Browse entries in the PDBbind-CN Database
HEADER DNA BINDING PROTEIN 26-JUN-19 6KBS TITLE CRYSTAL STRUCTURE OF YEDK IN COMPLEX WITH SSDNA COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOS RESPONSE-ASSOCIATED PROTEIN; COMPND 3 CHAIN: B; COMPND 4 SYNONYM: E.COLI YEDK; COMPND 5 EC: 3.4.-.-; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: DNA (5'-D(*CP*GP*GP*TP*CP*GP*AP*TP*TP*C)-3'); COMPND 9 CHAIN: D; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: YEDK, C4J69_22885, ECTO6_01993, EFV06_12905, EFV16_12155, SOURCE 5 SAMEA3472108_01185, SAMEA3752559_04370; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG'; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 866768; SOURCE 8 MOL_ID: 2; SOURCE 9 SYNTHETIC: YES; SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 11 ORGANISM_TAXID: 562 KEYWDS DNA REPAIR. ABASIC SITE., DNA BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR N.WANG,H.BAO,H.HUANG REVDAT 2 22-JAN-20 6KBS 1 JRNL REVDAT 1 10-JUL-19 6KBS 0 JRNL AUTH N.WANG,H.BAO,L.CHEN,Y.LIU,Y.LI,B.WU,H.HUANG JRNL TITL MOLECULAR BASIS OF ABASIC SITE SENSING IN SINGLE-STRANDED JRNL TITL 2 DNA BY THE SRAP DOMAIN OF E. COLI YEDK. JRNL REF NUCLEIC ACIDS RES. V. 47 10388 2019 JRNL REFN ESSN 1362-4962 JRNL PMID 31504793 JRNL DOI 10.1093/NAR/GKZ744 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.12_2829: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.76 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 32237 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.173 REMARK 3 FREE R VALUE : 0.201 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 1608 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 37.7672 - 3.5603 0.99 2832 163 0.1438 0.1755 REMARK 3 2 3.5603 - 2.8262 1.00 2845 140 0.1636 0.1786 REMARK 3 3 2.8262 - 2.4691 0.99 2784 136 0.1831 0.1983 REMARK 3 4 2.4691 - 2.2433 1.00 2809 130 0.1769 0.2173 REMARK 3 5 2.2433 - 2.0826 0.99 2761 151 0.1768 0.2084 REMARK 3 6 2.0826 - 1.9598 1.00 2809 131 0.1863 0.2538 REMARK 3 7 1.9598 - 1.8616 1.00 2786 161 0.1903 0.2195 REMARK 3 8 1.8616 - 1.7806 0.99 2772 144 0.1906 0.2178 REMARK 3 9 1.7806 - 1.7121 1.00 2756 152 0.2144 0.2340 REMARK 3 10 1.7121 - 1.6530 1.00 2769 154 0.2369 0.2927 REMARK 3 11 1.6530 - 1.6013 0.96 2706 146 0.2717 0.2683 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.220 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 19.98 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.27 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 2103 REMARK 3 ANGLE : 0.845 2901 REMARK 3 CHIRALITY : 0.053 299 REMARK 3 PLANARITY : 0.005 355 REMARK 3 DIHEDRAL : 13.212 1641 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 7 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.8045 11.4137 7.8634 REMARK 3 T TENSOR REMARK 3 T11: 0.1694 T22: 0.1417 REMARK 3 T33: 0.1507 T12: -0.0228 REMARK 3 T13: -0.0119 T23: 0.0241 REMARK 3 L TENSOR REMARK 3 L11: 3.4609 L22: 1.2610 REMARK 3 L33: 4.2077 L12: -0.2693 REMARK 3 L13: 2.6605 L23: 0.0920 REMARK 3 S TENSOR REMARK 3 S11: -0.0606 S12: 0.1364 S13: 0.2366 REMARK 3 S21: -0.1214 S22: -0.0650 S23: 0.1339 REMARK 3 S31: -0.3085 S32: 0.1007 S33: 0.1525 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 19 THROUGH 74 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.3746 7.9116 17.0036 REMARK 3 T TENSOR REMARK 3 T11: 0.1120 T22: 0.1264 REMARK 3 T33: 0.1485 T12: -0.0027 REMARK 3 T13: 0.0152 T23: -0.0212 REMARK 3 L TENSOR REMARK 3 L11: 2.1803 L22: 1.9912 REMARK 3 L33: 3.5421 L12: -0.5957 REMARK 3 L13: 1.2477 L23: -0.2684 REMARK 3 S TENSOR REMARK 3 S11: -0.0290 S12: -0.1150 S13: -0.0307 REMARK 3 S21: 0.0498 S22: -0.0515 S23: 0.2960 REMARK 3 S31: -0.1108 S32: -0.2983 S33: 0.0454 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 75 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.0477 0.7219 12.2271 REMARK 3 T TENSOR REMARK 3 T11: 0.1070 T22: 0.1805 REMARK 3 T33: 0.1604 T12: -0.0062 REMARK 3 T13: 0.0042 T23: -0.0153 REMARK 3 L TENSOR REMARK 3 L11: 1.2671 L22: 2.3843 REMARK 3 L33: 2.7281 L12: 0.6599 REMARK 3 L13: 0.4100 L23: 1.1967 REMARK 3 S TENSOR REMARK 3 S11: -0.0230 S12: 0.0882 S13: -0.1700 REMARK 3 S21: -0.0113 S22: 0.1698 S23: -0.1482 REMARK 3 S31: 0.1253 S32: 0.4335 S33: -0.0302 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 130 THROUGH 159 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.8139 0.6981 16.9117 REMARK 3 T TENSOR REMARK 3 T11: 0.1021 T22: 0.0922 REMARK 3 T33: 0.1023 T12: -0.0048 REMARK 3 T13: 0.0042 T23: 0.0137 REMARK 3 L TENSOR REMARK 3 L11: 5.7235 L22: 3.5809 REMARK 3 L33: 3.7273 L12: -0.3771 REMARK 3 L13: -0.9940 L23: 1.2696 REMARK 3 S TENSOR REMARK 3 S11: -0.0411 S12: 0.1471 S13: -0.1622 REMARK 3 S21: 0.0406 S22: 0.0473 S23: -0.1018 REMARK 3 S31: 0.0894 S32: 0.0871 S33: -0.0129 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 160 THROUGH 203 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.0127 -3.5193 5.8225 REMARK 3 T TENSOR REMARK 3 T11: 0.1480 T22: 0.1408 REMARK 3 T33: 0.1447 T12: -0.0146 REMARK 3 T13: 0.0007 T23: -0.0104 REMARK 3 L TENSOR REMARK 3 L11: 4.6260 L22: 2.6088 REMARK 3 L33: 3.7401 L12: 2.1938 REMARK 3 L13: 0.3532 L23: 1.5612 REMARK 3 S TENSOR REMARK 3 S11: 0.0223 S12: 0.1400 S13: -0.2159 REMARK 3 S21: -0.0056 S22: 0.0980 S23: -0.0102 REMARK 3 S31: 0.1447 S32: 0.3891 S33: -0.0353 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 204 THROUGH 228 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.2657 16.7522 9.1212 REMARK 3 T TENSOR REMARK 3 T11: 0.2724 T22: 0.3531 REMARK 3 T33: 0.2246 T12: -0.1407 REMARK 3 T13: -0.0303 T23: 0.0305 REMARK 3 L TENSOR REMARK 3 L11: 1.9264 L22: 0.2993 REMARK 3 L33: 1.1314 L12: 0.2138 REMARK 3 L13: -1.6431 L23: -0.3740 REMARK 3 S TENSOR REMARK 3 S11: -0.1086 S12: 0.2164 S13: 0.3603 REMARK 3 S21: -0.0917 S22: 0.2535 S23: -0.1329 REMARK 3 S31: 0.4325 S32: -0.0625 S33: -0.1398 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'D' AND (RESID -1 THROUGH 7 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.9803 3.1204 24.7007 REMARK 3 T TENSOR REMARK 3 T11: 0.2874 T22: 0.4026 REMARK 3 T33: 0.2820 T12: 0.0305 REMARK 3 T13: -0.0882 T23: 0.0615 REMARK 3 L TENSOR REMARK 3 L11: 1.4180 L22: 1.6874 REMARK 3 L33: 0.8788 L12: 1.1614 REMARK 3 L13: -0.7083 L23: 0.0954 REMARK 3 S TENSOR REMARK 3 S11: 0.0091 S12: 0.0892 S13: -0.2903 REMARK 3 S21: 0.3505 S22: 0.1040 S23: -0.4904 REMARK 3 S31: 0.2434 S32: 0.4398 S33: 0.1035 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6KBS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JUN-19. REMARK 100 THE DEPOSITION ID IS D_1300012693. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-JAN-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL19U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32253 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : 0.06000 REMARK 200 R SYM (I) : NULL REMARK 200
FOR THE DATA SET : 4.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 REMARK 200 DATA REDUNDANCY IN SHELL : 5.90 REMARK 200 R MERGE FOR SHELL (I) : 0.60200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200
FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 6KBU REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.40 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRIC PH 4.0, 3% PEG6000, REMARK 280 EVAPORATION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -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 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 45.94500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.16100 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.94500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.16100 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1820 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 11610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D 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 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 D 101 LIES ON A SPECIAL POSITION. 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 DC D -2 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 NE2 GLN B 198 O HOH B 301 2.15 REMARK 500 OH TYR B 119 O HOH B 302 2.16 REMARK 500 O HOH B 398 O HOH B 470 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 DG D 3 O3' DG D 3 C3' -0.037 REMARK 500 REMARK 500 REMARK: NULL 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 DT D 6 O4' - C1' - N1 ANGL. DEV. = 2.5 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 ASP B 25 55.17 -101.58 REMARK 500 GLN B 154 -124.08 47.13 REMARK 500 REMARK 500 REMARK: NULL DBREF1 6KBS B 2 222 UNP A0A2S5ZH06_ECOLX DBREF2 6KBS B A0A2S5ZH06 2 222 DBREF 6KBS D -2 7 PDB 6KBS 6KBS -2 7 SEQADV 6KBS LEU B 223 UNP A0A2S5ZH0 EXPRESSION TAG SEQADV 6KBS GLU B 224 UNP A0A2S5ZH0 EXPRESSION TAG SEQADV 6KBS VAL B 225 UNP A0A2S5ZH0 EXPRESSION TAG SEQADV 6KBS LEU B 226 UNP A0A2S5ZH0 EXPRESSION TAG SEQADV 6KBS PHE B 227 UNP A0A2S5ZH0 EXPRESSION TAG SEQADV 6KBS GLN B 228 UNP A0A2S5ZH0 EXPRESSION TAG SEQRES 1 B 227 CYS GLY ARG PHE ALA GLN SER GLN THR ARG GLU ASP TYR SEQRES 2 B 227 LEU ALA LEU LEU ALA GLU ASP ILE GLU ARG ASP ILE PRO SEQRES 3 B 227 TYR ASP PRO GLU PRO ILE GLY ARG TYR ASN VAL ALA PRO SEQRES 4 B 227 GLY THR LYS VAL LEU LEU LEU SER GLU ARG ASP GLU HIS SEQRES 5 B 227 LEU HIS LEU ASP PRO VAL PHE TRP GLY TYR ALA PRO GLY SEQRES 6 B 227 TRP TRP ASP LYS PRO PRO LEU ILE ASN ALA ARG VAL GLU SEQRES 7 B 227 THR ALA ALA THR SER ARG MET PHE LYS PRO LEU TRP GLN SEQRES 8 B 227 HIS GLY ARG ALA ILE CYS PHE ALA ASP GLY TRP PHE GLU SEQRES 9 B 227 TRP LYS LYS GLU GLY ASP LYS LYS GLN PRO PHE PHE ILE SEQRES 10 B 227 TYR ARG ALA ASP GLY GLN PRO ILE PHE MET ALA ALA ILE SEQRES 11 B 227 GLY SER THR PRO PHE GLU ARG GLY ASP GLU ALA GLU GLY SEQRES 12 B 227 PHE LEU ILE VAL THR ALA ALA ALA ASP GLN GLY LEU VAL SEQRES 13 B 227 ASP ILE HIS ASP ARG ARG PRO LEU VAL LEU SER PRO GLU SEQRES 14 B 227 ALA ALA ARG GLU TRP MET ARG GLN GLU ILE SER GLY LYS SEQRES 15 B 227 GLU ALA SER GLU ILE ALA ALA SER GLY CYS VAL PRO ALA SEQRES 16 B 227 ASN GLN PHE SER TRP HIS PRO VAL SER ARG ALA VAL GLY SEQRES 17 B 227 ASN VAL LYS ASN GLN GLY ALA GLU LEU ILE GLN PRO VAL SEQRES 18 B 227 LEU GLU VAL LEU PHE GLN SEQRES 1 D 10 DC DG DG DT DC DG DA DT DT DC FORMUL 3 HOH *237(H2 O) HELIX 1 AA1 THR B 10 ALA B 19 1 10 HELIX 2 AA2 THR B 80 SER B 84 5 5 HELIX 3 AA3 PHE B 87 GLY B 94 1 8 HELIX 4 AA4 PRO B 135 GLY B 139 5 5 HELIX 5 AA5 GLY B 155 HIS B 160 1 6 HELIX 6 AA6 SER B 168 ARG B 177 1 10 HELIX 7 AA7 SER B 181 CYS B 193 1 13 HELIX 8 AA8 PRO B 195 ASN B 197 5 3 HELIX 9 AA9 SER B 205 ASN B 210 5 6 HELIX 10 AB1 GLY B 215 GLN B 220 5 6 SHEET 1 AA1 5 ARG B 35 VAL B 38 0 SHEET 2 AA1 5 PHE B 5 GLN B 7 -1 N PHE B 5 O VAL B 38 SHEET 3 AA1 5 GLY B 102 LYS B 108 -1 O GLY B 102 N ALA B 6 SHEET 4 AA1 5 LYS B 113 ARG B 120 -1 O PHE B 116 N GLU B 105 SHEET 5 AA1 5 PHE B 199 PRO B 203 -1 O SER B 200 N TYR B 119 SHEET 1 AA2 3 GLU B 23 ARG B 24 0 SHEET 2 AA2 3 HIS B 53 PHE B 60 1 O LEU B 54 N GLU B 23 SHEET 3 AA2 3 LYS B 43 ARG B 50 -1 N SER B 48 O HIS B 55 SHEET 1 AA3 4 ASN B 75 ARG B 77 0 SHEET 2 AA3 4 PHE B 145 ALA B 151 1 O THR B 149 N ALA B 76 SHEET 3 AA3 4 ILE B 126 GLY B 132 -1 N ILE B 131 O LEU B 146 SHEET 4 AA3 4 ARG B 162 PRO B 164 0 SHEET 1 AA4 4 ARG B 95 ALA B 100 0 SHEET 2 AA4 4 ILE B 126 GLY B 132 -1 O ILE B 126 N ALA B 100 SHEET 3 AA4 4 PHE B 145 ALA B 151 -1 O LEU B 146 N ILE B 131 SHEET 4 AA4 4 VAL B 166 LEU B 167 0 CISPEP 1 THR B 134 PRO B 135 0 -2.87 CRYST1 91.890 50.322 54.531 90.00 99.08 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010883 0.000000 0.001740 0.00000 SCALE2 0.000000 0.019872 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018571 0.00000 ATOM 1 N ACYS B 2 -9.571 1.340 14.311 0.69 27.24 N ANISOU 1 N ACYS B 2 3509 3677 3165 163 -469 -100 N ATOM 2 N BCYS B 2 -7.563 1.976 14.536 0.31 25.04 N ANISOU 2 N BCYS B 2 3059 3684 2770 234 -407 -178 N ATOM 3 CA ACYS B 2 -8.800 2.576 14.416 0.69 23.63 C ANISOU 3 CA ACYS B 2 2933 3400 2644 101 -329 -95 C ATOM 4 CA BCYS B 2 -8.875 2.606 14.424 0.31 23.33 C ANISOU 4 CA BCYS B 2 2900 3356 2610 93 -325 -90 C ATOM 5 C ACYS B 2 -9.183 3.378 15.651 0.69 21.20 C ANISOU 5 C ACYS B 2 2647 3049 2357 -57 -254 -6 C ATOM 6 C BCYS B 2 -9.220 3.422 15.653 0.31 21.15 C ANISOU 6 C BCYS B 2 2641 3042 2352 -62 -249 -4 C ATOM 7 O ACYS B 2 -10.232 3.140 16.249 0.69 19.80 O ANISOU 7 O ACYS B 2 2548 2751 2225 -126 -267 60 O ATOM 8 O BCYS B 2 -10.269 3.227 16.265 0.31 20.53 O ANISOU 8 O BCYS B 2 2637 2845 2317 -134 -258 63 O ATOM 9 CB ACYS B 2 -9.001 3.429 13.172 0.69 18.53 C ANISOU 9 CB ACYS B 2 2220 2856 1965 78 -232 -99 C ATOM 10 CB BCYS B 2 -9.965 1.566 14.205 0.31 26.19 C ANISOU 10 CB BCYS B 2 3381 3526 3045 122 -438 -76 C ATOM 11 SG ACYS B 2 -10.746 3.668 12.757 0.69 23.32 S ANISOU 11 SG ACYS B 2 2915 3294 2652 -6 -207 -34 S ATOM 12 SG BCYS B 2 -11.466 2.270 13.581 0.31 30.80 S ANISOU 12 SG BCYS B 2 3981 4046 3676 8 -348 -11 S ATOM 13 N GLY B 3 -8.337 4.341 16.013 1.00 19.19 N ANISOU 13 N GLY B 3 2314 2918 2060 -114 -184 -9 N ATOM 14 CA GLY B 3 -8.579 5.163 17.184 1.00 17.54 C ANISOU 14 CA GLY B 3 2128 2679 1857 -231 -135 36 C ATOM 15 C GLY B 3 -8.601 6.643 16.877 1.00 15.60 C ANISOU 15 C GLY B 3 1845 2465 1615 -333 -54 49 C ATOM 16 O GLY B 3 -8.419 7.469 17.777 1.00 16.10 O ANISOU 16 O GLY B 3 1914 2527 1674 -408 -40 49 O ATOM 17 N ARG B 4 -8.795 6.987 15.606 1.00 14.99 N ANISOU 17 N ARG B 4 1741 2411 1544 -334 -23 59 N ATOM 18 CA ARG B 4 -8.875 8.380 15.193 1.00 14.99 C ANISOU 18 CA ARG B 4 1731 2406 1558 -445 17 99 C ATOM 19 C ARG B 4 -9.403 8.417 13.774 1.00 13.72 C ANISOU 19 C ARG B 4 1566 2253 1395 -425 36 126 C ATOM 20 O ARG B 4 -8.999 7.594 12.949 1.00 16.59 O ANISOU 20 O ARG B 4 1874 2726 1705 -335 27 100 O ATOM 21 CB ARG B 4 -7.495 9.061 15.252 1.00 17.82 C ANISOU 21 CB ARG B 4 1997 2903 1870 -533 10 119 C ATOM 22 CG ARG B 4 -7.521 10.547 15.603 1.00 17.31 C ANISOU 22 CG ARG B 4 1975 2752 1849 -682 -10 160 C ATOM 23 CD ARG B 4 -7.876 10.773 17.070 1.00 13.48 C ANISOU 23 CD ARG B 4 1569 2156 1395 -673 -39 99 C ATOM 24 NE ARG B 4 -6.775 10.386 17.974 1.00 14.05 N ANISOU 24 NE ARG B 4 1581 2334 1422 -674 -65 68 N ATOM 25 CZ ARG B 4 -5.611 11.024 18.071 1.00 16.83 C ANISOU 25 CZ ARG B 4 1860 2778 1757 -783 -105 90 C ATOM 26 NH1 ARG B 4 -4.674 10.561 18.902 1.00 17.28 N ANISOU 26 NH1 ARG B 4 1855 2942 1770 -761 -135 53 N ATOM 27 NH2 ARG B 4 -5.392 12.159 17.400 1.00 17.59 N ANISOU 27 NH2 ARG B 4 1948 2852 1882 -931 -135 162 N ATOM 28 N PHE B 5 -10.290 9.366 13.493 1.00 12.98 N ANISOU 28 N PHE B 5 1532 2050 1350 -486 46 164 N ATOM 29 CA PHE B 5 -10.779 9.520 12.123 1.00 12.17 C ANISOU 29 CA PHE B 5 1429 1959 1236 -477 54 203 C ATOM 30 C PHE B 5 -11.270 10.949 11.915 1.00 17.04 C ANISOU 30 C PHE B 5 2109 2465 1902 -577 32 264 C ATOM 31 O PHE B 5 -11.227 11.785 12.826 1.00 16.33 O ANISOU 31 O PHE B 5 2066 2281 1858 -637 -1 253 O ATOM 32 CB PHE B 5 -11.858 8.463 11.777 1.00 14.32 C ANISOU 32 CB PHE B 5 1739 2166 1535 -364 44 160 C ATOM 33 CG PHE B 5 -13.075 8.489 12.675 1.00 13.18 C ANISOU 33 CG PHE B 5 1659 1885 1464 -362 41 144 C ATOM 34 CD1 PHE B 5 -13.125 7.718 13.838 1.00 13.36 C ANISOU 34 CD1 PHE B 5 1689 1894 1493 -345 32 121 C ATOM 35 CD2 PHE B 5 -14.186 9.260 12.331 1.00 15.16 C ANISOU 35 CD2 PHE B 5 1948 2050 1762 -371 41 157 C ATOM 36 CE1 PHE B 5 -14.263 7.738 14.639 1.00 16.82 C ANISOU 36 CE1 PHE B 5 2150 2280 1962 -355 43 121 C ATOM 37 CE2 PHE B 5 -15.312 9.304 13.134 1.00 14.16 C ANISOU 37 CE2 PHE B 5 1838 1865 1677 -351 47 128 C ATOM 38 CZ PHE B 5 -15.347 8.543 14.291 1.00 16.97 C ANISOU 38 CZ PHE B 5 2178 2252 2017 -351 58 115 C ATOM 39 N ALA B 6 -11.697 11.238 10.673 1.00 15.18 N ANISOU 39 N ALA B 6 1883 2236 1649 -586 26 322 N ATOM 40 CA ALA B 6 -12.221 12.542 10.306 1.00 18.20 C ANISOU 40 CA ALA B 6 2347 2487 2082 -668 -32 392 C ATOM 41 C ALA B 6 -13.689 12.404 9.933 1.00 17.75 C ANISOU 41 C ALA B 6 2349 2316 2078 -565 -44 353 C ATOM 42 O ALA B 6 -14.080 11.447 9.252 1.00 17.62 O ANISOU 42 O ALA B 6 2298 2369 2028 -483 -13 331 O ATOM 43 CB ALA B 6 -11.428 13.147 9.142 1.00 16.87 C ANISOU 43 CB ALA B 6 2135 2443 1833 -799 -48 532 C ATOM 44 N GLN B 7 -14.509 13.350 10.408 1.00 16.73 N ANISOU 44 N GLN B 7 2307 2016 2033 -554 -106 326 N ATOM 45 CA GLN B 7 -15.942 13.408 10.092 1.00 14.80 C ANISOU 45 CA GLN B 7 2100 1684 1840 -451 -130 284 C ATOM 46 C GLN B 7 -16.244 14.895 9.895 1.00 19.71 C ANISOU 46 C GLN B 7 2831 2135 2524 -481 -252 317 C ATOM 47 O GLN B 7 -16.734 15.580 10.800 1.00 16.56 O ANISOU 47 O GLN B 7 2487 1618 2189 -418 -314 223 O ATOM 48 CB GLN B 7 -16.786 12.769 11.199 1.00 14.60 C ANISOU 48 CB GLN B 7 2039 1667 1842 -351 -86 171 C ATOM 49 CG GLN B 7 -18.250 12.511 10.841 1.00 15.44 C ANISOU 49 CG GLN B 7 2128 1759 1981 -253 -92 132 C ATOM 50 CD GLN B 7 -19.073 12.154 12.061 1.00 17.66 C ANISOU 50 CD GLN B 7 2349 2093 2268 -188 -54 43 C ATOM 51 OE1 GLN B 7 -19.374 13.020 12.896 1.00 17.57 O ANISOU 51 OE1 GLN B 7 2355 2051 2270 -133 -83 -38 O ATOM 52 NE2 GLN B 7 -19.423 10.866 12.193 1.00 14.64 N ANISOU 52 NE2 GLN B 7 1896 1803 1864 -198 -4 58 N ATOM 53 N SER B 8 -15.910 15.411 8.703 1.00 16.50 N ANISOU 53 N SER B 8 2461 1721 2089 -575 -307 452 N ATOM 54 CA SER B 8 -15.795 16.854 8.520 1.00 17.53 C ANISOU 54 CA SER B 8 2717 1666 2276 -667 -463 534 C ATOM 55 C SER B 8 -16.871 17.482 7.645 1.00 18.62 C ANISOU 55 C SER B 8 2948 1668 2458 -600 -573 567 C ATOM 56 O SER B 8 -17.017 18.709 7.670 1.00 20.80 O ANISOU 56 O SER B 8 3362 1727 2813 -631 -748 602 O ATOM 57 CB SER B 8 -14.418 17.207 7.934 1.00 21.77 C ANISOU 57 CB SER B 8 3234 2299 2740 -889 -479 718 C ATOM 58 OG SER B 8 -14.275 16.700 6.611 1.00 19.36 O ANISOU 58 OG SER B 8 2857 2180 2318 -925 -417 832 O ATOM 59 N GLN B 9 -17.617 16.699 6.878 1.00 18.46 N ANISOU 59 N GLN B 9 2867 1750 2396 -507 -505 553 N ATOM 60 CA GLN B 9 -18.504 17.281 5.882 1.00 19.15 C ANISOU 60 CA GLN B 9 3034 1736 2506 -460 -617 610 C ATOM 61 C GLN B 9 -19.943 17.302 6.397 1.00 18.28 C ANISOU 61 C GLN B 9 2925 1536 2484 -251 -651 439 C ATOM 62 O GLN B 9 -20.214 17.018 7.570 1.00 22.46 O ANISOU 62 O GLN B 9 3399 2086 3047 -163 -595 292 O ATOM 63 CB GLN B 9 -18.341 16.525 4.561 1.00 22.49 C ANISOU 63 CB GLN B 9 3388 2351 2806 -499 -544 713 C ATOM 64 CG GLN B 9 -16.882 16.565 4.117 1.00 24.47 C ANISOU 64 CG GLN B 9 3598 2760 2939 -693 -502 871 C ATOM 65 CD GLN B 9 -16.428 17.971 3.788 1.00 24.62 C ANISOU 65 CD GLN B 9 3741 2637 2977 -874 -662 1059 C ATOM 66 OE1 GLN B 9 -17.090 18.705 3.036 1.00 22.76 O ANISOU 66 OE1 GLN B 9 3616 2267 2764 -874 -799 1149 O ATOM 67 NE2 GLN B 9 -15.345 18.401 4.437 1.00 22.06 N ANISOU 67 NE2 GLN B 9 3410 2311 2661 -1029 -675 1114 N ATOM 68 N THR B 10 -20.880 17.666 5.522 1.00 19.87 N ANISOU 68 N THR B 10 3175 1668 2707 -171 -748 461 N ATOM 69 CA THR B 10 -22.272 17.797 5.931 1.00 19.99 C ANISOU 69 CA THR B 10 3167 1632 2797 36 -797 299 C ATOM 70 C THR B 10 -22.922 16.427 6.086 1.00 21.34 C ANISOU 70 C THR B 10 3169 2009 2931 104 -641 213 C ATOM 71 O THR B 10 -22.525 15.451 5.440 1.00 16.71 O ANISOU 71 O THR B 10 2525 1551 2272 23 -549 284 O ATOM 72 CB THR B 10 -23.078 18.608 4.910 1.00 24.46 C ANISOU 72 CB THR B 10 3835 2061 3399 110 -972 351 C ATOM 73 OG1 THR B 10 -23.503 17.756 3.833 1.00 25.58 O ANISOU 73 OG1 THR B 10 3899 2350 3470 110 -905 408 O ATOM 74 CG2 THR B 10 -22.251 19.753 4.333 1.00 30.60 C ANISOU 74 CG2 THR B 10 4794 2647 4186 -43 -1140 535 C ATOM 75 N ARG B 11 -23.941 16.374 6.956 1.00 24.89 N ANISOU 75 N ARG B 11 3535 2498 3424 254 -631 55 N ATOM 76 CA ARG B 11 -24.785 15.184 7.086 1.00 20.65 C ANISOU 76 CA ARG B 11 2834 2148 2864 295 -524 -2 C ATOM 77 C ARG B 11 -25.286 14.702 5.733 1.00 17.92 C ANISOU 77 C ARG B 11 2477 1831 2501 288 -554 70 C ATOM 78 O ARG B 11 -25.308 13.499 5.457 1.00 16.96 O ANISOU 78 O ARG B 11 2275 1826 2343 229 -476 92 O ATOM 79 CB ARG B 11 -25.989 15.481 7.990 1.00 25.33 C ANISOU 79 CB ARG B 11 3321 2818 3487 465 -540 -162 C ATOM 80 CG ARG B 11 -25.670 15.799 9.444 1.00 28.85 C ANISOU 80 CG ARG B 11 3745 3300 3918 504 -499 -270 C ATOM 81 CD ARG B 11 -26.884 16.481 10.100 1.00 20.95 C ANISOU 81 CD ARG B 11 2656 2377 2927 732 -562 -454 C ATOM 82 NE ARG B 11 -26.779 16.562 11.554 1.00 31.13 N ANISOU 82 NE ARG B 11 3873 3796 4161 791 -498 -581 N ATOM 83 CZ ARG B 11 -25.938 17.366 12.190 1.00 31.13 C ANISOU 83 CZ ARG B 11 4004 3651 4173 807 -565 -638 C ATOM 84 NH1 ARG B 11 -25.137 18.169 11.498 1.00 33.77 N ANISOU 84 NH1 ARG B 11 4545 3703 4582 743 -702 -557 N ATOM 85 NH2 ARG B 11 -25.906 17.385 13.515 1.00 37.40 N ANISOU 85 NH2 ARG B 11 4721 4594 4895 877 -506 -767 N ATOM 86 N GLU B 12 -25.754 15.624 4.891 1.00 19.64 N ANISOU 86 N GLU B 12 2783 1932 2746 361 -694 97 N ATOM 87 CA GLU B 12 -26.344 15.168 3.643 1.00 21.88 C ANISOU 87 CA GLU B 12 3046 2264 3002 373 -731 149 C ATOM 88 C GLU B 12 -25.303 14.588 2.696 1.00 19.52 C ANISOU 88 C GLU B 12 2796 2013 2608 233 -684 280 C ATOM 89 O GLU B 12 -25.661 13.785 1.833 1.00 19.94 O ANISOU 89 O GLU B 12 2803 2157 2616 238 -680 290 O ATOM 90 CB GLU B 12 -27.125 16.297 2.962 1.00 32.97 C ANISOU 90 CB GLU B 12 4539 3538 4451 495 -911 153 C ATOM 91 CG GLU B 12 -28.448 16.638 3.664 1.00 32.55 C ANISOU 91 CG GLU B 12 4382 3517 4470 696 -965 -18 C ATOM 92 CD GLU B 12 -28.223 17.420 4.945 1.00 39.36 C ANISOU 92 CD GLU B 12 5272 4309 5375 773 -982 -130 C ATOM 93 OE1 GLU B 12 -29.104 17.390 5.832 1.00 31.26 O ANISOU 93 OE1 GLU B 12 4101 3413 4363 923 -956 -293 O ATOM 94 OE2 GLU B 12 -27.147 18.058 5.068 1.00 35.40 O ANISOU 94 OE2 GLU B 12 4926 3645 4880 679 -1025 -55 O ATOM 95 N ASP B 13 -24.028 14.958 2.840 1.00 17.03 N ANISOU 95 N ASP B 13 2556 1663 2251 115 -656 368 N ATOM 96 CA ASP B 13 -22.995 14.331 2.013 1.00 20.63 C ANISOU 96 CA ASP B 13 3011 2241 2586 4 -592 469 C ATOM 97 C ASP B 13 -22.905 12.841 2.287 1.00 18.84 C ANISOU 97 C ASP B 13 2674 2150 2333 14 -482 382 C ATOM 98 O ASP B 13 -22.830 12.028 1.359 1.00 20.09 O ANISOU 98 O ASP B 13 2806 2415 2410 24 -478 386 O ATOM 99 CB ASP B 13 -21.636 14.988 2.262 1.00 18.41 C ANISOU 99 CB ASP B 13 2792 1940 2264 -137 -577 577 C ATOM 100 CG ASP B 13 -21.545 16.398 1.682 1.00 21.66 C ANISOU 100 CG ASP B 13 3342 2206 2682 -202 -729 722 C ATOM 101 OD1 ASP B 13 -20.616 17.136 2.084 1.00 19.50 O ANISOU 101 OD1 ASP B 13 3131 1862 2415 -332 -760 811 O ATOM 102 OD2 ASP B 13 -22.337 16.744 0.780 1.00 19.71 O ANISOU 102 OD2 ASP B 13 3146 1913 2429 -143 -834 764 O ATOM 103 N TYR B 14 -22.894 12.463 3.558 1.00 15.30 N ANISOU 103 N TYR B 14 2171 1696 1948 15 -415 301 N ATOM 104 CA TYR B 14 -22.847 11.046 3.894 1.00 15.33 C ANISOU 104 CA TYR B 14 2093 1788 1942 9 -349 241 C ATOM 105 C TYR B 14 -24.175 10.365 3.603 1.00 17.12 C ANISOU 105 C TYR B 14 2255 2033 2216 68 -398 185 C ATOM 106 O TYR B 14 -24.203 9.232 3.103 1.00 17.45 O ANISOU 106 O TYR B 14 2275 2122 2233 63 -417 163 O ATOM 107 CB TYR B 14 -22.476 10.888 5.369 1.00 16.56 C ANISOU 107 CB TYR B 14 2214 1941 2138 -26 -276 200 C ATOM 108 CG TYR B 14 -21.203 11.641 5.723 1.00 15.16 C ANISOU 108 CG TYR B 14 2094 1740 1927 -93 -247 250 C ATOM 109 CD1 TYR B 14 -19.955 11.144 5.350 1.00 17.43 C ANISOU 109 CD1 TYR B 14 2379 2116 2129 -152 -206 293 C ATOM 110 CD2 TYR B 14 -21.248 12.852 6.397 1.00 18.00 C ANISOU 110 CD2 TYR B 14 2503 1998 2336 -90 -282 244 C ATOM 111 CE1 TYR B 14 -18.778 11.836 5.658 1.00 18.10 C ANISOU 111 CE1 TYR B 14 2489 2209 2177 -239 -184 353 C ATOM 112 CE2 TYR B 14 -20.079 13.552 6.703 1.00 16.08 C ANISOU 112 CE2 TYR B 14 2318 1717 2073 -180 -284 300 C ATOM 113 CZ TYR B 14 -18.853 13.031 6.334 1.00 19.37 C ANISOU 113 CZ TYR B 14 2711 2245 2405 -270 -228 366 C ATOM 114 OH TYR B 14 -17.690 13.706 6.612 1.00 18.94 O ANISOU 114 OH TYR B 14 2685 2187 2326 -383 -234 436 O ATOM 115 N LEU B 15 -25.288 11.037 3.916 1.00 16.02 N ANISOU 115 N LEU B 15 2079 1863 2144 131 -437 151 N ATOM 116 CA LEU B 15 -26.593 10.390 3.802 1.00 16.06 C ANISOU 116 CA LEU B 15 1981 1926 2195 166 -477 103 C ATOM 117 C LEU B 15 -26.988 10.159 2.351 1.00 19.19 C ANISOU 117 C LEU B 15 2408 2322 2560 201 -570 121 C ATOM 118 O LEU B 15 -27.650 9.161 2.045 1.00 19.61 O ANISOU 118 O LEU B 15 2397 2420 2633 185 -614 93 O ATOM 119 CB LEU B 15 -27.657 11.230 4.498 1.00 17.58 C ANISOU 119 CB LEU B 15 2094 2140 2444 256 -494 41 C ATOM 120 CG LEU B 15 -27.540 11.197 6.022 1.00 17.63 C ANISOU 120 CG LEU B 15 2025 2214 2458 233 -402 -2 C ATOM 121 CD1 LEU B 15 -28.442 12.242 6.651 1.00 21.07 C ANISOU 121 CD1 LEU B 15 2392 2695 2920 376 -431 -100 C ATOM 122 CD2 LEU B 15 -27.862 9.796 6.535 1.00 21.83 C ANISOU 122 CD2 LEU B 15 2442 2863 2991 123 -355 19 C ATOM 123 N ALA B 16 -26.587 11.056 1.452 1.00 17.82 N ANISOU 123 N ALA B 16 2338 2102 2333 233 -616 179 N ATOM 124 CA ALA B 16 -26.921 10.874 0.040 1.00 19.22 C ANISOU 124 CA ALA B 16 2547 2308 2449 270 -705 202 C ATOM 125 C ALA B 16 -26.269 9.621 -0.527 1.00 19.58 C ANISOU 125 C ALA B 16 2595 2431 2414 237 -691 179 C ATOM 126 O ALA B 16 -26.866 8.924 -1.360 1.00 23.41 O ANISOU 126 O ALA B 16 3063 2950 2880 276 -774 136 O ATOM 127 CB ALA B 16 -26.494 12.103 -0.758 1.00 21.80 C ANISOU 127 CB ALA B 16 2989 2584 2708 279 -761 306 C ATOM 128 N LEU B 17 -25.036 9.336 -0.112 1.00 20.36 N ANISOU 128 N LEU B 17 2717 2559 2462 184 -606 192 N ATOM 129 CA LEU B 17 -24.344 8.138 -0.577 1.00 24.00 C ANISOU 129 CA LEU B 17 3180 3096 2842 197 -612 136 C ATOM 130 C LEU B 17 -24.951 6.885 0.039 1.00 23.37 C ANISOU 130 C LEU B 17 3054 2961 2865 182 -657 54 C ATOM 131 O LEU B 17 -25.078 5.851 -0.633 1.00 22.35 O ANISOU 131 O LEU B 17 2939 2839 2713 224 -754 -19 O ATOM 132 CB LEU B 17 -22.854 8.229 -0.249 1.00 23.76 C ANISOU 132 CB LEU B 17 3166 3135 2728 159 -517 166 C ATOM 133 CG LEU B 17 -21.977 7.046 -0.677 1.00 23.81 C ANISOU 133 CG LEU B 17 3165 3247 2634 218 -530 78 C ATOM 134 CD1 LEU B 17 -22.127 6.760 -2.170 1.00 25.40 C ANISOU 134 CD1 LEU B 17 3383 3567 2701 312 -610 37 C ATOM 135 CD2 LEU B 17 -20.515 7.280 -0.319 1.00 29.28 C ANISOU 135 CD2 LEU B 17 3839 4049 3236 185 -430 112 C ATOM 136 N LEU B 18 -25.327 6.957 1.319 1.00 21.10 N ANISOU 136 N LEU B 18 2712 2622 2683 117 -606 69 N ATOM 137 CA LEU B 18 -25.975 5.819 1.960 1.00 18.98 C ANISOU 137 CA LEU B 18 2390 2318 2505 55 -659 41 C ATOM 138 C LEU B 18 -27.256 5.438 1.239 1.00 19.89 C ANISOU 138 C LEU B 18 2460 2430 2667 62 -782 17 C ATOM 139 O LEU B 18 -27.597 4.253 1.155 1.00 21.91 O ANISOU 139 O LEU B 18 2714 2640 2972 12 -894 -11 O ATOM 140 CB LEU B 18 -26.261 6.140 3.424 1.00 17.40 C ANISOU 140 CB LEU B 18 2112 2129 2371 -20 -570 80 C ATOM 141 CG LEU B 18 -26.938 5.032 4.227 1.00 21.04 C ANISOU 141 CG LEU B 18 2497 2589 2906 -134 -617 102 C ATOM 142 CD1 LEU B 18 -26.002 3.836 4.351 1.00 19.27 C ANISOU 142 CD1 LEU B 18 2361 2282 2678 -171 -677 92 C ATOM 143 CD2 LEU B 18 -27.316 5.573 5.604 1.00 20.72 C ANISOU 143 CD2 LEU B 18 2352 2637 2884 -186 -510 140 C ATOM 144 N ALA B 19 -27.988 6.435 0.731 1.00 20.57 N ANISOU 144 N ALA B 19 2687 2746 2384 486 -1133 -628 N ATOM 145 CA ALA B 19 -29.151 6.220 -0.136 1.00 26.07 C ANISOU 145 CA ALA B 19 3349 3468 3089 521 -1323 -711 C ATOM 146 C ALA B 19 -30.206 5.328 0.519 1.00 28.48 C ANISOU 146 C ALA B 19 3497 3739 3583 407 -1391 -788 C ATOM 147 O ALA B 19 -30.736 4.397 -0.094 1.00 30.07 O ANISOU 147 O ALA B 19 3706 3916 3802 370 -1496 -864 O ATOM 148 CB ALA B 19 -28.723 5.656 -1.491 1.00 28.70 C ANISOU 148 CB ALA B 19 3833 3828 3244 595 -1403 -769 C ATOM 149 N GLU B 20 -30.538 5.644 1.768 1.00 26.04 N ANISOU 149 N GLU B 20 3050 3426 3416 341 -1287 -737 N ATOM 150 CA GLU B 20 -31.590 4.907 2.452 1.00 25.39 C ANISOU 150 CA GLU B 20 2789 3346 3510 219 -1330 -777 C ATOM 151 C GLU B 20 -32.945 5.175 1.808 1.00 29.87 C ANISOU 151 C GLU B 20 3239 3986 4123 247 -1471 -807 C ATOM 152 O GLU B 20 -33.235 6.280 1.347 1.00 36.73 O ANISOU 152 O GLU B 20 4112 4909 4934 374 -1503 -780 O ATOM 153 CB GLU B 20 -31.648 5.283 3.932 1.00 28.46 C ANISOU 153 CB GLU B 20 3056 3750 4006 165 -1164 -706 C ATOM 154 CG GLU B 20 -30.681 4.507 4.814 1.00 26.35 C ANISOU 154 CG GLU B 20 2855 3405 3752 71 -1029 -676 C ATOM 155 CD GLU B 20 -31.165 3.110 5.157 1.00 33.61 C ANISOU 155 CD GLU B 20 3710 4274 4787 -88 -1082 -712 C ATOM 156 OE1 GLU B 20 -30.563 2.475 6.049 1.00 31.28 O ANISOU 156 OE1 GLU B 20 3449 3914 4523 -170 -977 -675 O ATOM 157 OE2 GLU B 20 -32.135 2.638 4.532 1.00 33.38 O ANISOU 157 OE2 GLU B 20 3604 4260 4819 -139 -1241 -772 O ATOM 158 N ASP B 21 -33.782 4.146 1.801 1.00 29.98 N ANISOU 158 N ASP B 21 3163 3991 4238 118 -1532 -841 N ATOM 159 CA ASP B 21 -35.151 4.259 1.326 1.00 38.09 C ANISOU 159 CA ASP B 21 4050 5100 5320 110 -1639 -851 C ATOM 160 C ASP B 21 -36.159 4.395 2.460 1.00 41.03 C ANISOU 160 C ASP B 21 4167 5575 5850 27 -1572 -803 C ATOM 161 O ASP B 21 -37.344 4.611 2.190 1.00 49.60 O ANISOU 161 O ASP B 21 5100 6764 6983 31 -1646 -800 O ATOM 162 CB ASP B 21 -35.514 3.043 0.465 1.00 49.32 C ANISOU 162 CB ASP B 21 5533 6466 6738 15 -1770 -914 C ATOM 163 CG ASP B 21 -35.106 1.727 1.109 1.00 59.58 C ANISOU 163 CG ASP B 21 6872 7657 8109 -149 -1731 -921 C ATOM 164 OD1 ASP B 21 -34.183 1.727 1.952 1.00 62.48 O ANISOU 164 OD1 ASP B 21 7286 7975 8479 -157 -1606 -890 O ATOM 165 OD2 ASP B 21 -35.712 0.689 0.772 1.00 65.61 O ANISOU 165 OD2 ASP B 21 7628 8378 8924 -271 -1834 -956 O ATOM 166 N ILE B 22 -35.724 4.272 3.713 1.00 38.56 N ANISOU 166 N ILE B 22 3797 5251 5604 -42 -1430 -761 N ATOM 167 CA ILE B 22 -36.643 4.343 4.842 1.00 35.48 C ANISOU 167 CA ILE B 22 3162 4980 5337 -119 -1338 -705 C ATOM 168 C ILE B 22 -36.804 5.790 5.283 1.00 35.28 C ANISOU 168 C ILE B 22 3062 5050 5291 66 -1261 -686 C ATOM 169 O ILE B 22 -36.037 6.672 4.875 1.00 33.75 O ANISOU 169 O ILE B 22 3025 4800 5000 220 -1269 -702 O ATOM 170 CB ILE B 22 -36.171 3.464 6.016 1.00 35.93 C ANISOU 170 CB ILE B 22 3201 4986 5466 -285 -1212 -658 C ATOM 171 CG1 ILE B 22 -34.814 3.945 6.532 1.00 33.53 C ANISOU 171 CG1 ILE B 22 3034 4601 5103 -201 -1104 -660 C ATOM 172 CG2 ILE B 22 -36.135 1.989 5.604 1.00 36.37 C ANISOU 172 CG2 ILE B 22 3350 4926 5544 -464 -1303 -673 C ATOM 173 CD1 ILE B 22 -34.326 3.187 7.731 1.00 34.08 C ANISOU 173 CD1 ILE B 22 3105 4620 5225 -344 -964 -600 C ATOM 174 N GLU B 23 -37.815 6.035 6.113 1.00 31.80 N ANISOU 174 N GLU B 23 2394 4757 4932 55 -1186 -644 N ATOM 175 CA GLU B 23 -38.055 7.368 6.639 1.00 32.17 C ANISOU 175 CA GLU B 23 2380 4887 4955 250 -1105 -636 C ATOM 176 C GLU B 23 -36.843 7.848 7.427 1.00 28.52 C ANISOU 176 C GLU B 23 2048 4342 4448 310 -979 -634 C ATOM 177 O GLU B 23 -36.213 7.089 8.171 1.00 30.57 O ANISOU 177 O GLU B 23 2318 4559 4739 174 -884 -613 O ATOM 178 CB GLU B 23 -39.300 7.369 7.525 1.00 39.44 C ANISOU 178 CB GLU B 23 3031 5996 5960 221 -1021 -586 C ATOM 179 CG GLU B 23 -39.793 8.755 7.908 1.00 53.70 C ANISOU 179 CG GLU B 23 4781 7890 7733 456 -966 -596 C ATOM 180 CD GLU B 23 -40.886 8.710 8.960 1.00 64.19 C ANISOU 180 CD GLU B 23 5847 9412 9131 438 -846 -541 C ATOM 181 OE1 GLU B 23 -41.934 8.081 8.706 1.00 65.72 O ANISOU 181 OE1 GLU B 23 5845 9721 9406 325 -908 -498 O ATOM 182 OE2 GLU B 23 -40.689 9.297 10.047 1.00 65.86 O ANISOU 182 OE2 GLU B 23 6053 9659 9311 536 -691 -536 O ATOM 183 N ARG B 24 -36.516 9.119 7.252 1.00 30.21 N ANISOU 183 N ARG B 24 2373 4519 4585 511 -988 -649 N ATOM 184 CA ARG B 24 -35.351 9.732 7.869 1.00 31.10 C ANISOU 184 CA ARG B 24 2660 4528 4629 569 -879 -627 C ATOM 185 C ARG B 24 -35.835 10.678 8.961 1.00 30.04 C ANISOU 185 C ARG B 24 2425 4481 4509 712 -777 -636 C ATOM 186 O ARG B 24 -36.607 11.602 8.683 1.00 37.83 O ANISOU 186 O ARG B 24 3386 5509 5478 874 -833 -653 O ATOM 187 CB ARG B 24 -34.527 10.463 6.805 1.00 35.55 C ANISOU 187 CB ARG B 24 3473 4957 5077 665 -971 -615 C ATOM 188 CG ARG B 24 -33.697 11.631 7.310 1.00 38.11 C ANISOU 188 CG ARG B 24 3973 5180 5328 770 -893 -577 C ATOM 189 CD ARG B 24 -33.014 12.371 6.163 1.00 34.53 C ANISOU 189 CD ARG B 24 3743 4612 4764 842 -996 -538 C ATOM 190 NE ARG B 24 -32.328 13.576 6.636 1.00 35.22 N ANISOU 190 NE ARG B 24 3995 4587 4799 925 -951 -493 N ATOM 191 CZ ARG B 24 -31.391 14.224 5.951 1.00 37.79 C ANISOU 191 CZ ARG B 24 4538 4795 5025 930 -991 -420 C ATOM 192 NH1 ARG B 24 -30.823 15.307 6.467 1.00 35.86 N ANISOU 192 NH1 ARG B 24 4438 4434 4754 979 -966 -377 N ATOM 193 NH2 ARG B 24 -31.015 13.785 4.753 1.00 37.80 N ANISOU 193 NH2 ARG B 24 4616 4799 4948 881 -1058 -386 N ATOM 194 N ASP B 25 -35.426 10.421 10.201 1.00 28.88 N ANISOU 194 N ASP B 25 2266 4344 4363 642 -608 -608 N ATOM 195 CA ASP B 25 -35.729 11.308 11.326 1.00 30.66 C ANISOU 195 CA ASP B 25 2435 4644 4569 791 -499 -629 C ATOM 196 C ASP B 25 -34.515 12.163 11.666 1.00 27.42 C ANISOU 196 C ASP B 25 2295 4059 4064 858 -458 -618 C ATOM 197 O ASP B 25 -34.010 12.176 12.787 1.00 27.33 O ANISOU 197 O ASP B 25 2326 4039 4020 834 -326 -607 O ATOM 198 CB ASP B 25 -36.188 10.500 12.532 1.00 34.08 C ANISOU 198 CB ASP B 25 2670 5232 5047 674 -341 -599 C ATOM 199 CG ASP B 25 -37.584 9.932 12.364 1.00 41.32 C ANISOU 199 CG ASP B 25 3353 6311 6035 600 -359 -564 C ATOM 200 OD1 ASP B 25 -38.292 10.319 11.400 1.00 43.10 O ANISOU 200 OD1 ASP B 25 3547 6554 6277 682 -491 -587 O ATOM 201 OD2 ASP B 25 -37.978 9.097 13.204 1.00 43.65 O ANISOU 201 OD2 ASP B 25 3500 6716 6370 453 -243 -500 O ATOM 202 N ILE B 26 -34.026 12.870 10.653 1.00 27.19 N ANISOU 202 N ILE B 26 2454 3890 3987 930 -582 -613 N ATOM 203 CA ILE B 26 -32.804 13.665 10.734 1.00 22.31 C ANISOU 203 CA ILE B 26 2098 3093 3288 951 -575 -580 C ATOM 204 C ILE B 26 -33.082 14.975 10.009 1.00 25.56 C ANISOU 204 C ILE B 26 2626 3419 3666 1141 -716 -594 C ATOM 205 O ILE B 26 -33.200 14.974 8.779 1.00 27.61 O ANISOU 205 O ILE B 26 2925 3654 3911 1147 -840 -570 O ATOM 206 CB ILE B 26 -31.612 12.935 10.090 1.00 22.72 C ANISOU 206 CB ILE B 26 2287 3048 3299 775 -574 -514 C ATOM 207 CG1 ILE B 26 -31.422 11.527 10.663 1.00 20.11 C ANISOU 207 CG1 ILE B 26 1852 2780 3007 600 -469 -502 C ATOM 208 CG2 ILE B 26 -30.338 13.752 10.236 1.00 25.68 C ANISOU 208 CG2 ILE B 26 2892 3269 3597 771 -559 -464 C ATOM 209 CD1 ILE B 26 -30.432 10.696 9.841 1.00 21.32 C ANISOU 209 CD1 ILE B 26 2120 2860 3121 470 -494 -462 C ATOM 210 N PRO B 27 -33.219 16.096 10.706 1.00 28.38 N ANISOU 210 N PRO B 27 3056 3724 4004 1309 -716 -634 N ATOM 211 CA PRO B 27 -33.566 17.346 10.020 1.00 32.33 C ANISOU 211 CA PRO B 27 3696 4119 4467 1467 -853 -634 C ATOM 212 C PRO B 27 -32.450 17.808 9.094 1.00 28.98 C ANISOU 212 C PRO B 27 3524 3500 3988 1416 -956 -545 C ATOM 213 O PRO B 27 -31.272 17.489 9.285 1.00 29.36 O ANISOU 213 O PRO B 27 3679 3474 4004 1248 -884 -484 O ATOM 214 CB PRO B 27 -33.787 18.339 11.168 1.00 38.48 C ANISOU 214 CB PRO B 27 4541 4864 5215 1591 -798 -690 C ATOM 215 CG PRO B 27 -33.143 17.726 12.361 1.00 38.39 C ANISOU 215 CG PRO B 27 4492 4887 5208 1506 -653 -707 C ATOM 216 CD PRO B 27 -33.171 16.243 12.170 1.00 34.97 C ANISOU 216 CD PRO B 27 3859 4596 4831 1346 -583 -681 C ATOM 217 N TYR B 28 -32.844 18.572 8.077 1.00 30.00 N ANISOU 217 N TYR B 28 3753 3569 4078 1490 -1083 -513 N ATOM 218 CA TYR B 28 -31.878 19.118 7.133 1.00 28.40 C ANISOU 218 CA TYR B 28 3791 3198 3803 1431 -1175 -403 C ATOM 219 C TYR B 28 -30.899 20.043 7.840 1.00 27.85 C ANISOU 219 C TYR B 28 3935 2940 3707 1399 -1158 -363 C ATOM 220 O TYR B 28 -31.302 20.985 8.526 1.00 30.93 O ANISOU 220 O TYR B 28 4382 3269 4099 1502 -1169 -421 O ATOM 221 CB TYR B 28 -32.605 19.879 6.029 1.00 30.84 C ANISOU 221 CB TYR B 28 4166 3482 4070 1528 -1305 -380 C ATOM 222 CG TYR B 28 -31.695 20.597 5.061 1.00 28.22 C ANISOU 222 CG TYR B 28 4087 2988 3649 1462 -1388 -247 C ATOM 223 CD1 TYR B 28 -30.968 19.888 4.107 1.00 27.37 C ANISOU 223 CD1 TYR B 28 4013 2911 3474 1340 -1396 -154 C ATOM 224 CD2 TYR B 28 -31.585 21.987 5.077 1.00 26.95 C ANISOU 224 CD2 TYR B 28 4127 2653 3459 1517 -1459 -210 C ATOM 225 CE1 TYR B 28 -30.151 20.542 3.209 1.00 28.92 C ANISOU 225 CE1 TYR B 28 4421 2996 3572 1265 -1447 -13 C ATOM 226 CE2 TYR B 28 -30.772 22.648 4.184 1.00 27.50 C ANISOU 226 CE2 TYR B 28 4412 2586 3451 1427 -1525 -68 C ATOM 227 CZ TYR B 28 -30.061 21.915 3.251 1.00 26.52 C ANISOU 227 CZ TYR B 28 4299 2522 3257 1298 -1508 38 C ATOM 228 OH TYR B 28 -29.242 22.556 2.367 1.00 27.32 O ANISOU 228 OH TYR B 28 4590 2524 3266 1196 -1547 195 O ATOM 229 N ASP B 29 -29.616 19.792 7.649 1.00 26.45 N ANISOU 229 N ASP B 29 3875 2682 3493 1237 -1132 -262 N ATOM 230 CA ASP B 29 -28.567 20.620 8.242 1.00 27.91 C ANISOU 230 CA ASP B 29 4262 2684 3659 1160 -1132 -205 C ATOM 231 C ASP B 29 -27.392 20.661 7.281 1.00 27.10 C ANISOU 231 C ASP B 29 4295 2523 3481 974 -1147 -42 C ATOM 232 O ASP B 29 -26.636 19.685 7.164 1.00 30.00 O ANISOU 232 O ASP B 29 4577 3001 3820 811 -1033 -2 O ATOM 233 CB ASP B 29 -28.139 20.087 9.605 1.00 29.08 C ANISOU 233 CB ASP B 29 4326 2883 3838 1082 -988 -273 C ATOM 234 CG ASP B 29 -27.230 21.044 10.340 1.00 34.67 C ANISOU 234 CG ASP B 29 5240 3399 4535 1031 -1021 -246 C ATOM 235 OD1 ASP B 29 -26.694 21.980 9.708 1.00 32.25 O ANISOU 235 OD1 ASP B 29 5122 2938 4193 970 -1124 -142 O ATOM 236 OD2 ASP B 29 -27.060 20.857 11.559 1.00 36.34 O ANISOU 236 OD2 ASP B 29 5412 3633 4762 1024 -937 -324 O ATOM 237 N PRO B 30 -27.197 21.774 6.568 1.00 29.01 N ANISOU 237 N PRO B 30 4728 2618 3675 973 -1262 57 N ATOM 238 CA PRO B 30 -26.078 21.859 5.628 1.00 28.73 C ANISOU 238 CA PRO B 30 4810 2552 3554 795 -1267 237 C ATOM 239 C PRO B 30 -24.755 22.241 6.269 1.00 28.22 C ANISOU 239 C PRO B 30 4848 2383 3492 602 -1223 323 C ATOM 240 O PRO B 30 -23.763 22.387 5.546 1.00 27.34 O ANISOU 240 O PRO B 30 4804 2274 3308 432 -1207 483 O ATOM 241 CB PRO B 30 -26.541 22.949 4.660 1.00 26.45 C ANISOU 241 CB PRO B 30 4648 2182 3221 850 -1378 295 C ATOM 242 CG PRO B 30 -27.303 23.892 5.544 1.00 28.74 C ANISOU 242 CG PRO B 30 4982 2360 3580 990 -1438 171 C ATOM 243 CD PRO B 30 -27.968 23.028 6.618 1.00 29.84 C ANISOU 243 CD PRO B 30 4928 2619 3790 1102 -1357 7 C ATOM 244 N GLU B 31 -24.702 22.432 7.584 1.00 25.95 N ANISOU 244 N GLU B 31 4559 2028 3274 618 -1198 222 N ATOM 245 CA GLU B 31 -23.445 22.877 8.171 1.00 28.35 C ANISOU 245 CA GLU B 31 4953 2240 3580 423 -1177 296 C ATOM 246 C GLU B 31 -22.473 21.709 8.249 1.00 23.77 C ANISOU 246 C GLU B 31 4241 1814 2976 260 -1039 349 C ATOM 247 O GLU B 31 -22.852 20.631 8.717 1.00 24.23 O ANISOU 247 O GLU B 31 4119 2030 3056 313 -927 234 O ATOM 248 CB GLU B 31 -23.652 23.463 9.559 1.00 31.19 C ANISOU 248 CB GLU B 31 5351 2506 3994 490 -1195 157 C ATOM 249 CG GLU B 31 -22.330 23.658 10.298 1.00 49.08 C ANISOU 249 CG GLU B 31 7667 4717 6264 283 -1171 212 C ATOM 250 CD GLU B 31 -22.400 24.701 11.389 1.00 67.02 C ANISOU 250 CD GLU B 31 10048 6863 8554 330 -1248 111 C ATOM 251 OE1 GLU B 31 -23.383 24.691 12.159 1.00 72.25 O ANISOU 251 OE1 GLU B 31 10675 7547 9230 530 -1239 -48 O ATOM 252 OE2 GLU B 31 -21.471 25.533 11.473 1.00 73.03 O ANISOU 252 OE2 GLU B 31 10919 7520 9308 168 -1318 192 O ATOM 253 N PRO B 32 -21.229 21.878 7.803 1.00 22.54 N ANISOU 253 N PRO B 32 4134 1658 2771 53 -1022 515 N ATOM 254 CA PRO B 32 -20.250 20.795 7.932 1.00 21.77 C ANISOU 254 CA PRO B 32 3873 1755 2645 -87 -870 541 C ATOM 255 C PRO B 32 -20.047 20.422 9.392 1.00 20.04 C ANISOU 255 C PRO B 32 3585 1537 2493 -96 -812 418 C ATOM 256 O PRO B 32 -20.044 21.279 10.279 1.00 22.19 O ANISOU 256 O PRO B 32 3978 1639 2815 -91 -897 376 O ATOM 257 CB PRO B 32 -18.974 21.387 7.317 1.00 25.80 C ANISOU 257 CB PRO B 32 4460 2245 3097 -304 -888 752 C ATOM 258 CG PRO B 32 -19.442 22.512 6.457 1.00 33.94 C ANISOU 258 CG PRO B 32 5632 3159 4105 -265 -999 818 C ATOM 259 CD PRO B 32 -20.682 23.048 7.092 1.00 29.72 C ANISOU 259 CD PRO B 32 5179 2469 3645 -65 -1100 658 C ATOM 260 N ILE B 33 -19.894 19.121 9.641 1.00 18.06 N ANISOU 260 N ILE B 33 3156 1472 2235 -97 -677 357 N ATOM 261 CA ILE B 33 -19.639 18.676 11.009 1.00 17.84 C ANISOU 261 CA ILE B 33 3063 1462 2252 -111 -616 259 C ATOM 262 C ILE B 33 -18.302 19.209 11.498 1.00 19.86 C ANISOU 262 C ILE B 33 3377 1662 2507 -292 -642 351 C ATOM 263 O ILE B 33 -18.140 19.527 12.687 1.00 21.69 O ANISOU 263 O ILE B 33 3654 1810 2776 -301 -673 280 O ATOM 264 CB ILE B 33 -19.709 17.140 11.071 1.00 17.07 C ANISOU 264 CB ILE B 33 2785 1556 2145 -86 -483 198 C ATOM 265 CG1 ILE B 33 -21.145 16.702 10.776 1.00 16.36 C ANISOU 265 CG1 ILE B 33 2635 1502 2078 74 -483 97 C ATOM 266 CG2 ILE B 33 -19.199 16.621 12.424 1.00 17.52 C ANISOU 266 CG2 ILE B 33 2785 1645 2229 -127 -417 137 C ATOM 267 CD1 ILE B 33 -21.307 15.225 10.430 1.00 17.59 C ANISOU 267 CD1 ILE B 33 2644 1815 2224 83 -391 58 C ATOM 268 N GLY B 34 -17.330 19.317 10.597 1.00 18.19 N ANISOU 268 N GLY B 34 3155 1510 2245 -441 -633 511 N ATOM 269 CA GLY B 34 -16.111 20.067 10.835 1.00 20.67 C ANISOU 269 CA GLY B 34 3525 1762 2565 -642 -688 636 C ATOM 270 C GLY B 34 -15.053 19.400 11.685 1.00 19.26 C ANISOU 270 C GLY B 34 3218 1705 2395 -745 -615 627 C ATOM 271 O GLY B 34 -14.096 20.078 12.086 1.00 22.26 O ANISOU 271 O GLY B 34 3625 2036 2794 -906 -679 700 O ATOM 272 N ARG B 35 -15.174 18.105 11.973 1.00 17.30 N ANISOU 272 N ARG B 35 2821 1618 2133 -653 -494 533 N ATOM 273 CA ARG B 35 -14.225 17.416 12.841 1.00 16.07 C ANISOU 273 CA ARG B 35 2551 1572 1982 -719 -436 516 C ATOM 274 C ARG B 35 -13.187 16.683 12.009 1.00 19.10 C ANISOU 274 C ARG B 35 2782 2174 2303 -792 -340 628 C ATOM 275 O ARG B 35 -13.519 15.748 11.277 1.00 23.23 O ANISOU 275 O ARG B 35 3230 2820 2778 -686 -252 600 O ATOM 276 CB ARG B 35 -14.926 16.435 13.778 1.00 17.34 C ANISOU 276 CB ARG B 35 2660 1765 2162 -574 -371 358 C ATOM 277 CG ARG B 35 -16.050 17.047 14.586 1.00 21.25 C ANISOU 277 CG ARG B 35 3276 2101 2698 -465 -436 237 C ATOM 278 CD ARG B 35 -16.667 16.005 15.494 1.00 16.17 C ANISOU 278 CD ARG B 35 2556 1530 2058 -349 -349 114 C ATOM 279 NE ARG B 35 -15.773 15.585 16.579 1.00 14.82 N ANISOU 279 NE ARG B 35 2345 1409 1875 -412 -329 103 N ATOM 280 CZ ARG B 35 -16.110 14.672 17.486 1.00 16.94 C ANISOU 280 CZ ARG B 35 2561 1742 2135 -338 -256 24 C ATOM 281 NH1 ARG B 35 -17.295 14.070 17.414 1.00 16.28 N ANISOU 281 NH1 ARG B 35 2438 1686 2061 -222 -192 -42 N ATOM 282 NH2 ARG B 35 -15.267 14.358 18.471 1.00 15.51 N ANISOU 282 NH2 ARG B 35 2361 1601 1932 -388 -256 21 N ATOM 283 N TYR B 36 -11.936 17.108 12.122 1.00 18.31 N ANISOU 283 N TYR B 36 2631 2128 2198 -967 -363 747 N ATOM 284 CA TYR B 36 -10.846 16.470 11.405 1.00 16.99 C ANISOU 284 CA TYR B 36 2291 2204 1961 -1027 -263 856 C ATOM 285 C TYR B 36 -10.009 15.565 12.290 1.00 18.53 C ANISOU 285 C TYR B 36 2341 2536 2165 -1018 -213 806 C ATOM 286 O TYR B 36 -9.095 14.909 11.782 1.00 19.12 O ANISOU 286 O TYR B 36 2254 2834 2179 -1020 -125 869 O ATOM 287 CB TYR B 36 -9.953 17.529 10.757 1.00 18.81 C ANISOU 287 CB TYR B 36 2508 2462 2176 -1167 -308 991 C ATOM 288 CG TYR B 36 -10.647 18.221 9.617 1.00 19.58 C ANISOU 288 CG TYR B 36 2722 2481 2238 -1154 -334 1058 C ATOM 289 CD1 TYR B 36 -11.443 19.333 9.842 1.00 20.99 C ANISOU 289 CD1 TYR B 36 3094 2408 2473 -1162 -464 1036 C ATOM 290 CD2 TYR B 36 -10.527 17.738 8.331 1.00 20.74 C ANISOU 290 CD2 TYR B 36 2792 2806 2281 -1106 -234 1130 C ATOM 291 CE1 TYR B 36 -12.093 19.977 8.788 1.00 22.10 C ANISOU 291 CE1 TYR B 36 3347 2471 2578 -1134 -500 1100 C ATOM 292 CE2 TYR B 36 -11.174 18.363 7.272 1.00 23.96 C ANISOU 292 CE2 TYR B 36 3316 3147 2643 -1086 -264 1195 C ATOM 293 CZ TYR B 36 -11.953 19.474 7.512 1.00 24.86 C ANISOU 293 CZ TYR B 36 3618 3004 2824 -1104 -399 1185 C ATOM 294 OH TYR B 36 -12.588 20.084 6.453 1.00 28.89 O ANISOU 294 OH TYR B 36 4244 3449 3285 -1068 -438 1251 O ATOM 295 N ASN B 37 -10.323 15.481 13.593 1.00 15.39 N ANISOU 295 N ASN B 37 2000 2021 1828 -979 -264 685 N ATOM 296 CA ASN B 37 -9.518 14.720 14.545 1.00 15.55 C ANISOU 296 CA ASN B 37 1907 2150 1852 -974 -242 646 C ATOM 297 C ASN B 37 -10.462 14.183 15.624 1.00 14.17 C ANISOU 297 C ASN B 37 1815 1865 1704 -834 -243 486 C ATOM 298 O ASN B 37 -10.408 14.590 16.799 1.00 16.25 O ANISOU 298 O ASN B 37 2146 2031 1996 -867 -321 432 O ATOM 299 CB ASN B 37 -8.410 15.593 15.145 1.00 16.64 C ANISOU 299 CB ASN B 37 2021 2282 2022 -1162 -343 727 C ATOM 300 CG ASN B 37 -7.306 14.787 15.777 1.00 16.82 C ANISOU 300 CG ASN B 37 1875 2485 2030 -1163 -316 727 C ATOM 301 OD1 ASN B 37 -7.291 13.561 15.710 1.00 16.37 O ANISOU 301 OD1 ASN B 37 1722 2561 1937 -1027 -219 681 O ATOM 302 ND2 ASN B 37 -6.356 15.488 16.413 1.00 18.26 N ANISOU 302 ND2 ASN B 37 2042 2662 2236 -1276 -415 761 N ATOM 303 N VAL B 38 -11.308 13.229 15.228 1.00 12.96 N ANISOU 303 N VAL B 38 1651 1739 1533 -682 -159 414 N ATOM 304 CA VAL B 38 -12.312 12.634 16.111 1.00 11.55 C ANISOU 304 CA VAL B 38 1531 1482 1376 -562 -140 288 C ATOM 305 C VAL B 38 -11.632 11.630 17.021 1.00 14.19 C ANISOU 305 C VAL B 38 1791 1906 1696 -532 -110 262 C ATOM 306 O VAL B 38 -11.033 10.659 16.543 1.00 14.54 O ANISOU 306 O VAL B 38 1732 2081 1710 -487 -51 287 O ATOM 307 CB VAL B 38 -13.426 11.952 15.301 1.00 13.00 C ANISOU 307 CB VAL B 38 1718 1664 1557 -443 -79 237 C ATOM 308 CG1 VAL B 38 -14.429 11.319 16.247 1.00 14.94 C ANISOU 308 CG1 VAL B 38 1995 1853 1829 -352 -53 132 C ATOM 309 CG2 VAL B 38 -14.102 12.940 14.347 1.00 15.55 C ANISOU 309 CG2 VAL B 38 2116 1907 1885 -455 -123 267 C ATOM 310 N ALA B 39 -11.750 11.850 18.341 1.00 13.98 N ANISOU 310 N ALA B 39 1829 1805 1677 -536 -155 205 N ATOM 311 CA ALA B 39 -11.007 11.073 19.324 1.00 15.31 C ANISOU 311 CA ALA B 39 1947 2048 1821 -519 -153 195 C ATOM 312 C ALA B 39 -11.920 10.207 20.190 1.00 14.83 C ANISOU 312 C ALA B 39 1939 1949 1747 -409 -103 115 C ATOM 313 O ALA B 39 -13.083 10.552 20.440 1.00 14.35 O ANISOU 313 O ALA B 39 1959 1797 1696 -368 -90 56 O ATOM 314 CB ALA B 39 -10.192 12.000 20.235 1.00 14.94 C ANISOU 314 CB ALA B 39 1931 1973 1771 -629 -264 209 C ATOM 315 N PRO B 40 -11.405 9.076 20.669 1.00 13.86 N ANISOU 315 N PRO B 40 1767 1901 1599 -358 -75 122 N ATOM 316 CA PRO B 40 -12.147 8.266 21.633 1.00 14.84 C ANISOU 316 CA PRO B 40 1948 1988 1701 -284 -35 77 C ATOM 317 C PRO B 40 -12.557 9.105 22.832 1.00 15.93 C ANISOU 317 C PRO B 40 2184 2064 1804 -300 -75 28 C ATOM 318 O PRO B 40 -11.909 10.096 23.165 1.00 15.55 O ANISOU 318 O PRO B 40 2164 1999 1745 -367 -163 26 O ATOM 319 CB PRO B 40 -11.140 7.179 22.025 1.00 13.79 C ANISOU 319 CB PRO B 40 1763 1938 1539 -243 -42 113 C ATOM 320 CG PRO B 40 -10.247 7.075 20.791 1.00 17.95 C ANISOU 320 CG PRO B 40 2178 2560 2082 -248 -40 157 C ATOM 321 CD PRO B 40 -10.104 8.484 20.322 1.00 15.89 C ANISOU 321 CD PRO B 40 1909 2289 1841 -358 -81 180 C ATOM 322 N GLY B 41 -13.671 8.720 23.461 1.00 14.35 N ANISOU 322 N GLY B 41 2037 1834 1582 -238 -13 -12 N ATOM 323 CA GLY B 41 -14.117 9.413 24.652 1.00 16.58 C ANISOU 323 CA GLY B 41 2413 2085 1801 -216 -32 -70 C ATOM 324 C GLY B 41 -14.891 10.683 24.394 1.00 14.48 C ANISOU 324 C GLY B 41 2206 1742 1554 -204 -59 -134 C ATOM 325 O GLY B 41 -15.229 11.389 25.355 1.00 19.36 O ANISOU 325 O GLY B 41 2918 2330 2109 -161 -88 -204 O ATOM 326 N THR B 42 -15.175 11.004 23.128 1.00 14.60 N ANISOU 326 N THR B 42 2182 1723 1642 -223 -58 -118 N ATOM 327 CA THR B 42 -16.028 12.128 22.782 1.00 14.83 C ANISOU 327 CA THR B 42 2273 1667 1694 -188 -88 -174 C ATOM 328 C THR B 42 -17.341 11.570 22.262 1.00 13.29 C ANISOU 328 C THR B 42 2017 1502 1532 -115 5 -190 C ATOM 329 O THR B 42 -17.424 10.405 21.867 1.00 14.92 O ANISOU 329 O THR B 42 2140 1767 1762 -126 71 -147 O ATOM 330 CB THR B 42 -15.409 13.023 21.695 1.00 16.73 C ANISOU 330 CB THR B 42 2528 1843 1987 -272 -175 -127 C ATOM 331 OG1 THR B 42 -15.257 12.277 20.479 1.00 16.68 O ANISOU 331 OG1 THR B 42 2418 1900 2019 -296 -122 -58 O ATOM 332 CG2 THR B 42 -14.038 13.567 22.100 1.00 18.14 C ANISOU 332 CG2 THR B 42 2735 2005 2150 -385 -280 -89 C ATOM 333 N LYS B 43 -18.366 12.414 22.272 1.00 16.08 N ANISOU 333 N LYS B 43 2412 1809 1888 -35 -4 -258 N ATOM 334 CA LYS B 43 -19.597 12.102 21.553 1.00 12.67 C ANISOU 334 CA LYS B 43 1901 1408 1504 25 56 -271 C ATOM 335 C LYS B 43 -19.379 12.242 20.052 1.00 14.02 C ANISOU 335 C LYS B 43 2049 1539 1738 -20 9 -222 C ATOM 336 O LYS B 43 -18.810 13.232 19.588 1.00 16.35 O ANISOU 336 O LYS B 43 2420 1752 2039 -56 -80 -203 O ATOM 337 CB LYS B 43 -20.723 13.029 22.004 1.00 17.95 C ANISOU 337 CB LYS B 43 2611 2059 2152 154 52 -364 C ATOM 338 CG LYS B 43 -21.137 12.846 23.441 1.00 21.56 C ANISOU 338 CG LYS B 43 3075 2595 2520 226 124 -416 C ATOM 339 CD LYS B 43 -22.294 13.759 23.796 1.00 31.64 C ANISOU 339 CD LYS B 43 4375 3884 3765 390 130 -520 C ATOM 340 CE LYS B 43 -21.988 14.587 25.036 1.00 43.38 C ANISOU 340 CE LYS B 43 6006 5335 5140 474 86 -611 C ATOM 341 NZ LYS B 43 -23.119 15.480 25.413 1.00 50.41 N ANISOU 341 NZ LYS B 43 6927 6245 5982 677 92 -732 N ATOM 342 N VAL B 44 -19.830 11.242 19.296 1.00 14.13 N ANISOU 342 N VAL B 44 1968 1610 1791 -27 61 -195 N ATOM 343 CA VAL B 44 -19.697 11.214 17.842 1.00 11.64 C ANISOU 343 CA VAL B 44 1630 1283 1510 -51 25 -156 C ATOM 344 C VAL B 44 -21.077 10.978 17.247 1.00 11.22 C ANISOU 344 C VAL B 44 1511 1253 1500 14 40 -194 C ATOM 345 O VAL B 44 -21.829 10.126 17.733 1.00 15.05 O ANISOU 345 O VAL B 44 1920 1796 2004 25 103 -215 O ATOM 346 CB VAL B 44 -18.725 10.101 17.395 1.00 13.56 C ANISOU 346 CB VAL B 44 1829 1579 1744 -112 51 -100 C ATOM 347 CG1 VAL B 44 -18.528 10.130 15.874 1.00 14.23 C ANISOU 347 CG1 VAL B 44 1901 1675 1832 -120 19 -64 C ATOM 348 CG2 VAL B 44 -17.394 10.238 18.111 1.00 14.06 C ANISOU 348 CG2 VAL B 44 1922 1652 1768 -170 36 -62 C ATOM 349 N LEU B 45 -21.409 11.718 16.192 1.00 13.12 N ANISOU 349 N LEU B 45 1777 1453 1756 46 -26 -193 N ATOM 350 CA LEU B 45 -22.673 11.476 15.501 1.00 15.41 C ANISOU 350 CA LEU B 45 1991 1776 2088 108 -34 -228 C ATOM 351 C LEU B 45 -22.660 10.078 14.897 1.00 12.26 C ANISOU 351 C LEU B 45 1518 1431 1708 55 -6 -211 C ATOM 352 O LEU B 45 -21.737 9.742 14.152 1.00 14.36 O ANISOU 352 O LEU B 45 1816 1695 1944 14 -22 -170 O ATOM 353 CB LEU B 45 -22.889 12.530 14.413 1.00 16.03 C ANISOU 353 CB LEU B 45 2132 1793 2164 158 -128 -217 C ATOM 354 CG LEU B 45 -23.098 13.948 14.941 1.00 19.87 C ANISOU 354 CG LEU B 45 2719 2188 2643 233 -186 -248 C ATOM 355 CD1 LEU B 45 -23.076 14.957 13.815 1.00 18.65 C ANISOU 355 CD1 LEU B 45 2662 1945 2481 258 -294 -205 C ATOM 356 CD2 LEU B 45 -24.390 14.030 15.684 1.00 17.88 C ANISOU 356 CD2 LEU B 45 2393 1987 2415 355 -155 -337 C ATOM 357 N LEU B 46 -23.684 9.279 15.226 1.00 14.33 N ANISOU 357 N LEU B 46 1681 1746 2018 58 31 -243 N ATOM 358 CA LEU B 46 -23.758 7.852 14.919 1.00 14.13 C ANISOU 358 CA LEU B 46 1604 1741 2023 -7 44 -233 C ATOM 359 C LEU B 46 -25.115 7.538 14.301 1.00 13.83 C ANISOU 359 C LEU B 46 1465 1740 2049 4 3 -269 C ATOM 360 O LEU B 46 -26.150 7.910 14.860 1.00 14.19 O ANISOU 360 O LEU B 46 1420 1844 2128 38 29 -292 O ATOM 361 CB LEU B 46 -23.574 6.999 16.192 1.00 11.96 C ANISOU 361 CB LEU B 46 1312 1483 1749 -66 124 -207 C ATOM 362 CG LEU B 46 -23.439 5.481 15.991 1.00 13.72 C ANISOU 362 CG LEU B 46 1528 1682 2003 -139 119 -186 C ATOM 363 CD1 LEU B 46 -22.056 5.143 15.453 1.00 14.61 C ANISOU 363 CD1 LEU B 46 1730 1754 2066 -129 92 -172 C ATOM 364 CD2 LEU B 46 -23.662 4.786 17.353 1.00 14.24 C ANISOU 364 CD2 LEU B 46 1568 1768 2075 -199 197 -143 C ATOM 365 N LEU B 47 -25.109 6.820 13.177 1.00 12.34 N ANISOU 365 N LEU B 47 1283 1533 1872 -19 -64 -281 N ATOM 366 CA LEU B 47 -26.341 6.450 12.485 1.00 12.82 C ANISOU 366 CA LEU B 47 1248 1626 1996 -24 -133 -320 C ATOM 367 C LEU B 47 -26.870 5.120 13.006 1.00 14.60 C ANISOU 367 C LEU B 47 1398 1856 2294 -135 -113 -310 C ATOM 368 O LEU B 47 -26.111 4.168 13.197 1.00 16.12 O ANISOU 368 O LEU B 47 1663 1985 2475 -193 -100 -289 O ATOM 369 CB LEU B 47 -26.093 6.328 10.979 1.00 18.63 C ANISOU 369 CB LEU B 47 2050 2335 2693 9 -235 -346 C ATOM 370 CG LEU B 47 -26.098 7.579 10.115 1.00 24.44 C ANISOU 370 CG LEU B 47 2835 3078 3374 105 -293 -345 C ATOM 371 CD1 LEU B 47 -25.651 7.185 8.695 1.00 23.28 C ANISOU 371 CD1 LEU B 47 2767 2923 3154 126 -373 -358 C ATOM 372 CD2 LEU B 47 -27.494 8.181 10.079 1.00 22.26 C ANISOU 372 CD2 LEU B 47 2449 2850 3158 162 -344 -379 C ATOM 373 N SER B 48 -28.180 5.041 13.203 1.00 16.13 N ANISOU 373 N SER B 48 1443 2123 2563 -165 -121 -320 N ATOM 374 CA SER B 48 -28.793 3.771 13.558 1.00 14.70 C ANISOU 374 CA SER B 48 1180 1943 2463 -306 -122 -292 C ATOM 375 C SER B 48 -30.235 3.785 13.079 1.00 19.12 C ANISOU 375 C SER B 48 1564 2594 3108 -332 -193 -319 C ATOM 376 O SER B 48 -30.757 4.814 12.650 1.00 23.32 O ANISOU 376 O SER B 48 2035 3198 3629 -216 -224 -360 O ATOM 377 CB SER B 48 -28.683 3.505 15.075 1.00 19.94 C ANISOU 377 CB SER B 48 1815 2643 3119 -368 12 -219 C ATOM 378 OG SER B 48 -29.394 4.481 15.829 1.00 21.53 O ANISOU 378 OG SER B 48 1897 2978 3304 -296 97 -220 O ATOM 379 N GLU B 49 -30.869 2.618 13.129 1.00 19.47 N ANISOU 379 N GLU B 49 1529 2628 3241 -489 -234 -291 N ATOM 380 CA GLU B 49 -32.246 2.452 12.670 1.00 20.75 C ANISOU 380 CA GLU B 49 1497 2885 3501 -553 -319 -309 C ATOM 381 C GLU B 49 -33.068 1.899 13.822 1.00 30.60 C ANISOU 381 C GLU B 49 2563 4240 4821 -703 -220 -216 C ATOM 382 O GLU B 49 -32.746 0.834 14.362 1.00 29.09 O ANISOU 382 O GLU B 49 2435 3960 4656 -856 -196 -145 O ATOM 383 CB GLU B 49 -32.310 1.532 11.444 1.00 25.65 C ANISOU 383 CB GLU B 49 2190 3389 4167 -630 -503 -363 C ATOM 384 CG GLU B 49 -33.713 1.176 10.995 1.00 30.66 C ANISOU 384 CG GLU B 49 2620 4110 4918 -737 -619 -377 C ATOM 385 CD GLU B 49 -33.745 0.383 9.688 1.00 38.61 C ANISOU 385 CD GLU B 49 3742 4993 5935 -782 -821 -452 C ATOM 386 OE1 GLU B 49 -34.857 0.048 9.221 1.00 34.91 O ANISOU 386 OE1 GLU B 49 3166 4594 5505 -860 -912 -452 O ATOM 387 OE2 GLU B 49 -32.667 0.105 9.124 1.00 37.86 O ANISOU 387 OE2 GLU B 49 3864 4751 5769 -719 -872 -507 O ATOM 388 N ARG B 50 -34.106 2.641 14.217 1.00 32.80 N ANISOU 388 N ARG B 50 2622 4720 5122 -648 -158 -211 N ATOM 389 CA ARG B 50 -35.065 2.196 15.217 1.00 29.70 C ANISOU 389 CA ARG B 50 2004 4493 4789 -785 -53 -116 C ATOM 390 C ARG B 50 -36.466 2.539 14.735 1.00 35.74 C ANISOU 390 C ARG B 50 2555 5422 5603 -750 -122 -111 C ATOM 391 O ARG B 50 -36.674 3.547 14.052 1.00 31.25 O ANISOU 391 O ARG B 50 1962 4900 5013 -565 -182 -209 O ATOM 392 CB ARG B 50 -34.798 2.816 16.608 1.00 32.91 C ANISOU 392 CB ARG B 50 2399 5011 5094 -694 151 -69 C ATOM 393 CG ARG B 50 -34.821 4.343 16.695 1.00 34.45 C ANISOU 393 CG ARG B 50 2586 5300 5203 -430 199 -157 C ATOM 394 CD ARG B 50 -34.498 4.810 18.125 1.00 32.81 C ANISOU 394 CD ARG B 50 2402 5182 4883 -351 383 -122 C ATOM 395 NE ARG B 50 -34.248 6.249 18.252 1.00 31.82 N ANISOU 395 NE ARG B 50 2351 5073 4665 -97 404 -219 N ATOM 396 CZ ARG B 50 -33.050 6.828 18.138 1.00 29.79 C ANISOU 396 CZ ARG B 50 2341 4643 4335 -7 371 -263 C ATOM 397 NH1 ARG B 50 -31.972 6.103 17.884 1.00 25.47 N ANISOU 397 NH1 ARG B 50 1970 3922 3787 -125 330 -225 N ATOM 398 NH2 ARG B 50 -32.927 8.142 18.279 1.00 30.71 N ANISOU 398 NH2 ARG B 50 2527 4762 4380 202 371 -344 N ATOM 399 N ASP B 51 -37.423 1.672 15.075 1.00 32.09 N ANISOU 399 N ASP B 51 1952 4978 5263 -910 -115 -22 N ATOM 400 CA ASP B 51 -38.812 1.820 14.624 1.00 39.24 C ANISOU 400 CA ASP B 51 2635 6003 6270 -901 -181 -39 C ATOM 401 C ASP B 51 -38.902 2.001 13.107 1.00 38.79 C ANISOU 401 C ASP B 51 2629 5973 6138 -880 -404 -80 C ATOM 402 O ASP B 51 -39.783 2.703 12.599 1.00 38.49 O ANISOU 402 O ASP B 51 2439 6047 6140 -759 -466 -109 O ATOM 403 CB ASP B 51 -39.501 2.973 15.356 1.00 45.95 C ANISOU 403 CB ASP B 51 3315 7075 7069 -709 -38 -31 C ATOM 404 CG ASP B 51 -39.407 2.839 16.868 1.00 61.90 C ANISOU 404 CG ASP B 51 5324 9169 9026 -735 185 31 C ATOM 405 OD1 ASP B 51 -39.830 1.788 17.400 1.00 66.95 O ANISOU 405 OD1 ASP B 51 5905 9808 9724 -939 239 99 O ATOM 406 OD2 ASP B 51 -38.903 3.778 17.522 1.00 65.67 O ANISOU 406 OD2 ASP B 51 5872 9706 9373 -552 299 8 O ATOM 407 N GLU B 52 -37.992 1.348 12.376 1.00 36.33 N ANISOU 407 N GLU B 52 2541 5484 5780 -959 -505 -174 N ATOM 408 CA GLU B 52 -37.915 1.393 10.913 1.00 33.96 C ANISOU 408 CA GLU B 52 2350 5070 5482 -895 -700 -283 C ATOM 409 C GLU B 52 -37.583 2.787 10.384 1.00 28.94 C ANISOU 409 C GLU B 52 1756 4442 4797 -626 -717 -369 C ATOM 410 O GLU B 52 -37.889 3.106 9.224 1.00 29.74 O ANISOU 410 O GLU B 52 1886 4533 4882 -539 -867 -439 O ATOM 411 CB GLU B 52 -39.209 0.884 10.262 1.00 41.08 C ANISOU 411 CB GLU B 52 3095 6088 6426 -1017 -827 -284 C ATOM 412 CG GLU B 52 -39.754 -0.396 10.862 1.00 54.43 C ANISOU 412 CG GLU B 52 4708 7800 8174 -1279 -781 -262 C ATOM 413 CD GLU B 52 -38.857 -1.584 10.595 1.00 61.86 C ANISOU 413 CD GLU B 52 5918 8450 9133 -1400 -851 -278 C ATOM 414 OE1 GLU B 52 -38.703 -2.426 11.503 1.00 67.29 O ANISOU 414 OE1 GLU B 52 6638 9061 9868 -1545 -753 -215 O ATOM 415 OE2 GLU B 52 -38.303 -1.674 9.480 1.00 62.46 O ANISOU 415 OE2 GLU B 52 6186 8370 9176 -1326 -1005 -351 O ATOM 416 N HIS B 53 -36.980 3.634 11.219 1.00 28.31 N ANISOU 416 N HIS B 53 1696 4387 4675 -491 -568 -371 N ATOM 417 CA HIS B 53 -36.586 4.983 10.839 1.00 30.05 C ANISOU 417 CA HIS B 53 1986 4606 4826 -245 -578 -454 C ATOM 418 C HIS B 53 -35.093 5.183 11.068 1.00 24.04 C ANISOU 418 C HIS B 53 1481 3682 3973 -196 -506 -459 C ATOM 419 O HIS B 53 -34.509 4.637 12.010 1.00 24.07 O ANISOU 419 O HIS B 53 1540 3643 3965 -294 -384 -399 O ATOM 420 CB HIS B 53 -37.361 6.045 11.638 1.00 26.70 C ANISOU 420 CB HIS B 53 1403 4364 4378 -86 -462 -437 C ATOM 421 CG HIS B 53 -38.850 5.970 11.478 1.00 36.08 C ANISOU 421 CG HIS B 53 2365 5717 5627 -106 -505 -392 C ATOM 422 ND1 HIS B 53 -39.479 4.970 10.766 1.00 43.68 N ANISOU 422 ND1 HIS B 53 3254 6680 6661 -287 -637 -359 N ATOM 423 CD2 HIS B 53 -39.835 6.771 11.946 1.00 43.85 C ANISOU 423 CD2 HIS B 53 3180 6866 6614 36 -440 -377 C ATOM 424 CE1 HIS B 53 -40.785 5.159 10.800 1.00 42.76 C ANISOU 424 CE1 HIS B 53 2909 6731 6605 -269 -653 -312 C ATOM 425 NE2 HIS B 53 -41.029 6.247 11.508 1.00 45.30 N ANISOU 425 NE2 HIS B 53 3168 7154 6892 -65 -529 -327 N ATOM 426 N LEU B 54 -34.483 6.015 10.230 1.00 22.66 N ANISOU 426 N LEU B 54 1477 3422 3712 -41 -576 -507 N ATOM 427 CA LEU B 54 -33.067 6.334 10.356 1.00 20.62 C ANISOU 427 CA LEU B 54 1459 3027 3348 7 -509 -491 C ATOM 428 C LEU B 54 -32.874 7.475 11.352 1.00 21.55 C ANISOU 428 C LEU B 54 1587 3186 3417 135 -383 -477 C ATOM 429 O LEU B 54 -33.545 8.508 11.263 1.00 25.19 O ANISOU 429 O LEU B 54 1978 3720 3874 288 -412 -511 O ATOM 430 CB LEU B 54 -32.486 6.714 8.992 1.00 26.10 C ANISOU 430 CB LEU B 54 2326 3629 3963 94 -634 -528 C ATOM 431 CG LEU B 54 -30.965 6.854 8.892 1.00 22.75 C ANISOU 431 CG LEU B 54 2128 3083 3431 111 -581 -500 C ATOM 432 CD1 LEU B 54 -30.274 5.518 9.142 1.00 24.53 C ANISOU 432 CD1 LEU B 54 2416 3236 3668 -26 -547 -487 C ATOM 433 CD2 LEU B 54 -30.601 7.421 7.520 1.00 25.40 C ANISOU 433 CD2 LEU B 54 2598 3381 3674 211 -694 -519 C ATOM 434 N HIS B 55 -31.945 7.291 12.288 1.00 18.77 N ANISOU 434 N HIS B 55 1334 2776 3021 86 -262 -435 N ATOM 435 CA HIS B 55 -31.642 8.292 13.300 1.00 23.28 C ANISOU 435 CA HIS B 55 1947 3366 3533 195 -156 -432 C ATOM 436 C HIS B 55 -30.151 8.604 13.321 1.00 21.13 C ANISOU 436 C HIS B 55 1900 2951 3176 199 -137 -410 C ATOM 437 O HIS B 55 -29.320 7.773 12.953 1.00 19.29 O ANISOU 437 O HIS B 55 1758 2640 2931 100 -151 -383 O ATOM 438 CB HIS B 55 -32.087 7.817 14.680 1.00 24.95 C ANISOU 438 CB HIS B 55 2023 3693 3764 131 -14 -396 C ATOM 439 CG HIS B 55 -33.569 7.847 14.871 1.00 25.08 C ANISOU 439 CG HIS B 55 1782 3900 3846 159 -1 -410 C ATOM 440 ND1 HIS B 55 -34.229 8.943 15.378 1.00 27.35 N ANISOU 440 ND1 HIS B 55 1982 4309 4102 348 44 -459 N ATOM 441 CD2 HIS B 55 -34.523 6.926 14.596 1.00 26.57 C ANISOU 441 CD2 HIS B 55 1774 4188 4132 26 -36 -383 C ATOM 442 CE1 HIS B 55 -35.526 8.691 15.428 1.00 31.29 C ANISOU 442 CE1 HIS B 55 2215 5003 4670 341 53 -458 C ATOM 443 NE2 HIS B 55 -35.731 7.471 14.962 1.00 28.29 N ANISOU 443 NE2 HIS B 55 1759 4614 4376 128 3 -405 N ATOM 444 N LEU B 56 -29.829 9.827 13.736 1.00 19.25 N ANISOU 444 N LEU B 56 1749 2683 2882 322 -118 -426 N ATOM 445 CA LEU B 56 -28.453 10.284 13.910 1.00 15.29 C ANISOU 445 CA LEU B 56 1438 2064 2308 313 -103 -398 C ATOM 446 C LEU B 56 -28.346 10.841 15.322 1.00 18.10 C ANISOU 446 C LEU B 56 1810 2440 2626 365 -10 -412 C ATOM 447 O LEU B 56 -28.953 11.871 15.628 1.00 22.33 O ANISOU 447 O LEU B 56 2339 2997 3150 507 -24 -464 O ATOM 448 CB LEU B 56 -28.091 11.352 12.873 1.00 17.01 C ANISOU 448 CB LEU B 56 1785 2190 2486 395 -210 -396 C ATOM 449 CG LEU B 56 -26.624 11.800 12.807 1.00 17.27 C ANISOU 449 CG LEU B 56 1995 2115 2452 350 -211 -343 C ATOM 450 CD1 LEU B 56 -25.708 10.644 12.411 1.00 16.91 C ANISOU 450 CD1 LEU B 56 1965 2071 2388 229 -183 -301 C ATOM 451 CD2 LEU B 56 -26.453 12.976 11.842 1.00 21.25 C ANISOU 451 CD2 LEU B 56 2621 2534 2919 420 -318 -319 C ATOM 452 N ASP B 57 -27.584 10.168 16.184 1.00 16.31 N ANISOU 452 N ASP B 57 1617 2207 2371 269 74 -374 N ATOM 453 CA ASP B 57 -27.488 10.589 17.577 1.00 15.32 C ANISOU 453 CA ASP B 57 1514 2116 2190 317 159 -391 C ATOM 454 C ASP B 57 -26.033 10.786 17.958 1.00 13.76 C ANISOU 454 C ASP B 57 1481 1814 1933 267 155 -363 C ATOM 455 O ASP B 57 -25.167 10.042 17.505 1.00 14.83 O ANISOU 455 O ASP B 57 1655 1905 2075 163 142 -311 O ATOM 456 CB ASP B 57 -28.091 9.546 18.528 1.00 16.46 C ANISOU 456 CB ASP B 57 1521 2390 2343 246 276 -360 C ATOM 457 CG ASP B 57 -29.500 9.170 18.159 1.00 24.11 C ANISOU 457 CG ASP B 57 2288 3487 3386 249 281 -368 C ATOM 458 OD1 ASP B 57 -30.414 9.986 18.379 1.00 23.67 O ANISOU 458 OD1 ASP B 57 2143 3529 3322 391 294 -425 O ATOM 459 OD2 ASP B 57 -29.690 8.046 17.654 1.00 23.94 O ANISOU 459 OD2 ASP B 57 2196 3468 3432 113 263 -321 O ATOM 460 N PRO B 58 -25.743 11.745 18.838 1.00 16.34 N ANISOU 460 N PRO B 58 1901 2110 2197 345 159 -403 N ATOM 461 CA PRO B 58 -24.377 11.836 19.387 1.00 15.26 C ANISOU 461 CA PRO B 58 1895 1896 2006 277 151 -373 C ATOM 462 C PRO B 58 -24.183 10.760 20.446 1.00 15.99 C ANISOU 462 C PRO B 58 1942 2069 2063 209 253 -338 C ATOM 463 O PRO B 58 -24.901 10.735 21.449 1.00 18.33 O ANISOU 463 O PRO B 58 2186 2462 2316 268 333 -366 O ATOM 464 CB PRO B 58 -24.332 13.243 19.991 1.00 18.06 C ANISOU 464 CB PRO B 58 2372 2181 2310 391 97 -444 C ATOM 465 CG PRO B 58 -25.766 13.546 20.344 1.00 24.80 C ANISOU 465 CG PRO B 58 3129 3135 3160 543 142 -519 C ATOM 466 CD PRO B 58 -26.638 12.793 19.364 1.00 18.57 C ANISOU 466 CD PRO B 58 2178 2427 2453 513 157 -487 C ATOM 467 N VAL B 59 -23.235 9.850 20.208 1.00 14.67 N ANISOU 467 N VAL B 59 1794 1873 1906 97 251 -272 N ATOM 468 CA VAL B 59 -22.999 8.716 21.094 1.00 14.63 C ANISOU 468 CA VAL B 59 1766 1919 1873 30 327 -221 C ATOM 469 C VAL B 59 -21.537 8.705 21.519 1.00 12.46 C ANISOU 469 C VAL B 59 1595 1592 1546 -11 294 -192 C ATOM 470 O VAL B 59 -20.636 8.929 20.706 1.00 14.98 O ANISOU 470 O VAL B 59 1955 1853 1885 -41 226 -176 O ATOM 471 CB VAL B 59 -23.392 7.378 20.426 1.00 15.19 C ANISOU 471 CB VAL B 59 1753 2004 2017 -54 342 -171 C ATOM 472 CG1 VAL B 59 -23.198 6.205 21.389 1.00 15.38 C ANISOU 472 CG1 VAL B 59 1776 2053 2013 -128 408 -103 C ATOM 473 CG2 VAL B 59 -24.844 7.424 19.959 1.00 17.98 C ANISOU 473 CG2 VAL B 59 1978 2422 2432 -30 354 -198 C ATOM 474 N APHE B 60 -21.315 8.447 22.805 0.54 14.76 N ANISOU 474 N APHE B 60 1919 1926 1763 -11 344 -179 N ATOM 475 N BPHE B 60 -21.298 8.462 22.800 0.46 15.00 N ANISOU 475 N BPHE B 60 1951 1954 1793 -10 342 -179 N ATOM 476 CA APHE B 60 -19.974 8.289 23.359 0.54 16.05 C ANISOU 476 CA APHE B 60 2164 2061 1873 -47 307 -148 C ATOM 477 CA BPHE B 60 -19.918 8.436 23.251 0.46 15.06 C ANISOU 477 CA BPHE B 60 2043 1928 1753 -45 295 -154 C ATOM 478 C APHE B 60 -19.198 7.204 22.613 0.54 13.89 C ANISOU 478 C APHE B 60 1869 1762 1648 -112 285 -85 C ATOM 479 C BPHE B 60 -19.188 7.258 22.626 0.46 14.00 C ANISOU 479 C BPHE B 60 1885 1775 1660 -111 283 -87 C ATOM 480 O APHE B 60 -19.693 6.087 22.442 0.54 15.69 O ANISOU 480 O APHE B 60 2051 1997 1912 -143 325 -47 O ATOM 481 O BPHE B 60 -19.712 6.145 22.547 0.46 15.40 O ANISOU 481 O BPHE B 60 2017 1965 1869 -140 328 -48 O ATOM 482 CB APHE B 60 -20.143 7.945 24.849 0.54 17.49 C ANISOU 482 CB APHE B 60 2374 2313 1957 -28 374 -135 C ATOM 483 CB BPHE B 60 -19.850 8.374 24.774 0.46 19.26 C ANISOU 483 CB BPHE B 60 2626 2514 2177 -18 339 -156 C ATOM 484 CG APHE B 60 -18.875 7.631 25.588 0.54 16.76 C ANISOU 484 CG APHE B 60 2359 2210 1798 -56 333 -99 C ATOM 485 CG BPHE B 60 -19.844 9.725 25.421 0.46 18.83 C ANISOU 485 CG BPHE B 60 2658 2445 2053 59 296 -243 C ATOM 486 CD1APHE B 60 -18.005 8.635 25.980 0.54 18.10 C ANISOU 486 CD1APHE B 60 2612 2348 1918 -39 246 -147 C ATOM 487 CD1BPHE B 60 -18.673 10.460 25.517 0.46 18.89 C ANISOU 487 CD1BPHE B 60 2759 2378 2039 33 186 -262 C ATOM 488 CD2APHE B 60 -18.599 6.327 25.958 0.54 16.11 C ANISOU 488 CD2APHE B 60 2272 2147 1704 -99 366 -16 C ATOM 489 CD2BPHE B 60 -21.017 10.274 25.910 0.46 20.76 C ANISOU 489 CD2BPHE B 60 2887 2748 2252 162 355 -310 C ATOM 490 CE1APHE B 60 -16.853 8.335 26.686 0.54 16.69 C ANISOU 490 CE1APHE B 60 2485 2178 1679 -65 194 -115 C ATOM 491 CE1BPHE B 60 -18.665 11.717 26.099 0.46 13.60 C ANISOU 491 CE1BPHE B 60 2198 1659 1311 98 116 -353 C ATOM 492 CE2APHE B 60 -17.464 6.017 26.654 0.54 13.86 C ANISOU 492 CE2APHE B 60 2051 1860 1353 -104 318 18 C ATOM 493 CE2BPHE B 60 -21.018 11.519 26.498 0.46 20.11 C ANISOU 493 CE2BPHE B 60 2912 2632 2098 262 299 -411 C ATOM 494 CZ APHE B 60 -16.583 7.025 27.030 0.54 20.47 C ANISOU 494 CZ APHE B 60 2948 2691 2140 -86 233 -34 C ATOM 495 CZ BPHE B 60 -19.839 12.244 26.597 0.46 19.24 C ANISOU 495 CZ BPHE B 60 2926 2411 1972 224 169 -435 C ATOM 496 N TRP B 61 -17.982 7.526 22.150 1.00 13.61 N ANISOU 496 N TRP B 61 1864 1697 1612 -131 215 -74 N ATOM 497 CA TRP B 61 -17.113 6.513 21.548 1.00 11.76 C ANISOU 497 CA TRP B 61 1607 1464 1398 -154 198 -26 C ATOM 498 C TRP B 61 -16.317 5.843 22.673 1.00 12.86 C ANISOU 498 C TRP B 61 1783 1626 1478 -155 197 13 C ATOM 499 O TRP B 61 -15.360 6.412 23.219 1.00 15.03 O ANISOU 499 O TRP B 61 2085 1921 1705 -161 148 14 O ATOM 500 CB TRP B 61 -16.221 7.144 20.478 1.00 13.24 C ANISOU 500 CB TRP B 61 1777 1653 1600 -168 140 -20 C ATOM 501 CG TRP B 61 -15.351 6.158 19.733 1.00 12.53 C ANISOU 501 CG TRP B 61 1651 1596 1515 -155 133 14 C ATOM 502 CD1 TRP B 61 -15.461 4.792 19.739 1.00 14.26 C ANISOU 502 CD1 TRP B 61 1873 1800 1745 -124 152 22 C ATOM 503 CD2 TRP B 61 -14.233 6.467 18.890 1.00 10.63 C ANISOU 503 CD2 TRP B 61 1367 1412 1259 -162 101 42 C ATOM 504 NE1 TRP B 61 -14.477 4.236 18.951 1.00 13.27 N ANISOU 504 NE1 TRP B 61 1720 1714 1607 -80 129 34 N ATOM 505 CE2 TRP B 61 -13.705 5.241 18.427 1.00 11.75 C ANISOU 505 CE2 TRP B 61 1483 1590 1393 -102 110 50 C ATOM 506 CE3 TRP B 61 -13.630 7.663 18.477 1.00 14.70 C ANISOU 506 CE3 TRP B 61 1866 1955 1765 -217 64 70 C ATOM 507 CZ2 TRP B 61 -12.610 5.177 17.556 1.00 12.58 C ANISOU 507 CZ2 TRP B 61 1522 1790 1466 -72 102 76 C ATOM 508 CZ3 TRP B 61 -12.527 7.594 17.634 1.00 12.43 C ANISOU 508 CZ3 TRP B 61 1507 1764 1454 -224 58 119 C ATOM 509 CH2 TRP B 61 -12.038 6.363 17.178 1.00 15.83 C ANISOU 509 CH2 TRP B 61 1890 2263 1863 -141 86 118 C ATOM 510 N GLY B 62 -16.726 4.638 23.021 1.00 14.35 N ANISOU 510 N GLY B 62 1978 1803 1670 -157 238 51 N ATOM 511 CA GLY B 62 -16.159 3.885 24.126 1.00 13.27 C ANISOU 511 CA GLY B 62 1895 1677 1471 -150 237 102 C ATOM 512 C GLY B 62 -17.240 3.069 24.796 1.00 17.73 C ANISOU 512 C GLY B 62 2476 2232 2027 -180 308 150 C ATOM 513 O GLY B 62 -18.418 3.418 24.816 1.00 18.07 O ANISOU 513 O GLY B 62 2477 2302 2088 -202 369 132 O ATOM 514 N TYR B 63 -16.829 1.937 25.370 1.00 13.46 N ANISOU 514 N TYR B 63 1995 1661 1460 -183 297 222 N ATOM 515 CA TYR B 63 -17.765 0.989 25.954 1.00 15.50 C ANISOU 515 CA TYR B 63 2278 1897 1716 -243 356 302 C ATOM 516 C TYR B 63 -17.152 0.407 27.214 1.00 19.44 C ANISOU 516 C TYR B 63 2872 2403 2112 -228 347 384 C ATOM 517 O TYR B 63 -16.140 -0.298 27.146 1.00 21.02 O ANISOU 517 O TYR B 63 3131 2545 2312 -183 269 410 O ATOM 518 CB TYR B 63 -18.089 -0.128 24.967 1.00 16.93 C ANISOU 518 CB TYR B 63 2459 1970 2003 -283 321 324 C ATOM 519 CG TYR B 63 -19.125 -1.095 25.476 1.00 15.95 C ANISOU 519 CG TYR B 63 2353 1807 1900 -388 368 423 C ATOM 520 CD1 TYR B 63 -20.455 -0.716 25.587 1.00 15.65 C ANISOU 520 CD1 TYR B 63 2217 1847 1883 -463 455 432 C ATOM 521 CD2 TYR B 63 -18.773 -2.385 25.854 1.00 16.41 C ANISOU 521 CD2 TYR B 63 2523 1756 1957 -413 320 516 C ATOM 522 CE1 TYR B 63 -21.409 -1.598 26.060 1.00 19.01 C ANISOU 522 CE1 TYR B 63 2631 2263 2329 -587 505 544 C ATOM 523 CE2 TYR B 63 -19.719 -3.275 26.322 1.00 18.80 C ANISOU 523 CE2 TYR B 63 2848 2011 2283 -542 356 632 C ATOM 524 CZ TYR B 63 -21.042 -2.877 26.420 1.00 19.10 C ANISOU 524 CZ TYR B 63 2764 2149 2344 -643 454 652 C ATOM 525 OH TYR B 63 -21.980 -3.764 26.891 1.00 23.64 O ANISOU 525 OH TYR B 63 3336 2702 2945 -798 495 789 O ATOM 526 N ALA B 64 -17.787 0.677 28.354 1.00 16.70 N ANISOU 526 N ALA B 64 2540 2138 1666 -250 427 425 N ATOM 527 CA ALA B 64 -17.298 0.200 29.649 1.00 21.34 C ANISOU 527 CA ALA B 64 3231 2752 2126 -233 423 511 C ATOM 528 C ALA B 64 -18.485 -0.066 30.558 1.00 20.30 C ANISOU 528 C ALA B 64 3097 2699 1917 -301 547 602 C ATOM 529 O ALA B 64 -18.968 0.833 31.264 1.00 22.61 O ANISOU 529 O ALA B 64 3365 3121 2104 -266 623 561 O ATOM 530 CB ALA B 64 -16.337 1.201 30.289 1.00 23.02 C ANISOU 530 CB ALA B 64 3478 3035 2233 -150 368 439 C ATOM 531 N PRO B 65 -18.982 -1.299 30.581 1.00 24.99 N ANISOU 531 N PRO B 65 3719 3221 2554 -398 567 731 N ATOM 532 CA PRO B 65 -20.003 -1.656 31.571 1.00 23.60 C ANISOU 532 CA PRO B 65 3537 3143 2286 -484 692 859 C ATOM 533 C PRO B 65 -19.479 -1.486 32.991 1.00 27.51 C ANISOU 533 C PRO B 65 4140 3736 2577 -418 713 910 C ATOM 534 O PRO B 65 -18.274 -1.420 33.236 1.00 27.03 O ANISOU 534 O PRO B 65 4176 3630 2465 -327 605 876 O ATOM 535 CB PRO B 65 -20.304 -3.129 31.265 1.00 26.98 C ANISOU 535 CB PRO B 65 4016 3420 2814 -617 658 1002 C ATOM 536 CG PRO B 65 -19.874 -3.311 29.832 1.00 22.96 C ANISOU 536 CG PRO B 65 3492 2759 2473 -591 541 898 C ATOM 537 CD PRO B 65 -18.703 -2.395 29.637 1.00 22.60 C ANISOU 537 CD PRO B 65 3455 2744 2389 -438 475 762 C ATOM 538 N GLY B 66 -20.408 -1.437 33.947 1.00 29.48 N ANISOU 538 N GLY B 66 4347 4141 2713 -449 842 990 N ATOM 539 CA GLY B 66 -19.999 -1.246 35.328 1.00 29.34 C ANISOU 539 CA GLY B 66 4408 4246 2493 -382 840 1018 C ATOM 540 C GLY B 66 -19.038 -2.310 35.822 1.00 34.93 C ANISOU 540 C GLY B 66 5258 4839 3176 -372 733 1139 C ATOM 541 O GLY B 66 -18.183 -2.036 36.671 1.00 33.41 O ANISOU 541 O GLY B 66 5161 4693 2840 -287 666 1113 O ATOM 542 N TRP B 67 -19.154 -3.531 35.296 1.00 28.61 N ANISOU 542 N TRP B 67 4482 3870 2519 -455 699 1253 N ATOM 543 CA TRP B 67 -18.300 -4.635 35.721 1.00 32.44 C ANISOU 543 CA TRP B 67 5108 4224 2992 -437 586 1362 C ATOM 544 C TRP B 67 -16.926 -4.613 35.061 1.00 33.98 C ANISOU 544 C TRP B 67 5395 4287 3228 -342 425 1267 C ATOM 545 O TRP B 67 -16.067 -5.424 35.430 1.00 32.25 O ANISOU 545 O TRP B 67 5289 3975 2989 -285 313 1333 O ATOM 546 CB TRP B 67 -18.992 -5.975 35.445 1.00 30.72 C ANISOU 546 CB TRP B 67 4907 3853 2913 -556 599 1501 C ATOM 547 CG TRP B 67 -19.477 -6.166 34.035 1.00 30.31 C ANISOU 547 CG TRP B 67 4785 3672 3061 -644 574 1436 C ATOM 548 CD1 TRP B 67 -20.750 -5.991 33.572 1.00 32.03 C ANISOU 548 CD1 TRP B 67 4863 3938 3369 -754 682 1425 C ATOM 549 CD2 TRP B 67 -18.700 -6.596 32.912 1.00 29.00 C ANISOU 549 CD2 TRP B 67 4686 3313 3019 -615 426 1365 C ATOM 550 NE1 TRP B 67 -20.811 -6.276 32.228 1.00 35.62 N ANISOU 550 NE1 TRP B 67 5291 4246 3998 -807 596 1355 N ATOM 551 CE2 TRP B 67 -19.563 -6.646 31.799 1.00 32.13 C ANISOU 551 CE2 TRP B 67 4984 3651 3574 -717 444 1315 C ATOM 552 CE3 TRP B 67 -17.354 -6.935 32.737 1.00 30.90 C ANISOU 552 CE3 TRP B 67 5058 3436 3248 -491 278 1330 C ATOM 553 CZ2 TRP B 67 -19.126 -7.028 30.534 1.00 31.99 C ANISOU 553 CZ2 TRP B 67 5009 3456 3688 -698 321 1232 C ATOM 554 CZ3 TRP B 67 -16.924 -7.313 31.477 1.00 25.96 C ANISOU 554 CZ3 TRP B 67 4466 2642 2756 -456 168 1248 C ATOM 555 CH2 TRP B 67 -17.804 -7.349 30.393 1.00 28.71 C ANISOU 555 CH2 TRP B 67 4731 2930 3247 -559 191 1198 C ATOM 556 N TRP B 68 -16.699 -3.703 34.117 1.00 30.96 N ANISOU 556 N TRP B 68 4961 3905 2898 -308 417 1119 N ATOM 557 CA TRP B 68 -15.443 -3.603 33.385 1.00 26.74 C ANISOU 557 CA TRP B 68 4430 3290 2440 -195 275 1011 C ATOM 558 C TRP B 68 -14.510 -2.638 34.106 1.00 30.43 C ANISOU 558 C TRP B 68 4906 3881 2775 -85 222 927 C ATOM 559 O TRP B 68 -14.798 -1.439 34.189 1.00 34.85 O ANISOU 559 O TRP B 68 5390 4556 3295 -77 275 820 O ATOM 560 CB TRP B 68 -15.720 -3.121 31.961 1.00 21.68 C ANISOU 560 CB TRP B 68 3653 2614 1969 -212 281 881 C ATOM 561 CG TRP B 68 -14.522 -2.949 31.058 1.00 24.43 C ANISOU 561 CG TRP B 68 3966 2918 2397 -105 161 772 C ATOM 562 CD1 TRP B 68 -13.951 -1.776 30.662 1.00 26.32 C ANISOU 562 CD1 TRP B 68 4108 3247 2643 -52 138 643 C ATOM 563 CD2 TRP B 68 -13.784 -3.994 30.417 1.00 25.54 C ANISOU 563 CD2 TRP B 68 4163 2924 2617 -39 53 788 C ATOM 564 NE1 TRP B 68 -12.894 -2.024 29.805 1.00 22.18 N ANISOU 564 NE1 TRP B 68 3552 2682 2195 31 39 592 N ATOM 565 CE2 TRP B 68 -12.769 -3.383 29.651 1.00 23.66 C ANISOU 565 CE2 TRP B 68 3831 2738 2420 60 -12 668 C ATOM 566 CE3 TRP B 68 -13.878 -5.388 30.426 1.00 27.24 C ANISOU 566 CE3 TRP B 68 4508 2974 2869 -49 -1 893 C ATOM 567 CZ2 TRP B 68 -11.860 -4.123 28.889 1.00 25.13 C ANISOU 567 CZ2 TRP B 68 4028 2851 2668 173 -112 641 C ATOM 568 CZ3 TRP B 68 -12.972 -6.121 29.671 1.00 31.07 C ANISOU 568 CZ3 TRP B 68 5033 3349 3423 74 -121 852 C ATOM 569 CH2 TRP B 68 -11.979 -5.483 28.912 1.00 26.89 C ANISOU 569 CH2 TRP B 68 4388 2910 2920 196 -166 722 C ATOM 570 N ASP B 69 -13.378 -3.152 34.594 1.00 30.29 N ANISOU 570 N ASP B 69 4984 3832 2694 6 97 969 N ATOM 571 CA ASP B 69 -12.451 -2.377 35.413 1.00 38.58 C ANISOU 571 CA ASP B 69 6053 4998 3608 97 18 908 C ATOM 572 C ASP B 69 -11.173 -1.993 34.662 1.00 37.08 C ANISOU 572 C ASP B 69 5773 4806 3511 181 -116 795 C ATOM 573 O ASP B 69 -10.095 -1.915 35.258 1.00 40.22 O ANISOU 573 O ASP B 69 6198 5258 3826 266 -238 788 O ATOM 574 CB ASP B 69 -12.115 -3.139 36.697 1.00 50.33 C ANISOU 574 CB ASP B 69 7665 6503 4956 134 -30 1032 C ATOM 575 CG ASP B 69 -11.230 -4.351 36.454 1.00 66.00 C ANISOU 575 CG ASP B 69 9709 8355 7013 206 -160 1103 C ATOM 576 OD1 ASP B 69 -11.300 -4.938 35.351 1.00 69.13 O ANISOU 576 OD1 ASP B 69 10099 8616 7552 202 -174 1105 O ATOM 577 OD2 ASP B 69 -10.467 -4.722 37.375 1.00 72.57 O ANISOU 577 OD2 ASP B 69 10597 9220 7758 279 -255 1148 O ATOM 578 N LYS B 70 -11.278 -1.746 33.363 1.00 32.65 N ANISOU 578 N LYS B 70 5092 4202 3111 156 -96 714 N ATOM 579 CA LYS B 70 -10.185 -1.288 32.522 1.00 34.16 C ANISOU 579 CA LYS B 70 5165 4425 3388 214 -190 617 C ATOM 580 C LYS B 70 -10.652 -0.080 31.727 1.00 27.77 C ANISOU 580 C LYS B 70 4242 3655 2656 143 -127 508 C ATOM 581 O LYS B 70 -11.836 0.276 31.772 1.00 26.91 O ANISOU 581 O LYS B 70 4143 3538 2543 73 -18 500 O ATOM 582 CB LYS B 70 -9.725 -2.428 31.593 1.00 33.50 C ANISOU 582 CB LYS B 70 5074 4241 3416 286 -240 644 C ATOM 583 CG LYS B 70 -9.297 -3.681 32.345 1.00 34.15 C ANISOU 583 CG LYS B 70 5299 4247 3430 372 -321 758 C ATOM 584 CD LYS B 70 -8.979 -4.816 31.393 1.00 38.59 C ANISOU 584 CD LYS B 70 5883 4679 4102 463 -376 765 C ATOM 585 CE LYS B 70 -9.640 -6.111 31.829 1.00 43.33 C ANISOU 585 CE LYS B 70 6674 5099 4690 439 -381 898 C ATOM 586 NZ LYS B 70 -9.295 -6.450 33.238 1.00 43.95 N ANISOU 586 NZ LYS B 70 6885 5196 4618 476 -439 1014 N ATOM 587 N PRO B 71 -9.761 0.600 31.010 1.00 28.18 N ANISOU 587 N PRO B 71 4177 3758 2771 159 -195 430 N ATOM 588 CA PRO B 71 -10.204 1.713 30.176 1.00 29.84 C ANISOU 588 CA PRO B 71 4298 3982 3057 87 -147 345 C ATOM 589 C PRO B 71 -11.249 1.251 29.188 1.00 19.45 C ANISOU 589 C PRO B 71 2965 2584 1841 55 -48 350 C ATOM 590 O PRO B 71 -11.251 0.080 28.757 1.00 25.47 O ANISOU 590 O PRO B 71 3752 3275 2652 93 -49 399 O ATOM 591 CB PRO B 71 -8.920 2.166 29.470 1.00 33.07 C ANISOU 591 CB PRO B 71 4581 4461 3523 104 -240 307 C ATOM 592 CG PRO B 71 -7.836 1.802 30.455 1.00 36.21 C ANISOU 592 CG PRO B 71 5003 4923 3832 171 -354 343 C ATOM 593 CD PRO B 71 -8.284 0.497 31.033 1.00 33.34 C ANISOU 593 CD PRO B 71 4766 4483 3418 236 -325 427 C ATOM 594 N PRO B 72 -12.183 2.123 28.806 1.00 21.42 N ANISOU 594 N PRO B 72 3184 2832 2125 -7 24 295 N ATOM 595 CA PRO B 72 -13.243 1.712 27.878 1.00 21.53 C ANISOU 595 CA PRO B 72 3169 2778 2232 -42 104 297 C ATOM 596 C PRO B 72 -12.672 1.193 26.571 1.00 24.19 C ANISOU 596 C PRO B 72 3445 3080 2666 -8 65 282 C ATOM 597 O PRO B 72 -11.691 1.716 26.039 1.00 19.91 O ANISOU 597 O PRO B 72 2830 2597 2139 19 10 246 O ATOM 598 CB PRO B 72 -14.062 2.992 27.667 1.00 20.85 C ANISOU 598 CB PRO B 72 3043 2721 2158 -85 154 223 C ATOM 599 CG PRO B 72 -13.752 3.841 28.886 1.00 21.63 C ANISOU 599 CG PRO B 72 3200 2881 2138 -70 123 195 C ATOM 600 CD PRO B 72 -12.341 3.520 29.254 1.00 25.59 C ANISOU 600 CD PRO B 72 3713 3408 2602 -37 17 223 C ATOM 601 N LEU B 73 -13.290 0.136 26.065 1.00 20.34 N ANISOU 601 N LEU B 73 2988 2502 2236 -10 89 312 N ATOM 602 CA LEU B 73 -12.902 -0.397 24.776 1.00 17.31 C ANISOU 602 CA LEU B 73 2569 2080 1929 44 54 278 C ATOM 603 C LEU B 73 -13.475 0.486 23.681 1.00 15.52 C ANISOU 603 C LEU B 73 2258 1877 1760 0 93 211 C ATOM 604 O LEU B 73 -14.568 1.038 23.818 1.00 16.66 O ANISOU 604 O LEU B 73 2394 2016 1920 -72 150 201 O ATOM 605 CB LEU B 73 -13.394 -1.840 24.636 1.00 19.00 C ANISOU 605 CB LEU B 73 2877 2157 2185 53 37 322 C ATOM 606 CG LEU B 73 -12.712 -2.798 25.616 1.00 23.80 C ANISOU 606 CG LEU B 73 3591 2719 2733 116 -23 399 C ATOM 607 CD1 LEU B 73 -13.467 -4.107 25.677 1.00 26.67 C ANISOU 607 CD1 LEU B 73 4079 2914 3141 76 -40 468 C ATOM 608 CD2 LEU B 73 -11.251 -3.034 25.210 1.00 19.26 C ANISOU 608 CD2 LEU B 73 2981 2195 2142 268 -107 362 C ATOM 609 N ILE B 74 -12.719 0.652 22.600 1.00 15.27 N ANISOU 609 N ILE B 74 2160 1890 1751 55 62 169 N ATOM 610 CA ILE B 74 -13.167 1.492 21.496 1.00 15.91 C ANISOU 610 CA ILE B 74 2175 1996 1872 20 89 120 C ATOM 611 C ILE B 74 -13.288 0.736 20.187 1.00 15.80 C ANISOU 611 C ILE B 74 2160 1944 1898 78 76 83 C ATOM 612 O ILE B 74 -13.865 1.282 19.233 1.00 14.00 O ANISOU 612 O ILE B 74 1897 1725 1699 51 94 46 O ATOM 613 CB ILE B 74 -12.254 2.724 21.317 1.00 19.80 C ANISOU 613 CB ILE B 74 2588 2599 2338 3 72 115 C ATOM 614 CG1 ILE B 74 -10.818 2.298 21.031 1.00 18.78 C ANISOU 614 CG1 ILE B 74 2395 2563 2178 85 30 131 C ATOM 615 CG2 ILE B 74 -12.315 3.604 22.563 1.00 19.98 C ANISOU 615 CG2 ILE B 74 2639 2633 2321 -58 64 125 C ATOM 616 CD1 ILE B 74 -9.961 3.472 20.554 1.00 22.51 C ANISOU 616 CD1 ILE B 74 2759 3158 2638 35 17 144 C ATOM 617 N ASN B 75 -12.774 -0.493 20.111 1.00 14.72 N ANISOU 617 N ASN B 75 1830 1916 1849 114 -166 127 N ATOM 618 CA ASN B 75 -12.867 -1.341 18.931 1.00 15.73 C ANISOU 618 CA ASN B 75 1935 2006 2037 160 -165 101 C ATOM 619 C ASN B 75 -13.336 -2.718 19.364 1.00 14.94 C ANISOU 619 C ASN B 75 1984 1768 1926 207 -201 152 C ATOM 620 O ASN B 75 -13.124 -3.126 20.511 1.00 16.59 O ANISOU 620 O ASN B 75 2304 1929 2071 240 -260 199 O ATOM 621 CB ASN B 75 -11.502 -1.504 18.232 1.00 14.67 C ANISOU 621 CB ASN B 75 1679 1971 1925 253 -222 16 C ATOM 622 CG ASN B 75 -10.917 -0.174 17.766 1.00 20.17 C ANISOU 622 CG ASN B 75 2240 2806 2619 180 -179 -40 C ATOM 623 OD1 ASN B 75 -9.797 0.173 18.132 1.00 28.43 O ANISOU 623 OD1 ASN B 75 3199 3956 3645 212 -226 -92 O ATOM 624 ND2 ASN B 75 -11.659 0.562 16.953 1.00 17.38 N ANISOU 624 ND2 ASN B 75 1873 2448 2282 79 -98 -31 N ATOM 625 N ALA B 76 -13.957 -3.439 18.430 1.00 13.65 N ANISOU 625 N ALA B 76 1839 1534 1814 201 -171 145 N ATOM 626 CA ALA B 76 -14.343 -4.832 18.601 1.00 14.52 C ANISOU 626 CA ALA B 76 2098 1499 1921 237 -204 181 C ATOM 627 C ALA B 76 -13.885 -5.602 17.371 1.00 16.96 C ANISOU 627 C ALA B 76 2360 1794 2288 324 -236 112 C ATOM 628 O ALA B 76 -14.198 -5.202 16.249 1.00 15.57 O ANISOU 628 O ALA B 76 2089 1671 2155 275 -177 67 O ATOM 629 CB ALA B 76 -15.859 -4.974 18.777 1.00 15.33 C ANISOU 629 CB ALA B 76 2285 1514 2027 102 -113 232 C ATOM 630 N ARG B 77 -13.175 -6.708 17.574 1.00 17.44 N ANISOU 630 N ARG B 77 2502 1778 2347 457 -333 100 N ATOM 631 CA ARG B 77 -12.604 -7.451 16.455 1.00 18.04 C ANISOU 631 CA ARG B 77 2526 1847 2481 561 -364 10 C ATOM 632 C ARG B 77 -13.676 -8.256 15.725 1.00 20.91 C ANISOU 632 C ARG B 77 2986 2084 2874 493 -315 21 C ATOM 633 O ARG B 77 -14.418 -9.018 16.349 1.00 20.44 O ANISOU 633 O ARG B 77 3102 1874 2791 450 -324 94 O ATOM 634 CB ARG B 77 -11.485 -8.369 16.952 1.00 19.95 C ANISOU 634 CB ARG B 77 2820 2036 2724 751 -503 -21 C ATOM 635 CG ARG B 77 -10.277 -7.606 17.499 1.00 20.38 C ANISOU 635 CG ARG B 77 2736 2245 2764 830 -567 -65 C ATOM 636 CD ARG B 77 -9.264 -8.541 18.137 1.00 27.57 C ANISOU 636 CD ARG B 77 3707 3092 3678 1034 -736 -90 C ATOM 637 NE ARG B 77 -8.752 -9.537 17.203 1.00 33.91 N ANISOU 637 NE ARG B 77 4478 3848 4557 1181 -778 -198 N ATOM 638 CZ ARG B 77 -7.621 -9.410 16.516 1.00 35.59 C ANISOU 638 CZ ARG B 77 4480 4209 4833 1296 -796 -348 C ATOM 639 NH1 ARG B 77 -7.233 -10.377 15.698 1.00 38.97 N ANISOU 639 NH1 ARG B 77 4893 4584 5330 1432 -825 -456 N ATOM 640 NH2 ARG B 77 -6.872 -8.321 16.654 1.00 35.63 N ANISOU 640 NH2 ARG B 77 4287 4418 4832 1267 -777 -403 N ATOM 641 N VAL B 78 -13.770 -8.080 14.396 1.00 19.08 N ANISOU 641 N VAL B 78 2650 1916 2683 466 -260 -55 N ATOM 642 CA VAL B 78 -14.793 -8.800 13.636 1.00 19.26 C ANISOU 642 CA VAL B 78 2753 1833 2733 394 -222 -57 C ATOM 643 C VAL B 78 -14.605 -10.311 13.748 1.00 19.65 C ANISOU 643 C VAL B 78 2962 1709 2795 494 -295 -68 C ATOM 644 O VAL B 78 -15.568 -11.074 13.610 1.00 22.99 O ANISOU 644 O VAL B 78 3513 1996 3226 413 -275 -40 O ATOM 645 CB VAL B 78 -14.807 -8.357 12.157 1.00 17.42 C ANISOU 645 CB VAL B 78 2396 1700 2521 355 -169 -141 C ATOM 646 CG1 VAL B 78 -13.629 -8.931 11.420 1.00 18.87 C ANISOU 646 CG1 VAL B 78 2528 1921 2722 493 -203 -256 C ATOM 647 CG2 VAL B 78 -16.125 -8.783 11.481 1.00 20.17 C ANISOU 647 CG2 VAL B 78 2811 1963 2890 240 -131 -130 C ATOM 648 N GLU B 79 -13.376 -10.769 13.999 1.00 20.07 N ANISOU 648 N GLU B 79 3011 1759 2855 671 -388 -118 N ATOM 649 CA GLU B 79 -13.122 -12.205 14.051 1.00 23.26 C ANISOU 649 CA GLU B 79 3579 1980 3279 795 -478 -139 C ATOM 650 C GLU B 79 -13.898 -12.877 15.176 1.00 27.49 C ANISOU 650 C GLU B 79 4358 2322 3765 729 -512 -10 C ATOM 651 O GLU B 79 -14.308 -14.038 15.038 1.00 26.52 O ANISOU 651 O GLU B 79 4418 2009 3650 732 -542 -2 O ATOM 652 CB GLU B 79 -11.624 -12.464 14.205 1.00 32.30 C ANISOU 652 CB GLU B 79 4650 3171 4451 1020 -589 -226 C ATOM 653 CG GLU B 79 -10.789 -12.039 12.996 1.00 36.06 C ANISOU 653 CG GLU B 79 4898 3828 4975 1080 -540 -382 C ATOM 654 CD GLU B 79 -10.290 -10.602 13.088 1.00 37.72 C ANISOU 654 CD GLU B 79 4902 4267 5162 1019 -485 -395 C ATOM 655 OE1 GLU B 79 -10.927 -9.783 13.795 1.00 26.80 O ANISOU 655 OE1 GLU B 79 3544 2907 3733 889 -450 -283 O ATOM 656 OE2 GLU B 79 -9.257 -10.294 12.447 1.00 34.24 O ANISOU 656 OE2 GLU B 79 4276 3983 4749 1094 -469 -527 O ATOM 657 N THR B 80 -14.139 -12.156 16.277 1.00 22.42 N ANISOU 657 N THR B 80 3734 1724 3063 650 -497 86 N ATOM 658 CA THR B 80 -14.669 -12.756 17.495 1.00 25.49 C ANISOU 658 CA THR B 80 4366 1943 3376 589 -531 206 C ATOM 659 C THR B 80 -15.896 -12.061 18.089 1.00 23.31 C ANISOU 659 C THR B 80 4106 1701 3050 364 -405 288 C ATOM 660 O THR B 80 -16.514 -12.629 18.999 1.00 27.64 O ANISOU 660 O THR B 80 4869 2107 3526 267 -398 379 O ATOM 661 CB THR B 80 -13.580 -12.782 18.574 1.00 26.45 C ANISOU 661 CB THR B 80 4548 2057 3444 744 -671 240 C ATOM 662 OG1 THR B 80 -12.865 -11.539 18.551 1.00 27.33 O ANISOU 662 OG1 THR B 80 4421 2395 3569 781 -657 190 O ATOM 663 CG2 THR B 80 -12.599 -13.910 18.300 1.00 26.04 C ANISOU 663 CG2 THR B 80 4577 1883 3435 973 -824 177 C ATOM 664 N ALA B 81 -16.259 -10.857 17.633 1.00 22.27 N ANISOU 664 N ALA B 81 3765 1746 2951 279 -306 254 N ATOM 665 CA ALA B 81 -17.267 -10.064 18.339 1.00 22.86 C ANISOU 665 CA ALA B 81 3828 1869 2986 104 -200 312 C ATOM 666 C ALA B 81 -18.640 -10.735 18.361 1.00 26.04 C ANISOU 666 C ALA B 81 4351 2153 3389 -72 -113 342 C ATOM 667 O ALA B 81 -19.380 -10.587 19.341 1.00 23.66 O ANISOU 667 O ALA B 81 4134 1830 3027 -209 -41 402 O ATOM 668 CB ALA B 81 -17.375 -8.667 17.716 1.00 20.95 C ANISOU 668 CB ALA B 81 3349 1818 2793 69 -132 258 C ATOM 669 N ALA B 82 -19.006 -11.466 17.302 1.00 22.67 N ANISOU 669 N ALA B 82 3929 1660 3025 -84 -110 291 N ATOM 670 CA ALA B 82 -20.347 -12.038 17.237 1.00 25.04 C ANISOU 670 CA ALA B 82 4311 1869 3336 -271 -23 302 C ATOM 671 C ALA B 82 -20.572 -13.118 18.286 1.00 28.08 C ANISOU 671 C ALA B 82 4978 2059 3633 -345 -33 387 C ATOM 672 O ALA B 82 -21.725 -13.386 18.640 1.00 32.56 O ANISOU 672 O ALA B 82 5578 2609 4182 -534 69 400 O ATOM 673 CB ALA B 82 -20.620 -12.606 15.835 1.00 23.32 C ANISOU 673 CB ALA B 82 4045 1620 3196 -268 -33 220 C ATOM 674 N THR B 83 -19.508 -13.749 18.781 1.00 26.01 N ANISOU 674 N THR B 83 4881 1687 3316 -190 -158 430 N ATOM 675 CA THR B 83 -19.610 -14.788 19.795 1.00 33.26 C ANISOU 675 CA THR B 83 6001 2501 4138 -230 -185 495 C ATOM 676 C THR B 83 -19.003 -14.374 21.127 1.00 32.16 C ANISOU 676 C THR B 83 5943 2388 3888 -185 -234 571 C ATOM 677 O THR B 83 -18.986 -15.180 22.062 1.00 36.57 O ANISOU 677 O THR B 83 6692 2858 4347 -212 -273 628 O ATOM 678 CB THR B 83 -18.934 -16.073 19.302 1.00 34.89 C ANISOU 678 CB THR B 83 6323 2568 4364 -84 -305 468 C ATOM 679 OG1 THR B 83 -17.613 -15.765 18.836 1.00 33.70 O ANISOU 679 OG1 THR B 83 6088 2452 4264 156 -427 419 O ATOM 680 CG2 THR B 83 -19.739 -16.699 18.166 1.00 34.81 C ANISOU 680 CG2 THR B 83 6282 2512 4433 -175 -244 401 C ATOM 681 N SER B 84 -18.489 -13.154 21.231 1.00 31.33 N ANISOU 681 N SER B 84 5713 2399 3792 -121 -243 570 N ATOM 682 CA SER B 84 -17.922 -12.674 22.483 1.00 28.56 C ANISOU 682 CA SER B 84 5430 2089 3333 -86 -293 633 C ATOM 683 C SER B 84 -19.008 -12.583 23.545 1.00 26.69 C ANISOU 683 C SER B 84 5273 1872 2995 -310 -157 679 C ATOM 684 O SER B 84 -20.089 -12.055 23.284 1.00 28.13 O ANISOU 684 O SER B 84 5335 2131 3221 -473 -4 644 O ATOM 685 CB SER B 84 -17.283 -11.299 22.268 1.00 25.92 C ANISOU 685 CB SER B 84 4862 1944 3043 3 -300 588 C ATOM 686 OG SER B 84 -17.174 -10.598 23.495 1.00 24.13 O ANISOU 686 OG SER B 84 4682 1779 2707 -46 -289 643 O ATOM 687 N ARG B 85 -18.728 -13.090 24.752 1.00 27.13 N ANISOU 687 N ARG B 85 5520 1869 2919 -315 -217 741 N ATOM 688 CA ARG B 85 -19.675 -12.891 25.847 1.00 31.59 C ANISOU 688 CA ARG B 85 6156 2471 3374 -521 -85 768 C ATOM 689 C ARG B 85 -19.964 -11.408 26.057 1.00 31.09 C ANISOU 689 C ARG B 85 5918 2572 3321 -587 25 742 C ATOM 690 O ARG B 85 -21.103 -11.019 26.349 1.00 29.42 O ANISOU 690 O ARG B 85 5637 2436 3104 -768 191 706 O ATOM 691 CB ARG B 85 -19.147 -13.513 27.140 1.00 31.11 C ANISOU 691 CB ARG B 85 6339 2324 3155 -499 -187 836 C ATOM 692 CG ARG B 85 -20.131 -13.395 28.300 1.00 34.19 C ANISOU 692 CG ARG B 85 6828 2746 3418 -721 -45 852 C ATOM 693 CD ARG B 85 -19.575 -13.918 29.621 1.00 35.64 C ANISOU 693 CD ARG B 85 7271 2842 3429 -708 -153 920 C ATOM 694 NE ARG B 85 -20.482 -13.586 30.718 1.00 34.41 N ANISOU 694 NE ARG B 85 7184 2740 3149 -922 -2 918 N ATOM 695 CZ ARG B 85 -20.142 -13.572 32.001 1.00 36.75 C ANISOU 695 CZ ARG B 85 7666 3013 3284 -952 -53 963 C ATOM 696 NH1 ARG B 85 -21.040 -13.250 32.924 1.00 42.61 N ANISOU 696 NH1 ARG B 85 8457 3812 3921 -1157 104 942 N ATOM 697 NH2 ARG B 85 -18.907 -13.885 32.361 1.00 41.70 N ANISOU 697 NH2 ARG B 85 8422 3563 3859 -774 -264 1018 N ATOM 698 N MET B 86 -18.944 -10.564 25.898 1.00 24.18 N ANISOU 698 N MET B 86 4959 1760 2467 -437 -68 746 N ATOM 699 CA MET B 86 -19.113 -9.124 26.067 1.00 25.73 C ANISOU 699 CA MET B 86 5003 2104 2669 -491 26 722 C ATOM 700 C MET B 86 -19.840 -8.491 24.884 1.00 23.63 C ANISOU 700 C MET B 86 4476 1940 2562 -533 138 631 C ATOM 701 O MET B 86 -20.752 -7.675 25.066 1.00 21.81 O ANISOU 701 O MET B 86 4127 1809 2352 -666 285 586 O ATOM 702 CB MET B 86 -17.744 -8.475 26.265 1.00 22.21 C ANISOU 702 CB MET B 86 4492 1741 2207 -303 -124 721 C ATOM 703 CG MET B 86 -17.767 -7.014 26.634 1.00 28.61 C ANISOU 703 CG MET B 86 5125 2731 3014 -342 -48 671 C ATOM 704 SD MET B 86 -16.083 -6.465 27.004 1.00 27.65 S ANISOU 704 SD MET B 86 4950 2701 2857 -139 -243 664 S ATOM 705 CE MET B 86 -16.392 -4.951 27.915 1.00 27.56 C ANISOU 705 CE MET B 86 4858 2839 2776 -259 -129 633 C ATOM 706 N PHE B 87 -19.436 -8.831 23.660 1.00 23.35 N ANISOU 706 N PHE B 87 4335 1893 2642 -410 63 588 N ATOM 707 CA PHE B 87 -19.910 -8.095 22.496 1.00 21.38 C ANISOU 707 CA PHE B 87 3829 1764 2533 -417 131 498 C ATOM 708 C PHE B 87 -21.156 -8.694 21.844 1.00 22.20 C ANISOU 708 C PHE B 87 3925 1808 2703 -556 228 468 C ATOM 709 O PHE B 87 -21.832 -7.985 21.085 1.00 21.96 O ANISOU 709 O PHE B 87 3691 1880 2773 -597 296 397 O ATOM 710 CB PHE B 87 -18.790 -7.990 21.451 1.00 19.75 C ANISOU 710 CB PHE B 87 3493 1607 2403 -226 12 451 C ATOM 711 CG PHE B 87 -17.626 -7.145 21.889 1.00 18.44 C ANISOU 711 CG PHE B 87 3254 1549 2202 -108 -68 447 C ATOM 712 CD1 PHE B 87 -17.828 -5.966 22.581 1.00 21.29 C ANISOU 712 CD1 PHE B 87 3543 2019 2528 -176 -1 444 C ATOM 713 CD2 PHE B 87 -16.334 -7.515 21.561 1.00 21.99 C ANISOU 713 CD2 PHE B 87 3692 1999 2665 71 -206 427 C ATOM 714 CE1 PHE B 87 -16.748 -5.181 22.974 1.00 24.86 C ANISOU 714 CE1 PHE B 87 3929 2571 2947 -83 -76 432 C ATOM 715 CE2 PHE B 87 -15.252 -6.741 21.942 1.00 24.01 C ANISOU 715 CE2 PHE B 87 3857 2370 2896 167 -279 407 C ATOM 716 CZ PHE B 87 -15.458 -5.574 22.646 1.00 21.93 C ANISOU 716 CZ PHE B 87 3535 2208 2587 82 -215 413 C ATOM 717 N LYS B 88 -21.490 -9.955 22.126 1.00 25.19 N ANISOU 717 N LYS B 88 4524 2020 3027 -635 228 519 N ATOM 718 CA LYS B 88 -22.621 -10.603 21.454 1.00 23.85 C ANISOU 718 CA LYS B 88 4315 1818 2928 -762 306 470 C ATOM 719 C LYS B 88 -23.916 -9.801 21.520 1.00 23.84 C ANISOU 719 C LYS B 88 4121 1957 2980 -912 454 400 C ATOM 720 O LYS B 88 -24.551 -9.616 20.470 1.00 22.90 O ANISOU 720 O LYS B 88 3839 1885 2977 -940 480 328 O ATOM 721 CB LYS B 88 -22.832 -12.013 22.024 1.00 28.47 C ANISOU 721 CB LYS B 88 5111 2277 3430 -813 283 512 C ATOM 722 CG LYS B 88 -23.909 -12.811 21.315 1.00 29.40 C ANISOU 722 CG LYS B 88 5193 2363 3613 -931 344 458 C ATOM 723 CD LYS B 88 -23.853 -14.288 21.692 1.00 36.08 C ANISOU 723 CD LYS B 88 6278 3052 4380 -952 294 504 C ATOM 724 CE LYS B 88 -24.557 -15.148 20.656 1.00 48.61 C ANISOU 724 CE LYS B 88 7838 4583 6049 -1018 309 448 C ATOM 725 NZ LYS B 88 -23.880 -16.464 20.462 1.00 56.47 N ANISOU 725 NZ LYS B 88 9045 5400 7012 -926 193 482 N ATOM 726 N PRO B 89 -24.357 -9.287 22.674 1.00 23.03 N ANISOU 726 N PRO B 89 4017 1930 2802 -997 542 403 N ATOM 727 CA PRO B 89 -25.601 -8.500 22.676 1.00 25.73 C ANISOU 727 CA PRO B 89 4150 2410 3215 -1103 668 310 C ATOM 728 C PRO B 89 -25.540 -7.267 21.800 1.00 24.60 C ANISOU 728 C PRO B 89 3783 2371 3194 -1031 662 251 C ATOM 729 O PRO B 89 -26.571 -6.867 21.243 1.00 25.01 O ANISOU 729 O PRO B 89 3645 2509 3350 -1076 712 163 O ATOM 730 CB PRO B 89 -25.777 -8.115 24.150 1.00 27.70 C ANISOU 730 CB PRO B 89 4473 2709 3344 -1173 748 322 C ATOM 731 CG PRO B 89 -24.944 -9.073 24.906 1.00 35.09 C ANISOU 731 CG PRO B 89 5680 3515 4137 -1150 669 423 C ATOM 732 CD PRO B 89 -23.787 -9.396 24.031 1.00 28.84 C ANISOU 732 CD PRO B 89 4940 2632 3386 -993 522 475 C ATOM 733 N LEU B 90 -24.367 -6.637 21.689 1.00 19.57 N ANISOU 733 N LEU B 90 3154 1739 2541 -902 583 289 N ATOM 734 CA LEU B 90 -24.227 -5.447 20.856 1.00 19.11 C ANISOU 734 CA LEU B 90 2873 1801 2584 -795 544 228 C ATOM 735 C LEU B 90 -24.255 -5.820 19.388 1.00 21.78 C ANISOU 735 C LEU B 90 3130 2125 3020 -737 470 194 C ATOM 736 O LEU B 90 -24.820 -5.092 18.558 1.00 21.10 O ANISOU 736 O LEU B 90 2868 2118 3033 -727 469 128 O ATOM 737 CB LEU B 90 -22.915 -4.726 21.174 1.00 17.93 C ANISOU 737 CB LEU B 90 2735 1697 2378 -655 458 265 C ATOM 738 CG LEU B 90 -22.564 -4.483 22.642 1.00 22.40 C ANISOU 738 CG LEU B 90 3426 2266 2818 -688 492 311 C ATOM 739 CD1 LEU B 90 -21.335 -3.589 22.730 1.00 20.01 C ANISOU 739 CD1 LEU B 90 3076 2036 2490 -552 399 319 C ATOM 740 CD2 LEU B 90 -23.734 -3.859 23.380 1.00 28.71 C ANISOU 740 CD2 LEU B 90 4166 3123 3618 -830 644 257 C ATOM 741 N TRP B 91 -23.620 -6.942 19.055 1.00 19.54 N ANISOU 741 N TRP B 91 2987 1734 2703 -690 396 236 N ATOM 742 CA TRP B 91 -23.650 -7.455 17.689 1.00 19.56 C ANISOU 742 CA TRP B 91 2941 1711 2781 -649 334 197 C ATOM 743 C TRP B 91 -25.069 -7.806 17.263 1.00 22.73 C ANISOU 743 C TRP B 91 3277 2103 3255 -799 406 139 C ATOM 744 O TRP B 91 -25.429 -7.635 16.092 1.00 19.88 O ANISOU 744 O TRP B 91 2793 1785 2977 -781 366 80 O ATOM 745 CB TRP B 91 -22.742 -8.682 17.595 1.00 23.63 C ANISOU 745 CB TRP B 91 3641 2095 3245 -570 251 240 C ATOM 746 CG TRP B 91 -22.490 -9.188 16.214 1.00 19.87 C ANISOU 746 CG TRP B 91 3127 1594 2827 -500 182 190 C ATOM 747 CD1 TRP B 91 -23.227 -10.113 15.528 1.00 24.06 C ANISOU 747 CD1 TRP B 91 3703 2041 3399 -583 192 155 C ATOM 748 CD2 TRP B 91 -21.414 -8.810 15.351 1.00 17.72 C ANISOU 748 CD2 TRP B 91 2775 1389 2571 -346 102 158 C ATOM 749 NE1 TRP B 91 -22.675 -10.333 14.284 1.00 24.58 N ANISOU 749 NE1 TRP B 91 3727 2112 3499 -482 118 103 N ATOM 750 CE2 TRP B 91 -21.561 -9.544 14.153 1.00 22.04 C ANISOU 750 CE2 TRP B 91 3326 1886 3160 -339 69 103 C ATOM 751 CE3 TRP B 91 -20.336 -7.930 15.476 1.00 19.11 C ANISOU 751 CE3 TRP B 91 2874 1664 2723 -230 62 161 C ATOM 752 CZ2 TRP B 91 -20.675 -9.414 13.088 1.00 24.17 C ANISOU 752 CZ2 TRP B 91 3531 2211 3443 -221 11 49 C ATOM 753 CZ3 TRP B 91 -19.460 -7.794 14.408 1.00 19.35 C ANISOU 753 CZ3 TRP B 91 2827 1752 2772 -123 7 107 C ATOM 754 CH2 TRP B 91 -19.633 -8.540 13.233 1.00 22.29 C ANISOU 754 CH2 TRP B 91 3211 2079 3180 -119 -13 52 C ATOM 755 N GLN B 92 -25.890 -8.274 18.204 1.00 20.07 N ANISOU 755 N GLN B 92 3021 1721 2882 -959 512 148 N ATOM 756 CA GLN B 92 -27.240 -8.722 17.893 1.00 21.41 C ANISOU 756 CA GLN B 92 3102 1925 3109 -1075 558 82 C ATOM 757 C GLN B 92 -28.215 -7.559 17.787 1.00 24.15 C ANISOU 757 C GLN B 92 3209 2426 3542 -1094 604 -3 C ATOM 758 O GLN B 92 -29.029 -7.515 16.859 1.00 28.29 O ANISOU 758 O GLN B 92 3593 2999 4159 -1113 577 -76 O ATOM 759 CB GLN B 92 -27.711 -9.698 18.966 1.00 26.15 C ANISOU 759 CB GLN B 92 3855 2468 3615 -1186 624 117 C ATOM 760 CG GLN B 92 -27.250 -11.121 18.744 1.00 30.64 C ANISOU 760 CG GLN B 92 4633 2875 4134 -1184 562 169 C ATOM 761 CD GLN B 92 -27.601 -12.032 19.908 1.00 45.15 C ANISOU 761 CD GLN B 92 6652 4645 5857 -1292 621 215 C ATOM 762 OE1 GLN B 92 -28.147 -11.587 20.919 1.00 48.91 O ANISOU 762 OE1 GLN B 92 7103 5199 6280 -1374 716 205 O ATOM 763 NE2 GLN B 92 -27.295 -13.314 19.766 1.00 49.75 N ANISOU 763 NE2 GLN B 92 7427 5080 6397 -1293 565 256 N ATOM 764 N HIS B 93 -28.145 -6.608 18.723 1.00 23.15 N ANISOU 764 N HIS B 93 3041 2370 3383 -1077 661 -1 N ATOM 765 CA HIS B 93 -29.165 -5.581 18.856 1.00 25.87 C ANISOU 765 CA HIS B 93 3184 2845 3800 -1087 712 -92 C ATOM 766 C HIS B 93 -28.648 -4.155 18.758 1.00 21.68 C ANISOU 766 C HIS B 93 2548 2380 3312 -976 682 -106 C ATOM 767 O HIS B 93 -29.464 -3.230 18.691 1.00 23.74 O ANISOU 767 O HIS B 93 2639 2731 3650 -953 697 -190 O ATOM 768 CB HIS B 93 -29.901 -5.737 20.200 1.00 30.35 C ANISOU 768 CB HIS B 93 3790 3446 4294 -1193 835 -113 C ATOM 769 CG HIS B 93 -30.384 -7.128 20.468 1.00 43.66 C ANISOU 769 CG HIS B 93 5607 5060 5921 -1319 877 -95 C ATOM 770 ND1 HIS B 93 -31.295 -7.769 19.656 1.00 48.08 N ANISOU 770 ND1 HIS B 93 6088 5625 6556 -1383 867 -152 N ATOM 771 CD2 HIS B 93 -30.079 -8.004 21.456 1.00 46.72 C ANISOU 771 CD2 HIS B 93 6211 5364 6176 -1395 922 -25 C ATOM 772 CE1 HIS B 93 -31.532 -8.979 20.132 1.00 48.33 C ANISOU 772 CE1 HIS B 93 6278 5577 6508 -1500 914 -121 C ATOM 773 NE2 HIS B 93 -30.807 -9.146 21.224 1.00 47.14 N ANISOU 773 NE2 HIS B 93 6315 5368 6229 -1507 945 -41 N ATOM 774 N GLY B 94 -27.336 -3.942 18.745 1.00 17.72 N ANISOU 774 N GLY B 94 2141 1828 2765 -902 637 -33 N ATOM 775 CA GLY B 94 -26.798 -2.598 18.842 1.00 15.43 C ANISOU 775 CA GLY B 94 1775 1607 2481 -789 599 -37 C ATOM 776 C GLY B 94 -25.955 -2.204 17.646 1.00 15.27 C ANISOU 776 C GLY B 94 1726 1592 2482 -654 464 -14 C ATOM 777 O GLY B 94 -25.029 -1.397 17.769 1.00 15.80 O ANISOU 777 O GLY B 94 1807 1689 2509 -567 421 16 O ATOM 778 N ARG B 95 -26.271 -2.744 16.473 1.00 16.90 N ANISOU 778 N ARG B 95 1898 1779 2746 -653 403 -36 N ATOM 779 CA ARG B 95 -25.485 -2.387 15.298 1.00 13.74 C ANISOU 779 CA ARG B 95 1484 1389 2346 -546 290 -20 C ATOM 780 C ARG B 95 -25.821 -0.971 14.844 1.00 14.42 C ANISOU 780 C ARG B 95 1446 1540 2494 -492 245 -59 C ATOM 781 O ARG B 95 -26.952 -0.492 14.995 1.00 15.71 O ANISOU 781 O ARG B 95 1494 1733 2741 -523 272 -124 O ATOM 782 CB ARG B 95 -25.712 -3.406 14.169 1.00 17.74 C ANISOU 782 CB ARG B 95 2011 1851 2878 -566 237 -37 C ATOM 783 CG ARG B 95 -25.154 -4.796 14.516 1.00 17.80 C ANISOU 783 CG ARG B 95 2177 1766 2819 -591 256 6 C ATOM 784 CD ARG B 95 -25.293 -5.802 13.371 1.00 20.19 C ANISOU 784 CD ARG B 95 2516 2013 3144 -605 202 -21 C ATOM 785 NE ARG B 95 -26.591 -5.633 12.725 1.00 22.53 N ANISOU 785 NE ARG B 95 2686 2346 3529 -681 196 -91 N ATOM 786 CZ ARG B 95 -27.697 -6.242 13.127 1.00 23.56 C ANISOU 786 CZ ARG B 95 2795 2452 3705 -814 264 -130 C ATOM 787 NH1 ARG B 95 -27.661 -7.104 14.136 1.00 21.05 N ANISOU 787 NH1 ARG B 95 2607 2056 3335 -897 348 -93 N ATOM 788 NH2 ARG B 95 -28.844 -5.999 12.517 1.00 27.54 N ANISOU 788 NH2 ARG B 95 3151 3009 4301 -870 243 -210 N ATOM 789 N ALA B 96 -24.804 -0.299 14.316 1.00 13.81 N ANISOU 789 N ALA B 96 1396 1479 2372 -410 176 -25 N ATOM 790 CA ALA B 96 -24.879 1.109 13.959 1.00 14.13 C ANISOU 790 CA ALA B 96 1373 1554 2442 -359 125 -41 C ATOM 791 C ALA B 96 -23.834 1.378 12.882 1.00 13.07 C ANISOU 791 C ALA B 96 1293 1427 2247 -312 44 -6 C ATOM 792 O ALA B 96 -23.018 0.513 12.555 1.00 13.61 O ANISOU 792 O ALA B 96 1424 1488 2258 -308 42 16 O ATOM 793 CB ALA B 96 -24.652 2.001 15.185 1.00 13.56 C ANISOU 793 CB ALA B 96 1300 1502 2349 -350 186 -38 C ATOM 794 N ILE B 97 -23.838 2.603 12.361 1.00 13.02 N ANISOU 794 N ILE B 97 1268 1430 2248 -279 -17 -8 N ATOM 795 CA ILE B 97 -22.886 3.022 11.329 1.00 12.45 C ANISOU 795 CA ILE B 97 1259 1369 2102 -265 -79 22 C ATOM 796 C ILE B 97 -22.290 4.360 11.727 1.00 12.65 C ANISOU 796 C ILE B 97 1310 1403 2093 -253 -80 42 C ATOM 797 O ILE B 97 -23.023 5.291 12.082 1.00 15.34 O ANISOU 797 O ILE B 97 1620 1716 2493 -231 -99 23 O ATOM 798 CB ILE B 97 -23.561 3.140 9.947 1.00 11.86 C ANISOU 798 CB ILE B 97 1184 1274 2047 -264 -180 8 C ATOM 799 CG1 ILE B 97 -23.931 1.754 9.401 1.00 13.88 C ANISOU 799 CG1 ILE B 97 1434 1524 2316 -291 -182 -16 C ATOM 800 CG2 ILE B 97 -22.666 3.901 8.963 1.00 15.86 C ANISOU 800 CG2 ILE B 97 1779 1788 2458 -272 -234 42 C ATOM 801 CD1 ILE B 97 -22.714 0.853 9.036 1.00 14.60 C ANISOU 801 CD1 ILE B 97 1596 1631 2319 -298 -147 -3 C ATOM 802 N CYS B 98 -20.967 4.475 11.645 1.00 11.27 N ANISOU 802 N CYS B 98 1186 1265 1829 -267 -61 67 N ATOM 803 CA CYS B 98 -20.292 5.747 11.853 1.00 11.23 C ANISOU 803 CA CYS B 98 1219 1269 1780 -282 -65 82 C ATOM 804 C CYS B 98 -19.715 6.196 10.518 1.00 13.56 C ANISOU 804 C CYS B 98 1581 1570 1999 -322 -115 99 C ATOM 805 O CYS B 98 -18.784 5.564 10.007 1.00 14.42 O ANISOU 805 O CYS B 98 1699 1736 2043 -348 -88 93 O ATOM 806 CB CYS B 98 -19.194 5.599 12.895 1.00 13.49 C ANISOU 806 CB CYS B 98 1500 1610 2017 -290 0 84 C ATOM 807 SG CYS B 98 -18.480 7.183 13.351 1.00 17.39 S ANISOU 807 SG CYS B 98 2033 2111 2463 -328 3 89 S ATOM 808 N PHE B 99 -20.258 7.276 9.953 1.00 13.63 N ANISOU 808 N PHE B 99 1647 1517 2014 -328 -189 116 N ATOM 809 CA PHE B 99 -19.701 7.711 8.679 1.00 13.60 C ANISOU 809 CA PHE B 99 1745 1512 1911 -390 -233 142 C ATOM 810 C PHE B 99 -18.485 8.604 8.914 1.00 13.86 C ANISOU 810 C PHE B 99 1834 1576 1858 -466 -185 154 C ATOM 811 O PHE B 99 -18.276 9.158 10.003 1.00 14.83 O ANISOU 811 O PHE B 99 1932 1696 2007 -458 -149 148 O ATOM 812 CB PHE B 99 -20.746 8.410 7.786 1.00 17.96 C ANISOU 812 CB PHE B 99 2371 1971 2481 -369 -361 164 C ATOM 813 CG PHE B 99 -21.564 9.484 8.469 1.00 16.38 C ANISOU 813 CG PHE B 99 2170 1686 2369 -306 -416 160 C ATOM 814 CD1 PHE B 99 -20.967 10.634 8.974 1.00 16.64 C ANISOU 814 CD1 PHE B 99 2275 1682 2364 -338 -398 178 C ATOM 815 CD2 PHE B 99 -22.951 9.370 8.523 1.00 18.91 C ANISOU 815 CD2 PHE B 99 2413 1961 2810 -216 -492 126 C ATOM 816 CE1 PHE B 99 -21.729 11.626 9.575 1.00 19.61 C ANISOU 816 CE1 PHE B 99 2658 1968 2825 -267 -451 160 C ATOM 817 CE2 PHE B 99 -23.725 10.349 9.115 1.00 18.95 C ANISOU 817 CE2 PHE B 99 2400 1893 2908 -141 -542 99 C ATOM 818 CZ PHE B 99 -23.113 11.486 9.642 1.00 22.42 C ANISOU 818 CZ PHE B 99 2925 2283 3309 -160 -523 117 C ATOM 819 N ALA B 100 -17.643 8.705 7.888 1.00 13.51 N ANISOU 819 N ALA B 100 1863 1570 1700 -556 -173 162 N ATOM 820 CA ALA B 100 -16.379 9.411 8.030 1.00 15.94 C ANISOU 820 CA ALA B 100 2204 1933 1919 -657 -107 157 C ATOM 821 C ALA B 100 -15.805 9.713 6.650 1.00 16.53 C ANISOU 821 C ALA B 100 2396 2027 1860 -780 -104 169 C ATOM 822 O ALA B 100 -16.210 9.128 5.645 1.00 16.98 O ANISOU 822 O ALA B 100 2489 2076 1885 -776 -140 172 O ATOM 823 CB ALA B 100 -15.384 8.587 8.849 1.00 17.60 C ANISOU 823 CB ALA B 100 2282 2264 2142 -641 -15 104 C ATOM 824 N ASP B 101 -14.836 10.619 6.618 1.00 16.29 N ANISOU 824 N ASP B 101 2427 2024 1739 -907 -53 169 N ATOM 825 CA ASP B 101 -14.114 10.899 5.379 1.00 14.88 C ANISOU 825 CA ASP B 101 2362 1885 1409 -1063 -14 170 C ATOM 826 C ASP B 101 -12.964 9.938 5.140 1.00 19.86 C ANISOU 826 C ASP B 101 2861 2688 1997 -1107 107 80 C ATOM 827 O ASP B 101 -12.523 9.786 3.992 1.00 20.61 O ANISOU 827 O ASP B 101 3021 2836 1973 -1215 153 58 O ATOM 828 CB ASP B 101 -13.570 12.325 5.403 1.00 19.79 C ANISOU 828 CB ASP B 101 3121 2455 1942 -1211 -1 203 C ATOM 829 CG ASP B 101 -14.624 13.318 5.772 1.00 23.16 C ANISOU 829 CG ASP B 101 3671 2700 2427 -1144 -125 274 C ATOM 830 OD1 ASP B 101 -15.646 13.364 5.054 1.00 25.71 O ANISOU 830 OD1 ASP B 101 4100 2915 2753 -1083 -242 325 O ATOM 831 OD2 ASP B 101 -14.448 14.023 6.779 1.00 22.26 O ANISOU 831 OD2 ASP B 101 3540 2556 2360 -1142 -112 267 O ATOM 832 N GLY B 102 -12.495 9.289 6.195 1.00 18.71 N ANISOU 832 N GLY B 102 2540 2628 1943 -1019 153 24 N ATOM 833 CA GLY B 102 -11.284 8.499 6.182 1.00 15.35 C ANISOU 833 CA GLY B 102 1967 2367 1499 -1036 253 -78 C ATOM 834 C GLY B 102 -10.828 8.377 7.620 1.00 17.16 C ANISOU 834 C GLY B 102 2057 2645 1818 -954 260 -109 C ATOM 835 O GLY B 102 -11.433 8.954 8.522 1.00 17.99 O ANISOU 835 O GLY B 102 2196 2660 1978 -912 206 -52 O ATOM 836 N TRP B 103 -9.758 7.608 7.828 1.00 14.41 N ANISOU 836 N TRP B 103 1553 2441 1483 -925 320 -207 N ATOM 837 CA TRP B 103 -9.285 7.416 9.199 1.00 15.28 C ANISOU 837 CA TRP B 103 1540 2600 1668 -838 302 -236 C ATOM 838 C TRP B 103 -7.770 7.562 9.256 1.00 18.38 C ANISOU 838 C TRP B 103 1791 3169 2023 -919 375 -350 C ATOM 839 O TRP B 103 -7.088 7.615 8.228 1.00 19.32 O ANISOU 839 O TRP B 103 1899 3374 2068 -1018 450 -418 O ATOM 840 CB TRP B 103 -9.751 6.063 9.766 1.00 16.64 C ANISOU 840 CB TRP B 103 1651 2738 1933 -650 249 -236 C ATOM 841 CG TRP B 103 -9.045 4.873 9.197 1.00 18.95 C ANISOU 841 CG TRP B 103 1842 3125 2235 -583 281 -332 C ATOM 842 CD1 TRP B 103 -7.970 4.222 9.726 1.00 18.67 C ANISOU 842 CD1 TRP B 103 1655 3204 2236 -501 284 -428 C ATOM 843 CD2 TRP B 103 -9.365 4.195 7.968 1.00 15.90 C ANISOU 843 CD2 TRP B 103 1497 2722 1820 -584 305 -355 C ATOM 844 NE1 TRP B 103 -7.607 3.165 8.915 1.00 20.92 N ANISOU 844 NE1 TRP B 103 1881 3539 2528 -437 312 -516 N ATOM 845 CE2 TRP B 103 -8.450 3.130 7.829 1.00 20.15 C ANISOU 845 CE2 TRP B 103 1906 3365 2387 -495 333 -473 C ATOM 846 CE3 TRP B 103 -10.358 4.370 6.996 1.00 15.76 C ANISOU 846 CE3 TRP B 103 1617 2610 1760 -639 291 -293 C ATOM 847 CZ2 TRP B 103 -8.491 2.244 6.750 1.00 19.76 C ANISOU 847 CZ2 TRP B 103 1866 3324 2320 -470 365 -535 C ATOM 848 CZ3 TRP B 103 -10.390 3.488 5.911 1.00 18.59 C ANISOU 848 CZ3 TRP B 103 1988 2986 2090 -626 317 -348 C ATOM 849 CH2 TRP B 103 -9.458 2.450 5.800 1.00 19.03 C ANISOU 849 CH2 TRP B 103 1918 3143 2170 -547 362 -470 C ATOM 850 N PHE B 104 -7.232 7.663 10.475 1.00 15.95 N ANISOU 850 N PHE B 104 1385 2914 1762 -871 345 -377 N ATOM 851 CA PHE B 104 -5.795 7.804 10.664 1.00 18.57 C ANISOU 851 CA PHE B 104 1596 3387 2074 -897 376 -488 C ATOM 852 C PHE B 104 -5.206 6.517 11.227 1.00 17.45 C ANISOU 852 C PHE B 104 1276 3342 2013 -726 336 -573 C ATOM 853 O PHE B 104 -5.853 5.813 12.010 1.00 20.11 O ANISOU 853 O PHE B 104 1613 3613 2416 -588 260 -523 O ATOM 854 CB PHE B 104 -5.449 8.961 11.617 1.00 17.60 C ANISOU 854 CB PHE B 104 1504 3252 1931 -966 353 -470 C ATOM 855 CG PHE B 104 -5.970 10.316 11.186 1.00 18.37 C ANISOU 855 CG PHE B 104 1790 3235 1955 -1112 374 -392 C ATOM 856 CD1 PHE B 104 -5.238 11.125 10.317 1.00 20.13 C ANISOU 856 CD1 PHE B 104 2074 3494 2080 -1259 436 -434 C ATOM 857 CD2 PHE B 104 -7.159 10.804 11.697 1.00 18.36 C ANISOU 857 CD2 PHE B 104 1908 3088 1981 -1099 324 -287 C ATOM 858 CE1 PHE B 104 -5.704 12.387 9.951 1.00 18.39 C ANISOU 858 CE1 PHE B 104 2047 3154 1788 -1382 436 -360 C ATOM 859 CE2 PHE B 104 -7.634 12.055 11.334 1.00 18.34 C ANISOU 859 CE2 PHE B 104 2084 2964 1921 -1206 321 -223 C ATOM 860 CZ PHE B 104 -6.906 12.854 10.460 1.00 17.83 C ANISOU 860 CZ PHE B 104 2095 2925 1755 -1344 372 -254 C ATOM 861 N GLU B 105 -3.969 6.220 10.820 1.00 20.05 N ANISOU 861 N GLU B 105 1490 3797 2331 -720 371 -699 N ATOM 862 CA GLU B 105 -3.170 5.149 11.401 1.00 22.56 C ANISOU 862 CA GLU B 105 1643 4203 2726 -548 312 -796 C ATOM 863 C GLU B 105 -1.750 5.656 11.585 1.00 25.23 C ANISOU 863 C GLU B 105 1877 4670 3042 -603 330 -908 C ATOM 864 O GLU B 105 -1.303 6.543 10.860 1.00 23.72 O ANISOU 864 O GLU B 105 1725 4518 2770 -773 417 -940 O ATOM 865 CB GLU B 105 -3.162 3.881 10.533 1.00 26.70 C ANISOU 865 CB GLU B 105 2112 4746 3286 -437 331 -868 C ATOM 866 CG GLU B 105 -4.454 3.083 10.601 1.00 26.27 C ANISOU 866 CG GLU B 105 2122 4579 3280 -333 290 -782 C ATOM 867 CD GLU B 105 -4.508 1.955 9.581 1.00 27.88 C ANISOU 867 CD GLU B 105 2313 4776 3502 -248 322 -853 C ATOM 868 OE1 GLU B 105 -3.446 1.587 9.041 1.00 32.75 O ANISOU 868 OE1 GLU B 105 2824 5500 4120 -227 361 -988 O ATOM 869 OE2 GLU B 105 -5.615 1.429 9.317 1.00 32.95 O ANISOU 869 OE2 GLU B 105 3104 5264 4152 -198 293 -759 O ATOM 870 N TRP B 106 -1.054 5.115 12.581 1.00 24.30 N ANISOU 870 N TRP B 106 1633 4612 2988 -462 240 -967 N ATOM 871 CA TRP B 106 0.313 5.524 12.882 1.00 23.31 C ANISOU 871 CA TRP B 106 1384 4618 2854 -500 242 -1084 C ATOM 872 C TRP B 106 1.253 4.373 12.564 1.00 34.26 C ANISOU 872 C TRP B 106 2613 6100 4304 -352 218 -1229 C ATOM 873 O TRP B 106 1.113 3.276 13.116 1.00 34.56 O ANISOU 873 O TRP B 106 2614 6097 4419 -147 110 -1227 O ATOM 874 CB TRP B 106 0.459 5.964 14.340 1.00 25.66 C ANISOU 874 CB TRP B 106 1666 4915 3168 -468 143 -1045 C ATOM 875 CG TRP B 106 -0.052 7.351 14.585 1.00 23.00 C ANISOU 875 CG TRP B 106 1461 4517 2760 -649 187 -954 C ATOM 876 CD1 TRP B 106 0.684 8.501 14.675 1.00 28.17 C ANISOU 876 CD1 TRP B 106 2113 5235 3358 -807 236 -997 C ATOM 877 CD2 TRP B 106 -1.420 7.737 14.755 1.00 20.42 C ANISOU 877 CD2 TRP B 106 1296 4048 2417 -687 183 -811 C ATOM 878 NE1 TRP B 106 -0.143 9.576 14.904 1.00 24.14 N ANISOU 878 NE1 TRP B 106 1765 4613 2794 -930 256 -886 N ATOM 879 CE2 TRP B 106 -1.439 9.133 14.953 1.00 24.74 C ANISOU 879 CE2 TRP B 106 1940 4562 2897 -857 224 -774 C ATOM 880 CE3 TRP B 106 -2.632 7.035 14.763 1.00 18.88 C ANISOU 880 CE3 TRP B 106 1171 3747 2258 -595 148 -719 C ATOM 881 CZ2 TRP B 106 -2.622 9.838 15.157 1.00 21.54 C ANISOU 881 CZ2 TRP B 106 1700 4016 2468 -921 224 -652 C ATOM 882 CZ3 TRP B 106 -3.805 7.739 14.973 1.00 18.69 C ANISOU 882 CZ3 TRP B 106 1294 3597 2208 -673 157 -600 C ATOM 883 CH2 TRP B 106 -3.792 9.124 15.162 1.00 19.71 C ANISOU 883 CH2 TRP B 106 1520 3689 2279 -827 192 -570 C ATOM 884 N LYS B 107 2.197 4.627 11.667 1.00 35.68 N ANISOU 884 N LYS B 107 2714 6396 4446 -456 314 -1358 N ATOM 885 CA LYS B 107 3.145 3.626 11.203 1.00 41.83 C ANISOU 885 CA LYS B 107 3336 7275 5281 -339 310 -1521 C ATOM 886 C LYS B 107 4.423 3.789 12.010 1.00 41.87 C ANISOU 886 C LYS B 107 3177 7408 5323 -299 251 -1638 C ATOM 887 O LYS B 107 5.089 4.827 11.931 1.00 38.73 O ANISOU 887 O LYS B 107 2745 7105 4866 -475 323 -1692 O ATOM 888 CB LYS B 107 3.395 3.791 9.706 1.00 36.55 C ANISOU 888 CB LYS B 107 2674 6668 4545 -490 456 -1606 C ATOM 889 CG LYS B 107 4.529 2.957 9.128 1.00 44.20 C ANISOU 889 CG LYS B 107 3464 7768 5562 -412 478 -1807 C ATOM 890 CD LYS B 107 4.639 3.234 7.640 1.00 43.34 C ANISOU 890 CD LYS B 107 3391 7713 5365 -597 631 -1875 C ATOM 891 CE LYS B 107 5.936 2.717 7.043 1.00 50.69 C ANISOU 891 CE LYS B 107 4127 8807 6325 -580 682 -2101 C ATOM 892 NZ LYS B 107 5.667 1.913 5.818 1.00 48.87 N ANISOU 892 NZ LYS B 107 3918 8564 6086 -568 753 -2157 N ATOM 893 N LYS B 108 4.743 2.778 12.810 1.00 42.73 N ANISOU 893 N LYS B 108 3198 7510 5526 -69 111 -1675 N ATOM 894 CA LYS B 108 5.975 2.789 13.590 1.00 43.10 C ANISOU 894 CA LYS B 108 3080 7678 5620 -2 30 -1795 C ATOM 895 C LYS B 108 7.165 2.690 12.643 1.00 50.11 C ANISOU 895 C LYS B 108 3797 8729 6512 -56 124 -2002 C ATOM 896 O LYS B 108 7.336 1.680 11.952 1.00 51.82 O ANISOU 896 O LYS B 108 3959 8953 6778 60 128 -2093 O ATOM 897 CB LYS B 108 5.972 1.643 14.597 1.00 40.65 C ANISOU 897 CB LYS B 108 2749 7297 5401 270 -162 -1776 C ATOM 898 CG LYS B 108 7.169 1.649 15.530 1.00 41.54 C ANISOU 898 CG LYS B 108 2704 7519 5560 355 -277 -1883 C ATOM 899 CD LYS B 108 6.754 1.494 16.985 1.00 46.13 C ANISOU 899 CD LYS B 108 3372 8001 6156 481 -455 -1755 C ATOM 900 CE LYS B 108 7.978 1.319 17.867 1.00 48.57 C ANISOU 900 CE LYS B 108 3525 8413 6517 596 -595 -1870 C ATOM 901 NZ LYS B 108 7.758 0.408 19.022 1.00 49.62 N ANISOU 901 NZ LYS B 108 3739 8427 6688 826 -814 -1788 N ATOM 902 N GLU B 109 7.980 3.744 12.597 1.00 48.36 N ANISOU 902 N GLU B 109 3497 8639 6237 -240 204 -2085 N ATOM 903 CA GLU B 109 9.125 3.775 11.694 1.00 52.94 C ANISOU 903 CA GLU B 109 3913 9392 6811 -327 309 -2293 C ATOM 904 C GLU B 109 10.425 3.815 12.486 1.00 62.13 C ANISOU 904 C GLU B 109 4864 10706 8036 -262 231 -2446 C ATOM 905 O GLU B 109 11.328 4.604 12.184 1.00 66.77 O ANISOU 905 O GLU B 109 5344 11447 8580 -438 329 -2576 O ATOM 906 CB GLU B 109 9.024 4.967 10.738 1.00 53.04 C ANISOU 906 CB GLU B 109 4020 9439 6693 -628 491 -2283 C ATOM 907 CG GLU B 109 7.903 4.832 9.703 1.00 50.92 C ANISOU 907 CG GLU B 109 3937 9047 6365 -694 572 -2171 C ATOM 908 CD GLU B 109 7.867 5.988 8.721 1.00 51.33 C ANISOU 908 CD GLU B 109 4101 9124 6278 -988 733 -2164 C ATOM 909 OE1 GLU B 109 8.811 6.801 8.734 1.00 54.81 O ANISOU 909 OE1 GLU B 109 4459 9693 6672 -1145 797 -2271 O ATOM 910 OE2 GLU B 109 6.897 6.085 7.937 1.00 47.90 O ANISOU 910 OE2 GLU B 109 3844 8579 5779 -1066 789 -2053 O ATOM 911 N GLY B 110 10.530 2.945 13.489 1.00 58.77 N ANISOU 911 N GLY B 110 4384 10237 7709 -10 47 -2436 N ATOM 912 CA GLY B 110 11.680 2.896 14.369 1.00 62.73 C ANISOU 912 CA GLY B 110 4695 10863 8278 85 -66 -2565 C ATOM 913 C GLY B 110 11.240 3.059 15.806 1.00 63.37 C ANISOU 913 C GLY B 110 4864 10845 8370 175 -230 -2412 C ATOM 914 O GLY B 110 10.537 2.202 16.349 1.00 65.14 O ANISOU 914 O GLY B 110 5195 10921 8635 370 -365 -2297 O ATOM 915 N ASP B 111 11.661 4.153 16.436 1.00 61.26 N ANISOU 915 N ASP B 111 4560 10656 8060 27 -221 -2413 N ATOM 916 CA ASP B 111 11.050 4.642 17.664 1.00 59.74 C ANISOU 916 CA ASP B 111 4494 10363 7841 29 -332 -2246 C ATOM 917 C ASP B 111 10.199 5.873 17.390 1.00 61.66 C ANISOU 917 C ASP B 111 4912 10540 7975 -222 -191 -2111 C ATOM 918 O ASP B 111 9.855 6.617 18.314 1.00 65.67 O ANISOU 918 O ASP B 111 5507 11000 8445 -289 -243 -2006 O ATOM 919 CB ASP B 111 12.123 4.938 18.710 1.00 59.51 C ANISOU 919 CB ASP B 111 4305 10457 7847 63 -455 -2342 C ATOM 920 CG ASP B 111 12.762 3.678 19.250 1.00 61.79 C ANISOU 920 CG ASP B 111 4471 10764 8244 351 -651 -2430 C ATOM 921 OD1 ASP B 111 12.103 2.618 19.198 1.00 59.65 O ANISOU 921 OD1 ASP B 111 4304 10354 8008 537 -729 -2353 O ATOM 922 OD2 ASP B 111 13.918 3.743 19.720 1.00 63.37 O ANISOU 922 OD2 ASP B 111 4476 11109 8493 392 -731 -2580 O ATOM 923 N LYS B 112 9.854 6.084 16.121 1.00 61.12 N ANISOU 923 N LYS B 112 4907 10462 7853 -359 -21 -2117 N ATOM 924 CA LYS B 112 9.156 7.260 15.621 1.00 59.33 C ANISOU 924 CA LYS B 112 4850 10175 7517 -605 122 -2012 C ATOM 925 C LYS B 112 7.927 6.779 14.864 1.00 53.21 C ANISOU 925 C LYS B 112 4243 9250 6722 -575 167 -1887 C ATOM 926 O LYS B 112 8.034 5.886 14.019 1.00 55.18 O ANISOU 926 O LYS B 112 4440 9519 7006 -490 197 -1962 O ATOM 927 CB LYS B 112 10.083 8.082 14.710 1.00 64.14 C ANISOU 927 CB LYS B 112 5375 10934 8059 -833 284 -2160 C ATOM 928 CG LYS B 112 10.488 7.331 13.434 1.00 66.63 C ANISOU 928 CG LYS B 112 5602 11326 8389 -814 376 -2297 C ATOM 929 CD LYS B 112 11.448 8.069 12.520 1.00 71.19 C ANISOU 929 CD LYS B 112 6092 12064 8893 -1046 539 -2461 C ATOM 930 CE LYS B 112 12.880 7.591 12.708 1.00 72.57 C ANISOU 930 CE LYS B 112 5982 12441 9150 -962 504 -2696 C ATOM 931 NZ LYS B 112 13.836 8.726 12.671 1.00 74.68 N ANISOU 931 NZ LYS B 112 6162 12862 9351 -1200 605 -2816 N ATOM 932 N LYS B 113 6.760 7.338 15.176 1.00 48.33 N ANISOU 932 N LYS B 113 3821 8486 6056 -639 166 -1707 N ATOM 933 CA LYS B 113 5.524 6.942 14.516 1.00 46.55 C ANISOU 933 CA LYS B 113 3753 8119 5815 -616 202 -1585 C ATOM 934 C LYS B 113 5.072 8.032 13.557 1.00 44.72 C ANISOU 934 C LYS B 113 3671 7847 5476 -858 350 -1532 C ATOM 935 O LYS B 113 5.031 9.213 13.918 1.00 43.04 O ANISOU 935 O LYS B 113 3539 7616 5199 -1014 379 -1482 O ATOM 936 CB LYS B 113 4.422 6.630 15.525 1.00 39.02 C ANISOU 936 CB LYS B 113 2914 7020 4892 -491 81 -1426 C ATOM 937 CG LYS B 113 4.591 5.272 16.175 1.00 44.42 C ANISOU 937 CG LYS B 113 3512 7694 5671 -230 -71 -1452 C ATOM 938 CD LYS B 113 3.414 4.923 17.054 1.00 49.32 C ANISOU 938 CD LYS B 113 4271 8167 6302 -125 -179 -1293 C ATOM 939 CE LYS B 113 3.600 5.471 18.457 1.00 55.07 C ANISOU 939 CE LYS B 113 5005 8904 7016 -127 -291 -1255 C ATOM 940 NZ LYS B 113 2.810 6.718 18.690 1.00 52.46 N ANISOU 940 NZ LYS B 113 4812 8509 6610 -316 -224 -1149 N ATOM 941 N GLN B 114 4.733 7.627 12.336 1.00 37.11 N ANISOU 941 N GLN B 114 2754 6860 4487 -885 434 -1542 N ATOM 942 CA GLN B 114 4.314 8.555 11.300 1.00 35.97 C ANISOU 942 CA GLN B 114 2768 6669 4230 -1104 558 -1492 C ATOM 943 C GLN B 114 2.833 8.358 11.036 1.00 32.12 C ANISOU 943 C GLN B 114 2461 6008 3735 -1067 541 -1327 C ATOM 944 O GLN B 114 2.427 7.246 10.666 1.00 30.00 O ANISOU 944 O GLN B 114 2166 5711 3521 -928 518 -1328 O ATOM 945 CB GLN B 114 5.113 8.338 10.020 1.00 40.59 C ANISOU 945 CB GLN B 114 3277 7373 4774 -1196 671 -1643 C ATOM 946 CG GLN B 114 4.514 9.058 8.818 1.00 35.24 C ANISOU 946 CG GLN B 114 2793 6621 3974 -1399 780 -1577 C ATOM 947 CD GLN B 114 4.716 10.557 8.893 1.00 40.17 C ANISOU 947 CD GLN B 114 3534 7235 4493 -1624 834 -1544 C ATOM 948 OE1 GLN B 114 5.830 11.028 9.108 1.00 40.29 O ANISOU 948 OE1 GLN B 114 3434 7384 4490 -1715 873 -1668 O ATOM 949 NE2 GLN B 114 3.640 11.314 8.730 1.00 34.85 N ANISOU 949 NE2 GLN B 114 3089 6399 3754 -1709 832 -1383 N ATOM 950 N PRO B 115 1.999 9.385 11.217 1.00 28.35 N ANISOU 950 N PRO B 115 2165 5410 3198 -1183 549 -1191 N ATOM 951 CA PRO B 115 0.572 9.247 10.906 1.00 24.68 C ANISOU 951 CA PRO B 115 1865 4784 2728 -1156 533 -1044 C ATOM 952 C PRO B 115 0.302 9.267 9.412 1.00 24.97 C ANISOU 952 C PRO B 115 2000 4799 2688 -1265 624 -1047 C ATOM 953 O PRO B 115 0.911 10.027 8.652 1.00 26.56 O ANISOU 953 O PRO B 115 2243 5053 2795 -1443 709 -1105 O ATOM 954 CB PRO B 115 -0.056 10.477 11.575 1.00 24.97 C ANISOU 954 CB PRO B 115 2056 4709 2724 -1253 511 -925 C ATOM 955 CG PRO B 115 1.060 11.492 11.553 1.00 26.05 C ANISOU 955 CG PRO B 115 2166 4942 2791 -1417 569 -1014 C ATOM 956 CD PRO B 115 2.310 10.696 11.815 1.00 28.54 C ANISOU 956 CD PRO B 115 2246 5433 3165 -1328 559 -1171 C ATOM 957 N PHE B 116 -0.650 8.433 9.012 1.00 25.88 N ANISOU 957 N PHE B 116 2161 4834 2838 -1165 603 -984 N ATOM 958 CA PHE B 116 -1.184 8.397 7.663 1.00 23.48 C ANISOU 958 CA PHE B 116 1977 4483 2461 -1256 669 -959 C ATOM 959 C PHE B 116 -2.684 8.655 7.713 1.00 26.76 C ANISOU 959 C PHE B 116 2570 4725 2872 -1247 622 -791 C ATOM 960 O PHE B 116 -3.365 8.276 8.671 1.00 23.05 O ANISOU 960 O PHE B 116 2080 4192 2487 -1116 546 -720 O ATOM 961 CB PHE B 116 -0.919 7.039 7.001 1.00 24.03 C ANISOU 961 CB PHE B 116 1925 4627 2577 -1143 692 -1062 C ATOM 962 CG PHE B 116 0.528 6.808 6.631 1.00 27.46 C ANISOU 962 CG PHE B 116 2196 5230 3006 -1174 752 -1246 C ATOM 963 CD1 PHE B 116 1.474 6.533 7.602 1.00 31.93 C ANISOU 963 CD1 PHE B 116 2584 5896 3652 -1067 702 -1339 C ATOM 964 CD2 PHE B 116 0.932 6.843 5.307 1.00 36.81 C ANISOU 964 CD2 PHE B 116 3405 6476 4106 -1312 855 -1332 C ATOM 965 CE1 PHE B 116 2.800 6.316 7.262 1.00 32.75 C ANISOU 965 CE1 PHE B 116 2522 6161 3759 -1091 754 -1521 C ATOM 966 CE2 PHE B 116 2.259 6.631 4.964 1.00 37.68 C ANISOU 966 CE2 PHE B 116 3351 6750 4217 -1348 918 -1516 C ATOM 967 CZ PHE B 116 3.190 6.366 5.940 1.00 35.21 C ANISOU 967 CZ PHE B 116 2847 6539 3992 -1234 867 -1614 C ATOM 968 N PHE B 117 -3.200 9.304 6.677 1.00 23.31 N ANISOU 968 N PHE B 117 2310 4212 2334 -1390 662 -732 N ATOM 969 CA PHE B 117 -4.636 9.433 6.489 1.00 25.71 C ANISOU 969 CA PHE B 117 2779 4356 2632 -1376 613 -588 C ATOM 970 C PHE B 117 -5.041 8.480 5.377 1.00 25.24 C ANISOU 970 C PHE B 117 2733 4305 2550 -1356 647 -607 C ATOM 971 O PHE B 117 -4.382 8.425 4.337 1.00 25.61 O ANISOU 971 O PHE B 117 2785 4429 2518 -1456 721 -693 O ATOM 972 CB PHE B 117 -5.035 10.866 6.153 1.00 22.17 C ANISOU 972 CB PHE B 117 2548 3791 2084 -1531 603 -496 C ATOM 973 CG PHE B 117 -6.515 11.051 5.983 1.00 21.00 C ANISOU 973 CG PHE B 117 2568 3471 1940 -1503 533 -354 C ATOM 974 CD1 PHE B 117 -7.394 10.843 7.049 1.00 21.98 C ANISOU 974 CD1 PHE B 117 2666 3513 2173 -1375 459 -279 C ATOM 975 CD2 PHE B 117 -7.041 11.409 4.754 1.00 23.37 C ANISOU 975 CD2 PHE B 117 3055 3690 2134 -1606 531 -300 C ATOM 976 CE1 PHE B 117 -8.761 11.018 6.874 1.00 24.96 C ANISOU 976 CE1 PHE B 117 3187 3732 2565 -1350 388 -161 C ATOM 977 CE2 PHE B 117 -8.398 11.582 4.590 1.00 23.67 C ANISOU 977 CE2 PHE B 117 3247 3567 2180 -1569 445 -173 C ATOM 978 CZ PHE B 117 -9.255 11.380 5.627 1.00 23.88 C ANISOU 978 CZ PHE B 117 3230 3515 2327 -1441 375 -108 C ATOM 979 N ILE B 118 -6.085 7.700 5.619 1.00 19.62 N ANISOU 979 N ILE B 118 2022 3524 1910 -1234 598 -540 N ATOM 980 CA ILE B 118 -6.513 6.656 4.693 1.00 19.31 C ANISOU 980 CA ILE B 118 1983 3497 1858 -1196 628 -567 C ATOM 981 C ILE B 118 -7.938 6.945 4.255 1.00 20.25 C ANISOU 981 C ILE B 118 2295 3460 1938 -1233 574 -425 C ATOM 982 O ILE B 118 -8.793 7.289 5.074 1.00 18.17 O ANISOU 982 O ILE B 118 2090 3068 1747 -1153 474 -322 O ATOM 983 CB ILE B 118 -6.391 5.267 5.344 1.00 22.59 C ANISOU 983 CB ILE B 118 2211 3974 2399 -998 611 -640 C ATOM 984 CG1 ILE B 118 -4.948 5.064 5.828 1.00 25.72 C ANISOU 984 CG1 ILE B 118 2430 4503 2839 -942 627 -775 C ATOM 985 CG2 ILE B 118 -6.789 4.178 4.372 1.00 21.11 C ANISOU 985 CG2 ILE B 118 2050 3769 2200 -932 627 -680 C ATOM 986 CD1 ILE B 118 -4.840 4.131 6.986 1.00 30.63 C ANISOU 986 CD1 ILE B 118 2905 5141 3591 -736 552 -803 C ATOM 987 N TYR B 119 -8.192 6.822 2.956 1.00 20.73 N ANISOU 987 N TYR B 119 2477 3510 1890 -1320 606 -426 N ATOM 988 CA TYR B 119 -9.494 7.219 2.446 1.00 23.15 C ANISOU 988 CA TYR B 119 2996 3641 2157 -1328 502 -293 C ATOM 989 C TYR B 119 -9.719 6.492 1.130 1.00 18.63 C ANISOU 989 C TYR B 119 2500 3084 1496 -1355 525 -330 C ATOM 990 O TYR B 119 -8.792 5.916 0.556 1.00 20.51 O ANISOU 990 O TYR B 119 2646 3467 1679 -1405 645 -459 O ATOM 991 CB TYR B 119 -9.561 8.740 2.287 1.00 24.55 C ANISOU 991 CB TYR B 119 3354 3743 2233 -1502 488 -202 C ATOM 992 CG TYR B 119 -8.629 9.290 1.232 1.00 27.17 C ANISOU 992 CG TYR B 119 3764 4134 2427 -1660 556 -272 C ATOM 993 CD1 TYR B 119 -7.275 9.466 1.486 1.00 29.33 C ANISOU 993 CD1 TYR B 119 3900 4539 2706 -1708 641 -393 C ATOM 994 CD2 TYR B 119 -9.113 9.628 -0.023 1.00 27.78 C ANISOU 994 CD2 TYR B 119 4056 4128 2371 -1768 523 -219 C ATOM 995 CE1 TYR B 119 -6.427 9.978 0.496 1.00 40.17 C ANISOU 995 CE1 TYR B 119 5341 5964 3956 -1880 710 -464 C ATOM 996 CE2 TYR B 119 -8.292 10.132 -1.001 1.00 37.40 C ANISOU 996 CE2 TYR B 119 5354 5389 3468 -1934 587 -282 C ATOM 997 CZ TYR B 119 -6.954 10.306 -0.744 1.00 44.61 C ANISOU 997 CZ TYR B 119 6123 6437 4389 -1999 688 -406 C ATOM 998 OH TYR B 119 -6.156 10.809 -1.746 1.00 52.62 O ANISOU 998 OH TYR B 119 7220 7494 5278 -2187 760 -474 O ATOM 999 N ARG B 120 -10.970 6.504 0.670 1.00 19.72 N ANISOU 999 N ARG B 120 2793 3075 1624 -1314 405 -230 N ATOM 1000 CA ARG B 120 -11.303 5.803 -0.575 1.00 22.15 C ANISOU 1000 CA ARG B 120 3190 3385 1842 -1338 404 -262 C ATOM 1001 C ARG B 120 -10.622 6.432 -1.787 1.00 24.16 C ANISOU 1001 C ARG B 120 3589 3710 1880 -1570 504 -289 C ATOM 1002 O ARG B 120 -10.645 7.651 -1.974 1.00 24.37 O ANISOU 1002 O ARG B 120 3775 3669 1814 -1706 477 -203 O ATOM 1003 CB ARG B 120 -12.818 5.781 -0.784 1.00 21.33 C ANISOU 1003 CB ARG B 120 3214 3114 1775 -1253 235 -152 C ATOM 1004 CG ARG B 120 -13.544 4.804 0.134 1.00 19.68 C ANISOU 1004 CG ARG B 120 2866 2855 1756 -1049 166 -156 C ATOM 1005 CD ARG B 120 -15.032 4.774 -0.139 1.00 21.95 C ANISOU 1005 CD ARG B 120 3252 3004 2084 -985 10 -73 C ATOM 1006 NE ARG B 120 -15.283 4.230 -1.468 1.00 24.53 N ANISOU 1006 NE ARG B 120 3686 3338 2298 -1040 -9 -105 N ATOM 1007 CZ ARG B 120 -15.822 3.037 -1.698 1.00 28.78 C ANISOU 1007 CZ ARG B 120 4177 3863 2896 -954 -40 -155 C ATOM 1008 NH1 ARG B 120 -16.199 2.263 -0.694 1.00 23.94 N ANISOU 1008 NH1 ARG B 120 3424 3221 2451 -816 -55 -170 N ATOM 1009 NH2 ARG B 120 -15.993 2.619 -2.946 1.00 29.64 N ANISOU 1009 NH2 ARG B 120 4397 3982 2883 -1021 -57 -191 N ATOM 1010 N ALA B 121 -10.042 5.582 -2.641 1.00 25.19 N ANISOU 1010 N ALA B 121 3678 3960 1934 -1611 613 -414 N ATOM 1011 CA ALA B 121 -9.373 6.093 -3.832 1.00 27.55 C ANISOU 1011 CA ALA B 121 4077 4283 2109 -1788 675 -451 C ATOM 1012 C ALA B 121 -10.349 6.798 -4.762 1.00 28.23 C ANISOU 1012 C ALA B 121 4444 4212 2071 -1878 552 -316 C ATOM 1013 O ALA B 121 -9.952 7.705 -5.506 1.00 31.73 O ANISOU 1013 O ALA B 121 5024 4618 2415 -2041 565 -295 O ATOM 1014 CB ALA B 121 -8.655 4.959 -4.568 1.00 27.23 C ANISOU 1014 CB ALA B 121 3917 4372 2058 -1775 792 -614 C ATOM 1015 N ASP B 122 -11.626 6.407 -4.736 1.00 26.11 N ANISOU 1015 N ASP B 122 4270 3846 1807 -1770 415 -232 N ATOM 1016 CA ASP B 122 -12.594 7.030 -5.627 1.00 28.74 C ANISOU 1016 CA ASP B 122 4854 4023 2043 -1822 262 -110 C ATOM 1017 C ASP B 122 -13.159 8.335 -5.077 1.00 27.69 C ANISOU 1017 C ASP B 122 4846 3740 1936 -1823 130 31 C ATOM 1018 O ASP B 122 -14.022 8.936 -5.723 1.00 31.40 O ANISOU 1018 O ASP B 122 5519 4060 2351 -1834 -27 131 O ATOM 1019 CB ASP B 122 -13.722 6.042 -5.971 1.00 27.70 C ANISOU 1019 CB ASP B 122 4760 3849 1917 -1702 139 -104 C ATOM 1020 CG ASP B 122 -14.561 5.609 -4.764 1.00 31.04 C ANISOU 1020 CG ASP B 122 5021 4204 2568 -1485 30 -75 C ATOM 1021 OD1 ASP B 122 -14.453 6.184 -3.661 1.00 27.56 O ANISOU 1021 OD1 ASP B 122 4488 3738 2246 -1430 29 -34 O ATOM 1022 OD2 ASP B 122 -15.354 4.648 -4.926 1.00 30.96 O ANISOU 1022 OD2 ASP B 122 4967 4162 2636 -1370 -50 -101 O ATOM 1023 N GLY B 123 -12.681 8.797 -3.922 1.00 25.20 N ANISOU 1023 N GLY B 123 4411 3452 1710 -1802 181 30 N ATOM 1024 CA GLY B 123 -13.069 10.086 -3.395 1.00 25.51 C ANISOU 1024 CA GLY B 123 4564 3350 1781 -1805 73 137 C ATOM 1025 C GLY B 123 -14.316 10.093 -2.541 1.00 27.62 C ANISOU 1025 C GLY B 123 4823 3499 2174 -1630 -87 234 C ATOM 1026 O GLY B 123 -14.658 11.147 -1.988 1.00 27.04 O ANISOU 1026 O GLY B 123 4831 3302 2140 -1616 -173 317 O ATOM 1027 N GLN B 124 -14.992 8.956 -2.394 1.00 22.76 N ANISOU 1027 N GLN B 124 4061 2899 1685 -1463 -135 192 N ATOM 1028 CA GLN B 124 -16.225 8.900 -1.630 1.00 20.73 C ANISOU 1028 CA GLN B 124 3733 2530 1614 -1271 -287 240 C ATOM 1029 C GLN B 124 -15.929 8.756 -0.143 1.00 19.04 C ANISOU 1029 C GLN B 124 3303 2358 1574 -1169 -215 204 C ATOM 1030 O GLN B 124 -14.859 8.281 0.247 1.00 21.39 O ANISOU 1030 O GLN B 124 3466 2786 1876 -1201 -66 125 O ATOM 1031 CB GLN B 124 -17.088 7.735 -2.103 1.00 22.91 C ANISOU 1031 CB GLN B 124 3953 2807 1945 -1166 -363 204 C ATOM 1032 CG GLN B 124 -17.600 7.930 -3.535 1.00 21.71 C ANISOU 1032 CG GLN B 124 4031 2596 1624 -1249 -480 249 C ATOM 1033 CD GLN B 124 -18.491 6.788 -4.002 1.00 33.78 C ANISOU 1033 CD GLN B 124 5502 4126 3208 -1154 -566 204 C ATOM 1034 OE1 GLN B 124 -18.248 5.626 -3.681 1.00 41.10 O ANISOU 1034 OE1 GLN B 124 6257 5139 4219 -1098 -467 114 O ATOM 1035 NE2 GLN B 124 -19.529 7.119 -4.764 1.00 48.55 N ANISOU 1035 NE2 GLN B 124 7522 5894 5030 -1136 -762 266 N ATOM 1036 N PRO B 125 -16.857 9.172 0.710 1.00 19.10 N ANISOU 1036 N PRO B 125 3274 2260 1723 -1043 -322 253 N ATOM 1037 CA PRO B 125 -16.709 8.914 2.149 1.00 19.10 C ANISOU 1037 CA PRO B 125 3081 2297 1880 -942 -260 217 C ATOM 1038 C PRO B 125 -17.002 7.452 2.465 1.00 19.64 C ANISOU 1038 C PRO B 125 2981 2426 2055 -828 -231 154 C ATOM 1039 O PRO B 125 -17.431 6.677 1.602 1.00 19.24 O ANISOU 1039 O PRO B 125 2955 2379 1976 -819 -269 134 O ATOM 1040 CB PRO B 125 -17.737 9.854 2.783 1.00 22.18 C ANISOU 1040 CB PRO B 125 3511 2548 2368 -855 -385 279 C ATOM 1041 CG PRO B 125 -18.779 10.035 1.705 1.00 21.38 C ANISOU 1041 CG PRO B 125 3552 2345 2227 -834 -546 327 C ATOM 1042 CD PRO B 125 -18.041 9.995 0.402 1.00 22.60 C ANISOU 1042 CD PRO B 125 3862 2545 2182 -991 -509 335 C ATOM 1043 N ILE B 126 -16.756 7.078 3.726 1.00 18.14 N ANISOU 1043 N ILE B 126 2638 2275 1978 -750 -169 123 N ATOM 1044 CA ILE B 126 -16.859 5.694 4.175 1.00 15.48 C ANISOU 1044 CA ILE B 126 2165 1983 1733 -655 -132 68 C ATOM 1045 C ILE B 126 -17.932 5.545 5.241 1.00 16.71 C ANISOU 1045 C ILE B 126 2245 2068 2034 -545 -184 90 C ATOM 1046 O ILE B 126 -18.280 6.483 5.966 1.00 13.92 O ANISOU 1046 O ILE B 126 1898 1663 1726 -528 -212 125 O ATOM 1047 CB ILE B 126 -15.535 5.136 4.728 1.00 13.78 C ANISOU 1047 CB ILE B 126 1842 1884 1511 -656 -12 2 C ATOM 1048 CG1 ILE B 126 -15.026 6.006 5.876 1.00 19.02 C ANISOU 1048 CG1 ILE B 126 2464 2562 2202 -664 18 20 C ATOM 1049 CG2 ILE B 126 -14.500 5.001 3.625 1.00 17.27 C ANISOU 1049 CG2 ILE B 126 2317 2424 1822 -760 64 -58 C ATOM 1050 CD1 ILE B 126 -13.706 5.514 6.474 1.00 18.00 C ANISOU 1050 CD1 ILE B 126 2212 2555 2072 -655 109 -53 C ATOM 1051 N PHE B 127 -18.425 4.313 5.341 1.00 11.93 N ANISOU 1051 N PHE B 127 1572 1463 1499 -481 -183 57 N ATOM 1052 CA PHE B 127 -19.350 3.879 6.386 1.00 11.97 C ANISOU 1052 CA PHE B 127 1495 1422 1632 -402 -196 59 C ATOM 1053 C PHE B 127 -18.642 2.818 7.217 1.00 11.87 C ANISOU 1053 C PHE B 127 1411 1454 1644 -362 -113 26 C ATOM 1054 O PHE B 127 -18.343 1.728 6.717 1.00 14.53 O ANISOU 1054 O PHE B 127 1745 1810 1964 -350 -94 -15 O ATOM 1055 CB PHE B 127 -20.634 3.349 5.761 1.00 13.09 C ANISOU 1055 CB PHE B 127 1636 1511 1828 -382 -279 50 C ATOM 1056 CG PHE B 127 -21.335 4.382 4.922 1.00 16.53 C ANISOU 1056 CG PHE B 127 2149 1894 2237 -399 -395 82 C ATOM 1057 CD1 PHE B 127 -21.992 5.451 5.533 1.00 15.47 C ANISOU 1057 CD1 PHE B 127 2002 1705 2172 -359 -449 107 C ATOM 1058 CD2 PHE B 127 -21.277 4.333 3.544 1.00 18.32 C ANISOU 1058 CD2 PHE B 127 2478 2121 2362 -451 -456 84 C ATOM 1059 CE1 PHE B 127 -22.603 6.439 4.778 1.00 15.54 C ANISOU 1059 CE1 PHE B 127 2099 1645 2161 -353 -580 138 C ATOM 1060 CE2 PHE B 127 -21.882 5.316 2.781 1.00 22.84 C ANISOU 1060 CE2 PHE B 127 3152 2630 2894 -462 -587 126 C ATOM 1061 CZ PHE B 127 -22.546 6.370 3.395 1.00 17.15 C ANISOU 1061 CZ PHE B 127 2420 1840 2255 -405 -658 155 C ATOM 1062 N MET B 128 -18.333 3.147 8.468 1.00 11.03 N ANISOU 1062 N MET B 128 1262 1358 1571 -337 -74 39 N ATOM 1063 CA MET B 128 -17.646 2.208 9.348 1.00 13.11 C ANISOU 1063 CA MET B 128 1479 1652 1849 -288 -21 18 C ATOM 1064 C MET B 128 -18.673 1.455 10.181 1.00 11.11 C ANISOU 1064 C MET B 128 1211 1332 1678 -252 -22 30 C ATOM 1065 O MET B 128 -19.607 2.058 10.721 1.00 13.83 O ANISOU 1065 O MET B 128 1541 1640 2074 -261 -31 50 O ATOM 1066 CB MET B 128 -16.649 2.939 10.248 1.00 13.35 C ANISOU 1066 CB MET B 128 1483 1739 1849 -292 14 22 C ATOM 1067 CG MET B 128 -15.504 3.616 9.473 1.00 11.85 C ANISOU 1067 CG MET B 128 1298 1632 1573 -357 37 -6 C ATOM 1068 SD MET B 128 -14.323 4.350 10.632 1.00 16.11 S ANISOU 1068 SD MET B 128 1783 2249 2088 -371 73 -19 S ATOM 1069 CE MET B 128 -15.350 5.631 11.363 1.00 16.17 C ANISOU 1069 CE MET B 128 1845 2168 2129 -397 45 41 C ATOM 1070 N ALA B 129 -18.535 0.132 10.222 1.00 11.89 N ANISOU 1070 N ALA B 129 1320 1411 1788 -218 -10 9 N ATOM 1071 CA ALA B 129 -19.438 -0.688 11.017 1.00 12.45 C ANISOU 1071 CA ALA B 129 1401 1411 1918 -213 2 23 C ATOM 1072 C ALA B 129 -19.183 -0.445 12.497 1.00 13.27 C ANISOU 1072 C ALA B 129 1507 1518 2018 -198 38 53 C ATOM 1073 O ALA B 129 -18.031 -0.458 12.952 1.00 14.65 O ANISOU 1073 O ALA B 129 1686 1733 2147 -156 40 53 O ATOM 1074 CB ALA B 129 -19.230 -2.163 10.686 1.00 12.52 C ANISOU 1074 CB ALA B 129 1456 1375 1927 -184 -1 -4 C ATOM 1075 N ALA B 130 -20.261 -0.239 13.253 1.00 10.06 N ANISOU 1075 N ALA B 130 1174 1495 1152 -126 11 -88 N ATOM 1076 CA ALA B 130 -20.159 -0.010 14.685 1.00 11.61 C ANISOU 1076 CA ALA B 130 1419 1552 1439 -121 37 1 C ATOM 1077 C ALA B 130 -21.136 -0.924 15.407 1.00 11.90 C ANISOU 1077 C ALA B 130 1437 1509 1577 -173 71 -50 C ATOM 1078 O ALA B 130 -22.126 -1.389 14.829 1.00 12.53 O ANISOU 1078 O ALA B 130 1437 1647 1678 -222 60 -157 O ATOM 1079 CB ALA B 130 -20.440 1.456 15.037 1.00 15.43 C ANISOU 1079 CB ALA B 130 1920 2052 1891 -79 15 112 C ATOM 1080 N ILE B 131 -20.819 -1.216 16.675 1.00 12.44 N ANISOU 1080 N ILE B 131 1571 1455 1700 -169 116 25 N ATOM 1081 CA ILE B 131 -21.760 -1.858 17.584 1.00 11.84 C ANISOU 1081 CA ILE B 131 1501 1300 1699 -226 188 38 C ATOM 1082 C ILE B 131 -21.753 -1.068 18.886 1.00 15.09 C ANISOU 1082 C ILE B 131 1969 1716 2048 -189 206 145 C ATOM 1083 O ILE B 131 -20.750 -0.448 19.251 1.00 14.99 O ANISOU 1083 O ILE B 131 2006 1718 1971 -128 160 194 O ATOM 1084 CB ILE B 131 -21.435 -3.353 17.835 1.00 13.26 C ANISOU 1084 CB ILE B 131 1731 1311 1996 -261 256 33 C ATOM 1085 CG1 ILE B 131 -20.087 -3.530 18.535 1.00 14.04 C ANISOU 1085 CG1 ILE B 131 1926 1339 2071 -163 236 148 C ATOM 1086 CG2 ILE B 131 -21.497 -4.176 16.517 1.00 15.90 C ANISOU 1086 CG2 ILE B 131 1996 1634 2410 -310 250 -145 C ATOM 1087 CD1 ILE B 131 -19.757 -4.993 18.796 1.00 14.22 C ANISOU 1087 CD1 ILE B 131 2011 1157 2234 -153 300 181 C ATOM 1088 N GLY B 132 -22.884 -1.078 19.583 1.00 15.77 N ANISOU 1088 N GLY B 132 2030 1809 2154 -237 282 150 N ATOM 1089 CA GLY B 132 -22.970 -0.254 20.772 1.00 15.88 C ANISOU 1089 CA GLY B 132 2088 1863 2081 -200 312 207 C ATOM 1090 C GLY B 132 -24.213 -0.547 21.580 1.00 18.38 C ANISOU 1090 C GLY B 132 2370 2192 2419 -268 443 208 C ATOM 1091 O GLY B 132 -24.977 -1.465 21.282 1.00 17.97 O ANISOU 1091 O GLY B 132 2257 2094 2476 -363 518 176 O ATOM 1092 N SER B 133 -24.393 0.249 22.632 1.00 16.94 N ANISOU 1092 N SER B 133 2218 2079 2139 -232 487 221 N ATOM 1093 CA SER B 133 -25.427 0.001 23.635 1.00 17.29 C ANISOU 1093 CA SER B 133 2244 2165 2159 -294 650 233 C ATOM 1094 C SER B 133 -26.692 0.779 23.291 1.00 19.89 C ANISOU 1094 C SER B 133 2399 2579 2580 -294 682 101 C ATOM 1095 O SER B 133 -26.727 2.005 23.405 1.00 19.85 O ANISOU 1095 O SER B 133 2366 2627 2548 -201 637 32 O ATOM 1096 CB SER B 133 -24.922 0.389 25.020 1.00 18.78 C ANISOU 1096 CB SER B 133 2558 2427 2151 -244 688 292 C ATOM 1097 OG SER B 133 -25.962 0.267 25.984 1.00 21.58 O ANISOU 1097 OG SER B 133 2893 2860 2447 -303 874 296 O ATOM 1098 N THR B 134 -27.740 0.063 22.905 1.00 21.42 N ANISOU 1098 N THR B 134 2460 2775 2904 -395 764 52 N ATOM 1099 CA THR B 134 -29.020 0.719 22.718 1.00 22.18 C ANISOU 1099 CA THR B 134 2351 2984 3094 -382 797 -80 C ATOM 1100 C THR B 134 -29.744 0.857 24.058 1.00 24.91 C ANISOU 1100 C THR B 134 2678 3402 3385 -420 1005 -90 C ATOM 1101 O THR B 134 -29.527 0.058 24.976 1.00 26.42 O ANISOU 1101 O THR B 134 2997 3557 3484 -510 1150 26 O ATOM 1102 CB THR B 134 -29.883 -0.077 21.744 1.00 24.26 C ANISOU 1102 CB THR B 134 2430 3265 3524 -486 788 -177 C ATOM 1103 OG1 THR B 134 -29.941 -1.438 22.187 1.00 26.34 O ANISOU 1103 OG1 THR B 134 2748 3416 3843 -659 945 -121 O ATOM 1104 CG2 THR B 134 -29.299 -0.013 20.334 1.00 20.67 C ANISOU 1104 CG2 THR B 134 1970 2807 3075 -424 579 -206 C ATOM 1105 N PRO B 135 -30.623 1.864 24.203 1.00 25.26 N ANISOU 1105 N PRO B 135 2563 3555 3478 -340 1034 -219 N ATOM 1106 CA PRO B 135 -30.968 2.929 23.249 1.00 23.80 C ANISOU 1106 CA PRO B 135 2235 3406 3401 -190 872 -316 C ATOM 1107 C PRO B 135 -29.900 4.013 23.129 1.00 24.59 C ANISOU 1107 C PRO B 135 2490 3427 3427 -46 734 -276 C ATOM 1108 O PRO B 135 -29.472 4.593 24.122 1.00 21.47 O ANISOU 1108 O PRO B 135 2205 3019 2932 -11 799 -295 O ATOM 1109 CB PRO B 135 -32.265 3.508 23.821 1.00 27.86 C ANISOU 1109 CB PRO B 135 2540 4041 4005 -149 1010 -458 C ATOM 1110 CG PRO B 135 -32.253 3.132 25.266 1.00 28.94 C ANISOU 1110 CG PRO B 135 2802 4203 3991 -242 1215 -420 C ATOM 1111 CD PRO B 135 -31.536 1.833 25.358 1.00 27.86 C ANISOU 1111 CD PRO B 135 2835 3980 3772 -391 1243 -259 C ATOM 1112 N PHE B 136 -29.493 4.289 21.890 1.00 21.30 N ANISOU 1112 N PHE B 136 2071 2968 3055 24 553 -234 N ATOM 1113 CA PHE B 136 -28.421 5.248 21.651 1.00 20.10 C ANISOU 1113 CA PHE B 136 2061 2715 2863 123 446 -177 C ATOM 1114 C PHE B 136 -28.804 6.663 22.055 1.00 22.04 C ANISOU 1114 C PHE B 136 2268 2917 3188 265 468 -255 C ATOM 1115 O PHE B 136 -27.920 7.473 22.374 1.00 22.46 O ANISOU 1115 O PHE B 136 2452 2861 3222 302 450 -255 O ATOM 1116 CB PHE B 136 -28.029 5.223 20.175 1.00 15.27 C ANISOU 1116 CB PHE B 136 1446 2090 2266 161 284 -98 C ATOM 1117 CG PHE B 136 -27.265 4.009 19.783 1.00 16.44 C ANISOU 1117 CG PHE B 136 1674 2232 2341 41 261 -48 C ATOM 1118 CD1 PHE B 136 -26.046 3.733 20.362 1.00 17.91 C ANISOU 1118 CD1 PHE B 136 2022 2339 2442 -8 283 8 C ATOM 1119 CD2 PHE B 136 -27.747 3.153 18.801 1.00 19.96 C ANISOU 1119 CD2 PHE B 136 2014 2757 2814 -11 206 -82 C ATOM 1120 CE1 PHE B 136 -25.323 2.613 19.999 1.00 16.40 C ANISOU 1120 CE1 PHE B 136 1894 2122 2217 -85 264 50 C ATOM 1121 CE2 PHE B 136 -27.027 2.021 18.431 1.00 18.91 C ANISOU 1121 CE2 PHE B 136 1953 2586 2644 -114 200 -70 C ATOM 1122 CZ PHE B 136 -25.808 1.754 19.029 1.00 18.23 C ANISOU 1122 CZ PHE B 136 2036 2394 2497 -139 234 7 C ATOM 1123 N GLU B 137 -30.095 6.994 22.017 1.00 23.09 N ANISOU 1123 N GLU B 137 2207 3126 3441 348 507 -344 N ATOM 1124 CA GLU B 137 -30.507 8.366 22.269 1.00 24.76 C ANISOU 1124 CA GLU B 137 2368 3262 3778 522 523 -425 C ATOM 1125 C GLU B 137 -30.432 8.753 23.740 1.00 26.29 C ANISOU 1125 C GLU B 137 2622 3447 3920 496 692 -573 C ATOM 1126 O GLU B 137 -30.636 9.930 24.057 1.00 30.45 O ANISOU 1126 O GLU B 137 3129 3875 4565 632 723 -683 O ATOM 1127 CB GLU B 137 -31.929 8.607 21.739 1.00 24.66 C ANISOU 1127 CB GLU B 137 2092 3352 3925 657 495 -485 C ATOM 1128 CG GLU B 137 -33.029 7.792 22.405 1.00 28.34 C ANISOU 1128 CG GLU B 137 2360 4001 4409 555 651 -619 C ATOM 1129 CD GLU B 137 -33.271 6.431 21.749 1.00 32.27 C ANISOU 1129 CD GLU B 137 2771 4620 4870 389 609 -579 C ATOM 1130 OE1 GLU B 137 -32.343 5.874 21.110 1.00 26.34 O ANISOU 1130 OE1 GLU B 137 2176 3813 4020 311 503 -459 O ATOM 1131 OE2 GLU B 137 -34.407 5.916 21.880 1.00 33.14 O ANISOU 1131 OE2 GLU B 137 2692 4859 5042 322 676 -661 O ATOM 1132 N ARG B 138 -30.122 7.817 24.642 1.00 24.22 N ANISOU 1132 N ARG B 138 2443 3282 3477 336 802 -576 N ATOM 1133 CA ARG B 138 -30.096 8.160 26.060 1.00 25.55 C ANISOU 1133 CA ARG B 138 2669 3508 3530 318 961 -721 C ATOM 1134 C ARG B 138 -28.834 8.906 26.476 1.00 24.76 C ANISOU 1134 C ARG B 138 2754 3302 3353 331 894 -765 C ATOM 1135 O ARG B 138 -28.780 9.411 27.606 1.00 27.94 O ANISOU 1135 O ARG B 138 3198 3761 3658 336 1000 -940 O ATOM 1136 CB ARG B 138 -30.252 6.899 26.912 1.00 23.42 C ANISOU 1136 CB ARG B 138 2437 3398 3062 156 1111 -668 C ATOM 1137 CG ARG B 138 -28.993 6.039 27.026 1.00 24.45 C ANISOU 1137 CG ARG B 138 2775 3508 3008 53 1033 -502 C ATOM 1138 CD ARG B 138 -29.370 4.729 27.699 1.00 26.11 C ANISOU 1138 CD ARG B 138 3012 3830 3081 -85 1196 -396 C ATOM 1139 NE ARG B 138 -28.247 3.890 28.121 1.00 27.32 N ANISOU 1139 NE ARG B 138 3370 3976 3035 -147 1151 -228 N ATOM 1140 CZ ARG B 138 -27.581 3.052 27.330 1.00 26.60 C ANISOU 1140 CZ ARG B 138 3339 3774 2996 -186 1033 -77 C ATOM 1141 NH1 ARG B 138 -27.881 2.953 26.037 1.00 21.30 N ANISOU 1141 NH1 ARG B 138 2551 3011 2533 -188 942 -84 N ATOM 1142 NH2 ARG B 138 -26.595 2.317 27.834 1.00 25.99 N ANISOU 1142 NH2 ARG B 138 3433 3695 2749 -206 999 72 N ATOM 1143 N GLY B 139 -27.824 8.977 25.616 1.00 24.45 N ANISOU 1143 N GLY B 139 2810 3133 3347 322 733 -640 N ATOM 1144 CA GLY B 139 -26.639 9.760 25.930 1.00 24.52 C ANISOU 1144 CA GLY B 139 2948 3031 3335 315 674 -710 C ATOM 1145 C GLY B 139 -25.795 9.178 27.045 1.00 27.55 C ANISOU 1145 C GLY B 139 3450 3560 3459 210 691 -749 C ATOM 1146 O GLY B 139 -25.261 9.930 27.871 1.00 28.10 O ANISOU 1146 O GLY B 139 3571 3633 3472 208 701 -934 O ATOM 1147 N ASP B 140 -25.633 7.858 27.064 1.00 25.37 N ANISOU 1147 N ASP B 140 3213 3397 3028 132 685 -583 N ATOM 1148 CA ASP B 140 -24.891 7.195 28.125 1.00 26.76 C ANISOU 1148 CA ASP B 140 3506 3725 2936 70 690 -563 C ATOM 1149 C ASP B 140 -23.427 7.612 28.112 1.00 24.39 C ANISOU 1149 C ASP B 140 3279 3383 2605 59 535 -602 C ATOM 1150 O ASP B 140 -22.802 7.721 27.053 1.00 27.10 O ANISOU 1150 O ASP B 140 3611 3585 3101 54 429 -523 O ATOM 1151 CB ASP B 140 -25.003 5.680 27.983 1.00 22.16 C ANISOU 1151 CB ASP B 140 2959 3197 2264 6 716 -338 C ATOM 1152 CG ASP B 140 -24.776 4.964 29.295 1.00 27.87 C ANISOU 1152 CG ASP B 140 3796 4101 2691 -25 791 -278 C ATOM 1153 OD1 ASP B 140 -23.610 4.642 29.613 1.00 26.64 O ANISOU 1153 OD1 ASP B 140 3743 3993 2387 -13 668 -210 O ATOM 1154 OD2 ASP B 140 -25.768 4.758 30.035 1.00 35.34 O ANISOU 1154 OD2 ASP B 140 4723 5165 3542 -52 978 -297 O ATOM 1155 N GLU B 141 -22.881 7.853 29.308 1.00 21.66 N ANISOU 1155 N GLU B 141 2993 3190 2045 50 527 -742 N ATOM 1156 CA GLU B 141 -21.521 8.359 29.421 1.00 28.72 C ANISOU 1156 CA GLU B 141 3911 4078 2923 27 377 -848 C ATOM 1157 C GLU B 141 -20.473 7.258 29.432 1.00 32.81 C ANISOU 1157 C GLU B 141 4481 4698 3286 15 249 -664 C ATOM 1158 O GLU B 141 -19.282 7.555 29.292 1.00 36.85 O ANISOU 1158 O GLU B 141 4967 5202 3830 -6 111 -731 O ATOM 1159 CB GLU B 141 -21.382 9.194 30.698 1.00 36.66 C ANISOU 1159 CB GLU B 141 4928 5233 3766 25 399 -1145 C ATOM 1160 CG GLU B 141 -22.149 10.502 30.658 1.00 55.54 C ANISOU 1160 CG GLU B 141 7257 7463 6381 51 510 -1389 C ATOM 1161 CD GLU B 141 -21.535 11.485 29.694 1.00 70.17 C ANISOU 1161 CD GLU B 141 9071 9025 8567 27 438 -1446 C ATOM 1162 OE1 GLU B 141 -22.224 12.445 29.284 1.00 76.79 O ANISOU 1162 OE1 GLU B 141 9866 9641 9668 79 525 -1538 O ATOM 1163 OE2 GLU B 141 -20.346 11.299 29.360 1.00 74.25 O ANISOU 1163 OE2 GLU B 141 9592 9532 9086 -38 305 -1390 O ATOM 1164 N ALA B 142 -20.879 6.010 29.615 1.00 24.10 N ANISOU 1164 N ALA B 142 3437 3676 2043 31 301 -444 N ATOM 1165 CA ALA B 142 -19.960 4.889 29.752 1.00 22.93 C ANISOU 1165 CA ALA B 142 3351 3606 1755 58 192 -252 C ATOM 1166 C ALA B 142 -20.172 3.816 28.701 1.00 21.05 C ANISOU 1166 C ALA B 142 3115 3207 1677 49 216 -25 C ATOM 1167 O ALA B 142 -19.205 3.211 28.238 1.00 21.67 O ANISOU 1167 O ALA B 142 3194 3245 1794 76 101 76 O ATOM 1168 CB ALA B 142 -20.104 4.256 31.136 1.00 26.34 C ANISOU 1168 CB ALA B 142 3892 4278 1837 98 237 -173 C ATOM 1169 N GLU B 143 -21.414 3.542 28.343 1.00 19.33 N ANISOU 1169 N GLU B 143 2877 2911 1557 11 365 28 N ATOM 1170 CA GLU B 143 -21.756 2.500 27.380 1.00 21.40 C ANISOU 1170 CA GLU B 143 3125 3033 1973 -21 398 189 C ATOM 1171 C GLU B 143 -22.211 3.189 26.101 1.00 17.85 C ANISOU 1171 C GLU B 143 2562 2462 1759 -39 384 98 C ATOM 1172 O GLU B 143 -23.393 3.497 25.934 1.00 18.47 O ANISOU 1172 O GLU B 143 2566 2532 1920 -57 483 42 O ATOM 1173 CB GLU B 143 -22.834 1.579 27.934 1.00 21.20 C ANISOU 1173 CB GLU B 143 3139 3030 1885 -71 578 311 C ATOM 1174 CG GLU B 143 -22.294 0.608 28.948 1.00 24.70 C ANISOU 1174 CG GLU B 143 3729 3549 2107 -37 590 504 C ATOM 1175 CD GLU B 143 -23.326 -0.405 29.408 1.00 34.52 C ANISOU 1175 CD GLU B 143 5004 4765 3349 -121 782 655 C ATOM 1176 OE1 GLU B 143 -22.974 -1.265 30.237 1.00 40.68 O ANISOU 1176 OE1 GLU B 143 5874 5574 4008 -111 760 821 O ATOM 1177 OE2 GLU B 143 -24.483 -0.344 28.942 1.00 35.47 O ANISOU 1177 OE2 GLU B 143 5019 4830 3628 -209 921 585 O ATOM 1178 N GLY B 144 -21.255 3.422 25.203 1.00 16.05 N ANISOU 1178 N GLY B 144 2312 2159 1626 -25 261 92 N ATOM 1179 CA GLY B 144 -21.496 4.060 23.930 1.00 13.83 C ANISOU 1179 CA GLY B 144 1953 1781 1520 -27 235 55 C ATOM 1180 C GLY B 144 -21.365 3.080 22.775 1.00 19.07 C ANISOU 1180 C GLY B 144 2596 2389 2261 -47 206 147 C ATOM 1181 O GLY B 144 -22.040 2.044 22.758 1.00 17.93 O ANISOU 1181 O GLY B 144 2448 2236 2127 -82 270 200 O ATOM 1182 N PHE B 145 -20.495 3.374 21.812 1.00 15.13 N ANISOU 1182 N PHE B 145 2078 1850 1819 -40 130 149 N ATOM 1183 CA PHE B 145 -20.275 2.468 20.691 1.00 14.47 C ANISOU 1183 CA PHE B 145 1972 1741 1784 -55 110 193 C ATOM 1184 C PHE B 145 -18.790 2.150 20.531 1.00 15.33 C ANISOU 1184 C PHE B 145 2095 1846 1884 -41 50 206 C ATOM 1185 O PHE B 145 -17.906 2.809 21.093 1.00 14.54 O ANISOU 1185 O PHE B 145 1996 1772 1758 -30 7 174 O ATOM 1186 CB PHE B 145 -20.829 3.033 19.366 1.00 15.01 C ANISOU 1186 CB PHE B 145 1979 1814 1909 -50 94 182 C ATOM 1187 CG PHE B 145 -20.013 4.153 18.783 1.00 15.68 C ANISOU 1187 CG PHE B 145 2070 1875 2014 -34 62 197 C ATOM 1188 CD1 PHE B 145 -20.197 5.469 19.222 1.00 15.42 C ANISOU 1188 CD1 PHE B 145 2046 1785 2027 -11 75 178 C ATOM 1189 CD2 PHE B 145 -19.068 3.897 17.791 1.00 12.69 C ANISOU 1189 CD2 PHE B 145 1683 1513 1625 -51 45 221 C ATOM 1190 CE1 PHE B 145 -19.441 6.509 18.695 1.00 14.35 C ANISOU 1190 CE1 PHE B 145 1924 1577 1951 -22 76 206 C ATOM 1191 CE2 PHE B 145 -18.304 4.933 17.258 1.00 12.63 C ANISOU 1191 CE2 PHE B 145 1679 1474 1644 -65 55 255 C ATOM 1192 CZ PHE B 145 -18.495 6.238 17.703 1.00 17.18 C ANISOU 1192 CZ PHE B 145 2276 1960 2289 -58 73 260 C ATOM 1193 N LEU B 146 -18.538 1.119 19.735 1.00 13.44 N ANISOU 1193 N LEU B 146 1841 1581 1685 -42 51 220 N ATOM 1194 CA LEU B 146 -17.206 0.710 19.302 1.00 13.14 C ANISOU 1194 CA LEU B 146 1778 1543 1671 -14 13 209 C ATOM 1195 C LEU B 146 -17.191 0.620 17.785 1.00 12.60 C ANISOU 1195 C LEU B 146 1661 1494 1632 -39 34 164 C ATOM 1196 O LEU B 146 -18.214 0.313 17.163 1.00 13.97 O ANISOU 1196 O LEU B 146 1827 1674 1807 -67 57 140 O ATOM 1197 CB LEU B 146 -16.813 -0.661 19.868 1.00 13.62 C ANISOU 1197 CB LEU B 146 1876 1545 1755 41 8 256 C ATOM 1198 CG LEU B 146 -17.073 -0.898 21.360 1.00 13.23 C ANISOU 1198 CG LEU B 146 1906 1496 1623 76 5 348 C ATOM 1199 CD1 LEU B 146 -18.428 -1.549 21.582 1.00 17.20 C ANISOU 1199 CD1 LEU B 146 2463 1926 2147 20 108 397 C ATOM 1200 CD2 LEU B 146 -15.971 -1.763 21.931 1.00 16.90 C ANISOU 1200 CD2 LEU B 146 2392 1945 2084 187 -60 422 C ATOM 1201 N ILE B 147 -16.027 0.861 17.191 1.00 12.26 N ANISOU 1201 N ILE B 147 1570 1489 1598 -34 29 138 N ATOM 1202 CA ILE B 147 -15.833 0.616 15.762 1.00 10.69 C ANISOU 1202 CA ILE B 147 1331 1347 1383 -51 68 90 C ATOM 1203 C ILE B 147 -15.328 -0.805 15.568 1.00 12.63 C ANISOU 1203 C ILE B 147 1553 1554 1693 -9 82 12 C ATOM 1204 O ILE B 147 -14.333 -1.215 16.182 1.00 15.54 O ANISOU 1204 O ILE B 147 1892 1887 2124 52 60 12 O ATOM 1205 CB ILE B 147 -14.857 1.628 15.142 1.00 13.94 C ANISOU 1205 CB ILE B 147 1698 1823 1775 -84 103 105 C ATOM 1206 CG1 ILE B 147 -15.389 3.051 15.268 1.00 17.14 C ANISOU 1206 CG1 ILE B 147 2144 2203 2164 -119 107 190 C ATOM 1207 CG2 ILE B 147 -14.654 1.285 13.656 1.00 15.44 C ANISOU 1207 CG2 ILE B 147 1857 2115 1892 -97 166 59 C ATOM 1208 CD1 ILE B 147 -16.574 3.330 14.397 1.00 22.19 C ANISOU 1208 CD1 ILE B 147 2822 2884 2724 -105 107 245 C ATOM 1209 N VAL B 148 -16.013 -1.563 14.716 1.00 14.34 N ANISOU 1209 N VAL B 148 1768 1775 1907 -30 111 -72 N ATOM 1210 CA VAL B 148 -15.576 -2.924 14.417 1.00 13.17 C ANISOU 1210 CA VAL B 148 1598 1546 1859 7 145 -184 C ATOM 1211 C VAL B 148 -14.314 -2.878 13.561 1.00 14.93 C ANISOU 1211 C VAL B 148 1741 1866 2065 40 188 -269 C ATOM 1212 O VAL B 148 -14.210 -2.074 12.621 1.00 14.53 O ANISOU 1212 O VAL B 148 1664 1972 1884 -7 220 -279 O ATOM 1213 CB VAL B 148 -16.706 -3.690 13.711 1.00 16.74 C ANISOU 1213 CB VAL B 148 2051 1982 2326 -55 169 -310 C ATOM 1214 CG1 VAL B 148 -16.242 -5.086 13.339 1.00 16.81 C ANISOU 1214 CG1 VAL B 148 2041 1867 2481 -24 224 -467 C ATOM 1215 CG2 VAL B 148 -17.968 -3.743 14.606 1.00 13.81 C ANISOU 1215 CG2 VAL B 148 1726 1524 1999 -106 157 -234 C ATOM 1216 N THR B 149 -13.339 -3.744 13.875 1.00 14.39 N ANISOU 1216 N THR B 149 1629 1708 2130 131 198 -318 N ATOM 1217 CA THR B 149 -12.087 -3.798 13.134 1.00 14.04 C ANISOU 1217 CA THR B 149 1471 1762 2102 173 257 -427 C ATOM 1218 C THR B 149 -11.900 -5.142 12.436 1.00 16.65 C ANISOU 1218 C THR B 149 1768 2015 2544 233 325 -622 C ATOM 1219 O THR B 149 -12.523 -6.153 12.776 1.00 19.41 O ANISOU 1219 O THR B 149 2183 2170 3021 259 316 -652 O ATOM 1220 CB THR B 149 -10.882 -3.510 14.036 1.00 19.64 C ANISOU 1220 CB THR B 149 2095 2476 2893 255 206 -360 C ATOM 1221 OG1 THR B 149 -10.783 -4.539 15.029 1.00 18.45 O ANISOU 1221 OG1 THR B 149 1977 2153 2881 386 138 -311 O ATOM 1222 CG2 THR B 149 -11.056 -2.162 14.699 1.00 16.27 C ANISOU 1222 CG2 THR B 149 1695 2113 2374 176 151 -227 C ATOM 1223 N ALA B 150 -11.015 -5.131 11.443 1.00 18.25 N ANISOU 1223 N ALA B 150 1862 2361 2712 246 415 -769 N ATOM 1224 CA ALA B 150 -10.656 -6.320 10.685 1.00 22.69 C ANISOU 1224 CA ALA B 150 2367 2873 3382 314 502 -1011 C ATOM 1225 C ALA B 150 -9.148 -6.343 10.480 1.00 19.91 C ANISOU 1225 C ALA B 150 1848 2609 3110 412 572 -1094 C ATOM 1226 O ALA B 150 -8.456 -5.338 10.675 1.00 21.50 O ANISOU 1226 O ALA B 150 1970 2953 3245 380 571 -986 O ATOM 1227 CB ALA B 150 -11.380 -6.367 9.326 1.00 22.72 C ANISOU 1227 CB ALA B 150 2391 3042 3197 208 572 -1195 C ATOM 1228 N ALA B 151 -8.641 -7.506 10.076 1.00 23.56 N ANISOU 1228 N ALA B 151 2257 2973 3723 513 627 -1277 N ATOM 1229 CA ALA B 151 -7.244 -7.603 9.693 1.00 31.86 C ANISOU 1229 CA ALA B 151 3159 4131 4816 582 684 -1345 C ATOM 1230 C ALA B 151 -6.969 -6.705 8.493 1.00 28.46 C ANISOU 1230 C ALA B 151 2679 3999 4137 443 805 -1401 C ATOM 1231 O ALA B 151 -7.770 -6.622 7.555 1.00 25.56 O ANISOU 1231 O ALA B 151 2400 3740 3573 337 850 -1471 O ATOM 1232 CB ALA B 151 -6.877 -9.054 9.363 1.00 37.02 C ANISOU 1232 CB ALA B 151 3804 4615 5645 694 713 -1501 C ATOM 1233 N ALA B 152 -5.840 -6.012 8.538 1.00 28.37 N ANISOU 1233 N ALA B 152 2530 4123 4127 438 849 -1348 N ATOM 1234 CA ALA B 152 -5.397 -5.228 7.397 1.00 29.46 C ANISOU 1234 CA ALA B 152 2629 4508 4055 310 992 -1363 C ATOM 1235 C ALA B 152 -5.007 -6.157 6.255 1.00 32.51 C ANISOU 1235 C ALA B 152 2986 4953 4413 346 1094 -1580 C ATOM 1236 O ALA B 152 -4.307 -7.155 6.458 1.00 31.78 O ANISOU 1236 O ALA B 152 2803 4743 4531 481 1086 -1706 O ATOM 1237 CB ALA B 152 -4.222 -4.338 7.789 1.00 31.56 C ANISOU 1237 CB ALA B 152 2740 4863 4387 277 1026 -1269 C ATOM 1238 N ASP B 153 -5.473 -5.836 5.055 1.00 32.27 N ANISOU 1238 N ASP B 153 3036 5110 4116 237 1182 -1616 N ATOM 1239 CA ASP B 153 -5.221 -6.639 3.871 1.00 38.13 C ANISOU 1239 CA ASP B 153 3756 5950 4782 253 1280 -1839 C ATOM 1240 C ASP B 153 -4.383 -5.845 2.879 1.00 43.42 C ANISOU 1240 C ASP B 153 4365 6879 5255 173 1451 -1804 C ATOM 1241 O ASP B 153 -4.325 -4.613 2.934 1.00 43.28 O ANISOU 1241 O ASP B 153 4373 6957 5115 76 1492 -1583 O ATOM 1242 CB ASP B 153 -6.538 -7.080 3.217 1.00 38.60 C ANISOU 1242 CB ASP B 153 3955 6035 4675 202 1223 -1938 C ATOM 1243 CG ASP B 153 -7.522 -5.926 3.024 1.00 41.31 C ANISOU 1243 CG ASP B 153 4425 6525 4745 90 1178 -1732 C ATOM 1244 OD1 ASP B 153 -7.529 -4.989 3.856 1.00 37.21 O ANISOU 1244 OD1 ASP B 153 3920 5962 4257 63 1146 -1509 O ATOM 1245 OD2 ASP B 153 -8.310 -5.965 2.044 1.00 38.75 O ANISOU 1245 OD2 ASP B 153 4181 6363 4179 36 1164 -1795 O ATOM 1246 N GLN B 154 -3.730 -6.574 1.970 1.00 41.55 N ANISOU 1246 N GLN B 154 4050 6735 5002 213 1567 -2021 N ATOM 1247 CA GLN B 154 -3.008 -5.973 0.853 1.00 45.68 C ANISOU 1247 CA GLN B 154 4528 7519 5308 139 1760 -2014 C ATOM 1248 C GLN B 154 -2.119 -4.813 1.301 1.00 44.73 C ANISOU 1248 C GLN B 154 4314 7440 5242 74 1842 -1798 C ATOM 1249 O GLN B 154 -1.268 -4.981 2.181 1.00 40.16 O ANISOU 1249 O GLN B 154 3577 6745 4938 140 1809 -1820 O ATOM 1250 CB GLN B 154 -4.005 -5.539 -0.231 1.00 50.37 C ANISOU 1250 CB GLN B 154 5295 8315 5529 47 1780 -1961 C ATOM 1251 CG GLN B 154 -5.091 -6.593 -0.492 1.00 54.29 C ANISOU 1251 CG GLN B 154 5873 8757 5999 83 1650 -2171 C ATOM 1252 CD GLN B 154 -6.371 -6.030 -1.099 1.00 61.11 C ANISOU 1252 CD GLN B 154 6903 9777 6541 5 1569 -2059 C ATOM 1253 OE1 GLN B 154 -6.396 -4.911 -1.606 1.00 67.22 O ANISOU 1253 OE1 GLN B 154 7755 10728 7058 -59 1638 -1831 O ATOM 1254 NE2 GLN B 154 -7.447 -6.806 -1.028 1.00 59.95 N ANISOU 1254 NE2 GLN B 154 6805 9548 6427 15 1420 -2209 N ATOM 1255 N GLY B 155 -2.301 -3.630 0.715 1.00 46.68 N ANISOU 1255 N GLY B 155 4653 7842 5241 -53 1943 -1582 N ATOM 1256 CA GLY B 155 -1.380 -2.541 0.991 1.00 42.46 C ANISOU 1256 CA GLY B 155 4017 7335 4782 -141 2059 -1398 C ATOM 1257 C GLY B 155 -1.426 -2.042 2.422 1.00 44.98 C ANISOU 1257 C GLY B 155 4292 7460 5336 -153 1908 -1265 C ATOM 1258 O GLY B 155 -0.430 -1.516 2.933 1.00 43.11 O ANISOU 1258 O GLY B 155 3892 7207 5279 -197 1955 -1221 O ATOM 1259 N LEU B 156 -2.561 -2.216 3.096 1.00 34.88 N ANISOU 1259 N LEU B 156 3145 6046 4062 -117 1724 -1219 N ATOM 1260 CA LEU B 156 -2.752 -1.567 4.390 1.00 32.09 C ANISOU 1260 CA LEU B 156 2781 5538 3873 -145 1593 -1068 C ATOM 1261 C LEU B 156 -1.904 -2.197 5.487 1.00 34.58 C ANISOU 1261 C LEU B 156 2908 5735 4497 -36 1489 -1192 C ATOM 1262 O LEU B 156 -1.565 -1.520 6.463 1.00 36.09 O ANISOU 1262 O LEU B 156 3021 5860 4832 -76 1417 -1093 O ATOM 1263 CB LEU B 156 -4.230 -1.598 4.771 1.00 31.79 C ANISOU 1263 CB LEU B 156 2930 5409 3741 -132 1443 -990 C ATOM 1264 CG LEU B 156 -5.077 -0.522 4.093 1.00 33.95 C ANISOU 1264 CG LEU B 156 3385 5769 3746 -240 1493 -767 C ATOM 1265 CD1 LEU B 156 -6.559 -0.758 4.377 1.00 28.05 C ANISOU 1265 CD1 LEU B 156 2793 4962 2901 -206 1331 -741 C ATOM 1266 CD2 LEU B 156 -4.645 0.864 4.554 1.00 31.88 C ANISOU 1266 CD2 LEU B 156 3101 5452 3561 -358 1553 -535 C ATOM 1267 N VAL B 157 -1.547 -3.477 5.353 1.00 33.83 N ANISOU 1267 N VAL B 157 2737 5608 4508 111 1470 -1404 N ATOM 1268 CA VAL B 157 -0.769 -4.132 6.402 1.00 41.32 C ANISOU 1268 CA VAL B 157 3522 6436 5743 258 1351 -1484 C ATOM 1269 C VAL B 157 0.609 -3.502 6.549 1.00 40.72 C ANISOU 1269 C VAL B 157 3224 6467 5782 209 1423 -1482 C ATOM 1270 O VAL B 157 1.235 -3.622 7.608 1.00 45.66 O ANISOU 1270 O VAL B 157 3706 7029 6614 298 1288 -1488 O ATOM 1271 CB VAL B 157 -0.651 -5.649 6.137 1.00 50.08 C ANISOU 1271 CB VAL B 157 4610 7455 6962 436 1336 -1694 C ATOM 1272 CG1 VAL B 157 0.514 -5.946 5.210 1.00 49.43 C ANISOU 1272 CG1 VAL B 157 4362 7522 6896 454 1508 -1862 C ATOM 1273 CG2 VAL B 157 -0.503 -6.410 7.452 1.00 50.65 C ANISOU 1273 CG2 VAL B 157 4631 7319 7295 626 1145 -1679 C ATOM 1274 N ASP B 158 1.093 -2.816 5.513 1.00 37.81 N ANISOU 1274 N ASP B 158 2820 6268 5277 68 1630 -1467 N ATOM 1275 CA ASP B 158 2.373 -2.128 5.622 1.00 45.46 C ANISOU 1275 CA ASP B 158 3570 7335 6369 -15 1721 -1467 C ATOM 1276 C ASP B 158 2.288 -0.986 6.626 1.00 42.60 C ANISOU 1276 C ASP B 158 3201 6904 6082 -135 1618 -1301 C ATOM 1277 O ASP B 158 3.246 -0.727 7.365 1.00 42.10 O ANISOU 1277 O ASP B 158 2932 6852 6211 -140 1556 -1348 O ATOM 1278 CB ASP B 158 2.812 -1.603 4.256 1.00 43.07 C ANISOU 1278 CB ASP B 158 3257 7218 5892 -151 1994 -1453 C ATOM 1279 CG ASP B 158 3.153 -2.717 3.267 1.00 55.25 C ANISOU 1279 CG ASP B 158 4753 8862 7377 -36 2112 -1671 C ATOM 1280 OD1 ASP B 158 3.310 -2.417 2.060 1.00 55.40 O ANISOU 1280 OD1 ASP B 158 4807 9052 7192 -127 2334 -1662 O ATOM 1281 OD2 ASP B 158 3.280 -3.886 3.692 1.00 51.58 O ANISOU 1281 OD2 ASP B 158 4223 8302 7073 149 1990 -1845 O ATOM 1282 N ILE B 159 1.146 -0.297 6.666 1.00 37.07 N ANISOU 1282 N ILE B 159 2717 6134 5233 -230 1591 -1123 N ATOM 1283 CA ILE B 159 0.979 0.817 7.595 1.00 42.39 C ANISOU 1283 CA ILE B 159 3403 6720 5981 -351 1501 -980 C ATOM 1284 C ILE B 159 0.740 0.301 9.005 1.00 40.83 C ANISOU 1284 C ILE B 159 3174 6408 5932 -214 1242 -1028 C ATOM 1285 O ILE B 159 1.389 0.738 9.963 1.00 48.13 O ANISOU 1285 O ILE B 159 3955 7322 7011 -237 1133 -1051 O ATOM 1286 CB ILE B 159 -0.178 1.728 7.149 1.00 41.24 C ANISOU 1286 CB ILE B 159 3502 6529 5638 -478 1563 -762 C ATOM 1287 CG1 ILE B 159 0.003 2.192 5.709 1.00 45.49 C ANISOU 1287 CG1 ILE B 159 4099 7198 5989 -577 1812 -667 C ATOM 1288 CG2 ILE B 159 -0.306 2.930 8.093 1.00 31.88 C ANISOU 1288 CG2 ILE B 159 2329 5224 4561 -611 1485 -634 C ATOM 1289 CD1 ILE B 159 -1.061 3.181 5.314 1.00 44.74 C ANISOU 1289 CD1 ILE B 159 4239 7051 5710 -672 1857 -408 C ATOM 1290 N HIS B 160 -0.205 -0.623 9.155 1.00 33.03 N ANISOU 1290 N HIS B 160 2085 7081 3382 -173 -32 -1617 N ATOM 1291 CA HIS B 160 -0.636 -1.094 10.459 1.00 37.82 C ANISOU 1291 CA HIS B 160 2704 7601 4064 -18 -212 -1413 C ATOM 1292 C HIS B 160 -1.438 -2.372 10.265 1.00 31.90 C ANISOU 1292 C HIS B 160 1987 6612 3521 245 -349 -1311 C ATOM 1293 O HIS B 160 -1.997 -2.609 9.195 1.00 35.16 O ANISOU 1293 O HIS B 160 2457 6908 3992 244 -259 -1371 O ATOM 1294 CB HIS B 160 -1.465 -0.031 11.177 1.00 45.57 C ANISOU 1294 CB HIS B 160 3875 8532 4909 -253 -141 -1257 C ATOM 1295 CG HIS B 160 -1.658 -0.304 12.630 1.00 51.40 C ANISOU 1295 CG HIS B 160 4625 9269 5636 -180 -311 -1084 C ATOM 1296 ND1 HIS B 160 -0.639 -0.186 13.550 1.00 56.14 N ANISOU 1296 ND1 HIS B 160 5094 10077 6161 -175 -390 -1110 N ATOM 1297 CD2 HIS B 160 -2.753 -0.692 13.325 1.00 53.99 C ANISOU 1297 CD2 HIS B 160 5095 9431 5987 -135 -423 -879 C ATOM 1298 CE1 HIS B 160 -1.096 -0.493 14.750 1.00 55.64 C ANISOU 1298 CE1 HIS B 160 5100 9972 6069 -138 -548 -916 C ATOM 1299 NE2 HIS B 160 -2.376 -0.802 14.641 1.00 54.17 N ANISOU 1299 NE2 HIS B 160 5090 9561 5931 -120 -565 -775 N ATOM 1300 N ASP B 161 -1.512 -3.179 11.324 1.00 32.01 N ANISOU 1300 N ASP B 161 1988 6545 3630 451 -575 -1143 N ATOM 1301 CA ASP B 161 -1.995 -4.551 11.209 1.00 33.78 C ANISOU 1301 CA ASP B 161 2240 6518 4077 741 -740 -1053 C ATOM 1302 C ASP B 161 -3.513 -4.695 11.287 1.00 36.77 C ANISOU 1302 C ASP B 161 2840 6669 4460 722 -755 -863 C ATOM 1303 O ASP B 161 -4.028 -5.764 10.935 1.00 32.88 O ANISOU 1303 O ASP B 161 2408 5933 4152 933 -840 -821 O ATOM 1304 CB ASP B 161 -1.341 -5.425 12.288 1.00 44.27 C ANISOU 1304 CB ASP B 161 3488 7822 5512 967 -1008 -917 C ATOM 1305 CG ASP B 161 -1.834 -5.101 13.685 1.00 54.75 C ANISOU 1305 CG ASP B 161 4953 9169 6680 863 -1138 -652 C ATOM 1306 OD1 ASP B 161 -2.108 -6.047 14.452 1.00 65.16 O ANISOU 1306 OD1 ASP B 161 6359 10314 8086 1031 -1373 -420 O ATOM 1307 OD2 ASP B 161 -1.940 -3.903 14.022 1.00 55.04 O ANISOU 1307 OD2 ASP B 161 5032 9382 6498 588 -996 -675 O ATOM 1308 N ARG B 162 -4.243 -3.663 11.715 1.00 28.10 N ANISOU 1308 N ARG B 162 1897 5601 3177 464 -654 -760 N ATOM 1309 CA ARG B 162 -5.699 -3.683 11.750 1.00 26.45 C ANISOU 1309 CA ARG B 162 1997 5087 2967 388 -592 -576 C ATOM 1310 C ARG B 162 -6.250 -2.515 10.941 1.00 24.69 C ANISOU 1310 C ARG B 162 1873 4854 2652 132 -355 -650 C ATOM 1311 O ARG B 162 -5.535 -1.562 10.624 1.00 25.91 O ANISOU 1311 O ARG B 162 1906 5234 2705 -38 -242 -797 O ATOM 1312 CB ARG B 162 -6.247 -3.606 13.188 1.00 28.24 C ANISOU 1312 CB ARG B 162 2379 5272 3081 314 -695 -349 C ATOM 1313 CG ARG B 162 -5.615 -4.575 14.169 1.00 32.70 C ANISOU 1313 CG ARG B 162 2861 5887 3677 515 -967 -217 C ATOM 1314 CD ARG B 162 -6.166 -5.976 14.003 1.00 29.93 C ANISOU 1314 CD ARG B 162 2640 5210 3523 751 -1107 -75 C ATOM 1315 NE ARG B 162 -7.616 -6.065 14.196 1.00 26.68 N ANISOU 1315 NE ARG B 162 2522 4539 3076 624 -1029 92 N ATOM 1316 CZ ARG B 162 -8.340 -7.112 13.807 1.00 29.17 C ANISOU 1316 CZ ARG B 162 2986 4543 3556 754 -1072 178 C ATOM 1317 NH1 ARG B 162 -7.743 -8.140 13.206 1.00 33.85 N ANISOU 1317 NH1 ARG B 162 3469 5017 4374 1024 -1191 105 N ATOM 1318 NH2 ARG B 162 -9.649 -7.144 14.012 1.00 27.20 N ANISOU 1318 NH2 ARG B 162 2975 4101 3259 610 -991 308 N ATOM 1319 N ARG B 163 -7.542 -2.592 10.630 1.00 22.14 N ANISOU 1319 N ARG B 163 1778 4264 2371 98 -294 -537 N ATOM 1320 CA ARG B 163 -8.249 -1.550 9.902 1.00 19.41 C ANISOU 1320 CA ARG B 163 1554 3851 1970 -112 -118 -554 C ATOM 1321 C ARG B 163 -9.701 -1.556 10.356 1.00 20.63 C ANISOU 1321 C ARG B 163 1935 3751 2154 -144 -111 -387 C ATOM 1322 O ARG B 163 -10.191 -2.573 10.857 1.00 19.84 O ANISOU 1322 O ARG B 163 1906 3510 2121 -8 -218 -276 O ATOM 1323 CB ARG B 163 -8.179 -1.783 8.387 1.00 21.11 C ANISOU 1323 CB ARG B 163 1731 4057 2234 -96 -38 -676 C ATOM 1324 CG ARG B 163 -8.733 -3.150 7.969 1.00 20.04 C ANISOU 1324 CG ARG B 163 1644 3722 2249 117 -116 -652 C ATOM 1325 CD ARG B 163 -8.876 -3.242 6.473 1.00 24.83 C ANISOU 1325 CD ARG B 163 2240 4333 2862 71 -13 -778 C ATOM 1326 NE ARG B 163 -10.051 -2.497 6.056 1.00 28.16 N ANISOU 1326 NE ARG B 163 2856 4615 3227 -96 64 -657 N ATOM 1327 CZ ARG B 163 -10.620 -2.626 4.864 1.00 29.98 C ANISOU 1327 CZ ARG B 163 3147 4795 3449 -149 119 -688 C ATOM 1328 NH1 ARG B 163 -10.119 -3.474 3.982 1.00 27.69 N ANISOU 1328 NH1 ARG B 163 2739 4589 3193 -70 135 -865 N ATOM 1329 NH2 ARG B 163 -11.689 -1.907 4.569 1.00 31.40 N ANISOU 1329 NH2 ARG B 163 3489 4849 3593 -279 150 -557 N ATOM 1330 N PRO B 164 -10.421 -0.449 10.185 1.00 16.79 N ANISOU 1330 N PRO B 164 1558 3189 1633 -326 10 -371 N ATOM 1331 CA PRO B 164 -11.865 -0.494 10.438 1.00 16.51 C ANISOU 1331 CA PRO B 164 1694 2922 1657 -340 26 -258 C ATOM 1332 C PRO B 164 -12.556 -1.372 9.417 1.00 17.22 C ANISOU 1332 C PRO B 164 1845 2851 1848 -225 5 -231 C ATOM 1333 O PRO B 164 -12.130 -1.483 8.264 1.00 17.61 O ANISOU 1333 O PRO B 164 1837 2951 1905 -207 30 -312 O ATOM 1334 CB PRO B 164 -12.315 0.967 10.302 1.00 18.30 C ANISOU 1334 CB PRO B 164 1983 3101 1870 -530 147 -282 C ATOM 1335 CG PRO B 164 -11.241 1.625 9.501 1.00 24.74 C ANISOU 1335 CG PRO B 164 2708 4073 2621 -625 200 -379 C ATOM 1336 CD PRO B 164 -9.964 0.895 9.796 1.00 21.92 C ANISOU 1336 CD PRO B 164 2177 3946 2205 -530 128 -457 C ATOM 1337 N LEU B 165 -13.634 -2.010 9.865 1.00 15.40 N ANISOU 1337 N LEU B 165 1727 2448 1678 -179 -30 -134 N ATOM 1338 CA LEU B 165 -14.537 -2.673 8.938 1.00 12.98 C ANISOU 1338 CA LEU B 165 1492 1979 1463 -119 -30 -118 C ATOM 1339 C LEU B 165 -15.344 -1.593 8.240 1.00 15.29 C ANISOU 1339 C LEU B 165 1834 2213 1763 -240 53 -119 C ATOM 1340 O LEU B 165 -16.222 -0.975 8.841 1.00 16.39 O ANISOU 1340 O LEU B 165 2030 2268 1929 -313 89 -79 O ATOM 1341 CB LEU B 165 -15.431 -3.651 9.697 1.00 17.72 C ANISOU 1341 CB LEU B 165 2193 2425 2114 -70 -86 -18 C ATOM 1342 CG LEU B 165 -16.573 -4.300 8.911 1.00 18.98 C ANISOU 1342 CG LEU B 165 2432 2414 2364 -49 -74 -9 C ATOM 1343 CD1 LEU B 165 -16.024 -4.991 7.680 1.00 22.45 C ANISOU 1343 CD1 LEU B 165 2816 2860 2854 53 -95 -105 C ATOM 1344 CD2 LEU B 165 -17.351 -5.280 9.799 1.00 14.98 C ANISOU 1344 CD2 LEU B 165 2033 1770 1889 -45 -120 90 C ATOM 1345 N VAL B 166 -15.020 -1.333 6.980 1.00 15.13 N ANISOU 1345 N VAL B 166 1784 2246 1719 -268 77 -169 N ATOM 1346 CA VAL B 166 -15.711 -0.343 6.160 1.00 14.43 C ANISOU 1346 CA VAL B 166 1756 2095 1634 -379 112 -129 C ATOM 1347 C VAL B 166 -16.685 -1.088 5.268 1.00 16.94 C ANISOU 1347 C VAL B 166 2119 2319 2000 -329 75 -107 C ATOM 1348 O VAL B 166 -16.311 -2.079 4.632 1.00 18.29 O ANISOU 1348 O VAL B 166 2251 2545 2155 -266 60 -179 O ATOM 1349 CB VAL B 166 -14.708 0.474 5.326 1.00 13.51 C ANISOU 1349 CB VAL B 166 1597 2127 1408 -503 156 -172 C ATOM 1350 CG1 VAL B 166 -15.441 1.443 4.406 1.00 15.96 C ANISOU 1350 CG1 VAL B 166 2002 2344 1717 -621 151 -77 C ATOM 1351 CG2 VAL B 166 -13.751 1.210 6.242 1.00 16.96 C ANISOU 1351 CG2 VAL B 166 1977 2671 1796 -575 199 -216 C ATOM 1352 N LEU B 167 -17.939 -0.634 5.242 1.00 13.52 N ANISOU 1352 N LEU B 167 1747 1749 1643 -355 61 -35 N ATOM 1353 CA LEU B 167 -18.998 -1.280 4.473 1.00 15.11 C ANISOU 1353 CA LEU B 167 1974 1878 1887 -325 17 -18 C ATOM 1354 C LEU B 167 -19.413 -0.427 3.280 1.00 13.05 C ANISOU 1354 C LEU B 167 1741 1624 1594 -411 -25 50 C ATOM 1355 O LEU B 167 -19.548 0.792 3.397 1.00 15.34 O ANISOU 1355 O LEU B 167 2057 1852 1918 -467 -34 122 O ATOM 1356 CB LEU B 167 -20.226 -1.540 5.358 1.00 14.19 C ANISOU 1356 CB LEU B 167 1879 1629 1885 -290 15 3 C ATOM 1357 CG LEU B 167 -20.021 -2.496 6.544 1.00 15.55 C ANISOU 1357 CG LEU B 167 2062 1782 2063 -243 34 -17 C ATOM 1358 CD1 LEU B 167 -21.308 -2.585 7.368 1.00 15.18 C ANISOU 1358 CD1 LEU B 167 2033 1641 2093 -276 58 -7 C ATOM 1359 CD2 LEU B 167 -19.596 -3.869 6.058 1.00 17.62 C ANISOU 1359 CD2 LEU B 167 2334 2046 2316 -168 1 -56 C ATOM 1360 N SER B 168 -19.642 -1.074 2.129 1.00 12.48 N ANISOU 1360 N SER B 168 1668 1618 1457 -429 -61 29 N ATOM 1361 CA SER B 168 -20.207 -0.365 0.992 1.00 14.70 C ANISOU 1361 CA SER B 168 1984 1917 1683 -523 -138 130 C ATOM 1362 C SER B 168 -21.607 0.105 1.377 1.00 16.54 C ANISOU 1362 C SER B 168 2222 1984 2079 -467 -210 212 C ATOM 1363 O SER B 168 -22.208 -0.425 2.315 1.00 18.51 O ANISOU 1363 O SER B 168 2439 2150 2445 -385 -176 153 O ATOM 1364 CB SER B 168 -20.231 -1.267 -0.243 1.00 19.13 C ANISOU 1364 CB SER B 168 2530 2620 2118 -575 -156 61 C ATOM 1365 OG SER B 168 -20.817 -2.508 0.072 1.00 25.93 O ANISOU 1365 OG SER B 168 3363 3422 3069 -480 -142 -40 O ATOM 1366 N PRO B 169 -22.124 1.141 0.714 1.00 16.11 N ANISOU 1366 N PRO B 169 2200 1878 2042 -516 -313 349 N ATOM 1367 CA PRO B 169 -23.426 1.695 1.140 1.00 17.43 C ANISOU 1367 CA PRO B 169 2330 1878 2416 -430 -389 397 C ATOM 1368 C PRO B 169 -24.537 0.666 1.250 1.00 17.11 C ANISOU 1368 C PRO B 169 2211 1846 2444 -363 -401 312 C ATOM 1369 O PRO B 169 -25.324 0.710 2.202 1.00 18.55 O ANISOU 1369 O PRO B 169 2327 1928 2792 -292 -368 247 O ATOM 1370 CB PRO B 169 -23.731 2.738 0.053 1.00 18.87 C ANISOU 1370 CB PRO B 169 2566 2020 2582 -489 -549 585 C ATOM 1371 CG PRO B 169 -22.373 3.180 -0.432 1.00 21.63 C ANISOU 1371 CG PRO B 169 3012 2468 2738 -638 -504 641 C ATOM 1372 CD PRO B 169 -21.496 1.942 -0.352 1.00 18.73 C ANISOU 1372 CD PRO B 169 2605 2291 2220 -659 -369 470 C ATOM 1373 N GLU B 170 -24.649 -0.255 0.288 1.00 17.05 N ANISOU 1373 N GLU B 170 2201 1970 2306 -411 -436 287 N ATOM 1374 CA GLU B 170 -25.712 -1.244 0.377 1.00 16.47 C ANISOU 1374 CA GLU B 170 2059 1902 2297 -380 -439 194 C ATOM 1375 C GLU B 170 -25.551 -2.124 1.613 1.00 20.12 C ANISOU 1375 C GLU B 170 2522 2303 2820 -341 -302 72 C ATOM 1376 O GLU B 170 -26.550 -2.524 2.222 1.00 21.74 O ANISOU 1376 O GLU B 170 2671 2457 3134 -325 -280 10 O ATOM 1377 CB GLU B 170 -25.765 -2.074 -0.912 1.00 21.30 C ANISOU 1377 CB GLU B 170 2675 2674 2746 -467 -488 161 C ATOM 1378 CG GLU B 170 -25.061 -3.416 -0.865 1.00 33.86 C ANISOU 1378 CG GLU B 170 4292 4314 4261 -487 -369 3 C ATOM 1379 CD GLU B 170 -23.546 -3.279 -0.904 1.00 31.95 C ANISOU 1379 CD GLU B 170 4097 4132 3912 -503 -294 -16 C ATOM 1380 OE1 GLU B 170 -23.057 -2.182 -1.249 1.00 36.25 O ANISOU 1380 OE1 GLU B 170 4670 4721 4381 -556 -333 98 O ATOM 1381 OE2 GLU B 170 -22.842 -4.264 -0.588 1.00 26.63 O ANISOU 1381 OE2 GLU B 170 3427 3452 3240 -466 -203 -147 O ATOM 1382 N ALA B 171 -24.313 -2.414 2.016 1.00 17.40 N ANISOU 1382 N ALA B 171 2234 1976 2401 -339 -218 43 N ATOM 1383 CA ALA B 171 -24.088 -3.227 3.205 1.00 15.23 C ANISOU 1383 CA ALA B 171 1980 1640 2168 -305 -127 -24 C ATOM 1384 C ALA B 171 -24.299 -2.430 4.486 1.00 17.12 C ANISOU 1384 C ALA B 171 2201 1808 2496 -292 -80 -7 C ATOM 1385 O ALA B 171 -24.759 -2.987 5.490 1.00 18.44 O ANISOU 1385 O ALA B 171 2369 1933 2706 -307 -23 -49 O ATOM 1386 CB ALA B 171 -22.677 -3.818 3.175 1.00 15.85 C ANISOU 1386 CB ALA B 171 2096 1770 2155 -282 -87 -64 C ATOM 1387 N ALA B 172 -23.971 -1.136 4.474 1.00 14.62 N ANISOU 1387 N ALA B 172 1875 1480 2201 -292 -96 45 N ATOM 1388 CA ALA B 172 -24.269 -0.284 5.623 1.00 15.40 C ANISOU 1388 CA ALA B 172 1938 1507 2406 -291 -40 15 C ATOM 1389 C ALA B 172 -25.770 -0.224 5.892 1.00 15.42 C ANISOU 1389 C ALA B 172 1849 1452 2558 -276 -47 -46 C ATOM 1390 O ALA B 172 -26.202 -0.241 7.049 1.00 16.21 O ANISOU 1390 O ALA B 172 1906 1540 2712 -307 45 -137 O ATOM 1391 CB ALA B 172 -23.703 1.116 5.390 1.00 15.64 C ANISOU 1391 CB ALA B 172 1985 1495 2463 -302 -64 72 C ATOM 1392 N ARG B 173 -26.584 -0.159 4.833 1.00 17.84 N ANISOU 1392 N ARG B 173 2108 1752 2919 -246 -155 -9 N ATOM 1393 CA ARG B 173 -28.034 -0.197 5.014 1.00 16.92 C ANISOU 1393 CA ARG B 173 1862 1614 2952 -225 -172 -93 C ATOM 1394 C ARG B 173 -28.472 -1.518 5.632 1.00 16.78 C ANISOU 1394 C ARG B 173 1843 1653 2879 -302 -76 -188 C ATOM 1395 O ARG B 173 -29.282 -1.545 6.568 1.00 16.79 O ANISOU 1395 O ARG B 173 1758 1658 2964 -344 10 -303 O ATOM 1396 CB ARG B 173 -28.743 0.006 3.670 1.00 18.81 C ANISOU 1396 CB ARG B 173 2047 1873 3229 -184 -340 -17 C ATOM 1397 CG ARG B 173 -28.534 1.371 3.066 1.00 18.17 C ANISOU 1397 CG ARG B 173 1979 1699 3225 -122 -468 115 C ATOM 1398 CD ARG B 173 -29.552 1.646 1.974 1.00 23.22 C ANISOU 1398 CD ARG B 173 2531 2352 3941 -69 -667 197 C ATOM 1399 NE ARG B 173 -29.508 0.638 0.915 1.00 23.49 N ANISOU 1399 NE ARG B 173 2605 2553 3768 -154 -723 235 N ATOM 1400 CZ ARG B 173 -28.754 0.751 -0.176 1.00 25.45 C ANISOU 1400 CZ ARG B 173 2966 2877 3826 -226 -808 377 C ATOM 1401 NH1 ARG B 173 -28.766 -0.199 -1.106 1.00 28.52 N ANISOU 1401 NH1 ARG B 173 3370 3438 4028 -319 -836 360 N ATOM 1402 NH2 ARG B 173 -27.990 1.821 -0.346 1.00 21.96 N ANISOU 1402 NH2 ARG B 173 2622 2351 3373 -232 -853 519 N ATOM 1403 N GLU B 174 -27.959 -2.631 5.096 1.00 15.76 N ANISOU 1403 N GLU B 174 1809 1565 2614 -337 -84 -153 N ATOM 1404 CA GLU B 174 -28.324 -3.947 5.601 1.00 16.15 C ANISOU 1404 CA GLU B 174 1896 1617 2623 -420 -11 -217 C ATOM 1405 C GLU B 174 -27.902 -4.113 7.052 1.00 16.41 C ANISOU 1405 C GLU B 174 1990 1625 2619 -475 99 -225 C ATOM 1406 O GLU B 174 -28.650 -4.668 7.865 1.00 18.19 O ANISOU 1406 O GLU B 174 2205 1858 2850 -583 178 -287 O ATOM 1407 CB GLU B 174 -27.689 -5.024 4.723 1.00 17.62 C ANISOU 1407 CB GLU B 174 2179 1809 2708 -425 -45 -195 C ATOM 1408 CG GLU B 174 -28.340 -5.060 3.350 1.00 16.91 C ANISOU 1408 CG GLU B 174 2021 1791 2613 -432 -142 -214 C ATOM 1409 CD GLU B 174 -27.451 -5.568 2.227 1.00 22.32 C ANISOU 1409 CD GLU B 174 2774 2528 3179 -430 -180 -210 C ATOM 1410 OE1 GLU B 174 -26.239 -5.801 2.426 1.00 18.99 O ANISOU 1410 OE1 GLU B 174 2432 2082 2702 -394 -139 -198 O ATOM 1411 OE2 GLU B 174 -27.988 -5.712 1.104 1.00 19.89 O ANISOU 1411 OE2 GLU B 174 2417 2314 2827 -475 -255 -236 O ATOM 1412 N TRP B 175 -26.702 -3.635 7.380 1.00 16.27 N ANISOU 1412 N TRP B 175 2035 1606 2542 -430 104 -163 N ATOM 1413 CA TRP B 175 -26.151 -3.790 8.723 1.00 16.69 C ANISOU 1413 CA TRP B 175 2149 1670 2522 -490 179 -151 C ATOM 1414 C TRP B 175 -27.065 -3.187 9.787 1.00 17.37 C ANISOU 1414 C TRP B 175 2146 1794 2660 -585 278 -253 C ATOM 1415 O TRP B 175 -27.215 -3.748 10.877 1.00 17.56 O ANISOU 1415 O TRP B 175 2218 1857 2598 -714 355 -264 O ATOM 1416 CB TRP B 175 -24.775 -3.131 8.744 1.00 15.60 C ANISOU 1416 CB TRP B 175 2043 1560 2324 -425 156 -95 C ATOM 1417 CG TRP B 175 -24.033 -3.088 10.035 1.00 13.47 C ANISOU 1417 CG TRP B 175 1816 1342 1959 -480 205 -76 C ATOM 1418 CD1 TRP B 175 -23.880 -1.998 10.852 1.00 14.19 C ANISOU 1418 CD1 TRP B 175 1857 1486 2046 -531 270 -132 C ATOM 1419 CD2 TRP B 175 -23.241 -4.134 10.613 1.00 16.07 C ANISOU 1419 CD2 TRP B 175 2244 1680 2182 -486 172 8 C ATOM 1420 NE1 TRP B 175 -23.072 -2.319 11.928 1.00 16.15 N ANISOU 1420 NE1 TRP B 175 2162 1817 2155 -594 285 -90 N ATOM 1421 CE2 TRP B 175 -22.675 -3.624 11.806 1.00 18.35 C ANISOU 1421 CE2 TRP B 175 2534 2064 2375 -556 209 16 C ATOM 1422 CE3 TRP B 175 -22.979 -5.464 10.256 1.00 15.08 C ANISOU 1422 CE3 TRP B 175 2204 1475 2050 -437 105 72 C ATOM 1423 CZ2 TRP B 175 -21.856 -4.391 12.632 1.00 17.71 C ANISOU 1423 CZ2 TRP B 175 2535 2021 2173 -573 152 120 C ATOM 1424 CZ3 TRP B 175 -22.181 -6.229 11.083 1.00 17.12 C ANISOU 1424 CZ3 TRP B 175 2550 1724 2231 -431 50 171 C ATOM 1425 CH2 TRP B 175 -21.625 -5.692 12.261 1.00 17.90 C ANISOU 1425 CH2 TRP B 175 2647 1938 2216 -497 61 211 C ATOM 1426 N MET B 176 -27.684 -2.047 9.492 1.00 15.27 N ANISOU 1426 N MET B 176 1750 1517 2536 -533 275 -335 N ATOM 1427 CA MET B 176 -28.464 -1.352 10.510 1.00 15.36 C ANISOU 1427 CA MET B 176 1640 1566 2631 -606 386 -491 C ATOM 1428 C MET B 176 -29.852 -1.937 10.736 1.00 19.37 C ANISOU 1428 C MET B 176 2042 2127 3190 -704 448 -614 C ATOM 1429 O MET B 176 -30.501 -1.553 11.717 1.00 20.07 O ANISOU 1429 O MET B 176 2029 2293 3302 -791 568 -771 O ATOM 1430 CB MET B 176 -28.589 0.121 10.147 1.00 18.49 C ANISOU 1430 CB MET B 176 1926 1885 3214 -490 351 -550 C ATOM 1431 CG MET B 176 -27.268 0.877 10.299 1.00 17.24 C ANISOU 1431 CG MET B 176 1858 1696 2996 -466 345 -481 C ATOM 1432 SD MET B 176 -27.483 2.635 10.053 1.00 18.70 S ANISOU 1432 SD MET B 176 1944 1731 3432 -366 317 -557 S ATOM 1433 CE MET B 176 -27.830 2.671 8.290 1.00 16.85 C ANISOU 1433 CE MET B 176 1717 1405 3279 -229 111 -386 C ATOM 1434 N ARG B 177 -30.313 -2.852 9.882 1.00 19.79 N ANISOU 1434 N ARG B 177 2114 2167 3236 -700 379 -566 N ATOM 1435 CA ARG B 177 -31.684 -3.340 9.987 1.00 18.44 C ANISOU 1435 CA ARG B 177 1816 2066 3126 -807 436 -704 C ATOM 1436 C ARG B 177 -31.856 -4.226 11.216 1.00 26.24 C ANISOU 1436 C ARG B 177 2914 3139 3916 -974 553 -701 C ATOM 1437 O ARG B 177 -31.087 -5.169 11.441 1.00 24.22 O ANISOU 1437 O ARG B 177 2851 2838 3513 -1037 535 -554 O ATOM 1438 CB ARG B 177 -32.074 -4.092 8.712 1.00 22.42 C ANISOU 1438 CB ARG B 177 2325 2550 3644 -767 323 -653 C ATOM 1439 CG ARG B 177 -32.195 -3.156 7.523 1.00 27.46 C ANISOU 1439 CG ARG B 177 2855 3161 4416 -581 170 -623 C ATOM 1440 CD ARG B 177 -32.519 -3.854 6.205 1.00 27.33 C ANISOU 1440 CD ARG B 177 2842 3172 4371 -568 50 -576 C ATOM 1441 NE ARG B 177 -32.475 -2.869 5.129 1.00 31.49 N ANISOU 1441 NE ARG B 177 3300 3684 4979 -414 -118 -495 N ATOM 1442 CZ ARG B 177 -32.031 -3.105 3.899 1.00 35.94 C ANISOU 1442 CZ ARG B 177 3941 4270 5447 -385 -241 -382 C ATOM 1443 NH1 ARG B 177 -31.598 -4.313 3.567 1.00 32.21 N ANISOU 1443 NH1 ARG B 177 3592 3818 4827 -475 -203 -377 N ATOM 1444 NH2 ARG B 177 -32.027 -2.128 2.999 1.00 37.15 N ANISOU 1444 NH2 ARG B 177 4048 4416 5650 -279 -403 -278 N ATOM 1445 N GLN B 178 -32.884 -3.928 12.009 1.00 25.56 N ANISOU 1445 N GLN B 178 2704 3170 3837 -1045 662 -867 N ATOM 1446 CA GLN B 178 -33.090 -4.676 13.239 1.00 25.15 C ANISOU 1446 CA GLN B 178 2761 3218 3579 -1232 769 -869 C ATOM 1447 C GLN B 178 -33.625 -6.074 12.983 1.00 28.16 C ANISOU 1447 C GLN B 178 3236 3587 3875 -1348 756 -801 C ATOM 1448 O GLN B 178 -33.488 -6.944 13.849 1.00 33.70 O ANISOU 1448 O GLN B 178 4098 4310 4396 -1508 797 -717 O ATOM 1449 CB GLN B 178 -34.035 -3.916 14.174 1.00 30.68 C ANISOU 1449 CB GLN B 178 3303 4059 4295 -1291 907 -1111 C ATOM 1450 CG GLN B 178 -33.464 -2.607 14.715 1.00 34.83 C ANISOU 1450 CG GLN B 178 3768 4586 4880 -1216 948 -1206 C ATOM 1451 CD GLN B 178 -32.019 -2.721 15.188 1.00 41.07 C ANISOU 1451 CD GLN B 178 4750 5350 5505 -1247 913 -1019 C ATOM 1452 OE1 GLN B 178 -31.162 -1.923 14.799 1.00 43.75 O ANISOU 1452 OE1 GLN B 178 5080 5604 5938 -1122 859 -977 O ATOM 1453 NE2 GLN B 178 -31.744 -3.710 16.034 1.00 41.11 N ANISOU 1453 NE2 GLN B 178 4926 5425 5267 -1420 931 -906 N ATOM 1454 N GLU B 179 -34.212 -6.317 11.813 1.00 24.98 N ANISOU 1454 N GLU B 179 2745 3147 3598 -1284 688 -831 N ATOM 1455 CA GLU B 179 -34.827 -7.609 11.559 1.00 32.57 C ANISOU 1455 CA GLU B 179 3782 4101 4491 -1407 691 -806 C ATOM 1456 C GLU B 179 -33.806 -8.719 11.331 1.00 34.48 C ANISOU 1456 C GLU B 179 4267 4181 4652 -1425 615 -601 C ATOM 1457 O GLU B 179 -34.160 -9.894 11.473 1.00 42.06 O ANISOU 1457 O GLU B 179 5342 5101 5538 -1555 633 -560 O ATOM 1458 CB GLU B 179 -35.779 -7.509 10.361 1.00 37.29 C ANISOU 1458 CB GLU B 179 4196 4736 5238 -1342 634 -921 C ATOM 1459 CG GLU B 179 -35.182 -6.841 9.116 1.00 44.91 C ANISOU 1459 CG GLU B 179 5098 5623 6343 -1158 491 -876 C ATOM 1460 CD GLU B 179 -35.393 -5.332 9.078 1.00 49.54 C ANISOU 1460 CD GLU B 179 5470 6248 7104 -1012 465 -981 C ATOM 1461 OE1 GLU B 179 -35.708 -4.734 10.130 1.00 50.80 O ANISOU 1461 OE1 GLU B 179 5561 6473 7269 -1035 576 -1092 O ATOM 1462 OE2 GLU B 179 -35.252 -4.743 7.983 1.00 54.69 O ANISOU 1462 OE2 GLU B 179 6023 6859 7897 -875 323 -960 O ATOM 1463 N ILE B 180 -32.547 -8.396 10.991 1.00 29.72 N ANISOU 1463 N ILE B 180 3745 3472 4074 -1295 532 -486 N ATOM 1464 CA ILE B 180 -31.609 -9.465 10.658 1.00 32.11 C ANISOU 1464 CA ILE B 180 4253 3606 4342 -1277 454 -332 C ATOM 1465 C ILE B 180 -30.976 -10.020 11.929 1.00 34.16 C ANISOU 1465 C ILE B 180 4690 3828 4463 -1372 470 -190 C ATOM 1466 O ILE B 180 -30.886 -9.346 12.962 1.00 37.90 O ANISOU 1466 O ILE B 180 5137 4417 4845 -1429 529 -198 O ATOM 1467 CB ILE B 180 -30.538 -8.998 9.653 1.00 31.01 C ANISOU 1467 CB ILE B 180 4124 3379 4280 -1102 360 -293 C ATOM 1468 CG1 ILE B 180 -29.628 -7.967 10.291 1.00 30.30 C ANISOU 1468 CG1 ILE B 180 4029 3321 4160 -1040 369 -247 C ATOM 1469 CG2 ILE B 180 -31.172 -8.449 8.384 1.00 30.33 C ANISOU 1469 CG2 ILE B 180 3870 3346 4308 -1034 319 -413 C ATOM 1470 CD1 ILE B 180 -28.260 -7.940 9.704 1.00 29.91 C ANISOU 1470 CD1 ILE B 180 4066 3185 4113 -878 275 -150 C ATOM 1471 N SER B 181 -30.537 -11.271 11.841 1.00 33.44 N ANISOU 1471 N SER B 181 4777 3569 4360 -1389 407 -65 N ATOM 1472 CA SER B 181 -29.968 -11.982 12.969 1.00 36.95 C ANISOU 1472 CA SER B 181 5407 3947 4685 -1477 381 106 C ATOM 1473 C SER B 181 -28.480 -11.675 13.096 1.00 34.16 C ANISOU 1473 C SER B 181 5134 3520 4326 -1333 285 238 C ATOM 1474 O SER B 181 -27.859 -11.097 12.206 1.00 30.81 O ANISOU 1474 O SER B 181 4647 3064 3994 -1171 245 194 O ATOM 1475 CB SER B 181 -30.183 -13.482 12.809 1.00 38.28 C ANISOU 1475 CB SER B 181 5726 3931 4886 -1542 341 184 C ATOM 1476 OG SER B 181 -29.299 -14.004 11.829 1.00 36.55 O ANISOU 1476 OG SER B 181 5567 3509 4811 -1362 240 221 O ATOM 1477 N GLY B 182 -27.901 -12.080 14.227 1.00 36.83 N ANISOU 1477 N GLY B 182 5615 3844 4535 -1404 237 405 N ATOM 1478 CA GLY B 182 -26.460 -11.963 14.389 1.00 32.68 C ANISOU 1478 CA GLY B 182 5169 3248 3999 -1262 116 550 C ATOM 1479 C GLY B 182 -25.668 -12.690 13.313 1.00 34.54 C ANISOU 1479 C GLY B 182 5464 3249 4409 -1050 2 583 C ATOM 1480 O GLY B 182 -24.642 -12.189 12.840 1.00 28.50 O ANISOU 1480 O GLY B 182 4673 2462 3693 -878 -69 586 O ATOM 1481 N LYS B 183 -26.125 -13.880 12.912 1.00 33.65 N ANISOU 1481 N LYS B 183 5425 2966 4396 -1064 -10 582 N ATOM 1482 CA LYS B 183 -25.421 -14.615 11.866 1.00 31.54 C ANISOU 1482 CA LYS B 183 5188 2480 4314 -863 -94 554 C ATOM 1483 C LYS B 183 -25.522 -13.882 10.539 1.00 24.21 C ANISOU 1483 C LYS B 183 4117 1618 3465 -772 -46 354 C ATOM 1484 O LYS B 183 -24.548 -13.823 9.775 1.00 26.20 O ANISOU 1484 O LYS B 183 4352 1796 3806 -582 -116 306 O ATOM 1485 CB LYS B 183 -25.986 -16.034 11.722 1.00 40.11 C ANISOU 1485 CB LYS B 183 6373 3367 5501 -930 -91 567 C ATOM 1486 CG LYS B 183 -25.846 -16.965 12.947 1.00 56.85 C ANISOU 1486 CG LYS B 183 8672 5372 7558 -1020 -161 789 C ATOM 1487 CD LYS B 183 -26.522 -16.485 14.148 1.00 64.61 C ANISOU 1487 CD LYS B 183 9674 6563 8312 -1253 -102 863 C ATOM 1488 CE LYS B 183 -27.942 -16.476 13.941 1.00 69.45 C ANISOU 1488 CE LYS B 183 10217 7279 8892 -1448 39 717 C ATOM 1489 NZ LYS B 183 -28.615 -15.576 14.821 1.00 67.37 N ANISOU 1489 NZ LYS B 183 9882 7290 8427 -1631 137 675 N ATOM 1490 N GLU B 184 -26.698 -13.312 10.248 1.00 26.61 N ANISOU 1490 N GLU B 184 4304 2075 3732 -903 61 228 N ATOM 1491 CA GLU B 184 -26.847 -12.513 9.038 1.00 23.77 C ANISOU 1491 CA GLU B 184 3807 1805 3420 -832 88 65 C ATOM 1492 C GLU B 184 -25.926 -11.309 9.069 1.00 20.61 C ANISOU 1492 C GLU B 184 3324 1532 2976 -697 62 83 C ATOM 1493 O GLU B 184 -25.331 -10.951 8.049 1.00 21.60 O ANISOU 1493 O GLU B 184 3361 1703 3141 -545 28 5 O ATOM 1494 CB GLU B 184 -28.301 -12.082 8.854 1.00 26.41 C ANISOU 1494 CB GLU B 184 4001 2301 3734 -971 176 -52 C ATOM 1495 CG GLU B 184 -29.211 -13.251 8.480 1.00 30.85 C ANISOU 1495 CG GLU B 184 4590 2790 4340 -1073 192 -110 C ATOM 1496 CD GLU B 184 -30.650 -12.849 8.278 1.00 39.86 C ANISOU 1496 CD GLU B 184 5577 4110 5459 -1196 265 -236 C ATOM 1497 OE1 GLU B 184 -31.265 -12.365 9.246 1.00 38.81 O ANISOU 1497 OE1 GLU B 184 5392 4103 5253 -1296 334 -229 O ATOM 1498 OE2 GLU B 184 -31.167 -13.026 7.152 1.00 42.93 O ANISOU 1498 OE2 GLU B 184 5887 4528 5896 -1193 252 -357 O ATOM 1499 N ALA B 185 -25.782 -10.674 10.241 1.00 21.59 N ANISOU 1499 N ALA B 185 3453 1754 2998 -759 84 172 N ATOM 1500 CA ALA B 185 -24.866 -9.545 10.348 1.00 20.09 C ANISOU 1500 CA ALA B 185 3167 1702 2766 -635 63 178 C ATOM 1501 C ALA B 185 -23.438 -9.964 10.016 1.00 16.09 C ANISOU 1501 C ALA B 185 2695 1126 2293 -444 -45 230 C ATOM 1502 O ALA B 185 -22.678 -9.196 9.410 1.00 18.09 O ANISOU 1502 O ALA B 185 2841 1483 2550 -321 -58 170 O ATOM 1503 CB ALA B 185 -24.934 -8.951 11.758 1.00 22.50 C ANISOU 1503 CB ALA B 185 3482 2125 2942 -768 112 243 C ATOM 1504 N SER B 186 -23.048 -11.169 10.434 1.00 23.38 N ANISOU 1504 N SER B 186 3763 1871 3251 -423 -128 337 N ATOM 1505 CA SER B 186 -21.719 -11.671 10.110 1.00 19.63 C ANISOU 1505 CA SER B 186 3287 1313 2858 -210 -243 353 C ATOM 1506 C SER B 186 -21.555 -11.855 8.607 1.00 19.05 C ANISOU 1506 C SER B 186 3122 1217 2899 -93 -221 165 C ATOM 1507 O SER B 186 -20.481 -11.586 8.056 1.00 20.77 O ANISOU 1507 O SER B 186 3234 1513 3144 63 -253 86 O ATOM 1508 CB SER B 186 -21.471 -12.993 10.830 1.00 25.29 C ANISOU 1508 CB SER B 186 4187 1785 3636 -199 -362 516 C ATOM 1509 OG SER B 186 -21.426 -12.794 12.236 1.00 28.06 O ANISOU 1509 OG SER B 186 4624 2206 3831 -322 -405 712 O ATOM 1510 N GLU B 187 -22.602 -12.335 7.941 1.00 21.36 N ANISOU 1510 N GLU B 187 3445 1430 3242 -193 -160 77 N ATOM 1511 CA GLU B 187 -22.552 -12.465 6.487 1.00 21.12 C ANISOU 1511 CA GLU B 187 3323 1427 3275 -131 -131 -115 C ATOM 1512 C GLU B 187 -22.477 -11.103 5.808 1.00 17.30 C ANISOU 1512 C GLU B 187 2687 1199 2689 -130 -87 -179 C ATOM 1513 O GLU B 187 -21.774 -10.951 4.806 1.00 17.83 O ANISOU 1513 O GLU B 187 2665 1356 2753 -49 -87 -299 O ATOM 1514 CB GLU B 187 -23.762 -13.243 5.983 1.00 19.70 C ANISOU 1514 CB GLU B 187 3202 1136 3146 -272 -80 -198 C ATOM 1515 CG GLU B 187 -23.753 -13.432 4.476 1.00 21.42 C ANISOU 1515 CG GLU B 187 3328 1415 3397 -245 -51 -410 C ATOM 1516 CD GLU B 187 -24.808 -14.408 4.009 1.00 27.41 C ANISOU 1516 CD GLU B 187 4149 2046 4219 -388 -10 -515 C ATOM 1517 OE1 GLU B 187 -24.858 -14.697 2.798 1.00 26.87 O ANISOU 1517 OE1 GLU B 187 4014 2033 4164 -398 18 -709 O ATOM 1518 OE2 GLU B 187 -25.582 -14.893 4.856 1.00 31.81 O ANISOU 1518 OE2 GLU B 187 4823 2467 4795 -518 3 -416 O ATOM 1519 N ILE B 188 -23.190 -10.099 6.331 1.00 16.94 N ANISOU 1519 N ILE B 188 2610 1265 2563 -230 -49 -110 N ATOM 1520 CA ILE B 188 -23.063 -8.741 5.795 1.00 18.16 C ANISOU 1520 CA ILE B 188 2646 1606 2649 -219 -32 -134 C ATOM 1521 C ILE B 188 -21.648 -8.217 5.980 1.00 18.34 C ANISOU 1521 C ILE B 188 2629 1711 2629 -115 -57 -112 C ATOM 1522 O ILE B 188 -21.083 -7.566 5.092 1.00 18.57 O ANISOU 1522 O ILE B 188 2578 1866 2610 -90 -53 -172 O ATOM 1523 CB ILE B 188 -24.083 -7.804 6.456 1.00 17.14 C ANISOU 1523 CB ILE B 188 2481 1533 2500 -321 9 -88 C ATOM 1524 CG1 ILE B 188 -25.493 -8.239 6.067 1.00 26.25 C ANISOU 1524 CG1 ILE B 188 3619 2657 3698 -424 32 -149 C ATOM 1525 CG2 ILE B 188 -23.798 -6.338 6.052 1.00 17.03 C ANISOU 1525 CG2 ILE B 188 2371 1648 2451 -291 6 -85 C ATOM 1526 CD1 ILE B 188 -26.552 -7.528 6.803 1.00 30.48 C ANISOU 1526 CD1 ILE B 188 4090 3243 4248 -517 82 -150 C ATOM 1527 N ALA B 189 -21.048 -8.480 7.141 1.00 18.41 N ANISOU 1527 N ALA B 189 2689 1674 2634 -78 -89 -22 N ATOM 1528 CA ALA B 189 -19.685 -8.015 7.360 1.00 18.23 C ANISOU 1528 CA ALA B 189 2600 1757 2568 16 -122 -17 C ATOM 1529 C ALA B 189 -18.717 -8.663 6.382 1.00 18.20 C ANISOU 1529 C ALA B 189 2533 1758 2623 144 -151 -142 C ATOM 1530 O ALA B 189 -17.761 -8.020 5.934 1.00 23.77 O ANISOU 1530 O ALA B 189 3131 2625 3276 179 -136 -214 O ATOM 1531 CB ALA B 189 -19.267 -8.286 8.803 1.00 18.18 C ANISOU 1531 CB ALA B 189 2657 1720 2532 24 -180 114 C ATOM 1532 N ALA B 190 -18.969 -9.919 6.005 1.00 18.78 N ANISOU 1532 N ALA B 190 2663 1662 2810 194 -175 -200 N ATOM 1533 CA ALA B 190 -18.085 -10.624 5.089 1.00 19.71 C ANISOU 1533 CA ALA B 190 2701 1772 3017 321 -187 -375 C ATOM 1534 C ALA B 190 -18.351 -10.275 3.636 1.00 23.61 C ANISOU 1534 C ALA B 190 3118 2410 3443 236 -104 -540 C ATOM 1535 O ALA B 190 -17.457 -10.437 2.799 1.00 27.76 O ANISOU 1535 O ALA B 190 3531 3043 3975 295 -76 -720 O ATOM 1536 CB ALA B 190 -18.231 -12.135 5.262 1.00 23.01 C ANISOU 1536 CB ALA B 190 3218 1909 3616 408 -247 -393 C ATOM 1537 N ASER B 191 -19.556 -9.811 3.317 0.62 19.46 N ANISOU 1537 N ASER B 191 2637 1911 2845 92 -69 -491 N ATOM 1538 N BSER B 191 -19.559 -9.812 3.323 0.38 19.80 N ANISOU 1538 N BSER B 191 2681 1954 2889 92 -69 -490 N ATOM 1539 CA ASER B 191 -19.935 -9.541 1.939 0.62 19.64 C ANISOU 1539 CA ASER B 191 2604 2077 2782 -9 -25 -609 C ATOM 1540 CA BSER B 191 -19.953 -9.541 1.949 0.38 19.86 C ANISOU 1540 CA BSER B 191 2633 2102 2809 -10 -26 -607 C ATOM 1541 C ASER B 191 -19.782 -8.083 1.548 0.62 18.05 C ANISOU 1541 C ASER B 191 2347 2084 2426 -95 -15 -540 C ATOM 1542 C BSER B 191 -19.758 -8.089 1.556 0.38 18.68 C ANISOU 1542 C BSER B 191 2426 2164 2506 -93 -15 -541 C ATOM 1543 O ASER B 191 -19.574 -7.791 0.364 0.62 24.05 O ANISOU 1543 O ASER B 191 3052 3014 3073 -177 9 -631 O ATOM 1544 O BSER B 191 -19.508 -7.803 0.378 0.38 23.28 O ANISOU 1544 O BSER B 191 2951 2917 2976 -172 10 -635 O ATOM 1545 CB ASER B 191 -21.384 -9.974 1.697 0.62 20.89 C ANISOU 1545 CB ASER B 191 2827 2147 2964 -115 -24 -602 C ATOM 1546 CB BSER B 191 -21.421 -9.914 1.743 0.38 20.68 C ANISOU 1546 CB BSER B 191 2802 2122 2935 -117 -25 -591 C ATOM 1547 OG ASER B 191 -21.624 -11.271 2.219 0.62 20.13 O ANISOU 1547 OG ASER B 191 2819 1815 3013 -73 -32 -630 O ATOM 1548 OG BSER B 191 -22.260 -9.013 2.446 0.38 21.90 O ANISOU 1548 OG BSER B 191 2977 2286 3058 -179 -40 -430 O ATOM 1549 N GLY B 192 -19.884 -7.167 2.503 1.00 17.37 N ANISOU 1549 N GLY B 192 2284 1987 2329 -99 -31 -385 N ATOM 1550 CA GLY B 192 -19.829 -5.756 2.199 1.00 20.03 C ANISOU 1550 CA GLY B 192 2594 2456 2561 -182 -29 -308 C ATOM 1551 C GLY B 192 -18.546 -5.053 2.582 1.00 20.99 C ANISOU 1551 C GLY B 192 2667 2681 2626 -164 -6 -302 C ATOM 1552 O GLY B 192 -18.461 -3.830 2.429 1.00 18.63 O ANISOU 1552 O GLY B 192 2368 2457 2253 -252 0 -228 O ATOM 1553 N ACYS B 193 -17.557 -5.792 3.080 0.38 19.84 N ANISOU 1553 N ACYS B 193 2478 2534 2527 -54 -4 -379 N ATOM 1554 N BCYS B 193 -17.532 -5.780 3.065 0.62 19.78 N ANISOU 1554 N BCYS B 193 2468 2530 2517 -55 -3 -381 N ATOM 1555 CA ACYS B 193 -16.277 -5.185 3.422 0.38 19.40 C ANISOU 1555 CA ACYS B 193 2341 2618 2413 -42 14 -403 C ATOM 1556 CA BCYS B 193 -16.285 -5.134 3.470 0.62 18.97 C ANISOU 1556 CA BCYS B 193 2288 2562 2357 -45 14 -396 C ATOM 1557 C ACYS B 193 -15.619 -4.618 2.168 0.38 20.40 C ANISOU 1557 C ACYS B 193 2393 2952 2405 -156 71 -505 C ATOM 1558 C BCYS B 193 -15.509 -4.661 2.243 0.62 20.03 C ANISOU 1558 C BCYS B 193 2338 2909 2364 -144 70 -513 C ATOM 1559 O ACYS B 193 -15.601 -5.262 1.115 0.38 21.39 O ANISOU 1559 O ACYS B 193 2482 3140 2504 -175 96 -640 O ATOM 1560 O BCYS B 193 -15.281 -5.420 1.299 0.62 24.60 O ANISOU 1560 O BCYS B 193 2861 3554 2934 -135 97 -670 O ATOM 1561 CB ACYS B 193 -15.370 -6.219 4.087 0.38 19.99 C ANISOU 1561 CB ACYS B 193 2354 2655 2585 125 -29 -474 C ATOM 1562 CB BCYS B 193 -15.421 -6.080 4.310 0.62 18.24 C ANISOU 1562 CB BCYS B 193 2145 2427 2360 119 -34 -442 C ATOM 1563 SG ACYS B 193 -15.375 -7.826 3.261 0.38 25.32 S ANISOU 1563 SG ACYS B 193 3005 3221 3393 244 -40 -652 S ATOM 1564 SG BCYS B 193 -13.876 -5.304 4.970 0.62 25.37 S ANISOU 1564 SG BCYS B 193 2913 3538 3190 132 -33 -472 S ATOM 1565 N VAL B 194 -15.098 -3.400 2.272 1.00 19.75 N ANISOU 1565 N VAL B 194 2296 2985 2223 -266 100 -449 N ATOM 1566 CA VAL B 194 -14.432 -2.739 1.153 1.00 21.38 C ANISOU 1566 CA VAL B 194 2455 3402 2265 -432 159 -516 C ATOM 1567 C VAL B 194 -12.961 -3.134 1.177 1.00 22.44 C ANISOU 1567 C VAL B 194 2421 3727 2376 -386 213 -713 C ATOM 1568 O VAL B 194 -12.284 -2.878 2.180 1.00 21.96 O ANISOU 1568 O VAL B 194 2304 3686 2353 -326 202 -703 O ATOM 1569 CB VAL B 194 -14.605 -1.219 1.240 1.00 19.71 C ANISOU 1569 CB VAL B 194 2329 3184 1976 -592 161 -353 C ATOM 1570 CG1 VAL B 194 -13.826 -0.533 0.127 1.00 22.97 C ANISOU 1570 CG1 VAL B 194 2717 3819 2191 -810 221 -395 C ATOM 1571 CG2 VAL B 194 -16.078 -0.867 1.167 1.00 19.75 C ANISOU 1571 CG2 VAL B 194 2458 2999 2048 -599 89 -187 C ATOM 1572 N PRO B 195 -12.422 -3.728 0.119 1.00 21.68 N ANISOU 1572 N PRO B 195 2220 3800 2218 -421 273 -917 N ATOM 1573 CA PRO B 195 -11.029 -4.190 0.160 1.00 25.69 C ANISOU 1573 CA PRO B 195 2518 4494 2748 -344 324 -1155 C ATOM 1574 C PRO B 195 -10.033 -3.038 0.198 1.00 31.88 C ANISOU 1574 C PRO B 195 3225 5513 3376 -523 393 -1169 C ATOM 1575 O PRO B 195 -10.315 -1.913 -0.216 1.00 27.66 O ANISOU 1575 O PRO B 195 2807 5022 2680 -757 425 -1028 O ATOM 1576 CB PRO B 195 -10.872 -4.996 -1.138 1.00 31.39 C ANISOU 1576 CB PRO B 195 3146 5354 3427 -387 400 -1405 C ATOM 1577 CG PRO B 195 -12.248 -5.141 -1.702 1.00 27.07 C ANISOU 1577 CG PRO B 195 2774 4661 2849 -455 364 -1277 C ATOM 1578 CD PRO B 195 -13.069 -4.023 -1.175 1.00 22.48 C ANISOU 1578 CD PRO B 195 2366 3952 2222 -539 298 -968 C ATOM 1579 N ALA B 196 -8.821 -3.364 0.669 1.00 34.11 N ANISOU 1579 N ALA B 196 3298 5943 3717 -413 407 -1350 N ATOM 1580 CA ALA B 196 -7.783 -2.352 0.850 1.00 33.44 C ANISOU 1580 CA ALA B 196 3120 6073 3511 -581 456 -1378 C ATOM 1581 C ALA B 196 -7.366 -1.689 -0.457 1.00 33.29 C ANISOU 1581 C ALA B 196 3110 6204 3335 -877 511 -1411 C ATOM 1582 O ALA B 196 -7.013 -0.503 -0.458 1.00 33.43 O ANISOU 1582 O ALA B 196 3189 6273 3241 -1096 525 -1313 O ATOM 1583 CB ALA B 196 -6.560 -2.967 1.525 1.00 39.36 C ANISOU 1583 CB ALA B 196 3637 6935 4384 -386 404 -1563 C ATOM 1584 N ASN B 197 -7.373 -2.422 -1.576 1.00 30.92 N ANISOU 1584 N ASN B 197 2747 5973 3029 -905 543 -1558 N ATOM 1585 CA ASN B 197 -6.955 -1.772 -2.814 1.00 35.08 C ANISOU 1585 CA ASN B 197 3265 6675 3389 -1217 597 -1584 C ATOM 1586 C ASN B 197 -7.933 -0.699 -3.274 1.00 26.51 C ANISOU 1586 C ASN B 197 2426 5488 2161 -1440 587 -1298 C ATOM 1587 O ASN B 197 -7.650 -0.018 -4.263 1.00 32.22 O ANISOU 1587 O ASN B 197 3179 6334 2731 -1721 610 -1274 O ATOM 1588 CB ASN B 197 -6.744 -2.804 -3.927 1.00 40.23 C ANISOU 1588 CB ASN B 197 3775 7450 4059 -1224 642 -1822 C ATOM 1589 CG ASN B 197 -7.896 -3.788 -4.046 1.00 42.91 C ANISOU 1589 CG ASN B 197 4199 7611 4494 -1048 625 -1804 C ATOM 1590 OD1 ASN B 197 -9.016 -3.514 -3.610 1.00 43.71 O ANISOU 1590 OD1 ASN B 197 4499 7527 4584 -1002 583 -1581 O ATOM 1591 ND2 ASN B 197 -7.622 -4.945 -4.641 1.00 49.29 N ANISOU 1591 ND2 ASN B 197 4857 8468 5402 -959 652 -2063 N ATOM 1592 N GLN B 198 -9.056 -0.518 -2.577 1.00 30.67 N ANISOU 1592 N GLN B 198 3130 5792 2730 -1328 536 -1090 N ATOM 1593 CA GLN B 198 -9.967 0.578 -2.869 1.00 25.53 C ANISOU 1593 CA GLN B 198 2715 5013 1974 -1506 488 -815 C ATOM 1594 C GLN B 198 -9.606 1.849 -2.107 1.00 27.76 C ANISOU 1594 C GLN B 198 3081 5220 2245 -1600 472 -691 C ATOM 1595 O GLN B 198 -10.278 2.869 -2.272 1.00 26.37 O ANISOU 1595 O GLN B 198 3108 4898 2015 -1729 415 -468 O ATOM 1596 CB GLN B 198 -11.409 0.161 -2.562 1.00 25.94 C ANISOU 1596 CB GLN B 198 2912 4868 2076 -1356 427 -678 C ATOM 1597 CG GLN B 198 -11.856 -1.101 -3.334 1.00 27.61 C ANISOU 1597 CG GLN B 198 3066 5126 2298 -1272 432 -823 C ATOM 1598 CD GLN B 198 -11.709 -0.993 -4.849 1.00 39.63 C ANISOU 1598 CD GLN B 198 4567 6818 3673 -1510 457 -844 C ATOM 1599 OE1 GLN B 198 -10.962 -1.751 -5.468 1.00 37.47 O ANISOU 1599 OE1 GLN B 198 4116 6715 3407 -1525 534 -1083 O ATOM 1600 NE2 GLN B 198 -12.437 -0.065 -5.451 1.00 39.00 N ANISOU 1600 NE2 GLN B 198 4664 6690 3466 -1700 378 -599 N ATOM 1601 N PHE B 199 -8.545 1.825 -1.308 1.00 25.83 N ANISOU 1601 N PHE B 199 2688 5068 2058 -1536 504 -837 N ATOM 1602 CA PHE B 199 -8.166 2.975 -0.502 1.00 25.24 C ANISOU 1602 CA PHE B 199 2687 4927 1976 -1620 496 -757 C ATOM 1603 C PHE B 199 -6.848 3.568 -0.988 1.00 28.99 C ANISOU 1603 C PHE B 199 3080 5606 2329 -1835 528 -899 C ATOM 1604 O PHE B 199 -6.017 2.882 -1.592 1.00 31.89 O ANISOU 1604 O PHE B 199 3257 6194 2666 -1859 562 -1110 O ATOM 1605 CB PHE B 199 -8.063 2.599 0.980 1.00 27.73 C ANISOU 1605 CB PHE B 199 2913 5195 2427 -1399 490 -795 C ATOM 1606 CG PHE B 199 -9.370 2.167 1.573 1.00 24.03 C ANISOU 1606 CG PHE B 199 2543 4528 2061 -1231 465 -655 C ATOM 1607 CD1 PHE B 199 -10.258 3.102 2.074 1.00 22.90 C ANISOU 1607 CD1 PHE B 199 2576 4161 1963 -1291 445 -454 C ATOM 1608 CD2 PHE B 199 -9.734 0.829 1.581 1.00 29.19 C ANISOU 1608 CD2 PHE B 199 3123 5169 2799 -1006 437 -735 C ATOM 1609 CE1 PHE B 199 -11.477 2.706 2.603 1.00 21.63 C ANISOU 1609 CE1 PHE B 199 2506 3751 1963 -1101 359 -340 C ATOM 1610 CE2 PHE B 199 -10.958 0.423 2.108 1.00 25.45 C ANISOU 1610 CE2 PHE B 199 2771 4422 2475 -834 344 -592 C ATOM 1611 CZ PHE B 199 -11.823 1.364 2.622 1.00 24.18 C ANISOU 1611 CZ PHE B 199 2768 4055 2365 -888 311 -403 C ATOM 1612 N SER B 200 -6.691 4.869 -0.756 1.00 25.88 N ANISOU 1612 N SER B 200 2840 5129 1864 -2000 523 -795 N ATOM 1613 CA SER B 200 -5.431 5.575 -0.918 1.00 28.14 C ANISOU 1613 CA SER B 200 3075 5593 2025 -2206 561 -932 C ATOM 1614 C SER B 200 -4.978 6.045 0.457 1.00 29.64 C ANISOU 1614 C SER B 200 3238 5743 2280 -2128 571 -966 C ATOM 1615 O SER B 200 -5.797 6.208 1.366 1.00 25.57 O ANISOU 1615 O SER B 200 2816 5017 1883 -1988 550 -830 O ATOM 1616 CB SER B 200 -5.564 6.769 -1.873 1.00 30.04 C ANISOU 1616 CB SER B 200 3539 5778 2097 -2493 553 -787 C ATOM 1617 OG SER B 200 -5.921 6.354 -3.189 1.00 35.84 O ANISOU 1617 OG SER B 200 4289 6591 2737 -2605 532 -760 O ATOM 1618 N TRP B 201 -3.668 6.241 0.617 1.00 29.34 N ANISOU 1618 N TRP B 201 3061 5905 2181 -2201 614 -1141 N ATOM 1619 CA TRP B 201 -3.150 6.649 1.919 1.00 29.08 C ANISOU 1619 CA TRP B 201 2983 5875 2193 -2137 622 -1188 C ATOM 1620 C TRP B 201 -1.828 7.373 1.742 1.00 37.36 C ANISOU 1620 C TRP B 201 3972 7105 3116 -2329 686 -1322 C ATOM 1621 O TRP B 201 -1.080 7.107 0.798 1.00 38.52 O ANISOU 1621 O TRP B 201 4012 7443 3180 -2429 722 -1446 O ATOM 1622 CB TRP B 201 -2.970 5.462 2.867 1.00 31.07 C ANISOU 1622 CB TRP B 201 3021 6210 2573 -1850 578 -1282 C ATOM 1623 CG TRP B 201 -2.130 4.331 2.342 1.00 38.00 C ANISOU 1623 CG TRP B 201 3659 7322 3459 -1741 579 -1483 C ATOM 1624 CD1 TRP B 201 -0.763 4.258 2.326 1.00 40.51 C ANISOU 1624 CD1 TRP B 201 3793 7884 3716 -1769 608 -1690 C ATOM 1625 CD2 TRP B 201 -2.602 3.091 1.800 1.00 35.32 C ANISOU 1625 CD2 TRP B 201 3230 6996 3195 -1579 550 -1536 C ATOM 1626 NE1 TRP B 201 -0.359 3.052 1.806 1.00 42.62 N ANISOU 1626 NE1 TRP B 201 3861 8308 4024 -1624 595 -1880 N ATOM 1627 CE2 TRP B 201 -1.468 2.324 1.463 1.00 34.57 C ANISOU 1627 CE2 TRP B 201 2901 7144 3092 -1508 561 -1793 C ATOM 1628 CE3 TRP B 201 -3.873 2.565 1.541 1.00 29.27 C ANISOU 1628 CE3 TRP B 201 2557 6065 2499 -1494 520 -1412 C ATOM 1629 CZ2 TRP B 201 -1.569 1.057 0.906 1.00 36.71 C ANISOU 1629 CZ2 TRP B 201 3033 7474 3440 -1347 539 -1946 C ATOM 1630 CZ3 TRP B 201 -3.967 1.311 0.996 1.00 34.34 C ANISOU 1630 CZ3 TRP B 201 3072 6760 3217 -1327 515 -1530 C ATOM 1631 CH2 TRP B 201 -2.824 0.570 0.680 1.00 39.34 C ANISOU 1631 CH2 TRP B 201 3474 7622 3852 -1261 518 -1809 C ATOM 1632 N HIS B 202 -1.554 8.290 2.670 1.00 33.26 N ANISOU 1632 N HIS B 202 3520 6538 2580 -2393 709 -1316 N ATOM 1633 CA HIS B 202 -0.401 9.172 2.576 1.00 34.80 C ANISOU 1633 CA HIS B 202 3697 6883 2641 -2613 780 -1432 C ATOM 1634 C HIS B 202 -0.069 9.710 3.953 1.00 34.65 C ANISOU 1634 C HIS B 202 3659 6851 2655 -2576 795 -1470 C ATOM 1635 O HIS B 202 -0.962 9.837 4.803 1.00 32.63 O ANISOU 1635 O HIS B 202 3502 6403 2492 -2470 765 -1364 O ATOM 1636 CB HIS B 202 -0.667 10.334 1.614 1.00 36.38 C ANISOU 1636 CB HIS B 202 4154 6987 2682 -2924 819 -1333 C ATOM 1637 CG HIS B 202 -1.880 11.138 1.954 1.00 38.81 C ANISOU 1637 CG HIS B 202 4733 6985 3027 -2949 797 -1131 C ATOM 1638 ND1 HIS B 202 -1.971 11.918 3.089 1.00 44.60 N ANISOU 1638 ND1 HIS B 202 5533 7574 3838 -2927 837 -1107 N ATOM 1639 CD2 HIS B 202 -3.066 11.268 1.313 1.00 38.18 C ANISOU 1639 CD2 HIS B 202 4835 6656 3018 -2919 753 -888 C ATOM 1640 CE1 HIS B 202 -3.154 12.505 3.123 1.00 37.01 C ANISOU 1640 CE1 HIS B 202 4770 6273 3017 -2880 820 -872 C ATOM 1641 NE2 HIS B 202 -3.837 12.129 2.055 1.00 42.77 N ANISOU 1641 NE2 HIS B 202 5573 6932 3744 -2868 760 -726 N ATOM 1642 N PRO B 203 1.185 10.064 4.198 1.00 37.01 N ANISOU 1642 N PRO B 203 3833 7364 2868 -2681 846 -1630 N ATOM 1643 CA PRO B 203 1.538 10.658 5.491 1.00 37.28 C ANISOU 1643 CA PRO B 203 3849 7407 2907 -2681 868 -1674 C ATOM 1644 C PRO B 203 0.917 12.038 5.672 1.00 37.41 C ANISOU 1644 C PRO B 203 4142 7193 2880 -2884 932 -1580 C ATOM 1645 O PRO B 203 0.745 12.805 4.724 1.00 38.68 O ANISOU 1645 O PRO B 203 4495 7271 2929 -3116 979 -1528 O ATOM 1646 CB PRO B 203 3.072 10.741 5.439 1.00 40.35 C ANISOU 1646 CB PRO B 203 4042 8108 3182 -2788 918 -1884 C ATOM 1647 CG PRO B 203 3.424 10.667 4.010 1.00 42.06 C ANISOU 1647 CG PRO B 203 4257 8422 3303 -2945 955 -1934 C ATOM 1648 CD PRO B 203 2.355 9.876 3.320 1.00 39.82 C ANISOU 1648 CD PRO B 203 4034 7987 3110 -2807 892 -1802 C ATOM 1649 N VAL B 204 0.594 12.358 6.927 1.00 28.06 N ANISOU 1649 N VAL B 204 4078 4283 2299 -1708 -193 254 N ATOM 1650 CA VAL B 204 0.098 13.683 7.279 1.00 25.39 C ANISOU 1650 CA VAL B 204 3546 3992 2109 -1690 -254 338 C ATOM 1651 C VAL B 204 1.004 14.270 8.353 1.00 22.97 C ANISOU 1651 C VAL B 204 3156 3606 1963 -1515 -274 264 C ATOM 1652 O VAL B 204 1.912 13.596 8.846 1.00 28.50 O ANISOU 1652 O VAL B 204 3948 4239 2642 -1407 -254 164 O ATOM 1653 CB VAL B 204 -1.366 13.650 7.765 1.00 24.21 C ANISOU 1653 CB VAL B 204 3405 3885 1910 -1780 -295 401 C ATOM 1654 CG1 VAL B 204 -2.298 13.291 6.597 1.00 25.92 C ANISOU 1654 CG1 VAL B 204 3652 4228 1969 -1974 -280 488 C ATOM 1655 CG2 VAL B 204 -1.525 12.685 8.934 1.00 24.94 C ANISOU 1655 CG2 VAL B 204 3649 3884 1941 -1718 -300 305 C ATOM 1656 N SER B 205 0.743 15.519 8.727 1.00 22.58 N ANISOU 1656 N SER B 205 2930 3576 2075 -1490 -303 314 N ATOM 1657 CA SER B 205 1.521 16.180 9.778 1.00 23.45 C ANISOU 1657 CA SER B 205 2941 3631 2339 -1351 -317 228 C ATOM 1658 C SER B 205 1.441 15.397 11.082 1.00 29.37 C ANISOU 1658 C SER B 205 3800 4335 3025 -1273 -347 136 C ATOM 1659 O SER B 205 0.390 14.866 11.445 1.00 22.68 O ANISOU 1659 O SER B 205 3042 3489 2088 -1332 -368 166 O ATOM 1660 CB SER B 205 1.008 17.601 9.995 1.00 27.47 C ANISOU 1660 CB SER B 205 3255 4155 3028 -1365 -318 297 C ATOM 1661 OG SER B 205 1.514 18.156 11.204 1.00 32.27 O ANISOU 1661 OG SER B 205 3782 4717 3764 -1261 -328 191 O ATOM 1662 N ARG B 206 2.558 15.335 11.801 1.00 22.06 N ANISOU 1662 N ARG B 206 2857 3383 2143 -1139 -347 29 N ATOM 1663 CA ARG B 206 2.531 14.655 13.087 1.00 21.97 C ANISOU 1663 CA ARG B 206 2924 3352 2072 -1049 -373 -44 C ATOM 1664 C ARG B 206 1.625 15.352 14.093 1.00 21.66 C ANISOU 1664 C ARG B 206 2799 3320 2108 -1063 -418 -41 C ATOM 1665 O ARG B 206 1.314 14.757 15.131 1.00 24.34 O ANISOU 1665 O ARG B 206 3214 3652 2382 -1009 -443 -80 O ATOM 1666 CB ARG B 206 3.964 14.521 13.625 1.00 26.00 C ANISOU 1666 CB ARG B 206 3402 3870 2607 -899 -365 -145 C ATOM 1667 CG ARG B 206 4.786 13.599 12.735 1.00 40.44 C ANISOU 1667 CG ARG B 206 5350 5673 4342 -875 -307 -141 C ATOM 1668 CD ARG B 206 6.009 13.014 13.415 1.00 49.65 C ANISOU 1668 CD ARG B 206 6536 6849 5478 -712 -290 -214 C ATOM 1669 NE ARG B 206 7.234 13.736 13.072 1.00 59.13 N ANISOU 1669 NE ARG B 206 7602 8083 6783 -655 -282 -256 N ATOM 1670 CZ ARG B 206 7.736 13.871 11.843 1.00 67.32 C ANISOU 1670 CZ ARG B 206 8638 9097 7844 -699 -240 -226 C ATOM 1671 NH1 ARG B 206 8.858 14.556 11.670 1.00 67.06 N ANISOU 1671 NH1 ARG B 206 8473 9092 7914 -638 -233 -271 N ATOM 1672 NH2 ARG B 206 7.140 13.323 10.788 1.00 69.55 N ANISOU 1672 NH2 ARG B 206 9046 9337 8042 -811 -201 -158 N ATOM 1673 N ALA B 207 1.179 16.581 13.804 1.00 21.43 N ANISOU 1673 N ALA B 207 2619 3303 2221 -1129 -414 15 N ATOM 1674 CA ALA B 207 0.321 17.319 14.728 1.00 27.38 C ANISOU 1674 CA ALA B 207 3286 4052 3066 -1146 -436 21 C ATOM 1675 C ALA B 207 -0.998 16.610 15.026 1.00 23.90 C ANISOU 1675 C ALA B 207 2968 3604 2509 -1211 -466 86 C ATOM 1676 O ALA B 207 -1.600 16.859 16.077 1.00 22.90 O ANISOU 1676 O ALA B 207 2817 3466 2420 -1194 -491 65 O ATOM 1677 CB ALA B 207 0.025 18.712 14.180 1.00 27.53 C ANISOU 1677 CB ALA B 207 3127 4070 3264 -1210 -394 99 C ATOM 1678 N VAL B 208 -1.478 15.746 14.134 1.00 22.25 N ANISOU 1678 N VAL B 208 2889 3406 2159 -1293 -459 158 N ATOM 1679 CA VAL B 208 -2.754 15.095 14.395 1.00 20.85 C ANISOU 1679 CA VAL B 208 2821 3227 1873 -1368 -481 213 C ATOM 1680 C VAL B 208 -2.668 14.195 15.620 1.00 22.14 C ANISOU 1680 C VAL B 208 3103 3349 1959 -1271 -499 122 C ATOM 1681 O VAL B 208 -3.689 13.912 16.255 1.00 20.51 O ANISOU 1681 O VAL B 208 2953 3129 1710 -1301 -523 147 O ATOM 1682 CB VAL B 208 -3.235 14.311 13.160 1.00 23.02 C ANISOU 1682 CB VAL B 208 3208 3539 2001 -1497 -457 286 C ATOM 1683 CG1 VAL B 208 -2.270 13.196 12.824 1.00 21.56 C ANISOU 1683 CG1 VAL B 208 3169 3321 1704 -1450 -416 204 C ATOM 1684 CG2 VAL B 208 -4.631 13.749 13.422 1.00 21.48 C ANISOU 1684 CG2 VAL B 208 3104 3355 1702 -1593 -477 342 C ATOM 1685 N GLY B 209 -1.461 13.762 15.996 1.00 20.95 N ANISOU 1685 N GLY B 209 2983 3186 1792 -1146 -486 26 N ATOM 1686 CA GLY B 209 -1.344 12.856 17.124 1.00 21.81 C ANISOU 1686 CA GLY B 209 3196 3274 1817 -1038 -492 -38 C ATOM 1687 C GLY B 209 -1.964 13.422 18.383 1.00 21.70 C ANISOU 1687 C GLY B 209 3107 3271 1868 -1006 -541 -59 C ATOM 1688 O GLY B 209 -2.580 12.691 19.166 1.00 21.54 O ANISOU 1688 O GLY B 209 3190 3230 1765 -978 -550 -60 O ATOM 1689 N ASN B 210 -1.819 14.728 18.588 1.00 20.53 N ANISOU 1689 N ASN B 210 2779 3149 1873 -1014 -558 -79 N ATOM 1690 CA ASN B 210 -2.368 15.406 19.756 1.00 20.31 C ANISOU 1690 CA ASN B 210 2664 3129 1924 -999 -587 -112 C ATOM 1691 C ASN B 210 -3.819 15.804 19.498 1.00 19.95 C ANISOU 1691 C ASN B 210 2614 3051 1913 -1123 -591 -1 C ATOM 1692 O ASN B 210 -4.099 16.556 18.560 1.00 20.23 O ANISOU 1692 O ASN B 210 2566 3087 2035 -1212 -565 83 O ATOM 1693 CB ASN B 210 -1.527 16.634 20.076 1.00 20.52 C ANISOU 1693 CB ASN B 210 2498 3189 2108 -965 -576 -199 C ATOM 1694 CG ASN B 210 -1.794 17.167 21.470 1.00 20.53 C ANISOU 1694 CG ASN B 210 2418 3214 2167 -931 -596 -281 C ATOM 1695 OD1 ASN B 210 -2.947 17.318 21.873 1.00 23.42 O ANISOU 1695 OD1 ASN B 210 2804 3544 2550 -986 -605 -228 O ATOM 1696 ND2 ASN B 210 -0.728 17.390 22.237 1.00 25.48 N ANISOU 1696 ND2 ASN B 210 2955 3915 2811 -841 -603 -412 N ATOM 1697 N VAL B 211 -4.736 15.325 20.344 1.00 21.16 N ANISOU 1697 N VAL B 211 2849 3186 2005 -1121 -617 11 N ATOM 1698 CA VAL B 211 -6.157 15.560 20.109 1.00 20.67 C ANISOU 1698 CA VAL B 211 2795 3102 1956 -1237 -622 127 C ATOM 1699 C VAL B 211 -6.561 17.013 20.292 1.00 23.59 C ANISOU 1699 C VAL B 211 2986 3464 2513 -1278 -602 163 C ATOM 1700 O VAL B 211 -7.671 17.386 19.885 1.00 28.23 O ANISOU 1700 O VAL B 211 3546 4045 3134 -1375 -591 290 O ATOM 1701 CB VAL B 211 -7.014 14.654 21.016 1.00 20.68 C ANISOU 1701 CB VAL B 211 2932 3078 1849 -1218 -649 127 C ATOM 1702 CG1 VAL B 211 -6.741 13.196 20.686 1.00 26.43 C ANISOU 1702 CG1 VAL B 211 3845 3793 2405 -1193 -634 112 C ATOM 1703 CG2 VAL B 211 -6.750 14.940 22.496 1.00 23.41 C ANISOU 1703 CG2 VAL B 211 3225 3429 2241 -1110 -672 26 C ATOM 1704 N LYS B 212 -5.687 17.844 20.874 1.00 21.98 N ANISOU 1704 N LYS B 212 2654 3266 2433 -1212 -583 55 N ATOM 1705 CA LYS B 212 -5.973 19.267 20.981 1.00 22.51 C ANISOU 1705 CA LYS B 212 2548 3304 2700 -1257 -528 77 C ATOM 1706 C LYS B 212 -5.988 19.944 19.620 1.00 29.75 C ANISOU 1706 C LYS B 212 3377 4220 3707 -1329 -474 199 C ATOM 1707 O LYS B 212 -6.636 20.984 19.470 1.00 31.63 O ANISOU 1707 O LYS B 212 3499 4422 4096 -1368 -408 289 O ATOM 1708 CB LYS B 212 -4.954 19.948 21.903 1.00 27.82 C ANISOU 1708 CB LYS B 212 3104 3992 3475 -1186 -506 -93 C ATOM 1709 CG LYS B 212 -3.610 20.236 21.262 1.00 30.33 C ANISOU 1709 CG LYS B 212 3347 4339 3838 -1152 -479 -162 C ATOM 1710 CD LYS B 212 -2.573 20.608 22.321 1.00 41.93 C ANISOU 1710 CD LYS B 212 4723 5860 5350 -1080 -476 -353 C ATOM 1711 CE LYS B 212 -1.204 20.829 21.702 1.00 52.33 C ANISOU 1711 CE LYS B 212 5966 7215 6702 -1044 -452 -424 C ATOM 1712 NZ LYS B 212 -1.270 21.729 20.517 1.00 56.79 N ANISOU 1712 NZ LYS B 212 6439 7718 7420 -1116 -375 -328 N ATOM 1713 N ASN B 213 -5.313 19.363 18.629 1.00 24.06 N ANISOU 1713 N ASN B 213 2712 3533 2895 -1327 -486 212 N ATOM 1714 CA ASN B 213 -5.184 19.967 17.310 1.00 20.19 C ANISOU 1714 CA ASN B 213 2134 3061 2477 -1385 -435 322 C ATOM 1715 C ASN B 213 -6.390 19.595 16.463 1.00 26.84 C ANISOU 1715 C ASN B 213 3037 3939 3221 -1472 -444 496 C ATOM 1716 O ASN B 213 -6.752 18.418 16.372 1.00 26.51 O ANISOU 1716 O ASN B 213 3147 3928 2997 -1518 -499 501 O ATOM 1717 CB ASN B 213 -3.894 19.505 16.641 1.00 21.82 C ANISOU 1717 CB ASN B 213 2376 3293 2623 -1339 -440 250 C ATOM 1718 CG ASN B 213 -2.670 20.045 17.341 1.00 27.11 C ANISOU 1718 CG ASN B 213 2952 3949 3400 -1247 -420 89 C ATOM 1719 OD1 ASN B 213 -2.677 21.188 17.803 1.00 30.65 O ANISOU 1719 OD1 ASN B 213 3253 4366 4026 -1250 -365 58 O ATOM 1720 ND2 ASN B 213 -1.621 19.230 17.443 1.00 24.72 N ANISOU 1720 ND2 ASN B 213 2729 3673 2990 -1168 -453 -15 N ATOM 1721 N GLN B 214 -7.006 20.597 15.838 1.00 24.12 N ANISOU 1721 N GLN B 214 2594 3584 2987 -1434 -369 614 N ATOM 1722 CA GLN B 214 -8.278 20.324 15.180 1.00 28.10 C ANISOU 1722 CA GLN B 214 3152 4139 3385 -1454 -382 752 C ATOM 1723 C GLN B 214 -8.423 20.974 13.801 1.00 35.69 C ANISOU 1723 C GLN B 214 4031 5152 4378 -1430 -334 870 C ATOM 1724 O GLN B 214 -9.546 21.053 13.285 1.00 34.68 O ANISOU 1724 O GLN B 214 3900 5080 4198 -1425 -344 978 O ATOM 1725 CB GLN B 214 -9.430 20.758 16.093 1.00 31.26 C ANISOU 1725 CB GLN B 214 3538 4490 3849 -1413 -368 782 C ATOM 1726 CG GLN B 214 -9.596 19.884 17.343 1.00 32.74 C ANISOU 1726 CG GLN B 214 3837 4652 3953 -1443 -433 693 C ATOM 1727 CD GLN B 214 -10.027 18.465 17.014 1.00 36.27 C ANISOU 1727 CD GLN B 214 4448 5162 4172 -1522 -505 713 C ATOM 1728 OE1 GLN B 214 -10.648 18.224 15.983 1.00 33.66 O ANISOU 1728 OE1 GLN B 214 4136 4906 3745 -1553 -514 805 O ATOM 1729 NE2 GLN B 214 -9.689 17.514 17.890 1.00 27.53 N ANISOU 1729 NE2 GLN B 214 3457 4026 2976 -1550 -556 608 N ATOM 1730 N GLY B 215 -7.336 21.398 13.161 1.00 33.29 N ANISOU 1730 N GLY B 215 3655 4844 4148 -1416 -292 847 N ATOM 1731 CA GLY B 215 -7.463 22.074 11.876 1.00 43.94 C ANISOU 1731 CA GLY B 215 4923 6241 5533 -1385 -243 960 C ATOM 1732 C GLY B 215 -7.776 21.149 10.695 1.00 39.58 C ANISOU 1732 C GLY B 215 4446 5822 4770 -1458 -309 1029 C ATOM 1733 O GLY B 215 -7.553 19.942 10.715 1.00 35.05 O ANISOU 1733 O GLY B 215 4000 5291 4028 -1544 -371 969 O ATOM 1734 N ALA B 216 -8.283 21.747 9.608 1.00 40.94 N ANISOU 1734 N ALA B 216 4538 6064 4952 -1428 -286 1148 N ATOM 1735 CA ALA B 216 -8.500 20.988 8.376 1.00 27.06 C ANISOU 1735 CA ALA B 216 2822 4453 3007 -1504 -346 1198 C ATOM 1736 C ALA B 216 -7.195 20.543 7.726 1.00 31.16 C ANISOU 1736 C ALA B 216 3372 4989 3477 -1550 -336 1139 C ATOM 1737 O ALA B 216 -7.207 19.621 6.907 1.00 31.94 O ANISOU 1737 O ALA B 216 3546 5194 3396 -1642 -384 1129 O ATOM 1738 CB ALA B 216 -9.320 21.808 7.378 1.00 37.68 C ANISOU 1738 CB ALA B 216 4050 5886 4381 -1458 -331 1341 C ATOM 1739 N GLU B 217 -6.067 21.171 8.066 1.00 29.65 N ANISOU 1739 N GLU B 217 3123 4697 3448 -1495 -272 1085 N ATOM 1740 CA GLU B 217 -4.775 20.743 7.540 1.00 33.71 C ANISOU 1740 CA GLU B 217 3663 5219 3926 -1535 -263 1021 C ATOM 1741 C GLU B 217 -4.367 19.356 8.017 1.00 29.29 C ANISOU 1741 C GLU B 217 3263 4661 3204 -1635 -318 908 C ATOM 1742 O GLU B 217 -3.429 18.776 7.455 1.00 31.56 O ANISOU 1742 O GLU B 217 3603 4970 3418 -1689 -312 858 O ATOM 1743 CB GLU B 217 -3.683 21.743 7.930 1.00 44.74 C ANISOU 1743 CB GLU B 217 4945 6506 5548 -1453 -187 966 C ATOM 1744 CG GLU B 217 -3.560 22.945 7.007 1.00 59.99 C ANISOU 1744 CG GLU B 217 6742 8432 7618 -1373 -104 1059 C ATOM 1745 CD GLU B 217 -4.841 23.758 6.928 1.00 71.85 C ANISOU 1745 CD GLU B 217 8187 9939 9174 -1314 -75 1173 C ATOM 1746 OE1 GLU B 217 -5.560 23.649 5.910 1.00 73.96 O ANISOU 1746 OE1 GLU B 217 8448 10324 9328 -1330 -107 1289 O ATOM 1747 OE2 GLU B 217 -5.130 24.504 7.888 1.00 74.26 O ANISOU 1747 OE2 GLU B 217 8448 10138 9628 -1258 -20 1139 O ATOM 1748 N LEU B 218 -5.043 18.811 9.031 1.00 28.89 N ANISOU 1748 N LEU B 218 3300 4580 3098 -1659 -359 867 N ATOM 1749 CA LEU B 218 -4.608 17.550 9.615 1.00 26.63 C ANISOU 1749 CA LEU B 218 3173 4266 2680 -1741 -393 752 C ATOM 1750 C LEU B 218 -4.770 16.368 8.666 1.00 23.31 C ANISOU 1750 C LEU B 218 2895 3924 2038 -1850 -401 746 C ATOM 1751 O LEU B 218 -4.092 15.353 8.848 1.00 28.79 O ANISOU 1751 O LEU B 218 3737 4568 2635 -1874 -391 636 O ATOM 1752 CB LEU B 218 -5.369 17.287 10.912 1.00 26.81 C ANISOU 1752 CB LEU B 218 3253 4233 2700 -1732 -429 716 C ATOM 1753 CG LEU B 218 -5.062 18.249 12.064 1.00 28.32 C ANISOU 1753 CG LEU B 218 3328 4337 3094 -1639 -420 667 C ATOM 1754 CD1 LEU B 218 -5.874 17.883 13.287 1.00 30.63 C ANISOU 1754 CD1 LEU B 218 3691 4587 3358 -1635 -460 632 C ATOM 1755 CD2 LEU B 218 -3.576 18.256 12.386 1.00 29.38 C ANISOU 1755 CD2 LEU B 218 3459 4412 3292 -1538 -410 517 C ATOM 1756 N ILE B 219 -5.625 16.467 7.642 1.00 27.89 N ANISOU 1756 N ILE B 219 3438 4614 2545 -1871 -420 826 N ATOM 1757 CA ILE B 219 -5.709 15.393 6.658 1.00 26.27 C ANISOU 1757 CA ILE B 219 3340 4487 2155 -1982 -428 778 C ATOM 1758 C ILE B 219 -4.913 15.704 5.403 1.00 34.73 C ANISOU 1758 C ILE B 219 4346 5621 3228 -1988 -395 808 C ATOM 1759 O ILE B 219 -4.792 14.831 4.526 1.00 33.59 O ANISOU 1759 O ILE B 219 4285 5529 2947 -2084 -388 749 O ATOM 1760 CB ILE B 219 -7.169 15.071 6.267 1.00 24.39 C ANISOU 1760 CB ILE B 219 3089 4349 1830 -2043 -487 803 C ATOM 1761 CG1 ILE B 219 -7.825 16.273 5.591 1.00 29.44 C ANISOU 1761 CG1 ILE B 219 3543 5091 2550 -1977 -508 948 C ATOM 1762 CG2 ILE B 219 -7.974 14.611 7.487 1.00 30.17 C ANISOU 1762 CG2 ILE B 219 3899 5011 2553 -2047 -515 760 C ATOM 1763 CD1 ILE B 219 -9.183 15.952 4.988 1.00 33.02 C ANISOU 1763 CD1 ILE B 219 3961 5680 2907 -2057 -569 978 C ATOM 1764 N GLN B 220 -4.367 16.908 5.292 1.00 31.98 N ANISOU 1764 N GLN B 220 3850 5254 3046 -1890 -366 885 N ATOM 1765 CA GLN B 220 -3.616 17.285 4.106 1.00 39.80 C ANISOU 1765 CA GLN B 220 4769 6301 4054 -1883 -331 923 C ATOM 1766 C GLN B 220 -2.282 16.541 4.070 1.00 41.64 C ANISOU 1766 C GLN B 220 5111 6471 4237 -1931 -286 819 C ATOM 1767 O GLN B 220 -1.636 16.367 5.109 1.00 31.74 O ANISOU 1767 O GLN B 220 3905 5110 3045 -1916 -270 746 O ATOM 1768 CB GLN B 220 -3.382 18.797 4.084 1.00 35.33 C ANISOU 1768 CB GLN B 220 4016 5698 3709 -1752 -291 1020 C ATOM 1769 CG GLN B 220 -4.645 19.626 3.906 1.00 36.14 C ANISOU 1769 CG GLN B 220 4010 5857 3863 -1693 -309 1144 C ATOM 1770 CD GLN B 220 -5.372 19.346 2.585 1.00 49.81 C ANISOU 1770 CD GLN B 220 5720 7762 5443 -1758 -352 1215 C ATOM 1771 OE1 GLN B 220 -4.819 18.723 1.673 1.00 52.78 O ANISOU 1771 OE1 GLN B 220 6143 8209 5703 -1836 -354 1176 O ATOM 1772 NE2 GLN B 220 -6.612 19.812 2.482 1.00 53.95 N ANISOU 1772 NE2 GLN B 220 6167 8359 5973 -1732 -386 1313 N ATOM 1773 N PRO B 221 -1.830 16.118 2.895 1.00 42.01 N ANISOU 1773 N PRO B 221 5193 6585 4182 -1988 -262 806 N ATOM 1774 CA PRO B 221 -0.646 15.257 2.816 1.00 32.52 C ANISOU 1774 CA PRO B 221 4132 5317 2906 -2034 -203 704 C ATOM 1775 C PRO B 221 0.646 16.064 2.879 1.00 33.16 C ANISOU 1775 C PRO B 221 4111 5321 3169 -1909 -172 690 C ATOM 1776 O PRO B 221 0.664 17.274 2.652 1.00 36.34 O ANISOU 1776 O PRO B 221 4324 5758 3726 -1869 -164 798 O ATOM 1777 CB PRO B 221 -0.804 14.563 1.456 1.00 45.83 C ANISOU 1777 CB PRO B 221 5878 7100 4435 -2123 -195 678 C ATOM 1778 CG PRO B 221 -2.030 15.195 0.790 1.00 45.28 C ANISOU 1778 CG PRO B 221 5663 7173 4369 -2130 -262 781 C ATOM 1779 CD PRO B 221 -2.385 16.416 1.564 1.00 46.97 C ANISOU 1779 CD PRO B 221 5733 7356 4757 -2011 -284 887 C ATOM 1780 N VAL B 222 1.735 15.365 3.219 1.00 31.30 N ANISOU 1780 N VAL B 222 4001 4965 2927 -1818 -150 545 N ATOM 1781 CA VAL B 222 3.040 15.986 3.445 1.00 33.15 C ANISOU 1781 CA VAL B 222 4153 5110 3330 -1667 -132 488 C ATOM 1782 C VAL B 222 4.114 15.173 2.724 1.00 33.62 C ANISOU 1782 C VAL B 222 4334 5135 3305 -1655 -79 410 C ATOM 1783 O VAL B 222 4.177 13.947 2.862 1.00 35.85 O ANISOU 1783 O VAL B 222 4805 5371 3447 -1678 -53 326 O ATOM 1784 CB VAL B 222 3.374 16.113 4.949 1.00 37.07 C ANISOU 1784 CB VAL B 222 4646 5497 3940 -1529 -164 387 C ATOM 1785 CG1 VAL B 222 2.503 17.175 5.624 1.00 34.48 C ANISOU 1785 CG1 VAL B 222 4167 5188 3745 -1527 -196 460 C ATOM 1786 CG2 VAL B 222 3.229 14.788 5.664 1.00 42.60 C ANISOU 1786 CG2 VAL B 222 5548 6141 4498 -1520 -170 291 C ATOM 1787 N LEU B 223 4.956 15.855 1.958 1.00 31.94 N ANISOU 1787 N LEU B 223 4014 4935 3187 -1615 -48 442 N ATOM 1788 CA LEU B 223 6.083 15.207 1.292 1.00 36.10 C ANISOU 1788 CA LEU B 223 4640 5419 3660 -1587 8 372 C ATOM 1789 C LEU B 223 7.240 15.088 2.276 1.00 38.67 C ANISOU 1789 C LEU B 223 4986 5619 4089 -1414 10 254 C ATOM 1790 O LEU B 223 7.640 16.086 2.882 1.00 33.78 O ANISOU 1790 O LEU B 223 4214 4976 3646 -1314 -15 246 O ATOM 1791 CB LEU B 223 6.508 16.011 0.061 1.00 31.39 C ANISOU 1791 CB LEU B 223 3910 4894 3121 -1612 41 463 C ATOM 1792 CG LEU B 223 7.815 15.628 -0.640 1.00 40.69 C ANISOU 1792 CG LEU B 223 5150 6019 4292 -1561 101 401 C ATOM 1793 CD1 LEU B 223 7.629 14.394 -1.512 1.00 45.59 C ANISOU 1793 CD1 LEU B 223 5956 6676 4689 -1695 153 372 C ATOM 1794 CD2 LEU B 223 8.352 16.795 -1.460 1.00 35.84 C ANISOU 1794 CD2 LEU B 223 4351 5448 3819 -1527 123 489 C ATOM 1795 N GLU B 224 7.787 13.876 2.427 1.00 34.46 N ANISOU 1795 N GLU B 224 4633 5014 3446 -1380 53 165 N ATOM 1796 CA GLU B 224 8.681 13.562 3.543 1.00 36.19 C ANISOU 1796 CA GLU B 224 4883 5143 3724 -1215 52 70 C ATOM 1797 C GLU B 224 10.142 13.332 3.151 1.00 38.78 C ANISOU 1797 C GLU B 224 5230 5417 4086 -1112 110 22 C ATOM 1798 O GLU B 224 10.935 12.936 4.014 1.00 44.59 O ANISOU 1798 O GLU B 224 5996 6100 4847 -973 118 -45 O ATOM 1799 CB GLU B 224 8.164 12.327 4.287 1.00 39.20 C ANISOU 1799 CB GLU B 224 5447 5475 3970 -1219 68 22 C ATOM 1800 CG GLU B 224 6.736 12.444 4.797 1.00 44.99 C ANISOU 1800 CG GLU B 224 6177 6254 4665 -1312 11 61 C ATOM 1801 CD GLU B 224 6.677 12.991 6.205 1.00 53.40 C ANISOU 1801 CD GLU B 224 7146 7304 5839 -1196 -57 31 C ATOM 1802 OE1 GLU B 224 7.734 13.415 6.721 1.00 53.79 O ANISOU 1802 OE1 GLU B 224 7107 7333 5998 -1059 -66 -21 O ATOM 1803 OE2 GLU B 224 5.579 12.991 6.800 1.00 54.66 O ANISOU 1803 OE2 GLU B 224 7316 7483 5970 -1249 -100 54 O ATOM 1804 N VAL B 225 10.532 13.553 1.891 1.00 34.34 N ANISOU 1804 N VAL B 225 4646 4878 3522 -1171 153 62 N ATOM 1805 CA VAL B 225 11.932 13.325 1.537 1.00 27.46 C ANISOU 1805 CA VAL B 225 3796 3950 2689 -1068 213 18 C ATOM 1806 C VAL B 225 12.856 14.237 2.372 1.00 35.41 C ANISOU 1806 C VAL B 225 4633 4946 3876 -911 170 -23 C ATOM 1807 O VAL B 225 12.505 15.369 2.731 1.00 31.94 O ANISOU 1807 O VAL B 225 4025 4548 3564 -913 114 -4 O ATOM 1808 CB VAL B 225 12.177 13.521 0.032 1.00 32.76 C ANISOU 1808 CB VAL B 225 4456 4656 3336 -1159 264 71 C ATOM 1809 CG1 VAL B 225 11.395 12.476 -0.775 1.00 30.94 C ANISOU 1809 CG1 VAL B 225 4403 4449 2903 -1327 321 82 C ATOM 1810 CG2 VAL B 225 11.805 14.927 -0.396 1.00 32.99 C ANISOU 1810 CG2 VAL B 225 4277 4769 3490 -1198 216 157 C ATOM 1811 N LEU B 226 14.043 13.711 2.704 1.00 26.25 N ANISOU 1811 N LEU B 226 3516 3733 2723 -778 209 -82 N ATOM 1812 CA LEU B 226 15.073 14.497 3.386 1.00 28.36 C ANISOU 1812 CA LEU B 226 3620 4014 3141 -641 178 -134 C ATOM 1813 C LEU B 226 15.598 15.631 2.510 1.00 27.51 C ANISOU 1813 C LEU B 226 3355 3922 3174 -657 188 -109 C ATOM 1814 O LEU B 226 15.800 16.754 2.991 1.00 26.87 O ANISOU 1814 O LEU B 226 3090 3869 3249 -620 153 -137 O ATOM 1815 CB LEU B 226 16.229 13.588 3.803 1.00 27.06 C ANISOU 1815 CB LEU B 226 3536 3812 2932 -497 227 -179 C ATOM 1816 CG LEU B 226 17.503 14.254 4.332 1.00 28.01 C ANISOU 1816 CG LEU B 226 3492 3970 3182 -358 208 -235 C ATOM 1817 CD1 LEU B 226 17.181 15.017 5.600 1.00 26.37 C ANISOU 1817 CD1 LEU B 226 3135 3834 3051 -327 124 -291 C ATOM 1818 CD2 LEU B 226 18.583 13.211 4.593 1.00 27.36 C ANISOU 1818 CD2 LEU B 226 3502 3863 3031 -218 271 -245 C ATOM 1819 N PHE B 227 15.871 15.355 1.243 1.00 26.35 N ANISOU 1819 N PHE B 227 3276 3754 2980 -712 249 -62 N ATOM 1820 CA PHE B 227 16.483 16.341 0.356 1.00 26.43 C ANISOU 1820 CA PHE B 227 3146 3774 3120 -711 273 -30 C ATOM 1821 C PHE B 227 15.378 17.043 -0.429 1.00 30.11 C ANISOU 1821 C PHE B 227 3546 4299 3596 -848 263 70 C ATOM 1822 O PHE B 227 14.839 16.503 -1.403 1.00 26.60 O ANISOU 1822 O PHE B 227 3206 3884 3017 -961 292 132 O ATOM 1823 CB PHE B 227 17.514 15.675 -0.547 1.00 26.94 C ANISOU 1823 CB PHE B 227 3309 3792 3134 -677 350 -32 C ATOM 1824 CG PHE B 227 18.672 15.081 0.210 1.00 27.19 C ANISOU 1824 CG PHE B 227 3378 3781 3174 -524 370 -106 C ATOM 1825 CD1 PHE B 227 19.455 15.877 1.041 1.00 27.10 C ANISOU 1825 CD1 PHE B 227 3193 3796 3306 -410 330 -165 C ATOM 1826 CD2 PHE B 227 18.956 13.728 0.124 1.00 27.68 C ANISOU 1826 CD2 PHE B 227 3636 3784 3095 -497 439 -112 C ATOM 1827 CE1 PHE B 227 20.519 15.338 1.748 1.00 27.49 C ANISOU 1827 CE1 PHE B 227 3254 3843 3346 -267 344 -218 C ATOM 1828 CE2 PHE B 227 20.026 13.181 0.826 1.00 28.05 C ANISOU 1828 CE2 PHE B 227 3703 3807 3150 -339 468 -151 C ATOM 1829 CZ PHE B 227 20.803 13.991 1.644 1.00 27.96 C ANISOU 1829 CZ PHE B 227 3505 3850 3268 -222 411 -199 C ATOM 1830 N GLN B 228 15.038 18.251 0.009 1.00 26.10 N ANISOU 1830 N GLN B 228 2855 3816 3246 -841 231 88 N ATOM 1831 CA GLN B 228 14.062 19.077 -0.679 1.00 26.10 C ANISOU 1831 CA GLN B 228 2754 3877 3287 -943 236 209 C ATOM 1832 C GLN B 228 14.204 20.525 -0.219 1.00 29.77 C ANISOU 1832 C GLN B 228 2997 4327 3988 -890 247 210 C ATOM 1833 O GLN B 228 13.717 21.457 -0.864 1.00 28.77 O ANISOU 1833 O GLN B 228 2741 4235 3957 -937 284 323 O ATOM 1834 CB GLN B 228 12.644 18.568 -0.421 1.00 26.06 C ANISOU 1834 CB GLN B 228 2838 3924 3140 -1051 192 258 C ATOM 1835 CG GLN B 228 12.231 18.592 1.024 1.00 28.14 C ANISOU 1835 CG GLN B 228 3093 4162 3439 -1007 137 187 C ATOM 1836 CD GLN B 228 10.749 18.349 1.170 1.00 31.81 C ANISOU 1836 CD GLN B 228 3608 4683 3796 -1120 99 258 C ATOM 1837 OE1 GLN B 228 9.932 19.153 0.722 1.00 36.00 O ANISOU 1837 OE1 GLN B 228 4024 5275 4380 -1191 104 374 O ATOM 1838 NE2 GLN B 228 10.393 17.227 1.769 1.00 25.24 N ANISOU 1838 NE2 GLN B 228 2943 3832 2814 -1134 71 201 N ATOM 1839 OXT GLN B 228 14.827 20.794 0.811 1.00 28.71 O ANISOU 1839 OXT GLN B 228 2802 4152 3954 -802 232 96 O TER 1840 GLN B 228 ATOM 1841 P DG D -1 -12.364 -12.486 31.832 1.00 74.19 P ANISOU 1841 P DG D -1 11275 8034 8880 1043 -938 1043 P ATOM 1842 OP1 DG D -1 -13.060 -13.353 32.812 1.00 78.60 O ANISOU 1842 OP1 DG D -1 12013 8463 9390 999 -908 1074 O ATOM 1843 OP2 DG D -1 -11.100 -12.945 31.211 1.00 78.14 O ANISOU 1843 OP2 DG D -1 11564 8554 9572 1186 -988 1014 O ATOM 1844 O5' DG D -1 -13.385 -12.091 30.658 1.00 58.56 O ANISOU 1844 O5' DG D -1 9230 6157 6862 927 -729 916 O ATOM 1845 C5' DG D -1 -13.885 -13.097 29.774 1.00 48.90 C ANISOU 1845 C5' DG D -1 8001 4873 5705 942 -567 817 C ATOM 1846 C4' DG D -1 -14.884 -12.517 28.781 1.00 37.08 C ANISOU 1846 C4' DG D -1 6445 3504 4140 804 -405 723 C ATOM 1847 O4' DG D -1 -16.204 -12.436 29.387 1.00 35.89 O ANISOU 1847 O4' DG D -1 6495 3285 3856 696 -343 751 O ATOM 1848 C3' DG D -1 -14.571 -11.107 28.287 1.00 30.68 C ANISOU 1848 C3' DG D -1 5459 2895 3302 738 -433 716 C ATOM 1849 O3' DG D -1 -15.004 -10.975 26.951 1.00 27.48 O ANISOU 1849 O3' DG D -1 4923 2611 2908 664 -289 612 O ATOM 1850 C2' DG D -1 -15.413 -10.241 29.210 1.00 32.01 C ANISOU 1850 C2' DG D -1 5775 3057 3330 633 -461 792 C ATOM 1851 C1' DG D -1 -16.660 -11.101 29.342 1.00 35.48 C ANISOU 1851 C1' DG D -1 6396 3368 3717 583 -339 766 C ATOM 1852 N9 DG D -1 -17.424 -10.823 30.549 1.00 33.75 N ANISOU 1852 N9 DG D -1 6382 3056 3385 511 -362 837 N ATOM 1853 C8 DG D -1 -16.969 -10.862 31.850 1.00 36.92 C ANISOU 1853 C8 DG D -1 6810 3430 3788 516 -473 877 C ATOM 1854 N7 DG D -1 -17.886 -10.554 32.729 1.00 34.48 N ANISOU 1854 N7 DG D -1 6555 3124 3420 395 -421 848 N ATOM 1855 C5 DG D -1 -19.017 -10.291 31.956 1.00 32.22 C ANISOU 1855 C5 DG D -1 6253 2876 3114 312 -277 785 C ATOM 1856 C6 DG D -1 -20.323 -9.905 32.353 1.00 43.40 C ANISOU 1856 C6 DG D -1 7689 4307 4496 186 -172 726 C ATOM 1857 O6 DG D -1 -20.754 -9.716 33.507 1.00 48.14 O ANISOU 1857 O6 DG D -1 8346 4880 5066 122 -177 708 O ATOM 1858 N1 DG D -1 -21.171 -9.756 31.259 1.00 32.58 N ANISOU 1858 N1 DG D -1 6265 2983 3129 136 -54 683 N ATOM 1859 C2 DG D -1 -20.799 -9.938 29.944 1.00 37.77 C ANISOU 1859 C2 DG D -1 6880 3676 3796 184 -27 698 C ATOM 1860 N2 DG D -1 -21.756 -9.737 29.021 1.00 34.49 N ANISOU 1860 N2 DG D -1 6414 3322 3367 102 92 660 N ATOM 1861 N3 DG D -1 -19.577 -10.299 29.559 1.00 31.17 N ANISOU 1861 N3 DG D -1 6047 2815 2982 305 -111 745 N ATOM 1862 C4 DG D -1 -18.744 -10.456 30.614 1.00 31.74 C ANISOU 1862 C4 DG D -1 6146 2837 3077 371 -240 785 C ATOM 1863 P DG D 0 -13.996 -11.320 25.754 1.00 28.24 P ANISOU 1863 P DG D 0 4803 2791 3138 725 -246 512 P ATOM 1864 OP1 DG D 0 -14.845 -11.484 24.557 1.00 32.80 O ANISOU 1864 OP1 DG D 0 5334 3449 3680 614 -76 411 O ATOM 1865 OP2 DG D 0 -13.087 -12.411 26.158 1.00 30.02 O ANISOU 1865 OP2 DG D 0 5042 2870 3496 877 -305 519 O ATOM 1866 O5' DG D 0 -13.130 -9.994 25.609 1.00 27.77 O ANISOU 1866 O5' DG D 0 4571 2896 3083 714 -343 541 O ATOM 1867 C5' DG D 0 -13.766 -8.778 25.248 1.00 26.25 C ANISOU 1867 C5' DG D 0 4336 2847 2791 585 -308 553 C ATOM 1868 C4' DG D 0 -12.724 -7.753 24.870 1.00 26.17 C ANISOU 1868 C4' DG D 0 4136 2987 2820 591 -375 551 C ATOM 1869 O4' DG D 0 -11.859 -7.534 25.999 1.00 28.37 O ANISOU 1869 O4' DG D 0 4445 3211 3124 677 -537 631 O ATOM 1870 C3' DG D 0 -11.806 -8.202 23.749 1.00 27.03 C ANISOU 1870 C3' DG D 0 4061 3164 3046 636 -321 445 C ATOM 1871 O3' DG D 0 -12.308 -7.697 22.518 1.00 26.15 O ANISOU 1871 O3' DG D 0 3850 3202 2883 512 -201 381 O ATOM 1872 C2' DG D 0 -10.440 -7.595 24.099 1.00 28.56 C ANISOU 1872 C2' DG D 0 4125 3411 3316 714 -455 473 C ATOM 1873 C1' DG D 0 -10.621 -7.074 25.528 1.00 27.43 C ANISOU 1873 C1' DG D 0 4128 3202 3094 722 -591 598 C ATOM 1874 N9 DG D 0 -9.585 -7.508 26.450 1.00 28.90 N ANISOU 1874 N9 DG D 0 4320 3300 3360 850 -744 652 N ATOM 1875 C8 DG D 0 -9.215 -8.793 26.764 1.00 32.95 C ANISOU 1875 C8 DG D 0 4879 3665 3976 974 -775 655 C ATOM 1876 N7 DG D 0 -8.237 -8.849 27.637 1.00 32.85 N ANISOU 1876 N7 DG D 0 4849 3609 4024 1072 -945 731 N ATOM 1877 C5 DG D 0 -7.955 -7.508 27.898 1.00 30.89 C ANISOU 1877 C5 DG D 0 4543 3496 3698 997 -1019 766 C ATOM 1878 C6 DG D 0 -7.002 -6.916 28.750 1.00 41.32 C ANISOU 1878 C6 DG D 0 5820 4856 5024 1029 -1198 842 C ATOM 1879 O6 DG D 0 -6.177 -7.466 29.486 1.00 37.08 O ANISOU 1879 O6 DG D 0 5280 4245 4564 1138 -1349 908 O ATOM 1880 N1 DG D 0 -7.068 -5.528 28.703 1.00 41.58 N ANISOU 1880 N1 DG D 0 5806 5031 4963 913 -1195 841 N ATOM 1881 C2 DG D 0 -7.932 -4.798 27.933 1.00 40.87 C ANISOU 1881 C2 DG D 0 5707 5027 4796 793 -1047 791 C ATOM 1882 N2 DG D 0 -7.840 -3.462 28.026 1.00 31.43 N ANISOU 1882 N2 DG D 0 4463 3949 3531 698 -1062 807 N ATOM 1883 N3 DG D 0 -8.825 -5.337 27.131 1.00 28.12 N ANISOU 1883 N3 DG D 0 4124 3385 3174 764 -897 733 N ATOM 1884 C4 DG D 0 -8.784 -6.687 27.167 1.00 29.19 C ANISOU 1884 C4 DG D 0 4312 3390 3389 865 -889 718 C ATOM 1885 P DT D 1 -11.533 -7.964 21.142 1.00 26.88 P ANISOU 1885 P DT D 1 3751 3401 3059 500 -107 253 P ATOM 1886 OP1 DT D 1 -12.592 -7.904 20.100 1.00 26.09 O ANISOU 1886 OP1 DT D 1 3652 3398 2864 352 28 205 O ATOM 1887 OP2 DT D 1 -10.715 -9.195 21.295 1.00 28.50 O ANISOU 1887 OP2 DT D 1 3945 3474 3411 635 -107 193 O ATOM 1888 O5' DT D 1 -10.535 -6.730 21.016 1.00 26.70 O ANISOU 1888 O5' DT D 1 3569 3518 3058 497 -189 274 O ATOM 1889 C5' DT D 1 -11.060 -5.413 20.854 1.00 25.37 C ANISOU 1889 C5' DT D 1 3380 3476 2782 382 -195 335 C ATOM 1890 C4' DT D 1 -9.953 -4.382 20.906 1.00 25.48 C ANISOU 1890 C4' DT D 1 3255 3591 2836 399 -277 350 C ATOM 1891 O4' DT D 1 -9.445 -4.307 22.256 1.00 25.88 O ANISOU 1891 O4' DT D 1 3374 3543 2915 498 -422 427 O ATOM 1892 C3' DT D 1 -8.741 -4.716 20.051 1.00 26.65 C ANISOU 1892 C3' DT D 1 3225 3800 3100 440 -241 236 C ATOM 1893 O3' DT D 1 -8.910 -4.168 18.750 1.00 26.21 O ANISOU 1893 O3' DT D 1 3064 3903 2993 310 -132 178 O ATOM 1894 C2' DT D 1 -7.587 -4.031 20.786 1.00 27.11 C ANISOU 1894 C2' DT D 1 3202 3876 3223 516 -378 277 C ATOM 1895 C1' DT D 1 -8.106 -3.875 22.226 1.00 26.66 C ANISOU 1895 C1' DT D 1 3318 3709 3101 552 -495 401 C ATOM 1896 N1 DT D 1 -7.339 -4.664 23.228 1.00 28.00 N ANISOU 1896 N1 DT D 1 3522 3749 3366 697 -619 430 N ATOM 1897 C2 DT D 1 -6.634 -4.002 24.202 1.00 28.32 C ANISOU 1897 C2 DT D 1 3553 3800 3409 733 -769 502 C ATOM 1898 O2 DT D 1 -6.607 -2.786 24.296 1.00 29.08 O ANISOU 1898 O2 DT D 1 3617 3998 3435 651 -791 534 O ATOM 1899 N3 DT D 1 -5.960 -4.818 25.068 1.00 29.77 N ANISOU 1899 N3 DT D 1 3764 3866 3679 863 -893 541 N ATOM 1900 C4 DT D 1 -5.923 -6.204 25.063 1.00 32.04 C ANISOU 1900 C4 DT D 1 4091 4017 4067 969 -875 518 C ATOM 1901 O4 DT D 1 -5.281 -6.862 25.892 1.00 37.81 O ANISOU 1901 O4 DT D 1 4842 4640 4883 1090 -1003 574 O ATOM 1902 C5 DT D 1 -6.673 -6.832 24.018 1.00 31.78 C ANISOU 1902 C5 DT D 1 4070 3972 4033 924 -696 427 C ATOM 1903 C7 DT D 1 -6.696 -8.327 23.924 1.00 39.16 C ANISOU 1903 C7 DT D 1 5049 4752 5078 1024 -642 385 C ATOM 1904 C6 DT D 1 -7.340 -6.045 23.156 1.00 29.03 C ANISOU 1904 C6 DT D 1 3693 3753 3584 786 -582 386 C ATOM 1905 P DC D 2 -7.836 -4.451 17.597 1.00 27.38 P ANISOU 1905 P DC D 2 3030 4136 3235 300 -45 35 P ATOM 1906 OP1 DC D 2 -8.572 -4.323 16.288 1.00 26.94 O ANISOU 1906 OP1 DC D 2 2953 4207 3076 136 92 -17 O ATOM 1907 OP2 DC D 2 -7.076 -5.694 17.841 1.00 28.89 O ANISOU 1907 OP2 DC D 2 3198 4195 3582 436 -42 -42 O ATOM 1908 O5' DC D 2 -6.839 -3.228 17.699 1.00 30.26 O ANISOU 1908 O5' DC D 2 3263 4608 3626 300 -124 59 O ATOM 1909 C5' DC D 2 -7.311 -1.918 17.462 1.00 34.86 C ANISOU 1909 C5' DC D 2 3839 5314 4093 182 -127 133 C ATOM 1910 C4' DC D 2 -6.319 -0.908 17.990 1.00 42.61 C ANISOU 1910 C4' DC D 2 4730 6344 5117 216 -226 165 C ATOM 1911 O4' DC D 2 -6.081 -1.163 19.375 1.00 44.17 O ANISOU 1911 O4' DC D 2 5009 6415 5360 338 -359 231 O ATOM 1912 C3' DC D 2 -4.955 -0.993 17.349 1.00 47.73 C ANISOU 1912 C3' DC D 2 5196 7058 5882 243 -198 46 C ATOM 1913 O3' DC D 2 -4.952 -0.188 16.136 1.00 48.33 O ANISOU 1913 O3' DC D 2 5179 7295 5891 97 -97 5 O ATOM 1914 C2' DC D 2 -3.983 -0.531 18.458 1.00 49.36 C ANISOU 1914 C2' DC D 2 5357 7232 6164 345 -347 91 C ATOM 1915 C1' DC D 2 -4.839 -0.608 19.737 1.00 49.67 C ANISOU 1915 C1' DC D 2 5584 7153 6134 389 -447 218 C ATOM 1916 N1 DC D 2 -4.283 -1.446 20.864 1.00 44.55 N ANISOU 1916 N1 DC D 2 4977 6369 5581 539 -574 244 N ATOM 1917 C2 DC D 2 -3.872 -0.827 22.053 1.00 45.25 C ANISOU 1917 C2 DC D 2 5097 6439 5655 574 -723 330 C ATOM 1918 O2 DC D 2 -3.918 0.405 22.134 1.00 52.45 O ANISOU 1918 O2 DC D 2 5995 7443 6490 484 -732 368 O ATOM 1919 N3 DC D 2 -3.407 -1.597 23.079 1.00 37.09 N ANISOU 1919 N3 DC D 2 4109 5289 4694 700 -854 372 N ATOM 1920 C4 DC D 2 -3.379 -2.917 22.942 1.00 36.20 C ANISOU 1920 C4 DC D 2 4010 5066 4677 798 -831 335 C ATOM 1921 N4 DC D 2 -2.934 -3.628 23.960 1.00 34.60 N ANISOU 1921 N4 DC D 2 3854 4746 4546 921 -968 396 N ATOM 1922 C5 DC D 2 -3.821 -3.568 21.745 1.00 32.18 C ANISOU 1922 C5 DC D 2 3474 4563 4192 764 -661 235 C ATOM 1923 C6 DC D 2 -4.262 -2.804 20.749 1.00 42.95 C ANISOU 1923 C6 DC D 2 4794 6056 5468 629 -543 193 C ATOM 1924 P DG D 3 -4.317 1.288 16.012 1.00 47.67 P ANISOU 1924 P DG D 3 4992 7338 5783 29 -126 34 P ATOM 1925 OP1 DG D 3 -4.796 1.790 14.697 1.00 42.03 O ANISOU 1925 OP1 DG D 3 4244 6760 4966 -134 -6 16 O ATOM 1926 OP2 DG D 3 -2.868 1.227 16.301 1.00 59.78 O ANISOU 1926 OP2 DG D 3 6387 8869 7458 122 -179 -45 O ATOM 1927 O5' DG D 3 -5.024 2.178 17.138 1.00 48.88 O ANISOU 1927 O5' DG D 3 5266 7448 5857 32 -227 189 O ATOM 1928 C5' DG D 3 -4.203 2.952 18.043 1.00 37.56 C ANISOU 1928 C5' DG D 3 3792 6014 4466 80 -333 222 C ATOM 1929 C4' DG D 3 -4.140 4.428 17.654 1.00 25.18 C ANISOU 1929 C4' DG D 3 2166 4565 2835 -37 -301 262 C ATOM 1930 O4' DG D 3 -5.445 5.025 17.825 1.00 27.10 O ANISOU 1930 O4' DG D 3 2534 4790 2974 -111 -280 383 O ATOM 1931 C3' DG D 3 -3.205 5.263 18.527 1.00 26.87 C ANISOU 1931 C3' DG D 3 2327 4791 3091 -6 -396 277 C ATOM 1932 O3' DG D 3 -1.973 5.375 17.912 1.00 29.62 O ANISOU 1932 O3' DG D 3 2505 5228 3521 -7 -374 168 O ATOM 1933 C2' DG D 3 -3.884 6.617 18.597 1.00 24.40 C ANISOU 1933 C2' DG D 3 2067 4520 2686 -116 -366 378 C ATOM 1934 C1' DG D 3 -5.345 6.218 18.576 1.00 23.89 C ANISOU 1934 C1' DG D 3 2144 4386 2547 -138 -328 459 C ATOM 1935 N9 DG D 3 -5.896 5.960 19.887 1.00 29.04 N ANISOU 1935 N9 DG D 3 2943 4907 3184 -76 -408 530 N ATOM 1936 C8 DG D 3 -6.115 4.733 20.475 1.00 30.89 C ANISOU 1936 C8 DG D 3 3268 5030 3439 20 -461 518 C ATOM 1937 N7 DG D 3 -6.640 4.816 21.664 1.00 26.77 N ANISOU 1937 N7 DG D 3 2886 4404 2880 41 -524 595 N ATOM 1938 C5 DG D 3 -6.791 6.180 21.864 1.00 23.00 C ANISOU 1938 C5 DG D 3 2406 3970 2365 -48 -502 654 C ATOM 1939 C6 DG D 3 -7.328 6.880 22.951 1.00 21.98 C ANISOU 1939 C6 DG D 3 2398 3766 2189 -85 -525 734 C ATOM 1940 O6 DG D 3 -7.785 6.427 24.016 1.00 23.92 O ANISOU 1940 O6 DG D 3 2788 3894 2405 -51 -579 772 O ATOM 1941 N1 DG D 3 -7.283 8.254 22.738 1.00 22.89 N ANISOU 1941 N1 DG D 3 2457 3947 2294 -179 -470 766 N ATOM 1942 C2 DG D 3 -6.789 8.869 21.626 1.00 34.92 C ANISOU 1942 C2 DG D 3 3835 5596 3839 -230 -409 734 C ATOM 1943 N2 DG D 3 -6.839 10.204 21.620 1.00 51.39 N ANISOU 1943 N2 DG D 3 5894 7715 5916 -319 -356 781 N ATOM 1944 N3 DG D 3 -6.286 8.230 20.594 1.00 22.13 N ANISOU 1944 N3 DG D 3 2106 4054 2248 -206 -390 659 N ATOM 1945 C4 DG D 3 -6.318 6.893 20.782 1.00 22.51 C ANISOU 1945 C4 DG D 3 2200 4036 2316 -114 -435 618 C ATOM 1946 P DA D 4 -0.667 5.544 18.810 1.00 27.56 P ANISOU 1946 P DA D 4 2150 4962 3360 77 -495 134 P ATOM 1947 OP1 DA D 4 0.468 5.262 17.907 1.00 28.79 O ANISOU 1947 OP1 DA D 4 2119 5193 3626 85 -437 -5 O ATOM 1948 OP2 DA D 4 -0.835 4.774 20.072 1.00 31.90 O ANISOU 1948 OP2 DA D 4 2807 5380 3933 194 -625 194 O ATOM 1949 O5' DA D 4 -0.631 7.099 19.191 1.00 26.90 O ANISOU 1949 O5' DA D 4 2073 4944 3205 -21 -507 200 O ATOM 1950 C5' DA D 4 -0.711 8.088 18.161 1.00 29.00 C ANISOU 1950 C5' DA D 4 2279 5320 3421 -150 -390 189 C ATOM 1951 C4' DA D 4 -0.861 9.470 18.757 1.00 25.83 C ANISOU 1951 C4' DA D 4 1919 4936 2959 -227 -403 271 C ATOM 1952 O4' DA D 4 -2.035 9.496 19.612 1.00 24.85 O ANISOU 1952 O4' DA D 4 1970 4707 2766 -220 -436 388 O ATOM 1953 C3' DA D 4 0.319 9.928 19.620 1.00 26.70 C ANISOU 1953 C3' DA D 4 1951 5068 3127 -198 -500 230 C ATOM 1954 O3' DA D 4 0.587 11.301 19.369 1.00 26.51 O ANISOU 1954 O3' DA D 4 1877 5124 3071 -312 -436 237 O ATOM 1955 C2' DA D 4 -0.177 9.690 21.049 1.00 26.44 C ANISOU 1955 C2' DA D 4 2067 4921 3059 -141 -616 317 C ATOM 1956 C1' DA D 4 -1.680 9.911 20.917 1.00 25.08 C ANISOU 1956 C1' DA D 4 2046 4687 2794 -198 -536 419 C ATOM 1957 N9 DA D 4 -2.459 9.133 21.881 1.00 24.77 N ANISOU 1957 N9 DA D 4 2166 4521 2724 -131 -608 483 N ATOM 1958 C8 DA D 4 -2.489 7.772 22.024 1.00 25.22 C ANISOU 1958 C8 DA D 4 2253 4511 2819 -22 -666 460 C ATOM 1959 N7 DA D 4 -3.281 7.356 23.004 1.00 24.86 N ANISOU 1959 N7 DA D 4 2373 4347 2724 9 -721 535 N ATOM 1960 C5 DA D 4 -3.799 8.539 23.539 1.00 24.13 C ANISOU 1960 C5 DA D 4 2361 4247 2562 -89 -690 603 C ATOM 1961 C6 DA D 4 -4.699 8.796 24.604 1.00 26.41 C ANISOU 1961 C6 DA D 4 2825 4431 2780 -124 -702 686 C ATOM 1962 N6 DA D 4 -5.259 7.834 25.346 1.00 28.78 N ANISOU 1962 N6 DA D 4 3265 4617 3054 -63 -761 720 N ATOM 1963 N1 DA D 4 -4.999 10.087 24.877 1.00 31.44 N ANISOU 1963 N1 DA D 4 3491 5076 3380 -230 -639 728 N ATOM 1964 C2 DA D 4 -4.440 11.051 24.117 1.00 36.34 C ANISOU 1964 C2 DA D 4 3976 5803 4027 -294 -574 698 C ATOM 1965 N3 DA D 4 -3.589 10.927 23.077 1.00 25.54 N ANISOU 1965 N3 DA D 4 2445 4546 2713 -274 -561 624 N ATOM 1966 C4 DA D 4 -3.310 9.639 22.844 1.00 24.17 C ANISOU 1966 C4 DA D 4 2243 4361 2579 -172 -619 576 C ATOM 1967 P DT D 5 1.870 12.028 20.002 1.00 27.48 P ANISOU 1967 P DT D 5 1892 5306 3243 -327 -503 177 P ATOM 1968 OP1 DT D 5 2.123 13.245 19.205 1.00 31.69 O ANISOU 1968 OP1 DT D 5 2352 5934 3753 -452 -385 157 O ATOM 1969 OP2 DT D 5 2.954 11.061 20.286 1.00 28.83 O ANISOU 1969 OP2 DT D 5 1948 5483 3524 -213 -610 87 O ATOM 1970 O5' DT D 5 1.348 12.514 21.429 1.00 27.02 O ANISOU 1970 O5' DT D 5 1985 5163 3118 -338 -584 275 O ATOM 1971 C5' DT D 5 0.326 13.470 21.517 1.00 25.92 C ANISOU 1971 C5' DT D 5 1963 4986 2899 -434 -497 369 C ATOM 1972 C4' DT D 5 -0.062 13.652 22.967 1.00 25.79 C ANISOU 1972 C4' DT D 5 2090 4876 2832 -436 -577 434 C ATOM 1973 O4' DT D 5 -0.711 12.453 23.425 1.00 25.58 O ANISOU 1973 O4' DT D 5 2173 4753 2794 -340 -650 474 O ATOM 1974 C3' DT D 5 1.127 13.890 23.908 1.00 26.98 C ANISOU 1974 C3' DT D 5 2181 5070 3002 -437 -695 378 C ATOM 1975 O3' DT D 5 1.043 15.215 24.456 1.00 26.81 O ANISOU 1975 O3' DT D 5 2210 5049 2929 -561 -638 402 O ATOM 1976 C2' DT D 5 1.008 12.781 24.983 1.00 27.43 C ANISOU 1976 C2' DT D 5 2336 5040 3045 -338 -848 411 C ATOM 1977 C1' DT D 5 -0.418 12.283 24.806 1.00 26.21 C ANISOU 1977 C1' DT D 5 2332 4781 2847 -317 -781 491 C ATOM 1978 N1 DT D 5 -0.659 10.831 25.176 1.00 26.49 N ANISOU 1978 N1 DT D 5 2435 4734 2896 -193 -883 509 N ATOM 1979 C2 DT D 5 -1.586 10.544 26.153 1.00 26.07 C ANISOU 1979 C2 DT D 5 2573 4563 2768 -194 -917 588 C ATOM 1980 O2 DT D 5 -2.195 11.401 26.765 1.00 27.72 O ANISOU 1980 O2 DT D 5 2895 4730 2908 -290 -867 637 O ATOM 1981 N3 DT D 5 -1.760 9.217 26.409 1.00 26.41 N ANISOU 1981 N3 DT D 5 2673 4531 2829 -82 -1001 603 N ATOM 1982 C4 DT D 5 -1.128 8.152 25.801 1.00 32.42 C ANISOU 1982 C4 DT D 5 3319 5314 3686 33 -1047 548 C ATOM 1983 O4 DT D 5 -1.352 6.977 26.115 1.00 32.52 O ANISOU 1983 O4 DT D 5 3400 5239 3718 131 -1114 569 O ATOM 1984 C5 DT D 5 -0.182 8.504 24.790 1.00 27.60 C ANISOU 1984 C5 DT D 5 2505 4823 3157 27 -999 458 C ATOM 1985 C7 DT D 5 0.574 7.418 24.074 1.00 32.02 C ANISOU 1985 C7 DT D 5 2921 5403 3841 140 -1022 378 C ATOM 1986 C6 DT D 5 0.013 9.819 24.525 1.00 27.23 C ANISOU 1986 C6 DT D 5 2404 4861 3082 -88 -923 443 C ATOM 1987 P DT D 6 2.281 15.911 25.216 1.00 28.05 P ANISOU 1987 P DT D 6 2286 5283 3088 -623 -714 334 P ATOM 1988 OP1 DT D 6 2.024 17.366 25.178 1.00 28.39 O ANISOU 1988 OP1 DT D 6 2360 5330 3096 -765 -574 348 O ATOM 1989 OP2 DT D 6 3.582 15.392 24.748 1.00 29.22 O ANISOU 1989 OP2 DT D 6 2240 5537 3327 -555 -793 234 O ATOM 1990 O5' DT D 6 2.104 15.441 26.716 1.00 28.51 O ANISOU 1990 O5' DT D 6 2486 5264 3081 -604 -858 380 O ATOM 1991 C5' DT D 6 1.125 16.030 27.512 1.00 27.85 C ANISOU 1991 C5' DT D 6 2587 5083 2911 -693 -799 450 C ATOM 1992 C4' DT D 6 1.065 15.305 28.824 1.00 28.51 C ANISOU 1992 C4' DT D 6 2799 5104 2929 -664 -954 486 C ATOM 1993 O4' DT D 6 0.533 13.975 28.589 1.00 28.14 O ANISOU 1993 O4' DT D 6 2796 4990 2906 -528 -1010 527 O ATOM 1994 C3' DT D 6 2.444 15.116 29.501 1.00 31.93 C ANISOU 1994 C3' DT D 6 3130 5634 3368 -655 -1135 432 C ATOM 1995 O3' DT D 6 2.419 15.633 30.806 1.00 30.85 O ANISOU 1995 O3' DT D 6 3124 5474 3122 -772 -1188 452 O ATOM 1996 C2' DT D 6 2.620 13.604 29.528 1.00 30.78 C ANISOU 1996 C2' DT D 6 2963 5461 3272 -491 -1286 457 C ATOM 1997 C1' DT D 6 1.184 13.119 29.482 1.00 33.75 C ANISOU 1997 C1' DT D 6 3517 5702 3604 -462 -1204 533 C ATOM 1998 N1 DT D 6 1.081 11.723 29.036 1.00 29.44 N ANISOU 1998 N1 DT D 6 2946 5114 3126 -305 -1269 547 N ATOM 1999 C2 DT D 6 0.214 10.895 29.685 1.00 32.57 C ANISOU 1999 C2 DT D 6 3520 5389 3466 -261 -1315 620 C ATOM 2000 O2 DT D 6 -0.528 11.281 30.565 1.00 33.62 O ANISOU 2000 O2 DT D 6 3832 5447 3495 -350 -1293 671 O ATOM 2001 N3 DT D 6 0.235 9.601 29.270 1.00 29.41 N ANISOU 2001 N3 DT D 6 3085 4950 3139 -117 -1372 625 N ATOM 2002 C4 DT D 6 1.043 9.056 28.297 1.00 29.95 C ANISOU 2002 C4 DT D 6 2958 5085 3336 -17 -1382 558 C ATOM 2003 O4 DT D 6 0.994 7.875 28.001 1.00 35.23 O ANISOU 2003 O4 DT D 6 3612 5699 4073 105 -1418 560 O ATOM 2004 C5 DT D 6 1.952 9.984 27.659 1.00 30.24 C ANISOU 2004 C5 DT D 6 2812 5253 3426 -75 -1332 477 C ATOM 2005 C7 DT D 6 2.887 9.517 26.601 1.00 30.96 C ANISOU 2005 C7 DT D 6 2684 5420 3658 10 -1321 386 C ATOM 2006 C6 DT D 6 1.943 11.255 28.073 1.00 29.98 C ANISOU 2006 C6 DT D 6 2815 5262 3315 -213 -1285 478 C ATOM 2007 P DC D 7 3.462 16.757 31.308 0.59 33.05 P ANISOU 2007 P DC D 7 3323 5866 3369 -915 -1207 381 P ATOM 2008 OP1 DC D 7 4.629 16.841 30.396 0.59 37.65 O ANISOU 2008 OP1 DC D 7 3662 6579 4062 -866 -1226 297 O ATOM 2009 OP2 DC D 7 3.651 16.497 32.750 0.59 35.87 O ANISOU 2009 OP2 DC D 7 3804 6212 3614 -972 -1371 413 O ATOM 2010 O5' DC D 7 2.631 18.114 31.177 0.59 40.75 O ANISOU 2010 O5' DC D 7 4394 6782 4306 -1065 -974 380 O ATOM 2011 C5' DC D 7 1.521 18.359 32.035 0.59 34.69 C ANISOU 2011 C5' DC D 7 3848 5886 3447 -1150 -903 437 C ATOM 2012 C4' DC D 7 1.143 19.828 32.004 0.59 38.42 C ANISOU 2012 C4' DC D 7 4361 6325 3913 -1309 -692 412 C ATOM 2013 O4' DC D 7 2.175 20.606 32.664 0.59 35.07 O ANISOU 2013 O4' DC D 7 3890 5997 3436 -1445 -733 334 O ATOM 2014 C3' DC D 7 0.987 20.417 30.605 0.59 43.32 C ANISOU 2014 C3' DC D 7 4855 6963 4642 -1281 -528 407 C ATOM 2015 O3' DC D 7 -0.110 21.327 30.566 0.59 46.64 O ANISOU 2015 O3' DC D 7 5385 7264 5074 -1370 -322 452 O ATOM 2016 C2' DC D 7 2.323 21.118 30.357 0.59 40.53 C ANISOU 2016 C2' DC D 7 4332 6753 4313 -1345 -545 312 C ATOM 2017 C1' DC D 7 2.757 21.528 31.762 0.59 41.45 C ANISOU 2017 C1' DC D 7 4541 6885 4323 -1485 -616 273 C ATOM 2018 N1 DC D 7 4.236 21.497 31.955 0.59 43.66 N ANISOU 2018 N1 DC D 7 4664 7325 4600 -1502 -770 189 N ATOM 2019 C2 DC D 7 4.918 22.674 32.289 0.59 46.61 C ANISOU 2019 C2 DC D 7 4998 7768 4943 -1670 -701 107 C ATOM 2020 O2 DC D 7 4.278 23.726 32.419 0.59 47.91 O ANISOU 2020 O2 DC D 7 5265 7849 5089 -1799 -503 105 O ATOM 2021 N3 DC D 7 6.264 22.626 32.464 0.59 46.23 N ANISOU 2021 N3 DC D 7 4794 7873 4898 -1688 -847 30 N ATOM 2022 C4 DC D 7 6.918 21.471 32.313 0.59 45.53 C ANISOU 2022 C4 DC D 7 4586 7857 4857 -1537 -1052 40 C ATOM 2023 N4 DC D 7 8.244 21.474 32.494 0.59 46.40 N ANISOU 2023 N4 DC D 7 4527 8116 4989 -1556 -1194 -34 N ATOM 2024 C5 DC D 7 6.241 20.263 31.971 0.59 42.28 C ANISOU 2024 C5 DC D 7 4217 7364 4484 -1361 -1114 123 C ATOM 2025 C6 DC D 7 4.915 20.322 31.805 0.59 41.79 C ANISOU 2025 C6 DC D 7 4316 7161 4402 -1355 -970 192 C TER 2026 DC D 7 HETATM 2027 O HOH B 301 -13.890 1.388 -4.803 1.00 40.20 O HETATM 2028 O HOH B 302 -4.238 11.676 -1.242 1.00 35.00 O HETATM 2029 O HOH B 303 -18.491 10.091 29.290 1.00 39.97 O HETATM 2030 O HOH B 304 -7.959 19.594 4.320 1.00 40.51 O HETATM 2031 O HOH B 305 -0.820 16.958 7.208 1.00 27.98 O HETATM 2032 O HOH B 306 -37.774 3.668 19.632 1.00 46.87 O HETATM 2033 O HOH B 307 -31.257 0.247 6.641 1.00 26.66 O HETATM 2034 O HOH B 308 -23.041 11.588 -1.080 1.00 26.22 O HETATM 2035 O HOH B 309 -11.439 19.452 13.696 1.00 25.11 O HETATM 2036 O HOH B 310 -24.679 18.832 8.507 1.00 24.83 O HETATM 2037 O HOH B 311 -26.841 -15.298 7.016 1.00 35.60 O HETATM 2038 O HOH B 312 -13.378 22.459 11.589 1.00 34.78 O HETATM 2039 O HOH B 313 -27.628 21.141 1.011 1.00 25.89 O HETATM 2040 O HOH B 314 -30.054 -9.577 15.769 1.00 37.03 O HETATM 2041 O HOH B 315 -8.071 -0.225 12.958 1.00 23.23 O HETATM 2042 O HOH B 316 -3.847 -0.804 8.228 1.00 26.65 O HETATM 2043 O HOH B 317 -27.858 6.415 16.495 1.00 23.85 O HETATM 2044 O HOH B 318 -6.446 1.393 12.309 1.00 32.77 O HETATM 2045 O HOH B 319 -16.989 -6.835 -0.353 1.00 32.14 O HETATM 2046 O HOH B 320 -22.039 18.785 -0.738 1.00 24.82 O HETATM 2047 O HOH B 321 -22.039 -14.927 13.545 1.00 33.81 O HETATM 2048 O HOH B 322 -19.207 3.941 -1.978 1.00 24.13 O HETATM 2049 O HOH B 323 -22.853 -12.702 30.207 1.00 40.06 O HETATM 2050 O HOH B 324 -26.838 -6.026 -1.190 1.00 26.79 O HETATM 2051 O HOH B 325 -22.827 23.967 3.721 1.00 33.00 O HETATM 2052 O HOH B 326 9.712 20.968 -1.116 1.00 44.82 O HETATM 2053 O HOH B 327 -7.696 -12.266 11.791 1.00 47.76 O HETATM 2054 O HOH B 328 -8.686 -0.442 20.401 1.00 28.44 O HETATM 2055 O HOH B 329 -22.924 -15.734 9.085 1.00 35.28 O HETATM 2056 O HOH B 330 -6.568 8.078 -5.028 1.00 42.53 O HETATM 2057 O HOH B 331 -26.885 -14.597 16.512 1.00 61.65 O HETATM 2058 O HOH B 332 -25.177 21.882 13.048 1.00 38.44 O HETATM 2059 O HOH B 333 -31.284 11.847 3.025 1.00 37.34 O HETATM 2060 O HOH B 334 -3.775 17.111 24.346 1.00 30.13 O HETATM 2061 O HOH B 335 -35.307 3.534 21.274 1.00 36.65 O HETATM 2062 O HOH B 336 -31.346 3.487 17.265 1.00 25.19 O HETATM 2063 O HOH B 337 11.888 21.594 -2.740 1.00 37.32 O HETATM 2064 O HOH B 338 -18.818 -12.396 12.334 1.00 32.62 O HETATM 2065 O HOH B 339 1.494 0.063 2.046 1.00 43.00 O HETATM 2066 O HOH B 340 -32.049 11.514 14.432 1.00 31.17 O HETATM 2067 O HOH B 341 4.755 3.613 4.008 1.00 36.59 O HETATM 2068 O HOH B 342 -1.968 6.158 -1.511 1.00 27.84 O HETATM 2069 O HOH B 343 -29.414 -0.110 27.619 1.00 37.28 O HETATM 2070 O HOH B 344 -17.558 -12.289 14.872 1.00 29.42 O HETATM 2071 O HOH B 345 -29.650 7.883 3.230 1.00 28.04 O HETATM 2072 O HOH B 346 -27.377 10.072 22.333 1.00 23.93 O HETATM 2073 O HOH B 347 -31.013 2.945 -2.307 1.00 33.88 O HETATM 2074 O HOH B 348 -23.615 8.054 24.535 1.00 19.01 O HETATM 2075 O HOH B 349 -10.132 -11.704 17.923 1.00 34.85 O HETATM 2076 O HOH B 350 -14.361 -10.024 20.161 1.00 26.09 O HETATM 2077 O HOH B 351 -18.277 2.084 33.519 1.00 34.67 O HETATM 2078 O HOH B 352 -25.138 4.580 -2.983 1.00 25.32 O HETATM 2079 O HOH B 353 -11.658 19.370 4.048 1.00 29.92 O HETATM 2080 O HOH B 354 -29.848 17.116 11.527 1.00 29.94 O HETATM 2081 O HOH B 355 -19.476 13.845 15.449 1.00 15.07 O HETATM 2082 O HOH B 356 -14.911 13.884 2.524 1.00 25.52 O HETATM 2083 O HOH B 357 -12.063 9.318 -0.410 1.00 29.44 O HETATM 2084 O HOH B 358 -26.377 -2.354 26.431 1.00 34.95 O HETATM 2085 O HOH B 359 -28.624 25.168 2.123 1.00 27.70 O HETATM 2086 O HOH B 360 -32.053 -2.850 19.362 1.00 42.47 O HETATM 2087 O HOH B 361 -26.948 -1.405 29.270 1.00 43.60 O HETATM 2088 O HOH B 362 -33.749 -12.487 6.522 1.00 40.30 O HETATM 2089 O HOH B 363 -9.152 -0.951 27.379 1.00 29.71 O HETATM 2090 O HOH B 364 -13.688 1.341 33.448 1.00 37.32 O HETATM 2091 O HOH B 365 0.629 -3.048 13.764 1.00 48.19 O HETATM 2092 O HOH B 366 -18.312 4.309 0.587 1.00 22.35 O HETATM 2093 O HOH B 367 -21.248 -6.324 27.487 1.00 26.81 O HETATM 2094 O HOH B 368 -1.955 15.948 10.540 1.00 27.19 O HETATM 2095 O HOH B 369 -21.331 5.192 -5.501 1.00 38.65 O HETATM 2096 O HOH B 370 -10.207 -9.728 9.722 1.00 39.37 O HETATM 2097 O HOH B 371 -5.814 4.796 14.556 1.00 22.44 O HETATM 2098 O HOH B 372 -12.998 7.744 2.193 1.00 18.08 O HETATM 2099 O HOH B 373 -17.908 2.903 2.769 1.00 16.85 O HETATM 2100 O HOH B 374 -25.158 4.210 23.907 1.00 21.49 O HETATM 2101 O HOH B 375 -23.430 -12.495 26.311 1.00 40.20 O HETATM 2102 O HOH B 376 -32.032 -6.449 16.141 1.00 39.04 O HETATM 2103 O HOH B 377 -29.075 -0.975 16.694 1.00 22.99 O HETATM 2104 O HOH B 378 -23.568 -1.380 32.933 1.00 48.89 O HETATM 2105 O HOH B 379 -18.110 -11.894 9.442 1.00 29.97 O HETATM 2106 O HOH B 380 -24.266 -3.664 30.714 1.00 47.89 O HETATM 2107 O HOH B 381 -38.337 6.555 15.112 1.00 38.72 O HETATM 2108 O HOH B 382 -21.174 -6.264 -1.527 1.00 27.97 O HETATM 2109 O HOH B 383 -15.824 12.647 0.029 1.00 18.76 O HETATM 2110 O HOH B 384 -16.356 20.747 14.426 1.00 28.97 O HETATM 2111 O HOH B 385 -18.338 15.862 20.342 1.00 28.56 O HETATM 2112 O HOH B 386 -18.718 23.658 10.819 1.00 39.15 O HETATM 2113 O HOH B 387 -22.217 8.601 11.666 1.00 16.59 O HETATM 2114 O HOH B 388 1.434 11.984 15.268 1.00 21.91 O HETATM 2115 O HOH B 389 -27.975 -0.657 -3.742 1.00 31.93 O HETATM 2116 O HOH B 390 -31.781 -6.810 4.802 1.00 29.33 O HETATM 2117 O HOH B 391 -15.317 20.877 7.217 1.00 27.68 O HETATM 2118 O HOH B 392 -29.018 -2.514 0.435 1.00 28.98 O HETATM 2119 O HOH B 393 -31.314 0.631 16.751 1.00 25.24 O HETATM 2120 O HOH B 394 -14.857 14.015 26.230 1.00 32.60 O HETATM 2121 O HOH B 395 -33.181 -0.059 4.480 1.00 41.98 O HETATM 2122 O HOH B 396 -12.335 3.611 -4.029 1.00 27.14 O HETATM 2123 O HOH B 397 -29.511 9.278 -2.229 1.00 35.34 O HETATM 2124 O HOH B 398 -3.309 -8.783 8.521 1.00 46.52 O HETATM 2125 O HOH B 399 -11.122 4.477 25.895 1.00 30.73 O HETATM 2126 O HOH B 400 -2.157 3.221 14.360 1.00 37.17 O HETATM 2127 O HOH B 401 -26.667 20.042 3.118 1.00 34.58 O HETATM 2128 O HOH B 402 -34.887 -2.140 11.134 1.00 41.95 O HETATM 2129 O HOH B 403 -30.347 12.339 19.944 1.00 38.46 O HETATM 2130 O HOH B 404 -17.108 -15.027 16.153 1.00 38.75 O HETATM 2131 O HOH B 405 -24.128 10.914 24.164 1.00 28.60 O HETATM 2132 O HOH B 406 1.415 22.625 20.552 1.00 48.24 O HETATM 2133 O HOH B 407 -29.183 0.359 13.474 1.00 21.01 O HETATM 2134 O HOH B 408 -34.847 -0.933 6.565 1.00 42.55 O HETATM 2135 O HOH B 409 -24.101 -13.178 17.109 1.00 35.81 O HETATM 2136 O HOH B 410 -8.489 -12.908 15.971 1.00 45.40 O HETATM 2137 O HOH B 411 -26.021 6.633 24.316 1.00 20.48 O HETATM 2138 O HOH B 412 1.145 15.555 17.858 1.00 24.64 O HETATM 2139 O HOH B 413 1.892 17.264 21.128 1.00 30.20 O HETATM 2140 O HOH B 414 -13.237 16.855 16.853 1.00 25.99 O HETATM 2141 O HOH B 415 -23.751 2.711 31.706 1.00 39.50 O HETATM 2142 O HOH B 416 -32.520 10.871 16.616 1.00 36.92 O HETATM 2143 O HOH B 417 0.805 20.078 18.696 1.00 36.44 O HETATM 2144 O HOH B 418 7.142 19.769 0.584 1.00 37.79 O HETATM 2145 O HOH B 419 -13.583 5.966 25.426 1.00 21.28 O HETATM 2146 O HOH B 420 4.541 18.698 1.777 1.00 35.68 O HETATM 2147 O HOH B 421 -27.331 -2.831 22.245 1.00 28.59 O HETATM 2148 O HOH B 422 -16.207 -14.365 25.353 1.00 37.86 O HETATM 2149 O HOH B 423 -31.410 3.347 19.945 1.00 23.49 O HETATM 2150 O HOH B 424 -28.323 -2.562 24.798 1.00 41.99 O HETATM 2151 O HOH B 425 -31.823 -0.986 0.284 1.00 36.83 O HETATM 2152 O HOH B 426 -36.078 -0.633 13.287 1.00 39.05 O HETATM 2153 O HOH B 427 -12.434 -0.313 -8.355 1.00 43.13 O HETATM 2154 O HOH B 428 -15.228 -12.255 3.298 1.00 46.48 O HETATM 2155 O HOH B 429 -7.700 2.165 18.563 1.00 32.79 O HETATM 2156 O HOH B 430 -37.787 10.872 5.286 1.00 42.96 O HETATM 2157 O HOH B 431 -10.384 -1.090 22.279 1.00 21.17 O HETATM 2158 O HOH B 432 -29.250 19.526 13.001 1.00 39.02 O HETATM 2159 O HOH B 433 -28.678 -4.265 15.724 1.00 23.46 O HETATM 2160 O HOH B 434 3.652 10.821 15.972 1.00 36.57 O HETATM 2161 O HOH B 435 -17.849 15.159 23.242 1.00 29.98 O HETATM 2162 O HOH B 436 -33.888 8.395 3.779 1.00 36.87 O HETATM 2163 O HOH B 437 -10.461 10.033 -7.276 1.00 45.67 O HETATM 2164 O HOH B 438 -22.932 -6.289 30.134 1.00 37.79 O HETATM 2165 O HOH B 439 -15.763 -14.855 20.991 1.00 40.58 O HETATM 2166 O HOH B 440 -16.579 8.415 -7.190 1.00 33.33 O HETATM 2167 O HOH B 441 -26.399 1.960 30.906 1.00 37.83 O HETATM 2168 O HOH B 442 5.093 16.647 10.865 1.00 35.80 O HETATM 2169 O HOH B 443 12.667 16.734 -3.471 1.00 30.60 O HETATM 2170 O HOH B 444 -11.127 -6.434 3.067 1.00 39.83 O HETATM 2171 O HOH B 445 -26.476 2.417 -2.915 1.00 26.66 O HETATM 2172 O HOH B 446 -15.232 -8.766 7.465 1.00 32.08 O HETATM 2173 O HOH B 447 -6.827 23.516 16.714 1.00 34.96 O HETATM 2174 O HOH B 448 2.701 3.407 1.843 1.00 38.69 O HETATM 2175 O HOH B 449 -28.736 13.919 1.606 1.00 33.80 O HETATM 2176 O HOH B 450 -12.847 -7.347 1.318 1.00 39.14 O HETATM 2177 O HOH B 451 -13.767 20.709 15.123 1.00 34.59 O HETATM 2178 O HOH B 452 3.278 5.575 21.558 1.00 36.16 O HETATM 2179 O HOH B 453 -23.109 20.471 12.084 1.00 33.73 O HETATM 2180 O HOH B 454 -14.659 21.403 3.872 1.00 36.13 O HETATM 2181 O HOH B 455 -4.237 -8.833 15.030 1.00 41.28 O HETATM 2182 O HOH B 456 -27.240 25.003 10.413 1.00 46.45 O HETATM 2183 O HOH B 457 -16.874 -17.264 23.144 1.00 50.56 O HETATM 2184 O HOH B 458 -15.011 -12.808 11.027 1.00 40.58 O HETATM 2185 O HOH B 459 -16.844 21.798 2.350 1.00 35.01 O HETATM 2186 O HOH B 460 -32.833 -2.879 21.989 1.00 50.87 O HETATM 2187 O HOH B 461 -36.689 -1.461 15.494 1.00 51.99 O HETATM 2188 O HOH B 462 -11.573 -0.178 37.598 1.00 45.94 O HETATM 2189 O HOH B 463 -18.038 2.405 -5.495 1.00 45.30 O HETATM 2190 O HOH B 464 -11.346 2.924 -6.524 1.00 36.96 O HETATM 2191 O HOH B 465 -29.878 -12.235 16.975 1.00 47.86 O HETATM 2192 O HOH B 466 -19.188 1.540 -3.285 1.00 30.33 O HETATM 2193 O HOH B 467 -28.270 15.017 16.796 1.00 46.58 O HETATM 2194 O HOH B 468 -36.746 8.389 19.238 1.00 44.50 O HETATM 2195 O HOH B 469 -8.962 0.119 24.669 1.00 37.75 O HETATM 2196 O HOH B 470 -3.337 -9.174 10.660 1.00 48.33 O HETATM 2197 O HOH B 471 -15.704 0.872 -6.284 1.00 43.46 O HETATM 2198 O HOH B 472 -20.583 -15.192 7.615 1.00 36.93 O HETATM 2199 O HOH B 473 -28.358 12.545 23.489 1.00 40.82 O HETATM 2200 O HOH B 474 -37.493 -0.305 18.994 1.00 52.87 O HETATM 2201 O HOH B 475 -27.487 -4.532 23.717 1.00 43.49 O HETATM 2202 O HOH B 476 -35.542 -3.111 3.150 1.00 50.58 O HETATM 2203 O HOH B 477 -24.087 26.058 6.772 1.00 34.78 O HETATM 2204 O HOH B 478 -19.098 17.358 18.183 1.00 37.83 O HETATM 2205 O HOH B 479 1.823 17.745 18.506 1.00 38.09 O HETATM 2206 O HOH B 480 -18.320 -14.818 8.375 1.00 39.08 O HETATM 2207 O HOH B 481 3.093 19.824 8.050 1.00 45.70 O HETATM 2208 O HOH B 482 -29.171 2.628 -4.050 1.00 33.39 O HETATM 2209 O HOH B 483 -38.051 9.385 17.673 1.00 48.12 O HETATM 2210 O HOH B 484 -16.997 23.443 12.805 1.00 47.04 O HETATM 2211 O HOH B 485 -16.021 -11.422 8.452 1.00 33.47 O HETATM 2212 O HOH B 486 -17.221 19.387 17.225 1.00 39.13 O HETATM 2213 O HOH B 487 -14.262 19.759 17.249 1.00 44.06 O HETATM 2214 O HOH B 488 -20.448 16.432 16.135 1.00 19.81 O HETATM 2215 O HOH B 489 -10.342 -8.096 -4.005 1.00 55.19 O HETATM 2216 O HOH B 490 -24.151 26.363 4.204 1.00 27.08 O HETATM 2217 O HOH B 491 -32.993 -0.523 18.557 1.00 35.89 O HETATM 2218 O HOH B 492 -22.021 18.713 14.666 1.00 36.70 O HETATM 2219 O HOH B 493 -2.373 17.714 26.175 1.00 37.58 O HETATM 2220 O HOH B 494 -21.956 -17.026 11.794 1.00 44.30 O HETATM 2221 O HOH B 495 -33.178 1.395 20.758 1.00 31.02 O HETATM 2222 O HOH B 496 -31.777 9.592 4.030 1.00 37.78 O HETATM 2223 O HOH B 497 -29.621 0.226 -5.373 1.00 40.18 O HETATM 2224 O HOH B 498 -14.089 3.963 32.780 1.00 44.64 O HETATM 2225 O HOH B 499 -26.542 6.244 -4.973 1.00 39.71 O HETATM 2226 O HOH B 500 -25.505 0.149 -4.239 1.00 33.77 O HETATM 2227 O HOH B 501 -31.539 7.615 -3.342 1.00 49.35 O HETATM 2228 O HOH B 502 -22.989 3.520 -4.193 1.00 33.87 O HETATM 2229 O HOH B 503 -12.993 -8.417 6.517 1.00 41.21 O HETATM 2230 O HOH B 504 -25.074 16.950 18.362 1.00 48.90 O HETATM 2231 O HOH B 505 -14.957 -13.043 6.194 1.00 46.03 O HETATM 2232 O HOH B 506 -1.895 20.746 25.740 1.00 43.95 O HETATM 2233 O HOH B 507 -29.207 5.489 -4.968 1.00 47.89 O HETATM 2234 O HOH D 101 -4.304 -4.401 26.924 0.50 35.65 O HETATM 2235 O HOH D 102 3.783 9.500 18.433 1.00 38.96 O HETATM 2236 O HOH D 103 -10.936 -11.694 21.987 1.00 34.14 O HETATM 2237 O HOH D 104 6.912 15.867 29.577 1.00 35.72 O HETATM 2238 O HOH D 105 -8.099 -9.126 21.430 1.00 37.48 O HETATM 2239 O HOH D 106 -1.660 2.279 20.116 1.00 36.11 O HETATM 2240 O HOH D 107 -6.263 -7.477 19.725 1.00 41.93 O HETATM 2241 O HOH D 108 -13.974 -14.695 24.915 1.00 45.10 O HETATM 2242 O HOH D 109 -4.341 -5.468 17.704 1.00 43.56 O HETATM 2243 O HOH D 110 4.996 18.088 34.548 1.00 38.13 O HETATM 2244 O HOH D 111 4.201 13.114 26.177 1.00 35.37 O HETATM 2245 O HOH D 112 3.867 13.685 17.108 1.00 36.54 O HETATM 2246 O HOH D 113 -13.606 -11.960 22.106 1.00 31.63 O HETATM 2247 O HOH D 114 3.696 14.735 34.952 1.00 17.78 O HETATM 2248 O HOH D 115 2.920 10.062 22.926 1.00 23.99 O HETATM 2249 O HOH D 116 -0.582 18.436 24.990 1.00 26.88 O HETATM 2250 O HOH D 117 -3.415 13.724 22.536 1.00 21.06 O HETATM 2251 O HOH D 118 3.663 15.293 20.574 1.00 39.46 O HETATM 2252 O HOH D 119 -24.013 -9.086 31.730 1.00 47.40 O HETATM 2253 O HOH D 120 -2.302 14.259 27.562 1.00 22.39 O HETATM 2254 O HOH D 121 -7.095 2.393 23.419 1.00 40.06 O HETATM 2255 O HOH D 122 -0.101 2.641 16.250 1.00 41.44 O HETATM 2256 O HOH D 123 -5.037 4.464 25.377 1.00 44.67 O HETATM 2257 O HOH D 124 -2.221 -0.364 26.001 1.00 36.24 O HETATM 2258 O HOH D 125 -3.861 14.406 25.078 1.00 34.17 O HETATM 2259 O HOH D 126 -24.478 -10.596 33.907 1.00 48.31 O HETATM 2260 O HOH D 127 -13.965 -14.773 22.442 1.00 42.77 O HETATM 2261 O HOH D 128 -9.476 -11.517 24.613 1.00 37.46 O HETATM 2262 O HOH D 129 -2.226 17.023 28.695 1.00 31.46 O HETATM 2263 O HOH D 130 4.788 7.371 25.863 1.00 27.19 O MASTER 392 0 0 10 16 0 0 6 2232 2 0 19 END
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Entry Information
PDB ID
6kbs
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
SOS response-associated protein, yedK
Ligand Name
10-mer
EC.Number
E.C.3.4
Resolution
1.6(Å)
Affinity (Kd/Ki/IC50)
Kd=2.2uM
Release Year
2019
Protein/NA Sequence
Check fasta file
Primary Reference
(2019) Nucleic Acids Res. Vol. 47: pp. 10388-10399
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P76318
A0A2S5ZH06
Entrez Gene ID
NCBI Entrez Gene ID:
946435
ASD
Information of known allosteric effects of PDB entries
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