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1z82.pdb
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HEADER OXIDOREDUCTASE 29-MAR-05 1Z82
TITLE CRYSTAL STRUCTURE OF GLYCEROL-3-PHOSPHATE DEHYDROGENASE (TM0378) FROM
TITLE 2 THERMOTOGA MARITIMA AT 2.00 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCEROL-3-PHOSPHATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.1.1.8;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 243274;
SOURCE 4 STRAIN: MSB8;
SOURCE 5 GENE: TM0378;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TM0378, GLYCEROL-3-PHOSPHATE DEHYDROGENASE, STRUCTURAL GENOMICS,
KEYWDS 2 JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, PSI, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 4 13-JUL-11 1Z82 1 VERSN
REVDAT 3 24-FEB-09 1Z82 1 VERSN
REVDAT 2 03-MAY-05 1Z82 1 REMARK
REVDAT 1 12-APR-05 1Z82 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF GLYCEROL-3-PHOSPHATE DEHYDROGENASE
JRNL TITL 2 (TM0378) FROM THERMOTOGA MARITIMA AT 2.00 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 37984
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2024
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2780
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 163
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4812
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 180
REMARK 3 SOLVENT ATOMS : 323
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.37000
REMARK 3 B22 (A**2) : -0.29000
REMARK 3 B33 (A**2) : -2.39000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.87000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.192
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.162
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.364
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5095 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4846 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6908 ; 1.621 ; 2.009
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11187 ; 1.032 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 622 ; 5.536 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 205 ;34.880 ;23.561
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 885 ;15.171 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;20.557 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 791 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5472 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 990 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1051 ; 0.212 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5111 ; 0.182 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2538 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3168 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 303 ; 0.158 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 12 ; 0.173 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 59 ; 0.233 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.157 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3360 ; 1.052 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1280 ; 0.209 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4992 ; 1.284 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2179 ; 2.346 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1916 ; 3.441 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 313 6
REMARK 3 1 B 3 B 313 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 4660 ; 0.420 ; 5.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 4660 ; 1.470 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 313
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2869 31.6552 17.4348
REMARK 3 T TENSOR
REMARK 3 T11: -0.1303 T22: -0.1701
REMARK 3 T33: -0.1574 T12: -0.0347
REMARK 3 T13: 0.0337 T23: -0.0527
REMARK 3 L TENSOR
REMARK 3 L11: 1.8413 L22: 2.4764
REMARK 3 L33: 3.0504 L12: -0.4911
REMARK 3 L13: -0.6751 L23: -0.3386
REMARK 3 S TENSOR
REMARK 3 S11: 0.1653 S12: 0.0386 S13: 0.0656
REMARK 3 S21: -0.3558 S22: -0.0650 S23: -0.1830
REMARK 3 S31: -0.2527 S32: 0.2278 S33: -0.1003
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 314
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8928 30.7562 52.9347
REMARK 3 T TENSOR
REMARK 3 T11: -0.1693 T22: -0.1384
REMARK 3 T33: -0.1582 T12: -0.0786
REMARK 3 T13: 0.0117 T23: -0.0619
REMARK 3 L TENSOR
REMARK 3 L11: 1.6780 L22: 1.7943
REMARK 3 L33: 3.9252 L12: -0.1753
REMARK 3 L13: -0.1724 L23: -0.6623
REMARK 3 S TENSOR
REMARK 3 S11: 0.0813 S12: -0.2043 S13: 0.0549
REMARK 3 S21: 0.2259 S22: -0.0476 S23: -0.0026
REMARK 3 S31: -0.2238 S32: 0.2870 S33: -0.0337
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1Z82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-05.
REMARK 100 THE RCSB ID CODE IS RCSB032415.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.891940,0.979245
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40008
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 29.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.55800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MGCL2, 35.0% MPD, 0.1M IMIDAZOLE
REMARK 280 PH 8.0, VAPOR DIFFUSION,SITTING DROP,NANODROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.72550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 ARG A 314
REMARK 465 SER A 315
REMARK 465 LEU A 316
REMARK 465 LYS A 317
REMARK 465 ASP A 318
REMARK 465 GLU A 319
REMARK 465 PHE A 320
REMARK 465 TRP A 321
REMARK 465 ALA A 322
REMARK 465 SER A 323
REMARK 465 MET B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ILE B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 GLU B 2
REMARK 465 SER B 315
REMARK 465 LEU B 316
REMARK 465 LYS B 317
REMARK 465 ASP B 318
REMARK 465 GLU B 319
REMARK 465 PHE B 320
REMARK 465 TRP B 321
REMARK 465 ALA B 322
REMARK 465 SER B 323
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 35 CD CE NZ
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 GLU A 52 CG CD OE1 OE2
REMARK 470 LYS A 54 CG CD CE NZ
REMARK 470 LYS A 68 CG CD CE NZ
REMARK 470 GLU A 69 CD OE1 OE2
REMARK 470 GLU A 115 CD OE1 OE2
REMARK 470 LYS A 150 CD CE NZ
REMARK 470 ARG A 162 CD NE CZ NH1 NH2
REMARK 470 LYS A 222 CG CD CE NZ
REMARK 470 GLU B 27 CD OE1 OE2
REMARK 470 LYS B 35 CD CE NZ
REMARK 470 GLU B 52 CG CD OE1 OE2
REMARK 470 LYS B 54 CD CE NZ
REMARK 470 PRO B 89 CB
REMARK 470 LYS B 150 CE NZ
REMARK 470 LYS B 154 CD CE NZ
REMARK 470 GLU B 159 CG CD OE1 OE2
REMARK 470 LYS B 222 CG CD CE NZ
REMARK 470 LYS B 279 CD CE NZ
REMARK 470 ARG B 314 CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 240 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 109 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 243 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 243 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 10 54.55 -114.46
REMARK 500 GLU A 52 59.51 35.58
REMARK 500 ALA B 10 51.85 -112.18
REMARK 500 PRO B 121 157.43 -48.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G3H A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G3P B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 354146 RELATED DB: TARGETDB
DBREF 1Z82 A 1 323 GB 15644628 NP_228189 1 323
DBREF 1Z82 B 1 323 GB 15644628 NP_228189 1 323
SEQADV 1Z82 MET A -11 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 GLY A -10 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 SER A -9 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 ASP A -8 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 LYS A -7 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 ILE A -6 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS A -5 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS A -4 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS A -3 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS A -2 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS A -1 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS A 0 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 MSE A 1 GB 15644628 MET 1 MODIFIED RESIDUE
SEQADV 1Z82 MSE A 3 GB 15644628 MET 3 MODIFIED RESIDUE
SEQADV 1Z82 MSE A 20 GB 15644628 MET 20 MODIFIED RESIDUE
SEQADV 1Z82 MSE A 94 GB 15644628 MET 94 MODIFIED RESIDUE
SEQADV 1Z82 MSE A 215 GB 15644628 MET 215 MODIFIED RESIDUE
SEQADV 1Z82 MSE A 225 GB 15644628 MET 225 MODIFIED RESIDUE
SEQADV 1Z82 MSE A 234 GB 15644628 MET 234 MODIFIED RESIDUE
SEQADV 1Z82 MSE A 278 GB 15644628 MET 278 MODIFIED RESIDUE
SEQADV 1Z82 MSE A 288 GB 15644628 MET 288 MODIFIED RESIDUE
SEQADV 1Z82 MSE A 308 GB 15644628 MET 308 MODIFIED RESIDUE
SEQADV 1Z82 MSE A 312 GB 15644628 MET 312 MODIFIED RESIDUE
SEQADV 1Z82 MET B -11 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 GLY B -10 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 SER B -9 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 ASP B -8 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 LYS B -7 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 ILE B -6 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS B -5 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS B -4 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS B -3 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS B -2 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS B -1 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 HIS B 0 GB 15644628 LEADER SEQUENCE
SEQADV 1Z82 MSE B 1 GB 15644628 MET 1 MODIFIED RESIDUE
SEQADV 1Z82 MSE B 3 GB 15644628 MET 3 MODIFIED RESIDUE
SEQADV 1Z82 MSE B 20 GB 15644628 MET 20 MODIFIED RESIDUE
SEQADV 1Z82 MSE B 94 GB 15644628 MET 94 MODIFIED RESIDUE
SEQADV 1Z82 MSE B 215 GB 15644628 MET 215 MODIFIED RESIDUE
SEQADV 1Z82 MSE B 225 GB 15644628 MET 225 MODIFIED RESIDUE
SEQADV 1Z82 MSE B 234 GB 15644628 MET 234 MODIFIED RESIDUE
SEQADV 1Z82 MSE B 278 GB 15644628 MET 278 MODIFIED RESIDUE
SEQADV 1Z82 MSE B 288 GB 15644628 MET 288 MODIFIED RESIDUE
SEQADV 1Z82 MSE B 308 GB 15644628 MET 308 MODIFIED RESIDUE
SEQADV 1Z82 MSE B 312 GB 15644628 MET 312 MODIFIED RESIDUE
SEQRES 1 A 335 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 A 335 GLU MSE ARG PHE PHE VAL LEU GLY ALA GLY SER TRP GLY
SEQRES 3 A 335 THR VAL PHE ALA GLN MSE LEU HIS GLU ASN GLY GLU GLU
SEQRES 4 A 335 VAL ILE LEU TRP ALA ARG ARG LYS GLU ILE VAL ASP LEU
SEQRES 5 A 335 ILE ASN VAL SER HIS THR SER PRO TYR VAL GLU GLU SER
SEQRES 6 A 335 LYS ILE THR VAL ARG ALA THR ASN ASP LEU GLU GLU ILE
SEQRES 7 A 335 LYS LYS GLU ASP ILE LEU VAL ILE ALA ILE PRO VAL GLN
SEQRES 8 A 335 TYR ILE ARG GLU HIS LEU LEU ARG LEU PRO VAL LYS PRO
SEQRES 9 A 335 SER MSE VAL LEU ASN LEU SER LYS GLY ILE GLU ILE LYS
SEQRES 10 A 335 THR GLY LYS ARG VAL SER GLU ILE VAL GLU GLU ILE LEU
SEQRES 11 A 335 GLY CYS PRO TYR ALA VAL LEU SER GLY PRO SER HIS ALA
SEQRES 12 A 335 GLU GLU VAL ALA LYS LYS LEU PRO THR ALA VAL THR LEU
SEQRES 13 A 335 ALA GLY GLU ASN SER LYS GLU LEU GLN LYS ARG ILE SER
SEQRES 14 A 335 THR GLU TYR PHE ARG VAL TYR THR CYS GLU ASP VAL VAL
SEQRES 15 A 335 GLY VAL GLU ILE ALA GLY ALA LEU LYS ASN VAL ILE ALA
SEQRES 16 A 335 ILE ALA ALA GLY ILE LEU ASP GLY PHE GLY GLY TRP ASP
SEQRES 17 A 335 ASN ALA LYS ALA ALA LEU GLU THR ARG GLY ILE TYR GLU
SEQRES 18 A 335 ILE ALA ARG PHE GLY MSE PHE PHE GLY ALA ASP GLN LYS
SEQRES 19 A 335 THR PHE MSE GLY LEU ALA GLY ILE GLY ASP LEU MSE VAL
SEQRES 20 A 335 THR CYS ASN SER ARG TYR SER ARG ASN ARG ARG PHE GLY
SEQRES 21 A 335 GLU LEU ILE ALA ARG GLY PHE ASN PRO LEU LYS LEU LEU
SEQRES 22 A 335 GLU SER SER ASN GLN VAL VAL GLU GLY ALA PHE THR VAL
SEQRES 23 A 335 LYS ALA VAL MSE LYS ILE ALA LYS GLU ASN LYS ILE ASP
SEQRES 24 A 335 MSE PRO ILE SER GLU GLU VAL TYR ARG VAL VAL TYR GLU
SEQRES 25 A 335 GLY LYS PRO PRO LEU GLN SER MSE ARG ASP LEU MSE ARG
SEQRES 26 A 335 ARG SER LEU LYS ASP GLU PHE TRP ALA SER
SEQRES 1 B 335 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 B 335 GLU MSE ARG PHE PHE VAL LEU GLY ALA GLY SER TRP GLY
SEQRES 3 B 335 THR VAL PHE ALA GLN MSE LEU HIS GLU ASN GLY GLU GLU
SEQRES 4 B 335 VAL ILE LEU TRP ALA ARG ARG LYS GLU ILE VAL ASP LEU
SEQRES 5 B 335 ILE ASN VAL SER HIS THR SER PRO TYR VAL GLU GLU SER
SEQRES 6 B 335 LYS ILE THR VAL ARG ALA THR ASN ASP LEU GLU GLU ILE
SEQRES 7 B 335 LYS LYS GLU ASP ILE LEU VAL ILE ALA ILE PRO VAL GLN
SEQRES 8 B 335 TYR ILE ARG GLU HIS LEU LEU ARG LEU PRO VAL LYS PRO
SEQRES 9 B 335 SER MSE VAL LEU ASN LEU SER LYS GLY ILE GLU ILE LYS
SEQRES 10 B 335 THR GLY LYS ARG VAL SER GLU ILE VAL GLU GLU ILE LEU
SEQRES 11 B 335 GLY CYS PRO TYR ALA VAL LEU SER GLY PRO SER HIS ALA
SEQRES 12 B 335 GLU GLU VAL ALA LYS LYS LEU PRO THR ALA VAL THR LEU
SEQRES 13 B 335 ALA GLY GLU ASN SER LYS GLU LEU GLN LYS ARG ILE SER
SEQRES 14 B 335 THR GLU TYR PHE ARG VAL TYR THR CYS GLU ASP VAL VAL
SEQRES 15 B 335 GLY VAL GLU ILE ALA GLY ALA LEU LYS ASN VAL ILE ALA
SEQRES 16 B 335 ILE ALA ALA GLY ILE LEU ASP GLY PHE GLY GLY TRP ASP
SEQRES 17 B 335 ASN ALA LYS ALA ALA LEU GLU THR ARG GLY ILE TYR GLU
SEQRES 18 B 335 ILE ALA ARG PHE GLY MSE PHE PHE GLY ALA ASP GLN LYS
SEQRES 19 B 335 THR PHE MSE GLY LEU ALA GLY ILE GLY ASP LEU MSE VAL
SEQRES 20 B 335 THR CYS ASN SER ARG TYR SER ARG ASN ARG ARG PHE GLY
SEQRES 21 B 335 GLU LEU ILE ALA ARG GLY PHE ASN PRO LEU LYS LEU LEU
SEQRES 22 B 335 GLU SER SER ASN GLN VAL VAL GLU GLY ALA PHE THR VAL
SEQRES 23 B 335 LYS ALA VAL MSE LYS ILE ALA LYS GLU ASN LYS ILE ASP
SEQRES 24 B 335 MSE PRO ILE SER GLU GLU VAL TYR ARG VAL VAL TYR GLU
SEQRES 25 B 335 GLY LYS PRO PRO LEU GLN SER MSE ARG ASP LEU MSE ARG
SEQRES 26 B 335 ARG SER LEU LYS ASP GLU PHE TRP ALA SER
MODRES 1Z82 MSE A 3 MET SELENOMETHIONINE
MODRES 1Z82 MSE A 20 MET SELENOMETHIONINE
MODRES 1Z82 MSE A 94 MET SELENOMETHIONINE
MODRES 1Z82 MSE A 215 MET SELENOMETHIONINE
MODRES 1Z82 MSE A 225 MET SELENOMETHIONINE
MODRES 1Z82 MSE A 234 MET SELENOMETHIONINE
MODRES 1Z82 MSE A 278 MET SELENOMETHIONINE
MODRES 1Z82 MSE A 288 MET SELENOMETHIONINE
MODRES 1Z82 MSE A 308 MET SELENOMETHIONINE
MODRES 1Z82 MSE A 312 MET SELENOMETHIONINE
MODRES 1Z82 MSE B 3 MET SELENOMETHIONINE
MODRES 1Z82 MSE B 20 MET SELENOMETHIONINE
MODRES 1Z82 MSE B 94 MET SELENOMETHIONINE
MODRES 1Z82 MSE B 215 MET SELENOMETHIONINE
MODRES 1Z82 MSE B 225 MET SELENOMETHIONINE
MODRES 1Z82 MSE B 234 MET SELENOMETHIONINE
MODRES 1Z82 MSE B 278 MET SELENOMETHIONINE
MODRES 1Z82 MSE B 288 MET SELENOMETHIONINE
MODRES 1Z82 MSE B 308 MET SELENOMETHIONINE
MODRES 1Z82 MSE B 312 MET SELENOMETHIONINE
HET MSE A 3 8
HET MSE A 20 8
HET MSE A 94 8
HET MSE A 215 8
HET MSE A 225 12
HET MSE A 234 8
HET MSE A 278 8
HET MSE A 288 8
HET MSE A 308 8
HET MSE A 312 8
HET MSE B 3 8
HET MSE B 20 8
HET MSE B 94 8
HET MSE B 215 8
HET MSE B 225 12
HET MSE B 234 8
HET MSE B 278 8
HET MSE B 288 8
HET MSE B 308 8
HET MSE B 312 8
HET NDP A 500 48
HET G3H A 600 10
HET NDP B 500 48
HET G3P B 600 10
HET MRD B 601 8
HET MRD A 601 8
HET MRD B 602 8
HET MRD B 603 8
HET MRD B 604 8
HET MPD A 602 8
HET MPD A 603 8
HET MPD A 604 8
HETNAM MSE SELENOMETHIONINE
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM G3H GLYCERALDEHYDE-3-PHOSPHATE
HETNAM G3P SN-GLYCEROL-3-PHOSPHATE
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 NDP 2(C21 H30 N7 O17 P3)
FORMUL 4 G3H C3 H7 O6 P
FORMUL 6 G3P C3 H9 O6 P
FORMUL 7 MRD 5(C6 H14 O2)
FORMUL 12 MPD 3(C6 H14 O2)
FORMUL 15 HOH *323(H2 O)
HELIX 1 1 GLY A 11 ASN A 24 1 14
HELIX 2 2 ARG A 34 HIS A 45 1 12
HELIX 3 3 ASP A 62 ILE A 66 5 5
HELIX 4 4 PRO A 77 GLN A 79 5 3
HELIX 5 5 TYR A 80 LEU A 86 1 7
HELIX 6 6 ARG A 109 LEU A 118 1 10
HELIX 7 7 HIS A 130 LYS A 136 1 7
HELIX 8 8 ASN A 148 SER A 157 1 10
HELIX 9 9 ASP A 168 PHE A 192 1 25
HELIX 10 10 TRP A 195 PHE A 217 1 23
HELIX 11 11 ASP A 220 MSE A 225 1 6
HELIX 12 12 GLY A 229 SER A 239 1 11
HELIX 13 13 SER A 242 GLY A 254 1 13
HELIX 14 14 ASN A 256 SER A 263 1 8
HELIX 15 15 GLU A 269 ASN A 284 1 16
HELIX 16 16 MSE A 288 GLU A 300 1 13
HELIX 17 17 PRO A 303 ARG A 313 1 11
HELIX 18 18 GLY B 11 ASN B 24 1 14
HELIX 19 19 ARG B 34 SER B 44 1 11
HELIX 20 20 ASP B 62 ILE B 66 5 5
HELIX 21 21 PRO B 77 GLN B 79 5 3
HELIX 22 22 TYR B 80 LEU B 86 1 7
HELIX 23 23 ARG B 109 LEU B 118 1 10
HELIX 24 24 HIS B 130 LYS B 136 1 7
HELIX 25 25 ASN B 148 SER B 157 1 10
HELIX 26 26 ASP B 168 PHE B 192 1 25
HELIX 27 27 TRP B 195 PHE B 217 1 23
HELIX 28 28 ASP B 220 GLY B 226 5 7
HELIX 29 29 GLY B 229 SER B 239 1 11
HELIX 30 30 SER B 242 ARG B 253 1 12
HELIX 31 31 ASN B 256 SER B 263 1 8
HELIX 32 32 VAL B 268 LYS B 285 1 18
HELIX 33 33 MSE B 288 GLU B 300 1 13
HELIX 34 34 PRO B 303 ARG B 314 1 12
SHEET 1 A 8 ARG A 58 THR A 60 0
SHEET 2 A 8 GLU A 27 TRP A 31 1 N LEU A 30 O ARG A 58
SHEET 3 A 8 ARG A 4 LEU A 8 1 N VAL A 7 O TRP A 31
SHEET 4 A 8 ASP A 70 ILE A 74 1 O ILE A 71 N ARG A 4
SHEET 5 A 8 MSE A 94 ASN A 97 1 O LEU A 96 N LEU A 72
SHEET 6 A 8 TYR A 122 SER A 126 1 O ALA A 123 N ASN A 97
SHEET 7 A 8 THR A 140 GLY A 146 -1 O ALA A 145 N VAL A 124
SHEET 8 A 8 PHE A 161 CYS A 166 1 O ARG A 162 N VAL A 142
SHEET 1 B 8 ALA B 59 THR B 60 0
SHEET 2 B 8 VAL B 28 TRP B 31 1 N LEU B 30 O THR B 60
SHEET 3 B 8 PHE B 5 LEU B 8 1 N VAL B 7 O TRP B 31
SHEET 4 B 8 ILE B 71 ILE B 74 1 O ILE B 71 N PHE B 6
SHEET 5 B 8 MSE B 94 ASN B 97 1 O MSE B 94 N LEU B 72
SHEET 6 B 8 TYR B 122 SER B 126 1 O ALA B 123 N ASN B 97
SHEET 7 B 8 THR B 140 GLY B 146 -1 O ALA B 145 N VAL B 124
SHEET 8 B 8 PHE B 161 CYS B 166 1 O ARG B 162 N THR B 140
LINK C GLU A 2 N MSE A 3 1555 1555 1.34
LINK C MSE A 3 N ARG A 4 1555 1555 1.33
LINK C GLN A 19 N MSE A 20 1555 1555 1.33
LINK C MSE A 20 N LEU A 21 1555 1555 1.33
LINK C SER A 93 N MSE A 94 1555 1555 1.33
LINK C MSE A 94 N VAL A 95 1555 1555 1.32
LINK C GLY A 214 N MSE A 215 1555 1555 1.33
LINK C MSE A 215 N PHE A 216 1555 1555 1.33
LINK C PHE A 224 N MSE A 225 1555 1555 1.33
LINK C MSE A 225 N GLY A 226 1555 1555 1.32
LINK C LEU A 233 N MSE A 234 1555 1555 1.33
LINK C MSE A 234 N VAL A 235 1555 1555 1.33
LINK C VAL A 277 N MSE A 278 1555 1555 1.33
LINK C MSE A 278 N LYS A 279 1555 1555 1.33
LINK C ASP A 287 N MSE A 288 1555 1555 1.32
LINK C MSE A 288 N PRO A 289 1555 1555 1.34
LINK C SER A 307 N MSE A 308 1555 1555 1.33
LINK C MSE A 308 N ARG A 309 1555 1555 1.33
LINK C LEU A 311 N MSE A 312 1555 1555 1.32
LINK C MSE A 312 N ARG A 313 1555 1555 1.32
LINK C MSE B 3 N ARG B 4 1555 1555 1.33
LINK C GLN B 19 N MSE B 20 1555 1555 1.32
LINK C MSE B 20 N LEU B 21 1555 1555 1.33
LINK C SER B 93 N MSE B 94 1555 1555 1.33
LINK C MSE B 94 N VAL B 95 1555 1555 1.33
LINK C GLY B 214 N MSE B 215 1555 1555 1.32
LINK C MSE B 215 N PHE B 216 1555 1555 1.32
LINK C PHE B 224 N MSE B 225 1555 1555 1.33
LINK C MSE B 225 N GLY B 226 1555 1555 1.32
LINK C LEU B 233 N MSE B 234 1555 1555 1.32
LINK C MSE B 234 N VAL B 235 1555 1555 1.33
LINK C VAL B 277 N MSE B 278 1555 1555 1.32
LINK C MSE B 278 N LYS B 279 1555 1555 1.33
LINK C ASP B 287 N MSE B 288 1555 1555 1.34
LINK C MSE B 288 N PRO B 289 1555 1555 1.33
LINK C SER B 307 N MSE B 308 1555 1555 1.34
LINK C MSE B 308 N ARG B 309 1555 1555 1.33
LINK C LEU B 311 N MSE B 312 1555 1555 1.33
LINK C MSE B 312 N ARG B 313 1555 1555 1.33
SITE 1 AC1 32 ALA A 10 GLY A 11 SER A 12 TRP A 13
SITE 2 AC1 32 ARG A 33 ARG A 34 TYR A 49 ALA A 75
SITE 3 AC1 32 PRO A 77 TYR A 80 HIS A 84 SER A 99
SITE 4 AC1 32 LYS A 100 SER A 129 HIS A 130 ALA A 131
SITE 5 AC1 32 ARG A 243 ASN A 265 GLN A 266 VAL A 267
SITE 6 AC1 32 GLU A 269 HOH A 621 HOH A 626 HOH A 629
SITE 7 AC1 32 HOH A 634 HOH A 641 HOH A 648 HOH A 651
SITE 8 AC1 32 HOH A 663 HOH A 664 HOH A 687 G3P B 600
SITE 1 AC2 17 HOH A 613 LYS B 100 GLY B 127 PRO B 128
SITE 2 AC2 17 SER B 129 HIS B 130 LYS B 179 ASN B 180
SITE 3 AC2 17 ASP B 232 THR B 236 TYR B 241 SER B 242
SITE 4 AC2 17 ARG B 243 ASN B 244 NDP B 500 HOH B 618
SITE 5 AC2 17 HOH B 635
SITE 1 AC3 33 ARG A 87 G3H A 600 ALA B 10 GLY B 11
SITE 2 AC3 33 SER B 12 TRP B 13 ARG B 33 ARG B 34
SITE 3 AC3 33 TYR B 49 ALA B 75 PRO B 77 TYR B 80
SITE 4 AC3 33 GLU B 83 HIS B 84 SER B 99 LYS B 100
SITE 5 AC3 33 SER B 129 HIS B 130 ALA B 131 ARG B 243
SITE 6 AC3 33 ASN B 265 GLN B 266 VAL B 267 GLU B 269
SITE 7 AC3 33 HOH B 618 HOH B 620 HOH B 621 HOH B 633
SITE 8 AC3 33 HOH B 635 HOH B 636 HOH B 638 HOH B 652
SITE 9 AC3 33 HOH B 653
SITE 1 AC4 15 LYS A 100 GLY A 127 SER A 129 HIS A 130
SITE 2 AC4 15 LYS A 179 ASP A 232 THR A 236 TYR A 241
SITE 3 AC4 15 SER A 242 ARG A 243 ASN A 244 NDP A 500
SITE 4 AC4 15 HOH A 621 HOH A 626 HOH B 630
SITE 1 AC5 8 ALA B 185 ILE B 188 GLU B 293 SER B 307
SITE 2 AC5 8 MSE B 308 LEU B 311 MRD B 602 HOH B 684
SITE 1 AC6 9 ALA A 185 ILE A 188 LEU A 189 GLU A 293
SITE 2 AC6 9 VAL A 294 SER A 307 MSE A 308 LEU A 311
SITE 3 AC6 9 HOH A 735
SITE 1 AC7 4 THR A 140 MSE B 312 MRD B 601 HOH B 684
SITE 1 AC8 7 ARG B 243 ARG B 246 LEU B 260 SER B 263
SITE 2 AC8 7 SER B 264 GLN B 266 VAL B 268
SITE 1 AC9 4 VAL A 43 SER A 44 MSE B 3 GLU B 151
SITE 1 BC1 3 ARG A 205 LEU A 311 HOH A 735
SITE 1 BC2 6 ARG A 243 ARG A 246 LEU A 260 SER A 263
SITE 2 BC2 6 SER A 264 GLN A 266
SITE 1 BC3 2 GLY A 254 PHE A 255
CRYST1 65.090 67.451 75.597 90.00 113.67 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015360 0.000000 0.006740 0.00000
SCALE2 0.000000 0.014830 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014440 0.00000
ATOM 1 N GLU A 2 26.796 54.539 1.997 1.00 54.03 N
ATOM 2 CA GLU A 2 28.174 54.679 2.546 1.00 53.92 C
ATOM 3 C GLU A 2 28.958 53.344 2.672 1.00 53.81 C
ATOM 4 O GLU A 2 30.165 53.350 2.470 1.00 54.04 O
ATOM 5 CB GLU A 2 28.142 55.444 3.892 1.00 53.94 C
ATOM 6 CG GLU A 2 29.371 55.219 4.811 1.00 54.16 C
ATOM 7 CD GLU A 2 29.592 56.319 5.842 1.00 53.86 C
ATOM 8 OE1 GLU A 2 28.972 57.387 5.711 1.00 52.59 O
ATOM 9 OE2 GLU A 2 30.396 56.112 6.780 1.00 53.44 O
HETATM 10 N MSE A 3 28.320 52.210 2.970 1.00 53.05 N
HETATM 11 CA MSE A 3 29.108 51.043 3.391 1.00 53.60 C
HETATM 12 C MSE A 3 28.423 49.660 3.298 1.00 49.32 C
HETATM 13 O MSE A 3 27.220 49.534 3.496 1.00 49.28 O
HETATM 14 CB MSE A 3 29.605 51.349 4.806 1.00 53.47 C
HETATM 15 CG MSE A 3 29.929 50.189 5.719 1.00 56.96 C
HETATM 16 SE MSE A 3 29.874 50.857 7.616 1.00 64.40 SE
HETATM 17 CE MSE A 3 30.684 52.778 7.349 1.00 62.46 C
ATOM 18 N ARG A 4 29.214 48.629 2.999 1.00 45.18 N
ATOM 19 CA ARG A 4 28.689 47.279 2.775 1.00 41.91 C
ATOM 20 C ARG A 4 29.517 46.208 3.488 1.00 38.91 C
ATOM 21 O ARG A 4 30.733 46.241 3.444 1.00 37.82 O
ATOM 22 CB ARG A 4 28.669 46.959 1.282 1.00 41.84 C
ATOM 23 CG ARG A 4 28.012 45.614 0.959 1.00 41.78 C
ATOM 24 CD ARG A 4 27.898 45.369 -0.543 1.00 42.14 C
ATOM 25 NE ARG A 4 29.121 44.744 -1.052 1.00 42.79 N
ATOM 26 CZ ARG A 4 29.183 43.919 -2.090 1.00 41.41 C
ATOM 27 NH1 ARG A 4 28.092 43.578 -2.757 1.00 41.45 N
ATOM 28 NH2 ARG A 4 30.349 43.419 -2.450 1.00 39.51 N
ATOM 29 N PHE A 5 28.844 45.251 4.118 1.00 35.85 N
ATOM 30 CA PHE A 5 29.517 44.160 4.835 1.00 34.05 C
ATOM 31 C PHE A 5 29.579 42.899 3.975 1.00 32.63 C
ATOM 32 O PHE A 5 28.548 42.362 3.585 1.00 32.07 O
ATOM 33 CB PHE A 5 28.796 43.856 6.148 1.00 33.43 C
ATOM 34 CG PHE A 5 28.805 44.996 7.118 1.00 33.09 C
ATOM 35 CD1 PHE A 5 27.878 46.022 7.010 1.00 32.33 C
ATOM 36 CD2 PHE A 5 29.742 45.052 8.129 1.00 33.30 C
ATOM 37 CE1 PHE A 5 27.882 47.074 7.903 1.00 32.85 C
ATOM 38 CE2 PHE A 5 29.746 46.102 9.033 1.00 34.13 C
ATOM 39 CZ PHE A 5 28.815 47.118 8.911 1.00 32.97 C
ATOM 40 N PHE A 6 30.799 42.469 3.651 1.00 31.44 N
ATOM 41 CA PHE A 6 31.036 41.215 2.962 1.00 30.27 C
ATOM 42 C PHE A 6 31.428 40.161 4.010 1.00 29.79 C
ATOM 43 O PHE A 6 32.561 40.095 4.446 1.00 29.41 O
ATOM 44 CB PHE A 6 32.130 41.384 1.933 1.00 30.08 C
ATOM 45 CG PHE A 6 32.184 40.280 0.904 1.00 30.80 C
ATOM 46 CD1 PHE A 6 31.479 40.377 -0.285 1.00 31.45 C
ATOM 47 CD2 PHE A 6 32.975 39.176 1.092 1.00 31.73 C
ATOM 48 CE1 PHE A 6 31.538 39.382 -1.235 1.00 29.82 C
ATOM 49 CE2 PHE A 6 33.038 38.189 0.121 1.00 31.68 C
ATOM 50 CZ PHE A 6 32.321 38.305 -1.037 1.00 29.67 C
ATOM 51 N VAL A 7 30.460 39.356 4.414 1.00 29.60 N
ATOM 52 CA VAL A 7 30.669 38.329 5.413 1.00 29.84 C
ATOM 53 C VAL A 7 31.210 37.058 4.771 1.00 30.52 C
ATOM 54 O VAL A 7 30.544 36.420 3.958 1.00 30.32 O
ATOM 55 CB VAL A 7 29.396 38.009 6.177 1.00 29.92 C
ATOM 56 CG1 VAL A 7 29.699 37.016 7.313 1.00 29.64 C
ATOM 57 CG2 VAL A 7 28.787 39.292 6.746 1.00 29.83 C
ATOM 58 N LEU A 8 32.435 36.723 5.175 1.00 30.78 N
ATOM 59 CA LEU A 8 33.223 35.634 4.626 1.00 31.36 C
ATOM 60 C LEU A 8 33.134 34.414 5.527 1.00 30.38 C
ATOM 61 O LEU A 8 33.797 34.345 6.557 1.00 30.24 O
ATOM 62 CB LEU A 8 34.664 36.098 4.517 1.00 31.42 C
ATOM 63 CG LEU A 8 35.651 35.231 3.771 1.00 33.34 C
ATOM 64 CD1 LEU A 8 35.514 35.407 2.322 1.00 34.59 C
ATOM 65 CD2 LEU A 8 37.065 35.621 4.203 1.00 33.74 C
ATOM 66 N GLY A 9 32.280 33.474 5.131 1.00 30.05 N
ATOM 67 CA GLY A 9 32.101 32.209 5.838 1.00 29.50 C
ATOM 68 C GLY A 9 30.677 32.076 6.325 1.00 28.81 C
ATOM 69 O GLY A 9 30.202 32.908 7.066 1.00 28.64 O
ATOM 70 N ALA A 10 29.997 31.025 5.883 1.00 28.11 N
ATOM 71 CA ALA A 10 28.593 30.810 6.196 1.00 27.97 C
ATOM 72 C ALA A 10 28.414 29.552 7.068 1.00 27.73 C
ATOM 73 O ALA A 10 27.668 28.626 6.726 1.00 26.95 O
ATOM 74 CB ALA A 10 27.776 30.711 4.905 1.00 28.28 C
ATOM 75 N GLY A 11 29.134 29.536 8.180 1.00 27.55 N
ATOM 76 CA GLY A 11 28.914 28.582 9.264 1.00 28.05 C
ATOM 77 C GLY A 11 27.854 29.153 10.180 1.00 28.23 C
ATOM 78 O GLY A 11 27.105 30.021 9.785 1.00 29.30 O
ATOM 79 N SER A 12 27.787 28.666 11.405 1.00 29.20 N
ATOM 80 CA SER A 12 26.789 29.095 12.368 1.00 29.83 C
ATOM 81 C SER A 12 26.834 30.577 12.657 1.00 29.91 C
ATOM 82 O SER A 12 25.818 31.265 12.637 1.00 30.26 O
ATOM 83 CB SER A 12 26.959 28.334 13.694 1.00 30.26 C
ATOM 84 OG SER A 12 27.084 26.945 13.463 1.00 33.49 O
ATOM 85 N TRP A 13 28.022 31.063 12.938 1.00 29.76 N
ATOM 86 CA TRP A 13 28.211 32.449 13.368 1.00 29.28 C
ATOM 87 C TRP A 13 28.255 33.435 12.195 1.00 28.14 C
ATOM 88 O TRP A 13 27.671 34.495 12.270 1.00 28.54 O
ATOM 89 CB TRP A 13 29.465 32.530 14.249 1.00 29.33 C
ATOM 90 CG TRP A 13 29.680 33.839 14.969 1.00 28.21 C
ATOM 91 CD1 TRP A 13 30.873 34.425 15.184 1.00 29.52 C
ATOM 92 CD2 TRP A 13 28.696 34.722 15.541 1.00 29.56 C
ATOM 93 NE1 TRP A 13 30.730 35.571 15.901 1.00 28.19 N
ATOM 94 CE2 TRP A 13 29.396 35.797 16.115 1.00 29.17 C
ATOM 95 CE3 TRP A 13 27.296 34.701 15.640 1.00 30.37 C
ATOM 96 CZ2 TRP A 13 28.763 36.849 16.752 1.00 28.32 C
ATOM 97 CZ3 TRP A 13 26.663 35.747 16.292 1.00 29.52 C
ATOM 98 CH2 TRP A 13 27.402 36.815 16.835 1.00 31.02 C
ATOM 99 N GLY A 14 28.933 33.090 11.115 1.00 27.52 N
ATOM 100 CA GLY A 14 28.931 33.929 9.916 1.00 28.16 C
ATOM 101 C GLY A 14 27.518 34.196 9.407 1.00 27.55 C
ATOM 102 O GLY A 14 27.137 35.315 9.120 1.00 27.01 O
ATOM 103 N THR A 15 26.719 33.140 9.353 1.00 27.93 N
ATOM 104 CA THR A 15 25.347 33.230 8.885 1.00 28.07 C
ATOM 105 C THR A 15 24.445 34.028 9.830 1.00 28.22 C
ATOM 106 O THR A 15 23.607 34.801 9.392 1.00 29.68 O
ATOM 107 CB THR A 15 24.785 31.835 8.757 1.00 27.22 C
ATOM 108 OG1 THR A 15 25.652 31.076 7.915 1.00 27.80 O
ATOM 109 CG2 THR A 15 23.386 31.884 8.176 1.00 26.86 C
ATOM 110 N VAL A 16 24.576 33.771 11.115 1.00 28.54 N
ATOM 111 CA VAL A 16 23.770 34.462 12.127 1.00 29.09 C
ATOM 112 C VAL A 16 24.141 35.950 12.185 1.00 27.70 C
ATOM 113 O VAL A 16 23.266 36.782 12.133 1.00 25.68 O
ATOM 114 CB VAL A 16 23.883 33.768 13.503 1.00 29.30 C
ATOM 115 CG1 VAL A 16 23.216 34.593 14.578 1.00 30.63 C
ATOM 116 CG2 VAL A 16 23.232 32.403 13.432 1.00 30.54 C
ATOM 117 N PHE A 17 25.440 36.249 12.236 1.00 27.72 N
ATOM 118 CA PHE A 17 25.937 37.623 12.231 1.00 28.16 C
ATOM 119 C PHE A 17 25.492 38.411 10.984 1.00 27.58 C
ATOM 120 O PHE A 17 24.962 39.503 11.098 1.00 27.87 O
ATOM 121 CB PHE A 17 27.472 37.641 12.398 1.00 28.06 C
ATOM 122 CG PHE A 17 28.033 39.003 12.708 1.00 29.74 C
ATOM 123 CD1 PHE A 17 27.981 39.507 13.992 1.00 29.55 C
ATOM 124 CD2 PHE A 17 28.610 39.782 11.711 1.00 29.06 C
ATOM 125 CE1 PHE A 17 28.466 40.733 14.275 1.00 30.11 C
ATOM 126 CE2 PHE A 17 29.129 41.014 12.012 1.00 28.92 C
ATOM 127 CZ PHE A 17 29.044 41.494 13.290 1.00 27.73 C
ATOM 128 N ALA A 18 25.680 37.828 9.805 1.00 27.45 N
ATOM 129 CA ALA A 18 25.248 38.421 8.540 1.00 27.28 C
ATOM 130 C ALA A 18 23.761 38.724 8.534 1.00 26.88 C
ATOM 131 O ALA A 18 23.358 39.818 8.175 1.00 26.70 O
ATOM 132 CB ALA A 18 25.603 37.489 7.370 1.00 26.81 C
ATOM 133 N GLN A 19 22.965 37.745 8.950 1.00 27.01 N
ATOM 134 CA GLN A 19 21.512 37.897 9.075 1.00 26.61 C
ATOM 135 C GLN A 19 21.163 39.026 10.049 1.00 26.31 C
ATOM 136 O GLN A 19 20.302 39.832 9.759 1.00 24.35 O
ATOM 137 CB GLN A 19 20.868 36.585 9.548 1.00 26.99 C
ATOM 138 CG GLN A 19 19.322 36.606 9.573 1.00 28.26 C
ATOM 139 CD GLN A 19 18.681 36.861 8.224 1.00 30.67 C
ATOM 140 OE1 GLN A 19 19.233 36.529 7.176 1.00 30.74 O
ATOM 141 NE2 GLN A 19 17.499 37.454 8.240 1.00 31.88 N
HETATM 142 N MSE A 20 21.858 39.103 11.181 1.00 26.77 N
HETATM 143 CA MSE A 20 21.599 40.179 12.133 1.00 28.38 C
HETATM 144 C MSE A 20 21.871 41.539 11.530 1.00 27.13 C
HETATM 145 O MSE A 20 21.068 42.428 11.679 1.00 26.02 O
HETATM 146 CB MSE A 20 22.446 40.044 13.380 1.00 27.34 C
HETATM 147 CG MSE A 20 22.128 41.075 14.482 1.00 28.94 C
HETATM 148 SE MSE A 20 23.186 40.590 16.102 1.00 36.01 SE
HETATM 149 CE MSE A 20 25.025 40.885 15.349 1.00 35.82 C
ATOM 150 N LEU A 21 23.028 41.691 10.891 1.00 27.86 N
ATOM 151 CA LEU A 21 23.353 42.922 10.185 1.00 28.27 C
ATOM 152 C LEU A 21 22.349 43.291 9.097 1.00 28.02 C
ATOM 153 O LEU A 21 21.988 44.469 8.955 1.00 27.91 O
ATOM 154 CB LEU A 21 24.752 42.853 9.603 1.00 28.98 C
ATOM 155 CG LEU A 21 25.882 42.995 10.615 1.00 31.12 C
ATOM 156 CD1 LEU A 21 27.206 42.792 9.890 1.00 34.43 C
ATOM 157 CD2 LEU A 21 25.844 44.347 11.280 1.00 33.32 C
ATOM 158 N HIS A 22 21.908 42.283 8.339 1.00 27.18 N
ATOM 159 CA HIS A 22 20.871 42.447 7.330 1.00 26.42 C
ATOM 160 C HIS A 22 19.576 42.962 7.993 1.00 26.62 C
ATOM 161 O HIS A 22 18.941 43.861 7.468 1.00 25.34 O
ATOM 162 CB HIS A 22 20.672 41.118 6.580 1.00 26.16 C
ATOM 163 CG HIS A 22 19.573 41.124 5.566 1.00 25.27 C
ATOM 164 ND1 HIS A 22 19.668 41.773 4.352 1.00 24.63 N
ATOM 165 CD2 HIS A 22 18.352 40.541 5.584 1.00 25.74 C
ATOM 166 CE1 HIS A 22 18.544 41.609 3.679 1.00 24.86 C
ATOM 167 NE2 HIS A 22 17.731 40.858 4.401 1.00 24.56 N
ATOM 168 N GLU A 23 19.228 42.434 9.164 1.00 26.58 N
ATOM 169 CA GLU A 23 18.025 42.848 9.906 1.00 27.44 C
ATOM 170 C GLU A 23 18.111 44.233 10.567 1.00 26.01 C
ATOM 171 O GLU A 23 17.090 44.859 10.885 1.00 25.39 O
ATOM 172 CB GLU A 23 17.707 41.796 10.956 1.00 27.55 C
ATOM 173 CG GLU A 23 16.982 40.581 10.362 1.00 30.85 C
ATOM 174 CD GLU A 23 16.752 39.500 11.384 1.00 31.35 C
ATOM 175 OE1 GLU A 23 16.550 39.856 12.564 1.00 38.90 O
ATOM 176 OE2 GLU A 23 16.787 38.300 11.030 1.00 35.62 O
ATOM 177 N ASN A 24 19.344 44.673 10.777 1.00 25.99 N
ATOM 178 CA ASN A 24 19.682 46.038 11.170 1.00 26.89 C
ATOM 179 C ASN A 24 19.492 47.071 10.054 1.00 26.41 C
ATOM 180 O ASN A 24 19.598 48.264 10.307 1.00 26.26 O
ATOM 181 CB ASN A 24 21.152 46.114 11.646 1.00 27.43 C
ATOM 182 CG ASN A 24 21.337 45.663 13.088 1.00 29.83 C
ATOM 183 OD1 ASN A 24 20.363 45.429 13.801 1.00 35.57 O
ATOM 184 ND2 ASN A 24 22.592 45.519 13.516 1.00 30.92 N
ATOM 185 N GLY A 25 19.241 46.619 8.831 1.00 26.22 N
ATOM 186 CA GLY A 25 19.090 47.507 7.701 1.00 26.53 C
ATOM 187 C GLY A 25 20.394 47.852 6.996 1.00 26.84 C
ATOM 188 O GLY A 25 20.431 48.772 6.156 1.00 26.58 O
ATOM 189 N GLU A 26 21.453 47.116 7.333 1.00 27.31 N
ATOM 190 CA GLU A 26 22.735 47.274 6.671 1.00 27.67 C
ATOM 191 C GLU A 26 22.734 46.538 5.340 1.00 27.94 C
ATOM 192 O GLU A 26 21.913 45.665 5.099 1.00 26.95 O
ATOM 193 CB GLU A 26 23.876 46.789 7.546 1.00 27.94 C
ATOM 194 CG GLU A 26 24.001 47.530 8.864 1.00 29.89 C
ATOM 195 CD GLU A 26 24.251 49.016 8.683 1.00 32.58 C
ATOM 196 OE1 GLU A 26 25.027 49.380 7.777 1.00 34.89 O
ATOM 197 OE2 GLU A 26 23.679 49.817 9.444 1.00 34.22 O
ATOM 198 N GLU A 27 23.641 46.955 4.473 1.00 28.71 N
ATOM 199 CA GLU A 27 23.863 46.315 3.196 1.00 29.74 C
ATOM 200 C GLU A 27 24.849 45.185 3.433 1.00 28.90 C
ATOM 201 O GLU A 27 25.971 45.410 3.868 1.00 28.05 O
ATOM 202 CB GLU A 27 24.410 47.339 2.219 1.00 30.25 C
ATOM 203 CG GLU A 27 24.550 46.846 0.786 1.00 32.37 C
ATOM 204 CD GLU A 27 25.015 47.948 -0.161 1.00 32.70 C
ATOM 205 OE1 GLU A 27 24.941 49.159 0.222 1.00 35.62 O
ATOM 206 OE2 GLU A 27 25.449 47.590 -1.295 1.00 38.35 O
ATOM 207 N VAL A 28 24.407 43.960 3.171 1.00 28.53 N
ATOM 208 CA VAL A 28 25.165 42.760 3.545 1.00 28.02 C
ATOM 209 C VAL A 28 25.050 41.741 2.430 1.00 27.43 C
ATOM 210 O VAL A 28 23.982 41.599 1.813 1.00 25.94 O
ATOM 211 CB VAL A 28 24.627 42.114 4.876 1.00 27.92 C
ATOM 212 CG1 VAL A 28 25.428 40.896 5.290 1.00 28.40 C
ATOM 213 CG2 VAL A 28 24.641 43.118 6.011 1.00 28.21 C
ATOM 214 N ILE A 29 26.171 41.043 2.210 1.00 27.49 N
ATOM 215 CA ILE A 29 26.250 39.856 1.373 1.00 27.39 C
ATOM 216 C ILE A 29 27.065 38.805 2.142 1.00 27.01 C
ATOM 217 O ILE A 29 28.034 39.123 2.826 1.00 26.24 O
ATOM 218 CB ILE A 29 26.847 40.179 0.000 1.00 27.98 C
ATOM 219 CG1 ILE A 29 26.748 38.966 -0.905 1.00 29.67 C
ATOM 220 CG2 ILE A 29 28.307 40.632 0.098 1.00 28.24 C
ATOM 221 CD1 ILE A 29 27.050 39.283 -2.303 1.00 31.84 C