM   856  C  CA  . PRO A 1 114 ? 39.280  12.806  40.110 1.00 24.61 ? 114 PRO A CA  1
+ATOM   857  C  C   . PRO A 1 114 ? 39.927  14.077  40.967 1.00 23.92 ? 114 PRO A C   1
+ATOM   858  O  O   . PRO A 1 114 ? 39.316  14.285  41.886 1.00 21.99 ? 114 PRO A O   1
+ATOM   859  C  CB  . PRO A 1 114 ? 40.464  11.988  39.723 1.00 23.94 ? 114 PRO A CB  1
+ATOM   860  C  CG  . PRO A 1 114 ? 41.095  12.179  38.419 1.00 18.92 ? 114 PRO A CG  1
+ATOM   861  C  CD  . PRO A 1 114 ? 39.914  12.862  37.661 1.00 16.59 ? 114 PRO A CD  1
+ATOM   862  N  N   . ALA A 1 115 ? 40.743  14.991  40.381 1.00 18.42 ? 115 ALA A N   1
+ATOM   863  C  CA  . ALA A 1 115 ? 41.335  15.997  41.417 1.00 21.98 ? 115 ALA A CA  1
+ATOM   864  C  C   . ALA A 1 115 ? 40.245  17.067  41.773 1.00 22.41 ? 115 ALA A C   1
+ATOM   865  O  O   . ALA A 1 115 ? 40.199  17.647  42.733 1.00 22.94 ? 115 ALA A O   1
+ATOM   866  C  CB  . ALA A 1 115 ? 42.491  16.560  40.735 1.00 30.20 ? 115 ALA A CB  1
+ATOM   867  N  N   . GLU A 1 116 ? 39.477  17.420  40.797 1.00 15.58 ? 116 GLU A N   1
+ATOM   868  C  CA  . GLU A 1 116 ? 38.611  18.707  40.892 1.00 17.43 ? 116 GLU A CA  1
+ATOM   869  C  C   . GLU A 1 116 ? 37.138  18.361  41.386 1.00 15.97 ? 116 GLU A C   1
+ATOM   870  O  O   . GLU A 1 116 ? 36.423  19.338  41.741 1.00 23.49 ? 116 GLU A O   1
+ATOM   871  C  CB  . GLU A 1 116 ? 38.400  19.196  39.339 1.00 21.21 ? 116 GLU A CB  1
+ATOM   872  C  CG  . GLU A 1 116 ? 39.570  19.899  38.769 1.00 24.18 ? 116 GLU A CG  1
+ATOM   873  C  CD  . GLU A 1 116 ? 40.366  18.705  38.293 1.00 26.12 ? 116 GLU A CD  1
+ATOM   874  O  OE1 . GLU A 1 116 ? 40.190  17.457  37.981 1.00 28.16 ? 116 GLU A OE1 1
+ATOM   875  O  OE2 . GLU A 1 116 ? 41.594  19.102  37.666 1.00 33.82 ? 116 GLU A OE2 1
+ATOM   876  N  N   . PHE A 1 117 ? 36.708  17.170  41.386 1.00 16.62 ? 117 PHE A N   1
+ATOM   877  C  CA  . PHE A 1 117 ? 35.472  16.697  41.837 1.00 14.17 ? 117 PHE A CA  1
+ATOM   878  C  C   . PHE A 1 117 ? 35.217  16.603  43.446 1.00 17.74 ? 117 PHE A C   1
+ATOM   879  O  O   . PHE A 1 117 ? 34.799  15.572  43.821 1.00 19.92 ? 117 PHE A O   1
+ATOM   880  C  CB  . PHE A 1 117 ? 34.921  15.499  41.070 1.00 12.47 ? 117 PHE A CB  1
+ATOM   881  C  CG  . PHE A 1 117 ? 33.357  15.208  40.941 1.00 9.61  ? 117 PHE A CG  1
+ATOM   882  C  CD1 . PHE A 1 117 ? 32.670  16.060  40.127 1.00 15.09 ? 117 PHE A CD1 1
+ATOM   883  C  CD2 . PHE A 1 117 ? 32.869  14.247  41.802 1.00 15.73 ? 117 PHE A CD2 1
+ATOM   884  C  CE1 . PHE A 1 117 ? 31.311  15.742  40.069 1.00 17.90 ? 117 PHE A CE1 1
+ATOM   885  C  CE2 . PHE A 1 117 ? 31.353  14.125  41.867 1.00 23.05 ? 117 PHE A CE2 1
+ATOM   886  C  CZ  . PHE A 1 117 ? 30.731  14.870  40.934 1.00 14.00 ? 117 PHE A CZ  1
+ATOM   887  N  N   . THR A 1 118 ? 35.373  17.750  44.038 1.00 11.56 ? 118 THR A N   1
+ATOM   888  C  CA  . THR A 1 118 ? 35.254  17.744  45.458 1.00 10.93 ? 118 THR A CA  1
+ATOM   889  C  C   . THR A 1 118 ? 33.839  17.687  45.728 1.00 15.34 ? 118 THR A C   1
+ATOM   890  O  O   . THR A 1 118 ? 33.054  18.199  44.968 1.00 14.33 ? 118 THR A O   1
+ATOM   891  C  CB  . THR A 1 118 ? 35.811  19.052  45.798 1.00 22.78 ? 118 THR A CB  1
+ATOM   892  O  OG1 . THR A 1 118 ? 35.369  20.263  45.417 1.00 25.00 ? 118 THR A OG1 1
+ATOM   893  C  CG2 . THR A 1 118 ? 37.432  19.021  45.774 1.00 25.00 ? 118 THR A CG2 1
+ATOM   894  N  N   . PRO A 1 119 ? 33.493  17.762  47.020 1.00 16.93 ? 119 PRO A N   1
+ATOM   895  C  CA  . PRO A 1 119 ? 32.076  17.845  47.465 1.00 7.97  ? 119 PRO A CA  1
+ATOM   896  C  C   . PRO A 1 119 ? 31.470  19.036  47.093 1.00 9.71  ? 119 PRO A C   1
+ATOM   897  O  O   . PRO A 1 119 ? 30.316  19.256  46.665 1.00 13.14 ? 119 PRO A O   1
+ATOM   898  C  CB  . PRO A 1 119 ? 32.077  17.606  48.966 1.00 15.02 ? 119 PRO A CB  1
+ATOM   899  C  CG  . PRO A 1 119 ? 33.149  16.608  49.169 1.00 20.08 ? 119 PRO A CG  1
+ATOM   900  C  CD  . PRO A 1 119 ? 34.300  17.026  48.068 1.00 23.85 ? 119 PRO A CD  1
+ATOM   901  N  N   . ALA A 1 120 ? 32.224  20.164  47.313 1.00 18.30 ? 120 ALA A N   1
+ATOM   902  C  CA  . ALA A 1 120 ? 31.842  21.408  47.057 1.00 20.48 ? 120 ALA A CA  1
+ATOM   903  C  C   . ALA A 1 120 ? 31.621  21.740  45.501 1.00 11.11 ? 120 ALA A C   1
+ATOM   904  O  O   . ALA A 1 120 ? 30.559  22.242  45.018 1.00 14.90 ? 120 ALA A O   1
+ATOM   905  C  CB  . ALA A 1 120 ? 32.505  22.690  47.619 1.00 21.25 ? 120 ALA A CB  1
+ATOM   906  N  N   . VAL A 1 121 ? 32.342  21.214  44.747 1.00 15.02 ? 121 VAL A N   1
+ATOM   907  C  CA  . VAL A 1 121 ? 32.236  21.278  43.328 1.00 11.64 ? 121 VAL A CA  1
+ATOM   908  C  C   . VAL A 1 121 ? 31.024  20.437  42.763 1.00 13.80 ? 121 VAL A C   1
+ATOM   909  O  O   . VAL A 1 121 ? 30.291  20.874  41.941 1.00 15.60 ? 121 VAL A O   1
+ATOM   910  C  CB  . VAL A 1 121 ? 33.529  20.991  42.582 1.00 16.28 ? 121 VAL A CB  1
+ATOM   911  C  CG1 . VAL A 1 121 ? 33.412  20.911  40.957 1.00 17.80 ? 121 VAL A CG1 1
+ATOM   912  C  CG2 . VAL A 1 121 ? 34.616  22.049  42.812 1.00 19.30 ? 121 VAL A CG2 1
+ATOM   913  N  N   . HIS A 1 122 ? 30.968  19.297  43.270 1.00 15.45 ? 122 HIS A N   1
+ATOM   914  C  CA  . HIS A 1 122 ? 29.712  18.239  43.050 1.00 11.57 ? 122 HIS A CA  1
+ATOM   915  C  C   . HIS A 1 122 ? 28.559  19.258  43.157 1.00 13.88 ? 122 HIS A C   1
+ATOM   916  O  O   . HIS A 1 122 ? 27.615  19.099  42.440 1.00 13.87 ? 122 HIS A O   1
+ATOM   917  C  CB  . HIS A 1 122 ? 30.075  17.054  43.880 1.00 12.36 ? 122 HIS A CB  1
+ATOM   918  C  CG  . HIS A 1 122 ? 29.005  16.136  43.833 1.00 15.49 ? 122 HIS A CG  1
+ATOM   919  N  ND1 . HIS A 1 122 ? 29.307  14.827  44.464 1.00 14.41 ? 122 HIS A ND1 1
+ATOM   920  C  CD2 . HIS A 1 122 ? 27.852  16.006  43.165 1.00 16.00 ? 122 HIS A CD2 1
+ATOM   921  C  CE1 . HIS A 1 122 ? 28.060  14.004  44.133 1.00 20.76 ? 122 HIS A CE1 1
+ATOM   922  N  NE2 . HIS A 1 122 ? 27.179  14.693  43.361 1.00 17.17 ? 122 HIS A NE2 1
+ATOM   923  N  N   . ALA A 1 123 ? 28.406  19.715  44.364 1.00 12.31 ? 123 ALA A N   1
+ATOM   924  C  CA  . ALA A 1 123 ? 27.282  20.460  44.773 1.00 12.34 ? 123 ALA A CA  1
+ATOM   925  C  C   . ALA A 1 123 ? 26.955  21.613  43.753 1.00 12.36 ? 123 ALA A C   1
+ATOM   926  O  O   . ALA A 1 123 ? 25.734  21.801  43.251 1.00 16.22 ? 123 ALA A O   1
+ATOM   927  C  CB  . ALA A 1 123 ? 27.337  21.026  46.168 1.00 18.20 ? 123 ALA A CB  1
+ATOM   928  N  N   . SER A 1 124 ? 28.074  22.355  43.329 1.00 11.72 ? 124 SER A N   1
+ATOM   929  C  CA  . SER A 1 124 ? 27.869  23.445  42.517 1.00 15.71 ? 124 SER A CA  1
+ATOM   930  C  C   . SER A 1 124 ? 27.468  22.934  41.046 1.00 11.97 ? 124 SER A C   1
+ATOM   931  O  O   . SER A 1 124 ? 26.609  23.602  40.432 1.00 13.78 ? 124 SER A O   1
+ATOM   932  C  CB  . SER A 1 124 ? 29.091  24.305  42.331 1.00 17.31 ? 124 SER A CB  1
+ATOM   933  O  OG  . SER A 1 124 ? 29.403  24.925  43.592 1.00 19.36 ? 124 SER A OG  1
+ATOM   934  N  N   . LEU A 1 125 ? 28.120  21.852  40.685 1.00 11.45 ? 125 LEU A N   1
+ATOM   935  C  CA  . LEU A 1 125 ? 27.743  21.454  39.340 1.00 9.77  ? 125 LEU A CA  1
+ATOM   936  C  C   . LEU A 1 125 ? 26.437  20.912  39.292 1.00 13.87 ? 125 LEU A C   1
+ATOM   937  O  O   . LEU A 1 125 ? 25.705  21.020  38.235 1.00 12.03 ? 125 LEU A O   1
+ATOM   938  C  CB  . LEU A 1 125 ? 28.681  20.367  38.957 1.00 14.61 ? 125 LEU A CB  1
+ATOM   939  C  CG  . LEU A 1 125 ? 30.138  20.621  38.452 1.00 15.39 ? 125 LEU A CG  1
+ATOM   940  C  CD1 . LEU A 1 125 ? 31.004  19.480  38.447 1.00 26.84 ? 125 LEU A CD1 1
+ATOM   941  C  CD2 . LEU A 1 125 ? 30.095  21.415  37.241 1.00 19.46 ? 125 LEU A CD2 1
+ATOM   942  N  N   . ASP A 1 126 ? 25.835  20.210  40.266 1.00 13.89 ? 126 ASP A N   1
+ATOM   943  C  CA  . ASP A 1 126 ? 24.505  19.681  40.409 1.00 14.28 ? 126 ASP A CA  1
+ATOM   944  C  C   . ASP A 1 126 ? 23.589  20.757  40.242 1.00 13.60 ? 126 ASP A C   1
+ATOM   945  O  O   . ASP A 1 126 ? 22.492  20.897  39.594 1.00 12.25 ? 126 ASP A O   1
+ATOM   946  C  CB  . ASP A 1 126 ? 24.293  18.835  41.586 1.00 9.77  ? 126 ASP A CB  1
+ATOM   947  C  CG  . ASP A 1 126 ? 22.993  17.965  41.708 1.00 17.51 ? 126 ASP A CG  1
+ATOM   948  O  OD1 . ASP A 1 126 ? 22.693  17.462  40.610 1.00 22.67 ? 126 ASP A OD1 1
+ATOM   949  O  OD2 . ASP A 1 126 ? 22.121  18.221  42.404 1.00 20.83 ? 126 ASP A OD2 1
+ATOM   950  N  N   . LYS A 1 127 ? 23.791  21.958  40.968 1.00 11.87 ? 127 LYS A N   1
+ATOM   951  C  CA  . LYS A 1 127 ? 23.075  23.151  40.945 1.00 11.94 ? 127 LYS A CA  1
+ATOM   952  C  C   . LYS A 1 127 ? 23.108  23.675  39.518 1.00 16.34 ? 127 LYS A C   1
+ATOM   953  O  O   . LYS A 1 127 ? 21.995  24.194  39.091 1.00 15.26 ? 127 LYS A O   1
+ATOM   954  C  CB  . LYS A 1 127 ? 23.361  23.933  42.324 1.00 27.23 ? 127 LYS A CB  1
+ATOM   955  C  CG  . LYS A 1 127 ? 23.050  24.571  42.382 1.00 41.38 ? 127 LYS A CG  1
+ATOM   956  C  CD  . LYS A 1 127 ? 23.405  25.008  44.274 1.00 22.35 ? 127 LYS A CD  1
+ATOM   957  C  CE  . LYS A 1 127 ? 22.951  26.352  44.048 1.00 24.85 ? 127 LYS A CE  1
+ATOM   958  N  NZ  . LYS A 1 127 ? 23.359  27.311  45.174 1.00 27.43 ? 127 LYS A NZ  1
+ATOM   959  N  N   . PHE A 1 128 ? 24.149  23.834  39.026 1.00 9.60  ? 128 PHE A N   1
+ATOM   960  C  CA  . PHE A 1 128 ? 24.281  24.440  37.666 1.00 9.45  ? 128 PHE A CA  1
+ATOM   961  C  C   . PHE A 1 128 ? 23.510  23.612  36.660 1.00 11.35 ? 128 PHE A C   1
+ATOM   962  O  O   . PHE A 1 128 ? 22.731  24.239  35.874 1.00 13.72 ? 128 PHE A O   1
+ATOM   963  C  CB  . PHE A 1 128 ? 25.746  24.402  37.282 1.00 10.04 ? 128 PHE A CB  1
+ATOM   964  C  CG  . PHE A 1 128 ? 25.879  24.780  35.815 1.00 12.71 ? 128 PHE A CG  1
+ATOM   965  C  CD1 . PHE A 1 128 ? 25.661  26.173  35.380 1.00 22.47 ? 128 PHE A CD1 1
+ATOM   966  C  CD2 . PHE A 1 128 ? 26.305  23.939  35.044 1.00 15.10 ? 128 PHE A CD2 1
+ATOM   967  C  CE1 . PHE A 1 128 ? 25.831  26.372  34.010 1.00 21.90 ? 128 PHE A CE1 1
+ATOM   968  C  CE2 . PHE A 1 128 ? 26.807  24.009  33.619 1.00 24.41 ? 128 PHE A CE2 1
+ATOM   969  C  CZ  . PHE A 1 128 ? 26.482  25.336  33.332 1.00 19.00 ? 128 PHE A CZ  1
+ATOM   970  N  N   . LEU A 1 129 ? 23.514  22.246  36.770 1.00 10.92 ? 129 LEU A N   1
+ATOM   971  C  CA  . LEU A 1 129 ? 22.716  21.543  35.727 1.00 8.59  ? 129 LEU A CA  1
+ATOM   972  C  C   . LEU A 1 129 ? 21.353  21.554  35.966 1.00 15.58 ? 129 LEU A C   1
+ATOM   973  O  O   . LEU A 1 129 ? 20.533  21.614  35.038 1.00 12.33 ? 129 LEU A O   1
+ATOM   974  C  CB  . LEU A 1 129 ? 23.215  20.096  35.689 1.00 11.08 ? 129 LEU A CB  1
+ATOM   975  C  CG  . LEU A 1 129 ? 24.740  19.751  35.250 1.00 16.43 ? 129 LEU A CG  1
+ATOM   976  C  CD1 . LEU A 1 129 ? 25.168  18.497  35.470 1.00 21.21 ? 129 LEU A CD1 1
+ATOM   977  C  CD2 . LEU A 1 129 ? 24.681  20.243  33.623 1.00 24.11 ? 129 LEU A CD2 1
+ATOM   978  N  N   . ALA A 1 130 ? 20.872  21.754  37.150 1.00 13.59 ? 130 ALA A N   1
+ATOM   979  C  CA  . ALA A 1 130 ? 19.455  21.983  37.526 1.00 12.80 ? 130 ALA A CA  1
+ATOM   980  C  C   . ALA A 1 130 ? 18.959  23.277  36.957 1.00 13.10 ? 130 ALA A C   1
+ATOM   981  O  O   . ALA A 1 130 ? 17.877  23.520  36.410 1.00 16.72 ? 130 ALA A O   1
+ATOM   982  C  CB  . ALA A 1 130 ? 19.238  21.954  39.051 1.00 11.70 ? 130 ALA A CB  1
+ATOM   983  N  N   . SER A 1 131 ? 19.876  24.361  36.976 1.00 12.15 ? 131 SER A N   1
+ATOM   984  C  CA  . SER A 1 131 ? 19.427  25.616  36.430 1.00 17.97 ? 131 SER A CA  1
+ATOM   985  C  C   . SER A 1 131 ? 19.409  25.535  34.834 1.00 14.23 ? 131 SER A C   1
+ATOM   986  O  O   . SER A 1 131 ? 18.395  26.257  34.407 1.00 17.89 ? 131 SER A O   1
+ATOM   987  C  CB  . SER A 1 131 ? 20.555  26.729  36.834 1.00 19.09 ? 131 SER A CB  1
+ATOM   988  O  OG  . SER A 1 131 ? 20.389  26.812  38.036 1.00 34.89 ? 131 SER A OG  1
+ATOM   989  N  N   . VAL A 1 132 ? 20.409  24.938  34.376 1.00 11.02 ? 132 VAL A N   1
+ATOM   990  C  CA  . VAL A 1 132 ? 20.283  24.913  32.863 1.00 13.44 ? 132 VAL A CA  1
+ATOM   991  C  C   . VAL A 1 132 ? 19.029  24.122  32.606 1.00 13.26 ? 132 VAL A C   1
+ATOM   992  O  O   . VAL A 1 132 ? 18.248  24.688  31.621 1.00 14.28 ? 132 VAL A O   1
+ATOM   993  C  CB  . VAL A 1 132 ? 21.357  24.177  32.402 1.00 17.47 ? 132 VAL A CB  1
+ATOM   994  C  CG1 . VAL A 1 132 ? 21.413  23.724  30.933 1.00 23.96 ? 132 VAL A CG1 1
+ATOM   995  C  CG2 . VAL A 1 132 ? 22.716  24.922  32.465 1.00 15.24 ? 132 VAL A CG2 1
+ATOM   996  N  N   . SER A 1 133 ? 18.586  23.020  33.190 1.00 11.44 ? 133 SER A N   1
+ATOM   997  C  CA  . SER A 1 133 ? 17.360  22.290  32.998 1.00 14.28 ? 133 SER A CA  1
+ATOM   998  C  C   . SER A 1 133 ? 16.153  23.195  33.280 1.00 22.70 ? 133 SER A C   1
+ATOM   999  O  O   . SER A 1 133 ? 15.275  23.082  32.379 1.00 18.73 ? 133 SER A O   1
+ATOM   1000 C  CB  . SER A 1 133 ? 17.429  21.112  33.913 1.00 14.07 ? 133 SER A CB  1
+ATOM   1001 O  OG  . SER A 1 133 ? 18.393  20.163  33.582 1.00 16.41 ? 133 SER A OG  1
+ATOM   1002 N  N   . THR A 1 134 ? 16.105  24.077  34.173 1.00 14.75 ? 134 THR A N   1
+ATOM   1003 C  CA  . THR A 1 134 ? 14.989  24.856  34.285 1.00 11.93 ? 134 THR A CA  1
+ATOM   1004 C  C   . THR A 1 134 ? 14.917  25.790  33.367 1.00 12.33 ? 134 THR A C   1
+ATOM   1005 O  O   . THR A 1 134 ? 13.820  26.152  32.889 1.00 15.87 ? 134 THR A O   1
+ATOM   1006 C  CB  . THR A 1 134 ? 15.318  25.445  35.675 1.00 23.98 ? 134 THR A CB  1
+ATOM   1007 O  OG1 . THR A 1 134 ? 15.160  24.821  36.657 1.00 24.65 ? 134 THR A OG1 1
+ATOM   1008 C  CG2 . THR A 1 134 ? 14.308  26.695  35.959 1.00 35.48 ? 134 THR A CG2 1
+ATOM   1009 N  N   . VAL A 1 135 ? 15.901  26.476  32.741 1.00 16.85 ? 135 VAL A N   1
+ATOM   1010 C  CA  . VAL A 1 135 ? 15.860  27.465  31.729 1.00 15.02 ? 135 VAL A CA  1
+ATOM   1011 C  C   . VAL A 1 135 ? 15.576  26.659  30.467 1.00 18.49 ? 135 VAL A C   1
+ATOM   1012 O  O   . VAL A 1 135 ? 14.593  27.208  29.765 1.00 17.84 ? 135 VAL A O   1
+ATOM   1013 C  CB  . VAL A 1 135 ? 17.301  28.155  31.489 1.00 21.41 ? 135 VAL A CB  1
+ATOM   1014 C  CG1 . VAL A 1 135 ? 17.360  28.820  30.158 1.00 28.88 ? 135 VAL A CG1 1
+ATOM   1015 C  CG2 . VAL A 1 135 ? 17.666  28.942  32.668 1.00 18.54 ? 135 VAL A CG2 1
+ATOM   1016 N  N   . LEU A 1 136 ? 15.937  25.476  30.146 1.00 15.13 ? 136 LEU A N   1
+ATOM   1017 C  CA  . LEU A 1 136 ? 15.442  24.728  28.988 1.00 14.14 ? 136 LEU A CA  1
+ATOM   1018 C  C   . LEU A 1 136 ? 13.898  24.423  28.942 1.00 16.82 ? 136 LEU A C   1
+ATOM   1019 O  O   . LEU A 1 136 ? 13.356  24.038  27.808 1.00 16.56 ? 136 LEU A O   1
+ATOM   1020 C  CB  . LEU A 1 136 ? 16.388  23.591  28.673 1.00 19.05 ? 136 LEU A CB  1
+ATOM   1021 C  CG  . LEU A 1 136 ? 17.789  23.816  27.944 1.00 19.99 ? 136 LEU A CG  1
+ATOM   1022 C  CD1 . LEU A 1 136 ? 18.498  22.572  28.082 1.00 23.33 ? 136 LEU A CD1 1
+ATOM   1023 C  CD2 . LEU A 1 136 ? 17.951  24.924  27.051 1.00 20.84 ? 136 LEU A CD2 1
+ATOM   1024 N  N   . THR A 1 137 ? 13.409  24.308  30.091 1.00 14.14 ? 137 THR A N   1
+ATOM   1025 C  CA  . THR A 1 137 ? 11.868  23.759  30.279 1.00 17.11 ? 137 THR A CA  1
+ATOM   1026 C  C   . THR A 1 137 ? 11.174  24.984  30.546 1.00 15.43 ? 137 THR A C   1
+ATOM   1027 O  O   . THR A 1 137 ? 9.885   24.822  30.687 1.00 15.99 ? 137 THR A O   1
+ATOM   1028 C  CB  . THR A 1 137 ? 11.872  22.866  31.967 1.00 17.27 ? 137 THR A CB  1
+ATOM   1029 O  OG1 . THR A 1 137 ? 12.346  21.655  30.930 1.00 28.37 ? 137 THR A OG1 1
+ATOM   1030 C  CG2 . THR A 1 137 ? 12.708  23.088  32.483 1.00 47.04 ? 137 THR A CG2 1
+ATOM   1031 N  N   . SER A 1 138 ? 11.582  26.134  30.523 1.00 16.91 ? 138 SER A N   1
+ATOM   1032 C  CA  . SER A 1 138 ? 11.007  27.371  30.879 1.00 23.51 ? 138 SER A CA  1
+ATOM   1033 C  C   . SER A 1 138 ? 9.706   27.886  30.080 1.00 23.60 ? 138 SER A C   1
+ATOM   1034 O  O   . SER A 1 138 ? 8.807   28.281  30.694 1.00 27.80 ? 138 SER A O   1
+ATOM   1035 C  CB  . SER A 1 138 ? 12.256  29.024  30.432 1.00 22.76 ? 138 SER A CB  1
+ATOM   1036 O  OG  . SER A 1 138 ? 11.938  28.569  31.612 1.00 45.85 ? 138 SER A OG  1
+ATOM   1037 N  N   . LYS A 1 139 ? 9.814   27.464  28.890 1.00 19.13 ? 139 LYS A N   1
+ATOM   1038 C  CA  . LYS A 1 139 ? 8.804   28.073  27.820 1.00 21.43 ? 139 LYS A CA  1
+ATOM   1039 C  C   . LYS A 1 139 ? 7.846   26.906  27.589 1.00 18.35 ? 139 LYS A C   1
+ATOM   1040 O  O   . LYS A 1 139 ? 7.219   27.010  26.637 1.00 22.16 ? 139 LYS A O   1
+ATOM   1041 C  CB  . LYS A 1 139 ? 9.426   28.678  26.637 1.00 24.13 ? 139 LYS A CB  1
+ATOM   1042 C  CG  . LYS A 1 139 ? 10.268  29.778  26.985 1.00 28.98 ? 139 LYS A CG  1
+ATOM   1043 C  CD  . LYS A 1 139 ? 11.231  30.175  25.810 1.00 33.18 ? 139 LYS A CD  1
+ATOM   1044 C  CE  . LYS A 1 139 ? 11.836  31.387  26.028 1.00 52.82 ? 139 LYS A CE  1
+ATOM   1045 N  NZ  . LYS A 1 139 ? 13.057  31.429  24.501 1.00 55.02 ? 139 LYS A NZ  1
+ATOM   1046 N  N   . TYR A 1 140 ? 7.786   25.762  28.196 1.00 17.12 ? 140 TYR A N   1
+ATOM   1047 C  CA  . TYR A 1 140 ? 7.030   24.682  27.951 1.00 22.48 ? 140 TYR A CA  1
+ATOM   1048 C  C   . TYR A 1 140 ? 5.484   24.848  28.048 1.00 18.75 ? 140 TYR A C   1
+ATOM   1049 O  O   . TYR A 1 140 ? 4.740   24.283  27.139 1.00 22.47 ? 140 TYR A O   1
+ATOM   1050 C  CB  . TYR A 1 140 ? 7.248   23.357  28.784 1.00 23.15 ? 140 TYR A CB  1
+ATOM   1051 C  CG  . TYR A 1 140 ? 8.341   22.538  28.191 1.00 15.57 ? 140 TYR A CG  1
+ATOM   1052 C  CD1 . TYR A 1 140 ? 8.262   21.025  28.230 1.00 16.98 ? 140 TYR A CD1 1
+ATOM   1053 C  CD2 . TYR A 1 140 ? 9.581   22.957  27.681 1.00 18.11 ? 140 TYR A CD2 1
+ATOM   1054 C  CE1 . TYR A 1 140 ? 9.324   20.260  27.686 1.00 19.97 ? 140 TYR A CE1 1
+ATOM   1055 C  CE2 . TYR A 1 140 ? 10.629  22.029  27.267 1.00 14.94 ? 140 TYR A CE2 1
+ATOM   1056 C  CZ  . TYR A 1 140 ? 10.423  20.609  27.292 1.00 17.89 ? 140 TYR A CZ  1
+ATOM   1057 O  OH  . TYR A 1 140 ? 11.366  19.964  26.904 1.00 18.05 ? 140 TYR A OH  1
+ATOM   1058 N  N   . ARG A 1 141 ? 5.091   25.732  28.777 1.00 17.59 ? 141 ARG A N   1
+ATOM   1059 C  CA  . ARG A 1 141 ? 3.543   26.104  29.057 1.00 24.58 ? 141 ARG A CA  1
+ATOM   1060 C  C   . ARG A 1 141 ? 3.490   27.656  29.556 1.00 44.44 ? 141 ARG A C   1
+ATOM   1061 O  O   . ARG A 1 141 ? 4.424   27.979  30.158 1.00 21.81 ? 141 ARG A O   1
+ATOM   1062 C  CB  . ARG A 1 141 ? 2.907   25.003  29.515 1.00 33.40 ? 141 ARG A CB  1
+ATOM   1063 C  CG  . ARG A 1 141 ? 3.391   24.818  31.230 1.00 17.28 ? 141 ARG A CG  1
+ATOM   1064 C  CD  . ARG A 1 141 ? 2.255   23.813  31.672 1.00 14.66 ? 141 ARG A CD  1
+ATOM   1065 N  NE  . ARG A 1 141 ? 2.987   23.633  32.900 1.00 22.73 ? 141 ARG A NE  1
+ATOM   1066 C  CZ  . ARG A 1 141 ? 2.066   23.002  33.850 1.00 26.88 ? 141 ARG A CZ  1
+ATOM   1067 N  NH1 . ARG A 1 141 ? 0.996   22.173  33.694 1.00 23.24 ? 141 ARG A NH1 1
+ATOM   1068 N  NH2 . ARG A 1 141 ? 2.694   22.926  35.095 1.00 33.34 ? 141 ARG A NH2 1
+ATOM   1069 O  OXT . ARG A 1 141 ? 2.359   27.895  29.445 1.00 31.52 ? 141 ARG A OXT 1
+ATOM   1070 N  N   . VAL B 2 1   ? 16.303  -7.918  42.567 1.00 46.08 ? 1   VAL B N   1
+ATOM   1071 C  CA  . VAL B 2 1   ? 15.768  -7.377  41.064 1.00 70.96 ? 1   VAL B CA  1
+ATOM   1072 C  C   . VAL B 2 1   ? 16.461  -8.681  39.591 1.00 69.74 ? 1   VAL B C   1
+ATOM   1073 O  O   . VAL B 2 1   ? 15.976  -10.100 40.396 1.00 71.82 ? 1   VAL B O   1
+ATOM   1074 C  CB  . VAL B 2 1   ? 16.598  -5.775  40.614 1.00 59.18 ? 1   VAL B CB  1
+ATOM   1075 C  CG1 . VAL B 2 1   ? 14.879  -4.766  40.240 1.00 57.89 ? 1   VAL B CG1 1
+ATOM   1076 C  CG2 . VAL B 2 1   ? 17.783  -5.679  40.973 1.00 44.20 ? 1   VAL B CG2 1
+ATOM   1077 N  N   . HIS B 2 2   ? 16.096  -8.250  39.043 1.00 53.55 ? 2   HIS B N   1
+ATOM   1078 C  CA  . HIS B 2 2   ? 16.878  -9.200  38.097 1.00 62.62 ? 2   HIS B CA  1
+ATOM   1079 C  C   . HIS B 2 2   ? 18.129  -8.434  36.985 1.00 51.71 ? 2   HIS B C   1
+ATOM   1080 O  O   . HIS B 2 2   ? 18.065  -7.419  35.976 1.00 48.42 ? 2   HIS B O   1
+ATOM   1081 C  CB  . HIS B 2 2   ? 15.819  -8.758  36.444 1.00 62.58 ? 2   HIS B CB  1
+ATOM   1082 C  CG  . HIS B 2 2   ? 15.894  -8.973  35.642 1.00 73.96 ? 2   HIS B CG  1
+ATOM   1083 N  ND1 . HIS B 2 2   ? 16.285  -7.740  34.272 1.00 80.12 ? 2   HIS B ND1 1
+ATOM   1084 C  CD2 . HIS B 2 2   ? 16.263  -10.962 35.294 1.00 63.02 ? 2   HIS B CD2 1
+ATOM   1085 C  CE1 . HIS B 2 2   ? 16.985  -9.461  33.138 1.00 76.40 ? 2   HIS B CE1 1
+ATOM   1086 N  NE2 . HIS B 2 2   ? 17.454  -10.935 33.581 1.00 62.86 ? 2   HIS B NE2 1
+ATOM   1087 N  N   . LEU B 2 3   ? 19.032  -8.933  37.415 1.00 43.89 ? 3   LEU B N   1
+ATOM   1088 C  CA  . LEU B 2 3   ? 20.285  -8.668  36.472 1.00 43.79 ? 3   LEU B CA  1
+ATOM   1089 C  C   . LEU B 2 3   ? 20.993  -10.025 35.882 1.00 32.77 ? 3   LEU B C   1
+ATOM   1090 O  O   . LEU B 2 3   ? 20.622  -11.123 36.345 1.00 41.84 ? 3   LEU B O   1
+ATOM   1091 C  CB  . LEU B 2 3   ? 21.338  -8.366  37.863 1.00 28.80 ? 3   LEU B CB  1
+ATOM   1092 C  CG  . LEU B 2 3   ? 21.053  -6.980  38.587 1.00 28.70 ? 3   LEU B CG  1
+ATOM   1093 C  CD1 . LEU B 2 3   ? 21.999  -6.887  39.503 1.00 63.39 ? 3   LEU B CD1 1
+ATOM   1094 C  CD2 . LEU B 2 3   ? 21.683  -6.067  37.645 1.00 32.10 ? 3   LEU B CD2 1
+ATOM   1095 N  N   . THR B 2 4   ? 21.283  -9.574  34.662 1.00 42.35 ? 4   THR B N   1
+ATOM   1096 C  CA  . THR B 2 4   ? 22.096  -10.826 34.241 1.00 41.74 ? 4   THR B CA  1
+ATOM   1097 C  C   . THR B 2 4   ? 23.082  -11.288 34.886 1.00 36.91 ? 4   THR B C   1
+ATOM   1098 O  O   . THR B 2 4   ? 23.751  -10.520 35.615 1.00 31.57 ? 4   THR B O   1
+ATOM   1099 C  CB  . THR B 2 4   ? 22.204  -10.187 32.827 1.00 38.91 ? 4   THR B CB  1
+ATOM   1100 O  OG1 . THR B 2 4   ? 23.352  -9.327  32.684 1.00 52.85 ? 4   THR B OG1 1
+ATOM   1101 C  CG2 . THR B 2 4   ? 21.258  -9.536  31.869 1.00 56.94 ? 4   THR B CG2 1
+ATOM   1102 N  N   . PRO B 2 5   ? 23.875  -12.390 34.465 1.00 45.56 ? 5   PRO B N   1
+ATOM   1103 C  CA  . PRO B 2 5   ? 24.679  -13.099 34.970 1.00 47.54 ? 5   PRO B CA  1
+ATOM   1104 C  C   . PRO B 2 5   ? 26.082  -12.002 35.046 1.00 37.80 ? 5   PRO B C   1
+ATOM   1105 O  O   . PRO B 2 5   ? 26.874  -11.968 35.960 1.00 33.06 ? 5   PRO B O   1
+ATOM   1106 C  CB  . PRO B 2 5   ? 25.273  -14.398 34.765 1.00 62.12 ? 5   PRO B CB  1
+ATOM   1107 C  CG  . PRO B 2 5   ? 23.928  -14.683 34.012 1.00 42.55 ? 5   PRO B CG  1
+ATOM   1108 C  CD  . PRO B 2 5   ? 22.934  -13.780 33.779 1.00 48.08 ? 5   PRO B CD  1
+ATOM   1109 N  N   . GLU B 2 6   ? 25.979  -11.464 33.785 1.00 27.00 ? 6   GLU B N   1
+ATOM   1110 C  CA  . GLU B 2 6   ? 27.151  -10.845 33.398 1.00 34.37 ? 6   GLU B CA  1
+ATOM   1111 C  C   . GLU B 2 6   ? 27.063  -9.364  34.364 1.00 23.02 ? 6   GLU B C   1
+ATOM   1112 O  O   . GLU B 2 6   ? 28.360  -8.802  34.768 1.00 28.54 ? 6   GLU B O   1
+ATOM   1113 C  CB  . GLU B 2 6   ? 27.123  -10.140 31.903 1.00 37.20 ? 6   GLU B CB  1
+ATOM   1114 C  CG  . GLU B 2 6   ? 26.412  -9.884  31.193 1.00 66.65 ? 6   GLU B CG  1
+ATOM   1115 C  CD  . GLU B 2 6   ? 25.132  -11.404 30.618 1.00 60.44 ? 6   GLU B CD  1
+ATOM   1116 O  OE1 . GLU B 2 6   ? 25.989  -12.745 31.120 1.00 63.16 ? 6   GLU B OE1 1
+ATOM   1117 O  OE2 . GLU B 2 6   ? 24.244  -11.626 30.873 1.00 70.62 ? 6   GLU B OE2 1
+ATOM   1118 N  N   . GLU B 2 7   ? 25.968  -8.945  34.599 1.00 31.47 ? 7   GLU B N   1
+ATOM   1119 C  CA  . GLU B 2 7   ? 25.410  -7.639  35.376 1.00 34.08 ? 7   GLU B CA  1
+ATOM   1120 C  C   . GLU B 2 7   ? 26.025  -8.114  36.822 1.00 21.49 ? 7   GLU B C   1
+ATOM   1121 O  O   . GLU B 2 7   ? 26.670  -7.205  37.380 1.00 27.04 ? 7   GLU B O   1
+ATOM   1122 C  CB  . GLU B 2 7   ? 24.500  -7.325  35.178 1.00 35.55 ? 7   GLU B CB  1
+ATOM   1123 C  CG  . GLU B 2 7   ? 24.024  -6.472  33.702 1.00 33.74 ? 7   GLU B CG  1
+ATOM   1124 C  CD  . GLU B 2 7   ? 22.752  -5.967  33.883 1.00 31.89 ? 7   GLU B CD  1
+ATOM   1125 O  OE1 . GLU B 2 7   ? 22.611  -4.832  33.230 1.00 52.51 ? 7   GLU B OE1 1
+ATOM   1126 O  OE2 . GLU B 2 7   ? 21.635  -6.665  34.260 1.00 32.56 ? 7   GLU B OE2 1
+ATOM   1127 N  N   . LYS B 2 8   ? 25.484  -9.070  37.386 1.00 26.08 ? 8   LYS B N   1
+ATOM   1128 C  CA  . LYS B 2 8   ? 25.777  -9.448  38.625 1.00 32.23 ? 8   LYS B CA  1
+ATOM   1129 C  C   . LYS B 2 8   ? 27.225  -9.572  38.754 1.00 26.59 ? 8   LYS B C   1
+ATOM   1130 O  O   . LYS B 2 8   ? 28.069  -9.108  39.858 1.00 26.11 ? 8   LYS B O   1
+ATOM   1131 C  CB  . LYS B 2 8   ? 24.916  -10.930 38.948 1.00 36.34 ? 8   LYS B CB  1
+ATOM   1132 C  CG  . LYS B 2 8   ? 25.315  -11.260 39.644 1.00 64.20 ? 8   LYS B CG  1
+ATOM   1133 C  CD  . LYS B 2 8   ? 25.115  -12.674 40.713 1.00 73.64 ? 8   LYS B CD  1
+ATOM   1134 C  CE  . LYS B 2 8   ? 25.818  -13.055 41.799 1.00 79.30 ? 8   LYS B CE  1
+ATOM   1135 N  NZ  . LYS B 2 8   ? 25.896  -15.297 42.163 1.00 66.73 ? 8   LYS B NZ  1
+ATOM   1136 N  N   . SER B 2 9   ? 28.090  -10.243 38.007 1.00 23.88 ? 9   SER B N   1
+ATOM   1137 C  CA  . SER B 2 9   ? 29.173  -10.409 38.052 1.00 36.76 ? 9   SER B CA  1
+ATOM   1138 C  C   . SER B 2 9   ? 30.351  -8.960  38.047 1.00 37.61 ? 9   SER B C   1
+ATOM   1139 O  O   . SER B 2 9   ? 31.227  -8.786  38.776 1.00 28.84 ? 9   SER B O   1
+ATOM   1140 C  CB  . SER B 2 9   ? 29.979  -11.803 37.274 1.00 36.63 ? 9   SER B CB  1
+ATOM   1141 O  OG  . SER B 2 9   ? 30.447  -10.713 36.371 1.00 64.02 ? 9   SER B OG  1
+ATOM   1142 N  N   . ALA B 2 10  ? 29.669  -8.043  37.212 1.00 21.54 ? 10  ALA B N   1
+ATOM   1143 C  CA  . ALA B 2 10  ? 30.388  -6.975  37.145 1.00 32.77 ? 10  ALA B CA  1
+ATOM   1144 C  C   . ALA B 2 10  ? 30.157  -5.965  38.591 1.00 23.64 ? 10  ALA B C   1
+ATOM   1145 O  O   . ALA B 2 10  ? 31.142  -5.271  39.029 1.00 26.26 ? 10  ALA B O   1
+ATOM   1146 C  CB  . ALA B 2 10  ? 29.710  -6.088  36.222 1.00 30.88 ? 10  ALA B CB  1
+ATOM   1147 N  N   . VAL B 2 11  ? 28.951  -6.098  39.209 1.00 22.75 ? 11  VAL B N   1
+ATOM   1148 C  CA  . VAL B 2 11  ? 28.708  -5.462  40.539 1.00 18.12 ? 11  VAL B CA  1
+ATOM   1149 C  C   . VAL B 2 11  ? 29.770  -5.947  41.527 1.00 18.13 ? 11  VAL B C   1
+ATOM   1150 O  O   . VAL B 2 11  ? 30.362  -5.128  42.234 1.00 19.40 ? 11  VAL B O   1
+ATOM   1151 C  CB  . VAL B 2 11  ? 27.347  -5.671  40.753 1.00 19.48 ? 11  VAL B CB  1
+ATOM   1152 C  CG1 . VAL B 2 11  ? 27.022  -5.358  42.187 1.00 26.15 ? 11  VAL B CG1 1
+ATOM   1153 C  CG2 . VAL B 2 11  ? 26.397  -4.744  39.946 1.00 23.37 ? 11  VAL B CG2 1
+ATOM   1154 N  N   . THR B 2 12  ? 29.713  -7.218  41.558 1.00 19.01 ? 12  THR B N   1
+ATOM   1155 C  CA  . THR B 2 12  ? 30.415  -8.061  42.603 1.00 25.04 ? 12  THR B CA  1
+ATOM   1156 C  C   . THR B 2 12  ? 31.891  -7.795  42.538 1.00 20.68 ? 12  THR B C   1
+ATOM   1157 O  O   . THR B 2 12  ? 32.691  -7.432  43.355 1.00 23.87 ? 12  THR B O   1
+ATOM   1158 C  CB  . THR B 2 12  ? 30.184  -9.749  42.564 1.00 42.63 ? 12  THR B CB  1
+ATOM   1159 O  OG1 . THR B 2 12  ? 29.010  -9.686  42.902 1.00 42.78 ? 12  THR B OG1 1
+ATOM   1160 C  CG2 . THR B 2 12  ? 30.685  -9.913  42.330 1.00 67.38 ? 12  THR B CG2 1
+ATOM   1161 N  N   . ALA B 2 13  ? 32.449  -7.807  41.322 1.00 22.79 ? 13  ALA B N   1
+ATOM   1162 C  CA  . ALA B 2 13  ? 33.717  -7.491  41.106 1.00 26.66 ? 13  ALA B CA  1
+ATOM   1163 C  C   . ALA B 2 13  ? 34.359  -6.293  41.381 1.00 26.26 ? 13  ALA B C   1
+ATOM   1164 O  O   . ALA B 2 13  ? 35.239  -6.032  42.098 1.00 27.07 ? 13  ALA B O   1
+ATOM   1165 C  CB  . ALA B 2 13  ? 34.055  -7.685  39.478 1.00 26.35 ? 13  ALA B CB  1
+ATOM   1166 N  N   . LEU B 2 14  ? 33.622  -5.060  40.984 1.00 15.70 ? 14  LEU B N   1
+ATOM   1167 C  CA  . LEU B 2 14  ? 34.030  -3.783  41.613 1.00 15.10 ? 14  LEU B CA  1
+ATOM   1168 C  C   . LEU B 2 14  ? 34.027  -3.705  43.040 1.00 17.25 ? 14  LEU B C   1
+ATOM   1169 O  O   . LEU B 2 14  ? 34.634  -2.952  43.648 1.00 15.43 ? 14  LEU B O   1
+ATOM   1170 C  CB  . LEU B 2 14  ? 33.058  -2.776  40.745 1.00 16.82 ? 14  LEU B CB  1
+ATOM   1171 C  CG  . LEU B 2 14  ? 33.542  -1.403  40.711 1.00 27.27 ? 14  LEU B CG  1
+ATOM   1172 C  CD1 . LEU B 2 14  ? 34.749  -1.222  40.263 1.00 40.43 ? 14  LEU B CD1 1
+ATOM   1173 C  CD2 . LEU B 2 14  ? 32.306  -0.474  40.615 1.00 24.81 ? 14  LEU B CD2 1
+ATOM   1174 N  N   . TRP B 2 15  ? 32.809  -4.226  43.599 1.00 17.75 ? 15  TRP B N   1
+ATOM   1175 C  CA  . TRP B 2 15  ? 32.612  -4.051  45.053 1.00 20.73 ? 15  TRP B CA  1
+ATOM   1176 C  C   . TRP B 2 15  ? 33.812  -4.677  45.876 1.00 17.66 ? 15  TRP B C   1
+ATOM   1177 O  O   . TRP B 2 15  ? 33.987  -4.054  46.970 1.00 18.75 ? 15  TRP B O   1
+ATOM   1178 C  CB  . TRP B 2 15  ? 31.325  -4.555  45.370 1.00 17.11 ? 15  TRP B CB  1
+ATOM   1179 C  CG  . TRP B 2 15  ? 30.929  -4.067  46.853 1.00 17.91 ? 15  TRP B CG  1
+ATOM   1180 C  CD1 . TRP B 2 15  ? 30.923  -4.649  47.964 1.00 21.87 ? 15  TRP B CD1 1
+ATOM   1181 C  CD2 . TRP B 2 15  ? 30.336  -2.821  47.043 1.00 17.58 ? 15  TRP B CD2 1
+ATOM   1182 N  NE1 . TRP B 2 15  ? 30.408  -3.970  49.009 1.00 18.04 ? 15  TRP B NE1 1
+ATOM   1183 C  CE2 . TRP B 2 15  ? 30.114  -2.620  48.507 1.00 16.29 ? 15  TRP B CE2 1
+ATOM   1184 C  CE3 . TRP B 2 15  ? 30.087  -1.669  46.224 1.00 16.29 ? 15  TRP B CE3 1
+ATOM   1185 C  CZ2 . TRP B 2 15  ? 29.510  -1.446  49.040 1.00 25.87 ? 15  TRP B CZ2 1
+ATOM   1186 C  CZ3 . TRP B 2 15  ? 29.529  -0.511  46.874 1.00 17.96 ? 15  TRP B CZ3 1
+ATOM   1187 C  CH2 . TRP B 2 15  ? 29.203  -0.550  48.185 1.00 24.12 ? 15  TRP B CH2 1
+ATOM   1188 N  N   . GLY B 2 16  ? 34.336  -5.678  45.229 1.00 18.59 ? 16  GLY B N   1
+ATOM   1189 C  CA  . GLY B 2 16  ? 35.598  -6.298  45.942 1.00 18.72 ? 16  GLY B CA  1
+ATOM   1190 C  C   . GLY B 2 16  ? 36.617  -5.354  46.070 1.00 24.14 ? 16  GLY B C   1
+ATOM   1191 O  O   . GLY B 2 16  ? 37.530  -5.584  46.969 1.00 24.08 ? 16  GLY B O   1
+ATOM   1192 N  N   . LYS B 2 17  ? 36.637  -4.322  45.404 1.00 16.20 ? 17  LYS B N   1
+ATOM   1193 C  CA  . LYS B 2 17  ? 37.615  -3.342  45.409 1.00 17.17 ? 17  LYS B CA  1
+ATOM   1194 C  C   . LYS B 2 17  ? 37.215  -2.258  46.175 1.00 17.84 ? 17  LYS B C   1
+ATOM   1195 O  O   . LYS B 2 17  ? 38.137  -1.233  46.497 1.00 23.03 ? 17  LYS B O   1
+ATOM   1196 C  CB  . LYS B 2 17  ? 37.958  -2.612  44.129 1.00 27.63 ? 17  LYS B CB  1
+ATOM   1197 C  CG  . LYS B 2 17  ? 38.327  -3.900  43.129 1.00 26.84 ? 17  LYS B CG  1
+ATOM   1198 C  CD  . LYS B 2 17  ? 38.750  -3.495  41.930 1.00 36.92 ? 17  LYS B CD  1
+ATOM   1199 C  CE  . LYS B 2 17  ? 39.022  -4.655  40.729 1.00 48.09 ? 17  LYS B CE  1
+ATOM   1200 N  NZ  . LYS B 2 17  ? 39.714  -3.537  39.951 1.00 51.60 ? 17  LYS B NZ  1
+ATOM   1201 N  N   . VAL B 2 18  ? 36.179  -2.026  46.917 1.00 19.79 ? 18  VAL B N   1
+ATOM   1202 C  CA  . VAL B 2 18  ? 35.593  -0.920  47.607 1.00 15.59 ? 18  VAL B CA  1
+ATOM   1203 C  C   . VAL B 2 18  ? 36.055  -0.982  49.098 1.00 24.20 ? 18  VAL B C   1
+ATOM   1204 O  O   . VAL B 2 18  ? 35.902  -1.947  49.847 1.00 22.49 ? 18  VAL B O   1
+ATOM   1205 C  CB  . VAL B 2 18  ? 34.087  -1.068  47.678 1.00 13.43 ? 18  VAL B CB  1
+ATOM   1206 C  CG1 . VAL B 2 18  ? 33.594  -0.078  48.591 1.00 20.38 ? 18  VAL B CG1 1
+ATOM   1207 C  CG2 . VAL B 2 18  ? 33.857  -0.367  46.132 1.00 25.54 ? 18  VAL B CG2 1
+ATOM   1208 N  N   . ASN B 2 19  ? 36.559  0.125   49.695 1.00 20.52 ? 19  ASN B N   1
+ATOM   1209 C  CA  . ASN B 2 19  ? 36.789  0.138   51.218 1.00 15.58 ? 19  ASN B CA  1
+ATOM   1210 C  C   . ASN B 2 19  ? 35.410  0.735   51.766 1.00 13.56 ? 19  ASN B C   1
+ATOM   1211 O  O   . ASN B 2 19  ? 35.137  1.986   51.540 1.00 14.77 ? 19  ASN B O   1
+ATOM   1212 C  CB  . ASN B 2 19  ? 37.893  1.288   51.572 1.00 26.08 ? 19  ASN B CB  1
+ATOM   1213 C  CG  . ASN B 2 19  ? 37.831  1.586   53.047 1.00 29.11 ? 19  ASN B CG  1
+ATOM   1214 O  OD1 . ASN B 2 19  ? 37.206  1.253   53.841 1.00 27.77 ? 19  ASN B OD1 1
+ATOM   1215 N  ND2 . ASN B 2 19  ? 39.275  1.902   53.239 1.00 33.88 ? 19  ASN B ND2 1
+ATOM   1216 N  N   . VAL B 2 20  ? 34.753  -0.142  52.343 1.00 18.83 ? 20  VAL B N   1
+ATOM   1217 C  CA  . VAL B 2 20  ? 33.259  0.118   52.703 1.00 19.05 ? 20  VAL B CA  1
+ATOM   1218 C  C   . VAL B 2 20  ? 33.227  1.099   53.561 1.00 20.02 ? 20  VAL B C   1
+ATOM   1219 O  O   . VAL B 2 20  ? 32.447  2.243   53.553 1.00 17.50 ? 20  VAL B O   1
+ATOM   1220 C  CB  . VAL B 2 20  ? 32.666  -1.256  53.173 1.00 25.16 ? 20  VAL B CB  1
+ATOM   1221 C  CG1 . VAL B 2 20  ? 31.255  -0.837  53.554 1.00 29.32 ? 20  VAL B CG1 1
+ATOM   1222 C  CG2 . VAL B 2 20  ? 32.505  -2.176  51.988 1.00 21.26 ? 20  VAL B CG2 1
+ATOM   1223 N  N   . ASP B 2 21  ? 34.050  1.489   54.502 1.00 19.64 ? 21  ASP B N   1
+ATOM   1224 C  CA  . ASP B 2 21  ? 34.001  2.521   55.583 1.00 20.67 ? 21  ASP B CA  1
+ATOM   1225 C  C   . ASP B 2 21  ? 34.452  3.735   54.924 1.00 18.97 ? 21  ASP B C   1
+ATOM   1226 O  O   . ASP B 2 21  ? 33.658  4.760   55.107 1.00 21.29 ? 21  ASP B O   1
+ATOM   1227 C  CB  . ASP B 2 21  ? 35.051  2.151   56.566 1.00 34.10 ? 21  ASP B CB  1
+ATOM   1228 C  CG  . ASP B 2 21  ? 34.623  0.846   57.786 1.00 53.28 ? 21  ASP B CG  1
+ATOM   1229 O  OD1 . ASP B 2 21  ? 33.411  0.788   57.706 1.00 40.86 ? 21  ASP B OD1 1
+ATOM   1230 O  OD2 . ASP B 2 21  ? 35.575  1.132   58.854 1.00 50.69 ? 21  ASP B OD2 1
+ATOM   1231 N  N   . GLU B 2 22  ? 35.321  3.783   53.983 1.00 17.77 ? 22  GLU B N   1
+ATOM   1232 C  CA  . GLU B 2 22  ? 35.793  5.201   53.370 1.00 21.32 ? 22  GLU B CA  1
+ATOM   1233 C  C   . GLU B 2 22  ? 34.589  5.722   52.414 1.00 17.53 ? 22  GLU B C   1
+ATOM   1234 O  O   . GLU B 2 22  ? 34.195  6.805   52.511 1.00 21.51 ? 22  GLU B O   1
+ATOM   1235 C  CB  . GLU B 2 22  ? 36.981  4.797   52.589 1.00 24.38 ? 22  GLU B CB  1
+ATOM   1236 C  CG  . GLU B 2 22  ? 37.299  5.809   51.812 1.00 38.60 ? 22  GLU B CG  1
+ATOM   1237 C  CD  . GLU B 2 22  ? 38.280  6.403   50.355 1.00 75.75 ? 22  GLU B CD  1
+ATOM   1238 O  OE1 . GLU B 2 22  ? 38.370  4.765   49.700 1.00 53.89 ? 22  GLU B OE1 1
+ATOM   1239 O  OE2 . GLU B 2 22  ? 39.831  5.356   51.346 1.00 65.14 ? 22  GLU B OE2 1
+ATOM   1240 N  N   . VAL B 2 23  ? 34.196  4.700   51.552 1.00 19.15 ? 23  VAL B N   1
+ATOM   1241 C  CA  . VAL B 2 23  ? 33.129  5.010   50.536 1.00 16.52 ? 23  VAL B CA  1
+ATOM   1242 C  C   . VAL B 2 23  ? 31.770  5.361   51.431 1.00 19.25 ? 23  VAL B C   1
+ATOM   1243 O  O   . VAL B 2 23  ? 30.985  6.303   50.887 1.00 16.10 ? 23  VAL B O   1
+ATOM   1244 C  CB  . VAL B 2 23  ? 32.876  3.855   49.527 1.00 21.83 ? 23  VAL B CB  1
+ATOM   1245 C  CG1 . VAL B 2 23  ? 31.629  4.093   48.860 1.00 26.98 ? 23  VAL B CG1 1
+ATOM   1246 C  CG2 . VAL B 2 23  ? 34.272  3.980   48.837 1.00 24.14 ? 23  VAL B CG2 1
+ATOM   1247 N  N   . GLY B 2 24  ? 31.547  4.709   52.448 1.00 11.83 ? 24  GLY B N   1
+ATOM   1248 C  CA  . GLY B 2 24  ? 30.456  5.040   53.221 1.00 15.96 ? 24  GLY B CA  1
+ATOM   1249 C  C   . GLY B 2 24  ? 30.324  6.411   53.808 1.00 15.32 ? 24  GLY B C   1
+ATOM   1250 O  O   . GLY B 2 24  ? 29.443  7.250   53.740 1.00 13.59 ? 24  GLY B O   1
+ATOM   1251 N  N   . GLY B 2 25  ? 31.404  6.844   54.406 1.00 19.52 ? 25  GLY B N   1
+ATOM   1252 C  CA  . GLY B 2 25  ? 31.752  8.157   54.855 1.00 15.79 ? 25  GLY B CA  1
+ATOM   1253 C  C   . GLY B 2 25  ? 31.577  9.245   53.717 1.00 12.82 ? 25  GLY B C   1
+ATOM   1254 O  O   . GLY B 2 25  ? 31.023  10.283  53.890 1.00 18.05 ? 25  GLY B O   1
+ATOM   1255 N  N   . GLU B 2 26  ? 32.153  8.944   52.627 1.00 12.16 ? 26  GLU B N   1
+ATOM   1256 C  CA  . GLU B 2 26  ? 32.201  9.859   51.429 1.00 11.32 ? 26  GLU B CA  1
+ATOM   1257 C  C   . GLU B 2 26  ? 30.652  10.015  50.962 1.00 13.79 ? 26  GLU B C   1
+ATOM   1258 O  O   . GLU B 2 26  ? 30.385  11.219  50.649 1.00 14.59 ? 26  GLU B O   1
+ATOM   1259 C  CB  . GLU B 2 26  ? 33.076  9.362   50.445 1.00 13.18 ? 26  GLU B CB  1
+ATOM   1260 C  CG  . GLU B 2 26  ? 33.694  10.657  49.486 1.00 29.90 ? 26  GLU B CG  1
+ATOM   1261 C  CD  . GLU B 2 26  ? 34.351  11.713  48.885 1.00 51.34 ? 26  GLU B CD  1
+ATOM   1262 O  OE1 . GLU B 2 26  ? 34.229  10.380  46.396 1.00 54.93 ? 26  GLU B OE1 1
+ATOM   1263 O  OE2 . GLU B 2 26  ? 34.999  9.374   48.820 1.00 37.93 ? 26  GLU B OE2 1
+ATOM   1264 N  N   . ALA B 2 27  ? 30.077  8.909   50.820 1.00 13.14 ? 27  ALA B N   1
+ATOM   1265 C  CA  . ALA B 2 27  ? 28.738  9.136   50.184 1.00 9.05  ? 27  ALA B CA  1
+ATOM   1266 C  C   . ALA B 2 27  ? 27.731  9.816   51.071 1.00 10.83 ? 27  ALA B C   1
+ATOM   1267 O  O   . ALA B 2 27  ? 26.877  10.576  50.701 1.00 11.12 ? 27  ALA B O   1
+ATOM   1268 C  CB  . ALA B 2 27  ? 28.284  7.747   49.981 1.00 14.07 ? 27  ALA B CB  1
+ATOM   1269 N  N   . LEU B 2 28  ? 27.660  9.478   52.412 1.00 11.19 ? 28  LEU B N   1
+ATOM   1270 C  CA  . LEU B 2 28  ? 27.003  10.113  53.451 1.00 14.47 ? 28  LEU B CA  1
+ATOM   1271 C  C   . LEU B 2 28  ? 27.149  11.493  53.423 1.00 12.13 ? 28  LEU B C   1
+ATOM   1272 O  O   . LEU B 2 28  ? 26.371  12.453  53.501 1.00 12.32 ? 28  LEU B O   1
+ATOM   1273 C  CB  . LEU B 2 28  ? 26.755  9.380   54.731 1.00 9.21  ? 28  LEU B CB  1
+ATOM   1274 C  CG  . LEU B 2 28  ? 25.416  10.158  55.511 1.00 20.67 ? 28  LEU B CG  1
+ATOM   1275 C  CD1 . LEU B 2 28  ? 24.240  9.610   55.014 1.00 17.60 ? 28  LEU B CD1 1
+ATOM   1276 C  CD2 . LEU B 2 28  ? 25.816  9.463   56.759 1.00 34.99 ? 28  LEU B CD2 1
+ATOM   1277 N  N   . GLY B 2 29  ? 28.511  11.899  53.530 1.00 10.00 ? 29  GLY B N   1
+ATOM   1278 C  CA  . GLY B 2 29  ? 28.799  13.234  53.611 1.00 15.27 ? 29  GLY B CA  1
+ATOM   1279 C  C   . GLY B 2 29  ? 28.443  14.055  52.306 1.00 10.88 ? 29  GLY B C   1
+ATOM   1280 O  O   . GLY B 2 29  ? 27.873  15.137  52.427 1.00 14.42 ? 29  GLY B O   1
+ATOM   1281 N  N   . ARG B 2 30  ? 28.639  13.435  51.164 1.00 11.39 ? 30  ARG B N   1
+ATOM   1282 C  CA  . ARG B 2 30  ? 28.338  14.277  50.006 1.00 14.49 ? 30  ARG B CA  1
+ATOM   1283 C  C   . ARG B 2 30  ? 26.690  14.296  49.889 1.00 10.79 ? 30  ARG B C   1
+ATOM   1284 O  O   . ARG B 2 30  ? 26.308  15.377  49.394 1.00 13.81 ? 30  ARG B O   1
+ATOM   1285 C  CB  . ARG B 2 30  ? 28.901  13.526  48.744 1.00 19.88 ? 30  ARG B CB  1
+ATOM   1286 C  CG  . ARG B 2 30  ? 30.349  13.968  48.318 1.00 16.11 ? 30  ARG B CG  1
+ATOM   1287 C  CD  . ARG B 2 30  ? 30.710  13.159  47.119 1.00 14.71 ? 30  ARG B CD  1
+ATOM   1288 N  NE  . ARG B 2 30  ? 32.141  13.197  46.967 1.00 21.05 ? 30  ARG B NE  1
+ATOM   1289 C  CZ  . ARG B 2 30  ? 32.889  13.884  46.230 1.00 18.56 ? 30  ARG B CZ  1
+ATOM   1290 N  NH1 . ARG B 2 30  ? 32.234  14.727  45.337 1.00 19.13 ? 30  ARG B NH1 1
+ATOM   1291 N  NH2 . ARG B 2 30  ? 34.158  14.074  46.112 1.00 19.91 ? 30  ARG B NH2 1
+ATOM   1292 N  N   . LEU B 2 31  ? 25.987  13.300  50.388 1.00 12.04 ? 31  LEU B N   1
+ATOM   1293 C  CA  . LEU B 2 31  ? 24.600  13.446  50.509 1.00 10.54 ? 31  LEU B CA  1
+ATOM   1294 C  C   . LEU B 2 31  ? 24.360  14.737  51.155 1.00 13.93 ? 31  LEU B C   1
+ATOM   1295 O  O   . LEU B 2 31  ? 23.435  15.571  50.831 1.00 14.67 ? 31  LEU B O   1
+ATOM   1296 C  CB  . LEU B 2 31  ? 23.868  12.237  51.013 1.00 12.99 ? 31  LEU B CB  1
+ATOM   1297 C  CG  . LEU B 2 31  ? 22.362  12.369  51.327 1.00 10.97 ? 31  LEU B CG  1
+ATOM   1298 C  CD1 . LEU B 2 31  ? 21.826  12.312  49.933 1.00 19.46 ? 31  LEU B CD1 1
+ATOM   1299 C  CD2 . LEU B 2 31  ? 21.879  11.343  52.340 1.00 13.98 ? 31  LEU B CD2 1
+ATOM   1300 N  N   . LEU B 2 32  ? 24.922  14.962  52.322 1.00 10.13 ? 32  LEU B N   1
+ATOM   1301 C  CA  . LEU B 2 32  ? 24.470  15.949  53.149 1.00 11.52 ? 32  LEU B CA  1
+ATOM   1302 C  C   . LEU B 2 32  ? 24.933  17.315  52.659 1.00 12.11 ? 32  LEU B C   1
+ATOM   1303 O  O   . LEU B 2 32  ? 24.443  18.456  52.983 1.00 15.31 ? 32  LEU B O   1
+ATOM   1304 C  CB  . LEU B 2 32  ? 25.121  15.866  54.637 1.00 11.75 ? 32  LEU B CB  1
+ATOM   1305 C  CG  . LEU B 2 32  ? 24.360  14.943  55.432 1.00 16.68 ? 32  LEU B CG  1
+ATOM   1306 C  CD1 . LEU B 2 32  ? 23.493  14.045  55.244 1.00 22.26 ? 32  LEU B CD1 1
+ATOM   1307 C  CD2 . LEU B 2 32  ? 25.146  14.592  56.667 1.00 28.90 ? 32  LEU B CD2 1
+ATOM   1308 N  N   . VAL B 2 33  ? 26.012  17.361  51.869 1.00 10.32 ? 33  VAL B N   1
+ATOM   1309 C  CA  . VAL B 2 33  ? 26.547  18.516  51.251 1.00 11.98 ? 33  VAL B CA  1
+ATOM   1310 C  C   . VAL B 2 33  ? 25.600  18.923  49.944 1.00 12.10 ? 33  VAL B C   1
+ATOM   1311 O  O   . VAL B 2 33  ? 25.430  20.179  49.799 1.00 13.28 ? 33  VAL B O   1
+ATOM   1312 C  CB  . VAL B 2 33  ? 28.032  18.376  50.810 1.00 14.87 ? 33  VAL B CB  1
+ATOM   1313 C  CG1 . VAL B 2 33  ? 28.558  19.530  50.033 1.00 11.54 ? 33  VAL B CG1 1
+ATOM   1314 C  CG2 . VAL B 2 33  ? 28.713  18.354  52.037 1.00 16.57 ? 33  VAL B CG2 1
+ATOM   1315 N  N   . VAL B 2 34  ? 25.514  17.948  49.127 1.00 13.66 ? 34  VAL B N   1
+ATOM   1316 C  CA  . VAL B 2 34  ? 24.831  18.380  47.752 1.00 9.59  ? 34  VAL B CA  1
+ATOM   1317 C  C   . VAL B 2 34  ? 23.288  18.584  47.955 1.00 8.72  ? 34  VAL B C   1
+ATOM   1318 O  O   . VAL B 2 34  ? 22.847  19.475  47.304 1.00 9.42  ? 34  VAL B O   1
+ATOM   1319 C  CB  . VAL B 2 34  ? 25.122  17.183  46.892 1.00 9.09  ? 34  VAL B CB  1
+ATOM   1320 C  CG1 . VAL B 2 34  ? 24.476  17.449  45.540 1.00 9.82  ? 34  VAL B CG1 1
+ATOM   1321 C  CG2 . VAL B 2 34  ? 26.505  17.045  46.733 1.00 17.00 ? 34  VAL B CG2 1
+ATOM   1322 N  N   . TYR B 2 35  ? 22.718  17.864  48.951 1.00 10.80 ? 35  TYR B N   1
+ATOM   1323 C  CA  . TYR B 2 35  ? 21.254  17.977  49.191 1.00 13.73 ? 35  TYR B CA  1
+ATOM   1324 C  C   . TYR B 2 35  ? 21.038  18.380  50.736 1.00 14.87 ? 35  TYR B C   1
+ATOM   1325 O  O   . TYR B 2 35  ? 20.720  17.388  51.398 1.00 16.30 ? 35  TYR B O   1
+ATOM   1326 C  CB  . TYR B 2 35  ? 20.565  16.644  48.903 1.00 14.97 ? 35  TYR B CB  1
+ATOM   1327 C  CG  . TYR B 2 35  ? 20.853  16.234  47.500 1.00 16.57 ? 35  TYR B CG  1
+ATOM   1328 C  CD1 . TYR B 2 35  ? 20.362  16.953  46.315 1.00 17.11 ? 35  TYR B CD1 1
+ATOM   1329 C  CD2 . TYR B 2 35  ? 21.567  15.117  47.080 1.00 21.02 ? 35  TYR B CD2 1
+ATOM   1330 C  CE1 . TYR B 2 35  ? 20.636  16.509  45.009 1.00 16.53 ? 35  TYR B CE1 1
+ATOM   1331 C  CE2 . TYR B 2 35  ? 21.970  14.951  45.868 1.00 21.07 ? 35  TYR B CE2 1
+ATOM   1332 C  CZ  . TYR B 2 35  ? 21.427  15.438  44.815 1.00 16.91 ? 35  TYR B CZ  1
+ATOM   1333 O  OH  . TYR B 2 35  ? 21.949  15.134  43.472 1.00 21.07 ? 35  TYR B OH  1
+ATOM   1334 N  N   . PRO B 2 36  ? 21.329  19.525  51.046 1.00 18.32 ? 36  PRO B N   1
+ATOM   1335 C  CA  . PRO B 2 36  ? 21.434  19.922  52.430 1.00 15.72 ? 36  PRO B CA  1
+ATOM   1336 C  C   . PRO B 2 36  ? 20.140  19.751  53.145 1.00 27.07 ? 36  PRO B C   1
+ATOM   1337 O  O   . PRO B 2 36  ? 20.209  19.602  54.451 1.00 15.67 ? 36  PRO B O   1
+ATOM   1338 C  CB  . PRO B 2 36  ? 21.826  21.374  52.544 1.00 16.26 ? 36  PRO B CB  1
+ATOM   1339 C  CG  . PRO B 2 36  ? 21.899  21.925  51.270 1.00 21.27 ? 36  PRO B CG  1
+ATOM   1340 C  CD  . PRO B 2 36  ? 21.649  20.731  50.382 1.00 25.93 ? 36  PRO B CD  1
+ATOM   1341 N  N   . TRP B 2 37  ? 18.969  19.536  52.679 1.00 14.10 ? 37  TRP B N   1
+ATOM   1342 C  CA  . TRP B 2 37  ? 17.867  19.291  53.542 1.00 12.74 ? 37  TRP B CA  1
+ATOM   1343 C  C   . TRP B 2 37  ? 17.822  17.908  54.096 1.00 15.06 ? 37  TRP B C   1
+ATOM   1344 O  O   . TRP B 2 37  ? 17.119  17.588  55.067 1.00 15.27 ? 37  TRP B O   1
+ATOM   1345 C  CB  . TRP B 2 37  ? 16.667  19.463  52.495 1.00 19.41 ? 37  TRP B CB  1
+ATOM   1346 C  CG  . TRP B 2 37  ? 16.577  18.713  51.318 1.00 14.79 ? 37  TRP B CG  1
+ATOM   1347 C  CD1 . TRP B 2 37  ? 15.879  17.451  50.989 1.00 18.82 ? 37  TRP B CD1 1
+ATOM   1348 C  CD2 . TRP B 2 37  ? 17.073  19.131  49.973 1.00 18.23 ? 37  TRP B CD2 1
+ATOM   1349 N  NE1 . TRP B 2 37  ? 16.146  17.215  49.743 1.00 23.72 ? 37  TRP B NE1 1
+ATOM   1350 C  CE2 . TRP B 2 37  ? 16.759  18.033  49.018 1.00 22.13 ? 37  TRP B CE2 1
+ATOM   1351 C  CE3 . TRP B 2 37  ? 17.915  20.227  49.510 1.00 21.52 ? 37  TRP B CE3 1
+ATOM   1352 C  CZ2 . TRP B 2 37  ? 17.084  18.014  47.655 1.00 18.19 ? 37  TRP B CZ2 1
+ATOM   1353 C  CZ3 . TRP B 2 37  ? 18.071  20.166  48.223 1.00 31.71 ? 37  TRP B CZ3 1
+ATOM   1354 C  CH2 . TRP B 2 37  ? 17.755  19.199  47.441 1.00 14.12 ? 37  TRP B CH2 1
+ATOM   1355 N  N   . THR B 2 38  ? 18.738  16.962  53.716 1.00 14.17 ? 38  THR B N   1
+ATOM   1356 C  CA  . THR B 2 38  ? 18.981  15.633  54.143 1.00 13.46 ? 38  THR B CA  1
+ATOM   1357 C  C   . THR B 2 38  ? 19.386  15.759  55.653 1.00 16.65 ? 38  THR B C   1
+ATOM   1358 O  O   . THR B 2 38  ? 19.576  14.733  56.326 1.00 18.86 ? 38  THR B O   1
+ATOM   1359 C  CB  . THR B 2 38  ? 19.779  14.622  53.398 1.00 12.74 ? 38  THR B CB  1
+ATOM   1360 O  OG1 . THR B 2 38  ? 20.939  15.287  53.154 1.00 14.09 ? 38  THR B OG1 1
+ATOM   1361 C  CG2 . THR B 2 38  ? 19.099  14.621  52.024 1.00 15.42 ? 38  THR B CG2 1
+ATOM   1362 N  N   . GLN B 2 39  ? 20.027  16.851  55.924 1.00 19.91 ? 39  GLN B N   1
+ATOM   1363 C  CA  . GLN B 2 39  ? 20.646  17.349  57.305 1.00 23.22 ? 39  GLN B CA  1
+ATOM   1364 C  C   . GLN B 2 39  ? 19.621  17.236  58.371 1.00 19.19 ? 39  GLN B C   1
+ATOM   1365 O  O   . GLN B 2 39  ? 20.027  17.060  59.501 1.00 19.29 ? 39  GLN B O   1
+ATOM   1366 C  CB  . GLN B 2 39  ? 21.470  18.553  57.299 1.00 24.35 ? 39  GLN B CB  1
+ATOM   1367 C  CG  . GLN B 2 39  ? 22.567  18.566  56.447 1.00 25.27 ? 39  GLN B CG  1
+ATOM   1368 C  CD  . GLN B 2 39  ? 23.378  19.959  56.435 1.00 24.35 ? 39  GLN B CD  1
+ATOM   1369 O  OE1 . GLN B 2 39  ? 23.038  20.668  57.411 1.00 26.75 ? 39  GLN B OE1 1
+ATOM   1370 N  NE2 . GLN B 2 39  ? 24.224  20.109  55.396 1.00 30.18 ? 39  GLN B NE2 1
+ATOM   1371 N  N   . ARG B 2 40  ? 18.331  17.279  57.998 1.00 20.02 ? 40  ARG B N   1
+ATOM   1372 C  CA  . ARG B 2 40  ? 17.214  17.313  58.995 1.00 21.80 ? 40  ARG B CA  1
+ATOM   1373 C  C   . ARG B 2 40  ? 17.379  15.955  59.913 1.00 29.36 ? 40  ARG B C   1
+ATOM   1374 O  O   . ARG B 2 40  ? 16.869  16.306  61.046 1.00 24.42 ? 40  ARG B O   1
+ATOM   1375 C  CB  . ARG B 2 40  ? 15.907  17.291  58.206 1.00 16.52 ? 40  ARG B CB  1
+ATOM   1376 C  CG  . ARG B 2 40  ? 15.427  16.028  57.806 1.00 20.34 ? 40  ARG B CG  1
+ATOM   1377 C  CD  . ARG B 2 40  ? 14.140  16.233  56.771 1.00 25.31 ? 40  ARG B CD  1
+ATOM   1378 N  NE  . ARG B 2 40  ? 13.162  16.778  57.306 1.00 29.70 ? 40  ARG B NE  1
+ATOM   1379 C  CZ  . ARG B 2 40  ? 12.136  16.180  58.270 1.00 34.46 ? 40  ARG B CZ  1
+ATOM   1380 N  NH1 . ARG B 2 40  ? 12.232  15.027  58.266 1.00 31.34 ? 40  ARG B NH1 1
+ATOM   1381 N  NH2 . ARG B 2 40  ? 11.138  17.359  58.475 1.00 39.12 ? 40  ARG B NH2 1
+ATOM   1382 N  N   . PHE B 2 41  ? 17.856  14.940  59.785 1.00 19.21 ? 41  PHE B N   1
+ATOM   1383 C  CA  . PHE B 2 41  ? 17.694  13.748  60.596 1.00 16.53 ? 41  PHE B CA  1
+ATOM   1384 C  C   . PHE B 2 41  ? 19.084  13.745  61.697 1.00 21.34 ? 41  PHE B C   1
+ATOM   1385 O  O   . PHE B 2 41  ? 18.953  12.892  62.333 1.00 23.45 ? 41  PHE B O   1
+ATOM   1386 C  CB  . PHE B 2 41  ? 17.988  12.518  59.599 1.00 10.39 ? 41  PHE B CB  1
+ATOM   1387 C  CG  . PHE B 2 41  ? 16.790  12.444  58.756 1.00 13.84 ? 41  PHE B CG  1
+ATOM   1388 C  CD1 . PHE B 2 41  ? 16.986  12.830  57.379 1.00 17.38 ? 41  PHE B CD1 1
+ATOM   1389 C  CD2 . PHE B 2 41  ? 15.421  12.027  59.315 1.00 25.55 ? 41  PHE B CD2 1
+ATOM   1390 C  CE1 . PHE B 2 41  ? 15.846  12.656  56.562 1.00 15.72 ? 41  PHE B CE1 1
+ATOM   1391 C  CE2 . PHE B 2 41  ? 14.386  12.065  58.259 1.00 21.40 ? 41  PHE B CE2 1
+ATOM   1392 C  CZ  . PHE B 2 41  ? 14.690  12.439  56.948 1.00 13.46 ? 41  PHE B CZ  1
+ATOM   1393 N  N   . PHE B 2 42  ? 19.848  14.631  61.386 1.00 18.41 ? 42  PHE B N   1
+ATOM   1394 C  CA  . PHE B 2 42  ? 21.236  14.531  61.779 1.00 17.88 ? 42  PHE B CA  1
+ATOM   1395 C  C   . PHE B 2 42  ? 21.717  15.631  62.653 1.00 26.28 ? 42  PHE B C   1
+ATOM   1396 O  O   . PHE B 2 42  ? 22.822  15.904  62.949 1.00 30.16 ? 42  PHE B O   1
+ATOM   1397 C  CB  . PHE B 2 42  ? 22.287  14.343  60.677 1.00 16.57 ? 42  PHE B CB  1
+ATOM   1398 C  CG  . PHE B 2 42  ? 22.021  13.138  60.095 1.00 18.87 ? 42  PHE B CG  1
+ATOM   1399 C  CD1 . PHE B 2 42  ? 21.624  13.241  58.460 1.00 17.08 ? 42  PHE B CD1 1
+ATOM   1400 C  CD2 . PHE B 2 42  ? 22.107  11.811  60.357 1.00 17.75 ? 42  PHE B CD2 1
+ATOM   1401 C  CE1 . PHE B 2 42  ? 21.315  11.940  57.996 1.00 12.34 ? 42  PHE B CE1 1
+ATOM   1402 C  CE2 . PHE B 2 42  ? 21.715  10.734  59.718 1.00 16.32 ? 42  PHE B CE2 1
+ATOM   1403 C  CZ  . PHE B 2 42  ? 21.379  10.780  58.241 1.00 14.29 ? 42  PHE B CZ  1
+ATOM   1404 N  N   . GLU B 2 43  ? 20.861  16.294  63.207 1.00 32.94 ? 43  GLU B N   1
+ATOM   1405 C  CA  . GLU B 2 43  ? 21.428  17.547  63.954 1.00 42.17 ? 43  GLU B CA  1
+ATOM   1406 C  C   . GLU B 2 43  ? 21.773  17.283  65.517 1.00 21.09 ? 43  GLU B C   1
+ATOM   1407 O  O   . GLU B 2 43  ? 22.764  17.627  66.097 1.00 37.55 ? 43  GLU B O   1
+ATOM   1408 C  CB  . GLU B 2 43  ? 20.271  18.048  63.993 1.00 73.91 ? 43  GLU B CB  1
+ATOM   1409 C  CG  . GLU B 2 43  ? 19.034  18.030  64.943 1.00 61.81 ? 43  GLU B CG  1
+ATOM   1410 C  CD  . GLU B 2 43  ? 17.534  19.892  64.537 1.00 78.77 ? 43  GLU B CD  1
+ATOM   1411 O  OE1 . GLU B 2 43  ? 18.099  20.391  64.148 1.00 63.33 ? 43  GLU B OE1 1
+ATOM   1412 O  OE2 . GLU B 2 43  ? 16.921  18.912  65.510 1.00 59.41 ? 43  GLU B OE2 1
+ATOM   1413 N  N   . SER B 2 44  ? 21.672  15.857  65.830 1.00 22.68 ? 44  SER B N   1
+ATOM   1414 C  CA  . SER B 2 44  ? 22.503  15.307  67.058 1.00 28.45 ? 44  SER B CA  1
+ATOM   1415 C  C   . SER B 2 44  ? 23.855  15.814  66.816 1.00 36.10 ? 44  SER B C   1
+ATOM   1416 O  O   . SER B 2 44  ? 24.793  14.805  67.412 1.00 25.24 ? 44  SER B O   1
+ATOM   1417 C  CB  . SER B 2 44  ? 22.000  14.024  67.279 1.00 27.61 ? 44  SER B CB  1
+ATOM   1418 O  OG  . SER B 2 44  ? 22.051  12.879  67.014 1.00 37.26 ? 44  SER B OG  1
+ATOM   1419 N  N   . PHE B 2 45  ? 24.467  15.260  65.502 1.00 28.36 ? 45  PHE B N   1
+ATOM   1420 C  CA  . PHE B 2 45  ? 25.770  14.989  64.990 1.00 25.47 ? 45  PHE B CA  1
+ATOM   1421 C  C   . PHE B 2 45  ? 26.527  16.169  65.164 1.00 26.28 ? 45  PHE B C   1
+ATOM   1422 O  O   . PHE B 2 45  ? 27.753  16.023  64.770 1.00 31.39 ? 45  PHE B O   1
+ATOM   1423 C  CB  . PHE B 2 45  ? 25.572  14.491  63.473 1.00 22.10 ? 45  PHE B CB  1
+ATOM   1424 C  CG  . PHE B 2 45  ? 25.225  12.900  63.251 1.00 18.85 ? 45  PHE B CG  1
+ATOM   1425 C  CD1 . PHE B 2 45  ? 25.493  12.509  61.991 1.00 29.27 ? 45  PHE B CD1 1
+ATOM   1426 C  CD2 . PHE B 2 45  ? 24.577  12.234  63.730 1.00 31.57 ? 45  PHE B CD2 1
+ATOM   1427 C  CE1 . PHE B 2 45  ? 24.975  10.984  61.785 1.00 29.02 ? 45  PHE B CE1 1
+ATOM   1428 C  CE2 . PHE B 2 45  ? 24.034  10.950  63.873 1.00 30.34 ? 45  PHE B CE2 1
+ATOM   1429 C  CZ  . PHE B 2 45  ? 24.465  10.568  62.553 1.00 36.33 ? 45  PHE B CZ  1
+ATOM   1430 N  N   . GLY B 2 46  ? 26.313  17.393  65.510 1.00 39.28 ? 46  GLY B N   1
+ATOM   1431 C  CA  . GLY B 2 46  ? 27.246  18.341  65.733 1.00 46.90 ? 46  GLY B CA  1
+ATOM   1432 C  C   . GLY B 2 46  ? 27.536  19.388  64.456 1.00 45.06 ? 46  GLY B C   1
+ATOM   1433 O  O   . GLY B 2 46  ? 26.302  19.697  63.787 1.00 36.42 ? 46  GLY B O   1
+ATOM   1434 N  N   . ASP B 2 47  ? 28.571  19.603  64.265 1.00 38.00 ? 47  ASP B N   1
+ATOM   1435 C  CA  . ASP B 2 47  ? 28.744  20.945  63.285 1.00 38.15 ? 47  ASP B CA  1
+ATOM   1436 C  C   . ASP B 2 47  ? 28.923  20.320  61.664 1.00 25.86 ? 47  ASP B C   1
+ATOM   1437 O  O   . ASP B 2 47  ? 29.507  19.212  61.459 1.00 25.46 ? 47  ASP B O   1
+ATOM   1438 C  CB  . ASP B 2 47  ? 30.305  21.062  63.500 1.00 44.07 ? 47  ASP B CB  1
+ATOM   1439 C  CG  . ASP B 2 47  ? 30.598  22.356  63.064 1.00 52.06 ? 47  ASP B CG  1
+ATOM   1440 O  OD1 . ASP B 2 47  ? 31.810  22.713  62.656 1.00 44.54 ? 47  ASP B OD1 1
+ATOM   1441 O  OD2 . ASP B 2 47  ? 29.498  23.189  61.934 1.00 35.33 ? 47  ASP B OD2 1
+ATOM   1442 N  N   . LEU B 2 48  ? 27.616  20.817  61.159 1.00 25.27 ? 48  LEU B N   1
+ATOM   1443 C  CA  . LEU B 2 48  ? 27.195  20.516  59.658 1.00 28.75 ? 48  LEU B CA  1
+ATOM   1444 C  C   . LEU B 2 48  ? 27.359  21.868  58.837 1.00 27.19 ? 48  LEU B C   1
+ATOM   1445 O  O   . LEU B 2 48  ? 26.783  21.885  57.854 1.00 27.20 ? 48  LEU B O   1
+ATOM   1446 C  CB  . LEU B 2 48  ? 26.061  19.712  59.685 1.00 23.96 ? 48  LEU B CB  1
+ATOM   1447 C  CG  . LEU B 2 48  ? 26.147  18.366  60.193 1.00 24.35 ? 48  LEU B CG  1
+ATOM   1448 C  CD1 . LEU B 2 48  ? 24.674  17.669  60.176 1.00 34.74 ? 48  LEU B CD1 1
+ATOM   1449 C  CD2 . LEU B 2 48  ? 27.014  17.420  59.898 1.00 34.58 ? 48  LEU B CD2 1
+ATOM   1450 N  N   . SER B 2 49  ? 28.166  22.710  59.317 1.00 41.94 ? 49  SER B N   1
+ATOM   1451 C  CA  . SER B 2 49  ? 27.653  24.095  58.528 1.00 46.28 ? 49  SER B CA  1
+ATOM   1452 C  C   . SER B 2 49  ? 28.836  24.315  58.009 1.00 38.86 ? 49  SER B C   1
+ATOM   1453 O  O   . SER B 2 49  ? 28.145  25.309  56.692 1.00 41.94 ? 49  SER B O   1
+ATOM   1454 C  CB  . SER B 2 49  ? 28.211  25.226  59.859 1.00 37.98 ? 49  SER B CB  1
+ATOM   1455 O  OG  . SER B 2 49  ? 29.864  24.821  59.990 1.00 37.71 ? 49  SER B OG  1
+ATOM   1456 N  N   . THR B 2 50  ? 29.633  23.753  57.118 1.00 28.29 ? 50  THR B N   1
+ATOM   1457 C  CA  . THR B 2 50  ? 30.293  23.646  56.020 1.00 30.77 ? 50  THR B CA  1
+ATOM   1458 C  C   . THR B 2 50  ? 30.692  22.309  55.262 1.00 28.12 ? 50  THR B C   1
+ATOM   1459 O  O   . THR B 2 50  ? 30.596  21.318  56.121 1.00 25.38 ? 50  THR B O   1
+ATOM   1460 C  CB  . THR B 2 50  ? 31.281  24.343  56.431 1.00 33.39 ? 50  THR B CB  1
+ATOM   1461 O  OG1 . THR B 2 50  ? 32.568  23.798  56.723 1.00 37.96 ? 50  THR B OG1 1
+ATOM   1462 C  CG2 . THR B 2 50  ? 31.581  26.014  56.850 1.00 29.64 ? 50  THR B CG2 1
+ATOM   1463 N  N   . PRO B 2 51  ? 31.235  22.383  54.039 1.00 28.96 ? 51  PRO B N   1
+ATOM   1464 C  CA  . PRO B 2 51  ? 31.363  21.112  53.427 1.00 22.25 ? 51  PRO B CA  1
+ATOM   1465 C  C   . PRO B 2 51  ? 32.464  20.383  54.092 1.00 19.80 ? 51  PRO B C   1
+ATOM   1466 O  O   . PRO B 2 51  ? 32.509  19.064  54.592 1.00 21.55 ? 51  PRO B O   1
+ATOM   1467 C  CB  . PRO B 2 51  ? 31.777  21.411  52.043 1.00 27.29 ? 51  PRO B CB  1
+ATOM   1468 C  CG  . PRO B 2 51  ? 30.901  22.636  51.765 1.00 23.54 ? 51  PRO B CG  1
+ATOM   1469 C  CD  . PRO B 2 51  ? 30.984  23.482  52.882 1.00 26.04 ? 51  PRO B CD  1
+ATOM   1470 N  N   . ASP B 2 52  ? 33.573  21.100  54.587 1.00 21.99 ? 52  ASP B N   1
+ATOM   1471 C  CA  . ASP B 2 52  ? 34.693  20.555  55.266 1.00 20.50 ? 52  ASP B CA  1
+ATOM   1472 C  C   . ASP B 2 52  ? 34.268  19.949  56.573 1.00 16.32 ? 52  ASP B C   1
+ATOM   1473 O  O   . ASP B 2 52  ? 34.691  18.896  57.123 1.00 25.55 ? 52  ASP B O   1
+ATOM   1474 C  CB  . ASP B 2 52  ? 35.752  21.612  55.477 1.00 32.17 ? 52  ASP B CB  1
+ATOM   1475 C  CG  . ASP B 2 52  ? 36.929  21.429  54.164 1.00 47.24 ? 52  ASP B CG  1
+ATOM   1476 O  OD1 . ASP B 2 52  ? 36.680  20.750  53.390 1.00 41.78 ? 52  ASP B OD1 1
+ATOM   1477 O  OD2 . ASP B 2 52  ? 36.916  22.731  53.687 1.00 62.08 ? 52  ASP B OD2 1
+ATOM   1478 N  N   . ALA B 2 53  ? 33.361  20.726  57.276 1.00 23.18 ? 53  ALA B N   1
+ATOM   1479 C  CA  . ALA B 2 53  ? 32.844  20.258  58.619 1.00 24.60 ? 53  ALA B CA  1
+ATOM   1480 C  C   . ALA B 2 53  ? 32.206  18.895  58.668 1.00 20.91 ? 53  ALA B C   1
+ATOM   1481 O  O   . ALA B 2 53  ? 32.090  17.908  59.278 1.00 20.19 ? 53  ALA B O   1
+ATOM   1482 C  CB  . ALA B 2 53  ? 32.049  21.204  59.196 1.00 23.45 ? 53  ALA B CB  1
+ATOM   1483 N  N   . VAL B 2 54  ? 31.308  18.796  57.491 1.00 19.02 ? 54  VAL B N   1
+ATOM   1484 C  CA  . VAL B 2 54  ? 30.564  17.620  57.179 1.00 17.30 ? 54  VAL B CA  1
+ATOM   1485 C  C   . VAL B 2 54  ? 31.369  16.629  56.892 1.00 15.03 ? 54  VAL B C   1
+ATOM   1486 O  O   . VAL B 2 54  ? 31.270  15.401  57.462 1.00 19.06 ? 54  VAL B O   1
+ATOM   1487 C  CB  . VAL B 2 54  ? 29.403  17.941  55.990 1.00 27.63 ? 54  VAL B CB  1
+ATOM   1488 C  CG1 . VAL B 2 54  ? 28.907  16.562  55.615 1.00 22.46 ? 54  VAL B CG1 1
+ATOM   1489 C  CG2 . VAL B 2 54  ? 28.538  19.064  56.220 1.00 27.27 ? 54  VAL B CG2 1
+ATOM   1490 N  N   . MET B 2 55  ? 32.357  16.743  55.982 1.00 21.73 ? 55  MET B N   1
+ATOM   1491 C  CA  . MET B 2 55  ? 33.054  15.609  55.540 1.00 17.86 ? 55  MET B CA  1
+ATOM   1492 C  C   . MET B 2 55  ? 33.996  15.072  56.627 1.00 32.16 ? 55  MET B C   1
+ATOM   1493 O  O   . MET B 2 55  ? 34.290  13.907  56.420 1.00 26.15 ? 55  MET B O   1
+ATOM   1494 C  CB  . MET B 2 55  ? 33.952  15.947  54.243 1.00 19.12 ? 55  MET B CB  1
+ATOM   1495 C  CG  . MET B 2 55  ? 33.141  16.382  53.020 1.00 18.10 ? 55  MET B CG  1
+ATOM   1496 S  SD  . MET B 2 55  ? 31.861  15.161  52.513 1.00 21.28 ? 55  MET B SD  1
+ATOM   1497 C  CE  . MET B 2 55  ? 32.682  13.865  51.996 1.00 20.66 ? 55  MET B CE  1
+ATOM   1498 N  N   . GLY B 2 56  ? 34.386  16.003  57.436 1.00 24.42 ? 56  GLY B N   1
+ATOM   1499 C  CA  . GLY B 2 56  ? 35.296  15.455  58.518 1.00 36.79 ? 56  GLY B CA  1
+ATOM   1500 C  C   . GLY B 2 56  ? 34.541  15.418  59.871 1.00 33.28 ? 56  GLY B C   1
+ATOM   1501 O  O   . GLY B 2 56  ? 35.077  14.753  60.847 1.00 24.94 ? 56  GLY B O   1
+ATOM   1502 N  N   . ASN B 2 57  ? 33.307  15.048  60.021 1.00 22.01 ? 57  ASN B N   1
+ATOM   1503 C  CA  . ASN B 2 57  ? 32.555  14.951  61.137 1.00 15.71 ? 57  ASN B CA  1
+ATOM   1504 C  C   . ASN B 2 57  ? 32.541  13.537  61.403 1.00 17.88 ? 57  ASN B C   1
+ATOM   1505 O  O   . ASN B 2 57  ? 32.081  12.554  60.633 1.00 18.04 ? 57  ASN B O   1
+ATOM   1506 C  CB  . ASN B 2 57  ? 31.187  15.397  61.070 1.00 21.80 ? 57  ASN B CB  1
+ATOM   1507 C  CG  . ASN B 2 57  ? 30.292  15.074  62.241 1.00 18.78 ? 57  ASN B CG  1
+ATOM   1508 O  OD1 . ASN B 2 57  ? 30.186  14.142  62.763 1.00 23.41 ? 57  ASN B OD1 1
+ATOM   1509 N  ND2 . ASN B 2 57  ? 29.822  16.185  62.680 1.00 26.53 ? 57  ASN B ND2 1
+ATOM   1510 N  N   . PRO B 2 58  ? 32.939  12.966  62.539 1.00 24.81 ? 58  PRO B N   1
+ATOM   1511 C  CA  . PRO B 2 58  ? 32.953  11.618  62.948 1.00 24.38 ? 58  PRO B CA  1
+ATOM   1512 C  C   . PRO B 2 58  ? 31.744  10.783  62.954 1.00 16.45 ? 58  PRO B C   1
+ATOM   1513 O  O   . PRO B 2 58  ? 31.842  9.571   62.749 1.00 22.03 ? 58  PRO B O   1
+ATOM   1514 C  CB  . PRO B 2 58  ? 33.878  11.716  64.309 1.00 41.00 ? 58  PRO B CB  1
+ATOM   1515 C  CG  . PRO B 2 58  ? 33.855  12.879  64.413 1.00 36.46 ? 58  PRO B CG  1
+ATOM   1516 C  CD  . PRO B 2 58  ? 33.593  14.084  63.761 1.00 41.75 ? 58  PRO B CD  1
+ATOM   1517 N  N   . LYS B 2 59  ? 30.690  11.607  63.326 1.00 16.03 ? 59  LYS B N   1
+ATOM   1518 C  CA  . LYS B 2 59  ? 29.316  10.910  63.478 1.00 22.04 ? 59  LYS B CA  1
+ATOM   1519 C  C   . LYS B 2 59  ? 28.703  10.687  62.045 1.00 13.98 ? 59  LYS B C   1
+ATOM   1520 O  O   . LYS B 2 59  ? 28.239  9.529   61.769 1.00 15.67 ? 59  LYS B O   1
+ATOM   1521 C  CB  . LYS B 2 59  ? 28.485  11.682  64.225 1.00 22.22 ? 59  LYS B CB  1
+ATOM   1522 C  CG  . LYS B 2 59  ? 28.634  11.389  65.718 1.00 45.70 ? 59  LYS B CG  1
+ATOM   1523 C  CD  . LYS B 2 59  ? 28.929  12.249  66.141 1.00 44.05 ? 59  LYS B CD  1
+ATOM   1524 C  CE  . LYS B 2 59  ? 29.074  11.269  68.286 1.00 71.22 ? 59  LYS B CE  1
+ATOM   1525 N  NZ  . LYS B 2 59  ? 28.349  13.036  68.475 1.00 61.54 ? 59  LYS B NZ  1
+ATOM   1526 N  N   . VAL B 2 60  ? 29.170  11.514  61.262 1.00 17.28 ? 60  VAL B N   1
+ATOM   1527 C  CA  . VAL B 2 60  ? 28.793  11.401  59.842 1.00 18.21 ? 60  VAL B CA  1
+ATOM   1528 C  C   . VAL B 2 60  ? 29.285  10.148  59.387 1.00 17.60 ? 60  VAL B C   1
+ATOM   1529 O  O   . VAL B 2 60  ? 28.947  9.166   58.616 1.00 19.11 ? 60  VAL B O   1
+ATOM   1530 C  CB  . VAL B 2 60  ? 28.859  12.595  58.944 1.00 19.15 ? 60  VAL B CB  1
+ATOM   1531 C  CG1 . VAL B 2 60  ? 29.001  12.193  57.505 1.00 20.44 ? 60  VAL B CG1 1
+ATOM   1532 C  CG2 . VAL B 2 60  ? 28.092  13.731  59.411 1.00 20.64 ? 60  VAL B CG2 1
+ATOM   1533 N  N   . LYS B 2 61  ? 30.720  10.149  59.394 1.00 16.19 ? 61  LYS B N   1
+ATOM   1534 C  CA  . LYS B 2 61  ? 31.437  8.994   58.922 1.00 15.00 ? 61  LYS B CA  1
+ATOM   1535 C  C   . LYS B 2 61  ? 31.123  7.619   59.620 1.00 17.90 ? 61  LYS B C   1
+ATOM   1536 O  O   . LYS B 2 61  ? 30.729  6.567   58.998 1.00 20.52 ? 61  LYS B O   1
+ATOM   1537 C  CB  . LYS B 2 61  ? 32.919  9.167   59.431 1.00 23.50 ? 61  LYS B CB  1
+ATOM   1538 C  CG  . LYS B 2 61  ? 33.482  10.037  58.754 1.00 34.21 ? 61  LYS B CG  1
+ATOM   1539 C  CD  . LYS B 2 61  ? 35.156  10.532  59.573 1.00 48.05 ? 61  LYS B CD  1
+ATOM   1540 C  CE  . LYS B 2 61  ? 35.886  10.897  58.086 1.00 65.12 ? 61  LYS B CE  1
+ATOM   1541 N  NZ  . LYS B 2 61  ? 37.309  11.433  58.945 1.00 66.26 ? 61  LYS B NZ  1
+ATOM   1542 N  N   . ALA B 2 62  ? 30.722  7.614   60.851 1.00 18.99 ? 62  ALA B N   1
+ATOM   1543 C  CA  . ALA B 2 62  ? 30.224  6.336   61.457 1.00 20.11 ? 62  ALA B CA  1
+ATOM   1544 C  C   . ALA B 2 62  ? 28.818  5.927   60.836 1.00 23.44 ? 62  ALA B C   1
+ATOM   1545 O  O   . ALA B 2 62  ? 28.572  4.833   60.810 1.00 21.26 ? 62  ALA B O   1
+ATOM   1546 C  CB  . ALA B 2 62  ? 30.032  6.664   62.964 1.00 28.90 ? 62  ALA B CB  1
+ATOM   1547 N  N   . HIS B 2 63  ? 28.015  7.012   60.880 1.00 20.40 ? 63  HIS B N   1
+ATOM   1548 C  CA  . HIS B 2 63  ? 26.729  6.650   60.193 1.00 18.39 ? 63  HIS B CA  1
+ATOM   1549 C  C   . HIS B 2 63  ? 26.889  6.129   58.666 1.00 14.88 ? 63  HIS B C   1
+ATOM   1550 O  O   . HIS B 2 63  ? 26.280  4.992   58.407 1.00 18.29 ? 63  HIS B O   1
+ATOM   1551 C  CB  . HIS B 2 63  ? 25.810  7.692   60.227 1.00 22.46 ? 63  HIS B CB  1
+ATOM   1552 C  CG  . HIS B 2 63  ? 24.387  7.524   60.034 1.00 25.19 ? 63  HIS B CG  1
+ATOM   1553 N  ND1 . HIS B 2 63  ? 23.737  6.196   60.755 1.00 24.68 ? 63  HIS B ND1 1
+ATOM   1554 C  CD2 . HIS B 2 63  ? 23.573  7.600   58.834 1.00 20.46 ? 63  HIS B CD2 1
+ATOM   1555 C  CE1 . HIS B 2 63  ? 22.354  6.140   60.009 1.00 21.48 ? 63  HIS B CE1 1
+ATOM   1556 N  NE2 . HIS B 2 63  ? 22.342  6.888   59.069 1.00 20.00 ? 63  HIS B NE2 1
+ATOM   1557 N  N   . GLY B 2 64  ? 27.810  6.672   58.105 1.00 15.81 ? 64  GLY B N   1
+ATOM   1558 C  CA  . GLY B 2 64  ? 28.033  6.146   56.689 1.00 16.57 ? 64  GLY B CA  1
+ATOM   1559 C  C   . GLY B 2 64  ? 28.412  4.786   56.441 1.00 14.05 ? 64  GLY B C   1
+ATOM   1560 O  O   . GLY B 2 64  ? 28.198  3.916   55.788 1.00 17.38 ? 64  GLY B O   1
+ATOM   1561 N  N   . LYS B 2 65  ? 29.289  4.417   57.455 1.00 15.77 ? 65  LYS B N   1
+ATOM   1562 C  CA  . LYS B 2 65  ? 29.624  3.111   57.646 1.00 17.79 ? 65  LYS B CA  1
+ATOM   1563 C  C   . LYS B 2 65  ? 28.652  2.044   57.934 1.00 18.32 ? 65  LYS B C   1
+ATOM   1564 O  O   . LYS B 2 65  ? 28.717  0.965   57.492 1.00 19.33 ? 65  LYS B O   1
+ATOM   1565 C  CB  . LYS B 2 65  ? 31.038  2.891   58.736 1.00 34.65 ? 65  LYS B CB  1
+ATOM   1566 C  CG  . LYS B 2 65  ? 30.760  2.836   59.239 1.00 64.04 ? 65  LYS B CG  1
+ATOM   1567 C  CD  . LYS B 2 65  ? 32.863  2.562   60.547 1.00 58.77 ? 65  LYS B CD  1
+ATOM   1568 C  CE  . LYS B 2 65  ? 31.301  0.821   60.759 1.00 64.47 ? 65  LYS B CE  1
+ATOM   1569 N  NZ  . LYS B 2 65  ? 32.645  1.005   62.961 1.00 67.19 ? 65  LYS B NZ  1
+ATOM   1570 N  N   . LYS B 2 66  ? 27.784  2.452   58.741 1.00 17.45 ? 66  LYS B N   1
+ATOM   1571 C  CA  . LYS B 2 66  ? 26.981  1.647   59.064 1.00 20.10 ? 66  LYS B CA  1
+ATOM   1572 C  C   . LYS B 2 66  ? 25.732  1.397   57.905 1.00 21.06 ? 66  LYS B C   1
+ATOM   1573 O  O   . LYS B 2 66  ? 25.275  0.239   57.722 1.00 17.84 ? 66  LYS B O   1
+ATOM   1574 C  CB  . LYS B 2 66  ? 26.005  2.163   60.308 1.00 22.19 ? 66  LYS B CB  1
+ATOM   1575 C  CG  . LYS B 2 66  ? 24.848  1.534   60.799 1.00 40.97 ? 66  LYS B CG  1
+ATOM   1576 C  CD  . LYS B 2 66  ? 24.242  2.135   62.106 1.00 49.22 ? 66  LYS B CD  1
+ATOM   1577 C  CE  . LYS B 2 66  ? 24.502  0.018   63.132 1.00 72.58 ? 66  LYS B CE  1
+ATOM   1578 N  NZ  . LYS B 2 66  ? 23.240  0.427   64.358 1.00 70.66 ? 66  LYS B NZ  1
+ATOM   1579 N  N   . VAL B 2 67  ? 25.441  2.603   57.382 1.00 16.93 ? 67  VAL B N   1
+ATOM   1580 C  CA  . VAL B 2 67  ? 24.566  2.397   56.066 1.00 19.22 ? 67  VAL B CA  1
+ATOM   1581 C  C   . VAL B 2 67  ? 25.228  1.688   54.977 1.00 11.08 ? 67  VAL B C   1
+ATOM   1582 O  O   . VAL B 2 67  ? 24.646  0.608   54.474 1.00 14.57 ? 67  VAL B O   1
+ATOM   1583 C  CB  . VAL B 2 67  ? 24.039  3.841   55.692 1.00 21.56 ? 67  VAL B CB  1
+ATOM   1584 C  CG1 . VAL B 2 67  ? 23.664  3.987   54.212 1.00 18.58 ? 67  VAL B CG1 1
+ATOM   1585 C  CG2 . VAL B 2 67  ? 23.367  4.561   56.784 1.00 21.34 ? 67  VAL B CG2 1
+ATOM   1586 N  N   . LEU B 2 68  ? 26.430  1.946   54.676 1.00 11.62 ? 68  LEU B N   1
+ATOM   1587 C  CA  . LEU B 2 68  ? 27.064  1.154   53.609 1.00 15.23 ? 68  LEU B CA  1
+ATOM   1588 C  C   . LEU B 2 68  ? 27.274  -0.376  53.915 1.00 13.22 ? 68  LEU B C   1
+ATOM   1589 O  O   . LEU B 2 68  ? 27.457  -1.280  52.955 1.00 14.49 ? 68  LEU B O   1
+ATOM   1590 C  CB  . LEU B 2 68  ? 28.180  1.832   53.061 1.00 22.80 ? 68  LEU B CB  1
+ATOM   1591 C  CG  . LEU B 2 68  ? 28.319  2.218   51.578 1.00 26.57 ? 68  LEU B CG  1
+ATOM   1592 C  CD1 . LEU B 2 68  ? 29.430  1.318   51.450 1.00 62.38 ? 68  LEU B CD1 1
+ATOM   1593 C  CD2 . LEU B 2 68  ? 27.310  2.639   50.926 1.00 35.30 ? 68  LEU B CD2 1
+ATOM   1594 N  N   . GLY B 2 69  ? 27.605  -0.730  55.128 1.00 14.77 ? 69  GLY B N   1
+ATOM   1595 C  CA  . GLY B 2 69  ? 27.764  -1.956  55.488 1.00 20.29 ? 69  GLY B CA  1
+ATOM   1596 C  C   . GLY B 2 69  ? 26.565  -3.074  55.341 1.00 17.59 ? 69  GLY B C   1
+ATOM   1597 O  O   . GLY B 2 69  ? 26.517  -4.018  54.774 1.00 19.02 ? 69  GLY B O   1
+ATOM   1598 N  N   . ALA B 2 70  ? 25.321  -2.265  55.727 1.00 19.76 ? 70  ALA B N   1
+ATOM   1599 C  CA  . ALA B 2 70  ? 24.154  -2.840  55.368 1.00 20.35 ? 70  ALA B CA  1
+ATOM   1600 C  C   . ALA B 2 70  ? 23.895  -3.052  53.845 1.00 16.36 ? 70  ALA B C   1
+ATOM   1601 O  O   . ALA B 2 70  ? 23.394  -4.060  53.258 1.00 18.12 ? 70  ALA B O   1
+ATOM   1602 C  CB  . ALA B 2 70  ? 22.975  -2.192  55.902 1.00 18.92 ? 70  ALA B CB  1
+ATOM   1603 N  N   . PHE B 2 71  ? 24.173  -1.974  53.096 1.00 14.47 ? 71  PHE B N   1
+ATOM   1604 C  CA  . PHE B 2 71  ? 24.100  -2.103  51.628 1.00 18.37 ? 71  PHE B CA  1
+ATOM   1605 C  C   . PHE B 2 71  ? 25.108  -3.282  51.143 1.00 23.80 ? 71  PHE B C   1
+ATOM   1606 O  O   . PHE B 2 71  ? 24.583  -4.033  50.415 1.00 20.23 ? 71  PHE B O   1
+ATOM   1607 C  CB  . PHE B 2 71  ? 24.589  -0.722  51.190 1.00 13.73 ? 71  PHE B CB  1
+ATOM   1608 C  CG  . PHE B 2 71  ? 24.545  -0.688  49.683 1.00 18.08 ? 71  PHE B CG  1
+ATOM   1609 C  CD1 . PHE B 2 71  ? 23.496  -0.251  49.042 1.00 25.10 ? 71  PHE B CD1 1
+ATOM   1610 C  CD2 . PHE B 2 71  ? 25.736  -1.034  48.847 1.00 17.17 ? 71  PHE B CD2 1
+ATOM   1611 C  CE1 . PHE B 2 71  ? 23.331  -0.083  47.561 1.00 19.10 ? 71  PHE B CE1 1
+ATOM   1612 C  CE2 . PHE B 2 71  ? 25.512  -0.889  47.564 1.00 22.20 ? 71  PHE B CE2 1
+ATOM   1613 C  CZ  . PHE B 2 71  ? 24.336  -0.387  46.863 1.00 12.94 ? 71  PHE B CZ  1
+ATOM   1614 N  N   . SER B 2 72  ? 26.042  -3.403  51.598 1.00 20.10 ? 72  SER B N   1
+ATOM   1615 C  CA  . SER B 2 72  ? 27.257  -4.417  51.326 1.00 20.52 ? 72  SER B CA  1
+ATOM   1616 C  C   . SER B 2 72  ? 26.517  -5.733  51.387 1.00 24.58 ? 72  SER B C   1
+ATOM   1617 O  O   . SER B 2 72  ? 26.572  -6.730  50.496 1.00 22.06 ? 72  SER B O   1
+ATOM   1618 C  CB  . SER B 2 72  ? 28.639  -4.010  51.938 1.00 15.28 ? 72  SER B CB  1
+ATOM   1619 O  OG  . SER B 2 72  ? 29.686  -4.749  51.603 1.00 25.10 ? 72  SER B OG  1
+ATOM   1620 N  N   . ASP B 2 73  ? 26.041  -5.856  52.512 1.00 27.59 ? 73  ASP B N   1
+ATOM   1621 C  CA  . ASP B 2 73  ? 25.352  -7.250  52.855 1.00 37.45 ? 73  ASP B CA  1
+ATOM   1622 C  C   . ASP B 2 73  ? 24.444  -7.421  52.094 1.00 25.08 ? 73  ASP B C   1
+ATOM   1623 O  O   . ASP B 2 73  ? 23.895  -8.615  51.627 1.00 31.64 ? 73  ASP B O   1
+ATOM   1624 C  CB  . ASP B 2 73  ? 25.023  -7.152  54.512 1.00 36.32 ? 73  ASP B CB  1
+ATOM   1625 C  CG  . ASP B 2 73  ? 26.461  -7.272  55.438 1.00 45.09 ? 73  ASP B CG  1
+ATOM   1626 O  OD1 . ASP B 2 73  ? 27.834  -7.343  54.925 1.00 37.33 ? 73  ASP B OD1 1
+ATOM   1627 O  OD2 . ASP B 2 73  ? 26.237  -7.047  56.395 1.00 52.94 ? 73  ASP B OD2 1
+ATOM   1628 N  N   . GLY B 2 74  ? 23.441  -6.572  51.599 1.00 21.04 ? 74  GLY B N   1
+ATOM   1629 C  CA  . GLY B 2 74  ? 22.564  -6.653  50.680 1.00 15.14 ? 74  GLY B CA  1
+ATOM   1630 C  C   . GLY B 2 74  ? 22.673  -7.130  49.454 1.00 22.81 ? 74  GLY B C   1
+ATOM   1631 O  O   . GLY B 2 74  ? 22.161  -7.736  48.432 1.00 25.94 ? 74  GLY B O   1
+ATOM   1632 N  N   . LEU B 2 75  ? 24.224  -6.851  48.812 1.00 20.94 ? 75  LEU B N   1
+ATOM   1633 C  CA  . LEU B 2 75  ? 24.631  -7.205  47.555 1.00 15.84 ? 75  LEU B CA  1
+ATOM   1634 C  C   . LEU B 2 75  ? 24.817  -8.740  47.543 1.00 26.11 ? 75  LEU B C   1
+ATOM   1635 O  O   . LEU B 2 75  ? 24.856  -9.260  46.476 1.00 28.14 ? 75  LEU B O   1
+ATOM   1636 C  CB  . LEU B 2 75  ? 26.040  -6.751  47.143 1.00 21.09 ? 75  LEU B CB  1
+ATOM   1637 C  CG  . LEU B 2 75  ? 26.031  -5.478  47.234 1.00 27.76 ? 75  LEU B CG  1
+ATOM   1638 C  CD1 . LEU B 2 75  ? 27.415  -4.635  46.802 1.00 33.03 ? 75  LEU B CD1 1
+ATOM   1639 C  CD2 . LEU B 2 75  ? 25.121  -4.676  46.233 1.00 30.01 ? 75  LEU B CD2 1
+ATOM   1640 N  N   . ALA B 2 76  ? 24.841  -9.392  48.682 1.00 21.21 ? 76  ALA B N   1
+ATOM   1641 C  CA  . ALA B 2 76  ? 24.814  -10.715 48.578 1.00 22.79 ? 76  ALA B CA  1
+ATOM   1642 C  C   . ALA B 2 76  ? 23.577  -11.620 48.492 1.00 40.88 ? 76  ALA B C   1
+ATOM   1643 O  O   . ALA B 2 76  ? 23.432  -12.482 48.230 1.00 38.44 ? 76  ALA B O   1
+ATOM   1644 C  CB  . ALA B 2 76  ? 25.238  -11.384 49.962 1.00 29.05 ? 76  ALA B CB  1
+ATOM   1645 N  N   . HIS B 2 77  ? 22.286  -10.617 48.422 1.00 23.87 ? 77  HIS B N   1
+ATOM   1646 C  CA  . HIS B 2 77  ? 20.883  -11.221 48.468 1.00 21.57 ? 77  HIS B CA  1
+ATOM   1647 C  C   . HIS B 2 77  ? 20.295  -10.394 47.301 1.00 18.37 ? 77  HIS B C   1
+ATOM   1648 O  O   . HIS B 2 77  ? 19.103  -10.123 47.433 1.00 23.13 ? 77  HIS B O   1
+ATOM   1649 C  CB  . HIS B 2 77  ? 20.342  -10.717 49.648 1.00 29.02 ? 77  HIS B CB  1
+ATOM   1650 C  CG  . HIS B 2 77  ? 21.130  -11.489 50.886 1.00 36.16 ? 77  HIS B CG  1
+ATOM   1651 N  ND1 . HIS B 2 77  ? 22.096  -11.238 51.877 1.00 45.10 ? 77  HIS B ND1 1
+ATOM   1652 C  CD2 . HIS B 2 77  ? 20.846  -13.295 50.729 1.00 41.12 ? 77  HIS B CD2 1
+ATOM   1653 C  CE1 . HIS B 2 77  ? 22.200  -12.279 52.330 1.00 37.52 ? 77  HIS B CE1 1
+ATOM   1654 N  NE2 . HIS B 2 77  ? 21.671  -13.347 51.883 1.00 42.04 ? 77  HIS B NE2 1
+ATOM   1655 N  N   . LEU B 2 78  ? 20.851  -10.262 46.194 1.00 22.31 ? 78  LEU B N   1
+ATOM   1656 C  CA  . LEU B 2 78  ? 20.365  -9.324  45.195 1.00 20.28 ? 78  LEU B CA  1
+ATOM   1657 C  C   . LEU B 2 78  ? 19.156  -10.132 44.409 1.00 31.20 ? 78  LEU B C   1
+ATOM   1658 O  O   . LEU B 2 78  ? 18.262  -9.371  44.280 1.00 34.80 ? 78  LEU B O   1
+ATOM   1659 C  CB  . LEU B 2 78  ? 21.253  -9.352  43.861 1.00 19.92 ? 78  LEU B CB  1
+ATOM   1660 C  CG  . LEU B 2 78  ? 22.225  -8.042  44.227 1.00 39.49 ? 78  LEU B CG  1
+ATOM   1661 C  CD1 . LEU B 2 78  ? 23.582  -8.277  43.406 1.00 34.16 ? 78  LEU B CD1 1
+ATOM   1662 C  CD2 . LEU B 2 78  ? 21.878  -6.684  44.615 1.00 31.09 ? 78  LEU B CD2 1
+ATOM   1663 N  N   . ASP B 2 79  ? 18.771  -11.459 44.723 1.00 31.59 ? 79  ASP B N   1
+ATOM   1664 C  CA  . ASP B 2 79  ? 17.589  -12.316 44.081 1.00 37.85 ? 79  ASP B CA  1
+ATOM   1665 C  C   . ASP B 2 79  ? 16.449  -11.812 45.092 1.00 38.72 ? 79  ASP B C   1
+ATOM   1666 O  O   . ASP B 2 79  ? 15.611  -12.366 45.259 1.00 37.62 ? 79  ASP B O   1
+ATOM   1667 C  CB  . ASP B 2 79  ? 18.040  -13.706 44.668 1.00 48.10 ? 79  ASP B CB  1
+ATOM   1668 C  CG  . ASP B 2 79  ? 18.889  -13.996 43.907 1.00 61.60 ? 79  ASP B CG  1
+ATOM   1669 O  OD1 . ASP B 2 79  ? 19.356  -15.070 44.043 1.00 57.05 ? 79  ASP B OD1 1
+ATOM   1670 O  OD2 . ASP B 2 79  ? 18.847  -13.631 42.277 1.00 50.26 ? 79  ASP B OD2 1
+ATOM   1671 N  N   . ASN B 2 80  ? 16.795  -11.295 46.409 1.00 35.73 ? 80  ASN B N   1
+ATOM   1672 C  CA  . ASN B 2 80  ? 15.651  -11.345 47.702 1.00 42.30 ? 80  ASN B CA  1
+ATOM   1673 C  C   . ASN B 2 80  ? 16.175  -9.748  48.337 1.00 30.43 ? 80  ASN B C   1
+ATOM   1674 O  O   . ASN B 2 80  ? 16.151  -9.872  49.408 1.00 27.17 ? 80  ASN B O   1
+ATOM   1675 C  CB  . ASN B 2 80  ? 15.776  -12.483 48.444 1.00 45.64 ? 80  ASN B CB  1
+ATOM   1676 C  CG  . ASN B 2 80  ? 14.480  -12.719 49.598 1.00 49.79 ? 80  ASN B CG  1
+ATOM   1677 O  OD1 . ASN B 2 80  ? 13.587  -11.566 49.220 1.00 49.18 ? 80  ASN B OD1 1
+ATOM   1678 N  ND2 . ASN B 2 80  ? 15.278  -12.953 50.676 1.00 48.18 ? 80  ASN B ND2 1
+ATOM   1679 N  N   . LEU B 2 81  ? 16.091  -8.671  47.578 1.00 31.23 ? 81  LEU B N   1
+ATOM   1680 C  CA  . LEU B 2 81  ? 16.192  -7.362  48.628 1.00 24.59 ? 81  LEU B CA  1
+ATOM   1681 C  C   . LEU B 2 81  ? 15.248  -7.218  49.540 1.00 25.32 ? 81  LEU B C   1
+ATOM   1682 O  O   . LEU B 2 81  ? 15.246  -6.602  50.524 1.00 23.54 ? 81  LEU B O   1
+ATOM   1683 C  CB  . LEU B 2 81  ? 16.577  -6.500  47.545 1.00 29.09 ? 81  LEU B CB  1
+ATOM   1684 C  CG  . LEU B 2 81  ? 17.741  -6.352  46.662 1.00 21.46 ? 81  LEU B CG  1
+ATOM   1685 C  CD1 . LEU B 2 81  ? 17.754  -5.398  45.555 1.00 28.62 ? 81  LEU B CD1 1
+ATOM   1686 C  CD2 . LEU B 2 81  ? 19.020  -6.122  47.440 1.00 30.82 ? 81  LEU B CD2 1
+ATOM   1687 N  N   . LYS B 2 82  ? 13.754  -7.466  48.870 1.00 26.15 ? 82  LYS B N   1
+ATOM   1688 C  CA  . LYS B 2 82  ? 12.752  -6.939  49.865 1.00 24.25 ? 82  LYS B CA  1
+ATOM   1689 C  C   . LYS B 2 82  ? 12.748  -7.633  50.937 1.00 23.08 ? 82  LYS B C   1
+ATOM   1690 O  O   . LYS B 2 82  ? 12.539  -7.237  52.062 1.00 24.88 ? 82  LYS B O   1
+ATOM   1691 C  CB  . LYS B 2 82  ? 11.591  -7.426  48.920 1.00 40.41 ? 82  LYS B CB  1
+ATOM   1692 C  CG  . LYS B 2 82  ? 11.076  -6.189  48.197 1.00 39.73 ? 82  LYS B CG  1
+ATOM   1693 C  CD  . LYS B 2 82  ? 9.628   -6.569  47.342 1.00 66.91 ? 82  LYS B CD  1
+ATOM   1694 C  CE  . LYS B 2 82  ? 9.192   -6.472  47.878 1.00 59.33 ? 82  LYS B CE  1
+ATOM   1695 N  NZ  . LYS B 2 82  ? 7.242   -7.574  47.181 1.00 80.12 ? 82  LYS B NZ  1
+ATOM   1696 N  N   . GLY B 2 83  ? 13.057  -9.002  50.923 1.00 26.18 ? 83  GLY B N   1
+ATOM   1697 C  CA  . GLY B 2 83  ? 13.107  -9.670  52.371 1.00 41.64 ? 83  GLY B CA  1
+ATOM   1698 C  C   . GLY B 2 83  ? 14.245  -9.296  53.110 1.00 31.59 ? 83  GLY B C   1
+ATOM   1699 O  O   . GLY B 2 83  ? 14.105  -9.373  54.400 1.00 36.40 ? 83  GLY B O   1
+ATOM   1700 N  N   . THR B 2 84  ? 15.413  -9.150  52.440 1.00 26.72 ? 84  THR B N   1
+ATOM   1701 C  CA  . THR B 2 84  ? 16.708  -8.664  53.039 1.00 25.47 ? 84  THR B CA  1
+ATOM   1702 C  C   . THR B 2 84  ? 16.396  -7.544  54.027 1.00 33.72 ? 84  THR B C   1
+ATOM   1703 O  O   . THR B 2 84  ? 16.873  -7.154  54.961 1.00 27.43 ? 84  THR B O   1
+ATOM   1704 C  CB  . THR B 2 84  ? 17.962  -8.427  52.225 1.00 25.58 ? 84  THR B CB  1
+ATOM   1705 O  OG1 . THR B 2 84  ? 18.109  -9.894  51.626 1.00 39.04 ? 84  THR B OG1 1
+ATOM   1706 C  CG2 . THR B 2 84  ? 19.008  -8.264  52.889 1.00 30.76 ? 84  THR B CG2 1
+ATOM   1707 N  N   . PHE B 2 85  ? 15.643  -6.499  53.320 1.00 23.61 ? 85  PHE B N   1
+ATOM   1708 C  CA  . PHE B 2 85  ? 15.395  -5.051  53.846 1.00 21.59 ? 85  PHE B CA  1
+ATOM   1709 C  C   . PHE B 2 85  ? 14.189  -4.889  54.587 1.00 28.51 ? 85  PHE B C   1
+ATOM   1710 O  O   . PHE B 2 85  ? 13.901  -3.747  54.911 1.00 18.85 ? 85  PHE B O   1
+ATOM   1711 C  CB  . PHE B 2 85  ? 15.855  -3.968  52.826 1.00 18.34 ? 85  PHE B CB  1
+ATOM   1712 C  CG  . PHE B 2 85  ? 17.194  -3.959  52.461 1.00 13.87 ? 85  PHE B CG  1
+ATOM   1713 C  CD1 . PHE B 2 85  ? 17.734  -4.377  51.221 1.00 16.61 ? 85  PHE B CD1 1
+ATOM   1714 C  CD2 . PHE B 2 85  ? 18.032  -3.541  53.480 1.00 18.32 ? 85  PHE B CD2 1
+ATOM   1715 C  CE1 . PHE B 2 85  ? 19.176  -4.355  51.065 1.00 27.99 ? 85  PHE B CE1 1
+ATOM   1716 C  CE2 . PHE B 2 85  ? 19.422  -3.517  52.938 1.00 21.68 ? 85  PHE B CE2 1
+ATOM   1717 C  CZ  . PHE B 2 85  ? 20.124  -3.954  51.826 1.00 21.59 ? 85  PHE B CZ  1
+ATOM   1718 N  N   . ALA B 2 86  ? 13.377  -5.856  54.682 1.00 22.16 ? 86  ALA B N   1
+ATOM   1719 C  CA  . ALA B 2 86  ? 11.993  -5.682  55.343 1.00 23.14 ? 86  ALA B CA  1
+ATOM   1720 C  C   . ALA B 2 86  ? 11.972  -5.100  56.603 1.00 20.99 ? 86  ALA B C   1
+ATOM   1721 O  O   . ALA B 2 86  ? 11.299  -4.139  56.922 1.00 20.07 ? 86  ALA B O   1
+ATOM   1722 C  CB  . ALA B 2 86  ? 11.146  -6.991  55.344 1.00 23.69 ? 86  ALA B CB  1
+ATOM   1723 N  N   . THR B 2 87  ? 12.735  -5.635  57.509 1.00 14.82 ? 87  THR B N   1
+ATOM   1724 C  CA  . THR B 2 87  ? 12.678  -4.986  58.753 1.00 18.61 ? 87  THR B CA  1
+ATOM   1725 C  C   . THR B 2 87  ? 13.386  -3.568  58.875 1.00 25.42 ? 87  THR B C   1
+ATOM   1726 O  O   . THR B 2 87  ? 12.826  -2.709  59.502 1.00 23.63 ? 87  THR B O   1
+ATOM   1727 C  CB  . THR B 2 87  ? 14.000  -5.767  59.952 1.00 36.27 ? 87  THR B CB  1
+ATOM   1728 O  OG1 . THR B 2 87  ? 13.210  -6.808  60.088 1.00 56.82 ? 87  THR B OG1 1
+ATOM   1729 C  CG2 . THR B 2 87  ? 12.976  -5.320  61.638 1.00 60.80 ? 87  THR B CG2 1
+ATOM   1730 N  N   . LEU B 2 88  ? 14.494  -3.311  58.021 1.00 19.44 ? 88  LEU B N   1
+ATOM   1731 C  CA  . LEU B 2 88  ? 14.863  -1.940  57.992 1.00 17.97 ? 88  LEU B CA  1
+ATOM   1732 C  C   . LEU B 2 88  ? 13.869  -0.972  57.418 1.00 11.34 ? 88  LEU B C   1
+ATOM   1733 O  O   . LEU B 2 88  ? 13.870  0.172   57.765 1.00 17.71 ? 88  LEU B O   1
+ATOM   1734 C  CB  . LEU B 2 88  ? 16.225  -1.909  57.279 1.00 20.20 ? 88  LEU B CB  1
+ATOM   1735 C  CG  . LEU B 2 88  ? 17.476  -2.541  58.000 1.00 27.17 ? 88  LEU B CG  1
+ATOM   1736 C  CD1 . LEU B 2 88  ? 18.459  -2.175  57.121 1.00 32.32 ? 88  LEU B CD1 1
+ATOM   1737 C  CD2 . LEU B 2 88  ? 17.694  -1.401  59.012 1.00 27.72 ? 88  LEU B CD2 1
+ATOM   1738 N  N   . SER B 2 89  ? 13.086  -1.527  56.438 1.00 12.58 ? 89  SER B N   1
+ATOM   1739 C  CA  . SER B 2 89  ? 12.011  -0.626  55.862 1.00 15.21 ? 89  SER B CA  1
+ATOM   1740 C  C   . SER B 2 89  ? 11.062  -0.058  56.910 1.00 14.13 ? 89  SER B C   1
+ATOM   1741 O  O   . SER B 2 89  ? 10.732  1.133   57.128 1.00 14.29 ? 89  SER B O   1
+ATOM   1742 C  CB  . SER B 2 89  ? 11.475  -1.595  54.765 1.00 18.34 ? 89  SER B CB  1
+ATOM   1743 O  OG  . SER B 2 89  ? 10.337  -0.650  54.202 1.00 17.85 ? 89  SER B OG  1
+ATOM   1744 N  N   . GLU B 2 90  ? 10.552  -1.138  57.623 1.00 14.25 ? 90  GLU B N   1
+ATOM   1745 C  CA  . GLU B 2 90  ? 9.965   -0.806  58.777 1.00 20.50 ? 90  GLU B CA  1
+ATOM   1746 C  C   . GLU B 2 90  ? 10.137  0.214   59.891 1.00 13.47 ? 90  GLU B C   1
+ATOM   1747 O  O   . GLU B 2 90  ? 9.609   1.234   60.149 1.00 16.05 ? 90  GLU B O   1
+ATOM   1748 C  CB  . GLU B 2 90  ? 9.223   -2.276  59.606 1.00 21.76 ? 90  GLU B CB  1
+ATOM   1749 C  CG  . GLU B 2 90  ? 8.725   -2.865  58.558 1.00 48.13 ? 90  GLU B CG  1
+ATOM   1750 C  CD  . GLU B 2 90  ? 7.720   -4.495  59.331 1.00 78.64 ? 90  GLU B CD  1
+ATOM   1751 O  OE1 . GLU B 2 90  ? 7.415   -4.113  60.110 1.00 55.55 ? 90  GLU B OE1 1
+ATOM   1752 O  OE2 . GLU B 2 90  ? 8.521   -5.507  59.138 1.00 74.37 ? 90  GLU B OE2 1
+ATOM   1753 N  N   . LEU B 2 91  ? 11.567  -0.057  60.180 1.00 13.36 ? 91  LEU B N   1
+ATOM   1754 C  CA  . LEU B 2 91  ? 12.181  0.902   61.007 1.00 14.20 ? 91  LEU B CA  1
+ATOM   1755 C  C   . LEU B 2 91  ? 12.185  2.302   60.529 1.00 8.80  ? 91  LEU B C   1
+ATOM   1756 O  O   . LEU B 2 91  ? 12.016  3.329   61.175 1.00 10.74 ? 91  LEU B O   1
+ATOM   1757 C  CB  . LEU B 2 91  ? 13.489  0.161   61.281 1.00 12.00 ? 91  LEU B CB  1
+ATOM   1758 C  CG  . LEU B 2 91  ? 14.259  1.136   62.068 1.00 18.50 ? 91  LEU B CG  1
+ATOM   1759 C  CD1 . LEU B 2 91  ? 13.765  0.939   63.614 1.00 20.79 ? 91  LEU B CD1 1
+ATOM   1760 C  CD2 . LEU B 2 91  ? 15.545  1.089   62.089 1.00 37.40 ? 91  LEU B CD2 1
+ATOM   1761 N  N   . HIS B 2 92  ? 12.647  2.280   59.217 1.00 10.78 ? 92  HIS B N   1
+ATOM   1762 C  CA  . HIS B 2 92  ? 12.817  3.637   58.852 1.00 11.85 ? 92  HIS B CA  1
+ATOM   1763 C  C   . HIS B 2 92  ? 11.420  4.503   58.520 1.00 11.06 ? 92  HIS B C   1
+ATOM   1764 O  O   . HIS B 2 92  ? 11.376  5.713   58.688 1.00 13.45 ? 92  HIS B O   1
+ATOM   1765 C  CB  . HIS B 2 92  ? 13.457  3.591   57.357 1.00 9.95  ? 92  HIS B CB  1
+ATOM   1766 C  CG  . HIS B 2 92  ? 15.014  3.542   57.496 1.00 15.50 ? 92  HIS B CG  1
+ATOM   1767 N  ND1 . HIS B 2 92  ? 15.623  2.168   57.649 1.00 15.27 ? 92  HIS B ND1 1
+ATOM   1768 C  CD2 . HIS B 2 92  ? 16.075  4.369   57.297 1.00 23.76 ? 92  HIS B CD2 1
+ATOM   1769 C  CE1 . HIS B 2 92  ? 17.046  2.567   57.759 1.00 16.99 ? 92  HIS B CE1 1
+ATOM   1770 N  NE2 . HIS B 2 92  ? 17.154  3.772   57.405 1.00 14.76 ? 92  HIS B NE2 1
+ATOM   1771 N  N   . CYS B 2 93  ? 10.367  3.719   58.295 1.00 14.83 ? 93  CYS B N   1
+ATOM   1772 C  CA  . CYS B 2 93  ? 9.112   4.377   58.294 1.00 12.23 ? 93  CYS B CA  1
+ATOM   1773 C  C   . CYS B 2 93  ? 8.587   4.705   59.800 1.00 10.49 ? 93  CYS B C   1
+ATOM   1774 O  O   . CYS B 2 93  ? 8.276   5.751   59.973 1.00 18.01 ? 93  CYS B O   1
+ATOM   1775 C  CB  . CYS B 2 93  ? 8.281   3.423   57.531 1.00 15.43 ? 93  CYS B CB  1
+ATOM   1776 S  SG  . CYS B 2 93  ? 6.420   4.028   57.501 1.00 18.37 ? 93  CYS B SG  1
+ATOM   1777 N  N   . ASP B 2 94  ? 8.477   3.628   60.511 1.00 13.11 ? 94  ASP B N   1
+ATOM   1778 C  CA  . ASP B 2 94  ? 7.602   3.892   61.681 1.00 15.32 ? 94  ASP B CA  1
+ATOM   1779 C  C   . ASP B 2 94  ? 8.486   4.482   62.659 1.00 25.71 ? 94  ASP B C   1
+ATOM   1780 O  O   . ASP B 2 94  ? 7.929   5.292   63.634 1.00 21.65 ? 94  ASP B O   1
+ATOM   1781 C  CB  . ASP B 2 94  ? 7.209   2.585   62.280 1.00 21.65 ? 94  ASP B CB  1
+ATOM   1782 C  CG  . ASP B 2 94  ? 6.070   1.596   61.499 1.00 42.42 ? 94  ASP B CG  1
+ATOM   1783 O  OD1 . ASP B 2 94  ? 5.627   2.378   60.842 1.00 30.02 ? 94  ASP B OD1 1
+ATOM   1784 O  OD2 . ASP B 2 94  ? 6.292   0.683   61.756 1.00 43.30 ? 94  ASP B OD2 1
+ATOM   1785 N  N   . LYS B 2 95  ? 9.743   4.399   62.920 1.00 18.55 ? 95  LYS B N   1
+ATOM   1786 C  CA  . LYS B 2 95  ? 10.356  5.174   63.859 1.00 19.10 ? 95  LYS B CA  1
+ATOM   1787 C  C   . LYS B 2 95  ? 11.233  6.129   63.665 1.00 19.57 ? 95  LYS B C   1
+ATOM   1788 O  O   . LYS B 2 95  ? 11.350  7.105   64.149 1.00 21.87 ? 95  LYS B O   1
+ATOM   1789 C  CB  . LYS B 2 95  ? 11.286  3.933   64.605 1.00 25.95 ? 95  LYS B CB  1
+ATOM   1790 C  CG  . LYS B 2 95  ? 10.453  2.784   65.248 1.00 24.86 ? 95  LYS B CG  1
+ATOM   1791 C  CD  . LYS B 2 95  ? 9.495   3.620   66.283 1.00 36.14 ? 95  LYS B CD  1
+ATOM   1792 C  CE  . LYS B 2 95  ? 8.951   2.491   67.133 1.00 47.76 ? 95  LYS B CE  1
+ATOM   1793 N  NZ  . LYS B 2 95  ? 7.999   2.968   67.996 1.00 55.91 ? 95  LYS B NZ  1
+ATOM   1794 N  N   . LEU B 2 96  ? 12.022  6.029   62.377 1.00 12.40 ? 96  LEU B N   1
+ATOM   1795 C  CA  . LEU B 2 96  ? 12.770  7.089   61.920 1.00 11.86 ? 96  LEU B CA  1
+ATOM   1796 C  C   . LEU B 2 96  ? 12.265  8.264   61.098 1.00 15.10 ? 96  LEU B C   1
+ATOM   1797 O  O   . LEU B 2 96  ? 12.803  9.268   61.003 1.00 17.50 ? 96  LEU B O   1
+ATOM   1798 C  CB  . LEU B 2 96  ? 14.049  6.506   61.428 1.00 14.08 ? 96  LEU B CB  1
+ATOM   1799 C  CG  . LEU B 2 96  ? 14.773  5.204   62.092 1.00 12.34 ? 96  LEU B CG  1
+ATOM   1800 C  CD1 . LEU B 2 96  ? 15.909  4.719   61.156 1.00 13.78 ? 96  LEU B CD1 1
+ATOM   1801 C  CD2 . LEU B 2 96  ? 15.329  6.095   63.362 1.00 22.81 ? 96  LEU B CD2 1
+ATOM   1802 N  N   . HIS B 2 97  ? 11.140  7.868   60.450 1.00 15.44 ? 97  HIS B N   1
+ATOM   1803 C  CA  . HIS B 2 97  ? 10.417  8.927   59.716 1.00 18.15 ? 97  HIS B CA  1
+ATOM   1804 C  C   . HIS B 2 97  ? 11.255  9.475   58.551 1.00 12.24 ? 97  HIS B C   1
+ATOM   1805 O  O   . HIS B 2 97  ? 11.180  10.677  58.193 1.00 15.82 ? 97  HIS B O   1
+ATOM   1806 C  CB  . HIS B 2 97  ? 9.811   10.112  60.495 1.00 17.74 ? 97  HIS B CB  1
+ATOM   1807 C  CG  . HIS B 2 97  ? 9.130   9.569   61.875 1.00 16.77 ? 97  HIS B CG  1
+ATOM   1808 N  ND1 . HIS B 2 97  ? 8.081   8.671   61.788 1.00 19.56 ? 97  HIS B ND1 1
+ATOM   1809 C  CD2 . HIS B 2 97  ? 9.746   9.660   63.051 1.00 23.33 ? 97  HIS B CD2 1
+ATOM   1810 C  CE1 . HIS B 2 97  ? 7.935   8.302   63.061 1.00 19.82 ? 97  HIS B CE1 1
+ATOM   1811 N  NE2 . HIS B 2 97  ? 8.797   8.957   63.817 1.00 20.39 ? 97  HIS B NE2 1
+ATOM   1812 N  N   . VAL B 2 98  ? 11.844  8.510   57.770 1.00 13.81 ? 98  VAL B N   1
+ATOM   1813 C  CA  . VAL B 2 98  ? 12.806  9.035   56.715 1.00 9.22  ? 98  VAL B CA  1
+ATOM   1814 C  C   . VAL B 2 98  ? 11.854  8.910   55.326 1.00 9.86  ? 98  VAL B C   1
+ATOM   1815 O  O   . VAL B 2 98  ? 11.626  7.784   54.937 1.00 12.90 ? 98  VAL B O   1
+ATOM   1816 C  CB  . VAL B 2 98  ? 13.977  8.127   56.532 1.00 9.87  ? 98  VAL B CB  1
+ATOM   1817 C  CG1 . VAL B 2 98  ? 14.839  8.538   55.444 1.00 14.91 ? 98  VAL B CG1 1
+ATOM   1818 C  CG2 . VAL B 2 98  ? 14.946  8.305   57.863 1.00 11.36 ? 98  VAL B CG2 1
+ATOM   1819 N  N   . ASP B 2 99  ? 11.695  10.032  54.646 1.00 11.46 ? 99  ASP B N   1
+ATOM   1820 C  CA  . ASP B 2 99  ? 10.839  10.096  53.453 1.00 9.02  ? 99  ASP B CA  1
+ATOM   1821 C  C   . ASP B 2 99  ? 11.861  9.238   52.549 1.00 15.41 ? 99  ASP B C   1
+ATOM   1822 O  O   . ASP B 2 99  ? 13.084  9.428   52.306 1.00 10.63 ? 99  ASP B O   1
+ATOM   1823 C  CB  . ASP B 2 99  ? 11.004  11.443  52.964 1.00 9.79  ? 99  ASP B CB  1
+ATOM   1824 C  CG  . ASP B 2 99  ? 10.392  11.733  51.498 1.00 10.69 ? 99  ASP B CG  1
+ATOM   1825 O  OD1 . ASP B 2 99  ? 10.276  13.006  51.280 1.00 15.04 ? 99  ASP B OD1 1
+ATOM   1826 O  OD2 . ASP B 2 99  ? 10.115  10.654  50.905 1.00 11.07 ? 99  ASP B OD2 1
+ATOM   1827 N  N   . PRO B 2 100 ? 11.370  8.210   51.844 1.00 10.46 ? 100 PRO B N   1
+ATOM   1828 C  CA  . PRO B 2 100 ? 12.169  7.243   50.975 1.00 11.87 ? 100 PRO B CA  1
+ATOM   1829 C  C   . PRO B 2 100 ? 12.704  7.988   49.722 1.00 13.04 ? 100 PRO B C   1
+ATOM   1830 O  O   . PRO B 2 100 ? 13.720  7.314   49.176 1.00 13.79 ? 100 PRO B O   1
+ATOM   1831 C  CB  . PRO B 2 100 ? 11.245  6.194   50.534 1.00 17.03 ? 100 PRO B CB  1
+ATOM   1832 C  CG  . PRO B 2 100 ? 10.001  6.451   51.317 1.00 17.33 ? 100 PRO B CG  1
+ATOM   1833 C  CD  . PRO B 2 100 ? 9.983   7.753   52.015 1.00 9.97  ? 100 PRO B CD  1
+ATOM   1834 N  N   . GLU B 2 101 ? 12.441  9.226   49.510 1.00 9.66  ? 101 GLU B N   1
+ATOM   1835 C  CA  . GLU B 2 101 ? 13.146  10.025  48.465 1.00 11.29 ? 101 GLU B CA  1
+ATOM   1836 C  C   . GLU B 2 101 ? 14.600  10.176  48.709 1.00 17.59 ? 101 GLU B C   1
+ATOM   1837 O  O   . GLU B 2 101 ? 15.512  9.964   48.029 1.00 16.98 ? 101 GLU B O   1
+ATOM   1838 C  CB  . GLU B 2 101 ? 12.565  11.264  48.090 1.00 18.71 ? 101 GLU B CB  1
+ATOM   1839 C  CG  . GLU B 2 101 ? 13.234  12.142  47.080 1.00 30.25 ? 101 GLU B CG  1
+ATOM   1840 C  CD  . GLU B 2 101 ? 12.792  11.184  45.354 1.00 26.27 ? 101 GLU B CD  1
+ATOM   1841 O  OE1 . GLU B 2 101 ? 11.846  10.542  45.593 1.00 25.29 ? 101 GLU B OE1 1
+ATOM   1842 O  OE2 . GLU B 2 101 ? 13.771  11.867  45.076 1.00 34.30 ? 101 GLU B OE2 1
+ATOM   1843 N  N   . ASN B 2 102 ? 14.961  10.136  50.184 1.00 12.60 ? 102 ASN B N   1
+ATOM   1844 C  CA  . ASN B 2 102 ? 16.369  10.152  50.493 1.00 9.48  ? 102 ASN B CA  1
+ATOM   1845 C  C   . ASN B 2 102 ? 17.063  8.970   50.127 1.00 8.44  ? 102 ASN B C   1
+ATOM   1846 O  O   . ASN B 2 102 ? 18.341  9.096   49.822 1.00 13.92 ? 102 ASN B O   1
+ATOM   1847 C  CB  . ASN B 2 102 ? 16.392  10.174  52.043 1.00 18.27 ? 102 ASN B CB  1
+ATOM   1848 C  CG  . ASN B 2 102 ? 16.035  11.675  52.508 1.00 26.18 ? 102 ASN B CG  1
+ATOM   1849 O  OD1 . ASN B 2 102 ? 16.519  12.467  52.399 1.00 20.87 ? 102 ASN B OD1 1
+ATOM   1850 N  ND2 . ASN B 2 102 ? 14.769  11.607  53.284 1.00 25.76 ? 102 ASN B ND2 1
+ATOM   1851 N  N   . PHE B 2 103 ? 16.576  7.740   50.008 1.00 11.66 ? 103 PHE B N   1
+ATOM   1852 C  CA  . PHE B 2 103 ? 17.117  6.527   49.615 1.00 11.79 ? 103 PHE B CA  1
+ATOM   1853 C  C   . PHE B 2 103 ? 17.682  6.793   48.117 1.00 19.35 ? 103 PHE B C   1
+ATOM   1854 O  O   . PHE B 2 103 ? 18.655  6.279   47.673 1.00 16.06 ? 103 PHE B O   1
+ATOM   1855 C  CB  . PHE B 2 103 ? 16.402  5.295   49.735 1.00 12.75 ? 103 PHE B CB  1
+ATOM   1856 C  CG  . PHE B 2 103 ? 15.792  5.043   51.183 1.00 17.48 ? 103 PHE B CG  1
+ATOM   1857 C  CD1 . PHE B 2 103 ? 16.626  5.371   52.232 1.00 13.65 ? 103 PHE B CD1 1
+ATOM   1858 C  CD2 . PHE B 2 103 ? 14.575  4.624   51.277 1.00 13.36 ? 103 PHE B CD2 1
+ATOM   1859 C  CE1 . PHE B 2 103 ? 16.035  5.299   53.523 1.00 14.94 ? 103 PHE B CE1 1
+ATOM   1860 C  CE2 . PHE B 2 103 ? 14.089  4.494   52.678 1.00 14.24 ? 103 PHE B CE2 1
+ATOM   1861 C  CZ  . PHE B 2 103 ? 15.001  4.752   53.694 1.00 19.61 ? 103 PHE B CZ  1
+ATOM   1862 N  N   . ARG B 2 104 ? 16.765  7.434   47.327 1.00 13.60 ? 104 ARG B N   1
+ATOM   1863 C  CA  . ARG B 2 104 ? 17.161  7.494   45.912 1.00 17.00 ? 104 ARG B CA  1
+ATOM   1864 C  C   . ARG B 2 104 ? 18.212  8.452   45.689 1.00 13.66 ? 104 ARG B C   1
+ATOM   1865 O  O   . ARG B 2 104 ? 19.173  8.356   44.830 1.00 13.41 ? 104 ARG B O   1
+ATOM   1866 C  CB  . ARG B 2 104 ? 15.783  8.094   45.173 1.00 18.62 ? 104 ARG B CB  1
+ATOM   1867 C  CG  . ARG B 2 104 ? 14.727  7.128   45.067 1.00 31.60 ? 104 ARG B CG  1
+ATOM   1868 C  CD  . ARG B 2 104 ? 13.095  7.525   44.551 1.00 44.99 ? 104 ARG B CD  1
+ATOM   1869 N  NE  . ARG B 2 104 ? 12.264  6.376   45.402 1.00 53.69 ? 104 ARG B NE  1
+ATOM   1870 C  CZ  . ARG B 2 104 ? 11.048  7.024   43.780 1.00 80.12 ? 104 ARG B CZ  1
+ATOM   1871 N  NH1 . ARG B 2 104 ? 10.472  8.797   43.599 1.00 72.76 ? 104 ARG B NH1 1
+ATOM   1872 N  NH2 . ARG B 2 104 ? 10.315  5.334   43.073 1.00 80.07 ? 104 ARG B NH2 1
+ATOM   1873 N  N   . LEU B 2 105 ? 18.179  9.611   46.497 1.00 12.29 ? 105 LEU B N   1
+ATOM   1874 C  CA  . LEU B 2 105 ? 19.191  10.635  46.494 1.00 11.07 ? 105 LEU B CA  1
+ATOM   1875 C  C   . LEU B 2 105 ? 20.552  9.924   46.959 1.00 13.91 ? 105 LEU B C   1
+ATOM   1876 O  O   . LEU B 2 105 ? 21.557  10.172  46.270 1.00 14.94 ? 105 LEU B O   1
+ATOM   1877 C  CB  . LEU B 2 105 ? 18.946  11.643  47.458 1.00 12.50 ? 105 LEU B CB  1
+ATOM   1878 C  CG  . LEU B 2 105 ? 17.748  12.696  46.997 1.00 17.21 ? 105 LEU B CG  1
+ATOM   1879 C  CD1 . LEU B 2 105 ? 17.583  13.597  48.206 1.00 19.52 ? 105 LEU B CD1 1
+ATOM   1880 C  CD2 . LEU B 2 105 ? 18.097  13.435  45.709 1.00 25.82 ? 105 LEU B CD2 1
+ATOM   1881 N  N   . LEU B 2 106 ? 20.450  9.089   47.973 1.00 16.16 ? 106 LEU B N   1
+ATOM   1882 C  CA  . LEU B 2 106 ? 21.763  8.425   48.378 1.00 11.19 ? 106 LEU B CA  1
+ATOM   1883 C  C   . LEU B 2 106 ? 22.214  7.553   47.269 1.00 11.49 ? 106 LEU B C   1
+ATOM   1884 O  O   . LEU B 2 106 ? 23.428  7.518   46.964 1.00 14.59 ? 106 LEU B O   1
+ATOM   1885 C  CB  . LEU B 2 106 ? 21.660  7.731   49.668 1.00 9.57  ? 106 LEU B CB  1
+ATOM   1886 C  CG  . LEU B 2 106 ? 22.897  7.065   50.305 1.00 14.52 ? 106 LEU B CG  1
+ATOM   1887 C  CD1 . LEU B 2 106 ? 23.904  8.021   50.433 1.00 20.21 ? 106 LEU B CD1 1
+ATOM   1888 C  CD2 . LEU B 2 106 ? 22.520  6.257   51.230 1.00 25.23 ? 106 LEU B CD2 1
+ATOM   1889 N  N   . GLY B 2 107 ? 21.445  6.806   46.520 1.00 8.80  ? 107 GLY B N   1
+ATOM   1890 C  CA  . GLY B 2 107 ? 21.817  5.869   45.562 1.00 11.35 ? 107 GLY B CA  1
+ATOM   1891 C  C   . GLY B 2 107 ? 22.384  6.743   44.438 1.00 11.83 ? 107 GLY B C   1
+ATOM   1892 O  O   . GLY B 2 107 ? 23.467  6.245   43.887 1.00 14.42 ? 107 GLY B O   1
+ATOM   1893 N  N   . ASN B 2 108 ? 21.960  7.978   44.074 1.00 11.55 ? 108 ASN B N   1
+ATOM   1894 C  CA  . ASN B 2 108 ? 22.608  8.523   42.962 1.00 9.47  ? 108 ASN B CA  1
+ATOM   1895 C  C   . ASN B 2 108 ? 23.992  9.226   43.457 1.00 9.85  ? 108 ASN B C   1
+ATOM   1896 O  O   . ASN B 2 108 ? 24.912  9.193   42.667 1.00 13.16 ? 108 ASN B O   1
+ATOM   1897 C  CB  . ASN B 2 108 ? 21.780  9.680   42.568 1.00 16.47 ? 108 ASN B CB  1
+ATOM   1898 C  CG  . ASN B 2 108 ? 20.492  8.989   41.450 1.00 25.36 ? 108 ASN B CG  1
+ATOM   1899 O  OD1 . ASN B 2 108 ? 20.887  7.781   40.992 1.00 28.00 ? 108 ASN B OD1 1
+ATOM   1900 N  ND2 . ASN B 2 108 ? 19.971  10.061  41.576 1.00 42.45 ? 108 ASN B ND2 1
+ATOM   1901 N  N   . VAL B 2 109 ? 24.115  9.650   44.728 1.00 11.97 ? 109 VAL B N   1
+ATOM   1902 C  CA  . VAL B 2 109 ? 25.412  10.103  45.113 1.00 8.99  ? 109 VAL B CA  1
+ATOM   1903 C  C   . VAL B 2 109 ? 26.324  9.000   45.263 1.00 12.55 ? 109 VAL B C   1
+ATOM   1904 O  O   . VAL B 2 109 ? 27.607  9.148   44.937 1.00 13.71 ? 109 VAL B O   1
+ATOM   1905 C  CB  . VAL B 2 109 ? 25.253  10.738  46.568 1.00 15.07 ? 109 VAL B CB  1
+ATOM   1906 C  CG1 . VAL B 2 109 ? 26.590  11.020  47.035 1.00 19.91 ? 109 VAL B CG1 1
+ATOM   1907 C  CG2 . VAL B 2 109 ? 24.461  12.184  46.410 1.00 15.78 ? 109 VAL B CG2 1
+ATOM   1908 N  N   . LEU B 2 110 ? 25.910  7.733   45.661 1.00 9.97  ? 110 LEU B N   1
+ATOM   1909 C  CA  . LEU B 2 110 ? 26.757  6.506   45.671 1.00 9.78  ? 110 LEU B CA  1
+ATOM   1910 C  C   . LEU B 2 110 ? 27.367  6.331   44.318 1.00 13.14 ? 110 LEU B C   1
+ATOM   1911 O  O   . LEU B 2 110 ? 28.535  5.997   44.117 1.00 11.97 ? 110 LEU B O   1
+ATOM   1912 C  CB  . LEU B 2 110 ? 25.957  5.401   46.310 1.00 11.11 ? 110 LEU B CB  1
+ATOM   1913 C  CG  . LEU B 2 110 ? 26.834  4.024   46.377 1.00 18.59 ? 110 LEU B CG  1
+ATOM   1914 C  CD1 . LEU B 2 110 ? 28.130  4.203   47.137 1.00 24.07 ? 110 LEU B CD1 1
+ATOM   1915 C  CD2 . LEU B 2 110 ? 26.205  2.843   46.850 1.00 21.67 ? 110 LEU B CD2 1
+ATOM   1916 N  N   . VAL B 2 111 ? 26.547  6.334   43.267 1.00 10.25 ? 111 VAL B N   1
+ATOM   1917 C  CA  . VAL B 2 111 ? 26.938  6.102   41.847 1.00 8.08  ? 111 VAL B CA  1
+ATOM   1918 C  C   . VAL B 2 111 ? 28.040  7.090   41.618 1.00 10.10 ? 111 VAL B C   1
+ATOM   1919 O  O   . VAL B 2 111 ? 29.124  6.855   40.914 1.00 14.18 ? 111 VAL B O   1
+ATOM   1920 C  CB  . VAL B 2 111 ? 25.676  6.121   40.970 1.00 11.95 ? 111 VAL B CB  1
+ATOM   1921 C  CG1 . VAL B 2 111 ? 26.242  6.178   39.537 1.00 16.64 ? 111 VAL B CG1 1
+ATOM   1922 C  CG2 . VAL B 2 111 ? 25.037  4.792   41.207 1.00 12.92 ? 111 VAL B CG2 1
+ATOM   1923 N  N   . CYS B 2 112 ? 27.960  8.420   41.863 1.00 10.01 ? 112 CYS B N   1
+ATOM   1924 C  CA  . CYS B 2 112 ? 28.847  9.563   41.594 1.00 9.19  ? 112 CYS B CA  1
+ATOM   1925 C  C   . CYS B 2 112 ? 30.131  9.178   42.422 1.00 14.92 ? 112 CYS B C   1
+ATOM   1926 O  O   . CYS B 2 112 ? 31.189  9.331   41.766 1.00 13.93 ? 112 CYS B O   1
+ATOM   1927 C  CB  . CYS B 2 112 ? 28.575  10.834  42.020 1.00 15.04 ? 112 CYS B CB  1
+ATOM   1928 S  SG  . CYS B 2 112 ? 27.139  11.500  40.895 1.00 18.10 ? 112 CYS B SG  1
+ATOM   1929 N  N   . VAL B 2 113 ? 29.951  8.757   43.546 1.00 9.52  ? 113 VAL B N   1
+ATOM   1930 C  CA  . VAL B 2 113 ? 31.171  8.317   44.247 1.00 11.92 ? 113 VAL B CA  1
+ATOM   1931 C  C   . VAL B 2 113 ? 31.798  7.137   43.764 1.00 15.57 ? 113 VAL B C   1
+ATOM   1932 O  O   . VAL B 2 113 ? 33.201  7.308   43.648 1.00 13.38 ? 113 VAL B O   1
+ATOM   1933 C  CB  . VAL B 2 113 ? 30.902  8.062   45.830 1.00 12.70 ? 113 VAL B CB  1
+ATOM   1934 C  CG1 . VAL B 2 113 ? 32.013  7.512   46.532 1.00 17.23 ? 113 VAL B CG1 1
+ATOM   1935 C  CG2 . VAL B 2 113 ? 30.520  9.259   46.525 1.00 17.43 ? 113 VAL B CG2 1
+ATOM   1936 N  N   . LEU B 2 114 ? 31.324  6.062   43.240 1.00 10.74 ? 114 LEU B N   1
+ATOM   1937 C  CA  . LEU B 2 114 ? 31.995  5.039   42.534 1.00 10.20 ? 114 LEU B CA  1
+ATOM   1938 C  C   . LEU B 2 114 ? 32.751  5.641   41.395 1.00 10.87 ? 114 LEU B C   1
+ATOM   1939 O  O   . LEU B 2 114 ? 33.824  5.007   41.071 1.00 12.76 ? 114 LEU B O   1
+ATOM   1940 C  CB  . LEU B 2 114 ? 31.037  4.015   42.440 1.00 6.84  ? 114 LEU B CB  1
+ATOM   1941 C  CG  . LEU B 2 114 ? 30.484  3.267   43.633 1.00 10.74 ? 114 LEU B CG  1
+ATOM   1942 C  CD1 . LEU B 2 114 ? 29.376  2.363   43.252 1.00 15.38 ? 114 LEU B CD1 1
+ATOM   1943 C  CD2 . LEU B 2 114 ? 31.564  2.546   44.369 1.00 21.35 ? 114 LEU B CD2 1
+ATOM   1944 N  N   . ALA B 2 115 ? 31.950  6.449   40.603 1.00 9.28  ? 115 ALA B N   1
+ATOM   1945 C  CA  . ALA B 2 115 ? 32.629  6.932   39.378 1.00 9.22  ? 115 ALA B CA  1
+ATOM   1946 C  C   . ALA B 2 115 ? 33.943  7.706   39.770 1.00 9.44  ? 115 ALA B C   1
+ATOM   1947 O  O   . ALA B 2 115 ? 34.940  7.623   39.058 1.00 12.10 ? 115 ALA B O   1
+ATOM   1948 C  CB  . ALA B 2 115 ? 31.504  7.732   38.806 1.00 12.15 ? 115 ALA B CB  1
+ATOM   1949 N  N   . HIS B 2 116 ? 33.816  8.499   40.800 1.00 13.11 ? 116 HIS B N   1
+ATOM   1950 C  CA  . HIS B 2 116 ? 35.039  9.373   41.116 1.00 12.81 ? 116 HIS B CA  1
+ATOM   1951 C  C   . HIS B 2 116 ? 36.081  8.435   41.541 1.00 18.85 ? 116 HIS B C   1
+ATOM   1952 O  O   . HIS B 2 116 ? 37.296  8.634   41.255 1.00 16.05 ? 116 HIS B O   1
+ATOM   1953 C  CB  . HIS B 2 116 ? 34.646  10.209  42.207 1.00 17.43 ? 116 HIS B CB  1
+ATOM   1954 C  CG  . HIS B 2 116 ? 35.561  11.207  42.576 1.00 27.80 ? 116 HIS B CG  1
+ATOM   1955 N  ND1 . HIS B 2 116 ? 36.060  11.260  44.002 1.00 27.30 ? 116 HIS B ND1 1
+ATOM   1956 C  CD2 . HIS B 2 116 ? 36.306  12.087  41.963 1.00 25.62 ? 116 HIS B CD2 1
+ATOM   1957 C  CE1 . HIS B 2 116 ? 36.918  12.464  43.926 1.00 29.22 ? 116 HIS B CE1 1
+ATOM   1958 N  NE2 . HIS B 2 116 ? 37.254  12.813  42.709 1.00 26.05 ? 116 HIS B NE2 1
+ATOM   1959 N  N   . HIS B 2 117 ? 35.860  7.439   42.432 1.00 11.35 ? 117 HIS B N   1
+ATOM   1960 C  CA  . HIS B 2 117 ? 36.734  6.446   42.798 1.00 18.75 ? 117 HIS B CA  1
+ATOM   1961 C  C   . HIS B 2 117 ? 37.377  5.630   41.862 1.00 20.53 ? 117 HIS B C   1
+ATOM   1962 O  O   . HIS B 2 117 ? 38.574  5.322   41.965 1.00 17.07 ? 117 HIS B O   1
+ATOM   1963 C  CB  . HIS B 2 117 ? 36.171  5.346   43.914 1.00 19.57 ? 117 HIS B CB  1
+ATOM   1964 C  CG  . HIS B 2 117 ? 36.730  5.390   45.148 1.00 39.90 ? 117 HIS B CG  1
+ATOM   1965 N  ND1 . HIS B 2 117 ? 35.958  7.148   45.440 1.00 47.73 ? 117 HIS B ND1 1
+ATOM   1966 C  CD2 . HIS B 2 117 ? 37.731  4.613   46.215 1.00 38.82 ? 117 HIS B CD2 1
+ATOM   1967 C  CE1 . HIS B 2 117 ? 36.348  7.354   47.132 1.00 27.38 ? 117 HIS B CE1 1
+ATOM   1968 N  NE2 . HIS B 2 117 ? 36.619  5.926   47.606 1.00 51.83 ? 117 HIS B NE2 1
+ATOM   1969 N  N   . PHE B 2 118 ? 36.692  4.986   40.818 1.00 13.44 ? 118 PHE B N   1
+ATOM   1970 C  CA  . PHE B 2 118 ? 37.014  4.043   39.859 1.00 13.47 ? 118 PHE B CA  1
+ATOM   1971 C  C   . PHE B 2 118 ? 37.444  4.713   38.545 1.00 14.52 ? 118 PHE B C   1
+ATOM   1972 O  O   . PHE B 2 118 ? 38.084  3.890   37.815 1.00 15.85 ? 118 PHE B O   1
+ATOM   1973 C  CB  . PHE B 2 118 ? 36.116  2.965   39.861 1.00 14.99 ? 118 PHE B CB  1
+ATOM   1974 C  CG  . PHE B 2 118 ? 36.191  2.189   40.958 1.00 22.65 ? 118 PHE B CG  1
+ATOM   1975 C  CD1 . PHE B 2 118 ? 35.152  2.240   41.907 1.00 28.61 ? 118 PHE B CD1 1
+ATOM   1976 C  CD2 . PHE B 2 118 ? 37.350  1.364   41.568 1.00 34.26 ? 118 PHE B CD2 1
+ATOM   1977 C  CE1 . PHE B 2 118 ? 35.094  1.336   43.117 1.00 29.50 ? 118 PHE B CE1 1
+ATOM   1978 C  CE2 . PHE B 2 118 ? 37.061  0.545   42.336 1.00 36.60 ? 118 PHE B CE2 1
+ATOM   1979 C  CZ  . PHE B 2 118 ? 36.420  0.704   43.514 1.00 30.15 ? 118 PHE B CZ  1
+ATOM   1980 N  N   . GLY B 2 119 ? 37.037  5.931   38.263 1.00 13.81 ? 119 GLY B N   1
+ATOM   1981 C  CA  . GLY B 2 119 ? 37.483  6.600   36.972 1.00 14.28 ? 119 GLY B CA  1
+ATOM   1982 C  C   . GLY B 2 119 ? 36.993  5.780   35.914 1.00 17.07 ? 119 GLY B C   1
+ATOM   1983 O  O   . GLY B 2 119 ? 35.856  5.078   35.849 1.00 16.48 ? 119 GLY B O   1
+ATOM   1984 N  N   . LYS B 2 120 ? 37.833  5.452   35.098 1.00 19.17 ? 120 LYS B N   1
+ATOM   1985 C  CA  . LYS B 2 120 ? 37.444  4.794   33.789 1.00 27.00 ? 120 LYS B CA  1
+ATOM   1986 C  C   . LYS B 2 120 ? 37.151  3.243   33.898 1.00 25.94 ? 120 LYS B C   1
+ATOM   1987 O  O   . LYS B 2 120 ? 36.407  2.864   32.926 1.00 20.66 ? 120 LYS B O   1
+ATOM   1988 C  CB  . LYS B 2 120 ? 38.717  4.719   32.695 1.00 31.85 ? 120 LYS B CB  1
+ATOM   1989 C  CG  . LYS B 2 120 ? 39.715  3.907   32.983 1.00 36.58 ? 120 LYS B CG  1
+ATOM   1990 C  CD  . LYS B 2 120 ? 40.877  3.964   31.828 1.00 49.76 ? 120 LYS B CD  1
+ATOM   1991 C  CE  . LYS B 2 120 ? 41.776  2.748   32.527 1.00 55.47 ? 120 LYS B CE  1
+ATOM   1992 N  NZ  . LYS B 2 120 ? 42.747  2.136   31.882 1.00 71.03 ? 120 LYS B NZ  1
+ATOM   1993 N  N   . GLU B 2 121 ? 37.349  2.635   34.924 1.00 20.26 ? 121 GLU B N   1
+ATOM   1994 C  CA  . GLU B 2 121 ? 36.843  1.463   35.180 1.00 15.17 ? 121 GLU B CA  1
+ATOM   1995 C  C   . GLU B 2 121 ? 35.221  1.422   35.454 1.00 13.63 ? 121 GLU B C   1
+ATOM   1996 O  O   . GLU B 2 121 ? 34.600  0.299   35.287 1.00 17.16 ? 121 GLU B O   1
+ATOM   1997 C  CB  . GLU B 2 121 ? 37.641  0.681   36.440 1.00 29.40 ? 121 GLU B CB  1
+ATOM   1998 C  CG  . GLU B 2 121 ? 37.776  -0.389  36.350 1.00 50.25 ? 121 GLU B CG  1
+ATOM   1999 C  CD  . GLU B 2 121 ? 38.514  -0.879  38.219 1.00 42.74 ? 121 GLU B CD  1
+ATOM   2000 O  OE1 . GLU B 2 121 ? 37.769  -2.588  38.099 1.00 47.83 ? 121 GLU B OE1 1
+ATOM   2001 O  OE2 . GLU B 2 121 ? 39.522  -0.612  37.786 1.00 34.52 ? 121 GLU B OE2 1
+ATOM   2002 N  N   . PHE B 2 122 ? 34.686  2.592   35.779 1.00 14.63 ? 122 PHE B N   1
+ATOM   2003 C  CA  . PHE B 2 122 ? 33.208  2.598   36.050 1.00 15.34 ? 122 PHE B CA  1
+ATOM   2004 C  C   . PHE B 2 122 ? 32.600  2.904   34.602 1.00 13.61 ? 122 PHE B C   1
+ATOM   2005 O  O   . PHE B 2 122 ? 32.214  3.990   34.311 1.00 14.29 ? 122 PHE B O   1
+ATOM   2006 C  CB  . PHE B 2 122 ? 33.007  3.812   37.059 1.00 12.07 ? 122 PHE B CB  1
+ATOM   2007 C  CG  . PHE B 2 122 ? 31.605  3.616   37.638 1.00 11.02 ? 122 PHE B CG  1
+ATOM   2008 C  CD1 . PHE B 2 122 ? 31.260  2.534   38.386 1.00 16.65 ? 122 PHE B CD1 1
+ATOM   2009 C  CD2 . PHE B 2 122 ? 30.777  4.610   37.392 1.00 10.83 ? 122 PHE B CD2 1
+ATOM   2010 C  CE1 . PHE B 2 122 ? 30.002  2.369   39.056 1.00 13.73 ? 122 PHE B CE1 1
+ATOM   2011 C  CE2 . PHE B 2 122 ? 29.411  4.522   37.920 1.00 12.97 ? 122 PHE B CE2 1
+ATOM   2012 C  CZ  . PHE B 2 122 ? 29.152  3.303   38.695 1.00 16.05 ? 122 PHE B CZ  1
+ATOM   2013 N  N   . THR B 2 123 ? 32.600  1.895   33.880 1.00 18.07 ? 123 THR B N   1
+ATOM   2014 C  CA  . THR B 2 123 ? 32.186  2.047   32.424 1.00 21.03 ? 123 THR B CA  1
+ATOM   2015 C  C   . THR B 2 123 ? 30.529  2.404   32.419 1.00 27.18 ? 123 THR B C   1
+ATOM   2016 O  O   . THR B 2 123 ? 30.008  1.994   33.304 1.00 14.31 ? 123 THR B O   1
+ATOM   2017 C  CB  . THR B 2 123 ? 32.440  0.829   31.675 1.00 19.82 ? 123 THR B CB  1
+ATOM   2018 O  OG1 . THR B 2 123 ? 31.959  -0.285  32.119 1.00 17.47 ? 123 THR B OG1 1
+ATOM   2019 C  CG2 . THR B 2 123 ? 34.001  0.539   31.530 1.00 22.67 ? 123 THR B CG2 1
+ATOM   2020 N  N   . PRO B 2 124 ? 30.151  2.681   31.324 1.00 19.47 ? 124 PRO B N   1
+ATOM   2021 C  CA  . PRO B 2 124 ? 28.633  2.868   31.089 1.00 20.19 ? 124 PRO B CA  1
+ATOM   2022 C  C   . PRO B 2 124 ? 27.998  1.571   31.347 1.00 20.69 ? 124 PRO B C   1
+ATOM   2023 O  O   . PRO B 2 124 ? 26.917  1.728   32.159 1.00 13.34 ? 124 PRO B O   1
+ATOM   2024 C  CB  . PRO B 2 124 ? 28.395  3.364   29.685 1.00 17.09 ? 124 PRO B CB  1
+ATOM   2025 C  CG  . PRO B 2 124 ? 29.748  4.109   29.363 1.00 18.87 ? 124 PRO B CG  1
+ATOM   2026 C  CD  . PRO B 2 124 ? 31.011  3.279   29.986 1.00 24.42 ? 124 PRO B CD  1
+ATOM   2027 N  N   . PRO B 2 125 ? 28.286  0.449   31.039 1.00 16.20 ? 125 PRO B N   1
+ATOM   2028 C  CA  . PRO B 2 125 ? 27.684  -0.856  31.332 1.00 16.84 ? 125 PRO B CA  1
+ATOM   2029 C  C   . PRO B 2 125 ? 27.690  -1.176  32.808 1.00 14.92 ? 125 PRO B C   1
+ATOM   2030 O  O   . PRO B 2 125 ? 26.663  -1.615  33.381 1.00 16.05 ? 125 PRO B O   1
+ATOM   2031 C  CB  . PRO B 2 125 ? 28.185  -2.049  30.625 1.00 19.48 ? 125 PRO B CB  1
+ATOM   2032 C  CG  . PRO B 2 125 ? 28.809  -1.362  29.575 1.00 21.56 ? 125 PRO B CG  1
+ATOM   2033 C  CD  . PRO B 2 125 ? 29.414  -0.069  29.918 1.00 25.73 ? 125 PRO B CD  1
+ATOM   2034 N  N   . VAL B 2 126 ? 28.765  -0.867  33.373 1.00 13.83 ? 126 VAL B N   1
+ATOM   2035 C  CA  . VAL B 2 126 ? 28.840  -1.009  34.813 1.00 19.80 ? 126 VAL B CA  1
+ATOM   2036 C  C   . VAL B 2 126 ? 28.184  0.063   35.537 1.00 14.89 ? 126 VAL B C   1
+ATOM   2037 O  O   . VAL B 2 126 ? 27.330  -0.369  36.578 1.00 13.92 ? 126 VAL B O   1
+ATOM   2038 C  CB  . VAL B 2 126 ? 30.424  -0.798  35.209 1.00 19.55 ? 126 VAL B CB  1
+ATOM   2039 C  CG1 . VAL B 2 126 ? 30.451  -1.057  36.707 1.00 21.55 ? 126 VAL B CG1 1
+ATOM   2040 C  CG2 . VAL B 2 126 ? 31.158  -2.038  34.830 1.00 27.82 ? 126 VAL B CG2 1
+ATOM   2041 N  N   . GLN B 2 127 ? 28.001  1.226   35.276 1.00 13.64 ? 127 GLN B N   1
+ATOM   2042 C  CA  . GLN B 2 127 ? 27.063  2.198   35.706 1.00 9.72  ? 127 GLN B CA  1
+ATOM   2043 C  C   . GLN B 2 127 ? 25.754  1.653   35.823 1.00 16.14 ? 127 GLN B C   1
+ATOM   2044 O  O   . GLN B 2 127 ? 24.830  1.725   36.597 1.00 12.24 ? 127 GLN B O   1
+ATOM   2045 C  CB  . GLN B 2 127 ? 27.221  3.578   35.167 1.00 13.15 ? 127 GLN B CB  1
+ATOM   2046 C  CG  . GLN B 2 127 ? 26.051  4.427   35.657 1.00 13.42 ? 127 GLN B CG  1
+ATOM   2047 C  CD  . GLN B 2 127 ? 26.125  5.650   34.901 1.00 16.28 ? 127 GLN B CD  1
+ATOM   2048 O  OE1 . GLN B 2 127 ? 26.945  6.018   34.026 1.00 16.20 ? 127 GLN B OE1 1
+ATOM   2049 N  NE2 . GLN B 2 127 ? 25.193  6.494   35.246 1.00 19.47 ? 127 GLN B NE2 1
+ATOM   2050 N  N   . ALA B 2 128 ? 25.230  1.263   34.553 1.00 15.15 ? 128 ALA B N   1
+ATOM   2051 C  CA  . ALA B 2 128 ? 23.943  0.688   34.376 1.00 15.02 ? 128 ALA B CA  1
+ATOM   2052 C  C   . ALA B 2 128 ? 23.465  -0.396  35.309 1.00 11.97 ? 128 ALA B C   1
+ATOM   2053 O  O   . ALA B 2 128 ? 22.404  -0.371  35.894 1.00 16.35 ? 128 ALA B O   1
+ATOM   2054 C  CB  . ALA B 2 128 ? 23.720  0.401   32.857 1.00 17.08 ? 128 ALA B CB  1
+ATOM   2055 N  N   . ALA B 2 129 ? 24.308  -1.350  35.606 1.00 13.66 ? 129 ALA B N   1
+ATOM   2056 C  CA  . ALA B 2 129 ? 24.137  -2.397  36.522 1.00 13.76 ? 129 ALA B CA  1
+ATOM   2057 C  C   . ALA B 2 129 ? 24.115  -1.791  37.970 1.00 10.22 ? 129 ALA B C   1
+ATOM   2058 O  O   . ALA B 2 129 ? 23.052  -2.233  38.660 1.00 10.46 ? 129 ALA B O   1
+ATOM   2059 C  CB  . ALA B 2 129 ? 25.227  -3.323  36.466 1.00 13.23 ? 129 ALA B CB  1
+ATOM   2060 N  N   . TYR B 2 130 ? 24.953  -0.861  38.304 1.00 10.66 ? 130 TYR B N   1
+ATOM   2061 C  CA  . TYR B 2 130 ? 24.699  -0.367  39.652 1.00 13.05 ? 130 TYR B CA  1
+ATOM   2062 C  C   . TYR B 2 130 ? 23.477  0.552   39.831 1.00 11.70 ? 130 TYR B C   1
+ATOM   2063 O  O   . TYR B 2 130 ? 22.913  0.650   40.845 1.00 11.83 ? 130 TYR B O   1
+ATOM   2064 C  CB  . TYR B 2 130 ? 25.960  0.538   39.984 1.00 11.97 ? 130 TYR B CB  1
+ATOM   2065 C  CG  . TYR B 2 130 ? 26.969  -0.272  40.746 1.00 13.90 ? 130 TYR B CG  1
+ATOM   2066 C  CD1 . TYR B 2 130 ? 27.053  -0.401  42.107 1.00 15.61 ? 130 TYR B CD1 1
+ATOM   2067 C  CD2 . TYR B 2 130 ? 28.019  -0.794  40.024 1.00 14.18 ? 130 TYR B CD2 1
+ATOM   2068 C  CE1 . TYR B 2 130 ? 27.942  -1.247  42.656 1.00 19.97 ? 130 TYR B CE1 1
+ATOM   2069 C  CE2 . TYR B 2 130 ? 28.984  -1.867  40.700 1.00 19.65 ? 130 TYR B CE2 1
+ATOM   2070 C  CZ  . TYR B 2 130 ? 28.982  -1.768  42.071 1.00 22.28 ? 130 TYR B CZ  1
+ATOM   2071 O  OH  . TYR B 2 130 ? 29.856  -2.624  42.725 1.00 21.52 ? 130 TYR B OH  1
+ATOM   2072 N  N   . GLN B 2 131 ? 23.022  1.228   38.763 1.00 12.03 ? 131 GLN B N   1
+ATOM   2073 C  CA  . GLN B 2 131 ? 21.778  1.837   38.789 1.00 12.03 ? 131 GLN B CA  1
+ATOM   2074 C  C   . GLN B 2 131 ? 20.577  1.009   39.031 1.00 12.76 ? 131 GLN B C   1
+ATOM   2075 O  O   . GLN B 2 131 ? 19.836  1.404   39.992 1.00 15.09 ? 131 GLN B O   1
+ATOM   2076 C  CB  . GLN B 2 131 ? 21.473  2.529   37.496 1.00 14.85 ? 131 GLN B CB  1
+ATOM   2077 C  CG  . GLN B 2 131 ? 22.463  3.744   37.342 1.00 19.57 ? 131 GLN B CG  1
+ATOM   2078 C  CD  . GLN B 2 131 ? 22.222  5.037   38.069 1.00 22.82 ? 131 GLN B CD  1
+ATOM   2079 O  OE1 . GLN B 2 131 ? 23.080  5.884   37.743 1.00 18.44 ? 131 GLN B OE1 1
+ATOM   2080 N  NE2 . GLN B 2 131 ? 21.302  5.379   38.758 1.00 16.43 ? 131 GLN B NE2 1
+ATOM   2081 N  N   . LYS B 2 132 ? 20.642  -0.209  38.501 1.00 12.50 ? 132 LYS B N   1
+ATOM   2082 C  CA  . LYS B 2 132 ? 19.628  -1.158  38.688 1.00 14.23 ? 132 LYS B CA  1
+ATOM   2083 C  C   . LYS B 2 132 ? 19.603  -1.526  40.213 1.00 17.46 ? 132 LYS B C   1
+ATOM   2084 O  O   . LYS B 2 132 ? 18.636  -1.554  41.008 1.00 14.87 ? 132 LYS B O   1
+ATOM   2085 C  CB  . LYS B 2 132 ? 19.703  -2.298  38.028 1.00 19.74 ? 132 LYS B CB  1
+ATOM   2086 C  CG  . LYS B 2 132 ? 19.268  -2.097  36.520 1.00 26.28 ? 132 LYS B CG  1
+ATOM   2087 C  CD  . LYS B 2 132 ? 19.459  -3.362  35.832 1.00 31.58 ? 132 LYS B CD  1
+ATOM   2088 C  CE  . LYS B 2 132 ? 19.150  -2.682  34.349 1.00 32.98 ? 132 LYS B CE  1
+ATOM   2089 N  NZ  . LYS B 2 132 ? 19.296  -4.500  33.885 1.00 37.48 ? 132 LYS B NZ  1
+ATOM   2090 N  N   . VAL B 2 133 ? 20.883  -1.767  40.854 1.00 17.22 ? 133 VAL B N   1
+ATOM   2091 C  CA  . VAL B 2 133 ? 21.078  -2.183  42.204 1.00 11.45 ? 133 VAL B CA  1
+ATOM   2092 C  C   . VAL B 2 133 ? 20.658  -1.126  43.188 1.00 11.90 ? 133 VAL B C   1
+ATOM   2093 O  O   . VAL B 2 133 ? 19.814  -1.391  44.165 1.00 13.71 ? 133 VAL B O   1
+ATOM   2094 C  CB  . VAL B 2 133 ? 22.473  -2.573  42.494 1.00 16.41 ? 133 VAL B CB  1
+ATOM   2095 C  CG1 . VAL B 2 133 ? 22.695  -2.768  43.854 1.00 36.18 ? 133 VAL B CG1 1
+ATOM   2096 C  CG2 . VAL B 2 133 ? 22.782  -3.857  41.663 1.00 15.51 ? 133 VAL B CG2 1
+ATOM   2097 N  N   . VAL B 2 134 ? 20.967  0.166   42.969 1.00 13.21 ? 134 VAL B N   1
+ATOM   2098 C  CA  . VAL B 2 134 ? 20.747  1.185   43.730 1.00 12.26 ? 134 VAL B CA  1
+ATOM   2099 C  C   . VAL B 2 134 ? 19.296  1.364   43.726 1.00 16.19 ? 134 VAL B C   1
+ATOM   2100 O  O   . VAL B 2 134 ? 18.548  1.822   44.782 1.00 17.40 ? 134 VAL B O   1
+ATOM   2101 C  CB  . VAL B 2 134 ? 21.244  2.575   43.789 1.00 11.96 ? 134 VAL B CB  1
+ATOM   2102 C  CG1 . VAL B 2 134 ? 22.708  2.231   44.018 1.00 18.38 ? 134 VAL B CG1 1
+ATOM   2103 C  CG2 . VAL B 2 134 ? 21.229  3.233   42.423 1.00 14.78 ? 134 VAL B CG2 1
+ATOM   2104 N  N   . ALA B 2 135 ? 18.529  1.389   42.550 1.00 13.32 ? 135 ALA B N   1
+ATOM   2105 C  CA  . ALA B 2 135 ? 17.087  1.483   42.500 1.00 21.37 ? 135 ALA B CA  1
+ATOM   2106 C  C   . ALA B 2 135 ? 16.385  0.390   43.301 1.00 17.09 ? 135 ALA B C   1
+ATOM   2107 O  O   . ALA B 2 135 ? 15.325  0.595   43.933 1.00 17.43 ? 135 ALA B O   1
+ATOM   2108 C  CB  . ALA B 2 135 ? 16.671  1.712   41.153 1.00 28.77 ? 135 ALA B CB  1
+ATOM   2109 N  N   . GLY B 2 136 ? 16.821  -0.845  43.230 1.00 18.26 ? 136 GLY B N   1
+ATOM   2110 C  CA  . GLY B 2 136 ? 16.294  -2.144  43.929 1.00 19.82 ? 136 GLY B CA  1
+ATOM   2111 C  C   . GLY B 2 136 ? 16.345  -1.871  45.356 1.00 16.67 ? 136 GLY B C   1
+ATOM   2112 O  O   . GLY B 2 136 ? 15.438  -2.166  46.045 1.00 15.34 ? 136 GLY B O   1
+ATOM   2113 N  N   . VAL B 2 137 ? 17.613  -1.453  45.878 1.00 19.06 ? 137 VAL B N   1
+ATOM   2114 C  CA  . VAL B 2 137 ? 17.706  -1.212  47.261 1.00 13.40 ? 137 VAL B CA  1
+ATOM   2115 C  C   . VAL B 2 137 ? 16.842  -0.110  47.730 1.00 14.98 ? 137 VAL B C   1
+ATOM   2116 O  O   . VAL B 2 137 ? 16.084  -0.308  48.760 1.00 15.32 ? 137 VAL B O   1
+ATOM   2117 C  CB  . VAL B 2 137 ? 19.208  -0.860  47.594 1.00 12.05 ? 137 VAL B CB  1
+ATOM   2118 C  CG1 . VAL B 2 137 ? 19.242  -0.564  49.024 1.00 24.37 ? 137 VAL B CG1 1
+ATOM   2119 C  CG2 . VAL B 2 137 ? 19.986  -2.076  47.196 1.00 11.44 ? 137 VAL B CG2 1
+ATOM   2120 N  N   . ALA B 2 138 ? 16.582  0.983   47.051 1.00 14.63 ? 138 ALA B N   1
+ATOM   2121 C  CA  . ALA B 2 138 ? 15.669  2.054   47.422 1.00 14.97 ? 138 ALA B CA  1
+ATOM   2122 C  C   . ALA B 2 138 ? 14.323  1.579   47.621 1.00 14.00 ? 138 ALA B C   1
+ATOM   2123 O  O   . ALA B 2 138 ? 13.443  1.860   48.406 1.00 15.18 ? 138 ALA B O   1
+ATOM   2124 C  CB  . ALA B 2 138 ? 15.791  3.182   46.492 1.00 21.60 ? 138 ALA B CB  1
+ATOM   2125 N  N   . ASN B 2 139 ? 13.929  0.927   46.472 1.00 14.76 ? 139 ASN B N   1
+ATOM   2126 C  CA  . ASN B 2 139 ? 12.524  0.326   46.511 1.00 19.56 ? 139 ASN B CA  1
+ATOM   2127 C  C   . ASN B 2 139 ? 12.207  -0.857  47.450 1.00 16.64 ? 139 ASN B C   1
+ATOM   2128 O  O   . ASN B 2 139 ? 11.238  -0.716  48.124 1.00 15.66 ? 139 ASN B O   1
+ATOM   2129 C  CB  . ASN B 2 139 ? 12.246  -0.607  45.179 1.00 32.30 ? 139 ASN B CB  1
+ATOM   2130 C  CG  . ASN B 2 139 ? 12.022  -0.138  44.774 1.00 58.46 ? 139 ASN B CG  1
+ATOM   2131 O  OD1 . ASN B 2 139 ? 11.927  1.326   44.175 1.00 49.38 ? 139 ASN B OD1 1
+ATOM   2132 N  ND2 . ASN B 2 139 ? 12.448  0.081   42.819 1.00 59.02 ? 139 ASN B ND2 1
+ATOM   2133 N  N   . ALA B 2 140 ? 13.329  -1.535  47.917 1.00 12.53 ? 140 ALA B N   1
+ATOM   2134 C  CA  . ALA B 2 140 ? 13.134  -2.493  48.899 1.00 19.39 ? 140 ALA B CA  1
+ATOM   2135 C  C   . ALA B 2 140 ? 13.131  -1.747  50.190 1.00 15.37 ? 140 ALA B C   1
+ATOM   2136 O  O   . ALA B 2 140 ? 12.315  -2.151  51.168 1.00 15.92 ? 140 ALA B O   1
+ATOM   2137 C  CB  . ALA B 2 140 ? 14.408  -3.543  48.977 1.00 22.20 ? 140 ALA B CB  1
+ATOM   2138 N  N   . LEU B 2 141 ? 13.770  -0.735  50.537 1.00 12.47 ? 141 LEU B N   1
+ATOM   2139 C  CA  . LEU B 2 141 ? 13.729  0.097   51.695 1.00 15.63 ? 141 LEU B CA  1
+ATOM   2140 C  C   . LEU B 2 141 ? 12.380  0.588   51.872 1.00 21.66 ? 141 LEU B C   1
+ATOM   2141 O  O   . LEU B 2 141 ? 11.950  1.162   52.919 1.00 17.40 ? 141 LEU B O   1
+ATOM   2142 C  CB  . LEU B 2 141 ? 14.921  0.942   51.906 1.00 15.12 ? 141 LEU B CB  1
+ATOM   2143 C  CG  . LEU B 2 141 ? 16.109  0.356   52.467 1.00 17.02 ? 141 LEU B CG  1
+ATOM   2144 C  CD1 . LEU B 2 141 ? 17.216  1.388   52.514 1.00 19.94 ? 141 LEU B CD1 1
+ATOM   2145 C  CD2 . LEU B 2 141 ? 16.088  -0.046  53.879 1.00 21.74 ? 141 LEU B CD2 1
+ATOM   2146 N  N   . ALA B 2 142 ? 11.734  1.042   50.715 1.00 12.86 ? 142 ALA B N   1
+ATOM   2147 C  CA  . ALA B 2 142 ? 10.616  1.841   50.701 1.00 14.61 ? 142 ALA B CA  1
+ATOM   2148 C  C   . ALA B 2 142 ? 9.219   0.685   50.868 1.00 20.31 ? 142 ALA B C   1
+ATOM   2149 O  O   . ALA B 2 142 ? 8.120   1.456   51.083 1.00 18.06 ? 142 ALA B O   1
+ATOM   2150 C  CB  . ALA B 2 142 ? 10.361  2.736   49.492 1.00 21.40 ? 142 ALA B CB  1
+ATOM   2151 N  N   . HIS B 2 143 ? 9.474   -0.423  50.699 1.00 17.95 ? 143 HIS B N   1
+ATOM   2152 C  CA  . HIS B 2 143 ? 8.444   -1.540  50.352 1.00 26.37 ? 143 HIS B CA  1
+ATOM   2153 C  C   . HIS B 2 143 ? 7.295   -1.440  51.687 1.00 19.76 ? 143 HIS B C   1
+ATOM   2154 O  O   . HIS B 2 143 ? 6.112   -1.718  51.417 1.00 21.59 ? 143 HIS B O   1
+ATOM   2155 C  CB  . HIS B 2 143 ? 8.998   -2.781  50.250 1.00 35.96 ? 143 HIS B CB  1
+ATOM   2156 C  CG  . HIS B 2 143 ? 7.765   -3.902  49.751 1.00 57.59 ? 143 HIS B CG  1
+ATOM   2157 N  ND1 . HIS B 2 143 ? 8.002   -4.786  51.186 1.00 48.44 ? 143 HIS B ND1 1
+ATOM   2158 C  CD2 . HIS B 2 143 ? 7.156   -3.540  48.815 1.00 54.87 ? 143 HIS B CD2 1
+ATOM   2159 C  CE1 . HIS B 2 143 ? 6.759   -5.456  49.788 1.00 74.03 ? 143 HIS B CE1 1
+ATOM   2160 N  NE2 . HIS B 2 143 ? 6.180   -4.518  48.682 1.00 57.99 ? 143 HIS B NE2 1
+ATOM   2161 N  N   . LYS B 2 144 ? 7.795   -1.252  52.873 1.00 18.69 ? 144 LYS B N   1
+ATOM   2162 C  CA  . LYS B 2 144 ? 6.882   -1.448  53.988 1.00 14.86 ? 144 LYS B CA  1
+ATOM   2163 C  C   . LYS B 2 144 ? 6.429   -0.210  54.295 1.00 16.55 ? 144 LYS B C   1
+ATOM   2164 O  O   . LYS B 2 144 ? 5.773   -0.087  55.489 1.00 18.03 ? 144 LYS B O   1
+ATOM   2165 C  CB  . LYS B 2 144 ? 7.761   -2.127  55.021 1.00 17.13 ? 144 LYS B CB  1
+ATOM   2166 C  CG  . LYS B 2 144 ? 7.912   -3.743  54.642 1.00 20.99 ? 144 LYS B CG  1
+ATOM   2167 C  CD  . LYS B 2 144 ? 6.927   -4.649  54.980 1.00 34.56 ? 144 LYS B CD  1
+ATOM   2168 C  CE  . LYS B 2 144 ? 5.890   -6.268  55.554 1.00 62.41 ? 144 LYS B CE  1
+ATOM   2169 N  NZ  . LYS B 2 144 ? 6.963   -6.953  57.087 1.00 62.40 ? 144 LYS B NZ  1
+ATOM   2170 N  N   . TYR B 2 145 ? 6.580   0.942   53.895 1.00 19.33 ? 145 TYR B N   1
+ATOM   2171 C  CA  . TYR B 2 145 ? 6.088   2.279   54.004 1.00 25.80 ? 145 TYR B CA  1
+ATOM   2172 C  C   . TYR B 2 145 ? 4.352   2.273   54.218 1.00 37.10 ? 145 TYR B C   1
+ATOM   2173 O  O   . TYR B 2 145 ? 4.002   1.435   53.221 1.00 25.59 ? 145 TYR B O   1
+ATOM   2174 C  CB  . TYR B 2 145 ? 6.540   3.388   53.530 1.00 20.19 ? 145 TYR B CB  1
+ATOM   2175 C  CG  . TYR B 2 145 ? 7.984   4.002   53.941 1.00 16.11 ? 145 TYR B CG  1
+ATOM   2176 C  CD1 . TYR B 2 145 ? 8.011   5.228   54.513 1.00 13.84 ? 145 TYR B CD1 1
+ATOM   2177 C  CD2 . TYR B 2 145 ? 8.900   2.987   53.861 1.00 19.35 ? 145 TYR B CD2 1
+ATOM   2178 C  CE1 . TYR B 2 145 ? 9.122   5.680   54.975 1.00 14.00 ? 145 TYR B CE1 1
+ATOM   2179 C  CE2 . TYR B 2 145 ? 10.301  3.462   54.525 1.00 16.15 ? 145 TYR B CE2 1
+ATOM   2180 C  CZ  . TYR B 2 145 ? 10.429  4.819   55.044 1.00 11.23 ? 145 TYR B CZ  1
+ATOM   2181 O  OH  . TYR B 2 145 ? 11.654  5.281   55.305 1.00 11.07 ? 145 TYR B OH  1
+ATOM   2182 N  N   . HIS B 2 146 ? 3.837   2.750   54.887 1.00 22.40 ? 146 HIS B N   1
+ATOM   2183 C  CA  . HIS B 2 146 ? 2.231   2.924   55.194 1.00 24.36 ? 146 HIS B CA  1
+ATOM   2184 C  C   . HIS B 2 146 ? 1.887   4.073   55.859 1.00 19.29 ? 146 HIS B C   1
+ATOM   2185 O  O   . HIS B 2 146 ? 2.796   4.816   56.420 1.00 20.20 ? 146 HIS B O   1
+ATOM   2186 C  CB  . HIS B 2 146 ? 1.811   1.603   55.768 1.00 17.91 ? 146 HIS B CB  1
+ATOM   2187 C  CG  . HIS B 2 146 ? 1.964   2.037   57.761 1.00 30.29 ? 146 HIS B CG  1
+ATOM   2188 N  ND1 . HIS B 2 146 ? 1.691   1.180   58.151 1.00 56.02 ? 146 HIS B ND1 1
+ATOM   2189 C  CD2 . HIS B 2 146 ? 3.500   1.506   57.819 1.00 32.02 ? 146 HIS B CD2 1
+ATOM   2190 C  CE1 . HIS B 2 146 ? 2.501   0.959   59.788 1.00 45.40 ? 146 HIS B CE1 1
+ATOM   2191 N  NE2 . HIS B 2 146 ? 3.352   1.790   59.196 1.00 35.25 ? 146 HIS B NE2 1
+ATOM   2192 O  OXT . HIS B 2 146 ? 0.693   4.385   55.848 1.00 28.98 ? 146 HIS B OXT 1
+ATOM   2193 N  N   . VAL C 1 1   ? 5.540   29.983  34.085 1.00 53.78 ? 1   VAL C N   1
+ATOM   2194 C  CA  . VAL C 1 1   ? 5.845   32.286  33.885 1.00 39.83 ? 1   VAL C CA  1
+ATOM   2195 C  C   . VAL C 1 1   ? 4.073   32.400  33.434 1.00 29.73 ? 1   VAL C C   1
+ATOM   2196 O  O   . VAL C 1 1   ? 3.314   31.736  32.624 1.00 31.20 ? 1   VAL C O   1
+ATOM   2197 C  CB  . VAL C 1 1   ? 6.279   31.688  32.877 1.00 52.94 ? 1   VAL C CB  1
+ATOM   2198 C  CG1 . VAL C 1 1   ? 5.941   33.809  32.322 1.00 47.73 ? 1   VAL C CG1 1
+ATOM   2199 C  CG2 . VAL C 1 1   ? 7.884   33.561  33.163 1.00 67.01 ? 1   VAL C CG2 1
+ATOM   2200 N  N   . LEU C 1 2   ? 3.466   33.064  34.360 1.00 33.50 ? 2   LEU C N   1
+ATOM   2201 C  CA  . LEU C 1 2   ? 2.119   33.120  34.564 1.00 35.54 ? 2   LEU C CA  1
+ATOM   2202 C  C   . LEU C 1 2   ? 1.461   34.272  33.361 1.00 25.83 ? 2   LEU C C   1
+ATOM   2203 O  O   . LEU C 1 2   ? 2.042   35.373  33.863 1.00 37.30 ? 2   LEU C O   1
+ATOM   2204 C  CB  . LEU C 1 2   ? 1.762   33.547  35.812 1.00 38.49 ? 2   LEU C CB  1
+ATOM   2205 C  CG  . LEU C 1 2   ? 1.567   32.274  36.861 1.00 34.89 ? 2   LEU C CG  1
+ATOM   2206 C  CD1 . LEU C 1 2   ? 1.497   32.614  38.058 1.00 40.00 ? 2   LEU C CD1 1
+ATOM   2207 C  CD2 . LEU C 1 2   ? 1.175   31.161  36.473 1.00 36.30 ? 2   LEU C CD2 1
+ATOM   2208 N  N   . SER C 1 3   ? 0.885   33.930  32.371 1.00 20.82 ? 3   SER C N   1
+ATOM   2209 C  CA  . SER C 1 3   ? 0.274   34.937  31.507 1.00 16.99 ? 3   SER C CA  1
+ATOM   2210 C  C   . SER C 1 3   ? -0.660  35.703  32.287 1.00 19.86 ? 3   SER C C   1
+ATOM   2211 O  O   . SER C 1 3   ? -1.379  35.373  33.257 1.00 23.30 ? 3   SER C O   1
+ATOM   2212 C  CB  . SER C 1 3   ? -0.065  34.183  30.371 1.00 21.69 ? 3   SER C CB  1
+ATOM   2213 O  OG  . SER C 1 3   ? -1.298  33.584  30.548 1.00 24.96 ? 3   SER C OG  1
+ATOM   2214 N  N   . PRO C 1 4   ? -1.281  36.868  31.684 1.00 27.73 ? 4   PRO C N   1
+ATOM   2215 C  CA  . PRO C 1 4   ? -2.231  37.566  32.130 1.00 18.30 ? 4   PRO C CA  1
+ATOM   2216 C  C   . PRO C 1 4   ? -3.635  36.714  32.222 1.00 21.79 ? 4   PRO C C   1
+ATOM   2217 O  O   . PRO C 1 4   ? -4.300  36.837  33.171 1.00 30.78 ? 4   PRO C O   1
+ATOM   2218 C  CB  . PRO C 1 4   ? -2.428  38.831  31.107 1.00 35.17 ? 4   PRO C CB  1
+ATOM   2219 C  CG  . PRO C 1 4   ? -0.947  38.937  30.529 1.00 39.10 ? 4   PRO C CG  1
+ATOM   2220 C  CD  . PRO C 1 4   ? -0.364  37.496  30.672 1.00 33.69 ? 4   PRO C CD  1
+ATOM   2221 N  N   . ALA C 1 5   ? -3.565  35.986  31.246 1.00 20.53 ? 5   ALA C N   1
+ATOM   2222 C  CA  . ALA C 1 5   ? -4.728  35.027  31.236 1.00 15.17 ? 5   ALA C CA  1
+ATOM   2223 C  C   . ALA C 1 5   ? -4.768  34.125  32.631 1.00 17.36 ? 5   ALA C C   1
+ATOM   2224 O  O   . ALA C 1 5   ? -5.719  33.702  33.140 1.00 18.86 ? 5   ALA C O   1
+ATOM   2225 C  CB  . ALA C 1 5   ? -5.084  34.190  30.055 1.00 14.70 ? 5   ALA C CB  1
+ATOM   2226 N  N   . ASP C 1 6   ? -3.589  33.505  32.635 1.00 17.28 ? 6   ASP C N   1
+ATOM   2227 C  CA  . ASP C 1 6   ? -3.344  32.617  33.787 1.00 13.65 ? 6   ASP C CA  1
+ATOM   2228 C  C   . ASP C 1 6   ? -3.813  33.321  35.084 1.00 16.19 ? 6   ASP C C   1
+ATOM   2229 O  O   . ASP C 1 6   ? -4.369  32.669  36.015 1.00 18.77 ? 6   ASP C O   1
+ATOM   2230 C  CB  . ASP C 1 6   ? -1.888  32.151  33.930 1.00 14.90 ? 6   ASP C CB  1
+ATOM   2231 C  CG  . ASP C 1 6   ? -1.558  31.130  32.826 1.00 15.46 ? 6   ASP C CG  1
+ATOM   2232 O  OD1 . ASP C 1 6   ? -2.478  30.188  32.398 1.00 20.59 ? 6   ASP C OD1 1
+ATOM   2233 O  OD2 . ASP C 1 6   ? -0.384  31.136  32.528 1.00 19.80 ? 6   ASP C OD2 1
+ATOM   2234 N  N   . LYS C 1 7   ? -3.272  34.523  35.173 1.00 17.95 ? 7   LYS C N   1
+ATOM   2235 C  CA  . LYS C 1 7   ? -3.751  35.483  36.555 1.00 25.53 ? 7   LYS C CA  1
+ATOM   2236 C  C   . LYS C 1 7   ? -4.881  35.555  36.905 1.00 19.12 ? 7   LYS C C   1
+ATOM   2237 O  O   . LYS C 1 7   ? -5.554  35.358  37.811 1.00 19.71 ? 7   LYS C O   1
+ATOM   2238 C  CB  . LYS C 1 7   ? -2.782  36.578  36.490 1.00 27.50 ? 7   LYS C CB  1
+ATOM   2239 C  CG  . LYS C 1 7   ? -1.409  36.284  36.193 1.00 53.71 ? 7   LYS C CG  1
+ATOM   2240 C  CD  . LYS C 1 7   ? -0.226  37.637  36.941 1.00 60.72 ? 7   LYS C CD  1
+ATOM   2241 C  CE  . LYS C 1 7   ? 0.556   37.739  36.022 1.00 63.74 ? 7   LYS C CE  1
+ATOM   2242 N  NZ  . LYS C 1 7   ? 1.514   38.295  35.577 1.00 80.12 ? 7   LYS C NZ  1
+ATOM   2243 N  N   . THR C 1 8   ? -5.600  35.904  35.627 1.00 18.59 ? 8   THR C N   1
+ATOM   2244 C  CA  . THR C 1 8   ? -7.111  35.935  35.708 1.00 17.68 ? 8   THR C CA  1
+ATOM   2245 C  C   . THR C 1 8   ? -7.830  34.912  36.149 1.00 15.92 ? 8   THR C C   1
+ATOM   2246 O  O   . THR C 1 8   ? -8.746  34.904  36.940 1.00 18.11 ? 8   THR C O   1
+ATOM   2247 C  CB  . THR C 1 8   ? -7.671  36.597  34.086 1.00 18.41 ? 8   THR C CB  1
+ATOM   2248 O  OG1 . THR C 1 8   ? -7.057  37.816  34.129 1.00 22.00 ? 8   THR C OG1 1
+ATOM   2249 C  CG2 . THR C 1 8   ? -8.957  36.916  34.252 1.00 19.72 ? 8   THR C CG2 1
+ATOM   2250 N  N   . ASN C 1 9   ? -7.429  33.704  35.553 1.00 14.52 ? 9   ASN C N   1
+ATOM   2251 C  CA  . ASN C 1 9   ? -7.931  32.304  35.865 1.00 11.76 ? 9   ASN C CA  1
+ATOM   2252 C  C   . ASN C 1 9   ? -7.759  31.911  37.241 1.00 13.43 ? 9   ASN C C   1
+ATOM   2253 O  O   . ASN C 1 9   ? -8.726  31.508  37.930 1.00 14.77 ? 9   ASN C O   1
+ATOM   2254 C  CB  . ASN C 1 9   ? -7.425  31.238  34.829 1.00 15.52 ? 9   ASN C CB  1
+ATOM   2255 C  CG  . ASN C 1 9   ? -8.078  31.135  33.453 1.00 21.23 ? 9   ASN C CG  1
+ATOM   2256 O  OD1 . ASN C 1 9   ? -9.036  31.839  33.320 1.00 17.78 ? 9   ASN C OD1 1
+ATOM   2257 N  ND2 . ASN C 1 9   ? -7.321  30.799  32.610 1.00 16.93 ? 9   ASN C ND2 1
+ATOM   2258 N  N   . VAL C 1 10  ? -6.600  32.228  37.664 1.00 15.37 ? 10  VAL C N   1
+ATOM   2259 C  CA  . VAL C 1 10  ? -6.328  31.915  39.012 1.00 15.09 ? 10  VAL C CA  1
+ATOM   2260 C  C   . VAL C 1 10  ? -7.145  32.895  40.299 1.00 19.82 ? 10  VAL C C   1
+ATOM   2261 O  O   . VAL C 1 10  ? -7.619  32.223  41.099 1.00 21.55 ? 10  VAL C O   1
+ATOM   2262 C  CB  . VAL C 1 10  ? -4.831  32.028  39.355 1.00 23.83 ? 10  VAL C CB  1
+ATOM   2263 C  CG1 . VAL C 1 10  ? -4.386  31.675  40.908 1.00 26.38 ? 10  VAL C CG1 1
+ATOM   2264 C  CG2 . VAL C 1 10  ? -4.096  30.933  38.607 1.00 22.96 ? 10  VAL C CG2 1
+ATOM   2265 N  N   . LYS C 1 11  ? -7.146  34.124  39.921 1.00 19.06 ? 11  LYS C N   1
+ATOM   2266 C  CA  . LYS C 1 11  ? -8.100  34.998  40.673 1.00 21.27 ? 11  LYS C CA  1
+ATOM   2267 C  C   . LYS C 1 11  ? -9.313  34.765  40.704 1.00 24.36 ? 11  LYS C C   1
+ATOM   2268 O  O   . LYS C 1 11  ? -10.096 34.565  41.636 1.00 26.88 ? 11  LYS C O   1
+ATOM   2269 C  CB  . LYS C 1 11  ? -7.549  36.329  40.437 1.00 24.11 ? 11  LYS C CB  1
+ATOM   2270 C  CG  . LYS C 1 11  ? -6.216  36.879  40.591 1.00 39.96 ? 11  LYS C CG  1
+ATOM   2271 C  CD  . LYS C 1 11  ? -6.192  38.396  40.319 1.00 36.60 ? 11  LYS C CD  1
+ATOM   2272 C  CE  . LYS C 1 11  ? -5.013  38.953  40.465 1.00 40.99 ? 11  LYS C CE  1
+ATOM   2273 N  NZ  . LYS C 1 11  ? -4.163  39.646  38.897 1.00 57.68 ? 11  LYS C NZ  1
+ATOM   2274 N  N   . ALA C 1 12  ? -9.820  34.358  39.473 1.00 26.89 ? 12  ALA C N   1
+ATOM   2275 C  CA  . ALA C 1 12  ? -11.033 33.860  39.531 1.00 22.80 ? 12  ALA C CA  1
+ATOM   2276 C  C   . ALA C 1 12  ? -11.669 32.905  40.303 1.00 22.96 ? 12  ALA C C   1
+ATOM   2277 O  O   . ALA C 1 12  ? -12.618 32.557  41.227 1.00 25.17 ? 12  ALA C O   1
+ATOM   2278 C  CB  . ALA C 1 12  ? -11.715 33.630  38.320 1.00 30.68 ? 12  ALA C CB  1
+ATOM   2279 N  N   . ALA C 1 13  ? -10.866 31.601  40.085 1.00 19.81 ? 13  ALA C N   1
+ATOM   2280 C  CA  . ALA C 1 13  ? -10.918 30.303  40.760 1.00 20.52 ? 13  ALA C CA  1
+ATOM   2281 C  C   . ALA C 1 13  ? -10.841 30.520  42.190 1.00 17.10 ? 13  ALA C C   1
+ATOM   2282 O  O   . ALA C 1 13  ? -11.728 29.997  43.038 1.00 22.70 ? 13  ALA C O   1
+ATOM   2283 C  CB  . ALA C 1 13  ? -10.079 29.298  40.142 1.00 20.00 ? 13  ALA C CB  1
+ATOM   2284 N  N   . TRP C 1 14  ? -9.726  31.117  42.725 1.00 18.93 ? 14  TRP C N   1
+ATOM   2285 C  CA  . TRP C 1 14  ? -9.418  31.151  44.177 1.00 19.61 ? 14  TRP C CA  1
+ATOM   2286 C  C   . TRP C 1 14  ? -10.387 32.105  44.718 1.00 29.50 ? 14  TRP C C   1
+ATOM   2287 O  O   . TRP C 1 14  ? -11.065 31.943  45.914 1.00 22.89 ? 14  TRP C O   1
+ATOM   2288 C  CB  . TRP C 1 14  ? -8.169  31.928  44.377 1.00 20.94 ? 14  TRP C CB  1
+ATOM   2289 C  CG  . TRP C 1 14  ? -7.649  31.375  45.621 1.00 20.44 ? 14  TRP C CG  1
+ATOM   2290 C  CD1 . TRP C 1 14  ? -7.709  32.443  46.772 1.00 25.06 ? 14  TRP C CD1 1
+ATOM   2291 C  CD2 . TRP C 1 14  ? -7.161  30.069  45.988 1.00 19.23 ? 14  TRP C CD2 1
+ATOM   2292 N  NE1 . TRP C 1 14  ? -7.038  31.497  47.684 1.00 26.03 ? 14  TRP C NE1 1
+ATOM   2293 C  CE2 . TRP C 1 14  ? -6.842  30.284  47.514 1.00 27.20 ? 14  TRP C CE2 1
+ATOM   2294 C  CE3 . TRP C 1 14  ? -7.086  29.017  45.404 1.00 24.26 ? 14  TRP C CE3 1
+ATOM   2295 C  CZ2 . TRP C 1 14  ? -6.557  29.128  48.102 1.00 29.42 ? 14  TRP C CZ2 1
+ATOM   2296 C  CZ3 . TRP C 1 14  ? -6.673  27.709  45.944 1.00 27.47 ? 14  TRP C CZ3 1
+ATOM   2297 C  CH2 . TRP C 1 14  ? -6.477  28.031  47.627 1.00 31.11 ? 14  TRP C CH2 1
+ATOM   2298 N  N   . GLY C 1 15  ? -11.067 33.012  44.312 1.00 39.26 ? 15  GLY C N   1
+ATOM   2299 C  CA  . GLY C 1 15  ? -12.200 33.991  44.321 1.00 27.60 ? 15  GLY C CA  1
+ATOM   2300 C  C   . GLY C 1 15  ? -13.348 33.145  44.695 1.00 35.88 ? 15  GLY C C   1
+ATOM   2301 O  O   . GLY C 1 15  ? -13.899 33.251  46.165 1.00 44.35 ? 15  GLY C O   1
+ATOM   2302 N  N   . LYS C 1 16  ? -13.796 32.301  44.169 1.00 34.61 ? 16  LYS C N   1
+ATOM   2303 C  CA  . LYS C 1 16  ? -14.921 31.376  43.828 1.00 36.98 ? 16  LYS C CA  1
+ATOM   2304 C  C   . LYS C 1 16  ? -14.668 30.334  45.295 1.00 26.09 ? 16  LYS C C   1
+ATOM   2305 O  O   . LYS C 1 16  ? -15.530 29.816  46.013 1.00 33.01 ? 16  LYS C O   1
+ATOM   2306 C  CB  . LYS C 1 16  ? -15.493 30.617  42.732 1.00 27.30 ? 16  LYS C CB  1
+ATOM   2307 C  CG  . LYS C 1 16  ? -17.229 31.274  42.187 1.00 50.84 ? 16  LYS C CG  1
+ATOM   2308 C  CD  . LYS C 1 16  ? -17.588 29.602  42.783 1.00 68.28 ? 16  LYS C CD  1
+ATOM   2309 C  CE  . LYS C 1 16  ? -19.795 29.751  43.035 1.00 73.16 ? 16  LYS C CE  1
+ATOM   2310 N  NZ  . LYS C 1 16  ? -19.621 28.381  44.042 1.00 69.52 ? 16  LYS C NZ  1
+ATOM   2311 N  N   . VAL C 1 17  ? -13.345 30.285  45.759 1.00 35.88 ? 17  VAL C N   1
+ATOM   2312 C  CA  . VAL C 1 17  ? -12.923 29.473  46.874 1.00 27.62 ? 17  VAL C CA  1
+ATOM   2313 C  C   . VAL C 1 17  ? -13.619 30.083  47.919 1.00 30.67 ? 17  VAL C C   1
+ATOM   2314 O  O   . VAL C 1 17  ? -14.308 29.630  49.026 1.00 29.27 ? 17  VAL C O   1
+ATOM   2315 C  CB  . VAL C 1 17  ? -11.403 28.794  46.973 1.00 24.84 ? 17  VAL C CB  1
+ATOM   2316 C  CG1 . VAL C 1 17  ? -11.134 28.602  48.246 1.00 24.66 ? 17  VAL C CG1 1
+ATOM   2317 C  CG2 . VAL C 1 17  ? -11.269 27.706  45.733 1.00 36.95 ? 17  VAL C CG2 1
+ATOM   2318 N  N   . GLY C 1 18  ? -12.886 31.393  48.035 1.00 37.42 ? 18  GLY C N   1
+ATOM   2319 C  CA  . GLY C 1 18  ? -13.566 32.147  49.231 1.00 36.79 ? 18  GLY C CA  1
+ATOM   2320 C  C   . GLY C 1 18  ? -13.170 31.930  50.514 1.00 35.54 ? 18  GLY C C   1
+ATOM   2321 O  O   . GLY C 1 18  ? -12.001 31.272  50.982 1.00 34.05 ? 18  GLY C O   1
+ATOM   2322 N  N   . ALA C 1 19  ? -14.429 31.877  51.106 1.00 30.07 ? 19  ALA C N   1
+ATOM   2323 C  CA  . ALA C 1 19  ? -14.214 31.564  52.388 1.00 42.34 ? 19  ALA C CA  1
+ATOM   2324 C  C   . ALA C 1 19  ? -14.168 30.165  52.791 1.00 38.75 ? 19  ALA C C   1
+ATOM   2325 O  O   . ALA C 1 19  ? -13.768 29.539  54.021 1.00 34.11 ? 19  ALA C O   1
+ATOM   2326 C  CB  . ALA C 1 19  ? -15.311 32.082  53.094 1.00 49.98 ? 19  ALA C CB  1
+ATOM   2327 N  N   . HIS C 1 20  ? -14.286 29.085  51.940 1.00 27.23 ? 20  HIS C N   1
+ATOM   2328 C  CA  . HIS C 1 20  ? -14.083 27.577  52.200 1.00 31.96 ? 20  HIS C CA  1
+ATOM   2329 C  C   . HIS C 1 20  ? -12.499 27.269  52.098 1.00 24.34 ? 20  HIS C C   1
+ATOM   2330 O  O   . HIS C 1 20  ? -12.227 26.000  52.209 1.00 23.07 ? 20  HIS C O   1
+ATOM   2331 C  CB  . HIS C 1 20  ? -14.624 26.932  51.107 1.00 47.99 ? 20  HIS C CB  1
+ATOM   2332 C  CG  . HIS C 1 20  ? -16.284 27.113  50.754 1.00 49.70 ? 20  HIS C CG  1
+ATOM   2333 N  ND1 . HIS C 1 20  ? -16.816 26.491  52.180 1.00 46.00 ? 20  HIS C ND1 1
+ATOM   2334 C  CD2 . HIS C 1 20  ? -16.967 28.106  50.273 1.00 46.72 ? 20  HIS C CD2 1
+ATOM   2335 C  CE1 . HIS C 1 20  ? -18.391 27.294  51.929 1.00 49.28 ? 20  HIS C CE1 1
+ATOM   2336 N  NE2 . HIS C 1 20  ? -18.093 27.951  50.536 1.00 51.94 ? 20  HIS C NE2 1
+ATOM   2337 N  N   . ALA C 1 21  ? -11.683 28.217  51.671 1.00 28.71 ? 21  ALA C N   1
+ATOM   2338 C  CA  . ALA C 1 21  ? -10.191 27.959  51.518 1.00 32.59 ? 21  ALA C CA  1
+ATOM   2339 C  C   . ALA C 1 21  ? -9.535  27.165  52.686 1.00 33.22 ? 21  ALA C C   1
+ATOM   2340 O  O   . ALA C 1 21  ? -9.040  26.045  52.231 1.00 25.05 ? 21  ALA C O   1
+ATOM   2341 C  CB  . ALA C 1 21  ? -9.677  29.391  51.272 1.00 28.99 ? 21  ALA C CB  1
+ATOM   2342 N  N   . GLY C 1 22  ? -9.737  27.260  53.831 1.00 30.50 ? 22  GLY C N   1
+ATOM   2343 C  CA  . GLY C 1 22  ? -9.401  26.437  54.901 1.00 25.20 ? 22  GLY C CA  1
+ATOM   2344 C  C   . GLY C 1 22  ? -9.918  25.352  54.898 1.00 28.87 ? 22  GLY C C   1
+ATOM   2345 O  O   . GLY C 1 22  ? -9.221  24.169  55.031 1.00 21.09 ? 22  GLY C O   1
+ATOM   2346 N  N   . GLU C 1 23  ? -11.189 24.753  54.705 1.00 19.95 ? 23  GLU C N   1
+ATOM   2347 C  CA  . GLU C 1 23  ? -11.784 23.593  54.641 1.00 21.38 ? 23  GLU C CA  1
+ATOM   2348 C  C   . GLU C 1 23  ? -11.015 22.700  53.407 1.00 15.02 ? 23  GLU C C   1
+ATOM   2349 O  O   . GLU C 1 23  ? -10.842 21.432  53.518 1.00 16.54 ? 23  GLU C O   1
+ATOM   2350 C  CB  . GLU C 1 23  ? -13.361 23.641  54.229 1.00 29.82 ? 23  GLU C CB  1
+ATOM   2351 C  CG  . GLU C 1 23  ? -13.962 22.385  54.659 1.00 36.93 ? 23  GLU C CG  1
+ATOM   2352 C  CD  . GLU C 1 23  ? -15.965 23.172  54.601 1.00 80.12 ? 23  GLU C CD  1
+ATOM   2353 O  OE1 . GLU C 1 23  ? -15.865 21.949  52.569 1.00 66.02 ? 23  GLU C OE1 1
+ATOM   2354 O  OE2 . GLU C 1 23  ? -15.635 23.864  54.184 1.00 59.79 ? 23  GLU C OE2 1
+ATOM   2355 N  N   . TYR C 1 24  ? -10.983 23.452  52.311 1.00 21.28 ? 24  TYR C N   1
+ATOM   2356 C  CA  . TYR C 1 24  ? -10.338 22.880  51.194 1.00 19.46 ? 24  TYR C CA  1
+ATOM   2357 C  C   . TYR C 1 24  ? -8.826  22.313  51.411 1.00 15.33 ? 24  TYR C C   1
+ATOM   2358 O  O   . TYR C 1 24  ? -8.279  21.460  50.939 1.00 13.77 ? 24  TYR C O   1
+ATOM   2359 C  CB  . TYR C 1 24  ? -10.529 23.603  49.963 1.00 16.14 ? 24  TYR C CB  1
+ATOM   2360 C  CG  . TYR C 1 24  ? -11.962 23.899  49.423 1.00 13.71 ? 24  TYR C CG  1
+ATOM   2361 C  CD1 . TYR C 1 24  ? -11.977 24.808  48.190 1.00 24.76 ? 24  TYR C CD1 1
+ATOM   2362 C  CD2 . TYR C 1 24  ? -12.971 23.201  50.098 1.00 21.84 ? 24  TYR C CD2 1
+ATOM   2363 C  CE1 . TYR C 1 24  ? -13.434 25.120  48.002 1.00 25.66 ? 24  TYR C CE1 1
+ATOM   2364 C  CE2 . TYR C 1 24  ? -14.423 23.495  49.620 1.00 17.49 ? 24  TYR C CE2 1
+ATOM   2365 C  CZ  . TYR C 1 24  ? -14.222 24.322  48.539 1.00 27.32 ? 24  TYR C CZ  1
+ATOM   2366 O  OH  . TYR C 1 24  ? -15.683 24.715  48.218 1.00 31.23 ? 24  TYR C OH  1
+ATOM   2367 N  N   . GLY C 1 25  ? -8.074  23.227  52.066 1.00 18.29 ? 25  GLY C N   1
+ATOM   2368 C  CA  . GLY C 1 25  ? -6.804  23.029  52.426 1.00 15.33 ? 25  GLY C CA  1
+ATOM   2369 C  C   . GLY C 1 25  ? -6.699  21.965  53.360 1.00 12.64 ? 25  GLY C C   1
+ATOM   2370 O  O   . GLY C 1 25  ? -5.806  20.821  53.132 1.00 15.23 ? 25  GLY C O   1
+ATOM   2371 N  N   . ALA C 1 26  ? -7.463  21.493  54.359 1.00 16.00 ? 26  ALA C N   1
+ATOM   2372 C  CA  . ALA C 1 26  ? -7.534  20.341  55.113 1.00 11.42 ? 26  ALA C CA  1
+ATOM   2373 C  C   . ALA C 1 26  ? -7.619  19.067  54.311 1.00 10.94 ? 26  ALA C C   1
+ATOM   2374 O  O   . ALA C 1 26  ? -7.206  18.031  54.381 1.00 13.65 ? 26  ALA C O   1
+ATOM   2375 C  CB  . ALA C 1 26  ? -8.500  20.452  56.364 1.00 11.99 ? 26  ALA C CB  1
+ATOM   2376 N  N   . GLU C 1 27  ? -8.783  19.226  53.331 1.00 12.87 ? 27  GLU C N   1
+ATOM   2377 C  CA  . GLU C 1 27  ? -9.244  17.976  52.576 1.00 15.51 ? 27  GLU C CA  1
+ATOM   2378 C  C   . GLU C 1 27  ? -8.096  17.706  51.661 1.00 12.84 ? 27  GLU C C   1
+ATOM   2379 O  O   . GLU C 1 27  ? -7.734  16.473  51.484 1.00 15.95 ? 27  GLU C O   1
+ATOM   2380 C  CB  . GLU C 1 27  ? -10.316 18.457  51.593 1.00 15.50 ? 27  GLU C CB  1
+ATOM   2381 C  CG  . GLU C 1 27  ? -10.758 17.303  50.863 1.00 17.08 ? 27  GLU C CG  1
+ATOM   2382 C  CD  . GLU C 1 27  ? -12.022 17.548  50.026 1.00 30.48 ? 27  GLU C CD  1
+ATOM   2383 O  OE1 . GLU C 1 27  ? -12.072 17.252  48.763 1.00 18.71 ? 27  GLU C OE1 1
+ATOM   2384 O  OE2 . GLU C 1 27  ? -12.898 18.441  50.458 1.00 24.16 ? 27  GLU C OE2 1
+ATOM   2385 N  N   . ALA C 1 28  ? -7.324  18.786  51.063 1.00 11.36 ? 28  ALA C N   1
+ATOM   2386 C  CA  . ALA C 1 28  ? -6.088  18.408  50.170 1.00 9.58  ? 28  ALA C CA  1
+ATOM   2387 C  C   . ALA C 1 28  ? -5.039  17.570  51.002 1.00 9.29  ? 28  ALA C C   1
+ATOM   2388 O  O   . ALA C 1 28  ? -4.547  16.643  50.468 1.00 12.64 ? 28  ALA C O   1
+ATOM   2389 C  CB  . ALA C 1 28  ? -5.617  19.678  49.690 1.00 13.35 ? 28  ALA C CB  1
+ATOM   2390 N  N   . LEU C 1 29  ? -4.867  18.086  52.289 1.00 12.01 ? 29  LEU C N   1
+ATOM   2391 C  CA  . LEU C 1 29  ? -3.865  17.192  53.090 1.00 9.42  ? 29  LEU C CA  1
+ATOM   2392 C  C   . LEU C 1 29  ? -4.173  15.905  53.289 1.00 8.04  ? 29  LEU C C   1
+ATOM   2393 O  O   . LEU C 1 29  ? -3.538  14.863  53.260 1.00 11.27 ? 29  LEU C O   1
+ATOM   2394 C  CB  . LEU C 1 29  ? -3.658  18.059  54.497 1.00 13.39 ? 29  LEU C CB  1
+ATOM   2395 C  CG  . LEU C 1 29  ? -2.876  19.278  54.399 1.00 14.28 ? 29  LEU C CG  1
+ATOM   2396 C  CD1 . LEU C 1 29  ? -3.094  19.952  55.595 1.00 21.17 ? 29  LEU C CD1 1
+ATOM   2397 C  CD2 . LEU C 1 29  ? -1.571  19.096  53.905 1.00 17.52 ? 29  LEU C CD2 1
+ATOM   2398 N  N   . GLU C 1 30  ? -5.462  15.535  53.648 1.00 12.13 ? 30  GLU C N   1
+ATOM   2399 C  CA  . GLU C 1 30  ? -6.102  14.366  53.851 1.00 15.15 ? 30  GLU C CA  1
+ATOM   2400 C  C   . GLU C 1 30  ? -5.835  13.527  52.661 1.00 15.74 ? 30  GLU C C   1
+ATOM   2401 O  O   . GLU C 1 30  ? -5.582  12.341  52.786 1.00 15.15 ? 30  GLU C O   1
+ATOM   2402 C  CB  . GLU C 1 30  ? -7.561  14.405  54.364 1.00 16.95 ? 30  GLU C CB  1
+ATOM   2403 C  CG  . GLU C 1 30  ? -7.999  13.072  54.661 1.00 22.01 ? 30  GLU C CG  1
+ATOM   2404 C  CD  . GLU C 1 30  ? -9.745  12.903  55.530 1.00 33.25 ? 30  GLU C CD  1
+ATOM   2405 O  OE1 . GLU C 1 30  ? -9.926  14.090  55.536 1.00 33.78 ? 30  GLU C OE1 1
+ATOM   2406 O  OE2 . GLU C 1 30  ? -9.657  12.146  55.771 1.00 40.59 ? 30  GLU C OE2 1
+ATOM   2407 N  N   . ARG C 1 31  ? -6.245  14.159  51.535 1.00 9.68  ? 31  ARG C N   1
+ATOM   2408 C  CA  . ARG C 1 31  ? -6.127  13.392  50.254 1.00 8.70  ? 31  ARG C CA  1
+ATOM   2409 C  C   . ARG C 1 31  ? -4.580  12.893  50.083 1.00 13.62 ? 31  ARG C C   1
+ATOM   2410 O  O   . ARG C 1 31  ? -4.392  11.761  49.708 1.00 13.67 ? 31  ARG C O   1
+ATOM   2411 C  CB  . ARG C 1 31  ? -6.560  14.268  49.178 1.00 12.42 ? 31  ARG C CB  1
+ATOM   2412 C  CG  . ARG C 1 31  ? -8.118  14.275  49.084 1.00 11.84 ? 31  ARG C CG  1
+ATOM   2413 C  CD  . ARG C 1 31  ? -8.437  15.159  47.997 1.00 15.20 ? 31  ARG C CD  1
+ATOM   2414 N  NE  . ARG C 1 31  ? -10.007 15.331  47.812 1.00 14.19 ? 31  ARG C NE  1
+ATOM   2415 C  CZ  . ARG C 1 31  ? -10.854 14.431  47.288 1.00 11.42 ? 31  ARG C CZ  1
+ATOM   2416 N  NH1 . ARG C 1 31  ? -10.341 13.256  46.830 1.00 11.92 ? 31  ARG C NH1 1
+ATOM   2417 N  NH2 . ARG C 1 31  ? -12.062 14.695  47.485 1.00 15.15 ? 31  ARG C NH2 1
+ATOM   2418 N  N   . MET C 1 32  ? -3.708  13.821  50.267 1.00 10.57 ? 32  MET C N   1
+ATOM   2419 C  CA  . MET C 1 32  ? -2.214  13.598  50.222 1.00 8.16  ? 32  MET C CA  1
+ATOM   2420 C  C   . MET C 1 32  ? -1.757  12.475  51.159 1.00 7.80  ? 32  MET C C   1
+ATOM   2421 O  O   . MET C 1 32  ? -1.101  11.542  50.687 1.00 11.64 ? 32  MET C O   1
+ATOM   2422 C  CB  . MET C 1 32  ? -1.488  14.925  50.426 1.00 8.09  ? 32  MET C CB  1
+ATOM   2423 C  CG  . MET C 1 32  ? -0.080  14.657  50.300 1.00 11.10 ? 32  MET C CG  1
+ATOM   2424 S  SD  . MET C 1 32  ? 0.910   16.107  50.699 1.00 18.02 ? 32  MET C SD  1
+ATOM   2425 C  CE  . MET C 1 32  ? 0.605   16.186  52.438 1.00 20.04 ? 32  MET C CE  1
+ATOM   2426 N  N   . PHE C 1 33  ? -2.172  12.561  52.488 1.00 13.50 ? 33  PHE C N   1
+ATOM   2427 C  CA  . PHE C 1 33  ? -1.762  11.448  53.384 1.00 12.85 ? 33  PHE C CA  1
+ATOM   2428 C  C   . PHE C 1 33  ? -2.261  10.215  53.037 1.00 15.05 ? 33  PHE C C   1
+ATOM   2429 O  O   . PHE C 1 33  ? -1.578  9.141   53.270 1.00 13.38 ? 33  PHE C O   1
+ATOM   2430 C  CB  . PHE C 1 33  ? -2.101  11.908  54.764 1.00 12.45 ? 33  PHE C CB  1
+ATOM   2431 C  CG  . PHE C 1 33  ? -1.665  13.245  55.277 1.00 10.81 ? 33  PHE C CG  1
+ATOM   2432 C  CD1 . PHE C 1 33  ? -0.325  13.419  55.129 1.00 14.60 ? 33  PHE C CD1 1
+ATOM   2433 C  CD2 . PHE C 1 33  ? -2.465  14.016  56.113 1.00 15.15 ? 33  PHE C CD2 1
+ATOM   2434 C  CE1 . PHE C 1 33  ? 0.265   14.558  55.632 1.00 15.80 ? 33  PHE C CE1 1
+ATOM   2435 C  CE2 . PHE C 1 33  ? -1.739  15.156  56.434 1.00 13.43 ? 33  PHE C CE2 1
+ATOM   2436 C  CZ  . PHE C 1 33  ? -0.471  15.399  56.218 1.00 22.23 ? 33  PHE C CZ  1
+ATOM   2437 N  N   . LEU C 1 34  ? -3.467  10.015  52.475 1.00 11.85 ? 34  LEU C N   1
+ATOM   2438 C  CA  . LEU C 1 34  ? -4.060  8.695   52.074 1.00 12.31 ? 34  LEU C CA  1
+ATOM   2439 C  C   . LEU C 1 34  ? -3.489  8.195   50.756 1.00 15.72 ? 34  LEU C C   1
+ATOM   2440 O  O   . LEU C 1 34  ? -3.186  7.026   50.593 1.00 19.67 ? 34  LEU C O   1
+ATOM   2441 C  CB  . LEU C 1 34  ? -5.561  8.656   51.943 1.00 16.89 ? 34  LEU C CB  1
+ATOM   2442 C  CG  . LEU C 1 34  ? -6.276  8.888   53.285 1.00 26.21 ? 34  LEU C CG  1
+ATOM   2443 C  CD1 . LEU C 1 34  ? -7.791  8.930   53.163 1.00 26.59 ? 34  LEU C CD1 1
+ATOM   2444 C  CD2 . LEU C 1 34  ? -5.945  7.900   54.377 1.00 38.34 ? 34  LEU C CD2 1
+ATOM   2445 N  N   . SER C 1 35  ? -3.374  9.127   49.760 1.00 12.82 ? 35  SER C N   1
+ATOM   2446 C  CA  . SER C 1 35  ? -2.817  8.650   48.555 1.00 10.93 ? 35  SER C CA  1
+ATOM   2447 C  C   . SER C 1 35  ? -1.422  8.375   48.315 1.00 14.27 ? 35  SER C C   1
+ATOM   2448 O  O   . SER C 1 35  ? -0.907  7.716   47.538 1.00 16.71 ? 35  SER C O   1
+ATOM   2449 C  CB  . SER C 1 35  ? -3.146  9.673   47.396 1.00 13.98 ? 35  SER C CB  1
+ATOM   2450 O  OG  . SER C 1 35  ? -4.554  9.755   47.217 1.00 18.75 ? 35  SER C OG  1
+ATOM   2451 N  N   . PHE C 1 36  ? -0.515  9.177   49.129 1.00 11.09 ? 36  PHE C N   1
+ATOM   2452 C  CA  . PHE C 1 36  ? 0.928   9.230   49.073 1.00 10.70 ? 36  PHE C CA  1
+ATOM   2453 C  C   . PHE C 1 36  ? 1.442   9.244   50.598 1.00 13.97 ? 36  PHE C C   1
+ATOM   2454 O  O   . PHE C 1 36  ? 1.897   10.208  51.186 1.00 16.32 ? 36  PHE C O   1
+ATOM   2455 C  CB  . PHE C 1 36  ? 1.366   10.496  48.464 1.00 12.71 ? 36  PHE C CB  1
+ATOM   2456 C  CG  . PHE C 1 36  ? 0.831   10.743  47.018 1.00 14.13 ? 36  PHE C CG  1
+ATOM   2457 C  CD1 . PHE C 1 36  ? -0.200  11.709  46.855 1.00 14.98 ? 36  PHE C CD1 1
+ATOM   2458 C  CD2 . PHE C 1 36  ? 1.146   9.782   45.870 1.00 21.47 ? 36  PHE C CD2 1
+ATOM   2459 C  CE1 . PHE C 1 36  ? -0.795  11.967  45.602 1.00 23.41 ? 36  PHE C CE1 1
+ATOM   2460 C  CE2 . PHE C 1 36  ? 0.543   10.112  44.816 1.00 24.62 ? 36  PHE C CE2 1
+ATOM   2461 C  CZ  . PHE C 1 36  ? -0.438  11.152  44.672 1.00 15.55 ? 36  PHE C CZ  1
+ATOM   2462 N  N   . PRO C 1 37  ? 1.375   7.958   50.950 1.00 18.65 ? 37  PRO C N   1
+ATOM   2463 C  CA  . PRO C 1 37  ? 1.595   7.767   52.370 1.00 17.35 ? 37  PRO C CA  1
+ATOM   2464 C  C   . PRO C 1 37  ? 3.075   8.220   52.886 1.00 18.35 ? 37  PRO C C   1
+ATOM   2465 O  O   . PRO C 1 37  ? 3.306   8.543   54.086 1.00 14.04 ? 37  PRO C O   1
+ATOM   2466 C  CB  . PRO C 1 37  ? 1.345   6.277   52.714 1.00 27.87 ? 37  PRO C CB  1
+ATOM   2467 C  CG  . PRO C 1 37  ? 1.106   5.699   51.582 1.00 37.42 ? 37  PRO C CG  1
+ATOM   2468 C  CD  . PRO C 1 37  ? 0.889   6.839   50.576 1.00 22.48 ? 37  PRO C CD  1
+ATOM   2469 N  N   . THR C 1 38  ? 3.945   8.303   51.974 1.00 12.63 ? 38  THR C N   1
+ATOM   2470 C  CA  . THR C 1 38  ? 5.319   8.916   52.410 1.00 17.25 ? 38  THR C CA  1
+ATOM   2471 C  C   . THR C 1 38  ? 5.331   10.143  52.974 1.00 15.32 ? 38  THR C C   1
+ATOM   2472 O  O   . THR C 1 38  ? 6.235   10.553  53.686 1.00 11.09 ? 38  THR C O   1
+ATOM   2473 C  CB  . THR C 1 38  ? 6.349   8.251   51.084 1.00 12.40 ? 38  THR C CB  1
+ATOM   2474 O  OG1 . THR C 1 38  ? 5.950   9.501   50.148 1.00 15.33 ? 38  THR C OG1 1
+ATOM   2475 C  CG2 . THR C 1 38  ? 5.401   8.189   50.082 1.00 80.12 ? 38  THR C CG2 1
+ATOM   2476 N  N   . THR C 1 39  ? 4.389   10.931  52.424 1.00 10.35 ? 39  THR C N   1
+ATOM   2477 C  CA  . THR C 1 39  ? 4.247   12.291  52.960 1.00 11.60 ? 39  THR C CA  1
+ATOM   2478 C  C   . THR C 1 39  ? 3.926   12.334  54.475 1.00 11.25 ? 39  THR C C   1
+ATOM   2479 O  O   . THR C 1 39  ? 4.278   13.349  55.136 1.00 15.31 ? 39  THR C O   1
+ATOM   2480 C  CB  . THR C 1 39  ? 3.160   13.097  52.249 1.00 10.41 ? 39  THR C CB  1
+ATOM   2481 O  OG1 . THR C 1 39  ? 1.787   12.616  52.383 1.00 8.43  ? 39  THR C OG1 1
+ATOM   2482 C  CG2 . THR C 1 39  ? 3.577   13.036  50.712 1.00 7.27  ? 39  THR C CG2 1
+ATOM   2483 N  N   . LYS C 1 40  ? 3.512   11.306  55.020 1.00 12.10 ? 40  LYS C N   1
+ATOM   2484 C  CA  . LYS C 1 40  ? 3.174   11.353  56.579 1.00 12.37 ? 40  LYS C CA  1
+ATOM   2485 C  C   . LYS C 1 40  ? 4.469   11.360  57.368 1.00 12.69 ? 40  LYS C C   1
+ATOM   2486 O  O   . LYS C 1 40  ? 4.366   11.655  58.531 1.00 13.50 ? 40  LYS C O   1
+ATOM   2487 C  CB  . LYS C 1 40  ? 2.403   9.990   56.942 1.00 13.01 ? 40  LYS C CB  1
+ATOM   2488 C  CG  . LYS C 1 40  ? 0.969   9.952   56.346 1.00 16.35 ? 40  LYS C CG  1
+ATOM   2489 C  CD  . LYS C 1 40  ? 0.649   8.359   56.605 1.00 21.60 ? 40  LYS C CD  1
+ATOM   2490 C  CE  . LYS C 1 40  ? -0.193  8.248   56.553 1.00 41.58 ? 40  LYS C CE  1
+ATOM   2491 N  NZ  . LYS C 1 40  ? -0.139  6.607   56.962 1.00 24.62 ? 40  LYS C NZ  1
+ATOM   2492 N  N   . THR C 1 41  ? 5.528   11.065  56.723 1.00 15.39 ? 41  THR C N   1
+ATOM   2493 C  CA  . THR C 1 41  ? 6.922   10.921  57.459 1.00 15.24 ? 41  THR C CA  1
+ATOM   2494 C  C   . THR C 1 41  ? 7.123   12.284  57.801 1.00 24.53 ? 41  THR C C   1
+ATOM   2495 O  O   . THR C 1 41  ? 8.072   12.498  58.835 1.00 20.94 ? 41  THR C O   1
+ATOM   2496 C  CB  . THR C 1 41  ? 8.064   10.477  56.566 1.00 10.27 ? 41  THR C CB  1
+ATOM   2497 O  OG1 . THR C 1 41  ? 8.284   11.337  55.536 1.00 10.56 ? 41  THR C OG1 1
+ATOM   2498 C  CG2 . THR C 1 41  ? 7.786   9.146   56.124 1.00 13.16 ? 41  THR C CG2 1
+ATOM   2499 N  N   . TYR C 1 42  ? 6.638   13.545  57.531 1.00 15.74 ? 42  TYR C N   1
+ATOM   2500 C  CA  . TYR C 1 42  ? 7.006   14.840  57.845 1.00 10.60 ? 42  TYR C CA  1
+ATOM   2501 C  C   . TYR C 1 42  ? 6.076   15.316  59.042 1.00 12.75 ? 42  TYR C C   1
+ATOM   2502 O  O   . TYR C 1 42  ? 6.204   16.390  59.558 1.00 15.68 ? 42  TYR C O   1
+ATOM   2503 C  CB  . TYR C 1 42  ? 6.733   15.915  56.788 1.00 16.68 ? 42  TYR C CB  1
+ATOM   2504 C  CG  . TYR C 1 42  ? 7.813   15.489  55.713 1.00 10.99 ? 42  TYR C CG  1
+ATOM   2505 C  CD1 . TYR C 1 42  ? 9.207   16.044  55.836 1.00 17.16 ? 42  TYR C CD1 1
+ATOM   2506 C  CD2 . TYR C 1 42  ? 7.533   14.755  54.517 1.00 12.51 ? 42  TYR C CD2 1
+ATOM   2507 C  CE1 . TYR C 1 42  ? 10.103  15.679  54.940 1.00 15.83 ? 42  TYR C CE1 1
+ATOM   2508 C  CE2 . TYR C 1 42  ? 8.459   14.511  53.606 1.00 12.91 ? 42  TYR C CE2 1
+ATOM   2509 C  CZ  . TYR C 1 42  ? 9.872   14.963  53.797 1.00 12.97 ? 42  TYR C CZ  1
+ATOM   2510 O  OH  . TYR C 1 42  ? 10.781  14.763  52.777 1.00 13.25 ? 42  TYR C OH  1
+ATOM   2511 N  N   . PHE C 1 43  ? 5.152   14.452  59.371 1.00 15.49 ? 43  PHE C N   1
+ATOM   2512 C  CA  . PHE C 1 43  ? 4.069   14.816  60.478 1.00 17.75 ? 43  PHE C CA  1
+ATOM   2513 C  C   . PHE C 1 43  ? 3.884   13.661  61.477 1.00 20.04 ? 43  PHE C C   1
+ATOM   2514 O  O   . PHE C 1 43  ? 2.749   13.346  61.865 1.00 17.05 ? 43  PHE C O   1
+ATOM   2515 C  CB  . PHE C 1 43  ? 2.709   15.201  59.703 1.00 26.70 ? 43  PHE C CB  1
+ATOM   2516 C  CG  . PHE C 1 43  ? 2.732   16.251  58.715 1.00 14.42 ? 43  PHE C CG  1
+ATOM   2517 C  CD1 . PHE C 1 43  ? 3.037   15.910  57.330 1.00 15.73 ? 43  PHE C CD1 1
+ATOM   2518 C  CD2 . PHE C 1 43  ? 2.168   17.573  59.210 1.00 15.90 ? 43  PHE C CD2 1
+ATOM   2519 C  CE1 . PHE C 1 43  ? 2.972   16.995  56.504 1.00 16.99 ? 43  PHE C CE1 1
+ATOM   2520 C  CE2 . PHE C 1 43  ? 2.369   18.466  58.178 1.00 19.76 ? 43  PHE C CE2 1
+ATOM   2521 C  CZ  . PHE C 1 43  ? 2.678   18.396  56.822 1.00 10.96 ? 43  PHE C CZ  1
+ATOM   2522 N  N   . PRO C 1 44  ? 5.089   13.280  62.132 1.00 17.51 ? 44  PRO C N   1
+ATOM   2523 C  CA  . PRO C 1 44  ? 4.820   12.079  63.073 1.00 22.01 ? 44  PRO C CA  1
+ATOM   2524 C  C   . PRO C 1 44  ? 4.417   12.817  64.424 1.00 23.34 ? 44  PRO C C   1
+ATOM   2525 O  O   . PRO C 1 44  ? 3.858   11.984  65.132 1.00 23.67 ? 44  PRO C O   1
+ATOM   2526 C  CB  . PRO C 1 44  ? 6.514   11.803  63.224 1.00 28.76 ? 44  PRO C CB  1
+ATOM   2527 C  CG  . PRO C 1 44  ? 7.129   13.041  62.978 1.00 30.00 ? 44  PRO C CG  1
+ATOM   2528 C  CD  . PRO C 1 44  ? 6.478   13.814  61.795 1.00 18.17 ? 44  PRO C CD  1
+ATOM   2529 N  N   . HIS C 1 45  ? 4.305   13.912  64.562 1.00 23.82 ? 45  HIS C N   1
+ATOM   2530 C  CA  . HIS C 1 45  ? 3.666   14.662  65.745 1.00 24.33 ? 45  HIS C CA  1
+ATOM   2531 C  C   . HIS C 1 45  ? 2.039   14.941  65.696 1.00 36.67 ? 45  HIS C C   1
+ATOM   2532 O  O   . HIS C 1 45  ? 1.771   15.645  66.599 1.00 32.61 ? 45  HIS C O   1
+ATOM   2533 C  CB  . HIS C 1 45  ? 4.294   15.937  65.949 1.00 29.73 ? 45  HIS C CB  1
+ATOM   2534 C  CG  . HIS C 1 45  ? 4.645   17.139  64.937 1.00 29.43 ? 45  HIS C CG  1
+ATOM   2535 N  ND1 . HIS C 1 45  ? 5.085   16.497  63.657 1.00 26.84 ? 45  HIS C ND1 1
+ATOM   2536 C  CD2 . HIS C 1 45  ? 4.120   18.333  64.811 1.00 33.54 ? 45  HIS C CD2 1
+ATOM   2537 C  CE1 . HIS C 1 45  ? 4.879   17.511  63.169 1.00 37.75 ? 45  HIS C CE1 1
+ATOM   2538 N  NE2 . HIS C 1 45  ? 4.436   18.751  63.634 1.00 39.11 ? 45  HIS C NE2 1
+ATOM   2539 N  N   . PHE C 1 46  ? 1.609   14.731  64.494 1.00 19.71 ? 46  PHE C N   1
+ATOM   2540 C  CA  . PHE C 1 46  ? 0.306   15.065  64.360 1.00 16.71 ? 46  PHE C CA  1
+ATOM   2541 C  C   . PHE C 1 46  ? -0.430  13.925  64.600 1.00 21.27 ? 46  PHE C C   1
+ATOM   2542 O  O   . PHE C 1 46  ? -0.267  12.658  64.220 1.00 23.84 ? 46  PHE C O   1
+ATOM   2543 C  CB  . PHE C 1 46  ? -0.011  15.514  62.776 1.00 21.57 ? 46  PHE C CB  1
+ATOM   2544 C  CG  . PHE C 1 46  ? 0.114   16.856  62.790 1.00 17.89 ? 46  PHE C CG  1
+ATOM   2545 C  CD1 . PHE C 1 46  ? -0.605  17.595  61.827 1.00 29.22 ? 46  PHE C CD1 1
+ATOM   2546 C  CD2 . PHE C 1 46  ? 1.023   17.809  63.228 1.00 29.35 ? 46  PHE C CD2 1
+ATOM   2547 C  CE1 . PHE C 1 46  ? -0.351  18.995  61.517 1.00 23.51 ? 46  PHE C CE1 1
+ATOM   2548 C  CE2 . PHE C 1 46  ? 0.956   18.685  62.965 1.00 34.19 ? 46  PHE C CE2 1
+ATOM   2549 C  CZ  . PHE C 1 46  ? 0.537   19.703  61.848 1.00 30.38 ? 46  PHE C CZ  1
+ATOM   2550 N  N   . ASP C 1 47  ? -1.925  13.966  64.948 1.00 21.22 ? 47  ASP C N   1
+ATOM   2551 C  CA  . ASP C 1 47  ? -2.839  12.896  64.685 1.00 21.17 ? 47  ASP C CA  1
+ATOM   2552 C  C   . ASP C 1 47  ? -3.681  13.044  63.245 1.00 15.44 ? 47  ASP C C   1
+ATOM   2553 O  O   . ASP C 1 47  ? -3.923  14.278  63.014 1.00 19.22 ? 47  ASP C O   1
+ATOM   2554 C  CB  . ASP C 1 47  ? -4.083  13.376  65.772 1.00 26.87 ? 47  ASP C CB  1
+ATOM   2555 C  CG  . ASP C 1 47  ? -5.052  11.954  65.737 1.00 44.60 ? 47  ASP C CG  1
+ATOM   2556 O  OD1 . ASP C 1 47  ? -5.160  11.792  64.719 1.00 38.14 ? 47  ASP C OD1 1
+ATOM   2557 O  OD2 . ASP C 1 47  ? -5.925  12.234  66.642 1.00 35.16 ? 47  ASP C OD2 1
+ATOM   2558 N  N   . LEU C 1 48  ? -3.179  12.085  62.497 1.00 20.23 ? 48  LEU C N   1
+ATOM   2559 C  CA  . LEU C 1 48  ? -3.688  12.319  61.005 1.00 22.13 ? 48  LEU C CA  1
+ATOM   2560 C  C   . LEU C 1 48  ? -4.802  11.660  60.740 1.00 26.79 ? 48  LEU C C   1
+ATOM   2561 O  O   . LEU C 1 48  ? -5.457  11.516  59.513 1.00 28.79 ? 48  LEU C O   1
+ATOM   2562 C  CB  . LEU C 1 48  ? -2.551  11.656  60.237 1.00 20.10 ? 48  LEU C CB  1
+ATOM   2563 C  CG  . LEU C 1 48  ? -1.277  12.170  60.036 1.00 22.13 ? 48  LEU C CG  1
+ATOM   2564 C  CD1 . LEU C 1 48  ? -0.083  11.612  59.311 1.00 30.66 ? 48  LEU C CD1 1
+ATOM   2565 C  CD2 . LEU C 1 48  ? -1.174  13.889  59.773 1.00 21.27 ? 48  LEU C CD2 1
+ATOM   2566 N  N   . SER C 1 49  ? -5.849  11.353  61.642 1.00 29.67 ? 49  SER C N   1
+ATOM   2567 C  CA  . SER C 1 49  ? -7.213  10.679  61.793 1.00 26.45 ? 49  SER C CA  1
+ATOM   2568 C  C   . SER C 1 49  ? -7.806  11.616  61.067 1.00 19.97 ? 49  SER C C   1
+ATOM   2569 O  O   . SER C 1 49  ? -7.872  12.886  60.969 1.00 20.96 ? 49  SER C O   1
+ATOM   2570 C  CB  . SER C 1 49  ? -7.654  9.961   63.116 1.00 26.72 ? 49  SER C CB  1
+ATOM   2571 O  OG  . SER C 1 49  ? -7.349  10.585  63.974 1.00 34.29 ? 49  SER C OG  1
+ATOM   2572 N  N   . HIS C 1 50  ? -9.058  10.938  60.378 1.00 28.23 ? 50  HIS C N   1
+ATOM   2573 C  CA  . HIS C 1 50  ? -9.989  11.753  59.695 1.00 26.06 ? 50  HIS C CA  1
+ATOM   2574 C  C   . HIS C 1 50  ? -10.723 12.840  60.792 1.00 24.81 ? 50  HIS C C   1
+ATOM   2575 O  O   . HIS C 1 50  ? -11.005 12.232  61.727 1.00 27.33 ? 50  HIS C O   1
+ATOM   2576 C  CB  . HIS C 1 50  ? -11.185 10.845  58.864 1.00 33.58 ? 50  HIS C CB  1
+ATOM   2577 C  CG  . HIS C 1 50  ? -11.812 11.755  58.159 1.00 21.75 ? 50  HIS C CG  1
+ATOM   2578 N  ND1 . HIS C 1 50  ? -13.399 11.819  58.670 1.00 37.61 ? 50  HIS C ND1 1
+ATOM   2579 C  CD2 . HIS C 1 50  ? -11.939 12.681  57.336 1.00 24.11 ? 50  HIS C CD2 1
+ATOM   2580 C  CE1 . HIS C 1 50  ? -13.904 12.788  58.021 1.00 35.12 ? 50  HIS C CE1 1
+ATOM   2581 N  NE2 . HIS C 1 50  ? -13.088 13.562  56.956 1.00 42.35 ? 50  HIS C NE2 1
+ATOM   2582 N  N   . GLY C 1 51  ? -10.727 14.002  60.432 1.00 24.42 ? 51  GLY C N   1
+ATOM   2583 C  CA  . GLY C 1 51  ? -11.270 14.900  61.213 1.00 26.56 ? 51  GLY C CA  1
+ATOM   2584 C  C   . GLY C 1 51  ? -10.541 15.602  62.210 1.00 23.39 ? 51  GLY C C   1
+ATOM   2585 O  O   . GLY C 1 51  ? -10.797 16.611  62.951 1.00 25.53 ? 51  GLY C O   1
+ATOM   2586 N  N   . SER C 1 52  ? -9.223  15.273  62.098 1.00 22.06 ? 52  SER C N   1
+ATOM   2587 C  CA  . SER C 1 52  ? -8.075  15.847  63.074 1.00 25.03 ? 52  SER C CA  1
+ATOM   2588 C  C   . SER C 1 52  ? -8.030  17.123  63.178 1.00 31.37 ? 52  SER C C   1
+ATOM   2589 O  O   . SER C 1 52  ? -7.998  17.964  62.109 1.00 22.94 ? 52  SER C O   1
+ATOM   2590 C  CB  . SER C 1 52  ? -6.799  15.297  62.750 1.00 30.26 ? 52  SER C CB  1
+ATOM   2591 O  OG  . SER C 1 52  ? -5.835  15.898  63.565 1.00 21.66 ? 52  SER C OG  1
+ATOM   2592 N  N   . ALA C 1 53  ? -8.245  17.975  64.239 1.00 22.15 ? 53  ALA C N   1
+ATOM   2593 C  CA  . ALA C 1 53  ? -7.913  19.411  64.437 1.00 29.32 ? 53  ALA C CA  1
+ATOM   2594 C  C   . ALA C 1 53  ? -6.627  19.950  63.856 1.00 23.50 ? 53  ALA C C   1
+ATOM   2595 O  O   . ALA C 1 53  ? -6.601  21.082  63.529 1.00 19.56 ? 53  ALA C O   1
+ATOM   2596 C  CB  . ALA C 1 53  ? -8.583  19.836  65.595 1.00 46.37 ? 53  ALA C CB  1
+ATOM   2597 N  N   . GLN C 1 54  ? -5.817  18.961  64.252 1.00 20.69 ? 54  GLN C N   1
+ATOM   2598 C  CA  . GLN C 1 54  ? -4.343  19.380  63.936 1.00 22.13 ? 54  GLN C CA  1
+ATOM   2599 C  C   . GLN C 1 54  ? -4.212  19.710  62.226 1.00 21.00 ? 54  GLN C C   1
+ATOM   2600 O  O   . GLN C 1 54  ? -3.565  20.642  61.831 1.00 19.66 ? 54  GLN C O   1
+ATOM   2601 C  CB  . GLN C 1 54  ? -3.307  18.507  64.329 1.00 23.01 ? 54  GLN C CB  1
+ATOM   2602 C  CG  . GLN C 1 54  ? -3.086  18.473  65.690 1.00 26.98 ? 54  GLN C CG  1
+ATOM   2603 C  CD  . GLN C 1 54  ? -2.066  17.388  66.316 1.00 17.64 ? 54  GLN C CD  1
+ATOM   2604 O  OE1 . GLN C 1 54  ? -2.244  16.204  65.989 1.00 23.97 ? 54  GLN C OE1 1
+ATOM   2605 N  NE2 . GLN C 1 54  ? -0.960  17.945  66.788 1.00 35.16 ? 54  GLN C NE2 1
+ATOM   2606 N  N   . VAL C 1 55  ? -4.931  18.617  61.614 1.00 18.58 ? 55  VAL C N   1
+ATOM   2607 C  CA  . VAL C 1 55  ? -4.793  18.683  60.011 1.00 18.23 ? 55  VAL C CA  1
+ATOM   2608 C  C   . VAL C 1 55  ? -5.634  19.910  59.692 1.00 15.73 ? 55  VAL C C   1
+ATOM   2609 O  O   . VAL C 1 55  ? -5.344  20.592  58.740 1.00 16.15 ? 55  VAL C O   1
+ATOM   2610 C  CB  . VAL C 1 55  ? -5.286  17.310  59.526 1.00 16.13 ? 55  VAL C CB  1
+ATOM   2611 C  CG1 . VAL C 1 55  ? -5.449  17.575  58.027 1.00 22.56 ? 55  VAL C CG1 1
+ATOM   2612 C  CG2 . VAL C 1 55  ? -4.343  16.309  59.863 1.00 16.34 ? 55  VAL C CG2 1
+ATOM   2613 N  N   . LYS C 1 56  ? -6.854  20.164  60.277 1.00 17.00 ? 56  LYS C N   1
+ATOM   2614 C  CA  . LYS C 1 56  ? -7.662  21.228  59.942 1.00 18.57 ? 56  LYS C CA  1
+ATOM   2615 C  C   . LYS C 1 56  ? -7.108  22.391  60.069 1.00 20.36 ? 56  LYS C C   1
+ATOM   2616 O  O   . LYS C 1 56  ? -6.966  23.419  59.326 1.00 20.10 ? 56  LYS C O   1
+ATOM   2617 C  CB  . LYS C 1 56  ? -8.921  21.267  60.796 1.00 27.04 ? 56  LYS C CB  1
+ATOM   2618 C  CG  . LYS C 1 56  ? -9.866  20.028  60.378 1.00 42.35 ? 56  LYS C CG  1
+ATOM   2619 C  CD  . LYS C 1 56  ? -11.616 21.441  60.667 1.00 43.36 ? 56  LYS C CD  1
+ATOM   2620 C  CE  . LYS C 1 56  ? -12.255 19.139  60.522 1.00 48.38 ? 56  LYS C CE  1
+ATOM   2621 N  NZ  . LYS C 1 56  ? -13.406 19.860  61.584 1.00 67.70 ? 56  LYS C NZ  1
+ATOM   2622 N  N   . GLY C 1 57  ? -6.220  22.581  61.161 1.00 16.00 ? 57  GLY C N   1
+ATOM   2623 C  CA  . GLY C 1 57  ? -5.534  23.718  61.495 1.00 21.54 ? 57  GLY C CA  1
+ATOM   2624 C  C   . GLY C 1 57  ? -4.411  24.118  60.535 1.00 18.61 ? 57  GLY C C   1
+ATOM   2625 O  O   . GLY C 1 57  ? -4.106  25.381  60.090 1.00 24.59 ? 57  GLY C O   1
+ATOM   2626 N  N   . HIS C 1 58  ? -3.714  23.014  60.250 1.00 15.81 ? 58  HIS C N   1
+ATOM   2627 C  CA  . HIS C 1 58  ? -2.577  23.110  59.257 1.00 16.10 ? 58  HIS C CA  1
+ATOM   2628 C  C   . HIS C 1 58  ? -3.303  23.581  57.803 1.00 21.16 ? 58  HIS C C   1
+ATOM   2629 O  O   . HIS C 1 58  ? -2.579  24.318  57.149 1.00 17.74 ? 58  HIS C O   1
+ATOM   2630 C  CB  . HIS C 1 58  ? -1.798  21.921  59.173 1.00 15.43 ? 58  HIS C CB  1
+ATOM   2631 C  CG  . HIS C 1 58  ? -0.595  22.031  58.374 1.00 18.98 ? 58  HIS C CG  1
+ATOM   2632 N  ND1 . HIS C 1 58  ? 0.305   23.017  58.784 1.00 21.14 ? 58  HIS C ND1 1
+ATOM   2633 C  CD2 . HIS C 1 58  ? -0.197  21.395  57.415 1.00 16.95 ? 58  HIS C CD2 1
+ATOM   2634 C  CE1 . HIS C 1 58  ? 1.197   22.783  57.658 1.00 21.77 ? 58  HIS C CE1 1
+ATOM   2635 N  NE2 . HIS C 1 58  ? 0.960   21.773  56.730 1.00 17.45 ? 58  HIS C NE2 1
+ATOM   2636 N  N   . GLY C 1 59  ? -4.296  22.876  57.544 1.00 20.04 ? 59  GLY C N   1
+ATOM   2637 C  CA  . GLY C 1 59  ? -4.838  23.208  56.376 1.00 24.32 ? 59  GLY C CA  1
+ATOM   2638 C  C   . GLY C 1 59  ? -5.306  24.581  56.096 1.00 16.44 ? 59  GLY C C   1
+ATOM   2639 O  O   . GLY C 1 59  ? -5.015  25.292  54.988 1.00 16.63 ? 59  GLY C O   1
+ATOM   2640 N  N   . LYS C 1 60  ? -5.781  25.258  57.176 1.00 14.40 ? 60  LYS C N   1
+ATOM   2641 C  CA  . LYS C 1 60  ? -5.960  26.683  57.223 1.00 14.87 ? 60  LYS C CA  1
+ATOM   2642 C  C   . LYS C 1 60  ? -4.842  27.533  56.982 1.00 17.20 ? 60  LYS C C   1
+ATOM   2643 O  O   . LYS C 1 60  ? -4.747  28.487  56.243 1.00 19.10 ? 60  LYS C O   1
+ATOM   2644 C  CB  . LYS C 1 60  ? -6.895  26.995  58.493 1.00 20.14 ? 60  LYS C CB  1
+ATOM   2645 C  CG  . LYS C 1 60  ? -7.071  28.403  58.258 1.00 36.22 ? 60  LYS C CG  1
+ATOM   2646 C  CD  . LYS C 1 60  ? -8.196  29.061  59.122 1.00 67.45 ? 60  LYS C CD  1
+ATOM   2647 C  CE  . LYS C 1 60  ? -8.607  30.169  58.486 1.00 61.41 ? 60  LYS C CE  1
+ATOM   2648 N  NZ  . LYS C 1 60  ? -7.187  31.227  59.448 1.00 67.02 ? 60  LYS C NZ  1
+ATOM   2649 N  N   . LYS C 1 61  ? -3.715  27.130  57.611 1.00 17.79 ? 61  LYS C N   1
+ATOM   2650 C  CA  . LYS C 1 61  ? -2.518  27.878  57.458 1.00 21.13 ? 61  LYS C CA  1
+ATOM   2651 C  C   . LYS C 1 61  ? -1.910  27.871  55.802 1.00 16.24 ? 61  LYS C C   1
+ATOM   2652 O  O   . LYS C 1 61  ? -1.487  28.880  55.333 1.00 15.80 ? 61  LYS C O   1
+ATOM   2653 C  CB  . LYS C 1 61  ? -1.395  27.243  58.272 1.00 23.05 ? 61  LYS C CB  1
+ATOM   2654 C  CG  . LYS C 1 61  ? -1.631  27.643  59.520 1.00 29.48 ? 61  LYS C CG  1
+ATOM   2655 C  CD  . LYS C 1 61  ? -0.739  27.206  60.480 1.00 35.76 ? 61  LYS C CD  1
+ATOM   2656 C  CE  . LYS C 1 61  ? -1.233  27.929  62.061 1.00 58.26 ? 61  LYS C CE  1
+ATOM   2657 N  NZ  . LYS C 1 61  ? 0.169   26.603  62.489 1.00 59.87 ? 61  LYS C NZ  1
+ATOM   2658 N  N   . VAL C 1 62  ? -2.048  26.506  55.279 1.00 15.31 ? 62  VAL C N   1
+ATOM   2659 C  CA  . VAL C 1 62  ? -1.708  26.402  53.887 1.00 17.56 ? 62  VAL C CA  1
+ATOM   2660 C  C   . VAL C 1 62  ? -2.389  27.261  52.819 1.00 16.25 ? 62  VAL C C   1
+ATOM   2661 O  O   . VAL C 1 62  ? -1.946  28.030  52.063 1.00 13.61 ? 62  VAL C O   1
+ATOM   2662 C  CB  . VAL C 1 62  ? -1.736  24.806  53.584 1.00 18.84 ? 62  VAL C CB  1
+ATOM   2663 C  CG1 . VAL C 1 62  ? -1.649  24.613  52.156 1.00 17.19 ? 62  VAL C CG1 1
+ATOM   2664 C  CG2 . VAL C 1 62  ? -0.645  24.196  54.363 1.00 18.33 ? 62  VAL C CG2 1
+ATOM   2665 N  N   . ALA C 1 63  ? -3.724  27.181  53.303 1.00 13.67 ? 63  ALA C N   1
+ATOM   2666 C  CA  . ALA C 1 63  ? -4.787  27.914  52.463 1.00 21.56 ? 63  ALA C CA  1
+ATOM   2667 C  C   . ALA C 1 63  ? -4.472  29.237  52.416 1.00 19.04 ? 63  ALA C C   1
+ATOM   2668 O  O   . ALA C 1 63  ? -4.499  30.099  51.589 1.00 17.01 ? 63  ALA C O   1
+ATOM   2669 C  CB  . ALA C 1 63  ? -6.236  27.549  52.778 1.00 17.02 ? 63  ALA C CB  1
+ATOM   2670 N  N   . ASP C 1 64  ? -4.236  29.883  53.617 1.00 16.51 ? 64  ASP C N   1
+ATOM   2671 C  CA  . ASP C 1 64  ? -4.057  31.303  53.742 1.00 19.49 ? 64  ASP C CA  1
+ATOM   2672 C  C   . ASP C 1 64  ? -2.831  31.770  53.119 1.00 14.91 ? 64  ASP C C   1
+ATOM   2673 O  O   . ASP C 1 64  ? -2.747  32.786  52.503 1.00 19.95 ? 64  ASP C O   1
+ATOM   2674 C  CB  . ASP C 1 64  ? -4.185  31.736  55.280 1.00 24.76 ? 64  ASP C CB  1
+ATOM   2675 C  CG  . ASP C 1 64  ? -5.551  31.754  56.224 1.00 34.25 ? 64  ASP C CG  1
+ATOM   2676 O  OD1 . ASP C 1 64  ? -6.413  31.417  55.564 1.00 28.85 ? 64  ASP C OD1 1
+ATOM   2677 O  OD2 . ASP C 1 64  ? -5.168  31.654  57.218 1.00 27.13 ? 64  ASP C OD2 1
+ATOM   2678 N  N   . ALA C 1 65  ? -1.773  30.926  53.227 1.00 16.65 ? 65  ALA C N   1
+ATOM   2679 C  CA  . ALA C 1 65  ? -0.528  31.302  52.536 1.00 16.32 ? 65  ALA C CA  1
+ATOM   2680 C  C   . ALA C 1 65  ? -0.689  31.436  50.930 1.00 13.95 ? 65  ALA C C   1
+ATOM   2681 O  O   . ALA C 1 65  ? -0.333  32.281  50.186 1.00 16.33 ? 65  ALA C O   1
+ATOM   2682 C  CB  . ALA C 1 65  ? 0.470   30.251  52.620 1.00 16.15 ? 65  ALA C CB  1
+ATOM   2683 N  N   . LEU C 1 66  ? -1.697  30.499  50.348 1.00 17.13 ? 66  LEU C N   1
+ATOM   2684 C  CA  . LEU C 1 66  ? -2.065  30.439  48.927 1.00 13.55 ? 66  LEU C CA  1
+ATOM   2685 C  C   . LEU C 1 66  ? -2.841  31.631  48.590 1.00 14.32 ? 66  LEU C C   1
+ATOM   2686 O  O   . LEU C 1 66  ? -2.666  32.360  47.576 1.00 15.99 ? 66  LEU C O   1
+ATOM   2687 C  CB  . LEU C 1 66  ? -2.744  29.160  48.521 1.00 12.37 ? 66  LEU C CB  1
+ATOM   2688 C  CG  . LEU C 1 66  ? -1.704  27.929  48.478 1.00 14.22 ? 66  LEU C CG  1
+ATOM   2689 C  CD1 . LEU C 1 66  ? -2.488  26.860  48.518 1.00 25.53 ? 66  LEU C CD1 1
+ATOM   2690 C  CD2 . LEU C 1 66  ? -0.822  27.984  47.400 1.00 14.43 ? 66  LEU C CD2 1
+ATOM   2691 N  N   . THR C 1 67  ? -3.757  32.031  49.539 1.00 14.80 ? 67  THR C N   1
+ATOM   2692 C  CA  . THR C 1 67  ? -4.586  33.302  49.331 1.00 15.27 ? 67  THR C CA  1
+ATOM   2693 C  C   . THR C 1 67  ? -3.576  34.416  49.286 1.00 19.15 ? 67  THR C C   1
+ATOM   2694 O  O   . THR C 1 67  ? -3.756  35.264  48.398 1.00 21.53 ? 67  THR C O   1
+ATOM   2695 C  CB  . THR C 1 67  ? -5.506  33.327  50.606 1.00 13.22 ? 67  THR C CB  1
+ATOM   2696 O  OG1 . THR C 1 67  ? -6.463  32.350  50.524 1.00 17.30 ? 67  THR C OG1 1
+ATOM   2697 C  CG2 . THR C 1 67  ? -6.216  34.788  50.479 1.00 30.44 ? 67  THR C CG2 1
+ATOM   2698 N  N   . ASN C 1 68  ? -2.555  34.510  50.237 1.00 19.52 ? 68  ASN C N   1
+ATOM   2699 C  CA  . ASN C 1 68  ? -1.627  35.443  50.058 1.00 21.49 ? 68  ASN C CA  1
+ATOM   2700 C  C   . ASN C 1 68  ? -0.828  35.422  48.767 1.00 19.25 ? 68  ASN C C   1
+ATOM   2701 O  O   . ASN C 1 68  ? -0.410  36.683  48.126 1.00 22.73 ? 68  ASN C O   1
+ATOM   2702 C  CB  . ASN C 1 68  ? -0.748  35.427  51.279 1.00 16.47 ? 68  ASN C CB  1
+ATOM   2703 C  CG  . ASN C 1 68  ? 0.437   36.527  51.329 1.00 43.34 ? 68  ASN C CG  1
+ATOM   2704 O  OD1 . ASN C 1 68  ? 0.400   37.382  51.002 1.00 49.22 ? 68  ASN C OD1 1
+ATOM   2705 N  ND2 . ASN C 1 68  ? 1.865   36.112  51.739 1.00 50.67 ? 68  ASN C ND2 1
+ATOM   2706 N  N   . ALA C 1 69  ? -0.504  34.278  48.379 1.00 16.22 ? 69  ALA C N   1
+ATOM   2707 C  CA  . ALA C 1 69  ? 0.259   34.163  46.931 1.00 15.27 ? 69  ALA C CA  1
+ATOM   2708 C  C   . ALA C 1 69  ? -0.714  34.844  45.828 1.00 20.32 ? 69  ALA C C   1
+ATOM   2709 O  O   . ALA C 1 69  ? 0.001   35.361  44.937 1.00 22.38 ? 69  ALA C O   1
+ATOM   2710 C  CB  . ALA C 1 69  ? 0.666   32.749  46.769 1.00 15.52 ? 69  ALA C CB  1
+ATOM   2711 N  N   . VAL C 1 70  ? -1.927  34.331  45.895 1.00 18.62 ? 70  VAL C N   1
+ATOM   2712 C  CA  . VAL C 1 70  ? -2.964  34.974  44.745 1.00 21.72 ? 70  VAL C CA  1
+ATOM   2713 C  C   . VAL C 1 70  ? -2.916  36.702  44.954 1.00 33.94 ? 70  VAL C C   1
+ATOM   2714 O  O   . VAL C 1 70  ? -2.772  37.063  43.754 1.00 26.93 ? 70  VAL C O   1
+ATOM   2715 C  CB  . VAL C 1 70  ? -4.245  34.348  44.978 1.00 16.50 ? 70  VAL C CB  1
+ATOM   2716 C  CG1 . VAL C 1 70  ? -5.101  34.914  43.930 1.00 19.06 ? 70  VAL C CG1 1
+ATOM   2717 C  CG2 . VAL C 1 70  ? -4.240  32.837  44.692 1.00 16.14 ? 70  VAL C CG2 1
+ATOM   2718 N  N   . ALA C 1 71  ? -2.998  37.046  45.877 1.00 27.30 ? 71  ALA C N   1
+ATOM   2719 C  CA  . ALA C 1 71  ? -2.975  38.665  46.275 1.00 22.92 ? 71  ALA C CA  1
+ATOM   2720 C  C   . ALA C 1 71  ? -1.980  39.066  45.570 1.00 25.79 ? 71  ALA C C   1
+ATOM   2721 O  O   . ALA C 1 71  ? -1.732  40.323  45.271 1.00 24.88 ? 71  ALA C O   1
+ATOM   2722 C  CB  . ALA C 1 71  ? -3.349  38.894  47.479 1.00 26.73 ? 71  ALA C CB  1
+ATOM   2723 N  N   . HIS C 1 72  ? -0.734  38.591  45.606 1.00 25.11 ? 72  HIS C N   1
+ATOM   2724 C  CA  . HIS C 1 72  ? 0.467   38.729  45.190 1.00 31.54 ? 72  HIS C CA  1
+ATOM   2725 C  C   . HIS C 1 72  ? 1.149   38.415  44.263 1.00 23.73 ? 72  HIS C C   1
+ATOM   2726 O  O   . HIS C 1 72  ? 2.526   37.993  44.076 1.00 26.60 ? 72  HIS C O   1
+ATOM   2727 C  CB  . HIS C 1 72  ? 1.697   38.854  46.573 1.00 34.18 ? 72  HIS C CB  1
+ATOM   2728 C  CG  . HIS C 1 72  ? 1.215   39.460  47.510 1.00 46.84 ? 72  HIS C CG  1
+ATOM   2729 N  ND1 . HIS C 1 72  ? 1.429   41.195  47.922 1.00 41.84 ? 72  HIS C ND1 1
+ATOM   2730 C  CD2 . HIS C 1 72  ? 0.085   39.454  48.671 1.00 36.64 ? 72  HIS C CD2 1
+ATOM   2731 C  CE1 . HIS C 1 72  ? 0.953   41.315  48.864 1.00 46.81 ? 72  HIS C CE1 1
+ATOM   2732 N  NE2 . HIS C 1 72  ? 0.028   40.545  49.630 1.00 49.65 ? 72  HIS C NE2 1
+ATOM   2733 N  N   . VAL C 1 73  ? 0.382   37.854  43.241 1.00 19.28 ? 73  VAL C N   1
+ATOM   2734 C  CA  . VAL C 1 73  ? 0.868   37.050  42.293 1.00 19.45 ? 73  VAL C CA  1
+ATOM   2735 C  C   . VAL C 1 73  ? 2.226   37.610  41.462 1.00 29.84 ? 73  VAL C C   1
+ATOM   2736 O  O   . VAL C 1 73  ? 2.903   36.689  41.009 1.00 35.51 ? 73  VAL C O   1
+ATOM   2737 C  CB  . VAL C 1 73  ? -0.334  36.263  41.210 1.00 30.11 ? 73  VAL C CB  1
+ATOM   2738 C  CG1 . VAL C 1 73  ? -0.817  37.529  40.871 1.00 33.72 ? 73  VAL C CG1 1
+ATOM   2739 C  CG2 . VAL C 1 73  ? 0.274   35.077  40.729 1.00 28.74 ? 73  VAL C CG2 1
+ATOM   2740 N  N   . ASP C 1 74  ? 2.225   38.968  41.509 1.00 28.51 ? 74  ASP C N   1
+ATOM   2741 C  CA  . ASP C 1 74  ? 3.488   39.553  40.724 1.00 28.33 ? 74  ASP C CA  1
+ATOM   2742 C  C   . ASP C 1 74  ? 4.867   39.594  41.422 1.00 41.00 ? 74  ASP C C   1
+ATOM   2743 O  O   . ASP C 1 74  ? 5.472   40.117  40.994 1.00 39.68 ? 74  ASP C O   1
+ATOM   2744 C  CB  . ASP C 1 74  ? 2.869   40.877  40.194 1.00 34.16 ? 74  ASP C CB  1
+ATOM   2745 C  CG  . ASP C 1 74  ? 1.846   41.100  39.343 1.00 52.11 ? 74  ASP C CG  1
+ATOM   2746 O  OD1 . ASP C 1 74  ? 1.459   40.193  38.190 1.00 41.95 ? 74  ASP C OD1 1
+ATOM   2747 O  OD2 . ASP C 1 74  ? 0.818   41.596  39.286 1.00 57.27 ? 74  ASP C OD2 1
+ATOM   2748 N  N   . ASP C 1 75  ? 4.530   39.344  42.676 1.00 29.36 ? 75  ASP C N   1
+ATOM   2749 C  CA  . ASP C 1 75  ? 5.885   39.444  43.710 1.00 35.73 ? 75  ASP C CA  1
+ATOM   2750 C  C   . ASP C 1 75  ? 5.395   38.444  44.762 1.00 33.10 ? 75  ASP C C   1
+ATOM   2751 O  O   . ASP C 1 75  ? 5.862   38.605  45.862 1.00 33.04 ? 75  ASP C O   1
+ATOM   2752 C  CB  . ASP C 1 75  ? 5.626   40.888  44.363 1.00 60.97 ? 75  ASP C CB  1
+ATOM   2753 C  CG  . ASP C 1 75  ? 6.659   41.695  45.067 1.00 66.84 ? 75  ASP C CG  1
+ATOM   2754 O  OD1 . ASP C 1 75  ? 7.831   41.449  44.621 1.00 48.92 ? 75  ASP C OD1 1
+ATOM   2755 O  OD2 . ASP C 1 75  ? 5.778   41.915  46.066 1.00 62.98 ? 75  ASP C OD2 1
+ATOM   2756 N  N   . MET C 1 76  ? 5.509   37.013  44.084 1.00 27.58 ? 76  MET C N   1
+ATOM   2757 C  CA  . MET C 1 76  ? 5.590   35.936  45.135 1.00 27.89 ? 76  MET C CA  1
+ATOM   2758 C  C   . MET C 1 76  ? 6.688   35.707  45.849 1.00 27.58 ? 76  MET C C   1
+ATOM   2759 O  O   . MET C 1 76  ? 6.558   35.463  47.024 1.00 20.50 ? 76  MET C O   1
+ATOM   2760 C  CB  . MET C 1 76  ? 4.997   34.709  44.257 1.00 26.12 ? 76  MET C CB  1
+ATOM   2761 C  CG  . MET C 1 76  ? 3.522   34.862  44.023 1.00 43.36 ? 76  MET C CG  1
+ATOM   2762 S  SD  . MET C 1 76  ? 3.162   32.924  43.454 1.00 37.03 ? 76  MET C SD  1
+ATOM   2763 C  CE  . MET C 1 76  ? 3.949   32.921  42.030 1.00 44.39 ? 76  MET C CE  1
+ATOM   2764 N  N   . PRO C 1 77  ? 7.843   35.794  45.201 1.00 20.45 ? 77  PRO C N   1
+ATOM   2765 C  CA  . PRO C 1 77  ? 8.997   35.727  46.194 1.00 25.45 ? 77  PRO C CA  1
+ATOM   2766 C  C   . PRO C 1 77  ? 9.273   36.312  47.376 1.00 36.43 ? 77  PRO C C   1
+ATOM   2767 O  O   . PRO C 1 77  ? 9.598   35.903  48.495 1.00 30.57 ? 77  PRO C O   1
+ATOM   2768 C  CB  . PRO C 1 77  ? 10.181  35.844  45.094 1.00 26.13 ? 77  PRO C CB  1
+ATOM   2769 C  CG  . PRO C 1 77  ? 9.769   35.805  43.715 1.00 24.41 ? 77  PRO C CG  1
+ATOM   2770 C  CD  . PRO C 1 77  ? 8.272   36.272  43.940 1.00 18.39 ? 77  PRO C CD  1
+ATOM   2771 N  N   . ASN C 1 78  ? 8.931   37.605  47.478 1.00 27.78 ? 78  ASN C N   1
+ATOM   2772 C  CA  . ASN C 1 78  ? 8.609   38.419  48.607 1.00 53.47 ? 78  ASN C CA  1
+ATOM   2773 C  C   . ASN C 1 78  ? 7.967   38.184  49.523 1.00 25.06 ? 78  ASN C C   1
+ATOM   2774 O  O   . ASN C 1 78  ? 7.886   38.023  50.727 1.00 27.11 ? 78  ASN C O   1
+ATOM   2775 C  CB  . ASN C 1 78  ? 9.065   40.007  48.218 1.00 49.62 ? 78  ASN C CB  1
+ATOM   2776 C  CG  . ASN C 1 78  ? 9.222   41.034  49.645 1.00 27.09 ? 78  ASN C CG  1
+ATOM   2777 O  OD1 . ASN C 1 78  ? 10.057  40.641  50.404 1.00 25.78 ? 78  ASN C OD1 1
+ATOM   2778 N  ND2 . ASN C 1 78  ? 8.096   41.605  50.116 1.00 30.98 ? 78  ASN C ND2 1
+ATOM   2779 N  N   . ALA C 1 79  ? 6.568   38.027  49.002 1.00 21.32 ? 79  ALA C N   1
+ATOM   2780 C  CA  . ALA C 1 79  ? 5.525   37.695  49.876 1.00 21.47 ? 79  ALA C CA  1
+ATOM   2781 C  C   . ALA C 1 79  ? 5.612   36.303  50.715 1.00 24.81 ? 79  ALA C C   1
+ATOM   2782 O  O   . ALA C 1 79  ? 5.013   36.222  51.775 1.00 25.13 ? 79  ALA C O   1
+ATOM   2783 C  CB  . ALA C 1 79  ? 4.141   37.353  49.170 1.00 25.42 ? 79  ALA C CB  1
+ATOM   2784 N  N   . LEU C 1 80  ? 6.200   35.376  49.969 1.00 14.71 ? 80  LEU C N   1
+ATOM   2785 C  CA  . LEU C 1 80  ? 6.360   33.995  50.612 1.00 14.80 ? 80  LEU C CA  1
+ATOM   2786 C  C   . LEU C 1 80  ? 7.916   33.751  51.078 1.00 13.69 ? 80  LEU C C   1
+ATOM   2787 O  O   . LEU C 1 80  ? 8.155   32.670  51.532 1.00 17.02 ? 80  LEU C O   1
+ATOM   2788 C  CB  . LEU C 1 80  ? 6.213   32.969  49.595 1.00 23.31 ? 80  LEU C CB  1
+ATOM   2789 C  CG  . LEU C 1 80  ? 4.744   32.939  48.817 1.00 28.90 ? 80  LEU C CG  1
+ATOM   2790 C  CD1 . LEU C 1 80  ? 4.636   31.790  47.883 1.00 22.59 ? 80  LEU C CD1 1
+ATOM   2791 C  CD2 . LEU C 1 80  ? 3.876   32.793  49.926 1.00 28.24 ? 80  LEU C CD2 1
+ATOM   2792 N  N   . SER C 1 81  ? 8.637   34.957  51.321 1.00 15.20 ? 81  SER C N   1
+ATOM   2793 C  CA  . SER C 1 81  ? 10.118  34.769  51.745 1.00 16.69 ? 81  SER C CA  1
+ATOM   2794 C  C   . SER C 1 81  ? 10.171  34.025  53.099 1.00 15.66 ? 81  SER C C   1
+ATOM   2795 O  O   . SER C 1 81  ? 11.015  33.176  53.201 1.00 18.30 ? 81  SER C O   1
+ATOM   2796 C  CB  . SER C 1 81  ? 10.370  36.393  51.992 1.00 20.04 ? 81  SER C CB  1
+ATOM   2797 O  OG  . SER C 1 81  ? 11.885  36.133  51.935 1.00 27.86 ? 81  SER C OG  1
+ATOM   2798 N  N   . ALA C 1 82  ? 9.386   34.439  54.044 1.00 16.14 ? 82  ALA C N   1
+ATOM   2799 C  CA  . ALA C 1 82  ? 9.652   33.701  55.293 1.00 27.63 ? 82  ALA C CA  1
+ATOM   2800 C  C   . ALA C 1 82  ? 9.432   32.330  55.324 1.00 26.48 ? 82  ALA C C   1
+ATOM   2801 O  O   . ALA C 1 82  ? 9.785   31.358  55.981 1.00 22.53 ? 82  ALA C O   1
+ATOM   2802 C  CB  . ALA C 1 82  ? 8.850   34.409  56.391 1.00 26.01 ? 82  ALA C CB  1
+ATOM   2803 N  N   . LEU C 1 83  ? 8.152   31.833  54.342 1.00 16.69 ? 83  LEU C N   1
+ATOM   2804 C  CA  . LEU C 1 83  ? 7.896   30.456  54.448 1.00 11.24 ? 83  LEU C CA  1
+ATOM   2805 C  C   . LEU C 1 83  ? 8.856   29.779  53.416 1.00 14.18 ? 83  LEU C C   1
+ATOM   2806 O  O   . LEU C 1 83  ? 9.185   28.509  53.818 1.00 18.82 ? 83  LEU C O   1
+ATOM   2807 C  CB  . LEU C 1 83  ? 6.600   30.419  53.464 1.00 19.57 ? 83  LEU C CB  1
+ATOM   2808 C  CG  . LEU C 1 83  ? 5.369   30.425  54.513 1.00 31.08 ? 83  LEU C CG  1
+ATOM   2809 C  CD1 . LEU C 1 83  ? 4.117   30.125  53.531 1.00 37.56 ? 83  LEU C CD1 1
+ATOM   2810 C  CD2 . LEU C 1 83  ? 5.455   29.578  55.768 1.00 31.25 ? 83  LEU C CD2 1
+ATOM   2811 N  N   . SER C 1 84  ? 9.482   30.403  52.535 1.00 17.80 ? 84  SER C N   1
+ATOM   2812 C  CA  . SER C 1 84  ? 10.629  29.798  51.849 1.00 16.31 ? 84  SER C CA  1
+ATOM   2813 C  C   . SER C 1 84  ? 11.796  29.506  52.710 1.00 16.72 ? 84  SER C C   1
+ATOM   2814 O  O   . SER C 1 84  ? 12.511  28.523  52.756 1.00 20.08 ? 84  SER C O   1
+ATOM   2815 C  CB  . SER C 1 84  ? 11.633  30.458  50.520 1.00 25.74 ? 84  SER C CB  1
+ATOM   2816 O  OG  . SER C 1 84  ? 10.617  30.948  50.170 1.00 36.74 ? 84  SER C OG  1
+ATOM   2817 N  N   . ASP C 1 85  ? 12.093  30.572  53.672 1.00 14.56 ? 85  ASP C N   1
+ATOM   2818 C  CA  . ASP C 1 85  ? 13.100  30.213  54.746 1.00 16.51 ? 85  ASP C CA  1
+ATOM   2819 C  C   . ASP C 1 85  ? 12.859  29.115  55.613 1.00 12.46 ? 85  ASP C C   1
+ATOM   2820 O  O   . ASP C 1 85  ? 13.619  28.317  55.928 1.00 15.88 ? 85  ASP C O   1
+ATOM   2821 C  CB  . ASP C 1 85  ? 13.262  31.435  55.481 1.00 24.70 ? 85  ASP C CB  1
+ATOM   2822 C  CG  . ASP C 1 85  ? 13.998  32.536  54.769 1.00 34.11 ? 85  ASP C CG  1
+ATOM   2823 O  OD1 . ASP C 1 85  ? 14.572  32.547  53.890 1.00 25.15 ? 85  ASP C OD1 1
+ATOM   2824 O  OD2 . ASP C 1 85  ? 13.760  33.689  55.473 1.00 33.76 ? 85  ASP C OD2 1
+ATOM   2825 N  N   . LEU C 1 86  ? 11.448  29.029  55.948 1.00 12.70 ? 86  LEU C N   1
+ATOM   2826 C  CA  . LEU C 1 86  ? 11.064  28.076  56.832 1.00 16.53 ? 86  LEU C CA  1
+ATOM   2827 C  C   . LEU C 1 86  ? 11.267  26.602  56.520 1.00 14.13 ? 86  LEU C C   1
+ATOM   2828 O  O   . LEU C 1 86  ? 11.744  25.686  56.985 1.00 17.79 ? 86  LEU C O   1
+ATOM   2829 C  CB  . LEU C 1 86  ? 9.587   28.289  57.256 1.00 18.93 ? 86  LEU C CB  1
+ATOM   2830 C  CG  . LEU C 1 86  ? 8.993   27.495  58.443 1.00 29.36 ? 86  LEU C CG  1
+ATOM   2831 C  CD1 . LEU C 1 86  ? 9.803   27.626  59.742 1.00 25.18 ? 86  LEU C CD1 1
+ATOM   2832 C  CD2 . LEU C 1 86  ? 7.577   27.659  58.611 1.00 37.62 ? 86  LEU C CD2 1
+ATOM   2833 N  N   . HIS C 1 87  ? 10.837  26.530  55.161 1.00 15.64 ? 87  HIS C N   1
+ATOM   2834 C  CA  . HIS C 1 87  ? 10.746  25.173  54.651 1.00 15.27 ? 87  HIS C CA  1
+ATOM   2835 C  C   . HIS C 1 87  ? 12.425  24.652  54.183 1.00 11.96 ? 87  HIS C C   1
+ATOM   2836 O  O   . HIS C 1 87  ? 12.684  23.500  54.475 1.00 15.54 ? 87  HIS C O   1
+ATOM   2837 C  CB  . HIS C 1 87  ? 9.939   24.941  53.282 1.00 15.31 ? 87  HIS C CB  1
+ATOM   2838 C  CG  . HIS C 1 87  ? 8.455   25.010  53.631 1.00 12.16 ? 87  HIS C CG  1
+ATOM   2839 N  ND1 . HIS C 1 87  ? 7.809   26.108  54.024 1.00 15.96 ? 87  HIS C ND1 1
+ATOM   2840 C  CD2 . HIS C 1 87  ? 7.491   23.932  53.862 1.00 14.58 ? 87  HIS C CD2 1
+ATOM   2841 C  CE1 . HIS C 1 87  ? 6.446   25.748  54.351 1.00 13.46 ? 87  HIS C CE1 1
+ATOM   2842 N  NE2 . HIS C 1 87  ? 6.358   24.601  54.168 1.00 17.27 ? 87  HIS C NE2 1
+ATOM   2843 N  N   . ALA C 1 88  ? 13.128  25.779  53.770 1.00 14.25 ? 88  ALA C N   1
+ATOM   2844 C  CA  . ALA C 1 88  ? 14.424  25.541  53.419 1.00 15.37 ? 88  ALA C CA  1
+ATOM   2845 C  C   . ALA C 1 88  ? 15.369  24.911  54.659 1.00 19.72 ? 88  ALA C C   1
+ATOM   2846 O  O   . ALA C 1 88  ? 16.269  24.187  54.401 1.00 18.60 ? 88  ALA C O   1
+ATOM   2847 C  CB  . ALA C 1 88  ? 15.128  26.614  52.626 1.00 17.41 ? 88  ALA C CB  1
+ATOM   2848 N  N   . HIS C 1 89  ? 15.312  25.858  55.662 1.00 17.52 ? 89  HIS C N   1
+ATOM   2849 C  CA  . HIS C 1 89  ? 16.108  25.828  56.944 1.00 20.01 ? 89  HIS C CA  1
+ATOM   2850 C  C   . HIS C 1 89  ? 15.626  25.038  58.032 1.00 19.52 ? 89  HIS C C   1
+ATOM   2851 O  O   . HIS C 1 89  ? 16.552  24.515  58.765 1.00 22.69 ? 89  HIS C O   1
+ATOM   2852 C  CB  . HIS C 1 89  ? 16.708  27.283  57.158 1.00 26.82 ? 89  HIS C CB  1
+ATOM   2853 C  CG  . HIS C 1 89  ? 17.416  27.775  55.845 1.00 23.76 ? 89  HIS C CG  1
+ATOM   2854 N  ND1 . HIS C 1 89  ? 18.429  27.194  55.146 1.00 28.14 ? 89  HIS C ND1 1
+ATOM   2855 C  CD2 . HIS C 1 89  ? 17.017  28.929  55.440 1.00 25.55 ? 89  HIS C CD2 1
+ATOM   2856 C  CE1 . HIS C 1 89  ? 18.333  28.062  54.262 1.00 32.36 ? 89  HIS C CE1 1
+ATOM   2857 N  NE2 . HIS C 1 89  ? 17.821  29.133  54.211 1.00 29.26 ? 89  HIS C NE2 1
+ATOM   2858 N  N   . LYS C 1 90  ? 14.465  24.732  58.206 1.00 16.72 ? 90  LYS C N   1
+ATOM   2859 C  CA  . LYS C 1 90  ? 13.834  24.344  59.285 1.00 20.32 ? 90  LYS C CA  1
+ATOM   2860 C  C   . LYS C 1 90  ? 13.157  22.884  59.012 1.00 20.91 ? 90  LYS C C   1
+ATOM   2861 O  O   . LYS C 1 90  ? 13.569  21.761  59.394 1.00 23.22 ? 90  LYS C O   1
+ATOM   2862 C  CB  . LYS C 1 90  ? 13.156  25.174  60.278 1.00 20.81 ? 90  LYS C CB  1
+ATOM   2863 C  CG  . LYS C 1 90  ? 12.604  24.065  61.250 1.00 29.14 ? 90  LYS C CG  1
+ATOM   2864 C  CD  . LYS C 1 90  ? 11.672  25.465  62.126 1.00 67.74 ? 90  LYS C CD  1
+ATOM   2865 C  CE  . LYS C 1 90  ? 11.530  24.314  63.641 1.00 66.29 ? 90  LYS C CE  1
+ATOM   2866 N  NZ  . LYS C 1 90  ? 11.982  25.980  64.771 1.00 56.99 ? 90  LYS C NZ  1
+ATOM   2867 N  N   . LEU C 1 91  ? 11.960  22.979  58.221 1.00 13.37 ? 91  LEU C N   1
+ATOM   2868 C  CA  . LEU C 1 91  ? 11.199  21.743  57.916 1.00 10.47 ? 91  LEU C CA  1
+ATOM   2869 C  C   . LEU C 1 91  ? 12.003  20.807  57.005 1.00 15.87 ? 91  LEU C C   1
+ATOM   2870 O  O   . LEU C 1 91  ? 11.885  19.655  57.161 1.00 17.45 ? 91  LEU C O   1
+ATOM   2871 C  CB  . LEU C 1 91  ? 9.910   22.430  57.324 1.00 11.80 ? 91  LEU C CB  1
+ATOM   2872 C  CG  . LEU C 1 91  ? 9.330   23.372  58.169 1.00 14.59 ? 91  LEU C CG  1
+ATOM   2873 C  CD1 . LEU C 1 91  ? 8.038   23.895  57.411 1.00 18.31 ? 91  LEU C CD1 1
+ATOM   2874 C  CD2 . LEU C 1 91  ? 8.831   22.522  59.350 1.00 19.42 ? 91  LEU C CD2 1
+ATOM   2875 N  N   . ARG C 1 92  ? 12.593  21.341  55.914 1.00 17.30 ? 92  ARG C N   1
+ATOM   2876 C  CA  . ARG C 1 92  ? 13.509  20.619  55.120 1.00 16.69 ? 92  ARG C CA  1
+ATOM   2877 C  C   . ARG C 1 92  ? 12.834  19.342  54.438 1.00 18.80 ? 92  ARG C C   1
+ATOM   2878 O  O   . ARG C 1 92  ? 13.165  18.365  54.335 1.00 19.26 ? 92  ARG C O   1
+ATOM   2879 C  CB  . ARG C 1 92  ? 14.738  20.166  55.937 1.00 13.64 ? 92  ARG C CB  1
+ATOM   2880 C  CG  . ARG C 1 92  ? 15.688  21.358  55.981 1.00 14.42 ? 92  ARG C CG  1
+ATOM   2881 C  CD  . ARG C 1 92  ? 16.829  21.078  56.977 1.00 27.16 ? 92  ARG C CD  1
+ATOM   2882 N  NE  . ARG C 1 92  ? 17.564  21.770  56.604 1.00 44.94 ? 92  ARG C NE  1
+ATOM   2883 C  CZ  . ARG C 1 92  ? 18.480  21.111  59.346 1.00 38.22 ? 92  ARG C CZ  1
+ATOM   2884 N  NH1 . ARG C 1 92  ? 16.729  21.065  59.997 1.00 33.94 ? 92  ARG C NH1 1
+ATOM   2885 N  NH2 . ARG C 1 92  ? 18.734  21.606  58.537 1.00 48.21 ? 92  ARG C NH2 1
+ATOM   2886 N  N   . VAL C 1 93  ? 11.538  19.751  53.894 1.00 13.36 ? 93  VAL C N   1
+ATOM   2887 C  CA  . VAL C 1 93  ? 10.712  18.740  53.156 1.00 14.31 ? 93  VAL C CA  1
+ATOM   2888 C  C   . VAL C 1 93  ? 11.315  18.588  51.756 1.00 12.63 ? 93  VAL C C   1
+ATOM   2889 O  O   . VAL C 1 93  ? 11.579  19.505  50.967 1.00 14.78 ? 93  VAL C O   1
+ATOM   2890 C  CB  . VAL C 1 93  ? 9.298   19.482  52.944 1.00 8.72  ? 93  VAL C CB  1
+ATOM   2891 C  CG1 . VAL C 1 93  ? 8.421   18.612  52.058 1.00 14.83 ? 93  VAL C CG1 1
+ATOM   2892 C  CG2 . VAL C 1 93  ? 8.779   19.770  54.303 1.00 15.34 ? 93  VAL C CG2 1
+ATOM   2893 N  N   . ASP C 1 94  ? 11.452  17.326  51.402 1.00 14.84 ? 94  ASP C N   1
+ATOM   2894 C  CA  . ASP C 1 94  ? 11.938  17.096  50.160 1.00 17.19 ? 94  ASP C CA  1
+ATOM   2895 C  C   . ASP C 1 94  ? 11.101  17.682  49.011 1.00 13.94 ? 94  ASP C C   1
+ATOM   2896 O  O   . ASP C 1 94  ? 9.902   17.524  49.052 1.00 13.55 ? 94  ASP C O   1
+ATOM   2897 C  CB  . ASP C 1 94  ? 12.158  15.544  49.790 1.00 19.19 ? 94  ASP C CB  1
+ATOM   2898 C  CG  . ASP C 1 94  ? 13.118  15.221  48.591 1.00 25.98 ? 94  ASP C CG  1
+ATOM   2899 O  OD1 . ASP C 1 94  ? 14.178  15.051  48.683 1.00 23.44 ? 94  ASP C OD1 1
+ATOM   2900 O  OD2 . ASP C 1 94  ? 12.454  15.350  47.423 1.00 20.10 ? 94  ASP C OD2 1
+ATOM   2901 N  N   . PRO C 1 95  ? 11.830  18.304  48.068 1.00 13.43 ? 95  PRO C N   1
+ATOM   2902 C  CA  . PRO C 1 95  ? 10.996  19.018  46.888 1.00 16.10 ? 95  PRO C CA  1
+ATOM   2903 C  C   . PRO C 1 95  ? 10.224  18.168  46.192 1.00 11.12 ? 95  PRO C C   1
+ATOM   2904 O  O   . PRO C 1 95  ? 9.068   18.760  45.798 1.00 14.55 ? 95  PRO C O   1
+ATOM   2905 C  CB  . PRO C 1 95  ? 12.085  19.500  46.035 1.00 19.09 ? 95  PRO C CB  1
+ATOM   2906 C  CG  . PRO C 1 95  ? 13.094  19.636  46.885 1.00 18.28 ? 95  PRO C CG  1
+ATOM   2907 C  CD  . PRO C 1 95  ? 13.251  18.567  47.906 1.00 15.64 ? 95  PRO C CD  1
+ATOM   2908 N  N   . VAL C 1 96  ? 10.140  16.784  46.061 1.00 15.60 ? 96  VAL C N   1
+ATOM   2909 C  CA  . VAL C 1 96  ? 9.246   15.972  45.364 1.00 13.24 ? 96  VAL C CA  1
+ATOM   2910 C  C   . VAL C 1 96  ? 7.869   16.060  45.968 1.00 11.50 ? 96  VAL C C   1
+ATOM   2911 O  O   . VAL C 1 96  ? 6.766   15.959  45.278 1.00 13.19 ? 96  VAL C O   1
+ATOM   2912 C  CB  . VAL C 1 96  ? 9.748   14.492  45.448 1.00 20.64 ? 96  VAL C CB  1
+ATOM   2913 C  CG1 . VAL C 1 96  ? 11.097  14.613  44.875 1.00 37.75 ? 96  VAL C CG1 1
+ATOM   2914 C  CG2 . VAL C 1 96  ? 9.660   13.703  46.544 1.00 28.85 ? 96  VAL C CG2 1
+ATOM   2915 N  N   . ASN C 1 97  ? 7.721   16.361  47.299 1.00 9.54  ? 97  ASN C N   1
+ATOM   2916 C  CA  . ASN C 1 97  ? 6.477   16.380  47.914 1.00 11.68 ? 97  ASN C CA  1
+ATOM   2917 C  C   . ASN C 1 97  ? 5.596   17.457  47.476 1.00 9.63  ? 97  ASN C C   1
+ATOM   2918 O  O   . ASN C 1 97  ? 4.322   17.366  47.757 1.00 9.95  ? 97  ASN C O   1
+ATOM   2919 C  CB  . ASN C 1 97  ? 6.746   16.339  49.271 1.00 13.42 ? 97  ASN C CB  1
+ATOM   2920 C  CG  . ASN C 1 97  ? 7.408   15.010  49.836 1.00 14.06 ? 97  ASN C CG  1
+ATOM   2921 O  OD1 . ASN C 1 97  ? 6.812   13.835  49.789 1.00 8.45  ? 97  ASN C OD1 1
+ATOM   2922 N  ND2 . ASN C 1 97  ? 8.678   15.082  50.104 1.00 18.92 ? 97  ASN C ND2 1
+ATOM   2923 N  N   . PHE C 1 98  ? 6.158   18.530  47.091 1.00 11.20 ? 98  PHE C N   1
+ATOM   2924 C  CA  . PHE C 1 98  ? 5.465   19.706  46.666 1.00 10.00 ? 98  PHE C CA  1
+ATOM   2925 C  C   . PHE C 1 98  ? 4.407   19.340  45.460 1.00 12.29 ? 98  PHE C C   1
+ATOM   2926 O  O   . PHE C 1 98  ? 3.261   19.812  45.454 1.00 11.85 ? 98  PHE C O   1
+ATOM   2927 C  CB  . PHE C 1 98  ? 6.221   20.972  46.362 1.00 11.84 ? 98  PHE C CB  1
+ATOM   2928 C  CG  . PHE C 1 98  ? 6.937   21.463  47.656 1.00 10.85 ? 98  PHE C CG  1
+ATOM   2929 C  CD1 . PHE C 1 98  ? 6.300   22.484  48.369 1.00 20.50 ? 98  PHE C CD1 1
+ATOM   2930 C  CD2 . PHE C 1 98  ? 7.951   20.865  48.164 1.00 15.66 ? 98  PHE C CD2 1
+ATOM   2931 C  CE1 . PHE C 1 98  ? 6.698   23.019  49.537 1.00 25.62 ? 98  PHE C CE1 1
+ATOM   2932 C  CE2 . PHE C 1 98  ? 8.301   21.552  49.424 1.00 23.17 ? 98  PHE C CE2 1
+ATOM   2933 C  CZ  . PHE C 1 98  ? 7.862   22.617  50.141 1.00 16.17 ? 98  PHE C CZ  1
+ATOM   2934 N  N   . LYS C 1 99  ? 4.960   18.468  44.643 1.00 12.40 ? 99  LYS C N   1
+ATOM   2935 C  CA  . LYS C 1 99  ? 4.086   18.035  43.543 1.00 16.89 ? 99  LYS C CA  1
+ATOM   2936 C  C   . LYS C 1 99  ? 2.784   17.449  43.881 1.00 16.36 ? 99  LYS C C   1
+ATOM   2937 O  O   . LYS C 1 99  ? 1.848   17.341  43.293 1.00 12.00 ? 99  LYS C O   1
+ATOM   2938 C  CB  . LYS C 1 99  ? 4.955   17.342  42.343 1.00 37.75 ? 99  LYS C CB  1
+ATOM   2939 C  CG  . LYS C 1 99  ? 5.174   16.640  42.279 1.00 60.42 ? 99  LYS C CG  1
+ATOM   2940 C  CD  . LYS C 1 99  ? 6.092   15.824  40.934 1.00 80.12 ? 99  LYS C CD  1
+ATOM   2941 C  CE  . LYS C 1 99  ? 5.178   13.849  41.548 1.00 54.41 ? 99  LYS C CE  1
+ATOM   2942 N  NZ  . LYS C 1 99  ? 6.043   12.581  41.219 1.00 73.17 ? 99  LYS C NZ  1
+ATOM   2943 N  N   . LEU C 1 100 ? 3.148   16.575  44.955 1.00 11.58 ? 100 LEU C N   1
+ATOM   2944 C  CA  . LEU C 1 100 ? 2.119   15.611  45.595 1.00 10.08 ? 100 LEU C CA  1
+ATOM   2945 C  C   . LEU C 1 100 ? 1.020   16.499  46.129 1.00 15.81 ? 100 LEU C C   1
+ATOM   2946 O  O   . LEU C 1 100 ? -0.161  16.244  45.902 1.00 12.64 ? 100 LEU C O   1
+ATOM   2947 C  CB  . LEU C 1 100 ? 2.753   14.528  46.440 1.00 11.52 ? 100 LEU C CB  1
+ATOM   2948 C  CG  . LEU C 1 100 ? 3.848   13.813  45.983 1.00 12.29 ? 100 LEU C CG  1
+ATOM   2949 C  CD1 . LEU C 1 100 ? 4.308   12.786  46.984 1.00 13.43 ? 100 LEU C CD1 1
+ATOM   2950 C  CD2 . LEU C 1 100 ? 3.435   13.174  44.764 1.00 20.82 ? 100 LEU C CD2 1
+ATOM   2951 N  N   . LEU C 1 101 ? 1.389   17.493  46.966 1.00 9.97  ? 101 LEU C N   1
+ATOM   2952 C  CA  . LEU C 1 101 ? 0.303   18.207  47.579 1.00 11.48 ? 101 LEU C CA  1
+ATOM   2953 C  C   . LEU C 1 101 ? -0.403  19.108  46.409 1.00 15.63 ? 101 LEU C C   1
+ATOM   2954 O  O   . LEU C 1 101 ? -1.613  19.226  46.568 1.00 14.14 ? 101 LEU C O   1
+ATOM   2955 C  CB  . LEU C 1 101 ? 0.919   19.253  48.600 1.00 14.89 ? 101 LEU C CB  1
+ATOM   2956 C  CG  . LEU C 1 101 ? 0.010   20.153  49.167 1.00 22.22 ? 101 LEU C CG  1
+ATOM   2957 C  CD1 . LEU C 1 101 ? -1.249  19.367  49.738 1.00 22.49 ? 101 LEU C CD1 1
+ATOM   2958 C  CD2 . LEU C 1 101 ? 0.632   20.912  50.281 1.00 23.89 ? 101 LEU C CD2 1
+ATOM   2959 N  N   . SER C 1 102 ? 0.350   19.583  45.409 1.00 13.80 ? 102 SER C N   1
+ATOM   2960 C  CA  . SER C 1 102 ? -0.254  20.469  44.437 1.00 7.27  ? 102 SER C CA  1
+ATOM   2961 C  C   . SER C 1 102 ? -1.281  19.505  43.715 1.00 8.13  ? 102 SER C C   1
+ATOM   2962 O  O   . SER C 1 102 ? -2.395  20.144  43.427 1.00 14.48 ? 102 SER C O   1
+ATOM   2963 C  CB  . SER C 1 102 ? 0.852   20.834  43.461 1.00 12.53 ? 102 SER C CB  1
+ATOM   2964 O  OG  . SER C 1 102 ? 1.766   21.783  44.015 1.00 16.99 ? 102 SER C OG  1
+ATOM   2965 N  N   . HIS C 1 103 ? -0.971  18.289  43.358 1.00 9.47  ? 103 HIS C N   1
+ATOM   2966 C  CA  . HIS C 1 103 ? -1.998  17.473  42.647 1.00 7.87  ? 103 HIS C CA  1
+ATOM   2967 C  C   . HIS C 1 103 ? -3.098  17.345  43.514 1.00 9.96  ? 103 HIS C C   1
+ATOM   2968 O  O   . HIS C 1 103 ? -4.313  17.375  43.052 1.00 11.06 ? 103 HIS C O   1
+ATOM   2969 C  CB  . HIS C 1 103 ? -1.401  16.127  42.490 1.00 13.28 ? 103 HIS C CB  1
+ATOM   2970 C  CG  . HIS C 1 103 ? -2.249  15.127  41.871 1.00 12.69 ? 103 HIS C CG  1
+ATOM   2971 N  ND1 . HIS C 1 103 ? -2.654  13.891  42.776 1.00 13.59 ? 103 HIS C ND1 1
+ATOM   2972 C  CD2 . HIS C 1 103 ? -2.926  15.085  40.776 1.00 11.80 ? 103 HIS C CD2 1
+ATOM   2973 C  CE1 . HIS C 1 103 ? -3.485  13.297  41.750 1.00 18.03 ? 103 HIS C CE1 1
+ATOM   2974 N  NE2 . HIS C 1 103 ? -3.703  13.879  40.535 1.00 12.75 ? 103 HIS C NE2 1
+ATOM   2975 N  N   . CYS C 1 104 ? -3.053  17.083  44.815 1.00 11.32 ? 104 CYS C N   1
+ATOM   2976 C  CA  . CYS C 1 104 ? -4.179  16.941  45.851 1.00 10.36 ? 104 CYS C CA  1
+ATOM   2977 C  C   . CYS C 1 104 ? -5.004  18.267  45.893 1.00 10.40 ? 104 CYS C C   1
+ATOM   2978 O  O   . CYS C 1 104 ? -6.231  18.125  46.088 1.00 13.45 ? 104 CYS C O   1
+ATOM   2979 C  CB  . CYS C 1 104 ? -3.766  16.377  47.166 1.00 10.60 ? 104 CYS C CB  1
+ATOM   2980 S  SG  . CYS C 1 104 ? -3.115  14.679  47.003 1.00 14.84 ? 104 CYS C SG  1
+ATOM   2981 N  N   . LEU C 1 105 ? -4.306  19.356  45.843 1.00 7.19  ? 105 LEU C N   1
+ATOM   2982 C  CA  . LEU C 1 105 ? -5.085  20.449  45.809 1.00 7.94  ? 105 LEU C CA  1
+ATOM   2983 C  C   . LEU C 1 105 ? -5.912  20.552  44.514 1.00 12.20 ? 105 LEU C C   1
+ATOM   2984 O  O   . LEU C 1 105 ? -7.090  21.066  44.613 1.00 10.34 ? 105 LEU C O   1
+ATOM   2985 C  CB  . LEU C 1 105 ? -4.202  21.664  45.904 1.00 21.49 ? 105 LEU C CB  1
+ATOM   2986 C  CG  . LEU C 1 105 ? -4.625  22.955  46.383 1.00 44.61 ? 105 LEU C CG  1
+ATOM   2987 C  CD1 . LEU C 1 105 ? -4.563  22.839  48.167 1.00 29.90 ? 105 LEU C CD1 1
+ATOM   2988 C  CD2 . LEU C 1 105 ? -2.601  23.530  46.634 1.00 67.41 ? 105 LEU C CD2 1
+ATOM   2989 N  N   . LEU C 1 106 ? -5.249  20.342  43.470 1.00 12.01 ? 106 LEU C N   1
+ATOM   2990 C  CA  . LEU C 1 106 ? -6.190  20.220  42.204 1.00 11.59 ? 106 LEU C CA  1
+ATOM   2991 C  C   . LEU C 1 106 ? -7.255  19.431  42.339 1.00 13.18 ? 106 LEU C C   1
+ATOM   2992 O  O   . LEU C 1 106 ? -8.344  19.865  41.835 1.00 13.67 ? 106 LEU C O   1
+ATOM   2993 C  CB  . LEU C 1 106 ? -5.266  20.087  40.885 1.00 15.01 ? 106 LEU C CB  1
+ATOM   2994 C  CG  . LEU C 1 106 ? -4.403  21.055  40.323 1.00 26.98 ? 106 LEU C CG  1
+ATOM   2995 C  CD1 . LEU C 1 106 ? -3.674  20.399  39.338 1.00 27.15 ? 106 LEU C CD1 1
+ATOM   2996 C  CD2 . LEU C 1 106 ? -4.971  22.437  40.008 1.00 28.82 ? 106 LEU C CD2 1
+ATOM   2997 N  N   . VAL C 1 107 ? -7.225  18.240  42.735 1.00 9.69  ? 107 VAL C N   1
+ATOM   2998 C  CA  . VAL C 1 107 ? -8.097  17.151  42.999 1.00 13.59 ? 107 VAL C CA  1
+ATOM   2999 C  C   . VAL C 1 107 ? -9.334  17.761  43.796 1.00 17.84 ? 107 VAL C C   1
+ATOM   3000 O  O   . VAL C 1 107 ? -10.605 17.851  43.570 1.00 16.17 ? 107 VAL C O   1
+ATOM   3001 C  CB  . VAL C 1 107 ? -7.686  15.819  43.488 1.00 6.66  ? 107 VAL C CB  1
+ATOM   3002 C  CG1 . VAL C 1 107 ? -8.867  15.071  43.857 1.00 10.41 ? 107 VAL C CG1 1
+ATOM   3003 C  CG2 . VAL C 1 107 ? -6.824  15.228  42.429 1.00 9.95  ? 107 VAL C CG2 1
+ATOM   3004 N  N   . THR C 1 108 ? -8.969  18.530  44.900 1.00 12.50 ? 108 THR C N   1
+ATOM   3005 C  CA  . THR C 1 108 ? -9.983  19.048  45.826 1.00 12.00 ? 108 THR C CA  1
+ATOM   3006 C  C   . THR C 1 108 ? -10.703 20.192  45.053 1.00 8.53  ? 108 THR C C   1
+ATOM   3007 O  O   . THR C 1 108 ? -11.945 20.338  45.325 1.00 13.95 ? 108 THR C O   1
+ATOM   3008 C  CB  . THR C 1 108 ? -9.141  19.631  47.079 1.00 10.15 ? 108 THR C CB  1
+ATOM   3009 O  OG1 . THR C 1 108 ? -8.397  18.582  47.585 1.00 10.65 ? 108 THR C OG1 1
+ATOM   3010 C  CG2 . THR C 1 108 ? -10.079 20.284  48.088 1.00 9.30  ? 108 THR C CG2 1
+ATOM   3011 N  N   . LEU C 1 109 ? -10.021 21.063  44.371 1.00 9.01  ? 109 LEU C N   1
+ATOM   3012 C  CA  . LEU C 1 109 ? -10.721 22.186  43.590 1.00 9.31  ? 109 LEU C CA  1
+ATOM   3013 C  C   . LEU C 1 109 ? -11.750 21.501  42.850 1.00 15.85 ? 109 LEU C C   1
+ATOM   3014 O  O   . LEU C 1 109 ? -12.733 22.037  42.548 1.00 14.26 ? 109 LEU C O   1
+ATOM   3015 C  CB  . LEU C 1 109 ? -9.635  23.068  43.064 1.00 11.02 ? 109 LEU C CB  1
+ATOM   3016 C  CG  . LEU C 1 109 ? -8.837  24.041  43.987 1.00 19.91 ? 109 LEU C CG  1
+ATOM   3017 C  CD1 . LEU C 1 109 ? -7.614  24.623  43.185 1.00 29.96 ? 109 LEU C CD1 1
+ATOM   3018 C  CD2 . LEU C 1 109 ? -9.618  24.633  44.864 1.00 27.29 ? 109 LEU C CD2 1
+ATOM   3019 N  N   . ALA C 1 110 ? -11.190 20.497  41.906 1.00 14.51 ? 110 ALA C N   1
+ATOM   3020 C  CA  . ALA C 1 110 ? -12.000 19.763  40.820 1.00 13.69 ? 110 ALA C CA  1
+ATOM   3021 C  C   . ALA C 1 110 ? -13.227 19.487  41.499 1.00 24.66 ? 110 ALA C C   1
+ATOM   3022 O  O   . ALA C 1 110 ? -14.452 19.395  40.917 1.00 18.31 ? 110 ALA C O   1
+ATOM   3023 C  CB  . ALA C 1 110 ? -11.178 18.668  40.227 1.00 13.14 ? 110 ALA C CB  1
+ATOM   3024 N  N   . ALA C 1 111 ? -13.205 18.738  42.734 1.00 17.30 ? 111 ALA C N   1
+ATOM   3025 C  CA  . ALA C 1 111 ? -14.305 18.098  43.459 1.00 14.98 ? 111 ALA C CA  1
+ATOM   3026 C  C   . ALA C 1 111 ? -15.388 19.256  43.865 1.00 17.59 ? 111 ALA C C   1
+ATOM   3027 O  O   . ALA C 1 111 ? -16.435 18.699  44.301 1.00 18.70 ? 111 ALA C O   1
+ATOM   3028 C  CB  . ALA C 1 111 ? -13.757 17.297  44.599 1.00 14.01 ? 111 ALA C CB  1
+ATOM   3029 N  N   . HIS C 1 112 ? -14.920 20.402  44.183 1.00 17.57 ? 112 HIS C N   1
+ATOM   3030 C  CA  . HIS C 1 112 ? -15.737 21.504  44.746 1.00 17.81 ? 112 HIS C CA  1
+ATOM   3031 C  C   . HIS C 1 112 ? -16.096 22.400  43.670 1.00 23.35 ? 112 HIS C C   1
+ATOM   3032 O  O   . HIS C 1 112 ? -16.998 23.288  44.028 1.00 25.70 ? 112 HIS C O   1
+ATOM   3033 C  CB  . HIS C 1 112 ? -15.023 22.204  45.947 1.00 19.09 ? 112 HIS C CB  1
+ATOM   3034 C  CG  . HIS C 1 112 ? -15.204 21.354  46.928 1.00 25.33 ? 112 HIS C CG  1
+ATOM   3035 N  ND1 . HIS C 1 112 ? -13.894 20.338  47.579 1.00 35.05 ? 112 HIS C ND1 1
+ATOM   3036 C  CD2 . HIS C 1 112 ? -15.975 21.063  48.048 1.00 26.57 ? 112 HIS C CD2 1
+ATOM   3037 C  CE1 . HIS C 1 112 ? -14.311 19.789  48.608 1.00 18.65 ? 112 HIS C CE1 1
+ATOM   3038 N  NE2 . HIS C 1 112 ? -15.592 20.178  48.970 1.00 32.92 ? 112 HIS C NE2 1
+ATOM   3039 N  N   . LEU C 1 113 ? -15.607 22.765  42.674 1.00 23.20 ? 113 LEU C N   1
+ATOM   3040 C  CA  . LEU C 1 113 ? -15.750 23.678  41.562 1.00 19.73 ? 113 LEU C CA  1
+ATOM   3041 C  C   . LEU C 1 113 ? -16.154 22.871  40.174 1.00 24.44 ? 113 LEU C C   1
+ATOM   3042 O  O   . LEU C 1 113 ? -15.491 23.502  39.415 1.00 27.49 ? 113 LEU C O   1
+ATOM   3043 C  CB  . LEU C 1 113 ? -14.636 24.396  41.453 1.00 30.36 ? 113 LEU C CB  1
+ATOM   3044 C  CG  . LEU C 1 113 ? -14.383 25.240  42.521 1.00 29.78 ? 113 LEU C CG  1
+ATOM   3045 C  CD1 . LEU C 1 113 ? -12.972 25.848  41.684 1.00 35.69 ? 113 LEU C CD1 1
+ATOM   3046 C  CD2 . LEU C 1 113 ? -15.127 25.868  43.248 1.00 47.79 ? 113 LEU C CD2 1
+ATOM   3047 N  N   . PRO C 1 114 ? -17.265 22.369  40.000 1.00 23.63 ? 114 PRO C N   1
+ATOM   3048 C  CA  . PRO C 1 114 ? -17.949 21.304  38.835 1.00 26.62 ? 114 PRO C CA  1
+ATOM   3049 C  C   . PRO C 1 114 ? -18.017 22.689  37.529 1.00 35.32 ? 114 PRO C C   1
+ATOM   3050 O  O   . PRO C 1 114 ? -16.877 22.781  36.754 1.00 38.93 ? 114 PRO C O   1
+ATOM   3051 C  CB  . PRO C 1 114 ? -18.747 20.609  39.624 1.00 32.82 ? 114 PRO C CB  1
+ATOM   3052 C  CG  . PRO C 1 114 ? -19.527 21.928  40.236 1.00 48.45 ? 114 PRO C CG  1
+ATOM   3053 C  CD  . PRO C 1 114 ? -18.255 22.329  41.244 1.00 44.41 ? 114 PRO C CD  1
+ATOM   3054 N  N   . ALA C 1 115 ? -18.236 23.897  37.893 1.00 34.13 ? 115 ALA C N   1
+ATOM   3055 C  CA  . ALA C 1 115 ? -18.263 24.805  36.982 1.00 25.13 ? 115 ALA C CA  1
+ATOM   3056 C  C   . ALA C 1 115 ? -17.257 25.386  36.630 1.00 23.70 ? 115 ALA C C   1
+ATOM   3057 O  O   . ALA C 1 115 ? -16.911 25.875  35.442 1.00 28.59 ? 115 ALA C O   1
+ATOM   3058 C  CB  . ALA C 1 115 ? -19.556 25.912  36.885 1.00 49.66 ? 115 ALA C CB  1
+ATOM   3059 N  N   . GLU C 1 116 ? -16.279 25.750  37.456 1.00 19.87 ? 116 GLU C N   1
+ATOM   3060 C  CA  . GLU C 1 116 ? -15.153 26.784  37.211 1.00 15.46 ? 116 GLU C CA  1
+ATOM   3061 C  C   . GLU C 1 116 ? -13.830 25.965  36.929 1.00 17.63 ? 116 GLU C C   1
+ATOM   3062 O  O   . GLU C 1 116 ? -13.118 26.633  36.106 1.00 21.65 ? 116 GLU C O   1
+ATOM   3063 C  CB  . GLU C 1 116 ? -14.616 27.106  38.724 1.00 24.21 ? 116 GLU C CB  1
+ATOM   3064 C  CG  . GLU C 1 116 ? -16.453 26.925  40.151 1.00 64.07 ? 116 GLU C CG  1
+ATOM   3065 C  CD  . GLU C 1 116 ? -16.755 28.239  39.591 1.00 64.09 ? 116 GLU C CD  1
+ATOM   3066 O  OE1 . GLU C 1 116 ? -16.540 28.897  38.702 1.00 59.54 ? 116 GLU C OE1 1
+ATOM   3067 O  OE2 . GLU C 1 116 ? -18.076 27.960  40.124 1.00 58.51 ? 116 GLU C OE2 1
+ATOM   3068 N  N   . PHE C 1 117 ? -13.803 24.773  37.165 1.00 18.06 ? 117 PHE C N   1
+ATOM   3069 C  CA  . PHE C 1 117 ? -12.670 23.867  36.690 1.00 15.96 ? 117 PHE C CA  1
+ATOM   3070 C  C   . PHE C 1 117 ? -12.602 23.420  35.266 1.00 17.62 ? 117 PHE C C   1
+ATOM   3071 O  O   . PHE C 1 117 ? -12.658 22.272  35.046 1.00 20.40 ? 117 PHE C O   1
+ATOM   3072 C  CB  . PHE C 1 117 ? -12.528 22.764  37.675 1.00 11.69 ? 117 PHE C CB  1
+ATOM   3073 C  CG  . PHE C 1 117 ? -11.295 22.061  37.911 1.00 15.94 ? 117 PHE C CG  1
+ATOM   3074 C  CD1 . PHE C 1 117 ? -10.159 22.819  38.505 1.00 20.23 ? 117 PHE C CD1 1
+ATOM   3075 C  CD2 . PHE C 1 117 ? -10.917 20.801  37.387 1.00 18.29 ? 117 PHE C CD2 1
+ATOM   3076 C  CE1 . PHE C 1 117 ? -8.741  22.092  38.633 1.00 21.74 ? 117 PHE C CE1 1
+ATOM   3077 C  CE2 . PHE C 1 117 ? -9.620  20.189  37.310 1.00 15.69 ? 117 PHE C CE2 1
+ATOM   3078 C  CZ  . PHE C 1 117 ? -8.682  20.937  38.034 1.00 19.08 ? 117 PHE C CZ  1
+ATOM   3079 N  N   . THR C 1 118 ? -12.541 24.446  34.352 1.00 16.36 ? 118 THR C N   1
+ATOM   3080 C  CA  . THR C 1 118 ? -12.556 23.963  32.992 1.00 24.73 ? 118 THR C CA  1
+ATOM   3081 C  C   . THR C 1 118 ? -11.037 23.565  32.516 1.00 20.24 ? 118 THR C C   1
+ATOM   3082 O  O   . THR C 1 118 ? -10.190 23.699  33.492 1.00 17.57 ? 118 THR C O   1
+ATOM   3083 C  CB  . THR C 1 118 ? -12.591 25.531  32.213 1.00 24.50 ? 118 THR C CB  1
+ATOM   3084 O  OG1 . THR C 1 118 ? -13.952 26.016  32.475 1.00 43.24 ? 118 THR C OG1 1
+ATOM   3085 C  CG2 . THR C 1 118 ? -11.854 26.358  32.302 1.00 20.86 ? 118 THR C CG2 1
+ATOM   3086 N  N   . PRO C 1 119 ? -10.961 23.143  31.538 1.00 16.01 ? 119 PRO C N   1
+ATOM   3087 C  CA  . PRO C 1 119 ? -9.582  22.807  31.012 1.00 19.05 ? 119 PRO C CA  1
+ATOM   3088 C  C   . PRO C 1 119 ? -8.631  23.935  31.277 1.00 19.72 ? 119 PRO C C   1
+ATOM   3089 O  O   . PRO C 1 119 ? -7.446  23.742  31.618 1.00 14.74 ? 119 PRO C O   1
+ATOM   3090 C  CB  . PRO C 1 119 ? -9.692  22.227  29.678 1.00 21.12 ? 119 PRO C CB  1
+ATOM   3091 C  CG  . PRO C 1 119 ? -11.223 21.633  29.570 1.00 19.58 ? 119 PRO C CG  1
+ATOM   3092 C  CD  . PRO C 1 119 ? -12.100 22.575  30.516 1.00 19.86 ? 119 PRO C CD  1
+ATOM   3093 N  N   . ALA C 1 120 ? -8.952  25.114  30.710 1.00 19.86 ? 120 ALA C N   1
+ATOM   3094 C  CA  . ALA C 1 120 ? -8.065  26.179  30.730 1.00 18.74 ? 120 ALA C CA  1
+ATOM   3095 C  C   . ALA C 1 120 ? -7.747  26.631  32.181 1.00 10.87 ? 120 ALA C C   1
+ATOM   3096 O  O   . ALA C 1 120 ? -6.502  27.085  32.440 1.00 14.38 ? 120 ALA C O   1
+ATOM   3097 C  CB  . ALA C 1 120 ? -8.626  27.435  30.018 1.00 23.51 ? 120 ALA C CB  1
+ATOM   3098 N  N   . VAL C 1 121 ? -8.718  26.571  33.051 1.00 15.38 ? 121 VAL C N   1
+ATOM   3099 C  CA  . VAL C 1 121 ? -8.627  26.871  34.506 1.00 17.86 ? 121 VAL C CA  1
+ATOM   3100 C  C   . VAL C 1 121 ? -7.595  25.867  35.121 1.00 13.56 ? 121 VAL C C   1
+ATOM   3101 O  O   . VAL C 1 121 ? -6.737  26.346  35.804 1.00 14.98 ? 121 VAL C O   1
+ATOM   3102 C  CB  . VAL C 1 121 ? -9.843  27.195  35.170 1.00 16.82 ? 121 VAL C CB  1
+ATOM   3103 C  CG1 . VAL C 1 121 ? -9.618  27.273  36.643 1.00 15.23 ? 121 VAL C CG1 1
+ATOM   3104 C  CG2 . VAL C 1 121 ? -10.368 28.479  34.552 1.00 18.21 ? 121 VAL C CG2 1
+ATOM   3105 N  N   . HIS C 1 122 ? -7.805  24.636  34.771 1.00 13.62 ? 122 HIS C N   1
+ATOM   3106 C  CA  . HIS C 1 122 ? -6.937  23.451  35.259 1.00 13.41 ? 122 HIS C CA  1
+ATOM   3107 C  C   . HIS C 1 122 ? -5.548  23.814  34.921 1.00 19.70 ? 122 HIS C C   1
+ATOM   3108 O  O   . HIS C 1 122 ? -4.642  23.728  35.783 1.00 15.94 ? 122 HIS C O   1
+ATOM   3109 C  CB  . HIS C 1 122 ? -7.560  22.306  34.759 1.00 13.44 ? 122 HIS C CB  1
+ATOM   3110 C  CG  . HIS C 1 122 ? -6.979  21.032  34.925 1.00 11.42 ? 122 HIS C CG  1
+ATOM   3111 N  ND1 . HIS C 1 122 ? -7.464  19.754  34.592 1.00 16.43 ? 122 HIS C ND1 1
+ATOM   3112 C  CD2 . HIS C 1 122 ? -5.726  20.863  35.683 1.00 17.04 ? 122 HIS C CD2 1
+ATOM   3113 C  CE1 . HIS C 1 122 ? -6.597  18.852  34.961 1.00 20.17 ? 122 HIS C CE1 1
+ATOM   3114 N  NE2 . HIS C 1 122 ? -5.616  19.365  35.742 1.00 16.87 ? 122 HIS C NE2 1
+ATOM   3115 N  N   . ALA C 1 123 ? -5.282  24.241  33.685 1.00 13.94 ? 123 ALA C N   1
+ATOM   3116 C  CA  . ALA C 1 123 ? -3.852  24.440  33.281 1.00 17.63 ? 123 ALA C CA  1
+ATOM   3117 C  C   . ALA C 1 123 ? -3.238  25.574  33.993 1.00 15.63 ? 123 ALA C C   1
+ATOM   3118 O  O   . ALA C 1 123 ? -2.180  25.505  34.534 1.00 16.32 ? 123 ALA C O   1
+ATOM   3119 C  CB  . ALA C 1 123 ? -3.944  24.690  31.702 1.00 21.15 ? 123 ALA C CB  1
+ATOM   3120 N  N   . SER C 1 124 ? -4.035  26.650  34.175 1.00 11.75 ? 124 SER C N   1
+ATOM   3121 C  CA  . SER C 1 124 ? -3.394  27.839  34.907 1.00 15.01 ? 124 SER C CA  1
+ATOM   3122 C  C   . SER C 1 124 ? -3.253  27.454  36.479 1.00 15.67 ? 124 SER C C   1
+ATOM   3123 O  O   . SER C 1 124 ? -2.271  27.979  36.892 1.00 13.45 ? 124 SER C O   1
+ATOM   3124 C  CB  . SER C 1 124 ? -4.541  28.990  34.858 1.00 14.78 ? 124 SER C CB  1
+ATOM   3125 O  OG  . SER C 1 124 ? -4.824  29.479  33.477 1.00 17.64 ? 124 SER C OG  1
+ATOM   3126 N  N   . LEU C 1 125 ? -4.169  26.806  36.953 1.00 10.43 ? 125 LEU C N   1
+ATOM   3127 C  CA  . LEU C 1 125 ? -3.974  26.408  38.376 1.00 12.66 ? 125 LEU C CA  1
+ATOM   3128 C  C   . LEU C 1 125 ? -2.805  25.517  38.660 1.00 12.01 ? 125 LEU C C   1
+ATOM   3129 O  O   . LEU C 1 125 ? -1.878  25.722  39.523 1.00 10.58 ? 125 LEU C O   1
+ATOM   3130 C  CB  . LEU C 1 125 ? -5.183  25.713  38.887 1.00 10.32 ? 125 LEU C CB  1
+ATOM   3131 C  CG  . LEU C 1 125 ? -6.317  26.694  39.349 1.00 16.01 ? 125 LEU C CG  1
+ATOM   3132 C  CD1 . LEU C 1 125 ? -7.563  25.849  39.464 1.00 21.31 ? 125 LEU C CD1 1
+ATOM   3133 C  CD2 . LEU C 1 125 ? -5.941  27.687  40.494 1.00 19.17 ? 125 LEU C CD2 1
+ATOM   3134 N  N   . ASP C 1 126 ? -2.469  24.629  37.706 1.00 15.23 ? 126 ASP C N   1
+ATOM   3135 C  CA  . ASP C 1 126 ? -1.315  23.690  37.774 1.00 15.01 ? 126 ASP C CA  1
+ATOM   3136 C  C   . ASP C 1 126 ? -0.148  24.556  37.653 1.00 17.34 ? 126 ASP C C   1
+ATOM   3137 O  O   . ASP C 1 126 ? 0.876   24.355  38.319 1.00 17.16 ? 126 ASP C O   1
+ATOM   3138 C  CB  . ASP C 1 126 ? -1.474  22.643  36.761 1.00 14.23 ? 126 ASP C CB  1
+ATOM   3139 C  CG  . ASP C 1 126 ? -0.460  21.302  37.002 1.00 15.33 ? 126 ASP C CG  1
+ATOM   3140 O  OD1 . ASP C 1 126 ? -0.386  21.135  38.130 1.00 21.18 ? 126 ASP C OD1 1
+ATOM   3141 O  OD2 . ASP C 1 126 ? 0.404   21.221  36.236 1.00 18.49 ? 126 ASP C OD2 1
+ATOM   3142 N  N   . LYS C 1 127 ? -0.049  25.579  36.721 1.00 10.51 ? 127 LYS C N   1
+ATOM   3143 C  CA  . LYS C 1 127 ? 1.127   26.368  36.501 1.00 9.26  ? 127 LYS C CA  1
+ATOM   3144 C  C   . LYS C 1 127 ? 1.198   27.236  37.820 1.00 10.60 ? 127 LYS C C   1
+ATOM   3145 O  O   . LYS C 1 127 ? 2.530   27.485  38.248 1.00 13.38 ? 127 LYS C O   1
+ATOM   3146 C  CB  . LYS C 1 127 ? 0.944   27.435  35.345 1.00 12.57 ? 127 LYS C CB  1
+ATOM   3147 C  CG  . LYS C 1 127 ? 1.047   26.668  34.147 1.00 21.03 ? 127 LYS C CG  1
+ATOM   3148 C  CD  . LYS C 1 127 ? 0.884   27.656  32.897 1.00 27.03 ? 127 LYS C CD  1
+ATOM   3149 C  CE  . LYS C 1 127 ? 1.961   28.782  32.875 1.00 36.89 ? 127 LYS C CE  1
+ATOM   3150 N  NZ  . LYS C 1 127 ? 1.824   29.648  31.599 1.00 25.75 ? 127 LYS C NZ  1
+ATOM   3151 N  N   . PHE C 1 128 ? 0.182   27.705  38.310 1.00 12.44 ? 128 PHE C N   1
+ATOM   3152 C  CA  . PHE C 1 128 ? 0.320   28.558  39.393 1.00 14.73 ? 128 PHE C CA  1
+ATOM   3153 C  C   . PHE C 1 128 ? 0.834   27.636  40.759 1.00 19.70 ? 128 PHE C C   1
+ATOM   3154 O  O   . PHE C 1 128 ? 1.819   28.285  41.403 1.00 15.58 ? 128 PHE C O   1
+ATOM   3155 C  CB  . PHE C 1 128 ? -0.978  29.203  39.876 1.00 11.17 ? 128 PHE C CB  1
+ATOM   3156 C  CG  . PHE C 1 128 ? -1.104  29.851  41.419 1.00 11.86 ? 128 PHE C CG  1
+ATOM   3157 C  CD1 . PHE C 1 128 ? -0.435  31.097  41.491 1.00 15.77 ? 128 PHE C CD1 1
+ATOM   3158 C  CD2 . PHE C 1 128 ? -1.795  29.083  42.065 1.00 23.89 ? 128 PHE C CD2 1
+ATOM   3159 C  CE1 . PHE C 1 128 ? -0.694  31.457  42.818 1.00 14.00 ? 128 PHE C CE1 1
+ATOM   3160 C  CE2 . PHE C 1 128 ? -1.764  29.704  43.512 1.00 26.48 ? 128 PHE C CE2 1
+ATOM   3161 C  CZ  . PHE C 1 128 ? -1.293  30.841  43.728 1.00 15.47 ? 128 PHE C CZ  1
+ATOM   3162 N  N   . LEU C 1 129 ? 0.268   26.489  40.924 1.00 14.00 ? 129 LEU C N   1
+ATOM   3163 C  CA  . LEU C 1 129 ? 0.802   25.691  42.128 1.00 13.04 ? 129 LEU C CA  1
+ATOM   3164 C  C   . LEU C 1 129 ? 2.281   25.274  41.854 1.00 17.30 ? 129 LEU C C   1
+ATOM   3165 O  O   . LEU C 1 129 ? 3.223   25.257  42.778 1.00 14.75 ? 129 LEU C O   1
+ATOM   3166 C  CB  . LEU C 1 129 ? 0.131   24.471  42.304 1.00 12.12 ? 129 LEU C CB  1
+ATOM   3167 C  CG  . LEU C 1 129 ? -1.196  24.824  42.763 1.00 20.92 ? 129 LEU C CG  1
+ATOM   3168 C  CD1 . LEU C 1 129 ? -2.184  23.738  42.800 1.00 26.64 ? 129 LEU C CD1 1
+ATOM   3169 C  CD2 . LEU C 1 129 ? -1.317  25.375  44.089 1.00 35.02 ? 129 LEU C CD2 1
+ATOM   3170 N  N   . ALA C 1 130 ? 2.783   25.067  40.644 1.00 16.20 ? 130 ALA C N   1
+ATOM   3171 C  CA  . ALA C 1 130 ? 4.130   24.887  40.263 1.00 14.56 ? 130 ALA C CA  1
+ATOM   3172 C  C   . ALA C 1 130 ? 4.988   26.018  40.658 1.00 19.27 ? 130 ALA C C   1
+ATOM   3173 O  O   . ALA C 1 130 ? 6.260   25.974  41.137 1.00 14.14 ? 130 ALA C O   1
+ATOM   3174 C  CB  . ALA C 1 130 ? 4.429   24.580  38.944 1.00 17.10 ? 130 ALA C CB  1
+ATOM   3175 N  N   . SER C 1 131 ? 4.515   27.143  40.269 1.00 18.74 ? 131 SER C N   1
+ATOM   3176 C  CA  . SER C 1 131 ? 5.434   28.451  40.568 1.00 19.45 ? 131 SER C CA  1
+ATOM   3177 C  C   . SER C 1 131 ? 5.316   28.778  42.289 1.00 14.53 ? 131 SER C C   1
+ATOM   3178 O  O   . SER C 1 131 ? 6.499   29.056  42.559 1.00 12.58 ? 131 SER C O   1
+ATOM   3179 C  CB  . SER C 1 131 ? 4.548   29.829  40.023 1.00 22.90 ? 131 SER C CB  1
+ATOM   3180 O  OG  . SER C 1 131 ? 4.633   29.504  38.554 1.00 37.64 ? 131 SER C OG  1
+ATOM   3181 N  N   . VAL C 1 132 ? 4.265   28.414  42.889 1.00 12.03 ? 132 VAL C N   1
+ATOM   3182 C  CA  . VAL C 1 132 ? 4.285   28.486  44.328 1.00 13.41 ? 132 VAL C CA  1
+ATOM   3183 C  C   . VAL C 1 132 ? 5.425   27.574  44.897 1.00 19.42 ? 132 VAL C C   1
+ATOM   3184 O  O   . VAL C 1 132 ? 6.323   27.908  45.797 1.00 14.00 ? 132 VAL C O   1
+ATOM   3185 C  CB  . VAL C 1 132 ? 3.041   28.224  44.915 1.00 15.91 ? 132 VAL C CB  1
+ATOM   3186 C  CG1 . VAL C 1 132 ? 3.206   28.020  46.471 1.00 17.14 ? 132 VAL C CG1 1
+ATOM   3187 C  CG2 . VAL C 1 132 ? 1.924   29.519  44.726 1.00 19.41 ? 132 VAL C CG2 1
+ATOM   3188 N  N   . SER C 1 133 ? 5.323   26.253  44.379 1.00 14.01 ? 133 SER C N   1
+ATOM   3189 C  CA  . SER C 1 133 ? 6.255   25.227  44.640 1.00 13.12 ? 133 SER C CA  1
+ATOM   3190 C  C   . SER C 1 133 ? 7.667   25.691  44.362 1.00 21.83 ? 133 SER C C   1
+ATOM   3191 O  O   . SER C 1 133 ? 8.644   25.349  45.371 1.00 18.12 ? 133 SER C O   1
+ATOM   3192 C  CB  . SER C 1 133 ? 6.129   23.890  43.936 1.00 13.61 ? 133 SER C CB  1
+ATOM   3193 O  OG  . SER C 1 133 ? 4.860   23.486  44.569 1.00 18.98 ? 133 SER C OG  1
+ATOM   3194 N  N   . THR C 1 134 ? 8.003   26.208  43.359 1.00 17.53 ? 134 THR C N   1
+ATOM   3195 C  CA  . THR C 1 134 ? 9.374   26.766  43.002 1.00 15.95 ? 134 THR C CA  1
+ATOM   3196 C  C   . THR C 1 134 ? 9.837   27.861  43.927 1.00 16.97 ? 134 THR C C   1
+ATOM   3197 O  O   . THR C 1 134 ? 11.031  27.733  44.511 1.00 20.39 ? 134 THR C O   1
+ATOM   3198 C  CB  . THR C 1 134 ? 9.253   27.334  41.503 1.00 18.28 ? 134 THR C CB  1
+ATOM   3199 O  OG1 . THR C 1 134 ? 9.163   26.304  40.689 1.00 22.72 ? 134 THR C OG1 1
+ATOM   3200 C  CG2 . THR C 1 134 ? 10.563  27.996  41.073 1.00 22.70 ? 134 THR C CG2 1
+ATOM   3201 N  N   . VAL C 1 135 ? 8.919   28.666  44.254 1.00 15.13 ? 135 VAL C N   1
+ATOM   3202 C  CA  . VAL C 1 135 ? 9.371   29.799  45.211 1.00 16.51 ? 135 VAL C CA  1
+ATOM   3203 C  C   . VAL C 1 135 ? 9.815   28.972  46.549 1.00 16.40 ? 135 VAL C C   1
+ATOM   3204 O  O   . VAL C 1 135 ? 10.718  29.479  47.192 1.00 15.94 ? 135 VAL C O   1
+ATOM   3205 C  CB  . VAL C 1 135 ? 8.238   30.917  45.401 1.00 18.21 ? 135 VAL C CB  1
+ATOM   3206 C  CG1 . VAL C 1 135 ? 8.498   31.879  46.554 1.00 17.40 ? 135 VAL C CG1 1
+ATOM   3207 C  CG2 . VAL C 1 135 ? 8.106   31.621  44.135 1.00 19.71 ? 135 VAL C CG2 1
+ATOM   3208 N  N   . LEU C 1 136 ? 8.742   28.165  47.127 1.00 12.10 ? 136 LEU C N   1
+ATOM   3209 C  CA  . LEU C 1 136 ? 8.933   27.615  48.489 1.00 15.98 ? 136 LEU C CA  1
+ATOM   3210 C  C   . LEU C 1 136 ? 10.286  26.819  48.496 1.00 16.04 ? 136 LEU C C   1
+ATOM   3211 O  O   . LEU C 1 136 ? 10.758  26.477  49.698 1.00 16.42 ? 136 LEU C O   1
+ATOM   3212 C  CB  . LEU C 1 136 ? 7.767   26.818  48.732 1.00 16.86 ? 136 LEU C CB  1
+ATOM   3213 C  CG  . LEU C 1 136 ? 6.498   27.699  48.975 1.00 24.99 ? 136 LEU C CG  1
+ATOM   3214 C  CD1 . LEU C 1 136 ? 5.550   26.680  49.621 1.00 18.69 ? 136 LEU C CD1 1
+ATOM   3215 C  CD2 . LEU C 1 136 ? 6.699   28.662  50.043 1.00 43.05 ? 136 LEU C CD2 1
+ATOM   3216 N  N   . THR C 1 137 ? 10.776  26.405  47.315 1.00 14.30 ? 137 THR C N   1
+ATOM   3217 C  CA  . THR C 1 137 ? 11.945  25.420  47.391 1.00 16.72 ? 137 THR C CA  1
+ATOM   3218 C  C   . THR C 1 137 ? 13.327  26.347  46.875 1.00 20.27 ? 137 THR C C   1
+ATOM   3219 O  O   . THR C 1 137 ? 14.280  25.718  46.849 1.00 19.99 ? 137 THR C O   1
+ATOM   3220 C  CB  . THR C 1 137 ? 11.713  24.163  46.386 1.00 21.82 ? 137 THR C CB  1
+ATOM   3221 O  OG1 . THR C 1 137 ? 11.583  24.585  45.250 1.00 20.00 ? 137 THR C OG1 1
+ATOM   3222 C  CG2 . THR C 1 137 ? 10.791  23.269  47.207 1.00 20.00 ? 137 THR C CG2 1
+ATOM   3223 N  N   . SER C 1 138 ? 13.112  27.550  46.526 1.00 21.45 ? 138 SER C N   1
+ATOM   3224 C  CA  . SER C 1 138 ? 14.205  28.364  45.991 1.00 24.00 ? 138 SER C CA  1
+ATOM   3225 C  C   . SER C 1 138 ? 15.527  28.466  46.961 1.00 26.98 ? 138 SER C C   1
+ATOM   3226 O  O   . SER C 1 138 ? 16.346  28.964  46.250 1.00 21.99 ? 138 SER C O   1
+ATOM   3227 C  CB  . SER C 1 138 ? 13.326  30.261  46.447 1.00 21.69 ? 138 SER C CB  1
+ATOM   3228 O  OG  . SER C 1 138 ? 13.564  29.793  45.266 1.00 42.20 ? 138 SER C OG  1
+ATOM   3229 N  N   . LYS C 1 139 ? 15.286  28.359  48.265 1.00 22.73 ? 139 LYS C N   1
+ATOM   3230 C  CA  . LYS C 1 139 ? 16.479  28.792  49.122 1.00 27.59 ? 139 LYS C CA  1
+ATOM   3231 C  C   . LYS C 1 139 ? 17.078  27.376  49.688 1.00 19.22 ? 139 LYS C C   1
+ATOM   3232 O  O   . LYS C 1 139 ? 17.820  27.414  50.655 1.00 14.35 ? 139 LYS C O   1
+ATOM   3233 C  CB  . LYS C 1 139 ? 15.819  29.558  50.203 1.00 19.55 ? 139 LYS C CB  1
+ATOM   3234 C  CG  . LYS C 1 139 ? 15.724  31.042  49.451 1.00 22.79 ? 139 LYS C CG  1
+ATOM   3235 C  CD  . LYS C 1 139 ? 15.105  31.677  50.391 1.00 42.21 ? 139 LYS C CD  1
+ATOM   3236 C  CE  . LYS C 1 139 ? 15.141  33.521  49.749 1.00 36.26 ? 139 LYS C CE  1
+ATOM   3237 N  NZ  . LYS C 1 139 ? 13.856  33.453  51.064 1.00 30.87 ? 139 LYS C NZ  1
+ATOM   3238 N  N   . TYR C 1 140 ? 16.640  26.262  49.172 1.00 18.17 ? 140 TYR C N   1
+ATOM   3239 C  CA  . TYR C 1 140 ? 17.145  25.044  49.743 1.00 17.49 ? 140 TYR C CA  1
+ATOM   3240 C  C   . TYR C 1 140 ? 18.595  24.819  49.658 1.00 19.10 ? 140 TYR C C   1
+ATOM   3241 O  O   . TYR C 1 140 ? 19.021  24.039  50.654 1.00 22.35 ? 140 TYR C O   1
+ATOM   3242 C  CB  . TYR C 1 140 ? 16.357  23.842  49.007 1.00 16.87 ? 140 TYR C CB  1
+ATOM   3243 C  CG  . TYR C 1 140 ? 15.105  23.332  49.674 1.00 12.61 ? 140 TYR C CG  1
+ATOM   3244 C  CD1 . TYR C 1 140 ? 14.777  22.178  49.904 1.00 19.13 ? 140 TYR C CD1 1
+ATOM   3245 C  CD2 . TYR C 1 140 ? 13.994  24.273  50.011 1.00 16.63 ? 140 TYR C CD2 1
+ATOM   3246 C  CE1 . TYR C 1 140 ? 13.578  21.811  50.477 1.00 21.26 ? 140 TYR C CE1 1
+ATOM   3247 C  CE2 . TYR C 1 140 ? 12.813  23.902  50.651 1.00 17.45 ? 140 TYR C CE2 1
+ATOM   3248 C  CZ  . TYR C 1 140 ? 12.514  22.725  50.795 1.00 14.84 ? 140 TYR C CZ  1
+ATOM   3249 O  OH  . TYR C 1 140 ? 11.453  22.162  51.421 1.00 15.53 ? 140 TYR C OH  1
+ATOM   3250 N  N   . ARG C 1 141 ? 19.195  25.330  48.574 1.00 20.34 ? 141 ARG C N   1
+ATOM   3251 C  CA  . ARG C 1 141 ? 20.604  25.087  48.416 1.00 25.59 ? 141 ARG C CA  1
+ATOM   3252 C  C   . ARG C 1 141 ? 21.380  26.389  47.709 1.00 21.46 ? 141 ARG C C   1
+ATOM   3253 O  O   . ARG C 1 141 ? 20.521  26.915  47.109 1.00 24.60 ? 141 ARG C O   1
+ATOM   3254 C  CB  . ARG C 1 141 ? 20.984  23.676  47.960 1.00 27.67 ? 141 ARG C CB  1
+ATOM   3255 C  CG  . ARG C 1 141 ? 20.481  23.506  46.506 1.00 20.44 ? 141 ARG C CG  1
+ATOM   3256 C  CD  . ARG C 1 141 ? 21.083  21.977  46.306 1.00 27.35 ? 141 ARG C CD  1
+ATOM   3257 N  NE  . ARG C 1 141 ? 20.504  21.713  44.918 1.00 21.57 ? 141 ARG C NE  1
+ATOM   3258 C  CZ  . ARG C 1 141 ? 21.147  20.787  44.092 1.00 17.72 ? 141 ARG C CZ  1
+ATOM   3259 N  NH1 . ARG C 1 141 ? 21.870  19.869  44.542 1.00 16.11 ? 141 ARG C NH1 1
+ATOM   3260 N  NH2 . ARG C 1 141 ? 20.297  20.745  42.929 1.00 19.55 ? 141 ARG C NH2 1
+ATOM   3261 O  OXT . ARG C 1 141 ? 22.581  26.235  47.657 1.00 22.97 ? 141 ARG C OXT 1
+ATOM   3262 N  N   . VAL D 2 1   ? -1.814  -5.610  41.065 1.00 44.53 ? 1   VAL D N   1
+ATOM   3263 C  CA  . VAL D 2 1   ? -1.372  -4.526  42.392 1.00 40.54 ? 1   VAL D CA  1
+ATOM   3264 C  C   . VAL D 2 1   ? -2.305  -5.400  43.956 1.00 54.57 ? 1   VAL D C   1
+ATOM   3265 O  O   . VAL D 2 1   ? -3.353  -5.931  43.347 1.00 46.03 ? 1   VAL D O   1
+ATOM   3266 C  CB  . VAL D 2 1   ? -2.154  -3.023  42.460 1.00 59.62 ? 1   VAL D CB  1
+ATOM   3267 C  CG1 . VAL D 2 1   ? -1.269  -1.974  41.408 1.00 56.25 ? 1   VAL D CG1 1
+ATOM   3268 C  CG2 . VAL D 2 1   ? -3.214  -2.974  41.963 1.00 44.49 ? 1   VAL D CG2 1
+ATOM   3269 N  N   . HIS D 2 2   ? -1.881  -4.480  44.565 1.00 54.55 ? 2   HIS D N   1
+ATOM   3270 C  CA  . HIS D 2 2   ? -2.494  -4.541  45.879 1.00 76.16 ? 2   HIS D CA  1
+ATOM   3271 C  C   . HIS D 2 2   ? -3.834  -3.786  46.487 1.00 40.79 ? 2   HIS D C   1
+ATOM   3272 O  O   . HIS D 2 2   ? -3.055  -2.719  47.278 1.00 42.23 ? 2   HIS D O   1
+ATOM   3273 C  CB  . HIS D 2 2   ? -1.158  -5.937  46.959 1.00 61.25 ? 2   HIS D CB  1
+ATOM   3274 C  CG  . HIS D 2 2   ? -1.766  -6.426  47.663 1.00 73.35 ? 2   HIS D CG  1
+ATOM   3275 N  ND1 . HIS D 2 2   ? -1.563  -4.633  49.363 1.00 63.32 ? 2   HIS D ND1 1
+ATOM   3276 C  CD2 . HIS D 2 2   ? -3.067  -7.358  48.599 1.00 68.03 ? 2   HIS D CD2 1
+ATOM   3277 C  CE1 . HIS D 2 2   ? -2.903  -4.790  50.700 1.00 55.48 ? 2   HIS D CE1 1
+ATOM   3278 N  NE2 . HIS D 2 2   ? -3.454  -6.335  49.732 1.00 54.14 ? 2   HIS D NE2 1
+ATOM   3279 N  N   . LEU D 2 3   ? -5.006  -4.528  46.453 1.00 31.51 ? 3   LEU D N   1
+ATOM   3280 C  CA  . LEU D 2 3   ? -5.944  -3.493  46.645 1.00 32.74 ? 3   LEU D CA  1
+ATOM   3281 C  C   . LEU D 2 3   ? -5.932  -4.056  48.199 1.00 43.55 ? 3   LEU D C   1
+ATOM   3282 O  O   . LEU D 2 3   ? -7.131  -5.337  48.007 1.00 38.09 ? 3   LEU D O   1
+ATOM   3283 C  CB  . LEU D 2 3   ? -7.274  -3.188  45.938 1.00 39.97 ? 3   LEU D CB  1
+ATOM   3284 C  CG  . LEU D 2 3   ? -6.527  -2.253  44.809 1.00 33.25 ? 3   LEU D CG  1
+ATOM   3285 C  CD1 . LEU D 2 3   ? -7.751  -1.778  44.047 1.00 35.36 ? 3   LEU D CD1 1
+ATOM   3286 C  CD2 . LEU D 2 3   ? -6.305  -0.965  45.139 1.00 43.98 ? 3   LEU D CD2 1
+ATOM   3287 N  N   . THR D 2 4   ? -7.078  -3.625  49.100 1.00 40.52 ? 4   THR D N   1
+ATOM   3288 C  CA  . THR D 2 4   ? -7.788  -3.977  50.057 1.00 35.01 ? 4   THR D CA  1
+ATOM   3289 C  C   . THR D 2 4   ? -9.299  -4.493  49.814 1.00 36.50 ? 4   THR D C   1
+ATOM   3290 O  O   . THR D 2 4   ? -9.504  -3.755  48.628 1.00 26.93 ? 4   THR D O   1
+ATOM   3291 C  CB  . THR D 2 4   ? -7.829  -2.890  51.512 1.00 42.32 ? 4   THR D CB  1
+ATOM   3292 O  OG1 . THR D 2 4   ? -8.724  -1.949  51.086 1.00 35.61 ? 4   THR D OG1 1
+ATOM   3293 C  CG2 . THR D 2 4   ? -6.692  -2.661  51.928 1.00 41.74 ? 4   THR D CG2 1
+ATOM   3294 N  N   . PRO D 2 5   ? -9.852  -5.187  50.202 1.00 38.01 ? 5   PRO D N   1
+ATOM   3295 C  CA  . PRO D 2 5   ? -11.337 -5.221  49.120 1.00 45.26 ? 5   PRO D CA  1
+ATOM   3296 C  C   . PRO D 2 5   ? -12.310 -4.132  49.413 1.00 40.88 ? 5   PRO D C   1
+ATOM   3297 O  O   . PRO D 2 5   ? -13.164 -3.742  48.743 1.00 35.71 ? 5   PRO D O   1
+ATOM   3298 C  CB  . PRO D 2 5   ? -12.067 -6.220  51.069 1.00 80.12 ? 5   PRO D CB  1
+ATOM   3299 C  CG  . PRO D 2 5   ? -11.233 -6.668  51.529 1.00 36.53 ? 5   PRO D CG  1
+ATOM   3300 C  CD  . PRO D 2 5   ? -9.657  -6.371  51.226 1.00 38.83 ? 5   PRO D CD  1
+ATOM   3301 N  N   . GLU D 2 6   ? -11.939 -3.175  50.361 1.00 38.95 ? 6   GLU D N   1
+ATOM   3302 C  CA  . GLU D 2 6   ? -12.804 -2.252  50.717 1.00 54.36 ? 6   GLU D CA  1
+ATOM   3303 C  C   . GLU D 2 6   ? -12.069 -0.723  49.156 1.00 29.53 ? 6   GLU D C   1
+ATOM   3304 O  O   . GLU D 2 6   ? -12.968 -0.346  48.860 1.00 34.33 ? 6   GLU D O   1
+ATOM   3305 C  CB  . GLU D 2 6   ? -12.522 -1.044  51.914 1.00 67.37 ? 6   GLU D CB  1
+ATOM   3306 C  CG  . GLU D 2 6   ? -11.847 -1.262  52.529 1.00 68.32 ? 6   GLU D CG  1
+ATOM   3307 C  CD  . GLU D 2 6   ? -11.713 -2.810  53.740 1.00 80.07 ? 6   GLU D CD  1
+ATOM   3308 O  OE1 . GLU D 2 6   ? -11.276 -3.564  53.394 1.00 62.33 ? 6   GLU D OE1 1
+ATOM   3309 O  OE2 . GLU D 2 6   ? -9.409  -3.309  52.664 1.00 75.27 ? 6   GLU D OE2 1
+ATOM   3310 N  N   . GLU D 2 7   ? -10.901 -1.071  49.080 1.00 32.30 ? 7   GLU D N   1
+ATOM   3311 C  CA  . GLU D 2 7   ? -10.347 -0.216  47.921 1.00 26.92 ? 7   GLU D CA  1
+ATOM   3312 C  C   . GLU D 2 7   ? -11.011 -1.039  46.532 1.00 36.61 ? 7   GLU D C   1
+ATOM   3313 O  O   . GLU D 2 7   ? -11.472 -0.149  45.829 1.00 31.61 ? 7   GLU D O   1
+ATOM   3314 C  CB  . GLU D 2 7   ? -8.837  -0.457  47.764 1.00 22.74 ? 7   GLU D CB  1
+ATOM   3315 C  CG  . GLU D 2 7   ? -8.185  0.634   49.144 1.00 25.68 ? 7   GLU D CG  1
+ATOM   3316 C  CD  . GLU D 2 7   ? -6.922  0.161   49.164 1.00 21.07 ? 7   GLU D CD  1
+ATOM   3317 O  OE1 . GLU D 2 7   ? -6.344  1.496   49.329 1.00 41.17 ? 7   GLU D OE1 1
+ATOM   3318 O  OE2 . GLU D 2 7   ? -6.064  -0.735  48.554 1.00 26.19 ? 7   GLU D OE2 1
+ATOM   3319 N  N   . LYS D 2 8   ? -10.933 -2.215  46.557 1.00 24.35 ? 8   LYS D N   1
+ATOM   3320 C  CA  . LYS D 2 8   ? -11.473 -2.886  45.115 1.00 27.18 ? 8   LYS D CA  1
+ATOM   3321 C  C   . LYS D 2 8   ? -12.769 -2.751  44.882 1.00 23.43 ? 8   LYS D C   1
+ATOM   3322 O  O   . LYS D 2 8   ? -13.428 -2.180  44.002 1.00 23.08 ? 8   LYS D O   1
+ATOM   3323 C  CB  . LYS D 2 8   ? -11.138 -4.610  45.700 1.00 28.41 ? 8   LYS D CB  1
+ATOM   3324 C  CG  . LYS D 2 8   ? -11.452 -4.860  43.957 1.00 48.31 ? 8   LYS D CG  1
+ATOM   3325 C  CD  . LYS D 2 8   ? -11.087 -6.025  43.852 1.00 69.34 ? 8   LYS D CD  1
+ATOM   3326 C  CE  . LYS D 2 8   ? -12.105 -6.662  42.214 1.00 38.29 ? 8   LYS D CE  1
+ATOM   3327 N  NZ  . LYS D 2 8   ? -11.369 -8.405  41.800 1.00 72.55 ? 8   LYS D NZ  1
+ATOM   3328 N  N   . SER D 2 9   ? -13.620 -2.615  45.994 1.00 21.45 ? 9   SER D N   1
+ATOM   3329 C  CA  . SER D 2 9   ? -14.903 -2.143  45.734 1.00 23.49 ? 9   SER D CA  1
+ATOM   3330 C  C   . SER D 2 9   ? -15.111 -0.709  45.482 1.00 32.73 ? 9   SER D C   1
+ATOM   3331 O  O   . SER D 2 9   ? -16.196 -0.546  44.863 1.00 27.24 ? 9   SER D O   1
+ATOM   3332 C  CB  . SER D 2 9   ? -15.747 -2.789  46.868 1.00 48.80 ? 9   SER D CB  1
+ATOM   3333 O  OG  . SER D 2 9   ? -16.466 -2.355  47.669 1.00 54.12 ? 9   SER D OG  1
+ATOM   3334 N  N   . ALA D 2 10  ? -14.233 -0.002  46.237 1.00 26.97 ? 10  ALA D N   1
+ATOM   3335 C  CA  . ALA D 2 10  ? -14.740 1.506   46.024 1.00 27.01 ? 10  ALA D CA  1
+ATOM   3336 C  C   . ALA D 2 10  ? -14.275 1.733   44.348 1.00 23.29 ? 10  ALA D C   1
+ATOM   3337 O  O   . ALA D 2 10  ? -15.121 2.514   43.744 1.00 20.87 ? 10  ALA D O   1
+ATOM   3338 C  CB  . ALA D 2 10  ? -13.589 2.138   46.432 1.00 28.42 ? 10  ALA D CB  1
+ATOM   3339 N  N   . VAL D 2 11  ? -13.320 1.053   43.828 1.00 31.33 ? 11  VAL D N   1
+ATOM   3340 C  CA  . VAL D 2 11  ? -12.901 1.312   42.330 1.00 25.10 ? 11  VAL D CA  1
+ATOM   3341 C  C   . VAL D 2 11  ? -13.953 0.818   41.418 1.00 18.64 ? 11  VAL D C   1
+ATOM   3342 O  O   . VAL D 2 11  ? -14.305 1.593   40.610 1.00 19.73 ? 11  VAL D O   1
+ATOM   3343 C  CB  . VAL D 2 11  ? -11.589 0.475   42.157 1.00 18.52 ? 11  VAL D CB  1
+ATOM   3344 C  CG1 . VAL D 2 11  ? -11.406 0.500   40.891 1.00 28.45 ? 11  VAL D CG1 1
+ATOM   3345 C  CG2 . VAL D 2 11  ? -10.365 1.421   42.850 1.00 21.05 ? 11  VAL D CG2 1
+ATOM   3346 N  N   . THR D 2 12  ? -14.304 -0.432  41.866 1.00 19.99 ? 12  THR D N   1
+ATOM   3347 C  CA  . THR D 2 12  ? -15.410 -1.147  40.817 1.00 26.25 ? 12  THR D CA  1
+ATOM   3348 C  C   . THR D 2 12  ? -16.601 -0.482  40.917 1.00 24.29 ? 12  THR D C   1
+ATOM   3349 O  O   . THR D 2 12  ? -17.394 -0.059  39.851 1.00 26.52 ? 12  THR D O   1
+ATOM   3350 C  CB  . THR D 2 12  ? -15.640 -2.828  41.734 1.00 24.72 ? 12  THR D CB  1
+ATOM   3351 O  OG1 . THR D 2 12  ? -14.353 -3.294  41.042 1.00 32.38 ? 12  THR D OG1 1
+ATOM   3352 C  CG2 . THR D 2 12  ? -16.834 -3.048  41.049 1.00 56.05 ? 12  THR D CG2 1
+ATOM   3353 N  N   . ALA D 2 13  ? -17.111 0.030   41.924 1.00 25.46 ? 13  ALA D N   1
+ATOM   3354 C  CA  . ALA D 2 13  ? -18.308 0.747   42.220 1.00 25.21 ? 13  ALA D CA  1
+ATOM   3355 C  C   . ALA D 2 13  ? -18.617 2.086   41.320 1.00 24.39 ? 13  ALA D C   1
+ATOM   3356 O  O   . ALA D 2 13  ? -19.408 2.380   40.613 1.00 27.12 ? 13  ALA D O   1
+ATOM   3357 C  CB  . ALA D 2 13  ? -18.812 1.000   43.174 1.00 40.91 ? 13  ALA D CB  1
+ATOM   3358 N  N   . LEU D 2 14  ? -17.334 2.893   41.468 1.00 21.51 ? 14  LEU D N   1
+ATOM   3359 C  CA  . LEU D 2 14  ? -17.418 4.000   40.737 1.00 19.28 ? 14  LEU D CA  1
+ATOM   3360 C  C   . LEU D 2 14  ? -17.280 3.833   39.222 1.00 20.58 ? 14  LEU D C   1
+ATOM   3361 O  O   . LEU D 2 14  ? -17.966 4.648   38.542 1.00 19.87 ? 14  LEU D O   1
+ATOM   3362 C  CB  . LEU D 2 14  ? -16.152 4.973   41.380 1.00 18.39 ? 14  LEU D CB  1
+ATOM   3363 C  CG  . LEU D 2 14  ? -16.156 6.398   40.759 1.00 32.12 ? 14  LEU D CG  1
+ATOM   3364 C  CD1 . LEU D 2 14  ? -17.023 7.032   41.940 1.00 41.26 ? 14  LEU D CD1 1
+ATOM   3365 C  CD2 . LEU D 2 14  ? -15.015 7.007   40.947 1.00 34.27 ? 14  LEU D CD2 1
+ATOM   3366 N  N   . TRP D 2 15  ? -16.558 2.791   38.917 1.00 16.79 ? 15  TRP D N   1
+ATOM   3367 C  CA  . TRP D 2 15  ? -16.231 2.780   37.400 1.00 13.47 ? 15  TRP D CA  1
+ATOM   3368 C  C   . TRP D 2 15  ? -17.544 2.168   36.758 1.00 22.23 ? 15  TRP D C   1
+ATOM   3369 O  O   . TRP D 2 15  ? -17.827 2.548   35.648 1.00 22.75 ? 15  TRP D O   1
+ATOM   3370 C  CB  . TRP D 2 15  ? -15.143 1.692   37.312 1.00 17.27 ? 15  TRP D CB  1
+ATOM   3371 C  CG  . TRP D 2 15  ? -14.595 1.723   35.935 1.00 18.39 ? 15  TRP D CG  1
+ATOM   3372 C  CD1 . TRP D 2 15  ? -14.816 0.889   34.905 1.00 29.85 ? 15  TRP D CD1 1
+ATOM   3373 C  CD2 . TRP D 2 15  ? -13.720 2.887   35.416 1.00 19.14 ? 15  TRP D CD2 1
+ATOM   3374 N  NE1 . TRP D 2 15  ? -14.172 1.244   33.768 1.00 25.67 ? 15  TRP D NE1 1
+ATOM   3375 C  CE2 . TRP D 2 15  ? -13.383 2.497   33.924 1.00 18.90 ? 15  TRP D CE2 1
+ATOM   3376 C  CE3 . TRP D 2 15  ? -13.080 3.915   36.031 1.00 24.35 ? 15  TRP D CE3 1
+ATOM   3377 C  CZ2 . TRP D 2 15  ? -12.641 3.361   33.151 1.00 22.83 ? 15  TRP D CZ2 1
+ATOM   3378 C  CZ3 . TRP D 2 15  ? -12.106 4.660   35.230 1.00 24.62 ? 15  TRP D CZ3 1
+ATOM   3379 C  CH2 . TRP D 2 15  ? -12.019 4.234   33.747 1.00 30.44 ? 15  TRP D CH2 1
+ATOM   3380 N  N   . GLY D 2 16  ? -18.491 1.478   37.485 1.00 23.06 ? 16  GLY D N   1
+ATOM   3381 C  CA  . GLY D 2 16  ? -19.793 1.191   36.728 1.00 23.16 ? 16  GLY D CA  1
+ATOM   3382 C  C   . GLY D 2 16  ? -20.459 2.371   36.417 1.00 26.54 ? 16  GLY D C   1
+ATOM   3383 O  O   . GLY D 2 16  ? -21.452 2.217   35.507 1.00 26.11 ? 16  GLY D O   1
+ATOM   3384 N  N   . LYS D 2 17  ? -20.410 3.631   36.818 1.00 18.84 ? 17  LYS D N   1
+ATOM   3385 C  CA  . LYS D 2 17  ? -21.028 4.830   36.770 1.00 24.96 ? 17  LYS D CA  1
+ATOM   3386 C  C   . LYS D 2 17  ? -20.676 5.690   35.682 1.00 22.00 ? 17  LYS D C   1
+ATOM   3387 O  O   . LYS D 2 17  ? -20.568 6.824   35.031 1.00 24.63 ? 17  LYS D O   1
+ATOM   3388 C  CB  . LYS D 2 17  ? -21.116 5.801   38.090 1.00 28.33 ? 17  LYS D CB  1
+ATOM   3389 C  CG  . LYS D 2 17  ? -21.714 5.050   38.992 1.00 27.71 ? 17  LYS D CG  1
+ATOM   3390 C  CD  . LYS D 2 17  ? -21.804 6.103   39.890 1.00 33.37 ? 17  LYS D CD  1
+ATOM   3391 C  CE  . LYS D 2 17  ? -21.674 6.250   41.300 1.00 43.68 ? 17  LYS D CE  1
+ATOM   3392 N  NZ  . LYS D 2 17  ? -22.932 7.781   41.294 1.00 36.22 ? 17  LYS D NZ  1
+ATOM   3393 N  N   . VAL D 2 18  ? -19.223 5.295   35.122 1.00 33.39 ? 18  VAL D N   1
+ATOM   3394 C  CA  . VAL D 2 18  ? -18.148 6.126   34.101 1.00 24.51 ? 18  VAL D CA  1
+ATOM   3395 C  C   . VAL D 2 18  ? -18.899 5.836   32.572 1.00 27.24 ? 18  VAL D C   1
+ATOM   3396 O  O   . VAL D 2 18  ? -18.938 4.608   32.580 1.00 26.54 ? 18  VAL D O   1
+ATOM   3397 C  CB  . VAL D 2 18  ? -16.931 5.822   34.176 1.00 31.98 ? 18  VAL D CB  1
+ATOM   3398 C  CG1 . VAL D 2 18  ? -15.989 6.139   33.348 1.00 31.25 ? 18  VAL D CG1 1
+ATOM   3399 C  CG2 . VAL D 2 18  ? -16.164 6.263   35.739 1.00 22.12 ? 18  VAL D CG2 1
+ATOM   3400 N  N   . ASN D 2 19  ? -19.102 6.858   32.015 1.00 25.81 ? 19  ASN D N   1
+ATOM   3401 C  CA  . ASN D 2 19  ? -19.052 6.863   30.602 1.00 27.55 ? 19  ASN D CA  1
+ATOM   3402 C  C   . ASN D 2 19  ? -17.973 6.590   30.015 1.00 24.31 ? 19  ASN D C   1
+ATOM   3403 O  O   . ASN D 2 19  ? -17.248 7.826   29.859 1.00 20.67 ? 19  ASN D O   1
+ATOM   3404 C  CB  . ASN D 2 19  ? -20.035 7.864   30.104 1.00 40.49 ? 19  ASN D CB  1
+ATOM   3405 C  CG  . ASN D 2 19  ? -20.692 7.172   28.675 1.00 44.62 ? 19  ASN D CG  1
+ATOM   3406 O  OD1 . ASN D 2 19  ? -19.563 7.478   27.587 1.00 45.68 ? 19  ASN D OD1 1
+ATOM   3407 N  ND2 . ASN D 2 19  ? -21.322 8.574   27.924 1.00 50.78 ? 19  ASN D ND2 1
+ATOM   3408 N  N   . VAL D 2 20  ? -17.436 5.688   29.546 1.00 22.82 ? 20  VAL D N   1
+ATOM   3409 C  CA  . VAL D 2 20  ? -15.916 5.675   28.951 1.00 40.38 ? 20  VAL D CA  1
+ATOM   3410 C  C   . VAL D 2 20  ? -15.515 6.534   28.237 1.00 37.93 ? 20  VAL D C   1
+ATOM   3411 O  O   . VAL D 2 20  ? -14.531 7.216   27.787 1.00 32.18 ? 20  VAL D O   1
+ATOM   3412 C  CB  . VAL D 2 20  ? -15.212 3.705   29.066 1.00 54.80 ? 20  VAL D CB  1
+ATOM   3413 C  CG1 . VAL D 2 20  ? -15.630 3.549   30.126 1.00 34.72 ? 20  VAL D CG1 1
+ATOM   3414 C  CG2 . VAL D 2 20  ? -14.780 4.198   28.091 1.00 63.33 ? 20  VAL D CG2 1
+ATOM   3415 N  N   . ASP D 2 21  ? -16.430 6.546   27.136 1.00 36.66 ? 21  ASP D N   1
+ATOM   3416 C  CA  . ASP D 2 21  ? -16.393 7.840   26.241 1.00 54.12 ? 21  ASP D CA  1
+ATOM   3417 C  C   . ASP D 2 21  ? -16.366 8.806   26.284 1.00 46.84 ? 21  ASP D C   1
+ATOM   3418 O  O   . ASP D 2 21  ? -15.134 9.597   25.944 1.00 32.53 ? 21  ASP D O   1
+ATOM   3419 C  CB  . ASP D 2 21  ? -17.519 7.615   25.194 1.00 60.03 ? 21  ASP D CB  1
+ATOM   3420 C  CG  . ASP D 2 21  ? -17.740 5.940   24.636 1.00 75.30 ? 21  ASP D CG  1
+ATOM   3421 O  OD1 . ASP D 2 21  ? -16.630 4.820   24.473 1.00 51.52 ? 21  ASP D OD1 1
+ATOM   3422 O  OD2 . ASP D 2 21  ? -18.227 5.979   23.552 1.00 64.70 ? 21  ASP D OD2 1
+ATOM   3423 N  N   . GLU D 2 22  ? -17.119 9.533   27.126 1.00 27.09 ? 22  GLU D N   1
+ATOM   3424 C  CA  . GLU D 2 22  ? -17.179 10.878  27.543 1.00 23.15 ? 22  GLU D CA  1
+ATOM   3425 C  C   . GLU D 2 22  ? -15.584 11.071  28.411 1.00 19.08 ? 22  GLU D C   1
+ATOM   3426 O  O   . GLU D 2 22  ? -15.170 12.158  28.517 1.00 21.80 ? 22  GLU D O   1
+ATOM   3427 C  CB  . GLU D 2 22  ? -18.485 11.097  28.232 1.00 35.52 ? 22  GLU D CB  1
+ATOM   3428 C  CG  . GLU D 2 22  ? -18.323 11.436  28.888 1.00 68.74 ? 22  GLU D CG  1
+ATOM   3429 C  CD  . GLU D 2 22  ? -19.783 13.017  29.918 1.00 80.12 ? 22  GLU D CD  1
+ATOM   3430 O  OE1 . GLU D 2 22  ? -20.488 12.431  31.030 1.00 61.13 ? 22  GLU D OE1 1
+ATOM   3431 O  OE2 . GLU D 2 22  ? -20.311 13.300  28.822 1.00 73.88 ? 22  GLU D OE2 1
+ATOM   3432 N  N   . VAL D 2 23  ? -15.634 10.381  29.480 1.00 20.94 ? 23  VAL D N   1
+ATOM   3433 C  CA  . VAL D 2 23  ? -14.463 10.509  30.460 1.00 17.82 ? 23  VAL D CA  1
+ATOM   3434 C  C   . VAL D 2 23  ? -13.138 10.322  29.642 1.00 15.07 ? 23  VAL D C   1
+ATOM   3435 O  O   . VAL D 2 23  ? -12.180 11.062  29.913 1.00 21.11 ? 23  VAL D O   1
+ATOM   3436 C  CB  . VAL D 2 23  ? -14.558 9.448   31.669 1.00 18.64 ? 23  VAL D CB  1
+ATOM   3437 C  CG1 . VAL D 2 23  ? -13.341 9.420   32.240 1.00 21.45 ? 23  VAL D CG1 1
+ATOM   3438 C  CG2 . VAL D 2 23  ? -15.769 10.085  32.385 1.00 21.02 ? 23  VAL D CG2 1
+ATOM   3439 N  N   . GLY D 2 24  ? -12.986 9.434   28.824 1.00 12.96 ? 24  GLY D N   1
+ATOM   3440 C  CA  . GLY D 2 24  ? -11.878 9.121   28.034 1.00 18.39 ? 24  GLY D CA  1
+ATOM   3441 C  C   . GLY D 2 24  ? -11.547 10.306  27.267 1.00 16.60 ? 24  GLY D C   1
+ATOM   3442 O  O   . GLY D 2 24  ? -10.409 10.924  27.177 1.00 15.31 ? 24  GLY D O   1
+ATOM   3443 N  N   . GLY D 2 25  ? -12.355 11.061  26.453 1.00 17.32 ? 25  GLY D N   1
+ATOM   3444 C  CA  . GLY D 2 25  ? -12.188 12.350  25.657 1.00 16.45 ? 25  GLY D CA  1
+ATOM   3445 C  C   . GLY D 2 25  ? -11.852 13.370  26.543 1.00 12.17 ? 25  GLY D C   1
+ATOM   3446 O  O   . GLY D 2 25  ? -10.851 14.085  26.162 1.00 21.20 ? 25  GLY D O   1
+ATOM   3447 N  N   . GLU D 2 26  ? -12.460 13.474  27.705 1.00 15.97 ? 26  GLU D N   1
+ATOM   3448 C  CA  . GLU D 2 26  ? -12.152 14.515  28.557 1.00 13.66 ? 26  GLU D CA  1
+ATOM   3449 C  C   . GLU D 2 26  ? -10.557 14.406  29.156 1.00 11.75 ? 26  GLU D C   1
+ATOM   3450 O  O   . GLU D 2 26  ? -9.912  15.423  29.196 1.00 13.88 ? 26  GLU D O   1
+ATOM   3451 C  CB  . GLU D 2 26  ? -13.123 14.726  29.831 1.00 18.62 ? 26  GLU D CB  1
+ATOM   3452 C  CG  . GLU D 2 26  ? -14.188 16.572  29.376 1.00 39.81 ? 26  GLU D CG  1
+ATOM   3453 C  CD  . GLU D 2 26  ? -12.894 16.082  30.681 1.00 31.77 ? 26  GLU D CD  1
+ATOM   3454 O  OE1 . GLU D 2 26  ? -13.289 17.828  30.717 1.00 34.99 ? 26  GLU D OE1 1
+ATOM   3455 O  OE2 . GLU D 2 26  ? -14.399 15.969  31.477 1.00 54.79 ? 26  GLU D OE2 1
+ATOM   3456 N  N   . ALA D 2 27  ? -10.347 13.228  29.564 1.00 12.60 ? 27  ALA D N   1
+ATOM   3457 C  CA  . ALA D 2 27  ? -8.949  12.868  30.128 1.00 17.85 ? 27  ALA D CA  1
+ATOM   3458 C  C   . ALA D 2 27  ? -7.850  13.176  29.161 1.00 15.51 ? 27  ALA D C   1
+ATOM   3459 O  O   . ALA D 2 27  ? -6.855  13.911  29.420 1.00 14.90 ? 27  ALA D O   1
+ATOM   3460 C  CB  . ALA D 2 27  ? -8.896  11.574  30.777 1.00 15.58 ? 27  ALA D CB  1
+ATOM   3461 N  N   . LEU D 2 28  ? -8.001  12.691  27.938 1.00 16.04 ? 28  LEU D N   1
+ATOM   3462 C  CA  . LEU D 2 28  ? -7.021  12.868  26.889 1.00 11.08 ? 28  LEU D CA  1
+ATOM   3463 C  C   . LEU D 2 28  ? -6.874  14.257  26.635 1.00 13.51 ? 28  LEU D C   1
+ATOM   3464 O  O   . LEU D 2 28  ? -5.774  14.841  26.314 1.00 14.05 ? 28  LEU D O   1
+ATOM   3465 C  CB  . LEU D 2 28  ? -7.318  12.029  25.637 1.00 12.20 ? 28  LEU D CB  1
+ATOM   3466 C  CG  . LEU D 2 28  ? -6.054  12.043  24.605 1.00 28.52 ? 28  LEU D CG  1
+ATOM   3467 C  CD1 . LEU D 2 28  ? -4.874  11.596  25.317 1.00 36.95 ? 28  LEU D CD1 1
+ATOM   3468 C  CD2 . LEU D 2 28  ? -6.499  11.363  23.512 1.00 34.25 ? 28  LEU D CD2 1
+ATOM   3469 N  N   . GLY D 2 29  ? -8.055  15.036  26.323 1.00 12.33 ? 29  GLY D N   1
+ATOM   3470 C  CA  . GLY D 2 29  ? -8.082  16.413  26.098 1.00 13.25 ? 29  GLY D CA  1
+ATOM   3471 C  C   . GLY D 2 29  ? -7.264  17.259  27.110 1.00 12.50 ? 29  GLY D C   1
+ATOM   3472 O  O   . GLY D 2 29  ? -6.525  18.181  26.694 1.00 16.69 ? 29  GLY D O   1
+ATOM   3473 N  N   . ARG D 2 30  ? -7.651  16.962  28.330 1.00 15.15 ? 30  ARG D N   1
+ATOM   3474 C  CA  . ARG D 2 30  ? -6.952  17.711  29.330 1.00 17.77 ? 30  ARG D CA  1
+ATOM   3475 C  C   . ARG D 2 30  ? -5.473  17.416  29.428 1.00 14.35 ? 30  ARG D C   1
+ATOM   3476 O  O   . ARG D 2 30  ? -4.736  18.387  29.661 1.00 14.59 ? 30  ARG D O   1
+ATOM   3477 C  CB  . ARG D 2 30  ? -7.784  17.510  30.710 1.00 15.53 ? 30  ARG D CB  1
+ATOM   3478 C  CG  . ARG D 2 30  ? -9.052  18.260  30.959 1.00 16.65 ? 30  ARG D CG  1
+ATOM   3479 C  CD  . ARG D 2 30  ? -9.694  17.989  32.143 1.00 28.01 ? 30  ARG D CD  1
+ATOM   3480 N  NE  . ARG D 2 30  ? -10.782 18.510  32.366 1.00 23.10 ? 30  ARG D NE  1
+ATOM   3481 C  CZ  . ARG D 2 30  ? -11.218 19.589  32.911 1.00 16.06 ? 30  ARG D CZ  1
+ATOM   3482 N  NH1 . ARG D 2 30  ? -12.376 20.084  33.152 1.00 17.46 ? 30  ARG D NH1 1
+ATOM   3483 N  NH2 . ARG D 2 30  ? -10.366 20.253  33.854 1.00 10.32 ? 30  ARG D NH2 1
+ATOM   3484 N  N   . LEU D 2 31  ? -5.090  16.308  29.208 1.00 15.53 ? 31  LEU D N   1
+ATOM   3485 C  CA  . LEU D 2 31  ? -3.720  16.020  29.031 1.00 14.63 ? 31  LEU D CA  1
+ATOM   3486 C  C   . LEU D 2 31  ? -2.934  17.040  28.180 1.00 16.67 ? 31  LEU D C   1
+ATOM   3487 O  O   . LEU D 2 31  ? -1.909  17.489  28.340 1.00 15.33 ? 31  LEU D O   1
+ATOM   3488 C  CB  . LEU D 2 31  ? -3.385  14.471  28.727 1.00 12.02 ? 31  LEU D CB  1
+ATOM   3489 C  CG  . LEU D 2 31  ? -1.994  14.084  28.648 1.00 17.81 ? 31  LEU D CG  1
+ATOM   3490 C  CD1 . LEU D 2 31  ? -1.285  13.877  29.979 1.00 18.94 ? 31  LEU D CD1 1
+ATOM   3491 C  CD2 . LEU D 2 31  ? -1.814  12.913  27.800 1.00 18.38 ? 31  LEU D CD2 1
+ATOM   3492 N  N   . LEU D 2 32  ? -3.593  16.981  26.876 1.00 8.95  ? 32  LEU D N   1
+ATOM   3493 C  CA  . LEU D 2 32  ? -3.068  17.791  25.894 1.00 13.61 ? 32  LEU D CA  1
+ATOM   3494 C  C   . LEU D 2 32  ? -3.063  19.193  26.147 1.00 13.07 ? 32  LEU D C   1
+ATOM   3495 O  O   . LEU D 2 32  ? -2.160  20.018  25.560 1.00 15.98 ? 32  LEU D O   1
+ATOM   3496 C  CB  . LEU D 2 32  ? -3.694  17.478  24.626 1.00 14.00 ? 32  LEU D CB  1
+ATOM   3497 C  CG  . LEU D 2 32  ? -3.365  16.122  24.112 1.00 23.55 ? 32  LEU D CG  1
+ATOM   3498 C  CD1 . LEU D 2 32  ? -4.407  15.861  22.841 1.00 25.80 ? 32  LEU D CD1 1
+ATOM   3499 C  CD2 . LEU D 2 32  ? -2.276  15.484  23.939 1.00 26.67 ? 32  LEU D CD2 1
+ATOM   3500 N  N   . VAL D 2 33  ? -4.034  19.732  27.005 1.00 13.83 ? 33  VAL D N   1
+ATOM   3501 C  CA  . VAL D 2 33  ? -4.155  21.214  27.399 1.00 13.13 ? 33  VAL D CA  1
+ATOM   3502 C  C   . VAL D 2 33  ? -3.024  21.494  28.382 1.00 16.82 ? 33  VAL D C   1
+ATOM   3503 O  O   . VAL D 2 33  ? -2.443  22.499  28.367 1.00 15.10 ? 33  VAL D O   1
+ATOM   3504 C  CB  . VAL D 2 33  ? -5.581  21.447  27.790 1.00 11.59 ? 33  VAL D CB  1
+ATOM   3505 C  CG1 . VAL D 2 33  ? -5.545  22.833  28.313 1.00 21.42 ? 33  VAL D CG1 1
+ATOM   3506 C  CG2 . VAL D 2 33  ? -6.447  21.404  26.485 1.00 18.60 ? 33  VAL D CG2 1
+ATOM   3507 N  N   . VAL D 2 34  ? -3.179  20.690  29.465 1.00 12.61 ? 34  VAL D N   1
+ATOM   3508 C  CA  . VAL D 2 34  ? -2.460  21.056  30.666 1.00 13.03 ? 34  VAL D CA  1
+ATOM   3509 C  C   . VAL D 2 34  ? -0.965  20.975  30.488 1.00 15.88 ? 34  VAL D C   1
+ATOM   3510 O  O   . VAL D 2 34  ? -0.192  21.524  31.192 1.00 16.40 ? 34  VAL D O   1
+ATOM   3511 C  CB  . VAL D 2 34  ? -3.052  20.377  31.966 1.00 15.07 ? 34  VAL D CB  1
+ATOM   3512 C  CG1 . VAL D 2 34  ? -2.235  20.513  33.158 1.00 13.90 ? 34  VAL D CG1 1
+ATOM   3513 C  CG2 . VAL D 2 34  ? -4.455  20.818  32.193 1.00 18.23 ? 34  VAL D CG2 1
+ATOM   3514 N  N   . TYR D 2 35  ? -0.611  19.818  29.788 1.00 11.62 ? 35  TYR D N   1
+ATOM   3515 C  CA  . TYR D 2 35  ? 0.841   19.416  29.575 1.00 14.47 ? 35  TYR D CA  1
+ATOM   3516 C  C   . TYR D 2 35  ? 0.955   19.363  27.998 1.00 16.31 ? 35  TYR D C   1
+ATOM   3517 O  O   . TYR D 2 35  ? 1.108   18.244  27.443 1.00 17.14 ? 35  TYR D O   1
+ATOM   3518 C  CB  . TYR D 2 35  ? 1.042   18.023  30.126 1.00 14.04 ? 35  TYR D CB  1
+ATOM   3519 C  CG  . TYR D 2 35  ? 0.668   17.871  31.513 1.00 16.50 ? 35  TYR D CG  1
+ATOM   3520 C  CD1 . TYR D 2 35  ? 1.430   18.580  32.422 1.00 16.28 ? 35  TYR D CD1 1
+ATOM   3521 C  CD2 . TYR D 2 35  ? -0.282  17.215  31.952 1.00 21.92 ? 35  TYR D CD2 1
+ATOM   3522 C  CE1 . TYR D 2 35  ? 1.275   18.601  33.883 1.00 18.51 ? 35  TYR D CE1 1
+ATOM   3523 C  CE2 . TYR D 2 35  ? -0.563  17.205  33.318 1.00 25.13 ? 35  TYR D CE2 1
+ATOM   3524 C  CZ  . TYR D 2 35  ? 0.220   17.834  34.263 1.00 19.91 ? 35  TYR D CZ  1
+ATOM   3525 O  OH  . TYR D 2 35  ? -0.317  17.844  35.599 1.00 21.91 ? 35  TYR D OH  1
+ATOM   3526 N  N   . PRO D 2 36  ? 1.144   20.561  27.440 1.00 14.59 ? 36  PRO D N   1
+ATOM   3527 C  CA  . PRO D 2 36  ? 1.097   20.557  25.815 1.00 16.73 ? 36  PRO D CA  1
+ATOM   3528 C  C   . PRO D 2 36  ? 2.215   19.894  25.100 1.00 13.23 ? 36  PRO D C   1
+ATOM   3529 O  O   . PRO D 2 36  ? 2.004   19.535  23.916 1.00 15.17 ? 36  PRO D O   1
+ATOM   3530 C  CB  . PRO D 2 36  ? 0.923   22.086  25.619 1.00 24.30 ? 36  PRO D CB  1
+ATOM   3531 C  CG  . PRO D 2 36  ? 1.397   22.726  26.914 1.00 25.67 ? 36  PRO D CG  1
+ATOM   3532 C  CD  . PRO D 2 36  ? 1.182   21.785  27.886 1.00 17.58 ? 36  PRO D CD  1
+ATOM   3533 N  N   . TRP D 2 37  ? 3.339   19.527  25.839 1.00 13.75 ? 37  TRP D N   1
+ATOM   3534 C  CA  . TRP D 2 37  ? 4.287   18.875  25.146 1.00 15.13 ? 37  TRP D CA  1
+ATOM   3535 C  C   . TRP D 2 37  ? 3.976   17.467  24.807 1.00 14.32 ? 37  TRP D C   1
+ATOM   3536 O  O   . TRP D 2 37  ? 4.491   16.809  23.810 1.00 19.70 ? 37  TRP D O   1
+ATOM   3537 C  CB  . TRP D 2 37  ? 5.593   18.777  25.996 1.00 13.13 ? 37  TRP D CB  1
+ATOM   3538 C  CG  . TRP D 2 37  ? 5.442   18.275  27.445 1.00 8.65  ? 37  TRP D CG  1
+ATOM   3539 C  CD1 . TRP D 2 37  ? 5.572   17.038  27.908 1.00 13.10 ? 37  TRP D CD1 1
+ATOM   3540 C  CD2 . TRP D 2 37  ? 5.232   19.094  28.699 1.00 14.59 ? 37  TRP D CD2 1
+ATOM   3541 N  NE1 . TRP D 2 37  ? 5.519   16.937  29.212 1.00 17.65 ? 37  TRP D NE1 1
+ATOM   3542 C  CE2 . TRP D 2 37  ? 5.109   18.185  29.669 1.00 16.05 ? 37  TRP D CE2 1
+ATOM   3543 C  CE3 . TRP D 2 37  ? 4.863   20.419  28.889 1.00 11.20 ? 37  TRP D CE3 1
+ATOM   3544 C  CZ2 . TRP D 2 37  ? 4.948   18.598  31.166 1.00 26.88 ? 37  TRP D CZ2 1
+ATOM   3545 C  CZ3 . TRP D 2 37  ? 4.499   20.859  30.171 1.00 11.28 ? 37  TRP D CZ3 1
+ATOM   3546 C  CH2 . TRP D 2 37  ? 4.692   19.881  31.135 1.00 16.90 ? 37  TRP D CH2 1
+ATOM   3547 N  N   . THR D 2 38  ? 2.886   16.922  25.439 1.00 16.64 ? 38  THR D N   1
+ATOM   3548 C  CA  . THR D 2 38  ? 2.279   15.632  25.171 1.00 14.14 ? 38  THR D CA  1
+ATOM   3549 C  C   . THR D 2 38  ? 1.753   15.612  23.657 1.00 18.16 ? 38  THR D C   1
+ATOM   3550 O  O   . THR D 2 38  ? 1.414   14.497  23.146 1.00 16.15 ? 38  THR D O   1
+ATOM   3551 C  CB  . THR D 2 38  ? 1.172   15.206  26.129 1.00 11.09 ? 38  THR D CB  1
+ATOM   3552 O  OG1 . THR D 2 38  ? 0.118   16.074  26.157 1.00 14.48 ? 38  THR D OG1 1
+ATOM   3553 C  CG2 . THR D 2 38  ? 1.918   14.925  27.370 1.00 16.14 ? 38  THR D CG2 1
+ATOM   3554 N  N   . GLN D 2 39  ? 1.369   16.888  23.154 1.00 12.07 ? 39  GLN D N   1
+ATOM   3555 C  CA  . GLN D 2 39  ? 0.788   16.834  21.801 1.00 10.72 ? 39  GLN D CA  1
+ATOM   3556 C  C   . GLN D 2 39  ? 1.782   16.440  20.761 1.00 16.84 ? 39  GLN D C   1
+ATOM   3557 O  O   . GLN D 2 39  ? 1.457   16.070  19.685 1.00 21.52 ? 39  GLN D O   1
+ATOM   3558 C  CB  . GLN D 2 39  ? 0.644   18.385  21.518 1.00 13.63 ? 39  GLN D CB  1
+ATOM   3559 C  CG  . GLN D 2 39  ? -0.469  18.790  22.447 1.00 17.04 ? 39  GLN D CG  1
+ATOM   3560 C  CD  . GLN D 2 39  ? -0.712  20.174  22.133 1.00 23.47 ? 39  GLN D CD  1
+ATOM   3561 O  OE1 . GLN D 2 39  ? -0.217  20.929  21.053 1.00 25.04 ? 39  GLN D OE1 1
+ATOM   3562 N  NE2 . GLN D 2 39  ? -1.425  20.941  23.093 1.00 28.38 ? 39  GLN D NE2 1
+ATOM   3563 N  N   . ARG D 2 40  ? 3.169   16.130  21.037 1.00 12.32 ? 40  ARG D N   1
+ATOM   3564 C  CA  . ARG D 2 40  ? 4.313   15.722  20.258 1.00 16.79 ? 40  ARG D CA  1
+ATOM   3565 C  C   . ARG D 2 40  ? 3.742   14.501  19.713 1.00 17.58 ? 40  ARG D C   1
+ATOM   3566 O  O   . ARG D 2 40  ? 4.352   13.997  18.482 1.00 20.86 ? 40  ARG D O   1
+ATOM   3567 C  CB  . ARG D 2 40  ? 5.431   15.240  21.141 1.00 22.83 ? 40  ARG D CB  1
+ATOM   3568 C  CG  . ARG D 2 40  ? 5.589   14.263  21.838 1.00 37.26 ? 40  ARG D CG  1
+ATOM   3569 C  CD  . ARG D 2 40  ? 6.966   14.500  22.611 1.00 23.75 ? 40  ARG D CD  1
+ATOM   3570 N  NE  . ARG D 2 40  ? 8.091   14.529  22.000 1.00 28.71 ? 40  ARG D NE  1
+ATOM   3571 C  CZ  . ARG D 2 40  ? 8.546   13.446  21.122 1.00 41.77 ? 40  ARG D CZ  1
+ATOM   3572 N  NH1 . ARG D 2 40  ? 8.306   12.392  21.501 1.00 31.05 ? 40  ARG D NH1 1
+ATOM   3573 N  NH2 . ARG D 2 40  ? 9.856   13.951  20.709 1.00 37.79 ? 40  ARG D NH2 1
+ATOM   3574 N  N   . PHE D 2 41  ? 2.837   13.601  20.156 1.00 15.17 ? 41  PHE D N   1
+ATOM   3575 C  CA  . PHE D 2 41  ? 2.466   12.283  19.683 1.00 16.55 ? 41  PHE D CA  1
+ATOM   3576 C  C   . PHE D 2 41  ? 1.139   12.469  18.585 1.00 20.00 ? 41  PHE D C   1
+ATOM   3577 O  O   . PHE D 2 41  ? 0.893   11.285  18.312 1.00 23.52 ? 41  PHE D O   1
+ATOM   3578 C  CB  . PHE D 2 41  ? 2.112   11.188  20.703 1.00 13.75 ? 41  PHE D CB  1
+ATOM   3579 C  CG  . PHE D 2 41  ? 3.390   11.045  21.728 1.00 12.41 ? 41  PHE D CG  1
+ATOM   3580 C  CD1 . PHE D 2 41  ? 3.334   11.831  22.940 1.00 16.97 ? 41  PHE D CD1 1
+ATOM   3581 C  CD2 . PHE D 2 41  ? 4.388   10.383  21.340 1.00 18.05 ? 41  PHE D CD2 1
+ATOM   3582 C  CE1 . PHE D 2 41  ? 4.534   11.379  23.527 1.00 23.07 ? 41  PHE D CE1 1
+ATOM   3583 C  CE2 . PHE D 2 41  ? 5.649   10.243  22.053 1.00 24.82 ? 41  PHE D CE2 1
+ATOM   3584 C  CZ  . PHE D 2 41  ? 5.469   10.894  23.293 1.00 25.09 ? 41  PHE D CZ  1
+ATOM   3585 N  N   . PHE D 2 42  ? 0.736   13.624  18.567 1.00 15.21 ? 42  PHE D N   1
+ATOM   3586 C  CA  . PHE D 2 42  ? -0.594  13.543  18.060 1.00 14.18 ? 42  PHE D CA  1
+ATOM   3587 C  C   . PHE D 2 42  ? -0.709  14.419  16.840 1.00 19.41 ? 42  PHE D C   1
+ATOM   3588 O  O   . PHE D 2 42  ? -1.639  15.320  16.588 1.00 18.71 ? 42  PHE D O   1
+ATOM   3589 C  CB  . PHE D 2 42  ? -1.647  13.942  18.951 1.00 21.58 ? 42  PHE D CB  1
+ATOM   3590 C  CG  . PHE D 2 42  ? -1.779  12.702  19.949 1.00 17.63 ? 42  PHE D CG  1
+ATOM   3591 C  CD1 . PHE D 2 42  ? -1.146  13.236  21.415 1.00 20.37 ? 42  PHE D CD1 1
+ATOM   3592 C  CD2 . PHE D 2 42  ? -2.404  11.476  19.753 1.00 20.14 ? 42  PHE D CD2 1
+ATOM   3593 C  CE1 . PHE D 2 42  ? -1.373  12.026  22.264 1.00 27.02 ? 42  PHE D CE1 1
+ATOM   3594 C  CE2 . PHE D 2 42  ? -2.374  10.556  20.656 1.00 27.08 ? 42  PHE D CE2 1
+ATOM   3595 C  CZ  . PHE D 2 42  ? -1.814  10.933  22.060 1.00 18.28 ? 42  PHE D CZ  1
+ATOM   3596 N  N   . GLU D 2 43  ? 0.555   14.470  16.272 1.00 32.32 ? 43  GLU D N   1
+ATOM   3597 C  CA  . GLU D 2 43  ? 0.518   15.755  15.308 1.00 33.61 ? 43  GLU D CA  1
+ATOM   3598 C  C   . GLU D 2 43  ? -0.610  15.692  13.734 1.00 12.75 ? 43  GLU D C   1
+ATOM   3599 O  O   . GLU D 2 43  ? -0.815  16.648  13.305 1.00 26.94 ? 43  GLU D O   1
+ATOM   3600 C  CB  . GLU D 2 43  ? 1.452   15.695  14.586 1.00 65.31 ? 43  GLU D CB  1
+ATOM   3601 C  CG  . GLU D 2 43  ? 2.122   15.519  14.233 1.00 43.00 ? 43  GLU D CG  1
+ATOM   3602 C  CD  . GLU D 2 43  ? 3.200   16.627  15.368 1.00 32.00 ? 43  GLU D CD  1
+ATOM   3603 O  OE1 . GLU D 2 43  ? 2.726   18.154  15.261 1.00 29.89 ? 43  GLU D OE1 1
+ATOM   3604 O  OE2 . GLU D 2 43  ? 4.662   17.157  15.678 1.00 58.55 ? 43  GLU D OE2 1
+ATOM   3605 N  N   . SER D 2 44  ? -0.860  14.341  13.723 1.00 19.02 ? 44  SER D N   1
+ATOM   3606 C  CA  . SER D 2 44  ? -1.752  13.785  12.602 1.00 25.67 ? 44  SER D CA  1
+ATOM   3607 C  C   . SER D 2 44  ? -2.950  14.205  13.024 1.00 26.66 ? 44  SER D C   1
+ATOM   3608 O  O   . SER D 2 44  ? -4.065  14.043  12.463 1.00 32.13 ? 44  SER D O   1
+ATOM   3609 C  CB  . SER D 2 44  ? -1.781  12.457  12.398 1.00 42.87 ? 44  SER D CB  1
+ATOM   3610 O  OG  . SER D 2 44  ? -2.245  11.599  13.186 1.00 44.29 ? 44  SER D OG  1
+ATOM   3611 N  N   . PHE D 2 45  ? -3.524  14.749  14.284 1.00 27.34 ? 45  PHE D N   1
+ATOM   3612 C  CA  . PHE D 2 45  ? -4.912  14.923  14.815 1.00 24.93 ? 45  PHE D CA  1
+ATOM   3613 C  C   . PHE D 2 45  ? -5.529  16.448  14.301 1.00 23.30 ? 45  PHE D C   1
+ATOM   3614 O  O   . PHE D 2 45  ? -6.784  16.280  14.827 1.00 31.71 ? 45  PHE D O   1
+ATOM   3615 C  CB  . PHE D 2 45  ? -4.790  14.822  16.348 1.00 26.07 ? 45  PHE D CB  1
+ATOM   3616 C  CG  . PHE D 2 45  ? -4.937  13.410  16.728 1.00 19.10 ? 45  PHE D CG  1
+ATOM   3617 C  CD1 . PHE D 2 45  ? -5.462  13.235  18.047 1.00 43.96 ? 45  PHE D CD1 1
+ATOM   3618 C  CD2 . PHE D 2 45  ? -4.642  12.334  16.222 1.00 26.17 ? 45  PHE D CD2 1
+ATOM   3619 C  CE1 . PHE D 2 45  ? -5.540  11.694  18.489 1.00 29.49 ? 45  PHE D CE1 1
+ATOM   3620 C  CE2 . PHE D 2 45  ? -4.576  11.056  16.662 1.00 32.75 ? 45  PHE D CE2 1
+ATOM   3621 C  CZ  . PHE D 2 45  ? -5.140  10.619  17.735 1.00 28.04 ? 45  PHE D CZ  1
+ATOM   3622 N  N   . GLY D 2 46  ? -4.976  17.029  13.971 1.00 35.08 ? 46  GLY D N   1
+ATOM   3623 C  CA  . GLY D 2 46  ? -5.663  18.107  13.666 1.00 34.51 ? 46  GLY D CA  1
+ATOM   3624 C  C   . GLY D 2 46  ? -5.445  19.748  14.426 1.00 32.00 ? 46  GLY D C   1
+ATOM   3625 O  O   . GLY D 2 46  ? -4.132  19.446  14.809 1.00 42.65 ? 46  GLY D O   1
+ATOM   3626 N  N   . ASP D 2 47  ? -6.609  20.220  14.854 1.00 33.75 ? 47  ASP D N   1
+ATOM   3627 C  CA  . ASP D 2 47  ? -5.368  21.899  14.875 1.00 43.29 ? 47  ASP D CA  1
+ATOM   3628 C  C   . ASP D 2 47  ? -5.953  21.259  17.141 1.00 24.69 ? 47  ASP D C   1
+ATOM   3629 O  O   . ASP D 2 47  ? -7.210  20.795  17.273 1.00 33.08 ? 47  ASP D O   1
+ATOM   3630 C  CB  . ASP D 2 47  ? -7.250  22.379  14.876 1.00 48.49 ? 47  ASP D CB  1
+ATOM   3631 C  CG  . ASP D 2 47  ? -7.024  23.961  15.603 1.00 50.77 ? 47  ASP D CG  1
+ATOM   3632 O  OD1 . ASP D 2 47  ? -8.290  24.345  15.588 1.00 57.75 ? 47  ASP D OD1 1
+ATOM   3633 O  OD2 . ASP D 2 47  ? -5.859  24.326  15.726 1.00 45.03 ? 47  ASP D OD2 1
+ATOM   3634 N  N   . LEU D 2 48  ? -4.839  21.609  17.351 1.00 25.73 ? 48  LEU D N   1
+ATOM   3635 C  CA  . LEU D 2 48  ? -4.614  21.236  19.012 1.00 29.97 ? 48  LEU D CA  1
+ATOM   3636 C  C   . LEU D 2 48  ? -4.356  22.697  19.812 1.00 32.06 ? 48  LEU D C   1
+ATOM   3637 O  O   . LEU D 2 48  ? -3.483  22.675  20.752 1.00 36.43 ? 48  LEU D O   1
+ATOM   3638 C  CB  . LEU D 2 48  ? -3.485  20.507  19.028 1.00 41.80 ? 48  LEU D CB  1
+ATOM   3639 C  CG  . LEU D 2 48  ? -4.131  19.086  18.662 1.00 22.03 ? 48  LEU D CG  1
+ATOM   3640 C  CD1 . LEU D 2 48  ? -2.764  18.027  18.946 1.00 37.56 ? 48  LEU D CD1 1
+ATOM   3641 C  CD2 . LEU D 2 48  ? -5.434  18.510  19.194 1.00 29.67 ? 48  LEU D CD2 1
+ATOM   3642 N  N   . SER D 2 49  ? -4.712  23.785  18.825 1.00 38.40 ? 49  SER D N   1
+ATOM   3643 C  CA  . SER D 2 49  ? -3.694  24.938  19.115 1.00 43.30 ? 49  SER D CA  1
+ATOM   3644 C  C   . SER D 2 49  ? -4.538  26.126  20.275 1.00 46.97 ? 49  SER D C   1
+ATOM   3645 O  O   . SER D 2 49  ? -3.694  26.522  21.319 1.00 46.32 ? 49  SER D O   1
+ATOM   3646 C  CB  . SER D 2 49  ? -3.847  26.023  17.936 1.00 47.25 ? 49  SER D CB  1
+ATOM   3647 O  OG  . SER D 2 49  ? -5.194  26.397  17.689 1.00 49.74 ? 49  SER D OG  1
+ATOM   3648 N  N   . THR D 2 50  ? -5.777  25.636  20.358 1.00 43.91 ? 50  THR D N   1
+ATOM   3649 C  CA  . THR D 2 50  ? -5.849  26.077  22.006 1.00 36.95 ? 50  THR D CA  1
+ATOM   3650 C  C   . THR D 2 50  ? -7.139  25.182  22.693 1.00 36.10 ? 50  THR D C   1
+ATOM   3651 O  O   . THR D 2 50  ? -7.492  24.147  22.063 1.00 28.99 ? 50  THR D O   1
+ATOM   3652 C  CB  . THR D 2 50  ? -7.457  27.261  21.332 1.00 37.26 ? 50  THR D CB  1
+ATOM   3653 O  OG1 . THR D 2 50  ? -8.756  26.720  20.713 1.00 36.38 ? 50  THR D OG1 1
+ATOM   3654 C  CG2 . THR D 2 50  ? -6.757  28.315  20.562 1.00 56.40 ? 50  THR D CG2 1
+ATOM   3655 N  N   . PRO D 2 51  ? -7.512  25.462  23.851 1.00 37.42 ? 51  PRO D N   1
+ATOM   3656 C  CA  . PRO D 2 51  ? -8.332  24.663  24.610 1.00 32.59 ? 51  PRO D CA  1
+ATOM   3657 C  C   . PRO D 2 51  ? -9.508  24.112  24.121 1.00 29.25 ? 51  PRO D C   1
+ATOM   3658 O  O   . PRO D 2 51  ? -10.079 22.866  24.103 1.00 26.15 ? 51  PRO D O   1
+ATOM   3659 C  CB  . PRO D 2 51  ? -8.592  25.471  25.978 1.00 37.41 ? 51  PRO D CB  1
+ATOM   3660 C  CG  . PRO D 2 51  ? -7.364  26.143  26.051 1.00 36.57 ? 51  PRO D CG  1
+ATOM   3661 C  CD  . PRO D 2 51  ? -6.905  26.754  24.543 1.00 42.54 ? 51  PRO D CD  1
+ATOM   3662 N  N   . ASP D 2 52  ? -10.302 25.101  23.369 1.00 30.65 ? 52  ASP D N   1
+ATOM   3663 C  CA  . ASP D 2 52  ? -11.863 24.475  22.836 1.00 39.40 ? 52  ASP D CA  1
+ATOM   3664 C  C   . ASP D 2 52  ? -11.353 23.586  21.588 1.00 56.69 ? 52  ASP D C   1
+ATOM   3665 O  O   . ASP D 2 52  ? -12.242 22.836  21.462 1.00 40.69 ? 52  ASP D O   1
+ATOM   3666 C  CB  . ASP D 2 52  ? -12.285 25.844  22.532 1.00 43.19 ? 52  ASP D CB  1
+ATOM   3667 C  CG  . ASP D 2 52  ? -12.845 27.083  23.638 1.00 63.04 ? 52  ASP D CG  1
+ATOM   3668 O  OD1 . ASP D 2 52  ? -12.875 26.403  24.543 1.00 49.71 ? 52  ASP D OD1 1
+ATOM   3669 O  OD2 . ASP D 2 52  ? -10.565 27.945  23.807 1.00 60.40 ? 52  ASP D OD2 1
+ATOM   3670 N  N   . ALA D 2 53  ? -10.482 24.050  20.860 1.00 26.05 ? 53  ALA D N   1
+ATOM   3671 C  CA  . ALA D 2 53  ? -10.066 23.415  19.717 1.00 33.75 ? 53  ALA D CA  1
+ATOM   3672 C  C   . ALA D 2 53  ? -9.706  21.714  20.002 1.00 42.76 ? 53  ALA D C   1
+ATOM   3673 O  O   . ALA D 2 53  ? -10.050 20.911  19.824 1.00 38.58 ? 53  ALA D O   1
+ATOM   3674 C  CB  . ALA D 2 53  ? -9.013  23.676  19.014 1.00 40.18 ? 53  ALA D CB  1
+ATOM   3675 N  N   . VAL D 2 54  ? -8.604  21.730  21.102 1.00 27.10 ? 54  VAL D N   1
+ATOM   3676 C  CA  . VAL D 2 54  ? -8.333  20.245  21.677 1.00 25.12 ? 54  VAL D CA  1
+ATOM   3677 C  C   . VAL D 2 54  ? -9.504  19.647  22.180 1.00 26.50 ? 54  VAL D C   1
+ATOM   3678 O  O   . VAL D 2 54  ? -9.901  18.373  21.823 1.00 24.76 ? 54  VAL D O   1
+ATOM   3679 C  CB  . VAL D 2 54  ? -7.239  20.560  22.712 1.00 26.67 ? 54  VAL D CB  1
+ATOM   3680 C  CG1 . VAL D 2 54  ? -7.129  19.006  23.293 1.00 25.19 ? 54  VAL D CG1 1
+ATOM   3681 C  CG2 . VAL D 2 54  ? -6.139  21.045  22.323 1.00 31.48 ? 54  VAL D CG2 1
+ATOM   3682 N  N   . MET D 2 55  ? -10.565 20.221  22.979 1.00 25.87 ? 55  MET D N   1
+ATOM   3683 C  CA  . MET D 2 55  ? -11.629 19.456  23.590 1.00 29.84 ? 55  MET D CA  1
+ATOM   3684 C  C   . MET D 2 55  ? -13.050 19.098  22.385 1.00 35.52 ? 55  MET D C   1
+ATOM   3685 O  O   . MET D 2 55  ? -13.443 18.078  22.769 1.00 32.07 ? 55  MET D O   1
+ATOM   3686 C  CB  . MET D 2 55  ? -12.288 20.389  24.814 1.00 26.28 ? 55  MET D CB  1
+ATOM   3687 C  CG  . MET D 2 55  ? -11.386 20.485  25.674 1.00 36.16 ? 55  MET D CG  1
+ATOM   3688 S  SD  . MET D 2 55  ? -10.260 19.313  26.642 1.00 25.36 ? 55  MET D SD  1
+ATOM   3689 C  CE  . MET D 2 55  ? -11.478 18.411  27.213 1.00 19.21 ? 55  MET D CE  1
+ATOM   3690 N  N   . GLY D 2 56  ? -12.706 20.117  21.518 1.00 30.97 ? 56  GLY D N   1
+ATOM   3691 C  CA  . GLY D 2 56  ? -13.876 19.519  20.829 1.00 35.09 ? 56  GLY D CA  1
+ATOM   3692 C  C   . GLY D 2 56  ? -13.378 18.656  19.701 1.00 44.75 ? 56  GLY D C   1
+ATOM   3693 O  O   . GLY D 2 56  ? -13.862 18.366  18.521 1.00 34.49 ? 56  GLY D O   1
+ATOM   3694 N  N   . ASN D 2 57  ? -12.009 18.431  19.287 1.00 25.90 ? 57  ASN D N   1
+ATOM   3695 C  CA  . ASN D 2 57  ? -11.361 17.710  18.254 1.00 29.86 ? 57  ASN D CA  1
+ATOM   3696 C  C   . ASN D 2 57  ? -11.866 16.331  18.408 1.00 26.15 ? 57  ASN D C   1
+ATOM   3697 O  O   . ASN D 2 57  ? -11.928 15.394  19.177 1.00 26.55 ? 57  ASN D O   1
+ATOM   3698 C  CB  . ASN D 2 57  ? -9.894  17.820  18.357 1.00 30.42 ? 57  ASN D CB  1
+ATOM   3699 C  CG  . ASN D 2 57  ? -9.245  17.042  17.310 1.00 23.49 ? 57  ASN D CG  1
+ATOM   3700 O  OD1 . ASN D 2 57  ? -9.378  15.869  16.906 1.00 31.02 ? 57  ASN D OD1 1
+ATOM   3701 N  ND2 . ASN D 2 57  ? -8.358  17.725  16.884 1.00 27.30 ? 57  ASN D ND2 1
+ATOM   3702 N  N   . PRO D 2 58  ? -12.452 15.845  17.208 1.00 29.25 ? 58  PRO D N   1
+ATOM   3703 C  CA  . PRO D 2 58  ? -13.131 14.529  17.192 1.00 25.97 ? 58  PRO D CA  1
+ATOM   3704 C  C   . PRO D 2 58  ? -11.869 13.412  17.167 1.00 16.05 ? 58  PRO D C   1
+ATOM   3705 O  O   . PRO D 2 58  ? -12.367 12.214  17.772 1.00 24.61 ? 58  PRO D O   1
+ATOM   3706 C  CB  . PRO D 2 58  ? -13.856 14.302  15.729 1.00 33.18 ? 58  PRO D CB  1
+ATOM   3707 C  CG  . PRO D 2 58  ? -12.983 16.101  15.724 1.00 59.49 ? 58  PRO D CG  1
+ATOM   3708 C  CD  . PRO D 2 58  ? -12.904 16.285  15.619 1.00 43.36 ? 58  PRO D CD  1
+ATOM   3709 N  N   . LYS D 2 59  ? -10.814 13.556  16.702 1.00 21.03 ? 59  LYS D N   1
+ATOM   3710 C  CA  . LYS D 2 59  ? -9.844  12.639  16.760 1.00 25.38 ? 59  LYS D CA  1
+ATOM   3711 C  C   . LYS D 2 59  ? -9.152  12.307  18.341 1.00 17.84 ? 59  LYS D C   1
+ATOM   3712 O  O   . LYS D 2 59  ? -8.920  11.109  18.549 1.00 21.39 ? 59  LYS D O   1
+ATOM   3713 C  CB  . LYS D 2 59  ? -8.725  12.767  15.846 1.00 32.15 ? 59  LYS D CB  1
+ATOM   3714 C  CG  . LYS D 2 59  ? -8.998  12.567  14.411 1.00 48.59 ? 59  LYS D CG  1
+ATOM   3715 C  CD  . LYS D 2 59  ? -8.385  13.051  13.829 1.00 53.12 ? 59  LYS D CD  1
+ATOM   3716 C  CE  . LYS D 2 59  ? -7.645  12.227  12.310 1.00 53.54 ? 59  LYS D CE  1
+ATOM   3717 N  NZ  . LYS D 2 59  ? -8.428  13.116  11.202 1.00 62.98 ? 59  LYS D NZ  1
+ATOM   3718 N  N   . VAL D 2 60  ? -9.307  13.560  18.909 1.00 18.98 ? 60  VAL D N   1
+ATOM   3719 C  CA  . VAL D 2 60  ? -9.026  13.424  20.544 1.00 19.06 ? 60  VAL D CA  1
+ATOM   3720 C  C   . VAL D 2 60  ? -9.834  12.542  21.124 1.00 17.34 ? 60  VAL D C   1
+ATOM   3721 O  O   . VAL D 2 60  ? -9.645  11.682  22.042 1.00 23.46 ? 60  VAL D O   1
+ATOM   3722 C  CB  . VAL D 2 60  ? -8.615  14.847  20.995 1.00 21.26 ? 60  VAL D CB  1
+ATOM   3723 C  CG1 . VAL D 2 60  ? -8.715  14.623  22.622 1.00 33.14 ? 60  VAL D CG1 1
+ATOM   3724 C  CG2 . VAL D 2 60  ? -7.625  15.562  20.290 1.00 22.06 ? 60  VAL D CG2 1
+ATOM   3725 N  N   . LYS D 2 61  ? -11.257 12.916  21.005 1.00 22.59 ? 61  LYS D N   1
+ATOM   3726 C  CA  . LYS D 2 61  ? -12.389 12.115  21.523 1.00 26.15 ? 61  LYS D CA  1
+ATOM   3727 C  C   . LYS D 2 61  ? -12.383 10.709  21.251 1.00 17.30 ? 61  LYS D C   1
+ATOM   3728 O  O   . LYS D 2 61  ? -12.358 9.777   22.054 1.00 21.45 ? 61  LYS D O   1
+ATOM   3729 C  CB  . LYS D 2 61  ? -13.783 12.701  21.249 1.00 26.85 ? 61  LYS D CB  1
+ATOM   3730 C  CG  . LYS D 2 61  ? -13.929 14.186  21.730 1.00 38.21 ? 61  LYS D CG  1
+ATOM   3731 C  CD  . LYS D 2 61  ? -14.977 14.603  21.141 1.00 63.66 ? 61  LYS D CD  1
+ATOM   3732 C  CE  . LYS D 2 61  ? -15.833 15.917  21.862 1.00 68.06 ? 61  LYS D CE  1
+ATOM   3733 N  NZ  . LYS D 2 61  ? -16.870 16.253  21.283 1.00 60.84 ? 61  LYS D NZ  1
+ATOM   3734 N  N   . ALA D 2 62  ? -12.043 10.369  19.968 1.00 19.16 ? 62  ALA D N   1
+ATOM   3735 C  CA  . ALA D 2 62  ? -11.956 8.912   19.500 1.00 20.58 ? 62  ALA D CA  1
+ATOM   3736 C  C   . ALA D 2 62  ? -10.898 8.037   20.192 1.00 20.27 ? 62  ALA D C   1
+ATOM   3737 O  O   . ALA D 2 62  ? -11.050 6.990   20.669 1.00 20.37 ? 62  ALA D O   1
+ATOM   3738 C  CB  . ALA D 2 62  ? -11.828 8.953   18.037 1.00 22.88 ? 62  ALA D CB  1
+ATOM   3739 N  N   . HIS D 2 63  ? -9.737  8.834   20.241 1.00 19.01 ? 63  HIS D N   1
+ATOM   3740 C  CA  . HIS D 2 63  ? -8.612  8.090   20.860 1.00 22.19 ? 63  HIS D CA  1
+ATOM   3741 C  C   . HIS D 2 63  ? -8.743  8.054   22.405 1.00 18.77 ? 63  HIS D C   1
+ATOM   3742 O  O   . HIS D 2 63  ? -8.277  6.980   22.894 1.00 19.91 ? 63  HIS D O   1
+ATOM   3743 C  CB  . HIS D 2 63  ? -7.488  8.607   20.573 1.00 33.38 ? 63  HIS D CB  1
+ATOM   3744 C  CG  . HIS D 2 63  ? -5.896  8.079   20.729 1.00 22.34 ? 63  HIS D CG  1
+ATOM   3745 N  ND1 . HIS D 2 63  ? -5.786  6.912   20.207 1.00 25.81 ? 63  HIS D ND1 1
+ATOM   3746 C  CD2 . HIS D 2 63  ? -5.209  8.477   21.930 1.00 33.81 ? 63  HIS D CD2 1
+ATOM   3747 C  CE1 . HIS D 2 63  ? -4.537  6.551   21.193 1.00 24.99 ? 63  HIS D CE1 1
+ATOM   3748 N  NE2 . HIS D 2 63  ? -4.230  7.653   21.515 1.00 32.42 ? 63  HIS D NE2 1
+ATOM   3749 N  N   . GLY D 2 64  ? -9.242  9.132   22.851 1.00 15.38 ? 64  GLY D N   1
+ATOM   3750 C  CA  . GLY D 2 64  ? -9.554  9.024   24.227 1.00 18.66 ? 64  GLY D CA  1
+ATOM   3751 C  C   . GLY D 2 64  ? -10.447 7.880   24.864 1.00 23.30 ? 64  GLY D C   1
+ATOM   3752 O  O   . GLY D 2 64  ? -10.228 7.092   25.688 1.00 21.27 ? 64  GLY D O   1
+ATOM   3753 N  N   . LYS D 2 65  ? -11.464 7.546   23.815 1.00 22.12 ? 65  LYS D N   1
+ATOM   3754 C  CA  . LYS D 2 65  ? -12.263 6.273   24.130 1.00 26.40 ? 65  LYS D CA  1
+ATOM   3755 C  C   . LYS D 2 65  ? -11.523 4.997   23.937 1.00 25.29 ? 65  LYS D C   1
+ATOM   3756 O  O   . LYS D 2 65  ? -11.789 4.125   24.765 1.00 24.58 ? 65  LYS D O   1
+ATOM   3757 C  CB  . LYS D 2 65  ? -13.404 6.447   22.983 1.00 42.10 ? 65  LYS D CB  1
+ATOM   3758 C  CG  . LYS D 2 65  ? -14.100 5.158   23.392 1.00 41.04 ? 65  LYS D CG  1
+ATOM   3759 C  CD  . LYS D 2 65  ? -15.188 5.627   21.460 1.00 41.66 ? 65  LYS D CD  1
+ATOM   3760 C  CE  . LYS D 2 65  ? -15.685 3.513   21.833 1.00 58.61 ? 65  LYS D CE  1
+ATOM   3761 N  NZ  . LYS D 2 65  ? -17.034 3.866   21.031 1.00 49.59 ? 65  LYS D NZ  1
+ATOM   3762 N  N   . LYS D 2 66  ? -10.562 4.917   22.975 1.00 22.59 ? 66  LYS D N   1
+ATOM   3763 C  CA  . LYS D 2 66  ? -9.754  3.721   22.658 1.00 23.91 ? 66  LYS D CA  1
+ATOM   3764 C  C   . LYS D 2 66  ? -9.155  3.530   24.092 1.00 25.32 ? 66  LYS D C   1
+ATOM   3765 O  O   . LYS D 2 66  ? -8.855  2.360   24.522 1.00 23.23 ? 66  LYS D O   1
+ATOM   3766 C  CB  . LYS D 2 66  ? -8.951  3.909   21.488 1.00 18.18 ? 66  LYS D CB  1
+ATOM   3767 C  CG  . LYS D 2 66  ? -8.199  3.427   20.843 1.00 49.93 ? 66  LYS D CG  1
+ATOM   3768 C  CD  . LYS D 2 66  ? -8.276  3.340   18.783 1.00 31.44 ? 66  LYS D CD  1
+ATOM   3769 C  CE  . LYS D 2 66  ? -7.754  1.136   18.911 1.00 50.83 ? 66  LYS D CE  1
+ATOM   3770 N  NZ  . LYS D 2 66  ? -6.349  0.958   17.571 1.00 53.30 ? 66  LYS D NZ  1
+ATOM   3771 N  N   . VAL D 2 67  ? -8.303  4.650   24.559 1.00 17.89 ? 67  VAL D N   1
+ATOM   3772 C  CA  . VAL D 2 67  ? -7.407  4.231   25.736 1.00 17.07 ? 67  VAL D CA  1
+ATOM   3773 C  C   . VAL D 2 67  ? -8.116  4.025   26.853 1.00 11.37 ? 67  VAL D C   1
+ATOM   3774 O  O   . VAL D 2 67  ? -7.746  3.109   27.634 1.00 18.26 ? 67  VAL D O   1
+ATOM   3775 C  CB  . VAL D 2 67  ? -6.515  5.745   25.639 1.00 18.16 ? 67  VAL D CB  1
+ATOM   3776 C  CG1 . VAL D 2 67  ? -6.137  5.772   27.197 1.00 22.61 ? 67  VAL D CG1 1
+ATOM   3777 C  CG2 . VAL D 2 67  ? -5.729  6.006   24.428 1.00 19.30 ? 67  VAL D CG2 1
+ATOM   3778 N  N   . LEU D 2 68  ? -9.240  4.638   27.165 1.00 12.24 ? 68  LEU D N   1
+ATOM   3779 C  CA  . LEU D 2 68  ? -9.850  4.367   28.407 1.00 14.83 ? 68  LEU D CA  1
+ATOM   3780 C  C   . LEU D 2 68  ? -10.660 3.010   28.456 1.00 13.25 ? 68  LEU D C   1
+ATOM   3781 O  O   . LEU D 2 68  ? -10.869 2.247   29.355 1.00 18.25 ? 68  LEU D O   1
+ATOM   3782 C  CB  . LEU D 2 68  ? -10.932 5.325   28.975 1.00 23.35 ? 68  LEU D CB  1
+ATOM   3783 C  CG  . LEU D 2 68  ? -10.864 6.001   30.117 1.00 32.52 ? 68  LEU D CG  1
+ATOM   3784 C  CD1 . LEU D 2 68  ? -9.971  5.868   30.964 1.00 40.78 ? 68  LEU D CD1 1
+ATOM   3785 C  CD2 . LEU D 2 68  ? -11.770 6.928   30.372 1.00 39.22 ? 68  LEU D CD2 1
+ATOM   3786 N  N   . GLY D 2 69  ? -11.036 2.649   27.122 1.00 22.38 ? 69  GLY D N   1
+ATOM   3787 C  CA  . GLY D 2 69  ? -11.414 1.282   26.939 1.00 27.48 ? 69  GLY D CA  1
+ATOM   3788 C  C   . GLY D 2 69  ? -10.534 0.068   27.326 1.00 17.57 ? 69  GLY D C   1
+ATOM   3789 O  O   . GLY D 2 69  ? -10.839 -0.765  28.070 1.00 21.01 ? 69  GLY D O   1
+ATOM   3790 N  N   . ALA D 2 70  ? -9.237  0.350   26.893 1.00 17.61 ? 70  ALA D N   1
+ATOM   3791 C  CA  . ALA D 2 70  ? -8.214  -0.639  27.268 1.00 17.42 ? 70  ALA D CA  1
+ATOM   3792 C  C   . ALA D 2 70  ? -7.977  -0.546  28.684 1.00 19.59 ? 70  ALA D C   1
+ATOM   3793 O  O   . ALA D 2 70  ? -7.636  -1.593  29.526 1.00 18.72 ? 70  ALA D O   1
+ATOM   3794 C  CB  . ALA D 2 70  ? -7.063  -0.292  26.421 1.00 18.83 ? 70  ALA D CB  1
+ATOM   3795 N  N   . PHE D 2 71  ? -8.028  0.658   29.208 1.00 18.97 ? 71  PHE D N   1
+ATOM   3796 C  CA  . PHE D 2 71  ? -7.876  0.928   30.811 1.00 24.55 ? 71  PHE D CA  1
+ATOM   3797 C  C   . PHE D 2 71  ? -9.029  0.141   31.539 1.00 22.73 ? 71  PHE D C   1
+ATOM   3798 O  O   . PHE D 2 71  ? -8.675  -0.580  32.378 1.00 26.00 ? 71  PHE D O   1
+ATOM   3799 C  CB  . PHE D 2 71  ? -7.797  2.431   31.037 1.00 18.78 ? 71  PHE D CB  1
+ATOM   3800 C  CG  . PHE D 2 71  ? -7.722  2.749   32.539 1.00 15.63 ? 71  PHE D CG  1
+ATOM   3801 C  CD1 . PHE D 2 71  ? -6.365  3.115   32.922 1.00 23.81 ? 71  PHE D CD1 1
+ATOM   3802 C  CD2 . PHE D 2 71  ? -9.070  2.790   33.111 1.00 34.86 ? 71  PHE D CD2 1
+ATOM   3803 C  CE1 . PHE D 2 71  ? -6.362  3.277   34.322 1.00 19.91 ? 71  PHE D CE1 1
+ATOM   3804 C  CE2 . PHE D 2 71  ? -8.645  2.966   34.544 1.00 36.36 ? 71  PHE D CE2 1
+ATOM   3805 C  CZ  . PHE D 2 71  ? -7.330  3.237   35.109 1.00 26.08 ? 71  PHE D CZ  1
+ATOM   3806 N  N   . SER D 2 72  ? -10.196 0.193   30.881 1.00 19.94 ? 72  SER D N   1
+ATOM   3807 C  CA  . SER D 2 72  ? -11.329 -0.461  31.259 1.00 23.38 ? 72  SER D CA  1
+ATOM   3808 C  C   . SER D 2 72  ? -11.054 -1.833  31.745 1.00 24.72 ? 72  SER D C   1
+ATOM   3809 O  O   . SER D 2 72  ? -11.342 -2.677  32.746 1.00 26.53 ? 72  SER D O   1
+ATOM   3810 C  CB  . SER D 2 72  ? -12.987 -0.317  31.167 1.00 29.23 ? 72  SER D CB  1
+ATOM   3811 O  OG  . SER D 2 72  ? -12.857 0.959   30.829 1.00 41.11 ? 72  SER D OG  1
+ATOM   3812 N  N   . ASP D 2 73  ? -10.722 -2.476  30.534 1.00 28.33 ? 73  ASP D N   1
+ATOM   3813 C  CA  . ASP D 2 73  ? -10.123 -3.743  30.555 1.00 41.54 ? 73  ASP D CA  1
+ATOM   3814 C  C   . ASP D 2 73  ? -9.475  -4.425  31.315 1.00 28.94 ? 73  ASP D C   1
+ATOM   3815 O  O   . ASP D 2 73  ? -9.466  -5.326  32.089 1.00 34.21 ? 73  ASP D O   1
+ATOM   3816 C  CB  . ASP D 2 73  ? -9.724  -4.601  28.955 1.00 46.96 ? 73  ASP D CB  1
+ATOM   3817 C  CG  . ASP D 2 73  ? -10.954 -4.359  28.687 1.00 54.92 ? 73  ASP D CG  1
+ATOM   3818 O  OD1 . ASP D 2 73  ? -12.180 -3.681  27.956 1.00 44.49 ? 73  ASP D OD1 1
+ATOM   3819 O  OD2 . ASP D 2 73  ? -10.386 -3.942  26.542 1.00 50.27 ? 73  ASP D OD2 1
+ATOM   3820 N  N   . GLY D 2 74  ? -8.374  -3.470  32.005 1.00 26.75 ? 74  GLY D N   1
+ATOM   3821 C  CA  . GLY D 2 74  ? -7.529  -3.845  33.010 1.00 22.69 ? 74  GLY D CA  1
+ATOM   3822 C  C   . GLY D 2 74  ? -7.920  -3.797  34.476 1.00 23.14 ? 74  GLY D C   1
+ATOM   3823 O  O   . GLY D 2 74  ? -7.528  -4.432  35.451 1.00 29.20 ? 74  GLY D O   1
+ATOM   3824 N  N   . LEU D 2 75  ? -9.130  -2.980  34.529 1.00 21.18 ? 75  LEU D N   1
+ATOM   3825 C  CA  . LEU D 2 75  ? -9.801  -3.227  35.793 1.00 34.17 ? 75  LEU D CA  1
+ATOM   3826 C  C   . LEU D 2 75  ? -10.241 -4.540  36.183 1.00 37.46 ? 75  LEU D C   1
+ATOM   3827 O  O   . LEU D 2 75  ? -10.652 -4.663  37.259 1.00 40.90 ? 75  LEU D O   1
+ATOM   3828 C  CB  . LEU D 2 75  ? -10.804 -1.867  35.854 1.00 36.63 ? 75  LEU D CB  1
+ATOM   3829 C  CG  . LEU D 2 75  ? -10.450 -0.567  36.230 1.00 28.96 ? 75  LEU D CG  1
+ATOM   3830 C  CD1 . LEU D 2 75  ? -9.127  -0.603  36.701 1.00 54.84 ? 75  LEU D CD1 1
+ATOM   3831 C  CD2 . LEU D 2 75  ? -10.796 0.541   35.801 1.00 41.72 ? 75  LEU D CD2 1
+ATOM   3832 N  N   . ALA D 2 76  ? -10.655 -5.131  35.130 1.00 36.74 ? 76  ALA D N   1
+ATOM   3833 C  CA  . ALA D 2 76  ? -11.087 -7.017  34.993 1.00 46.27 ? 76  ALA D CA  1
+ATOM   3834 C  C   . ALA D 2 76  ? -10.078 -7.313  35.204 1.00 39.68 ? 76  ALA D C   1
+ATOM   3835 O  O   . ALA D 2 76  ? -10.169 -8.663  35.825 1.00 39.55 ? 76  ALA D O   1
+ATOM   3836 C  CB  . ALA D 2 76  ? -11.633 -6.572  33.839 1.00 52.59 ? 76  ALA D CB  1
+ATOM   3837 N  N   . HIS D 2 77  ? -8.750  -7.014  35.590 1.00 34.88 ? 77  HIS D N   1
+ATOM   3838 C  CA  . HIS D 2 77  ? -7.821  -7.922  35.838 1.00 37.75 ? 77  HIS D CA  1
+ATOM   3839 C  C   . HIS D 2 77  ? -6.406  -7.315  36.454 1.00 36.30 ? 77  HIS D C   1
+ATOM   3840 O  O   . HIS D 2 77  ? -5.202  -7.364  36.420 1.00 30.91 ? 77  HIS D O   1
+ATOM   3841 C  CB  . HIS D 2 77  ? -6.809  -8.470  34.515 1.00 35.95 ? 77  HIS D CB  1
+ATOM   3842 C  CG  . HIS D 2 77  ? -7.630  -9.148  33.544 1.00 39.15 ? 77  HIS D CG  1
+ATOM   3843 N  ND1 . HIS D 2 77  ? -8.204  -8.210  32.652 1.00 58.22 ? 77  HIS D ND1 1
+ATOM   3844 C  CD2 . HIS D 2 77  ? -7.652  -10.563 33.475 1.00 48.66 ? 77  HIS D CD2 1
+ATOM   3845 C  CE1 . HIS D 2 77  ? -9.352  -9.416  31.720 1.00 49.77 ? 77  HIS D CE1 1
+ATOM   3846 N  NE2 . HIS D 2 77  ? -9.158  -10.158 32.425 1.00 36.55 ? 77  HIS D NE2 1
+ATOM   3847 N  N   . LEU D 2 78  ? -6.990  -6.739  37.768 1.00 30.38 ? 78  LEU D N   1
+ATOM   3848 C  CA  . LEU D 2 78  ? -6.267  -6.392  38.731 1.00 35.53 ? 78  LEU D CA  1
+ATOM   3849 C  C   . LEU D 2 78  ? -5.054  -6.608  39.330 1.00 31.52 ? 78  LEU D C   1
+ATOM   3850 O  O   . LEU D 2 78  ? -4.210  -6.312  39.810 1.00 30.87 ? 78  LEU D O   1
+ATOM   3851 C  CB  . LEU D 2 78  ? -7.145  -5.144  39.672 1.00 35.71 ? 78  LEU D CB  1
+ATOM   3852 C  CG  . LEU D 2 78  ? -7.268  -3.603  39.393 1.00 42.09 ? 78  LEU D CG  1
+ATOM   3853 C  CD1 . LEU D 2 78  ? -8.691  -3.415  40.303 1.00 40.33 ? 78  LEU D CD1 1
+ATOM   3854 C  CD2 . LEU D 2 78  ? -6.868  -2.931  38.988 1.00 43.79 ? 78  LEU D CD2 1
+ATOM   3855 N  N   . ASP D 2 79  ? -5.280  -8.088  39.342 1.00 27.09 ? 79  ASP D N   1
+ATOM   3856 C  CA  . ASP D 2 79  ? -4.129  -8.571  40.068 1.00 39.93 ? 79  ASP D CA  1
+ATOM   3857 C  C   . ASP D 2 79  ? -3.004  -9.514  38.971 1.00 38.31 ? 79  ASP D C   1
+ATOM   3858 O  O   . ASP D 2 79  ? -1.888  -9.798  39.229 1.00 37.24 ? 79  ASP D O   1
+ATOM   3859 C  CB  . ASP D 2 79  ? -4.915  -10.113 40.132 1.00 49.19 ? 79  ASP D CB  1
+ATOM   3860 C  CG  . ASP D 2 79  ? -6.011  -9.894  40.633 1.00 60.14 ? 79  ASP D CG  1
+ATOM   3861 O  OD1 . ASP D 2 79  ? -6.615  -11.491 41.656 1.00 58.54 ? 79  ASP D OD1 1
+ATOM   3862 O  OD2 . ASP D 2 79  ? -5.199  -9.424  42.378 1.00 49.76 ? 79  ASP D OD2 1
+ATOM   3863 N  N   . ASN D 2 80  ? -3.552  -8.871  37.829 1.00 33.30 ? 80  ASN D N   1
+ATOM   3864 C  CA  . ASN D 2 80  ? -2.127  -9.093  36.829 1.00 41.52 ? 80  ASN D CA  1
+ATOM   3865 C  C   . ASN D 2 80  ? -2.369  -8.063  35.456 1.00 29.72 ? 80  ASN D C   1
+ATOM   3866 O  O   . ASN D 2 80  ? -2.129  -8.409  34.476 1.00 26.63 ? 80  ASN D O   1
+ATOM   3867 C  CB  . ASN D 2 80  ? -2.224  -10.100 36.253 1.00 65.88 ? 80  ASN D CB  1
+ATOM   3868 C  CG  . ASN D 2 80  ? -2.322  -11.145 35.550 1.00 79.70 ? 80  ASN D CG  1
+ATOM   3869 O  OD1 . ASN D 2 80  ? -0.819  -11.569 34.989 1.00 64.12 ? 80  ASN D OD1 1
+ATOM   3870 N  ND2 . ASN D 2 80  ? -3.542  -11.010 35.462 1.00 80.04 ? 80  ASN D ND2 1
+ATOM   3871 N  N   . LEU D 2 81  ? -1.846  -6.974  36.152 1.00 24.36 ? 81  LEU D N   1
+ATOM   3872 C  CA  . LEU D 2 81  ? -1.812  -5.882  35.180 1.00 25.83 ? 81  LEU D CA  1
+ATOM   3873 C  C   . LEU D 2 81  ? -0.619  -6.084  34.147 1.00 31.94 ? 81  LEU D C   1
+ATOM   3874 O  O   . LEU D 2 81  ? -0.785  -5.796  32.956 1.00 25.17 ? 81  LEU D O   1
+ATOM   3875 C  CB  . LEU D 2 81  ? -1.618  -4.729  36.033 1.00 20.37 ? 81  LEU D CB  1
+ATOM   3876 C  CG  . LEU D 2 81  ? -2.921  -4.096  36.613 1.00 25.65 ? 81  LEU D CG  1
+ATOM   3877 C  CD1 . LEU D 2 81  ? -2.687  -3.196  37.443 1.00 40.59 ? 81  LEU D CD1 1
+ATOM   3878 C  CD2 . LEU D 2 81  ? -4.062  -3.952  35.870 1.00 23.30 ? 81  LEU D CD2 1
+ATOM   3879 N  N   . LYS D 2 82  ? 0.590   -6.479  34.724 1.00 30.20 ? 82  LYS D N   1
+ATOM   3880 C  CA  . LYS D 2 82  ? 1.630   -6.697  33.684 1.00 28.24 ? 82  LYS D CA  1
+ATOM   3881 C  C   . LYS D 2 82  ? 1.231   -7.600  32.646 1.00 33.91 ? 82  LYS D C   1
+ATOM   3882 O  O   . LYS D 2 82  ? 1.489   -7.495  31.492 1.00 25.48 ? 82  LYS D O   1
+ATOM   3883 C  CB  . LYS D 2 82  ? 2.935   -7.216  34.513 1.00 33.73 ? 82  LYS D CB  1
+ATOM   3884 C  CG  . LYS D 2 82  ? 3.615   -6.233  34.988 1.00 40.61 ? 82  LYS D CG  1
+ATOM   3885 C  CD  . LYS D 2 82  ? 5.270   -6.749  35.740 1.00 64.29 ? 82  LYS D CD  1
+ATOM   3886 C  CE  . LYS D 2 82  ? 4.871   -4.616  36.799 1.00 50.61 ? 82  LYS D CE  1
+ATOM   3887 N  NZ  . LYS D 2 82  ? 5.281   -6.232  37.797 1.00 57.77 ? 82  LYS D NZ  1
+ATOM   3888 N  N   . GLY D 2 83  ? 0.459   -8.915  32.793 1.00 30.21 ? 83  GLY D N   1
+ATOM   3889 C  CA  . GLY D 2 83  ? 0.370   -9.915  31.786 1.00 23.41 ? 83  GLY D CA  1
+ATOM   3890 C  C   . GLY D 2 83  ? -0.769  -9.467  31.084 1.00 31.79 ? 83  GLY D C   1
+ATOM   3891 O  O   . GLY D 2 83  ? -0.658  -9.293  29.599 1.00 27.38 ? 83  GLY D O   1
+ATOM   3892 N  N   . THR D 2 84  ? -1.808  -8.394  31.501 1.00 27.06 ? 84  THR D N   1
+ATOM   3893 C  CA  . THR D 2 84  ? -2.762  -7.938  30.700 1.00 31.17 ? 84  THR D CA  1
+ATOM   3894 C  C   . THR D 2 84  ? -2.036  -7.040  29.476 1.00 35.08 ? 84  THR D C   1
+ATOM   3895 O  O   . THR D 2 84  ? -2.823  -6.787  28.636 1.00 26.93 ? 84  THR D O   1
+ATOM   3896 C  CB  . THR D 2 84  ? -3.896  -7.137  31.498 1.00 26.68 ? 84  THR D CB  1
+ATOM   3897 O  OG1 . THR D 2 84  ? -4.265  -8.031  32.250 1.00 41.82 ? 84  THR D OG1 1
+ATOM   3898 C  CG2 . THR D 2 84  ? -5.082  -6.415  30.894 1.00 32.36 ? 84  THR D CG2 1
+ATOM   3899 N  N   . PHE D 2 85  ? -1.296  -6.110  30.189 1.00 23.78 ? 85  PHE D N   1
+ATOM   3900 C  CA  . PHE D 2 85  ? -0.960  -4.804  29.274 1.00 17.94 ? 85  PHE D CA  1
+ATOM   3901 C  C   . PHE D 2 85  ? 0.347   -5.217  28.453 1.00 20.32 ? 85  PHE D C   1
+ATOM   3902 O  O   . PHE D 2 85  ? 1.061   -4.377  27.758 1.00 18.46 ? 85  PHE D O   1
+ATOM   3903 C  CB  . PHE D 2 85  ? -0.615  -3.687  30.151 1.00 16.82 ? 85  PHE D CB  1
+ATOM   3904 C  CG  . PHE D 2 85  ? -1.992  -3.104  30.340 1.00 15.41 ? 85  PHE D CG  1
+ATOM   3905 C  CD1 . PHE D 2 85  ? -2.473  -3.199  31.723 1.00 21.43 ? 85  PHE D CD1 1
+ATOM   3906 C  CD2 . PHE D 2 85  ? -2.650  -2.338  29.446 1.00 29.52 ? 85  PHE D CD2 1
+ATOM   3907 C  CE1 . PHE D 2 85  ? -3.772  -2.604  32.121 1.00 27.35 ? 85  PHE D CE1 1
+ATOM   3908 C  CE2 . PHE D 2 85  ? -4.035  -1.925  29.866 1.00 23.38 ? 85  PHE D CE2 1
+ATOM   3909 C  CZ  . PHE D 2 85  ? -4.715  -2.007  31.138 1.00 20.96 ? 85  PHE D CZ  1
+ATOM   3910 N  N   . ALA D 2 86  ? 1.005   -6.402  28.558 1.00 16.78 ? 86  ALA D N   1
+ATOM   3911 C  CA  . ALA D 2 86  ? 2.480   -6.623  27.990 1.00 21.66 ? 86  ALA D CA  1
+ATOM   3912 C  C   . ALA D 2 86  ? 2.353   -6.370  26.367 1.00 13.70 ? 86  ALA D C   1
+ATOM   3913 O  O   . ALA D 2 86  ? 3.329   -5.701  25.891 1.00 16.83 ? 86  ALA D O   1
+ATOM   3914 C  CB  . ALA D 2 86  ? 2.727   -8.280  27.947 1.00 23.60 ? 86  ALA D CB  1
+ATOM   3915 N  N   . THR D 2 87  ? 1.304   -6.754  25.769 1.00 17.09 ? 87  THR D N   1
+ATOM   3916 C  CA  . THR D 2 87  ? 1.374   -6.426  24.324 1.00 15.85 ? 87  THR D CA  1
+ATOM   3917 C  C   . THR D 2 87  ? 1.385   -4.890  23.958 1.00 17.61 ? 87  THR D C   1
+ATOM   3918 O  O   . THR D 2 87  ? 2.108   -4.435  23.135 1.00 21.97 ? 87  THR D O   1
+ATOM   3919 C  CB  . THR D 2 87  ? 0.107   -7.089  23.607 1.00 23.34 ? 87  THR D CB  1
+ATOM   3920 O  OG1 . THR D 2 87  ? 0.209   -8.494  23.879 1.00 26.37 ? 87  THR D OG1 1
+ATOM   3921 C  CG2 . THR D 2 87  ? 0.248   -7.031  22.206 1.00 26.08 ? 87  THR D CG2 1
+ATOM   3922 N  N   . LEU D 2 88  ? 0.437   -4.264  24.552 1.00 19.60 ? 88  LEU D N   1
+ATOM   3923 C  CA  . LEU D 2 88  ? 0.354   -2.894  24.389 1.00 18.18 ? 88  LEU D CA  1
+ATOM   3924 C  C   . LEU D 2 88  ? 1.618   -2.083  24.969 1.00 15.66 ? 88  LEU D C   1
+ATOM   3925 O  O   . LEU D 2 88  ? 2.101   -1.046  24.363 1.00 16.54 ? 88  LEU D O   1
+ATOM   3926 C  CB  . LEU D 2 88  ? -0.877  -2.229  25.116 1.00 24.93 ? 88  LEU D CB  1
+ATOM   3927 C  CG  . LEU D 2 88  ? -2.151  -2.463  24.340 1.00 29.68 ? 88  LEU D CG  1
+ATOM   3928 C  CD1 . LEU D 2 88  ? -3.166  -2.157  25.370 1.00 33.11 ? 88  LEU D CD1 1
+ATOM   3929 C  CD2 . LEU D 2 88  ? -2.112  -1.945  23.113 1.00 21.96 ? 88  LEU D CD2 1
+ATOM   3930 N  N   . SER D 2 89  ? 2.220   -2.755  26.095 1.00 21.20 ? 89  SER D N   1
+ATOM   3931 C  CA  . SER D 2 89  ? 3.512   -2.255  26.594 1.00 17.78 ? 89  SER D CA  1
+ATOM   3932 C  C   . SER D 2 89  ? 4.586   -2.042  25.459 1.00 16.70 ? 89  SER D C   1
+ATOM   3933 O  O   . SER D 2 89  ? 5.389   -1.176  25.059 1.00 15.86 ? 89  SER D O   1
+ATOM   3934 C  CB  . SER D 2 89  ? 4.125   -2.988  27.687 1.00 19.29 ? 89  SER D CB  1
+ATOM   3935 O  OG  . SER D 2 89  ? 5.262   -2.362  28.200 1.00 14.95 ? 89  SER D OG  1
+ATOM   3936 N  N   . GLU D 2 90  ? 4.840   -3.312  24.808 1.00 15.58 ? 90  GLU D N   1
+ATOM   3937 C  CA  . GLU D 2 90  ? 5.608   -3.427  23.575 1.00 21.65 ? 90  GLU D CA  1
+ATOM   3938 C  C   . GLU D 2 90  ? 5.326   -2.506  22.383 1.00 13.57 ? 90  GLU D C   1
+ATOM   3939 O  O   . GLU D 2 90  ? 6.140   -1.944  21.856 1.00 18.38 ? 90  GLU D O   1
+ATOM   3940 C  CB  . GLU D 2 90  ? 5.605   -5.012  23.350 1.00 19.08 ? 90  GLU D CB  1
+ATOM   3941 C  CG  . GLU D 2 90  ? 6.857   -5.032  22.503 1.00 38.09 ? 90  GLU D CG  1
+ATOM   3942 C  CD  . GLU D 2 90  ? 6.802   -7.459  22.518 1.00 62.85 ? 90  GLU D CD  1
+ATOM   3943 O  OE1 . GLU D 2 90  ? 6.360   -7.013  21.004 1.00 54.38 ? 90  GLU D OE1 1
+ATOM   3944 O  OE2 . GLU D 2 90  ? 5.716   -7.581  23.171 1.00 49.69 ? 90  GLU D OE2 1
+ATOM   3945 N  N   . LEU D 2 91  ? 4.012   -2.449  22.221 1.00 12.64 ? 91  LEU D N   1
+ATOM   3946 C  CA  . LEU D 2 91  ? 3.798   -1.514  21.234 1.00 11.29 ? 91  LEU D CA  1
+ATOM   3947 C  C   . LEU D 2 91  ? 4.193   -0.028  21.310 1.00 14.82 ? 91  LEU D C   1
+ATOM   3948 O  O   . LEU D 2 91  ? 4.567   0.805   20.478 1.00 14.36 ? 91  LEU D O   1
+ATOM   3949 C  CB  . LEU D 2 91  ? 2.220   -1.626  21.025 1.00 13.30 ? 91  LEU D CB  1
+ATOM   3950 C  CG  . LEU D 2 91  ? 1.438   -0.601  20.105 1.00 17.13 ? 91  LEU D CG  1
+ATOM   3951 C  CD1 . LEU D 2 91  ? 1.945   -0.805  18.489 1.00 25.95 ? 91  LEU D CD1 1
+ATOM   3952 C  CD2 . LEU D 2 91  ? 0.005   -0.521  20.139 1.00 20.87 ? 91  LEU D CD2 1
+ATOM   3953 N  N   . HIS D 2 92  ? 3.827   0.419   22.684 1.00 14.55 ? 92  HIS D N   1
+ATOM   3954 C  CA  . HIS D 2 92  ? 3.932   1.978   22.792 1.00 18.41 ? 92  HIS D CA  1
+ATOM   3955 C  C   . HIS D 2 92  ? 5.663   2.049   23.081 1.00 25.22 ? 92  HIS D C   1
+ATOM   3956 O  O   . HIS D 2 92  ? 6.024   3.142   22.630 1.00 15.09 ? 92  HIS D O   1
+ATOM   3957 C  CB  . HIS D 2 92  ? 3.581   2.071   24.217 1.00 16.94 ? 92  HIS D CB  1
+ATOM   3958 C  CG  . HIS D 2 92  ? 2.067   2.591   24.193 1.00 14.87 ? 92  HIS D CG  1
+ATOM   3959 N  ND1 . HIS D 2 92  ? 1.075   1.405   24.078 1.00 14.65 ? 92  HIS D ND1 1
+ATOM   3960 C  CD2 . HIS D 2 92  ? 1.163   3.595   24.191 1.00 12.93 ? 92  HIS D CD2 1
+ATOM   3961 C  CE1 . HIS D 2 92  ? -0.103  2.199   24.076 1.00 12.97 ? 92  HIS D CE1 1
+ATOM   3962 N  NE2 . HIS D 2 92  ? -0.200  3.438   23.869 1.00 18.10 ? 92  HIS D NE2 1
+ATOM   3963 N  N   . CYS D 2 93  ? 6.415   0.987   23.308 1.00 16.12 ? 93  CYS D N   1
+ATOM   3964 C  CA  . CYS D 2 93  ? 7.983   1.187   23.132 1.00 16.35 ? 93  CYS D CA  1
+ATOM   3965 C  C   . CYS D 2 93  ? 8.423   1.240   21.584 1.00 18.55 ? 93  CYS D C   1
+ATOM   3966 O  O   . CYS D 2 93  ? 8.983   2.089   21.306 1.00 17.22 ? 93  CYS D O   1
+ATOM   3967 C  CB  . CYS D 2 93  ? 8.388   0.156   24.148 1.00 20.93 ? 93  CYS D CB  1
+ATOM   3968 S  SG  . CYS D 2 93  ? 10.370  0.363   23.998 1.00 18.90 ? 93  CYS D SG  1
+ATOM   3969 N  N   . ASP D 2 94  ? 8.081   -0.020  21.158 1.00 14.32 ? 94  ASP D N   1
+ATOM   3970 C  CA  . ASP D 2 94  ? 8.975   -0.311  19.769 1.00 16.01 ? 94  ASP D CA  1
+ATOM   3971 C  C   . ASP D 2 94  ? 8.295   0.417   18.704 1.00 19.68 ? 94  ASP D C   1
+ATOM   3972 O  O   . ASP D 2 94  ? 8.925   0.686   17.786 1.00 27.14 ? 94  ASP D O   1
+ATOM   3973 C  CB  . ASP D 2 94  ? 8.822   -1.803  19.762 1.00 20.44 ? 94  ASP D CB  1
+ATOM   3974 C  CG  . ASP D 2 94  ? 9.795   -2.754  20.702 1.00 36.43 ? 94  ASP D CG  1
+ATOM   3975 O  OD1 . ASP D 2 94  ? 10.260  -1.959  21.229 1.00 32.86 ? 94  ASP D OD1 1
+ATOM   3976 O  OD2 . ASP D 2 94  ? 9.080   -4.101  20.613 1.00 40.09 ? 94  ASP D OD2 1
+ATOM   3977 N  N   . LYS D 2 95  ? 7.025   0.561   18.645 1.00 14.90 ? 95  LYS D N   1
+ATOM   3978 C  CA  . LYS D 2 95  ? 6.317   1.245   17.392 1.00 16.76 ? 95  LYS D CA  1
+ATOM   3979 C  C   . LYS D 2 95  ? 6.157   2.593   17.543 1.00 18.82 ? 95  LYS D C   1
+ATOM   3980 O  O   . LYS D 2 95  ? 6.290   3.558   16.934 1.00 19.72 ? 95  LYS D O   1
+ATOM   3981 C  CB  . LYS D 2 95  ? 5.075   0.497   16.984 1.00 24.57 ? 95  LYS D CB  1
+ATOM   3982 C  CG  . LYS D 2 95  ? 5.162   -1.074  17.007 1.00 49.61 ? 95  LYS D CG  1
+ATOM   3983 C  CD  . LYS D 2 95  ? 6.536   -1.005  15.336 1.00 60.17 ? 95  LYS D CD  1
+ATOM   3984 C  CE  . LYS D 2 95  ? 7.182   -2.058  14.661 1.00 57.82 ? 95  LYS D CE  1
+ATOM   3985 N  NZ  . LYS D 2 95  ? 8.312   -1.306  13.212 1.00 59.53 ? 95  LYS D NZ  1
+ATOM   3986 N  N   . LEU D 2 96  ? 5.519   3.025   18.987 1.00 16.80 ? 96  LEU D N   1
+ATOM   3987 C  CA  . LEU D 2 96  ? 5.064   4.383   19.141 1.00 16.58 ? 96  LEU D CA  1
+ATOM   3988 C  C   . LEU D 2 96  ? 6.202   5.373   19.714 1.00 16.01 ? 96  LEU D C   1
+ATOM   3989 O  O   . LEU D 2 96  ? 5.914   6.557   19.632 1.00 15.73 ? 96  LEU D O   1
+ATOM   3990 C  CB  . LEU D 2 96  ? 3.752   4.302   19.915 1.00 21.01 ? 96  LEU D CB  1
+ATOM   3991 C  CG  . LEU D 2 96  ? 2.587   3.450   19.446 1.00 22.06 ? 96  LEU D CG  1
+ATOM   3992 C  CD1 . LEU D 2 96  ? 1.378   3.398   20.435 1.00 15.50 ? 96  LEU D CD1 1
+ATOM   3993 C  CD2 . LEU D 2 96  ? 2.243   3.991   18.155 1.00 34.04 ? 96  LEU D CD2 1
+ATOM   3994 N  N   . HIS D 2 97  ? 6.931   4.741   20.483 1.00 18.03 ? 97  HIS D N   1
+ATOM   3995 C  CA  . HIS D 2 97  ? 8.131   5.556   20.972 1.00 18.48 ? 97  HIS D CA  1
+ATOM   3996 C  C   . HIS D 2 97  ? 7.673   6.584   22.064 1.00 13.60 ? 97  HIS D C   1
+ATOM   3997 O  O   . HIS D 2 97  ? 8.046   7.731   22.173 1.00 15.07 ? 97  HIS D O   1
+ATOM   3998 C  CB  . HIS D 2 97  ? 8.960   6.339   20.025 1.00 24.24 ? 97  HIS D CB  1
+ATOM   3999 C  CG  . HIS D 2 97  ? 9.533   5.386   18.800 1.00 28.24 ? 97  HIS D CG  1
+ATOM   4000 N  ND1 . HIS D 2 97  ? 10.160  4.260   19.120 1.00 26.25 ? 97  HIS D ND1 1
+ATOM   4001 C  CD2 . HIS D 2 97  ? 8.970   5.509   17.568 1.00 35.10 ? 97  HIS D CD2 1
+ATOM   4002 C  CE1 . HIS D 2 97  ? 10.560  3.540   17.825 1.00 25.85 ? 97  HIS D CE1 1
+ATOM   4003 N  NE2 . HIS D 2 97  ? 9.833   4.359   17.187 1.00 28.28 ? 97  HIS D NE2 1
+ATOM   4004 N  N   . VAL D 2 98  ? 6.602   6.070   22.926 1.00 15.21 ? 98  VAL D N   1
+ATOM   4005 C  CA  . VAL D 2 98  ? 6.040   7.007   23.861 1.00 14.55 ? 98  VAL D CA  1
+ATOM   4006 C  C   . VAL D 2 98  ? 6.846   6.965   25.268 1.00 10.52 ? 98  VAL D C   1
+ATOM   4007 O  O   . VAL D 2 98  ? 6.819   5.840   25.822 1.00 11.77 ? 98  VAL D O   1
+ATOM   4008 C  CB  . VAL D 2 98  ? 4.634   6.576   24.231 1.00 15.30 ? 98  VAL D CB  1
+ATOM   4009 C  CG1 . VAL D 2 98  ? 4.019   7.324   25.397 1.00 15.30 ? 98  VAL D CG1 1
+ATOM   4010 C  CG2 . VAL D 2 98  ? 3.854   6.885   22.786 1.00 17.14 ? 98  VAL D CG2 1
+ATOM   4011 N  N   . ASP D 2 99  ? 7.374   8.054   25.728 1.00 9.86  ? 99  ASP D N   1
+ATOM   4012 C  CA  . ASP D 2 99  ? 8.017   8.047   27.111 1.00 10.99 ? 99  ASP D CA  1
+ATOM   4013 C  C   . ASP D 2 99  ? 6.941   7.592   28.066 1.00 12.34 ? 99  ASP D C   1
+ATOM   4014 O  O   . ASP D 2 99  ? 5.858   8.316   28.095 1.00 15.90 ? 99  ASP D O   1
+ATOM   4015 C  CB  . ASP D 2 99  ? 8.445   9.450   27.274 1.00 12.59 ? 99  ASP D CB  1
+ATOM   4016 C  CG  . ASP D 2 99  ? 9.240   9.779   28.695 1.00 12.64 ? 99  ASP D CG  1
+ATOM   4017 O  OD1 . ASP D 2 99  ? 9.727   10.961  28.581 1.00 11.35 ? 99  ASP D OD1 1
+ATOM   4018 O  OD2 . ASP D 2 99  ? 9.309   8.741   29.442 1.00 14.04 ? 99  ASP D OD2 1
+ATOM   4019 N  N   . PRO D 2 100 ? 7.197   6.649   28.819 1.00 16.57 ? 100 PRO D N   1
+ATOM   4020 C  CA  . PRO D 2 100 ? 6.390   6.162   29.965 1.00 11.14 ? 100 PRO D CA  1
+ATOM   4021 C  C   . PRO D 2 100 ? 5.929   7.307   30.950 1.00 11.03 ? 100 PRO D C   1
+ATOM   4022 O  O   . PRO D 2 100 ? 4.931   6.949   31.593 1.00 12.40 ? 100 PRO D O   1
+ATOM   4023 C  CB  . PRO D 2 100 ? 6.808   4.728   30.312 1.00 18.57 ? 100 PRO D CB  1
+ATOM   4024 C  CG  . PRO D 2 100 ? 8.135   4.655   30.034 1.00 16.52 ? 100 PRO D CG  1
+ATOM   4025 C  CD  . PRO D 2 100 ? 8.383   5.796   28.883 1.00 15.61 ? 100 PRO D CD  1
+ATOM   4026 N  N   . GLU D 2 101 ? 6.759   8.347   31.047 1.00 9.29  ? 101 GLU D N   1
+ATOM   4027 C  CA  . GLU D 2 101 ? 6.358   9.341   31.896 1.00 12.45 ? 101 GLU D CA  1
+ATOM   4028 C  C   . GLU D 2 101 ? 4.988   9.950   31.582 1.00 20.07 ? 101 GLU D C   1
+ATOM   4029 O  O   . GLU D 2 101 ? 4.092   10.300  32.471 1.00 15.47 ? 101 GLU D O   1
+ATOM   4030 C  CB  . GLU D 2 101 ? 7.368   10.418  31.921 1.00 18.48 ? 101 GLU D CB  1
+ATOM   4031 C  CG  . GLU D 2 101 ? 6.763   11.681  32.917 1.00 30.49 ? 101 GLU D CG  1
+ATOM   4032 C  CD  . GLU D 2 101 ? 6.620   11.195  34.919 1.00 32.99 ? 101 GLU D CD  1
+ATOM   4033 O  OE1 . GLU D 2 101 ? 7.608   10.361  34.777 1.00 22.72 ? 101 GLU D OE1 1
+ATOM   4034 O  OE2 . GLU D 2 101 ? 5.955   12.483  34.947 1.00 37.16 ? 101 GLU D OE2 1
+ATOM   4035 N  N   . ASN D 2 102 ? 4.618   9.786   30.286 1.00 14.86 ? 102 ASN D N   1
+ATOM   4036 C  CA  . ASN D 2 102 ? 3.233   10.269  29.742 1.00 14.38 ? 102 ASN D CA  1
+ATOM   4037 C  C   . ASN D 2 102 ? 2.197   9.315   30.341 1.00 12.83 ? 102 ASN D C   1
+ATOM   4038 O  O   . ASN D 2 102 ? 0.958   9.949   30.702 1.00 15.98 ? 102 ASN D O   1
+ATOM   4039 C  CB  . ASN D 2 102 ? 3.112   9.986   28.384 1.00 15.85 ? 102 ASN D CB  1
+ATOM   4040 C  CG  . ASN D 2 102 ? 3.914   11.127  27.705 1.00 20.86 ? 102 ASN D CG  1
+ATOM   4041 O  OD1 . ASN D 2 102 ? 3.663   12.211  27.655 1.00 17.49 ? 102 ASN D OD1 1
+ATOM   4042 N  ND2 . ASN D 2 102 ? 5.097   10.681  26.981 1.00 22.52 ? 102 ASN D ND2 1
+ATOM   4043 N  N   . PHE D 2 103 ? 2.310   8.117   30.720 1.00 11.06 ? 103 PHE D N   1
+ATOM   4044 C  CA  . PHE D 2 103 ? 1.405   7.138   31.360 1.00 11.10 ? 103 PHE D CA  1
+ATOM   4045 C  C   . PHE D 2 103 ? 0.967   7.783   32.803 1.00 14.83 ? 103 PHE D C   1
+ATOM   4046 O  O   . PHE D 2 103 ? -0.235  7.710   33.279 1.00 12.07 ? 103 PHE D O   1
+ATOM   4047 C  CB  . PHE D 2 103 ? 1.786   5.762   31.588 1.00 14.26 ? 103 PHE D CB  1
+ATOM   4048 C  CG  . PHE D 2 103 ? 2.292   5.238   30.156 1.00 14.43 ? 103 PHE D CG  1
+ATOM   4049 C  CD1 . PHE D 2 103 ? 1.508   5.493   28.917 1.00 22.91 ? 103 PHE D CD1 1
+ATOM   4050 C  CD2 . PHE D 2 103 ? 3.361   4.323   30.119 1.00 19.84 ? 103 PHE D CD2 1
+ATOM   4051 C  CE1 . PHE D 2 103 ? 1.796   4.959   27.707 1.00 22.48 ? 103 PHE D CE1 1
+ATOM   4052 C  CE2 . PHE D 2 103 ? 3.641   3.823   28.853 1.00 13.44 ? 103 PHE D CE2 1
+ATOM   4053 C  CZ  . PHE D 2 103 ? 2.976   4.144   27.632 1.00 16.91 ? 103 PHE D CZ  1
+ATOM   4054 N  N   . ARG D 2 104 ? 1.961   8.290   33.521 1.00 14.96 ? 104 ARG D N   1
+ATOM   4055 C  CA  . ARG D 2 104 ? 1.865   8.837   34.858 1.00 18.64 ? 104 ARG D CA  1
+ATOM   4056 C  C   . ARG D 2 104 ? 0.947   10.193  34.773 1.00 17.76 ? 104 ARG D C   1
+ATOM   4057 O  O   . ARG D 2 104 ? 0.109   10.357  35.602 1.00 14.29 ? 104 ARG D O   1
+ATOM   4058 C  CB  . ARG D 2 104 ? 3.284   9.125   35.588 1.00 19.67 ? 104 ARG D CB  1
+ATOM   4059 C  CG  . ARG D 2 104 ? 3.835   7.869   35.695 1.00 39.66 ? 104 ARG D CG  1
+ATOM   4060 C  CD  . ARG D 2 104 ? 5.416   8.009   36.307 1.00 67.99 ? 104 ARG D CD  1
+ATOM   4061 N  NE  . ARG D 2 104 ? 5.531   6.176   36.368 1.00 67.11 ? 104 ARG D NE  1
+ATOM   4062 C  CZ  . ARG D 2 104 ? 8.083   6.504   36.494 1.00 80.12 ? 104 ARG D CZ  1
+ATOM   4063 N  NH1 . ARG D 2 104 ? 7.919   7.975   36.556 1.00 77.56 ? 104 ARG D NH1 1
+ATOM   4064 N  NH2 . ARG D 2 104 ? 7.837   5.849   37.495 1.00 80.12 ? 104 ARG D NH2 1
+ATOM   4065 N  N   . LEU D 2 105 ? 1.360   11.002  33.800 1.00 14.78 ? 105 LEU D N   1
+ATOM   4066 C  CA  . LEU D 2 105 ? 0.620   12.231  33.611 1.00 11.66 ? 105 LEU D CA  1
+ATOM   4067 C  C   . LEU D 2 105 ? -0.887  11.997  33.347 1.00 13.52 ? 105 LEU D C   1
+ATOM   4068 O  O   . LEU D 2 105 ? -1.739  12.524  33.970 1.00 12.56 ? 105 LEU D O   1
+ATOM   4069 C  CB  . LEU D 2 105 ? 1.239   12.973  32.633 1.00 16.32 ? 105 LEU D CB  1
+ATOM   4070 C  CG  . LEU D 2 105 ? 2.607   13.707  32.652 1.00 23.61 ? 105 LEU D CG  1
+ATOM   4071 C  CD1 . LEU D 2 105 ? 3.261   14.404  31.634 1.00 25.65 ? 105 LEU D CD1 1
+ATOM   4072 C  CD2 . LEU D 2 105 ? 2.767   14.342  34.016 1.00 30.28 ? 105 LEU D CD2 1
+ATOM   4073 N  N   . LEU D 2 106 ? -1.118  11.020  32.462 1.00 11.11 ? 106 LEU D N   1
+ATOM   4074 C  CA  . LEU D 2 106 ? -2.582  10.775  32.168 1.00 10.81 ? 106 LEU D CA  1
+ATOM   4075 C  C   . LEU D 2 106 ? -3.263  10.235  33.305 1.00 7.04  ? 106 LEU D C   1
+ATOM   4076 O  O   . LEU D 2 106 ? -4.393  10.488  33.592 1.00 8.65  ? 106 LEU D O   1
+ATOM   4077 C  CB  . LEU D 2 106 ? -2.608  9.691   31.030 1.00 12.84 ? 106 LEU D CB  1
+ATOM   4078 C  CG  . LEU D 2 106 ? -4.041  9.411   30.587 1.00 16.25 ? 106 LEU D CG  1
+ATOM   4079 C  CD1 . LEU D 2 106 ? -4.842  10.589  30.057 1.00 16.77 ? 106 LEU D CD1 1
+ATOM   4080 C  CD2 . LEU D 2 106 ? -3.870  8.327   29.677 1.00 20.04 ? 106 LEU D CD2 1
+ATOM   4081 N  N   . GLY D 2 107 ? -2.646  9.424   34.129 1.00 12.52 ? 107 GLY D N   1
+ATOM   4082 C  CA  . GLY D 2 107 ? -3.130  8.774   35.385 1.00 16.15 ? 107 GLY D CA  1
+ATOM   4083 C  C   . GLY D 2 107 ? -3.626  9.896   36.319 1.00 14.99 ? 107 GLY D C   1
+ATOM   4084 O  O   . GLY D 2 107 ? -4.724  9.915   36.857 1.00 12.81 ? 107 GLY D O   1
+ATOM   4085 N  N   . ASN D 2 108 ? -2.826  10.941  36.456 1.00 12.36 ? 108 ASN D N   1
+ATOM   4086 C  CA  . ASN D 2 108 ? -3.129  12.025  37.287 1.00 14.00 ? 108 ASN D CA  1
+ATOM   4087 C  C   . ASN D 2 108 ? -4.189  12.926  36.808 1.00 11.43 ? 108 ASN D C   1
+ATOM   4088 O  O   . ASN D 2 108 ? -5.183  13.371  37.559 1.00 12.39 ? 108 ASN D O   1
+ATOM   4089 C  CB  . ASN D 2 108 ? -1.985  12.940  37.703 1.00 18.57 ? 108 ASN D CB  1
+ATOM   4090 C  CG  . ASN D 2 108 ? -0.830  12.006  38.769 1.00 22.26 ? 108 ASN D CG  1
+ATOM   4091 O  OD1 . ASN D 2 108 ? -1.510  11.169  39.567 1.00 22.78 ? 108 ASN D OD1 1
+ATOM   4092 N  ND2 . ASN D 2 108 ? 0.079   12.830  38.784 1.00 30.03 ? 108 ASN D ND2 1
+ATOM   4093 N  N   . VAL D 2 109 ? -4.189  13.146  35.496 1.00 10.09 ? 109 VAL D N   1
+ATOM   4094 C  CA  . VAL D 2 109 ? -5.275  13.805  34.867 1.00 8.21  ? 109 VAL D CA  1
+ATOM   4095 C  C   . VAL D 2 109 ? -6.576  13.066  34.950 1.00 9.89  ? 109 VAL D C   1
+ATOM   4096 O  O   . VAL D 2 109 ? -7.565  13.726  35.341 1.00 11.76 ? 109 VAL D O   1
+ATOM   4097 C  CB  . VAL D 2 109 ? -4.899  14.110  33.347 1.00 11.59 ? 109 VAL D CB  1
+ATOM   4098 C  CG1 . VAL D 2 109 ? -6.067  14.732  32.546 1.00 17.96 ? 109 VAL D CG1 1
+ATOM   4099 C  CG2 . VAL D 2 109 ? -3.838  15.133  33.305 1.00 17.98 ? 109 VAL D CG2 1
+ATOM   4100 N  N   . LEU D 2 110 ? -6.519  11.717  34.753 1.00 9.62  ? 110 LEU D N   1
+ATOM   4101 C  CA  . LEU D 2 110 ? -7.723  10.930  34.936 1.00 14.08 ? 110 LEU D CA  1
+ATOM   4102 C  C   . LEU D 2 110 ? -8.429  11.182  36.200 1.00 11.97 ? 110 LEU D C   1
+ATOM   4103 O  O   . LEU D 2 110 ? -9.601  11.176  36.600 1.00 10.97 ? 110 LEU D O   1
+ATOM   4104 C  CB  . LEU D 2 110 ? -7.525  9.600   34.628 1.00 15.34 ? 110 LEU D CB  1
+ATOM   4105 C  CG  . LEU D 2 110 ? -8.566  8.610   34.791 1.00 14.97 ? 110 LEU D CG  1
+ATOM   4106 C  CD1 . LEU D 2 110 ? -9.772  8.905   34.016 1.00 23.21 ? 110 LEU D CD1 1
+ATOM   4107 C  CD2 . LEU D 2 110 ? -8.195  7.133   34.513 1.00 26.92 ? 110 LEU D CD2 1
+ATOM   4108 N  N   . VAL D 2 111 ? -7.453  11.161  37.373 1.00 14.50 ? 111 VAL D N   1
+ATOM   4109 C  CA  . VAL D 2 111 ? -7.968  11.386  38.826 1.00 11.82 ? 111 VAL D CA  1
+ATOM   4110 C  C   . VAL D 2 111 ? -8.704  12.696  38.914 1.00 14.01 ? 111 VAL D C   1
+ATOM   4111 O  O   . VAL D 2 111 ? -9.727  12.813  39.573 1.00 12.03 ? 111 VAL D O   1
+ATOM   4112 C  CB  . VAL D 2 111 ? -6.846  11.131  39.833 1.00 12.62 ? 111 VAL D CB  1
+ATOM   4113 C  CG1 . VAL D 2 111 ? -7.336  11.624  41.181 1.00 15.85 ? 111 VAL D CG1 1
+ATOM   4114 C  CG2 . VAL D 2 111 ? -6.459  9.608   39.848 1.00 10.77 ? 111 VAL D CG2 1
+ATOM   4115 N  N   . CYS D 2 112 ? -8.018  13.784  38.237 1.00 13.62 ? 112 CYS D N   1
+ATOM   4116 C  CA  . CYS D 2 112 ? -8.548  15.049  38.171 1.00 13.72 ? 112 CYS D CA  1
+ATOM   4117 C  C   . CYS D 2 112 ? -10.151 15.142  37.752 1.00 20.10 ? 112 CYS D C   1
+ATOM   4118 O  O   . CYS D 2 112 ? -11.002 15.713  38.180 1.00 16.56 ? 112 CYS D O   1
+ATOM   4119 C  CB  . CYS D 2 112 ? -7.812  16.104  37.464 1.00 12.95 ? 112 CYS D CB  1
+ATOM   4120 S  SG  . CYS D 2 112 ? -6.469  16.588  38.540 1.00 15.21 ? 112 CYS D SG  1
+ATOM   4121 N  N   . VAL D 2 113 ? -10.189 14.319  36.647 1.00 17.02 ? 113 VAL D N   1
+ATOM   4122 C  CA  . VAL D 2 113 ? -11.413 14.208  35.765 1.00 12.28 ? 113 VAL D CA  1
+ATOM   4123 C  C   . VAL D 2 113 ? -12.489 13.489  36.497 1.00 12.56 ? 113 VAL D C   1
+ATOM   4124 O  O   . VAL D 2 113 ? -13.603 13.930  36.649 1.00 15.84 ? 113 VAL D O   1
+ATOM   4125 C  CB  . VAL D 2 113 ? -11.188 13.503  34.421 1.00 17.85 ? 113 VAL D CB  1
+ATOM   4126 C  CG1 . VAL D 2 113 ? -12.477 13.210  33.789 1.00 18.74 ? 113 VAL D CG1 1
+ATOM   4127 C  CG2 . VAL D 2 113 ? -10.361 14.622  33.373 1.00 21.41 ? 113 VAL D CG2 1
+ATOM   4128 N  N   . LEU D 2 114 ? -12.194 12.429  37.236 1.00 10.75 ? 114 LEU D N   1
+ATOM   4129 C  CA  . LEU D 2 114 ? -13.092 11.662  38.114 1.00 10.78 ? 114 LEU D CA  1
+ATOM   4130 C  C   . LEU D 2 114 ? -13.614 12.616  39.150 1.00 19.00 ? 114 LEU D C   1
+ATOM   4131 O  O   . LEU D 2 114 ? -14.717 12.695  39.481 1.00 11.46 ? 114 LEU D O   1
+ATOM   4132 C  CB  . LEU D 2 114 ? -12.451 10.458  38.582 1.00 14.56 ? 114 LEU D CB  1
+ATOM   4133 C  CG  . LEU D 2 114 ? -12.033 9.460   37.500 1.00 17.11 ? 114 LEU D CG  1
+ATOM   4134 C  CD1 . LEU D 2 114 ? -11.371 8.208   38.149 1.00 17.06 ? 114 LEU D CD1 1
+ATOM   4135 C  CD2 . LEU D 2 114 ? -13.472 8.879   36.865 1.00 20.86 ? 114 LEU D CD2 1
+ATOM   4136 N  N   . ALA D 2 115 ? -12.696 13.271  39.814 1.00 11.71 ? 115 ALA D N   1
+ATOM   4137 C  CA  . ALA D 2 115 ? -13.081 14.289  40.929 1.00 11.69 ? 115 ALA D CA  1
+ATOM   4138 C  C   . ALA D 2 115 ? -14.070 15.337  40.366 1.00 15.12 ? 115 ALA D C   1
+ATOM   4139 O  O   . ALA D 2 115 ? -14.897 15.647  41.054 1.00 15.47 ? 115 ALA D O   1
+ATOM   4140 C  CB  . ALA D 2 115 ? -11.758 14.944  41.582 1.00 12.28 ? 115 ALA D CB  1
+ATOM   4141 N  N   . HIS D 2 116 ? -13.739 15.965  39.225 1.00 15.03 ? 116 HIS D N   1
+ATOM   4142 C  CA  . HIS D 2 116 ? -14.586 16.976  38.585 1.00 12.09 ? 116 HIS D CA  1
+ATOM   4143 C  C   . HIS D 2 116 ? -15.923 16.396  38.270 1.00 12.50 ? 116 HIS D C   1
+ATOM   4144 O  O   . HIS D 2 116 ? -17.017 17.107  38.496 1.00 15.93 ? 116 HIS D O   1
+ATOM   4145 C  CB  . HIS D 2 116 ? -13.888 17.392  37.294 1.00 20.66 ? 116 HIS D CB  1
+ATOM   4146 C  CG  . HIS D 2 116 ? -14.663 18.571  36.668 1.00 27.72 ? 116 HIS D CG  1
+ATOM   4147 N  ND1 . HIS D 2 116 ? -14.880 18.449  35.445 1.00 29.99 ? 116 HIS D ND1 1
+ATOM   4148 C  CD2 . HIS D 2 116 ? -14.916 19.655  37.289 1.00 30.96 ? 116 HIS D CD2 1
+ATOM   4149 C  CE1 . HIS D 2 116 ? -15.407 19.733  35.024 1.00 27.26 ? 116 HIS D CE1 1
+ATOM   4150 N  NE2 . HIS D 2 116 ? -15.561 20.472  36.323 1.00 28.89 ? 116 HIS D NE2 1
+ATOM   4151 N  N   . HIS D 2 117 ? -15.997 15.219  37.723 1.00 13.33 ? 117 HIS D N   1
+ATOM   4152 C  CA  . HIS D 2 117 ? -17.200 14.578  37.260 1.00 15.24 ? 117 HIS D CA  1
+ATOM   4153 C  C   . HIS D 2 117 ? -17.989 14.233  38.521 1.00 17.50 ? 117 HIS D C   1
+ATOM   4154 O  O   . HIS D 2 117 ? -19.260 14.288  38.545 1.00 16.06 ? 117 HIS D O   1
+ATOM   4155 C  CB  . HIS D 2 117 ? -16.852 13.421  36.315 1.00 17.22 ? 117 HIS D CB  1
+ATOM   4156 C  CG  . HIS D 2 117 ? -17.868 12.886  35.837 1.00 54.91 ? 117 HIS D CG  1
+ATOM   4157 N  ND1 . HIS D 2 117 ? -18.691 13.689  34.534 1.00 47.40 ? 117 HIS D ND1 1
+ATOM   4158 C  CD2 . HIS D 2 117 ? -19.150 11.964  36.098 1.00 49.34 ? 117 HIS D CD2 1
+ATOM   4159 C  CE1 . HIS D 2 117 ? -19.892 12.565  34.499 1.00 48.36 ? 117 HIS D CE1 1
+ATOM   4160 N  NE2 . HIS D 2 117 ? -19.944 11.859  35.162 1.00 37.10 ? 117 HIS D NE2 1
+ATOM   4161 N  N   . PHE D 2 118 ? -17.535 13.490  39.513 1.00 14.50 ? 118 PHE D N   1
+ATOM   4162 C  CA  . PHE D 2 118 ? -18.249 12.863  40.700 1.00 19.30 ? 118 PHE D CA  1
+ATOM   4163 C  C   . PHE D 2 118 ? -18.321 13.790  41.826 1.00 20.52 ? 118 PHE D C   1
+ATOM   4164 O  O   . PHE D 2 118 ? -19.086 13.416  42.859 1.00 18.09 ? 118 PHE D O   1
+ATOM   4165 C  CB  . PHE D 2 118 ? -17.602 11.595  41.070 1.00 18.97 ? 118 PHE D CB  1
+ATOM   4166 C  CG  . PHE D 2 118 ? -17.846 10.574  39.867 1.00 18.93 ? 118 PHE D CG  1
+ATOM   4167 C  CD1 . PHE D 2 118 ? -17.063 9.973   38.951 1.00 24.34 ? 118 PHE D CD1 1
+ATOM   4168 C  CD2 . PHE D 2 118 ? -19.233 10.072  39.842 1.00 26.48 ? 118 PHE D CD2 1
+ATOM   4169 C  CE1 . PHE D 2 118 ? -17.124 9.126   37.900 1.00 20.81 ? 118 PHE D CE1 1
+ATOM   4170 C  CE2 . PHE D 2 118 ? -19.471 9.111   38.661 1.00 22.90 ? 118 PHE D CE2 1
+ATOM   4171 C  CZ  . PHE D 2 118 ? -18.579 8.945   37.668 1.00 38.52 ? 118 PHE D CZ  1
+ATOM   4172 N  N   . GLY D 2 119 ? -17.573 14.836  42.034 1.00 12.95 ? 119 GLY D N   1
+ATOM   4173 C  CA  . GLY D 2 119 ? -17.804 15.799  43.120 1.00 17.60 ? 119 GLY D CA  1
+ATOM   4174 C  C   . GLY D 2 119 ? -17.298 14.988  44.440 1.00 22.58 ? 119 GLY D C   1
+ATOM   4175 O  O   . GLY D 2 119 ? -16.509 14.155  44.660 1.00 17.60 ? 119 GLY D O   1
+ATOM   4176 N  N   . LYS D 2 120 ? -18.313 15.227  45.454 1.00 21.46 ? 120 LYS D N   1
+ATOM   4177 C  CA  . LYS D 2 120 ? -17.955 14.862  46.795 1.00 20.05 ? 120 LYS D CA  1
+ATOM   4178 C  C   . LYS D 2 120 ? -18.239 13.485  46.948 1.00 21.98 ? 120 LYS D C   1
+ATOM   4179 O  O   . LYS D 2 120 ? -17.543 12.816  47.838 1.00 18.57 ? 120 LYS D O   1
+ATOM   4180 C  CB  . LYS D 2 120 ? -19.059 15.697  47.683 1.00 27.28 ? 120 LYS D CB  1
+ATOM   4181 C  CG  . LYS D 2 120 ? -20.052 14.809  47.922 1.00 44.07 ? 120 LYS D CG  1
+ATOM   4182 C  CD  . LYS D 2 120 ? -21.401 14.795  48.896 1.00 48.21 ? 120 LYS D CD  1
+ATOM   4183 C  CE  . LYS D 2 120 ? -22.663 14.415  48.016 1.00 53.23 ? 120 LYS D CE  1
+ATOM   4184 N  NZ  . LYS D 2 120 ? -24.242 13.752  49.540 1.00 62.54 ? 120 LYS D NZ  1
+ATOM   4185 N  N   . GLU D 2 121 ? -18.469 12.595  45.994 1.00 25.88 ? 121 GLU D N   1
+ATOM   4186 C  CA  . GLU D 2 121 ? -18.440 11.310  46.022 1.00 20.02 ? 121 GLU D CA  1
+ATOM   4187 C  C   . GLU D 2 121 ? -16.952 10.570  45.792 1.00 18.96 ? 121 GLU D C   1
+ATOM   4188 O  O   . GLU D 2 121 ? -16.771 9.407   46.201 1.00 16.05 ? 121 GLU D O   1
+ATOM   4189 C  CB  . GLU D 2 121 ? -19.411 10.519  44.740 1.00 28.13 ? 121 GLU D CB  1
+ATOM   4190 C  CG  . GLU D 2 121 ? -19.539 9.448   44.871 1.00 40.20 ? 121 GLU D CG  1
+ATOM   4191 C  CD  . GLU D 2 121 ? -21.101 8.591   43.945 1.00 49.97 ? 121 GLU D CD  1
+ATOM   4192 O  OE1 . GLU D 2 121 ? -20.320 7.357   43.531 1.00 36.73 ? 121 GLU D OE1 1
+ATOM   4193 O  OE2 . GLU D 2 121 ? -21.018 9.392   42.959 1.00 38.86 ? 121 GLU D OE2 1
+ATOM   4194 N  N   . PHE D 2 122 ? -16.232 11.457  45.188 1.00 14.83 ? 122 PHE D N   1
+ATOM   4195 C  CA  . PHE D 2 122 ? -14.806 10.935  44.992 1.00 20.37 ? 122 PHE D CA  1
+ATOM   4196 C  C   . PHE D 2 122 ? -14.041 11.364  46.308 1.00 15.94 ? 122 PHE D C   1
+ATOM   4197 O  O   . PHE D 2 122 ? -13.223 12.305  46.342 1.00 17.73 ? 122 PHE D O   1
+ATOM   4198 C  CB  . PHE D 2 122 ? -14.415 11.754  43.886 1.00 14.63 ? 122 PHE D CB  1
+ATOM   4199 C  CG  . PHE D 2 122 ? -13.146 11.096  43.213 1.00 12.39 ? 122 PHE D CG  1
+ATOM   4200 C  CD1 . PHE D 2 122 ? -13.064 9.930   42.732 1.00 14.73 ? 122 PHE D CD1 1
+ATOM   4201 C  CD2 . PHE D 2 122 ? -11.761 11.672  43.293 1.00 15.96 ? 122 PHE D CD2 1
+ATOM   4202 C  CE1 . PHE D 2 122 ? -11.850 9.231   42.128 1.00 19.03 ? 122 PHE D CE1 1
+ATOM   4203 C  CE2 . PHE D 2 122 ? -10.524 11.140  42.913 1.00 16.31 ? 122 PHE D CE2 1
+ATOM   4204 C  CZ  . PHE D 2 122 ? -10.767 9.973   42.353 1.00 19.86 ? 122 PHE D CZ  1
+ATOM   4205 N  N   . THR D 2 123 ? -14.305 10.596  47.277 1.00 12.54 ? 123 THR D N   1
+ATOM   4206 C  CA  . THR D 2 123 ? -13.654 11.017  48.600 1.00 13.34 ? 123 THR D CA  1
+ATOM   4207 C  C   . THR D 2 123 ? -12.261 10.645  48.579 1.00 15.73 ? 123 THR D C   1
+ATOM   4208 O  O   . THR D 2 123 ? -11.731 9.962   47.799 1.00 13.84 ? 123 THR D O   1
+ATOM   4209 C  CB  . THR D 2 123 ? -14.250 10.114  49.692 1.00 17.72 ? 123 THR D CB  1
+ATOM   4210 O  OG1 . THR D 2 123 ? -14.213 8.755   49.434 1.00 19.04 ? 123 THR D OG1 1
+ATOM   4211 C  CG2 . THR D 2 123 ? -16.032 10.338  49.677 1.00 20.06 ? 123 THR D CG2 1
+ATOM   4212 N  N   . PRO D 2 124 ? -11.613 11.145  49.655 1.00 17.46 ? 124 PRO D N   1
+ATOM   4213 C  CA  . PRO D 2 124 ? -10.165 10.787  49.885 1.00 14.41 ? 124 PRO D CA  1
+ATOM   4214 C  C   . PRO D 2 124 ? -9.843  9.388   49.797 1.00 12.05 ? 124 PRO D C   1
+ATOM   4215 O  O   . PRO D 2 124 ? -8.887  9.027   49.109 1.00 13.28 ? 124 PRO D O   1
+ATOM   4216 C  CB  . PRO D 2 124 ? -9.806  11.553  51.109 1.00 14.54 ? 124 PRO D CB  1
+ATOM   4217 C  CG  . PRO D 2 124 ? -10.762 12.742  51.179 1.00 15.93 ? 124 PRO D CG  1
+ATOM   4218 C  CD  . PRO D 2 124 ? -12.048 12.068  50.719 1.00 14.57 ? 124 PRO D CD  1
+ATOM   4219 N  N   . PRO D 2 125 ? -10.524 8.419   50.394 1.00 11.40 ? 125 PRO D N   1
+ATOM   4220 C  CA  . PRO D 2 125 ? -10.284 7.124   50.249 1.00 17.87 ? 125 PRO D CA  1
+ATOM   4221 C  C   . PRO D 2 125 ? -10.363 6.364   48.936 1.00 15.21 ? 125 PRO D C   1
+ATOM   4222 O  O   . PRO D 2 125 ? -9.598  5.567   48.439 1.00 14.41 ? 125 PRO D O   1
+ATOM   4223 C  CB  . PRO D 2 125 ? -11.188 6.474   51.245 1.00 23.30 ? 125 PRO D CB  1
+ATOM   4224 C  CG  . PRO D 2 125 ? -11.492 7.400   52.139 1.00 26.37 ? 125 PRO D CG  1
+ATOM   4225 C  CD  . PRO D 2 125 ? -11.593 8.612   51.663 1.00 17.49 ? 125 PRO D CD  1
+ATOM   4226 N  N   . VAL D 2 126 ? -11.461 7.000   48.227 1.00 17.66 ? 126 VAL D N   1
+ATOM   4227 C  CA  . VAL D 2 126 ? -11.619 6.487   46.820 1.00 21.55 ? 126 VAL D CA  1
+ATOM   4228 C  C   . VAL D 2 126 ? -10.338 6.896   45.817 1.00 16.49 ? 126 VAL D C   1
+ATOM   4229 O  O   . VAL D 2 126 ? -9.966  6.194   45.062 1.00 13.46 ? 126 VAL D O   1
+ATOM   4230 C  CB  . VAL D 2 126 ? -13.193 7.159   46.221 1.00 13.98 ? 126 VAL D CB  1
+ATOM   4231 C  CG1 . VAL D 2 126 ? -13.233 6.625   44.941 1.00 20.70 ? 126 VAL D CG1 1
+ATOM   4232 C  CG2 . VAL D 2 126 ? -14.046 6.344   47.186 1.00 18.54 ? 126 VAL D CG2 1
+ATOM   4233 N  N   . GLN D 2 127 ? -10.081 8.341   46.123 1.00 10.60 ? 127 GLN D N   1
+ATOM   4234 C  CA  . GLN D 2 127 ? -8.869  8.759   45.495 1.00 12.83 ? 127 GLN D CA  1
+ATOM   4235 C  C   . GLN D 2 127 ? -7.752  7.883   45.581 1.00 13.74 ? 127 GLN D C   1
+ATOM   4236 O  O   . GLN D 2 127 ? -7.011  7.557   44.630 1.00 12.71 ? 127 GLN D O   1
+ATOM   4237 C  CB  . GLN D 2 127 ? -8.709  10.240  45.723 1.00 11.73 ? 127 GLN D CB  1
+ATOM   4238 C  CG  . GLN D 2 127 ? -7.328  10.704  45.021 1.00 13.68 ? 127 GLN D CG  1
+ATOM   4239 C  CD  . GLN D 2 127 ? -6.870  12.007  45.620 1.00 11.81 ? 127 GLN D CD  1
+ATOM   4240 O  OE1 . GLN D 2 127 ? -7.612  12.791  46.226 1.00 13.99 ? 127 GLN D OE1 1
+ATOM   4241 N  NE2 . GLN D 2 127 ? -5.794  12.384  44.981 1.00 15.96 ? 127 GLN D NE2 1
+ATOM   4242 N  N   . ALA D 2 128 ? -7.425  7.510   46.886 1.00 12.61 ? 128 ALA D N   1
+ATOM   4243 C  CA  . ALA D 2 128 ? -6.284  6.708   47.255 1.00 9.64  ? 128 ALA D CA  1
+ATOM   4244 C  C   . ALA D 2 128 ? -6.200  5.390   46.495 1.00 7.66  ? 128 ALA D C   1
+ATOM   4245 O  O   . ALA D 2 128 ? -5.196  5.017   45.975 1.00 11.68 ? 128 ALA D O   1
+ATOM   4246 C  CB  . ALA D 2 128 ? -6.224  6.481   48.747 1.00 13.80 ? 128 ALA D CB  1
+ATOM   4247 N  N   . ALA D 2 129 ? -7.447  4.929   46.356 1.00 13.18 ? 129 ALA D N   1
+ATOM   4248 C  CA  . ALA D 2 129 ? -7.605  3.606   45.705 1.00 11.17 ? 129 ALA D CA  1
+ATOM   4249 C  C   . ALA D 2 129 ? -7.232  3.804   44.181 1.00 11.52 ? 129 ALA D C   1
+ATOM   4250 O  O   . ALA D 2 129 ? -6.564  2.935   43.582 1.00 13.56 ? 129 ALA D O   1
+ATOM   4251 C  CB  . ALA D 2 129 ? -8.947  3.013   45.910 1.00 14.35 ? 129 ALA D CB  1
+ATOM   4252 N  N   . TYR D 2 130 ? -7.859  4.740   43.565 1.00 13.36 ? 130 TYR D N   1
+ATOM   4253 C  CA  . TYR D 2 130 ? -7.692  5.106   42.162 1.00 13.72 ? 130 TYR D CA  1
+ATOM   4254 C  C   . TYR D 2 130 ? -6.196  5.516   41.935 1.00 15.10 ? 130 TYR D C   1
+ATOM   4255 O  O   . TYR D 2 130 ? -5.614  5.098   40.917 1.00 13.21 ? 130 TYR D O   1
+ATOM   4256 C  CB  . TYR D 2 130 ? -8.499  6.213   41.726 1.00 13.30 ? 130 TYR D CB  1
+ATOM   4257 C  CG  . TYR D 2 130 ? -9.754  5.633   41.233 1.00 15.19 ? 130 TYR D CG  1
+ATOM   4258 C  CD1 . TYR D 2 130 ? -9.822  5.138   39.964 1.00 16.58 ? 130 TYR D CD1 1
+ATOM   4259 C  CD2 . TYR D 2 130 ? -10.894 5.379   41.926 1.00 11.73 ? 130 TYR D CD2 1
+ATOM   4260 C  CE1 . TYR D 2 130 ? -10.898 4.373   39.135 1.00 20.28 ? 130 TYR D CE1 1
+ATOM   4261 C  CE2 . TYR D 2 130 ? -12.082 4.726   41.285 1.00 14.90 ? 130 TYR D CE2 1
+ATOM   4262 C  CZ  . TYR D 2 130 ? -12.123 4.206   40.120 1.00 22.05 ? 130 TYR D CZ  1
+ATOM   4263 O  OH  . TYR D 2 130 ? -13.192 3.666   39.581 1.00 20.92 ? 130 TYR D OH  1
+ATOM   4264 N  N   . GLN D 2 131 ? -5.574  6.073   42.896 1.00 12.24 ? 131 GLN D N   1
+ATOM   4265 C  CA  . GLN D 2 131 ? -4.108  6.359   42.744 1.00 13.72 ? 131 GLN D CA  1
+ATOM   4266 C  C   . GLN D 2 131 ? -3.236  5.250   42.562 1.00 20.69 ? 131 GLN D C   1
+ATOM   4267 O  O   . GLN D 2 131 ? -2.419  5.044   41.854 1.00 17.83 ? 131 GLN D O   1
+ATOM   4268 C  CB  . GLN D 2 131 ? -3.534  7.388   43.772 1.00 13.45 ? 131 GLN D CB  1
+ATOM   4269 C  CG  . GLN D 2 131 ? -4.127  8.633   43.826 1.00 20.19 ? 131 GLN D CG  1
+ATOM   4270 C  CD  . GLN D 2 131 ? -3.529  9.873   42.716 1.00 18.43 ? 131 GLN D CD  1
+ATOM   4271 O  OE1 . GLN D 2 131 ? -4.263  10.790  42.812 1.00 14.48 ? 131 GLN D OE1 1
+ATOM   4272 N  NE2 . GLN D 2 131 ? -2.698  9.458   41.955 1.00 16.06 ? 131 GLN D NE2 1
+ATOM   4273 N  N   . LYS D 2 132 ? -3.633  4.146   43.364 1.00 12.67 ? 132 LYS D N   1
+ATOM   4274 C  CA  . LYS D 2 132 ? -2.807  2.887   43.390 1.00 15.63 ? 132 LYS D CA  1
+ATOM   4275 C  C   . LYS D 2 132 ? -3.029  2.188   42.022 1.00 18.80 ? 132 LYS D C   1
+ATOM   4276 O  O   . LYS D 2 132 ? -2.199  1.739   41.376 1.00 14.05 ? 132 LYS D O   1
+ATOM   4277 C  CB  . LYS D 2 132 ? -3.309  1.949   44.403 1.00 24.81 ? 132 LYS D CB  1
+ATOM   4278 C  CG  . LYS D 2 132 ? -2.740  2.319   45.801 1.00 25.97 ? 132 LYS D CG  1
+ATOM   4279 C  CD  . LYS D 2 132 ? -3.450  1.283   46.867 1.00 26.81 ? 132 LYS D CD  1
+ATOM   4280 C  CE  . LYS D 2 132 ? -3.647  2.409   48.135 1.00 50.23 ? 132 LYS D CE  1
+ATOM   4281 N  NZ  . LYS D 2 132 ? -3.659  0.122   49.107 1.00 63.38 ? 132 LYS D NZ  1
+ATOM   4282 N  N   . VAL D 2 133 ? -4.291  2.348   41.481 1.00 13.42 ? 133 VAL D N   1
+ATOM   4283 C  CA  . VAL D 2 133 ? -4.649  1.665   40.219 1.00 18.27 ? 133 VAL D CA  1
+ATOM   4284 C  C   . VAL D 2 133 ? -3.876  2.408   39.113 1.00 19.39 ? 133 VAL D C   1
+ATOM   4285 O  O   . VAL D 2 133 ? -3.292  1.705   38.236 1.00 15.06 ? 133 VAL D O   1
+ATOM   4286 C  CB  . VAL D 2 133 ? -6.222  1.610   39.979 1.00 17.40 ? 133 VAL D CB  1
+ATOM   4287 C  CG1 . VAL D 2 133 ? -6.471  1.441   38.484 1.00 22.79 ? 133 VAL D CG1 1
+ATOM   4288 C  CG2 . VAL D 2 133 ? -6.843  0.824   41.082 1.00 19.90 ? 133 VAL D CG2 1
+ATOM   4289 N  N   . VAL D 2 134 ? -3.994  3.629   39.031 1.00 14.66 ? 134 VAL D N   1
+ATOM   4290 C  CA  . VAL D 2 134 ? -3.343  4.293   37.859 1.00 17.41 ? 134 VAL D CA  1
+ATOM   4291 C  C   . VAL D 2 134 ? -1.721  4.226   37.826 1.00 17.93 ? 134 VAL D C   1
+ATOM   4292 O  O   . VAL D 2 134 ? -1.164  3.952   36.793 1.00 17.13 ? 134 VAL D O   1
+ATOM   4293 C  CB  . VAL D 2 134 ? -3.835  5.761   37.643 1.00 16.69 ? 134 VAL D CB  1
+ATOM   4294 C  CG1 . VAL D 2 134 ? -5.248  5.959   37.556 1.00 22.42 ? 134 VAL D CG1 1
+ATOM   4295 C  CG2 . VAL D 2 134 ? -3.246  6.570   38.773 1.00 16.30 ? 134 VAL D CG2 1
+ATOM   4296 N  N   . ALA D 2 135 ? -1.210  4.136   39.001 1.00 16.25 ? 135 ALA D N   1
+ATOM   4297 C  CA  . ALA D 2 135 ? 0.222   4.021   39.248 1.00 14.79 ? 135 ALA D CA  1
+ATOM   4298 C  C   . ALA D 2 135 ? 0.535   2.430   38.651 1.00 21.70 ? 135 ALA D C   1
+ATOM   4299 O  O   . ALA D 2 135 ? 1.545   2.138   38.048 1.00 16.89 ? 135 ALA D O   1
+ATOM   4300 C  CB  . ALA D 2 135 ? 0.696   4.015   40.592 1.00 18.34 ? 135 ALA D CB  1
+ATOM   4301 N  N   . GLY D 2 136 ? -0.303  1.437   38.989 1.00 17.40 ? 136 GLY D N   1
+ATOM   4302 C  CA  . GLY D 2 136 ? -0.330  0.170   38.691 1.00 16.77 ? 136 GLY D CA  1
+ATOM   4303 C  C   . GLY D 2 136 ? -0.250  0.004   37.137 1.00 21.35 ? 136 GLY D C   1
+ATOM   4304 O  O   . GLY D 2 136 ? 0.550   -0.717  36.435 1.00 16.80 ? 136 GLY D O   1
+ATOM   4305 N  N   . VAL D 2 137 ? -1.202  0.687   36.586 1.00 23.70 ? 137 VAL D N   1
+ATOM   4306 C  CA  . VAL D 2 137 ? -1.343  0.660   35.180 1.00 26.49 ? 137 VAL D CA  1
+ATOM   4307 C  C   . VAL D 2 137 ? -0.439  1.268   34.267 1.00 33.07 ? 137 VAL D C   1
+ATOM   4308 O  O   . VAL D 2 137 ? 0.284   0.740   33.543 1.00 30.90 ? 137 VAL D O   1
+ATOM   4309 C  CB  . VAL D 2 137 ? -2.815  1.314   34.539 1.00 15.94 ? 137 VAL D CB  1
+ATOM   4310 C  CG1 . VAL D 2 137 ? -2.835  1.555   32.993 1.00 21.57 ? 137 VAL D CG1 1
+ATOM   4311 C  CG2 . VAL D 2 137 ? -3.828  0.490   35.194 1.00 21.46 ? 137 VAL D CG2 1
+ATOM   4312 N  N   . ALA D 2 138 ? 0.242   2.363   34.809 1.00 14.66 ? 138 ALA D N   1
+ATOM   4313 C  CA  . ALA D 2 138 ? 1.452   3.050   34.226 1.00 18.95 ? 138 ALA D CA  1
+ATOM   4314 C  C   . ALA D 2 138 ? 2.592   2.120   34.226 1.00 18.17 ? 138 ALA D C   1
+ATOM   4315 O  O   . ALA D 2 138 ? 3.362   2.006   33.396 1.00 14.81 ? 138 ALA D O   1
+ATOM   4316 C  CB  . ALA D 2 138 ? 1.860   4.377   34.985 1.00 19.78 ? 138 ALA D CB  1
+ATOM   4317 N  N   . ASN D 2 139 ? 2.786   1.456   35.416 1.00 15.30 ? 139 ASN D N   1
+ATOM   4318 C  CA  . ASN D 2 139 ? 3.956   0.732   35.737 1.00 18.41 ? 139 ASN D CA  1
+ATOM   4319 C  C   . ASN D 2 139 ? 3.938   -0.487  34.720 1.00 25.63 ? 139 ASN D C   1
+ATOM   4320 O  O   . ASN D 2 139 ? 4.881   -1.132  34.071 1.00 23.38 ? 139 ASN D O   1
+ATOM   4321 C  CB  . ASN D 2 139 ? 3.870   0.156   36.790 1.00 50.89 ? 139 ASN D CB  1
+ATOM   4322 C  CG  . ASN D 2 139 ? 4.770   0.374   37.804 1.00 63.06 ? 139 ASN D CG  1
+ATOM   4323 O  OD1 . ASN D 2 139 ? 5.595   -1.037  37.424 1.00 52.41 ? 139 ASN D OD1 1
+ATOM   4324 N  ND2 . ASN D 2 139 ? 5.131   1.893   37.675 1.00 29.84 ? 139 ASN D ND2 1
+ATOM   4325 N  N   . ALA D 2 140 ? 2.648   -1.086  34.607 1.00 19.40 ? 140 ALA D N   1
+ATOM   4326 C  CA  . ALA D 2 140 ? 2.270   -2.273  33.687 1.00 23.09 ? 140 ALA D CA  1
+ATOM   4327 C  C   . ALA D 2 140 ? 2.538   -1.750  32.200 1.00 18.16 ? 140 ALA D C   1
+ATOM   4328 O  O   . ALA D 2 140 ? 3.180   -2.633  31.538 1.00 16.51 ? 140 ALA D O   1
+ATOM   4329 C  CB  . ALA D 2 140 ? 0.893   -2.659  33.730 1.00 18.14 ? 140 ALA D CB  1
+ATOM   4330 N  N   . LEU D 2 141 ? 2.248   -0.677  31.759 1.00 14.97 ? 141 LEU D N   1
+ATOM   4331 C  CA  . LEU D 2 141 ? 2.521   -0.240  30.461 1.00 14.94 ? 141 LEU D CA  1
+ATOM   4332 C  C   . LEU D 2 141 ? 4.024   -0.030  30.150 1.00 11.73 ? 141 LEU D C   1
+ATOM   4333 O  O   . LEU D 2 141 ? 4.585   0.103   29.049 1.00 15.21 ? 141 LEU D O   1
+ATOM   4334 C  CB  . LEU D 2 141 ? 1.582   1.022   30.122 1.00 15.16 ? 141 LEU D CB  1
+ATOM   4335 C  CG  . LEU D 2 141 ? 0.181   0.748   29.794 1.00 17.87 ? 141 LEU D CG  1
+ATOM   4336 C  CD1 . LEU D 2 141 ? -0.164  2.040   29.189 1.00 24.86 ? 141 LEU D CD1 1
+ATOM   4337 C  CD2 . LEU D 2 141 ? 0.442   0.005   28.202 1.00 16.07 ? 141 LEU D CD2 1
+ATOM   4338 N  N   . ALA D 2 142 ? 4.782   0.465   31.224 1.00 14.26 ? 142 ALA D N   1
+ATOM   4339 C  CA  . ALA D 2 142 ? 6.206   0.616   31.094 1.00 17.21 ? 142 ALA D CA  1
+ATOM   4340 C  C   . ALA D 2 142 ? 7.092   -0.595  31.194 1.00 18.46 ? 142 ALA D C   1
+ATOM   4341 O  O   . ALA D 2 142 ? 8.246   -0.429  30.861 1.00 18.92 ? 142 ALA D O   1
+ATOM   4342 C  CB  . ALA D 2 142 ? 6.590   1.614   32.154 1.00 19.11 ? 142 ALA D CB  1
+ATOM   4343 N  N   . HIS D 2 143 ? 6.554   -1.735  31.550 1.00 19.75 ? 143 HIS D N   1
+ATOM   4344 C  CA  . HIS D 2 143 ? 7.205   -3.008  31.859 1.00 26.63 ? 143 HIS D CA  1
+ATOM   4345 C  C   . HIS D 2 143 ? 8.170   -3.508  30.674 1.00 23.72 ? 143 HIS D C   1
+ATOM   4346 O  O   . HIS D 2 143 ? 9.184   -3.992  31.179 1.00 24.41 ? 143 HIS D O   1
+ATOM   4347 C  CB  . HIS D 2 143 ? 6.333   -3.963  32.578 1.00 25.89 ? 143 HIS D CB  1
+ATOM   4348 C  CG  . HIS D 2 143 ? 6.943   -5.113  32.890 1.00 56.45 ? 143 HIS D CG  1
+ATOM   4349 N  ND1 . HIS D 2 143 ? 6.761   -6.218  32.381 1.00 44.25 ? 143 HIS D ND1 1
+ATOM   4350 C  CD2 . HIS D 2 143 ? 8.001   -4.991  34.400 1.00 48.81 ? 143 HIS D CD2 1
+ATOM   4351 C  CE1 . HIS D 2 143 ? 7.886   -6.933  33.301 1.00 56.93 ? 143 HIS D CE1 1
+ATOM   4352 N  NE2 . HIS D 2 143 ? 8.173   -6.288  34.468 1.00 49.27 ? 143 HIS D NE2 1
+ATOM   4353 N  N   . LYS D 2 144 ? 7.711   -3.417  29.538 1.00 19.26 ? 144 LYS D N   1
+ATOM   4354 C  CA  . LYS D 2 144 ? 8.236   -3.890  28.184 1.00 33.94 ? 144 LYS D CA  1
+ATOM   4355 C  C   . LYS D 2 144 ? 9.323   -3.145  27.737 1.00 32.28 ? 144 LYS D C   1
+ATOM   4356 O  O   . LYS D 2 144 ? 9.807   -3.336  26.537 1.00 23.60 ? 144 LYS D O   1
+ATOM   4357 C  CB  . LYS D 2 144 ? 7.652   -4.830  27.501 1.00 31.20 ? 144 LYS D CB  1
+ATOM   4358 C  CG  . LYS D 2 144 ? 6.664   -5.972  28.248 1.00 40.85 ? 144 LYS D CG  1
+ATOM   4359 C  CD  . LYS D 2 144 ? 7.257   -7.191  28.181 1.00 59.03 ? 144 LYS D CD  1
+ATOM   4360 C  CE  . LYS D 2 144 ? 6.994   -8.215  28.490 1.00 56.19 ? 144 LYS D CE  1
+ATOM   4361 N  NZ  . LYS D 2 144 ? 7.258   -10.167 27.594 1.00 70.96 ? 144 LYS D NZ  1
+ATOM   4362 N  N   . TYR D 2 145 ? 9.560   -1.914  28.156 1.00 24.92 ? 145 TYR D N   1
+ATOM   4363 C  CA  . TYR D 2 145 ? 10.462  -1.026  27.720 1.00 29.13 ? 145 TYR D CA  1
+ATOM   4364 C  C   . TYR D 2 145 ? 11.937  -1.404  27.790 1.00 38.17 ? 145 TYR D C   1
+ATOM   4365 O  O   . TYR D 2 145 ? 12.253  -1.961  28.782 1.00 27.99 ? 145 TYR D O   1
+ATOM   4366 C  CB  . TYR D 2 145 ? 10.259  0.435   28.272 1.00 17.99 ? 145 TYR D CB  1
+ATOM   4367 C  CG  . TYR D 2 145 ? 9.220   1.295   27.599 1.00 17.42 ? 145 TYR D CG  1
+ATOM   4368 C  CD1 . TYR D 2 145 ? 9.255   2.396   26.840 1.00 16.93 ? 145 TYR D CD1 1
+ATOM   4369 C  CD2 . TYR D 2 145 ? 7.885   0.764   27.865 1.00 18.60 ? 145 TYR D CD2 1
+ATOM   4370 C  CE1 . TYR D 2 145 ? 8.295   3.092   26.280 1.00 17.99 ? 145 TYR D CE1 1
+ATOM   4371 C  CE2 . TYR D 2 145 ? 6.769   1.552   27.208 1.00 14.96 ? 145 TYR D CE2 1
+ATOM   4372 C  CZ  . TYR D 2 145 ? 6.944   2.560   26.530 1.00 12.85 ? 145 TYR D CZ  1
+ATOM   4373 O  OH  . TYR D 2 145 ? 5.973   3.362   25.924 1.00 13.31 ? 145 TYR D OH  1
+ATOM   4374 N  N   . HIS D 2 146 ? 12.625  -1.243  26.753 1.00 26.11 ? 146 HIS D N   1
+ATOM   4375 C  CA  . HIS D 2 146 ? 14.229  -1.501  26.683 1.00 31.89 ? 146 HIS D CA  1
+ATOM   4376 C  C   . HIS D 2 146 ? 14.684  -0.644  25.577 1.00 21.33 ? 146 HIS D C   1
+ATOM   4377 O  O   . HIS D 2 146 ? 14.298  0.285   25.043 1.00 27.92 ? 146 HIS D O   1
+ATOM   4378 C  CB  . HIS D 2 146 ? 14.106  -3.154  26.208 1.00 30.13 ? 146 HIS D CB  1
+ATOM   4379 C  CG  . HIS D 2 146 ? 13.302  -3.158  25.041 1.00 40.51 ? 146 HIS D CG  1
+ATOM   4380 N  ND1 . HIS D 2 146 ? 14.250  -3.363  23.467 1.00 47.51 ? 146 HIS D ND1 1
+ATOM   4381 C  CD2 . HIS D 2 146 ? 12.608  -2.661  24.150 1.00 45.49 ? 146 HIS D CD2 1
+ATOM   4382 C  CE1 . HIS D 2 146 ? 13.837  -3.447  22.948 1.00 56.67 ? 146 HIS D CE1 1
+ATOM   4383 N  NE2 . HIS D 2 146 ? 12.427  -2.792  22.588 1.00 37.33 ? 146 HIS D NE2 1
+ATOM   4384 O  OXT . HIS D 2 146 ? 16.064  -0.829  25.697 1.00 21.61 ? 146 HIS D OXT 1
+HETATM 4385 C  CHA . HEM E 3 .   ? 18.675  18.641  20.464 1.00 16.31 ? 142 HEM A CHA 1
+HETATM 4386 C  CHB . HEM E 3 .   ? 20.996  20.564  24.241 1.00 26.27 ? 142 HEM A CHB 1
+HETATM 4387 C  CHC . HEM E 3 .   ? 18.666  17.711  27.273 1.00 13.23 ? 142 HEM A CHC 1
+HETATM 4388 C  CHD . HEM E 3 .   ? 16.693  15.349  23.426 1.00 14.77 ? 142 HEM A CHD 1
+HETATM 4389 C  C1A . HEM E 3 .   ? 19.403  19.426  21.131 1.00 17.40 ? 142 HEM A C1A 1
+HETATM 4390 C  C2A . HEM E 3 .   ? 20.508  20.450  20.584 1.00 18.53 ? 142 HEM A C2A 1
+HETATM 4391 C  C3A . HEM E 3 .   ? 21.199  20.992  21.589 1.00 18.36 ? 142 HEM A C3A 1
+HETATM 4392 C  C4A . HEM E 3 .   ? 20.664  20.361  22.870 1.00 16.88 ? 142 HEM A C4A 1
+HETATM 4393 C  CMA . HEM E 3 .   ? 22.334  21.915  21.498 1.00 21.20 ? 142 HEM A CMA 1
+HETATM 4394 C  CAA . HEM E 3 .   ? 20.773  20.694  19.113 1.00 25.54 ? 142 HEM A CAA 1
+HETATM 4395 C  CBA . HEM E 3 .   ? 20.048  21.689  18.733 1.00 31.38 ? 142 HEM A CBA 1
+HETATM 4396 C  CGA . HEM E 3 .   ? 21.309  22.355  16.897 1.00 44.82 ? 142 HEM A CGA 1
+HETATM 4397 O  O1A . HEM E 3 .   ? 20.230  21.524  16.437 1.00 39.10 ? 142 HEM A O1A 1
+HETATM 4398 O  O2A . HEM E 3 .   ? 19.899  22.984  16.799 1.00 54.71 ? 142 HEM A O2A 1
+HETATM 4399 C  C1B . HEM E 3 .   ? 20.578  20.191  25.370 1.00 23.63 ? 142 HEM A C1B 1
+HETATM 4400 C  C2B . HEM E 3 .   ? 21.061  20.345  26.638 1.00 11.67 ? 142 HEM A C2B 1
+HETATM 4401 C  C3B . HEM E 3 .   ? 20.308  19.491  27.552 1.00 17.41 ? 142 HEM A C3B 1
+HETATM 4402 C  C4B . HEM E 3 .   ? 19.486  18.656  26.750 1.00 14.84 ? 142 HEM A C4B 1
+HETATM 4403 C  CMB . HEM E 3 .   ? 22.004  21.499  26.929 1.00 12.32 ? 142 HEM A CMB 1
+HETATM 4404 C  CAB . HEM E 3 .   ? 20.314  19.616  28.967 1.00 24.30 ? 142 HEM A CAB 1
+HETATM 4405 C  CBB . HEM E 3 .   ? 21.385  19.628  29.745 1.00 28.40 ? 142 HEM A CBB 1
+HETATM 4406 C  C1C . HEM E 3 .   ? 17.818  16.891  26.484 1.00 13.39 ? 142 HEM A C1C 1
+HETATM 4407 C  C2C . HEM E 3 .   ? 17.238  15.704  26.953 1.00 11.20 ? 142 HEM A C2C 1
+HETATM 4408 C  C3C . HEM E 3 .   ? 16.751  14.913  25.912 1.00 8.94  ? 142 HEM A C3C 1
+HETATM 4409 C  C4C . HEM E 3 .   ? 17.049  15.765  24.601 1.00 10.29 ? 142 HEM A C4C 1
+HETATM 4410 C  CMC . HEM E 3 .   ? 17.072  15.268  28.333 1.00 13.77 ? 142 HEM A CMC 1
+HETATM 4411 C  CAC . HEM E 3 .   ? 15.919  13.759  25.843 1.00 13.45 ? 142 HEM A CAC 1
+HETATM 4412 C  CBC . HEM E 3 .   ? 16.189  12.746  26.670 1.00 11.27 ? 142 HEM A CBC 1
+HETATM 4413 C  C1D . HEM E 3 .   ? 17.071  16.105  22.343 1.00 11.32 ? 142 HEM A C1D 1
+HETATM 4414 C  C2D . HEM E 3 .   ? 16.754  15.669  20.885 1.00 16.69 ? 142 HEM A C2D 1
+HETATM 4415 C  C3D . HEM E 3 .   ? 17.267  16.609  20.121 1.00 20.49 ? 142 HEM A C3D 1
+HETATM 4416 C  C4D . HEM E 3 .   ? 18.074  17.418  20.731 1.00 16.46 ? 142 HEM A C4D 1
+HETATM 4417 C  CMD . HEM E 3 .   ? 15.745  14.508  20.471 1.00 19.45 ? 142 HEM A CMD 1
+HETATM 4418 C  CAD . HEM E 3 .   ? 17.244  16.494  18.603 1.00 21.31 ? 142 HEM A CAD 1
+HETATM 4419 C  CBD . HEM E 3 .   ? 18.286  15.903  18.216 1.00 38.22 ? 142 HEM A CBD 1
+HETATM 4420 C  CGD . HEM E 3 .   ? 18.466  15.379  16.204 1.00 41.21 ? 142 HEM A CGD 1
+HETATM 4421 O  O1D . HEM E 3 .   ? 19.441  16.024  16.178 1.00 42.81 ? 142 HEM A O1D 1
+HETATM 4422 O  O2D . HEM E 3 .   ? 17.644  15.349  15.916 1.00 40.12 ? 142 HEM A O2D 1
+HETATM 4423 N  NA  . HEM E 3 .   ? 19.740  19.452  22.406 1.00 16.46 ? 142 HEM A NA  1
+HETATM 4424 N  NB  . HEM E 3 .   ? 19.787  19.035  25.367 1.00 12.29 ? 142 HEM A NB  1
+HETATM 4425 N  NC  . HEM E 3 .   ? 17.647  16.819  25.044 1.00 15.07 ? 142 HEM A NC  1
+HETATM 4426 N  ND  . HEM E 3 .   ? 17.661  17.229  22.154 1.00 13.07 ? 142 HEM A ND  1
+HETATM 4427 FE FE  . HEM E 3 .   ? 18.362  18.488  23.755 1.00 18.07 ? 142 HEM A FE  1
+HETATM 4428 P  P   . PO4 F 4 .   ? 13.048  -8.180  44.783 1.00 32.97 ? 147 PO4 B P   1
+HETATM 4429 C  CHA . HEM G 3 .   ? 19.696  3.883   60.882 1.00 21.59 ? 148 HEM B CHA 1
+HETATM 4430 C  CHB . HEM G 3 .   ? 20.531  1.307   56.812 1.00 16.50 ? 148 HEM B CHB 1
+HETATM 4431 C  CHC . HEM G 3 .   ? 19.636  5.274   54.083 1.00 16.82 ? 148 HEM B CHC 1
+HETATM 4432 C  CHD . HEM G 3 .   ? 18.716  7.814   58.136 1.00 16.19 ? 148 HEM B CHD 1
+HETATM 4433 C  C1A . HEM G 3 .   ? 20.038  2.914   60.015 1.00 24.57 ? 148 HEM B C1A 1
+HETATM 4434 C  C2A . HEM G 3 .   ? 20.601  1.628   60.340 1.00 17.10 ? 148 HEM B C2A 1
+HETATM 4435 C  C3A . HEM G 3 .   ? 21.004  0.790   59.288 1.00 13.46 ? 148 HEM B C3A 1
+HETATM 4436 C  C4A . HEM G 3 .   ? 20.456  1.693   58.135 1.00 18.78 ? 148 HEM B C4A 1
+HETATM 4437 C  CMA . HEM G 3 .   ? 21.475  -0.544  59.191 1.00 20.21 ? 148 HEM B CMA 1
+HETATM 4438 C  CAA . HEM G 3 .   ? 20.843  1.153   61.811 1.00 21.16 ? 148 HEM B CAA 1
+HETATM 4439 C  CBA . HEM G 3 .   ? 19.662  0.448   62.341 1.00 27.78 ? 148 HEM B CBA 1
+HETATM 4440 C  CGA . HEM G 3 .   ? 19.478  -0.348  64.072 1.00 59.12 ? 148 HEM B CGA 1
+HETATM 4441 O  O1A . HEM G 3 .   ? 19.826  1.004   64.507 1.00 44.32 ? 148 HEM B O1A 1
+HETATM 4442 O  O2A . HEM G 3 .   ? 19.035  -0.826  63.962 1.00 46.16 ? 148 HEM B O2A 1
+HETATM 4443 C  C1B . HEM G 3 .   ? 20.300  2.161   55.701 1.00 10.36 ? 148 HEM B C1B 1
+HETATM 4444 C  C2B . HEM G 3 .   ? 20.580  1.732   54.232 1.00 7.33  ? 148 HEM B C2B 1
+HETATM 4445 C  C3B . HEM G 3 .   ? 20.293  2.817   53.607 1.00 15.63 ? 148 HEM B C3B 1
+HETATM 4446 C  C4B . HEM G 3 .   ? 19.876  3.979   54.587 1.00 15.33 ? 148 HEM B C4B 1
+HETATM 4447 C  CMB . HEM G 3 .   ? 20.914  0.425   54.068 1.00 14.96 ? 148 HEM B CMB 1
+HETATM 4448 C  CAB . HEM G 3 .   ? 20.376  3.027   52.014 1.00 19.63 ? 148 HEM B CAB 1
+HETATM 4449 C  CBB . HEM G 3 .   ? 21.354  2.423   51.345 1.00 39.39 ? 148 HEM B CBB 1
+HETATM 4450 C  C1C . HEM G 3 .   ? 19.317  6.327   55.097 1.00 14.39 ? 148 HEM B C1C 1
+HETATM 4451 C  C2C . HEM G 3 .   ? 19.211  7.643   54.498 1.00 10.78 ? 148 HEM B C2C 1
+HETATM 4452 C  C3C . HEM G 3 .   ? 18.939  8.567   55.685 1.00 10.68 ? 148 HEM B C3C 1
+HETATM 4453 C  C4C . HEM G 3 .   ? 18.923  7.406   56.661 1.00 8.70  ? 148 HEM B C4C 1
+HETATM 4454 C  CMC . HEM G 3 .   ? 19.339  8.147   53.123 1.00 13.95 ? 148 HEM B CMC 1
+HETATM 4455 C  CAC . HEM G 3 .   ? 18.612  9.938   55.795 1.00 11.87 ? 148 HEM B CAC 1
+HETATM 4456 C  CBC . HEM G 3 .   ? 19.172  10.844  55.145 1.00 12.63 ? 148 HEM B CBC 1
+HETATM 4457 C  C1D . HEM G 3 .   ? 19.006  6.998   59.241 1.00 18.32 ? 148 HEM B C1D 1
+HETATM 4458 C  C2D . HEM G 3 .   ? 18.768  7.424   60.638 1.00 15.48 ? 148 HEM B C2D 1
+HETATM 4459 C  C3D . HEM G 3 .   ? 18.923  6.175   61.235 1.00 14.57 ? 148 HEM B C3D 1
+HETATM 4460 C  C4D . HEM G 3 .   ? 19.494  5.137   60.358 1.00 20.76 ? 148 HEM B C4D 1
+HETATM 4461 C  CMD . HEM G 3 .   ? 18.544  8.862   61.055 1.00 27.50 ? 148 HEM B CMD 1
+HETATM 4462 C  CAD . HEM G 3 .   ? 19.226  6.338   62.819 1.00 13.85 ? 148 HEM B CAD 1
+HETATM 4463 C  CBD . HEM G 3 .   ? 20.641  6.416   63.304 1.00 17.11 ? 148 HEM B CBD 1
+HETATM 4464 C  CGD . HEM G 3 .   ? 20.969  6.040   65.088 1.00 27.09 ? 148 HEM B CGD 1
+HETATM 4465 O  O1D . HEM G 3 .   ? 22.104  6.528   65.136 1.00 27.49 ? 148 HEM B O1D 1
+HETATM 4466 O  O2D . HEM G 3 .   ? 19.864  6.347   65.549 1.00 23.65 ? 148 HEM B O2D 1
+HETATM 4467 N  NA  . HEM G 3 .   ? 20.024  2.942   58.603 1.00 15.64 ? 148 HEM B NA  1
+HETATM 4468 N  NB  . HEM G 3 .   ? 19.891  3.489   55.821 1.00 12.71 ? 148 HEM B NB  1
+HETATM 4469 N  NC  . HEM G 3 .   ? 19.239  6.099   56.480 1.00 11.22 ? 148 HEM B NC  1
+HETATM 4470 N  ND  . HEM G 3 .   ? 19.310  5.720   59.043 1.00 16.72 ? 148 HEM B ND  1
+HETATM 4471 FE FE  . HEM G 3 .   ? 19.264  4.466   57.461 1.00 15.00 ? 148 HEM B FE  1
+HETATM 4472 C  CHA . HEM H 3 .   ? 4.251   24.237  57.868 1.00 18.96 ? 142 HEM C CHA 1
+HETATM 4473 C  CHB . HEM H 3 .   ? 2.656   26.418  53.811 1.00 20.49 ? 142 HEM C CHB 1
+HETATM 4474 C  CHC . HEM H 3 .   ? 3.909   22.343  51.451 1.00 15.25 ? 142 HEM C CHC 1
+HETATM 4475 C  CHD . HEM H 3 .   ? 5.199   20.082  55.472 1.00 14.70 ? 142 HEM C CHD 1
+HETATM 4476 C  C1A . HEM H 3 .   ? 3.765   25.124  56.889 1.00 16.72 ? 142 HEM C C1A 1
+HETATM 4477 C  C2A . HEM H 3 .   ? 3.135   26.409  57.330 1.00 15.73 ? 142 HEM C C2A 1
+HETATM 4478 C  C3A . HEM H 3 .   ? 2.610   27.080  56.333 1.00 17.27 ? 142 HEM C C3A 1
+HETATM 4479 C  C4A . HEM H 3 .   ? 2.943   26.193  55.143 1.00 12.07 ? 142 HEM C C4A 1
+HETATM 4480 C  CMA . HEM H 3 .   ? 1.983   28.371  56.084 1.00 31.88 ? 142 HEM C CMA 1
+HETATM 4481 C  CAA . HEM H 3 .   ? 3.046   27.117  58.679 1.00 24.60 ? 142 HEM C CAA 1
+HETATM 4482 C  CBA . HEM H 3 .   ? 4.329   27.945  58.911 1.00 36.28 ? 142 HEM C CBA 1
+HETATM 4483 C  CGA . HEM H 3 .   ? 3.775   28.911  60.911 1.00 43.70 ? 142 HEM C CGA 1
+HETATM 4484 O  O1A . HEM H 3 .   ? 4.106   27.643  61.358 1.00 38.93 ? 142 HEM C O1A 1
+HETATM 4485 O  O2A . HEM H 3 .   ? 4.343   29.355  60.524 1.00 46.28 ? 142 HEM C O2A 1
+HETATM 4486 C  C1B . HEM H 3 .   ? 2.913   25.638  52.726 1.00 18.45 ? 142 HEM C C1B 1
+HETATM 4487 C  C2B . HEM H 3 .   ? 2.364   25.645  51.278 1.00 12.95 ? 142 HEM C C2B 1
+HETATM 4488 C  C3B . HEM H 3 .   ? 2.881   24.580  50.703 1.00 12.49 ? 142 HEM C C3B 1
+HETATM 4489 C  C4B . HEM H 3 .   ? 3.490   23.673  51.737 1.00 8.33  ? 142 HEM C C4B 1
+HETATM 4490 C  CMB . HEM H 3 .   ? 1.854   26.863  50.871 1.00 15.16 ? 142 HEM C CMB 1
+HETATM 4491 C  CAB . HEM H 3 .   ? 2.665   24.241  49.128 1.00 21.83 ? 142 HEM C CAB 1
+HETATM 4492 C  CBB . HEM H 3 .   ? 1.687   24.897  48.641 1.00 33.11 ? 142 HEM C CBB 1
+HETATM 4493 C  C1C . HEM H 3 .   ? 4.385   21.516  52.292 1.00 15.97 ? 142 HEM C C1C 1
+HETATM 4494 C  C2C . HEM H 3 .   ? 4.563   20.035  51.932 1.00 9.41  ? 142 HEM C C2C 1
+HETATM 4495 C  C3C . HEM H 3 .   ? 4.974   19.383  53.137 1.00 11.73 ? 142 HEM C C3C 1
+HETATM 4496 C  C4C . HEM H 3 .   ? 5.066   20.383  54.236 1.00 15.36 ? 142 HEM C C4C 1
+HETATM 4497 C  CMC . HEM H 3 .   ? 4.502   19.452  50.568 1.00 13.23 ? 142 HEM C CMC 1
+HETATM 4498 C  CAC . HEM H 3 .   ? 5.196   18.038  53.366 1.00 19.55 ? 142 HEM C CAC 1
+HETATM 4499 C  CBC . HEM H 3 .   ? 4.661   16.883  52.628 1.00 14.52 ? 142 HEM C CBC 1
+HETATM 4500 C  C1D . HEM H 3 .   ? 5.018   21.161  56.456 1.00 11.54 ? 142 HEM C C1D 1
+HETATM 4501 C  C2D . HEM H 3 .   ? 5.407   20.858  57.961 1.00 12.94 ? 142 HEM C C2D 1
+HETATM 4502 C  C3D . HEM H 3 .   ? 5.052   22.019  58.552 1.00 11.38 ? 142 HEM C C3D 1
+HETATM 4503 C  C4D . HEM H 3 .   ? 4.735   23.011  57.662 1.00 11.29 ? 142 HEM C C4D 1
+HETATM 4504 C  CMD . HEM H 3 .   ? 5.894   19.560  58.433 1.00 13.29 ? 142 HEM C CMD 1
+HETATM 4505 C  CAD . HEM H 3 .   ? 5.092   22.124  60.147 1.00 15.84 ? 142 HEM C CAD 1
+HETATM 4506 C  CBD . HEM H 3 .   ? 3.813   21.818  60.637 1.00 21.27 ? 142 HEM C CBD 1
+HETATM 4507 C  CGD . HEM H 3 .   ? 3.734   22.247  62.515 1.00 26.94 ? 142 HEM C CGD 1
+HETATM 4508 O  O1D . HEM H 3 .   ? 2.827   22.571  62.603 1.00 30.21 ? 142 HEM C O1D 1
+HETATM 4509 O  O2D . HEM H 3 .   ? 4.388   21.393  62.880 1.00 25.95 ? 142 HEM C O2D 1
+HETATM 4510 N  NA  . HEM H 3 .   ? 3.598   25.067  55.570 1.00 16.55 ? 142 HEM C NA  1
+HETATM 4511 N  NB  . HEM H 3 .   ? 3.462   24.312  52.870 1.00 12.79 ? 142 HEM C NB  1
+HETATM 4512 N  NC  . HEM H 3 .   ? 4.712   21.591  53.665 1.00 12.28 ? 142 HEM C NC  1
+HETATM 4513 N  ND  . HEM H 3 .   ? 4.793   22.519  56.403 1.00 12.30 ? 142 HEM C ND  1
+HETATM 4514 FE FE  . HEM H 3 .   ? 4.445   23.463  54.548 1.00 16.89 ? 142 HEM C FE  1
+HETATM 4515 P  P   . PO4 I 4 .   ? 0.748   -6.346  38.809 1.00 31.17 ? 147 PO4 D P   1
+HETATM 4516 C  CHA . HEM J 3 .   ? -2.352  3.877   20.823 1.00 19.84 ? 148 HEM D CHA 1
+HETATM 4517 C  CHB . HEM J 3 .   ? -3.814  2.360   25.062 1.00 16.61 ? 148 HEM D CHB 1
+HETATM 4518 C  CHC . HEM J 3 .   ? -1.791  5.984   27.129 1.00 13.93 ? 148 HEM D CHC 1
+HETATM 4519 C  CHD . HEM J 3 .   ? 0.009   7.659   22.833 1.00 15.88 ? 148 HEM D CHD 1
+HETATM 4520 C  C1A . HEM J 3 .   ? -3.051  3.076   21.759 1.00 28.09 ? 148 HEM D C1A 1
+HETATM 4521 C  C2A . HEM J 3 .   ? -4.147  1.993   21.447 1.00 22.30 ? 148 HEM D C2A 1
+HETATM 4522 C  C3A . HEM J 3 .   ? -4.533  1.556   22.586 1.00 22.59 ? 148 HEM D C3A 1
+HETATM 4523 C  C4A . HEM J 3 .   ? -3.678  2.444   23.644 1.00 25.38 ? 148 HEM D C4A 1
+HETATM 4524 C  CMA . HEM J 3 .   ? -5.548  0.622   22.950 1.00 20.23 ? 148 HEM D CMA 1
+HETATM 4525 C  CAA . HEM J 3 .   ? -4.487  1.500   19.875 1.00 19.24 ? 148 HEM D CAA 1
+HETATM 4526 C  CBA . HEM J 3 .   ? -3.521  0.804   19.553 1.00 50.08 ? 148 HEM D CBA 1
+HETATM 4527 C  CGA . HEM J 3 .   ? -3.140  0.203   17.272 1.00 47.00 ? 148 HEM D CGA 1
+HETATM 4528 O  O1A . HEM J 3 .   ? -4.454  0.157   17.696 1.00 49.99 ? 148 HEM D O1A 1
+HETATM 4529 O  O2A . HEM J 3 .   ? -2.759  -1.510  17.524 1.00 55.24 ? 148 HEM D O2A 1
+HETATM 4530 C  C1B . HEM J 3 .   ? -3.322  3.050   26.126 1.00 14.32 ? 148 HEM D C1B 1
+HETATM 4531 C  C2B . HEM J 3 .   ? -3.550  3.027   27.437 1.00 15.75 ? 148 HEM D C2B 1
+HETATM 4532 C  C3B . HEM J 3 .   ? -2.926  3.983   28.016 1.00 14.95 ? 148 HEM D C3B 1
+HETATM 4533 C  C4B . HEM J 3 .   ? -2.272  4.739   26.961 1.00 12.78 ? 148 HEM D C4B 1
+HETATM 4534 C  CMB . HEM J 3 .   ? -4.267  1.954   27.997 1.00 18.74 ? 148 HEM D CMB 1
+HETATM 4535 C  CAB . HEM J 3 .   ? -2.846  4.354   29.573 1.00 16.19 ? 148 HEM D CAB 1
+HETATM 4536 C  CBB . HEM J 3 .   ? -3.708  4.424   30.032 1.00 34.22 ? 148 HEM D CBB 1
+HETATM 4537 C  C1C . HEM J 3 .   ? -1.235  6.715   26.253 1.00 14.15 ? 148 HEM D C1C 1
+HETATM 4538 C  C2C . HEM J 3 .   ? -0.436  8.144   26.363 1.00 16.84 ? 148 HEM D C2C 1
+HETATM 4539 C  C3C . HEM J 3 .   ? 0.127   8.530   25.154 1.00 13.21 ? 148 HEM D C3C 1
+HETATM 4540 C  C4C . HEM J 3 .   ? -0.351  7.466   24.259 1.00 15.07 ? 148 HEM D C4C 1
+HETATM 4541 C  CMC . HEM J 3 .   ? -0.442  8.954   27.749 1.00 18.77 ? 148 HEM D CMC 1
+HETATM 4542 C  CAC . HEM J 3 .   ? 0.809   9.659   24.837 1.00 13.84 ? 148 HEM D CAC 1
+HETATM 4543 C  CBC . HEM J 3 .   ? 0.524   10.806  25.274 1.00 20.77 ? 148 HEM D CBC 1
+HETATM 4544 C  C1D . HEM J 3 .   ? -0.498  6.544   21.800 1.00 18.28 ? 148 HEM D C1D 1
+HETATM 4545 C  C2D . HEM J 3 .   ? -0.447  6.890   20.467 1.00 20.40 ? 148 HEM D C2D 1
+HETATM 4546 C  C3D . HEM J 3 .   ? -1.152  5.676   19.845 1.00 19.16 ? 148 HEM D C3D 1
+HETATM 4547 C  C4D . HEM J 3 .   ? -1.929  5.008   20.769 1.00 19.80 ? 148 HEM D C4D 1
+HETATM 4548 C  CMD . HEM J 3 .   ? 0.398   7.913   19.789 1.00 25.65 ? 148 HEM D CMD 1
+HETATM 4549 C  CAD . HEM J 3 .   ? -1.337  5.671   18.300 1.00 23.94 ? 148 HEM D CAD 1
+HETATM 4550 C  CBD . HEM J 3 .   ? -2.315  6.581   17.878 1.00 45.78 ? 148 HEM D CBD 1
+HETATM 4551 C  CGD . HEM J 3 .   ? -3.042  6.103   16.062 1.00 48.49 ? 148 HEM D CGD 1
+HETATM 4552 O  O1D . HEM J 3 .   ? -2.171  7.406   15.697 1.00 40.71 ? 148 HEM D O1D 1
+HETATM 4553 O  O2D . HEM J 3 .   ? -2.568  5.381   15.796 1.00 45.79 ? 148 HEM D O2D 1
+HETATM 4554 N  NA  . HEM J 3 .   ? -2.975  3.248   23.071 1.00 15.98 ? 148 HEM D NA  1
+HETATM 4555 N  NB  . HEM J 3 .   ? -2.569  4.252   25.747 1.00 14.27 ? 148 HEM D NB  1
+HETATM 4556 N  NC  . HEM J 3 .   ? -1.102  6.496   24.910 1.00 12.21 ? 148 HEM D NC  1
+HETATM 4557 N  ND  . HEM J 3 .   ? -1.471  5.558   22.069 1.00 12.94 ? 148 HEM D ND  1
+HETATM 4558 FE FE  . HEM J 3 .   ? -1.727  4.699   23.942 1.00 15.46 ? 148 HEM D FE  1
+HETATM 4559 O  O   . HOH K 5 .   ? 37.888  9.993   38.795 1.00 21.15 ? 143 HOH A O   1
+HETATM 4560 O  O   . HOH K 5 .   ? 20.373  15.891  24.675 1.00 29.96 ? 144 HOH A O   1
+HETATM 4561 O  O   . HOH K 5 .   ? 25.776  7.463   13.007 1.00 23.65 ? 145 HOH A O   1
+HETATM 4562 O  O   . HOH K 5 .   ? 24.502  13.916  42.712 1.00 23.17 ? 146 HOH A O   1
+HETATM 4563 O  O   . HOH K 5 .   ? 29.383  24.405  46.762 1.00 26.86 ? 147 HOH A O   1
+HETATM 4564 O  O   . HOH K 5 .   ? 34.557  20.187  49.190 1.00 30.53 ? 148 HOH A O   1
+HETATM 4565 O  O   . HOH K 5 .   ? 35.010  7.121   31.358 1.00 27.68 ? 149 HOH A O   1
+HETATM 4566 O  O   . HOH K 5 .   ? 22.109  15.053  39.415 1.00 27.27 ? 150 HOH A O   1
+HETATM 4567 O  O   . HOH K 5 .   ? 41.542  15.549  37.394 1.00 29.31 ? 151 HOH A O   1
+HETATM 4568 O  O   . HOH K 5 .   ? 6.591   15.493  33.957 1.00 29.54 ? 152 HOH A O   1
+HETATM 4569 O  O   . HOH K 5 .   ? 44.159  19.200  43.061 1.00 35.74 ? 153 HOH A O   1
+HETATM 4570 O  O   . HOH K 5 .   ? 46.081  18.856  41.009 1.00 31.58 ? 154 HOH A O   1
+HETATM 4571 O  O   . HOH K 5 .   ? 39.830  9.144   36.957 1.00 37.73 ? 155 HOH A O   1
+HETATM 4572 O  O   . HOH K 5 .   ? 32.698  23.417  24.374 1.00 37.58 ? 156 HOH A O   1
+HETATM 4573 O  O   . HOH K 5 .   ? 21.214  18.454  38.464 1.00 29.83 ? 157 HOH A O   1
+HETATM 4574 O  O   . HOH K 5 .   ? 37.402  8.158   32.867 1.00 34.75 ? 158 HOH A O   1
+HETATM 4575 O  O   . HOH K 5 .   ? 21.828  16.575  16.931 1.00 35.95 ? 159 HOH A O   1
+HETATM 4576 O  O   . HOH K 5 .   ? 11.595  25.926  27.182 1.00 27.36 ? 160 HOH A O   1
+HETATM 4577 O  O   . HOH K 5 .   ? 14.533  4.664   32.017 1.00 27.80 ? 161 HOH A O   1
+HETATM 4578 O  O   . HOH K 5 .   ? 9.537   10.066  20.163 1.00 29.65 ? 162 HOH A O   1
+HETATM 4579 O  O   . HOH K 5 .   ? 5.313   22.342  25.119 1.00 30.27 ? 163 HOH A O   1
+HETATM 4580 O  O   . HOH K 5 .   ? 15.518  30.976  27.654 1.00 37.13 ? 164 HOH A O   1
+HETATM 4581 O  O   . HOH K 5 .   ? 19.771  14.847  38.487 1.00 31.92 ? 165 HOH A O   1
+HETATM 4582 O  O   . HOH K 5 .   ? 12.544  12.993  19.238 1.00 30.86 ? 166 HOH A O   1
+HETATM 4583 O  O   . HOH K 5 .   ? 18.314  18.718  36.329 1.00 34.91 ? 167 HOH A O   1
+HETATM 4584 O  O   . HOH K 5 .   ? 21.272  32.967  34.644 1.00 34.13 ? 168 HOH A O   1
+HETATM 4585 O  O   . HOH K 5 .   ? 31.580  13.773  20.641 1.00 36.10 ? 169 HOH A O   1
+HETATM 4586 O  O   . HOH K 5 .   ? 25.219  33.314  23.876 1.00 37.77 ? 170 HOH A O   1
+HETATM 4587 O  O   . HOH K 5 .   ? 39.072  15.237  45.020 1.00 39.01 ? 171 HOH A O   1
+HETATM 4588 O  O   . HOH K 5 .   ? 25.087  3.887   32.134 1.00 35.74 ? 172 HOH A O   1
+HETATM 4589 O  O   . HOH K 5 .   ? 28.205  5.638   21.827 1.00 36.03 ? 173 HOH A O   1
+HETATM 4590 O  O   . HOH K 5 .   ? 25.438  23.710  20.569 1.00 34.06 ? 174 HOH A O   1
+HETATM 4591 O  O   . HOH K 5 .   ? 40.122  11.821  32.127 1.00 35.04 ? 175 HOH A O   1
+HETATM 4592 O  O   . HOH K 5 .   ? 19.516  17.834  41.431 1.00 38.02 ? 176 HOH A O   1
+HETATM 4593 O  O   . HOH K 5 .   ? 4.438   24.846  21.275 1.00 39.72 ? 177 HOH A O   1
+HETATM 4594 O  O   . HOH K 5 .   ? 20.519  29.238  22.425 1.00 36.40 ? 178 HOH A O   1
+HETATM 4595 O  O   . HOH K 5 .   ? 26.629  25.655  46.764 1.00 37.52 ? 179 HOH A O   1
+HETATM 4596 O  O   . HOH K 5 .   ? 28.756  23.927  49.037 1.00 38.53 ? 180 HOH A O   1
+HETATM 4597 O  O   . HOH K 5 .   ? 13.609  18.788  35.045 1.00 42.85 ? 181 HOH A O   1
+HETATM 4598 O  O   . HOH K 5 .   ? 19.804  31.795  21.957 1.00 39.27 ? 182 HOH A O   1
+HETATM 4599 O  O   . HOH K 5 .   ? 19.738  0.604   34.452 1.00 38.61 ? 183 HOH A O   1
+HETATM 4600 O  O   . HOH K 5 .   ? 40.002  12.304  29.233 1.00 34.80 ? 184 HOH A O   1
+HETATM 4601 O  O   . HOH K 5 .   ? 34.849  9.935   27.178 1.00 42.30 ? 185 HOH A O   1
+HETATM 4602 O  O   . HOH K 5 .   ? 6.928   26.078  31.763 1.00 38.29 ? 186 HOH A O   1
+HETATM 4603 O  O   . HOH K 5 .   ? 36.929  29.682  38.432 1.00 39.37 ? 187 HOH A O   1
+HETATM 4604 O  O   . HOH K 5 .   ? 38.089  21.581  42.434 1.00 40.95 ? 188 HOH A O   1
+HETATM 4605 O  O   . HOH K 5 .   ? 28.217  35.466  32.478 1.00 41.35 ? 189 HOH A O   1
+HETATM 4606 O  O   . HOH K 5 .   ? 24.184  14.780  15.600 1.00 37.45 ? 190 HOH A O   1
+HETATM 4607 O  O   . HOH K 5 .   ? 24.733  4.657   22.757 1.00 39.12 ? 191 HOH A O   1
+HETATM 4608 O  O   . HOH K 5 .   ? 15.163  4.312   20.071 1.00 38.62 ? 192 HOH A O   1
+HETATM 4609 O  O   . HOH K 5 .   ? 31.681  5.918   25.911 1.00 37.05 ? 193 HOH A O   1
+HETATM 4610 O  O   . HOH K 5 .   ? 32.746  9.738   24.118 1.00 36.25 ? 194 HOH A O   1
+HETATM 4611 O  O   . HOH K 5 .   ? 35.759  16.236  22.395 1.00 35.85 ? 195 HOH A O   1
+HETATM 4612 O  O   . HOH K 5 .   ? 41.892  24.480  29.906 1.00 37.62 ? 196 HOH A O   1
+HETATM 4613 O  O   . HOH K 5 .   ? 40.074  25.608  35.391 1.00 42.54 ? 197 HOH A O   1
+HETATM 4614 O  O   . HOH K 5 .   ? 21.268  31.043  38.701 1.00 39.90 ? 198 HOH A O   1
+HETATM 4615 O  O   . HOH L 5 .   ? 11.128  12.595  56.195 1.00 21.64 ? 149 HOH B O   1
+HETATM 4616 O  O   . HOH L 5 .   ? 4.568   6.649   55.777 1.00 29.94 ? 150 HOH B O   1
+HETATM 4617 O  O   . HOH L 5 .   ? 24.881  -3.365  32.126 1.00 26.33 ? 151 HOH B O   1
+HETATM 4618 O  O   . HOH L 5 .   ? 18.928  3.797   39.407 1.00 27.87 ? 152 HOH B O   1
+HETATM 4619 O  O   . HOH L 5 .   ? 34.402  4.205   31.402 1.00 33.60 ? 153 HOH B O   1
+HETATM 4620 O  O   . HOH L 5 .   ? 39.801  1.973   38.725 1.00 27.86 ? 154 HOH B O   1
+HETATM 4621 O  O   . HOH L 5 .   ? 19.755  3.283   47.405 1.00 34.89 ? 155 HOH B O   1
+HETATM 4622 O  O   . HOH L 5 .   ? 10.933  -4.798  51.901 1.00 29.82 ? 156 HOH B O   1
+HETATM 4623 O  O   . HOH L 5 .   ? 35.020  -2.241  34.118 1.00 34.30 ? 157 HOH B O   1
+HETATM 4624 O  O   . HOH L 5 .   ? 13.498  -4.239  45.190 1.00 29.36 ? 158 HOH B O   1
+HETATM 4625 O  O   . HOH L 5 .   ? 40.077  7.217   34.998 1.00 34.23 ? 159 HOH B O   1
+HETATM 4626 O  O   . HOH L 5 .   ? 29.074  -7.819  49.640 1.00 34.06 ? 160 HOH B O   1
+HETATM 4627 O  O   . HOH L 5 .   ? 14.523  10.491  62.823 1.00 34.98 ? 161 HOH B O   1
+HETATM 4628 O  O   . HOH L 5 .   ? 35.156  18.919  51.618 1.00 34.02 ? 162 HOH B O   1
+HETATM 4629 O  O   . HOH L 5 .   ? 20.480  12.891  42.183 1.00 33.29 ? 163 HOH B O   1
+HETATM 4630 O  O   . HOH L 5 .   ? 25.633  -1.926  59.302 1.00 32.12 ? 164 HOH B O   1
+HETATM 4631 O  O   . HOH L 5 .   ? 6.897   7.942   59.455 1.00 35.56 ? 165 HOH B O   1
+HETATM 4632 O  O   . HOH L 5 .   ? 18.863  6.507   42.991 1.00 34.98 ? 166 HOH B O   1
+HETATM 4633 O  O   . HOH L 5 .   ? 33.339  -4.585  36.966 1.00 37.65 ? 167 HOH B O   1
+HETATM 4634 O  O   . HOH L 5 .   ? 8.784   -0.051  46.972 1.00 34.45 ? 168 HOH B O   1
+HETATM 4635 O  O   . HOH L 5 .   ? 34.155  -4.557  49.753 1.00 33.37 ? 169 HOH B O   1
+HETATM 4636 O  O   . HOH L 5 .   ? 44.085  3.217   28.983 1.00 35.71 ? 170 HOH B O   1
+HETATM 4637 O  O   . HOH L 5 .   ? 33.378  18.493  61.599 1.00 38.68 ? 171 HOH B O   1
+HETATM 4638 O  O   . HOH L 5 .   ? 29.832  -6.934  53.230 1.00 40.56 ? 172 HOH B O   1
+HETATM 4639 O  O   . HOH L 5 .   ? 16.083  -5.618  57.345 1.00 34.56 ? 173 HOH B O   1
+HETATM 4640 O  O   . HOH L 5 .   ? 8.449   4.205   70.977 1.00 36.28 ? 174 HOH B O   1
+HETATM 4641 O  O   . HOH L 5 .   ? 24.303  6.250   63.399 1.00 31.60 ? 175 HOH B O   1
+HETATM 4642 O  O   . HOH L 5 .   ? 32.258  -8.412  46.041 1.00 34.00 ? 176 HOH B O   1
+HETATM 4643 O  O   . HOH L 5 .   ? 16.542  9.589   63.860 1.00 36.71 ? 177 HOH B O   1
+HETATM 4644 O  O   . HOH L 5 .   ? 26.846  7.823   63.995 1.00 34.84 ? 178 HOH B O   1
+HETATM 4645 O  O   . HOH L 5 .   ? 33.275  11.732  55.070 1.00 33.20 ? 179 HOH B O   1
+HETATM 4646 O  O   . HOH L 5 .   ? 26.143  -5.553  30.845 1.00 37.19 ? 180 HOH B O   1
+HETATM 4647 O  O   . HOH L 5 .   ? 32.661  -2.801  31.194 1.00 35.87 ? 181 HOH B O   1
+HETATM 4648 O  O   . HOH L 5 .   ? -1.108  3.263   54.042 1.00 36.08 ? 182 HOH B O   1
+HETATM 4649 O  O   . HOH L 5 .   ? 25.210  22.546  61.505 1.00 38.22 ? 183 HOH B O   1
+HETATM 4650 O  O   . HOH L 5 .   ? 20.243  19.412  60.923 1.00 43.17 ? 184 HOH B O   1
+HETATM 4651 O  O   . HOH L 5 .   ? 38.545  -4.028  49.497 1.00 36.03 ? 185 HOH B O   1
+HETATM 4652 O  O   . HOH L 5 .   ? 21.918  -5.838  54.913 1.00 39.57 ? 186 HOH B O   1
+HETATM 4653 O  O   . HOH L 5 .   ? 35.351  20.809  61.223 1.00 37.45 ? 187 HOH B O   1
+HETATM 4654 O  O   . HOH L 5 .   ? 4.494   0.683   50.042 1.00 38.65 ? 188 HOH B O   1
+HETATM 4655 O  O   . HOH L 5 .   ? 26.253  27.350  57.373 1.00 36.93 ? 189 HOH B O   1
+HETATM 4656 O  O   . HOH L 5 .   ? 36.795  17.395  55.779 1.00 42.01 ? 190 HOH B O   1
+HETATM 4657 O  O   . HOH L 5 .   ? 16.456  -9.430  57.455 1.00 42.33 ? 191 HOH B O   1
+HETATM 4658 O  O   . HOH L 5 .   ? 2.494   5.651   59.158 1.00 38.06 ? 192 HOH B O   1
+HETATM 4659 O  O   . HOH L 5 .   ? 21.544  3.059   64.833 1.00 39.34 ? 193 HOH B O   1
+HETATM 4660 O  O   . HOH L 5 .   ? 13.594  9.764   42.687 1.00 42.17 ? 194 HOH B O   1
+HETATM 4661 O  O   . HOH L 5 .   ? 13.423  12.708  41.803 1.00 41.40 ? 195 HOH B O   1
+HETATM 4662 O  O   . HOH L 5 .   ? 11.664  -11.409 54.888 1.00 39.83 ? 196 HOH B O   1
+HETATM 4663 O  O   . HOH L 5 .   ? 15.794  -8.681  44.890 1.00 43.08 ? 197 HOH B O   1
+HETATM 4664 O  O   . HOH L 5 .   ? 33.903  7.800   62.887 1.00 38.10 ? 198 HOH B O   1
+HETATM 4665 O  O   . HOH L 5 .   ? 24.476  23.079  58.818 1.00 40.23 ? 199 HOH B O   1
+HETATM 4666 O  O   . HOH L 5 .   ? 30.912  18.554  65.903 1.00 39.03 ? 200 HOH B O   1
+HETATM 4667 O  O   . HOH L 5 .   ? 24.493  22.373  47.998 1.00 44.34 ? 201 HOH B O   1
+HETATM 4668 O  O   . HOH L 5 .   ? 35.356  8.568   53.861 1.00 39.78 ? 202 HOH B O   1
+HETATM 4669 O  O   . HOH L 5 .   ? 35.213  11.168  53.150 1.00 42.94 ? 203 HOH B O   1
+HETATM 4670 O  O   . HOH L 5 .   ? 31.256  -6.939  51.106 1.00 53.60 ? 204 HOH B O   1
+HETATM 4671 O  O   . HOH L 5 .   ? 32.523  -11.687 46.706 1.00 45.18 ? 205 HOH B O   1
+HETATM 4672 O  O   . HOH M 5 .   ? 7.751   11.347  49.533 1.00 21.26 ? 143 HOH C O   1
+HETATM 4673 O  O   . HOH M 5 .   ? 13.211  27.616  49.941 1.00 21.54 ? 144 HOH C O   1
+HETATM 4674 O  O   . HOH M 5 .   ? -4.882  28.113  30.481 1.00 23.30 ? 145 HOH C O   1
+HETATM 4675 O  O   . HOH M 5 .   ? -3.201  18.008  36.389 1.00 22.15 ? 146 HOH C O   1
+HETATM 4676 O  O   . HOH M 5 .   ? 17.864  22.968  52.831 1.00 28.02 ? 147 HOH C O   1
+HETATM 4677 O  O   . HOH M 5 .   ? -0.515  18.947  39.771 1.00 32.97 ? 148 HOH C O   1
+HETATM 4678 O  O   . HOH M 5 .   ? 1.730   21.367  54.232 1.00 33.04 ? 149 HOH C O   1
+HETATM 4679 O  O   . HOH M 5 .   ? 3.755   21.742  41.935 1.00 27.40 ? 150 HOH C O   1
+HETATM 4680 O  O   . HOH M 5 .   ? 10.212  13.984  60.044 1.00 29.84 ? 151 HOH C O   1
+HETATM 4681 O  O   . HOH M 5 .   ? 13.373  14.314  54.110 1.00 30.74 ? 152 HOH C O   1
+HETATM 4682 O  O   . HOH M 5 .   ? 12.514  34.126  57.906 1.00 29.22 ? 153 HOH C O   1
+HETATM 4683 O  O   . HOH M 5 .   ? -7.488  31.948  53.044 1.00 32.40 ? 154 HOH C O   1
+HETATM 4684 O  O   . HOH M 5 .   ? 1.816   18.203  40.742 1.00 28.46 ? 155 HOH C O   1
+HETATM 4685 O  O   . HOH M 5 .   ? 13.300  26.579  43.284 1.00 38.51 ? 156 HOH C O   1
+HETATM 4686 O  O   . HOH M 5 .   ? 5.712   34.152  54.021 1.00 35.20 ? 157 HOH C O   1
+HETATM 4687 O  O   . HOH M 5 .   ? 8.626   17.379  60.182 1.00 39.88 ? 158 HOH C O   1
+HETATM 4688 O  O   . HOH M 5 .   ? 7.723   10.076  47.130 1.00 36.39 ? 159 HOH C O   1
+HETATM 4689 O  O   . HOH M 5 .   ? 1.492   22.040  40.040 1.00 29.81 ? 160 HOH C O   1
+HETATM 4690 O  O   . HOH M 5 .   ? 13.101  36.241  54.430 1.00 33.74 ? 161 HOH C O   1
+HETATM 4691 O  O   . HOH M 5 .   ? 9.603   39.282  52.951 1.00 31.03 ? 162 HOH C O   1
+HETATM 4692 O  O   . HOH M 5 .   ? 14.492  15.367  45.494 1.00 29.72 ? 163 HOH C O   1
+HETATM 4693 O  O   . HOH M 5 .   ? 0.674   23.849  61.430 1.00 31.11 ? 164 HOH C O   1
+HETATM 4694 O  O   . HOH M 5 .   ? -0.437  31.011  56.519 1.00 30.77 ? 165 HOH C O   1
+HETATM 4695 O  O   . HOH M 5 .   ? -5.841  12.908  69.172 1.00 34.94 ? 166 HOH C O   1
+HETATM 4696 O  O   . HOH M 5 .   ? 10.707  32.085  58.456 1.00 34.58 ? 167 HOH C O   1
+HETATM 4697 O  O   . HOH M 5 .   ? -6.360  10.359  48.509 1.00 37.69 ? 168 HOH C O   1
+HETATM 4698 O  O   . HOH M 5 .   ? 4.625   27.341  36.340 1.00 34.39 ? 169 HOH C O   1
+HETATM 4699 O  O   . HOH M 5 .   ? 7.609   23.434  40.703 1.00 35.72 ? 170 HOH C O   1
+HETATM 4700 O  O   . HOH M 5 .   ? -15.101 16.635  48.609 1.00 32.50 ? 171 HOH C O   1
+HETATM 4701 O  O   . HOH M 5 .   ? 1.395   10.768  62.783 1.00 37.91 ? 172 HOH C O   1
+HETATM 4702 O  O   . HOH M 5 .   ? -2.069  22.416  63.264 1.00 36.81 ? 173 HOH C O   1
+HETATM 4703 O  O   . HOH M 5 .   ? -2.553  35.887  28.536 1.00 37.83 ? 174 HOH C O   1
+HETATM 4704 O  O   . HOH M 5 .   ? 5.645   36.313  41.309 1.00 35.70 ? 175 HOH C O   1
+HETATM 4705 O  O   . HOH M 5 .   ? 8.976   39.311  44.837 1.00 37.22 ? 176 HOH C O   1
+HETATM 4706 O  O   . HOH M 5 .   ? -10.754 30.936  31.207 1.00 34.30 ? 177 HOH C O   1
+HETATM 4707 O  O   . HOH M 5 .   ? -1.542  31.519  29.019 1.00 36.92 ? 178 HOH C O   1
+HETATM 4708 O  O   . HOH M 5 .   ? -6.187  36.528  47.282 1.00 34.30 ? 179 HOH C O   1
+HETATM 4709 O  O   . HOH M 5 .   ? 14.576  28.773  42.003 1.00 39.46 ? 180 HOH C O   1
+HETATM 4710 O  O   . HOH M 5 .   ? 11.133  33.696  48.526 1.00 37.49 ? 181 HOH C O   1
+HETATM 4711 O  O   . HOH M 5 .   ? 9.712   15.953  61.943 1.00 39.39 ? 182 HOH C O   1
+HETATM 4712 O  O   . HOH M 5 .   ? 20.931  25.461  52.434 1.00 34.40 ? 183 HOH C O   1
+HETATM 4713 O  O   . HOH M 5 .   ? 8.831   20.378  43.601 1.00 37.01 ? 184 HOH C O   1
+HETATM 4714 O  O   . HOH M 5 .   ? 18.338  22.987  42.474 1.00 35.17 ? 185 HOH C O   1
+HETATM 4715 O  O   . HOH M 5 .   ? 7.617   36.913  53.764 1.00 35.39 ? 186 HOH C O   1
+HETATM 4716 O  O   . HOH M 5 .   ? 3.667   33.827  55.220 1.00 39.95 ? 187 HOH C O   1
+HETATM 4717 O  O   . HOH M 5 .   ? 7.629   27.241  38.175 1.00 39.36 ? 188 HOH C O   1
+HETATM 4718 O  O   . HOH M 5 .   ? 5.014   8.798   46.167 1.00 40.89 ? 189 HOH C O   1
+HETATM 4719 O  O   . HOH M 5 .   ? 17.289  25.478  45.992 1.00 40.24 ? 190 HOH C O   1
+HETATM 4720 O  O   . HOH M 5 .   ? 8.302   30.847  40.892 1.00 36.37 ? 191 HOH C O   1
+HETATM 4721 O  O   . HOH M 5 .   ? 11.029  25.526  38.376 1.00 43.19 ? 192 HOH C O   1
+HETATM 4722 O  O   . HOH M 5 .   ? -8.186  9.686   56.832 1.00 35.55 ? 193 HOH C O   1
+HETATM 4723 O  O   . HOH M 5 .   ? 19.363  23.556  54.792 1.00 41.86 ? 194 HOH C O   1
+HETATM 4724 O  O   . HOH M 5 .   ? 14.769  37.111  51.861 1.00 43.02 ? 195 HOH C O   1
+HETATM 4725 O  O   . HOH M 5 .   ? 1.115   18.145  68.757 1.00 44.30 ? 196 HOH C O   1
+HETATM 4726 O  O   . HOH M 5 .   ? -10.016 7.592   56.161 1.00 40.17 ? 197 HOH C O   1
+HETATM 4727 O  O   . HOH M 5 .   ? 3.770   10.254  60.803 1.00 36.98 ? 198 HOH C O   1
+HETATM 4728 O  O   . HOH M 5 .   ? -12.098 19.754  55.112 1.00 33.31 ? 199 HOH C O   1
+HETATM 4729 O  O   . HOH M 5 .   ? -21.425 27.959  52.014 1.00 40.72 ? 200 HOH C O   1
+HETATM 4730 O  O   . HOH M 5 .   ? -2.250  28.436  30.695 1.00 43.21 ? 201 HOH C O   1
+HETATM 4731 O  O   . HOH N 5 .   ? 8.809   9.921   23.769 1.00 18.64 ? 149 HOH D O   1
+HETATM 4732 O  O   . HOH N 5 .   ? -1.782  -5.584  26.029 1.00 26.28 ? 150 HOH D O   1
+HETATM 4733 O  O   . HOH N 5 .   ? 11.814  8.780   30.485 1.00 23.08 ? 151 HOH D O   1
+HETATM 4734 O  O   . HOH N 5 .   ? 6.812   12.848  25.929 1.00 25.33 ? 152 HOH D O   1
+HETATM 4735 O  O   . HOH N 5 .   ? -0.557  7.407   41.880 1.00 30.48 ? 153 HOH D O   1
+HETATM 4736 O  O   . HOH N 5 .   ? -0.700  -8.692  26.698 1.00 34.60 ? 154 HOH D O   1
+HETATM 4737 O  O   . HOH N 5 .   ? -8.364  3.835   50.374 1.00 35.82 ? 155 HOH D O   1
+HETATM 4738 O  O   . HOH N 5 .   ? 13.063  2.419   25.471 1.00 27.68 ? 156 HOH D O   1
+HETATM 4739 O  O   . HOH N 5 .   ? -1.004  -10.790 23.437 1.00 35.93 ? 157 HOH D O   1
+HETATM 4740 O  O   . HOH N 5 .   ? 0.559   20.840  18.695 1.00 40.04 ? 158 HOH D O   1
+HETATM 4741 O  O   . HOH N 5 .   ? -8.450  9.149   16.631 1.00 32.57 ? 159 HOH D O   1
+HETATM 4742 O  O   . HOH N 5 .   ? 0.263   0.823   42.760 1.00 34.30 ? 160 HOH D O   1
+HETATM 4743 O  O   . HOH N 5 .   ? 5.703   13.936  28.226 1.00 34.78 ? 161 HOH D O   1
+HETATM 4744 O  O   . HOH N 5 .   ? -19.146 17.851  37.080 1.00 38.63 ? 162 HOH D O   1
+HETATM 4745 O  O   . HOH N 5 .   ? -18.092 1.509   32.880 1.00 33.22 ? 163 HOH D O   1
+HETATM 4746 O  O   . HOH N 5 .   ? 3.383   -5.740  20.675 1.00 35.47 ? 164 HOH D O   1
+HETATM 4747 O  O   . HOH N 5 .   ? 3.848   -5.540  31.013 1.00 30.23 ? 165 HOH D O   1
+HETATM 4748 O  O   . HOH N 5 .   ? -15.238 14.046  49.265 1.00 34.33 ? 166 HOH D O   1
+HETATM 4749 O  O   . HOH N 5 .   ? -2.598  5.396   46.962 1.00 38.68 ? 167 HOH D O   1
+HETATM 4750 O  O   . HOH N 5 .   ? 0.334   15.342  37.427 1.00 38.71 ? 168 HOH D O   1
+HETATM 4751 O  O   . HOH N 5 .   ? -16.856 4.135   45.005 1.00 36.60 ? 169 HOH D O   1
+HETATM 4752 O  O   . HOH N 5 .   ? 1.932   -2.877  37.452 1.00 34.43 ? 170 HOH D O   1
+HETATM 4753 O  O   . HOH N 5 .   ? 10.577  1.360   32.224 1.00 35.73 ? 171 HOH D O   1
+HETATM 4754 O  O   . HOH N 5 .   ? 14.306  0.292   22.332 1.00 32.39 ? 172 HOH D O   1
+HETATM 4755 O  O   . HOH N 5 .   ? -0.157  8.668   37.948 1.00 35.44 ? 173 HOH D O   1
+HETATM 4756 O  O   . HOH N 5 .   ? -10.003 -2.568  25.000 1.00 41.02 ? 174 HOH D O   1
+HETATM 4757 O  O   . HOH N 5 .   ? 0.016   9.621   16.373 1.00 37.14 ? 175 HOH D O   1
+HETATM 4758 O  O   . HOH N 5 .   ? -9.704  -0.129  23.261 1.00 34.89 ? 176 HOH D O   1
+HETATM 4759 O  O   . HOH N 5 .   ? 11.139  3.698   21.463 1.00 35.94 ? 177 HOH D O   1
+HETATM 4760 O  O   . HOH N 5 .   ? -15.230 6.969   50.970 1.00 38.01 ? 178 HOH D O   1
+HETATM 4761 O  O   . HOH N 5 .   ? 11.302  8.473   33.609 1.00 38.51 ? 179 HOH D O   1
+HETATM 4762 O  O   . HOH N 5 .   ? -21.938 1.645   40.956 1.00 36.37 ? 180 HOH D O   1
+HETATM 4763 O  O   . HOH N 5 .   ? 2.996   21.345  21.800 1.00 34.05 ? 181 HOH D O   1
+HETATM 4764 O  O   . HOH N 5 .   ? -14.402 16.687  25.951 1.00 39.14 ? 182 HOH D O   1
+HETATM 4765 O  O   . HOH N 5 .   ? -0.902  24.449  29.458 1.00 38.30 ? 183 HOH D O   1
+HETATM 4766 O  O   . HOH N 5 .   ? 2.391   9.196   16.953 1.00 36.68 ? 184 HOH D O   1
+HETATM 4767 O  O   . HOH N 5 .   ? 3.776   4.597   38.067 1.00 37.10 ? 185 HOH D O   1
+HETATM 4768 O  O   . HOH N 5 .   ? -14.891 10.992  17.341 1.00 37.97 ? 186 HOH D O   1
+HETATM 4769 O  O   . HOH N 5 .   ? -1.920  5.319   34.309 1.00 38.85 ? 187 HOH D O   1
+HETATM 4770 O  O   . HOH N 5 .   ? 1.297   6.235   43.512 1.00 43.37 ? 188 HOH D O   1
+HETATM 4771 O  O   . HOH N 5 .   ? -18.247 7.731   47.729 1.00 43.46 ? 189 HOH D O   1
+HETATM 4772 O  O   . HOH N 5 .   ? -5.249  16.239  10.190 1.00 41.77 ? 190 HOH D O   1
+HETATM 4773 O  O   . HOH N 5 .   ? -23.507 10.102  43.004 1.00 43.68 ? 191 HOH D O   1
+HETATM 4774 O  O   . HOH N 5 .   ? -19.966 5.347   44.610 1.00 45.36 ? 192 HOH D O   1
+HETATM 4775 O  O   . HOH N 5 .   ? 7.704   3.548   14.354 1.00 41.53 ? 193 HOH D O   1
+HETATM 4776 O  O   . HOH N 5 .   ? -12.629 5.336   19.151 1.00 36.25 ? 194 HOH D O   1
+HETATM 4777 O  O   . HOH N 5 .   ? -2.420  24.373  26.217 1.00 39.70 ? 195 HOH D O   1
+HETATM 4778 O  O   . HOH N 5 .   ? -15.654 13.836  26.085 1.00 37.79 ? 196 HOH D O   1
+HETATM 4779 O  O   . HOH N 5 .   ? 7.112   9.399   19.049 1.00 45.10 ? 197 HOH D O   1
+#
diff --git a/tests/protein/test_graphs.py b/tests/protein/test_graphs.py
index 9e08bfbf..6b913f47 100644
--- a/tests/protein/test_graphs.py
+++ b/tests/protein/test_graphs.py
@@ -50,7 +50,8 @@
 )
 from graphein.utils.dependencies import is_tool
 
-DATA_PATH = Path(__file__).resolve().parent / "test_data" / "4hhb.pdb"
+PDB_DATA_PATH = Path(__file__).resolve().parent / "test_data" / "4hhb.pdb"
+CIF_DATA_PATH = Path(__file__).resolve().parent / "test_data" / "4hhb.cif"
 
 DSSP_AVAILABLE = is_tool("mkdssp")
 
@@ -59,19 +60,25 @@ def generate_graph():
     """Generate PDB network.
     This is a helper function.
     """
-    return construct_graph(path=str(DATA_PATH))
+    return construct_graph(path=str(PDB_DATA_PATH))
 
 
 @pytest.fixture(scope="module")
 def net():
-    """Generate proteingraph from 2VUI.pdb."""
+    """Generate proteingraph from 4HHB.pdb."""
     return generate_graph()
 
 
 @pytest.fixture()
 def pdb_df():
-    """Generate pdb_df from 2VIU.pdb."""
-    return read_pdb_to_dataframe(DATA_PATH)
+    """Generate pdb_df from 4HHB.pdb."""
+    return read_pdb_to_dataframe(PDB_DATA_PATH)
+
+
+@pytest.fixture()
+def cif_to_pdb_df():
+    """Generate pdb_df from 4HHB.cif."""
+    return read_pdb_to_dataframe(CIF_DATA_PATH)
 
 
 def test_nodes_are_strings(net):
@@ -83,14 +90,20 @@ def test_nodes_are_strings(net):
         assert isinstance(n, str)
 
 
+def test_pdb_vs_cif_file_parsing():
+    """Generate graph from cif and pdb file and compare them"""
+    G_pdb = construct_graph(path=str(PDB_DATA_PATH))
+    G_cif = construct_graph(path=str(CIF_DATA_PATH))
+    assert len(G_cif.nodes()) == len(G_pdb.nodes())
+
+
 # Example-based Graph Construction test
 def test_construct_graph():
     """Example-based test that graph construction works correctly.
 
     Uses 4hhb PDB file as an example test case.
     """
-    file_path = Path(__file__).parent / "test_data" / "4hhb.pdb"
-    G = construct_graph(path=str(file_path))
+    G = construct_graph(path=str(PDB_DATA_PATH))
     assert isinstance(G, nx.Graph)
     assert len(G) == 574