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1bjt.pdb
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HEADER TOPOISOMERASE 29-JUN-98 1BJT
TITLE TOPOISOMERASE II RESIDUES 409-1201
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOPOISOMERASE II;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING AND CLEAVAGE CORE, RESIDUES 409-1201;
COMPND 5 EC: 5.99.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS TOPOISOMERASE, QUATERNARY CHANGE, DNA-BINDING, DNA TOPOLOGY
EXPDTA X-RAY DIFFRACTION
AUTHOR D.FASS,C.E.BOGDEN,J.M.BERGER
REVDAT 3 13-JUL-11 1BJT 1 VERSN
REVDAT 2 24-FEB-09 1BJT 1 VERSN
REVDAT 1 04-MAY-99 1BJT 0
JRNL AUTH D.FASS,C.E.BOGDEN,J.M.BERGER
JRNL TITL QUATERNARY CHANGES IN TOPOISOMERASE II MAY DIRECT ORTHOGONAL
JRNL TITL 2 MOVEMENT OF TWO DNA STRANDS.
JRNL REF NAT.STRUCT.BIOL. V. 6 322 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10201398
JRNL DOI 10.1038/7556
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.M.BERGER,S.J.GAMBLIN,S.C.HARRISON,J.C.WANG
REMARK 1 TITL STRUCTURE AND MECHANISM OF DNA TOPOISOMERASE II
REMARK 1 REF NATURE V. 379 225 1996
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.M.BERGER,S.J.GAMBLIN,S.C.HARRISON,J.C.WANG
REMARK 1 TITL ERRATUM. STRUCTURE AND MECHANISM OF DNA TOPOISOMERASE II
REMARK 1 REF NATURE V. 380 179 1996
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 40597
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) : 0.227
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2905
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4515
REMARK 3 BIN R VALUE (WORKING SET) : 0.3487
REMARK 3 BIN FREE R VALUE : 0.3731
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 373
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5598
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 217
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.59
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.16
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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:
REMARK 3 THE B FACTORS FOR RESIDUES 653 - 659 ARE VERY HIGH, BUT THE
REMARK 3 DENSITY FOR THESE RESIDUES WAS SEEN IN SOLVENT-FLATTENED
REMARK 3 MIR MAPS. THESE RESIDUES HELPED ASSIGN THE CONNECTIVITY
REMARK 3 BETWEEN DOMAINS IN THE DIMER.
REMARK 4
REMARK 4 1BJT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAR-97
REMARK 200 TEMPERATURE (KELVIN) : 118
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1402
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41611
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.20600
REMARK 200 R SYM FOR SHELL (I) : 0.20600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE ISOMORPHOUS
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.65000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.65000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 51.70000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.85000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 51.70000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.85000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 80.65000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 51.70000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 72.85000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 80.65000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 51.70000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 72.85000
REMARK 290 SMTRY3 8 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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 80.65000
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 GLU A 409
REMARK 465 ASN A 410
REMARK 465 ALA A 411
REMARK 465 LEU A 412
REMARK 465 LYS A 413
REMARK 465 LYS A 414
REMARK 465 SER A 415
REMARK 465 ASP A 416
REMARK 465 GLY A 417
REMARK 465 THR A 418
REMARK 465 SER A 485
REMARK 465 ALA A 486
REMARK 465 ASP A 487
REMARK 465 GLN A 488
REMARK 465 ILE A 489
REMARK 465 GLN A 527
REMARK 465 ASP A 528
REMARK 465 HIS A 529
REMARK 465 ASP A 530
REMARK 465 GLY A 531
REMARK 465 GLY A 632
REMARK 465 ASN A 633
REMARK 465 ASP A 634
REMARK 465 LYS A 635
REMARK 465 ASP A 636
REMARK 465 TYR A 637
REMARK 465 ILE A 638
REMARK 465 ASP A 639
REMARK 465 LEU A 640
REMARK 465 ALA A 641
REMARK 465 PHE A 642
REMARK 465 SER A 643
REMARK 465 LYS A 644
REMARK 465 LYS A 645
REMARK 465 LYS A 646
REMARK 465 ALA A 647
REMARK 465 ASP A 648
REMARK 465 ASP A 649
REMARK 465 ARG A 650
REMARK 465 LYS A 651
REMARK 465 GLU A 652
REMARK 465 GLY A 660
REMARK 465 THR A 661
REMARK 465 VAL A 662
REMARK 465 LEU A 663
REMARK 465 ASP A 664
REMARK 465 PRO A 665
REMARK 465 THR A 666
REMARK 465 LEU A 667
REMARK 465 LYS A 668
REMARK 465 GLU A 669
REMARK 465 ILE A 670
REMARK 465 PRO A 671
REMARK 465 ILE A 672
REMARK 465 SER A 673
REMARK 465 ASP A 674
REMARK 465 ASN A 1072
REMARK 465 ASP A 1073
REMARK 465 GLU A 1074
REMARK 465 ILE A 1075
REMARK 465 ALA A 1076
REMARK 465 GLU A 1077
REMARK 465 GLN A 1078
REMARK 465 ILE A 1079
REMARK 465 ASN A 1080
REMARK 465 ASP A 1081
REMARK 465 VAL A 1082
REMARK 465 LYS A 1083
REMARK 465 GLY A 1084
REMARK 465 ALA A 1085
REMARK 465 THR A 1086
REMARK 465 SER A 1087
REMARK 465 ASP A 1088
REMARK 465 GLU A 1089
REMARK 465 GLU A 1090
REMARK 465 ASP A 1091
REMARK 465 GLU A 1092
REMARK 465 GLU A 1093
REMARK 465 SER A 1094
REMARK 465 SER A 1095
REMARK 465 HIS A 1096
REMARK 465 GLU A 1097
REMARK 465 ASP A 1098
REMARK 465 THR A 1099
REMARK 465 GLU A 1100
REMARK 465 ASN A 1101
REMARK 465 VAL A 1102
REMARK 465 ILE A 1103
REMARK 465 ASN A 1104
REMARK 465 GLY A 1105
REMARK 465 PRO A 1106
REMARK 465 GLY A 1179
REMARK 465 ASN A 1180
REMARK 465 VAL A 1181
REMARK 465 PRO A 1182
REMARK 465 ASN A 1183
REMARK 465 LYS A 1184
REMARK 465 GLY A 1185
REMARK 465 SER A 1186
REMARK 465 LYS A 1187
REMARK 465 THR A 1188
REMARK 465 LYS A 1189
REMARK 465 GLY A 1190
REMARK 465 LYS A 1191
REMARK 465 GLY A 1192
REMARK 465 LYS A 1193
REMARK 465 ARG A 1194
REMARK 465 LYS A 1195
REMARK 465 LEU A 1196
REMARK 465 VAL A 1197
REMARK 465 ASP A 1198
REMARK 465 ASP A 1199
REMARK 465 GLU A 1200
REMARK 465 ASP A 1201
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 ALA A 484 O
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 PRO A 427 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO A 659 CA - C - O ANGL. DEV. = 29.3 DEGREES
REMARK 500 GLY A1178 CA - C - O ANGL. DEV. = 11.7 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 LYS A 420 99.71 -7.58
REMARK 500 THR A 437 -161.05 -101.47
REMARK 500 LEU A 547 -76.56 -45.49
REMARK 500 GLN A 553 -70.68 -34.52
REMARK 500 LYS A 570 -67.76 -94.06
REMARK 500 THR A 572 146.39 147.61
REMARK 500 LEU A 605 -71.63 -94.15
REMARK 500 GLU A 658 77.73 -115.94
REMARK 500 ASN A 677 -24.49 -18.84
REMARK 500 SER A 755 -119.62 -92.25
REMARK 500 ASP A 809 48.52 37.32
REMARK 500 VAL A 813 -159.27 -110.58
REMARK 500 SER A 921 74.26 -118.25
REMARK 500 PRO A 928 116.18 -39.93
REMARK 500 ASP A 938 -95.95 -88.14
REMARK 500 LYS A 942 89.62 -167.78
REMARK 500 ASN A 974 49.33 -141.50
REMARK 500 ASN A1042 14.59 51.66
REMARK 500 LEU A1116 -67.65 -100.96
REMARK 500 LYS A1126 -72.66 -65.21
REMARK 500 ARG A1177 43.08 -100.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ILE A 676 11.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 TRP A 653 21.1 L L OUTSIDE RANGE
REMARK 500 LEU A 654 21.3 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BJT A 409 1201 UNP P06786 TOP2_YEAST 409 1201
SEQADV 1BJT LEU A 547 UNP P06786 PRO 547 CONFLICT
SEQRES 1 A 793 GLU ASN ALA LEU LYS LYS SER ASP GLY THR ARG LYS SER
SEQRES 2 A 793 ARG ILE THR ASN TYR PRO LYS LEU GLU ASP ALA ASN LYS
SEQRES 3 A 793 ALA GLY THR LYS GLU GLY TYR LYS CYS THR LEU VAL LEU
SEQRES 4 A 793 THR GLU GLY ASP SER ALA LEU SER LEU ALA VAL ALA GLY
SEQRES 5 A 793 LEU ALA VAL VAL GLY ARG ASP TYR TYR GLY CYS TYR PRO
SEQRES 6 A 793 LEU ARG GLY LYS MET LEU ASN VAL ARG GLU ALA SER ALA
SEQRES 7 A 793 ASP GLN ILE LEU LYS ASN ALA GLU ILE GLN ALA ILE LYS
SEQRES 8 A 793 LYS ILE MET GLY LEU GLN HIS ARG LYS LYS TYR GLU ASP
SEQRES 9 A 793 THR LYS SER LEU ARG TYR GLY HIS LEU MET ILE MET THR
SEQRES 10 A 793 ASP GLN ASP HIS ASP GLY SER HIS ILE LYS GLY LEU ILE
SEQRES 11 A 793 ILE ASN PHE LEU GLU SER SER PHE LEU GLY LEU LEU ASP
SEQRES 12 A 793 ILE GLN GLY PHE LEU LEU GLU PHE ILE THR PRO ILE ILE
SEQRES 13 A 793 LYS VAL SER ILE THR LYS PRO THR LYS ASN THR ILE ALA
SEQRES 14 A 793 PHE TYR ASN MET PRO ASP TYR GLU LYS TRP ARG GLU GLU
SEQRES 15 A 793 GLU SER HIS LYS PHE THR TRP LYS GLN LYS TYR TYR LYS
SEQRES 16 A 793 GLY LEU GLY THR SER LEU ALA GLN GLU VAL ARG GLU TYR
SEQRES 17 A 793 PHE SER ASN LEU ASP ARG HIS LEU LYS ILE PHE HIS SER
SEQRES 18 A 793 LEU GLN GLY ASN ASP LYS ASP TYR ILE ASP LEU ALA PHE
SEQRES 19 A 793 SER LYS LYS LYS ALA ASP ASP ARG LYS GLU TRP LEU ARG
SEQRES 20 A 793 GLN TYR GLU PRO GLY THR VAL LEU ASP PRO THR LEU LYS
SEQRES 21 A 793 GLU ILE PRO ILE SER ASP PHE ILE ASN LYS GLU LEU ILE
SEQRES 22 A 793 LEU PHE SER LEU ALA ASP ASN ILE ARG SER ILE PRO ASN
SEQRES 23 A 793 VAL LEU ASP GLY PHE LYS PRO GLY GLN ARG LYS VAL LEU
SEQRES 24 A 793 TYR GLY CYS PHE LYS LYS ASN LEU LYS SER GLU LEU LYS
SEQRES 25 A 793 VAL ALA GLN LEU ALA PRO TYR VAL SER GLU CYS THR ALA
SEQRES 26 A 793 TYR HIS HIS GLY GLU GLN SER LEU ALA GLN THR ILE ILE
SEQRES 27 A 793 GLY LEU ALA GLN ASN PHE VAL GLY SER ASN ASN ILE TYR
SEQRES 28 A 793 LEU LEU LEU PRO ASN GLY ALA PHE GLY THR ARG ALA THR
SEQRES 29 A 793 GLY GLY LYS ASP ALA ALA ALA ALA ARG TYR ILE TYR THR
SEQRES 30 A 793 GLU LEU ASN LYS LEU THR ARG LYS ILE PHE HIS PRO ALA
SEQRES 31 A 793 ASP ASP PRO LEU TYR LYS TYR ILE GLN GLU ASP GLU LYS
SEQRES 32 A 793 THR VAL GLU PRO GLU TRP TYR LEU PRO ILE LEU PRO MET
SEQRES 33 A 793 ILE LEU VAL ASN GLY ALA GLU GLY ILE GLY THR GLY TRP
SEQRES 34 A 793 SER THR TYR ILE PRO PRO PHE ASN PRO LEU GLU ILE ILE
SEQRES 35 A 793 LYS ASN ILE ARG HIS LEU MET ASN ASP GLU GLU LEU GLU
SEQRES 36 A 793 GLN MET HIS PRO TRP PHE ARG GLY TRP THR GLY THR ILE
SEQRES 37 A 793 GLU GLU ILE GLU PRO LEU ARG TYR ARG MET TYR GLY ARG
SEQRES 38 A 793 ILE GLU GLN ILE GLY ASP ASN VAL LEU GLU ILE THR GLU
SEQRES 39 A 793 LEU PRO ALA ARG THR TRP THR SER THR ILE LYS GLU TYR
SEQRES 40 A 793 LEU LEU LEU GLY LEU SER GLY ASN ASP LYS ILE LYS PRO
SEQRES 41 A 793 TRP ILE LYS ASP MET GLU GLU GLN HIS ASP ASP ASN ILE
SEQRES 42 A 793 LYS PHE ILE ILE THR LEU SER PRO GLU GLU MET ALA LYS
SEQRES 43 A 793 THR ARG LYS ILE GLY PHE TYR GLU ARG PHE LYS LEU ILE
SEQRES 44 A 793 SER PRO ILE SER LEU MET ASN MET VAL ALA PHE ASP PRO
SEQRES 45 A 793 HIS GLY LYS ILE LYS LYS TYR ASN SER VAL ASN GLU ILE
SEQRES 46 A 793 LEU SER GLU PHE TYR TYR VAL ARG LEU GLU TYR TYR GLN
SEQRES 47 A 793 LYS ARG LYS ASP HIS MET SER GLU ARG LEU GLN TRP GLU
SEQRES 48 A 793 VAL GLU LYS TYR SER PHE GLN VAL LYS PHE ILE LYS MET
SEQRES 49 A 793 ILE ILE GLU LYS GLU LEU THR VAL THR ASN LYS PRO ARG
SEQRES 50 A 793 ASN ALA ILE ILE GLN GLU LEU GLU ASN LEU GLY PHE PRO
SEQRES 51 A 793 ARG PHE ASN LYS GLU GLY LYS PRO TYR TYR GLY SER PRO
SEQRES 52 A 793 ASN ASP GLU ILE ALA GLU GLN ILE ASN ASP VAL LYS GLY
SEQRES 53 A 793 ALA THR SER ASP GLU GLU ASP GLU GLU SER SER HIS GLU
SEQRES 54 A 793 ASP THR GLU ASN VAL ILE ASN GLY PRO GLU GLU LEU TYR
SEQRES 55 A 793 GLY THR TYR GLU TYR LEU LEU GLY MET ARG ILE TRP SER
SEQRES 56 A 793 LEU THR LYS GLU ARG TYR GLN LYS LEU LEU LYS GLN LYS
SEQRES 57 A 793 GLN GLU LYS GLU THR GLU LEU GLU ASN LEU LEU LYS LEU
SEQRES 58 A 793 SER ALA LYS ASP ILE TRP ASN THR ASP LEU LYS ALA PHE
SEQRES 59 A 793 GLU VAL GLY TYR GLN GLU PHE LEU GLN ARG ASP ALA GLU
SEQRES 60 A 793 ALA ARG GLY GLY ASN VAL PRO ASN LYS GLY SER LYS THR
SEQRES 61 A 793 LYS GLY LYS GLY LYS ARG LYS LEU VAL ASP ASP GLU ASP
FORMUL 2 HOH *217(H2 O)
HELIX 1 1 LYS A 438 LYS A 442 5 5
HELIX 2 2 ASP A 451 VAL A 464 1 14
HELIX 3 3 ASN A 492 MET A 502 1 11
HELIX 4 4 ILE A 534 SER A 545 1 12
HELIX 5 5 MET A 581 GLU A 590 1 10
HELIX 6 6 THR A 607 SER A 629 5 23
HELIX 7 7 ASN A 677 SER A 691 5 15
HELIX 8 8 PRO A 701 LYS A 713 1 13
HELIX 9 9 VAL A 721 THR A 732 1 12
HELIX 10 10 LEU A 741 ALA A 749 1 9
HELIX 11 11 ALA A 780 TYR A 782 5 3
HELIX 12 12 THR A 791 ILE A 794 1 4
HELIX 13 13 PRO A 797 LEU A 802 5 6
HELIX 14 14 MET A 824 VAL A 827 1 4
HELIX 15 15 PRO A 846 MET A 857 1 12
HELIX 16 16 THR A 909 LEU A 920 1 12
HELIX 17 17 PRO A 949 ILE A 958 1 10
HELIX 18 18 PHE A 960 ARG A 963 1 4
HELIX 19 19 VAL A 990 ILE A 1034 1 45
HELIX 20 20 ARG A 1045 ASN A 1054 1 10
HELIX 21 21 GLU A 1114 LEU A 1117 1 4
HELIX 22 22 ILE A 1121 LEU A 1124 5 4
HELIX 23 23 LYS A 1126 LEU A 1147 1 22
HELIX 24 24 ALA A 1151 ALA A 1176 1 26
SHEET 1 A 4 LEU A 556 GLU A 558 0
SHEET 2 A 4 HIS A 520 THR A 525 1 N LEU A 521 O LEU A 557
SHEET 3 A 4 THR A 444 GLU A 449 1 N LEU A 445 O HIS A 520
SHEET 4 A 4 TYR A 469 ARG A 475 1 N GLY A 470 O THR A 444
SHEET 1 B 3 ASN A 574 PHE A 578 0
SHEET 2 B 3 ILE A 564 ILE A 568 -1 N ILE A 568 O ASN A 574
SHEET 3 B 3 TRP A 597 GLN A 599 -1 N LYS A 598 O SER A 567
SHEET 1 C 2 LEU A 761 ASN A 764 0
SHEET 2 C 2 TYR A 784 LEU A 787 -1 N GLU A 786 O LEU A 762
SHEET 1 D 2 ALA A 830 ILE A 833 0
SHEET 2 D 2 SER A 838 ILE A 841 -1 N ILE A 841 O ALA A 830
SHEET 1 E 3 ILE A 967 SER A 971 0
SHEET 2 E 3 ARG A 883 TYR A 887 -1 N MET A 886 O SER A 968
SHEET 3 E 3 THR A 875 GLU A 880 -1 N GLU A 880 O ARG A 883
SHEET 1 F 4 ASP A 932 GLU A 935 0
SHEET 2 F 4 PHE A 943 THR A 946 -1 N THR A 946 O ASP A 932
SHEET 3 F 4 VAL A 897 GLU A 902 -1 N ILE A 900 O PHE A 943
SHEET 4 F 4 ARG A 889 GLN A 892 -1 N GLU A 891 O GLU A 899
SHEET 1 G 2 MET A 975 PHE A 978 0
SHEET 2 G 2 ILE A 984 TYR A 987 -1 N TYR A 987 O MET A 975
CRYST1 103.400 145.700 161.300 90.00 90.00 90.00 C 2 2 21 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 0.009671 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006863 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006200 0.00000
ATOM 1 N ARG A 419 -3.701 2.725 60.859 1.00 86.16 N
ATOM 2 CA ARG A 419 -3.827 2.382 62.309 1.00 89.17 C
ATOM 3 C ARG A 419 -4.741 3.360 63.027 1.00 89.09 C
ATOM 4 O ARG A 419 -4.609 3.570 64.235 1.00 93.23 O
ATOM 5 CB ARG A 419 -2.457 2.400 62.965 1.00 64.87 C
ATOM 6 CG ARG A 419 -1.542 1.364 62.388 1.00 62.78 C
ATOM 7 CD ARG A 419 -0.116 1.833 62.401 1.00 61.31 C
ATOM 8 NE ARG A 419 0.707 0.950 61.581 1.00 62.61 N
ATOM 9 CZ ARG A 419 1.657 0.154 62.064 1.00 53.76 C
ATOM 10 NH1 ARG A 419 1.922 0.127 63.368 1.00 57.91 N
ATOM 11 NH2 ARG A 419 2.310 -0.655 61.250 1.00 67.83 N
ATOM 12 N LYS A 420 -5.656 3.948 62.259 1.00 85.54 N
ATOM 13 CA LYS A 420 -6.639 4.924 62.719 1.00 79.92 C
ATOM 14 C LYS A 420 -6.720 5.155 64.229 1.00 78.33 C
ATOM 15 O LYS A 420 -7.258 4.321 64.963 1.00 79.32 O
ATOM 16 CB LYS A 420 -8.026 4.533 62.194 1.00 74.19 C
ATOM 17 CG LYS A 420 -8.798 5.677 61.573 1.00 67.10 C
ATOM 18 CD LYS A 420 -9.980 6.114 62.416 1.00 61.42 C
ATOM 19 CE LYS A 420 -10.796 7.159 61.674 1.00 56.59 C
ATOM 20 NZ LYS A 420 -12.134 7.334 62.272 1.00 59.63 N
ATOM 21 N SER A 421 -6.092 6.232 64.697 1.00 74.26 N
ATOM 22 CA SER A 421 -6.156 6.591 66.110 1.00 71.20 C
ATOM 23 C SER A 421 -7.601 7.058 66.266 1.00 69.78 C
ATOM 24 O SER A 421 -8.039 7.972 65.566 1.00 71.19 O
ATOM 25 CB SER A 421 -5.156 7.713 66.438 1.00 72.21 C
ATOM 26 OG SER A 421 -5.328 8.841 65.601 1.00 74.48 O
ATOM 27 N ARG A 422 -8.352 6.394 67.139 1.00 67.54 N
ATOM 28 CA ARG A 422 -9.765 6.708 67.319 1.00 64.71 C
ATOM 29 C ARG A 422 -10.109 7.611 68.496 1.00 60.45 C
ATOM 30 O ARG A 422 -9.571 7.451 69.591 1.00 62.88 O
ATOM 31 CB ARG A 422 -10.570 5.406 67.422 1.00 68.91 C
ATOM 32 CG ARG A 422 -10.100 4.320 66.464 1.00 78.38 C
ATOM 33 CD ARG A 422 -11.169 3.272 66.217 1.00 86.56 C
ATOM 34 NE ARG A 422 -11.783 3.416 64.895 1.00 94.95 N
ATOM 35 CZ ARG A 422 -11.360 2.791 63.797 1.00 97.85 C
ATOM 36 NH1 ARG A 422 -10.315 1.973 63.853 1.00 98.49 N
ATOM 37 NH2 ARG A 422 -11.991 2.973 62.642 1.00100.00 N
ATOM 38 N ILE A 423 -11.012 8.561 68.259 1.00 51.83 N
ATOM 39 CA ILE A 423 -11.462 9.477 69.297 1.00 45.41 C
ATOM 40 C ILE A 423 -12.737 8.907 69.898 1.00 46.36 C
ATOM 41 O ILE A 423 -13.768 8.858 69.236 1.00 46.51 O
ATOM 42 CB ILE A 423 -11.751 10.862 68.724 1.00 44.91 C
ATOM 43 CG1 ILE A 423 -10.533 11.369 67.963 1.00 41.93 C
ATOM 44 CG2 ILE A 423 -12.080 11.831 69.851 1.00 46.28 C
ATOM 45 CD1 ILE A 423 -9.291 11.449 68.813 1.00 40.55 C
ATOM 46 N THR A 424 -12.665 8.504 71.163 1.00 50.47 N
ATOM 47 CA THR A 424 -13.805 7.895 71.851 1.00 55.76 C
ATOM 48 C THR A 424 -14.597 8.795 72.806 1.00 56.23 C
ATOM 49 O THR A 424 -15.754 8.506 73.115 1.00 58.97 O
ATOM 50 CB THR A 424 -13.363 6.621 72.631 1.00 55.70 C
ATOM 51 OG1 THR A 424 -12.481 6.987 73.698 1.00 60.47 O
ATOM 52 CG2 THR A 424 -12.632 5.653 71.711 1.00 55.20 C
ATOM 53 N ASN A 425 -13.990 9.892 73.249 1.00 57.82 N
ATOM 54 CA ASN A 425 -14.639 10.802 74.195 1.00 56.24 C
ATOM 55 C ASN A 425 -15.447 11.991 73.644 1.00 54.32 C
ATOM 56 O ASN A 425 -15.863 12.856 74.418 1.00 55.90 O
ATOM 57 CB ASN A 425 -13.632 11.266 75.273 1.00 61.78 C
ATOM 58 CG ASN A 425 -12.311 11.803 74.688 1.00 70.31 C
ATOM 59 OD1 ASN A 425 -11.772 11.269 73.712 1.00 71.10 O
ATOM 60 ND2 ASN A 425 -11.773 12.848 75.313 1.00 69.74 N
ATOM 61 N TYR A 426 -15.701 12.022 72.332 1.00 49.27 N
ATOM 62 CA TYR A 426 -16.477 13.112 71.714 1.00 42.74 C
ATOM 63 C TYR A 426 -17.536 12.583 70.738 1.00 39.65 C
ATOM 64 O TYR A 426 -17.283 12.425 69.546 1.00 41.12 O
ATOM 65 CB TYR A 426 -15.551 14.122 71.024 1.00 40.00 C
ATOM 66 CG TYR A 426 -14.616 14.823 71.982 1.00 39.14 C
ATOM 67 CD1 TYR A 426 -15.063 15.879 72.779 1.00 42.11 C
ATOM 68 CD2 TYR A 426 -13.297 14.398 72.133 1.00 39.50 C
ATOM 69 CE1 TYR A 426 -14.220 16.489 73.711 1.00 40.92 C
ATOM 70 CE2 TYR A 426 -12.446 14.997 73.057 1.00 38.86 C
ATOM 71 CZ TYR A 426 -12.913 16.039 73.846 1.00 44.81 C
ATOM 72 OH TYR A 426 -12.080 16.610 74.787 1.00 48.36 O
ATOM 73 N PRO A 427 -18.754 12.336 71.247 1.00 35.85 N
ATOM 74 CA PRO A 427 -19.953 11.823 70.575 1.00 34.85 C
ATOM 75 C PRO A 427 -20.470 12.650 69.423 1.00 34.22 C
ATOM 76 O PRO A 427 -21.070 12.112 68.496 1.00 37.26 O
ATOM 77 CB PRO A 427 -20.989 11.798 71.700 1.00 35.89 C
ATOM 78 CG PRO A 427 -20.167 11.620 72.923 1.00 38.00 C
ATOM 79 CD PRO A 427 -19.041 12.576 72.670 1.00 38.07 C
ATOM 80 N LYS A 428 -20.318 13.965 69.534 1.00 36.63 N
ATOM 81 CA LYS A 428 -20.777 14.886 68.501 1.00 30.50 C
ATOM 82 C LYS A 428 -19.821 14.960 67.315 1.00 30.09 C
ATOM 83 O LYS A 428 -20.123 15.587 66.304 1.00 35.18 O
ATOM 84 CB LYS A 428 -21.024 16.271 69.099 1.00 28.73 C
ATOM 85 CG LYS A 428 -22.274 16.328 69.953 1.00 33.24 C
ATOM 86 CD LYS A 428 -22.444 17.663 70.663 1.00 37.60 C
ATOM 87 CE LYS A 428 -23.854 17.788 71.245 1.00 43.67 C
ATOM 88 NZ LYS A 428 -24.881 17.875 70.154 1.00 51.02 N
ATOM 89 N LEU A 429 -18.681 14.287 67.430 1.00 26.45 N
ATOM 90 CA LEU A 429 -17.695 14.268 66.360 1.00 24.97 C
ATOM 91 C LEU A 429 -18.003 13.238 65.280 1.00 29.87 C
ATOM 92 O LEU A 429 -18.307 12.083 65.572 1.00 31.38 O
ATOM 93 CB LEU A 429 -16.300 13.978 66.924 1.00 25.44 C
ATOM 94 CG LEU A 429 -15.192 13.645 65.913 1.00 26.90 C
ATOM 95 CD1 LEU A 429 -14.922 14.843 65.015 1.00 26.44 C
ATOM 96 CD2 LEU A 429 -13.918 13.227 66.638 1.00 26.30 C
ATOM 97 N GLU A 430 -17.942 13.678 64.030 1.00 30.22 N
ATOM 98 CA GLU A 430 -18.129 12.793 62.891 1.00 33.11 C
ATOM 99 C GLU A 430 -16.748 12.828 62.257 1.00 34.67 C
ATOM 100 O GLU A 430 -16.461 13.624 61.365 1.00 34.77 O
ATOM 101 CB GLU A 430 -19.209 13.300 61.935 1.00 30.07 C
ATOM 102 CG GLU A 430 -20.614 13.122 62.477 1.00 33.36 C
ATOM 103 CD GLU A 430 -21.672 13.712 61.571 1.00 42.91 C
ATOM 104 OE1 GLU A 430 -21.513 14.878 61.139 1.00 47.35 O
ATOM 105 OE2 GLU A 430 -22.670 13.007 61.300 1.00 45.39 O
ATOM 106 N ASP A 431 -15.875 12.012 62.832 1.00 34.36 N
ATOM 107 CA ASP A 431 -14.488 11.893 62.432 1.00 32.72 C
ATOM 108 C ASP A 431 -14.308 11.479 60.980 1.00 36.39 C
ATOM 109 O ASP A 431 -14.985 10.572 60.499 1.00 41.94 O
ATOM 110 CB ASP A 431 -13.819 10.881 63.352 1.00 27.71 C
ATOM 111 CG ASP A 431 -12.321 10.998 63.360 1.00 32.33 C
ATOM 112 OD1 ASP A 431 -11.797 12.127 63.452 1.00 39.10 O
ATOM 113 OD2 ASP A 431 -11.662 9.945 63.304 1.00 35.58 O
ATOM 114 N ALA A 432 -13.419 12.172 60.273 1.00 33.41 N
ATOM 115 CA ALA A 432 -13.139 11.841 58.884 1.00 31.11 C
ATOM 116 C ALA A 432 -12.563 10.433 58.911 1.00 33.88 C
ATOM 117 O ALA A 432 -11.714 10.126 59.743 1.00 39.60 O
ATOM 118 CB ALA A 432 -12.137 12.811 58.302 1.00 23.21 C
ATOM 119 N ASN A 433 -13.066 9.566 58.042 1.00 35.53 N
ATOM 120 CA ASN A 433 -12.620 8.175 57.982 1.00 39.34 C
ATOM 121 C ASN A 433 -11.107 7.995 57.979 1.00 41.31 C
ATOM 122 O ASN A 433 -10.588 7.078 58.622 1.00 47.36 O
ATOM 123 CB ASN A 433 -13.214 7.480 56.753 1.00 35.51 C
ATOM 124 CG ASN A 433 -14.722 7.378 56.815 1.00 32.47 C
ATOM 125 OD1 ASN A 433 -15.322 7.469 57.890 1.00 31.64 O
ATOM 126 ND2 ASN A 433 -15.346 7.183 55.660 1.00 31.03 N
ATOM 127 N LYS A 434 -10.408 8.869 57.257 1.00 40.50 N
ATOM 128 CA LYS A 434 -8.955 8.793 57.159 1.00 38.91 C
ATOM 129 C LYS A 434 -8.178 9.691 58.120 1.00 34.94 C
ATOM 130 O LYS A 434 -6.982 9.908 57.951 1.00 36.84 O
ATOM 131 CB LYS A 434 -8.516 9.003 55.708 1.00 41.18 C
ATOM 132 CG LYS A 434 -9.078 7.930 54.788 1.00 45.21 C
ATOM 133 CD LYS A 434 -8.405 7.895 53.435 1.00 55.74 C
ATOM 134 CE LYS A 434 -8.878 6.687 52.630 1.00 60.95 C
ATOM 135 NZ LYS A 434 -8.255 6.617 51.276 1.00 65.72 N
ATOM 136 N ALA A 435 -8.866 10.219 59.126 1.00 35.18 N
ATOM 137 CA ALA A 435 -8.223 11.052 60.129 1.00 35.79 C
ATOM 138 C ALA A 435 -7.592 10.082 61.114 1.00 39.77 C
ATOM 139 O ALA A 435 -8.174 9.041 61.421 1.00 40.63 O
ATOM 140 CB ALA A 435 -9.242 11.918 60.829 1.00 31.63 C
ATOM 141 N GLY A 436 -6.391 10.403 61.581 1.00 44.13 N
ATOM 142 CA GLY A 436 -5.707 9.531 62.523 1.00 49.05 C
ATOM 143 C GLY A 436 -4.923 8.414 61.859 1.00 51.67 C
ATOM 144 O GLY A 436 -4.290 7.604 62.534 1.00 54.54 O
ATOM 145 N THR A 437 -4.981 8.361 60.532 1.00 54.02 N
ATOM 146 CA THR A 437 -4.269 7.349 59.760 1.00 53.03 C
ATOM 147 C THR A 437 -3.015 8.003 59.187 1.00 57.10 C
ATOM 148 O THR A 437 -2.593 9.062 59.652 1.00 57.68 O
ATOM 149 CB THR A 437 -5.127 6.832 58.582 1.00 52.07 C
ATOM 150 OG1 THR A 437 -5.211 7.844 57.572 1.00 48.01 O
ATOM 151 CG2 THR A 437 -6.532 6.478 59.047 1.00 47.57 C
ATOM 152 N LYS A 438 -2.441 7.389 58.158 1.00 62.17 N
ATOM 153 CA LYS A 438 -1.246 7.927 57.517 1.00 68.39 C
ATOM 154 C LYS A 438 -1.615 9.175 56.716 1.00 67.86 C
ATOM 155 O LYS A 438 -0.850 10.141 56.667 1.00 70.66 O
ATOM 156 CB LYS A 438 -0.632 6.880 56.583 1.00 75.22 C
ATOM 157 CG LYS A 438 0.893 6.924 56.508 1.00 85.61 C
ATOM 158 CD LYS A 438 1.518 6.548 57.853 1.00 92.21 C
ATOM 159 CE LYS A 438 3.037 6.445 57.780 1.00 93.72 C
ATOM 160 NZ LYS A 438 3.609 6.063 59.105 1.00 96.57 N
ATOM 161 N GLU A 439 -2.802 9.148 56.110 1.00 65.25 N
ATOM 162 CA GLU A 439 -3.305 10.258 55.303 1.00 61.33 C
ATOM 163 C GLU A 439 -4.024 11.351 56.106 1.00 58.33 C
ATOM 164 O GLU A 439 -4.738 12.175 55.540 1.00 58.47 O
ATOM 165 CB GLU A 439 -4.243 9.728 54.218 1.00 61.82 C
ATOM 166 CG GLU A 439 -3.597 8.777 53.230 1.00 65.73 C
ATOM 167 CD GLU A 439 -4.570 8.312 52.162 1.00 70.27 C
ATOM 168 OE1 GLU A 439 -4.691 8.995 51.122 1.00 70.38 O
ATOM 169 OE2 GLU A 439 -5.220 7.264 52.364 1.00 74.62 O
ATOM 170 N GLY A 440 -3.821 11.367 57.419 1.00 55.90 N
ATOM 171 CA GLY A 440 -4.462 12.365 58.253 1.00 52.24 C
ATOM 172 C GLY A 440 -4.100 13.780 57.854 1.00 52.18 C
ATOM 173 O GLY A 440 -4.907 14.691 57.994 1.00 54.38 O
ATOM 174 N TYR A 441 -2.898 13.959 57.315 1.00 52.95 N
ATOM 175 CA TYR A 441 -2.434 15.277 56.895 1.00 53.42 C
ATOM 176 C TYR A 441 -3.254 15.792 55.717 1.00 49.60 C
ATOM 177 O TYR A 441 -3.199 16.972 55.390 1.00 53.22 O
ATOM 178 CB TYR A 441 -0.939 15.239 56.530 1.00 56.12 C
ATOM 179 CG TYR A 441 -0.617 14.465 55.269 1.00 54.86 C
ATOM 180 CD1 TYR A 441 -0.445 13.085 55.297 1.00 55.37 C
ATOM 181 CD2 TYR A 441 -0.503 15.117 54.045 1.00 57.55 C
ATOM 182 CE1 TYR A 441 -0.171 12.372 54.132 1.00 60.30 C
ATOM 183 CE2 TYR A 441 -0.229 14.416 52.876 1.00 60.84 C
ATOM 184 CZ TYR A 441 -0.066 13.046 52.925 1.00 62.38 C
ATOM 185 OH TYR A 441 0.200 12.358 51.760 1.00 67.01 O
ATOM 186 N LYS A 442 -3.994 14.890 55.078 1.00 46.23 N
ATOM 187 CA LYS A 442 -4.839 15.235 53.940 1.00 45.64 C
ATOM 188 C LYS A 442 -6.244 15.613 54.395 1.00 44.35 C
ATOM 189 O LYS A 442 -6.971 16.304 53.687 1.00 44.66 O
ATOM 190 CB LYS A 442 -4.969 14.052 52.984 1.00 48.23 C
ATOM 191 CG LYS A 442 -3.719 13.638 52.239 1.00 56.21 C
ATOM 192 CD LYS A 442 -4.071 12.519 51.267 1.00 59.47 C
ATOM 193 CE LYS A 442 -2.891 12.077 50.430 1.00 64.49 C
ATOM 194 NZ LYS A 442 -3.315 11.022 49.470 1.00 71.08 N
ATOM 195 N CYS A 443 -6.635 15.113 55.561 1.00 42.59 N
ATOM 196 CA CYS A 443 -7.964 15.369 56.102 1.00 41.89 C
ATOM 197 C CYS A 443 -8.181 16.793 56.599 1.00 40.13 C
ATOM 198 O CYS A 443 -7.227 17.495 56.929 1.00 41.01 O
ATOM 199 CB CYS A 443 -8.269 14.365 57.206 1.00 39.66 C
ATOM 200 SG CYS A 443 -8.067 12.660 56.661 1.00 39.93 S
ATOM 201 N THR A 444 -9.446 17.204 56.659 1.00 33.58 N
ATOM 202 CA THR A 444 -9.810 18.547 57.100 1.00 32.96 C
ATOM 203 C THR A 444 -10.870 18.487 58.189 1.00 36.39 C
ATOM 204 O THR A 444 -11.859 17.774 58.051 1.00 38.17 O
ATOM 205 CB THR A 444 -10.374 19.373 55.922 1.00 31.25 C
ATOM 206 OG1 THR A 444 -9.359 19.541 54.927 1.00 38.17 O
ATOM 207 CG2 THR A 444 -10.848 20.741 56.387 1.00 27.93 C
ATOM 208 N LEU A 445 -10.657 19.228 59.273 1.00 33.62 N
ATOM 209 CA LEU A 445 -11.618 19.268 60.369 1.00 33.11 C
ATOM 210 C LEU A 445 -12.439 20.556 60.330 1.00 29.04 C
ATOM 211 O LEU A 445 -11.894 21.646 60.385 1.00 31.64 O
ATOM 212 CB LEU A 445 -10.903 19.145 61.718 1.00 34.28 C
ATOM 213 CG LEU A 445 -11.790 19.257 62.967 1.00 33.94 C
ATOM 214 CD1 LEU A 445 -12.766 18.095 63.056 1.00 28.61 C
ATOM 215 CD2 LEU A 445 -10.917 19.304 64.197 1.00 37.54 C
ATOM 216 N VAL A 446 -13.755 20.422 60.270 1.00 29.04 N
ATOM 217 CA VAL A 446 -14.631 21.580 60.221 1.00 27.35 C
ATOM 218 C VAL A 446 -15.293 21.852 61.565 1.00 29.16 C
ATOM 219 O VAL A 446 -16.167 21.105 61.997 1.00 32.27 O
ATOM 220 CB VAL A 446 -15.741 21.405 59.154 1.00 25.13 C
ATOM 221 CG1 VAL A 446 -16.614 22.645 59.085 1.00 21.38 C
ATOM 222 CG2 VAL A 446 -15.134 21.110 57.796 1.00 22.96 C
ATOM 223 N LEU A 447 -14.846 22.908 62.236 1.00 31.73 N
ATOM 224 CA LEU A 447 -15.424 23.309 63.514 1.00 33.90 C
ATOM 225 C LEU A 447 -16.608 24.212 63.211 1.00 36.74 C
ATOM 226 O LEU A 447 -16.484 25.160 62.435 1.00 41.04 O
ATOM 227 CB LEU A 447 -14.418 24.096 64.345 1.00 29.92 C
ATOM 228 CG LEU A 447 -13.102 23.420 64.689 1.00 34.53 C
ATOM 229 CD1 LEU A 447 -12.314 24.353 65.589 1.00 37.76 C
ATOM 230 CD2 LEU A 447 -13.355 22.082 65.381 1.00 35.13 C
ATOM 231 N THR A 448 -17.747 23.934 63.833 1.00 37.95 N
ATOM 232 CA THR A 448 -18.938 24.740 63.606 1.00 33.69 C
ATOM 233 C THR A 448 -19.404 25.471 64.859 1.00 34.28 C
ATOM 234 O THR A 448 -19.180 25.017 65.982 1.00 35.71 O
ATOM 235 CB THR A 448 -20.105 23.891 63.044 1.00 34.44 C
ATOM 236 OG1 THR A 448 -20.498 22.905 64.005 1.00 34.91 O
ATOM 237 CG2 THR A 448 -19.686 23.196 61.763 1.00 29.43 C
ATOM 238 N GLU A 449 -20.046 26.614 64.645 1.00 33.96 N
ATOM 239 CA GLU A 449 -20.575 27.441 65.719 1.00 35.36 C
ATOM 240 C GLU A 449 -22.021 27.790 65.388 1.00 34.85 C
ATOM 241 O GLU A 449 -22.298 28.472 64.398 1.00 38.44 O
ATOM 242 CB GLU A 449 -19.758 28.727 65.845 1.00 44.42 C
ATOM 243 CG GLU A 449 -20.296 29.686 66.892 1.00 61.18 C
ATOM 244 CD GLU A 449 -19.886 31.119 66.639 1.00 68.84 C
ATOM 245 OE1 GLU A 449 -20.146 31.619 65.520 1.00 71.03 O
ATOM 246 OE2 GLU A 449 -19.318 31.743 67.564 1.00 74.76 O
ATOM 247 N GLY A 450 -22.947 27.325 66.215 1.00 32.93 N
ATOM 248 CA GLY A 450 -24.349 27.605 65.962 1.00 31.96 C
ATOM 249 C GLY A 450 -25.020 26.494 65.181 1.00 37.06 C
ATOM 250 O GLY A 450 -24.366 25.767 64.432 1.00 40.79 O
ATOM 251 N ASP A 451 -26.332 26.363 65.354 1.00 39.45 N
ATOM 252 CA ASP A 451 -27.106 25.326 64.672 1.00 39.07 C
ATOM 253 C ASP A 451 -27.060 25.448 63.156 1.00 39.28 C
ATOM 254 O ASP A 451 -26.926 24.450 62.452 1.00 43.45 O
ATOM 255 CB ASP A 451 -28.573 25.348 65.131 1.00 39.92 C
ATOM 256 CG ASP A 451 -28.758 24.875 66.564 1.00 43.18 C
ATOM 257 OD1 ASP A 451 -27.917 24.100 67.077 1.00 44.79 O
ATOM 258 OD2 ASP A 451 -29.767 25.277 67.177 1.00 48.69 O
ATOM 259 N SER A 452 -27.155 26.674 62.657 1.00 42.26 N
ATOM 260 CA SER A 452 -27.153 26.905 61.221 1.00 43.18 C
ATOM 261 C SER A 452 -25.819 26.591 60.549 1.00 39.79 C
ATOM 262 O SER A 452 -25.802 26.161 59.395 1.00 39.33 O
ATOM 263 CB SER A 452 -27.594 28.335 60.907 1.00 47.27 C
ATOM 264 OG SER A 452 -28.257 28.383 59.653 1.00 56.63 O
ATOM 265 N ALA A 453 -24.713 26.806 61.267 1.00 36.95 N
ATOM 266 CA ALA A 453 -23.373 26.524 60.740 1.00 33.99 C
ATOM 267 C ALA A 453 -23.145 25.020 60.629 1.00 36.80 C
ATOM 268 O ALA A 453 -22.372 24.555 59.784 1.00 36.00 O
ATOM 269 CB ALA A 453 -22.318 27.141 61.618 1.00 28.48 C
ATOM 270 N LEU A 454 -23.808 24.266 61.501 1.00 35.98 N
ATOM 271 CA LEU A 454 -23.701 22.818 61.482 1.00 34.02 C
ATOM 272 C LEU A 454 -24.406 22.271 60.235 1.00 31.65 C
ATOM 273 O LEU A 454 -23.862 21.419 59.536 1.00 36.57 O
ATOM 274 CB LEU A 454 -24.313 22.218 62.752 1.00 30.21 C
ATOM 275 CG LEU A 454 -24.275 20.686 62.816 1.00 29.76 C
ATOM 276 CD1 LEU A 454 -22.841 20.176 62.695 1.00 24.82 C
ATOM 277 CD2 LEU A 454 -24.913 20.212 64.096 1.00 19.47 C
ATOM 278 N SER A 455 -25.598 22.792 59.949 1.00 24.06 N
ATOM 279 CA SER A 455 -26.377 22.367 58.791 1.00 22.92 C
ATOM 280 C SER A 455 -25.626 22.628 57.499 1.00 29.05 C
ATOM 281 O SER A 455 -25.667 21.824 56.565 1.00 32.07 O
ATOM 282 CB SER A 455 -27.706 23.118 58.736 1.00 22.05 C
ATOM 283 OG SER A 455 -28.547 22.780 59.818 1.00 34.42 O
ATOM 284 N LEU A 456 -24.952 23.771 57.444 1.00 30.61 N
ATOM 285 CA LEU A 456 -24.200 24.152 56.256 1.00 31.02 C
ATOM 286 C LEU A 456 -22.962 23.288 56.066 1.00 30.60 C
ATOM 287 O LEU A 456 -22.670 22.863 54.950 1.00 33.27 O
ATOM 288 CB LEU A 456 -23.830 25.632 56.315 1.00 32.16 C
ATOM 289 CG LEU A 456 -25.020 26.592 56.379 1.00 31.06 C
ATOM 290 CD1 LEU A 456 -24.523 28.000 56.603 1.00 37.66 C
ATOM 291 CD2 LEU A 456 -25.837 26.515 55.099 1.00 31.81 C
ATOM 292 N ALA A 457 -22.245 23.023 57.157 1.00 29.40 N
ATOM 293 CA ALA A 457 -21.052 22.185 57.103 1.00 27.17 C
ATOM 294 C ALA A 457 -21.458 20.839 56.526 1.00 29.12 C
ATOM 295 O ALA A 457 -20.825 20.326 55.609 1.00 33.92 O
ATOM 296 CB ALA A 457 -20.485 22.005 58.490 1.00 24.88 C
ATOM 297 N VAL A 458 -22.550 20.297 57.058 1.00 31.11 N
ATOM 298 CA VAL A 458 -23.100 19.020 56.616 1.00 29.43 C
ATOM 299 C VAL A 458 -23.504 19.101 55.145 1.00 30.19 C
ATOM 300 O VAL A 458 -23.259 18.166 54.383 1.00 33.55 O
ATOM 301 CB VAL A 458 -24.330 18.623 57.479 1.00 31.52 C
ATOM 302 CG1 VAL A 458 -25.061 17.424 56.885 1.00 27.12 C
ATOM 303 CG2 VAL A 458 -23.888 18.318 58.892 1.00 28.38 C
ATOM 304 N ALA A 459 -24.105 20.223 54.750 1.00 27.43 N
ATOM 305 CA ALA A 459 -24.530 20.418 53.362 1.00 26.09 C
ATOM 306 C ALA A 459 -23.330 20.337 52.439 1.00 26.01 C
ATOM 307 O ALA A 459 -23.394 19.717 51.376 1.00 27.79 O
ATOM 308 CB ALA A 459 -25.222 21.760 53.197 1.00 22.34 C
ATOM 309 N GLY A 460 -22.231 20.951 52.869 1.00 24.54 N
ATOM 310 CA GLY A 460 -21.011 20.946 52.086 1.00 28.16 C
ATOM 311 C GLY A 460 -20.374 19.576 52.065 1.00 32.78 C
ATOM 312 O GLY A 460 -19.858 19.132 51.040 1.00 35.32 O
ATOM 313 N LEU A 461 -20.425 18.899 53.206 1.00 34.92 N
ATOM 314 CA LEU A 461 -19.861 17.564 53.336 1.00 34.20 C
ATOM 315 C LEU A 461 -20.594 16.535 52.484 1.00 34.53 C
ATOM 316 O LEU A 461 -20.037 15.493 52.141 1.00 38.00 O
ATOM 317 CB LEU A 461 -19.864 17.126 54.799 1.00 31.22 C
ATOM 318 CG LEU A 461 -18.522 17.232 55.519 1.00 31.89 C
ATOM 319 CD1 LEU A 461 -17.998 18.650 55.455 1.00 33.09 C
ATOM 320 CD2 LEU A 461 -18.680 16.778 56.955 1.00 34.57 C
ATOM 321 N ALA A 462 -21.843 16.826 52.141 1.00 31.69 N
ATOM 322 CA ALA A 462 -22.633 15.918 51.315 1.00 33.20 C
ATOM 323 C ALA A 462 -22.054 15.859 49.906 1.00 35.08 C
ATOM 324 O ALA A 462 -22.316 14.922 49.146 1.00 38.89 O
ATOM 325 CB ALA A 462 -24.073 16.385 51.266 1.00 34.68 C
ATOM 326 N VAL A 463 -21.252 16.868 49.583 1.00 35.40 N
ATOM 327 CA VAL A 463 -20.618 16.998 48.280 1.00 34.67 C
ATOM 328 C VAL A 463 -19.241 16.345 48.234 1.00 36.43 C
ATOM 329 O VAL A 463 -18.955 15.550 47.337 1.00 38.94 O
ATOM 330 CB VAL A 463 -20.482 18.493 47.904 1.00 33.72 C
ATOM 331 CG1 VAL A 463 -19.681 18.662 46.633 1.00 33.35 C
ATOM 332 CG2 VAL A 463 -21.859 19.111 47.748 1.00 33.22 C
ATOM 333 N VAL A 464 -18.412 16.651 49.228 1.00 36.90 N
ATOM 334 CA VAL A 464 -17.046 16.128 49.290 1.00 36.40 C
ATOM 335 C VAL A 464 -16.845 14.763 49.948 1.00 36.33 C
ATOM 336 O VAL A 464 -15.832 14.105 49.708 1.00 41.35 O
ATOM 337 CB VAL A 464 -16.091 17.153 49.949 1.00 37.24 C
ATOM 338 CG1 VAL A 464 -16.005 18.405 49.097 1.00 35.88 C
ATOM 339 CG2 VAL A 464 -16.569 17.508 51.345 1.00 35.52 C
ATOM 340 N GLY A 465 -17.796 14.342 50.776 1.00 33.21 N
ATOM 341 CA GLY A 465 -17.677 13.060 51.446 1.00 33.10 C
ATOM 342 C GLY A 465 -17.015 13.125 52.816 1.00 33.73 C
ATOM 343 O GLY A 465 -16.419 14.142 53.182 1.00 33.23 O
ATOM 344 N ARG A 466 -17.104 12.021 53.560 1.00 33.96 N
ATOM 345 CA ARG A 466 -16.540 11.922 54.904 1.00 30.48 C
ATOM 346 C ARG A 466 -15.187 11.221 54.964 1.00 30.46 C
ATOM 347 O ARG A 466 -14.674 10.965 56.048 1.00 32.19 O
ATOM 348 CB ARG A 466 -17.521 11.216 55.847 1.00 27.65 C
ATOM 349 CG ARG A 466 -18.835 11.957 56.058 1.00 25.15 C
ATOM 350 CD ARG A 466 -19.622 11.343 57.189 1.00 24.87 C
ATOM 351 NE ARG A 466 -20.904 12.007 57.401 1.00 30.67 N
ATOM 352 CZ ARG A 466 -21.059 13.177 58.013 1.00 35.63 C
ATOM 353 NH1 ARG A 466 -20.003 13.830 58.479 1.00 36.53 N
ATOM 354 NH2 ARG A 466 -22.278 13.680 58.182 1.00 36.27 N
ATOM 355 N ASP A 467 -14.606 10.915 53.807 1.00 36.13 N
ATOM 356 CA ASP A 467 -13.306 10.247 53.760 1.00 35.80 C
ATOM 357 C ASP A 467 -12.164 11.158 54.215 1.00 38.08 C
ATOM 358 O ASP A 467 -11.316 10.748 55.011 1.00 38.43 O
ATOM 359 CB ASP A 467 -13.016 9.745 52.342 1.00 42.42 C
ATOM 360 CG ASP A 467 -13.209 8.243 52.189 1.00 44.26 C
ATOM 361 OD1 ASP A 467 -13.791 7.598 53.088 1.00 45.97 O
ATOM 362 OD2 ASP A 467 -12.772 7.706 51.149 1.00 50.08 O
ATOM 363 N TYR A 468 -12.153 12.391 53.709 1.00 35.97 N
ATOM 364 CA TYR A 468 -11.114 13.358 54.042 1.00 35.59 C
ATOM 365 C TYR A 468 -11.625 14.590 54.775 1.00 34.14 C
ATOM 366 O TYR A 468 -10.948 15.615 54.817 1.00 35.11 O
ATOM 367 CB TYR A 468 -10.367 13.775 52.775 1.00 36.95 C
ATOM 368 CG TYR A 468 -9.626 12.627 52.135 1.00 42.45 C
ATOM 369 CD1 TYR A 468 -8.431 12.160 52.678 1.00 44.25 C
ATOM 370 CD2 TYR A 468 -10.143 11.972 51.019 1.00 46.07 C
ATOM 371 CE1 TYR A 468 -7.772 11.065 52.133 1.00 48.73 C
ATOM 372 CE2 TYR A 468 -9.490 10.874 50.465 1.00 50.16 C
ATOM 373 CZ TYR A 468 -8.305 10.425 51.028 1.00 51.19 C
ATOM 374 OH TYR A 468 -7.658 9.331 50.497 1.00 56.42 O
ATOM 375 N TYR A 469 -12.821 14.493 55.349 1.00 34.31 N
ATOM 376 CA TYR A 469 -13.405 15.611 56.079 1.00 30.08 C
ATOM 377 C TYR A 469 -14.101 15.152 57.347 1.00 30.95 C
ATOM 378 O TYR A 469 -14.846 14.175 57.347 1.00 31.48 O
ATOM 379 CB TYR A 469 -14.400 16.385 55.202 1.00 26.16 C
ATOM 380 CG TYR A 469 -13.784 17.065 53.994 1.00 28.37 C
ATOM 381 CD1 TYR A 469 -13.544 16.355 52.817 1.00 31.85 C
ATOM 382 CD2 TYR A 469 -13.436 18.411 54.029 1.00 27.78 C
ATOM 383 CE1 TYR A 469 -12.971 16.966 51.710 1.00 30.18 C
ATOM 384 CE2 TYR A 469 -12.865 19.033 52.924 1.00 28.93 C
ATOM 385 CZ TYR A 469 -12.635 18.300 51.769 1.00 31.90 C
ATOM 386 OH TYR A 469 -12.063 18.897 50.674 1.00 33.73 O
ATOM 387 N GLY A 470 -13.795 15.835 58.441 1.00 28.61 N
ATOM 388 CA GLY A 470 -14.409 15.535 59.717 1.00 29.69 C
ATOM 389 C GLY A 470 -15.272 16.726 60.082 1.00 27.23 C
ATOM 390 O GLY A 470 -15.080 17.810 59.532 1.00 28.69 O
ATOM 391 N CYS A 471 -16.205 16.543 61.011 1.00 25.01 N
ATOM 392 CA CYS A 471 -17.101 17.623 61.419 1.00 28.96 C
ATOM 393 C CYS A 471 -17.381 17.587 62.918 1.00 30.76 C
ATOM 394 O CYS A 471 -17.710 16.537 63.459 1.00 30.19 O
ATOM 395 CB CYS A 471 -18.416 17.515 60.648 1.00 28.11 C
ATOM 396 SG CYS A 471 -19.577 18.841 60.975 1.00 38.97 S
ATOM 397 N TYR A 472 -17.270 18.736 63.582 1.00 33.17 N
ATOM 398 CA TYR A 472 -17.517 18.814 65.021 1.00 34.23 C
ATOM 399 C TYR A 472 -18.138 20.133 65.452 1.00 36.13 C
ATOM 400 O TYR A 472 -17.621 21.205 65.135 1.00 38.94 O