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5E6E.pdb
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HEADER OXYGEN TRANSPORT 09-OCT-15 5E6E
TITLE CRYSTAL STRUCTURE OF CARBONMONOXY SICKLE HEMOGLOBIN IN R-STATE
TITLE 2 CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-GLOBIN, HEMOGLOBIN ALPHA CHAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HEMOGLOBIN SUBUNIT BETA;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: BETA-GLOBIN, HEMOGLOBIN BETA CHAIN;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HBA1, HBA2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: HBB;
SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS SICKLE CELL, HEMOGLOBIN, R-STATE, ALLOSTERIC, OXYGEN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.K.SAFO,M.H.AHMED
REVDAT 1 28-OCT-15 5E6E 0
JRNL AUTH M.H.AHMED,M.S.GHATGE,A.M.OMAR,G.E.KELLOGG,M.K.SAFO
JRNL TITL CRYSTAL STRUCTURE OF CARBONMONOXY SICKLE HEMOGLOBIN IN
JRNL TITL 2 R-STATE CONFORMATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1786400.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 27308
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 SET) : 0.193
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1387
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.76
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1907
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 106
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2190
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 109
REMARK 3 SOLVENT ATOMS : 441
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.78000
REMARK 3 B22 (A**2) : -0.78000
REMARK 3 B33 (A**2) : 1.56000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.340
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 57.68
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5E6E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214375.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK 9.2SSI
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27374
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760
REMARK 200 RESOLUTION RANGE LOW (A) : 53.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 4.760
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.81
REMARK 200 R MERGE FOR SHELL (I) : 0.17500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 1LJW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.2 M PHOSPHATE, PH 6.6, LIQUID
REMARK 280 DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.53400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 26.67600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 26.67600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 47.76700
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 26.67600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 26.67600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 143.30100
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 26.67600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 26.67600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 47.76700
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 26.67600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 26.67600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 143.30100
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 95.53400
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 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 350 BIOMT1 2 0.000000 -1.000000 0.000000 53.35200
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 53.35200
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 95.53400
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 495 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 533 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 536 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 316 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 C CMO B 201 FE HEM B 202 1.79
REMARK 500 C CMO A 201 FE HEM A 202 1.85
REMARK 500 O4 PO4 A 205 O HOH A 301 2.00
REMARK 500 O HOH B 325 O HOH B 408 2.10
REMARK 500 O2D HEM A 202 O HOH A 302 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 496 O HOH B 496 8665 1.13
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 ASP A 75 58.46 -154.06
REMARK 500 ASN B 80 53.78 -158.82
REMARK 500 CYS B 93 -64.99 -94.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 535 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH A 536 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH B 501 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B 502 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH B 503 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH B 504 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH B 505 DISTANCE = 6.54 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 87 NE2
REMARK 620 2 HEM A 202 NA 88.7
REMARK 620 3 HEM A 202 NB 86.2 91.9
REMARK 620 4 HEM A 202 NC 92.9 178.4 88.5
REMARK 620 5 HEM A 202 ND 92.8 89.2 178.5 90.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 92 NE2
REMARK 620 2 HEM B 202 NA 88.3
REMARK 620 3 HEM B 202 NB 85.8 88.2
REMARK 620 4 HEM B 202 NC 87.8 176.0 92.3
REMARK 620 5 HEM B 202 ND 90.9 91.6 176.6 87.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CMO A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MBN A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MBN A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CMO B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 202
DBREF 5E6E A 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 5E6E B 1 146 UNP P68871 HBB_HUMAN 2 147
SEQADV 5E6E VAL B 6 UNP P68871 GLU 7 CONFLICT
SEQRES 1 A 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 A 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 A 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 A 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 A 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 A 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 B 146 VAL HIS LEU THR PRO VAL GLU LYS SER ALA VAL THR ALA
SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 B 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 B 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 B 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 B 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 B 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 B 146 LYS TYR HIS
HET CMO A 201 2
HET HEM A 202 43
HET MBN A 203 7
HET MBN A 204 7
HET PO4 A 205 5
HET CMO B 201 2
HET HEM B 202 43
HETNAM CMO CARBON MONOXIDE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM MBN TOLUENE
HETNAM PO4 PHOSPHATE ION
HETSYN HEM HEME
FORMUL 3 CMO 2(C O)
FORMUL 4 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 MBN 2(C7 H8)
FORMUL 7 PO4 O4 P 3-
FORMUL 10 HOH *441(H2 O)
HELIX 1 AA1 SER A 3 GLY A 18 1 16
HELIX 2 AA2 HIS A 20 PHE A 36 1 17
HELIX 3 AA3 PRO A 37 PHE A 43 5 7
HELIX 4 AA4 SER A 52 HIS A 72 1 21
HELIX 5 AA5 ASP A 75 LEU A 80 1 6
HELIX 6 AA6 LEU A 80 HIS A 89 1 10
HELIX 7 AA7 PRO A 95 LEU A 113 1 19
HELIX 8 AA8 THR A 118 THR A 137 1 20
HELIX 9 AA9 THR B 4 GLY B 16 1 13
HELIX 10 AB1 GLU B 22 TYR B 35 1 14
HELIX 11 AB2 PRO B 36 GLY B 46 5 11
HELIX 12 AB3 THR B 50 ASN B 57 1 8
HELIX 13 AB4 ASN B 57 ALA B 76 1 20
HELIX 14 AB5 ASN B 80 CYS B 93 1 14
HELIX 15 AB6 PRO B 100 GLY B 119 1 20
HELIX 16 AB7 LYS B 120 PHE B 122 5 3
HELIX 17 AB8 THR B 123 ALA B 142 1 20
HELIX 18 AB9 HIS B 143 HIS B 146 5 4
LINK NE2 HIS A 87 FE HEM A 202 1555 1555 2.05
LINK NE2 HIS B 92 FE HEM B 202 1555 1555 2.07
SITE 1 AC1 4 LEU A 29 HIS A 58 VAL A 62 HEM A 202
SITE 1 AC2 21 TYR A 42 PHE A 43 HIS A 45 PHE A 46
SITE 2 AC2 21 HIS A 58 LYS A 61 LEU A 83 LEU A 86
SITE 3 AC2 21 HIS A 87 LEU A 91 VAL A 93 ASN A 97
SITE 4 AC2 21 PHE A 98 LEU A 101 LEU A 136 CMO A 201
SITE 5 AC2 21 HOH A 302 HOH A 304 HOH A 357 HOH A 419
SITE 6 AC2 21 HOH A 423
SITE 1 AC3 5 TRP A 14 VAL A 17 THR A 67 PHE A 128
SITE 2 AC3 5 MBN A 204
SITE 1 AC4 6 TYR A 24 ALA A 63 LEU A 66 LEU A 105
SITE 2 AC4 6 LEU A 109 MBN A 203
SITE 1 AC5 8 HIS A 112 HOH A 301 HOH A 320 HOH A 326
SITE 2 AC5 8 HOH A 345 HOH A 376 HOH A 421 LYS B 120
SITE 1 AC6 3 HIS B 63 VAL B 67 HEM B 202
SITE 1 AC7 17 PRO A 4 HOH A 310 THR B 38 PHE B 41
SITE 2 AC7 17 PHE B 42 HIS B 63 LYS B 66 PHE B 71
SITE 3 AC7 17 HIS B 92 ASN B 102 LEU B 106 LEU B 141
SITE 4 AC7 17 CMO B 201 HOH B 302 HOH B 306 HOH B 355
SITE 5 AC7 17 HOH B 391
CRYST1 53.352 53.352 191.068 90.00 90.00 90.00 P 41 21 2 8
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 0.018743 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018743 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005234 0.00000
ATOM 1 N VAL A 1 45.646 18.685 48.882 1.00 52.32 N
ATOM 2 CA VAL A 1 46.515 17.784 49.677 1.00 49.74 C
ATOM 3 C VAL A 1 47.359 18.587 50.675 1.00 46.76 C
ATOM 4 O VAL A 1 47.994 19.578 50.304 1.00 45.97 O
ATOM 5 CB VAL A 1 47.426 16.934 48.727 1.00 54.07 C
ATOM 6 CG1 VAL A 1 46.868 17.003 47.310 1.00 51.73 C
ATOM 7 CG2 VAL A 1 48.877 17.427 48.766 1.00 55.39 C
ATOM 8 N LEU A 2 47.353 18.161 51.940 1.00 41.81 N
ATOM 9 CA LEU A 2 48.103 18.841 53.001 1.00 35.73 C
ATOM 10 C LEU A 2 49.618 18.895 52.782 1.00 32.42 C
ATOM 11 O LEU A 2 50.265 17.895 52.450 1.00 30.36 O
ATOM 12 CB LEU A 2 47.815 18.183 54.348 1.00 34.36 C
ATOM 13 CG LEU A 2 46.384 18.378 54.868 1.00 34.97 C
ATOM 14 CD1 LEU A 2 46.230 17.713 56.235 1.00 39.10 C
ATOM 15 CD2 LEU A 2 46.076 19.864 54.971 1.00 34.71 C
ATOM 16 N SER A 3 50.182 20.074 52.992 1.00 34.06 N
ATOM 17 CA SER A 3 51.609 20.272 52.813 1.00 29.21 C
ATOM 18 C SER A 3 52.330 20.015 54.123 1.00 29.60 C
ATOM 19 O SER A 3 51.691 19.812 55.168 1.00 26.90 O
ATOM 20 CB SER A 3 51.872 21.705 52.372 1.00 27.47 C
ATOM 21 OG SER A 3 51.662 22.599 53.447 1.00 31.18 O
ATOM 22 N PRO A 4 53.673 19.980 54.086 1.00 31.49 N
ATOM 23 CA PRO A 4 54.419 19.748 55.325 1.00 29.04 C
ATOM 24 C PRO A 4 54.116 20.872 56.314 1.00 28.68 C
ATOM 25 O PRO A 4 53.920 20.624 57.508 1.00 28.31 O
ATOM 26 CB PRO A 4 55.877 19.754 54.856 1.00 31.02 C
ATOM 27 CG PRO A 4 55.772 19.152 53.497 1.00 29.56 C
ATOM 28 CD PRO A 4 54.566 19.875 52.914 1.00 31.10 C
ATOM 29 N ALA A 5 54.094 22.107 55.814 1.00 27.42 N
ATOM 30 CA ALA A 5 53.792 23.258 56.662 1.00 26.13 C
ATOM 31 C ALA A 5 52.373 23.127 57.244 1.00 21.74 C
ATOM 32 O ALA A 5 52.164 23.403 58.420 1.00 25.77 O
ATOM 33 CB ALA A 5 53.932 24.562 55.871 1.00 25.08 C
ATOM 34 N ASP A 6 51.401 22.702 56.439 1.00 22.97 N
ATOM 35 CA ASP A 6 50.045 22.537 56.979 1.00 25.04 C
ATOM 36 C ASP A 6 50.032 21.510 58.101 1.00 24.14 C
ATOM 37 O ASP A 6 49.461 21.751 59.163 1.00 23.62 O
ATOM 38 CB ASP A 6 49.053 22.084 55.906 1.00 23.65 C
ATOM 39 CG ASP A 6 48.808 23.133 54.862 1.00 23.05 C
ATOM 40 OD1 ASP A 6 48.827 24.337 55.197 1.00 23.60 O
ATOM 41 OD2 ASP A 6 48.576 22.741 53.700 1.00 28.41 O
ATOM 42 N LYS A 7 50.667 20.363 57.873 1.00 22.31 N
ATOM 43 CA LYS A 7 50.698 19.324 58.888 1.00 23.10 C
ATOM 44 C LYS A 7 51.336 19.846 60.172 1.00 27.21 C
ATOM 45 O LYS A 7 50.868 19.559 61.272 1.00 25.73 O
ATOM 46 CB LYS A 7 51.421 18.090 58.340 1.00 22.84 C
ATOM 47 CG LYS A 7 50.677 17.448 57.184 1.00 26.82 C
ATOM 48 CD LYS A 7 51.292 16.127 56.763 1.00 30.31 C
ATOM 49 CE LYS A 7 52.665 16.319 56.165 1.00 39.20 C
ATOM 50 NZ LYS A 7 53.275 15.000 55.864 1.00 39.72 N
ATOM 51 N THR A 8 52.383 20.649 60.026 1.00 26.55 N
ATOM 52 CA THR A 8 53.049 21.238 61.177 1.00 27.17 C
ATOM 53 C THR A 8 52.106 22.187 61.912 1.00 26.24 C
ATOM 54 O THR A 8 51.989 22.134 63.137 1.00 23.90 O
ATOM 55 CB THR A 8 54.315 22.024 60.744 1.00 30.97 C
ATOM 56 OG1 THR A 8 55.278 21.101 60.234 1.00 31.19 O
ATOM 57 CG2 THR A 8 54.928 22.785 61.916 1.00 35.19 C
ATOM 58 N ASN A 9 51.434 23.051 61.155 1.00 25.69 N
ATOM 59 CA ASN A 9 50.517 24.018 61.741 1.00 24.44 C
ATOM 60 C ASN A 9 49.366 23.352 62.459 1.00 23.91 C
ATOM 61 O ASN A 9 49.000 23.764 63.559 1.00 22.95 O
ATOM 62 CB ASN A 9 49.984 24.974 60.667 1.00 22.41 C
ATOM 63 CG ASN A 9 51.037 25.971 60.212 1.00 27.47 C
ATOM 64 OD1 ASN A 9 51.956 26.293 60.967 1.00 26.14 O
ATOM 65 ND2 ASN A 9 50.895 26.484 58.990 1.00 20.60 N
ATOM 66 N VAL A 10 48.801 22.317 61.851 1.00 23.96 N
ATOM 67 CA VAL A 10 47.693 21.605 62.474 1.00 22.88 C
ATOM 68 C VAL A 10 48.149 20.907 63.767 1.00 26.45 C
ATOM 69 O VAL A 10 47.461 20.979 64.794 1.00 21.92 O
ATOM 70 CB VAL A 10 47.097 20.576 61.505 1.00 24.55 C
ATOM 71 CG1 VAL A 10 46.056 19.726 62.216 1.00 22.29 C
ATOM 72 CG2 VAL A 10 46.494 21.297 60.306 1.00 19.94 C
ATOM 73 N LYS A 11 49.301 20.231 63.716 1.00 26.50 N
ATOM 74 CA LYS A 11 49.832 19.553 64.897 1.00 28.33 C
ATOM 75 C LYS A 11 50.050 20.543 66.042 1.00 28.65 C
ATOM 76 O LYS A 11 49.768 20.232 67.200 1.00 28.35 O
ATOM 77 CB LYS A 11 51.157 18.846 64.573 1.00 26.85 C
ATOM 78 CG LYS A 11 50.971 17.568 63.789 1.00 36.87 C
ATOM 79 CD LYS A 11 52.297 16.912 63.439 1.00 43.98 C
ATOM 80 CE LYS A 11 52.091 15.775 62.438 1.00 52.05 C
ATOM 81 NZ LYS A 11 53.377 15.253 61.889 1.00 52.54 N
ATOM 82 N ALA A 12 50.542 21.733 65.711 1.00 28.42 N
ATOM 83 CA ALA A 12 50.801 22.752 66.715 1.00 29.31 C
ATOM 84 C ALA A 12 49.504 23.283 67.338 1.00 30.88 C
ATOM 85 O ALA A 12 49.448 23.524 68.542 1.00 28.64 O
ATOM 86 CB ALA A 12 51.603 23.894 66.103 1.00 29.02 C
ATOM 87 N ALA A 13 48.467 23.481 66.525 1.00 24.97 N
ATOM 88 CA ALA A 13 47.190 23.957 67.060 1.00 22.21 C
ATOM 89 C ALA A 13 46.648 22.841 67.953 1.00 18.41 C
ATOM 90 O ALA A 13 46.151 23.098 69.046 1.00 24.96 O
ATOM 91 CB ALA A 13 46.204 24.264 65.919 1.00 22.32 C
ATOM 92 N TRP A 14 46.771 21.601 67.486 1.00 19.64 N
ATOM 93 CA TRP A 14 46.338 20.433 68.268 1.00 23.82 C
ATOM 94 C TRP A 14 47.010 20.412 69.637 1.00 27.15 C
ATOM 95 O TRP A 14 46.371 20.174 70.669 1.00 27.94 O
ATOM 96 CB TRP A 14 46.696 19.123 67.538 1.00 23.33 C
ATOM 97 CG TRP A 14 46.715 17.909 68.457 1.00 29.60 C
ATOM 98 CD1 TRP A 14 45.640 17.163 68.866 1.00 34.31 C
ATOM 99 CD2 TRP A 14 47.859 17.366 69.139 1.00 30.85 C
ATOM 100 NE1 TRP A 14 46.045 16.198 69.768 1.00 35.73 N
ATOM 101 CE2 TRP A 14 47.397 16.308 69.959 1.00 30.84 C
ATOM 102 CE3 TRP A 14 49.224 17.689 69.154 1.00 27.32 C
ATOM 103 CZ2 TRP A 14 48.262 15.552 70.769 1.00 34.60 C
ATOM 104 CZ3 TRP A 14 50.087 16.935 69.964 1.00 34.31 C
ATOM 105 CH2 TRP A 14 49.597 15.887 70.765 1.00 33.57 C
ATOM 106 N GLY A 15 48.314 20.640 69.636 1.00 27.03 N
ATOM 107 CA GLY A 15 49.044 20.630 70.883 1.00 27.65 C
ATOM 108 C GLY A 15 48.588 21.728 71.819 1.00 26.61 C
ATOM 109 O GLY A 15 48.438 21.496 73.015 1.00 29.30 O
ATOM 110 N LYS A 16 48.354 22.919 71.283 1.00 24.95 N
ATOM 111 CA LYS A 16 47.943 24.033 72.119 1.00 27.08 C
ATOM 112 C LYS A 16 46.550 23.800 72.700 1.00 29.40 C
ATOM 113 O LYS A 16 46.269 24.167 73.851 1.00 27.20 O
ATOM 114 CB LYS A 16 47.986 25.331 71.316 1.00 30.17 C
ATOM 115 CG LYS A 16 47.749 26.572 72.150 1.00 40.03 C
ATOM 116 CD LYS A 16 48.762 26.693 73.293 1.00 45.63 C
ATOM 117 CE LYS A 16 48.396 27.841 74.240 1.00 44.02 C
ATOM 118 NZ LYS A 16 48.323 29.156 73.534 1.00 50.82 N
ATOM 119 N VAL A 17 45.672 23.191 71.906 1.00 26.73 N
ATOM 120 CA VAL A 17 44.315 22.902 72.371 1.00 24.17 C
ATOM 121 C VAL A 17 44.430 21.938 73.546 1.00 20.45 C
ATOM 122 O VAL A 17 43.746 22.071 74.562 1.00 25.52 O
ATOM 123 CB VAL A 17 43.465 22.249 71.254 1.00 24.13 C
ATOM 124 CG1 VAL A 17 42.204 21.632 71.844 1.00 21.49 C
ATOM 125 CG2 VAL A 17 43.107 23.308 70.203 1.00 25.42 C
ATOM 126 N GLY A 18 45.317 20.969 73.399 1.00 25.40 N
ATOM 127 CA GLY A 18 45.530 19.996 74.459 1.00 23.77 C
ATOM 128 C GLY A 18 44.293 19.299 74.970 1.00 27.81 C
ATOM 129 O GLY A 18 43.373 19.017 74.203 1.00 28.25 O
ATOM 130 N ALA A 19 44.274 19.037 76.277 1.00 25.24 N
ATOM 131 CA ALA A 19 43.164 18.346 76.923 1.00 26.96 C
ATOM 132 C ALA A 19 41.794 19.014 76.839 1.00 26.54 C
ATOM 133 O ALA A 19 40.813 18.453 77.303 1.00 23.17 O
ATOM 134 CB ALA A 19 43.506 18.063 78.385 1.00 28.04 C
ATOM 135 N HIS A 20 41.728 20.209 76.266 1.00 24.25 N
ATOM 136 CA HIS A 20 40.458 20.908 76.101 1.00 23.52 C
ATOM 137 C HIS A 20 39.743 20.444 74.819 1.00 22.09 C
ATOM 138 O HIS A 20 38.597 20.809 74.589 1.00 19.50 O
ATOM 139 CB HIS A 20 40.699 22.409 75.953 1.00 22.31 C
ATOM 140 CG HIS A 20 41.179 23.076 77.198 1.00 29.26 C
ATOM 141 ND1 HIS A 20 40.348 23.351 78.261 1.00 36.55 N
ATOM 142 CD2 HIS A 20 42.404 23.531 77.546 1.00 35.48 C
ATOM 143 CE1 HIS A 20 41.043 23.948 79.212 1.00 40.97 C
ATOM 144 NE2 HIS A 20 42.293 24.069 78.804 1.00 39.09 N
ATOM 145 N ALA A 21 40.420 19.662 73.983 1.00 22.22 N
ATOM 146 CA ALA A 21 39.833 19.238 72.714 1.00 18.50 C
ATOM 147 C ALA A 21 38.385 18.753 72.821 1.00 22.20 C
ATOM 148 O ALA A 21 37.543 19.155 72.019 1.00 21.33 O
ATOM 149 CB ALA A 21 40.693 18.181 72.068 1.00 19.33 C
ATOM 150 N GLY A 22 38.108 17.901 73.809 1.00 23.54 N
ATOM 151 CA GLY A 22 36.763 17.369 74.000 1.00 25.11 C
ATOM 152 C GLY A 22 35.738 18.447 74.299 1.00 21.69 C
ATOM 153 O GLY A 22 34.639 18.470 73.741 1.00 21.53 O
ATOM 154 N GLU A 23 36.093 19.354 75.201 1.00 18.39 N
ATOM 155 CA GLU A 23 35.206 20.456 75.525 1.00 19.98 C
ATOM 156 C GLU A 23 35.007 21.321 74.277 1.00 15.66 C
ATOM 157 O GLU A 23 33.906 21.807 74.014 1.00 17.26 O
ATOM 158 CB GLU A 23 35.808 21.316 76.646 1.00 26.69 C
ATOM 159 CG GLU A 23 35.208 22.723 76.732 1.00 22.41 C
ATOM 160 CD GLU A 23 36.056 23.678 77.571 1.00 39.41 C
ATOM 161 OE1 GLU A 23 35.837 24.915 77.483 1.00 35.58 O
ATOM 162 OE2 GLU A 23 36.935 23.184 78.319 1.00 33.93 O
ATOM 163 N TYR A 24 36.077 21.523 73.514 1.00 14.84 N
ATOM 164 CA TYR A 24 35.975 22.357 72.320 1.00 15.72 C
ATOM 165 C TYR A 24 35.109 21.710 71.234 1.00 13.90 C
ATOM 166 O TYR A 24 34.459 22.412 70.481 1.00 15.24 O
ATOM 167 CB TYR A 24 37.362 22.685 71.756 1.00 17.40 C
ATOM 168 CG TYR A 24 38.193 23.621 72.639 1.00 17.67 C
ATOM 169 CD1 TYR A 24 39.480 23.991 72.268 1.00 18.20 C
ATOM 170 CD2 TYR A 24 37.696 24.096 73.856 1.00 21.92 C
ATOM 171 CE1 TYR A 24 40.267 24.819 73.091 1.00 20.03 C
ATOM 172 CE2 TYR A 24 38.478 24.919 74.697 1.00 18.94 C
ATOM 173 CZ TYR A 24 39.759 25.270 74.305 1.00 25.95 C
ATOM 174 OH TYR A 24 40.554 26.035 75.144 1.00 24.48 O
ATOM 175 N GLY A 25 35.139 20.385 71.155 1.00 16.86 N
ATOM 176 CA GLY A 25 34.303 19.689 70.182 1.00 21.15 C
ATOM 177 C GLY A 25 32.837 19.943 70.497 1.00 19.35 C
ATOM 178 O GLY A 25 32.014 20.168 69.595 1.00 14.41 O
ATOM 179 N ALA A 26 32.503 19.923 71.788 1.00 18.80 N
ATOM 180 CA ALA A 26 31.123 20.166 72.213 1.00 16.39 C
ATOM 181 C ALA A 26 30.720 21.601 71.910 1.00 17.89 C
ATOM 182 O ALA A 26 29.608 21.863 71.456 1.00 14.42 O
ATOM 183 CB ALA A 26 30.968 19.871 73.696 1.00 17.24 C
ATOM 184 N GLU A 27 31.622 22.538 72.168 1.00 14.40 N
ATOM 185 CA GLU A 27 31.345 23.930 71.896 1.00 14.95 C
ATOM 186 C GLU A 27 31.074 24.145 70.400 1.00 13.60 C
ATOM 187 O GLU A 27 30.153 24.875 70.010 1.00 13.63 O
ATOM 188 CB GLU A 27 32.533 24.792 72.333 1.00 15.97 C
ATOM 189 CG GLU A 27 32.291 26.247 72.063 1.00 18.02 C
ATOM 190 CD GLU A 27 33.438 27.131 72.508 1.00 16.01 C
ATOM 191 OE1 GLU A 27 34.157 26.738 73.458 1.00 20.32 O
ATOM 192 OE2 GLU A 27 33.593 28.221 71.927 1.00 17.70 O
ATOM 193 N ALA A 28 31.858 23.480 69.559 1.00 15.40 N
ATOM 194 CA ALA A 28 31.689 23.634 68.100 1.00 12.37 C
ATOM 195 C ALA A 28 30.313 23.110 67.660 1.00 9.76 C
ATOM 196 O ALA A 28 29.650 23.716 66.815 1.00 16.35 O
ATOM 197 CB ALA A 28 32.796 22.892 67.347 1.00 11.97 C
ATOM 198 N LEU A 29 29.887 21.996 68.241 1.00 12.02 N
ATOM 199 CA LEU A 29 28.569 21.445 67.925 1.00 12.47 C
ATOM 200 C LEU A 29 27.490 22.439 68.367 1.00 13.97 C
ATOM 201 O LEU A 29 26.566 22.736 67.615 1.00 16.48 O
ATOM 202 CB LEU A 29 28.360 20.108 68.627 1.00 12.52 C
ATOM 203 CG LEU A 29 29.167 18.924 68.098 1.00 11.10 C
ATOM 204 CD1 LEU A 29 29.088 17.730 69.075 1.00 17.60 C
ATOM 205 CD2 LEU A 29 28.628 18.557 66.682 1.00 16.70 C
ATOM 206 N GLU A 30 27.613 22.958 69.584 1.00 17.26 N
ATOM 207 CA GLU A 30 26.628 23.909 70.079 1.00 16.01 C
ATOM 208 C GLU A 30 26.531 25.129 69.171 1.00 17.68 C
ATOM 209 O GLU A 30 25.439 25.620 68.878 1.00 16.20 O
ATOM 210 CB GLU A 30 26.962 24.356 71.523 1.00 17.59 C
ATOM 211 CG GLU A 30 26.008 25.469 71.992 1.00 22.07 C
ATOM 212 CD GLU A 30 26.177 25.842 73.458 1.00 31.37 C
ATOM 213 OE1 GLU A 30 27.326 25.998 73.910 1.00 37.81 O
ATOM 214 OE2 GLU A 30 25.157 25.987 74.155 1.00 35.66 O
ATOM 215 N ARG A 31 27.681 25.637 68.742 1.00 15.91 N
ATOM 216 CA ARG A 31 27.705 26.777 67.844 1.00 13.80 C
ATOM 217 C ARG A 31 27.030 26.398 66.527 1.00 14.71 C
ATOM 218 O ARG A 31 26.319 27.213 65.933 1.00 17.66 O
ATOM 219 CB ARG A 31 29.141 27.208 67.558 1.00 12.81 C
ATOM 220 CG ARG A 31 29.851 27.885 68.751 1.00 10.81 C
ATOM 221 CD ARG A 31 31.338 28.129 68.441 1.00 13.94 C
ATOM 222 NE ARG A 31 31.965 28.800 69.588 1.00 15.93 N
ATOM 223 CZ ARG A 31 31.838 30.099 69.856 1.00 17.70 C
ATOM 224 NH1 ARG A 31 31.136 30.897 69.059 1.00 14.68 N
ATOM 225 NH2 ARG A 31 32.377 30.594 70.964 1.00 18.81 N
ATOM 226 N MET A 32 27.258 25.171 66.068 1.00 12.91 N
ATOM 227 CA MET A 32 26.640 24.734 64.817 1.00 10.41 C
ATOM 228 C MET A 32 25.108 24.675 64.920 1.00 14.58 C
ATOM 229 O MET A 32 24.405 25.146 64.035 1.00 15.09 O
ATOM 230 CB MET A 32 27.155 23.348 64.381 1.00 14.70 C
ATOM 231 CG MET A 32 26.526 22.906 63.048 1.00 13.04 C
ATOM 232 SD MET A 32 26.997 21.264 62.524 1.00 16.94 S
ATOM 233 CE MET A 32 26.225 20.294 63.800 1.00 18.20 C
ATOM 234 N PHE A 33 24.599 24.111 66.007 1.00 14.91 N
ATOM 235 CA PHE A 33 23.153 23.996 66.209 1.00 16.59 C
ATOM 236 C PHE A 33 22.432 25.339 66.343 1.00 15.15 C
ATOM 237 O PHE A 33 21.303 25.495 65.883 1.00 15.24 O
ATOM 238 CB PHE A 33 22.857 23.140 67.445 1.00 14.00 C
ATOM 239 CG PHE A 33 23.353 21.734 67.338 1.00 16.33 C
ATOM 240 CD1 PHE A 33 23.127 20.988 66.175 1.00 17.33 C
ATOM 241 CD2 PHE A 33 23.985 21.122 68.422 1.00 18.67 C
ATOM 242 CE1 PHE A 33 23.519 19.666 66.096 1.00 18.09 C
ATOM 243 CE2 PHE A 33 24.388 19.786 68.350 1.00 19.53 C
ATOM 244 CZ PHE A 33 24.150 19.054 67.183 1.00 20.98 C
ATOM 245 N LEU A 34 23.066 26.297 67.006 1.00 15.97 N
ATOM 246 CA LEU A 34 22.477 27.613 67.196 1.00 16.50 C
ATOM 247 C LEU A 34 22.566 28.438 65.912 1.00 19.50 C
ATOM 248 O LEU A 34 21.617 29.120 65.532 1.00 17.79 O
ATOM 249 CB LEU A 34 23.191 28.358 68.331 1.00 21.48 C
ATOM 250 CG LEU A 34 22.938 27.792 69.738 1.00 22.86 C
ATOM 251 CD1 LEU A 34 23.763 28.554 70.778 1.00 26.10 C
ATOM 252 CD2 LEU A 34 21.439 27.889 70.059 1.00 24.59 C
ATOM 253 N SER A 35 23.719 28.366 65.253 1.00 16.00 N
ATOM 254 CA SER A 35 23.954 29.115 64.029 1.00 14.69 C
ATOM 255 C SER A 35 23.290 28.582 62.785 1.00 11.85 C
ATOM 256 O SER A 35 22.845 29.365 61.932 1.00 17.89 O
ATOM 257 CB SER A 35 25.458 29.212 63.751 1.00 18.52 C
ATOM 258 OG SER A 35 26.070 30.184 64.581 1.00 20.60 O
ATOM 259 N PHE A 36 23.262 27.261 62.652 1.00 15.20 N
ATOM 260 CA PHE A 36 22.671 26.632 61.470 1.00 16.13 C
ATOM 261 C PHE A 36 21.626 25.634 61.931 1.00 14.61 C
ATOM 262 O PHE A 36 21.831 24.412 61.918 1.00 15.52 O
ATOM 263 CB PHE A 36 23.792 25.966 60.666 1.00 17.53 C
ATOM 264 CG PHE A 36 24.946 26.897 60.377 1.00 19.58 C
ATOM 265 CD1 PHE A 36 26.169 26.764 61.048 1.00 15.91 C
ATOM 266 CD2 PHE A 36 24.801 27.924 59.447 1.00 21.08 C
ATOM 267 CE1 PHE A 36 27.217 27.648 60.786 1.00 17.06 C
ATOM 268 CE2 PHE A 36 25.842 28.811 59.182 1.00 20.53 C
ATOM 269 CZ PHE A 36 27.055 28.671 59.853 1.00 19.20 C
ATOM 270 N PRO A 37 20.455 26.151 62.337 1.00 18.79 N
ATOM 271 CA PRO A 37 19.363 25.311 62.824 1.00 17.09 C
ATOM 272 C PRO A 37 18.989 24.085 61.999 1.00 15.89 C
ATOM 273 O PRO A 37 18.503 23.113 62.559 1.00 15.31 O
ATOM 274 CB PRO A 37 18.204 26.310 62.999 1.00 17.89 C
ATOM 275 CG PRO A 37 18.518 27.376 62.016 1.00 28.23 C
ATOM 276 CD PRO A 37 20.007 27.542 62.156 1.00 20.66 C
ATOM 277 N THR A 38 19.212 24.110 60.683 1.00 18.41 N
ATOM 278 CA THR A 38 18.860 22.932 59.876 1.00 21.98 C
ATOM 279 C THR A 38 19.648 21.696 60.301 1.00 22.06 C
ATOM 280 O THR A 38 19.203 20.561 60.109 1.00 21.34 O
ATOM 281 CB THR A 38 19.159 23.133 58.372 1.00 18.35 C
ATOM 282 OG1 THR A 38 20.521 23.556 58.208 1.00 19.52 O
ATOM 283 CG2 THR A 38 18.219 24.154 57.764 1.00 22.95 C
ATOM 284 N THR A 39 20.833 21.905 60.871 1.00 17.41 N
ATOM 285 CA THR A 39 21.648 20.766 61.265 1.00 16.89 C
ATOM 286 C THR A 39 21.059 19.985 62.416 1.00 21.67 C
ATOM 287 O THR A 39 21.420 18.832 62.631 1.00 19.71 O
ATOM 288 CB THR A 39 23.084 21.194 61.661 1.00 17.17 C
ATOM 289 OG1 THR A 39 23.038 22.037 62.831 1.00 14.08 O
ATOM 290 CG2 THR A 39 23.728 21.947 60.536 1.00 18.22 C
ATOM 291 N LYS A 40 20.156 20.610 63.164 1.00 18.15 N
ATOM 292 CA LYS A 40 19.551 19.934 64.317 1.00 17.84 C
ATOM 293 C LYS A 40 18.713 18.712 63.966 1.00 19.29 C
ATOM 294 O LYS A 40 18.520 17.841 64.816 1.00 23.71 O
ATOM 295 CB LYS A 40 18.703 20.930 65.117 1.00 18.73 C
ATOM 296 CG LYS A 40 19.495 22.155 65.552 1.00 15.81 C
ATOM 297 CD LYS A 40 18.701 23.030 66.531 1.00 20.93 C
ATOM 298 CE LYS A 40 17.611 23.824 65.844 1.00 25.79 C
ATOM 299 NZ LYS A 40 16.804 24.627 66.822 1.00 26.63 N
ATOM 300 N THR A 41 18.246 18.650 62.718 1.00 23.42 N
ATOM 301 CA THR A 41 17.403 17.547 62.253 1.00 28.65 C
ATOM 302 C THR A 41 18.059 16.176 62.388 1.00 26.81 C
ATOM 303 O THR A 41 17.369 15.158 62.538 1.00 25.72 O
ATOM 304 CB THR A 41 16.967 17.749 60.776 1.00 29.33 C
ATOM 305 OG1 THR A 41 18.120 17.892 59.942 1.00 39.91 O
ATOM 306 CG2 THR A 41 16.101 18.990 60.638 1.00 36.17 C
ATOM 307 N TYR A 42 19.390 16.157 62.368 1.00 23.45 N
ATOM 308 CA TYR A 42 20.156 14.913 62.481 1.00 21.30 C
ATOM 309 C TYR A 42 20.261 14.404 63.904 1.00 22.83 C
ATOM 310 O TYR A 42 20.624 13.250 64.140 1.00 25.04 O
ATOM 311 CB TYR A 42 21.561 15.128 61.924 1.00 21.61 C
ATOM 312 CG TYR A 42 21.590 15.270 60.444 1.00 21.91 C
ATOM 313 CD1 TYR A 42 21.660 14.149 59.625 1.00 19.76 C
ATOM 314 CD2 TYR A 42 21.483 16.525 59.851 1.00 18.42 C
ATOM 315 CE1 TYR A 42 21.619 14.278 58.258 1.00 20.59 C
ATOM 316 CE2 TYR A 42 21.434 16.667 58.494 1.00 26.40 C
ATOM 317 CZ TYR A 42 21.501 15.546 57.700 1.00 23.01 C
ATOM 318 OH TYR A 42 21.437 15.695 56.342 1.00 29.43 O
ATOM 319 N PHE A 43 19.928 15.259 64.861 1.00 23.28 N
ATOM 320 CA PHE A 43 20.007 14.875 66.259 1.00 23.19 C
ATOM 321 C PHE A 43 18.656 15.005 66.973 1.00 27.05 C
ATOM 322 O PHE A 43 18.574 15.568 68.059 1.00 22.96 O
ATOM 323 CB PHE A 43 21.048 15.750 66.966 1.00 19.45 C
ATOM 324 CG PHE A 43 22.433 15.669 66.355 1.00 18.05 C
ATOM 325 CD1 PHE A 43 22.760 16.414 65.222 1.00 17.78 C
ATOM 326 CD2 PHE A 43 23.402 14.847 66.925 1.00 22.37 C
ATOM 327 CE1 PHE A 43 24.033 16.346 64.671 1.00 18.22 C
ATOM 328 CE2 PHE A 43 24.691 14.770 66.379 1.00 19.03 C
ATOM 329 CZ PHE A 43 24.999 15.515 65.260 1.00 21.87 C
ATOM 330 N PRO A 44 17.587 14.445 66.380 1.00 28.35 N
ATOM 331 CA PRO A 44 16.253 14.528 66.985 1.00 28.38 C
ATOM 332 C PRO A 44 16.186 13.974 68.400 1.00 26.01 C
ATOM 333 O PRO A 44 15.495 14.528 69.251 1.00 32.98 O
ATOM 334 CB PRO A 44 15.379 13.750 65.998 1.00 28.10 C
ATOM 335 CG PRO A 44 16.323 12.686 65.501 1.00 33.46 C
ATOM 336 CD PRO A 44 17.608 13.472 65.272 1.00 27.30 C
ATOM 337 N HIS A 45 16.927 12.895 68.646 1.00 26.84 N
ATOM 338 CA HIS A 45 16.975 12.219 69.940 1.00 26.84 C
ATOM 339 C HIS A 45 17.940 12.806 70.970 1.00 26.43 C
ATOM 340 O HIS A 45 18.106 12.243 72.058 1.00 28.50 O
ATOM 341 CB HIS A 45 17.333 10.750 69.728 1.00 33.08 C
ATOM 342 CG HIS A 45 18.637 10.548 69.022 1.00 31.20 C
ATOM 343 ND1 HIS A 45 18.860 10.991 67.733 1.00 28.69 N
ATOM 344 CD2 HIS A 45 19.784 9.946 69.419 1.00 25.71 C
ATOM 345 CE1 HIS A 45 20.092 10.669 67.369 1.00 28.97 C
ATOM 346 NE2 HIS A 45 20.673 10.035 68.372 1.00 26.24 N
ATOM 347 N PHE A 46 18.599 13.905 70.610 1.00 23.64 N
ATOM 348 CA PHE A 46 19.534 14.590 71.499 1.00 23.38 C
ATOM 349 C PHE A 46 18.830 15.769 72.140 1.00 19.82 C
ATOM 350 O PHE A 46 17.976 16.400 71.511 1.00 22.72 O
ATOM 351 CB PHE A 46 20.705 15.225 70.716 1.00 22.22 C
ATOM 352 CG PHE A 46 21.836 14.297 70.401 1.00 27.81 C
ATOM 353 CD1 PHE A 46 23.132 14.621 70.812 1.00 26.57 C
ATOM 354 CD2 PHE A 46 21.639 13.153 69.629 1.00 22.48 C
ATOM 355 CE1 PHE A 46 24.215 13.826 70.462 1.00 22.76 C
ATOM 356 CE2 PHE A 46 22.720 12.343 69.272 1.00 27.06 C
ATOM 357 CZ PHE A 46 24.010 12.684 69.687 1.00 26.11 C
ATOM 358 N ASP A 47 19.170 16.053 73.391 1.00 18.79 N
ATOM 359 CA ASP A 47 18.681 17.255 74.052 1.00 19.32 C
ATOM 360 C ASP A 47 19.820 18.188 73.601 1.00 21.11 C
ATOM 361 O ASP A 47 20.980 17.939 73.934 1.00 21.22 O
ATOM 362 CB ASP A 47 18.737 17.122 75.569 1.00 23.37 C
ATOM 363 CG ASP A 47 18.533 18.452 76.276 1.00 26.52 C
ATOM 364 OD1 ASP A 47 18.720 19.502 75.648 1.00 33.96 O
ATOM 365 OD2 ASP A 47 18.201 18.452 77.478 1.00 37.91 O
ATOM 366 N LEU A 48 19.507 19.246 72.857 1.00 16.48 N
ATOM 367 CA LEU A 48 20.556 20.134 72.348 1.00 19.00 C
ATOM 368 C LEU A 48 20.728 21.416 73.145 1.00 22.70 C
ATOM 369 O LEU A 48 21.361 22.370 72.681 1.00 21.86 O
ATOM 370 CB LEU A 48 20.280 20.475 70.876 1.00 17.97 C
ATOM 371 CG LEU A 48 20.174 19.257 69.950 1.00 16.66 C
ATOM 372 CD1 LEU A 48 19.764 19.722 68.544 1.00 21.67 C
ATOM 373 CD2 LEU A 48 21.510 18.502 69.926 1.00 23.31 C
ATOM 374 N SER A 49 20.164 21.443 74.345 1.00 23.22 N
ATOM 375 CA SER A 49 20.280 22.617 75.191 1.00 21.61 C
ATOM 376 C SER A 49 21.708 22.771 75.692 1.00 22.85 C
ATOM 377 O SER A 49 22.497 21.820 75.716 1.00 23.16 O
ATOM 378 CB SER A 49 19.339 22.510 76.398 1.00 21.80 C
ATOM 379 OG SER A 49 19.665 21.388 77.190 1.00 22.26 O
ATOM 380 N HIS A 50 22.031 23.985 76.094 1.00 22.28 N
ATOM 381 CA HIS A 50 23.340 24.288 76.626 1.00 22.38 C
ATOM 382 C HIS A 50 23.563 23.393 77.850 1.00 24.18 C
ATOM 383 O HIS A 50 22.654 23.219 78.665 1.00 22.82 O
ATOM 384 CB HIS A 50 23.383 25.761 77.039 1.00 21.66 C
ATOM 385 CG HIS A 50 24.715 26.209 77.541 1.00 25.89 C
ATOM 386 ND1 HIS A 50 25.821 26.318 76.722 1.00 25.50 N
ATOM 387 CD2 HIS A 50 25.128 26.568 78.781 1.00 31.30 C
ATOM 388 CE1 HIS A 50 26.857 26.726 77.436 1.00 27.10 C
ATOM 389 NE2 HIS A 50 26.463 26.885 78.689 1.00 29.57 N
ATOM 390 N GLY A 51 24.752 22.811 77.968 1.00 23.65 N
ATOM 391 CA GLY A 51 25.042 21.974 79.118 1.00 22.43 C
ATOM 392 C GLY A 51 24.623 20.530 78.971 1.00 17.96 C
ATOM 393 O GLY A 51 24.839 19.709 79.866 1.00 20.84 O
ATOM 394 N SER A 52 24.008 20.214 77.840 1.00 18.19 N
ATOM 395 CA SER A 52 23.561 18.856 77.595 1.00 20.63 C
ATOM 396 C SER A 52 24.708 17.845 77.678 1.00 20.30 C
ATOM 397 O SER A 52 25.733 17.985 76.993 1.00 19.34 O
ATOM 398 CB SER A 52 22.926 18.765 76.216 1.00 16.71 C
ATOM 399 OG SER A 52 22.805 17.410 75.823 1.00 16.00 O
ATOM 400 N ALA A 53 24.536 16.825 78.512 1.00 17.53 N
ATOM 401 CA ALA A 53 25.547 15.778 78.638 1.00 16.74 C
ATOM 402 C ALA A 53 25.678 15.022 77.314 1.00 21.53 C
ATOM 403 O ALA A 53 26.723 14.443 77.034 1.00 19.89 O
ATOM 404 CB ALA A 53 25.168 14.806 79.753 1.00 19.42 C
ATOM 405 N GLN A 54 24.623 15.020 76.498 1.00 18.17 N
ATOM 406 CA GLN A 54 24.693 14.314 75.230 1.00 17.08 C
ATOM 407 C GLN A 54 25.593 15.049 74.243 1.00 18.39 C
ATOM 408 O GLN A 54 26.378 14.406 73.539 1.00 17.57 O
ATOM 409 CB GLN A 54 23.292 14.124 74.639 1.00 20.41 C
ATOM 410 CG GLN A 54 22.472 13.075 75.390 1.00 20.77 C
ATOM 411 CD GLN A 54 21.003 13.445 75.519 1.00 21.51 C
ATOM 412 OE1 GLN A 54 20.458 14.202 74.728 1.00 28.22 O
ATOM 413 NE2 GLN A 54 20.361 12.898 76.528 1.00 29.43 N
ATOM 414 N VAL A 55 25.456 16.377 74.184 1.00 17.32 N
ATOM 415 CA VAL A 55 26.280 17.183 73.303 1.00 18.27 C
ATOM 416 C VAL A 55 27.716 17.128 73.826 1.00 18.14 C
ATOM 417 O VAL A 55 28.653 17.056 73.048 1.00 16.23 O
ATOM 418 CB VAL A 55 25.818 18.658 73.222 1.00 15.24 C
ATOM 419 CG1 VAL A 55 26.806 19.445 72.352 1.00 19.36 C
ATOM 420 CG2 VAL A 55 24.403 18.750 72.605 1.00 18.65 C
ATOM 421 N LYS A 56 27.884 17.158 75.147 1.00 16.36 N
ATOM 422 CA LYS A 56 29.221 17.074 75.737 1.00 17.46 C
ATOM 423 C LYS A 56 29.915 15.759 75.340 1.00 17.84 C
ATOM 424 O LYS A 56 31.089 15.753 74.948 1.00 21.52 O
ATOM 425 CB LYS A 56 29.138 17.167 77.276 1.00 18.69 C
ATOM 426 CG LYS A 56 30.485 16.973 77.963 1.00 27.37 C
ATOM 427 CD LYS A 56 30.363 16.985 79.488 1.00 37.66 C
ATOM 428 CE LYS A 56 31.730 16.846 80.160 1.00 40.05 C
ATOM 429 NZ LYS A 56 31.610 16.864 81.647 1.00 40.10 N
ATOM 430 N GLY A 57 29.186 14.650 75.443 1.00 18.89 N
ATOM 431 CA GLY A 57 29.752 13.353 75.117 1.00 19.88 C
ATOM 432 C GLY A 57 30.075 13.248 73.640 1.00 17.77 C
ATOM 433 O GLY A 57 31.122 12.728 73.241 1.00 17.14 O
ATOM 434 N HIS A 58 29.174 13.759 72.816 1.00 19.04 N
ATOM 435 CA HIS A 58 29.388 13.687 71.391 1.00 17.42 C
ATOM 436 C HIS A 58 30.565 14.552 70.936 1.00 19.67 C
ATOM 437 O HIS A 58 31.289 14.180 69.996 1.00 15.97 O
ATOM 438 CB HIS A 58 28.127 14.089 70.660 1.00 15.99 C
ATOM 439 CG HIS A 58 28.015 13.440 69.332 1.00 17.93 C
ATOM 440 ND1 HIS A 58 27.956 12.072 69.197 1.00 16.04 N
ATOM 441 CD2 HIS A 58 28.081 13.948 68.081 1.00 17.21 C
ATOM 442 CE1 HIS A 58 28.005 11.763 67.914 1.00 18.87 C
ATOM 443 NE2 HIS A 58 28.082 12.882 67.218 1.00 19.06 N
ATOM 444 N GLY A 59 30.759 15.689 71.607 1.00 16.98 N
ATOM 445 CA GLY A 59 31.865 16.578 71.283 1.00 20.96 C
ATOM 446 C GLY A 59 33.192 15.869 71.466 1.00 17.25 C
ATOM 447 O GLY A 59 34.142 16.063 70.697 1.00 16.17 O
ATOM 448 N LYS A 60 33.278 15.060 72.513 1.00 13.20 N
ATOM 449 CA LYS A 60 34.484 14.307 72.782 1.00 16.75 C
ATOM 450 C LYS A 60 34.728 13.297 71.652 1.00 19.22 C
ATOM 451 O LYS A 60 35.872 13.060 71.249 1.00 17.86 O
ATOM 452 CB LYS A 60 34.346 13.581 74.129 1.00 17.42 C
ATOM 453 CG LYS A 60 35.400 12.526 74.352 1.00 25.57 C
ATOM 454 CD LYS A 60 36.788 13.137 74.461 1.00 34.94 C
ATOM 455 CE LYS A 60 37.808 12.103 74.930 1.00 38.01 C
ATOM 456 NZ LYS A 60 39.158 12.714 75.089 1.00 38.70 N
ATOM 457 N LYS A 61 33.648 12.707 71.137 1.00 17.82 N
ATOM 458 CA LYS A 61 33.768 11.734 70.050 1.00 17.05 C
ATOM 459 C LYS A 61 34.261 12.426 68.781 1.00 13.47 C
ATOM 460 O LYS A 61 35.150 11.913 68.083 1.00 14.08 O
ATOM 461 CB LYS A 61 32.416 11.061 69.794 1.00 16.54 C
ATOM 462 CG LYS A 61 31.997 10.139 70.924 1.00 21.41 C
ATOM 463 CD LYS A 61 30.608 9.570 70.673 1.00 31.10 C
ATOM 464 CE LYS A 61 30.157 8.730 71.867 1.00 27.65 C
ATOM 465 NZ LYS A 61 28.762 8.250 71.662 1.00 29.66 N
ATOM 466 N VAL A 62 33.686 13.590 68.489 1.00 13.98 N
ATOM 467 CA VAL A 62 34.094 14.348 67.299 1.00 13.83 C
ATOM 468 C VAL A 62 35.582 14.696 67.432 1.00 17.51 C
ATOM 469 O VAL A 62 36.367 14.480 66.514 1.00 13.65 O
ATOM 470 CB VAL A 62 33.254 15.634 67.152 1.00 14.87 C
ATOM 471 CG1 VAL A 62 33.833 16.539 66.082 1.00 12.22 C
ATOM 472 CG2 VAL A 62 31.784 15.235 66.812 1.00 15.17 C
ATOM 473 N ALA A 63 35.959 15.233 68.589 1.00 16.27 N
ATOM 474 CA ALA A 63 37.350 15.586 68.860 1.00 18.17 C
ATOM 475 C ALA A 63 38.298 14.411 68.648 1.00 15.95 C
ATOM 476 O ALA A 63 39.391 14.570 68.071 1.00 16.53 O
ATOM 477 CB ALA A 63 37.482 16.084 70.302 1.00 15.67 C
ATOM 478 N ASP A 64 37.916 13.239 69.154 1.00 16.68 N
ATOM 479 CA ASP A 64 38.756 12.042 69.020 1.00 20.39 C
ATOM 480 C ASP A 64 38.946 11.619 67.569 1.00 15.53 C
ATOM 481 O ASP A 64 40.006 11.117 67.189 1.00 16.16 O
ATOM 482 CB ASP A 64 38.162 10.862 69.794 1.00 18.38 C
ATOM 483 CG ASP A 64 38.406 10.954 71.293 1.00 24.06 C
ATOM 484 OD1 ASP A 64 39.149 11.852 71.749 1.00 26.00 O
ATOM 485 OD2 ASP A 64 37.850 10.107 72.020 1.00 27.50 O
ATOM 486 N ALA A 65 37.904 11.780 66.768 1.00 16.31 N
ATOM 487 CA ALA A 65 37.992 11.430 65.362 1.00 16.87 C
ATOM 488 C ALA A 65 38.954 12.405 64.663 1.00 14.04 C
ATOM 489 O ALA A 65 39.760 12.012 63.815 1.00 14.81 O
ATOM 490 CB ALA A 65 36.606 11.499 64.729 1.00 15.87 C
ATOM 491 N LEU A 66 38.877 13.683 65.026 1.00 11.52 N
ATOM 492 CA LEU A 66 39.746 14.672 64.411 1.00 13.92 C
ATOM 493 C LEU A 66 41.207 14.421 64.808 1.00 15.20 C
ATOM 494 O LEU A 66 42.122 14.573 63.971 1.00 14.43 O
ATOM 495 CB LEU A 66 39.306 16.079 64.811 1.00 11.57 C
ATOM 496 CG LEU A 66 37.953 16.507 64.204 1.00 11.13 C
ATOM 497 CD1 LEU A 66 37.523 17.874 64.711 1.00 15.00 C
ATOM 498 CD2 LEU A 66 38.118 16.567 62.672 1.00 16.16 C
ATOM 499 N THR A 67 41.447 14.058 66.063 1.00 17.21 N
ATOM 500 CA THR A 67 42.831 13.791 66.480 1.00 18.94 C
ATOM 501 C THR A 67 43.346 12.510 65.839 1.00 15.19 C
ATOM 502 O THR A 67 44.533 12.380 65.582 1.00 17.30 O
ATOM 503 CB THR A 67 42.969 13.726 68.009 1.00 21.27 C
ATOM 504 OG1 THR A 67 42.496 12.468 68.499 1.00 31.93 O
ATOM 505 CG2 THR A 67 42.175 14.816 68.610 1.00 12.89 C