Browse entries in the PDBbind-CN Database
HEADER HYDROLASE/PROTEIN BINDING 02-AUG-13 4M0W TITLE CRYSTAL STRUCTURE OF SARS-COV PAPAIN-LIKE PROTEASE C112S MUTANT IN TITLE 2 COMPLEX WITH UBIQUITIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: REPLICASE POLYPROTEIN 1A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: NSP3 PAPAIN-LIKE PROTEASE DOMAIN, UNP RESIDUES 1541-1858; COMPND 5 EC: 3.4.19.12, 3.4.22.69; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: UBIQUITIN; COMPND 10 CHAIN: B SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SARS CORONAVIRUS; SOURCE 3 ORGANISM_COMMON: SARS-COV; SOURCE 4 ORGANISM_TAXID: 227859; SOURCE 5 GENE: 1A, NSP3; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B+; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 13 ORGANISM_COMMON: BOVINE; SOURCE 14 ORGANISM_TAXID: 9913; SOURCE 15 TISSUE: ERYTHROCYTES KEYWDS PAPAIN-LIKE PROTEASE-UBIQUITIN COMPLEX, PROTEIN HYDROLASE AND KEYWDS 2 DEUBIQUITINATION, HYDROLASE-PROTEIN BINDING COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR C.-Y.CHOU,H.-Y.CHEN,H.-Y.LAI,S.-C.CHENG,Y.-W.CHOU REVDAT 2 30-APR-14 4M0W 1 JRNL REVDAT 1 12-FEB-14 4M0W 0 JRNL AUTH C.-Y.CHOU,H.-Y.LAI,H.-Y.CHEN,S.-C.CHENG,K.-W.CHENG,Y.-W.CHOU JRNL TITL STRUCTURAL BASIS FOR CATALYSIS AND UBIQUITIN RECOGNITION BY JRNL TITL 2 THE SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS JRNL TITL 3 PAPAIN-LIKE PROTEASE JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 572 2014 JRNL REFN ISSN 0907-4449 JRNL PMID 24531491 JRNL DOI 10.1107/S1399004713031040 REMARK 2 REMARK 2 RESOLUTION. 1.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0117 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 80733 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.157 REMARK 3 R VALUE (WORKING SET) : 0.156 REMARK 3 FREE R VALUE : 0.180 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4248 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.40 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.48 REMARK 3 REFLECTION IN BIN (WORKING SET) : 11418 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.78 REMARK 3 BIN R VALUE (WORKING SET) : 0.1650 REMARK 3 BIN FREE R VALUE SET COUNT : 581 REMARK 3 BIN FREE R VALUE : 0.2120 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3095 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 46 REMARK 3 SOLVENT ATOMS : 313 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.55 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.52000 REMARK 3 B22 (A**2) : -0.15000 REMARK 3 B33 (A**2) : 0.75000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.38000 REMARK 3 B23 (A**2) : -0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.060 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.054 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.032 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.723 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3292 ; 0.007 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4469 ; 1.380 ; 1.970 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 417 ; 5.291 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 143 ;38.160 ;24.825 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 586 ;11.867 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;13.277 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 513 ; 0.215 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2428 ; 0.005 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3292 ; 1.773 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 79 ;18.564 ; 5.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3456 ; 8.626 ; 5.000 REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN REMARK 3 THE INPUT REMARK 4 REMARK 4 4M0W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-AUG-13. REMARK 100 THE RCSB ID CODE IS RCSB081325. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-NOV-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSRRC REMARK 200 BEAMLINE : BL13C1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.976 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85006 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.39400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300 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: 2FE8, 2HD5 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.37 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3000, 0.1M CHES, PH 9.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 34.15450 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2000 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18320 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 GLU A 2 REMARK 465 LEU A 320 REMARK 465 GLU A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LYS A 280 -134.99 -115.12 REMARK 500 THR A 309 -73.51 -132.25 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 623 DISTANCE = 7.06 ANGSTROMS REMARK 525 HOH A 708 DISTANCE = 9.64 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 401 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 227 SG REMARK 620 2 CYS A 225 SG 105.1 REMARK 620 3 CYS A 190 SG 110.6 113.8 REMARK 620 4 CYS A 193 SG 107.9 105.7 113.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 402 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER A 112 O REMARK 620 2 SER A 116 OG 88.4 REMARK 620 3 TYR A 274 O 107.4 108.5 REMARK 620 4 SER A 115 OG 58.4 116.6 131.3 REMARK 620 5 HOH A 702 O 125.2 111.3 112.9 67.2 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A 404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 101 DBREF 4M0W A 2 319 UNP P0C6U8 R1A_CVHSA 1541 1858 DBREF 4M0W B 1 76 UNP P62992 RS27A_BOVIN 1 76 SEQADV 4M0W MET A 1 UNP P0C6U8 EXPRESSION TAG SEQADV 4M0W SER A 112 UNP P0C6U8 CYS 1651 ENGINEERED MUTATION SEQADV 4M0W LEU A 320 UNP P0C6U8 EXPRESSION TAG SEQADV 4M0W GLU A 321 UNP P0C6U8 EXPRESSION TAG SEQADV 4M0W HIS A 322 UNP P0C6U8 EXPRESSION TAG SEQADV 4M0W HIS A 323 UNP P0C6U8 EXPRESSION TAG SEQADV 4M0W HIS A 324 UNP P0C6U8 EXPRESSION TAG SEQADV 4M0W HIS A 325 UNP P0C6U8 EXPRESSION TAG SEQADV 4M0W HIS A 326 UNP P0C6U8 EXPRESSION TAG SEQADV 4M0W HIS A 327 UNP P0C6U8 EXPRESSION TAG SEQRES 1 A 327 MET GLU VAL LYS THR ILE LYS VAL PHE THR THR VAL ASP SEQRES 2 A 327 ASN THR ASN LEU HIS THR GLN LEU VAL ASP MET SER MET SEQRES 3 A 327 THR TYR GLY GLN GLN PHE GLY PRO THR TYR LEU ASP GLY SEQRES 4 A 327 ALA ASP VAL THR LYS ILE LYS PRO HIS VAL ASN HIS GLU SEQRES 5 A 327 GLY LYS THR PHE PHE VAL LEU PRO SER ASP ASP THR LEU SEQRES 6 A 327 ARG SER GLU ALA PHE GLU TYR TYR HIS THR LEU ASP GLU SEQRES 7 A 327 SER PHE LEU GLY ARG TYR MET SER ALA LEU ASN HIS THR SEQRES 8 A 327 LYS LYS TRP LYS PHE PRO GLN VAL GLY GLY LEU THR SER SEQRES 9 A 327 ILE LYS TRP ALA ASP ASN ASN SER TYR LEU SER SER VAL SEQRES 10 A 327 LEU LEU ALA LEU GLN GLN LEU GLU VAL LYS PHE ASN ALA SEQRES 11 A 327 PRO ALA LEU GLN GLU ALA TYR TYR ARG ALA ARG ALA GLY SEQRES 12 A 327 ASP ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA TYR SER SEQRES 13 A 327 ASN LYS THR VAL GLY GLU LEU GLY ASP VAL ARG GLU THR SEQRES 14 A 327 MET THR HIS LEU LEU GLN HIS ALA ASN LEU GLU SER ALA SEQRES 15 A 327 LYS ARG VAL LEU ASN VAL VAL CYS LYS HIS CYS GLY GLN SEQRES 16 A 327 LYS THR THR THR LEU THR GLY VAL GLU ALA VAL MET TYR SEQRES 17 A 327 MET GLY THR LEU SER TYR ASP ASN LEU LYS THR GLY VAL SEQRES 18 A 327 SER ILE PRO CYS VAL CYS GLY ARG ASP ALA THR GLN TYR SEQRES 19 A 327 LEU VAL GLN GLN GLU SER SER PHE VAL MET MET SER ALA SEQRES 20 A 327 PRO PRO ALA GLU TYR LYS LEU GLN GLN GLY THR PHE LEU SEQRES 21 A 327 CYS ALA ASN GLU TYR THR GLY ASN TYR GLN CYS GLY HIS SEQRES 22 A 327 TYR THR HIS ILE THR ALA LYS GLU THR LEU TYR ARG ILE SEQRES 23 A 327 ASP GLY ALA HIS LEU THR LYS MET SER GLU TYR LYS GLY SEQRES 24 A 327 PRO VAL THR ASP VAL PHE TYR LYS GLU THR SER TYR THR SEQRES 25 A 327 THR THR ILE LYS PRO VAL SER LEU GLU HIS HIS HIS HIS SEQRES 26 A 327 HIS HIS SEQRES 1 B 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 B 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL SEQRES 3 B 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 B 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 B 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 B 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY HET ZN A 401 1 HET NA A 402 1 HET NHE A 403 13 HET NHE A 404 13 HET GOL A 405 6 HET GOL A 406 6 HET GOL B 101 6 HETNAM ZN ZINC ION HETNAM NA SODIUM ION HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID HETNAM GOL GLYCEROL HETSYN NHE N-CYCLOHEXYLTAURINE; CHES HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 ZN ZN 2+ FORMUL 4 NA NA 1+ FORMUL 5 NHE 2(C8 H17 N O3 S) FORMUL 7 GOL 3(C3 H8 O3) FORMUL 10 HOH *313(H2 O) HELIX 1 1 THR A 27 PHE A 32 1 6 HELIX 2 2 HIS A 48 GLU A 52 5 5 HELIX 3 3 ASP A 62 HIS A 74 1 13 HELIX 4 4 SER A 79 LYS A 92 1 14 HELIX 5 5 ASN A 111 GLN A 122 1 12 HELIX 6 6 ALA A 130 ALA A 142 1 13 HELIX 7 7 ALA A 145 ASN A 157 1 13 HELIX 8 8 ASP A 165 GLN A 175 1 11 HELIX 9 9 VAL A 203 ALA A 205 5 3 HELIX 10 10 SER A 213 GLY A 220 1 8 HELIX 11 11 THR B 22 GLY B 35 1 14 HELIX 12 12 LEU B 56 ASN B 60 5 5 SHEET 1 A 5 HIS A 18 ASP A 23 0 SHEET 2 A 5 THR A 5 THR A 11 -1 N ILE A 6 O VAL A 22 SHEET 3 A 5 THR A 55 VAL A 58 1 O PHE A 56 N PHE A 9 SHEET 4 A 5 THR A 35 LEU A 37 -1 N TYR A 36 O PHE A 57 SHEET 5 A 5 ALA A 40 ASP A 41 -1 O ALA A 40 N LEU A 37 SHEET 1 B 2 GLN A 98 VAL A 99 0 SHEET 2 B 2 LEU A 102 THR A 103 -1 O LEU A 102 N VAL A 99 SHEET 1 C 4 GLY A 194 THR A 201 0 SHEET 2 C 4 LYS A 183 CYS A 190 -1 N ARG A 184 O LEU A 200 SHEET 3 C 4 ASP A 230 GLU A 239 -1 O VAL A 236 N VAL A 185 SHEET 4 C 4 VAL A 221 PRO A 224 -1 N ILE A 223 O ALA A 231 SHEET 1 D 4 GLY A 194 THR A 201 0 SHEET 2 D 4 LYS A 183 CYS A 190 -1 N ARG A 184 O LEU A 200 SHEET 3 D 4 ASP A 230 GLU A 239 -1 O VAL A 236 N VAL A 185 SHEET 4 D 4 SER A 310 THR A 312 -1 O TYR A 311 N GLN A 238 SHEET 1 E 7 MET A 207 MET A 209 0 SHEET 2 E 7 PHE A 242 GLN A 255 1 O SER A 246 N TYR A 208 SHEET 3 E 7 GLU A 296 LYS A 307 -1 O TYR A 297 N LEU A 254 SHEET 4 E 7 CYS A 261 GLY A 267 -1 N CYS A 261 O PHE A 305 SHEET 5 E 7 GLY A 272 ALA A 279 -1 O ILE A 277 N ALA A 262 SHEET 6 E 7 LEU A 283 ASP A 287 -1 O ILE A 286 N HIS A 276 SHEET 7 E 7 HIS A 290 MET A 294 -1 O THR A 292 N ARG A 285 SHEET 1 F 5 THR B 12 GLU B 16 0 SHEET 2 F 5 GLN B 2 LYS B 6 -1 N VAL B 5 O ILE B 13 SHEET 3 F 5 THR B 66 LEU B 71 1 O LEU B 67 N LYS B 6 SHEET 4 F 5 GLN B 41 PHE B 45 -1 N ARG B 42 O VAL B 70 SHEET 5 F 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45 LINK SG CYS A 227 ZN ZN A 401 1555 1555 2.24 LINK SG CYS A 225 ZN ZN A 401 1555 1555 2.29 LINK SG CYS A 190 ZN ZN A 401 1555 1555 2.31 LINK SG CYS A 193 ZN ZN A 401 1555 1555 2.35 LINK O SER A 112 NA NA A 402 1555 1555 2.74 LINK OG SER A 116 NA NA A 402 1555 1555 2.82 LINK O TYR A 274 NA NA A 402 1555 1555 2.91 LINK OG ASER A 115 NA NA A 402 1555 1555 2.95 LINK NA NA A 402 O HOH A 702 1555 1555 2.77 SITE 1 AC1 4 CYS A 190 CYS A 193 CYS A 225 CYS A 227 SITE 1 AC2 5 SER A 112 SER A 115 SER A 116 TYR A 274 SITE 2 AC2 5 HOH A 702 SITE 1 AC3 11 LYS A 106 TRP A 107 ASP A 287 GLY A 288 SITE 2 AC3 11 ALA A 289 HIS A 290 THR A 313 ILE A 315 SITE 3 AC3 11 HOH A 520 HOH A 561 HOH A 742 SITE 1 AC4 5 GLN A 123 LEU A 124 GLU A 125 ARG A 141 SITE 2 AC4 5 HOH A 703 SITE 1 AC5 6 HIS A 18 GLN A 20 ASP A 62 THR A 64 SITE 2 AC5 6 LEU A 65 HOH A 639 SITE 1 AC6 6 TYR A 252 LYS A 253 LEU A 254 GLN A 255 SITE 2 AC6 6 THR A 258 TYR A 306 SITE 1 AC7 3 GLU B 24 ASN B 25 ALA B 28 CRYST1 47.464 68.309 68.421 90.00 95.66 90.00 P 1 21 1 2 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 0.021069 0.000000 0.002087 0.00000 SCALE2 0.000000 0.014639 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014687 0.00000 ATOM 1 N VAL A 3 41.930 21.068 0.411 1.00 44.68 N ANISOU 1 N VAL A 3 7633 3408 5936 -961 955 1065 N ATOM 2 CA VAL A 3 41.128 19.976 1.040 1.00 38.34 C ANISOU 2 CA VAL A 3 6139 3265 5159 -1102 18 553 C ATOM 3 C VAL A 3 40.908 18.826 0.057 1.00 39.68 C ANISOU 3 C VAL A 3 6558 4194 4324 -941 -42 432 C ATOM 4 O VAL A 3 40.349 19.017 -1.028 1.00 42.03 O ANISOU 4 O VAL A 3 7173 3746 5050 -1128 -888 437 O ATOM 5 CB VAL A 3 39.766 20.491 1.570 1.00 42.25 C ANISOU 5 CB VAL A 3 6159 4198 5693 -910 -62 143 C ATOM 6 CG1 VAL A 3 38.919 19.346 2.110 1.00 40.22 C ANISOU 6 CG1 VAL A 3 5974 4175 5130 -751 9 51 C ATOM 7 CG2 VAL A 3 39.971 21.546 2.648 1.00 43.65 C ANISOU 7 CG2 VAL A 3 6356 4486 5740 -1086 -449 71 C ATOM 8 N LYS A 4 41.357 17.636 0.448 1.00 32.22 N ANISOU 8 N LYS A 4 4464 3440 4334 -1580 113 -358 N ATOM 9 CA LYS A 4 41.150 16.430 -0.343 1.00 27.21 C ANISOU 9 CA LYS A 4 3926 3135 3275 -1284 619 81 C ATOM 10 C LYS A 4 39.981 15.628 0.227 1.00 22.77 C ANISOU 10 C LYS A 4 3483 2856 2313 -857 405 90 C ATOM 11 O LYS A 4 39.863 15.480 1.446 1.00 23.03 O ANISOU 11 O LYS A 4 3441 3040 2267 -988 280 144 O ATOM 12 CB LYS A 4 42.429 15.591 -0.381 1.00 31.19 C ANISOU 12 CB LYS A 4 3791 4259 3798 -1103 485 -51 C ATOM 13 CG LYS A 4 43.479 16.132 -1.346 1.00 37.42 C ANISOU 13 CG LYS A 4 3976 5118 5121 -1611 871 162 C ATOM 14 CD LYS A 4 44.816 15.422 -1.203 1.00 42.78 C ANISOU 14 CD LYS A 4 5008 5335 5910 -676 332 -45 C ATOM 15 CE LYS A 4 45.716 16.133 -0.204 1.00 46.32 C ANISOU 15 CE LYS A 4 5365 6243 5992 -539 -217 66 C ATOM 16 NZ LYS A 4 47.107 15.606 -0.243 1.00 49.87 N ANISOU 16 NZ LYS A 4 5646 6970 6330 -200 380 547 N ATOM 17 N THR A 5 39.114 15.137 -0.658 1.00 22.88 N ANISOU 17 N THR A 5 3093 2804 2796 -849 290 222 N ATOM 18 CA THR A 5 37.931 14.373 -0.255 1.00 21.20 C ANISOU 18 CA THR A 5 3095 2474 2486 -678 360 192 C ATOM 19 C THR A 5 37.793 13.041 -0.985 1.00 22.27 C ANISOU 19 C THR A 5 3334 2556 2568 -625 464 148 C ATOM 20 O THR A 5 38.278 12.867 -2.105 1.00 26.22 O ANISOU 20 O THR A 5 3889 2949 3122 -892 1046 -187 O ATOM 21 CB THR A 5 36.615 15.167 -0.456 1.00 21.46 C ANISOU 21 CB THR A 5 3344 2377 2432 -752 -272 117 C ATOM 22 OG1 THR A 5 36.480 15.548 -1.831 1.00 25.81 O ANISOU 22 OG1 THR A 5 4086 3162 2559 -724 -682 294 O ATOM 23 CG2 THR A 5 36.561 16.402 0.445 1.00 23.02 C ANISOU 23 CG2 THR A 5 3885 2331 2529 -326 -500 118 C ATOM 24 N ILE A 6 37.137 12.094 -0.329 1.00 22.78 N ANISOU 24 N ILE A 6 3053 2468 3134 -702 441 106 N ATOM 25 CA ILE A 6 36.620 10.929 -1.031 1.00 23.13 C ANISOU 25 CA ILE A 6 2850 2581 3354 -522 531 -192 C ATOM 26 C ILE A 6 35.107 10.854 -0.856 1.00 21.23 C ANISOU 26 C ILE A 6 2865 2385 2813 -295 514 -93 C ATOM 27 O ILE A 6 34.536 11.404 0.093 1.00 21.77 O ANISOU 27 O ILE A 6 2880 2733 2657 -342 522 -190 O ATOM 28 CB ILE A 6 37.283 9.596 -0.613 1.00 28.50 C ANISOU 28 CB ILE A 6 3406 3153 4267 -163 537 265 C ATOM 29 CG1 ILE A 6 37.069 9.324 0.870 1.00 28.30 C ANISOU 29 CG1 ILE A 6 3552 3129 4070 -227 488 102 C ATOM 30 CG2 ILE A 6 38.765 9.570 -0.994 1.00 29.51 C ANISOU 30 CG2 ILE A 6 3607 3889 3714 -541 939 -80 C ATOM 31 CD1 ILE A 6 37.048 7.849 1.200 1.00 31.01 C ANISOU 31 CD1 ILE A 6 3880 2877 5025 -423 358 -385 C ATOM 32 N LYS A 7 34.467 10.180 -1.793 1.00 19.97 N ANISOU 32 N LYS A 7 2825 2567 2196 -335 421 336 N ATOM 33 CA LYS A 7 33.032 10.020 -1.772 1.00 16.94 C ANISOU 33 CA LYS A 7 2754 2329 1350 -215 185 202 C ATOM 34 C LYS A 7 32.666 8.692 -1.127 1.00 16.69 C ANISOU 34 C LYS A 7 2355 2211 1772 -157 318 134 C ATOM 35 O LYS A 7 33.251 7.657 -1.445 1.00 17.85 O ANISOU 35 O LYS A 7 2511 2273 1996 -217 249 -101 O ATOM 36 CB LYS A 7 32.518 10.069 -3.196 1.00 19.70 C ANISOU 36 CB LYS A 7 3169 2784 1530 -114 -122 287 C ATOM 37 CG LYS A 7 31.019 9.953 -3.317 1.00 20.36 C ANISOU 37 CG LYS A 7 3083 3163 1491 119 -267 -61 C ATOM 38 CD LYS A 7 30.673 9.920 -4.785 1.00 24.20 C ANISOU 38 CD LYS A 7 3567 4258 1368 245 -34 43 C ATOM 39 CE LYS A 7 29.236 10.293 -5.011 1.00 21.95 C ANISOU 39 CE LYS A 7 3098 3901 1339 -459 -30 7 C ATOM 40 NZ LYS A 7 29.004 10.564 -6.455 1.00 19.83 N ANISOU 40 NZ LYS A 7 2701 3440 1393 -669 -20 199 N ATOM 41 N VAL A 8 31.720 8.743 -0.195 1.00 14.98 N ANISOU 41 N VAL A 8 2470 1803 1416 -170 261 138 N ATOM 42 CA VAL A 8 31.199 7.545 0.468 1.00 15.13 C ANISOU 42 CA VAL A 8 2454 1829 1463 -214 143 173 C ATOM 43 C VAL A 8 29.687 7.670 0.610 1.00 14.73 C ANISOU 43 C VAL A 8 2463 1763 1371 -318 155 65 C ATOM 44 O VAL A 8 29.118 8.739 0.362 1.00 15.72 O ANISOU 44 O VAL A 8 2531 1804 1638 -228 272 123 O ATOM 45 CB VAL A 8 31.838 7.306 1.863 1.00 15.08 C ANISOU 45 CB VAL A 8 2221 2087 1419 -121 80 -172 C ATOM 46 CG1 VAL A 8 33.357 7.236 1.765 1.00 16.32 C ANISOU 46 CG1 VAL A 8 2234 2165 1799 16 178 29 C ATOM 47 CG2 VAL A 8 31.405 8.365 2.876 1.00 16.53 C ANISOU 47 CG2 VAL A 8 2550 1823 1906 -204 66 -330 C ATOM 48 N PHE A 9 29.046 6.579 1.025 1.00 14.55 N ANISOU 48 N PHE A 9 2314 2013 1201 -420 89 226 N ATOM 49 CA PHE A 9 27.612 6.571 1.267 1.00 14.58 C ANISOU 49 CA PHE A 9 2239 2013 1286 -242 -64 102 C ATOM 50 C PHE A 9 27.371 6.187 2.707 1.00 14.59 C ANISOU 50 C PHE A 9 2110 2062 1368 -284 81 145 C ATOM 51 O PHE A 9 28.032 5.284 3.233 1.00 17.21 O ANISOU 51 O PHE A 9 2726 2090 1721 -49 29 153 O ATOM 52 CB PHE A 9 26.914 5.597 0.313 1.00 15.00 C ANISOU 52 CB PHE A 9 2374 1810 1512 -294 91 -29 C ATOM 53 CG PHE A 9 27.090 5.973 -1.128 1.00 16.41 C ANISOU 53 CG PHE A 9 2765 1859 1610 -154 62 204 C ATOM 54 CD1 PHE A 9 26.262 6.925 -1.711 1.00 17.20 C ANISOU 54 CD1 PHE A 9 2836 2080 1618 -24 6 183 C ATOM 55 CD2 PHE A 9 28.118 5.419 -1.884 1.00 16.32 C ANISOU 55 CD2 PHE A 9 2461 2263 1476 -214 -144 80 C ATOM 56 CE1 PHE A 9 26.439 7.307 -3.035 1.00 18.72 C ANISOU 56 CE1 PHE A 9 3343 2337 1432 -230 -95 -62 C ATOM 57 CE2 PHE A 9 28.296 5.793 -3.212 1.00 17.57 C ANISOU 57 CE2 PHE A 9 2857 2412 1405 -155 -89 -51 C ATOM 58 CZ PHE A 9 27.459 6.739 -3.781 1.00 18.39 C ANISOU 58 CZ PHE A 9 3124 2226 1637 -186 -68 130 C ATOM 59 N THR A 10 26.450 6.893 3.354 1.00 13.80 N ANISOU 59 N THR A 10 2303 1667 1270 -233 81 334 N ATOM 60 CA THR A 10 26.082 6.543 4.721 1.00 13.53 C ANISOU 60 CA THR A 10 2220 1752 1167 -196 22 219 C ATOM 61 C THR A 10 24.666 6.001 4.754 1.00 13.92 C ANISOU 61 C THR A 10 2218 1764 1304 -202 63 405 C ATOM 62 O THR A 10 23.836 6.312 3.890 1.00 14.77 O ANISOU 62 O THR A 10 2347 1775 1488 -139 -79 363 O ATOM 63 CB THR A 10 26.183 7.733 5.684 1.00 14.01 C ANISOU 63 CB THR A 10 1944 1735 1644 -92 35 37 C ATOM 64 OG1 THR A 10 25.379 8.809 5.191 1.00 15.39 O ANISOU 64 OG1 THR A 10 2317 2006 1525 -79 -121 354 O ATOM 65 CG2 THR A 10 27.633 8.177 5.842 1.00 14.69 C ANISOU 65 CG2 THR A 10 2103 1807 1672 -404 75 -14 C ATOM 66 N THR A 11 24.391 5.182 5.759 1.00 13.82 N ANISOU 66 N THR A 11 2120 1469 1661 -240 79 496 N ATOM 67 CA THR A 11 23.085 4.549 5.854 1.00 13.64 C ANISOU 67 CA THR A 11 2077 1849 1256 -303 83 257 C ATOM 68 C THR A 11 22.804 4.139 7.284 1.00 13.20 C ANISOU 68 C THR A 11 2020 1711 1285 -255 99 285 C ATOM 69 O THR A 11 23.738 3.916 8.061 1.00 14.96 O ANISOU 69 O THR A 11 2165 1941 1579 -279 -95 267 O ATOM 70 CB THR A 11 22.989 3.320 4.914 1.00 14.64 C ANISOU 70 CB THR A 11 2139 1797 1624 -172 1 130 C ATOM 71 OG1 THR A 11 21.620 2.926 4.760 1.00 14.99 O ANISOU 71 OG1 THR A 11 2164 1952 1580 -280 64 209 O ATOM 72 CG2 THR A 11 23.809 2.136 5.435 1.00 15.72 C ANISOU 72 CG2 THR A 11 2259 1856 1857 -103 -20 163 C ATOM 73 N VAL A 12 21.519 4.025 7.609 1.00 13.94 N ANISOU 73 N VAL A 12 2061 1641 1592 -60 222 145 N ATOM 74 CA VAL A 12 21.102 3.316 8.825 1.00 14.83 C ANISOU 74 CA VAL A 12 2112 1730 1793 -61 311 296 C ATOM 75 C VAL A 12 20.307 2.050 8.518 1.00 15.17 C ANISOU 75 C VAL A 12 2064 1755 1941 -53 276 312 C ATOM 76 O VAL A 12 20.100 1.227 9.403 1.00 16.23 O ANISOU 76 O VAL A 12 2347 1751 2068 -158 193 449 O ATOM 77 CB VAL A 12 20.306 4.212 9.805 1.00 15.83 C ANISOU 77 CB VAL A 12 2172 1900 1942 56 150 70 C ATOM 78 CG1 VAL A 12 21.167 5.374 10.280 1.00 17.73 C ANISOU 78 CG1 VAL A 12 2552 2104 2077 -242 19 55 C ATOM 79 CG2 VAL A 12 18.998 4.698 9.189 1.00 16.34 C ANISOU 79 CG2 VAL A 12 2372 2091 1742 258 26 1 C ATOM 80 N ASP A 13 19.879 1.877 7.272 1.00 16.39 N ANISOU 80 N ASP A 13 2445 1704 2076 -390 99 232 N ATOM 81 CA ASP A 13 18.994 0.754 6.930 1.00 17.88 C ANISOU 81 CA ASP A 13 2459 1929 2404 -531 171 129 C ATOM 82 C ASP A 13 19.463 -0.113 5.750 1.00 19.31 C ANISOU 82 C ASP A 13 2975 2121 2239 -535 13 15 C ATOM 83 O ASP A 13 18.779 -1.064 5.360 1.00 22.88 O ANISOU 83 O ASP A 13 3488 2084 3120 -1050 296 236 O ATOM 84 CB ASP A 13 17.555 1.254 6.719 1.00 18.42 C ANISOU 84 CB ASP A 13 2613 2143 2240 -321 85 205 C ATOM 85 CG ASP A 13 17.422 2.219 5.555 1.00 19.12 C ANISOU 85 CG ASP A 13 2629 2232 2402 -126 222 312 C ATOM 86 OD1 ASP A 13 18.316 2.245 4.676 1.00 20.03 O ANISOU 86 OD1 ASP A 13 2675 2514 2422 -70 304 495 O ATOM 87 OD2 ASP A 13 16.407 2.950 5.517 1.00 19.54 O ANISOU 87 OD2 ASP A 13 2487 2470 2466 -158 134 385 O ATOM 88 N ASN A 14 20.631 0.227 5.204 1.00 19.16 N ANISOU 88 N ASN A 14 2810 2006 2465 -124 140 -2 N ATOM 89 CA ASN A 14 21.222 -0.419 4.014 1.00 20.82 C ANISOU 89 CA ASN A 14 2964 2340 2607 -242 125 -277 C ATOM 90 C ASN A 14 20.393 -0.348 2.716 1.00 22.07 C ANISOU 90 C ASN A 14 3324 2509 2550 -395 28 -325 C ATOM 91 O ASN A 14 20.727 -1.021 1.729 1.00 25.03 O ANISOU 91 O ASN A 14 3904 3235 2369 -211 18 -507 O ATOM 92 CB ASN A 14 21.698 -1.856 4.300 1.00 25.61 C ANISOU 92 CB ASN A 14 3854 2702 3173 268 -261 -128 C ATOM 93 CG ASN A 14 22.909 -2.243 3.462 1.00 30.06 C ANISOU 93 CG ASN A 14 4001 3441 3978 55 158 -264 C ATOM 94 OD1 ASN A 14 23.840 -1.448 3.278 1.00 33.59 O ANISOU 94 OD1 ASN A 14 3685 4049 5025 127 902 -709 O ATOM 95 ND2 ASN A 14 22.901 -3.465 2.942 1.00 36.48 N ANISOU 95 ND2 ASN A 14 5171 3449 5239 454 42 -399 N ATOM 96 N THR A 15 19.325 0.453 2.723 1.00 21.53 N ANISOU 96 N THR A 15 2867 2664 2648 -670 27 160 N ATOM 97 CA ATHR A 15 18.492 0.670 1.539 0.50 23.00 C ANISOU 97 CA ATHR A 15 2956 2811 2971 -620 -162 376 C ATOM 98 CA BTHR A 15 18.529 0.672 1.513 0.50 22.88 C ANISOU 98 CA BTHR A 15 3034 2786 2870 -538 -124 277 C ATOM 99 C THR A 15 18.576 2.135 1.105 1.00 22.34 C ANISOU 99 C THR A 15 3044 2853 2591 -594 -111 371 C ATOM 100 O THR A 15 18.831 2.442 -0.058 1.00 24.38 O ANISOU 100 O THR A 15 3976 3076 2207 -576 -282 80 O ATOM 101 CB ATHR A 15 17.022 0.283 1.812 0.50 23.85 C ANISOU 101 CB ATHR A 15 3117 2681 3262 -766 1 637 C ATOM 102 CB BTHR A 15 17.062 0.213 1.657 0.50 24.52 C ANISOU 102 CB BTHR A 15 3157 2879 3278 -660 100 258 C ATOM 103 OG1ATHR A 15 16.956 -1.086 2.232 0.50 28.44 O ANISOU 103 OG1ATHR A 15 3598 2835 4371 -1189 -84 1014 O ATOM 104 OG1BTHR A 15 16.484 0.803 2.827 0.50 27.41 O ANISOU 104 OG1BTHR A 15 3479 3260 3673 -513 344 21 O ATOM 105 CG2ATHR A 15 16.165 0.473 0.565 0.50 24.57 C ANISOU 105 CG2ATHR A 15 3151 2587 3595 -669 -302 471 C ATOM 106 CG2BTHR A 15 16.973 -1.311 1.740 0.50 25.52 C ANISOU 106 CG2BTHR A 15 3590 2851 3253 -743 42 -71 C ATOM 107 N ASN A 16 18.343 3.031 2.061 1.00 19.58 N ANISOU 107 N ASN A 16 2457 2350 2629 -677 -160 557 N ATOM 108 CA ASN A 16 18.467 4.458 1.830 1.00 18.01 C ANISOU 108 CA ASN A 16 2462 2371 2007 -393 -348 666 C ATOM 109 C ASN A 16 19.911 4.874 2.066 1.00 18.53 C ANISOU 109 C ASN A 16 2480 2428 2131 -443 -253 685 C ATOM 110 O ASN A 16 20.402 4.860 3.198 1.00 16.90 O ANISOU 110 O ASN A 16 2207 2263 1950 -322 -60 254 O ATOM 111 CB ASN A 16 17.512 5.229 2.736 1.00 21.39 C ANISOU 111 CB ASN A 16 2413 2872 2842 17 -219 621 C ATOM 112 CG ASN A 16 16.061 4.989 2.381 1.00 23.02 C ANISOU 112 CG ASN A 16 2627 3525 2594 -162 -484 559 C ATOM 113 OD1 ASN A 16 15.595 5.410 1.320 1.00 27.60 O ANISOU 113 OD1 ASN A 16 3066 4254 3165 74 -747 1096 O ATOM 114 ND2 ASN A 16 15.336 4.314 3.264 1.00 24.47 N ANISOU 114 ND2 ASN A 16 2492 3321 3482 -329 -158 461 N ATOM 115 N LEU A 17 20.589 5.202 0.976 1.00 16.59 N ANISOU 115 N LEU A 17 2363 2036 1905 -212 -278 541 N ATOM 116 CA LEU A 17 21.994 5.597 1.008 1.00 16.24 C ANISOU 116 CA LEU A 17 2359 2130 1678 -175 -78 289 C ATOM 117 C LEU A 17 22.116 7.095 0.805 1.00 16.72 C ANISOU 117 C LEU A 17 2633 2137 1582 -224 -80 326 C ATOM 118 O LEU A 17 21.460 7.672 -0.074 1.00 19.37 O ANISOU 118 O LEU A 17 2918 2584 1857 -149 -300 461 O ATOM 119 CB LEU A 17 22.787 4.852 -0.068 1.00 18.54 C ANISOU 119 CB LEU A 17 2939 2500 1604 -140 141 253 C ATOM 120 CG LEU A 17 22.603 3.330 -0.127 1.00 21.13 C ANISOU 120 CG LEU A 17 3124 2465 2437 184 176 145 C ATOM 121 CD1 LEU A 17 23.403 2.764 -1.285 1.00 21.80 C ANISOU 121 CD1 LEU A 17 3358 2857 2068 247 64 77 C ATOM 122 CD2 LEU A 17 22.971 2.631 1.178 1.00 20.20 C ANISOU 122 CD2 LEU A 17 2950 2401 2323 -159 82 64 C ATOM 123 N HIS A 18 22.959 7.712 1.625 1.00 15.30 N ANISOU 123 N HIS A 18 2401 1786 1626 -176 30 412 N ATOM 124 CA HIS A 18 23.148 9.154 1.612 1.00 14.76 C ANISOU 124 CA HIS A 18 2104 1802 1702 -109 175 245 C ATOM 125 C HIS A 18 24.527 9.499 1.127 1.00 13.81 C ANISOU 125 C HIS A 18 2092 1537 1616 -192 143 262 C ATOM 126 O HIS A 18 25.524 9.087 1.702 1.00 15.08 O ANISOU 126 O HIS A 18 2258 1811 1660 -181 27 366 O ATOM 127 CB HIS A 18 22.862 9.707 2.999 1.00 15.94 C ANISOU 127 CB HIS A 18 2213 1942 1901 -179 290 37 C ATOM 128 CG HIS A 18 21.453 9.417 3.466 1.00 17.04 C ANISOU 128 CG HIS A 18 2211 2048 2215 -155 358 247 C ATOM 129 ND1 HIS A 18 20.383 10.097 3.009 1.00 20.08 N ANISOU 129 ND1 HIS A 18 2452 2511 2664 -92 201 625 N ATOM 130 CD2 HIS A 18 20.959 8.450 4.336 1.00 15.91 C ANISOU 130 CD2 HIS A 18 2178 1795 2072 48 371 161 C ATOM 131 CE1 HIS A 18 19.264 9.607 3.577 1.00 19.22 C ANISOU 131 CE1 HIS A 18 2513 2370 2418 30 273 592 C ATOM 132 NE2 HIS A 18 19.617 8.595 4.382 1.00 18.23 N ANISOU 132 NE2 HIS A 18 2191 2083 2651 107 207 451 N ATOM 133 N THR A 19 24.596 10.248 0.034 1.00 15.36 N ANISOU 133 N THR A 19 2563 1683 1590 -210 72 271 N ATOM 134 CA THR A 19 25.880 10.588 -0.565 1.00 15.99 C ANISOU 134 CA THR A 19 2448 1976 1650 -286 -40 303 C ATOM 135 C THR A 19 26.629 11.582 0.311 1.00 15.26 C ANISOU 135 C THR A 19 2344 1900 1553 -287 57 327 C ATOM 136 O THR A 19 26.046 12.574 0.769 1.00 17.05 O ANISOU 136 O THR A 19 2470 2071 1937 -160 143 229 O ATOM 137 CB THR A 19 25.660 11.199 -1.954 1.00 16.75 C ANISOU 137 CB THR A 19 2583 2021 1757 -328 48 470 C ATOM 138 OG1 THR A 19 24.734 10.378 -2.676 1.00 19.37 O ANISOU 138 OG1 THR A 19 3240 2321 1798 -702 28 218 O ATOM 139 CG2 THR A 19 26.969 11.301 -2.731 1.00 19.39 C ANISOU 139 CG2 THR A 19 2893 2587 1884 -311 364 253 C ATOM 140 N GLN A 20 27.913 11.311 0.542 1.00 15.36 N ANISOU 140 N GLN A 20 2329 1851 1655 -309 107 186 N ATOM 141 CA GLN A 20 28.774 12.186 1.353 1.00 16.04 C ANISOU 141 CA GLN A 20 2431 1868 1793 -363 -74 323 C ATOM 142 C GLN A 20 30.135 12.391 0.721 1.00 16.68 C ANISOU 142 C GLN A 20 2591 1934 1810 -347 153 98 C ATOM 143 O GLN A 20 30.678 11.483 0.090 1.00 18.10 O ANISOU 143 O GLN A 20 2679 1788 2409 -328 196 43 O ATOM 144 CB GLN A 20 29.027 11.566 2.730 1.00 16.54 C ANISOU 144 CB GLN A 20 2576 2234 1471 -322 160 140 C ATOM 145 CG GLN A 20 27.800 11.079 3.469 1.00 17.25 C ANISOU 145 CG GLN A 20 2614 2369 1571 -422 203 205 C ATOM 146 CD GLN A 20 26.875 12.190 3.922 1.00 18.93 C ANISOU 146 CD GLN A 20 2997 2328 1865 -337 381 256 C ATOM 147 OE1 GLN A 20 27.237 13.380 3.940 1.00 20.64 O ANISOU 147 OE1 GLN A 20 3420 2165 2256 -117 284 -182 O ATOM 148 NE2 GLN A 20 25.667 11.803 4.316 1.00 22.60 N ANISOU 148 NE2 GLN A 20 3213 3138 2234 -809 444 120 N ATOM 149 N LEU A 21 30.691 13.585 0.911 1.00 16.50 N ANISOU 149 N LEU A 21 2585 2007 1676 -510 -152 380 N ATOM 150 CA LEU A 21 32.095 13.834 0.610 1.00 16.33 C ANISOU 150 CA LEU A 21 2638 2073 1491 -371 -101 430 C ATOM 151 C LEU A 21 32.805 14.063 1.935 1.00 17.27 C ANISOU 151 C LEU A 21 2585 2333 1642 -367 -192 296 C ATOM 152 O LEU A 21 32.431 14.959 2.698 1.00 21.62 O ANISOU 152 O LEU A 21 3447 2944 1823 56 -233 86 O ATOM 153 CB LEU A 21 32.250 15.052 -0.308 1.00 17.12 C ANISOU 153 CB LEU A 21 3129 1849 1523 -378 -176 312 C ATOM 154 CG LEU A 21 31.567 14.940 -1.676 1.00 17.75 C ANISOU 154 CG LEU A 21 3542 1702 1500 -360 -249 278 C ATOM 155 CD1 LEU A 21 31.847 16.199 -2.471 1.00 20.04 C ANISOU 155 CD1 LEU A 21 4085 1791 1736 -285 85 421 C ATOM 156 CD2 LEU A 21 31.993 13.705 -2.464 1.00 19.83 C ANISOU 156 CD2 LEU A 21 4168 1932 1431 -247 -185 172 C ATOM 157 N VAL A 22 33.816 13.245 2.211 1.00 16.67 N ANISOU 157 N VAL A 22 2287 2441 1604 -496 -72 284 N ATOM 158 CA VAL A 22 34.530 13.337 3.485 1.00 17.52 C ANISOU 158 CA VAL A 22 2333 2571 1751 -481 -198 375 C ATOM 159 C VAL A 22 35.959 13.826 3.303 1.00 17.83 C ANISOU 159 C VAL A 22 2336 2290 2148 -381 133 189 C ATOM 160 O VAL A 22 36.649 13.453 2.356 1.00 19.20 O ANISOU 160 O VAL A 22 2492 2623 2178 -518 345 304 O ATOM 161 CB VAL A 22 34.527 12.008 4.274 1.00 18.42 C ANISOU 161 CB VAL A 22 2448 2462 2086 -187 187 336 C ATOM 162 CG1 VAL A 22 33.154 11.763 4.875 1.00 21.14 C ANISOU 162 CG1 VAL A 22 2386 3116 2530 -603 103 309 C ATOM 163 CG2 VAL A 22 34.957 10.841 3.397 1.00 19.02 C ANISOU 163 CG2 VAL A 22 2656 2486 2082 -340 240 174 C ATOM 164 N ASP A 23 36.371 14.679 4.229 1.00 18.13 N ANISOU 164 N ASP A 23 2668 2396 1825 -456 -32 372 N ATOM 165 CA ASP A 23 37.695 15.273 4.264 1.00 18.89 C ANISOU 165 CA ASP A 23 2619 2565 1990 -421 14 256 C ATOM 166 C ASP A 23 38.680 14.225 4.789 1.00 20.00 C ANISOU 166 C ASP A 23 2658 2689 2251 -398 179 524 C ATOM 167 O ASP A 23 38.488 13.667 5.875 1.00 19.91 O ANISOU 167 O ASP A 23 3050 2463 2051 -622 130 322 O ATOM 168 CB ASP A 23 37.628 16.494 5.191 1.00 20.68 C ANISOU 168 CB ASP A 23 2989 2410 2454 -420 -214 124 C ATOM 169 CG ASP A 23 38.903 17.321 5.212 1.00 23.05 C ANISOU 169 CG ASP A 23 3059 2452 3243 -481 -162 215 C ATOM 170 OD1 ASP A 23 40.010 16.779 5.012 1.00 22.22 O ANISOU 170 OD1 ASP A 23 2852 2836 2755 -705 46 466 O ATOM 171 OD2 ASP A 23 38.778 18.536 5.471 1.00 26.77 O ANISOU 171 OD2 ASP A 23 3517 2476 4175 -428 -72 16 O ATOM 172 N MET A 24 39.735 13.976 4.012 1.00 19.63 N ANISOU 172 N MET A 24 2612 2845 2001 -514 73 301 N ATOM 173 CA AMET A 24 40.763 12.981 4.339 0.50 22.20 C ANISOU 173 CA AMET A 24 2945 2871 2617 -329 35 113 C ATOM 174 CA BMET A 24 40.732 12.968 4.369 0.50 21.64 C ANISOU 174 CA BMET A 24 2728 3299 2194 -59 323 18 C ATOM 175 C MET A 24 41.555 13.346 5.599 1.00 20.67 C ANISOU 175 C MET A 24 2654 2942 2255 -536 302 340 C ATOM 176 O MET A 24 42.185 12.485 6.221 1.00 22.54 O ANISOU 176 O MET A 24 2584 3046 2931 -385 131 185 O ATOM 177 CB AMET A 24 41.727 12.791 3.158 0.50 25.19 C ANISOU 177 CB AMET A 24 3289 3320 2961 -523 391 203 C ATOM 178 CB BMET A 24 41.644 12.676 3.182 0.50 23.08 C ANISOU 178 CB BMET A 24 2774 4230 1765 276 37 84 C ATOM 179 CG AMET A 24 41.062 12.439 1.833 0.50 29.59 C ANISOU 179 CG AMET A 24 4033 3803 3404 -698 -119 99 C ATOM 180 CG BMET A 24 40.902 12.107 1.989 0.50 23.47 C ANISOU 180 CG BMET A 24 2619 5166 1132 1160 81 24 C ATOM 181 SD AMET A 24 40.374 10.773 1.777 0.50 33.24 S ANISOU 181 SD AMET A 24 4322 3966 4339 -826 -270 -391 S ATOM 182 SD BMET A 24 42.039 11.510 0.737 0.50 30.07 S ANISOU 182 SD BMET A 24 3488 6145 1789 1115 1050 -194 S ATOM 183 CE AMET A 24 41.836 9.811 1.398 0.50 33.68 C ANISOU 183 CE AMET A 24 4847 3618 4331 -548 -26 -281 C ATOM 184 CE BMET A 24 42.992 10.308 1.663 0.50 31.18 C ANISOU 184 CE BMET A 24 3510 5553 2783 1346 825 -792 C ATOM 185 N SER A 25 41.528 14.626 5.968 1.00 20.79 N ANISOU 185 N SER A 25 2454 2952 2494 -694 165 244 N ATOM 186 CA SER A 25 42.296 15.107 7.117 1.00 21.07 C ANISOU 186 CA SER A 25 2842 2768 2395 -657 87 290 C ATOM 187 C SER A 25 41.538 14.995 8.439 1.00 19.64 C ANISOU 187 C SER A 25 2578 2631 2250 -692 -21 103 C ATOM 188 O SER A 25 42.097 15.296 9.498 1.00 21.67 O ANISOU 188 O SER A 25 2649 3038 2546 -730 -353 122 O ATOM 189 CB SER A 25 42.758 16.555 6.903 1.00 22.41 C ANISOU 189 CB SER A 25 2922 2937 2655 -927 221 466 C ATOM 190 OG SER A 25 41.693 17.476 7.121 1.00 22.72 O ANISOU 190 OG SER A 25 3399 2634 2597 -921 -133 221 O ATOM 191 N MET A 26 40.276 14.564 8.376 1.00 18.76 N ANISOU 191 N MET A 26 2425 2704 1997 -466 56 254 N ATOM 192 CA MET A 26 39.433 14.447 9.570 1.00 18.15 C ANISOU 192 CA MET A 26 2578 2413 1902 -334 67 77 C ATOM 193 C MET A 26 38.998 13.006 9.773 1.00 17.10 C ANISOU 193 C MET A 26 2286 2447 1763 -287 137 222 C ATOM 194 O MET A 26 38.820 12.266 8.815 1.00 18.72 O ANISOU 194 O MET A 26 2686 2404 2022 -419 218 30 O ATOM 195 CB MET A 26 38.198 15.353 9.470 1.00 18.74 C ANISOU 195 CB MET A 26 2583 2224 2310 -471 -85 91 C ATOM 196 CG MET A 26 38.522 16.836 9.353 1.00 21.32 C ANISOU 196 CG MET A 26 3095 2276 2728 -627 -19 311 C ATOM 197 SD MET A 26 37.096 17.826 8.849 1.00 26.01 S ANISOU 197 SD MET A 26 3742 2733 3407 -239 -399 305 S ATOM 198 CE MET A 26 36.182 17.912 10.385 1.00 27.41 C ANISOU 198 CE MET A 26 4999 2753 2662 -329 -496 -87 C ATOM 199 N THR A 27 38.827 12.606 11.028 1.00 17.04 N ANISOU 199 N THR A 27 2476 2224 1772 -339 60 210 N ATOM 200 CA THR A 27 38.316 11.266 11.322 1.00 16.84 C ANISOU 200 CA THR A 27 2226 2180 1990 -281 -112 327 C ATOM 201 C THR A 27 36.852 11.130 10.887 1.00 16.44 C ANISOU 201 C THR A 27 2306 2120 1819 -186 -209 52 C ATOM 202 O THR A 27 36.142 12.130 10.731 1.00 16.13 O ANISOU 202 O THR A 27 2377 2005 1743 -282 -111 341 O ATOM 203 CB THR A 27 38.400 10.950 12.824 1.00 17.13 C ANISOU 203 CB THR A 27 2356 2312 1840 -333 -181 -25 C ATOM 204 OG1 THR A 27 37.504 11.815 13.533 1.00 18.54 O ANISOU 204 OG1 THR A 27 2547 2444 2051 -218 -12 46 O ATOM 205 CG2 THR A 27 39.819 11.154 13.333 1.00 20.58 C ANISOU 205 CG2 THR A 27 2407 3022 2390 -18 -502 208 C ATOM 206 N TYR A 28 36.377 9.897 10.736 1.00 15.97 N ANISOU 206 N TYR A 28 2256 2246 1564 -328 -225 198 N ATOM 207 CA TYR A 28 34.942 9.705 10.529 1.00 15.57 C ANISOU 207 CA TYR A 28 2169 2022 1723 -318 15 0 C ATOM 208 C TYR A 28 34.142 10.256 11.715 1.00 15.21 C ANISOU 208 C TYR A 28 2196 2100 1481 -256 76 293 C ATOM 209 O TYR A 28 33.077 10.832 11.524 1.00 16.12 O ANISOU 209 O TYR A 28 2187 2051 1886 -282 -7 -30 O ATOM 210 CB TYR A 28 34.594 8.243 10.243 1.00 16.00 C ANISOU 210 CB TYR A 28 2522 1749 1807 -46 161 192 C ATOM 211 CG TYR A 28 34.965 7.821 8.844 1.00 16.13 C ANISOU 211 CG TYR A 28 2259 2084 1783 -339 133 130 C ATOM 212 CD1 TYR A 28 36.088 7.030 8.603 1.00 16.59 C ANISOU 212 CD1 TYR A 28 2181 2128 1993 -373 107 107 C ATOM 213 CD2 TYR A 28 34.203 8.240 7.748 1.00 16.53 C ANISOU 213 CD2 TYR A 28 2250 2097 1933 -316 -10 116 C ATOM 214 CE1 TYR A 28 36.438 6.661 7.314 1.00 17.67 C ANISOU 214 CE1 TYR A 28 2645 2017 2051 -269 0 -159 C ATOM 215 CE2 TYR A 28 34.537 7.870 6.453 1.00 16.79 C ANISOU 215 CE2 TYR A 28 2229 1827 2321 -327 285 -227 C ATOM 216 CZ TYR A 28 35.657 7.089 6.239 1.00 16.65 C ANISOU 216 CZ TYR A 28 2481 1979 1867 -79 274 -165 C ATOM 217 OH TYR A 28 35.993 6.730 4.953 1.00 18.87 O ANISOU 217 OH TYR A 28 2849 2440 1878 -374 401 -266 O ATOM 218 N GLY A 29 34.682 10.117 12.931 1.00 16.23 N ANISOU 218 N GLY A 29 2240 2160 1767 -342 -258 267 N ATOM 219 CA GLY A 29 34.042 10.668 14.130 1.00 17.89 C ANISOU 219 CA GLY A 29 2694 2356 1747 -377 -93 251 C ATOM 220 C GLY A 29 33.808 12.170 14.102 1.00 16.33 C ANISOU 220 C GLY A 29 2386 2359 1459 -400 6 75 C ATOM 221 O GLY A 29 32.798 12.657 14.624 1.00 16.81 O ANISOU 221 O GLY A 29 2500 2498 1385 -507 100 8 O ATOM 222 N GLN A 30 34.740 12.904 13.483 1.00 16.92 N ANISOU 222 N GLN A 30 2500 2444 1483 -479 -7 174 N ATOM 223 CA GLN A 30 34.612 14.350 13.284 1.00 17.15 C ANISOU 223 CA GLN A 30 2304 2479 1732 -306 -81 86 C ATOM 224 C GLN A 30 33.551 14.720 12.259 1.00 16.30 C ANISOU 224 C GLN A 30 2397 2157 1636 -280 -141 -75 C ATOM 225 O GLN A 30 33.113 15.874 12.197 1.00 20.09 O ANISOU 225 O GLN A 30 2904 2498 2230 138 -520 -263 O ATOM 226 CB GLN A 30 35.937 14.935 12.796 1.00 15.74 C ANISOU 226 CB GLN A 30 2298 2061 1618 -365 -195 67 C ATOM 227 CG GLN A 30 36.955 15.202 13.884 1.00 17.34 C ANISOU 227 CG GLN A 30 2182 2468 1939 -551 -266 36 C ATOM 228 CD GLN A 30 38.239 15.767 13.315 1.00 17.82 C ANISOU 228 CD GLN A 30 2329 2349 2094 -622 -71 -168 C ATOM 229 OE1 GLN A 30 38.459 16.984 13.319 1.00 21.60 O ANISOU 229 OE1 GLN A 30 3026 2340 2841 -610 -68 -364 O ATOM 230 NE2 GLN A 30 39.091 14.891 12.820 1.00 17.08 N ANISOU 230 NE2 GLN A 30 2162 2474 1852 -483 -37 137 N ATOM 231 N GLN A 31 33.160 13.754 11.431 1.00 17.21 N ANISOU 231 N GLN A 31 2524 2305 1711 -337 -250 -99 N ATOM 232 CA GLN A 31 32.310 14.048 10.287 1.00 16.04 C ANISOU 232 CA GLN A 31 2364 2145 1585 -380 -148 -266 C ATOM 233 C GLN A 31 30.907 13.464 10.434 1.00 16.28 C ANISOU 233 C GLN A 31 2312 2086 1784 -355 -323 -312 C ATOM 234 O GLN A 31 29.918 14.186 10.315 1.00 21.16 O ANISOU 234 O GLN A 31 2733 1996 3307 -178 -504 -159 O ATOM 235 CB GLN A 31 33.019 13.624 8.997 1.00 17.18 C ANISOU 235 CB GLN A 31 2568 2287 1673 -185 9 -129 C ATOM 236 CG GLN A 31 34.371 14.324 8.874 1.00 18.59 C ANISOU 236 CG GLN A 31 2490 2593 1981 -87 87 156 C ATOM 237 CD GLN A 31 35.101 14.042 7.587 1.00 17.82 C ANISOU 237 CD GLN A 31 2574 2255 1942 28 32 140 C ATOM 238 OE1 GLN A 31 34.795 14.636 6.564 1.00 19.45 O ANISOU 238 OE1 GLN A 31 2998 2436 1954 96 -60 172 O ATOM 239 NE2 GLN A 31 36.103 13.160 7.640 1.00 16.96 N ANISOU 239 NE2 GLN A 31 2585 1924 1932 -139 -140 141 N ATOM 240 N PHE A 32 30.826 12.172 10.736 1.00 16.72 N ANISOU 240 N PHE A 32 2451 2006 1894 -434 -167 -334 N ATOM 241 CA PHE A 32 29.534 11.500 10.926 1.00 16.73 C ANISOU 241 CA PHE A 32 2346 1933 2076 -340 -166 -340 C ATOM 242 C PHE A 32 29.220 11.153 12.379 1.00 18.34 C ANISOU 242 C PHE A 32 2375 2631 1959 -335 -144 -583 C ATOM 243 O PHE A 32 28.079 10.805 12.707 1.00 20.17 O ANISOU 243 O PHE A 32 2584 3051 2028 -620 10 -354 O ATOM 244 CB PHE A 32 29.496 10.175 10.160 1.00 16.74 C ANISOU 244 CB PHE A 32 2604 2025 1729 -383 -37 -328 C ATOM 245 CG PHE A 32 29.832 10.269 8.693 1.00 16.81 C ANISOU 245 CG PHE A 32 2668 2130 1586 -321 -365 -83 C ATOM 246 CD1 PHE A 32 29.429 11.355 7.909 1.00 17.09 C ANISOU 246 CD1 PHE A 32 2910 1963 1616 -311 -320 -216 C ATOM 247 CD2 PHE A 32 30.516 9.219 8.084 1.00 17.33 C ANISOU 247 CD2 PHE A 32 2369 2341 1873 -286 48 48 C ATOM 248 CE1 PHE A 32 29.734 11.393 6.554 1.00 17.35 C ANISOU 248 CE1 PHE A 32 2856 1908 1827 -364 89 90 C ATOM 249 CE2 PHE A 32 30.814 9.246 6.730 1.00 17.19 C ANISOU 249 CE2 PHE A 32 2421 2241 1869 -258 -34 245 C ATOM 250 CZ PHE A 32 30.424 10.338 5.966 1.00 16.28 C ANISOU 250 CZ PHE A 32 2372 2147 1664 -274 -109 113 C ATOM 251 N GLY A 33 30.225 11.202 13.245 1.00 17.20 N ANISOU 251 N GLY A 33 2559 2238 1737 -360 -179 -188 N ATOM 252 CA GLY A 33 30.107 10.571 14.555 1.00 18.93 C ANISOU 252 CA GLY A 33 2846 2625 1719 -449 -3 -116 C ATOM 253 C GLY A 33 30.424 9.090 14.407 1.00 17.99 C ANISOU 253 C GLY A 33 2677 2498 1660 -764 -195 3 C ATOM 254 O GLY A 33 31.199 8.709 13.526 1.00 18.16 O ANISOU 254 O GLY A 33 2729 2373 1796 -759 -61 102 O ATOM 255 N PRO A 34 29.835 8.236 15.260 1.00 19.50 N ANISOU 255 N PRO A 34 3190 2701 1518 -891 -40 -60 N ATOM 256 CA PRO A 34 30.124 6.803 15.147 1.00 19.01 C ANISOU 256 CA PRO A 34 3119 2650 1451 -695 -110 255 C ATOM 257 C PRO A 34 29.849 6.244 13.750 1.00 18.14 C ANISOU 257 C PRO A 34 2783 2518 1589 -599 -89 156 C ATOM 258 O PRO A 34 28.759 6.431 13.210 1.00 19.22 O ANISOU 258 O PRO A 34 2609 2588 2105 -684 -66 -12 O ATOM 259 CB PRO A 34 29.200 6.172 16.196 1.00 22.81 C ANISOU 259 CB PRO A 34 3758 2905 2003 -882 340 366 C ATOM 260 CG PRO A 34 28.982 7.259 17.187 1.00 25.80 C ANISOU 260 CG PRO A 34 4276 2991 2534 -921 159 97 C ATOM 261 CD PRO A 34 28.959 8.537 16.409 1.00 22.34 C ANISOU 261 CD PRO A 34 3877 3056 1554 -837 223 -160 C ATOM 262 N THR A 35 30.853 5.578 13.188 1.00 17.02 N ANISOU 262 N THR A 35 2803 2157 1506 -556 -170 176 N ATOM 263 CA THR A 35 30.841 5.135 11.788 1.00 15.66 C ANISOU 263 CA THR A 35 2495 1994 1458 -466 23 304 C ATOM 264 C THR A 35 31.408 3.728 11.715 1.00 17.21 C ANISOU 264 C THR A 35 2413 1981 2143 -533 -228 273 C ATOM 265 O THR A 35 32.432 3.423 12.346 1.00 19.78 O ANISOU 265 O THR A 35 2647 2242 2627 -433 -330 745 O ATOM 266 CB THR A 35 31.683 6.080 10.897 1.00 14.89 C ANISOU 266 CB THR A 35 2466 1750 1441 -394 -85 359 C ATOM 267 OG1 THR A 35 31.242 7.425 11.080 1.00 15.83 O ANISOU 267 OG1 THR A 35 2642 1737 1636 -330 -158 323 O ATOM 268 CG2 THR A 35 31.564 5.736 9.411 1.00 17.00 C ANISOU 268 CG2 THR A 35 2764 2145 1549 -452 -284 110 C ATOM 269 N TYR A 36 30.737 2.882 10.935 1.00 17.69 N ANISOU 269 N TYR A 36 2592 1965 2163 -477 -233 195 N ATOM 270 CA TYR A 36 31.057 1.470 10.865 1.00 18.15 C ANISOU 270 CA TYR A 36 2530 1908 2458 -523 -205 500 C ATOM 271 C TYR A 36 31.141 1.019 9.416 1.00 17.74 C ANISOU 271 C TYR A 36 2353 1928 2460 -334 -397 421 C ATOM 272 O TYR A 36 30.326 1.421 8.576 1.00 18.75 O ANISOU 272 O TYR A 36 2542 2178 2401 -176 -396 487 O ATOM 273 CB TYR A 36 30.010 0.638 11.628 1.00 19.02 C ANISOU 273 CB TYR A 36 2734 2190 2303 -660 -17 360 C ATOM 274 CG TYR A 36 29.721 1.153 13.024 1.00 17.89 C ANISOU 274 CG TYR A 36 2439 2042 2315 -782 -218 321 C ATOM 275 CD1 TYR A 36 30.388 0.626 14.128 1.00 19.71 C ANISOU 275 CD1 TYR A 36 2705 2182 2603 -874 -211 775 C ATOM 276 CD2 TYR A 36 28.785 2.173 13.239 1.00 19.79 C ANISOU 276 CD2 TYR A 36 3000 2037 2483 -655 -69 -23 C ATOM 277 CE1 TYR A 36 30.135 1.094 15.406 1.00 21.42 C ANISOU 277 CE1 TYR A 36 2985 2635 2518 -736 -253 803 C ATOM 278 CE2 TYR A 36 28.531 2.654 14.518 1.00 20.42 C ANISOU 278 CE2 TYR A 36 3227 2304 2225 -942 -311 22 C ATOM 279 CZ TYR A 36 29.203 2.101 15.597 1.00 23.15 C ANISOU 279 CZ TYR A 36 3455 2589 2750 -665 -391 272 C ATOM 280 OH TYR A 36 28.953 2.567 16.867 1.00 27.16 O ANISOU 280 OH TYR A 36 4117 3366 2834 -710 19 182 O ATOM 281 N LEU A 37 32.149 0.204 9.120 1.00 17.70 N ANISOU 281 N LEU A 37 2372 1873 2478 -321 -352 629 N ATOM 282 CA LEU A 37 32.337 -0.338 7.782 1.00 19.56 C ANISOU 282 CA LEU A 37 2676 1987 2769 -68 -174 368 C ATOM 283 C LEU A 37 32.310 -1.852 7.880 1.00 23.02 C ANISOU 283 C LEU A 37 3028 1979 3738 -84 -357 232 C ATOM 284 O LEU A 37 33.246 -2.459 8.408 1.00 25.07 O ANISOU 284 O LEU A 37 3231 1917 4374 -107 -250 818 O ATOM 285 CB LEU A 37 33.666 0.143 7.185 1.00 19.84 C ANISOU 285 CB LEU A 37 2564 1759 3216 28 -126 342 C ATOM 286 CG LEU A 37 34.038 -0.348 5.777 1.00 22.03 C ANISOU 286 CG LEU A 37 2449 2616 3304 179 173 342 C ATOM 287 CD1 LEU A 37 33.045 0.090 4.700 1.00 22.54 C ANISOU 287 CD1 LEU A 37 2857 2369 3335 -10 -135 135 C ATOM 288 CD2 LEU A 37 35.452 0.092 5.419 1.00 24.28 C ANISOU 288 CD2 LEU A 37 2554 2809 3860 -35 266 233 C ATOM 289 N ASP A 38 31.219 -2.445 7.390 1.00 22.61 N ANISOU 289 N ASP A 38 2759 2022 3809 -45 -345 693 N ATOM 290 CA ASP A 38 30.957 -3.878 7.523 1.00 27.22 C ANISOU 290 CA ASP A 38 3713 2054 4576 -176 -447 497 C ATOM 291 C ASP A 38 31.073 -4.342 8.985 1.00 25.29 C ANISOU 291 C ASP A 38 2990 2163 4455 -224 -505 502 C ATOM 292 O ASP A 38 31.626 -5.412 9.273 1.00 31.90 O ANISOU 292 O ASP A 38 3882 2096 6143 -343 -665 1026 O ATOM 293 CB ASP A 38 31.868 -4.678 6.581 1.00 29.87 C ANISOU 293 CB ASP A 38 3839 2250 5257 -393 -251 22 C ATOM 294 CG ASP A 38 31.701 -4.274 5.123 1.00 32.90 C ANISOU 294 CG ASP A 38 4254 3106 5138 -97 -177 -464 C ATOM 295 OD1 ASP A 38 30.549 -4.215 4.638 1.00 38.28 O ANISOU 295 OD1 ASP A 38 4600 3388 6556 -401 -829 -998 O ATOM 296 OD2 ASP A 38 32.724 -4.014 4.459 1.00 39.73 O ANISOU 296 OD2 ASP A 38 4397 4159 6537 -133 370 -720 O ATOM 297 N GLY A 39 30.551 -3.520 9.898 1.00 24.93 N ANISOU 297 N GLY A 39 3208 2445 3819 -529 -509 651 N ATOM 298 CA GLY A 39 30.525 -3.835 11.332 1.00 26.91 C ANISOU 298 CA GLY A 39 3441 2861 3921 -625 -776 827 C ATOM 299 C GLY A 39 31.674 -3.266 12.150 1.00 29.90 C ANISOU 299 C GLY A 39 3245 3891 4225 -895 -581 657 C ATOM 300 O GLY A 39 31.536 -3.054 13.370 1.00 27.83 O ANISOU 300 O GLY A 39 3151 2810 4612 -366 -39 546 O ATOM 301 N ALA A 40 32.799 -3.016 11.478 1.00 25.09 N ANISOU 301 N ALA A 40 2839 2398 4297 -246 -735 1142 N ATOM 302 CA ALA A 40 34.016 -2.544 12.132 1.00 26.30 C ANISOU 302 CA ALA A 40 3077 2641 4272 -203 -793 782 C ATOM 303 C ALA A 40 33.891 -1.064 12.445 1.00 24.89 C ANISOU 303 C ALA A 40 3327 2372 3758 -439 -572 1239 C ATOM 304 O ALA A 40 33.471 -0.286 11.594 1.00 24.46 O ANISOU 304 O ALA A 40 2683 2612 3997 -515 -894 1317 O ATOM 305 CB ALA A 40 35.227 -2.794 11.246 1.00 27.03 C ANISOU 305 CB ALA A 40 2956 3090 4221 -106 -759 1389 C ATOM 306 N ASP A 41 34.254 -0.689 13.669 1.00 25.59 N ANISOU 306 N ASP A 41 3062 2601 4059 -381 -791 1102 N ATOM 307 CA ASP A 41 34.176 0.690 14.126 1.00 24.89 C ANISOU 307 CA ASP A 41 3313 2653 3489 -737 -736 1043 C ATOM 308 C ASP A 41 35.333 1.495 13.531 1.00 24.50 C ANISOU 308 C ASP A 41 2976 2736 3596 -463 -776 1232 C ATOM 309 O ASP A 41 36.489 1.297 13.910 1.00 27.96 O ANISOU 309 O ASP A 41 2833 3069 4721 -559 -793 1644 O ATOM 310 CB ASP A 41 34.211 0.731 15.665 1.00 27.67 C ANISOU 310 CB ASP A 41 3910 3147 3457 -864 -502 1327 C ATOM 311 CG ASP A 41 33.956 2.121 16.229 1.00 27.36 C ANISOU 311 CG ASP A 41 3795 3220 3380 -984 -487 1232 C ATOM 312 OD1 ASP A 41 34.015 3.102 15.463 1.00 25.30 O ANISOU 312 OD1 ASP A 41 3372 3239 3000 -1129 -900 1158 O ATOM 313 OD2 ASP A 41 33.699 2.238 17.445 1.00 29.91 O ANISOU 313 OD2 ASP A 41 4687 3355 3320 -745 -761 1177 O ATOM 314 N VAL A 42 35.015 2.395 12.598 1.00 21.00 N ANISOU 314 N VAL A 42 2379 2478 3121 -439 -485 969 N ATOM 315 CA VAL A 42 36.031 3.238 11.945 1.00 21.72 C ANISOU 315 CA VAL A 42 2372 2692 3185 -605 -396 734 C ATOM 316 C VAL A 42 35.989 4.704 12.402 1.00 20.71 C ANISOU 316 C VAL A 42 2396 2747 2722 -617 -203 709 C ATOM 317 O VAL A 42 36.610 5.575 11.789 1.00 22.10 O ANISOU 317 O VAL A 42 2886 2582 2929 -636 -416 1003 O ATOM 318 CB VAL A 42 35.955 3.163 10.395 1.00 22.00 C ANISOU 318 CB VAL A 42 2707 2478 3171 -472 -351 403 C ATOM 319 CG1 VAL A 42 36.273 1.760 9.897 1.00 23.37 C ANISOU 319 CG1 VAL A 42 2813 2703 3363 -548 -195 62 C ATOM 320 CG2 VAL A 42 34.599 3.637 9.880 1.00 21.53 C ANISOU 320 CG2 VAL A 42 2814 2450 2915 -213 -183 513 C ATOM 321 N THR A 43 35.275 4.961 13.496 1.00 20.48 N ANISOU 321 N THR A 43 2739 2617 2424 -541 -260 723 N ATOM 322 CA THR A 43 35.083 6.314 14.035 1.00 20.06 C ANISOU 322 CA THR A 43 2717 2557 2345 -687 -250 669 C ATOM 323 C THR A 43 36.400 7.051 14.252 1.00 20.48 C ANISOU 323 C THR A 43 2728 2470 2581 -522 -710 653 C ATOM 324 O THR A 43 36.516 8.239 13.939 1.00 19.21 O ANISOU 324 O THR A 43 2696 2465 2138 -642 -493 566 O ATOM 325 CB THR A 43 34.311 6.259 15.372 1.00 21.06 C ANISOU 325 CB THR A 43 2880 2834 2286 -744 -295 799 C ATOM 326 OG1 THR A 43 33.110 5.505 15.183 1.00 21.74 O ANISOU 326 OG1 THR A 43 3192 3129 1939 -1104 -488 998 O ATOM 327 CG2 THR A 43 33.942 7.657 15.870 1.00 21.92 C ANISOU 327 CG2 THR A 43 3147 2928 2252 -714 -370 600 C ATOM 328 N LYS A 44 37.390 6.335 14.773 1.00 21.46 N ANISOU 328 N LYS A 44 2646 2725 2779 -624 -826 794 N ATOM 329 CA LYS A 44 38.660 6.939 15.164 1.00 21.17 C ANISOU 329 CA LYS A 44 2627 2815 2600 -591 -749 447 C ATOM 330 C LYS A 44 39.659 7.089 14.019 1.00 23.01 C ANISOU 330 C LYS A 44 2623 2916 3204 -333 -396 372 C ATOM 331 O LYS A 44 40.719 7.691 14.197 1.00 25.95 O ANISOU 331 O LYS A 44 2815 3523 3520 -751 -297 533 O ATOM 332 CB LYS A 44 39.285 6.151 16.316 1.00 22.98 C ANISOU 332 CB LYS A 44 2794 3012 2925 -438 -937 595 C ATOM 333 CG LYS A 44 38.584 6.382 17.641 1.00 27.95 C ANISOU 333 CG LYS A 44 3331 3990 3297 -180 -472 644 C ATOM 334 CD LYS A 44 39.247 5.616 18.770 1.00 29.69 C ANISOU 334 CD LYS A 44 3636 4530 3113 -361 -1039 417 C ATOM 335 CE LYS A 44 38.474 5.796 20.065 1.00 33.98 C ANISOU 335 CE LYS A 44 4429 5123 3357 287 -763 441 C ATOM 336 NZ LYS A 44 39.077 5.001 21.168 1.00 37.35 N ANISOU 336 NZ LYS A 44 4940 6194 3053 431 -847 656 N ATOM 337 N ILE A 45 39.332 6.550 12.848 1.00 23.06 N ANISOU 337 N ILE A 45 2808 2685 3267 -428 -358 427 N ATOM 338 CA ILE A 45 40.262 6.617 11.724 1.00 25.43 C ANISOU 338 CA ILE A 45 3476 2975 3209 178 -136 462 C ATOM 339 C ILE A 45 39.833 7.629 10.665 1.00 22.43 C ANISOU 339 C ILE A 45 2616 2752 3151 -104 -237 360 C ATOM 340 O ILE A 45 38.678 8.062 10.635 1.00 20.80 O ANISOU 340 O ILE A 45 2688 2259 2953 -80 131 75 O ATOM 341 CB ILE A 45 40.553 5.229 11.092 1.00 26.74 C ANISOU 341 CB ILE A 45 3832 2743 3585 139 -587 465 C ATOM 342 CG1 ILE A 45 39.378 4.744 10.240 1.00 27.60 C ANISOU 342 CG1 ILE A 45 3706 2887 3892 -20 -449 99 C ATOM 343 CG2 ILE A 45 40.931 4.216 12.169 1.00 28.14 C ANISOU 343 CG2 ILE A 45 4141 3053 3498 358 -743 480 C ATOM 344 CD1 ILE A 45 39.745 3.644 9.265 1.00 27.52 C ANISOU 344 CD1 ILE A 45 3071 3499 3884 432 -68 95 C ATOM 345 N LYS A 46 40.778 7.997 9.804 1.00 22.43 N ANISOU 345 N LYS A 46 2616 2709 3196 7 -203 411 N ATOM 346 CA LYS A 46 40.532 8.940 8.717 1.00 20.37 C ANISOU 346 CA LYS A 46 2272 2781 2685 -224 -93 294 C ATOM 347 C LYS A 46 40.205 8.218 7.407 1.00 21.17 C ANISOU 347 C LYS A 46 2442 2504 3097 -101 -21 31 C ATOM 348 O LYS A 46 40.594 7.055 7.216 1.00 24.05 O ANISOU 348 O LYS A 46 2899 2574 3664 -116 109 -272 O ATOM 349 CB LYS A 46 41.729 9.890 8.556 1.00 20.39 C ANISOU 349 CB LYS A 46 2549 2273 2923 -152 223 47 C ATOM 350 CG LYS A 46 42.014 10.710 9.805 1.00 22.33 C ANISOU 350 CG LYS A 46 2721 3200 2561 -497 -374 296 C ATOM 351 CD LYS A 46 43.095 11.756 9.579 1.00 23.32 C ANISOU 351 CD LYS A 46 3034 2925 2900 -533 -562 274 C ATOM 352 CE LYS A 46 43.345 12.540 10.858 1.00 26.96 C ANISOU 352 CE LYS A 46 3416 3581 3245 -618 -695 -177 C ATOM 353 NZ LYS A 46 44.332 13.641 10.678 1.00 32.54 N ANISOU 353 NZ LYS A 46 3884 3921 4556 -1130 -1366 -193 N ATOM 354 N PRO A 47 39.471 8.891 6.499 1.00 19.68 N ANISOU 354 N PRO A 47 2525 2271 2680 -319 76 83 N ATOM 355 CA PRO A 47 39.124 8.225 5.246 1.00 22.18 C ANISOU 355 CA PRO A 47 2834 2819 2774 -205 310 -286 C ATOM 356 C PRO A 47 40.355 7.761 4.470 1.00 24.61 C ANISOU 356 C PRO A 47 2957 3073 3321 -178 516 -333 C ATOM 357 O PRO A 47 41.379 8.452 4.429 1.00 28.17 O ANISOU 357 O PRO A 47 3021 3783 3896 -406 796 -432 O ATOM 358 CB PRO A 47 38.363 9.303 4.470 1.00 22.51 C ANISOU 358 CB PRO A 47 2778 2657 3114 -262 427 -156 C ATOM 359 CG PRO A 47 37.809 10.199 5.520 1.00 20.66 C ANISOU 359 CG PRO A 47 2661 2542 2647 -478 11 -196 C ATOM 360 CD PRO A 47 38.850 10.224 6.598 1.00 20.54 C ANISOU 360 CD PRO A 47 2510 2397 2896 -187 -52 27 C ATOM 361 N HIS A 48 40.239 6.581 3.878 1.00 24.68 N ANISOU 361 N HIS A 48 2806 3295 3274 207 474 -633 N ATOM 362 CA HIS A 48 41.306 5.977 3.113 1.00 28.31 C ANISOU 362 CA HIS A 48 3136 4022 3596 403 816 -628 C ATOM 363 C HIS A 48 40.880 5.984 1.678 1.00 27.64 C ANISOU 363 C HIS A 48 2910 3918 3674 339 727 -1026 C ATOM 364 O HIS A 48 39.682 5.940 1.381 1.00 27.04 O ANISOU 364 O HIS A 48 2809 3286 4178 251 678 -752 O ATOM 365 CB HIS A 48 41.536 4.550 3.602 1.00 32.65 C ANISOU 365 CB HIS A 48 3866 4147 4394 383 621 -461 C ATOM 366 CG HIS A 48 42.781 3.904 3.052 1.00 34.85 C ANISOU 366 CG HIS A 48 3707 4680 4851 585 354 -680 C ATOM 367 ND1 HIS A 48 43.941 3.867 3.736 1.00 41.21 N ANISOU 367 ND1 HIS A 48 4509 5900 5247 654 -309 -975 N ATOM 368 CD2 HIS A 48 43.015 3.254 1.846 1.00 33.49 C ANISOU 368 CD2 HIS A 48 3441 4342 4941 516 450 -756 C ATOM 369 CE1 HIS A 48 44.872 3.229 3.002 1.00 40.65 C ANISOU 369 CE1 HIS A 48 4277 5828 5339 676 -197 -754 C ATOM 370 NE2 HIS A 48 44.304 2.856 1.845 1.00 37.25 N ANISOU 370 NE2 HIS A 48 3612 5153 5388 995 122 -1101 N ATOM 371 N VAL A 49 41.846 6.043 0.764 1.00 30.20 N ANISOU 371 N VAL A 49 3146 4080 4247 -158 1084 -818 N ATOM 372 CA VAL A 49 41.545 6.001 -0.668 1.00 29.50 C ANISOU 372 CA VAL A 49 3136 3824 4246 -325 944 -853 C ATOM 373 C VAL A 49 40.673 4.789 -1.037 1.00 27.93 C ANISOU 373 C VAL A 49 3164 3294 4153 92 1185 -1168 C ATOM 374 O VAL A 49 39.807 4.888 -1.910 1.00 31.03 O ANISOU 374 O VAL A 49 3582 4301 3907 145 1332 -783 O ATOM 375 CB VAL A 49 42.828 6.060 -1.543 1.00 33.47 C ANISOU 375 CB VAL A 49 3419 4266 5029 -406 1345 -344 C ATOM 376 CG1 VAL A 49 43.497 7.423 -1.416 1.00 37.88 C ANISOU 376 CG1 VAL A 49 4404 4272 5714 -608 905 -141 C ATOM 377 CG2 VAL A 49 43.806 4.949 -1.181 1.00 34.31 C ANISOU 377 CG2 VAL A 49 3220 4467 5349 -292 1511 -446 C ATOM 378 N ASN A 50 40.883 3.670 -0.339 1.00 29.12 N ANISOU 378 N ASN A 50 3244 3621 4198 -57 1208 -875 N ATOM 379 CA ASN A 50 40.135 2.428 -0.580 1.00 31.44 C ANISOU 379 CA ASN A 50 3298 3517 5131 -34 821 -633 C ATOM 380 C ASN A 50 38.673 2.474 -0.130 1.00 28.44 C ANISOU 380 C ASN A 50 3493 3059 4253 126 1020 -956 C ATOM 381 O ASN A 50 37.904 1.559 -0.428 1.00 28.20 O ANISOU 381 O ASN A 50 3311 2829 4574 353 630 -692 O ATOM 382 CB ASN A 50 40.824 1.228 0.089 1.00 34.43 C ANISOU 382 CB ASN A 50 3751 3707 5623 319 563 -738 C ATOM 383 CG ASN A 50 42.127 0.836 -0.587 1.00 38.49 C ANISOU 383 CG ASN A 50 4303 4857 5462 751 871 -522 C ATOM 384 OD1 ASN A 50 42.953 0.150 0.012 1.00 43.86 O ANISOU 384 OD1 ASN A 50 4735 5097 6833 747 269 -274 O ATOM 385 ND2 ASN A 50 42.313 1.256 -1.837 1.00 41.20 N ANISOU 385 ND2 ASN A 50 5124 5148 5382 696 1451 -938 N ATOM 386 N HIS A 51 38.301 3.530 0.594 1.00 24.56 N ANISOU 386 N HIS A 51 3023 2514 3793 75 791 -528 N ATOM 387 CA HIS A 51 36.929 3.695 1.073 1.00 22.02 C ANISOU 387 CA HIS A 51 2841 2277 3248 -177 527 -509 C ATOM 388 C HIS A 51 36.037 4.301 0.019 1.00 22.10 C ANISOU 388 C HIS A 51 3048 2523 2825 -13 629 -560 C ATOM 389 O HIS A 51 34.819 4.366 0.204 1.00 22.51 O ANISOU 389 O HIS A 51 3063 3057 2432 -23 646 -446 O ATOM 390 CB HIS A 51 36.878 4.558 2.338 1.00 22.05 C ANISOU 390 CB HIS A 51 2890 2520 2968 1 330 -418 C ATOM 391 CG HIS A 51 37.511 3.921 3.556 1.00 23.19 C ANISOU 391 CG HIS A 51 2696 2787 3326 130 231 -253 C ATOM 392 ND1 HIS A 51 37.895 4.644 4.625 1.00 23.85 N ANISOU 392 ND1 HIS A 51 2613 3165 3282 256 125 -284 N ATOM 393 CD2 HIS A 51 37.822 2.593 3.848 1.00 24.37 C ANISOU 393 CD2 HIS A 51 2716 2935 3608 -10 140 231 C ATOM 394 CE1 HIS A 51 38.419 3.824 5.558 1.00 26.21 C ANISOU 394 CE1 HIS A 51 2925 3439 3593 298 -96 -70 C ATOM 395 NE2 HIS A 51 38.375 2.570 5.080 1.00 27.83 N ANISOU 395 NE2 HIS A 51 3281 3555 3737 353 -40 -255 N ATOM 396 N GLU A 52 36.630 4.756 -1.087 1.00 22.88 N ANISOU 396 N GLU A 52 3142 2692 2859 -186 599 -562 N ATOM 397 CA GLU A 52 35.883 5.429 -2.157 1.00 22.82 C ANISOU 397 CA GLU A 52 3298 2588 2783 -374 700 -365 C ATOM 398 C GLU A 52 34.691 4.599 -2.630 1.00 21.33 C ANISOU 398 C GLU A 52 2982 2538 2582 -156 912 -586 C ATOM 399 O GLU A 52 34.842 3.439 -3.029 1.00 24.86 O ANISOU 399 O GLU A 52 3861 2640 2943 -347 547 -1028 O ATOM 400 CB GLU A 52 36.804 5.760 -3.340 1.00 24.95 C ANISOU 400 CB GLU A 52 3807 2919 2753 -482 802 -236 C ATOM 401 CG GLU A 52 36.179 6.660 -4.403 1.00 27.48 C ANISOU 401 CG GLU A 52 4325 3421 2692 -588 473 -158 C ATOM 402 CD GLU A 52 36.462 8.140 -4.187 1.00 31.77 C ANISOU 402 CD GLU A 52 4583 3465 4021 -547 660 -146 C ATOM 403 OE1 GLU A 52 35.561 8.959 -4.446 1.00 30.29 O ANISOU 403 OE1 GLU A 52 3692 4364 3452 -213 1861 -603 O ATOM 404 OE2 GLU A 52 37.587 8.492 -3.772 1.00 36.21 O ANISOU 404 OE2 GLU A 52 5135 3497 5126 -651 12 -341 O ATOM 405 N GLY A 53 33.505 5.199 -2.569 1.00 19.83 N ANISOU 405 N GLY A 53 2949 2430 2153 -174 658 -417 N ATOM 406 CA GLY A 53 32.286 4.548 -3.040 1.00 20.65 C ANISOU 406 CA GLY A 53 2999 2382 2464 -254 573 -316 C ATOM 407 C GLY A 53 31.674 3.510 -2.115 1.00 20.33 C ANISOU 407 C GLY A 53 2909 2460 2356 18 496 -128 C ATOM 408 O GLY A 53 30.658 2.922 -2.452 1.00 21.57 O ANISOU 408 O GLY A 53 3294 2372 2526 -378 610 59 O ATOM 409 N LYS A 54 32.282 3.282 -0.953 1.00 20.08 N ANISOU 409 N LYS A 54 3138 2440 2052 -128 687 -137 N ATOM 410 CA LYS A 54 31.777 2.280 -0.010 1.00 19.48 C ANISOU 410 CA LYS A 54 2945 2182 2272 67 539 -22 C ATOM 411 C LYS A 54 30.627 2.800 0.857 1.00 18.63 C ANISOU 411 C LYS A 54 2939 1950 2187 -128 586 88 C ATOM 412 O LYS A 54 30.443 4.014 0.999 1.00 18.84 O ANISOU 412 O LYS A 54 3317 1974 1865 26 409 -18 O ATOM 413 CB LYS A 54 32.915 1.732 0.855 1.00 21.94 C ANISOU 413 CB LYS A 54 2948 2355 3032 277 425 30 C ATOM 414 CG LYS A 54 33.899 0.882 0.064 1.00 25.48 C ANISOU 414 CG LYS A 54 3286 2957 3438 554 857 127 C ATOM 415 CD LYS A 54 34.887 0.152 0.965 1.00 32.48 C ANISOU 415 CD LYS A 54 4320 3917 4103 621 -27 226 C ATOM 416 CE LYS A 54 35.317 -1.180 0.364 1.00 37.77 C ANISOU 416 CE LYS A 54 5063 4525 4760 267 364 -711 C ATOM 417 NZ LYS A 54 35.687 -1.079 -1.075 1.00 40.73 N ANISOU 417 NZ LYS A 54 4949 5555 4971 -176 608 -193 N ATOM 418 N THR A 55 29.849 1.869 1.406 1.00 17.33 N ANISOU 418 N THR A 55 2482 1996 2104 -135 255 157 N ATOM 419 CA THR A 55 28.733 2.189 2.293 1.00 17.35 C ANISOU 419 CA THR A 55 2422 2032 2135 -185 210 141 C ATOM 420 C THR A 55 29.120 2.000 3.753 1.00 16.54 C ANISOU 420 C THR A 55 2312 1792 2179 62 175 118 C ATOM 421 O THR A 55 29.665 0.961 4.142 1.00 18.56 O ANISOU 421 O THR A 55 2738 1791 2523 113 298 335 O ATOM 422 CB THR A 55 27.508 1.323 1.956 1.00 17.75 C ANISOU 422 CB THR A 55 2494 2203 2043 -144 44 -152 C ATOM 423 OG1 THR A 55 27.082 1.622 0.624 1.00 19.38 O ANISOU 423 OG1 THR A 55 2822 2368 2170 90 -293 -258 O ATOM 424 CG2 THR A 55 26.356 1.580 2.911 1.00 18.13 C ANISOU 424 CG2 THR A 55 2372 2096 2420 2 133 -7 C ATOM 425 N PHE A 56 28.826 3.024 4.546 1.00 15.22 N ANISOU 425 N PHE A 56 2311 1745 1727 12 -19 150 N ATOM 426 CA PHE A 56 29.117 3.052 5.976 1.00 15.29 C ANISOU 426 CA PHE A 56 2280 1742 1785 -95 -65 219 C ATOM 427 C PHE A 56 27.828 3.158 6.769 1.00 15.04 C ANISOU 427 C PHE A 56 2201 1806 1708 -191 -103 203 C ATOM 428 O PHE A 56 26.913 3.895 6.381 1.00 16.18 O ANISOU 428 O PHE A 56 2394 1944 1808 -79 -96 234 O ATOM 429 CB PHE A 56 30.015 4.252 6.311 1.00 15.89 C ANISOU 429 CB PHE A 56 2172 1657 2207 0 -95 163 C ATOM 430 CG PHE A 56 31.388 4.160 5.711 1.00 16.19 C ANISOU 430 CG PHE A 56 2290 1672 2188 -159 112 169 C ATOM 431 CD1 PHE A 56 32.464 3.723 6.470 1.00 17.18 C ANISOU 431 CD1 PHE A 56 2346 2001 2181 -235 -60 125 C ATOM 432 CD2 PHE A 56 31.605 4.491 4.373 1.00 16.89 C ANISOU 432 CD2 PHE A 56 2538 1778 2101 -164 49 102 C ATOM 433 CE1 PHE A 56 33.734 3.632 5.921 1.00 19.92 C ANISOU 433 CE1 PHE A 56 2529 2471 2567 -141 208 286 C ATOM 434 CE2 PHE A 56 32.875 4.388 3.815 1.00 18.43 C ANISOU 434 CE2 PHE A 56 2385 2183 2433 -49 -56 301 C ATOM 435 CZ PHE A 56 33.941 3.963 4.590 1.00 18.74 C ANISOU 435 CZ PHE A 56 2441 2233 2445 -227 -227 251 C ATOM 436 N PHE A 57 27.753 2.419 7.877 1.00 16.13 N ANISOU 436 N PHE A 57 2442 1715 1970 -213 -173 374 N ATOM 437 CA PHE A 57 26.643 2.579 8.812 1.00 16.44 C ANISOU 437 CA PHE A 57 2733 1819 1694 -357 -123 295 C ATOM 438 C PHE A 57 27.002 3.688 9.781 1.00 14.80 C ANISOU 438 C PHE A 57 2399 1920 1301 -330 -27 340 C ATOM 439 O PHE A 57 28.153 3.785 10.226 1.00 17.69 O ANISOU 439 O PHE A 57 2468 2296 1955 -373 -102 127 O ATOM 440 CB PHE A 57 26.333 1.282 9.567 1.00 18.83 C ANISOU 440 CB PHE A 57 3402 1977 1775 -381 -346 525 C ATOM 441 CG PHE A 57 25.325 0.406 8.880 1.00 20.24 C ANISOU 441 CG PHE A 57 3009 2042 2638 -224 -282 205 C ATOM 442 CD1 PHE A 57 25.630 -0.198 7.661 1.00 21.93 C ANISOU 442 CD1 PHE A 57 3379 2373 2577 -241 -78 234 C ATOM 443 CD2 PHE A 57 24.075 0.170 9.448 1.00 22.94 C ANISOU 443 CD2 PHE A 57 3118 2453 3144 31 -49 -54 C ATOM 444 CE1 PHE A 57 24.704 -1.002 7.016 1.00 23.67 C ANISOU 444 CE1 PHE A 57 3313 2446 3232 -376 -64 171 C ATOM 445 CE2 PHE A 57 23.147 -0.642 8.812 1.00 25.12 C ANISOU 445 CE2 PHE A 57 3016 2823 3704 -116 -246 161 C ATOM 446 CZ PHE A 57 23.462 -1.229 7.594 1.00 26.33 C ANISOU 446 CZ PHE A 57 3005 3392 3606 -461 -255 23 C ATOM 447 N VAL A 58 26.020 4.531 10.089 1.00 15.26 N ANISOU 447 N VAL A 58 2412 1873 1511 -412 -127 105 N ATOM 448 CA VAL A 58 26.206 5.632 11.030 1.00 15.36 C ANISOU 448 CA VAL A 58 2336 1804 1696 -412 -105 30 C ATOM 449 C VAL A 58 25.096 5.641 12.086 1.00 17.16 C ANISOU 449 C VAL A 58 2236 2225 2057 -518 -3 307 C ATOM 450 O VAL A 58 24.056 5.008 11.907 1.00 21.40 O ANISOU 450 O VAL A 58 2430 3809 1892 -1108 -7 264 O ATOM 451 CB VAL A 58 26.280 7.001 10.311 1.00 15.99 C ANISOU 451 CB VAL A 58 2119 1924 2033 -471 89 211 C ATOM 452 CG1 VAL A 58 27.497 7.058 9.392 1.00 16.52 C ANISOU 452 CG1 VAL A 58 2409 2011 1856 -319 208 147 C ATOM 453 CG2 VAL A 58 24.995 7.274 9.535 1.00 17.15 C ANISOU 453 CG2 VAL A 58 2298 2103 2113 -361 -65 222 C ATOM 454 N LEU A 59 25.327 6.347 13.189 1.00 18.34 N ANISOU 454 N LEU A 59 2445 2552 1972 -154 185 126 N ATOM 455 CA LEU A 59 24.284 6.561 14.201 1.00 20.58 C ANISOU 455 CA LEU A 59 2502 2865 2452 49 392 -52 C ATOM 456 C LEU A 59 23.265 7.562 13.649 1.00 17.64 C ANISOU 456 C LEU A 59 2561 2286 1855 -261 218 -118 C ATOM 457 O LEU A 59 23.638 8.505 12.945 1.00 19.12 O ANISOU 457 O LEU A 59 2768 2388 2108 -189 551 -81 O ATOM 458 CB LEU A 59 24.902 7.026 15.539 1.00 27.29 C ANISOU 458 CB LEU A 59 3687 4231 2449 -141 200 -164 C ATOM 459 CG LEU A 59 24.149 7.652 16.737 1.00 28.91 C ANISOU 459 CG LEU A 59 3574 4326 3081 57 -1 -753 C ATOM 460 CD1 LEU A 59 22.998 6.799 17.240 1.00 33.10 C ANISOU 460 CD1 LEU A 59 4019 4332 4224 -70 -95 45 C ATOM 461 CD2 LEU A 59 25.107 7.914 17.890 1.00 33.11 C ANISOU 461 CD2 LEU A 59 4402 5257 2921 152 -425 -213 C ATOM 462 N PRO A 60 21.966 7.351 13.938 1.00 16.34 N ANISOU 462 N PRO A 60 2554 1937 1715 -251 128 -19 N ATOM 463 CA PRO A 60 20.960 8.285 13.428 1.00 18.44 C ANISOU 463 CA PRO A 60 2538 1923 2543 -94 202 -139 C ATOM 464 C PRO A 60 21.063 9.653 14.118 1.00 20.34 C ANISOU 464 C PRO A 60 3183 1964 2582 -408 185 -124 C ATOM 465 O PRO A 60 20.663 9.801 15.268 1.00 25.19 O ANISOU 465 O PRO A 60 4368 2414 2787 -436 617 70 O ATOM 466 CB PRO A 60 19.623 7.588 13.741 1.00 20.23 C ANISOU 466 CB PRO A 60 2517 2346 2823 -158 213 84 C ATOM 467 CG PRO A 60 19.960 6.181 14.098 1.00 23.20 C ANISOU 467 CG PRO A 60 2727 2619 3469 -58 -133 338 C ATOM 468 CD PRO A 60 21.368 6.175 14.594 1.00 18.89 C ANISOU 468 CD PRO A 60 2596 2074 2507 -443 187 107 C ATOM 469 N SER A 61 21.590 10.638 13.395 1.00 19.92 N ANISOU 469 N SER A 61 3142 1876 2550 -378 261 -184 N ATOM 470 CA SER A 61 21.978 11.928 13.973 1.00 20.95 C ANISOU 470 CA SER A 61 3215 2088 2657 -209 123 -485 C ATOM 471 C SER A 61 21.201 13.128 13.427 1.00 21.91 C ANISOU 471 C SER A 61 3313 2094 2916 -139 255 -378 C ATOM 472 O SER A 61 21.469 14.275 13.807 1.00 25.91 O ANISOU 472 O SER A 61 3602 2322 3918 -419 330 -737 O ATOM 473 CB SER A 61 23.475 12.149 13.760 1.00 22.35 C ANISOU 473 CB SER A 61 3257 2308 2925 -300 323 -537 C ATOM 474 OG SER A 61 23.782 12.084 12.379 1.00 23.15 O ANISOU 474 OG SER A 61 3416 2411 2968 -744 532 -233 O ATOM 475 N ASP A 62 20.264 12.870 12.525 1.00 20.97 N ANISOU 475 N ASP A 62 3101 1956 2909 -28 336 -238 N ATOM 476 CA ASP A 62 19.348 13.904 12.038 1.00 21.70 C ANISOU 476 CA ASP A 62 3107 1893 3241 -21 168 -288 C ATOM 477 C ASP A 62 17.938 13.326 11.864 1.00 21.48 C ANISOU 477 C ASP A 62 2910 1850 3401 120 151 0 C ATOM 478 O ASP A 62 17.742 12.115 12.016 1.00 21.36 O ANISOU 478 O ASP A 62 3172 1858 3084 -113 302 -59 O ATOM 479 CB ASP A 62 19.872 14.585 10.756 1.00 23.47 C ANISOU 479 CB ASP A 62 3703 1860 3353 -82 341 -246 C ATOM 480 CG ASP A 62 20.079 13.614 9.594 1.00 24.14 C ANISOU 480 CG ASP A 62 3312 2478 3383 39 259 -453 C ATOM 481 OD1 ASP A 62 19.170 12.816 9.281 1.00 23.72 O ANISOU 481 OD1 ASP A 62 3573 2059 3378 -60 205 -25 O ATOM 482 OD2 ASP A 62 21.159 13.673 8.970 1.00 27.57 O ANISOU 482 OD2 ASP A 62 3941 3088 3446 -329 747 -382 O ATOM 483 N ASP A 63 16.958 14.180 11.568 1.00 22.52 N ANISOU 483 N ASP A 63 3141 1994 3422 354 9 -245 N ATOM 484 CA ASP A 63 15.561 13.734 11.465 1.00 24.73 C ANISOU 484 CA ASP A 63 3204 2302 3889 324 81 -75 C ATOM 485 C ASP A 63 15.329 12.640 10.418 1.00 22.45 C ANISOU 485 C ASP A 63 3293 1805 3431 268 227 358 C ATOM 486 O ASP A 63 14.577 11.689 10.659 1.00 23.03 O ANISOU 486 O ASP A 63 3318 1419 4013 410 480 -3 O ATOM 487 CB ASP A 63 14.630 14.923 11.201 1.00 27.76 C ANISOU 487 CB ASP A 63 4176 2104 4266 616 -95 -197 C ATOM 488 CG ASP A 63 14.423 15.798 12.432 1.00 30.54 C ANISOU 488 CG ASP A 63 4400 3157 4045 569 24 -365 C ATOM 489 OD1 ASP A 63 14.919 15.446 13.529 1.00 31.19 O ANISOU 489 OD1 ASP A 63 4498 3520 3830 346 -1 -590 O ATOM 490 OD2 ASP A 63 13.755 16.847 12.301 1.00 36.94 O ANISOU 490 OD2 ASP A 63 4537 3660 5839 1066 390 -340 O ATOM 491 N THR A 64 15.977 12.771 9.264 1.00 21.83 N ANISOU 491 N THR A 64 3222 1763 3307 373 156 380 N ATOM 492 CA THR A 64 15.851 11.784 8.191 1.00 21.53 C ANISOU 492 CA THR A 64 3150 2015 3013 472 123 452 C ATOM 493 C THR A 64 16.390 10.423 8.628 1.00 19.35 C ANISOU 493 C THR A 64 2756 1708 2887 133 3 234 C ATOM 494 O THR A 64 15.712 9.403 8.472 1.00 19.35 O ANISOU 494 O THR A 64 2675 1565 3112 137 357 397 O ATOM 495 CB THR A 64 16.549 12.258 6.902 1.00 22.94 C ANISOU 495 CB THR A 64 3629 1770 3313 237 350 597 C ATOM 496 OG1 THR A 64 15.964 13.496 6.486 1.00 26.98 O ANISOU 496 OG1 THR A 64 4205 2022 4022 394 312 1060 O ATOM 497 CG2 THR A 64 16.401 11.234 5.776 1.00 24.91 C ANISOU 497 CG2 THR A 64 3937 2360 3164 117 310 443 C ATOM 498 N LEU A 65 17.600 10.413 9.183 1.00 19.53 N ANISOU 498 N LEU A 65 2623 1809 2986 370 176 337 N ATOM 499 CA LEU A 65 18.203 9.174 9.667 1.00 17.20 C ANISOU 499 CA LEU A 65 2500 1712 2321 231 242 238 C ATOM 500 C LEU A 65 17.385 8.560 10.797 1.00 17.27 C ANISOU 500 C LEU A 65 2560 1462 2540 248 519 99 C ATOM 501 O LEU A 65 17.220 7.340 10.840 1.00 17.52 O ANISOU 501 O LEU A 65 2506 1526 2625 -23 198 245 O ATOM 502 CB LEU A 65 19.646 9.398 10.121 1.00 16.80 C ANISOU 502 CB LEU A 65 2399 1613 2370 95 345 307 C ATOM 503 CG LEU A 65 20.687 9.788 9.072 1.00 16.50 C ANISOU 503 CG LEU A 65 2436 1761 2069 98 333 39 C ATOM 504 CD1 LEU A 65 22.033 10.007 9.744 1.00 18.51 C ANISOU 504 CD1 LEU A 65 2389 2239 2404 229 137 200 C ATOM 505 CD2 LEU A 65 20.811 8.727 7.991 1.00 17.72 C ANISOU 505 CD2 LEU A 65 2685 1903 2141 180 439 -77 C ATOM 506 N ARG A 66 16.865 9.395 11.700 1.00 18.00 N ANISOU 506 N ARG A 66 2575 1729 2534 286 458 -7 N ATOM 507 CA ARG A 66 16.024 8.890 12.790 1.00 18.18 C ANISOU 507 CA ARG A 66 2608 1799 2497 219 351 -41 C ATOM 508 C ARG A 66 14.727 8.261 12.269 1.00 18.72 C ANISOU 508 C ARG A 66 2496 1855 2761 132 356 206 C ATOM 509 O ARG A 66 14.301 7.215 12.769 1.00 17.76 O ANISOU 509 O ARG A 66 2354 1685 2709 1 117 5 O ATOM 510 CB ARG A 66 15.742 9.976 13.835 1.00 19.41 C ANISOU 510 CB ARG A 66 2689 1701 2984 168 430 -252 C ATOM 511 CG ARG A 66 16.924 10.246 14.761 1.00 22.00 C ANISOU 511 CG ARG A 66 3215 2245 2899 193 127 -126 C ATOM 512 CD ARG A 66 16.578 11.253 15.851 1.00 27.08 C ANISOU 512 CD ARG A 66 3965 3005 3319 106 455 -626 C ATOM 513 NE ARG A 66 16.494 12.615 15.328 1.00 30.45 N ANISOU 513 NE ARG A 66 4150 3107 4312 -233 324 -355 N ATOM 514 CZ ARG A 66 17.478 13.512 15.387 1.00 28.89 C ANISOU 514 CZ ARG A 66 4245 2884 3847 -120 416 -829 C ATOM 515 NH1 ARG A 66 18.637 13.212 15.960 1.00 31.49 N ANISOU 515 NH1 ARG A 66 4426 3533 4003 425 425 -1255 N ATOM 516 NH2 ARG A 66 17.297 14.720 14.872 1.00 29.91 N ANISOU 516 NH2 ARG A 66 4834 2910 3618 32 727 -783 N ATOM 517 N SER A 67 14.129 8.872 11.243 1.00 19.41 N ANISOU 517 N SER A 67 2370 2141 2862 265 208 91 N ATOM 518 CA SER A 67 12.918 8.326 10.620 1.00 18.75 C ANISOU 518 CA SER A 67 2287 2028 2806 472 90 241 C ATOM 519 C SER A 67 13.230 6.984 9.968 1.00 17.58 C ANISOU 519 C SER A 67 2131 1948 2599 119 285 225 C ATOM 520 O SER A 67 12.498 6.014 10.148 1.00 18.20 O ANISOU 520 O SER A 67 2505 1671 2738 140 117 372 O ATOM 521 CB SER A 67 12.350 9.289 9.576 1.00 21.50 C ANISOU 521 CB SER A 67 2711 2096 3360 528 -123 514 C ATOM 522 OG SER A 67 11.219 8.724 8.931 1.00 27.57 O ANISOU 522 OG SER A 67 3407 2955 4112 46 -380 379 O ATOM 523 N GLU A 68 14.330 6.933 9.217 1.00 16.11 N ANISOU 523 N GLU A 68 2144 1688 2286 323 215 253 N ATOM 524 CA GLU A 68 14.736 5.715 8.518 1.00 15.86 C ANISOU 524 CA GLU A 68 2001 1582 2442 180 233 257 C ATOM 525 C GLU A 68 15.045 4.584 9.496 1.00 15.53 C ANISOU 525 C GLU A 68 2081 1669 2148 -48 -13 209 C ATOM 526 O GLU A 68 14.633 3.449 9.277 1.00 16.41 O ANISOU 526 O GLU A 68 2255 1569 2409 -39 207 175 O ATOM 527 CB GLU A 68 15.920 5.999 7.590 1.00 14.92 C ANISOU 527 CB GLU A 68 2120 1597 1951 180 115 402 C ATOM 528 CG GLU A 68 15.498 6.787 6.353 1.00 16.56 C ANISOU 528 CG GLU A 68 2325 1806 2161 326 200 638 C ATOM 529 CD GLU A 68 16.647 7.379 5.554 1.00 18.03 C ANISOU 529 CD GLU A 68 2606 1730 2514 122 308 729 C ATOM 530 OE1 GLU A 68 17.828 7.204 5.933 1.00 19.53 O ANISOU 530 OE1 GLU A 68 2598 2105 2715 -137 306 678 O ATOM 531 OE2 GLU A 68 16.357 8.030 4.530 1.00 21.82 O ANISOU 531 OE2 GLU A 68 3346 2080 2862 87 83 1018 O ATOM 532 N ALA A 69 15.734 4.900 10.588 1.00 14.84 N ANISOU 532 N ALA A 69 2040 1523 2073 210 -60 280 N ATOM 533 CA ALA A 69 16.043 3.908 11.622 1.00 15.54 C ANISOU 533 CA ALA A 69 2048 1774 2080 133 -51 426 C ATOM 534 C ALA A 69 14.764 3.397 12.290 1.00 15.56 C ANISOU 534 C ALA A 69 2093 1648 2171 169 108 230 C ATOM 535 O ALA A 69 14.603 2.196 12.497 1.00 15.95 O ANISOU 535 O ALA A 69 2074 1648 2338 -21 161 240 O ATOM 536 CB ALA A 69 17.002 4.486 12.653 1.00 16.11 C ANISOU 536 CB ALA A 69 2125 1826 2169 95 42 242 C ATOM 537 N PHE A 70 13.843 4.301 12.615 1.00 16.63 N ANISOU 537 N PHE A 70 2072 1694 2551 168 223 182 N ATOM 538 CA PHE A 70 12.602 3.887 13.263 1.00 16.75 C ANISOU 538 CA PHE A 70 1939 1911 2513 144 150 97 C ATOM 539 C PHE A 70 11.788 2.961 12.359 1.00 16.78 C ANISOU 539 C PHE A 70 2070 1854 2451 58 157 219 C ATOM 540 O PHE A 70 11.299 1.919 12.814 1.00 17.04 O ANISOU 540 O PHE A 70 1992 1845 2635 157 384 296 O ATOM 541 CB PHE A 70 11.767 5.098 13.703 1.00 18.17 C ANISOU 541 CB PHE A 70 2294 2001 2608 234 488 198 C ATOM 542 CG PHE A 70 10.424 4.728 14.272 1.00 21.35 C ANISOU 542 CG PHE A 70 2263 2988 2859 195 546 85 C ATOM 543 CD1 PHE A 70 10.326 4.093 15.510 1.00 23.43 C ANISOU 543 CD1 PHE A 70 2569 3388 2946 -254 752 244 C ATOM 544 CD2 PHE A 70 9.255 4.999 13.567 1.00 26.79 C ANISOU 544 CD2 PHE A 70 2373 4135 3671 16 242 449 C ATOM 545 CE1 PHE A 70 9.086 3.746 16.038 1.00 27.82 C ANISOU 545 CE1 PHE A 70 2387 4534 3647 -410 737 -43 C ATOM 546 CE2 PHE A 70 8.016 4.653 14.090 1.00 31.24 C ANISOU 546 CE2 PHE A 70 2763 5065 4042 -95 770 451 C ATOM 547 CZ PHE A 70 7.933 4.029 15.327 1.00 28.84 C ANISOU 547 CZ PHE A 70 2319 4787 3851 -199 846 237 C ATOM 548 N GLU A 71 11.657 3.324 11.085 1.00 15.97 N ANISOU 548 N GLU A 71 1821 1775 2470 269 46 160 N ATOM 549 CA GLU A 71 10.878 2.519 10.146 1.00 17.21 C ANISOU 549 CA GLU A 71 2192 2036 2311 243 -126 174 C ATOM 550 C GLU A 71 11.499 1.145 9.899 1.00 16.40 C ANISOU 550 C GLU A 71 2012 1809 2408 6 -48 345 C ATOM 551 O GLU A 71 10.789 0.158 9.674 1.00 18.18 O ANISOU 551 O GLU A 71 2120 1906 2880 -110 -33 350 O ATOM 552 CB GLU A 71 10.682 3.256 8.817 1.00 17.85 C ANISOU 552 CB GLU A 71 2241 1949 2590 242 -157 380 C ATOM 553 CG GLU A 71 9.884 4.555 8.914 1.00 21.64 C ANISOU 553 CG GLU A 71 2618 2266 3336 558 67 65 C ATOM 554 CD GLU A 71 8.476 4.375 9.471 1.00 25.50 C ANISOU 554 CD GLU A 71 2483 2969 4237 177 -132 216 C ATOM 555 OE1 GLU A 71 7.837 3.336 9.202 1.00 26.67 O ANISOU 555 OE1 GLU A 71 2634 3190 4307 -64 -168 249 O ATOM 556 OE2 GLU A 71 7.997 5.287 10.180 1.00 30.76 O ANISOU 556 OE2 GLU A 71 3274 4019 4392 498 -161 -348 O ATOM 557 N TYR A 72 12.828 1.090 9.931 1.00 15.53 N ANISOU 557 N TYR A 72 2019 1677 2203 163 145 261 N ATOM 558 CA TYR A 72 13.549 -0.148 9.660 1.00 15.05 C ANISOU 558 CA TYR A 72 1826 1671 2220 110 139 279 C ATOM 559 C TYR A 72 13.631 -1.073 10.879 1.00 14.23 C ANISOU 559 C TYR A 72 1724 1554 2127 141 -202 165 C ATOM 560 O TYR A 72 13.380 -2.281 10.758 1.00 14.66 O ANISOU 560 O TYR A 72 2064 1594 1909 -79 75 232 O ATOM 561 CB TYR A 72 14.949 0.168 9.136 1.00 14.38 C ANISOU 561 CB TYR A 72 1934 1359 2170 -90 147 235 C ATOM 562 CG TYR A 72 15.669 -1.008 8.520 1.00 14.95 C ANISOU 562 CG TYR A 72 1843 1682 2154 -29 299 174 C ATOM 563 CD1 TYR A 72 15.190 -1.612 7.361 1.00 15.90 C ANISOU 563 CD1 TYR A 72 2248 1737 2054 4 321 212 C ATOM 564 CD2 TYR A 72 16.850 -1.497 9.084 1.00 16.08 C ANISOU 564 CD2 TYR A 72 2203 1712 2194 274 217 333 C ATOM 565 CE1 TYR A 72 15.854 -2.684 6.785 1.00 16.77 C ANISOU 565 CE1 TYR A 72 2274 1879 2218 256 392 331 C ATOM 566 CE2 TYR A 72 17.535 -2.563 8.509 1.00 15.76 C ANISOU 566 CE2 TYR A 72 2339 1688 1958 235 246 347 C ATOM 567 CZ TYR A 72 17.029 -3.157 7.367 1.00 14.64 C ANISOU 567 CZ TYR A 72 2131 1463 1967 32 404 350 C ATOM 568 OH TYR A 72 17.698 -4.224 6.802 1.00 18.27 O ANISOU 568 OH TYR A 72 2659 1818 2461 373 609 307 O ATOM 569 N TYR A 73 13.967 -0.511 12.042 1.00 14.59 N ANISOU 569 N TYR A 73 1993 1673 1875 136 129 223 N ATOM 570 CA TYR A 73 14.219 -1.301 13.251 1.00 14.58 C ANISOU 570 CA TYR A 73 1883 1736 1920 77 69 257 C ATOM 571 C TYR A 73 13.030 -1.392 14.200 1.00 15.19 C ANISOU 571 C TYR A 73 1891 1829 2050 9 130 257 C ATOM 572 O TYR A 73 13.004 -2.273 15.061 1.00 16.32 O ANISOU 572 O TYR A 73 2165 1933 2100 61 150 428 O ATOM 573 CB TYR A 73 15.449 -0.778 14.008 1.00 14.91 C ANISOU 573 CB TYR A 73 1853 1911 1897 133 59 297 C ATOM 574 CG TYR A 73 16.721 -0.829 13.203 1.00 14.40 C ANISOU 574 CG TYR A 73 2127 1738 1605 150 190 471 C ATOM 575 CD1 TYR A 73 17.276 0.337 12.687 1.00 15.25 C ANISOU 575 CD1 TYR A 73 1884 1704 2204 64 35 504 C ATOM 576 CD2 TYR A 73 17.373 -2.044 12.952 1.00 15.06 C ANISOU 576 CD2 TYR A 73 1937 1798 1986 148 141 424 C ATOM 577 CE1 TYR A 73 18.440 0.303 11.941 1.00 16.17 C ANISOU 577 CE1 TYR A 73 1995 1857 2290 96 164 403 C ATOM 578 CE2 TYR A 73 18.540 -2.093 12.202 1.00 15.21 C ANISOU 578 CE2 TYR A 73 2004 1682 2093 117 205 422 C ATOM 579 CZ TYR A 73 19.068 -0.916 11.698 1.00 15.64 C ANISOU 579 CZ TYR A 73 1852 1804 2286 123 168 591 C ATOM 580 OH TYR A 73 20.227 -0.959 10.956 1.00 17.52 O ANISOU 580 OH TYR A 73 2131 1955 2568 181 471 481 O ATOM 581 N HIS A 74 12.064 -0.485 14.066 1.00 15.74 N ANISOU 581 N HIS A 74 1846 1953 2181 68 268 210 N ATOM 582 CA HIS A 74 10.902 -0.435 14.981 1.00 15.18 C ANISOU 582 CA HIS A 74 1827 1861 2077 -41 254 114 C ATOM 583 C HIS A 74 11.320 -0.230 16.415 1.00 17.56 C ANISOU 583 C HIS A 74 2338 2175 2157 -75 205 -55 C ATOM 584 O HIS A 74 10.801 -0.869 17.335 1.00 22.06 O ANISOU 584 O HIS A 74 3044 2607 2730 -404 530 137 O ATOM 585 CB HIS A 74 10.020 -1.686 14.843 1.00 16.21 C ANISOU 585 CB HIS A 74 1785 2060 2313 -139 101 17 C ATOM 586 CG HIS A 74 9.227 -1.742 13.563 1.00 15.67 C ANISOU 586 CG HIS A 74 1808 1954 2189 115 161 176 C ATOM 587 ND1 HIS A 74 8.253 -2.649 13.363 1.00 17.12 N ANISOU 587 ND1 HIS A 74 1994 1962 2547 27 22 212 N ATOM 588 CD2 HIS A 74 9.261 -0.944 12.418 1.00 17.20 C ANISOU 588 CD2 HIS A 74 2056 2113 2366 162 -116 344 C ATOM 589 CE1 HIS A 74 7.708 -2.463 12.146 1.00 18.05 C ANISOU 589 CE1 HIS A 74 2120 2115 2624 263 -38 358 C ATOM 590 NE2 HIS A 74 8.322 -1.419 11.570 1.00 19.14 N ANISOU 590 NE2 HIS A 74 2167 2230 2872 -145 -171 197 N ATOM 591 N THR A 75 12.288 0.658 16.613 1.00 17.85 N ANISOU 591 N THR A 75 2435 2040 2307 3 248 -229 N ATOM 592 CA THR A 75 12.664 1.074 17.953 1.00 20.20 C ANISOU 592 CA THR A 75 2792 2592 2288 -129 184 -211 C ATOM 593 C THR A 75 12.964 2.562 17.964 1.00 20.41 C ANISOU 593 C THR A 75 2788 2529 2438 54 169 -362 C ATOM 594 O THR A 75 13.347 3.130 16.942 1.00 23.01 O ANISOU 594 O THR A 75 3353 2700 2687 -86 212 -114 O ATOM 595 CB THR A 75 13.873 0.281 18.488 1.00 22.68 C ANISOU 595 CB THR A 75 3380 2799 2435 242 -110 -305 C ATOM 596 OG1 THR A 75 14.188 0.724 19.812 1.00 23.21 O ANISOU 596 OG1 THR A 75 3792 2585 2441 48 -136 -251 O ATOM 597 CG2 THR A 75 15.100 0.459 17.586 1.00 23.01 C ANISOU 597 CG2 THR A 75 2838 3040 2862 448 -203 -508 C ATOM 598 N LEU A 76 12.758 3.190 19.117 1.00 22.82 N ANISOU 598 N LEU A 76 3222 2728 2718 290 344 -593 N ATOM 599 CA LEU A 76 13.136 4.583 19.316 1.00 24.55 C ANISOU 599 CA LEU A 76 3250 2691 3386 388 21 -695 C ATOM 600 C LEU A 76 14.408 4.710 20.154 1.00 25.86 C ANISOU 600 C LEU A 76 3415 2574 3836 220 -194 -593 C ATOM 601 O LEU A 76 14.836 5.816 20.485 1.00 28.65 O ANISOU 601 O LEU A 76 3978 2606 4299 170 -396 -800 O ATOM 602 CB LEU A 76 11.986 5.364 19.961 1.00 27.63 C ANISOU 602 CB LEU A 76 3335 3314 3846 500 321 -783 C ATOM 603 CG LEU A 76 10.714 5.572 19.137 1.00 28.37 C ANISOU 603 CG LEU A 76 3448 3538 3793 590 363 -307 C ATOM 604 CD1 LEU A 76 9.571 6.017 20.039 1.00 32.51 C ANISOU 604 CD1 LEU A 76 4040 3667 4642 1102 537 -1132 C ATOM 605 CD2 LEU A 76 10.935 6.570 18.005 1.00 28.30 C ANISOU 605 CD2 LEU A 76 3969 3101 3682 608 -106 -433 C ATOM 606 N ASP A 77 15.012 3.574 20.485 1.00 23.96 N ANISOU 606 N ASP A 77 2849 2900 3353 365 -20 -502 N ATOM 607 CA ASP A 77 16.208 3.539 21.315 1.00 24.03 C ANISOU 607 CA ASP A 77 3388 2515 3228 611 -308 -820 C ATOM 608 C ASP A 77 17.405 4.064 20.532 1.00 26.39 C ANISOU 608 C ASP A 77 3574 2461 3991 187 -512 -329 C ATOM 609 O ASP A 77 17.877 3.427 19.584 1.00 26.57 O ANISOU 609 O ASP A 77 3296 2904 3894 256 -330 -94 O ATOM 610 CB ASP A 77 16.445 2.109 21.809 1.00 24.72 C ANISOU 610 CB ASP A 77 3440 2802 3150 816 -410 -414 C ATOM 611 CG ASP A 77 17.656 1.977 22.722 1.00 26.63 C ANISOU 611 CG ASP A 77 3793 2966 3356 520 -730 -613 C ATOM 612 OD1 ASP A 77 18.374 2.971 22.964 1.00 32.44 O ANISOU 612 OD1 ASP A 77 4301 3539 4482 155 -787 -932 O ATOM 613 OD2 ASP A 77 17.891 0.847 23.198 1.00 31.26 O ANISOU 613 OD2 ASP A 77 4545 3355 3974 794 -405 -109 O ATOM 614 N GLU A 78 17.887 5.232 20.946 1.00 28.66 N ANISOU 614 N GLU A 78 3809 2528 4550 66 -731 -258 N ATOM 615 CA GLU A 78 19.028 5.894 20.317 1.00 29.95 C ANISOU 615 CA GLU A 78 3367 2941 5069 431 -457 -391 C ATOM 616 C GLU A 78 20.305 5.052 20.334 1.00 27.71 C ANISOU 616 C GLU A 78 3219 2552 4757 166 -940 -239 C ATOM 617 O GLU A 78 21.152 5.205 19.459 1.00 32.64 O ANISOU 617 O GLU A 78 3668 2896 5836 411 -225 -193 O ATOM 618 CB GLU A 78 19.283 7.268 20.960 1.00 33.70 C ANISOU 618 CB GLU A 78 4727 2880 5197 60 -312 -286 C ATOM 619 CG GLU A 78 19.034 7.334 22.465 1.00 42.36 C ANISOU 619 CG GLU A 78 5679 5005 5410 26 222 -26 C ATOM 620 CD GLU A 78 17.553 7.276 22.832 1.00 43.01 C ANISOU 620 CD GLU A 78 5816 4992 5534 -439 467 618 C ATOM 621 OE1 GLU A 78 16.746 7.992 22.197 1.00 53.36 O ANISOU 621 OE1 GLU A 78 6889 6293 7092 -235 -594 1037 O ATOM 622 OE2 GLU A 78 17.192 6.510 23.753 1.00 45.50 O ANISOU 622 OE2 GLU A 78 7690 5036 4560 -437 1832 -314 O ATOM 623 N SER A 79 20.425 4.159 21.314 1.00 26.64 N ANISOU 623 N SER A 79 3526 1840 4755 -90 -825 -553 N ATOM 624 CA SER A 79 21.602 3.293 21.434 1.00 27.80 C ANISOU 624 CA SER A 79 3669 2091 4800 111 -887 -719 C ATOM 625 C SER A 79 21.582 2.077 20.488 1.00 24.95 C ANISOU 625 C SER A 79 3038 1805 4634 -53 -634 -511 C ATOM 626 O SER A 79 22.587 1.366 20.381 1.00 27.07 O ANISOU 626 O SER A 79 2992 2105 5186 45 -820 -541 O ATOM 627 CB SER A 79 21.772 2.824 22.886 1.00 29.45 C ANISOU 627 CB SER A 79 4024 2471 4694 -128 -964 -702 C ATOM 628 OG SER A 79 20.824 1.822 23.231 1.00 28.75 O ANISOU 628 OG SER A 79 4328 2082 4514 37 -1062 -528 O ATOM 629 N PHE A 80 20.464 1.850 19.795 1.00 23.31 N ANISOU 629 N PHE A 80 2955 1538 4361 -256 -431 -371 N ATOM 630 CA PHE A 80 20.267 0.585 19.062 1.00 20.33 C ANISOU 630 CA PHE A 80 2377 1631 3716 -177 -486 -243 C ATOM 631 C PHE A 80 21.321 0.273 17.993 1.00 20.89 C ANISOU 631 C PHE A 80 2495 1867 3573 -97 -404 171 C ATOM 632 O PHE A 80 21.931 -0.797 18.033 1.00 21.02 O ANISOU 632 O PHE A 80 2186 1808 3989 -158 -280 201 O ATOM 633 CB PHE A 80 18.850 0.472 18.468 1.00 20.58 C ANISOU 633 CB PHE A 80 2472 1990 3358 -280 -496 -156 C ATOM 634 CG PHE A 80 18.524 -0.904 17.944 1.00 18.14 C ANISOU 634 CG PHE A 80 2321 1781 2789 -128 -168 40 C ATOM 635 CD1 PHE A 80 17.899 -1.845 18.759 1.00 18.39 C ANISOU 635 CD1 PHE A 80 2492 1973 2521 -321 -128 -79 C ATOM 636 CD2 PHE A 80 18.861 -1.266 16.648 1.00 19.08 C ANISOU 636 CD2 PHE A 80 2524 2146 2578 -235 -376 187 C ATOM 637 CE1 PHE A 80 17.616 -3.121 18.282 1.00 16.87 C ANISOU 637 CE1 PHE A 80 2245 1891 2272 -186 -129 60 C ATOM 638 CE2 PHE A 80 18.583 -2.536 16.168 1.00 18.40 C ANISOU 638 CE2 PHE A 80 2288 2001 2699 -21 -60 193 C ATOM 639 CZ PHE A 80 17.953 -3.464 16.984 1.00 17.15 C ANISOU 639 CZ PHE A 80 2146 2183 2184 -76 -259 125 C ATOM 640 N LEU A 81 21.526 1.184 17.039 1.00 20.93 N ANISOU 640 N LEU A 81 2299 1834 3818 -106 -418 349 N ATOM 641 CA LEU A 81 22.444 0.924 15.918 1.00 22.51 C ANISOU 641 CA LEU A 81 2352 2155 4046 7 -195 513 C ATOM 642 C LEU A 81 23.869 0.624 16.391 1.00 20.25 C ANISOU 642 C LEU A 81 2446 1722 3524 117 -169 698 C ATOM 643 O LEU A 81 24.528 -0.292 15.875 1.00 21.69 O ANISOU 643 O LEU A 81 2423 1655 4161 96 123 907 O ATOM 644 CB LEU A 81 22.461 2.083 14.915 1.00 25.20 C ANISOU 644 CB LEU A 81 3221 2305 4047 216 -308 568 C ATOM 645 CG LEU A 81 21.648 1.889 13.636 1.00 29.56 C ANISOU 645 CG LEU A 81 3588 3671 3970 -31 -93 132 C ATOM 646 CD1 LEU A 81 20.300 2.580 13.757 1.00 29.22 C ANISOU 646 CD1 LEU A 81 3630 3366 4104 5 -253 -281 C ATOM 647 CD2 LEU A 81 22.417 2.409 12.426 1.00 29.15 C ANISOU 647 CD2 LEU A 81 3808 3224 4041 -607 -26 -203 C ATOM 648 N GLY A 82 24.321 1.398 17.376 1.00 23.00 N ANISOU 648 N GLY A 82 2592 2012 4135 -162 -653 728 N ATOM 649 CA GLY A 82 25.638 1.232 17.973 1.00 22.58 C ANISOU 649 CA GLY A 82 2495 2034 4048 48 -519 715 C ATOM 650 C GLY A 82 25.794 -0.142 18.595 1.00 21.81 C ANISOU 650 C GLY A 82 2421 2110 3756 -7 -130 815 C ATOM 651 O GLY A 82 26.825 -0.794 18.419 1.00 22.33 O ANISOU 651 O GLY A 82 2345 1923 4216 -38 -246 862 O ATOM 652 N ARG A 83 24.759 -0.596 19.299 1.00 20.32 N ANISOU 652 N ARG A 83 2253 1850 3616 -154 -384 687 N ATOM 653 CA ARG A 83 24.797 -1.915 19.943 1.00 19.10 C ANISOU 653 CA ARG A 83 2392 1891 2973 24 -118 583 C ATOM 654 C ARG A 83 24.728 -3.045 18.906 1.00 18.86 C ANISOU 654 C ARG A 83 2273 1780 3113 -108 -297 591 C ATOM 655 O ARG A 83 25.412 -4.076 19.042 1.00 18.16 O ANISOU 655 O ARG A 83 2233 1755 2910 -133 -206 666 O ATOM 656 CB ARG A 83 23.696 -2.045 21.003 1.00 20.57 C ANISOU 656 CB ARG A 83 2578 2232 3003 21 16 29 C ATOM 657 CG ARG A 83 23.893 -1.114 22.197 1.00 22.05 C ANISOU 657 CG ARG A 83 2630 2090 3655 153 -303 -301 C ATOM 658 CD ARG A 83 22.899 -1.370 23.323 1.00 23.31 C ANISOU 658 CD ARG A 83 2704 2704 3446 145 -394 -480 C ATOM 659 NE ARG A 83 21.535 -0.978 22.974 1.00 23.95 N ANISOU 659 NE ARG A 83 2710 2464 3923 136 -395 -502 N ATOM 660 CZ ARG A 83 20.588 -1.821 22.569 1.00 21.82 C ANISOU 660 CZ ARG A 83 2728 2401 3161 123 -183 -493 C ATOM 661 NH1 ARG A 83 20.845 -3.122 22.462 1.00 20.81 N ANISOU 661 NH1 ARG A 83 2758 2380 2767 124 -100 -464 N ATOM 662 NH2 ARG A 83 19.380 -1.363 22.274 1.00 23.94 N ANISOU 662 NH2 ARG A 83 3088 2587 3421 582 -333 -658 N ATOM 663 N TYR A 84 23.919 -2.829 17.867 1.00 18.06 N ANISOU 663 N TYR A 84 2073 1812 2976 -325 -230 535 N ATOM 664 CA TYR A 84 23.811 -3.742 16.723 1.00 17.70 C ANISOU 664 CA TYR A 84 1974 1954 2797 -67 12 592 C ATOM 665 C TYR A 84 25.158 -3.904 16.017 1.00 18.26 C ANISOU 665 C TYR A 84 2113 1810 3014 -155 270 788 C ATOM 666 O TYR A 84 25.615 -5.032 15.810 1.00 18.69 O ANISOU 666 O TYR A 84 1991 1883 3225 -43 439 1025 O ATOM 667 CB TYR A 84 22.711 -3.257 15.764 1.00 17.17 C ANISOU 667 CB TYR A 84 2056 1837 2630 60 24 481 C ATOM 668 CG TYR A 84 22.592 -3.959 14.419 1.00 17.55 C ANISOU 668 CG TYR A 84 2130 2041 2495 133 68 480 C ATOM 669 CD1 TYR A 84 22.833 -5.328 14.272 1.00 17.15 C ANISOU 669 CD1 TYR A 84 1787 1990 2737 -62 109 484 C ATOM 670 CD2 TYR A 84 22.170 -3.250 13.289 1.00 19.26 C ANISOU 670 CD2 TYR A 84 2667 2308 2341 377 295 563 C ATOM 671 CE1 TYR A 84 22.717 -5.949 13.034 1.00 18.47 C ANISOU 671 CE1 TYR A 84 2000 2330 2684 162 141 337 C ATOM 672 CE2 TYR A 84 22.031 -3.870 12.053 1.00 21.57 C ANISOU 672 CE2 TYR A 84 2903 2712 2577 228 563 304 C ATOM 673 CZ TYR A 84 22.310 -5.217 11.925 1.00 20.01 C ANISOU 673 CZ TYR A 84 2629 2645 2327 98 357 295 C ATOM 674 OH TYR A 84 22.168 -5.825 10.687 1.00 22.79 O ANISOU 674 OH TYR A 84 3217 2953 2486 493 629 57 O ATOM 675 N MET A 85 25.800 -2.784 15.673 1.00 20.30 N ANISOU 675 N MET A 85 2094 1987 3632 -175 301 1083 N ATOM 676 CA MET A 85 27.103 -2.834 15.005 1.00 20.83 C ANISOU 676 CA MET A 85 2221 2272 3419 -354 382 1170 C ATOM 677 C MET A 85 28.185 -3.473 15.884 1.00 20.32 C ANISOU 677 C MET A 85 2262 2045 3411 -313 315 1020 C ATOM 678 O MET A 85 28.997 -4.259 15.393 1.00 22.45 O ANISOU 678 O MET A 85 2257 2318 3954 -111 399 1162 O ATOM 679 CB MET A 85 27.547 -1.448 14.528 1.00 20.71 C ANISOU 679 CB MET A 85 2158 2108 3600 -367 112 1054 C ATOM 680 CG MET A 85 26.777 -0.888 13.329 1.00 24.29 C ANISOU 680 CG MET A 85 2388 2263 4576 -240 -510 1216 C ATOM 681 SD MET A 85 26.850 -1.870 11.814 1.00 27.29 S ANISOU 681 SD MET A 85 2807 3168 4393 359 724 1809 S ATOM 682 CE MET A 85 25.242 -2.654 11.801 1.00 25.35 C ANISOU 682 CE MET A 85 2843 2765 4022 362 563 928 C ATOM 683 N SER A 86 28.176 -3.158 17.180 1.00 20.25 N ANISOU 683 N SER A 86 2189 1865 3640 -349 19 831 N ATOM 684 CA SER A 86 29.142 -3.744 18.114 1.00 20.51 C ANISOU 684 CA SER A 86 2358 1910 3522 -411 -38 810 C ATOM 685 C SER A 86 29.024 -5.269 18.140 1.00 19.79 C ANISOU 685 C SER A 86 1975 1912 3631 -492 17 866 C ATOM 686 O SER A 86 30.031 -5.980 18.159 1.00 20.72 O ANISOU 686 O SER A 86 2059 2134 3678 -320 -156 693 O ATOM 687 CB SER A 86 28.969 -3.173 19.522 1.00 22.46 C ANISOU 687 CB SER A 86 2726 2126 3680 -483 -192 453 C ATOM 688 OG SER A 86 29.374 -1.815 19.569 1.00 25.96 O ANISOU 688 OG SER A 86 2766 2280 4816 -650 -25 235 O ATOM 689 N ALA A 87 27.794 -5.770 18.113 1.00 18.38 N ANISOU 689 N ALA A 87 1948 1722 3311 -423 -51 690 N ATOM 690 CA ALA A 87 27.582 -7.213 18.090 1.00 16.92 C ANISOU 690 CA ALA A 87 1895 1707 2825 -360 223 591 C ATOM 691 C ALA A 87 28.000 -7.796 16.738 1.00 16.71 C ANISOU 691 C ALA A 87 1995 1634 2718 -129 193 690 C ATOM 692 O ALA A 87 28.622 -8.858 16.678 1.00 16.24 O ANISOU 692 O ALA A 87 1750 1730 2686 -70 174 646 O ATOM 693 CB ALA A 87 26.130 -7.547 18.397 1.00 16.80 C ANISOU 693 CB ALA A 87 1682 1777 2921 -148 65 610 C ATOM 694 N LEU A 88 27.673 -7.086 15.657 1.00 15.91 N ANISOU 694 N LEU A 88 1838 1697 2511 -362 248 692 N ATOM 695 CA LEU A 88 27.903 -7.592 14.307 1.00 16.68 C ANISOU 695 CA LEU A 88 1911 1915 2510 112 205 730 C ATOM 696 C LEU A 88 29.378 -7.799 14.007 1.00 17.87 C ANISOU 696 C LEU A 88 1934 2113 2742 -51 310 829 C ATOM 697 O LEU A 88 29.752 -8.712 13.275 1.00 19.44 O ANISOU 697 O LEU A 88 1853 2152 3380 61 749 901 O ATOM 698 CB LEU A 88 27.289 -6.656 13.265 1.00 16.90 C ANISOU 698 CB LEU A 88 2100 1994 2325 139 317 806 C ATOM 699 CG LEU A 88 27.434 -7.036 11.785 1.00 16.71 C ANISOU 699 CG LEU A 88 2140 1925 2280 209 251 861 C ATOM 700 CD1 LEU A 88 26.763 -8.372 11.504 1.00 19.32 C ANISOU 700 CD1 LEU A 88 2705 1894 2740 127 204 638 C ATOM 701 CD2 LEU A 88 26.858 -5.948 10.887 1.00 18.54 C ANISOU 701 CD2 LEU A 88 2631 2030 2382 594 267 813 C ATOM 702 N ASN A 89 30.213 -6.943 14.576 1.00 19.81 N ANISOU 702 N ASN A 89 1731 2481 3313 -256 236 1001 N ATOM 703 CA ASN A 89 31.640 -7.086 14.380 1.00 21.22 C ANISOU 703 CA ASN A 89 1830 2376 3856 71 298 847 C ATOM 704 C ASN A 89 32.141 -8.458 14.847 1.00 21.57 C ANISOU 704 C ASN A 89 2298 2410 3485 118 293 937 C ATOM 705 O ASN A 89 33.115 -8.978 14.298 1.00 23.70 O ANISOU 705 O ASN A 89 2287 2635 4083 64 551 1076 O ATOM 706 CB ASN A 89 32.381 -5.959 15.079 1.00 24.12 C ANISOU 706 CB ASN A 89 2182 2531 4449 -72 192 563 C ATOM 707 CG ASN A 89 33.820 -5.840 14.620 1.00 25.57 C ANISOU 707 CG ASN A 89 2473 2753 4489 -12 635 521 C ATOM 708 OD1 ASN A 89 34.111 -5.863 13.423 1.00 28.76 O ANISOU 708 OD1 ASN A 89 2813 3351 4761 -314 963 892 O ATOM 709 ND2 ASN A 89 34.724 -5.719 15.571 1.00 32.47 N ANISOU 709 ND2 ASN A 89 3584 3765 4986 -211 -68 -159 N ATOM 710 N HIS A 90 31.464 -9.039 15.842 1.00 18.85 N ANISOU 710 N HIS A 90 1651 2111 3398 33 125 678 N ATOM 711 CA HIS A 90 31.789 -10.391 16.317 1.00 17.63 C ANISOU 711 CA HIS A 90 1682 2136 2878 137 -25 497 C ATOM 712 C HIS A 90 31.021 -11.467 15.603 1.00 17.41 C ANISOU 712 C HIS A 90 1524 2188 2902 -37 76 565 C ATOM 713 O HIS A 90 31.592 -12.497 15.252 1.00 18.77 O ANISOU 713 O HIS A 90 1564 2357 3209 24 148 446 O ATOM 714 CB HIS A 90 31.548 -10.537 17.813 1.00 20.28 C ANISOU 714 CB HIS A 90 2462 2546 2696 82 -344 304 C ATOM 715 CG HIS A 90 32.361 -9.597 18.660 1.00 22.12 C ANISOU 715 CG HIS A 90 2494 2980 2928 23 -593 248 C ATOM 716 ND1 HIS A 90 33.633 -9.858 19.019 1.00 27.83 N ANISOU 716 ND1 HIS A 90 2567 4133 3870 316 -664 -89 N ATOM 717 CD2 HIS A 90 32.032 -8.374 19.235 1.00 22.22 C ANISOU 717 CD2 HIS A 90 2995 2423 3023 49 -733 776 C ATOM 718 CE1 HIS A 90 34.099 -8.847 19.774 1.00 28.31 C ANISOU 718 CE1 HIS A 90 2938 3778 4039 105 -744 120 C ATOM 719 NE2 HIS A 90 33.120 -7.936 19.903 1.00 26.58 N ANISOU 719 NE2 HIS A 90 2963 3272 3865 27 -1042 603 N ATOM 720 N THR A 91 29.719 -11.263 15.385 1.00 16.30 N ANISOU 720 N THR A 91 1544 1900 2747 -76 135 669 N ATOM 721 CA THR A 91 28.916 -12.338 14.791 1.00 15.36 C ANISOU 721 CA THR A 91 1359 1889 2588 184 87 452 C ATOM 722 C THR A 91 29.277 -12.607 13.326 1.00 15.58 C ANISOU 722 C THR A 91 1520 1943 2456 -76 101 561 C ATOM 723 O THR A 91 29.061 -13.719 12.836 1.00 15.88 O ANISOU 723 O THR A 91 1654 1830 2548 87 151 627 O ATOM 724 CB THR A 91 27.399 -12.095 14.906 1.00 13.53 C ANISOU 724 CB THR A 91 1328 1670 2140 53 220 630 C ATOM 725 OG1 THR A 91 27.035 -10.963 14.102 1.00 15.30 O ANISOU 725 OG1 THR A 91 1628 1736 2446 -78 12 793 O ATOM 726 CG2 THR A 91 26.973 -11.876 16.368 1.00 15.01 C ANISOU 726 CG2 THR A 91 1846 1758 2097 42 145 434 C ATOM 727 N LYS A 92 29.821 -11.604 12.624 1.00 17.79 N ANISOU 727 N LYS A 92 1720 2155 2883 -61 401 676 N ATOM 728 CA LYS A 92 30.283 -11.826 11.250 1.00 18.73 C ANISOU 728 CA LYS A 92 2079 2249 2785 118 396 793 C ATOM 729 C LYS A 92 31.407 -12.870 11.181 1.00 18.71 C ANISOU 729 C LYS A 92 2175 2234 2697 183 366 612 C ATOM 730 O LYS A 92 31.643 -13.451 10.121 1.00 21.44 O ANISOU 730 O LYS A 92 2551 3050 2543 258 614 645 O ATOM 731 CB LYS A 92 30.692 -10.515 10.548 1.00 21.54 C ANISOU 731 CB LYS A 92 2503 2458 3221 -109 774 900 C ATOM 732 CG LYS A 92 31.948 -9.846 11.085 1.00 23.81 C ANISOU 732 CG LYS A 92 2982 2335 3730 -131 478 745 C ATOM 733 CD LYS A 92 32.194 -8.513 10.390 1.00 26.75 C ANISOU 733 CD LYS A 92 3444 2675 4043 -29 385 1210 C ATOM 734 CE LYS A 92 33.661 -8.123 10.455 1.00 32.78 C ANISOU 734 CE LYS A 92 3450 4503 4500 -198 245 429 C ATOM 735 NZ LYS A 92 34.204 -8.199 11.839 1.00 35.27 N ANISOU 735 NZ LYS A 92 3507 5709 4185 -12 783 1227 N ATOM 736 N LYS A 93 32.063 -13.122 12.316 1.00 17.30 N ANISOU 736 N LYS A 93 1666 2237 2670 122 591 612 N ATOM 737 CA LYS A 93 33.155 -14.105 12.410 1.00 17.50 C ANISOU 737 CA LYS A 93 1875 2003 2772 100 178 538 C ATOM 738 C LYS A 93 32.646 -15.507 12.754 1.00 15.75 C ANISOU 738 C LYS A 93 1580 2066 2337 61 521 391 C ATOM 739 O LYS A 93 33.394 -16.479 12.671 1.00 18.14 O ANISOU 739 O LYS A 93 1889 2080 2922 218 357 407 O ATOM 740 CB LYS A 93 34.185 -13.678 13.467 1.00 19.47 C ANISOU 740 CB LYS A 93 1762 2456 3178 -81 58 469 C ATOM 741 CG LYS A 93 34.776 -12.290 13.254 1.00 24.31 C ANISOU 741 CG LYS A 93 2711 2484 4039 -323 55 422 C ATOM 742 CD LYS A 93 35.725 -11.908 14.382 1.00 28.43 C ANISOU 742 CD LYS A 93 2842 3317 4642 -387 -214 231 C ATOM 743 CE LYS A 93 36.197 -10.470 14.227 1.00 31.90 C ANISOU 743 CE LYS A 93 3465 3477 5178 -686 -188 230 C ATOM 744 NZ LYS A 93 37.075 -10.050 15.353 1.00 38.96 N ANISOU 744 NZ LYS A 93 4898 5167 4735 -875 -411 118 N ATOM 745 N TRP A 94 31.389 -15.608 13.179 1.00 15.49 N ANISOU 745 N TRP A 94 1486 2173 2227 29 293 534 N ATOM 746 CA TRP A 94 30.811 -16.913 13.472 1.00 14.99 C ANISOU 746 CA TRP A 94 1580 2134 1977 9 306 287 C ATOM 747 C TRP A 94 30.598 -17.737 12.232 1.00 15.11 C ANISOU 747 C TRP A 94 1729 1926 2085 -22 311 261 C ATOM 748 O TRP A 94 30.511 -17.203 11.119 1.00 17.18 O ANISOU 748 O TRP A 94 2091 2163 2273 17 250 450 O ATOM 749 CB TRP A 94 29.495 -16.765 14.215 1.00 14.41 C ANISOU 749 CB TRP A 94 1453 2103 1918 34 181 438 C ATOM 750 CG TRP A 94 29.612 -16.155 15.588 1.00 13.48 C ANISOU 750 CG TRP A 94 1413 1760 1948 52 118 483 C ATOM 751 CD1 TRP A 94 30.772 -15.853 16.314 1.00 14.32 C ANISOU 751 CD1 TRP A 94 1695 1891 1854 -6 23 376 C ATOM 752 CD2 TRP A 94 28.502 -15.790 16.462 1.00 13.42 C ANISOU 752 CD2 TRP A 94 1568 1746 1782 56 163 446 C ATOM 753 NE1 TRP A 94 30.449 -15.331 17.544 1.00 14.58 N ANISOU 753 NE1 TRP A 94 1443 2224 1870 52 -43 252 N ATOM 754 CE2 TRP A 94 29.094 -15.267 17.692 1.00 13.72 C ANISOU 754 CE2 TRP A 94 1464 1946 1803 -40 165 442 C ATOM 755 CE3 TRP A 94 27.114 -15.847 16.349 1.00 12.62 C ANISOU 755 CE3 TRP A 94 1570 1644 1580 -31 -21 446 C ATOM 756 CZ2 TRP A 94 28.312 -14.815 18.747 1.00 13.59 C ANISOU 756 CZ2 TRP A 94 1517 1849 1798 170 97 489 C ATOM 757 CZ3 TRP A 94 26.336 -15.403 17.420 1.00 13.10 C ANISOU 757 CZ3 TRP A 94 1773 1450 1751 102 -66 138 C ATOM 758 CH2 TRP A 94 26.923 -14.895 18.590 1.00 13.08 C ANISOU 758 CH2 TRP A 94 1606 1673 1689 -113 -27 247 C ATOM 759 N LYS A 95 30.523 -19.051 12.429 1.00 13.72 N ANISOU 759 N LYS A 95 1509 1791 1912 62 164 38 N ATOM 760 CA LYS A 95 30.211 -19.986 11.352 1.00 13.86 C ANISOU 760 CA LYS A 95 1582 2033 1650 1 191 126 C ATOM 761 C LYS A 95 28.790 -20.510 11.508 1.00 12.76 C ANISOU 761 C LYS A 95 1534 1867 1445 130 219 261 C ATOM 762 O LYS A 95 28.351 -20.808 12.620 1.00 13.42 O ANISOU 762 O LYS A 95 1777 1749 1570 175 352 336 O ATOM 763 CB LYS A 95 31.209 -21.150 11.335 1.00 17.42 C ANISOU 763 CB LYS A 95 2085 2363 2171 407 207 193 C ATOM 764 CG LYS A 95 32.669 -20.738 11.168 1.00 24.11 C ANISOU 764 CG LYS A 95 2413 3465 3283 -147 351 141 C ATOM 765 CD LYS A 95 32.927 -19.903 9.921 1.00 27.24 C ANISOU 765 CD LYS A 95 2777 4227 3345 25 693 335 C ATOM 766 CE LYS A 95 34.371 -19.420 9.880 1.00 33.47 C ANISOU 766 CE LYS A 95 3036 5512 4168 -466 962 303 C ATOM 767 NZ LYS A 95 34.621 -18.527 8.717 1.00 38.72 N ANISOU 767 NZ LYS A 95 4289 5738 4685 -461 661 729 N ATOM 768 N PHE A 96 28.089 -20.623 10.382 1.00 13.30 N ANISOU 768 N PHE A 96 1538 1821 1691 186 -5 399 N ATOM 769 CA PHE A 96 26.679 -20.996 10.366 1.00 13.38 C ANISOU 769 CA PHE A 96 1599 1844 1637 173 27 230 C ATOM 770 C PHE A 96 26.470 -22.237 9.512 1.00 15.01 C ANISOU 770 C PHE A 96 2017 1782 1901 63 1 209 C ATOM 771 O PHE A 96 25.932 -22.153 8.408 1.00 17.66 O ANISOU 771 O PHE A 96 2654 2097 1958 123 -179 124 O ATOM 772 CB PHE A 96 25.835 -19.818 9.865 1.00 14.42 C ANISOU 772 CB PHE A 96 2009 1816 1651 256 -58 290 C ATOM 773 CG PHE A 96 26.006 -18.577 10.691 1.00 13.94 C ANISOU 773 CG PHE A 96 1741 1866 1689 120 26 257 C ATOM 774 CD1 PHE A 96 25.382 -18.469 11.931 1.00 13.67 C ANISOU 774 CD1 PHE A 96 1652 1830 1709 252 62 396 C ATOM 775 CD2 PHE A 96 26.818 -17.531 10.256 1.00 15.12 C ANISOU 775 CD2 PHE A 96 1929 1785 2029 195 66 434 C ATOM 776 CE1 PHE A 96 25.553 -17.341 12.718 1.00 15.65 C ANISOU 776 CE1 PHE A 96 1966 1902 2078 289 -131 257 C ATOM 777 CE2 PHE A 96 26.985 -16.397 11.040 1.00 16.00 C ANISOU 777 CE2 PHE A 96 2099 1986 1994 204 -44 315 C ATOM 778 CZ PHE A 96 26.345 -16.300 12.267 1.00 16.05 C ANISOU 778 CZ PHE A 96 1922 2051 2122 294 0 325 C ATOM 779 N PRO A 97 26.913 -23.405 10.015 1.00 13.85 N ANISOU 779 N PRO A 97 1841 1861 1558 291 98 53 N ATOM 780 CA PRO A 97 26.744 -24.631 9.246 1.00 14.89 C ANISOU 780 CA PRO A 97 1970 1785 1902 201 62 49 C ATOM 781 C PRO A 97 25.282 -25.040 9.155 1.00 13.88 C ANISOU 781 C PRO A 97 1883 1909 1481 281 254 -149 C ATOM 782 O PRO A 97 24.483 -24.707 10.045 1.00 14.32 O ANISOU 782 O PRO A 97 1960 2050 1429 278 342 17 O ATOM 783 CB PRO A 97 27.522 -25.666 10.060 1.00 14.36 C ANISOU 783 CB PRO A 97 1786 1818 1850 269 197 64 C ATOM 784 CG PRO A 97 27.469 -25.162 11.461 1.00 14.70 C ANISOU 784 CG PRO A 97 2022 1688 1874 124 81 43 C ATOM 785 CD PRO A 97 27.508 -23.659 11.340 1.00 14.08 C ANISOU 785 CD PRO A 97 1782 1732 1834 313 -63 415 C ATOM 786 N GLN A 98 24.941 -25.734 8.072 1.00 14.67 N ANISOU 786 N GLN A 98 2097 1956 1517 297 198 -180 N ATOM 787 CA GLN A 98 23.652 -26.389 7.956 1.00 14.43 C ANISOU 787 CA GLN A 98 2204 1915 1360 243 151 -160 C ATOM 788 C GLN A 98 23.706 -27.734 8.653 1.00 14.96 C ANISOU 788 C GLN A 98 2158 1926 1600 299 251 -61 C ATOM 789 O GLN A 98 24.517 -28.590 8.301 1.00 17.59 O ANISOU 789 O GLN A 98 2419 2037 2224 444 478 -53 O ATOM 790 CB GLN A 98 23.281 -26.568 6.490 1.00 14.97 C ANISOU 790 CB GLN A 98 2377 2030 1278 671 85 7 C ATOM 791 CG GLN A 98 23.191 -25.240 5.740 1.00 15.77 C ANISOU 791 CG GLN A 98 2372 1908 1711 643 101 43 C ATOM 792 CD GLN A 98 22.057 -24.354 6.234 1.00 14.36 C ANISOU 792 CD GLN A 98 2121 2129 1206 428 19 -158 C ATOM 793 OE1 GLN A 98 22.240 -23.153 6.507 1.00 17.79 O ANISOU 793 OE1 GLN A 98 3017 2215 1524 352 289 -340 O ATOM 794 NE2 GLN A 98 20.880 -24.937 6.353 1.00 13.86 N ANISOU 794 NE2 GLN A 98 2176 1886 1203 307 3 -54 N ATOM 795 N VAL A 99 22.860 -27.904 9.667 1.00 14.04 N ANISOU 795 N VAL A 99 2171 1747 1414 232 149 21 N ATOM 796 CA VAL A 99 22.850 -29.123 10.475 1.00 14.52 C ANISOU 796 CA VAL A 99 2335 1824 1355 238 104 56 C ATOM 797 C VAL A 99 21.415 -29.623 10.500 1.00 14.88 C ANISOU 797 C VAL A 99 2308 1721 1625 286 168 101 C ATOM 798 O VAL A 99 20.504 -28.896 10.914 1.00 15.64 O ANISOU 798 O VAL A 99 2284 1970 1688 340 307 132 O ATOM 799 CB VAL A 99 23.345 -28.877 11.924 1.00 14.42 C ANISOU 799 CB VAL A 99 2326 1881 1272 346 235 -4 C ATOM 800 CG1 VAL A 99 23.428 -30.189 12.697 1.00 17.04 C ANISOU 800 CG1 VAL A 99 2673 1715 2086 511 379 94 C ATOM 801 CG2 VAL A 99 24.697 -28.176 11.923 1.00 15.82 C ANISOU 801 CG2 VAL A 99 2228 2130 1650 314 15 -26 C ATOM 802 N GLY A 100 21.208 -30.847 10.023 1.00 17.01 N ANISOU 802 N GLY A 100 2625 1799 2036 21 21 66 N ATOM 803 CA GLY A 100 19.864 -31.390 9.896 1.00 17.64 C ANISOU 803 CA GLY A 100 2480 2044 2176 66 211 8 C ATOM 804 C GLY A 100 18.941 -30.500 9.077 1.00 16.02 C ANISOU 804 C GLY A 100 2511 1717 1858 3 224 -229 C ATOM 805 O GLY A 100 17.748 -30.421 9.359 1.00 20.01 O ANISOU 805 O GLY A 100 2402 2593 2606 1 154 -215 O ATOM 806 N GLY A 101 19.494 -29.829 8.062 1.00 16.72 N ANISOU 806 N GLY A 101 2999 1776 1575 194 236 -231 N ATOM 807 CA GLY A 101 18.712 -28.949 7.201 1.00 17.39 C ANISOU 807 CA GLY A 101 2842 2003 1763 177 -118 -446 C ATOM 808 C GLY A 101 18.420 -27.568 7.758 1.00 15.43 C ANISOU 808 C GLY A 101 2390 2001 1469 52 14 -378 C ATOM 809 O GLY A 101 17.726 -26.784 7.116 1.00 16.89 O ANISOU 809 O GLY A 101 2406 2514 1495 162 -224 -411 O ATOM 810 N LEU A 102 18.950 -27.275 8.948 1.00 13.02 N ANISOU 810 N LEU A 102 2075 1560 1311 27 101 -106 N ATOM 811 CA LEU A 102 18.696 -26.005 9.621 1.00 12.41 C ANISOU 811 CA LEU A 102 1826 1656 1232 73 198 -85 C ATOM 812 C LEU A 102 19.975 -25.197 9.720 1.00 12.59 C ANISOU 812 C LEU A 102 1747 1701 1334 158 -1 -47 C ATOM 813 O LEU A 102 21.060 -25.764 9.859 1.00 13.08 O ANISOU 813 O LEU A 102 1664 1929 1374 201 94 -75 O ATOM 814 CB LEU A 102 18.144 -26.253 11.027 1.00 13.69 C ANISOU 814 CB LEU A 102 1958 1989 1254 -122 218 -24 C ATOM 815 CG LEU A 102 16.832 -27.032 11.117 1.00 15.00 C ANISOU 815 CG LEU A 102 1985 2060 1653 -199 -27 175 C ATOM 816 CD1 LEU A 102 16.618 -27.589 12.521 1.00 17.91 C ANISOU 816 CD1 LEU A 102 2500 2663 1642 -51 44 298 C ATOM 817 CD2 LEU A 102 15.670 -26.140 10.692 1.00 20.15 C ANISOU 817 CD2 LEU A 102 2263 2373 3018 34 -93 521 C ATOM 818 N THR A 103 19.860 -23.873 9.657 1.00 11.61 N ANISOU 818 N THR A 103 1686 1674 1050 91 73 -85 N ATOM 819 CA THR A 103 21.016 -23.028 9.933 1.00 12.07 C ANISOU 819 CA THR A 103 1698 1698 1190 110 -77 -29 C ATOM 820 C THR A 103 21.287 -23.066 11.434 1.00 11.67 C ANISOU 820 C THR A 103 1559 1685 1188 133 -18 38 C ATOM 821 O THR A 103 20.446 -22.651 12.246 1.00 12.39 O ANISOU 821 O THR A 103 1660 1802 1243 121 144 165 O ATOM 822 CB THR A 103 20.792 -21.574 9.512 1.00 12.41 C ANISOU 822 CB THR A 103 1715 1753 1246 91 -124 53 C ATOM 823 OG1 THR A 103 20.388 -21.547 8.145 1.00 12.45 O ANISOU 823 OG1 THR A 103 1772 1789 1167 88 -40 111 O ATOM 824 CG2 THR A 103 22.076 -20.773 9.659 1.00 13.40 C ANISOU 824 CG2 THR A 103 1820 1743 1529 -61 41 132 C ATOM 825 N SER A 104 22.469 -23.556 11.792 1.00 11.72 N ANISOU 825 N SER A 104 1577 1575 1298 152 -37 90 N ATOM 826 CA SER A 104 22.900 -23.578 13.178 1.00 11.74 C ANISOU 826 CA SER A 104 1608 1546 1306 88 -49 156 C ATOM 827 C SER A 104 24.046 -22.584 13.376 1.00 11.51 C ANISOU 827 C SER A 104 1448 1738 1187 123 32 48 C ATOM 828 O SER A 104 24.369 -21.814 12.469 1.00 13.37 O ANISOU 828 O SER A 104 1650 2067 1362 32 0 270 O ATOM 829 CB SER A 104 23.300 -24.998 13.578 1.00 11.61 C ANISOU 829 CB SER A 104 1534 1615 1260 183 117 199 C ATOM 830 OG SER A 104 23.395 -25.082 14.986 1.00 12.43 O ANISOU 830 OG SER A 104 1678 1786 1259 64 98 209 O ATOM 831 N ILE A 105 24.623 -22.553 14.575 1.00 11.47 N ANISOU 831 N ILE A 105 1435 1575 1345 79 -146 21 N ATOM 832 CA ILE A 105 25.802 -21.716 14.817 1.00 11.98 C ANISOU 832 CA ILE A 105 1425 1610 1516 83 -144 59 C ATOM 833 C ILE A 105 26.885 -22.548 15.488 1.00 11.99 C ANISOU 833 C ILE A 105 1421 1601 1532 168 67 254 C ATOM 834 O ILE A 105 26.643 -23.129 16.542 1.00 12.72 O ANISOU 834 O ILE A 105 1433 1790 1608 98 69 387 O ATOM 835 CB ILE A 105 25.530 -20.483 15.716 1.00 12.41 C ANISOU 835 CB ILE A 105 1479 1627 1608 104 39 74 C ATOM 836 CG1 ILE A 105 24.142 -19.888 15.462 1.00 11.97 C ANISOU 836 CG1 ILE A 105 1589 1583 1374 154 -113 41 C ATOM 837 CG2 ILE A 105 26.646 -19.460 15.510 1.00 13.44 C ANISOU 837 CG2 ILE A 105 1713 1713 1678 -55 -86 203 C ATOM 838 CD1 ILE A 105 23.778 -18.775 16.425 1.00 12.49 C ANISOU 838 CD1 ILE A 105 1787 1492 1463 107 32 57 C ATOM 839 N LYS A 106 28.081 -22.581 14.907 1.00 11.94 N ANISOU 839 N LYS A 106 1467 1581 1488 216 59 153 N ATOM 840 CA LYS A 106 29.193 -23.254 15.568 1.00 13.45 C ANISOU 840 CA LYS A 106 1514 1928 1665 436 129 261 C ATOM 841 C LYS A 106 29.498 -22.522 16.874 1.00 12.12 C ANISOU 841 C LYS A 106 1311 1609 1684 415 78 335 C ATOM 842 O LYS A 106 29.423 -21.295 16.934 1.00 12.11 O ANISOU 842 O LYS A 106 1393 1592 1614 206 80 280 O ATOM 843 CB LYS A 106 30.424 -23.313 14.657 1.00 14.09 C ANISOU 843 CB LYS A 106 1551 2090 1713 266 220 430 C ATOM 844 CG LYS A 106 31.582 -24.132 15.225 1.00 16.04 C ANISOU 844 CG LYS A 106 1647 2653 1792 439 36 312 C ATOM 845 CD LYS A 106 32.645 -24.401 14.168 1.00 18.60 C ANISOU 845 CD LYS A 106 1999 2858 2210 459 327 2 C ATOM 846 CE LYS A 106 33.743 -25.282 14.744 1.00 22.78 C ANISOU 846 CE LYS A 106 2493 3669 2493 963 3 -193 C ATOM 847 NZ LYS A 106 34.593 -24.533 15.708 1.00 26.60 N ANISOU 847 NZ LYS A 106 2883 4458 2767 605 -66 -422 N ATOM 848 N TRP A 107 29.819 -23.265 17.930 1.00 12.21 N ANISOU 848 N TRP A 107 1201 1950 1486 266 -25 295 N ATOM 849 CA TRP A 107 29.964 -22.620 19.230 1.00 12.43 C ANISOU 849 CA TRP A 107 1490 1724 1508 135 -12 341 C ATOM 850 C TRP A 107 31.103 -21.616 19.302 1.00 12.61 C ANISOU 850 C TRP A 107 1569 1682 1541 126 2 354 C ATOM 851 O TRP A 107 32.240 -21.896 18.907 1.00 13.58 O ANISOU 851 O TRP A 107 1481 2000 1678 208 -171 247 O ATOM 852 CB TRP A 107 30.074 -23.646 20.360 1.00 13.36 C ANISOU 852 CB TRP A 107 1849 1713 1515 416 103 340 C ATOM 853 CG TRP A 107 29.983 -22.967 21.699 1.00 12.68 C ANISOU 853 CG TRP A 107 1575 1714 1527 291 86 314 C ATOM 854 CD1 TRP A 107 28.829 -22.691 22.426 1.00 13.93 C ANISOU 854 CD1 TRP A 107 1767 2029 1494 347 198 294 C ATOM 855 CD2 TRP A 107 31.077 -22.348 22.467 1.00 12.71 C ANISOU 855 CD2 TRP A 107 1478 1948 1402 348 1 527 C ATOM 856 NE1 TRP A 107 29.129 -21.994 23.566 1.00 14.59 N ANISOU 856 NE1 TRP A 107 1589 2107 1845 53 39 81 N ATOM 857 CE2 TRP A 107 30.458 -21.759 23.654 1.00 13.76 C ANISOU 857 CE2 TRP A 107 1520 2025 1682 272 132 357 C ATOM 858 CE3 TRP A 107 32.458 -22.233 22.296 1.00 14.33 C ANISOU 858 CE3 TRP A 107 1445 2493 1504 308 -217 527 C ATOM 859 CZ2 TRP A 107 31.203 -21.094 24.617 1.00 15.37 C ANISOU 859 CZ2 TRP A 107 1588 2347 1903 208 -11 221 C ATOM 860 CZ3 TRP A 107 33.200 -21.565 23.275 1.00 16.50 C ANISOU 860 CZ3 TRP A 107 1705 2854 1708 450 -192 85 C ATOM 861 CH2 TRP A 107 32.586 -21.002 24.403 1.00 15.61 C ANISOU 861 CH2 TRP A 107 1566 2737 1627 350 -68 236 C ATOM 862 N ALA A 108 30.785 -20.436 19.827 1.00 12.56 N ANISOU 862 N ALA A 108 1460 1626 1684 142 -125 332 N ATOM 863 CA ALA A 108 31.758 -19.368 20.085 1.00 12.20 C ANISOU 863 CA ALA A 108 1683 1508 1441 101 -150 369 C ATOM 864 C ALA A 108 31.060 -18.349 20.971 1.00 13.37 C ANISOU 864 C ALA A 108 1437 1845 1796 85 -96 114 C ATOM 865 O ALA A 108 29.834 -18.215 20.897 1.00 13.67 O ANISOU 865 O ALA A 108 1427 1849 1918 130 -107 272 O ATOM 866 CB ALA A 108 32.198 -18.708 18.777 1.00 14.10 C ANISOU 866 CB ALA A 108 1984 1826 1545 -164 73 352 C ATOM 867 N ASP A 109 31.814 -17.630 21.804 1.00 13.49 N ANISOU 867 N ASP A 109 1453 1738 1933 -16 -142 233 N ATOM 868 CA ASP A 109 31.281 -16.438 22.476 1.00 14.01 C ANISOU 868 CA ASP A 109 1521 1850 1952 -63 58 229 C ATOM 869 C ASP A 109 29.977 -16.714 23.239 1.00 13.19 C ANISOU 869 C ASP A 109 1432 1696 1881 -99 -66 237 C ATOM 870 O ASP A 109 29.054 -15.898 23.213 1.00 13.96 O ANISOU 870 O ASP A 109 1462 2040 1801 19 -70 138 O ATOM 871 CB ASP A 109 31.048 -15.308 21.452 1.00 14.94 C ANISOU 871 CB ASP A 109 1665 1912 2099 -288 -42 334 C ATOM 872 CG ASP A 109 32.330 -14.835 20.790 1.00 15.30 C ANISOU 872 CG ASP A 109 1447 2148 2215 -102 31 92 C ATOM 873 OD1 ASP A 109 33.301 -14.572 21.532 1.00 16.65 O ANISOU 873 OD1 ASP A 109 1820 2581 1924 -188 -130 283 O ATOM 874 OD2 ASP A 109 32.362 -14.710 19.540 1.00 17.26 O ANISOU 874 OD2 ASP A 109 1669 2588 2300 -308 -18 72 O ATOM 875 N ASN A 110 29.894 -17.871 23.899 1.00 12.86 N ANISOU 875 N ASN A 110 1397 1759 1728 -116 -29 240 N ATOM 876 CA ASN A 110 28.708 -18.191 24.718 1.00 13.30 C ANISOU 876 CA ASN A 110 1406 1946 1698 -54 30 -38 C ATOM 877 C ASN A 110 27.406 -18.147 23.912 1.00 13.31 C ANISOU 877 C ASN A 110 1415 1790 1852 32 -19 58 C ATOM 878 O ASN A 110 26.353 -17.726 24.416 1.00 13.33 O ANISOU 878 O ASN A 110 1352 1946 1767 -37 -86 -151 O ATOM 879 CB ASN A 110 28.626 -17.255 25.932 1.00 13.69 C ANISOU 879 CB ASN A 110 1509 1966 1726 6 -196 -18 C ATOM 880 CG ASN A 110 29.617 -17.624 27.007 1.00 14.34 C ANISOU 880 CG ASN A 110 1527 2069 1850 105 -218 89 C ATOM 881 OD1 ASN A 110 29.991 -18.789 27.141 1.00 16.01 O ANISOU 881 OD1 ASN A 110 1802 2266 2013 330 -160 158 O ATOM 882 ND2 ASN A 110 30.048 -16.637 27.781 1.00 17.89 N ANISOU 882 ND2 ASN A 110 2145 2304 2348 67 -610 -97 N ATOM 883 N ASN A 111 27.471 -18.603 22.666 1.00 12.41 N ANISOU 883 N ASN A 111 1405 1546 1764 -24 -205 200 N ATOM 884 CA ASN A 111 26.315 -18.474 21.780 1.00 12.19 C ANISOU 884 CA ASN A 111 1310 1607 1712 -83 -154 204 C ATOM 885 C ASN A 111 25.349 -19.661 21.689 1.00 11.77 C ANISOU 885 C ASN A 111 1368 1441 1661 -1 -100 131 C ATOM 886 O ASN A 111 24.480 -19.657 20.815 1.00 12.39 O ANISOU 886 O ASN A 111 1201 1806 1698 -69 -50 177 O ATOM 887 CB ASN A 111 26.745 -18.053 20.366 1.00 12.44 C ANISOU 887 CB ASN A 111 1393 1628 1703 114 -92 232 C ATOM 888 CG ASN A 111 27.481 -19.156 19.612 1.00 12.69 C ANISOU 888 CG ASN A 111 1480 1619 1721 78 26 244 C ATOM 889 OD1 ASN A 111 27.599 -20.294 20.082 1.00 12.70 O ANISOU 889 OD1 ASN A 111 1407 1624 1792 34 44 271 O ATOM 890 ND2 ASN A 111 27.997 -18.813 18.436 1.00 13.08 N ANISOU 890 ND2 ASN A 111 1266 1986 1715 68 -7 284 N ATOM 891 N SER A 112 25.459 -20.660 22.571 1.00 12.10 N ANISOU 891 N SER A 112 1288 1565 1744 -60 48 236 N ATOM 892 CA SER A 112 24.560 -21.804 22.442 1.00 11.48 C ANISOU 892 CA SER A 112 1312 1402 1645 67 -15 198 C ATOM 893 C SER A 112 23.096 -21.402 22.616 1.00 11.08 C ANISOU 893 C SER A 112 1338 1437 1432 111 -2 0 C ATOM 894 O SER A 112 22.217 -21.971 21.979 1.00 11.32 O ANISOU 894 O SER A 112 1392 1420 1488 66 -146 172 O ATOM 895 CB SER A 112 24.914 -22.948 23.388 1.00 13.29 C ANISOU 895 CB SER A 112 1637 1738 1673 105 -136 387 C ATOM 896 OG SER A 112 24.328 -22.787 24.663 1.00 13.92 O ANISOU 896 OG SER A 112 1465 1982 1841 236 39 631 O ATOM 897 N TYR A 113 22.821 -20.420 23.470 1.00 9.78 N ANISOU 897 N TYR A 113 1243 1185 1287 53 -4 127 N ATOM 898 CA TYR A 113 21.424 -20.013 23.640 1.00 10.70 C ANISOU 898 CA TYR A 113 1196 1568 1302 -2 -9 -34 C ATOM 899 C TYR A 113 20.900 -19.388 22.348 1.00 10.66 C ANISOU 899 C TYR A 113 1224 1437 1390 -2 56 70 C ATOM 900 O TYR A 113 19.740 -19.579 21.990 1.00 10.96 O ANISOU 900 O TYR A 113 1263 1502 1396 -34 -19 28 O ATOM 901 CB TYR A 113 21.212 -19.116 24.878 1.00 11.07 C ANISOU 901 CB TYR A 113 1524 1377 1303 13 72 47 C ATOM 902 CG TYR A 113 21.593 -17.659 24.703 1.00 10.78 C ANISOU 902 CG TYR A 113 1390 1419 1287 -95 35 46 C ATOM 903 CD1 TYR A 113 20.623 -16.695 24.403 1.00 11.83 C ANISOU 903 CD1 TYR A 113 1584 1547 1365 58 176 154 C ATOM 904 CD2 TYR A 113 22.921 -17.236 24.837 1.00 11.19 C ANISOU 904 CD2 TYR A 113 1388 1508 1354 -78 -2 124 C ATOM 905 CE1 TYR A 113 20.968 -15.363 24.227 1.00 11.44 C ANISOU 905 CE1 TYR A 113 1345 1544 1455 48 -124 53 C ATOM 906 CE2 TYR A 113 23.272 -15.905 24.663 1.00 11.79 C ANISOU 906 CE2 TYR A 113 1530 1473 1475 -100 -1 -52 C ATOM 907 CZ TYR A 113 22.292 -14.969 24.359 1.00 11.26 C ANISOU 907 CZ TYR A 113 1443 1423 1413 -117 8 -160 C ATOM 908 OH TYR A 113 22.607 -13.645 24.176 1.00 12.97 O ANISOU 908 OH TYR A 113 1785 1459 1684 -156 -253 -79 O ATOM 909 N LEU A 114 21.766 -18.653 21.648 1.00 10.75 N ANISOU 909 N LEU A 114 1495 1434 1155 -23 -8 194 N ATOM 910 CA LEU A 114 21.387 -18.050 20.377 1.00 10.08 C ANISOU 910 CA LEU A 114 1293 1424 1113 -83 -58 130 C ATOM 911 C LEU A 114 21.176 -19.107 19.304 1.00 10.07 C ANISOU 911 C LEU A 114 1137 1275 1411 31 -61 32 C ATOM 912 O LEU A 114 20.246 -18.987 18.508 1.00 10.81 O ANISOU 912 O LEU A 114 1267 1485 1354 76 -79 95 O ATOM 913 CB LEU A 114 22.418 -17.014 19.918 1.00 11.34 C ANISOU 913 CB LEU A 114 1404 1401 1502 -169 80 -55 C ATOM 914 CG LEU A 114 22.552 -15.791 20.825 1.00 11.36 C ANISOU 914 CG LEU A 114 1365 1349 1602 -89 -132 -52 C ATOM 915 CD1 LEU A 114 23.828 -15.027 20.514 1.00 13.78 C ANISOU 915 CD1 LEU A 114 1637 1484 2112 -350 -64 -19 C ATOM 916 CD2 LEU A 114 21.342 -14.881 20.692 1.00 12.81 C ANISOU 916 CD2 LEU A 114 1590 1503 1772 126 -20 116 C ATOM 917 N SER A 115 22.021 -20.141 19.276 1.00 10.03 N ANISOU 917 N SER A 115 1278 1250 1280 61 -9 48 N ATOM 918 CA ASER A 115 21.813 -21.209 18.305 0.50 10.90 C ANISOU 918 CA ASER A 115 1364 1325 1451 21 19 -37 C ATOM 919 CA BSER A 115 21.834 -21.233 18.333 0.50 10.23 C ANISOU 919 CA BSER A 115 1239 1297 1350 137 19 -44 C ATOM 920 C SER A 115 20.470 -21.911 18.538 1.00 10.57 C ANISOU 920 C SER A 115 1298 1379 1337 49 -4 -41 C ATOM 921 O SER A 115 19.754 -22.199 17.586 1.00 10.86 O ANISOU 921 O SER A 115 1321 1444 1359 113 -51 -70 O ATOM 922 CB ASER A 115 22.993 -22.189 18.252 0.50 13.09 C ANISOU 922 CB ASER A 115 1467 1678 1826 213 63 59 C ATOM 923 CB BSER A 115 22.982 -22.237 18.444 0.50 9.43 C ANISOU 923 CB BSER A 115 1261 1333 987 192 -36 -366 C ATOM 924 OG ASER A 115 23.307 -22.698 19.527 0.50 16.04 O ANISOU 924 OG ASER A 115 1992 2225 1876 -74 16 251 O ATOM 925 OG BSER A 115 22.981 -23.117 17.337 0.50 7.63 O ANISOU 925 OG BSER A 115 921 1082 894 184 7 -228 O ATOM 926 N SER A 116 20.107 -22.163 19.792 1.00 10.15 N ANISOU 926 N SER A 116 1175 1298 1383 89 24 -21 N ATOM 927 CA SER A 116 18.799 -22.766 20.071 1.00 10.42 C ANISOU 927 CA SER A 116 1226 1315 1417 57 12 21 C ATOM 928 C SER A 116 17.628 -21.857 19.679 1.00 10.12 C ANISOU 928 C SER A 116 1245 1227 1373 5 -24 36 C ATOM 929 O SER A 116 16.605 -22.350 19.204 1.00 10.60 O ANISOU 929 O SER A 116 1199 1455 1374 48 -96 2 O ATOM 930 CB SER A 116 18.695 -23.228 21.534 1.00 10.78 C ANISOU 930 CB SER A 116 1311 1252 1530 44 84 195 C ATOM 931 OG SER A 116 19.293 -24.510 21.698 1.00 11.76 O ANISOU 931 OG SER A 116 1572 1241 1654 54 15 141 O ATOM 932 N VAL A 117 17.771 -20.542 19.867 1.00 10.47 N ANISOU 932 N VAL A 117 1390 1217 1370 87 10 53 N ATOM 933 CA VAL A 117 16.734 -19.599 19.405 1.00 10.19 C ANISOU 933 CA VAL A 117 1374 1241 1254 53 -137 -82 C ATOM 934 C VAL A 117 16.591 -19.683 17.885 1.00 10.35 C ANISOU 934 C VAL A 117 1283 1413 1234 88 19 42 C ATOM 935 O VAL A 117 15.485 -19.837 17.356 1.00 11.30 O ANISOU 935 O VAL A 117 1343 1468 1480 122 -92 2 O ATOM 936 CB VAL A 117 17.058 -18.155 19.840 1.00 10.18 C ANISOU 936 CB VAL A 117 1513 1118 1236 212 -98 -55 C ATOM 937 CG1 VAL A 117 16.174 -17.137 19.124 1.00 12.07 C ANISOU 937 CG1 VAL A 117 1711 1226 1646 233 -281 77 C ATOM 938 CG2 VAL A 117 16.924 -17.994 21.346 1.00 11.30 C ANISOU 938 CG2 VAL A 117 1602 1431 1259 128 -96 -135 C ATOM 939 N LEU A 118 17.722 -19.601 17.188 1.00 10.49 N ANISOU 939 N LEU A 118 1494 1263 1226 31 180 7 N ATOM 940 CA LEU A 118 17.726 -19.635 15.736 1.00 10.50 C ANISOU 940 CA LEU A 118 1273 1463 1251 -40 100 -87 C ATOM 941 C LEU A 118 17.159 -20.951 15.180 1.00 10.16 C ANISOU 941 C LEU A 118 1328 1276 1257 141 -131 35 C ATOM 942 O LEU A 118 16.369 -20.930 14.231 1.00 10.24 O ANISOU 942 O LEU A 118 1437 1464 988 87 -34 99 O ATOM 943 CB LEU A 118 19.154 -19.384 15.235 1.00 10.97 C ANISOU 943 CB LEU A 118 1287 1613 1267 -100 96 56 C ATOM 944 CG LEU A 118 19.400 -19.452 13.721 1.00 11.11 C ANISOU 944 CG LEU A 118 1373 1655 1191 -61 -21 165 C ATOM 945 CD1 LEU A 118 18.513 -18.506 12.910 1.00 14.13 C ANISOU 945 CD1 LEU A 118 1852 1931 1584 140 -147 361 C ATOM 946 CD2 LEU A 118 20.875 -19.193 13.425 1.00 13.05 C ANISOU 946 CD2 LEU A 118 1378 1939 1638 -128 5 80 C ATOM 947 N LEU A 119 17.564 -22.079 15.768 1.00 10.01 N ANISOU 947 N LEU A 119 1323 1248 1230 77 -27 77 N ATOM 948 CA LEU A 119 17.099 -23.386 15.309 1.00 10.08 C ANISOU 948 CA LEU A 119 1266 1321 1243 27 -87 131 C ATOM 949 C LEU A 119 15.588 -23.518 15.475 1.00 10.36 C ANISOU 949 C LEU A 119 1308 1545 1080 -1 122 22 C ATOM 950 O LEU A 119 14.892 -23.988 14.575 1.00 11.28 O ANISOU 950 O LEU A 119 1485 1639 1160 -25 13 36 O ATOM 951 CB LEU A 119 17.839 -24.493 16.057 1.00 10.13 C ANISOU 951 CB LEU A 119 1292 1344 1213 145 0 94 C ATOM 952 CG LEU A 119 19.309 -24.656 15.658 1.00 10.95 C ANISOU 952 CG LEU A 119 1366 1715 1077 218 47 -36 C ATOM 953 CD1 LEU A 119 20.074 -25.449 16.705 1.00 11.99 C ANISOU 953 CD1 LEU A 119 1451 1618 1484 272 43 190 C ATOM 954 CD2 LEU A 119 19.422 -25.321 14.294 1.00 11.94 C ANISOU 954 CD2 LEU A 119 1602 1667 1268 177 152 -236 C ATOM 955 N ALA A 120 15.073 -23.085 16.625 1.00 10.00 N ANISOU 955 N ALA A 120 1323 1374 1103 104 92 10 N ATOM 956 CA ALA A 120 13.634 -23.184 16.879 1.00 10.41 C ANISOU 956 CA ALA A 120 1383 1580 991 -49 120 11 C ATOM 957 C ALA A 120 12.838 -22.301 15.930 1.00 10.98 C ANISOU 957 C ALA A 120 1363 1493 1313 16 3 -44 C ATOM 958 O ALA A 120 11.832 -22.742 15.365 1.00 11.17 O ANISOU 958 O ALA A 120 1352 1769 1121 47 -82 5 O ATOM 959 CB ALA A 120 13.324 -22.832 18.328 1.00 10.91 C ANISOU 959 CB ALA A 120 1452 1611 1081 167 239 -60 C ATOM 960 N LEU A 121 13.273 -21.055 15.744 1.00 11.29 N ANISOU 960 N LEU A 121 1348 1489 1451 163 94 151 N ATOM 961 CA LEU A 121 12.513 -20.136 14.890 1.00 11.38 C ANISOU 961 CA LEU A 121 1434 1515 1374 130 -103 13 C ATOM 962 C LEU A 121 12.268 -20.715 13.502 1.00 11.33 C ANISOU 962 C LEU A 121 1392 1690 1221 173 10 90 C ATOM 963 O LEU A 121 11.168 -20.579 12.942 1.00 12.45 O ANISOU 963 O LEU A 121 1427 1902 1401 77 -75 45 O ATOM 964 CB LEU A 121 13.250 -18.805 14.766 1.00 12.42 C ANISOU 964 CB LEU A 121 1511 1676 1530 -7 229 155 C ATOM 965 CG LEU A 121 13.161 -17.851 15.954 1.00 13.51 C ANISOU 965 CG LEU A 121 1477 1895 1759 28 88 -52 C ATOM 966 CD1 LEU A 121 14.175 -16.737 15.742 1.00 15.27 C ANISOU 966 CD1 LEU A 121 1916 1758 2127 -84 -27 180 C ATOM 967 CD2 LEU A 121 11.754 -17.279 16.096 1.00 14.92 C ANISOU 967 CD2 LEU A 121 1612 1974 2080 146 312 -124 C ATOM 968 N GLN A 122 13.293 -21.370 12.952 1.00 11.52 N ANISOU 968 N GLN A 122 1544 1646 1187 174 62 14 N ATOM 969 CA GLN A 122 13.218 -21.893 11.585 1.00 11.85 C ANISOU 969 CA GLN A 122 1571 1738 1192 9 -112 3 C ATOM 970 C GLN A 122 12.158 -22.972 11.407 1.00 11.99 C ANISOU 970 C GLN A 122 1451 1841 1262 -16 -184 201 C ATOM 971 O GLN A 122 11.771 -23.298 10.287 1.00 14.08 O ANISOU 971 O GLN A 122 1895 2091 1360 -184 -227 -83 O ATOM 972 CB GLN A 122 14.571 -22.431 11.160 1.00 12.20 C ANISOU 972 CB GLN A 122 1559 1908 1165 9 -64 83 C ATOM 973 CG GLN A 122 15.607 -21.350 10.933 1.00 11.85 C ANISOU 973 CG GLN A 122 1521 1726 1254 124 -179 205 C ATOM 974 CD GLN A 122 16.980 -21.950 10.780 1.00 12.30 C ANISOU 974 CD GLN A 122 1471 1927 1274 71 -9 140 C ATOM 975 OE1 GLN A 122 17.367 -22.401 9.694 1.00 14.34 O ANISOU 975 OE1 GLN A 122 1763 2192 1490 260 89 -32 O ATOM 976 NE2 GLN A 122 17.724 -21.985 11.879 1.00 12.65 N ANISOU 976 NE2 GLN A 122 1646 1900 1260 -65 -81 192 N ATOM 977 N GLN A 123 11.702 -23.534 12.517 1.00 11.77 N ANISOU 977 N GLN A 123 1549 1714 1207 -57 -36 26 N ATOM 978 CA GLN A 123 10.680 -24.569 12.492 1.00 12.04 C ANISOU 978 CA GLN A 123 1551 1729 1292 -72 -143 21 C ATOM 979 C GLN A 123 9.275 -24.065 12.786 1.00 12.08 C ANISOU 979 C GLN A 123 1559 1768 1261 8 -236 48 C ATOM 980 O GLN A 123 8.329 -24.855 12.763 1.00 14.32 O ANISOU 980 O GLN A 123 1648 2027 1766 -170 -219 76 O ATOM 981 CB GLN A 123 11.057 -25.679 13.472 1.00 12.67 C ANISOU 981 CB GLN A 123 1611 1822 1378 199 33 74 C ATOM 982 CG GLN A 123 12.359 -26.343 13.070 1.00 12.57 C ANISOU 982 CG GLN A 123 1634 1677 1462 199 1 -27 C ATOM 983 CD GLN A 123 12.905 -27.227 14.162 1.00 12.16 C ANISOU 983 CD GLN A 123 1504 1766 1348 -52 -35 56 C ATOM 984 OE1 GLN A 123 12.347 -28.292 14.448 1.00 13.42 O ANISOU 984 OE1 GLN A 123 1761 1819 1519 -213 103 -116 O ATOM 985 NE2 GLN A 123 14.011 -26.804 14.775 1.00 12.67 N ANISOU 985 NE2 GLN A 123 1571 1911 1331 -171 22 -99 N ATOM 986 N LEU A 124 9.145 -22.764 13.042 1.00 12.23 N ANISOU 986 N LEU A 124 1452 1781 1414 127 -151 138 N ATOM 987 CA LEU A 124 7.862 -22.127 13.363 1.00 12.42 C ANISOU 987 CA LEU A 124 1490 1849 1377 77 -75 60 C ATOM 988 C LEU A 124 7.357 -21.306 12.189 1.00 13.21 C ANISOU 988 C LEU A 124 1703 1799 1515 -15 -14 238 C ATOM 989 O LEU A 124 8.136 -20.667 11.482 1.00 14.65 O ANISOU 989 O LEU A 124 1857 2193 1514 -39 -52 511 O ATOM 990 CB LEU A 124 8.027 -21.193 14.569 1.00 13.15 C ANISOU 990 CB LEU A 124 1804 1889 1301 28 3 90 C ATOM 991 CG LEU A 124 8.680 -21.750 15.837 1.00 12.44 C ANISOU 991 CG LEU A 124 1505 1884 1336 63 58 105 C ATOM 992 CD1 LEU A 124 8.741 -20.680 16.910 1.00 13.66 C ANISOU 992 CD1 LEU A 124 1583 1966 1642 -140 189 -95 C ATOM 993 CD2 LEU A 124 7.940 -22.975 16.365 1.00 15.02 C ANISOU 993 CD2 LEU A 124 2089 1837 1780 -74 192 142 C ATOM 994 N GLU A 125 6.039 -21.281 12.020 1.00 13.91 N ANISOU 994 N GLU A 125 1645 2092 1549 9 45 237 N ATOM 995 CA GLU A 125 5.422 -20.389 11.051 1.00 15.53 C ANISOU 995 CA GLU A 125 1861 2249 1788 119 55 402 C ATOM 996 C GLU A 125 5.307 -19.033 11.739 1.00 14.64 C ANISOU 996 C GLU A 125 1775 2277 1509 14 -82 322 C ATOM 997 O GLU A 125 4.322 -18.754 12.424 1.00 16.62 O ANISOU 997 O GLU A 125 1919 2306 2088 -73 252 267 O ATOM 998 CB GLU A 125 4.044 -20.896 10.618 1.00 18.31 C ANISOU 998 CB GLU A 125 2173 2616 2166 -169 -155 325 C ATOM 999 CG GLU A 125 3.435 -20.154 9.434 1.00 26.75 C ANISOU 999 CG GLU A 125 3623 3545 2995 425 -603 774 C ATOM 1000 CD GLU A 125 3.893 -20.687 8.085 1.00 34.02 C ANISOU 1000 CD GLU A 125 4940 4172 3812 469 93 225 C ATOM 1001 OE1 GLU A 125 4.387 -21.838 8.020 1.00 39.74 O ANISOU 1001 OE1 GLU A 125 5327 4579 5193 1022 -261 153 O ATOM 1002 OE2 GLU A 125 3.750 -19.953 7.081 1.00 42.76 O ANISOU 1002 OE2 GLU A 125 6278 5307 4662 620 -672 945 O ATOM 1003 N VAL A 126 6.337 -18.211 11.580 1.00 16.13 N ANISOU 1003 N VAL A 126 1868 2198 2061 -53 -143 97 N ATOM 1004 CA VAL A 126 6.419 -16.924 12.257 1.00 16.98 C ANISOU 1004 CA VAL A 126 2203 2132 2116 -147 -101 191 C ATOM 1005 C VAL A 126 6.970 -15.906 11.274 1.00 17.50 C ANISOU 1005 C VAL A 126 2369 2373 1908 -242 44 81 C ATOM 1006 O VAL A 126 7.851 -16.223 10.470 1.00 19.77 O ANISOU 1006 O VAL A 126 2425 2340 2746 -403 506 -23 O ATOM 1007 CB VAL A 126 7.274 -17.006 13.559 1.00 18.36 C ANISOU 1007 CB VAL A 126 2400 2484 2090 49 -189 -367 C ATOM 1008 CG1 VAL A 126 8.723 -17.369 13.263 1.00 21.32 C ANISOU 1008 CG1 VAL A 126 2197 3069 2833 56 -415 -128 C ATOM 1009 CG2 VAL A 126 7.194 -15.717 14.369 1.00 21.48 C ANISOU 1009 CG2 VAL A 126 3348 2272 2538 -69 -293 -296 C ATOM 1010 N LYS A 127 6.414 -14.702 11.312 1.00 16.21 N ANISOU 1010 N LYS A 127 2014 2144 2000 -495 19 202 N ATOM 1011 CA LYS A 127 6.868 -13.617 10.452 1.00 18.35 C ANISOU 1011 CA LYS A 127 2497 2139 2333 -634 -57 313 C ATOM 1012 C LYS A 127 7.179 -12.408 11.316 1.00 17.39 C ANISOU 1012 C LYS A 127 2245 2290 2071 -436 7 178 C ATOM 1013 O LYS A 127 6.485 -12.140 12.298 1.00 19.80 O ANISOU 1013 O LYS A 127 2224 2905 2395 -723 336 305 O ATOM 1014 CB LYS A 127 5.798 -13.260 9.407 1.00 21.85 C ANISOU 1014 CB LYS A 127 3169 2739 2392 -331 -296 487 C ATOM 1015 CG LYS A 127 5.309 -14.431 8.552 1.00 27.83 C ANISOU 1015 CG LYS A 127 3994 3543 3036 -277 -639 -167 C ATOM 1016 CD LYS A 127 6.378 -14.965 7.607 1.00 33.98 C ANISOU 1016 CD LYS A 127 4481 4572 3858 128 -81 139 C ATOM 1017 CE LYS A 127 6.641 -14.022 6.442 1.00 37.10 C ANISOU 1017 CE LYS A 127 4721 4887 4489 46 472 484 C ATOM 1018 NZ LYS A 127 7.856 -14.410 5.673 1.00 41.51 N ANISOU 1018 NZ LYS A 127 4976 6110 4685 663 327 -98 N ATOM 1019 N PHE A 128 8.233 -11.683 10.963 1.00 15.23 N ANISOU 1019 N PHE A 128 1961 1935 1890 -91 -86 336 N ATOM 1020 CA PHE A 128 8.590 -10.475 11.703 1.00 15.11 C ANISOU 1020 CA PHE A 128 1691 1897 2150 58 -61 236 C ATOM 1021 C PHE A 128 7.968 -9.243 11.066 1.00 15.58 C ANISOU 1021 C PHE A 128 1805 2073 2039 -7 -122 453 C ATOM 1022 O PHE A 128 7.766 -9.207 9.853 1.00 18.71 O ANISOU 1022 O PHE A 128 2485 2591 2033 126 -145 547 O ATOM 1023 CB PHE A 128 10.109 -10.341 11.800 1.00 15.50 C ANISOU 1023 CB PHE A 128 1738 1941 2209 20 -65 454 C ATOM 1024 CG PHE A 128 10.725 -11.381 12.683 1.00 14.50 C ANISOU 1024 CG PHE A 128 1841 1641 2025 -51 191 472 C ATOM 1025 CD1 PHE A 128 10.570 -11.309 14.068 1.00 15.59 C ANISOU 1025 CD1 PHE A 128 1942 1950 2031 74 65 149 C ATOM 1026 CD2 PHE A 128 11.429 -12.449 12.145 1.00 15.69 C ANISOU 1026 CD2 PHE A 128 2020 1661 2278 -21 121 265 C ATOM 1027 CE1 PHE A 128 11.123 -12.274 14.893 1.00 15.85 C ANISOU 1027 CE1 PHE A 128 2000 1888 2134 190 -144 20 C ATOM 1028 CE2 PHE A 128 11.978 -13.420 12.969 1.00 15.37 C ANISOU 1028 CE2 PHE A 128 2001 2107 1730 101 116 210 C ATOM 1029 CZ PHE A 128 11.828 -13.331 14.340 1.00 15.05 C ANISOU 1029 CZ PHE A 128 2156 1837 1722 77 -121 -47 C ATOM 1030 N ASN A 129 7.659 -8.247 11.891 1.00 15.65 N ANISOU 1030 N ASN A 129 1824 1773 2350 -167 8 445 N ATOM 1031 CA ASN A 129 7.111 -6.979 11.409 1.00 16.58 C ANISOU 1031 CA ASN A 129 1923 1971 2405 14 12 512 C ATOM 1032 C ASN A 129 8.181 -5.958 11.045 1.00 16.57 C ANISOU 1032 C ASN A 129 2133 1778 2383 -209 -275 324 C ATOM 1033 O ASN A 129 8.030 -5.218 10.065 1.00 20.31 O ANISOU 1033 O ASN A 129 2603 2338 2775 -484 -543 749 O ATOM 1034 CB ASN A 129 6.159 -6.370 12.442 1.00 20.14 C ANISOU 1034 CB ASN A 129 2246 2382 3023 -72 424 178 C ATOM 1035 CG ASN A 129 4.860 -7.138 12.567 1.00 21.35 C ANISOU 1035 CG ASN A 129 2517 2369 3223 -308 128 202 C ATOM 1036 OD1 ASN A 129 4.331 -7.669 11.589 1.00 26.33 O ANISOU 1036 OD1 ASN A 129 2820 3766 3416 -691 -280 259 O ATOM 1037 ND2 ASN A 129 4.332 -7.185 13.776 1.00 22.72 N ANISOU 1037 ND2 ASN A 129 2759 2537 3334 277 424 411 N ATOM 1038 N ALA A 130 9.239 -5.883 11.853 1.00 15.70 N ANISOU 1038 N ALA A 130 1841 1752 2369 -60 -46 441 N ATOM 1039 CA ALA A 130 10.323 -4.932 11.601 1.00 15.71 C ANISOU 1039 CA ALA A 130 1904 1862 2202 -175 -19 260 C ATOM 1040 C ALA A 130 11.094 -5.349 10.347 1.00 15.00 C ANISOU 1040 C ALA A 130 1892 1765 2039 -23 -131 332 C ATOM 1041 O ALA A 130 11.584 -6.480 10.280 1.00 15.31 O ANISOU 1041 O ALA A 130 1840 1746 2232 -42 -86 300 O ATOM 1042 CB ALA A 130 11.260 -4.868 12.805 1.00 15.96 C ANISOU 1042 CB ALA A 130 1922 1773 2370 96 -158 211 C ATOM 1043 N PRO A 131 11.202 -4.450 9.344 1.00 14.77 N ANISOU 1043 N PRO A 131 1901 1649 2062 160 55 244 N ATOM 1044 CA PRO A 131 11.953 -4.794 8.135 1.00 14.36 C ANISOU 1044 CA PRO A 131 1831 1675 1947 -46 74 414 C ATOM 1045 C PRO A 131 13.379 -5.295 8.425 1.00 13.86 C ANISOU 1045 C PRO A 131 1801 1781 1683 -77 14 346 C ATOM 1046 O PRO A 131 13.856 -6.189 7.725 1.00 14.91 O ANISOU 1046 O PRO A 131 2015 1665 1983 22 -16 351 O ATOM 1047 CB PRO A 131 11.966 -3.478 7.355 1.00 15.62 C ANISOU 1047 CB PRO A 131 1904 1699 2332 252 -92 551 C ATOM 1048 CG PRO A 131 10.660 -2.841 7.729 1.00 16.51 C ANISOU 1048 CG PRO A 131 1725 2260 2288 235 -184 476 C ATOM 1049 CD PRO A 131 10.529 -3.140 9.206 1.00 16.06 C ANISOU 1049 CD PRO A 131 2031 1766 2302 245 -68 475 C ATOM 1050 N ALA A 132 14.046 -4.751 9.449 1.00 13.49 N ANISOU 1050 N ALA A 132 1662 1609 1852 41 -52 304 N ATOM 1051 CA ALA A 132 15.405 -5.201 9.773 1.00 13.26 C ANISOU 1051 CA ALA A 132 1728 1497 1811 84 -50 260 C ATOM 1052 C ALA A 132 15.397 -6.697 10.079 1.00 13.31 C ANISOU 1052 C ALA A 132 1744 1485 1828 -42 111 285 C ATOM 1053 O ALA A 132 16.276 -7.439 9.627 1.00 13.72 O ANISOU 1053 O ALA A 132 1821 1679 1713 12 234 323 O ATOM 1054 CB ALA A 132 15.971 -4.438 10.958 1.00 14.15 C ANISOU 1054 CB ALA A 132 1901 1642 1833 23 -30 187 C ATOM 1055 N LEU A 133 14.405 -7.134 10.858 1.00 13.21 N ANISOU 1055 N LEU A 133 1773 1448 1796 -133 29 383 N ATOM 1056 CA LEU A 133 14.273 -8.553 11.207 1.00 13.22 C ANISOU 1056 CA LEU A 133 1937 1401 1685 18 154 277 C ATOM 1057 C LEU A 133 13.817 -9.413 10.026 1.00 13.57 C ANISOU 1057 C LEU A 133 1708 1649 1796 9 -75 226 C ATOM 1058 O LEU A 133 14.327 -10.514 9.846 1.00 14.08 O ANISOU 1058 O LEU A 133 1939 1557 1854 -53 125 153 O ATOM 1059 CB LEU A 133 13.356 -8.731 12.423 1.00 13.58 C ANISOU 1059 CB LEU A 133 1765 1599 1795 -62 151 322 C ATOM 1060 CG LEU A 133 13.978 -8.309 13.760 1.00 13.65 C ANISOU 1060 CG LEU A 133 1638 1701 1845 112 201 65 C ATOM 1061 CD1 LEU A 133 12.898 -8.193 14.829 1.00 15.32 C ANISOU 1061 CD1 LEU A 133 1684 2125 2009 -51 332 -22 C ATOM 1062 CD2 LEU A 133 15.059 -9.283 14.226 1.00 14.48 C ANISOU 1062 CD2 LEU A 133 1923 1590 1987 130 64 190 C ATOM 1063 N GLN A 134 12.868 -8.918 9.229 1.00 13.41 N ANISOU 1063 N GLN A 134 1724 1618 1750 -15 -65 229 N ATOM 1064 CA GLN A 134 12.422 -9.638 8.035 1.00 14.76 C ANISOU 1064 CA GLN A 134 2038 1717 1852 33 -182 144 C ATOM 1065 C GLN A 134 13.612 -9.951 7.141 1.00 14.83 C ANISOU 1065 C GLN A 134 2131 1702 1802 -81 -43 287 C ATOM 1066 O GLN A 134 13.812 -11.099 6.734 1.00 15.36 O ANISOU 1066 O GLN A 134 2070 1802 1963 9 -68 138 O ATOM 1067 CB GLN A 134 11.438 -8.793 7.224 1.00 17.14 C ANISOU 1067 CB GLN A 134 2169 2194 2148 239 -105 441 C ATOM 1068 CG GLN A 134 10.116 -8.493 7.905 1.00 18.01 C ANISOU 1068 CG GLN A 134 2043 2516 2283 294 -251 268 C ATOM 1069 CD GLN A 134 9.240 -7.552 7.095 1.00 21.17 C ANISOU 1069 CD GLN A 134 2782 3082 2176 282 -272 939 C ATOM 1070 OE1 GLN A 134 9.707 -6.880 6.163 1.00 24.05 O ANISOU 1070 OE1 GLN A 134 3128 3083 2926 3 -6 1130 O ATOM 1071 NE2 GLN A 134 7.967 -7.486 7.453 1.00 22.81 N ANISOU 1071 NE2 GLN A 134 2856 3024 2784 237 -136 778 N ATOM 1072 N GLU A 135 14.395 -8.919 6.836 1.00 15.17 N ANISOU 1072 N GLU A 135 2050 1937 1776 -117 22 422 N ATOM 1073 CA GLU A 135 15.491 -9.044 5.888 1.00 15.14 C ANISOU 1073 CA GLU A 135 2110 1890 1751 66 23 444 C ATOM 1074 C GLU A 135 16.588 -9.950 6.440 1.00 14.30 C ANISOU 1074 C GLU A 135 2127 1738 1567 106 77 284 C ATOM 1075 O GLU A 135 17.070 -10.843 5.744 1.00 15.54 O ANISOU 1075 O GLU A 135 2423 1697 1781 264 65 289 O ATOM 1076 CB GLU A 135 16.034 -7.651 5.522 1.00 15.85 C ANISOU 1076 CB GLU A 135 2304 1829 1886 -10 -102 363 C ATOM 1077 CG GLU A 135 15.058 -6.855 4.650 1.00 18.07 C ANISOU 1077 CG GLU A 135 2776 2051 2039 419 -90 412 C ATOM 1078 CD GLU A 135 15.532 -5.452 4.309 1.00 20.23 C ANISOU 1078 CD GLU A 135 3167 2389 2128 88 73 581 C ATOM 1079 OE1 GLU A 135 16.708 -5.132 4.556 1.00 21.22 O ANISOU 1079 OE1 GLU A 135 3216 2404 2443 -110 482 126 O ATOM 1080 OE2 GLU A 135 14.716 -4.661 3.784 1.00 27.08 O ANISOU 1080 OE2 GLU A 135 3964 3091 3234 538 -129 1101 O ATOM 1081 N ALA A 136 16.939 -9.751 7.706 1.00 13.50 N ANISOU 1081 N ALA A 136 1809 1766 1552 83 63 301 N ATOM 1082 CA ALA A 136 18.017 -10.514 8.317 1.00 13.77 C ANISOU 1082 CA ALA A 136 1893 1645 1692 62 -68 237 C ATOM 1083 C ALA A 136 17.614 -11.966 8.566 1.00 13.32 C ANISOU 1083 C ALA A 136 1772 1718 1571 1 -61 255 C ATOM 1084 O ALA A 136 18.437 -12.867 8.441 1.00 14.75 O ANISOU 1084 O ALA A 136 2312 1683 1607 193 66 148 O ATOM 1085 CB ALA A 136 18.484 -9.856 9.604 1.00 13.81 C ANISOU 1085 CB ALA A 136 1922 1649 1674 -63 -23 276 C ATOM 1086 N TYR A 137 16.347 -12.191 8.901 1.00 12.99 N ANISOU 1086 N TYR A 137 1850 1647 1437 1 4 379 N ATOM 1087 CA TYR A 137 15.866 -13.542 9.134 1.00 13.46 C ANISOU 1087 CA TYR A 137 1983 1567 1564 22 235 207 C ATOM 1088 C TYR A 137 15.849 -14.351 7.846 1.00 14.03 C ANISOU 1088 C TYR A 137 2175 1608 1547 32 -13 213 C ATOM 1089 O TYR A 137 16.208 -15.529 7.853 1.00 15.35 O ANISOU 1089 O TYR A 137 2402 1670 1757 152 156 57 O ATOM 1090 CB TYR A 137 14.492 -13.537 9.800 1.00 13.81 C ANISOU 1090 CB TYR A 137 1859 1652 1735 -46 154 267 C ATOM 1091 CG TYR A 137 14.011 -14.915 10.177 1.00 13.89 C ANISOU 1091 CG TYR A 137 1916 1668 1693 -91 181 247 C ATOM 1092 CD1 TYR A 137 14.816 -15.777 10.940 1.00 14.52 C ANISOU 1092 CD1 TYR A 137 2051 1643 1822 60 213 211 C ATOM 1093 CD2 TYR A 137 12.753 -15.348 9.802 1.00 13.68 C ANISOU 1093 CD2 TYR A 137 1928 1663 1605 -149 168 211 C ATOM 1094 CE1 TYR A 137 14.377 -17.044 11.284 1.00 14.26 C ANISOU 1094 CE1 TYR A 137 1808 1856 1753 -160 258 200 C ATOM 1095 CE2 TYR A 137 12.302 -16.611 10.147 1.00 13.39 C ANISOU 1095 CE2 TYR A 137 2069 1410 1606 24 15 73 C ATOM 1096 CZ TYR A 137 13.122 -17.451 10.884 1.00 13.10 C ANISOU 1096 CZ TYR A 137 1827 1567 1582 40 110 97 C ATOM 1097 OH TYR A 137 12.692 -18.702 11.224 1.00 14.38 O ANISOU 1097 OH TYR A 137 2007 1684 1773 -75 -58 253 O ATOM 1098 N TYR A 138 15.435 -13.716 6.747 1.00 13.90 N ANISOU 1098 N TYR A 138 2130 1617 1533 111 6 144 N ATOM 1099 CA TYR A 138 15.462 -14.348 5.441 1.00 15.14 C ANISOU 1099 CA TYR A 138 2469 1881 1399 192 12 273 C ATOM 1100 C TYR A 138 16.882 -14.808 5.126 1.00 15.13 C ANISOU 1100 C TYR A 138 2391 1754 1602 -5 130 230 C ATOM 1101 O TYR A 138 17.099 -15.965 4.746 1.00 16.45 O ANISOU 1101 O TYR A 138 2829 1974 1447 315 107 67 O ATOM 1102 CB TYR A 138 14.970 -13.349 4.392 1.00 16.92 C ANISOU 1102 CB TYR A 138 2733 2031 1664 161 -54 508 C ATOM 1103 CG TYR A 138 14.839 -13.915 3.009 1.00 19.62 C ANISOU 1103 CG TYR A 138 3325 2259 1870 290 -333 350 C ATOM 1104 CD1 TYR A 138 13.652 -14.510 2.591 1.00 22.18 C ANISOU 1104 CD1 TYR A 138 3891 2270 2266 50 -774 387 C ATOM 1105 CD2 TYR A 138 15.912 -13.875 2.117 1.00 21.85 C ANISOU 1105 CD2 TYR A 138 3740 2612 1949 212 -78 192 C ATOM 1106 CE1 TYR A 138 13.527 -15.031 1.313 1.00 25.50 C ANISOU 1106 CE1 TYR A 138 4673 2736 2280 453 -487 190 C ATOM 1107 CE2 TYR A 138 15.799 -14.400 0.841 1.00 23.90 C ANISOU 1107 CE2 TYR A 138 4262 3087 1730 210 -700 403 C ATOM 1108 CZ TYR A 138 14.607 -14.979 0.450 1.00 23.97 C ANISOU 1108 CZ TYR A 138 4668 3000 1438 112 -730 -202 C ATOM 1109 OH TYR A 138 14.485 -15.493 -0.821 1.00 31.17 O ANISOU 1109 OH TYR A 138 6483 3771 1587 480 -843 -598 O ATOM 1110 N ARG A 139 17.848 -13.900 5.291 1.00 13.81 N ANISOU 1110 N ARG A 139 2123 1895 1229 114 35 300 N ATOM 1111 CA ARG A 139 19.257 -14.233 5.101 1.00 15.21 C ANISOU 1111 CA ARG A 139 2200 1973 1603 182 225 386 C ATOM 1112 C ARG A 139 19.718 -15.368 6.023 1.00 15.54 C ANISOU 1112 C ARG A 139 2390 2041 1473 335 400 362 C ATOM 1113 O ARG A 139 20.453 -16.255 5.596 1.00 17.27 O ANISOU 1113 O ARG A 139 2778 2018 1765 442 419 192 O ATOM 1114 CB ARG A 139 20.129 -12.985 5.266 1.00 16.47 C ANISOU 1114 CB ARG A 139 2306 2180 1771 69 99 359 C ATOM 1115 CG ARG A 139 19.919 -11.945 4.178 1.00 19.23 C ANISOU 1115 CG ARG A 139 2640 2320 2343 68 183 700 C ATOM 1116 CD ARG A 139 20.624 -10.647 4.520 1.00 22.39 C ANISOU 1116 CD ARG A 139 2773 2542 3189 -141 341 376 C ATOM 1117 NE ARG A 139 22.075 -10.817 4.572 1.00 25.39 N ANISOU 1117 NE ARG A 139 2778 2786 4080 -145 290 250 N ATOM 1118 CZ ARG A 139 22.944 -9.840 4.822 1.00 27.39 C ANISOU 1118 CZ ARG A 139 3122 2763 4522 -238 34 167 C ATOM 1119 NH1 ARG A 139 22.525 -8.605 5.057 1.00 35.61 N ANISOU 1119 NH1 ARG A 139 4091 3165 6271 626 -283 155 N ATOM 1120 NH2 ARG A 139 24.241 -10.102 4.835 1.00 27.77 N ANISOU 1120 NH2 ARG A 139 3017 3331 4201 -368 110 564 N ATOM 1121 N ALA A 140 19.271 -15.352 7.274 1.00 14.32 N ANISOU 1121 N ALA A 140 2148 1947 1345 280 174 279 N ATOM 1122 CA ALA A 140 19.643 -16.387 8.229 1.00 13.93 C ANISOU 1122 CA ALA A 140 2023 1717 1551 304 430 321 C ATOM 1123 C ALA A 140 19.123 -17.755 7.798 1.00 14.87 C ANISOU 1123 C ALA A 140 2265 1777 1607 338 323 174 C ATOM 1124 O ALA A 140 19.842 -18.755 7.899 1.00 15.56 O ANISOU 1124 O ALA A 140 2510 1982 1419 570 259 211 O ATOM 1125 CB ALA A 140 19.119 -16.036 9.608 1.00 14.48 C ANISOU 1125 CB ALA A 140 2224 1724 1553 481 370 192 C ATOM 1126 N ARG A 141 17.878 -17.806 7.322 1.00 14.72 N ANISOU 1126 N ARG A 141 2451 1815 1327 224 177 83 N ATOM 1127 CA ARG A 141 17.322 -19.062 6.801 1.00 15.84 C ANISOU 1127 CA ARG A 141 2485 1857 1673 197 286 -120 C ATOM 1128 C ARG A 141 18.183 -19.578 5.640 1.00 16.93 C ANISOU 1128 C ARG A 141 2891 1964 1575 125 435 -65 C ATOM 1129 O ARG A 141 18.395 -20.781 5.502 1.00 20.20 O ANISOU 1129 O ARG A 141 3640 2142 1890 401 492 -344 O ATOM 1130 CB ARG A 141 15.867 -18.880 6.361 1.00 16.40 C ANISOU 1130 CB ARG A 141 2540 2157 1533 151 159 -65 C ATOM 1131 CG ARG A 141 14.884 -18.661 7.508 1.00 16.13 C ANISOU 1131 CG ARG A 141 2576 2117 1434 170 116 15 C ATOM 1132 CD ARG A 141 13.466 -18.301 7.050 1.00 18.42 C ANISOU 1132 CD ARG A 141 2475 2478 2046 30 -16 -231 C ATOM 1133 NE ARG A 141 12.892 -19.319 6.162 1.00 20.49 N ANISOU 1133 NE ARG A 141 3027 2596 2162 -86 -190 -302 N ATOM 1134 CZ ARG A 141 12.400 -19.089 4.943 1.00 20.63 C ANISOU 1134 CZ ARG A 141 3041 2640 2156 -67 -254 -418 C ATOM 1135 NH1 ARG A 141 12.357 -17.855 4.451 1.00 23.38 N ANISOU 1135 NH1 ARG A 141 3675 2959 2248 182 -260 -157 N ATOM 1136 NH2 ARG A 141 11.916 -20.098 4.221 1.00 22.08 N ANISOU 1136 NH2 ARG A 141 3115 2845 2428 63 -100 -752 N ATOM 1137 N ALA A 142 18.710 -18.645 4.846 1.00 17.53 N ANISOU 1137 N ALA A 142 2815 2286 1557 139 568 21 N ATOM 1138 CA ALA A 142 19.546 -18.959 3.683 1.00 19.46 C ANISOU 1138 CA ALA A 142 3053 2630 1709 66 714 -105 C ATOM 1139 C ALA A 142 20.986 -19.316 4.067 1.00 19.09 C ANISOU 1139 C ALA A 142 3060 2243 1951 337 781 -214 C ATOM 1140 O ALA A 142 21.785 -19.668 3.192 1.00 21.82 O ANISOU 1140 O ALA A 142 3377 2554 2359 316 981 -642 O ATOM 1141 CB ALA A 142 19.528 -17.791 2.705 1.00 21.76 C ANISOU 1141 CB ALA A 142 3674 3249 1344 179 473 67 C ATOM 1142 N GLY A 143 21.312 -19.234 5.364 1.00 18.78 N ANISOU 1142 N GLY A 143 2953 2246 1935 399 760 -35 N ATOM 1143 CA GLY A 143 22.650 -19.586 5.876 1.00 19.80 C ANISOU 1143 CA GLY A 143 3185 2573 1765 540 794 243 C ATOM 1144 C GLY A 143 23.556 -18.419 6.233 1.00 19.12 C ANISOU 1144 C GLY A 143 2832 2889 1542 547 676 341 C ATOM 1145 O GLY A 143 24.665 -18.609 6.729 1.00 22.14 O ANISOU 1145 O GLY A 143 3253 3123 2034 1066 473 671 O ATOM 1146 N ASP A 144 23.068 -17.208 5.977 1.00 20.21 N ANISOU 1146 N ASP A 144 3289 2586 1803 505 714 83 N ATOM 1147 CA ASP A 144 23.806 -15.964 6.176 1.00 19.07 C ANISOU 1147 CA ASP A 144 2817 2694 1733 412 652 274 C ATOM 1148 C ASP A 144 23.192 -15.273 7.400 1.00 18.54 C ANISOU 1148 C ASP A 144 2620 2568 1855 401 459 121 C ATOM 1149 O ASP A 144 22.385 -14.362 7.263 1.00 19.03 O ANISOU 1149 O ASP A 144 2679 2662 1887 483 442 176 O ATOM 1150 CB ASP A 144 23.653 -15.110 4.902 1.00 20.31 C ANISOU 1150 CB ASP A 144 3116 2876 1722 190 675 359 C ATOM 1151 CG ASP A 144 24.344 -13.757 4.983 1.00 21.35 C ANISOU 1151 CG ASP A 144 3227 2696 2189 364 484 479 C ATOM 1152 OD1 ASP A 144 25.207 -13.549 5.858 1.00 22.35 O ANISOU 1152 OD1 ASP A 144 3289 2904 2297 167 501 126 O ATOM 1153 OD2 ASP A 144 24.026 -12.892 4.132 1.00 24.57 O ANISOU 1153 OD2 ASP A 144 4104 2836 2396 120 399 753 O ATOM 1154 N ALA A 145 23.597 -15.706 8.593 1.00 16.78 N ANISOU 1154 N ALA A 145 2135 2208 2032 345 286 167 N ATOM 1155 CA ALA A 145 22.888 -15.383 9.834 1.00 15.50 C ANISOU 1155 CA ALA A 145 2059 1897 1931 282 251 347 C ATOM 1156 C ALA A 145 23.582 -14.372 10.752 1.00 14.87 C ANISOU 1156 C ALA A 145 1851 1932 1865 211 284 421 C ATOM 1157 O ALA A 145 23.071 -14.066 11.834 1.00 14.98 O ANISOU 1157 O ALA A 145 1929 1846 1915 77 385 309 O ATOM 1158 CB ALA A 145 22.564 -16.665 10.600 1.00 16.28 C ANISOU 1158 CB ALA A 145 2208 1875 2103 323 -35 454 C ATOM 1159 N ALA A 146 24.719 -13.822 10.326 1.00 14.80 N ANISOU 1159 N ALA A 146 1697 1883 2043 185 122 307 N ATOM 1160 CA ALA A 146 25.457 -12.897 11.190 1.00 14.26 C ANISOU 1160 CA ALA A 146 1785 1681 1949 106 214 453 C ATOM 1161 C ALA A 146 24.620 -11.684 11.584 1.00 13.35 C ANISOU 1161 C ALA A 146 1685 1604 1784 -16 217 425 C ATOM 1162 O ALA A 146 24.589 -11.299 12.756 1.00 14.38 O ANISOU 1162 O ALA A 146 1717 2002 1745 156 307 424 O ATOM 1163 CB ALA A 146 26.763 -12.466 10.541 1.00 16.08 C ANISOU 1163 CB ALA A 146 1722 2050 2335 203 268 706 C ATOM 1164 N ASN A 147 23.946 -11.080 10.610 1.00 14.43 N ANISOU 1164 N ASN A 147 1787 1771 1923 168 144 403 N ATOM 1165 CA ASN A 147 23.143 -9.897 10.887 1.00 13.04 C ANISOU 1165 CA ASN A 147 1722 1660 1572 103 67 466 C ATOM 1166 C ASN A 147 21.984 -10.208 11.825 1.00 12.31 C ANISOU 1166 C ASN A 147 1598 1516 1562 181 31 326 C ATOM 1167 O ASN A 147 21.754 -9.488 12.802 1.00 13.49 O ANISOU 1167 O ASN A 147 1764 1786 1572 99 134 289 O ATOM 1168 CB ASN A 147 22.665 -9.240 9.589 1.00 14.50 C ANISOU 1168 CB ASN A 147 1947 1841 1722 208 11 616 C ATOM 1169 CG ASN A 147 23.805 -8.586 8.825 1.00 19.33 C ANISOU 1169 CG ASN A 147 2598 2654 2092 87 637 725 C ATOM 1170 OD1 ASN A 147 24.492 -9.230 8.028 1.00 25.33 O ANISOU 1170 OD1 ASN A 147 3103 3515 3005 769 820 616 O ATOM 1171 ND2 ASN A 147 24.017 -7.298 9.070 1.00 23.67 N ANISOU 1171 ND2 ASN A 147 3197 2954 2840 -206 246 593 N ATOM 1172 N PHE A 148 21.306 -11.321 11.565 1.00 12.84 N ANISOU 1172 N PHE A 148 1520 1605 1753 135 25 449 N ATOM 1173 CA PHE A 148 20.184 -11.722 12.391 1.00 12.82 C ANISOU 1173 CA PHE A 148 1736 1536 1597 41 132 289 C ATOM 1174 C PHE A 148 20.640 -11.935 13.842 1.00 12.85 C ANISOU 1174 C PHE A 148 1597 1679 1604 195 89 171 C ATOM 1175 O PHE A 148 19.990 -11.472 14.793 1.00 12.84 O ANISOU 1175 O PHE A 148 1814 1626 1438 158 93 116 O ATOM 1176 CB PHE A 148 19.513 -12.982 11.838 1.00 13.38 C ANISOU 1176 CB PHE A 148 1740 1669 1674 56 171 117 C ATOM 1177 CG PHE A 148 18.233 -13.332 12.541 1.00 13.73 C ANISOU 1177 CG PHE A 148 1731 1650 1835 41 221 49 C ATOM 1178 CD1 PHE A 148 17.109 -12.513 12.425 1.00 14.19 C ANISOU 1178 CD1 PHE A 148 1883 1767 1739 158 152 -166 C ATOM 1179 CD2 PHE A 148 18.149 -14.473 13.335 1.00 14.58 C ANISOU 1179 CD2 PHE A 148 1880 1861 1795 -36 103 185 C ATOM 1180 CE1 PHE A 148 15.931 -12.829 13.085 1.00 14.93 C ANISOU 1180 CE1 PHE A 148 2118 1579 1975 -128 218 -104 C ATOM 1181 CE2 PHE A 148 16.966 -14.795 13.993 1.00 15.41 C ANISOU 1181 CE2 PHE A 148 1886 1919 2049 -49 162 128 C ATOM 1182 CZ PHE A 148 15.860 -13.969 13.868 1.00 14.16 C ANISOU 1182 CZ PHE A 148 1912 1793 1674 -15 214 -10 C ATOM 1183 N CYS A 149 21.772 -12.609 14.022 1.00 12.95 N ANISOU 1183 N CYS A 149 1732 1459 1729 180 -85 345 N ATOM 1184 CA CYS A 149 22.281 -12.856 15.377 1.00 13.08 C ANISOU 1184 CA CYS A 149 1709 1633 1625 258 0 263 C ATOM 1185 C CYS A 149 22.615 -11.553 16.096 1.00 13.35 C ANISOU 1185 C CYS A 149 1721 1502 1846 -18 54 399 C ATOM 1186 O CYS A 149 22.306 -11.399 17.284 1.00 13.81 O ANISOU 1186 O CYS A 149 1626 1763 1856 150 4 475 O ATOM 1187 CB CYS A 149 23.508 -13.775 15.349 1.00 13.80 C ANISOU 1187 CB CYS A 149 1715 1627 1901 280 -8 515 C ATOM 1188 SG CYS A 149 23.112 -15.477 14.917 1.00 15.89 S ANISOU 1188 SG CYS A 149 2124 1733 2178 275 43 357 S ATOM 1189 N ALA A 150 23.251 -10.613 15.386 1.00 13.04 N ANISOU 1189 N ALA A 150 1453 1570 1931 -67 -34 386 N ATOM 1190 CA ALA A 150 23.552 -9.309 15.972 1.00 13.93 C ANISOU 1190 CA ALA A 150 1511 1733 2045 -244 170 239 C ATOM 1191 C ALA A 150 22.268 -8.546 16.336 1.00 13.57 C ANISOU 1191 C ALA A 150 1653 1591 1910 -166 88 175 C ATOM 1192 O ALA A 150 22.205 -7.870 17.368 1.00 13.49 O ANISOU 1192 O ALA A 150 1637 1746 1744 -198 122 173 O ATOM 1193 CB ALA A 150 24.420 -8.493 15.030 1.00 14.34 C ANISOU 1193 CB ALA A 150 1522 1891 2036 -123 180 440 C ATOM 1194 N LEU A 151 21.236 -8.672 15.507 1.00 13.27 N ANISOU 1194 N LEU A 151 1569 1550 1921 6 77 396 N ATOM 1195 CA LEU A 151 19.942 -8.080 15.845 1.00 13.58 C ANISOU 1195 CA LEU A 151 1507 1907 1745 7 12 316 C ATOM 1196 C LEU A 151 19.291 -8.724 17.065 1.00 13.13 C ANISOU 1196 C LEU A 151 1785 1587 1617 -100 -79 224 C ATOM 1197 O LEU A 151 18.743 -8.018 17.909 1.00 14.06 O ANISOU 1197 O LEU A 151 2038 1724 1578 21 -32 248 O ATOM 1198 CB LEU A 151 18.991 -8.109 14.646 1.00 13.52 C ANISOU 1198 CB LEU A 151 1760 1721 1654 -36 -67 341 C ATOM 1199 CG LEU A 151 19.310 -7.157 13.488 1.00 13.66 C ANISOU 1199 CG LEU A 151 1910 1798 1480 141 80 273 C ATOM 1200 CD1 LEU A 151 18.412 -7.473 12.303 1.00 14.67 C ANISOU 1200 CD1 LEU A 151 2465 1598 1509 206 -78 149 C ATOM 1201 CD2 LEU A 151 19.183 -5.697 13.924 1.00 14.87 C ANISOU 1201 CD2 LEU A 151 2126 1757 1766 49 113 284 C ATOM 1202 N ILE A 152 19.353 -10.054 17.180 1.00 13.03 N ANISOU 1202 N ILE A 152 1712 1621 1617 8 -95 430 N ATOM 1203 CA ILE A 152 18.814 -10.707 18.381 1.00 13.46 C ANISOU 1203 CA ILE A 152 1926 1648 1538 -12 -121 352 C ATOM 1204 C ILE A 152 19.444 -10.095 19.624 1.00 13.60 C ANISOU 1204 C ILE A 152 1638 1855 1673 -54 -87 253 C ATOM 1205 O ILE A 152 18.743 -9.752 20.583 1.00 14.48 O ANISOU 1205 O ILE A 152 1925 1893 1682 -69 65 241 O ATOM 1206 CB ILE A 152 19.056 -12.230 18.413 1.00 14.22 C ANISOU 1206 CB ILE A 152 2298 1579 1524 -133 70 364 C ATOM 1207 CG1 ILE A 152 18.320 -12.942 17.276 1.00 15.27 C ANISOU 1207 CG1 ILE A 152 2365 1874 1560 -108 31 296 C ATOM 1208 CG2 ILE A 152 18.581 -12.785 19.749 1.00 14.45 C ANISOU 1208 CG2 ILE A 152 2167 1736 1587 67 111 474 C ATOM 1209 CD1 ILE A 152 18.750 -14.383 17.076 1.00 16.81 C ANISOU 1209 CD1 ILE A 152 2594 1879 1912 -132 298 299 C ATOM 1210 N LEU A 153 20.766 -9.934 19.588 1.00 13.07 N ANISOU 1210 N LEU A 153 1617 1752 1596 -75 -169 402 N ATOM 1211 CA LEU A 153 21.487 -9.356 20.714 1.00 13.52 C ANISOU 1211 CA LEU A 153 1656 1739 1741 -151 -41 150 C ATOM 1212 C LEU A 153 21.018 -7.916 20.965 1.00 14.18 C ANISOU 1212 C LEU A 153 1872 1740 1776 -63 -165 256 C ATOM 1213 O LEU A 153 20.705 -7.544 22.097 1.00 16.57 O ANISOU 1213 O LEU A 153 2275 2176 1845 -15 -133 151 O ATOM 1214 CB LEU A 153 23.000 -9.439 20.470 1.00 12.97 C ANISOU 1214 CB LEU A 153 1688 1496 1743 -112 -9 -50 C ATOM 1215 CG LEU A 153 23.550 -10.872 20.545 1.00 13.17 C ANISOU 1215 CG LEU A 153 1622 1652 1727 26 -71 253 C ATOM 1216 CD1 LEU A 153 24.931 -10.954 19.914 1.00 15.51 C ANISOU 1216 CD1 LEU A 153 1704 2055 2134 -76 94 76 C ATOM 1217 CD2 LEU A 153 23.592 -11.380 21.982 1.00 14.87 C ANISOU 1217 CD2 LEU A 153 2133 1842 1671 -60 -173 191 C ATOM 1218 N ALA A 154 20.939 -7.115 19.906 1.00 14.08 N ANISOU 1218 N ALA A 154 1841 1615 1894 17 40 295 N ATOM 1219 CA ALA A 154 20.522 -5.717 20.074 1.00 14.52 C ANISOU 1219 CA ALA A 154 2051 1511 1954 3 114 275 C ATOM 1220 C ALA A 154 19.084 -5.572 20.606 1.00 14.91 C ANISOU 1220 C ALA A 154 2094 1773 1796 37 131 51 C ATOM 1221 O ALA A 154 18.842 -4.799 21.539 1.00 15.84 O ANISOU 1221 O ALA A 154 2265 1813 1940 -43 278 -56 O ATOM 1222 CB ALA A 154 20.709 -4.934 18.783 1.00 15.71 C ANISOU 1222 CB ALA A 154 2351 1464 2152 -59 182 417 C ATOM 1223 N TYR A 155 18.147 -6.338 20.047 1.00 14.77 N ANISOU 1223 N TYR A 155 1781 1718 2111 83 115 339 N ATOM 1224 CA TYR A 155 16.755 -6.316 20.533 1.00 14.97 C ANISOU 1224 CA TYR A 155 1810 1934 1943 234 178 130 C ATOM 1225 C TYR A 155 16.603 -6.829 21.971 1.00 16.56 C ANISOU 1225 C TYR A 155 2382 1973 1936 259 114 168 C ATOM 1226 O TYR A 155 15.684 -6.414 22.681 1.00 20.15 O ANISOU 1226 O TYR A 155 2526 2568 2563 599 430 411 O ATOM 1227 CB TYR A 155 15.816 -7.103 19.610 1.00 16.06 C ANISOU 1227 CB TYR A 155 1879 2052 2172 22 -25 349 C ATOM 1228 CG TYR A 155 15.476 -6.375 18.327 1.00 14.33 C ANISOU 1228 CG TYR A 155 1685 1927 1832 -16 243 194 C ATOM 1229 CD1 TYR A 155 14.651 -5.240 18.333 1.00 15.32 C ANISOU 1229 CD1 TYR A 155 1978 1955 1887 97 -2 190 C ATOM 1230 CD2 TYR A 155 15.975 -6.814 17.107 1.00 14.07 C ANISOU 1230 CD2 TYR A 155 1833 1844 1667 -195 46 79 C ATOM 1231 CE1 TYR A 155 14.348 -4.567 17.154 1.00 14.71 C ANISOU 1231 CE1 TYR A 155 1952 1836 1799 -1 110 159 C ATOM 1232 CE2 TYR A 155 15.682 -6.148 15.931 1.00 13.75 C ANISOU 1232 CE2 TYR A 155 1680 1604 1939 170 14 119 C ATOM 1233 CZ TYR A 155 14.863 -5.035 15.951 1.00 13.36 C ANISOU 1233 CZ TYR A 155 1677 1474 1922 90 97 122 C ATOM 1234 OH TYR A 155 14.589 -4.395 14.771 1.00 15.24 O ANISOU 1234 OH TYR A 155 1827 2005 1957 82 50 214 O ATOM 1235 N SER A 156 17.495 -7.727 22.385 1.00 15.10 N ANISOU 1235 N SER A 156 1934 2059 1741 -25 36 238 N ATOM 1236 CA SER A 156 17.469 -8.317 23.725 1.00 15.62 C ANISOU 1236 CA SER A 156 2159 2002 1772 70 149 263 C ATOM 1237 C SER A 156 18.263 -7.503 24.744 1.00 16.78 C ANISOU 1237 C SER A 156 2284 2121 1971 104 123 10 C ATOM 1238 O SER A 156 18.258 -7.836 25.924 1.00 17.99 O ANISOU 1238 O SER A 156 2470 2481 1882 -3 84 -113 O ATOM 1239 CB SER A 156 18.023 -9.744 23.678 1.00 17.88 C ANISOU 1239 CB SER A 156 3176 1912 1702 147 -351 574 C ATOM 1240 OG SER A 156 17.215 -10.572 22.867 1.00 21.77 O ANISOU 1240 OG SER A 156 2806 2722 2743 -69 -141 -42 O ATOM 1241 N ASN A 157 18.940 -6.445 24.289 1.00 16.66 N ANISOU 1241 N ASN A 157 2272 2187 1869 40 -61 70 N ATOM 1242 CA ASN A 157 19.860 -5.654 25.131 1.00 17.38 C ANISOU 1242 CA ASN A 157 2329 2206 2065 187 -159 -196 C ATOM 1243 C ASN A 157 20.952 -6.509 25.781 1.00 16.29 C ANISOU 1243 C ASN A 157 2200 2210 1777 45 -240 -267 C ATOM 1244 O ASN A 157 21.264 -6.362 26.972 1.00 19.11 O ANISOU 1244 O ASN A 157 2868 2552 1840 -8 -342 -477 O ATOM 1245 CB ASN A 157 19.110 -4.801 26.173 1.00 20.92 C ANISOU 1245 CB ASN A 157 2974 2629 2344 218 10 -526 C ATOM 1246 CG ASN A 157 18.568 -3.515 25.583 1.00 26.33 C ANISOU 1246 CG ASN A 157 4020 2718 3264 167 -333 -250 C ATOM 1247 OD1 ASN A 157 19.231 -2.474 25.618 1.00 33.21 O ANISOU 1247 OD1 ASN A 157 4806 3553 4256 -771 -456 -287 O ATOM 1248 ND2 ASN A 157 17.367 -3.580 25.023 1.00 31.34 N ANISOU 1248 ND2 ASN A 157 3986 3903 4017 192 -344 -827 N ATOM 1249 N LYS A 158 21.519 -7.409 24.980 1.00 16.88 N ANISOU 1249 N LYS A 158 2360 2034 2017 144 -159 -128 N ATOM 1250 CA LYS A 158 22.608 -8.264 25.399 1.00 16.85 C ANISOU 1250 CA LYS A 158 2149 1902 2350 -97 13 31 C ATOM 1251 C LYS A 158 23.800 -8.050 24.494 1.00 16.04 C ANISOU 1251 C LYS A 158 2002 1953 2139 -255 -187 -34 C ATOM 1252 O LYS A 158 23.655 -7.659 23.332 1.00 17.52 O ANISOU 1252 O LYS A 158 2369 2140 2145 -70 -53 -4 O ATOM 1253 CB LYS A 158 22.177 -9.722 25.332 1.00 16.72 C ANISOU 1253 CB LYS A 158 2170 1800 2382 -2 -107 216 C ATOM 1254 CG LYS A 158 21.011 -10.030 26.247 1.00 18.39 C ANISOU 1254 CG LYS A 158 2161 2403 2423 -86 -90 197 C ATOM 1255 CD LYS A 158 20.612 -11.491 26.143 1.00 19.83 C ANISOU 1255 CD LYS A 158 2518 2262 2752 168 -355 -98 C ATOM 1256 CE LYS A 158 21.570 -12.400 26.907 1.00 18.30 C ANISOU 1256 CE LYS A 158 2480 2175 2296 -77 -288 84 C ATOM 1257 NZ LYS A 158 21.395 -12.265 28.379 1.00 18.32 N ANISOU 1257 NZ LYS A 158 2486 2137 2338 136 -35 127 N ATOM 1258 N THR A 159 24.983 -8.314 25.032 1.00 15.92 N ANISOU 1258 N THR A 159 2097 1812 2138 -86 -229 -85 N ATOM 1259 CA THR A 159 26.204 -8.186 24.253 1.00 16.53 C ANISOU 1259 CA THR A 159 2039 1894 2348 -278 -218 18 C ATOM 1260 C THR A 159 26.775 -9.546 23.891 1.00 15.91 C ANISOU 1260 C THR A 159 1852 1906 2287 -219 -162 214 C ATOM 1261 O THR A 159 26.466 -10.556 24.527 1.00 16.61 O ANISOU 1261 O THR A 159 1960 2071 2278 -420 -93 256 O ATOM 1262 CB THR A 159 27.277 -7.389 25.013 1.00 18.76 C ANISOU 1262 CB THR A 159 2523 1824 2780 -271 -548 -157 C ATOM 1263 OG1 THR A 159 27.509 -8.004 26.287 1.00 21.05 O ANISOU 1263 OG1 THR A 159 2781 2477 2739 -454 -766 -64 O ATOM 1264 CG2 THR A 159 26.851 -5.932 25.210 1.00 19.80 C ANISOU 1264 CG2 THR A 159 2500 1836 3185 -287 -181 -284 C ATOM 1265 N VAL A 160 27.633 -9.569 22.875 1.00 15.29 N ANISOU 1265 N VAL A 160 1913 1755 2139 -89 -173 93 N ATOM 1266 CA VAL A 160 28.354 -10.787 22.515 1.00 15.18 C ANISOU 1266 CA VAL A 160 1802 1781 2182 -64 -102 224 C ATOM 1267 C VAL A 160 29.127 -11.302 23.732 1.00 15.73 C ANISOU 1267 C VAL A 160 1803 1960 2214 -151 -257 116 C ATOM 1268 O VAL A 160 29.808 -10.540 24.413 1.00 17.52 O ANISOU 1268 O VAL A 160 2058 2148 2451 -317 -437 161 O ATOM 1269 CB VAL A 160 29.298 -10.544 21.317 1.00 16.02 C ANISOU 1269 CB VAL A 160 1895 1993 2197 58 -6 276 C ATOM 1270 CG1 VAL A 160 30.215 -11.739 21.086 1.00 16.97 C ANISOU 1270 CG1 VAL A 160 2038 1972 2438 91 -110 216 C ATOM 1271 CG2 VAL A 160 28.490 -10.274 20.061 1.00 16.19 C ANISOU 1271 CG2 VAL A 160 1790 2037 2322 88 -60 225 C ATOM 1272 N GLY A 161 28.985 -12.595 24.017 1.00 15.10 N ANISOU 1272 N GLY A 161 1735 1941 2058 -236 -249 169 N ATOM 1273 CA GLY A 161 29.661 -13.214 25.156 1.00 16.19 C ANISOU 1273 CA GLY A 161 1902 2281 1968 -334 -348 127 C ATOM 1274 C GLY A 161 28.842 -13.265 26.434 1.00 15.43 C ANISOU 1274 C GLY A 161 1654 2028 2178 -223 -254 143 C ATOM 1275 O GLY A 161 29.184 -14.002 27.348 1.00 16.48 O ANISOU 1275 O GLY A 161 1914 2140 2206 -92 -371 139 O ATOM 1276 N GLU A 162 27.756 -12.494 26.502 1.00 14.89 N ANISOU 1276 N GLU A 162 1634 1796 2226 -345 -175 61 N ATOM 1277 CA GLU A 162 26.880 -12.499 27.674 1.00 15.10 C ANISOU 1277 CA GLU A 162 1557 1864 2315 -424 -171 -46 C ATOM 1278 C GLU A 162 26.100 -13.810 27.734 1.00 13.93 C ANISOU 1278 C GLU A 162 1801 1640 1852 -284 -277 281 C ATOM 1279 O GLU A 162 25.616 -14.300 26.711 1.00 16.16 O ANISOU 1279 O GLU A 162 2047 2057 2033 -468 -350 87 O ATOM 1280 CB GLU A 162 25.917 -11.318 27.590 1.00 17.85 C ANISOU 1280 CB GLU A 162 1950 2049 2783 -151 -6 265 C ATOM 1281 CG GLU A 162 25.077 -11.035 28.822 1.00 19.39 C ANISOU 1281 CG GLU A 162 2392 2098 2874 -244 90 105 C ATOM 1282 CD GLU A 162 24.202 -9.803 28.649 1.00 23.12 C ANISOU 1282 CD GLU A 162 2820 2413 3549 154 320 328 C ATOM 1283 OE1 GLU A 162 23.082 -9.787 29.203 1.00 29.14 O ANISOU 1283 OE1 GLU A 162 3269 3294 4507 347 893 754 O ATOM 1284 OE2 GLU A 162 24.623 -8.850 27.954 1.00 21.06 O ANISOU 1284 OE2 GLU A 162 2835 2345 2818 295 242 114 O ATOM 1285 N LEU A 163 25.975 -14.381 28.924 1.00 13.11 N ANISOU 1285 N LEU A 163 1479 1771 1731 -297 -97 126 N ATOM 1286 CA LEU A 163 25.166 -15.579 29.091 1.00 12.76 C ANISOU 1286 CA LEU A 163 1405 1754 1687 -224 -102 129 C ATOM 1287 C LEU A 163 23.689 -15.234 28.899 1.00 13.22 C ANISOU 1287 C LEU A 163 1462 1819 1740 -151 -166 16 C ATOM 1288 O LEU A 163 23.272 -14.108 29.187 1.00 15.22 O ANISOU 1288 O LEU A 163 1670 1823 2287 -128 -223 -133 O ATOM 1289 CB LEU A 163 25.410 -16.179 30.472 1.00 12.96 C ANISOU 1289 CB LEU A 163 1178 2067 1678 -222 -189 170 C ATOM 1290 CG LEU A 163 26.849 -16.595 30.785 1.00 14.47 C ANISOU 1290 CG LEU A 163 1335 2215 1948 51 -227 142 C ATOM 1291 CD1 LEU A 163 26.928 -17.051 32.238 1.00 16.46 C ANISOU 1291 CD1 LEU A 163 1662 2638 1951 -189 -302 266 C ATOM 1292 CD2 LEU A 163 27.304 -17.697 29.844 1.00 17.46 C ANISOU 1292 CD2 LEU A 163 1868 2542 2223 186 -204 -102 C ATOM 1293 N GLY A 164 22.902 -16.198 28.425 1.00 11.88 N ANISOU 1293 N GLY A 164 1296 1823 1394 -94 -79 53 N ATOM 1294 CA GLY A 164 21.521 -15.919 28.055 1.00 11.77 C ANISOU 1294 CA GLY A 164 1322 1633 1514 -137 -135 -53 C ATOM 1295 C GLY A 164 20.522 -17.031 28.275 1.00 10.74 C ANISOU 1295 C GLY A 164 1361 1489 1227 -52 -165 -50 C ATOM 1296 O GLY A 164 20.869 -18.176 28.553 1.00 12.20 O ANISOU 1296 O GLY A 164 1322 1566 1746 74 -101 16 O ATOM 1297 N ASP A 165 19.263 -16.655 28.112 1.00 11.45 N ANISOU 1297 N ASP A 165 1308 1436 1606 -79 -114 25 N ATOM 1298 CA ASP A 165 18.117 -17.501 28.375 1.00 11.11 C ANISOU 1298 CA ASP A 165 1315 1467 1437 -84 -74 -36 C ATOM 1299 C ASP A 165 17.287 -17.544 27.092 1.00 10.52 C ANISOU 1299 C ASP A 165 1323 1323 1348 -24 -10 56 C ATOM 1300 O ASP A 165 16.856 -16.512 26.588 1.00 11.29 O ANISOU 1300 O ASP A 165 1424 1363 1503 16 -146 65 O ATOM 1301 CB ASP A 165 17.362 -16.913 29.589 1.00 11.16 C ANISOU 1301 CB ASP A 165 1208 1626 1405 10 -74 -21 C ATOM 1302 CG ASP A 165 16.099 -17.678 29.967 1.00 11.09 C ANISOU 1302 CG ASP A 165 1203 1457 1552 118 33 -78 C ATOM 1303 OD1 ASP A 165 15.278 -17.965 29.101 1.00 12.06 O ANISOU 1303 OD1 ASP A 165 1445 1581 1554 -118 -57 33 O ATOM 1304 OD2 ASP A 165 15.893 -17.913 31.172 1.00 13.03 O ANISOU 1304 OD2 ASP A 165 1405 2014 1531 -3 -47 -35 O ATOM 1305 N VAL A 166 17.104 -18.744 26.553 1.00 10.24 N ANISOU 1305 N VAL A 166 1196 1439 1254 73 19 -104 N ATOM 1306 CA VAL A 166 16.350 -18.933 25.306 1.00 10.20 C ANISOU 1306 CA VAL A 166 1265 1353 1256 85 -34 0 C ATOM 1307 C VAL A 166 14.908 -18.417 25.417 1.00 9.71 C ANISOU 1307 C VAL A 166 1204 1215 1270 -26 7 16 C ATOM 1308 O VAL A 166 14.424 -17.705 24.531 1.00 10.95 O ANISOU 1308 O VAL A 166 1475 1337 1345 161 -77 -7 O ATOM 1309 CB VAL A 166 16.333 -20.412 24.877 1.00 10.63 C ANISOU 1309 CB VAL A 166 1275 1383 1380 93 40 -43 C ATOM 1310 CG1 VAL A 166 15.298 -20.664 23.789 1.00 12.22 C ANISOU 1310 CG1 VAL A 166 1586 1625 1429 198 -137 -86 C ATOM 1311 CG2 VAL A 166 17.723 -20.850 24.419 1.00 11.85 C ANISOU 1311 CG2 VAL A 166 1350 1596 1557 226 94 -94 C ATOM 1312 N ARG A 167 14.230 -18.765 26.506 1.00 10.28 N ANISOU 1312 N ARG A 167 1207 1366 1331 -35 97 -44 N ATOM 1313 CA ARG A 167 12.851 -18.324 26.730 1.00 10.38 C ANISOU 1313 CA ARG A 167 1285 1316 1343 123 42 101 C ATOM 1314 C ARG A 167 12.750 -16.793 26.750 1.00 10.87 C ANISOU 1314 C ARG A 167 1387 1309 1434 39 -122 -30 C ATOM 1315 O ARG A 167 11.880 -16.217 26.082 1.00 10.88 O ANISOU 1315 O ARG A 167 1424 1170 1538 102 -122 -40 O ATOM 1316 CB ARG A 167 12.334 -18.920 28.044 1.00 10.88 C ANISOU 1316 CB ARG A 167 1121 1612 1401 -14 106 112 C ATOM 1317 CG ARG A 167 10.867 -18.648 28.352 1.00 10.53 C ANISOU 1317 CG ARG A 167 1150 1342 1506 36 131 106 C ATOM 1318 CD ARG A 167 10.489 -19.238 29.705 1.00 11.38 C ANISOU 1318 CD ARG A 167 1556 1329 1436 7 111 60 C ATOM 1319 NE ARG A 167 11.098 -18.536 30.840 1.00 12.21 N ANISOU 1319 NE ARG A 167 1585 1448 1606 -70 184 -113 N ATOM 1320 CZ ARG A 167 10.529 -17.534 31.511 1.00 12.03 C ANISOU 1320 CZ ARG A 167 1565 1397 1608 66 -125 -92 C ATOM 1321 NH1 ARG A 167 9.322 -17.079 31.161 1.00 12.59 N ANISOU 1321 NH1 ARG A 167 1472 1663 1646 -4 -87 83 N ATOM 1322 NH2 ARG A 167 11.177 -16.981 32.531 1.00 14.51 N ANISOU 1322 NH2 ARG A 167 1859 1847 1804 -188 -255 -202 N ATOM 1323 N GLU A 168 13.648 -16.153 27.496 1.00 10.82 N ANISOU 1323 N GLU A 168 1266 1318 1527 -48 9 -78 N ATOM 1324 CA GLU A 168 13.664 -14.694 27.600 1.00 11.98 C ANISOU 1324 CA GLU A 168 1679 1340 1531 65 -108 -68 C ATOM 1325 C GLU A 168 13.954 -14.035 26.247 1.00 11.73 C ANISOU 1325 C GLU A 168 1414 1444 1599 47 50 -90 C ATOM 1326 O GLU A 168 13.319 -13.050 25.876 1.00 12.68 O ANISOU 1326 O GLU A 168 1608 1347 1862 53 48 -124 O ATOM 1327 CB GLU A 168 14.698 -14.254 28.636 1.00 13.50 C ANISOU 1327 CB GLU A 168 2159 1403 1567 164 -360 -161 C ATOM 1328 CG GLU A 168 14.590 -12.778 28.987 1.00 16.05 C ANISOU 1328 CG GLU A 168 2687 1384 2026 -140 -372 -251 C ATOM 1329 CD GLU A 168 15.463 -12.390 30.162 1.00 23.35 C ANISOU 1329 CD GLU A 168 3790 2651 2430 -13 -1037 -495 C ATOM 1330 OE1 GLU A 168 16.291 -13.204 30.593 1.00 29.40 O ANISOU 1330 OE1 GLU A 168 4308 3643 3218 359 -1853 -429 O ATOM 1331 OE2 GLU A 168 15.330 -11.258 30.650 1.00 25.50 O ANISOU 1331 OE2 GLU A 168 4144 2838 2704 -478 -417 -779 O ATOM 1332 N THR A 169 14.917 -14.598 25.521 1.00 11.40 N ANISOU 1332 N THR A 169 1451 1537 1340 -73 74 -198 N ATOM 1333 CA THR A 169 15.320 -14.061 24.224 1.00 11.42 C ANISOU 1333 CA THR A 169 1569 1271 1499 130 68 17 C ATOM 1334 C THR A 169 14.183 -14.212 23.207 1.00 11.62 C ANISOU 1334 C THR A 169 1559 1194 1660 29 4 138 C ATOM 1335 O THR A 169 13.879 -13.274 22.454 1.00 12.47 O ANISOU 1335 O THR A 169 1719 1390 1627 66 -47 233 O ATOM 1336 CB THR A 169 16.625 -14.732 23.762 1.00 11.98 C ANISOU 1336 CB THR A 169 1571 1652 1326 207 177 233 C ATOM 1337 OG1 THR A 169 17.640 -14.500 24.753 1.00 14.10 O ANISOU 1337 OG1 THR A 169 1605 2050 1700 50 129 48 O ATOM 1338 CG2 THR A 169 17.076 -14.194 22.393 1.00 13.02 C ANISOU 1338 CG2 THR A 169 1910 1629 1409 198 377 210 C ATOM 1339 N MET A 170 13.554 -15.389 23.199 1.00 11.62 N ANISOU 1339 N MET A 170 1539 1247 1626 7 -30 -81 N ATOM 1340 CA AMET A 170 12.395 -15.632 22.348 0.25 12.86 C ANISOU 1340 CA AMET A 170 1519 1473 1893 -69 -115 58 C ATOM 1341 CA BMET A 170 12.414 -15.625 22.326 0.25 12.48 C ANISOU 1341 CA BMET A 170 1444 1319 1977 -165 -36 -125 C ATOM 1342 CA CMET A 170 12.420 -15.616 22.317 0.25 12.70 C ANISOU 1342 CA CMET A 170 1538 1401 1886 -46 -158 106 C ATOM 1343 CA DMET A 170 12.376 -15.646 22.371 0.25 12.68 C ANISOU 1343 CA DMET A 170 1650 1505 1662 20 -95 -111 C ATOM 1344 C MET A 170 11.300 -14.613 22.624 1.00 12.69 C ANISOU 1344 C MET A 170 1476 1482 1863 -52 -84 117 C ATOM 1345 O MET A 170 10.663 -14.095 21.695 1.00 15.33 O ANISOU 1345 O MET A 170 1791 1578 2453 -148 -474 423 O ATOM 1346 CB AMET A 170 11.853 -17.040 22.574 0.25 14.71 C ANISOU 1346 CB AMET A 170 1940 1663 1983 -319 -78 196 C ATOM 1347 CB BMET A 170 11.915 -17.068 22.465 0.25 10.78 C ANISOU 1347 CB BMET A 170 761 1120 2214 183 391 -606 C ATOM 1348 CB CMET A 170 11.938 -17.067 22.415 0.25 13.19 C ANISOU 1348 CB CMET A 170 1735 1447 1830 -125 -251 194 C ATOM 1349 CB DMET A 170 11.795 -17.017 22.694 0.25 12.17 C ANISOU 1349 CB DMET A 170 2310 1112 1198 340 268 -500 C ATOM 1350 CG AMET A 170 12.344 -18.059 21.569 0.25 15.83 C ANISOU 1350 CG AMET A 170 1886 2023 2104 -256 183 125 C ATOM 1351 CG BMET A 170 12.856 -18.132 21.928 0.25 11.61 C ANISOU 1351 CG BMET A 170 881 1111 2417 347 469 -839 C ATOM 1352 CG CMET A 170 10.896 -17.455 21.376 0.25 12.56 C ANISOU 1352 CG CMET A 170 1494 1371 1904 51 -291 283 C ATOM 1353 CG DMET A 170 12.370 -18.129 21.855 0.25 9.68 C ANISOU 1353 CG DMET A 170 1325 1016 1334 680 374 -323 C ATOM 1354 SD AMET A 170 11.848 -17.654 19.883 0.25 13.91 S ANISOU 1354 SD AMET A 170 1528 1697 2057 -360 239 -15 S ATOM 1355 SD BMET A 170 12.804 -18.303 20.135 0.25 16.13 S ANISOU 1355 SD BMET A 170 1861 1795 2472 239 619 -885 S ATOM 1356 SD CMET A 170 11.505 -17.426 19.677 0.25 13.12 S ANISOU 1356 SD CMET A 170 1648 1335 2002 390 -174 258 S ATOM 1357 SD DMET A 170 12.436 -17.674 20.111 0.25 13.29 S ANISOU 1357 SD DMET A 170 1914 1689 1443 129 763 -241 S ATOM 1358 CE AMET A 170 11.767 -19.306 19.196 0.25 14.58 C ANISOU 1358 CE AMET A 170 1801 1675 2061 -301 52 -3 C ATOM 1359 CE BMET A 170 11.047 -18.545 19.860 0.25 13.94 C ANISOU 1359 CE BMET A 170 1959 1633 1705 -127 633 -690 C ATOM 1360 CE CMET A 170 12.468 -18.938 19.649 0.25 14.29 C ANISOU 1360 CE CMET A 170 1800 1534 2094 599 -254 213 C ATOM 1361 CE DMET A 170 12.863 -19.250 19.377 0.25 12.00 C ANISOU 1361 CE DMET A 170 1572 1525 1460 222 357 -90 C ATOM 1362 N THR A 171 11.086 -14.318 23.907 1.00 12.94 N ANISOU 1362 N THR A 171 1324 1555 2036 47 185 0 N ATOM 1363 CA THR A 171 10.063 -13.345 24.308 1.00 14.35 C ANISOU 1363 CA THR A 171 1558 1566 2328 257 280 217 C ATOM 1364 C THR A 171 10.355 -11.969 23.694 1.00 14.79 C ANISOU 1364 C THR A 171 1692 1556 2369 91 52 227 C ATOM 1365 O THR A 171 9.452 -11.331 23.134 1.00 17.08 O ANISOU 1365 O THR A 171 2034 1736 2719 226 -149 335 O ATOM 1366 CB THR A 171 9.920 -13.231 25.838 1.00 15.55 C ANISOU 1366 CB THR A 171 1747 1746 2414 334 428 300 C ATOM 1367 OG1 THR A 171 9.694 -14.531 26.381 1.00 17.77 O ANISOU 1367 OG1 THR A 171 1624 2055 3070 507 634 851 O ATOM 1368 CG2 THR A 171 8.745 -12.335 26.225 1.00 16.99 C ANISOU 1368 CG2 THR A 171 1880 2051 2524 555 449 348 C ATOM 1369 N HIS A 172 11.607 -11.514 23.794 1.00 13.46 N ANISOU 1369 N HIS A 172 1737 1382 1994 44 82 215 N ATOM 1370 CA HIS A 172 12.013 -10.239 23.174 1.00 14.18 C ANISOU 1370 CA HIS A 172 1883 1323 2181 -79 70 172 C ATOM 1371 C HIS A 172 11.771 -10.219 21.692 1.00 14.58 C ANISOU 1371 C HIS A 172 1800 1513 2226 95 -19 162 C ATOM 1372 O HIS A 172 11.196 -9.257 21.156 1.00 15.44 O ANISOU 1372 O HIS A 172 2119 1529 2217 179 -34 189 O ATOM 1373 CB HIS A 172 13.486 -9.951 23.440 1.00 15.71 C ANISOU 1373 CB HIS A 172 2048 1606 2314 -261 -128 -82 C ATOM 1374 CG HIS A 172 13.756 -9.370 24.799 1.00 16.72 C ANISOU 1374 CG HIS A 172 2478 1578 2296 -200 -191 -49 C ATOM 1375 ND1 HIS A 172 14.471 -10.017 25.737 1.00 22.20 N ANISOU 1375 ND1 HIS A 172 3348 2478 2608 -157 -837 -119 N ATOM 1376 CD2 HIS A 172 13.383 -8.152 25.357 1.00 19.46 C ANISOU 1376 CD2 HIS A 172 3105 1634 2656 62 -116 -41 C ATOM 1377 CE1 HIS A 172 14.545 -9.260 26.840 1.00 21.39 C ANISOU 1377 CE1 HIS A 172 3092 2369 2666 -237 -620 -202 C ATOM 1378 NE2 HIS A 172 13.884 -8.115 26.606 1.00 25.59 N ANISOU 1378 NE2 HIS A 172 3786 2893 3042 179 -645 35 N ATOM 1379 N LEU A 173 12.209 -11.274 21.007 1.00 13.47 N ANISOU 1379 N LEU A 173 1589 1430 2096 -56 -34 161 N ATOM 1380 CA ALEU A 173 12.064 -11.359 19.552 0.50 14.27 C ANISOU 1380 CA ALEU A 173 1751 1623 2047 223 127 197 C ATOM 1381 CA BLEU A 173 12.067 -11.341 19.553 0.50 13.82 C ANISOU 1381 CA BLEU A 173 1700 1558 1992 187 202 254 C ATOM 1382 C LEU A 173 10.612 -11.361 19.111 1.00 14.18 C ANISOU 1382 C LEU A 173 1819 1727 1841 96 48 344 C ATOM 1383 O LEU A 173 10.250 -10.700 18.147 1.00 14.39 O ANISOU 1383 O LEU A 173 1805 1728 1932 327 78 418 O ATOM 1384 CB ALEU A 173 12.760 -12.604 19.002 0.50 17.41 C ANISOU 1384 CB ALEU A 173 2246 1645 2724 439 -92 8 C ATOM 1385 CB BLEU A 173 12.792 -12.556 18.979 0.50 14.71 C ANISOU 1385 CB BLEU A 173 1957 1490 2141 231 163 230 C ATOM 1386 CG ALEU A 173 14.050 -12.391 18.225 0.50 20.82 C ANISOU 1386 CG ALEU A 173 2550 2019 3338 127 194 -137 C ATOM 1387 CG BLEU A 173 14.309 -12.507 18.966 0.50 14.19 C ANISOU 1387 CG BLEU A 173 1984 1598 1808 -70 129 342 C ATOM 1388 CD1ALEU A 173 14.846 -11.229 18.801 0.50 20.86 C ANISOU 1388 CD1ALEU A 173 2524 2130 3270 18 -8 17 C ATOM 1389 CD1BLEU A 173 14.828 -13.856 18.498 0.50 15.54 C ANISOU 1389 CD1BLEU A 173 2041 1779 2082 27 265 170 C ATOM 1390 CD2ALEU A 173 14.853 -13.683 18.220 0.50 19.04 C ANISOU 1390 CD2ALEU A 173 2495 2145 2594 241 232 -95 C ATOM 1391 CD2BLEU A 173 14.758 -11.391 18.030 0.50 15.39 C ANISOU 1391 CD2BLEU A 173 2072 1689 2087 -397 449 245 C ATOM 1392 N LEU A 174 9.784 -12.119 19.822 1.00 14.17 N ANISOU 1392 N LEU A 174 1526 1660 2195 5 48 210 N ATOM 1393 CA LEU A 174 8.382 -12.267 19.438 1.00 14.10 C ANISOU 1393 CA LEU A 174 1573 1712 2073 -145 -1 176 C ATOM 1394 C LEU A 174 7.559 -10.981 19.603 1.00 13.80 C ANISOU 1394 C LEU A 174 1544 1731 1967 -88 -13 312 C ATOM 1395 O LEU A 174 6.479 -10.871 19.028 1.00 14.47 O ANISOU 1395 O LEU A 174 1711 1762 2025 -65 -184 337 O ATOM 1396 CB LEU A 174 7.740 -13.467 20.147 1.00 14.93 C ANISOU 1396 CB LEU A 174 1705 1618 2349 -188 -307 314 C ATOM 1397 CG LEU A 174 8.271 -14.836 19.708 1.00 16.08 C ANISOU 1397 CG LEU A 174 1906 1741 2462 -175 -509 19 C ATOM 1398 CD1 LEU A 174 7.637 -15.951 20.528 1.00 18.31 C ANISOU 1398 CD1 LEU A 174 1910 2109 2938 -333 -226 137 C ATOM 1399 CD2 LEU A 174 8.057 -15.083 18.223 1.00 18.81 C ANISOU 1399 CD2 LEU A 174 2689 2044 2414 -129 -653 193 C ATOM 1400 N GLN A 175 8.071 -10.011 20.365 1.00 14.59 N ANISOU 1400 N GLN A 175 1687 1665 2189 -45 115 190 N ATOM 1401 CA GLN A 175 7.431 -8.686 20.426 1.00 15.43 C ANISOU 1401 CA GLN A 175 1733 1850 2280 184 -32 165 C ATOM 1402 C GLN A 175 7.392 -8.044 19.045 1.00 15.67 C ANISOU 1402 C GLN A 175 1756 2002 2193 135 217 116 C ATOM 1403 O GLN A 175 6.549 -7.188 18.778 1.00 17.91 O ANISOU 1403 O GLN A 175 1968 2229 2607 382 379 323 O ATOM 1404 CB GLN A 175 8.170 -7.723 21.364 1.00 17.11 C ANISOU 1404 CB GLN A 175 2170 2030 2299 235 43 -157 C ATOM 1405 CG GLN A 175 8.411 -8.207 22.776 1.00 18.62 C ANISOU 1405 CG GLN A 175 2635 1805 2633 352 38 283 C ATOM 1406 CD GLN A 175 7.142 -8.529 23.531 1.00 19.23 C ANISOU 1406 CD GLN A 175 2490 2107 2709 495 20 313 C ATOM 1407 OE1 GLN A 175 7.079 -9.520 24.259 1.00 26.19 O ANISOU 1407 OE1 GLN A 175 3635 2703 3611 -46 -233 1010 O ATOM 1408 NE2 GLN A 175 6.127 -7.694 23.373 1.00 21.20 N ANISOU 1408 NE2 GLN A 175 2583 2525 2944 775 435 786 N ATOM 1409 N HIS A 176 8.331 -8.447 18.188 1.00 14.38 N ANISOU 1409 N HIS A 176 1641 1783 2037 169 81 128 N ATOM 1410 CA HIS A 176 8.430 -7.936 16.823 1.00 15.68 C ANISOU 1410 CA HIS A 176 1764 2009 2183 16 181 348 C ATOM 1411 C HIS A 176 7.871 -8.856 15.779 1.00 15.18 C ANISOU 1411 C HIS A 176 1890 1733 2142 279 156 354 C ATOM 1412 O HIS A 176 8.058 -8.631 14.582 1.00 17.71 O ANISOU 1412 O HIS A 176 2423 2120 2186 221 216 436 O ATOM 1413 CB HIS A 176 9.876 -7.592 16.507 1.00 17.04 C ANISOU 1413 CB HIS A 176 1836 2127 2510 18 399 166 C ATOM 1414 CG HIS A 176 10.377 -6.404 17.269 1.00 15.56 C ANISOU 1414 CG HIS A 176 1740 1885 2286 109 372 304 C ATOM 1415 ND1 HIS A 176 10.096 -5.135 16.900 1.00 17.41 N ANISOU 1415 ND1 HIS A 176 2276 1797 2539 -32 181 288 N ATOM 1416 CD2 HIS A 176 11.135 -6.318 18.431 1.00 17.80 C ANISOU 1416 CD2 HIS A 176 2010 2473 2280 -128 324 229 C ATOM 1417 CE1 HIS A 176 10.659 -4.282 17.778 1.00 20.03 C ANISOU 1417 CE1 HIS A 176 2534 2601 2472 -344 65 205 C ATOM 1418 NE2 HIS A 176 11.293 -5.005 18.713 1.00 20.34 N ANISOU 1418 NE2 HIS A 176 2490 2290 2946 -173 351 559 N ATOM 1419 N ALA A 177 7.180 -9.903 16.221 1.00 15.41 N ANISOU 1419 N ALA A 177 1639 2123 2091 69 158 343 N ATOM 1420 CA ALA A 177 6.567 -10.854 15.316 1.00 16.68 C ANISOU 1420 CA ALA A 177 1809 2184 2342 -15 -32 378 C ATOM 1421 C ALA A 177 5.091 -10.516 15.151 1.00 16.67 C ANISOU 1421 C ALA A 177 1772 2312 2248 -134 -10 498 C ATOM 1422 O ALA A 177 4.482 -9.887 16.023 1.00 17.92 O ANISOU 1422 O ALA A 177 1961 2081 2767 122 178 679 O ATOM 1423 CB ALA A 177 6.735 -12.272 15.844 1.00 17.37 C ANISOU 1423 CB ALA A 177 2039 1924 2636 110 -72 46 C ATOM 1424 N ASN A 178 4.512 -10.919 14.029 1.00 20.18 N ANISOU 1424 N ASN A 178 1879 3472 2314 -263 -114 444 N ATOM 1425 CA ASN A 178 3.088 -10.713 13.865 1.00 19.41 C ANISOU 1425 CA ASN A 178 1942 3325 2107 -118 -284 731 C ATOM 1426 C ASN A 178 2.301 -11.792 14.593 1.00 17.93 C ANISOU 1426 C ASN A 178 1848 2938 2025 17 -254 549 C ATOM 1427 O ASN A 178 2.043 -12.862 14.063 1.00 19.19 O ANISOU 1427 O ASN A 178 2474 3001 1817 411 -142 417 O ATOM 1428 CB ASN A 178 2.668 -10.610 12.398 1.00 22.72 C ANISOU 1428 CB ASN A 178 3010 3669 1954 27 -71 1002 C ATOM 1429 CG ASN A 178 1.236 -10.123 12.244 1.00 26.63 C ANISOU 1429 CG ASN A 178 3036 3968 3114 34 -93 998 C ATOM 1430 OD1 ASN A 178 0.466 -10.080 13.216 1.00 23.30 O ANISOU 1430 OD1 ASN A 178 2465 3137 3249 418 -294 1390 O ATOM 1431 ND2 ASN A 178 0.877 -9.731 11.029 1.00 33.12 N ANISOU 1431 ND2 ASN A 178 4541 4961 3082 331 -250 1086 N ATOM 1432 N LEU A 179 1.947 -11.491 15.835 1.00 17.01 N ANISOU 1432 N LEU A 179 1826 2608 2028 -385 49 631 N ATOM 1433 CA LEU A 179 1.138 -12.388 16.653 1.00 15.42 C ANISOU 1433 CA LEU A 179 1901 2009 1947 -233 -142 630 C ATOM 1434 C LEU A 179 -0.210 -11.741 16.946 1.00 16.83 C ANISOU 1434 C LEU A 179 2183 1943 2268 -26 16 467 C ATOM 1435 O LEU A 179 -0.850 -12.037 17.957 1.00 16.88 O ANISOU 1435 O LEU A 179 2161 1750 2500 -254 43 547 O ATOM 1436 CB LEU A 179 1.879 -12.740 17.944 1.00 14.20 C ANISOU 1436 CB LEU A 179 2002 1771 1622 -113 24 359 C ATOM 1437 CG LEU A 179 3.134 -13.593 17.743 1.00 14.77 C ANISOU 1437 CG LEU A 179 1935 1918 1758 -50 -188 185 C ATOM 1438 CD1 LEU A 179 3.856 -13.780 19.070 1.00 17.50 C ANISOU 1438 CD1 LEU A 179 2196 2514 1938 -97 -334 572 C ATOM 1439 CD2 LEU A 179 2.832 -14.943 17.116 1.00 16.35 C ANISOU 1439 CD2 LEU A 179 2451 1985 1773 212 -388 20 C ATOM 1440 N GLU A 180 -0.652 -10.867 16.042 1.00 18.31 N ANISOU 1440 N GLU A 180 2147 1969 2839 -67 159 807 N ATOM 1441 CA GLU A 180 -1.872 -10.098 16.277 1.00 21.10 C ANISOU 1441 CA GLU A 180 2217 2490 3307 148 181 794 C ATOM 1442 C GLU A 180 -3.098 -10.990 16.462 1.00 20.71 C ANISOU 1442 C GLU A 180 2560 2129 3178 82 327 903 C ATOM 1443 O GLU A 180 -3.994 -10.652 17.234 1.00 23.74 O ANISOU 1443 O GLU A 180 2465 2756 3798 363 487 895 O ATOM 1444 CB GLU A 180 -2.103 -9.058 15.169 1.00 23.17 C ANISOU 1444 CB GLU A 180 2664 2540 3596 412 -83 901 C ATOM 1445 CG GLU A 180 -2.487 -9.622 13.805 1.00 29.09 C ANISOU 1445 CG GLU A 180 3669 3300 4081 -124 -139 516 C ATOM 1446 CD GLU A 180 -2.512 -8.575 12.699 1.00 36.40 C ANISOU 1446 CD GLU A 180 5406 4133 4292 174 -240 908 C ATOM 1447 OE1 GLU A 180 -2.589 -7.360 13.004 1.00 42.18 O ANISOU 1447 OE1 GLU A 180 5767 4127 6132 424 -326 708 O ATOM 1448 OE2 GLU A 180 -2.457 -8.976 11.515 1.00 40.24 O ANISOU 1448 OE2 GLU A 180 5572 5420 4298 -330 -538 581 O ATOM 1449 N SER A 181 -3.129 -12.124 15.763 1.00 18.31 N ANISOU 1449 N SER A 181 2085 2131 2740 91 -213 1127 N ATOM 1450 CA SER A 181 -4.257 -13.044 15.869 1.00 19.23 C ANISOU 1450 CA SER A 181 2244 2143 2920 -22 -217 885 C ATOM 1451 C SER A 181 -3.996 -14.230 16.803 1.00 17.83 C ANISOU 1451 C SER A 181 2067 2204 2503 42 -286 737 C ATOM 1452 O SER A 181 -4.815 -15.149 16.873 1.00 19.70 O ANISOU 1452 O SER A 181 2159 2879 2447 -371 -540 819 O ATOM 1453 CB SER A 181 -4.683 -13.540 14.486 1.00 24.04 C ANISOU 1453 CB SER A 181 3192 2809 3131 -197 -337 569 C ATOM 1454 OG SER A 181 -3.693 -14.367 13.917 1.00 26.86 O ANISOU 1454 OG SER A 181 3422 3371 3412 68 -398 511 O ATOM 1455 N ALA A 182 -2.869 -14.230 17.516 1.00 15.08 N ANISOU 1455 N ALA A 182 1784 1845 2100 68 78 582 N ATOM 1456 CA ALA A 182 -2.639 -15.277 18.522 1.00 13.26 C ANISOU 1456 CA ALA A 182 1535 1667 1836 84 65 360 C ATOM 1457 C ALA A 182 -3.568 -15.060 19.710 1.00 13.11 C ANISOU 1457 C ALA A 182 1691 1597 1693 -92 73 381 C ATOM 1458 O ALA A 182 -3.655 -13.959 20.250 1.00 14.45 O ANISOU 1458 O ALA A 182 1967 1663 1857 -136 74 276 O ATOM 1459 CB ALA A 182 -1.190 -15.294 18.977 1.00 13.71 C ANISOU 1459 CB ALA A 182 1564 1916 1728 -18 -33 247 C ATOM 1460 N LYS A 183 -4.280 -16.110 20.096 1.00 11.38 N ANISOU 1460 N LYS A 183 1469 1504 1351 -9 -49 322 N ATOM 1461 CA LYS A 183 -5.314 -16.005 21.127 1.00 11.81 C ANISOU 1461 CA LYS A 183 1385 1393 1706 18 72 255 C ATOM 1462 C LYS A 183 -5.298 -17.266 21.982 1.00 11.23 C ANISOU 1462 C LYS A 183 1333 1467 1465 99 -62 227 C ATOM 1463 O LYS A 183 -5.197 -18.382 21.452 1.00 13.03 O ANISOU 1463 O LYS A 183 1604 1521 1823 108 -10 93 O ATOM 1464 CB LYS A 183 -6.681 -15.821 20.462 1.00 14.02 C ANISOU 1464 CB LYS A 183 1536 1896 1894 139 -74 240 C ATOM 1465 CG LYS A 183 -7.870 -15.705 21.408 1.00 15.96 C ANISOU 1465 CG LYS A 183 1746 2268 2049 236 96 351 C ATOM 1466 CD LYS A 183 -9.153 -15.586 20.585 1.00 17.94 C ANISOU 1466 CD LYS A 183 1783 2481 2549 387 -79 275 C ATOM 1467 CE LYS A 183 -10.405 -15.485 21.439 1.00 19.00 C ANISOU 1467 CE LYS A 183 1678 2867 2674 -219 -106 222 C ATOM 1468 NZ LYS A 183 -11.612 -15.411 20.561 1.00 21.49 N ANISOU 1468 NZ LYS A 183 1949 3080 3134 -71 -425 302 N ATOM 1469 N ARG A 184 -5.379 -17.083 23.301 1.00 11.05 N ANISOU 1469 N ARG A 184 1308 1442 1447 -5 23 280 N ATOM 1470 CA ARG A 184 -5.438 -18.196 24.248 1.00 10.61 C ANISOU 1470 CA ARG A 184 1171 1348 1513 33 31 235 C ATOM 1471 C ARG A 184 -6.529 -17.931 25.274 1.00 11.06 C ANISOU 1471 C ARG A 184 1219 1373 1607 128 71 196 C ATOM 1472 O ARG A 184 -6.578 -16.849 25.854 1.00 12.72 O ANISOU 1472 O ARG A 184 1536 1569 1728 -121 105 6 O ATOM 1473 CB ARG A 184 -4.082 -18.351 24.962 1.00 10.89 C ANISOU 1473 CB ARG A 184 1254 1425 1458 62 -62 248 C ATOM 1474 CG ARG A 184 -4.133 -19.187 26.245 1.00 10.66 C ANISOU 1474 CG ARG A 184 1257 1539 1255 98 -178 121 C ATOM 1475 CD ARG A 184 -2.750 -19.533 26.757 1.00 11.01 C ANISOU 1475 CD ARG A 184 1183 1464 1535 99 -115 79 C ATOM 1476 NE ARG A 184 -2.039 -20.367 25.799 1.00 11.78 N ANISOU 1476 NE ARG A 184 1350 1476 1647 134 40 102 N ATOM 1477 CZ ARG A 184 -0.748 -20.671 25.888 1.00 12.25 C ANISOU 1477 CZ ARG A 184 1378 1748 1527 248 4 -1 C ATOM 1478 NH1 ARG A 184 -0.020 -20.236 26.917 1.00 12.47 N ANISOU 1478 NH1 ARG A 184 1449 1594 1696 61 -271 474 N ATOM 1479 NH2 ARG A 184 -0.194 -21.422 24.940 1.00 13.39 N ANISOU 1479 NH2 ARG A 184 1583 2004 1499 529 102 99 N ATOM 1480 N VAL A 185 -7.395 -18.918 25.493 1.00 11.13 N ANISOU 1480 N VAL A 185 1271 1557 1399 -21 35 98 N ATOM 1481 CA VAL A 185 -8.422 -18.815 26.534 1.00 11.41 C ANISOU 1481 CA VAL A 185 1188 1587 1559 -90 64 166 C ATOM 1482 C VAL A 185 -8.122 -19.861 27.601 1.00 10.63 C ANISOU 1482 C VAL A 185 1240 1421 1375 37 64 -30 C ATOM 1483 O VAL A 185 -7.956 -21.036 27.284 1.00 11.40 O ANISOU 1483 O VAL A 185 1276 1443 1611 -103 -16 -208 O ATOM 1484 CB VAL A 185 -9.838 -19.015 25.953 1.00 12.10 C ANISOU 1484 CB VAL A 185 1223 1754 1618 62 -44 259 C ATOM 1485 CG1 VAL A 185 -10.894 -18.811 27.020 1.00 13.48 C ANISOU 1485 CG1 VAL A 185 1349 2073 1697 51 33 74 C ATOM 1486 CG2 VAL A 185 -10.063 -18.035 24.820 1.00 13.83 C ANISOU 1486 CG2 VAL A 185 1556 1969 1728 181 -165 404 C ATOM 1487 N LEU A 186 -8.036 -19.425 28.855 1.00 11.66 N ANISOU 1487 N LEU A 186 1385 1696 1349 -114 2 1 N ATOM 1488 CA LEU A 186 -7.732 -20.310 29.985 1.00 12.27 C ANISOU 1488 CA LEU A 186 1488 1622 1549 -124 52 95 C ATOM 1489 C LEU A 186 -8.846 -20.272 31.020 1.00 13.28 C ANISOU 1489 C LEU A 186 1568 1836 1641 14 139 -45 C ATOM 1490 O LEU A 186 -9.348 -19.200 31.351 1.00 14.63 O ANISOU 1490 O LEU A 186 1749 1742 2065 -30 252 -1 O ATOM 1491 CB LEU A 186 -6.436 -19.889 30.683 1.00 13.13 C ANISOU 1491 CB LEU A 186 1458 1715 1813 -138 122 -110 C ATOM 1492 CG LEU A 186 -5.137 -20.078 29.910 1.00 12.82 C ANISOU 1492 CG LEU A 186 1294 1769 1805 -23 -33 -182 C ATOM 1493 CD1 LEU A 186 -4.035 -19.243 30.552 1.00 15.54 C ANISOU 1493 CD1 LEU A 186 1325 2287 2292 -317 31 -331 C ATOM 1494 CD2 LEU A 186 -4.744 -21.544 29.842 1.00 14.59 C ANISOU 1494 CD2 LEU A 186 1417 1747 2377 -31 149 -400 C ATOM 1495 N ASN A 187 -9.217 -21.449 31.515 1.00 13.12 N ANISOU 1495 N ASN A 187 1642 1841 1501 -140 121 -157 N ATOM 1496 CA AASN A 187 -10.092 -21.544 32.667 0.50 13.94 C ANISOU 1496 CA AASN A 187 1732 2078 1485 -184 106 -124 C ATOM 1497 CA BASN A 187 -10.122 -21.596 32.660 0.50 13.32 C ANISOU 1497 CA BASN A 187 1619 1954 1486 -243 70 -140 C ATOM 1498 C ASN A 187 -9.362 -22.023 33.900 1.00 13.25 C ANISOU 1498 C ASN A 187 1647 1812 1574 -124 31 -176 C ATOM 1499 O ASN A 187 -8.435 -22.824 33.812 1.00 13.68 O ANISOU 1499 O ASN A 187 1796 2058 1340 68 75 -133 O ATOM 1500 CB AASN A 187 -11.295 -22.433 32.383 0.50 15.38 C ANISOU 1500 CB AASN A 187 1932 2135 1774 -254 53 -398 C ATOM 1501 CB BASN A 187 -11.186 -22.658 32.390 0.50 12.57 C ANISOU 1501 CB BASN A 187 1533 1878 1366 -119 -83 -150 C ATOM 1502 CG AASN A 187 -12.571 -21.644 32.351 0.50 20.52 C ANISOU 1502 CG AASN A 187 2154 2881 2758 96 257 -392 C ATOM 1503 CG BASN A 187 -12.378 -22.112 31.650 0.50 13.25 C ANISOU 1503 CG BASN A 187 1676 2036 1321 -18 -91 -33 C ATOM 1504 OD1AASN A 187 -12.966 -21.063 33.359 0.50 22.96 O ANISOU 1504 OD1AASN A 187 2714 3234 2774 -297 799 -358 O ATOM 1505 OD1BASN A 187 -12.427 -20.926 31.316 0.50 14.14 O ANISOU 1505 OD1BASN A 187 1570 2149 1654 -18 -171 187 O ATOM 1506 ND2AASN A 187 -13.206 -21.581 31.190 0.50 23.31 N ANISOU 1506 ND2AASN A 187 3138 3040 2677 341 144 -272 N ATOM 1507 ND2BASN A 187 -13.356 -22.975 31.396 0.50 13.50 N ANISOU 1507 ND2BASN A 187 1734 2095 1298 -23 -252 -60 N ATOM 1508 N VAL A 188 -9.780 -21.497 35.049 1.00 13.84 N ANISOU 1508 N VAL A 188 1716 1970 1572 -65 -8 -236 N ATOM 1509 CA VAL A 188 -9.290 -21.976 36.325 1.00 13.87 C ANISOU 1509 CA VAL A 188 1613 1992 1662 -110 95 21 C ATOM 1510 C VAL A 188 -10.516 -22.398 37.122 1.00 13.52 C ANISOU 1510 C VAL A 188 1710 2144 1283 -113 44 9 C ATOM 1511 O VAL A 188 -11.445 -21.604 37.293 1.00 15.65 O ANISOU 1511 O VAL A 188 1954 2416 1573 103 171 -51 O ATOM 1512 CB VAL A 188 -8.482 -20.899 37.068 1.00 14.57 C ANISOU 1512 CB VAL A 188 1821 2207 1508 -125 -2 -52 C ATOM 1513 CG1 VAL A 188 -8.052 -21.408 38.438 1.00 16.76 C ANISOU 1513 CG1 VAL A 188 1973 2743 1652 -166 -259 66 C ATOM 1514 CG2 VAL A 188 -7.275 -20.463 36.240 1.00 15.21 C ANISOU 1514 CG2 VAL A 188 1626 2176 1977 -232 61 -335 C ATOM 1515 N VAL A 189 -10.517 -23.652 37.579 1.00 14.85 N ANISOU 1515 N VAL A 189 1849 2278 1514 -288 -87 154 N ATOM 1516 CA VAL A 189 -11.647 -24.232 38.298 1.00 16.63 C ANISOU 1516 CA VAL A 189 1887 2478 1954 -410 27 76 C ATOM 1517 C VAL A 189 -11.209 -24.631 39.702 1.00 16.69 C ANISOU 1517 C VAL A 189 1945 2518 1876 -345 262 189 C ATOM 1518 O VAL A 189 -10.246 -25.381 39.875 1.00 18.53 O ANISOU 1518 O VAL A 189 2030 3057 1953 -145 185 164 O ATOM 1519 CB VAL A 189 -12.226 -25.458 37.546 1.00 16.49 C ANISOU 1519 CB VAL A 189 2267 2239 1759 -480 89 222 C ATOM 1520 CG1 VAL A 189 -13.322 -26.138 38.359 1.00 21.21 C ANISOU 1520 CG1 VAL A 189 2411 2972 2673 -817 367 229 C ATOM 1521 CG2 VAL A 189 -12.767 -25.041 36.182 1.00 17.55 C ANISOU 1521 CG2 VAL A 189 2162 2643 1863 -466 -269 -98 C ATOM 1522 N CYS A 190 -11.932 -24.127 40.699 1.00 18.63 N ANISOU 1522 N CYS A 190 2228 3025 1824 -375 331 94 N ATOM 1523 CA CYS A 190 -11.723 -24.498 42.087 1.00 19.46 C ANISOU 1523 CA CYS A 190 2439 3114 1841 -711 35 -6 C ATOM 1524 C CYS A 190 -13.010 -25.141 42.593 1.00 21.11 C ANISOU 1524 C CYS A 190 2815 3067 2138 -768 315 300 C ATOM 1525 O CYS A 190 -14.100 -24.647 42.301 1.00 24.05 O ANISOU 1525 O CYS A 190 2892 3849 2395 -635 454 598 O ATOM 1526 CB CYS A 190 -11.370 -23.264 42.918 1.00 21.07 C ANISOU 1526 CB CYS A 190 2865 3269 1871 -632 214 -281 C ATOM 1527 SG CYS A 190 -11.267 -23.578 44.697 1.00 22.59 S ANISOU 1527 SG CYS A 190 3150 3395 2037 -589 256 -63 S ATOM 1528 N LYS A 191 -12.878 -26.234 43.349 1.00 22.96 N ANISOU 1528 N LYS A 191 3315 3359 2050 -733 421 489 N ATOM 1529 CA LYS A 191 -14.031 -26.976 43.863 1.00 26.08 C ANISOU 1529 CA LYS A 191 3141 3740 3025 -825 333 569 C ATOM 1530 C LYS A 191 -14.895 -26.102 44.768 1.00 26.72 C ANISOU 1530 C LYS A 191 3171 3783 3197 -757 378 466 C ATOM 1531 O LYS A 191 -16.109 -26.309 44.864 1.00 29.85 O ANISOU 1531 O LYS A 191 3219 4450 3673 -865 434 717 O ATOM 1532 CB LYS A 191 -13.577 -28.231 44.617 1.00 30.16 C ANISOU 1532 CB LYS A 191 3781 4054 3624 -727 387 1076 C ATOM 1533 CG LYS A 191 -13.031 -29.340 43.725 1.00 37.77 C ANISOU 1533 CG LYS A 191 5079 4668 4602 -90 689 788 C ATOM 1534 CD LYS A 191 -12.679 -30.597 44.513 1.00 41.72 C ANISOU 1534 CD LYS A 191 5504 4621 5726 -177 469 1042 C ATOM 1535 CE LYS A 191 -13.906 -31.450 44.806 1.00 47.84 C ANISOU 1535 CE LYS A 191 6078 5474 6625 -636 850 1158 C ATOM 1536 NZ LYS A 191 -13.556 -32.665 45.593 1.00 50.66 N ANISOU 1536 NZ LYS A 191 6907 5494 6845 -147 889 1038 N ATOM 1537 N HIS A 192 -14.264 -25.130 45.426 1.00 27.42 N ANISOU 1537 N HIS A 192 3443 4018 2956 -832 612 232 N ATOM 1538 CA HIS A 192 -14.969 -24.189 46.295 1.00 30.63 C ANISOU 1538 CA HIS A 192 3709 4391 3536 -616 901 57 C ATOM 1539 C HIS A 192 -15.365 -22.907 45.596 1.00 30.60 C ANISOU 1539 C HIS A 192 3509 4432 3686 -596 1087 111 C ATOM 1540 O HIS A 192 -16.519 -22.485 45.680 1.00 35.71 O ANISOU 1540 O HIS A 192 3787 5280 4500 -141 1395 -58 O ATOM 1541 CB HIS A 192 -14.133 -23.891 47.537 1.00 33.52 C ANISOU 1541 CB HIS A 192 4447 4767 3521 -382 646 16 C ATOM 1542 CG HIS A 192 -14.888 -23.156 48.619 1.00 41.03 C ANISOU 1542 CG HIS A 192 5811 5183 4593 466 962 -361 C ATOM 1543 ND1 HIS A 192 -15.396 -23.780 49.700 1.00 44.49 N ANISOU 1543 ND1 HIS A 192 6829 5675 4398 442 466 212 N ATOM 1544 CD2 HIS A 192 -15.216 -21.805 48.753 1.00 43.81 C ANISOU 1544 CD2 HIS A 192 6256 5146 5243 614 454 -308 C ATOM 1545 CE1 HIS A 192 -16.014 -22.878 50.487 1.00 48.74 C ANISOU 1545 CE1 HIS A 192 6544 5860 6112 634 941 -130 C ATOM 1546 NE2 HIS A 192 -15.905 -21.671 49.905 1.00 48.05 N ANISOU 1546 NE2 HIS A 192 6617 5584 6054 772 1258 -446 N ATOM 1547 N CYS A 193 -14.420 -22.283 44.891 1.00 27.06 N ANISOU 1547 N CYS A 193 3283 4103 2894 -704 920 -427 N ATOM 1548 CA CYS A 193 -14.629 -20.950 44.302 1.00 29.06 C ANISOU 1548 CA CYS A 193 3198 4236 3606 -574 760 -261 C ATOM 1549 C CYS A 193 -15.315 -20.939 42.935 1.00 27.91 C ANISOU 1549 C CYS A 193 3014 3957 3632 -285 805 95 C ATOM 1550 O CYS A 193 -15.769 -19.891 42.474 1.00 32.52 O ANISOU 1550 O CYS A 193 3509 4690 4157 423 609 439 O ATOM 1551 CB CYS A 193 -13.299 -20.200 44.196 1.00 29.91 C ANISOU 1551 CB CYS A 193 3433 3721 4211 -671 880 -923 C ATOM 1552 SG CYS A 193 -12.447 -20.025 45.776 1.00 34.85 S ANISOU 1552 SG CYS A 193 4294 4576 4371 -832 828 -1385 S ATOM 1553 N GLY A 194 -15.379 -22.090 42.282 1.00 24.68 N ANISOU 1553 N GLY A 194 2299 4153 2923 -781 665 253 N ATOM 1554 CA GLY A 194 -15.962 -22.157 40.947 1.00 25.59 C ANISOU 1554 CA GLY A 194 2605 4186 2929 -459 426 719 C ATOM 1555 C GLY A 194 -14.947 -21.831 39.866 1.00 22.77 C ANISOU 1555 C GLY A 194 2194 3568 2887 -183 221 873 C ATOM 1556 O GLY A 194 -13.753 -22.091 40.029 1.00 20.65 O ANISOU 1556 O GLY A 194 2263 3270 2312 -203 34 528 O ATOM 1557 N GLN A 195 -15.431 -21.231 38.778 1.00 22.98 N ANISOU 1557 N GLN A 195 2735 3622 2371 -212 400 676 N ATOM 1558 CA GLN A 195 -14.693 -21.084 37.523 1.00 20.59 C ANISOU 1558 CA GLN A 195 2210 3100 2513 -152 385 367 C ATOM 1559 C GLN A 195 -14.367 -19.615 37.244 1.00 19.47 C ANISOU 1559 C GLN A 195 2337 2859 2200 171 442 193 C ATOM 1560 O GLN A 195 -15.183 -18.727 37.505 1.00 21.74 O ANISOU 1560 O GLN A 195 2601 3083 2576 327 578 -24 O ATOM 1561 CB GLN A 195 -15.543 -21.656 36.381 1.00 23.77 C ANISOU 1561 CB GLN A 195 3255 3121 2653 -404 308 1 C ATOM 1562 CG GLN A 195 -14.833 -21.775 35.044 1.00 24.51 C ANISOU 1562 CG GLN A 195 3030 3354 2926 -128 399 8 C ATOM 1563 CD GLN A 195 -15.721 -22.310 33.935 1.00 25.14 C ANISOU 1563 CD GLN A 195 3141 3155 3253 -180 53 354 C ATOM 1564 OE1 GLN A 195 -16.045 -23.501 33.892 1.00 26.29 O ANISOU 1564 OE1 GLN A 195 2503 3292 4193 -467 -134 319 O ATOM 1565 NE2 GLN A 195 -16.098 -21.430 33.008 1.00 28.36 N ANISOU 1565 NE2 GLN A 195 3104 4211 3459 156 -766 456 N ATOM 1566 N LYS A 196 -13.170 -19.373 36.714 1.00 18.57 N ANISOU 1566 N LYS A 196 2220 2994 1842 -8 231 -70 N ATOM 1567 CA LYS A 196 -12.759 -18.051 36.232 1.00 19.32 C ANISOU 1567 CA LYS A 196 2396 2770 2172 13 328 -417 C ATOM 1568 C LYS A 196 -12.108 -18.239 34.861 1.00 17.42 C ANISOU 1568 C LYS A 196 2045 2682 1891 245 -75 -352 C ATOM 1569 O LYS A 196 -11.411 -19.224 34.648 1.00 21.78 O ANISOU 1569 O LYS A 196 2891 3123 2261 869 288 0 O ATOM 1570 CB LYS A 196 -11.772 -17.404 37.215 1.00 22.81 C ANISOU 1570 CB LYS A 196 2795 3195 2675 -209 122 -657 C ATOM 1571 CG LYS A 196 -12.356 -17.171 38.602 1.00 26.16 C ANISOU 1571 CG LYS A 196 3246 3847 2844 -78 304 -718 C ATOM 1572 CD LYS A 196 -11.275 -16.972 39.654 1.00 28.53 C ANISOU 1572 CD LYS A 196 3554 4012 3273 230 -128 -941 C ATOM 1573 CE LYS A 196 -11.873 -16.892 41.054 1.00 31.63 C ANISOU 1573 CE LYS A 196 3759 5071 3186 88 -175 -901 C ATOM 1574 NZ LYS A 196 -10.831 -16.815 42.120 1.00 32.69 N ANISOU 1574 NZ LYS A 196 3187 5332 3902 -485 -199 -692 N ATOM 1575 N THR A 197 -12.338 -17.309 33.938 1.00 17.24 N ANISOU 1575 N THR A 197 1896 2430 2222 162 498 -127 N ATOM 1576 CA THR A 197 -11.812 -17.411 32.572 1.00 16.70 C ANISOU 1576 CA THR A 197 2048 2208 2088 174 273 -34 C ATOM 1577 C THR A 197 -11.041 -16.149 32.213 1.00 16.98 C ANISOU 1577 C THR A 197 2169 2071 2209 212 497 -118 C ATOM 1578 O THR A 197 -11.459 -15.045 32.580 1.00 19.05 O ANISOU 1578 O THR A 197 2472 2118 2648 273 712 -137 O ATOM 1579 CB THR A 197 -12.958 -17.569 31.556 1.00 18.10 C ANISOU 1579 CB THR A 197 2354 2249 2273 -168 87 -49 C ATOM 1580 OG1 THR A 197 -13.785 -18.671 31.948 1.00 19.77 O ANISOU 1580 OG1 THR A 197 2157 2419 2935 -253 192 -151 O ATOM 1581 CG2 THR A 197 -12.419 -17.806 30.147 1.00 17.91 C ANISOU 1581 CG2 THR A 197 2283 2185 2337 -51 107 -49 C ATOM 1582 N THR A 198 -9.920 -16.309 31.505 1.00 14.92 N ANISOU 1582 N THR A 198 1853 1925 1890 -165 221 -16 N ATOM 1583 CA THR A 198 -9.207 -15.165 30.935 1.00 15.41 C ANISOU 1583 CA THR A 198 2101 1888 1865 -165 167 -5 C ATOM 1584 C THR A 198 -8.790 -15.438 29.502 1.00 14.57 C ANISOU 1584 C THR A 198 1887 1698 1948 -21 148 -163 C ATOM 1585 O THR A 198 -8.684 -16.596 29.077 1.00 13.72 O ANISOU 1585 O THR A 198 1729 1610 1874 30 90 -71 O ATOM 1586 CB THR A 198 -7.943 -14.797 31.731 1.00 17.51 C ANISOU 1586 CB THR A 198 2274 2345 2033 -305 72 -378 C ATOM 1587 OG1 THR A 198 -7.060 -15.922 31.763 1.00 18.69 O ANISOU 1587 OG1 THR A 198 2238 2897 1964 29 -141 -180 O ATOM 1588 CG2 THR A 198 -8.283 -14.375 33.152 1.00 19.45 C ANISOU 1588 CG2 THR A 198 2737 2508 2145 -138 -30 -691 C ATOM 1589 N THR A 199 -8.554 -14.357 28.769 1.00 14.74 N ANISOU 1589 N THR A 199 1786 1707 2105 169 198 -78 N ATOM 1590 CA THR A 199 -8.137 -14.416 27.385 1.00 14.68 C ANISOU 1590 CA THR A 199 1753 1821 2004 53 42 -46 C ATOM 1591 C THR A 199 -6.842 -13.630 27.221 1.00 14.55 C ANISOU 1591 C THR A 199 1873 1539 2115 45 295 -158 C ATOM 1592 O THR A 199 -6.749 -12.463 27.634 1.00 17.11 O ANISOU 1592 O THR A 199 2308 1600 2592 74 606 -312 O ATOM 1593 CB THR A 199 -9.225 -13.859 26.449 1.00 15.58 C ANISOU 1593 CB THR A 199 1956 1910 2053 238 102 71 C ATOM 1594 OG1 THR A 199 -10.413 -14.640 26.610 1.00 17.66 O ANISOU 1594 OG1 THR A 199 1932 2393 2383 59 -142 217 O ATOM 1595 CG2 THR A 199 -8.772 -13.937 24.996 1.00 16.84 C ANISOU 1595 CG2 THR A 199 2582 1907 1907 183 14 232 C ATOM 1596 N LEU A 200 -5.853 -14.288 26.614 1.00 13.59 N ANISOU 1596 N LEU A 200 1696 1623 1843 30 238 75 N ATOM 1597 CA LEU A 200 -4.547 -13.703 26.358 1.00 13.38 C ANISOU 1597 CA LEU A 200 1684 1453 1945 9 96 -30 C ATOM 1598 C LEU A 200 -4.355 -13.558 24.866 1.00 13.34 C ANISOU 1598 C LEU A 200 1605 1515 1947 117 44 134 C ATOM 1599 O LEU A 200 -4.890 -14.346 24.078 1.00 13.58 O ANISOU 1599 O LEU A 200 1744 1408 2005 121 13 119 O ATOM 1600 CB LEU A 200 -3.433 -14.578 26.942 1.00 14.94 C ANISOU 1600 CB LEU A 200 1941 1869 1867 63 -112 170 C ATOM 1601 CG LEU A 200 -3.501 -14.859 28.449 1.00 16.23 C ANISOU 1601 CG LEU A 200 2481 1915 1769 184 125 -78 C ATOM 1602 CD1 LEU A 200 -2.326 -15.707 28.912 1.00 18.00 C ANISOU 1602 CD1 LEU A 200 2728 2176 1933 440 253 36 C ATOM 1603 CD2 LEU A 200 -3.590 -13.565 29.239 1.00 19.77 C ANISOU 1603 CD2 LEU A 200 3154 2501 1854 205 -218 -534 C ATOM 1604 N THR A 201 -3.611 -12.531 24.466 1.00 14.12 N ANISOU 1604 N THR A 201 1706 1621 2038 98 185 207 N ATOM 1605 CA THR A 201 -3.352 -12.311 23.046 1.00 14.12 C ANISOU 1605 CA THR A 201 1708 1691 1966 73 3 238 C ATOM 1606 C THR A 201 -1.871 -12.024 22.823 1.00 13.54 C ANISOU 1606 C THR A 201 1739 1494 1911 39 121 256 C ATOM 1607 O THR A 201 -1.130 -11.746 23.773 1.00 16.34 O ANISOU 1607 O THR A 201 2199 1920 2089 -329 -37 259 O ATOM 1608 CB THR A 201 -4.192 -11.144 22.489 1.00 16.41 C ANISOU 1608 CB THR A 201 1814 1822 2598 287 -109 183 C ATOM 1609 OG1 THR A 201 -3.824 -9.939 23.165 1.00 20.23 O ANISOU 1609 OG1 THR A 201 2750 1599 3337 221 86 119 O ATOM 1610 CG2 THR A 201 -5.691 -11.406 22.690 1.00 16.64 C ANISOU 1610 CG2 THR A 201 1906 1851 2565 441 290 300 C ATOM 1611 N GLY A 202 -1.431 -12.100 21.570 1.00 13.64 N ANISOU 1611 N GLY A 202 1773 1553 1857 132 90 409 N ATOM 1612 CA GLY A 202 -0.050 -11.761 21.235 1.00 14.14 C ANISOU 1612 CA GLY A 202 1582 1771 2019 224 -117 354 C ATOM 1613 C GLY A 202 0.955 -12.736 21.837 1.00 11.93 C ANISOU 1613 C GLY A 202 1514 1418 1600 24 -71 282 C ATOM 1614 O GLY A 202 0.703 -13.940 21.918 1.00 12.18 O ANISOU 1614 O GLY A 202 1681 1436 1511 14 -17 319 O ATOM 1615 N VAL A 203 2.095 -12.212 22.265 1.00 12.75 N ANISOU 1615 N VAL A 203 1411 1681 1752 36 -11 218 N ATOM 1616 CA VAL A 203 3.157 -13.042 22.832 1.00 12.29 C ANISOU 1616 CA VAL A 203 1415 1536 1717 10 -8 186 C ATOM 1617 C VAL A 203 2.652 -13.877 24.019 1.00 10.99 C ANISOU 1617 C VAL A 203 1359 1135 1680 96 25 77 C ATOM 1618 O VAL A 203 2.963 -15.076 24.127 1.00 11.27 O ANISOU 1618 O VAL A 203 1538 1103 1638 76 -6 62 O ATOM 1619 CB VAL A 203 4.378 -12.189 23.238 1.00 14.18 C ANISOU 1619 CB VAL A 203 1361 1687 2337 -137 1 383 C ATOM 1620 CG1 VAL A 203 5.419 -13.035 23.951 1.00 15.64 C ANISOU 1620 CG1 VAL A 203 1691 1940 2310 0 -57 519 C ATOM 1621 CG2 VAL A 203 4.995 -11.532 22.015 1.00 16.76 C ANISOU 1621 CG2 VAL A 203 1837 2121 2411 -192 135 500 C ATOM 1622 N GLU A 204 1.858 -13.265 24.898 1.00 10.99 N ANISOU 1622 N GLU A 204 1353 1382 1439 48 9 144 N ATOM 1623 CA GLU A 204 1.341 -13.992 26.058 1.00 11.16 C ANISOU 1623 CA GLU A 204 1477 1315 1446 -25 20 108 C ATOM 1624 C GLU A 204 0.476 -15.190 25.669 1.00 10.73 C ANISOU 1624 C GLU A 204 1238 1360 1477 25 -6 86 C ATOM 1625 O GLU A 204 0.331 -16.125 26.462 1.00 12.84 O ANISOU 1625 O GLU A 204 1920 1481 1477 -66 -130 165 O ATOM 1626 CB GLU A 204 0.522 -13.073 26.961 1.00 12.44 C ANISOU 1626 CB GLU A 204 1470 1582 1674 37 36 -57 C ATOM 1627 CG GLU A 204 1.352 -12.059 27.723 1.00 13.78 C ANISOU 1627 CG GLU A 204 1937 1567 1732 -82 39 -165 C ATOM 1628 CD GLU A 204 0.518 -11.201 28.660 1.00 15.78 C ANISOU 1628 CD GLU A 204 2155 1835 2003 303 142 -81 C ATOM 1629 OE1 GLU A 204 1.117 -10.497 29.493 1.00 17.42 O ANISOU 1629 OE1 GLU A 204 2419 1726 2472 314 -78 -201 O ATOM 1630 OE2 GLU A 204 -0.734 -11.218 28.570 1.00 18.48 O ANISOU 1630 OE2 GLU A 204 2188 2306 2526 460 48 -543 O ATOM 1631 N ALA A 205 -0.109 -15.165 24.472 1.00 10.12 N ANISOU 1631 N ALA A 205 1215 1069 1561 19 -53 83 N ATOM 1632 CA ALA A 205 -0.932 -16.286 24.036 1.00 10.17 C ANISOU 1632 CA ALA A 205 1310 1241 1313 -68 -152 90 C ATOM 1633 C ALA A 205 -0.128 -17.527 23.645 1.00 10.61 C ANISOU 1633 C ALA A 205 1231 1335 1465 -19 -114 144 C ATOM 1634 O ALA A 205 -0.706 -18.597 23.574 1.00 12.13 O ANISOU 1634 O ALA A 205 1403 1283 1922 -53 -142 1 O ATOM 1635 CB ALA A 205 -1.858 -15.876 22.900 1.00 12.12 C ANISOU 1635 CB ALA A 205 1448 1634 1523 0 -253 288 C ATOM 1636 N VAL A 206 1.178 -17.391 23.389 1.00 9.99 N ANISOU 1636 N VAL A 206 1224 1354 1218 170 -74 -9 N ATOM 1637 CA VAL A 206 1.977 -18.520 22.900 1.00 10.51 C ANISOU 1637 CA VAL A 206 1434 1420 1140 191 -50 -89 C ATOM 1638 C VAL A 206 3.072 -18.993 23.856 1.00 10.82 C ANISOU 1638 C VAL A 206 1400 1246 1463 54 -203 -131 C ATOM 1639 O VAL A 206 3.789 -19.914 23.525 1.00 12.69 O ANISOU 1639 O VAL A 206 1827 1412 1581 293 -224 -221 O ATOM 1640 CB VAL A 206 2.575 -18.239 21.498 1.00 10.38 C ANISOU 1640 CB VAL A 206 1385 1416 1142 76 -97 -12 C ATOM 1641 CG1 VAL A 206 1.483 -17.880 20.493 1.00 11.94 C ANISOU 1641 CG1 VAL A 206 1607 1587 1340 71 -231 253 C ATOM 1642 CG2 VAL A 206 3.670 -17.176 21.557 1.00 12.06 C ANISOU 1642 CG2 VAL A 206 1754 1493 1332 -156 -22 -54 C ATOM 1643 N MET A 207 3.159 -18.365 25.035 1.00 10.53 N ANISOU 1643 N MET A 207 1301 1359 1340 3 -142 -86 N ATOM 1644 CA AMET A 207 4.192 -18.689 26.020 0.50 10.86 C ANISOU 1644 CA AMET A 207 1382 1406 1337 138 -106 -24 C ATOM 1645 CA BMET A 207 4.195 -18.640 26.041 0.50 9.86 C ANISOU 1645 CA BMET A 207 1176 1186 1381 83 -74 -111 C ATOM 1646 C MET A 207 3.585 -19.208 27.321 1.00 9.40 C ANISOU 1646 C MET A 207 1207 1190 1174 182 -150 -187 C ATOM 1647 O MET A 207 2.467 -18.832 27.699 1.00 10.99 O ANISOU 1647 O MET A 207 1234 1573 1367 237 -61 -87 O ATOM 1648 CB AMET A 207 5.068 -17.458 26.291 0.50 12.30 C ANISOU 1648 CB AMET A 207 1556 1429 1686 66 -103 -53 C ATOM 1649 CB BMET A 207 4.928 -17.340 26.400 0.50 9.35 C ANISOU 1649 CB BMET A 207 1062 1097 1392 127 46 -94 C ATOM 1650 CG AMET A 207 5.664 -16.850 25.026 0.50 15.87 C ANISOU 1650 CG AMET A 207 2322 1925 1782 305 121 215 C ATOM 1651 CG BMET A 207 5.718 -16.705 25.264 0.50 9.93 C ANISOU 1651 CG BMET A 207 1067 1088 1618 143 206 -59 C ATOM 1652 SD AMET A 207 7.119 -15.819 25.286 0.50 23.57 S ANISOU 1652 SD AMET A 207 2856 2674 3425 71 -202 16 S ATOM 1653 SD BMET A 207 6.992 -17.799 24.599 0.50 8.89 S ANISOU 1653 SD BMET A 207 848 915 1612 133 39 73 S ATOM 1654 CE AMET A 207 8.411 -17.052 25.434 0.50 15.08 C ANISOU 1654 CE AMET A 207 2208 1551 1969 -615 35 115 C ATOM 1655 CE BMET A 207 8.102 -16.621 23.853 0.50 13.76 C ANISOU 1655 CE BMET A 207 1570 1598 2060 -158 405 393 C ATOM 1656 N TYR A 208 4.308 -20.095 28.000 1.00 10.16 N ANISOU 1656 N TYR A 208 1391 1231 1236 117 -70 17 N ATOM 1657 CA TYR A 208 3.854 -20.577 29.298 1.00 9.93 C ANISOU 1657 CA TYR A 208 1357 1300 1113 138 -111 -81 C ATOM 1658 C TYR A 208 5.056 -21.020 30.108 1.00 10.11 C ANISOU 1658 C TYR A 208 1245 1272 1323 87 -144 -110 C ATOM 1659 O TYR A 208 5.945 -21.679 29.577 1.00 11.31 O ANISOU 1659 O TYR A 208 1493 1466 1338 273 -74 -104 O ATOM 1660 CB TYR A 208 2.873 -21.757 29.154 1.00 10.69 C ANISOU 1660 CB TYR A 208 1440 1401 1217 -17 -69 89 C ATOM 1661 CG TYR A 208 2.199 -22.135 30.465 1.00 10.26 C ANISOU 1661 CG TYR A 208 1346 1321 1228 116 -31 69 C ATOM 1662 CD1 TYR A 208 0.980 -21.555 30.839 1.00 11.19 C ANISOU 1662 CD1 TYR A 208 1335 1412 1502 39 130 -15 C ATOM 1663 CD2 TYR A 208 2.784 -23.062 31.348 1.00 10.88 C ANISOU 1663 CD2 TYR A 208 1427 1458 1246 125 -131 80 C ATOM 1664 CE1 TYR A 208 0.360 -21.880 32.050 1.00 11.19 C ANISOU 1664 CE1 TYR A 208 1431 1423 1398 -1 39 5 C ATOM 1665 CE2 TYR A 208 2.174 -23.397 32.557 1.00 11.55 C ANISOU 1665 CE2 TYR A 208 1342 1704 1341 137 21 -65 C ATOM 1666 CZ TYR A 208 0.965 -22.807 32.902 1.00 10.64 C ANISOU 1666 CZ TYR A 208 1325 1478 1238 18 70 -57 C ATOM 1667 OH TYR A 208 0.388 -23.153 34.091 1.00 12.95 O ANISOU 1667 OH TYR A 208 1664 1936 1318 -55 191 0 O ATOM 1668 N MET A 209 5.086 -20.650 31.385 1.00 10.13 N ANISOU 1668 N MET A 209 1212 1405 1231 8 -93 40 N ATOM 1669 CA MET A 209 6.196 -21.033 32.250 1.00 10.71 C ANISOU 1669 CA MET A 209 1224 1340 1504 -7 -195 32 C ATOM 1670 C MET A 209 5.651 -21.851 33.415 1.00 10.90 C ANISOU 1670 C MET A 209 1369 1461 1309 147 -56 -36 C ATOM 1671 O MET A 209 4.974 -21.317 34.290 1.00 12.51 O ANISOU 1671 O MET A 209 1824 1659 1268 370 85 46 O ATOM 1672 CB MET A 209 6.989 -19.799 32.740 1.00 11.62 C ANISOU 1672 CB MET A 209 1554 1469 1390 5 -282 -274 C ATOM 1673 CG MET A 209 8.202 -20.134 33.609 1.00 12.36 C ANISOU 1673 CG MET A 209 1537 1442 1715 132 -285 -254 C ATOM 1674 SD MET A 209 9.342 -21.250 32.738 1.00 12.79 S ANISOU 1674 SD MET A 209 1612 1597 1650 106 -104 -196 S ATOM 1675 CE MET A 209 10.878 -21.025 33.648 1.00 13.31 C ANISOU 1675 CE MET A 209 1561 1627 1869 32 -179 8 C ATOM 1676 N GLY A 210 5.910 -23.157 33.401 1.00 10.74 N ANISOU 1676 N GLY A 210 1442 1368 1271 -86 -77 -14 N ATOM 1677 CA GLY A 210 5.483 -24.018 34.502 1.00 12.16 C ANISOU 1677 CA GLY A 210 1753 1359 1508 67 127 106 C ATOM 1678 C GLY A 210 5.378 -25.491 34.163 1.00 12.11 C ANISOU 1678 C GLY A 210 1755 1452 1394 59 -68 -48 C ATOM 1679 O GLY A 210 5.458 -26.338 35.059 1.00 15.50 O ANISOU 1679 O GLY A 210 2559 1787 1543 92 257 268 O ATOM 1680 N THR A 211 5.174 -25.798 32.886 1.00 11.37 N ANISOU 1680 N THR A 211 1368 1517 1433 -22 -41 -110 N ATOM 1681 CA THR A 211 5.163 -27.178 32.412 1.00 11.08 C ANISOU 1681 CA THR A 211 1343 1480 1386 15 110 0 C ATOM 1682 C THR A 211 5.654 -27.217 30.980 1.00 10.35 C ANISOU 1682 C THR A 211 1306 1318 1309 49 12 51 C ATOM 1683 O THR A 211 5.378 -26.294 30.196 1.00 10.47 O ANISOU 1683 O THR A 211 1407 1317 1254 21 -84 27 O ATOM 1684 CB THR A 211 3.778 -27.873 32.532 1.00 12.02 C ANISOU 1684 CB THR A 211 1383 1444 1738 -4 53 104 C ATOM 1685 OG1 THR A 211 3.904 -29.230 32.089 1.00 12.31 O ANISOU 1685 OG1 THR A 211 1435 1602 1638 80 237 -33 O ATOM 1686 CG2 THR A 211 2.674 -27.155 31.705 1.00 12.95 C ANISOU 1686 CG2 THR A 211 1416 1605 1900 71 4 64 C ATOM 1687 N LEU A 212 6.392 -28.282 30.657 1.00 9.85 N ANISOU 1687 N LEU A 212 1239 1325 1179 29 -7 34 N ATOM 1688 CA LEU A 212 6.837 -28.539 29.289 1.00 10.16 C ANISOU 1688 CA LEU A 212 1212 1392 1254 80 43 -39 C ATOM 1689 C LEU A 212 5.775 -29.172 28.415 1.00 9.88 C ANISOU 1689 C LEU A 212 1253 1118 1383 102 -88 118 C ATOM 1690 O LEU A 212 5.924 -29.181 27.190 1.00 10.89 O ANISOU 1690 O LEU A 212 1369 1372 1397 -14 -77 181 O ATOM 1691 CB LEU A 212 8.031 -29.489 29.296 1.00 10.87 C ANISOU 1691 CB LEU A 212 1196 1340 1592 55 -20 57 C ATOM 1692 CG LEU A 212 9.264 -29.019 30.047 1.00 10.43 C ANISOU 1692 CG LEU A 212 1310 1387 1266 6 -51 151 C ATOM 1693 CD1 LEU A 212 10.318 -30.121 30.065 1.00 11.65 C ANISOU 1693 CD1 LEU A 212 1435 1347 1642 60 120 130 C ATOM 1694 CD2 LEU A 212 9.832 -27.736 29.456 1.00 11.97 C ANISOU 1694 CD2 LEU A 212 1328 1566 1654 -159 93 212 C ATOM 1695 N SER A 213 4.723 -29.702 29.038 1.00 10.36 N ANISOU 1695 N SER A 213 1307 1187 1441 14 -125 83 N ATOM 1696 CA SER A 213 3.755 -30.551 28.360 1.00 11.08 C ANISOU 1696 CA SER A 213 1214 1310 1686 -59 -221 269 C ATOM 1697 C SER A 213 2.534 -29.754 27.898 1.00 10.36 C ANISOU 1697 C SER A 213 1246 1359 1330 67 -120 116 C ATOM 1698 O SER A 213 1.813 -29.160 28.706 1.00 11.59 O ANISOU 1698 O SER A 213 1260 1550 1593 48 30 -3 O ATOM 1699 CB SER A 213 3.339 -31.667 29.315 1.00 12.16 C ANISOU 1699 CB SER A 213 1402 1604 1611 -130 -175 349 C ATOM 1700 OG SER A 213 2.208 -32.366 28.825 1.00 12.89 O ANISOU 1700 OG SER A 213 1283 1540 2072 -131 -150 264 O ATOM 1701 N TYR A 214 2.315 -29.710 26.585 1.00 10.29 N ANISOU 1701 N TYR A 214 1211 1331 1367 -93 -222 177 N ATOM 1702 CA TYR A 214 1.125 -29.066 26.045 1.00 10.65 C ANISOU 1702 CA TYR A 214 1232 1429 1384 10 -150 196 C ATOM 1703 C TYR A 214 -0.106 -29.848 26.503 1.00 10.89 C ANISOU 1703 C TYR A 214 1286 1318 1534 11 -68 105 C ATOM 1704 O TYR A 214 -1.127 -29.256 26.877 1.00 10.65 O ANISOU 1704 O TYR A 214 1220 1500 1327 -31 -2 71 O ATOM 1705 CB TYR A 214 1.217 -28.999 24.518 1.00 10.38 C ANISOU 1705 CB TYR A 214 1215 1344 1385 57 -123 196 C ATOM 1706 CG TYR A 214 0.274 -28.030 23.809 1.00 9.37 C ANISOU 1706 CG TYR A 214 1200 1162 1197 -50 -41 216 C ATOM 1707 CD1 TYR A 214 -0.335 -26.960 24.479 1.00 10.13 C ANISOU 1707 CD1 TYR A 214 1155 1146 1547 1 36 246 C ATOM 1708 CD2 TYR A 214 0.061 -28.149 22.435 1.00 10.15 C ANISOU 1708 CD2 TYR A 214 1378 1298 1177 -221 -36 219 C ATOM 1709 CE1 TYR A 214 -1.156 -26.065 23.794 1.00 10.29 C ANISOU 1709 CE1 TYR A 214 1302 1458 1148 -3 -23 309 C ATOM 1710 CE2 TYR A 214 -0.761 -27.272 21.745 1.00 11.30 C ANISOU 1710 CE2 TYR A 214 1206 1326 1760 -31 14 137 C ATOM 1711 CZ TYR A 214 -1.367 -26.229 22.427 1.00 10.33 C ANISOU 1711 CZ TYR A 214 1292 1417 1215 -21 -8 186 C ATOM 1712 OH TYR A 214 -2.185 -25.341 21.762 1.00 11.12 O ANISOU 1712 OH TYR A 214 1325 1402 1499 -5 -109 202 O ATOM 1713 N ASP A 215 -0.007 -31.180 26.497 1.00 11.44 N ANISOU 1713 N ASP A 215 1303 1291 1751 -207 -82 79 N ATOM 1714 CA ASP A 215 -1.112 -32.007 26.993 1.00 11.82 C ANISOU 1714 CA ASP A 215 1306 1403 1779 -177 -20 173 C ATOM 1715 C ASP A 215 -1.503 -31.630 28.425 1.00 11.81 C ANISOU 1715 C ASP A 215 1265 1564 1658 -119 -143 208 C ATOM 1716 O ASP A 215 -2.692 -31.559 28.743 1.00 12.45 O ANISOU 1716 O ASP A 215 1388 1644 1698 -73 53 224 O ATOM 1717 CB ASP A 215 -0.760 -33.496 26.936 1.00 12.81 C ANISOU 1717 CB ASP A 215 1690 1330 1847 -257 -154 107 C ATOM 1718 CG ASP A 215 -0.848 -34.076 25.539 1.00 14.28 C ANISOU 1718 CG ASP A 215 1587 1907 1929 -431 -154 -23 C ATOM 1719 OD1 ASP A 215 -1.425 -33.418 24.648 1.00 16.07 O ANISOU 1719 OD1 ASP A 215 2258 1983 1864 -661 -252 181 O ATOM 1720 OD2 ASP A 215 -0.338 -35.198 25.349 1.00 17.43 O ANISOU 1720 OD2 ASP A 215 2340 1788 2490 -561 177 -251 O ATOM 1721 N ASN A 216 -0.517 -31.396 29.291 1.00 11.43 N ANISOU 1721 N ASN A 216 1325 1401 1615 8 -150 161 N ATOM 1722 CA ASN A 216 -0.821 -31.004 30.669 1.00 13.22 C ANISOU 1722 CA ASN A 216 1464 1852 1706 80 -36 114 C ATOM 1723 C ASN A 216 -1.612 -29.699 30.745 1.00 11.86 C ANISOU 1723 C ASN A 216 1375 1598 1532 -123 -72 224 C ATOM 1724 O ASN A 216 -2.552 -29.575 31.542 1.00 12.27 O ANISOU 1724 O ASN A 216 1412 1839 1408 -289 -80 227 O ATOM 1725 CB ASN A 216 0.453 -30.909 31.513 1.00 14.87 C ANISOU 1725 CB ASN A 216 1361 2300 1988 179 -83 222 C ATOM 1726 CG ASN A 216 1.004 -32.270 31.901 1.00 18.57 C ANISOU 1726 CG ASN A 216 2123 2491 2442 287 -208 497 C ATOM 1727 OD1 ASN A 216 0.417 -33.325 31.608 1.00 21.75 O ANISOU 1727 OD1 ASN A 216 2553 2762 2949 51 -127 600 O ATOM 1728 ND2 ASN A 216 2.148 -32.255 32.565 1.00 21.45 N ANISOU 1728 ND2 ASN A 216 2448 3476 2223 343 -480 651 N ATOM 1729 N LEU A 217 -1.246 -28.728 29.909 1.00 11.36 N ANISOU 1729 N LEU A 217 1440 1515 1360 -63 -185 160 N ATOM 1730 CA LEU A 217 -1.993 -27.478 29.883 1.00 11.06 C ANISOU 1730 CA LEU A 217 1319 1430 1453 -122 -161 -40 C ATOM 1731 C LEU A 217 -3.434 -27.731 29.412 1.00 11.18 C ANISOU 1731 C LEU A 217 1288 1536 1422 -109 -101 -57 C ATOM 1732 O LEU A 217 -4.373 -27.101 29.903 1.00 11.48 O ANISOU 1732 O LEU A 217 1322 1550 1486 0 -146 -46 O ATOM 1733 CB LEU A 217 -1.301 -26.431 29.004 1.00 12.26 C ANISOU 1733 CB LEU A 217 1452 1446 1760 -43 -85 125 C ATOM 1734 CG LEU A 217 -1.913 -25.020 29.030 1.00 12.39 C ANISOU 1734 CG LEU A 217 1658 1442 1605 2 -78 -82 C ATOM 1735 CD1 LEU A 217 -1.870 -24.399 30.430 1.00 14.98 C ANISOU 1735 CD1 LEU A 217 2255 1742 1694 -103 -274 -242 C ATOM 1736 CD2 LEU A 217 -1.226 -24.116 28.013 1.00 14.27 C ANISOU 1736 CD2 LEU A 217 1421 1735 2265 -102 -227 390 C ATOM 1737 N LYS A 218 -3.601 -28.668 28.476 1.00 10.28 N ANISOU 1737 N LYS A 218 1244 1425 1238 -102 -186 103 N ATOM 1738 CA LYS A 218 -4.925 -29.057 27.990 1.00 10.25 C ANISOU 1738 CA LYS A 218 1257 1387 1250 -194 -67 -53 C ATOM 1739 C LYS A 218 -5.755 -29.825 29.019 1.00 11.08 C ANISOU 1739 C LYS A 218 1308 1588 1312 -73 -42 134 C ATOM 1740 O LYS A 218 -6.966 -29.653 29.080 1.00 12.43 O ANISOU 1740 O LYS A 218 1287 1880 1556 -36 -70 165 O ATOM 1741 CB LYS A 218 -4.790 -29.869 26.698 1.00 10.37 C ANISOU 1741 CB LYS A 218 1387 1268 1282 -187 50 -20 C ATOM 1742 CG LYS A 218 -4.288 -29.052 25.523 1.00 10.38 C ANISOU 1742 CG LYS A 218 1382 1256 1307 -10 7 103 C ATOM 1743 CD LYS A 218 -4.004 -29.950 24.329 1.00 10.40 C ANISOU 1743 CD LYS A 218 1441 1398 1109 -103 -152 120 C ATOM 1744 CE LYS A 218 -3.537 -29.132 23.137 1.00 11.03 C ANISOU 1744 CE LYS A 218 1631 1450 1109 -15 -73 140 C ATOM 1745 NZ LYS A 218 -3.245 -30.042 21.995 1.00 12.44 N ANISOU 1745 NZ LYS A 218 1756 1542 1428 6 93 -45 N ATOM 1746 N THR A 219 -5.118 -30.652 29.842 1.00 10.74 N ANISOU 1746 N THR A 219 1315 1568 1196 -118 51 161 N ATOM 1747 CA THR A 219 -5.875 -31.535 30.726 1.00 11.84 C ANISOU 1747 CA THR A 219 1515 1541 1439 -235 144 112 C ATOM 1748 C THR A 219 -6.006 -31.012 32.145 1.00 12.75 C ANISOU 1748 C THR A 219 1577 1672 1595 -114 86 -143 C ATOM 1749 O THR A 219 -6.881 -31.455 32.892 1.00 16.32 O ANISOU 1749 O THR A 219 2098 2350 1751 -626 283 -346 O ATOM 1750 CB THR A 219 -5.302 -32.964 30.729 1.00 12.50 C ANISOU 1750 CB THR A 219 1701 1449 1598 -276 173 177 C ATOM 1751 OG1 THR A 219 -3.967 -32.958 31.230 1.00 15.00 O ANISOU 1751 OG1 THR A 219 1868 1710 2119 -128 -72 135 O ATOM 1752 CG2 THR A 219 -5.299 -33.524 29.322 1.00 14.68 C ANISOU 1752 CG2 THR A 219 1971 1887 1717 -345 319 -61 C ATOM 1753 N GLY A 220 -5.137 -30.074 32.514 1.00 12.69 N ANISOU 1753 N GLY A 220 1785 1636 1400 -167 -164 71 N ATOM 1754 CA GLY A 220 -5.202 -29.443 33.823 1.00 14.02 C ANISOU 1754 CA GLY A 220 1746 2098 1481 -261 -8 -122 C ATOM 1755 C GLY A 220 -3.865 -29.351 34.534 1.00 12.46 C ANISOU 1755 C GLY A 220 1795 1782 1155 -66 -40 84 C ATOM 1756 O GLY A 220 -3.179 -30.355 34.732 1.00 16.18 O ANISOU 1756 O GLY A 220 2577 1875 1695 130 -196 158 O ATOM 1757 N VAL A 221 -3.505 -28.123 34.906 1.00 13.47 N ANISOU 1757 N VAL A 221 1921 1853 1344 -193 -242 29 N ATOM 1758 CA VAL A 221 -2.317 -27.827 35.706 1.00 15.17 C ANISOU 1758 CA VAL A 221 2015 2150 1598 -81 -350 -175 C ATOM 1759 C VAL A 221 -2.808 -27.430 37.103 1.00 14.90 C ANISOU 1759 C VAL A 221 1915 2089 1654 51 -335 -184 C ATOM 1760 O VAL A 221 -3.701 -26.586 37.237 1.00 14.13 O ANISOU 1760 O VAL A 221 1891 2286 1188 164 -158 -27 O ATOM 1761 CB VAL A 221 -1.495 -26.663 35.066 1.00 15.95 C ANISOU 1761 CB VAL A 221 2033 2412 1613 -290 -282 -157 C ATOM 1762 CG1 VAL A 221 -0.327 -26.236 35.957 1.00 17.34 C ANISOU 1762 CG1 VAL A 221 2012 2568 2008 -148 -549 16 C ATOM 1763 CG2 VAL A 221 -0.998 -27.054 33.680 1.00 18.74 C ANISOU 1763 CG2 VAL A 221 2727 2678 1714 -148 47 96 C ATOM 1764 N SER A 222 -2.248 -28.046 38.142 1.00 16.13 N ANISOU 1764 N SER A 222 2414 2073 1640 12 -364 -143 N ATOM 1765 CA SER A 222 -2.603 -27.673 39.507 1.00 15.84 C ANISOU 1765 CA SER A 222 2456 1898 1661 266 -290 23 C ATOM 1766 C SER A 222 -1.948 -26.341 39.857 1.00 15.47 C ANISOU 1766 C SER A 222 2153 2122 1602 135 -340 12 C ATOM 1767 O SER A 222 -0.737 -26.200 39.738 1.00 17.80 O ANISOU 1767 O SER A 222 2138 2515 2110 218 -426 -260 O ATOM 1768 CB SER A 222 -2.158 -28.755 40.493 1.00 18.15 C ANISOU 1768 CB SER A 222 2885 2213 1797 177 -374 339 C ATOM 1769 OG SER A 222 -2.403 -28.346 41.829 1.00 23.40 O ANISOU 1769 OG SER A 222 3539 3352 1998 152 -101 90 O ATOM 1770 N ILE A 223 -2.757 -25.364 40.266 1.00 15.41 N ANISOU 1770 N ILE A 223 2292 1824 1737 0 -354 -85 N ATOM 1771 CA ILE A 223 -2.249 -24.041 40.666 1.00 14.93 C ANISOU 1771 CA ILE A 223 2219 1750 1702 15 -215 -6 C ATOM 1772 C ILE A 223 -2.900 -23.601 41.981 1.00 16.40 C ANISOU 1772 C ILE A 223 2268 2346 1616 80 -306 -36 C ATOM 1773 O ILE A 223 -4.022 -24.011 42.271 1.00 17.02 O ANISOU 1773 O ILE A 223 2462 2190 1812 -22 -126 -47 O ATOM 1774 CB ILE A 223 -2.431 -22.962 39.556 1.00 14.39 C ANISOU 1774 CB ILE A 223 2006 2056 1403 7 -170 2 C ATOM 1775 CG1 ILE A 223 -3.904 -22.571 39.361 1.00 15.16 C ANISOU 1775 CG1 ILE A 223 2109 1956 1694 111 -201 102 C ATOM 1776 CG2 ILE A 223 -1.785 -23.410 38.247 1.00 15.88 C ANISOU 1776 CG2 ILE A 223 2373 2095 1563 -113 80 -138 C ATOM 1777 CD1 ILE A 223 -4.110 -21.366 38.463 1.00 16.38 C ANISOU 1777 CD1 ILE A 223 2592 1667 1962 -119 -406 63 C ATOM 1778 N PRO A 224 -2.198 -22.778 42.788 1.00 16.46 N ANISOU 1778 N PRO A 224 2433 2036 1784 125 -192 -154 N ATOM 1779 CA PRO A 224 -2.820 -22.346 44.043 1.00 16.93 C ANISOU 1779 CA PRO A 224 2430 2134 1869 176 -98 -132 C ATOM 1780 C PRO A 224 -4.049 -21.468 43.794 1.00 17.04 C ANISOU 1780 C PRO A 224 2661 2075 1738 274 -103 218 C ATOM 1781 O PRO A 224 -4.060 -20.659 42.859 1.00 18.45 O ANISOU 1781 O PRO A 224 3185 2203 1620 467 276 229 O ATOM 1782 CB PRO A 224 -1.728 -21.517 44.729 1.00 19.74 C ANISOU 1782 CB PRO A 224 2943 2329 2228 34 -312 -429 C ATOM 1783 CG PRO A 224 -0.453 -21.899 44.077 1.00 20.45 C ANISOU 1783 CG PRO A 224 3045 2619 2105 -147 -253 -744 C ATOM 1784 CD PRO A 224 -0.786 -22.359 42.688 1.00 16.94 C ANISOU 1784 CD PRO A 224 2500 2150 1783 -36 -138 -294 C ATOM 1785 N CYS A 225 -5.080 -21.641 44.609 1.00 18.37 N ANISOU 1785 N CYS A 225 2829 2399 1749 104 35 -325 N ATOM 1786 CA CYS A 225 -6.216 -20.733 44.585 1.00 18.94 C ANISOU 1786 CA CYS A 225 2599 2753 1843 88 78 -192 C ATOM 1787 C CYS A 225 -6.109 -19.751 45.746 1.00 21.73 C ANISOU 1787 C CYS A 225 3066 2938 2251 140 -431 -417 C ATOM 1788 O CYS A 225 -5.559 -20.086 46.795 1.00 22.35 O ANISOU 1788 O CYS A 225 3537 3132 1822 402 -25 -245 O ATOM 1789 CB CYS A 225 -7.529 -21.515 44.670 1.00 22.77 C ANISOU 1789 CB CYS A 225 3023 3139 2486 -359 152 -308 C ATOM 1790 SG CYS A 225 -8.991 -20.465 44.529 1.00 22.23 S ANISOU 1790 SG CYS A 225 2886 3486 2074 -451 32 -205 S ATOM 1791 N VAL A 226 -6.634 -18.542 45.551 1.00 20.56 N ANISOU 1791 N VAL A 226 2630 2759 2420 36 -257 -471 N ATOM 1792 CA VAL A 226 -6.633 -17.525 46.615 1.00 21.67 C ANISOU 1792 CA VAL A 226 2955 2609 2666 94 -214 -502 C ATOM 1793 C VAL A 226 -7.356 -17.964 47.893 1.00 23.76 C ANISOU 1793 C VAL A 226 3155 3262 2609 -263 -242 -595 C ATOM 1794 O VAL A 226 -7.110 -17.410 48.968 1.00 26.45 O ANISOU 1794 O VAL A 226 3728 3689 2631 -491 -129 -855 O ATOM 1795 CB VAL A 226 -7.179 -16.149 46.142 1.00 21.50 C ANISOU 1795 CB VAL A 226 2459 2639 3068 3 -364 -412 C ATOM 1796 CG1 VAL A 226 -6.273 -15.540 45.078 1.00 22.37 C ANISOU 1796 CG1 VAL A 226 2466 2790 3242 140 -400 -14 C ATOM 1797 CG2 VAL A 226 -8.616 -16.265 45.643 1.00 23.90 C ANISOU 1797 CG2 VAL A 226 2459 3265 3357 -209 -440 -157 C ATOM 1798 N CYS A 227 -8.225 -18.968 47.785 1.00 22.81 N ANISOU 1798 N CYS A 227 3447 3199 2021 -421 187 -404 N ATOM 1799 CA CYS A 227 -8.913 -19.510 48.965 1.00 26.54 C ANISOU 1799 CA CYS A 227 3906 3786 2391 -776 567 -366 C ATOM 1800 C CYS A 227 -7.996 -20.378 49.835 1.00 28.90 C ANISOU 1800 C CYS A 227 4440 3940 2598 -476 449 -368 C ATOM 1801 O CYS A 227 -8.364 -20.737 50.954 1.00 31.94 O ANISOU 1801 O CYS A 227 5539 4291 2304 -552 772 -763 O ATOM 1802 CB CYS A 227 -10.175 -20.289 48.570 1.00 27.85 C ANISOU 1802 CB CYS A 227 4102 4069 2409 -977 699 -811 C ATOM 1803 SG CYS A 227 -9.879 -21.864 47.721 1.00 30.62 S ANISOU 1803 SG CYS A 227 5350 4063 2218 -1182 1117 -641 S ATOM 1804 N GLY A 228 -6.811 -20.706 49.322 1.00 28.58 N ANISOU 1804 N GLY A 228 4714 3742 2402 -114 388 -316 N ATOM 1805 CA GLY A 228 -5.830 -21.511 50.062 1.00 30.13 C ANISOU 1805 CA GLY A 228 5512 3391 2542 213 206 -383 C ATOM 1806 C GLY A 228 -5.804 -22.978 49.661 1.00 31.66 C ANISOU 1806 C GLY A 228 5731 3321 2976 519 178 -215 C ATOM 1807 O GLY A 228 -4.963 -23.745 50.141 1.00 34.35 O ANISOU 1807 O GLY A 228 5979 3852 3219 701 352 511 O ATOM 1808 N ARG A 229 -6.738 -23.365 48.794 1.00 32.24 N ANISOU 1808 N ARG A 229 5808 3557 2884 8 311 183 N ATOM 1809 CA ARG A 229 -6.783 -24.705 48.206 1.00 30.33 C ANISOU 1809 CA ARG A 229 5498 3540 2486 -83 410 226 C ATOM 1810 C ARG A 229 -6.055 -24.699 46.853 1.00 28.29 C ANISOU 1810 C ARG A 229 4953 3238 2556 -76 310 297 C ATOM 1811 O ARG A 229 -5.553 -23.661 46.414 1.00 26.82 O ANISOU 1811 O ARG A 229 4624 3122 2441 54 -68 377 O ATOM 1812 CB ARG A 229 -8.246 -25.147 48.040 1.00 34.49 C ANISOU 1812 CB ARG A 229 5422 4231 3449 -302 1008 336 C ATOM 1813 CG ARG A 229 -8.474 -26.555 47.500 1.00 40.74 C ANISOU 1813 CG ARG A 229 6458 4525 4496 -36 410 -151 C ATOM 1814 CD ARG A 229 -8.079 -27.632 48.499 1.00 48.78 C ANISOU 1814 CD ARG A 229 7502 4780 6249 -277 288 821 C ATOM 1815 NE ARG A 229 -8.004 -28.953 47.874 1.00 55.84 N ANISOU 1815 NE ARG A 229 7336 6099 7779 -57 342 -858 N ATOM 1816 CZ ARG A 229 -6.887 -29.509 47.410 1.00 57.34 C ANISOU 1816 CZ ARG A 229 6508 6557 8721 -265 118 -485 C ATOM 1817 NH1 ARG A 229 -5.729 -28.867 47.497 1.00 59.33 N ANISOU 1817 NH1 ARG A 229 7267 6966 8309 -1004 -317 -548 N ATOM 1818 NH2 ARG A 229 -6.928 -30.715 46.859 1.00 64.39 N ANISOU 1818 NH2 ARG A 229 8178 6693 9594 -464 -285 -828 N ATOM 1819 N ASP A 230 -5.975 -25.863 46.213 1.00 24.41 N ANISOU 1819 N ASP A 230 4426 3366 1483 -268 -433 386 N ATOM 1820 CA ASP A 230 -5.461 -25.954 44.852 1.00 23.99 C ANISOU 1820 CA ASP A 230 3625 3617 1873 -96 -187 154 C ATOM 1821 C ASP A 230 -6.611 -25.943 43.863 1.00 21.26 C ANISOU 1821 C ASP A 230 3245 2883 1949 -384 8 566 C ATOM 1822 O ASP A 230 -7.675 -26.513 44.115 1.00 24.63 O ANISOU 1822 O ASP A 230 3466 3322 2568 -699 -55 614 O ATOM 1823 CB ASP A 230 -4.618 -27.217 44.661 1.00 26.98 C ANISOU 1823 CB ASP A 230 3905 3588 2756 -19 -433 113 C ATOM 1824 CG ASP A 230 -3.314 -27.175 45.443 1.00 30.04 C ANISOU 1824 CG ASP A 230 4300 4365 2748 90 -775 -247 C ATOM 1825 OD1 ASP A 230 -2.610 -26.136 45.417 1.00 30.58 O ANISOU 1825 OD1 ASP A 230 4443 4300 2876 253 -463 -122 O ATOM 1826 OD2 ASP A 230 -2.988 -28.197 46.076 1.00 35.38 O ANISOU 1826 OD2 ASP A 230 5299 4508 3634 -161 -877 221 O ATOM 1827 N ALA A 231 -6.381 -25.272 42.742 1.00 18.80 N ANISOU 1827 N ALA A 231 2794 2777 1572 -209 -38 284 N ATOM 1828 CA ALA A 231 -7.326 -25.232 41.645 1.00 17.37 C ANISOU 1828 CA ALA A 231 2627 2436 1534 -165 53 -1 C ATOM 1829 C ALA A 231 -6.698 -25.884 40.412 1.00 15.55 C ANISOU 1829 C ALA A 231 2185 2173 1549 -245 218 291 C ATOM 1830 O ALA A 231 -5.527 -26.265 40.428 1.00 17.58 O ANISOU 1830 O ALA A 231 2175 2515 1987 -311 42 -190 O ATOM 1831 CB ALA A 231 -7.724 -23.795 41.357 1.00 18.05 C ANISOU 1831 CB ALA A 231 2440 2615 1803 39 -90 168 C ATOM 1832 N THR A 232 -7.493 -26.025 39.358 1.00 15.49 N ANISOU 1832 N THR A 232 2193 2130 1560 -183 186 167 N ATOM 1833 CA THR A 232 -7.019 -26.589 38.104 1.00 14.48 C ANISOU 1833 CA THR A 232 2077 1920 1503 -196 -109 -10 C ATOM 1834 C THR A 232 -7.163 -25.584 36.972 1.00 14.19 C ANISOU 1834 C THR A 232 1874 1849 1669 -249 88 52 C ATOM 1835 O THR A 232 -8.255 -25.093 36.703 1.00 14.59 O ANISOU 1835 O THR A 232 1849 2151 1542 -218 120 23 O ATOM 1836 CB THR A 232 -7.768 -27.901 37.754 1.00 16.55 C ANISOU 1836 CB THR A 232 2547 1944 1795 -407 128 -52 C ATOM 1837 OG1 THR A 232 -7.672 -28.815 38.852 1.00 21.79 O ANISOU 1837 OG1 THR A 232 3482 2556 2240 -484 220 399 O ATOM 1838 CG2 THR A 232 -7.186 -28.557 36.503 1.00 16.09 C ANISOU 1838 CG2 THR A 232 2551 1743 1819 -338 213 75 C ATOM 1839 N GLN A 233 -6.043 -25.308 36.313 1.00 13.33 N ANISOU 1839 N GLN A 233 1718 1823 1525 -252 -80 163 N ATOM 1840 CA GLN A 233 -5.992 -24.427 35.159 1.00 12.00 C ANISOU 1840 CA GLN A 233 1417 1729 1410 -268 -32 42 C ATOM 1841 C GLN A 233 -5.943 -25.267 33.888 1.00 12.44 C ANISOU 1841 C GLN A 233 1584 1711 1430 -134 -119 57 C ATOM 1842 O GLN A 233 -5.136 -26.190 33.784 1.00 13.65 O ANISOU 1842 O GLN A 233 1720 1775 1689 -1 -135 -2 O ATOM 1843 CB GLN A 233 -4.742 -23.552 35.254 1.00 12.70 C ANISOU 1843 CB GLN A 233 1424 1892 1506 -356 58 240 C ATOM 1844 CG GLN A 233 -4.544 -22.590 34.099 1.00 12.63 C ANISOU 1844 CG GLN A 233 1461 1910 1426 -221 20 222 C ATOM 1845 CD GLN A 233 -3.173 -21.978 34.157 1.00 12.32 C ANISOU 1845 CD GLN A 233 1399 1769 1513 -110 8 27 C ATOM 1846 OE1 GLN A 233 -2.173 -22.695 34.208 1.00 14.20 O ANISOU 1846 OE1 GLN A 233 1624 1801 1969 29 25 61 O ATOM 1847 NE2 GLN A 233 -3.111 -20.650 34.185 1.00 12.87 N ANISOU 1847 NE2 GLN A 233 1490 1758 1642 -140 107 -117 N ATOM 1848 N TYR A 234 -6.782 -24.942 32.908 1.00 11.83 N ANISOU 1848 N TYR A 234 1369 1806 1316 -147 -46 -86 N ATOM 1849 CA TYR A 234 -6.731 -25.676 31.644 1.00 11.69 C ANISOU 1849 CA TYR A 234 1603 1522 1314 -244 -19 -24 C ATOM 1850 C TYR A 234 -7.024 -24.798 30.430 1.00 11.43 C ANISOU 1850 C TYR A 234 1460 1523 1359 -24 -18 -10 C ATOM 1851 O TYR A 234 -7.664 -23.748 30.524 1.00 11.79 O ANISOU 1851 O TYR A 234 1578 1529 1370 -19 38 -195 O ATOM 1852 CB TYR A 234 -7.626 -26.937 31.657 1.00 11.83 C ANISOU 1852 CB TYR A 234 1454 1729 1309 -335 -14 98 C ATOM 1853 CG TYR A 234 -9.114 -26.666 31.666 1.00 12.10 C ANISOU 1853 CG TYR A 234 1478 1626 1491 -347 -10 -74 C ATOM 1854 CD1 TYR A 234 -9.805 -26.571 32.868 1.00 14.73 C ANISOU 1854 CD1 TYR A 234 1642 2260 1692 -319 222 -83 C ATOM 1855 CD2 TYR A 234 -9.823 -26.493 30.479 1.00 12.68 C ANISOU 1855 CD2 TYR A 234 1430 1689 1699 -420 -137 67 C ATOM 1856 CE1 TYR A 234 -11.167 -26.333 32.893 1.00 16.02 C ANISOU 1856 CE1 TYR A 234 1676 2530 1879 -173 8 -406 C ATOM 1857 CE2 TYR A 234 -11.190 -26.247 30.493 1.00 14.26 C ANISOU 1857 CE2 TYR A 234 1499 1868 2049 -234 83 -225 C ATOM 1858 CZ TYR A 234 -11.855 -26.171 31.705 1.00 14.67 C ANISOU 1858 CZ TYR A 234 1567 2000 2005 -162 21 -220 C ATOM 1859 OH TYR A 234 -13.210 -25.924 31.751 1.00 17.86 O ANISOU 1859 OH TYR A 234 1508 2284 2994 -290 -123 -609 O ATOM 1860 N LEU A 235 -6.528 -25.248 29.285 1.00 10.90 N ANISOU 1860 N LEU A 235 1311 1520 1309 -168 -19 28 N ATOM 1861 CA LEU A 235 -6.674 -24.526 28.032 1.00 10.71 C ANISOU 1861 CA LEU A 235 1135 1527 1408 -94 19 115 C ATOM 1862 C LEU A 235 -8.063 -24.738 27.407 1.00 11.13 C ANISOU 1862 C LEU A 235 1274 1371 1583 -151 -120 0 C ATOM 1863 O LEU A 235 -8.445 -25.854 27.083 1.00 11.86 O ANISOU 1863 O LEU A 235 1587 1326 1593 -38 -140 -130 O ATOM 1864 CB LEU A 235 -5.585 -25.012 27.076 1.00 10.78 C ANISOU 1864 CB LEU A 235 1342 1526 1226 -43 3 25 C ATOM 1865 CG LEU A 235 -5.475 -24.313 25.725 1.00 10.53 C ANISOU 1865 CG LEU A 235 1520 1318 1162 -120 13 -57 C ATOM 1866 CD1 LEU A 235 -5.135 -22.847 25.923 1.00 11.69 C ANISOU 1866 CD1 LEU A 235 1570 1370 1500 -270 -52 50 C ATOM 1867 CD2 LEU A 235 -4.409 -24.989 24.876 1.00 12.19 C ANISOU 1867 CD2 LEU A 235 1588 1593 1450 96 190 162 C ATOM 1868 N VAL A 236 -8.805 -23.656 27.213 1.00 11.18 N ANISOU 1868 N VAL A 236 1199 1562 1487 -38 -48 104 N ATOM 1869 CA VAL A 236 -10.130 -23.747 26.597 1.00 11.27 C ANISOU 1869 CA VAL A 236 1270 1617 1394 -8 -83 51 C ATOM 1870 C VAL A 236 -10.009 -23.647 25.080 1.00 10.61 C ANISOU 1870 C VAL A 236 1282 1365 1382 -132 -46 56 C ATOM 1871 O VAL A 236 -10.664 -24.390 24.342 1.00 10.79 O ANISOU 1871 O VAL A 236 1210 1369 1519 -78 -117 23 O ATOM 1872 CB VAL A 236 -11.058 -22.631 27.122 1.00 11.56 C ANISOU 1872 CB VAL A 236 1327 1676 1389 -3 -5 45 C ATOM 1873 CG1 VAL A 236 -12.368 -22.578 26.351 1.00 12.30 C ANISOU 1873 CG1 VAL A 236 1349 1897 1425 161 -39 28 C ATOM 1874 CG2 VAL A 236 -11.333 -22.841 28.598 1.00 12.44 C ANISOU 1874 CG2 VAL A 236 1470 1827 1430 -10 100 106 C ATOM 1875 N GLN A 237 -9.184 -22.710 24.615 1.00 11.38 N ANISOU 1875 N GLN A 237 1360 1591 1371 -198 39 127 N ATOM 1876 CA GLN A 237 -9.040 -22.496 23.187 1.00 10.64 C ANISOU 1876 CA GLN A 237 1209 1443 1387 -150 3 184 C ATOM 1877 C GLN A 237 -7.682 -21.885 22.897 1.00 11.05 C ANISOU 1877 C GLN A 237 1306 1439 1454 -277 -30 194 C ATOM 1878 O GLN A 237 -7.192 -21.056 23.660 1.00 12.09 O ANISOU 1878 O GLN A 237 1489 1467 1638 -211 21 -32 O ATOM 1879 CB GLN A 237 -10.165 -21.596 22.661 1.00 12.22 C ANISOU 1879 CB GLN A 237 1400 1769 1471 73 105 332 C ATOM 1880 CG GLN A 237 -10.261 -21.615 21.149 1.00 13.84 C ANISOU 1880 CG GLN A 237 1641 2123 1491 91 99 253 C ATOM 1881 CD GLN A 237 -11.575 -21.080 20.652 1.00 17.20 C ANISOU 1881 CD GLN A 237 1955 2235 2344 423 -145 116 C ATOM 1882 OE1 GLN A 237 -11.866 -19.898 20.818 1.00 20.01 O ANISOU 1882 OE1 GLN A 237 2624 2182 2795 513 171 293 O ATOM 1883 NE2 GLN A 237 -12.376 -21.944 20.019 1.00 17.21 N ANISOU 1883 NE2 GLN A 237 1985 2257 2295 285 -38 170 N ATOM 1884 N GLN A 238 -7.088 -22.302 21.787 1.00 11.60 N ANISOU 1884 N GLN A 238 1247 1489 1670 -273 126 173 N ATOM 1885 CA GLN A 238 -5.805 -21.773 21.341 1.00 10.65 C ANISOU 1885 CA GLN A 238 1088 1566 1389 -91 94 190 C ATOM 1886 C GLN A 238 -5.868 -21.521 19.845 1.00 10.67 C ANISOU 1886 C GLN A 238 1259 1428 1364 -68 39 132 C ATOM 1887 O GLN A 238 -6.242 -22.410 19.083 1.00 11.72 O ANISOU 1887 O GLN A 238 1543 1478 1430 -207 63 107 O ATOM 1888 CB GLN A 238 -4.681 -22.772 21.619 1.00 11.48 C ANISOU 1888 CB GLN A 238 1193 1512 1654 9 124 2 C ATOM 1889 CG GLN A 238 -3.291 -22.264 21.245 1.00 10.83 C ANISOU 1889 CG GLN A 238 1221 1422 1472 -115 -19 -41 C ATOM 1890 CD GLN A 238 -2.786 -21.188 22.178 1.00 10.32 C ANISOU 1890 CD GLN A 238 1261 1263 1395 -53 -42 82 C ATOM 1891 OE1 GLN A 238 -3.099 -21.198 23.366 1.00 11.95 O ANISOU 1891 OE1 GLN A 238 1506 1538 1495 -115 170 46 O ATOM 1892 NE2 GLN A 238 -1.983 -20.269 21.651 1.00 11.07 N ANISOU 1892 NE2 GLN A 238 1229 1301 1676 -54 21 135 N ATOM 1893 N GLU A 239 -5.515 -20.307 19.433 1.00 10.63 N ANISOU 1893 N GLU A 239 1232 1490 1314 72 35 311 N ATOM 1894 CA GLU A 239 -5.383 -19.992 18.014 1.00 11.04 C ANISOU 1894 CA GLU A 239 1314 1589 1291 -43 -83 319 C ATOM 1895 C GLU A 239 -4.012 -19.361 17.803 1.00 10.76 C ANISOU 1895 C GLU A 239 1271 1362 1455 24 -71 203 C ATOM 1896 O GLU A 239 -3.775 -18.229 18.218 1.00 12.35 O ANISOU 1896 O GLU A 239 1619 1372 1698 -28 162 85 O ATOM 1897 CB GLU A 239 -6.498 -19.036 17.549 1.00 12.99 C ANISOU 1897 CB GLU A 239 1458 1864 1614 77 -214 393 C ATOM 1898 CG GLU A 239 -7.893 -19.626 17.706 1.00 15.99 C ANISOU 1898 CG GLU A 239 1542 2113 2419 -69 -229 399 C ATOM 1899 CD GLU A 239 -9.016 -18.668 17.364 1.00 19.91 C ANISOU 1899 CD GLU A 239 2186 2369 3008 376 -447 331 C ATOM 1900 OE1 GLU A 239 -8.805 -17.436 17.313 1.00 24.19 O ANISOU 1900 OE1 GLU A 239 2246 2633 4309 30 -660 564 O ATOM 1901 OE2 GLU A 239 -10.133 -19.169 17.156 1.00 25.86 O ANISOU 1901 OE2 GLU A 239 2324 3509 3992 100 -617 -30 O ATOM 1902 N SER A 240 -3.112 -20.126 17.192 1.00 10.83 N ANISOU 1902 N SER A 240 1228 1560 1324 76 -96 213 N ATOM 1903 CA SER A 240 -1.751 -19.688 16.877 1.00 10.76 C ANISOU 1903 CA SER A 240 1155 1544 1387 87 -176 103 C ATOM 1904 C SER A 240 -1.096 -20.777 16.048 1.00 10.67 C ANISOU 1904 C SER A 240 1319 1621 1114 24 -71 129 C ATOM 1905 O SER A 240 -1.624 -21.892 15.956 1.00 11.70 O ANISOU 1905 O SER A 240 1450 1673 1322 -32 -101 115 O ATOM 1906 CB SER A 240 -0.928 -19.421 18.147 1.00 11.03 C ANISOU 1906 CB SER A 240 1467 1538 1186 42 -188 298 C ATOM 1907 OG SER A 240 -0.852 -20.594 18.946 1.00 11.09 O ANISOU 1907 OG SER A 240 1426 1537 1248 -14 -234 298 O ATOM 1908 N SER A 241 0.049 -20.477 15.445 1.00 10.93 N ANISOU 1908 N SER A 241 1274 1471 1406 94 -40 331 N ATOM 1909 CA SER A 241 0.713 -21.487 14.612 1.00 12.03 C ANISOU 1909 CA SER A 241 1447 1800 1325 76 31 140 C ATOM 1910 C SER A 241 1.651 -22.382 15.426 1.00 11.45 C ANISOU 1910 C SER A 241 1344 1727 1279 -29 -10 109 C ATOM 1911 O SER A 241 2.146 -23.380 14.916 1.00 12.22 O ANISOU 1911 O SER A 241 1502 1742 1397 33 -31 123 O ATOM 1912 CB SER A 241 1.484 -20.837 13.476 1.00 12.47 C ANISOU 1912 CB SER A 241 1604 1973 1162 57 -106 256 C ATOM 1913 OG SER A 241 2.568 -20.103 13.991 1.00 15.24 O ANISOU 1913 OG SER A 241 1823 2228 1738 -229 9 75 O ATOM 1914 N PHE A 242 1.901 -22.010 16.682 1.00 10.58 N ANISOU 1914 N PHE A 242 1275 1420 1322 55 -139 150 N ATOM 1915 CA PHE A 242 2.743 -22.786 17.588 1.00 10.37 C ANISOU 1915 CA PHE A 242 1123 1565 1251 45 -156 61 C ATOM 1916 C PHE A 242 2.437 -22.355 19.004 1.00 9.77 C ANISOU 1916 C PHE A 242 1216 1195 1298 -52 -101 69 C ATOM 1917 O PHE A 242 1.808 -21.315 19.228 1.00 10.90 O ANISOU 1917 O PHE A 242 1274 1349 1516 108 -109 107 O ATOM 1918 CB PHE A 242 4.241 -22.552 17.309 1.00 11.00 C ANISOU 1918 CB PHE A 242 1210 1500 1470 -11 -16 11 C ATOM 1919 CG PHE A 242 4.711 -21.166 17.681 1.00 11.09 C ANISOU 1919 CG PHE A 242 1253 1495 1465 -16 -125 42 C ATOM 1920 CD1 PHE A 242 5.306 -20.926 18.924 1.00 11.44 C ANISOU 1920 CD1 PHE A 242 1247 1693 1403 -184 68 -115 C ATOM 1921 CD2 PHE A 242 4.519 -20.094 16.813 1.00 12.34 C ANISOU 1921 CD2 PHE A 242 1468 1503 1714 -64 24 170 C ATOM 1922 CE1 PHE A 242 5.719 -19.653 19.274 1.00 12.80 C ANISOU 1922 CE1 PHE A 242 1377 1672 1813 -193 219 -191 C ATOM 1923 CE2 PHE A 242 4.919 -18.816 17.170 1.00 13.41 C ANISOU 1923 CE2 PHE A 242 1410 1604 2079 -62 45 -36 C ATOM 1924 CZ PHE A 242 5.518 -18.601 18.398 1.00 13.96 C ANISOU 1924 CZ PHE A 242 1372 1793 2136 -64 0 -51 C ATOM 1925 N VAL A 243 2.893 -23.162 19.957 1.00 10.03 N ANISOU 1925 N VAL A 243 1298 1302 1209 37 -226 -5 N ATOM 1926 CA VAL A 243 3.056 -22.719 21.344 1.00 10.22 C ANISOU 1926 CA VAL A 243 1163 1498 1219 15 -58 -60 C ATOM 1927 C VAL A 243 4.437 -23.127 21.838 1.00 9.52 C ANISOU 1927 C VAL A 243 1198 1204 1213 103 26 7 C ATOM 1928 O VAL A 243 5.042 -24.068 21.324 1.00 10.13 O ANISOU 1928 O VAL A 243 1295 1211 1343 16 28 -112 O ATOM 1929 CB VAL A 243 1.976 -23.293 22.296 1.00 10.25 C ANISOU 1929 CB VAL A 243 1231 1290 1371 93 6 65 C ATOM 1930 CG1 VAL A 243 0.580 -22.857 21.871 1.00 11.88 C ANISOU 1930 CG1 VAL A 243 1288 1643 1580 160 -94 118 C ATOM 1931 CG2 VAL A 243 2.063 -24.819 22.387 1.00 12.34 C ANISOU 1931 CG2 VAL A 243 1580 1276 1829 -31 142 168 C ATOM 1932 N MET A 244 4.932 -22.375 22.814 1.00 10.18 N ANISOU 1932 N MET A 244 1189 1297 1382 -92 -202 103 N ATOM 1933 CA MET A 244 6.184 -22.666 23.491 1.00 9.51 C ANISOU 1933 CA MET A 244 1173 1290 1151 -137 -131 96 C ATOM 1934 C MET A 244 5.868 -22.919 24.958 1.00 9.28 C ANISOU 1934 C MET A 244 1288 1117 1121 17 -74 11 C ATOM 1935 O MET A 244 5.363 -22.035 25.658 1.00 10.71 O ANISOU 1935 O MET A 244 1278 1290 1502 192 -5 -20 O ATOM 1936 CB MET A 244 7.132 -21.481 23.355 1.00 10.19 C ANISOU 1936 CB MET A 244 1200 1226 1445 -129 -133 -74 C ATOM 1937 CG MET A 244 8.495 -21.730 23.959 1.00 10.85 C ANISOU 1937 CG MET A 244 1371 1190 1561 4 -264 59 C ATOM 1938 SD MET A 244 9.485 -20.228 23.835 1.00 11.01 S ANISOU 1938 SD MET A 244 1335 1306 1539 -41 -73 5 S ATOM 1939 CE MET A 244 11.063 -20.802 24.459 1.00 11.12 C ANISOU 1939 CE MET A 244 1525 1344 1356 26 -296 59 C ATOM 1940 N MET A 245 6.136 -24.143 25.398 1.00 9.08 N ANISOU 1940 N MET A 245 1294 1148 1007 29 -105 56 N ATOM 1941 CA MET A 245 5.907 -24.551 26.788 1.00 9.17 C ANISOU 1941 CA MET A 245 1121 1301 1059 -5 -68 81 C ATOM 1942 C MET A 245 7.246 -24.650 27.510 1.00 9.38 C ANISOU 1942 C MET A 245 1048 1312 1204 82 -17 -46 C ATOM 1943 O MET A 245 8.140 -25.372 27.053 1.00 11.20 O ANISOU 1943 O MET A 245 1223 1612 1420 282 -4 -127 O ATOM 1944 CB MET A 245 5.210 -25.911 26.843 1.00 10.26 C ANISOU 1944 CB MET A 245 1264 1271 1363 -39 -200 -17 C ATOM 1945 CG MET A 245 3.868 -26.029 26.121 1.00 10.36 C ANISOU 1945 CG MET A 245 1161 1382 1392 1 -131 -50 C ATOM 1946 SD MET A 245 2.555 -24.990 26.784 1.00 11.09 S ANISOU 1946 SD MET A 245 1290 1345 1579 60 -87 32 S ATOM 1947 CE MET A 245 2.448 -25.555 28.480 1.00 11.79 C ANISOU 1947 CE MET A 245 1432 1611 1434 -7 -270 -22 C ATOM 1948 N SER A 246 7.382 -23.924 28.621 1.00 9.85 N ANISOU 1948 N SER A 246 1217 1246 1277 -26 -165 -40 N ATOM 1949 CA SER A 246 8.656 -23.832 29.319 1.00 9.56 C ANISOU 1949 CA SER A 246 1230 1234 1166 -62 -117 -97 C ATOM 1950 C SER A 246 8.520 -24.209 30.785 1.00 10.53 C ANISOU 1950 C SER A 246 1357 1492 1149 53 -122 -64 C ATOM 1951 O SER A 246 7.427 -24.127 31.362 1.00 10.99 O ANISOU 1951 O SER A 246 1309 1320 1544 58 -89 -116 O ATOM 1952 CB SER A 246 9.224 -22.415 29.213 1.00 9.48 C ANISOU 1952 CB SER A 246 1339 1191 1071 -50 -13 -118 C ATOM 1953 OG SER A 246 9.336 -22.030 27.859 1.00 10.67 O ANISOU 1953 OG SER A 246 1511 1375 1167 -113 -54 9 O ATOM 1954 N ALA A 247 9.632 -24.622 31.383 1.00 10.80 N ANISOU 1954 N ALA A 247 1407 1492 1203 137 -105 -95 N ATOM 1955 CA ALA A 247 9.651 -24.937 32.802 1.00 10.87 C ANISOU 1955 CA ALA A 247 1420 1445 1263 97 -96 50 C ATOM 1956 C ALA A 247 11.090 -24.876 33.276 1.00 11.64 C ANISOU 1956 C ALA A 247 1433 1700 1288 119 -131 -129 C ATOM 1957 O ALA A 247 12.000 -25.086 32.484 1.00 11.55 O ANISOU 1957 O ALA A 247 1320 1731 1337 107 -82 67 O ATOM 1958 CB ALA A 247 9.080 -26.331 33.047 1.00 11.33 C ANISOU 1958 CB ALA A 247 1612 1398 1292 112 2 0 C ATOM 1959 N PRO A 248 11.315 -24.622 34.579 1.00 11.04 N ANISOU 1959 N PRO A 248 1332 1653 1206 177 -14 -70 N ATOM 1960 CA PRO A 248 12.695 -24.709 35.082 1.00 11.52 C ANISOU 1960 CA PRO A 248 1426 1847 1102 99 -131 25 C ATOM 1961 C PRO A 248 13.301 -26.062 34.697 1.00 11.96 C ANISOU 1961 C PRO A 248 1517 1796 1230 39 -155 133 C ATOM 1962 O PRO A 248 12.608 -27.073 34.750 1.00 12.38 O ANISOU 1962 O PRO A 248 1544 1737 1421 14 -182 -23 O ATOM 1963 CB PRO A 248 12.521 -24.567 36.608 1.00 12.04 C ANISOU 1963 CB PRO A 248 1654 1794 1127 215 -125 -26 C ATOM 1964 CG PRO A 248 11.244 -23.787 36.758 1.00 13.27 C ANISOU 1964 CG PRO A 248 1448 2018 1573 102 -154 -250 C ATOM 1965 CD PRO A 248 10.352 -24.266 35.640 1.00 11.81 C ANISOU 1965 CD PRO A 248 1553 1727 1204 104 62 -226 C ATOM 1966 N PRO A 249 14.576 -26.084 34.274 1.00 12.30 N ANISOU 1966 N PRO A 249 1496 1721 1453 73 -95 63 N ATOM 1967 CA PRO A 249 15.145 -27.332 33.758 1.00 13.19 C ANISOU 1967 CA PRO A 249 1509 1684 1819 137 -41 158 C ATOM 1968 C PRO A 249 14.986 -28.501 34.734 1.00 13.30 C ANISOU 1968 C PRO A 249 1610 1648 1794 82 -90 116 C ATOM 1969 O PRO A 249 15.215 -28.360 35.937 1.00 15.38 O ANISOU 1969 O PRO A 249 1858 2146 1837 164 -179 247 O ATOM 1970 CB PRO A 249 16.622 -26.985 33.536 1.00 13.38 C ANISOU 1970 CB PRO A 249 1495 1813 1776 138 -42 230 C ATOM 1971 CG PRO A 249 16.617 -25.506 33.279 1.00 14.79 C ANISOU 1971 CG PRO A 249 1756 1784 2076 109 107 106 C ATOM 1972 CD PRO A 249 15.520 -24.956 34.162 1.00 13.46 C ANISOU 1972 CD PRO A 249 1442 1722 1948 90 -131 74 C ATOM 1973 N ALA A 250 14.559 -29.633 34.189 1.00 13.75 N ANISOU 1973 N ALA A 250 1570 1500 2153 -22 74 238 N ATOM 1974 CA ALA A 250 14.340 -30.851 34.954 1.00 14.79 C ANISOU 1974 CA ALA A 250 1850 1662 2106 85 115 365 C ATOM 1975 C ALA A 250 14.355 -32.023 33.989 1.00 14.03 C ANISOU 1975 C ALA A 250 1615 1787 1929 38 15 363 C ATOM 1976 O ALA A 250 14.085 -31.864 32.796 1.00 14.74 O ANISOU 1976 O ALA A 250 1894 1810 1897 72 111 411 O ATOM 1977 CB ALA A 250 13.006 -30.776 35.686 1.00 15.54 C ANISOU 1977 CB ALA A 250 1893 2014 1995 -18 188 493 C ATOM 1978 N GLU A 251 14.665 -33.202 34.510 1.00 15.34 N ANISOU 1978 N GLU A 251 2126 1812 1890 78 -46 390 N ATOM 1979 CA GLU A 251 14.699 -34.403 33.693 1.00 15.71 C ANISOU 1979 CA GLU A 251 2158 1770 2039 150 -284 445 C ATOM 1980 C GLU A 251 13.344 -34.648 33.043 1.00 15.10 C ANISOU 1980 C GLU A 251 2089 1768 1879 58 -133 427 C ATOM 1981 O GLU A 251 12.312 -34.625 33.711 1.00 17.10 O ANISOU 1981 O GLU A 251 2292 2182 2019 88 36 366 O ATOM 1982 CB GLU A 251 15.157 -35.600 34.534 1.00 18.51 C ANISOU 1982 CB GLU A 251 2837 2073 2123 142 -80 875 C ATOM 1983 CG GLU A 251 16.638 -35.544 34.908 1.00 23.05 C ANISOU 1983 CG GLU A 251 3062 2988 2708 44 -226 943 C ATOM 1984 CD GLU A 251 17.556 -35.533 33.692 1.00 26.12 C ANISOU 1984 CD GLU A 251 3384 3505 3034 433 98 1004 C ATOM 1985 OE1 GLU A 251 17.484 -36.484 32.880 1.00 31.99 O ANISOU 1985 OE1 GLU A 251 4615 4645 2892 305 191 561 O ATOM 1986 OE2 GLU A 251 18.352 -34.577 33.551 1.00 30.80 O ANISOU 1986 OE2 GLU A 251 3431 4719 3552 -60 -38 1788 O ATOM 1987 N TYR A 252 13.364 -34.846 31.728 1.00 13.86 N ANISOU 1987 N TYR A 252 1919 1508 1839 26 14 450 N ATOM 1988 CA TYR A 252 12.153 -35.010 30.936 1.00 14.36 C ANISOU 1988 CA TYR A 252 2019 1385 2049 53 -129 324 C ATOM 1989 C TYR A 252 12.449 -35.863 29.712 1.00 14.72 C ANISOU 1989 C TYR A 252 1972 1535 2085 -137 56 259 C ATOM 1990 O TYR A 252 13.545 -35.792 29.154 1.00 16.29 O ANISOU 1990 O TYR A 252 1927 1774 2485 -65 92 347 O ATOM 1991 CB TYR A 252 11.681 -33.633 30.475 1.00 14.30 C ANISOU 1991 CB TYR A 252 1883 1451 2099 114 -173 326 C ATOM 1992 CG TYR A 252 10.298 -33.578 29.864 1.00 13.46 C ANISOU 1992 CG TYR A 252 1703 1488 1921 160 60 434 C ATOM 1993 CD1 TYR A 252 9.157 -33.626 30.666 1.00 13.89 C ANISOU 1993 CD1 TYR A 252 1843 1664 1767 230 108 227 C ATOM 1994 CD2 TYR A 252 10.129 -33.418 28.485 1.00 13.98 C ANISOU 1994 CD2 TYR A 252 1964 1478 1868 -34 7 164 C ATOM 1995 CE1 TYR A 252 7.892 -33.540 30.119 1.00 14.22 C ANISOU 1995 CE1 TYR A 252 1899 1759 1742 94 65 267 C ATOM 1996 CE2 TYR A 252 8.861 -33.314 27.928 1.00 14.51 C ANISOU 1996 CE2 TYR A 252 1935 1447 2132 13 21 211 C ATOM 1997 CZ TYR A 252 7.747 -33.384 28.749 1.00 14.91 C ANISOU 1997 CZ TYR A 252 2065 1844 1756 99 -2 227 C ATOM 1998 OH TYR A 252 6.477 -33.288 28.225 1.00 16.83 O ANISOU 1998 OH TYR A 252 1972 2112 2310 227 13 -39 O ATOM 1999 N LYS A 253 11.476 -36.671 29.297 1.00 15.31 N ANISOU 1999 N LYS A 253 2251 1552 2014 -188 -127 258 N ATOM 2000 CA LYS A 253 11.656 -37.524 28.133 1.00 15.91 C ANISOU 2000 CA LYS A 253 2440 1758 1846 -280 204 413 C ATOM 2001 C LYS A 253 10.924 -36.964 26.921 1.00 15.59 C ANISOU 2001 C LYS A 253 2100 1809 2013 95 194 217 C ATOM 2002 O LYS A 253 9.707 -36.754 26.954 1.00 17.37 O ANISOU 2002 O LYS A 253 1972 2624 2000 -124 91 257 O ATOM 2003 CB LYS A 253 11.176 -38.947 28.439 1.00 18.75 C ANISOU 2003 CB LYS A 253 2897 1663 2562 -357 52 349 C ATOM 2004 CG LYS A 253 11.499 -39.962 27.348 1.00 22.91 C ANISOU 2004 CG LYS A 253 3481 2054 3169 -296 181 -94 C ATOM 2005 CD LYS A 253 11.216 -41.389 27.798 1.00 30.88 C ANISOU 2005 CD LYS A 253 4875 2388 4467 -994 288 188 C ATOM 2006 CE LYS A 253 9.727 -41.680 27.819 1.00 35.58 C ANISOU 2006 CE LYS A 253 4880 3527 5111 -901 161 413 C ATOM 2007 NZ LYS A 253 9.463 -43.063 28.302 1.00 42.40 N ANISOU 2007 NZ LYS A 253 6546 3683 5880 -1175 319 759 N ATOM 2008 N LEU A 254 11.680 -36.731 25.853 1.00 15.38 N ANISOU 2008 N LEU A 254 2189 1612 2043 17 273 160 N ATOM 2009 CA LEU A 254 11.109 -36.339 24.568 1.00 14.77 C ANISOU 2009 CA LEU A 254 1930 1727 1954 -218 66 -242 C ATOM 2010 C LEU A 254 10.937 -37.562 23.694 1.00 15.32 C ANISOU 2010 C LEU A 254 2093 1596 2130 -83 187 -248 C ATOM 2011 O LEU A 254 11.896 -38.311 23.468 1.00 16.11 O ANISOU 2011 O LEU A 254 2070 1575 2476 -116 304 -166 O ATOM 2012 CB LEU A 254 12.002 -35.319 23.853 1.00 15.13 C ANISOU 2012 CB LEU A 254 2013 1560 2174 -94 162 -186 C ATOM 2013 CG LEU A 254 12.169 -33.976 24.569 1.00 13.56 C ANISOU 2013 CG LEU A 254 1791 1477 1884 -77 202 -72 C ATOM 2014 CD1 LEU A 254 13.285 -33.166 23.924 1.00 13.97 C ANISOU 2014 CD1 LEU A 254 1632 1704 1971 33 73 280 C ATOM 2015 CD2 LEU A 254 10.852 -33.204 24.561 1.00 15.46 C ANISOU 2015 CD2 LEU A 254 1727 1867 2277 -32 77 -198 C ATOM 2016 N GLN A 255 9.714 -37.748 23.201 1.00 16.26 N ANISOU 2016 N GLN A 255 2272 1828 2078 -233 93 -319 N ATOM 2017 CA GLN A 255 9.375 -38.901 22.366 1.00 17.76 C ANISOU 2017 CA GLN A 255 2583 1874 2289 -321 31 -364 C ATOM 2018 C GLN A 255 8.966 -38.469 20.969 1.00 16.75 C ANISOU 2018 C GLN A 255 2551 1556 2256 -234 72 -408 C ATOM 2019 O GLN A 255 8.334 -37.429 20.798 1.00 18.07 O ANISOU 2019 O GLN A 255 2699 1657 2509 -92 100 -201 O ATOM 2020 CB GLN A 255 8.256 -39.704 23.022 1.00 21.86 C ANISOU 2020 CB GLN A 255 2766 2572 2965 -754 -75 -193 C ATOM 2021 CG GLN A 255 8.688 -40.332 24.334 1.00 24.99 C ANISOU 2021 CG GLN A 255 3393 3053 3047 -573 209 97 C ATOM 2022 CD GLN A 255 7.638 -41.248 24.905 1.00 27.97 C ANISOU 2022 CD GLN A 255 3545 3476 3603 -650 586 233 C ATOM 2023 OE1 GLN A 255 6.669 -40.794 25.506 1.00 35.02 O ANISOU 2023 OE1 GLN A 255 3364 4752 5189 -271 732 -32 O ATOM 2024 NE2 GLN A 255 7.830 -42.549 24.734 1.00 35.53 N ANISOU 2024 NE2 GLN A 255 4910 3565 5024 -502 576 -146 N ATOM 2025 N GLN A 256 9.313 -39.279 19.971 1.00 17.28 N ANISOU 2025 N GLN A 256 2362 1833 2369 -306 295 -487 N ATOM 2026 CA GLN A 256 8.917 -38.994 18.598 1.00 17.92 C ANISOU 2026 CA GLN A 256 2614 1677 2519 -24 198 -438 C ATOM 2027 C GLN A 256 7.402 -38.921 18.437 1.00 17.50 C ANISOU 2027 C GLN A 256 2584 1709 2353 -186 242 -519 C ATOM 2028 O GLN A 256 6.657 -39.610 19.143 1.00 19.15 O ANISOU 2028 O GLN A 256 2725 2091 2456 -459 186 -448 O ATOM 2029 CB GLN A 256 9.506 -40.021 17.636 1.00 19.58 C ANISOU 2029 CB GLN A 256 2607 2059 2774 54 500 -537 C ATOM 2030 CG GLN A 256 11.023 -40.023 17.639 1.00 23.12 C ANISOU 2030 CG GLN A 256 2648 2726 3410 -193 457 -550 C ATOM 2031 CD GLN A 256 11.609 -40.920 16.572 1.00 23.63 C ANISOU 2031 CD GLN A 256 3139 2727 3110 -35 508 -374 C ATOM 2032 OE1 GLN A 256 12.313 -41.886 16.878 1.00 30.35 O ANISOU 2032 OE1 GLN A 256 4082 2963 4485 343 463 43 O ATOM 2033 NE2 GLN A 256 11.310 -40.618 15.310 1.00 25.78 N ANISOU 2033 NE2 GLN A 256 3610 3183 2999 265 600 -433 N ATOM 2034 N GLY A 257 6.963 -38.067 17.515 1.00 18.36 N ANISOU 2034 N GLY A 257 2648 1987 2340 -47 43 -600 N ATOM 2035 CA GLY A 257 5.549 -37.928 17.181 1.00 17.37 C ANISOU 2035 CA GLY A 257 2536 1829 2233 -59 179 -516 C ATOM 2036 C GLY A 257 4.713 -37.092 18.135 1.00 15.97 C ANISOU 2036 C GLY A 257 2132 1572 2361 -218 -8 -656 C ATOM 2037 O GLY A 257 3.489 -37.056 18.008 1.00 20.79 O ANISOU 2037 O GLY A 257 2225 2800 2873 -244 -46 -855 O ATOM 2038 N THR A 258 5.362 -36.396 19.068 1.00 15.64 N ANISOU 2038 N THR A 258 2181 1695 2067 -363 97 -490 N ATOM 2039 CA THR A 258 4.633 -35.706 20.134 1.00 14.48 C ANISOU 2039 CA THR A 258 1890 1547 2064 -204 -9 -331 C ATOM 2040 C THR A 258 4.965 -34.219 20.279 1.00 14.22 C ANISOU 2040 C THR A 258 1817 1609 1975 -336 -8 -300 C ATOM 2041 O THR A 258 4.350 -33.531 21.090 1.00 15.19 O ANISOU 2041 O THR A 258 1914 1720 2137 -189 84 -373 O ATOM 2042 CB THR A 258 4.882 -36.370 21.512 1.00 15.86 C ANISOU 2042 CB THR A 258 2225 1634 2165 -309 -48 -202 C ATOM 2043 OG1 THR A 258 6.260 -36.194 21.872 1.00 17.58 O ANISOU 2043 OG1 THR A 258 2240 2022 2414 -234 -102 -199 O ATOM 2044 CG2 THR A 258 4.533 -37.867 21.493 1.00 17.69 C ANISOU 2044 CG2 THR A 258 2372 1622 2725 -291 -62 -202 C ATOM 2045 N PHE A 259 5.955 -33.729 19.539 1.00 13.09 N ANISOU 2045 N PHE A 259 1703 1392 1878 -33 41 -240 N ATOM 2046 CA PHE A 259 6.396 -32.331 19.672 1.00 12.62 C ANISOU 2046 CA PHE A 259 1644 1473 1678 -161 -140 -133 C ATOM 2047 C PHE A 259 7.131 -31.901 18.418 1.00 12.72 C ANISOU 2047 C PHE A 259 1735 1431 1666 -129 -60 -186 C ATOM 2048 O PHE A 259 7.534 -32.734 17.600 1.00 14.27 O ANISOU 2048 O PHE A 259 1956 1625 1839 -80 45 -305 O ATOM 2049 CB PHE A 259 7.286 -32.124 20.923 1.00 13.13 C ANISOU 2049 CB PHE A 259 1654 1547 1787 0 -190 -316 C ATOM 2050 CG PHE A 259 8.676 -32.685 20.786 1.00 12.27 C ANISOU 2050 CG PHE A 259 1649 1360 1652 -21 -248 -145 C ATOM 2051 CD1 PHE A 259 9.779 -31.854 20.575 1.00 12.76 C ANISOU 2051 CD1 PHE A 259 1654 1510 1684 -85 -176 -290 C ATOM 2052 CD2 PHE A 259 8.880 -34.061 20.854 1.00 12.35 C ANISOU 2052 CD2 PHE A 259 1852 1354 1485 61 -230 -98 C ATOM 2053 CE1 PHE A 259 11.056 -32.391 20.432 1.00 12.38 C ANISOU 2053 CE1 PHE A 259 1753 1411 1538 -32 -113 -140 C ATOM 2054 CE2 PHE A 259 10.154 -34.600 20.717 1.00 14.45 C ANISOU 2054 CE2 PHE A 259 1736 1758 1996 -30 28 -213 C ATOM 2055 CZ PHE A 259 11.245 -33.766 20.507 1.00 12.80 C ANISOU 2055 CZ PHE A 259 1747 1448 1668 76 -55 -92 C ATOM 2056 N LEU A 260 7.328 -30.595 18.282 1.00 12.10 N ANISOU 2056 N LEU A 260 1472 1458 1665 -171 -191 -143 N ATOM 2057 CA LEU A 260 8.001 -30.035 17.130 1.00 12.98 C ANISOU 2057 CA LEU A 260 1616 1606 1710 -60 -72 -54 C ATOM 2058 C LEU A 260 9.525 -29.985 17.343 1.00 12.00 C ANISOU 2058 C LEU A 260 1637 1479 1443 -311 -35 -139 C ATOM 2059 O LEU A 260 10.298 -30.580 16.588 1.00 13.04 O ANISOU 2059 O LEU A 260 1794 1567 1592 -80 -67 -126 O ATOM 2060 CB LEU A 260 7.438 -28.641 16.848 1.00 15.63 C ANISOU 2060 CB LEU A 260 2293 1625 2020 78 -115 -128 C ATOM 2061 CG LEU A 260 7.908 -27.955 15.576 1.00 16.80 C ANISOU 2061 CG LEU A 260 2365 2048 1968 69 41 -118 C ATOM 2062 CD1 LEU A 260 7.285 -28.574 14.327 1.00 19.07 C ANISOU 2062 CD1 LEU A 260 3044 2418 1784 370 -158 -172 C ATOM 2063 CD2 LEU A 260 7.538 -26.493 15.689 1.00 18.08 C ANISOU 2063 CD2 LEU A 260 3086 2008 1775 129 -168 -117 C ATOM 2064 N CYS A 261 9.949 -29.263 18.373 1.00 11.37 N ANISOU 2064 N CYS A 261 1414 1426 1480 -134 -84 -164 N ATOM 2065 CA CYS A 261 11.361 -29.151 18.711 1.00 10.68 C ANISOU 2065 CA CYS A 261 1394 1437 1225 -111 -34 -45 C ATOM 2066 C CYS A 261 11.458 -28.687 20.144 1.00 10.03 C ANISOU 2066 C CYS A 261 1303 1222 1285 162 -59 -97 C ATOM 2067 O CYS A 261 10.435 -28.383 20.770 1.00 10.63 O ANISOU 2067 O CYS A 261 1261 1333 1442 149 -19 -67 O ATOM 2068 CB CYS A 261 12.098 -28.211 17.748 1.00 11.42 C ANISOU 2068 CB CYS A 261 1741 1344 1253 14 12 113 C ATOM 2069 SG CYS A 261 11.504 -26.519 17.717 1.00 11.93 S ANISOU 2069 SG CYS A 261 1659 1392 1481 34 13 22 S ATOM 2070 N ALA A 262 12.672 -28.662 20.681 1.00 9.66 N ANISOU 2070 N ALA A 262 1334 1214 1122 109 -58 -123 N ATOM 2071 CA ALA A 262 12.855 -28.404 22.108 1.00 9.46 C ANISOU 2071 CA ALA A 262 1225 1274 1096 9 -26 -58 C ATOM 2072 C ALA A 262 14.289 -27.993 22.359 1.00 9.78 C ANISOU 2072 C ALA A 262 1258 1182 1275 23 -96 -79 C ATOM 2073 O ALA A 262 15.156 -28.159 21.504 1.00 10.76 O ANISOU 2073 O ALA A 262 1453 1268 1365 60 34 -116 O ATOM 2074 CB ALA A 262 12.538 -29.665 22.907 1.00 11.33 C ANISOU 2074 CB ALA A 262 1529 1307 1468 5 205 42 C ATOM 2075 N ASN A 263 14.555 -27.495 23.556 1.00 9.64 N ANISOU 2075 N ASN A 263 1306 1158 1198 64 -106 -35 N ATOM 2076 CA ASN A 263 15.949 -27.357 23.977 1.00 10.90 C ANISOU 2076 CA ASN A 263 1328 1389 1422 -63 -108 84 C ATOM 2077 C ASN A 263 16.125 -27.744 25.424 1.00 10.48 C ANISOU 2077 C ASN A 263 1255 1386 1341 93 102 30 C ATOM 2078 O ASN A 263 15.188 -27.649 26.240 1.00 9.74 O ANISOU 2078 O ASN A 263 1351 1279 1068 135 58 98 O ATOM 2079 CB ASN A 263 16.549 -25.979 23.669 1.00 12.57 C ANISOU 2079 CB ASN A 263 1639 1433 1703 -65 -168 232 C ATOM 2080 CG ASN A 263 15.674 -24.851 24.138 1.00 12.47 C ANISOU 2080 CG ASN A 263 1598 1590 1546 -120 -60 10 C ATOM 2081 OD1 ASN A 263 15.612 -24.550 25.341 1.00 16.53 O ANISOU 2081 OD1 ASN A 263 2289 2377 1612 84 -207 -148 O ATOM 2082 ND2 ASN A 263 15.023 -24.182 23.200 1.00 11.85 N ANISOU 2082 ND2 ASN A 263 1785 1680 1036 -191 74 -40 N ATOM 2083 N GLU A 264 17.330 -28.213 25.717 1.00 10.25 N ANISOU 2083 N GLU A 264 1344 1295 1253 77 -71 91 N ATOM 2084 CA GLU A 264 17.695 -28.632 27.053 1.00 10.60 C ANISOU 2084 CA GLU A 264 1361 1321 1343 132 -182 112 C ATOM 2085 C GLU A 264 18.815 -27.740 27.546 1.00 10.65 C ANISOU 2085 C GLU A 264 1302 1432 1310 46 -29 111 C ATOM 2086 O GLU A 264 19.613 -27.242 26.749 1.00 10.85 O ANISOU 2086 O GLU A 264 1261 1464 1394 110 6 156 O ATOM 2087 CB GLU A 264 18.103 -30.112 27.070 1.00 11.69 C ANISOU 2087 CB GLU A 264 1444 1395 1599 295 -77 84 C ATOM 2088 CG GLU A 264 19.337 -30.448 26.241 1.00 11.87 C ANISOU 2088 CG GLU A 264 1396 1462 1651 188 8 262 C ATOM 2089 CD GLU A 264 20.661 -30.211 26.946 1.00 11.72 C ANISOU 2089 CD GLU A 264 1609 1366 1478 87 -39 81 C ATOM 2090 OE1 GLU A 264 20.689 -30.072 28.187 1.00 11.82 O ANISOU 2090 OE1 GLU A 264 1418 1588 1483 249 -29 128 O ATOM 2091 OE2 GLU A 264 21.690 -30.198 26.234 1.00 13.43 O ANISOU 2091 OE2 GLU A 264 1733 1656 1713 233 122 275 O ATOM 2092 N TYR A 265 18.859 -27.556 28.864 1.00 10.65 N ANISOU 2092 N TYR A 265 1296 1435 1315 159 -196 56 N ATOM 2093 CA TYR A 265 19.864 -26.717 29.519 1.00 10.90 C ANISOU 2093 CA TYR A 265 1481 1285 1375 166 -194 -47 C ATOM 2094 C TYR A 265 20.619 -27.573 30.516 1.00 11.41 C ANISOU 2094 C TYR A 265 1380 1432 1520 207 -53 161 C ATOM 2095 O TYR A 265 20.063 -28.000 31.530 1.00 12.83 O ANISOU 2095 O TYR A 265 1452 1858 1561 313 25 240 O ATOM 2096 CB TYR A 265 19.166 -25.571 30.243 1.00 10.94 C ANISOU 2096 CB TYR A 265 1278 1459 1417 97 -56 -120 C ATOM 2097 CG TYR A 265 20.028 -24.621 31.052 1.00 10.14 C ANISOU 2097 CG TYR A 265 1198 1445 1206 64 14 -32 C ATOM 2098 CD1 TYR A 265 20.263 -24.838 32.412 1.00 10.90 C ANISOU 2098 CD1 TYR A 265 1381 1518 1243 62 15 50 C ATOM 2099 CD2 TYR A 265 20.545 -23.460 30.467 1.00 11.61 C ANISOU 2099 CD2 TYR A 265 1437 1372 1601 91 158 -75 C ATOM 2100 CE1 TYR A 265 21.014 -23.934 33.153 1.00 12.41 C ANISOU 2100 CE1 TYR A 265 1339 1673 1701 -48 27 -130 C ATOM 2101 CE2 TYR A 265 21.269 -22.547 31.200 1.00 12.14 C ANISOU 2101 CE2 TYR A 265 1389 1706 1515 110 -46 -42 C ATOM 2102 CZ TYR A 265 21.512 -22.786 32.533 1.00 11.97 C ANISOU 2102 CZ TYR A 265 1420 1649 1477 -1 -107 -123 C ATOM 2103 OH TYR A 265 22.213 -21.838 33.250 1.00 13.44 O ANISOU 2103 OH TYR A 265 1553 1833 1718 -121 -52 -330 O ATOM 2104 N THR A 266 21.891 -27.815 30.217 1.00 11.55 N ANISOU 2104 N THR A 266 1252 1653 1481 188 -226 228 N ATOM 2105 CA THR A 266 22.771 -28.592 31.090 1.00 12.05 C ANISOU 2105 CA THR A 266 1499 1565 1512 404 -144 201 C ATOM 2106 C THR A 266 23.649 -27.624 31.881 1.00 12.90 C ANISOU 2106 C THR A 266 1509 1778 1614 219 -102 184 C ATOM 2107 O THR A 266 24.359 -26.812 31.302 1.00 13.98 O ANISOU 2107 O THR A 266 1911 1814 1586 138 -85 313 O ATOM 2108 CB THR A 266 23.643 -29.542 30.254 1.00 12.43 C ANISOU 2108 CB THR A 266 1481 1565 1674 472 -261 90 C ATOM 2109 OG1 THR A 266 22.808 -30.553 29.690 1.00 13.43 O ANISOU 2109 OG1 THR A 266 1590 1723 1787 266 -235 85 O ATOM 2110 CG2 THR A 266 24.707 -30.222 31.119 1.00 14.03 C ANISOU 2110 CG2 THR A 266 1727 1832 1770 560 -409 176 C ATOM 2111 N GLY A 267 23.599 -27.726 33.203 1.00 13.57 N ANISOU 2111 N GLY A 267 1470 2097 1585 169 -243 122 N ATOM 2112 CA GLY A 267 24.368 -26.845 34.074 1.00 15.25 C ANISOU 2112 CA GLY A 267 1817 2369 1607 19 -116 -68 C ATOM 2113 C GLY A 267 23.544 -26.413 35.267 1.00 15.70 C ANISOU 2113 C GLY A 267 1860 2310 1795 -17 65 -31 C ATOM 2114 O GLY A 267 22.670 -27.150 35.728 1.00 18.80 O ANISOU 2114 O GLY A 267 2392 2676 2075 -309 374 8 O ATOM 2115 N ASN A 268 23.811 -25.209 35.761 1.00 15.89 N ANISOU 2115 N ASN A 268 2013 2231 1792 98 -33 1 N ATOM 2116 CA ASN A 268 23.140 -24.699 36.952 1.00 15.60 C ANISOU 2116 CA ASN A 268 2088 2169 1670 -16 -152 -118 C ATOM 2117 C ASN A 268 22.734 -23.250 36.748 1.00 15.77 C ANISOU 2117 C ASN A 268 1863 2195 1931 -100 -214 -42 C ATOM 2118 O ASN A 268 22.891 -22.729 35.647 1.00 16.59 O ANISOU 2118 O ASN A 268 2052 2345 1907 -91 -14 -91 O ATOM 2119 CB ASN A 268 24.003 -24.915 38.211 1.00 17.46 C ANISOU 2119 CB ASN A 268 2154 2530 1950 -87 -344 22 C ATOM 2120 CG ASN A 268 25.327 -24.159 38.175 1.00 16.68 C ANISOU 2120 CG ASN A 268 1974 2407 1956 78 -208 104 C ATOM 2121 OD1 ASN A 268 25.475 -23.131 37.503 1.00 16.95 O ANISOU 2121 OD1 ASN A 268 2341 2218 1878 32 -202 -89 O ATOM 2122 ND2 ASN A 268 26.295 -24.657 38.938 1.00 20.62 N ANISOU 2122 ND2 ASN A 268 2627 3317 1887 720 -311 55 N ATOM 2123 N TYR A 269 22.237 -22.588 37.790 1.00 17.77 N ANISOU 2123 N TYR A 269 1849 2269 2632 25 56 -256 N ATOM 2124 CA TYR A 269 21.782 -21.207 37.619 1.00 17.51 C ANISOU 2124 CA TYR A 269 2122 2273 2256 -13 42 -133 C ATOM 2125 C TYR A 269 22.909 -20.176 37.469 1.00 17.75 C ANISOU 2125 C TYR A 269 2041 2468 2234 -84 -142 11 C ATOM 2126 O TYR A 269 22.650 -19.019 37.137 1.00 20.04 O ANISOU 2126 O TYR A 269 2103 2498 3013 5 -68 96 O ATOM 2127 CB TYR A 269 20.747 -20.814 38.680 1.00 17.02 C ANISOU 2127 CB TYR A 269 1908 2379 2178 121 -66 -72 C ATOM 2128 CG TYR A 269 19.399 -21.453 38.412 1.00 15.67 C ANISOU 2128 CG TYR A 269 2008 2278 1668 51 -72 108 C ATOM 2129 CD1 TYR A 269 18.603 -21.026 37.346 1.00 15.38 C ANISOU 2129 CD1 TYR A 269 1943 1962 1937 333 -157 -74 C ATOM 2130 CD2 TYR A 269 18.943 -22.516 39.193 1.00 15.13 C ANISOU 2130 CD2 TYR A 269 1711 2197 1839 244 -99 229 C ATOM 2131 CE1 TYR A 269 17.380 -21.617 37.091 1.00 15.15 C ANISOU 2131 CE1 TYR A 269 2000 1759 1994 248 -56 -97 C ATOM 2132 CE2 TYR A 269 17.722 -23.122 38.943 1.00 16.53 C ANISOU 2132 CE2 TYR A 269 1820 2399 2062 154 -263 339 C ATOM 2133 CZ TYR A 269 16.948 -22.673 37.881 1.00 14.76 C ANISOU 2133 CZ TYR A 269 1978 2142 1486 237 -89 -4 C ATOM 2134 OH TYR A 269 15.728 -23.269 37.627 1.00 17.08 O ANISOU 2134 OH TYR A 269 2018 2263 2209 218 -250 -88 O ATOM 2135 N GLN A 270 24.153 -20.602 37.681 1.00 16.96 N ANISOU 2135 N GLN A 270 1973 2494 1977 -120 -50 -214 N ATOM 2136 CA GLN A 270 25.296 -19.729 37.431 1.00 16.61 C ANISOU 2136 CA GLN A 270 2096 2226 1988 -149 -252 -146 C ATOM 2137 C GLN A 270 25.764 -19.823 35.979 1.00 15.63 C ANISOU 2137 C GLN A 270 1815 2098 2025 -70 -208 -269 C ATOM 2138 O GLN A 270 26.138 -18.815 35.375 1.00 16.83 O ANISOU 2138 O GLN A 270 2060 2218 2116 -103 -180 -282 O ATOM 2139 CB GLN A 270 26.449 -20.058 38.378 1.00 18.84 C ANISOU 2139 CB GLN A 270 2156 2948 2055 -161 -471 -485 C ATOM 2140 CG GLN A 270 27.613 -19.086 38.265 1.00 22.02 C ANISOU 2140 CG GLN A 270 2423 2901 3040 -166 -94 -334 C ATOM 2141 CD GLN A 270 28.843 -19.541 39.020 1.00 24.81 C ANISOU 2141 CD GLN A 270 2458 3495 3473 170 -146 -398 C ATOM 2142 OE1 GLN A 270 29.291 -20.678 38.877 1.00 22.72 O ANISOU 2142 OE1 GLN A 270 2446 3360 2827 85 -128 -54 O ATOM 2143 NE2 GLN A 270 29.396 -18.652 39.829 1.00 30.84 N ANISOU 2143 NE2 GLN A 270 3804 4226 3687 -213 -363 -754 N ATOM 2144 N CYS A 271 25.735 -21.033 35.419 1.00 14.35 N ANISOU 2144 N CYS A 271 1874 2104 1471 21 -333 -100 N ATOM 2145 CA CYS A 271 26.195 -21.252 34.050 1.00 14.39 C ANISOU 2145 CA CYS A 271 1668 2189 1610 -49 -167 -97 C ATOM 2146 C CYS A 271 25.682 -22.578 33.512 1.00 13.60 C ANISOU 2146 C CYS A 271 1646 1937 1581 24 -16 88 C ATOM 2147 O CYS A 271 25.717 -23.595 34.198 1.00 14.66 O ANISOU 2147 O CYS A 271 1854 2103 1613 85 -75 231 O ATOM 2148 CB CYS A 271 27.730 -21.218 33.972 1.00 17.69 C ANISOU 2148 CB CYS A 271 1694 2503 2523 -303 20 -388 C ATOM 2149 SG CYS A 271 28.381 -21.331 32.281 1.00 26.32 S ANISOU 2149 SG CYS A 271 2586 4195 3217 -447 676 -749 S ATOM 2150 N GLY A 272 25.227 -22.560 32.268 1.00 13.48 N ANISOU 2150 N GLY A 272 1405 2041 1673 26 -83 18 N ATOM 2151 CA GLY A 272 24.799 -23.767 31.609 1.00 13.69 C ANISOU 2151 CA GLY A 272 1548 2009 1642 8 68 33 C ATOM 2152 C GLY A 272 25.113 -23.722 30.131 1.00 12.56 C ANISOU 2152 C GLY A 272 1465 1670 1637 70 94 -8 C ATOM 2153 O GLY A 272 25.756 -22.791 29.638 1.00 14.51 O ANISOU 2153 O GLY A 272 1960 1587 1962 31 49 150 O ATOM 2154 N HIS A 273 24.651 -24.747 29.433 1.00 12.32 N ANISOU 2154 N HIS A 273 1465 1857 1359 25 -93 35 N ATOM 2155 CA HIS A 273 24.854 -24.880 28.000 1.00 11.76 C ANISOU 2155 CA HIS A 273 1221 1908 1338 109 -93 203 C ATOM 2156 C HIS A 273 23.597 -25.475 27.407 1.00 11.50 C ANISOU 2156 C HIS A 273 1355 1491 1521 163 -232 217 C ATOM 2157 O HIS A 273 23.023 -26.415 27.968 1.00 13.02 O ANISOU 2157 O HIS A 273 1371 1734 1841 167 -18 392 O ATOM 2158 CB HIS A 273 26.064 -25.776 27.716 1.00 12.31 C ANISOU 2158 CB HIS A 273 1418 1825 1433 120 79 161 C ATOM 2159 CG HIS A 273 26.300 -26.006 26.247 1.00 12.37 C ANISOU 2159 CG HIS A 273 1395 1904 1398 227 -59 116 C ATOM 2160 ND1 HIS A 273 26.914 -25.099 25.461 1.00 15.12 N ANISOU 2160 ND1 HIS A 273 1897 2157 1691 124 110 179 N ATOM 2161 CD2 HIS A 273 25.919 -27.054 25.415 1.00 13.31 C ANISOU 2161 CD2 HIS A 273 1495 1826 1733 248 -92 66 C ATOM 2162 CE1 HIS A 273 26.939 -25.556 24.196 1.00 13.99 C ANISOU 2162 CE1 HIS A 273 1780 2086 1447 622 256 416 C ATOM 2163 NE2 HIS A 273 26.334 -26.747 24.170 1.00 15.51 N ANISOU 2163 NE2 HIS A 273 1625 2611 1655 382 -96 -19 N ATOM 2164 N TYR A 274 23.155 -24.978 26.242 1.00 11.01 N ANISOU 2164 N TYR A 274 1187 1649 1345 137 -171 118 N ATOM 2165 CA TYR A 274 21.944 -25.461 25.582 1.00 10.12 C ANISOU 2165 CA TYR A 274 1244 1244 1356 229 -183 7 C ATOM 2166 C TYR A 274 22.275 -26.392 24.399 1.00 10.87 C ANISOU 2166 C TYR A 274 1305 1548 1274 38 -12 -27 C ATOM 2167 O TYR A 274 23.213 -26.093 23.637 1.00 11.46 O ANISOU 2167 O TYR A 274 1310 1586 1457 166 82 3 O ATOM 2168 CB TYR A 274 21.180 -24.325 24.971 1.00 10.23 C ANISOU 2168 CB TYR A 274 1416 1125 1346 233 7 81 C ATOM 2169 CG TYR A 274 20.330 -23.483 25.901 1.00 9.97 C ANISOU 2169 CG TYR A 274 1173 1180 1432 186 25 87 C ATOM 2170 CD1 TYR A 274 20.807 -22.281 26.400 1.00 9.87 C ANISOU 2170 CD1 TYR A 274 1333 1213 1203 217 -165 69 C ATOM 2171 CD2 TYR A 274 19.036 -23.864 26.241 1.00 10.51 C ANISOU 2171 CD2 TYR A 274 1121 1510 1358 212 75 -51 C ATOM 2172 CE1 TYR A 274 20.037 -21.491 27.231 1.00 10.12 C ANISOU 2172 CE1 TYR A 274 1200 1426 1216 119 73 163 C ATOM 2173 CE2 TYR A 274 18.256 -23.080 27.075 1.00 9.83 C ANISOU 2173 CE2 TYR A 274 1345 1148 1239 158 -38 -92 C ATOM 2174 CZ TYR A 274 18.764 -21.895 27.566 1.00 9.65 C ANISOU 2174 CZ TYR A 274 1154 1248 1264 88 1 -97 C ATOM 2175 OH TYR A 274 18.011 -21.095 28.398 1.00 10.74 O ANISOU 2175 OH TYR A 274 1342 1381 1356 300 59 -7 O ATOM 2176 N THR A 275 21.472 -27.365 24.241 1.00 10.12 N ANISOU 2176 N THR A 275 1330 1321 1191 161 -54 -77 N ATOM 2177 CA THR A 275 21.396 -28.030 22.939 1.00 9.92 C ANISOU 2177 CA THR A 275 1350 1225 1191 234 -58 -64 C ATOM 2178 C THR A 275 19.935 -28.099 22.500 1.00 10.04 C ANISOU 2178 C THR A 275 1282 1109 1423 195 28 22 C ATOM 2179 O THR A 275 19.011 -27.990 23.313 1.00 10.71 O ANISOU 2179 O THR A 275 1406 1261 1401 99 65 91 O ATOM 2180 CB THR A 275 22.053 -29.426 22.883 1.00 10.68 C ANISOU 2180 CB THR A 275 1334 1272 1449 288 41 182 C ATOM 2181 OG1 THR A 275 21.280 -30.366 23.638 1.00 12.15 O ANISOU 2181 OG1 THR A 275 1554 1356 1704 217 210 204 O ATOM 2182 CG2 THR A 275 23.490 -29.376 23.408 1.00 12.14 C ANISOU 2182 CG2 THR A 275 1320 1698 1591 375 4 -160 C ATOM 2183 N HIS A 276 19.754 -28.286 21.198 1.00 10.62 N ANISOU 2183 N HIS A 276 1382 1221 1430 189 -107 119 N ATOM 2184 CA HIS A 276 18.447 -28.297 20.569 1.00 10.82 C ANISOU 2184 CA HIS A 276 1488 1230 1392 93 -179 51 C ATOM 2185 C HIS A 276 18.081 -29.693 20.148 1.00 10.26 C ANISOU 2185 C HIS A 276 1372 1238 1286 115 23 -11 C ATOM 2186 O HIS A 276 18.939 -30.438 19.679 1.00 12.77 O ANISOU 2186 O HIS A 276 1446 1450 1956 144 291 -135 O ATOM 2187 CB HIS A 276 18.523 -27.379 19.361 1.00 11.99 C ANISOU 2187 CB HIS A 276 1500 1547 1508 64 18 234 C ATOM 2188 CG HIS A 276 17.250 -27.298 18.559 1.00 12.43 C ANISOU 2188 CG HIS A 276 1558 1674 1489 86 -55 161 C ATOM 2189 ND1 HIS A 276 16.230 -26.475 18.885 1.00 12.77 N ANISOU 2189 ND1 HIS A 276 1443 1619 1787 41 -37 320 N ATOM 2190 CD2 HIS A 276 16.870 -27.950 17.392 1.00 12.00 C ANISOU 2190 CD2 HIS A 276 1527 1517 1513 12 -60 171 C ATOM 2191 CE1 HIS A 276 15.241 -26.615 17.974 1.00 12.60 C ANISOU 2191 CE1 HIS A 276 1564 1369 1854 -52 -117 263 C ATOM 2192 NE2 HIS A 276 15.631 -27.522 17.073 1.00 13.49 N ANISOU 2192 NE2 HIS A 276 1678 1720 1727 99 -188 284 N ATOM 2193 N ILE A 277 16.807 -30.053 20.278 1.00 10.30 N ANISOU 2193 N ILE A 277 1440 1313 1158 3 29 -73 N ATOM 2194 CA ILE A 277 16.321 -31.357 19.811 1.00 10.95 C ANISOU 2194 CA ILE A 277 1423 1357 1381 -10 119 -125 C ATOM 2195 C ILE A 277 15.185 -31.093 18.831 1.00 11.25 C ANISOU 2195 C ILE A 277 1503 1368 1402 6 30 -225 C ATOM 2196 O ILE A 277 14.201 -30.438 19.189 1.00 12.24 O ANISOU 2196 O ILE A 277 1578 1523 1547 121 57 -191 O ATOM 2197 CB ILE A 277 15.822 -32.273 20.958 1.00 12.01 C ANISOU 2197 CB ILE A 277 1709 1318 1533 -130 127 -63 C ATOM 2198 CG1 ILE A 277 16.921 -32.496 22.017 1.00 13.36 C ANISOU 2198 CG1 ILE A 277 1814 1633 1629 -231 8 -89 C ATOM 2199 CG2 ILE A 277 15.359 -33.622 20.391 1.00 14.82 C ANISOU 2199 CG2 ILE A 277 2074 1419 2137 -155 21 -281 C ATOM 2200 CD1 ILE A 277 16.966 -31.485 23.157 1.00 14.84 C ANISOU 2200 CD1 ILE A 277 2364 1576 1698 -195 -9 -71 C ATOM 2201 N THR A 278 15.331 -31.574 17.596 1.00 11.81 N ANISOU 2201 N THR A 278 1656 1411 1418 -121 50 -241 N ATOM 2202 CA THR A 278 14.292 -31.434 16.583 1.00 13.50 C ANISOU 2202 CA THR A 278 1695 1707 1726 91 -54 -372 C ATOM 2203 C THR A 278 13.781 -32.812 16.174 1.00 14.29 C ANISOU 2203 C THR A 278 1927 1608 1891 -20 -48 -119 C ATOM 2204 O THR A 278 14.557 -33.762 16.075 1.00 15.73 O ANISOU 2204 O THR A 278 1932 1809 2232 56 -115 -578 O ATOM 2205 CB THR A 278 14.759 -30.600 15.360 1.00 14.93 C ANISOU 2205 CB THR A 278 2072 1724 1875 218 -61 -203 C ATOM 2206 OG1 THR A 278 13.693 -30.519 14.412 1.00 16.02 O ANISOU 2206 OG1 THR A 278 2671 1748 1665 -54 -322 -281 O ATOM 2207 CG2 THR A 278 16.013 -31.178 14.669 1.00 16.46 C ANISOU 2207 CG2 THR A 278 2093 2193 1968 56 185 -172 C ATOM 2208 N ALA A 279 12.474 -32.920 15.957 1.00 14.48 N ANISOU 2208 N ALA A 279 2029 1767 1704 -241 -117 -164 N ATOM 2209 CA ALA A 279 11.872 -34.186 15.575 1.00 16.31 C ANISOU 2209 CA ALA A 279 2353 1733 2109 -245 -41 -294 C ATOM 2210 C ALA A 279 11.776 -34.279 14.056 1.00 18.46 C ANISOU 2210 C ALA A 279 2602 2248 2163 -120 -302 -521 C ATOM 2211 O ALA A 279 10.976 -33.579 13.439 1.00 20.32 O ANISOU 2211 O ALA A 279 2739 2320 2661 -91 -615 -669 O ATOM 2212 CB ALA A 279 10.503 -34.331 16.215 1.00 18.08 C ANISOU 2212 CB ALA A 279 2284 1930 2654 -319 6 -170 C ATOM 2213 N LYS A 280 12.618 -35.128 13.466 1.00 20.97 N ANISOU 2213 N LYS A 280 3200 2402 2364 -10 -15 -635 N ATOM 2214 CA ALYS A 280 12.635 -35.355 12.022 0.50 21.13 C ANISOU 2214 CA ALYS A 280 3070 2600 2356 -75 42 -556 C ATOM 2215 CA BLYS A 280 12.612 -35.350 12.021 0.50 21.25 C ANISOU 2215 CA BLYS A 280 3077 2625 2369 -98 63 -597 C ATOM 2216 C LYS A 280 12.222 -36.806 11.753 1.00 23.70 C ANISOU 2216 C LYS A 280 3320 2608 3073 -28 182 -699 C ATOM 2217 O LYS A 280 11.257 -37.294 12.353 1.00 24.83 O ANISOU 2217 O LYS A 280 3191 2683 3561 -281 19 -562 O ATOM 2218 CB ALYS A 280 14.014 -35.005 11.438 0.50 20.83 C ANISOU 2218 CB ALYS A 280 3146 2489 2277 -41 88 -582 C ATOM 2219 CB BLYS A 280 13.954 -34.941 11.395 0.50 21.53 C ANISOU 2219 CB BLYS A 280 3195 2636 2349 -149 143 -692 C ATOM 2220 CG ALYS A 280 14.358 -33.517 11.524 0.50 22.35 C ANISOU 2220 CG ALYS A 280 3395 2529 2568 -92 56 -450 C ATOM 2221 CG BLYS A 280 14.214 -33.433 11.427 0.50 22.74 C ANISOU 2221 CG BLYS A 280 3419 2608 2611 22 215 -574 C ATOM 2222 CD ALYS A 280 15.798 -33.236 11.120 0.50 22.26 C ANISOU 2222 CD ALYS A 280 3347 2558 2552 -64 -84 -19 C ATOM 2223 CD BLYS A 280 12.975 -32.651 11.012 0.50 23.99 C ANISOU 2223 CD BLYS A 280 3366 3220 2529 -16 64 -303 C ATOM 2224 CE ALYS A 280 16.077 -33.653 9.683 0.50 24.40 C ANISOU 2224 CE ALYS A 280 3683 2872 2713 -12 129 -188 C ATOM 2225 CE BLYS A 280 13.299 -31.244 10.526 0.50 26.52 C ANISOU 2225 CE BLYS A 280 3774 3400 2901 -224 -179 -188 C ATOM 2226 NZ ALYS A 280 15.250 -32.911 8.693 0.50 25.63 N ANISOU 2226 NZ ALYS A 280 3693 3345 2699 -85 258 200 N ATOM 2227 NZ BLYS A 280 13.675 -30.258 11.580 0.50 20.81 N ANISOU 2227 NZ BLYS A 280 2459 3981 1466 331 39 110 N ATOM 2228 N GLU A 281 12.935 -37.514 10.869 1.00 23.51 N ANISOU 2228 N GLU A 281 3522 2753 2656 -261 103 -795 N ATOM 2229 CA GLU A 281 12.643 -38.943 10.672 1.00 24.48 C ANISOU 2229 CA GLU A 281 3650 2681 2969 -64 189 -865 C ATOM 2230 C GLU A 281 13.042 -39.744 11.928 1.00 24.82 C ANISOU 2230 C GLU A 281 3966 2636 2826 -469 64 -859 C ATOM 2231 O GLU A 281 12.543 -40.847 12.169 1.00 26.91 O ANISOU 2231 O GLU A 281 4225 2645 3352 -617 272 -900 O ATOM 2232 CB GLU A 281 13.305 -39.496 9.401 1.00 26.68 C ANISOU 2232 CB GLU A 281 3885 3074 3178 -167 313 -1174 C ATOM 2233 CG GLU A 281 14.790 -39.813 9.516 1.00 28.26 C ANISOU 2233 CG GLU A 281 4000 3244 3491 -50 119 -1128 C ATOM 2234 CD GLU A 281 15.691 -38.591 9.459 1.00 27.61 C ANISOU 2234 CD GLU A 281 3882 3456 3152 -98 583 -1301 C ATOM 2235 OE1 GLU A 281 15.196 -37.450 9.284 1.00 27.82 O ANISOU 2235 OE1 GLU A 281 4297 3358 2912 -132 562 -1415 O ATOM 2236 OE2 GLU A 281 16.914 -38.783 9.591 1.00 31.30 O ANISOU 2236 OE2 GLU A 281 3941 4157 3792 -60 178 -1857 O ATOM 2237 N THR A 282 13.946 -39.160 12.714 1.00 23.41 N ANISOU 2237 N THR A 282 3500 2444 2949 -210 44 -699 N ATOM 2238 CA THR A 282 14.251 -39.584 14.081 1.00 22.40 C ANISOU 2238 CA THR A 282 3433 2073 3004 122 127 -646 C ATOM 2239 C THR A 282 14.529 -38.272 14.834 1.00 18.73 C ANISOU 2239 C THR A 282 2869 1947 2298 89 215 -332 C ATOM 2240 O THR A 282 14.425 -37.198 14.236 1.00 19.48 O ANISOU 2240 O THR A 282 3267 1728 2405 13 210 -537 O ATOM 2241 CB THR A 282 15.446 -40.571 14.124 1.00 21.10 C ANISOU 2241 CB THR A 282 3292 1749 2975 -86 146 -696 C ATOM 2242 OG1 THR A 282 15.591 -41.116 15.446 1.00 23.50 O ANISOU 2242 OG1 THR A 282 3808 2023 3098 301 282 -554 O ATOM 2243 CG2 THR A 282 16.747 -39.906 13.681 1.00 22.30 C ANISOU 2243 CG2 THR A 282 2957 2298 3216 119 145 -500 C ATOM 2244 N LEU A 283 14.860 -38.326 16.124 1.00 17.26 N ANISOU 2244 N LEU A 283 2643 1555 2361 -7 158 -667 N ATOM 2245 CA LEU A 283 15.258 -37.090 16.805 1.00 15.43 C ANISOU 2245 CA LEU A 283 2210 1379 2272 19 103 -445 C ATOM 2246 C LEU A 283 16.696 -36.730 16.480 1.00 15.92 C ANISOU 2246 C LEU A 283 2231 1562 2252 189 320 -294 C ATOM 2247 O LEU A 283 17.566 -37.601 16.387 1.00 16.86 O ANISOU 2247 O LEU A 283 2365 1594 2446 321 180 -240 O ATOM 2248 CB LEU A 283 15.083 -37.169 18.325 1.00 16.62 C ANISOU 2248 CB LEU A 283 2317 1638 2359 -62 362 -184 C ATOM 2249 CG LEU A 283 13.705 -37.517 18.881 1.00 15.56 C ANISOU 2249 CG LEU A 283 2182 1645 2085 -86 180 -309 C ATOM 2250 CD1 LEU A 283 13.714 -37.392 20.397 1.00 16.38 C ANISOU 2250 CD1 LEU A 283 2370 1787 2065 -258 161 -275 C ATOM 2251 CD2 LEU A 283 12.596 -36.667 18.274 1.00 16.99 C ANISOU 2251 CD2 LEU A 283 2194 1677 2583 79 63 -476 C ATOM 2252 N TYR A 284 16.930 -35.440 16.288 1.00 15.66 N ANISOU 2252 N TYR A 284 2289 1561 2099 140 287 -361 N ATOM 2253 CA TYR A 284 18.253 -34.911 16.037 1.00 15.74 C ANISOU 2253 CA TYR A 284 2168 1631 2180 72 8 -269 C ATOM 2254 C TYR A 284 18.585 -33.977 17.194 1.00 14.48 C ANISOU 2254 C TYR A 284 1896 1579 2026 296 117 -253 C ATOM 2255 O TYR A 284 17.865 -32.999 17.425 1.00 15.29 O ANISOU 2255 O TYR A 284 1854 1984 1969 493 128 -371 O ATOM 2256 CB TYR A 284 18.250 -34.075 14.748 1.00 18.84 C ANISOU 2256 CB TYR A 284 2869 2258 2032 -140 145 -191 C ATOM 2257 CG TYR A 284 18.261 -34.831 13.422 1.00 21.05 C ANISOU 2257 CG TYR A 284 3009 2731 2255 -293 285 -505 C ATOM 2258 CD1 TYR A 284 17.414 -35.914 13.183 1.00 20.63 C ANISOU 2258 CD1 TYR A 284 3263 2168 2407 -87 254 -611 C ATOM 2259 CD2 TYR A 284 19.106 -34.425 12.389 1.00 25.13 C ANISOU 2259 CD2 TYR A 284 3966 3270 2310 -495 590 -504 C ATOM 2260 CE1 TYR A 284 17.437 -36.587 11.964 1.00 25.49 C ANISOU 2260 CE1 TYR A 284 3900 3199 2584 -286 381 -970 C ATOM 2261 CE2 TYR A 284 19.134 -35.088 11.173 1.00 27.96 C ANISOU 2261 CE2 TYR A 284 4499 3670 2451 -385 523 -720 C ATOM 2262 CZ TYR A 284 18.298 -36.164 10.963 1.00 28.28 C ANISOU 2262 CZ TYR A 284 4410 3655 2679 -338 387 -543 C ATOM 2263 OH TYR A 284 18.334 -36.804 9.748 1.00 33.40 O ANISOU 2263 OH TYR A 284 5427 4278 2983 -359 750 -921 O ATOM 2264 N ARG A 285 19.665 -34.261 17.915 1.00 13.43 N ANISOU 2264 N ARG A 285 1871 1473 1758 -8 145 -229 N ATOM 2265 CA ARG A 285 20.181 -33.324 18.904 1.00 11.62 C ANISOU 2265 CA ARG A 285 1356 1403 1655 124 149 -91 C ATOM 2266 C ARG A 285 21.279 -32.503 18.255 1.00 12.28 C ANISOU 2266 C ARG A 285 1621 1378 1664 117 306 -56 C ATOM 2267 O ARG A 285 22.273 -33.061 17.776 1.00 14.50 O ANISOU 2267 O ARG A 285 1833 1399 2275 230 535 -21 O ATOM 2268 CB ARG A 285 20.681 -34.075 20.132 1.00 13.31 C ANISOU 2268 CB ARG A 285 1712 1654 1690 381 40 -97 C ATOM 2269 CG ARG A 285 21.127 -33.186 21.276 1.00 12.84 C ANISOU 2269 CG ARG A 285 1686 1603 1589 199 -22 70 C ATOM 2270 CD ARG A 285 21.569 -34.008 22.475 1.00 14.80 C ANISOU 2270 CD ARG A 285 2032 1687 1903 415 -153 188 C ATOM 2271 NE ARG A 285 21.956 -33.143 23.585 1.00 14.00 N ANISOU 2271 NE ARG A 285 1902 1686 1729 495 0 219 N ATOM 2272 CZ ARG A 285 22.710 -33.530 24.610 1.00 13.82 C ANISOU 2272 CZ ARG A 285 1680 1647 1923 645 -3 199 C ATOM 2273 NH1 ARG A 285 23.181 -34.775 24.651 1.00 16.50 N ANISOU 2273 NH1 ARG A 285 2154 1741 2374 868 138 230 N ATOM 2274 NH2 ARG A 285 23.010 -32.668 25.575 1.00 14.05 N ANISOU 2274 NH2 ARG A 285 1819 1441 2077 231 195 290 N ATOM 2275 N ILE A 286 21.082 -31.185 18.226 1.00 11.96 N ANISOU 2275 N ILE A 286 1590 1381 1573 91 143 -7 N ATOM 2276 CA ILE A 286 21.992 -30.271 17.539 1.00 12.06 C ANISOU 2276 CA ILE A 286 1472 1492 1615 96 165 -51 C ATOM 2277 C ILE A 286 22.700 -29.398 18.563 1.00 11.52 C ANISOU 2277 C ILE A 286 1406 1302 1667 141 169 1 C ATOM 2278 O ILE A 286 22.067 -28.599 19.267 1.00 12.18 O ANISOU 2278 O ILE A 286 1451 1656 1519 256 164 -57 O ATOM 2279 CB ILE A 286 21.264 -29.404 16.487 1.00 12.23 C ANISOU 2279 CB ILE A 286 1749 1453 1444 29 114 -87 C ATOM 2280 CG1 ILE A 286 20.583 -30.292 15.427 1.00 12.99 C ANISOU 2280 CG1 ILE A 286 1837 1528 1571 119 -93 -77 C ATOM 2281 CG2 ILE A 286 22.230 -28.374 15.888 1.00 12.54 C ANISOU 2281 CG2 ILE A 286 1546 1619 1597 0 142 -164 C ATOM 2282 CD1 ILE A 286 19.734 -29.551 14.407 1.00 14.00 C ANISOU 2282 CD1 ILE A 286 1842 1797 1680 103 -34 168 C ATOM 2283 N ASP A 287 24.014 -29.588 18.655 1.00 11.21 N ANISOU 2283 N ASP A 287 1372 1402 1485 6 15 127 N ATOM 2284 CA ASP A 287 24.876 -28.827 19.540 1.00 11.78 C ANISOU 2284 CA ASP A 287 1489 1539 1446 75 -102 111 C ATOM 2285 C ASP A 287 25.809 -28.007 18.665 1.00 11.78 C ANISOU 2285 C ASP A 287 1520 1486 1467 111 15 16 C ATOM 2286 O ASP A 287 26.890 -28.485 18.291 1.00 12.36 O ANISOU 2286 O ASP A 287 1390 1719 1585 171 -48 139 O ATOM 2287 CB ASP A 287 25.686 -29.778 20.430 1.00 12.61 C ANISOU 2287 CB ASP A 287 1517 1727 1545 185 -83 193 C ATOM 2288 CG ASP A 287 26.725 -29.055 21.282 1.00 13.75 C ANISOU 2288 CG ASP A 287 1713 1780 1729 47 -154 232 C ATOM 2289 OD1 ASP A 287 26.617 -27.822 21.452 1.00 14.50 O ANISOU 2289 OD1 ASP A 287 2011 1870 1627 96 -325 -64 O ATOM 2290 OD2 ASP A 287 27.655 -29.729 21.786 1.00 15.35 O ANISOU 2290 OD2 ASP A 287 1834 1683 2316 129 -228 302 O ATOM 2291 N GLY A 288 25.400 -26.784 18.330 1.00 11.92 N ANISOU 2291 N GLY A 288 1513 1609 1407 127 -99 126 N ATOM 2292 CA GLY A 288 26.160 -25.958 17.399 1.00 12.59 C ANISOU 2292 CA GLY A 288 1795 1604 1382 124 85 84 C ATOM 2293 C GLY A 288 26.318 -26.644 16.052 1.00 11.72 C ANISOU 2293 C GLY A 288 1455 1546 1450 217 144 66 C ATOM 2294 O GLY A 288 25.336 -26.898 15.345 1.00 13.07 O ANISOU 2294 O GLY A 288 1615 1748 1600 130 91 33 O ATOM 2295 N ALA A 289 27.563 -26.972 15.711 1.00 12.61 N ANISOU 2295 N ALA A 289 1409 1734 1646 204 154 145 N ATOM 2296 CA ALA A 289 27.870 -27.620 14.439 1.00 13.35 C ANISOU 2296 CA ALA A 289 1565 1749 1758 249 310 90 C ATOM 2297 C ALA A 289 27.680 -29.131 14.483 1.00 14.06 C ANISOU 2297 C ALA A 289 1748 1788 1806 131 171 -17 C ATOM 2298 O ALA A 289 27.749 -29.778 13.435 1.00 16.58 O ANISOU 2298 O ALA A 289 2353 2003 1943 164 311 -185 O ATOM 2299 CB ALA A 289 29.296 -27.297 14.003 1.00 15.52 C ANISOU 2299 CB ALA A 289 1619 2198 2080 226 382 345 C ATOM 2300 N HIS A 290 27.424 -29.687 15.670 1.00 14.57 N ANISOU 2300 N HIS A 290 1656 1769 2108 148 238 247 N ATOM 2301 CA AHIS A 290 27.371 -31.146 15.869 0.50 15.48 C ANISOU 2301 CA AHIS A 290 1891 1739 2251 117 318 83 C ATOM 2302 CA BHIS A 290 27.358 -31.135 15.805 0.50 14.40 C ANISOU 2302 CA BHIS A 290 1732 1753 1984 252 200 165 C ATOM 2303 C HIS A 290 25.972 -31.703 15.891 1.00 14.94 C ANISOU 2303 C HIS A 290 1897 1728 2049 96 451 -21 C ATOM 2304 O HIS A 290 25.071 -31.108 16.475 1.00 16.53 O ANISOU 2304 O HIS A 290 1867 2096 2314 169 421 -283 O ATOM 2305 CB AHIS A 290 28.072 -31.542 17.171 0.50 17.75 C ANISOU 2305 CB AHIS A 290 2358 2048 2335 3 159 168 C ATOM 2306 CB BHIS A 290 28.181 -31.601 16.987 0.50 14.93 C ANISOU 2306 CB BHIS A 290 1612 1969 2089 160 143 242 C ATOM 2307 CG AHIS A 290 29.572 -31.335 17.162 0.50 21.97 C ANISOU 2307 CG AHIS A 290 2487 2620 3239 -374 161 24 C ATOM 2308 CG BHIS A 290 28.445 -33.076 16.970 0.50 15.04 C ANISOU 2308 CG BHIS A 290 1406 1975 2332 236 68 275 C ATOM 2309 ND1AHIS A 290 30.272 -31.137 16.032 0.50 25.58 N ANISOU 2309 ND1AHIS A 290 2778 3356 3584 44 538 -24 N ATOM 2310 ND1BHIS A 290 29.289 -33.643 16.090 0.50 17.40 N ANISOU 2310 ND1BHIS A 290 1705 2011 2894 555 337 388 N ATOM 2311 CD2AHIS A 290 30.501 -31.339 18.203 0.50 24.01 C ANISOU 2311 CD2AHIS A 290 2883 3169 3067 -388 159 -241 C ATOM 2312 CD2BHIS A 290 27.907 -34.113 17.731 0.50 15.41 C ANISOU 2312 CD2BHIS A 290 1623 2062 2169 243 -204 411 C ATOM 2313 CE1AHIS A 290 31.579 -30.995 16.333 0.50 25.30 C ANISOU 2313 CE1AHIS A 290 2929 3038 3644 -289 266 -249 C ATOM 2314 CE1BHIS A 290 29.319 -34.974 16.298 0.50 17.88 C ANISOU 2314 CE1BHIS A 290 1933 1964 2895 188 14 366 C ATOM 2315 NE2AHIS A 290 31.717 -31.122 17.661 0.50 26.54 N ANISOU 2315 NE2AHIS A 290 2664 3710 3707 -369 104 -367 N ATOM 2316 NE2BHIS A 290 28.475 -35.259 17.302 0.50 16.79 N ANISOU 2316 NE2BHIS A 290 1887 1994 2499 270 -122 262 N ATOM 2317 N LEU A 291 25.800 -32.887 15.309 1.00 16.40 N ANISOU 2317 N LEU A 291 2173 1727 2330 8 545 -41 N ATOM 2318 CA LEU A 291 24.533 -33.590 15.282 1.00 15.84 C ANISOU 2318 CA LEU A 291 2068 1606 2344 210 504 -6 C ATOM 2319 C LEU A 291 24.661 -34.997 15.900 1.00 15.89 C ANISOU 2319 C LEU A 291 2113 1583 2341 177 520 -3 C ATOM 2320 O LEU A 291 25.614 -35.730 15.616 1.00 17.52 O ANISOU 2320 O LEU A 291 2236 1815 2605 285 738 14 O ATOM 2321 CB LEU A 291 24.066 -33.698 13.829 1.00 19.77 C ANISOU 2321 CB LEU A 291 2686 2388 2435 53 280 72 C ATOM 2322 CG LEU A 291 22.866 -34.575 13.486 1.00 22.35 C ANISOU 2322 CG LEU A 291 2713 3066 2712 -70 204 -94 C ATOM 2323 CD1 LEU A 291 21.643 -34.068 14.234 1.00 23.34 C ANISOU 2323 CD1 LEU A 291 3059 2613 3195 -30 386 -389 C ATOM 2324 CD2 LEU A 291 22.664 -34.589 11.976 1.00 24.48 C ANISOU 2324 CD2 LEU A 291 3479 3135 2683 436 263 -428 C ATOM 2325 N THR A 292 23.699 -35.357 16.744 1.00 15.38 N ANISOU 2325 N THR A 292 2102 1298 2444 121 505 60 N ATOM 2326 CA THR A 292 23.560 -36.724 17.257 1.00 14.98 C ANISOU 2326 CA THR A 292 2154 1221 2315 183 642 -80 C ATOM 2327 C THR A 292 22.131 -37.188 17.010 1.00 15.25 C ANISOU 2327 C THR A 292 2149 1339 2306 151 530 123 C ATOM 2328 O THR A 292 21.190 -36.561 17.502 1.00 16.97 O ANISOU 2328 O THR A 292 2131 1574 2741 278 392 -174 O ATOM 2329 CB THR A 292 23.825 -36.787 18.777 1.00 16.70 C ANISOU 2329 CB THR A 292 2177 1777 2391 242 383 323 C ATOM 2330 OG1 THR A 292 25.121 -36.256 19.060 1.00 18.64 O ANISOU 2330 OG1 THR A 292 2153 2179 2749 254 209 521 O ATOM 2331 CG2 THR A 292 23.743 -38.227 19.298 1.00 19.14 C ANISOU 2331 CG2 THR A 292 2877 1789 2605 144 744 296 C ATOM 2332 N LYS A 293 21.967 -38.268 16.248 1.00 17.65 N ANISOU 2332 N LYS A 293 2517 1711 2476 108 549 -162 N ATOM 2333 CA LYS A 293 20.646 -38.854 16.022 1.00 17.83 C ANISOU 2333 CA LYS A 293 2452 1776 2544 171 585 25 C ATOM 2334 C LYS A 293 20.289 -39.812 17.167 1.00 16.98 C ANISOU 2334 C LYS A 293 2310 1602 2538 127 533 -71 C ATOM 2335 O LYS A 293 21.151 -40.512 17.697 1.00 19.82 O ANISOU 2335 O LYS A 293 2632 1602 3294 402 634 219 O ATOM 2336 CB LYS A 293 20.580 -39.561 14.662 1.00 23.12 C ANISOU 2336 CB LYS A 293 3613 2337 2833 -378 571 -337 C ATOM 2337 CG LYS A 293 20.665 -38.628 13.453 1.00 25.36 C ANISOU 2337 CG LYS A 293 3962 3298 2374 -157 655 -360 C ATOM 2338 CD LYS A 293 20.711 -39.399 12.138 1.00 31.78 C ANISOU 2338 CD LYS A 293 4928 4450 2696 -305 878 -961 C ATOM 2339 CE LYS A 293 22.097 -39.978 11.876 1.00 37.26 C ANISOU 2339 CE LYS A 293 5086 5302 3766 -91 1172 -778 C ATOM 2340 NZ LYS A 293 22.149 -40.840 10.660 1.00 42.72 N ANISOU 2340 NZ LYS A 293 6667 6161 3403 -835 899 -751 N ATOM 2341 N MET A 294 19.016 -39.825 17.551 1.00 16.01 N ANISOU 2341 N MET A 294 2310 1398 2374 154 631 89 N ATOM 2342 CA MET A 294 18.545 -40.658 18.669 1.00 16.36 C ANISOU 2342 CA MET A 294 2390 1385 2438 314 464 284 C ATOM 2343 C MET A 294 17.037 -40.879 18.582 1.00 17.23 C ANISOU 2343 C MET A 294 2438 1442 2667 86 625 -131 C ATOM 2344 O MET A 294 16.310 -40.008 18.115 1.00 19.19 O ANISOU 2344 O MET A 294 2360 1886 3044 51 344 -6 O ATOM 2345 CB MET A 294 18.902 -40.004 20.003 1.00 17.65 C ANISOU 2345 CB MET A 294 2506 1797 2400 379 269 307 C ATOM 2346 CG MET A 294 18.378 -38.581 20.149 1.00 17.63 C ANISOU 2346 CG MET A 294 2460 2043 2193 680 175 133 C ATOM 2347 SD MET A 294 19.077 -37.673 21.542 1.00 18.32 S ANISOU 2347 SD MET A 294 2245 2555 2157 316 160 239 S ATOM 2348 CE MET A 294 20.797 -37.580 21.076 1.00 17.54 C ANISOU 2348 CE MET A 294 2164 2135 2362 446 229 429 C ATOM 2349 N SER A 295 16.567 -42.038 19.042 1.00 19.59 N ANISOU 2349 N SER A 295 2784 1621 3039 -117 958 -157 N ATOM 2350 CA SER A 295 15.139 -42.361 18.964 1.00 20.60 C ANISOU 2350 CA SER A 295 2863 1759 3204 -269 676 -245 C ATOM 2351 C SER A 295 14.312 -41.636 20.028 1.00 19.93 C ANISOU 2351 C SER A 295 2937 1760 2873 -38 423 -109 C ATOM 2352 O SER A 295 13.111 -41.447 19.862 1.00 21.77 O ANISOU 2352 O SER A 295 2882 2193 3193 -381 392 -304 O ATOM 2353 CB SER A 295 14.910 -43.873 19.043 1.00 23.23 C ANISOU 2353 CB SER A 295 3058 1742 4024 -266 548 -277 C ATOM 2354 OG SER A 295 15.321 -44.386 20.299 1.00 28.54 O ANISOU 2354 OG SER A 295 3970 2634 4239 -97 392 -117 O ATOM 2355 N GLU A 296 14.970 -41.240 21.114 1.00 18.62 N ANISOU 2355 N GLU A 296 2880 1472 2723 -69 419 71 N ATOM 2356 CA GLU A 296 14.349 -40.467 22.193 1.00 18.67 C ANISOU 2356 CA GLU A 296 2662 1711 2719 -49 233 -36 C ATOM 2357 C GLU A 296 15.443 -39.678 22.918 1.00 17.95 C ANISOU 2357 C GLU A 296 2286 1653 2881 300 150 -103 C ATOM 2358 O GLU A 296 16.641 -39.983 22.773 1.00 17.82 O ANISOU 2358 O GLU A 296 2391 1607 2770 366 373 119 O ATOM 2359 CB GLU A 296 13.554 -41.369 23.154 1.00 22.44 C ANISOU 2359 CB GLU A 296 3115 2529 2879 -359 529 -16 C ATOM 2360 CG GLU A 296 14.378 -42.399 23.909 1.00 27.12 C ANISOU 2360 CG GLU A 296 3660 3180 3463 -248 527 635 C ATOM 2361 CD GLU A 296 13.564 -43.222 24.905 1.00 30.41 C ANISOU 2361 CD GLU A 296 3987 3361 4203 -672 62 1430 C ATOM 2362 OE1 GLU A 296 12.334 -43.398 24.725 1.00 32.24 O ANISOU 2362 OE1 GLU A 296 4085 3308 4853 -659 -99 1445 O ATOM 2363 OE2 GLU A 296 14.171 -43.708 25.879 1.00 35.21 O ANISOU 2363 OE2 GLU A 296 4556 4705 4114 -158 -7 1532 O ATOM 2364 N TYR A 297 15.045 -38.636 23.647 1.00 17.67 N ANISOU 2364 N TYR A 297 2508 1866 2339 31 479 -117 N ATOM 2365 CA TYR A 297 15.997 -37.866 24.432 1.00 16.13 C ANISOU 2365 CA TYR A 297 2332 1527 2268 443 163 175 C ATOM 2366 C TYR A 297 15.488 -37.700 25.861 1.00 16.36 C ANISOU 2366 C TYR A 297 2210 1726 2278 301 162 55 C ATOM 2367 O TYR A 297 14.373 -37.232 26.074 1.00 19.85 O ANISOU 2367 O TYR A 297 2267 2528 2745 595 151 125 O ATOM 2368 CB TYR A 297 16.297 -36.486 23.813 1.00 15.96 C ANISOU 2368 CB TYR A 297 2242 1513 2307 297 -92 183 C ATOM 2369 CG TYR A 297 17.189 -35.667 24.724 1.00 15.22 C ANISOU 2369 CG TYR A 297 2131 1545 2106 153 124 157 C ATOM 2370 CD1 TYR A 297 18.560 -35.920 24.799 1.00 16.91 C ANISOU 2370 CD1 TYR A 297 2126 2110 2189 144 141 -7 C ATOM 2371 CD2 TYR A 297 16.652 -34.684 25.571 1.00 14.94 C ANISOU 2371 CD2 TYR A 297 2272 1421 1982 255 76 309 C ATOM 2372 CE1 TYR A 297 19.379 -35.190 25.655 1.00 15.60 C ANISOU 2372 CE1 TYR A 297 2330 1622 1974 -35 229 241 C ATOM 2373 CE2 TYR A 297 17.463 -33.960 26.437 1.00 15.38 C ANISOU 2373 CE2 TYR A 297 2117 1436 2290 173 -15 426 C ATOM 2374 CZ TYR A 297 18.822 -34.217 26.471 1.00 15.14 C ANISOU 2374 CZ TYR A 297 2137 1528 2087 195 -37 345 C ATOM 2375 OH TYR A 297 19.631 -33.524 27.337 1.00 15.48 O ANISOU 2375 OH TYR A 297 2219 1584 2078 200 48 169 O ATOM 2376 N LYS A 298 16.315 -38.069 26.832 1.00 16.96 N ANISOU 2376 N LYS A 298 2430 1711 2301 155 107 227 N ATOM 2377 CA LYS A 298 15.997 -37.831 28.229 1.00 16.86 C ANISOU 2377 CA LYS A 298 2556 1595 2254 0 -7 235 C ATOM 2378 C LYS A 298 17.077 -36.930 28.814 1.00 16.05 C ANISOU 2378 C LYS A 298 2288 1586 2222 214 63 108 C ATOM 2379 O LYS A 298 18.256 -37.255 28.760 1.00 19.18 O ANISOU 2379 O LYS A 298 2327 1992 2968 314 -18 132 O ATOM 2380 CB LYS A 298 15.885 -39.155 28.998 1.00 21.18 C ANISOU 2380 CB LYS A 298 3623 1965 2457 268 -38 655 C ATOM 2381 CG LYS A 298 15.416 -38.987 30.437 1.00 26.47 C ANISOU 2381 CG LYS A 298 4678 2742 2637 -79 246 457 C ATOM 2382 CD LYS A 298 15.425 -40.311 31.190 1.00 31.58 C ANISOU 2382 CD LYS A 298 5313 3064 3619 377 260 985 C ATOM 2383 CE LYS A 298 15.911 -40.142 32.625 1.00 36.28 C ANISOU 2383 CE LYS A 298 6141 4213 3428 174 534 959 C ATOM 2384 NZ LYS A 298 15.115 -39.154 33.406 1.00 42.28 N ANISOU 2384 NZ LYS A 298 7162 4213 4690 571 1145 952 N ATOM 2385 N GLY A 299 16.668 -35.790 29.358 1.00 14.35 N ANISOU 2385 N GLY A 299 2039 1518 1894 41 185 185 N ATOM 2386 CA GLY A 299 17.603 -34.839 29.939 1.00 13.90 C ANISOU 2386 CA GLY A 299 1770 1453 2058 194 156 281 C ATOM 2387 C GLY A 299 16.898 -33.599 30.431 1.00 12.50 C ANISOU 2387 C GLY A 299 1558 1455 1735 240 -16 422 C ATOM 2388 O GLY A 299 15.659 -33.578 30.517 1.00 12.51 O ANISOU 2388 O GLY A 299 1528 1262 1961 142 64 346 O ATOM 2389 N PRO A 300 17.673 -32.547 30.739 1.00 12.54 N ANISOU 2389 N PRO A 300 1395 1709 1659 184 -34 310 N ATOM 2390 CA PRO A 300 17.125 -31.368 31.419 1.00 11.77 C ANISOU 2390 CA PRO A 300 1438 1657 1377 137 -114 329 C ATOM 2391 C PRO A 300 16.445 -30.378 30.454 1.00 10.67 C ANISOU 2391 C PRO A 300 1378 1410 1265 78 -116 193 C ATOM 2392 O PRO A 300 16.875 -29.218 30.288 1.00 11.51 O ANISOU 2392 O PRO A 300 1500 1446 1425 18 41 63 O ATOM 2393 CB PRO A 300 18.363 -30.767 32.100 1.00 12.24 C ANISOU 2393 CB PRO A 300 1381 1986 1283 153 -131 281 C ATOM 2394 CG PRO A 300 19.482 -31.125 31.170 1.00 12.74 C ANISOU 2394 CG PRO A 300 1478 1802 1559 201 -23 220 C ATOM 2395 CD PRO A 300 19.149 -32.498 30.648 1.00 13.47 C ANISOU 2395 CD PRO A 300 1396 1811 1909 187 -106 214 C ATOM 2396 N VAL A 301 15.362 -30.842 29.839 1.00 10.62 N ANISOU 2396 N VAL A 301 1350 1425 1258 140 -152 198 N ATOM 2397 CA VAL A 301 14.604 -30.046 28.880 1.00 10.68 C ANISOU 2397 CA VAL A 301 1301 1321 1434 211 -165 175 C ATOM 2398 C VAL A 301 14.016 -28.833 29.599 1.00 10.36 C ANISOU 2398 C VAL A 301 1332 1414 1191 87 0 147 C ATOM 2399 O VAL A 301 13.606 -28.936 30.764 1.00 10.89 O ANISOU 2399 O VAL A 301 1344 1511 1280 213 83 307 O ATOM 2400 CB VAL A 301 13.499 -30.897 28.230 1.00 10.98 C ANISOU 2400 CB VAL A 301 1570 1220 1381 132 -139 108 C ATOM 2401 CG1 VAL A 301 12.723 -30.085 27.214 1.00 12.14 C ANISOU 2401 CG1 VAL A 301 1716 1594 1302 132 -241 169 C ATOM 2402 CG2 VAL A 301 14.093 -32.134 27.558 1.00 12.30 C ANISOU 2402 CG2 VAL A 301 1873 1289 1511 132 -145 -57 C ATOM 2403 N THR A 302 14.023 -27.679 28.928 1.00 9.82 N ANISOU 2403 N THR A 302 1228 1182 1319 78 -162 -14 N ATOM 2404 CA THR A 302 13.486 -26.464 29.527 1.00 9.52 C ANISOU 2404 CA THR A 302 1288 1186 1141 51 -112 29 C ATOM 2405 C THR A 302 12.465 -25.724 28.651 1.00 8.84 C ANISOU 2405 C THR A 302 1152 1012 1192 61 12 37 C ATOM 2406 O THR A 302 11.649 -24.965 29.177 1.00 9.69 O ANISOU 2406 O THR A 302 1239 1264 1178 164 57 1 O ATOM 2407 CB THR A 302 14.623 -25.544 30.035 1.00 10.59 C ANISOU 2407 CB THR A 302 1463 1289 1271 -149 61 -58 C ATOM 2408 OG1 THR A 302 14.081 -24.507 30.859 1.00 11.67 O ANISOU 2408 OG1 THR A 302 1530 1534 1371 222 -102 -83 O ATOM 2409 CG2 THR A 302 15.447 -24.957 28.867 1.00 10.72 C ANISOU 2409 CG2 THR A 302 1419 1208 1445 -74 111 92 C ATOM 2410 N ASP A 303 12.500 -25.937 27.331 1.00 9.43 N ANISOU 2410 N ASP A 303 1204 1191 1187 55 -77 48 N ATOM 2411 CA ASP A 303 11.471 -25.369 26.439 1.00 10.02 C ANISOU 2411 CA ASP A 303 1429 1186 1192 90 -129 94 C ATOM 2412 C ASP A 303 11.090 -26.419 25.423 1.00 9.62 C ANISOU 2412 C ASP A 303 1305 1363 984 110 -19 56 C ATOM 2413 O ASP A 303 11.972 -27.081 24.862 1.00 10.89 O ANISOU 2413 O ASP A 303 1224 1543 1369 146 -27 -126 O ATOM 2414 CB ASP A 303 11.987 -24.136 25.672 1.00 10.65 C ANISOU 2414 CB ASP A 303 1439 1259 1348 12 -51 111 C ATOM 2415 CG ASP A 303 12.600 -23.094 26.574 1.00 10.23 C ANISOU 2415 CG ASP A 303 1281 1175 1430 120 -127 152 C ATOM 2416 OD1 ASP A 303 11.871 -22.452 27.351 1.00 10.77 O ANISOU 2416 OD1 ASP A 303 1405 1444 1241 42 -38 119 O ATOM 2417 OD2 ASP A 303 13.825 -22.900 26.483 1.00 12.56 O ANISOU 2417 OD2 ASP A 303 1232 1579 1960 67 -83 -10 O ATOM 2418 N VAL A 304 9.790 -26.582 25.186 1.00 10.01 N ANISOU 2418 N VAL A 304 1355 1191 1258 97 -54 -208 N ATOM 2419 CA VAL A 304 9.309 -27.476 24.134 1.00 9.90 C ANISOU 2419 CA VAL A 304 1297 1221 1240 49 -110 -148 C ATOM 2420 C VAL A 304 8.322 -26.699 23.261 1.00 9.48 C ANISOU 2420 C VAL A 304 1118 1231 1252 45 -51 -151 C ATOM 2421 O VAL A 304 7.411 -26.030 23.775 1.00 10.19 O ANISOU 2421 O VAL A 304 1299 1352 1218 125 29 -204 O ATOM 2422 CB VAL A 304 8.624 -28.740 24.702 1.00 10.07 C ANISOU 2422 CB VAL A 304 1311 1278 1235 72 -133 -56 C ATOM 2423 CG1 VAL A 304 8.243 -29.672 23.565 1.00 11.02 C ANISOU 2423 CG1 VAL A 304 1398 1443 1346 -43 4 -232 C ATOM 2424 CG2 VAL A 304 9.547 -29.491 25.657 1.00 11.03 C ANISOU 2424 CG2 VAL A 304 1490 1301 1398 67 -189 112 C ATOM 2425 N PHE A 305 8.497 -26.810 21.946 1.00 9.71 N ANISOU 2425 N PHE A 305 1246 1219 1221 -36 -160 -87 N ATOM 2426 CA PHE A 305 7.630 -26.163 20.975 1.00 10.10 C ANISOU 2426 CA PHE A 305 1312 1263 1263 -120 -112 70 C ATOM 2427 C PHE A 305 6.712 -27.175 20.333 1.00 9.48 C ANISOU 2427 C PHE A 305 1236 1243 1120 -23 -23 -28 C ATOM 2428 O PHE A 305 7.125 -28.314 20.072 1.00 10.42 O ANISOU 2428 O PHE A 305 1392 1185 1381 10 -145 12 O ATOM 2429 CB PHE A 305 8.471 -25.507 19.884 1.00 10.10 C ANISOU 2429 CB PHE A 305 1307 1303 1226 -127 -81 45 C ATOM 2430 CG PHE A 305 9.376 -24.416 20.375 1.00 9.66 C ANISOU 2430 CG PHE A 305 1317 1262 1090 -95 18 -73 C ATOM 2431 CD1 PHE A 305 8.997 -23.071 20.265 1.00 10.05 C ANISOU 2431 CD1 PHE A 305 1460 1245 1112 -183 87 -53 C ATOM 2432 CD2 PHE A 305 10.625 -24.724 20.921 1.00 10.03 C ANISOU 2432 CD2 PHE A 305 1308 1309 1193 -146 -20 -144 C ATOM 2433 CE1 PHE A 305 9.846 -22.062 20.695 1.00 11.25 C ANISOU 2433 CE1 PHE A 305 1529 1543 1202 -349 66 -113 C ATOM 2434 CE2 PHE A 305 11.470 -23.714 21.365 1.00 10.74 C ANISOU 2434 CE2 PHE A 305 1434 1444 1201 -239 5 -218 C ATOM 2435 CZ PHE A 305 11.081 -22.388 21.244 1.00 11.46 C ANISOU 2435 CZ PHE A 305 1506 1509 1339 -149 176 -62 C ATOM 2436 N TYR A 306 5.472 -26.753 20.079 1.00 9.35 N ANISOU 2436 N TYR A 306 1145 1247 1159 -147 -95 -22 N ATOM 2437 CA TYR A 306 4.456 -27.612 19.469 1.00 10.55 C ANISOU 2437 CA TYR A 306 1170 1460 1378 -215 -126 -65 C ATOM 2438 C TYR A 306 3.787 -26.841 18.343 1.00 11.07 C ANISOU 2438 C TYR A 306 1416 1331 1459 -38 -119 -79 C ATOM 2439 O TYR A 306 3.525 -25.649 18.474 1.00 10.98 O ANISOU 2439 O TYR A 306 1409 1357 1404 -37 -66 -9 O ATOM 2440 CB TYR A 306 3.390 -28.008 20.498 1.00 11.01 C ANISOU 2440 CB TYR A 306 1321 1466 1396 -166 -62 44 C ATOM 2441 CG TYR A 306 3.917 -28.715 21.725 1.00 10.18 C ANISOU 2441 CG TYR A 306 1253 1247 1364 -84 40 -1 C ATOM 2442 CD1 TYR A 306 3.876 -30.112 21.815 1.00 10.59 C ANISOU 2442 CD1 TYR A 306 1233 1266 1523 -248 -59 -9 C ATOM 2443 CD2 TYR A 306 4.429 -27.992 22.810 1.00 10.47 C ANISOU 2443 CD2 TYR A 306 1171 1438 1368 -29 101 -100 C ATOM 2444 CE1 TYR A 306 4.359 -30.774 22.938 1.00 10.47 C ANISOU 2444 CE1 TYR A 306 1308 1283 1385 -97 34 -89 C ATOM 2445 CE2 TYR A 306 4.901 -28.638 23.944 1.00 10.73 C ANISOU 2445 CE2 TYR A 306 1274 1358 1445 44 139 -87 C ATOM 2446 CZ TYR A 306 4.850 -30.030 24.016 1.00 10.33 C ANISOU 2446 CZ TYR A 306 1216 1308 1399 -40 -57 -63 C ATOM 2447 OH TYR A 306 5.307 -30.698 25.135 1.00 11.63 O ANISOU 2447 OH TYR A 306 1468 1505 1443 -101 -34 101 O ATOM 2448 N LYS A 307 3.489 -27.535 17.245 1.00 11.50 N ANISOU 2448 N LYS A 307 1525 1559 1285 -39 -80 -53 N ATOM 2449 CA LYS A 307 2.700 -26.946 16.171 1.00 12.02 C ANISOU 2449 CA LYS A 307 1494 1712 1358 55 -142 -94 C ATOM 2450 C LYS A 307 1.247 -26.773 16.610 1.00 12.47 C ANISOU 2450 C LYS A 307 1389 1666 1680 25 -247 -10 C ATOM 2451 O LYS A 307 0.729 -27.570 17.397 1.00 14.45 O ANISOU 2451 O LYS A 307 1688 1929 1871 -60 -111 61 O ATOM 2452 CB LYS A 307 2.759 -27.837 14.925 1.00 15.55 C ANISOU 2452 CB LYS A 307 2262 2133 1512 241 -196 -374 C ATOM 2453 CG LYS A 307 2.208 -27.188 13.651 1.00 18.60 C ANISOU 2453 CG LYS A 307 2572 2734 1758 346 -575 -336 C ATOM 2454 CD LYS A 307 2.402 -28.078 12.431 1.00 22.85 C ANISOU 2454 CD LYS A 307 3319 2852 2511 343 -319 -790 C ATOM 2455 CE LYS A 307 2.224 -27.292 11.140 1.00 31.21 C ANISOU 2455 CE LYS A 307 4252 4206 3399 -32 -316 359 C ATOM 2456 NZ LYS A 307 3.459 -26.532 10.799 1.00 40.32 N ANISOU 2456 NZ LYS A 307 5087 4930 5302 -658 324 239 N ATOM 2457 N GLU A 308 0.594 -25.732 16.098 1.00 11.42 N ANISOU 2457 N GLU A 308 1301 1566 1469 73 -91 -161 N ATOM 2458 CA GLU A 308 -0.816 -25.485 16.389 1.00 12.28 C ANISOU 2458 CA GLU A 308 1331 1884 1447 80 -75 -24 C ATOM 2459 C GLU A 308 -1.477 -24.854 15.170 1.00 12.84 C ANISOU 2459 C GLU A 308 1511 1812 1553 25 -94 107 C ATOM 2460 O GLU A 308 -0.796 -24.344 14.274 1.00 12.96 O ANISOU 2460 O GLU A 308 1786 1711 1424 -225 -96 -138 O ATOM 2461 CB GLU A 308 -0.965 -24.584 17.641 1.00 11.42 C ANISOU 2461 CB GLU A 308 1335 1738 1265 -51 -15 100 C ATOM 2462 CG GLU A 308 -2.399 -24.387 18.146 1.00 12.02 C ANISOU 2462 CG GLU A 308 1292 1663 1608 -107 -42 206 C ATOM 2463 CD GLU A 308 -3.108 -25.709 18.368 1.00 12.04 C ANISOU 2463 CD GLU A 308 1590 1672 1309 -213 60 62 C ATOM 2464 OE1 GLU A 308 -3.766 -26.190 17.420 1.00 12.95 O ANISOU 2464 OE1 GLU A 308 1668 1914 1339 -166 -60 106 O ATOM 2465 OE2 GLU A 308 -2.984 -26.277 19.477 1.00 13.02 O ANISOU 2465 OE2 GLU A 308 1548 1870 1527 -87 -55 244 O ATOM 2466 N THR A 309 -2.802 -24.952 15.116 1.00 12.63 N ANISOU 2466 N THR A 309 1529 1812 1457 -61 -118 41 N ATOM 2467 CA THR A 309 -3.607 -24.164 14.193 1.00 13.89 C ANISOU 2467 CA THR A 309 1603 2086 1589 20 -63 205 C ATOM 2468 C THR A 309 -4.750 -23.573 15.013 1.00 12.89 C ANISOU 2468 C THR A 309 1482 1804 1609 -88 -34 305 C ATOM 2469 O THR A 309 -4.744 -22.382 15.349 1.00 13.40 O ANISOU 2469 O THR A 309 1697 1830 1564 -218 -268 287 O ATOM 2470 CB THR A 309 -4.134 -25.008 13.009 1.00 15.14 C ANISOU 2470 CB THR A 309 1498 2420 1833 -19 -27 -38 C ATOM 2471 OG1 THR A 309 -4.790 -26.191 13.498 1.00 18.53 O ANISOU 2471 OG1 THR A 309 2122 2534 2384 -302 -96 -59 O ATOM 2472 CG2 THR A 309 -2.987 -25.404 12.088 1.00 16.74 C ANISOU 2472 CG2 THR A 309 1867 2912 1578 -24 102 -214 C ATOM 2473 N SER A 310 -5.704 -24.426 15.373 1.00 12.31 N ANISOU 2473 N SER A 310 1397 1854 1423 -162 -94 123 N ATOM 2474 CA SER A 310 -6.802 -24.053 16.261 1.00 11.76 C ANISOU 2474 CA SER A 310 1488 1693 1285 -37 -122 166 C ATOM 2475 C SER A 310 -7.105 -25.256 17.140 1.00 11.67 C ANISOU 2475 C SER A 310 1580 1607 1246 -42 30 45 C ATOM 2476 O SER A 310 -7.245 -26.370 16.638 1.00 14.37 O ANISOU 2476 O SER A 310 2214 1705 1540 -162 -104 -37 O ATOM 2477 CB SER A 310 -8.047 -23.652 15.445 1.00 14.27 C ANISOU 2477 CB SER A 310 1513 2054 1853 200 -80 667 C ATOM 2478 OG SER A 310 -9.174 -23.422 16.286 1.00 19.37 O ANISOU 2478 OG SER A 310 1951 3028 2378 64 366 577 O ATOM 2479 N TYR A 311 -7.195 -25.028 18.450 1.00 10.45 N ANISOU 2479 N TYR A 311 1240 1537 1193 -12 79 173 N ATOM 2480 CA TYR A 311 -7.548 -26.073 19.413 1.00 10.74 C ANISOU 2480 CA TYR A 311 1238 1502 1338 -44 -49 194 C ATOM 2481 C TYR A 311 -8.718 -25.599 20.252 1.00 10.58 C ANISOU 2481 C TYR A 311 1293 1359 1367 -10 -86 59 C ATOM 2482 O TYR A 311 -8.722 -24.471 20.733 1.00 10.83 O ANISOU 2482 O TYR A 311 1245 1278 1593 -28 -125 56 O ATOM 2483 CB TYR A 311 -6.350 -26.383 20.327 1.00 11.54 C ANISOU 2483 CB TYR A 311 1409 1629 1347 -96 -194 297 C ATOM 2484 CG TYR A 311 -6.722 -27.255 21.513 1.00 10.86 C ANISOU 2484 CG TYR A 311 1315 1483 1325 -194 -114 155 C ATOM 2485 CD1 TYR A 311 -6.765 -28.646 21.385 1.00 11.50 C ANISOU 2485 CD1 TYR A 311 1426 1426 1516 -140 -192 323 C ATOM 2486 CD2 TYR A 311 -7.063 -26.697 22.746 1.00 10.73 C ANISOU 2486 CD2 TYR A 311 1260 1453 1363 -88 -126 151 C ATOM 2487 CE1 TYR A 311 -7.139 -29.458 22.439 1.00 10.69 C ANISOU 2487 CE1 TYR A 311 1334 1504 1222 -171 -146 115 C ATOM 2488 CE2 TYR A 311 -7.421 -27.506 23.827 1.00 10.57 C ANISOU 2488 CE2 TYR A 311 1138 1433 1446 -55 -93 194 C ATOM 2489 CZ TYR A 311 -7.456 -28.884 23.668 1.00 10.52 C ANISOU 2489 CZ TYR A 311 1311 1441 1244 -141 -90 137 C ATOM 2490 OH TYR A 311 -7.800 -29.715 24.707 1.00 11.33 O ANISOU 2490 OH TYR A 311 1499 1487 1315 -130 -85 198 O ATOM 2491 N THR A 312 -9.708 -26.464 20.420 1.00 10.66 N ANISOU 2491 N THR A 312 1208 1521 1319 -19 -146 243 N ATOM 2492 CA THR A 312 -10.812 -26.213 21.337 1.00 10.95 C ANISOU 2492 CA THR A 312 1240 1454 1465 94 -93 255 C ATOM 2493 C THR A 312 -10.968 -27.399 22.270 1.00 10.24 C ANISOU 2493 C THR A 312 1219 1369 1300 -11 -116 130 C ATOM 2494 O THR A 312 -10.961 -28.545 21.822 1.00 11.42 O ANISOU 2494 O THR A 312 1416 1384 1537 -28 -68 85 O ATOM 2495 CB THR A 312 -12.130 -25.994 20.565 1.00 12.03 C ANISOU 2495 CB THR A 312 1202 1735 1632 154 -70 495 C ATOM 2496 OG1 THR A 312 -11.963 -24.889 19.670 1.00 12.92 O ANISOU 2496 OG1 THR A 312 1583 1682 1642 134 -106 470 O ATOM 2497 CG2 THR A 312 -13.274 -25.681 21.524 1.00 13.28 C ANISOU 2497 CG2 THR A 312 1289 1977 1777 121 9 306 C ATOM 2498 N THR A 313 -11.110 -27.114 23.559 1.00 9.80 N ANISOU 2498 N THR A 313 1053 1362 1307 -45 54 240 N ATOM 2499 CA THR A 313 -11.238 -28.146 24.591 1.00 9.99 C ANISOU 2499 CA THR A 313 1238 1138 1418 -137 -18 159 C ATOM 2500 C THR A 313 -12.503 -28.986 24.423 1.00 10.64 C ANISOU 2500 C THR A 313 1209 1262 1568 -106 -179 94 C ATOM 2501 O THR A 313 -13.500 -28.544 23.837 1.00 11.32 O ANISOU 2501 O THR A 313 1292 1467 1541 0 -177 120 O ATOM 2502 CB THR A 313 -11.245 -27.517 26.001 1.00 11.18 C ANISOU 2502 CB THR A 313 1460 1380 1409 -42 -159 125 C ATOM 2503 OG1 THR A 313 -11.108 -28.543 26.990 1.00 11.39 O ANISOU 2503 OG1 THR A 313 1389 1292 1645 -258 -142 232 O ATOM 2504 CG2 THR A 313 -12.538 -26.749 26.261 1.00 12.27 C ANISOU 2504 CG2 THR A 313 1398 1561 1703 -94 -28 8 C ATOM 2505 N THR A 314 -12.446 -30.196 24.964 1.00 10.30 N ANISOU 2505 N THR A 314 1276 1272 1364 -272 -123 129 N ATOM 2506 CA THR A 314 -13.637 -31.028 25.125 1.00 10.81 C ANISOU 2506 CA THR A 314 1246 1269 1589 -227 0 183 C ATOM 2507 C THR A 314 -14.179 -30.971 26.550 1.00 11.46 C ANISOU 2507 C THR A 314 1402 1431 1521 -118 -59 70 C ATOM 2508 O THR A 314 -15.259 -31.519 26.826 1.00 12.65 O ANISOU 2508 O THR A 314 1574 1697 1535 -298 87 170 O ATOM 2509 CB THR A 314 -13.370 -32.504 24.770 1.00 10.93 C ANISOU 2509 CB THR A 314 1558 1341 1253 -107 -115 81 C ATOM 2510 OG1 THR A 314 -12.452 -33.084 25.712 1.00 12.38 O ANISOU 2510 OG1 THR A 314 1687 1316 1698 6 -146 263 O ATOM 2511 CG2 THR A 314 -12.848 -32.639 23.349 1.00 12.32 C ANISOU 2511 CG2 THR A 314 1669 1616 1396 -200 33 -170 C ATOM 2512 N ILE A 315 -13.457 -30.318 27.461 1.00 10.77 N ANISOU 2512 N ILE A 315 1470 1354 1265 -94 -18 236 N ATOM 2513 CA ILE A 315 -13.878 -30.252 28.862 1.00 11.67 C ANISOU 2513 CA ILE A 315 1480 1661 1293 -83 -30 -7 C ATOM 2514 C ILE A 315 -15.131 -29.383 29.013 1.00 11.22 C ANISOU 2514 C ILE A 315 1481 1573 1209 -63 -80 170 C ATOM 2515 O ILE A 315 -15.206 -28.296 28.435 1.00 13.07 O ANISOU 2515 O ILE A 315 1849 1525 1593 -48 -15 237 O ATOM 2516 CB ILE A 315 -12.738 -29.718 29.756 1.00 12.41 C ANISOU 2516 CB ILE A 315 1475 1747 1493 -189 -21 -54 C ATOM 2517 CG1 ILE A 315 -11.585 -30.722 29.776 1.00 13.22 C ANISOU 2517 CG1 ILE A 315 1375 1776 1871 -236 -100 -79 C ATOM 2518 CG2 ILE A 315 -13.240 -29.456 31.178 1.00 12.73 C ANISOU 2518 CG2 ILE A 315 1690 1722 1423 -203 61 130 C ATOM 2519 CD1 ILE A 315 -10.299 -30.165 30.354 1.00 14.24 C ANISOU 2519 CD1 ILE A 315 1475 2022 1913 -385 -192 12 C ATOM 2520 N LYS A 316 -16.096 -29.864 29.796 1.00 12.99 N ANISOU 2520 N LYS A 316 1409 1868 1656 9 150 101 N ATOM 2521 CA LYS A 316 -17.360 -29.155 30.011 1.00 14.52 C ANISOU 2521 CA LYS A 316 1558 2184 1773 160 293 56 C ATOM 2522 C LYS A 316 -17.359 -28.488 31.383 1.00 14.45 C ANISOU 2522 C LYS A 316 1685 2104 1701 219 96 156 C ATOM 2523 O LYS A 316 -16.648 -28.933 32.294 1.00 17.92 O ANISOU 2523 O LYS A 316 1928 2824 2056 629 54 387 O ATOM 2524 CB LYS A 316 -18.553 -30.129 29.926 1.00 17.61 C ANISOU 2524 CB LYS A 316 1659 2707 2325 -71 202 -81 C ATOM 2525 CG LYS A 316 -18.829 -30.685 28.539 1.00 22.83 C ANISOU 2525 CG LYS A 316 2665 3869 2140 441 161 -158 C ATOM 2526 CD LYS A 316 -19.873 -29.853 27.820 1.00 22.11 C ANISOU 2526 CD LYS A 316 2970 3487 1941 737 257 -416 C ATOM 2527 CE LYS A 316 -20.113 -30.331 26.398 1.00 20.37 C ANISOU 2527 CE LYS A 316 2075 3556 2109 426 13 -494 C ATOM 2528 NZ LYS A 316 -21.311 -31.211 26.265 1.00 21.71 N ANISOU 2528 NZ LYS A 316 2821 3164 2260 47 81 63 N ATOM 2529 N PRO A 317 -18.166 -27.424 31.546 1.00 15.69 N ANISOU 2529 N PRO A 317 1645 2391 1923 314 209 68 N ATOM 2530 CA PRO A 317 -18.322 -26.793 32.853 1.00 17.59 C ANISOU 2530 CA PRO A 317 1873 2737 2074 433 206 -39 C ATOM 2531 C PRO A 317 -18.838 -27.799 33.858 1.00 18.27 C ANISOU 2531 C PRO A 317 2246 2505 2191 454 -222 198 C ATOM 2532 O PRO A 317 -19.622 -28.699 33.508 1.00 18.10 O ANISOU 2532 O PRO A 317 2064 2473 2340 393 266 115 O ATOM 2533 CB PRO A 317 -19.368 -25.703 32.610 1.00 20.02 C ANISOU 2533 CB PRO A 317 2244 2769 2593 648 356 104 C ATOM 2534 CG PRO A 317 -19.357 -25.458 31.149 1.00 22.94 C ANISOU 2534 CG PRO A 317 3003 3156 2558 731 197 -161 C ATOM 2535 CD PRO A 317 -18.893 -26.710 30.483 1.00 18.93 C ANISOU 2535 CD PRO A 317 2397 2393 2400 510 53 434 C ATOM 2536 N VAL A 318 -18.378 -27.647 35.094 1.00 18.86 N ANISOU 2536 N VAL A 318 2268 2844 2053 383 -152 358 N ATOM 2537 CA VAL A 318 -18.821 -28.475 36.207 1.00 21.29 C ANISOU 2537 CA VAL A 318 2408 3227 2453 63 -50 664 C ATOM 2538 C VAL A 318 -20.322 -28.277 36.463 1.00 21.74 C ANISOU 2538 C VAL A 318 2578 3537 2144 168 145 333 C ATOM 2539 O VAL A 318 -20.831 -27.163 36.366 1.00 23.13 O ANISOU 2539 O VAL A 318 2658 3538 2590 212 -3 -105 O ATOM 2540 CB VAL A 318 -17.992 -28.149 37.478 1.00 24.58 C ANISOU 2540 CB VAL A 318 2192 4265 2879 317 -356 438 C ATOM 2541 CG1 VAL A 318 -18.524 -28.881 38.701 1.00 30.16 C ANISOU 2541 CG1 VAL A 318 3327 5009 3121 167 179 560 C ATOM 2542 CG2 VAL A 318 -16.525 -28.488 37.253 1.00 26.21 C ANISOU 2542 CG2 VAL A 318 2266 4506 3187 560 -367 587 C ATOM 2543 N SER A 319 -21.024 -29.366 36.771 1.00 24.17 N ANISOU 2543 N SER A 319 2793 3634 2755 -193 -64 360 N ATOM 2544 CA SER A 319 -22.459 -29.305 37.093 1.00 27.02 C ANISOU 2544 CA SER A 319 2884 4295 3086 0 18 357 C ATOM 2545 C SER A 319 -22.720 -29.187 38.595 1.00 28.92 C ANISOU 2545 C SER A 319 4194 3796 2998 -474 -113 324 C ATOM 2546 O SER A 319 -21.849 -29.489 39.414 1.00 33.62 O ANISOU 2546 O SER A 319 4733 5032 3007 258 -111 51 O ATOM 2547 CB SER A 319 -23.186 -30.523 36.529 1.00 31.80 C ANISOU 2547 CB SER A 319 3772 4665 3643 -445 -196 222 C ATOM 2548 OG SER A 319 -23.219 -30.479 35.115 1.00 35.26 O ANISOU 2548 OG SER A 319 4010 5636 3749 228 -296 54 O TER 2549 SER A 319 ATOM 2550 N MET B 1 -2.130 -5.392 51.085 1.00 16.21 N ANISOU 2550 N MET B 1 2299 1841 2018 169 413 -198 N ATOM 2551 CA MET B 1 -2.646 -6.785 50.958 1.00 15.78 C ANISOU 2551 CA MET B 1 2122 1840 2034 256 333 -2 C ATOM 2552 C MET B 1 -1.482 -7.757 51.004 1.00 13.77 C ANISOU 2552 C MET B 1 2119 1691 1419 213 241 -11 C ATOM 2553 O MET B 1 -0.341 -7.377 50.729 1.00 15.26 O ANISOU 2553 O MET B 1 2184 1772 1842 70 178 12 O ATOM 2554 CB MET B 1 -3.441 -6.966 49.663 1.00 16.07 C ANISOU 2554 CB MET B 1 2147 1864 2093 332 301 -82 C ATOM 2555 CG MET B 1 -2.615 -6.941 48.384 1.00 16.15 C ANISOU 2555 CG MET B 1 2442 1878 1815 77 204 -56 C ATOM 2556 SD MET B 1 -3.607 -7.003 46.881 1.00 16.71 S ANISOU 2556 SD MET B 1 2320 1919 2110 81 7 210 S ATOM 2557 CE MET B 1 -2.336 -7.107 45.614 1.00 17.19 C ANISOU 2557 CE MET B 1 2463 1853 2215 244 85 -206 C ATOM 2558 N GLN B 2 -1.775 -8.999 51.382 1.00 14.12 N ANISOU 2558 N GLN B 2 2167 1632 1565 265 212 -43 N ATOM 2559 CA GLN B 2 -0.783 -10.052 51.393 1.00 14.18 C ANISOU 2559 CA GLN B 2 2034 1766 1587 228 178 -71 C ATOM 2560 C GLN B 2 -0.782 -10.793 50.067 1.00 14.21 C ANISOU 2560 C GLN B 2 1976 1724 1697 326 128 -147 C ATOM 2561 O GLN B 2 -1.844 -11.129 49.540 1.00 15.84 O ANISOU 2561 O GLN B 2 2124 1909 1983 262 49 -278 O ATOM 2562 CB GLN B 2 -1.085 -11.040 52.518 1.00 18.16 C ANISOU 2562 CB GLN B 2 2926 2142 1830 271 -8 392 C ATOM 2563 CG GLN B 2 -0.631 -10.605 53.904 1.00 23.95 C ANISOU 2563 CG GLN B 2 4184 2713 2203 187 -192 -184 C ATOM 2564 CD GLN B 2 -0.056 -11.736 54.765 1.00 25.73 C ANISOU 2564 CD GLN B 2 3954 3051 2768 535 27 99 C ATOM 2565 OE1 GLN B 2 0.750 -11.474 55.653 1.00 31.63 O ANISOU 2565 OE1 GLN B 2 4619 4408 2989 712 -350 -87 O ATOM 2566 NE2 GLN B 2 -0.457 -12.990 54.506 1.00 20.63 N ANISOU 2566 NE2 GLN B 2 3636 2816 1385 914 596 198 N ATOM 2567 N ILE B 3 0.413 -11.033 49.534 1.00 13.09 N ANISOU 2567 N ILE B 3 1871 1662 1440 230 15 -110 N ATOM 2568 CA ILE B 3 0.592 -12.026 48.480 1.00 13.37 C ANISOU 2568 CA ILE B 3 1841 1687 1549 330 76 -149 C ATOM 2569 C ILE B 3 1.699 -12.998 48.872 1.00 12.68 C ANISOU 2569 C ILE B 3 1709 1648 1459 184 -92 -236 C ATOM 2570 O ILE B 3 2.467 -12.739 49.804 1.00 13.16 O ANISOU 2570 O ILE B 3 2069 1493 1436 174 -300 -112 O ATOM 2571 CB ILE B 3 0.886 -11.408 47.083 1.00 12.99 C ANISOU 2571 CB ILE B 3 1788 1456 1691 263 162 -82 C ATOM 2572 CG1 ILE B 3 2.234 -10.667 47.057 1.00 13.50 C ANISOU 2572 CG1 ILE B 3 1803 1640 1683 202 182 -59 C ATOM 2573 CG2 ILE B 3 -0.272 -10.524 46.621 1.00 14.20 C ANISOU 2573 CG2 ILE B 3 1981 1576 1837 275 -221 -177 C ATOM 2574 CD1 ILE B 3 2.710 -10.319 45.657 1.00 15.50 C ANISOU 2574 CD1 ILE B 3 2257 1896 1736 186 382 -38 C ATOM 2575 N PHE B 4 1.765 -14.114 48.150 1.00 12.24 N ANISOU 2575 N PHE B 4 1809 1505 1335 209 142 -92 N ATOM 2576 CA PHE B 4 2.745 -15.158 48.406 1.00 13.36 C ANISOU 2576 CA PHE B 4 1848 1535 1693 281 171 -131 C ATOM 2577 C PHE B 4 3.605 -15.357 47.181 1.00 12.67 C ANISOU 2577 C PHE B 4 1734 1587 1491 265 9 -143 C ATOM 2578 O PHE B 4 3.124 -15.193 46.059 1.00 13.70 O ANISOU 2578 O PHE B 4 1820 1984 1401 222 45 -123 O ATOM 2579 CB PHE B 4 2.021 -16.465 48.730 1.00 13.58 C ANISOU 2579 CB PHE B 4 1736 1743 1681 264 182 193 C ATOM 2580 CG PHE B 4 0.984 -16.308 49.801 1.00 14.06 C ANISOU 2580 CG PHE B 4 2003 1782 1557 541 195 55 C ATOM 2581 CD1 PHE B 4 -0.373 -16.344 49.494 1.00 14.27 C ANISOU 2581 CD1 PHE B 4 2003 1863 1554 294 309 126 C ATOM 2582 CD2 PHE B 4 1.368 -16.053 51.111 1.00 14.66 C ANISOU 2582 CD2 PHE B 4 2165 1803 1602 318 106 82 C ATOM 2583 CE1 PHE B 4 -1.330 -16.158 50.475 1.00 15.60 C ANISOU 2583 CE1 PHE B 4 2199 2216 1513 247 379 77 C ATOM 2584 CE2 PHE B 4 0.416 -15.861 52.103 1.00 16.22 C ANISOU 2584 CE2 PHE B 4 2201 2299 1659 348 195 143 C ATOM 2585 CZ PHE B 4 -0.936 -15.917 51.783 1.00 15.96 C ANISOU 2585 CZ PHE B 4 2185 2304 1575 357 212 25 C ATOM 2586 N VAL B 5 4.874 -15.696 47.396 1.00 13.49 N ANISOU 2586 N VAL B 5 1869 1648 1606 478 65 40 N ATOM 2587 CA VAL B 5 5.794 -15.980 46.299 1.00 13.61 C ANISOU 2587 CA VAL B 5 1798 1697 1674 341 100 -9 C ATOM 2588 C VAL B 5 6.474 -17.320 46.567 1.00 13.05 C ANISOU 2588 C VAL B 5 1795 1720 1440 345 11 -28 C ATOM 2589 O VAL B 5 7.229 -17.454 47.533 1.00 14.78 O ANISOU 2589 O VAL B 5 2233 1888 1493 470 -175 1 O ATOM 2590 CB VAL B 5 6.843 -14.855 46.112 1.00 14.19 C ANISOU 2590 CB VAL B 5 2076 1580 1733 314 257 167 C ATOM 2591 CG1 VAL B 5 7.758 -15.176 44.937 1.00 15.66 C ANISOU 2591 CG1 VAL B 5 1985 2093 1871 257 241 -90 C ATOM 2592 CG2 VAL B 5 6.165 -13.499 45.929 1.00 15.11 C ANISOU 2592 CG2 VAL B 5 2219 1617 1903 406 -79 -115 C ATOM 2593 N LYS B 6 6.169 -18.312 45.730 1.00 13.17 N ANISOU 2593 N LYS B 6 1998 1488 1515 331 79 36 N ATOM 2594 CA LYS B 6 6.718 -19.667 45.877 1.00 15.44 C ANISOU 2594 CA LYS B 6 2253 1718 1896 596 -14 131 C ATOM 2595 C LYS B 6 8.048 -19.749 45.139 1.00 14.90 C ANISOU 2595 C LYS B 6 2346 1707 1606 568 42 196 C ATOM 2596 O LYS B 6 8.110 -19.487 43.941 1.00 15.46 O ANISOU 2596 O LYS B 6 2467 1873 1532 375 31 67 O ATOM 2597 CB LYS B 6 5.718 -20.710 45.347 1.00 16.33 C ANISOU 2597 CB LYS B 6 2608 1806 1789 457 140 -13 C ATOM 2598 CG LYS B 6 6.193 -22.164 45.381 1.00 21.86 C ANISOU 2598 CG LYS B 6 3217 1888 3200 598 218 24 C ATOM 2599 CD LYS B 6 6.172 -22.759 46.778 1.00 28.71 C ANISOU 2599 CD LYS B 6 4725 2944 3237 629 -56 160 C ATOM 2600 CE LYS B 6 5.579 -24.165 46.788 1.00 35.26 C ANISOU 2600 CE LYS B 6 5579 3380 4435 -8 139 195 C ATOM 2601 NZ LYS B 6 5.945 -24.985 45.600 1.00 37.38 N ANISOU 2601 NZ LYS B 6 6886 3017 4297 961 132 735 N ATOM 2602 N THR B 7 9.109 -20.115 45.853 1.00 15.89 N ANISOU 2602 N THR B 7 2219 2120 1696 617 58 49 N ATOM 2603 CA THR B 7 10.443 -20.215 45.255 1.00 16.75 C ANISOU 2603 CA THR B 7 2323 2353 1687 559 185 154 C ATOM 2604 C THR B 7 10.692 -21.605 44.667 1.00 16.89 C ANISOU 2604 C THR B 7 2136 2295 1985 632 158 199 C ATOM 2605 O THR B 7 9.928 -22.543 44.932 1.00 19.12 O ANISOU 2605 O THR B 7 2505 2280 2477 644 457 275 O ATOM 2606 CB THR B 7 11.561 -19.912 46.266 1.00 18.06 C ANISOU 2606 CB THR B 7 2481 2488 1892 552 46 39 C ATOM 2607 OG1 THR B 7 11.679 -21.009 47.176 1.00 19.99 O ANISOU 2607 OG1 THR B 7 2820 2929 1845 798 217 321 O ATOM 2608 CG2 THR B 7 11.298 -18.620 47.031 1.00 20.32 C ANISOU 2608 CG2 THR B 7 2918 2630 2172 595 -30 -139 C ATOM 2609 N LEU B 8 11.765 -21.739 43.881 1.00 16.65 N ANISOU 2609 N LEU B 8 2287 2357 1682 584 121 31 N ATOM 2610 CA LEU B 8 12.112 -23.026 43.267 1.00 18.06 C ANISOU 2610 CA LEU B 8 2525 2303 2031 581 363 58 C ATOM 2611 C LEU B 8 12.360 -24.121 44.287 1.00 21.63 C ANISOU 2611 C LEU B 8 3397 2457 2364 601 231 266 C ATOM 2612 O LEU B 8 12.073 -25.295 44.015 1.00 25.88 O ANISOU 2612 O LEU B 8 4526 2439 2868 613 547 167 O ATOM 2613 CB LEU B 8 13.343 -22.893 42.359 1.00 16.83 C ANISOU 2613 CB LEU B 8 2241 2248 1903 706 169 117 C ATOM 2614 CG LEU B 8 13.201 -22.027 41.102 1.00 17.07 C ANISOU 2614 CG LEU B 8 1928 2248 2310 292 -333 342 C ATOM 2615 CD1 LEU B 8 14.568 -21.807 40.479 1.00 20.17 C ANISOU 2615 CD1 LEU B 8 2349 2938 2374 46 136 101 C ATOM 2616 CD2 LEU B 8 12.259 -22.685 40.105 1.00 18.65 C ANISOU 2616 CD2 LEU B 8 2439 2430 2216 281 -219 -211 C ATOM 2617 N THR B 9 12.900 -23.729 45.444 1.00 23.08 N ANISOU 2617 N THR B 9 3500 2893 2375 1130 -1 303 N ATOM 2618 CA THR B 9 13.281 -24.657 46.508 1.00 27.71 C ANISOU 2618 CA THR B 9 4260 3445 2824 1200 331 895 C ATOM 2619 C THR B 9 12.088 -25.044 47.373 1.00 26.84 C ANISOU 2619 C THR B 9 4499 3334 2363 1557 562 702 C ATOM 2620 O THR B 9 12.180 -25.960 48.188 1.00 32.13 O ANISOU 2620 O THR B 9 6037 3301 2867 1753 970 889 O ATOM 2621 CB THR B 9 14.385 -24.066 47.415 1.00 32.83 C ANISOU 2621 CB THR B 9 4635 4657 3179 1243 -418 1022 C ATOM 2622 OG1 THR B 9 13.942 -22.820 47.972 1.00 40.80 O ANISOU 2622 OG1 THR B 9 6044 5104 4352 1271 -936 264 O ATOM 2623 CG2 THR B 9 15.676 -23.848 46.637 1.00 37.13 C ANISOU 2623 CG2 THR B 9 4903 5365 3840 983 -88 774 C ATOM 2624 N GLY B 10 10.976 -24.335 47.207 1.00 24.62 N ANISOU 2624 N GLY B 10 4124 2923 2306 1331 929 155 N ATOM 2625 CA GLY B 10 9.743 -24.673 47.907 1.00 24.61 C ANISOU 2625 CA GLY B 10 4411 2201 2736 811 970 11 C ATOM 2626 C GLY B 10 9.397 -23.785 49.083 1.00 22.20 C ANISOU 2626 C GLY B 10 3839 2310 2284 674 531 73 C ATOM 2627 O GLY B 10 8.460 -24.076 49.816 1.00 26.20 O ANISOU 2627 O GLY B 10 4532 2854 2567 213 975 -183 O ATOM 2628 N LYS B 11 10.151 -22.709 49.273 1.00 20.94 N ANISOU 2628 N LYS B 11 3524 2524 1906 832 327 -116 N ATOM 2629 CA LYS B 11 9.809 -21.730 50.300 1.00 18.68 C ANISOU 2629 CA LYS B 11 3268 2000 1827 994 -86 74 C ATOM 2630 C LYS B 11 8.692 -20.815 49.799 1.00 16.93 C ANISOU 2630 C LYS B 11 2719 1950 1761 659 202 473 C ATOM 2631 O LYS B 11 8.652 -20.463 48.615 1.00 19.73 O ANISOU 2631 O LYS B 11 3352 2453 1689 923 150 414 O ATOM 2632 CB LYS B 11 11.035 -20.901 50.706 1.00 23.29 C ANISOU 2632 CB LYS B 11 2922 3301 2625 763 -254 225 C ATOM 2633 CG LYS B 11 10.690 -19.627 51.473 1.00 28.15 C ANISOU 2633 CG LYS B 11 3786 3485 3424 603 -255 -288 C ATOM 2634 CD LYS B 11 11.556 -19.390 52.697 1.00 31.57 C ANISOU 2634 CD LYS B 11 4494 3910 3591 911 -523 -541 C ATOM 2635 CE LYS B 11 10.961 -18.302 53.583 1.00 28.49 C ANISOU 2635 CE LYS B 11 4192 2563 4069 495 -656 -196 C ATOM 2636 NZ LYS B 11 11.988 -17.729 54.492 1.00 30.94 N ANISOU 2636 NZ LYS B 11 3805 3567 4381 498 -607 -399 N ATOM 2637 N THR B 12 7.786 -20.438 50.695 1.00 16.61 N ANISOU 2637 N THR B 12 2847 1912 1549 740 -126 -3 N ATOM 2638 CA THR B 12 6.804 -19.407 50.389 1.00 15.74 C ANISOU 2638 CA THR B 12 2721 1895 1364 668 -52 13 C ATOM 2639 C THR B 12 7.227 -18.093 51.059 1.00 16.36 C ANISOU 2639 C THR B 12 2636 1910 1669 448 -52 62 C ATOM 2640 O THR B 12 7.326 -18.022 52.284 1.00 18.26 O ANISOU 2640 O THR B 12 3320 1959 1658 519 -215 132 O ATOM 2641 CB THR B 12 5.374 -19.819 50.802 1.00 17.19 C ANISOU 2641 CB THR B 12 2684 1878 1968 521 -146 139 C ATOM 2642 OG1 THR B 12 4.991 -21.011 50.097 1.00 20.14 O ANISOU 2642 OG1 THR B 12 2977 2285 2390 311 -474 -6 O ATOM 2643 CG2 THR B 12 4.377 -18.716 50.455 1.00 18.84 C ANISOU 2643 CG2 THR B 12 2832 2241 2083 719 -102 357 C ATOM 2644 N ILE B 13 7.534 -17.088 50.244 1.00 15.55 N ANISOU 2644 N ILE B 13 2325 1663 1919 502 -81 5 N ATOM 2645 CA ILE B 13 7.814 -15.735 50.730 1.00 15.76 C ANISOU 2645 CA ILE B 13 2197 1907 1884 315 68 -194 C ATOM 2646 C ILE B 13 6.467 -15.034 50.894 1.00 15.75 C ANISOU 2646 C ILE B 13 2283 2112 1586 485 -73 3 C ATOM 2647 O ILE B 13 5.586 -15.168 50.043 1.00 16.84 O ANISOU 2647 O ILE B 13 2210 2290 1897 677 -172 -106 O ATOM 2648 CB ILE B 13 8.695 -14.949 49.724 1.00 15.89 C ANISOU 2648 CB ILE B 13 2217 1907 1912 316 48 -118 C ATOM 2649 CG1 ILE B 13 9.980 -15.726 49.399 1.00 17.97 C ANISOU 2649 CG1 ILE B 13 2205 2303 2319 446 154 145 C ATOM 2650 CG2 ILE B 13 9.020 -13.551 50.244 1.00 17.05 C ANISOU 2650 CG2 ILE B 13 2508 1821 2146 207 40 22 C ATOM 2651 CD1 ILE B 13 10.688 -15.247 48.147 1.00 20.74 C ANISOU 2651 CD1 ILE B 13 2640 2834 2406 89 293 100 C ATOM 2652 N THR B 14 6.303 -14.310 51.996 1.00 15.31 N ANISOU 2652 N THR B 14 2202 1804 1809 295 -1 -99 N ATOM 2653 CA THR B 14 5.064 -13.594 52.253 1.00 14.73 C ANISOU 2653 CA THR B 14 2252 1750 1592 322 88 -44 C ATOM 2654 C THR B 14 5.335 -12.102 52.198 1.00 15.05 C ANISOU 2654 C THR B 14 2172 1793 1751 275 -153 40 C ATOM 2655 O THR B 14 6.237 -11.605 52.873 1.00 17.25 O ANISOU 2655 O THR B 14 2493 2133 1928 185 -383 -59 O ATOM 2656 CB THR B 14 4.461 -13.983 53.619 1.00 15.32 C ANISOU 2656 CB THR B 14 2363 1925 1534 283 -74 80 C ATOM 2657 OG1 THR B 14 4.318 -15.409 53.676 1.00 17.79 O ANISOU 2657 OG1 THR B 14 3014 1912 1833 148 186 245 O ATOM 2658 CG2 THR B 14 3.095 -13.331 53.826 1.00 16.45 C ANISOU 2658 CG2 THR B 14 2271 2165 1814 167 296 -82 C ATOM 2659 N LEU B 15 4.578 -11.400 51.358 1.00 13.53 N ANISOU 2659 N LEU B 15 2063 1654 1423 235 -158 -199 N ATOM 2660 CA LEU B 15 4.816 -9.974 51.142 1.00 14.47 C ANISOU 2660 CA LEU B 15 2138 1707 1652 144 -6 -82 C ATOM 2661 C LEU B 15 3.584 -9.135 51.437 1.00 14.46 C ANISOU 2661 C LEU B 15 2069 1807 1616 133 -22 -148 C ATOM 2662 O LEU B 15 2.455 -9.580 51.238 1.00 15.52 O ANISOU 2662 O LEU B 15 2090 1651 2155 207 -46 -274 O ATOM 2663 CB LEU B 15 5.241 -9.717 49.695 1.00 14.92 C ANISOU 2663 CB LEU B 15 1991 1994 1683 183 88 -153 C ATOM 2664 CG LEU B 15 6.473 -10.445 49.153 1.00 15.01 C ANISOU 2664 CG LEU B 15 1843 1991 1865 178 3 -161 C ATOM 2665 CD1 LEU B 15 6.641 -10.100 47.683 1.00 17.60 C ANISOU 2665 CD1 LEU B 15 2213 2446 2025 79 267 0 C ATOM 2666 CD2 LEU B 15 7.714 -10.072 49.959 1.00 17.58 C ANISOU 2666 CD2 LEU B 15 2030 2205 2443 45 -244 -141 C ATOM 2667 N GLU B 16 3.820 -7.920 51.927 1.00 14.75 N ANISOU 2667 N GLU B 16 2216 1661 1725 298 -5 -64 N ATOM 2668 CA GLU B 16 2.782 -6.907 52.021 1.00 14.34 C ANISOU 2668 CA GLU B 16 2271 1689 1489 306 33 -211 C ATOM 2669 C GLU B 16 2.958 -5.959 50.850 1.00 14.38 C ANISOU 2669 C GLU B 16 2092 1606 1763 260 -86 -101 C ATOM 2670 O GLU B 16 4.005 -5.328 50.702 1.00 16.33 O ANISOU 2670 O GLU B 16 2243 2078 1883 58 -99 20 O ATOM 2671 CB GLU B 16 2.885 -6.165 53.351 1.00 16.67 C ANISOU 2671 CB GLU B 16 2657 2145 1531 280 29 -372 C ATOM 2672 CG GLU B 16 1.807 -5.117 53.561 1.00 19.67 C ANISOU 2672 CG GLU B 16 2882 2609 1983 614 31 -198 C ATOM 2673 CD GLU B 16 0.406 -5.698 53.668 1.00 22.40 C ANISOU 2673 CD GLU B 16 3127 3067 2314 295 239 -283 C ATOM 2674 OE1 GLU B 16 -0.542 -4.974 53.296 1.00 25.67 O ANISOU 2674 OE1 GLU B 16 3623 3754 2375 795 -18 -409 O ATOM 2675 OE2 GLU B 16 0.243 -6.858 54.136 1.00 24.32 O ANISOU 2675 OE2 GLU B 16 3735 3200 2305 27 480 -228 O ATOM 2676 N VAL B 17 1.929 -5.877 50.012 1.00 13.38 N ANISOU 2676 N VAL B 17 2021 1502 1559 242 19 44 N ATOM 2677 CA VAL B 17 2.000 -5.121 48.754 1.00 13.14 C ANISOU 2677 CA VAL B 17 1899 1706 1388 305 46 -42 C ATOM 2678 C VAL B 17 0.706 -4.340 48.522 1.00 13.51 C ANISOU 2678 C VAL B 17 1875 1569 1687 209 13 2 C ATOM 2679 O VAL B 17 -0.295 -4.532 49.227 1.00 14.35 O ANISOU 2679 O VAL B 17 2087 1669 1693 248 182 -7 O ATOM 2680 CB VAL B 17 2.260 -6.063 47.539 1.00 13.21 C ANISOU 2680 CB VAL B 17 1797 1714 1508 206 -60 -170 C ATOM 2681 CG1 VAL B 17 3.572 -6.831 47.699 1.00 14.63 C ANISOU 2681 CG1 VAL B 17 1861 1648 2048 231 35 -95 C ATOM 2682 CG2 VAL B 17 1.086 -7.018 47.349 1.00 14.00 C ANISOU 2682 CG2 VAL B 17 1910 1757 1650 127 -24 -156 C ATOM 2683 N GLU B 18 0.734 -3.463 47.526 1.00 13.97 N ANISOU 2683 N GLU B 18 2093 1674 1542 182 -140 -24 N ATOM 2684 CA GLU B 18 -0.482 -2.823 47.034 1.00 14.22 C ANISOU 2684 CA GLU B 18 2217 1454 1732 415 34 38 C ATOM 2685 C GLU B 18 -0.640 -3.111 45.545 1.00 12.58 C ANISOU 2685 C GLU B 18 1803 1217 1760 252 36 55 C ATOM 2686 O GLU B 18 0.354 -3.300 44.849 1.00 12.97 O ANISOU 2686 O GLU B 18 1772 1347 1808 158 85 67 O ATOM 2687 CB GLU B 18 -0.466 -1.310 47.291 1.00 15.55 C ANISOU 2687 CB GLU B 18 2612 1527 1768 410 -38 -119 C ATOM 2688 CG GLU B 18 -0.400 -0.929 48.765 1.00 18.32 C ANISOU 2688 CG GLU B 18 3267 1875 1816 517 -277 -259 C ATOM 2689 CD GLU B 18 -1.632 -1.342 49.566 1.00 20.88 C ANISOU 2689 CD GLU B 18 3618 2312 2004 761 144 -311 C ATOM 2690 OE1 GLU B 18 -2.716 -1.572 48.993 1.00 22.39 O ANISOU 2690 OE1 GLU B 18 3125 2825 2554 689 621 -12 O ATOM 2691 OE2 GLU B 18 -1.524 -1.435 50.800 1.00 28.97 O ANISOU 2691 OE2 GLU B 18 5009 4012 1983 784 114 -393 O ATOM 2692 N PRO B 19 -1.889 -3.165 45.051 1.00 12.43 N ANISOU 2692 N PRO B 19 1781 1376 1565 245 76 0 N ATOM 2693 CA PRO B 19 -2.108 -3.400 43.615 1.00 12.61 C ANISOU 2693 CA PRO B 19 1694 1541 1557 50 19 40 C ATOM 2694 C PRO B 19 -1.301 -2.456 42.703 1.00 11.64 C ANISOU 2694 C PRO B 19 1753 1123 1546 138 24 -96 C ATOM 2695 O PRO B 19 -0.896 -2.845 41.610 1.00 12.86 O ANISOU 2695 O PRO B 19 1891 1497 1495 100 129 -14 O ATOM 2696 CB PRO B 19 -3.617 -3.169 43.454 1.00 13.91 C ANISOU 2696 CB PRO B 19 1725 1743 1817 176 96 10 C ATOM 2697 CG PRO B 19 -4.177 -3.571 44.786 1.00 14.53 C ANISOU 2697 CG PRO B 19 1970 1779 1769 165 12 116 C ATOM 2698 CD PRO B 19 -3.157 -3.142 45.808 1.00 14.16 C ANISOU 2698 CD PRO B 19 1697 1595 2085 232 161 -222 C ATOM 2699 N SER B 20 -1.078 -1.223 43.156 1.00 11.30 N ANISOU 2699 N SER B 20 1496 1125 1670 75 -62 -72 N ATOM 2700 CA SER B 20 -0.357 -0.235 42.364 1.00 11.65 C ANISOU 2700 CA SER B 20 1550 1298 1577 154 165 -107 C ATOM 2701 C SER B 20 1.153 -0.482 42.259 1.00 11.67 C ANISOU 2701 C SER B 20 1568 1202 1662 232 108 -93 C ATOM 2702 O SER B 20 1.812 0.131 41.417 1.00 12.90 O ANISOU 2702 O SER B 20 1749 1395 1757 170 127 36 O ATOM 2703 CB SER B 20 -0.610 1.165 42.917 1.00 12.37 C ANISOU 2703 CB SER B 20 1724 1253 1724 201 114 -79 C ATOM 2704 OG SER B 20 -0.280 1.228 44.293 1.00 13.39 O ANISOU 2704 OG SER B 20 1811 1527 1748 94 168 -233 O ATOM 2705 N ASP B 21 1.700 -1.376 43.086 1.00 11.01 N ANISOU 2705 N ASP B 21 1508 1196 1478 249 101 -200 N ATOM 2706 CA ASP B 21 3.146 -1.608 43.090 1.00 11.93 C ANISOU 2706 CA ASP B 21 1565 1325 1640 291 121 -18 C ATOM 2707 C ASP B 21 3.617 -2.196 41.769 1.00 12.65 C ANISOU 2707 C ASP B 21 1742 1363 1701 194 180 -137 C ATOM 2708 O ASP B 21 2.963 -3.079 41.199 1.00 12.47 O ANISOU 2708 O ASP B 21 1831 1378 1528 224 66 -100 O ATOM 2709 CB ASP B 21 3.539 -2.593 44.185 1.00 12.32 C ANISOU 2709 CB ASP B 21 1700 1431 1550 295 35 9 C ATOM 2710 CG ASP B 21 3.336 -2.054 45.587 1.00 13.01 C ANISOU 2710 CG ASP B 21 1769 1661 1510 191 -58 -20 C ATOM 2711 OD1 ASP B 21 3.187 -0.831 45.777 1.00 14.38 O ANISOU 2711 OD1 ASP B 21 2016 1621 1827 70 -204 17 O ATOM 2712 OD2 ASP B 21 3.357 -2.880 46.522 1.00 13.88 O ANISOU 2712 OD2 ASP B 21 1846 1830 1595 230 -5 133 O ATOM 2713 N THR B 22 4.763 -1.724 41.286 1.00 12.72 N ANISOU 2713 N THR B 22 1794 1533 1504 260 300 -64 N ATOM 2714 CA THR B 22 5.372 -2.334 40.097 1.00 13.41 C ANISOU 2714 CA THR B 22 1823 1518 1753 271 364 -222 C ATOM 2715 C THR B 22 5.969 -3.700 40.436 1.00 13.91 C ANISOU 2715 C THR B 22 1731 1650 1904 372 461 -158 C ATOM 2716 O THR B 22 6.287 -3.988 41.591 1.00 14.04 O ANISOU 2716 O THR B 22 1812 1411 2108 188 338 -57 O ATOM 2717 CB THR B 22 6.498 -1.464 39.506 1.00 14.54 C ANISOU 2717 CB THR B 22 1959 1559 2005 267 464 -71 C ATOM 2718 OG1 THR B 22 7.551 -1.347 40.471 1.00 14.60 O ANISOU 2718 OG1 THR B 22 2039 1521 1986 185 479 -107 O ATOM 2719 CG2 THR B 22 5.983 -0.094 39.103 1.00 15.17 C ANISOU 2719 CG2 THR B 22 2248 1508 2007 159 343 -38 C ATOM 2720 N ILE B 23 6.141 -4.523 39.407 1.00 14.04 N ANISOU 2720 N ILE B 23 1912 1317 2105 340 379 -162 N ATOM 2721 CA ILE B 23 6.818 -5.805 39.569 1.00 14.41 C ANISOU 2721 CA ILE B 23 1999 1406 2067 430 276 -273 C ATOM 2722 C ILE B 23 8.259 -5.600 40.047 1.00 15.17 C ANISOU 2722 C ILE B 23 2038 1583 2143 167 370 -51 C ATOM 2723 O ILE B 23 8.739 -6.355 40.890 1.00 15.15 O ANISOU 2723 O ILE B 23 1899 1448 2407 296 292 -52 O ATOM 2724 CB ILE B 23 6.748 -6.620 38.263 1.00 14.30 C ANISOU 2724 CB ILE B 23 2098 1441 1895 339 333 -171 C ATOM 2725 CG1 ILE B 23 5.283 -6.953 37.913 1.00 15.71 C ANISOU 2725 CG1 ILE B 23 2141 1737 2089 138 278 -30 C ATOM 2726 CG2 ILE B 23 7.588 -7.890 38.338 1.00 16.24 C ANISOU 2726 CG2 ILE B 23 2198 1304 2669 321 383 -335 C ATOM 2727 CD1 ILE B 23 4.515 -7.735 38.962 1.00 18.58 C ANISOU 2727 CD1 ILE B 23 2414 2496 2150 -91 478 -5 C ATOM 2728 N GLU B 24 8.922 -4.557 39.533 1.00 15.67 N ANISOU 2728 N GLU B 24 2174 1418 2359 88 427 -155 N ATOM 2729 CA GLU B 24 10.263 -4.178 39.987 1.00 17.63 C ANISOU 2729 CA GLU B 24 2200 2024 2473 90 373 15 C ATOM 2730 C GLU B 24 10.269 -3.942 41.501 1.00 15.95 C ANISOU 2730 C GLU B 24 1917 1714 2429 156 394 34 C ATOM 2731 O GLU B 24 11.169 -4.402 42.206 1.00 16.35 O ANISOU 2731 O GLU B 24 2019 1585 2608 238 386 96 O ATOM 2732 CB GLU B 24 10.754 -2.928 39.232 1.00 22.49 C ANISOU 2732 CB GLU B 24 2913 2302 3327 -127 796 276 C ATOM 2733 CG GLU B 24 12.165 -2.484 39.601 1.00 27.82 C ANISOU 2733 CG GLU B 24 3180 3565 3824 -287 425 166 C ATOM 2734 CD GLU B 24 12.618 -1.187 38.939 1.00 35.68 C ANISOU 2734 CD GLU B 24 4179 4633 4742 -440 867 1184 C ATOM 2735 OE1 GLU B 24 11.776 -0.401 38.456 1.00 38.68 O ANISOU 2735 OE1 GLU B 24 4635 4796 5266 -122 1171 1612 O ATOM 2736 OE2 GLU B 24 13.844 -0.945 38.915 1.00 45.81 O ANISOU 2736 OE2 GLU B 24 4474 6631 6301 -921 95 1126 O ATOM 2737 N ASN B 25 9.249 -3.244 41.999 1.00 15.93 N ANISOU 2737 N ASN B 25 2044 1525 2484 153 396 -17 N ATOM 2738 CA ASN B 25 9.136 -2.992 43.432 1.00 14.88 C ANISOU 2738 CA ASN B 25 1894 1336 2422 342 212 -125 C ATOM 2739 C ASN B 25 8.938 -4.272 44.255 1.00 15.42 C ANISOU 2739 C ASN B 25 2073 1488 2296 253 312 -128 C ATOM 2740 O ASN B 25 9.516 -4.419 45.322 1.00 15.85 O ANISOU 2740 O ASN B 25 2179 1537 2306 227 298 -122 O ATOM 2741 CB ASN B 25 8.018 -1.982 43.716 1.00 15.11 C ANISOU 2741 CB ASN B 25 2106 1486 2149 500 291 -202 C ATOM 2742 CG ASN B 25 7.993 -1.534 45.164 1.00 15.26 C ANISOU 2742 CG ASN B 25 2054 1662 2080 345 109 -76 C ATOM 2743 OD1 ASN B 25 8.821 -0.725 45.592 1.00 19.79 O ANISOU 2743 OD1 ASN B 25 2458 2439 2622 47 -359 -207 O ATOM 2744 ND2 ASN B 25 7.036 -2.042 45.919 1.00 18.26 N ANISOU 2744 ND2 ASN B 25 2493 1778 2666 271 654 -175 N ATOM 2745 N VAL B 26 8.136 -5.197 43.731 1.00 16.12 N ANISOU 2745 N VAL B 26 2033 1395 2696 242 323 -102 N ATOM 2746 CA VAL B 26 7.947 -6.502 44.364 1.00 15.23 C ANISOU 2746 CA VAL B 26 2010 1566 2209 294 374 -2 C ATOM 2747 C VAL B 26 9.284 -7.265 44.415 1.00 14.18 C ANISOU 2747 C VAL B 26 1966 1394 2025 214 263 -125 C ATOM 2748 O VAL B 26 9.621 -7.867 45.440 1.00 16.32 O ANISOU 2748 O VAL B 26 2268 1654 2275 152 431 273 O ATOM 2749 CB VAL B 26 6.858 -7.324 43.628 1.00 15.19 C ANISOU 2749 CB VAL B 26 1852 1654 2263 197 339 209 C ATOM 2750 CG1 VAL B 26 6.747 -8.737 44.190 1.00 16.78 C ANISOU 2750 CG1 VAL B 26 2368 1740 2267 133 435 300 C ATOM 2751 CG2 VAL B 26 5.503 -6.632 43.715 1.00 17.54 C ANISOU 2751 CG2 VAL B 26 1941 1947 2774 349 548 134 C ATOM 2752 N LYS B 27 10.054 -7.219 43.326 1.00 14.20 N ANISOU 2752 N LYS B 27 1948 1279 2165 318 319 -242 N ATOM 2753 CA LYS B 27 11.383 -7.842 43.317 1.00 14.79 C ANISOU 2753 CA LYS B 27 1954 1601 2062 369 220 -259 C ATOM 2754 C LYS B 27 12.296 -7.249 44.384 1.00 15.05 C ANISOU 2754 C LYS B 27 2017 1636 2061 308 132 -92 C ATOM 2755 O LYS B 27 13.083 -7.970 45.003 1.00 14.69 O ANISOU 2755 O LYS B 27 2343 1616 1620 433 43 -283 O ATOM 2756 CB LYS B 27 12.052 -7.700 41.951 1.00 14.52 C ANISOU 2756 CB LYS B 27 1984 1624 1906 457 107 -180 C ATOM 2757 CG LYS B 27 11.424 -8.509 40.832 1.00 16.44 C ANISOU 2757 CG LYS B 27 2193 1857 2197 287 -47 -220 C ATOM 2758 CD LYS B 27 12.296 -8.361 39.607 1.00 20.13 C ANISOU 2758 CD LYS B 27 2798 2310 2541 430 364 46 C ATOM 2759 CE LYS B 27 11.832 -9.254 38.479 1.00 20.24 C ANISOU 2759 CE LYS B 27 3262 2140 2287 478 513 155 C ATOM 2760 NZ LYS B 27 12.752 -9.062 37.321 1.00 25.65 N ANISOU 2760 NZ LYS B 27 4463 2561 2719 332 1268 10 N ATOM 2761 N ALA B 28 12.190 -5.937 44.598 1.00 16.47 N ANISOU 2761 N ALA B 28 2452 1596 2208 58 439 -79 N ATOM 2762 CA ALA B 28 12.993 -5.276 45.629 1.00 17.75 C ANISOU 2762 CA ALA B 28 2827 1790 2124 74 380 -254 C ATOM 2763 C ALA B 28 12.672 -5.805 47.033 1.00 17.13 C ANISOU 2763 C ALA B 28 2866 1685 1957 -186 339 -528 C ATOM 2764 O ALA B 28 13.570 -5.985 47.849 1.00 19.37 O ANISOU 2764 O ALA B 28 3402 1968 1989 -398 260 -482 O ATOM 2765 CB ALA B 28 12.831 -3.763 45.571 1.00 18.44 C ANISOU 2765 CB ALA B 28 2853 1773 2378 108 485 -205 C ATOM 2766 N LYS B 29 11.391 -6.060 47.292 1.00 19.97 N ANISOU 2766 N LYS B 29 3307 2014 2265 -331 883 -706 N ATOM 2767 CA LYS B 29 10.968 -6.652 48.559 1.00 21.93 C ANISOU 2767 CA LYS B 29 3449 2678 2202 -131 965 -611 C ATOM 2768 C LYS B 29 11.480 -8.074 48.724 1.00 22.33 C ANISOU 2768 C LYS B 29 4025 2315 2145 -638 25 -604 C ATOM 2769 O LYS B 29 11.920 -8.456 49.808 1.00 25.81 O ANISOU 2769 O LYS B 29 4900 2703 2201 -1048 130 -22 O ATOM 2770 CB LYS B 29 9.455 -6.620 48.685 1.00 25.89 C ANISOU 2770 CB LYS B 29 3476 2729 3631 18 1093 -997 C ATOM 2771 CG LYS B 29 8.940 -5.215 48.852 1.00 27.32 C ANISOU 2771 CG LYS B 29 3605 2584 4190 -105 1401 -756 C ATOM 2772 CD LYS B 29 7.470 -5.208 49.160 1.00 27.85 C ANISOU 2772 CD LYS B 29 3391 2894 4295 259 964 -849 C ATOM 2773 CE LYS B 29 7.055 -3.785 49.456 1.00 26.21 C ANISOU 2773 CE LYS B 29 3652 2798 3508 30 671 -1117 C ATOM 2774 NZ LYS B 29 5.618 -3.608 49.161 1.00 29.18 N ANISOU 2774 NZ LYS B 29 3776 2946 4364 226 312 -597 N ATOM 2775 N ILE B 30 11.445 -8.847 47.638 1.00 19.40 N ANISOU 2775 N ILE B 30 3169 2196 2006 -471 433 -536 N ATOM 2776 CA ILE B 30 11.999 -10.195 47.644 1.00 17.74 C ANISOU 2776 CA ILE B 30 2930 2270 1540 -420 -239 -396 C ATOM 2777 C ILE B 30 13.491 -10.132 47.979 1.00 19.04 C ANISOU 2777 C ILE B 30 2977 2071 2184 -607 -405 -400 C ATOM 2778 O ILE B 30 13.992 -10.942 48.772 1.00 23.88 O ANISOU 2778 O ILE B 30 3805 2887 2381 -881 -910 104 O ATOM 2779 CB ILE B 30 11.707 -10.918 46.313 1.00 15.52 C ANISOU 2779 CB ILE B 30 2459 1907 1530 -167 -106 -414 C ATOM 2780 CG1 ILE B 30 10.202 -11.193 46.202 1.00 14.81 C ANISOU 2780 CG1 ILE B 30 2410 1708 1509 -57 -4 -459 C ATOM 2781 CG2 ILE B 30 12.511 -12.209 46.185 1.00 16.42 C ANISOU 2781 CG2 ILE B 30 2494 1989 1753 -44 -296 -197 C ATOM 2782 CD1 ILE B 30 9.754 -11.671 44.841 1.00 15.03 C ANISOU 2782 CD1 ILE B 30 2339 1922 1447 40 41 -505 C ATOM 2783 N AGLN B 31 14.213 -9.185 47.373 0.50 17.32 N ANISOU 2783 N AGLN B 31 2618 2355 1607 -442 -366 -351 N ATOM 2784 N BGLN B 31 14.169 -9.128 47.430 0.50 18.11 N ANISOU 2784 N BGLN B 31 2826 2333 1721 -542 -295 -343 N ATOM 2785 CA AGLN B 31 15.673 -9.086 47.558 0.50 17.92 C ANISOU 2785 CA AGLN B 31 2576 2136 2096 -544 -385 -469 C ATOM 2786 CA BGLN B 31 15.498 -8.799 47.905 0.50 19.11 C ANISOU 2786 CA BGLN B 31 2967 2251 2042 -814 -370 -498 C ATOM 2787 C AGLN B 31 16.126 -8.793 48.990 0.50 18.43 C ANISOU 2787 C AGLN B 31 2365 2459 2177 -79 -569 -446 C ATOM 2788 C BGLN B 31 15.462 -8.301 49.359 0.50 20.39 C ANISOU 2788 C BGLN B 31 3224 2369 2153 -628 -277 -688 C ATOM 2789 O AGLN B 31 17.070 -9.396 49.503 0.50 17.38 O ANISOU 2789 O AGLN B 31 2607 2251 1744 0 -473 -371 O ATOM 2790 O BGLN B 31 16.265 -8.745 50.173 0.50 22.29 O ANISOU 2790 O BGLN B 31 3436 2995 2036 -717 -158 -167 O ATOM 2791 CB AGLN B 31 16.279 -8.024 46.647 0.50 17.79 C ANISOU 2791 CB AGLN B 31 2383 2509 1866 -490 -355 -392 C ATOM 2792 CB BGLN B 31 16.184 -7.782 47.001 0.50 18.83 C ANISOU 2792 CB BGLN B 31 2812 2413 1929 -659 -239 -469 C ATOM 2793 CG AGLN B 31 17.749 -7.819 46.967 0.50 17.92 C ANISOU 2793 CG AGLN B 31 2519 2967 1322 -502 -664 -368 C ATOM 2794 CG BGLN B 31 17.635 -7.574 47.385 0.50 20.90 C ANISOU 2794 CG BGLN B 31 2686 2738 2515 -529 -244 -368 C ATOM 2795 CD AGLN B 31 18.409 -6.778 46.099 0.50 20.42 C ANISOU 2795 CD AGLN B 31 2552 2752 2453 -504 -485 -142 C ATOM 2796 CD BGLN B 31 18.439 -6.940 46.279 0.50 20.44 C ANISOU 2796 CD BGLN B 31 2563 2467 2735 -696 -493 -112 C ATOM 2797 OE1AGLN B 31 19.579 -6.912 45.731 0.50 24.31 O ANISOU 2797 OE1AGLN B 31 2650 3483 3100 -204 -372 32 O ATOM 2798 OE1BGLN B 31 19.528 -7.411 45.936 0.50 22.53 O ANISOU 2798 OE1BGLN B 31 2470 2837 3251 -662 -668 -317 O ATOM 2799 NE2AGLN B 31 17.664 -5.735 45.759 0.50 19.56 N ANISOU 2799 NE2AGLN B 31 2647 2665 2119 -425 -420 -305 N ATOM 2800 NE2BGLN B 31 17.903 -5.872 45.702 0.50 19.08 N ANISOU 2800 NE2BGLN B 31 2352 2377 2519 -517 -572 -464 N ATOM 2801 N AASP B 32 15.466 -7.836 49.618 0.50 16.83 N ANISOU 2801 N AASP B 32 1822 2473 2099 -397 -246 -452 N ATOM 2802 N BASP B 32 14.527 -7.408 49.688 0.50 19.98 N ANISOU 2802 N BASP B 32 3084 2366 2142 -689 -236 -402 N ATOM 2803 CA AASP B 32 15.790 -7.476 50.984 0.50 15.22 C ANISOU 2803 CA AASP B 32 1486 2135 2159 -267 -439 -383 C ATOM 2804 CA BASP B 32 14.422 -6.902 51.065 0.50 20.10 C ANISOU 2804 CA BASP B 32 2920 2660 2057 -509 -66 -282 C ATOM 2805 C AASP B 32 15.562 -8.661 51.920 0.50 19.13 C ANISOU 2805 C AASP B 32 2438 2357 2471 -186 -126 -163 C ATOM 2806 C BASP B 32 14.412 -8.060 52.077 0.50 24.44 C ANISOU 2806 C BASP B 32 3668 2866 2750 -540 -63 119 C ATOM 2807 O AASP B 32 16.308 -8.856 52.881 0.50 18.77 O ANISOU 2807 O AASP B 32 2527 1976 2629 -219 -59 343 O ATOM 2808 O BASP B 32 14.479 -7.821 53.279 0.50 26.02 O ANISOU 2808 O BASP B 32 3602 3673 2609 -339 -405 527 O ATOM 2809 CB AASP B 32 14.941 -6.282 51.425 0.50 16.29 C ANISOU 2809 CB AASP B 32 1875 2100 2211 -335 214 -287 C ATOM 2810 CB BASP B 32 13.167 -6.020 51.270 0.50 19.18 C ANISOU 2810 CB BASP B 32 2934 2537 1813 -604 87 -552 C ATOM 2811 CG AASP B 32 15.262 -5.830 52.834 0.50 16.32 C ANISOU 2811 CG AASP B 32 2241 1821 2138 -626 317 -140 C ATOM 2812 CG BASP B 32 13.293 -4.627 50.646 0.50 19.06 C ANISOU 2812 CG BASP B 32 2528 2484 2229 -66 12 -470 C ATOM 2813 OD1AASP B 32 16.417 -5.398 53.090 0.50 14.04 O ANISOU 2813 OD1AASP B 32 2181 1253 1898 -804 781 5 O ATOM 2814 OD1BASP B 32 14.427 -4.176 50.425 0.50 20.44 O ANISOU 2814 OD1BASP B 32 2706 2442 2616 -167 227 -373 O ATOM 2815 OD2AASP B 32 14.349 -5.903 53.683 0.50 21.43 O ANISOU 2815 OD2AASP B 32 2673 2812 2656 -627 790 -417 O ATOM 2816 OD2BASP B 32 12.257 -3.965 50.389 0.50 18.40 O ANISOU 2816 OD2BASP B 32 2542 2432 2017 -104 -227 -844 O ATOM 2817 N ALYS B 33 14.534 -9.454 51.624 0.50 22.01 N ANISOU 2817 N ALYS B 33 3108 2538 2716 -646 -175 19 N ATOM 2818 N BLYS B 33 14.347 -9.307 51.602 0.50 26.39 N ANISOU 2818 N BLYS B 33 4487 3023 2514 -687 -88 85 N ATOM 2819 CA ALYS B 33 14.096 -10.517 52.528 0.50 25.27 C ANISOU 2819 CA ALYS B 33 3726 3330 2543 -481 -319 572 C ATOM 2820 CA BLYS B 33 14.160 -10.449 52.516 0.50 26.89 C ANISOU 2820 CA BLYS B 33 4090 3549 2577 -430 -261 485 C ATOM 2821 C ALYS B 33 14.783 -11.859 52.299 0.50 26.60 C ANISOU 2821 C ALYS B 33 3985 3380 2738 -440 -494 366 C ATOM 2822 C BLYS B 33 15.027 -11.698 52.289 0.50 27.04 C ANISOU 2822 C BLYS B 33 4262 3311 2698 -615 -366 135 C ATOM 2823 O ALYS B 33 15.003 -12.612 53.252 0.50 27.03 O ANISOU 2823 O ALYS B 33 4009 3502 2758 -784 -968 405 O ATOM 2824 O BLYS B 33 15.586 -12.246 53.245 0.50 29.11 O ANISOU 2824 O BLYS B 33 4361 3557 3140 -860 -500 579 O ATOM 2825 CB ALYS B 33 12.578 -10.687 52.458 0.50 26.53 C ANISOU 2825 CB ALYS B 33 3796 3703 2580 -672 -212 691 C ATOM 2826 CB BLYS B 33 12.688 -10.859 52.539 0.50 26.66 C ANISOU 2826 CB BLYS B 33 4059 3830 2238 -447 -161 432 C ATOM 2827 CG ALYS B 33 11.800 -9.535 53.071 0.50 30.82 C ANISOU 2827 CG ALYS B 33 4419 3975 3313 -458 -325 220 C ATOM 2828 CG BLYS B 33 11.736 -9.712 52.824 0.50 28.56 C ANISOU 2828 CG BLYS B 33 4166 3853 2831 -381 -47 430 C ATOM 2829 CD ALYS B 33 10.317 -9.856 53.151 0.50 34.54 C ANISOU 2829 CD ALYS B 33 4387 4586 4148 -506 -838 347 C ATOM 2830 CD BLYS B 33 10.313 -10.095 52.467 0.50 29.54 C ANISOU 2830 CD BLYS B 33 4158 3943 3121 -218 -310 261 C ATOM 2831 CE ALYS B 33 10.074 -11.131 53.940 0.50 35.02 C ANISOU 2831 CE ALYS B 33 4840 4364 4100 -222 -886 263 C ATOM 2832 CE BLYS B 33 9.719 -11.042 53.495 0.50 31.49 C ANISOU 2832 CE BLYS B 33 4332 4163 3469 -303 -443 610 C ATOM 2833 NZ ALYS B 33 10.503 -11.005 55.361 0.50 37.65 N ANISOU 2833 NZ ALYS B 33 5165 4752 4387 -19 -1389 178 N ATOM 2834 NZ BLYS B 33 9.425 -10.356 54.784 0.50 35.37 N ANISOU 2834 NZ BLYS B 33 4450 4737 4251 -74 -362 -163 N ATOM 2835 N GLU B 34 15.105 -12.163 51.044 1.00 26.48 N ANISOU 2835 N GLU B 34 4195 3497 2368 -628 -1009 332 N ATOM 2836 CA GLU B 34 15.764 -13.438 50.708 1.00 26.00 C ANISOU 2836 CA GLU B 34 4278 3478 2120 -629 -929 566 C ATOM 2837 C GLU B 34 17.145 -13.291 50.083 1.00 28.64 C ANISOU 2837 C GLU B 34 3707 3552 3621 -488 -1269 266 C ATOM 2838 O GLU B 34 17.830 -14.291 49.834 1.00 30.74 O ANISOU 2838 O GLU B 34 3998 3948 3732 -264 -1220 615 O ATOM 2839 CB GLU B 34 14.881 -14.268 49.765 1.00 28.23 C ANISOU 2839 CB GLU B 34 3914 3824 2985 -547 -1126 202 C ATOM 2840 CG GLU B 34 13.554 -14.705 50.356 1.00 29.20 C ANISOU 2840 CG GLU B 34 3502 4337 3255 -204 -931 88 C ATOM 2841 CD GLU B 34 13.688 -15.759 51.442 1.00 30.26 C ANISOU 2841 CD GLU B 34 3533 4028 3935 -20 -696 298 C ATOM 2842 OE1 GLU B 34 14.610 -16.607 51.377 1.00 33.98 O ANISOU 2842 OE1 GLU B 34 4175 4413 4322 419 -730 673 O ATOM 2843 OE2 GLU B 34 12.856 -15.745 52.368 1.00 32.67 O ANISOU 2843 OE2 GLU B 34 4026 4305 4081 174 -413 434 O ATOM 2844 N GLY B 35 17.542 -12.051 49.807 1.00 26.91 N ANISOU 2844 N GLY B 35 3637 3876 2711 -733 -1261 507 N ATOM 2845 CA GLY B 35 18.862 -11.774 49.251 1.00 27.31 C ANISOU 2845 CA GLY B 35 3760 3484 3132 -763 -1056 400 C ATOM 2846 C GLY B 35 18.996 -12.140 47.791 1.00 24.86 C ANISOU 2846 C GLY B 35 3162 3055 3228 -368 -1038 285 C ATOM 2847 O GLY B 35 20.107 -12.201 47.266 1.00 29.56 O ANISOU 2847 O GLY B 35 3349 4720 3159 -226 -1148 -219 O ATOM 2848 N ILE B 36 17.867 -12.389 47.131 1.00 24.52 N ANISOU 2848 N ILE B 36 3662 2425 3227 -445 -1419 292 N ATOM 2849 CA ILE B 36 17.890 -12.733 45.718 1.00 24.13 C ANISOU 2849 CA ILE B 36 2999 2760 3407 -99 -1193 19 C ATOM 2850 C ILE B 36 17.969 -11.455 44.886 1.00 19.87 C ANISOU 2850 C ILE B 36 2476 2453 2621 -15 -908 -458 C ATOM 2851 O ILE B 36 17.063 -10.614 44.952 1.00 18.80 O ANISOU 2851 O ILE B 36 2356 2638 2147 69 -682 -588 O ATOM 2852 CB ILE B 36 16.668 -13.581 45.304 1.00 23.34 C ANISOU 2852 CB ILE B 36 3244 2410 3211 -229 -1183 169 C ATOM 2853 CG1 ILE B 36 16.507 -14.785 46.246 1.00 25.59 C ANISOU 2853 CG1 ILE B 36 3811 2401 3511 -239 -1299 286 C ATOM 2854 CG2 ILE B 36 16.808 -14.031 43.854 1.00 23.48 C ANISOU 2854 CG2 ILE B 36 3053 2459 3406 -142 -1111 -180 C ATOM 2855 CD1 ILE B 36 15.167 -15.483 46.143 1.00 26.24 C ANISOU 2855 CD1 ILE B 36 3901 2391 3676 -271 -1380 162 C ATOM 2856 N PRO B 37 19.048 -11.302 44.098 1.00 21.16 N ANISOU 2856 N PRO B 37 2253 2550 3236 250 -866 -508 N ATOM 2857 CA PRO B 37 19.182 -10.100 43.284 1.00 21.03 C ANISOU 2857 CA PRO B 37 2405 2773 2813 -84 -610 -534 C ATOM 2858 C PRO B 37 18.035 -9.985 42.278 1.00 18.33 C ANISOU 2858 C PRO B 37 2243 2286 2432 66 -364 -712 C ATOM 2859 O PRO B 37 17.686 -10.976 41.634 1.00 17.54 O ANISOU 2859 O PRO B 37 1797 2362 2505 -40 -206 -783 O ATOM 2860 CB PRO B 37 20.523 -10.303 42.567 1.00 24.98 C ANISOU 2860 CB PRO B 37 2344 3537 3610 35 -475 -661 C ATOM 2861 CG PRO B 37 21.267 -11.282 43.417 1.00 28.01 C ANISOU 2861 CG PRO B 37 3205 3618 3819 203 -349 -408 C ATOM 2862 CD PRO B 37 20.202 -12.206 43.932 1.00 24.14 C ANISOU 2862 CD PRO B 37 2672 3025 3474 642 -518 -399 C ATOM 2863 N PRO B 38 17.437 -8.787 42.154 1.00 17.46 N ANISOU 2863 N PRO B 38 2249 2051 2331 -204 -342 -508 N ATOM 2864 CA PRO B 38 16.333 -8.593 41.215 1.00 17.56 C ANISOU 2864 CA PRO B 38 2303 1955 2413 48 -352 -421 C ATOM 2865 C PRO B 38 16.656 -8.962 39.770 1.00 17.58 C ANISOU 2865 C PRO B 38 2192 2076 2412 -258 -67 -283 C ATOM 2866 O PRO B 38 15.764 -9.412 39.055 1.00 17.73 O ANISOU 2866 O PRO B 38 2193 2058 2482 -109 -7 -580 O ATOM 2867 CB PRO B 38 16.024 -7.099 41.337 1.00 18.16 C ANISOU 2867 CB PRO B 38 2194 1949 2755 -21 -513 -654 C ATOM 2868 CG PRO B 38 16.427 -6.760 42.728 1.00 22.51 C ANISOU 2868 CG PRO B 38 2765 3027 2758 207 -779 -559 C ATOM 2869 CD PRO B 38 17.668 -7.582 42.968 1.00 20.99 C ANISOU 2869 CD PRO B 38 2749 2210 3015 58 -720 -844 C ATOM 2870 N ASP B 39 17.908 -8.788 39.345 1.00 17.33 N ANISOU 2870 N ASP B 39 2265 2007 2312 -126 53 -441 N ATOM 2871 CA ASP B 39 18.264 -9.093 37.956 1.00 17.69 C ANISOU 2871 CA ASP B 39 2133 2122 2463 -457 219 -643 C ATOM 2872 C ASP B 39 18.202 -10.585 37.628 1.00 17.15 C ANISOU 2872 C ASP B 39 2195 2005 2314 -237 -30 -347 C ATOM 2873 O ASP B 39 18.107 -10.946 36.459 1.00 18.83 O ANISOU 2873 O ASP B 39 2568 2332 2253 -164 44 -378 O ATOM 2874 CB ASP B 39 19.607 -8.449 37.519 1.00 20.69 C ANISOU 2874 CB ASP B 39 2315 2581 2964 -740 250 -406 C ATOM 2875 CG ASP B 39 20.817 -8.912 38.345 1.00 21.41 C ANISOU 2875 CG ASP B 39 2150 2487 3496 -347 349 -614 C ATOM 2876 OD1 ASP B 39 20.701 -9.778 39.237 1.00 24.67 O ANISOU 2876 OD1 ASP B 39 2559 3136 3675 -240 8 -402 O ATOM 2877 OD2 ASP B 39 21.917 -8.376 38.087 1.00 29.67 O ANISOU 2877 OD2 ASP B 39 2540 3994 4738 -982 458 -497 O ATOM 2878 N GLN B 40 18.235 -11.431 38.660 1.00 16.79 N ANISOU 2878 N GLN B 40 1925 2166 2288 -312 51 -310 N ATOM 2879 CA GLN B 40 18.109 -12.879 38.505 1.00 16.27 C ANISOU 2879 CA GLN B 40 1937 2194 2048 -329 165 -371 C ATOM 2880 C GLN B 40 16.642 -13.319 38.570 1.00 14.24 C ANISOU 2880 C GLN B 40 1755 1810 1845 -39 33 -416 C ATOM 2881 O GLN B 40 16.258 -14.335 37.981 1.00 16.03 O ANISOU 2881 O GLN B 40 1850 2037 2201 22 -170 -642 O ATOM 2882 CB GLN B 40 18.852 -13.601 39.625 1.00 19.10 C ANISOU 2882 CB GLN B 40 2506 2337 2412 -44 -223 -442 C ATOM 2883 CG GLN B 40 20.349 -13.407 39.727 1.00 25.20 C ANISOU 2883 CG GLN B 40 2689 3205 3678 -63 -160 -298 C ATOM 2884 CD GLN B 40 20.917 -14.217 40.881 1.00 30.28 C ANISOU 2884 CD GLN B 40 3838 3817 3849 387 -421 -135 C ATOM 2885 OE1 GLN B 40 20.258 -15.135 41.398 1.00 29.22 O ANISOU 2885 OE1 GLN B 40 4166 2950 3983 822 -544 -298 O ATOM 2886 NE2 GLN B 40 22.133 -13.883 41.298 1.00 35.85 N ANISOU 2886 NE2 GLN B 40 3954 4701 4966 -56 -162 -688 N ATOM 2887 N GLN B 41 15.824 -12.547 39.281 1.00 14.81 N ANISOU 2887 N GLN B 41 1799 2025 1803 30 35 -414 N ATOM 2888 CA GLN B 41 14.439 -12.922 39.557 1.00 14.47 C ANISOU 2888 CA GLN B 41 1761 1755 1980 170 -37 -536 C ATOM 2889 C GLN B 41 13.552 -12.834 38.327 1.00 14.59 C ANISOU 2889 C GLN B 41 1962 1806 1774 -46 33 -303 C ATOM 2890 O GLN B 41 13.566 -11.833 37.598 1.00 14.84 O ANISOU 2890 O GLN B 41 2074 1861 1701 242 173 -291 O ATOM 2891 CB GLN B 41 13.839 -11.985 40.603 1.00 14.04 C ANISOU 2891 CB GLN B 41 1844 1825 1665 254 99 -287 C ATOM 2892 CG GLN B 41 14.461 -12.003 41.986 1.00 15.11 C ANISOU 2892 CG GLN B 41 1946 1954 1841 162 -130 -277 C ATOM 2893 CD GLN B 41 13.719 -11.063 42.917 1.00 14.16 C ANISOU 2893 CD GLN B 41 1768 1901 1710 -17 -69 -247 C ATOM 2894 OE1 GLN B 41 12.489 -10.973 42.857 1.00 14.74 O ANISOU 2894 OE1 GLN B 41 1825 2014 1761 226 -163 -284 O ATOM 2895 NE2 GLN B 41 14.457 -10.336 43.764 1.00 14.73 N ANISOU 2895 NE2 GLN B 41 2017 1828 1750 106 -216 -310 N ATOM 2896 N ARG B 42 12.741 -13.864 38.126 1.00 13.97 N ANISOU 2896 N ARG B 42 1644 1907 1756 20 -61 -373 N ATOM 2897 CA ARG B 42 11.695 -13.813 37.119 1.00 13.39 C ANISOU 2897 CA ARG B 42 1575 1822 1688 214 15 -200 C ATOM 2898 C ARG B 42 10.406 -14.238 37.803 1.00 12.70 C ANISOU 2898 C ARG B 42 1633 1461 1731 157 -38 -138 C ATOM 2899 O ARG B 42 10.295 -15.366 38.286 1.00 14.03 O ANISOU 2899 O ARG B 42 1848 1507 1976 304 162 23 O ATOM 2900 CB ARG B 42 12.032 -14.728 35.927 1.00 14.92 C ANISOU 2900 CB ARG B 42 1864 2005 1797 -12 168 -334 C ATOM 2901 CG ARG B 42 13.311 -14.354 35.178 1.00 16.25 C ANISOU 2901 CG ARG B 42 2094 2188 1890 139 374 -162 C ATOM 2902 CD ARG B 42 13.136 -13.029 34.462 1.00 16.62 C ANISOU 2902 CD ARG B 42 2016 2319 1978 52 228 16 C ATOM 2903 NE ARG B 42 14.317 -12.614 33.709 1.00 18.73 N ANISOU 2903 NE ARG B 42 2183 2614 2318 -227 401 -97 N ATOM 2904 CZ ARG B 42 15.257 -11.789 34.166 1.00 17.32 C ANISOU 2904 CZ ARG B 42 2187 2673 1717 -77 208 -165 C ATOM 2905 NH1 ARG B 42 16.282 -11.462 33.403 1.00 18.12 N ANISOU 2905 NH1 ARG B 42 2521 2995 1367 -340 171 66 N ATOM 2906 NH2 ARG B 42 15.185 -11.297 35.391 1.00 17.50 N ANISOU 2906 NH2 ARG B 42 2319 2437 1890 -99 89 -364 N ATOM 2907 N LEU B 43 9.445 -13.319 37.877 1.00 12.10 N ANISOU 2907 N LEU B 43 1524 1515 1556 127 166 -247 N ATOM 2908 CA LEU B 43 8.181 -13.614 38.530 1.00 11.21 C ANISOU 2908 CA LEU B 43 1481 1411 1365 90 36 -221 C ATOM 2909 C LEU B 43 7.144 -14.063 37.513 1.00 11.48 C ANISOU 2909 C LEU B 43 1528 1553 1279 58 21 -114 C ATOM 2910 O LEU B 43 7.030 -13.492 36.426 1.00 12.43 O ANISOU 2910 O LEU B 43 1825 1382 1514 125 -45 44 O ATOM 2911 CB LEU B 43 7.686 -12.412 39.353 1.00 11.74 C ANISOU 2911 CB LEU B 43 1498 1365 1598 195 -98 -269 C ATOM 2912 CG LEU B 43 8.478 -12.124 40.629 1.00 13.30 C ANISOU 2912 CG LEU B 43 1779 1604 1670 185 -230 -276 C ATOM 2913 CD1 LEU B 43 8.167 -10.721 41.137 1.00 14.93 C ANISOU 2913 CD1 LEU B 43 2119 1751 1802 386 190 -306 C ATOM 2914 CD2 LEU B 43 8.159 -13.166 41.697 1.00 13.84 C ANISOU 2914 CD2 LEU B 43 1726 1880 1652 152 -23 -221 C ATOM 2915 N ILE B 44 6.409 -15.106 37.898 1.00 11.57 N ANISOU 2915 N ILE B 44 1395 1543 1458 21 52 -235 N ATOM 2916 CA ILE B 44 5.408 -15.761 37.055 1.00 11.27 C ANISOU 2916 CA ILE B 44 1358 1407 1514 66 -88 -53 C ATOM 2917 C ILE B 44 4.084 -15.805 37.822 1.00 12.00 C ANISOU 2917 C ILE B 44 1495 1735 1327 87 -31 84 C ATOM 2918 O ILE B 44 4.076 -16.029 39.030 1.00 12.95 O ANISOU 2918 O ILE B 44 1691 1962 1265 133 -103 61 O ATOM 2919 CB ILE B 44 5.814 -17.219 36.720 1.00 11.26 C ANISOU 2919 CB ILE B 44 1406 1527 1343 73 -18 -298 C ATOM 2920 CG1 ILE B 44 7.287 -17.313 36.278 1.00 11.96 C ANISOU 2920 CG1 ILE B 44 1464 1570 1510 116 98 -57 C ATOM 2921 CG2 ILE B 44 4.864 -17.826 35.700 1.00 12.19 C ANISOU 2921 CG2 ILE B 44 1587 1563 1482 126 -265 -174 C ATOM 2922 CD1 ILE B 44 7.595 -16.626 34.961 1.00 12.66 C ANISOU 2922 CD1 ILE B 44 1762 1449 1598 107 154 -6 C ATOM 2923 N PHE B 45 2.965 -15.577 37.144 1.00 11.18 N ANISOU 2923 N PHE B 45 1375 1570 1301 19 31 -32 N ATOM 2924 CA PHE B 45 1.663 -15.708 37.784 1.00 11.04 C ANISOU 2924 CA PHE B 45 1443 1433 1317 95 142 -240 C ATOM 2925 C PHE B 45 0.813 -16.648 36.952 1.00 11.12 C ANISOU 2925 C PHE B 45 1414 1582 1229 1 99 -125 C ATOM 2926 O PHE B 45 0.428 -16.304 35.835 1.00 11.36 O ANISOU 2926 O PHE B 45 1384 1675 1255 206 76 -96 O ATOM 2927 CB PHE B 45 0.981 -14.344 37.918 1.00 12.46 C ANISOU 2927 CB PHE B 45 1503 1504 1725 213 162 -141 C ATOM 2928 CG PHE B 45 -0.355 -14.386 38.629 1.00 13.96 C ANISOU 2928 CG PHE B 45 1604 1907 1791 163 241 -96 C ATOM 2929 CD1 PHE B 45 -0.548 -15.190 39.758 1.00 15.00 C ANISOU 2929 CD1 PHE B 45 1753 1921 2024 284 374 60 C ATOM 2930 CD2 PHE B 45 -1.414 -13.596 38.184 1.00 15.67 C ANISOU 2930 CD2 PHE B 45 1843 2007 2101 387 223 -98 C ATOM 2931 CE1 PHE B 45 -1.780 -15.217 40.415 1.00 15.43 C ANISOU 2931 CE1 PHE B 45 1685 2157 2020 198 307 -231 C ATOM 2932 CE2 PHE B 45 -2.644 -13.614 38.837 1.00 17.21 C ANISOU 2932 CE2 PHE B 45 1802 2536 2199 506 219 115 C ATOM 2933 CZ PHE B 45 -2.828 -14.425 39.954 1.00 15.30 C ANISOU 2933 CZ PHE B 45 1652 2283 1877 220 345 -241 C ATOM 2934 N ALA B 46 0.552 -17.841 37.490 1.00 11.39 N ANISOU 2934 N ALA B 46 1559 1499 1270 -74 214 -280 N ATOM 2935 CA ALA B 46 -0.259 -18.862 36.822 1.00 11.77 C ANISOU 2935 CA ALA B 46 1467 1672 1332 -170 123 -215 C ATOM 2936 C ALA B 46 0.245 -19.104 35.395 1.00 12.07 C ANISOU 2936 C ALA B 46 1437 1778 1368 -70 205 -20 C ATOM 2937 O ALA B 46 -0.535 -19.229 34.459 1.00 13.33 O ANISOU 2937 O ALA B 46 1418 1870 1774 -142 29 -364 O ATOM 2938 CB ALA B 46 -1.748 -18.490 36.852 1.00 13.41 C ANISOU 2938 CB ALA B 46 1556 1977 1560 -38 354 -336 C ATOM 2939 N GLY B 47 1.569 -19.169 35.254 1.00 11.44 N ANISOU 2939 N GLY B 47 1403 1710 1231 -21 205 -88 N ATOM 2940 CA GLY B 47 2.198 -19.469 33.969 1.00 11.61 C ANISOU 2940 CA GLY B 47 1575 1606 1228 -67 248 -72 C ATOM 2941 C GLY B 47 2.606 -18.261 33.148 1.00 10.59 C ANISOU 2941 C GLY B 47 1402 1347 1273 75 108 -137 C ATOM 2942 O GLY B 47 3.386 -18.412 32.213 1.00 11.44 O ANISOU 2942 O GLY B 47 1351 1565 1429 232 148 -41 O ATOM 2943 N LYS B 48 2.080 -17.072 33.486 1.00 11.45 N ANISOU 2943 N LYS B 48 1571 1358 1421 186 27 -36 N ATOM 2944 CA LYS B 48 2.314 -15.842 32.721 1.00 11.24 C ANISOU 2944 CA LYS B 48 1397 1496 1376 192 19 19 C ATOM 2945 C LYS B 48 3.548 -15.105 33.231 1.00 11.12 C ANISOU 2945 C LYS B 48 1437 1526 1262 126 -38 85 C ATOM 2946 O LYS B 48 3.693 -14.890 34.438 1.00 11.34 O ANISOU 2946 O LYS B 48 1566 1490 1251 108 -29 39 O ATOM 2947 CB LYS B 48 1.089 -14.924 32.827 1.00 12.36 C ANISOU 2947 CB LYS B 48 1607 1435 1654 312 74 111 C ATOM 2948 CG LYS B 48 1.169 -13.654 31.987 1.00 12.62 C ANISOU 2948 CG LYS B 48 1692 1577 1524 442 92 175 C ATOM 2949 CD LYS B 48 0.080 -12.645 32.331 1.00 15.53 C ANISOU 2949 CD LYS B 48 1744 1944 2210 651 -48 -51 C ATOM 2950 CE LYS B 48 -1.297 -13.145 31.939 1.00 16.80 C ANISOU 2950 CE LYS B 48 1811 2262 2307 689 -57 -405 C ATOM 2951 NZ LYS B 48 -2.330 -12.122 32.269 1.00 18.83 N ANISOU 2951 NZ LYS B 48 2138 2785 2231 1116 -4 -365 N ATOM 2952 N GLN B 49 4.435 -14.709 32.316 1.00 11.07 N ANISOU 2952 N GLN B 49 1210 1579 1417 -6 -45 -98 N ATOM 2953 CA GLN B 49 5.605 -13.915 32.668 1.00 11.37 C ANISOU 2953 CA GLN B 49 1373 1615 1331 -127 -4 -126 C ATOM 2954 C GLN B 49 5.197 -12.501 33.094 1.00 12.79 C ANISOU 2954 C GLN B 49 1756 1531 1570 -11 25 44 C ATOM 2955 O GLN B 49 4.461 -11.828 32.376 1.00 15.25 O ANISOU 2955 O GLN B 49 2153 1832 1807 48 -353 -23 O ATOM 2956 CB GLN B 49 6.558 -13.835 31.466 1.00 13.65 C ANISOU 2956 CB GLN B 49 1596 2093 1497 -305 137 162 C ATOM 2957 CG GLN B 49 7.847 -13.058 31.734 1.00 13.84 C ANISOU 2957 CG GLN B 49 1755 1825 1676 -210 -140 -173 C ATOM 2958 CD GLN B 49 8.674 -13.659 32.857 1.00 13.67 C ANISOU 2958 CD GLN B 49 1914 1686 1591 35 -104 -372 C ATOM 2959 OE1 GLN B 49 9.146 -14.789 32.750 1.00 16.08 O ANISOU 2959 OE1 GLN B 49 2237 1734 2136 128 -115 -532 O ATOM 2960 NE2 GLN B 49 8.861 -12.899 33.947 1.00 13.67 N ANISOU 2960 NE2 GLN B 49 1885 1524 1782 37 -23 -505 N ATOM 2961 N LEU B 50 5.674 -12.058 34.257 1.00 13.01 N ANISOU 2961 N LEU B 50 1717 1515 1711 114 50 -149 N ATOM 2962 CA LEU B 50 5.429 -10.693 34.727 1.00 13.07 C ANISOU 2962 CA LEU B 50 1853 1567 1544 95 229 -131 C ATOM 2963 C LEU B 50 6.617 -9.796 34.372 1.00 13.09 C ANISOU 2963 C LEU B 50 1886 1703 1381 61 141 21 C ATOM 2964 O LEU B 50 7.775 -10.208 34.473 1.00 15.11 O ANISOU 2964 O LEU B 50 1865 1763 2111 15 -25 -43 O ATOM 2965 CB LEU B 50 5.176 -10.697 36.238 1.00 12.70 C ANISOU 2965 CB LEU B 50 1910 1421 1492 -16 140 -87 C ATOM 2966 CG LEU B 50 4.143 -11.716 36.752 1.00 13.01 C ANISOU 2966 CG LEU B 50 1745 1572 1624 52 220 0 C ATOM 2967 CD1 LEU B 50 3.916 -11.550 38.249 1.00 15.65 C ANISOU 2967 CD1 LEU B 50 2101 2264 1581 240 81 -65 C ATOM 2968 CD2 LEU B 50 2.814 -11.605 36.010 1.00 13.80 C ANISOU 2968 CD2 LEU B 50 2003 1612 1628 34 4 -57 C ATOM 2969 N GLU B 51 6.333 -8.575 33.930 1.00 15.41 N ANISOU 2969 N GLU B 51 2270 1574 2009 69 601 100 N ATOM 2970 CA GLU B 51 7.393 -7.675 33.477 1.00 17.18 C ANISOU 2970 CA GLU B 51 2266 2153 2106 -200 604 -25 C ATOM 2971 C GLU B 51 7.612 -6.530 34.471 1.00 16.64 C ANISOU 2971 C GLU B 51 2330 1772 2219 -55 648 99 C ATOM 2972 O GLU B 51 6.655 -6.011 35.043 1.00 18.41 O ANISOU 2972 O GLU B 51 2369 1973 2652 186 695 206 O ATOM 2973 CB GLU B 51 7.093 -7.155 32.062 1.00 21.38 C ANISOU 2973 CB GLU B 51 2753 3038 2330 -305 473 386 C ATOM 2974 CG GLU B 51 6.906 -8.245 30.993 1.00 23.44 C ANISOU 2974 CG GLU B 51 2891 3431 2583 170 757 -49 C ATOM 2975 CD GLU B 51 8.178 -9.008 30.611 1.00 27.14 C ANISOU 2975 CD GLU B 51 3055 3617 3638 352 672 -224 C ATOM 2976 OE1 GLU B 51 9.291 -8.553 30.948 1.00 29.36 O ANISOU 2976 OE1 GLU B 51 3347 3909 3898 250 427 -706 O ATOM 2977 OE2 GLU B 51 8.072 -10.075 29.951 1.00 26.55 O ANISOU 2977 OE2 GLU B 51 2635 3438 4014 89 910 -32 O ATOM 2978 N ASP B 52 8.876 -6.143 34.659 1.00 17.87 N ANISOU 2978 N ASP B 52 2450 1770 2568 -161 587 -141 N ATOM 2979 CA ASP B 52 9.299 -5.190 35.705 1.00 17.94 C ANISOU 2979 CA ASP B 52 2357 1934 2524 60 386 -140 C ATOM 2980 C ASP B 52 8.519 -3.881 35.797 1.00 17.63 C ANISOU 2980 C ASP B 52 2667 1931 2098 162 666 -100 C ATOM 2981 O ASP B 52 8.230 -3.394 36.897 1.00 19.62 O ANISOU 2981 O ASP B 52 3286 2137 2030 121 824 -45 O ATOM 2982 CB ASP B 52 10.778 -4.846 35.523 1.00 20.60 C ANISOU 2982 CB ASP B 52 2505 2357 2962 -270 661 -32 C ATOM 2983 CG ASP B 52 11.690 -5.955 35.970 1.00 25.35 C ANISOU 2983 CG ASP B 52 2637 2940 4052 395 341 -677 C ATOM 2984 OD1 ASP B 52 12.916 -5.727 36.026 1.00 33.22 O ANISOU 2984 OD1 ASP B 52 2694 3929 5997 315 -186 -1132 O ATOM 2985 OD2 ASP B 52 11.190 -7.054 36.262 1.00 28.30 O ANISOU 2985 OD2 ASP B 52 3321 3393 4037 304 189 163 O ATOM 2986 N GLY B 53 8.231 -3.293 34.642 1.00 19.10 N ANISOU 2986 N GLY B 53 2836 1817 2602 264 640 441 N ATOM 2987 CA GLY B 53 7.608 -1.977 34.578 1.00 19.41 C ANISOU 2987 CA GLY B 53 2592 1909 2872 367 604 -102 C ATOM 2988 C GLY B 53 6.102 -1.975 34.743 1.00 18.86 C ANISOU 2988 C GLY B 53 2528 1716 2922 377 435 -2 C ATOM 2989 O GLY B 53 5.497 -0.915 34.891 1.00 22.49 O ANISOU 2989 O GLY B 53 3232 1825 3487 681 326 -83 O ATOM 2990 N ARG B 54 5.491 -3.156 34.705 1.00 17.31 N ANISOU 2990 N ARG B 54 2486 1833 2255 267 391 12 N ATOM 2991 CA ARG B 54 4.049 -3.282 34.892 1.00 16.48 C ANISOU 2991 CA ARG B 54 2516 1699 2045 358 365 -27 C ATOM 2992 C ARG B 54 3.746 -3.426 36.383 1.00 16.27 C ANISOU 2992 C ARG B 54 2226 1894 2059 450 331 64 C ATOM 2993 O ARG B 54 4.666 -3.545 37.194 1.00 16.57 O ANISOU 2993 O ARG B 54 2299 1924 2073 480 295 -173 O ATOM 2994 CB ARG B 54 3.497 -4.455 34.075 1.00 17.96 C ANISOU 2994 CB ARG B 54 2982 1780 2059 189 360 -117 C ATOM 2995 CG ARG B 54 3.724 -4.305 32.573 1.00 23.27 C ANISOU 2995 CG ARG B 54 3814 2904 2121 84 543 -267 C ATOM 2996 CD ARG B 54 2.419 -4.036 31.845 1.00 29.53 C ANISOU 2996 CD ARG B 54 4072 4104 3042 -175 134 290 C ATOM 2997 NE ARG B 54 1.682 -5.280 31.619 1.00 34.41 N ANISOU 2997 NE ARG B 54 5173 4048 3851 61 -263 -905 N ATOM 2998 CZ ARG B 54 0.431 -5.356 31.170 1.00 38.61 C ANISOU 2998 CZ ARG B 54 5279 4349 5041 -669 -490 -818 C ATOM 2999 NH1 ARG B 54 -0.138 -6.544 31.006 1.00 41.54 N ANISOU 2999 NH1 ARG B 54 7751 3711 4318 -320 -1029 -1739 N ATOM 3000 NH2 ARG B 54 -0.255 -4.254 30.887 1.00 42.98 N ANISOU 3000 NH2 ARG B 54 5431 5480 5419 58 -238 63 N ATOM 3001 N THR B 55 2.464 -3.385 36.732 1.00 14.61 N ANISOU 3001 N THR B 55 2198 1592 1758 213 375 186 N ATOM 3002 CA THR B 55 2.035 -3.405 38.131 1.00 13.90 C ANISOU 3002 CA THR B 55 2133 1430 1716 335 304 42 C ATOM 3003 C THR B 55 1.243 -4.663 38.461 1.00 14.24 C ANISOU 3003 C THR B 55 1982 1672 1754 202 174 77 C ATOM 3004 O THR B 55 0.723 -5.352 37.577 1.00 15.04 O ANISOU 3004 O THR B 55 2402 1605 1706 375 134 3 O ATOM 3005 CB THR B 55 1.157 -2.181 38.484 1.00 14.43 C ANISOU 3005 CB THR B 55 1957 1511 2011 367 271 131 C ATOM 3006 OG1 THR B 55 -0.062 -2.228 37.733 1.00 15.32 O ANISOU 3006 OG1 THR B 55 2168 1464 2185 243 62 -36 O ATOM 3007 CG2 THR B 55 1.909 -0.881 38.211 1.00 13.81 C ANISOU 3007 CG2 THR B 55 1933 1613 1698 267 261 168 C ATOM 3008 N LEU B 56 1.123 -4.945 39.751 1.00 13.55 N ANISOU 3008 N LEU B 56 2048 1381 1716 198 165 -6 N ATOM 3009 CA LEU B 56 0.289 -6.054 40.178 1.00 13.41 C ANISOU 3009 CA LEU B 56 2276 1469 1349 -62 46 -178 C ATOM 3010 C LEU B 56 -1.134 -5.937 39.620 1.00 15.10 C ANISOU 3010 C LEU B 56 2348 1566 1823 -17 -114 -208 C ATOM 3011 O LEU B 56 -1.693 -6.926 39.151 1.00 15.18 O ANISOU 3011 O LEU B 56 2792 1416 1560 -104 -231 -91 O ATOM 3012 CB LEU B 56 0.287 -6.171 41.700 1.00 13.65 C ANISOU 3012 CB LEU B 56 2166 1654 1364 207 37 41 C ATOM 3013 CG LEU B 56 1.634 -6.499 42.350 1.00 13.37 C ANISOU 3013 CG LEU B 56 2227 1479 1372 307 -20 -131 C ATOM 3014 CD1 LEU B 56 1.466 -6.436 43.857 1.00 13.99 C ANISOU 3014 CD1 LEU B 56 2137 1775 1402 297 246 108 C ATOM 3015 CD2 LEU B 56 2.140 -7.875 41.944 1.00 14.31 C ANISOU 3015 CD2 LEU B 56 2418 1600 1417 335 145 -274 C ATOM 3016 N SER B 57 -1.696 -4.727 39.647 1.00 14.38 N ANISOU 3016 N SER B 57 2049 1745 1668 117 -81 -111 N ATOM 3017 CA SER B 57 -3.030 -4.455 39.127 1.00 15.06 C ANISOU 3017 CA SER B 57 2170 1678 1873 23 -259 -132 C ATOM 3018 C SER B 57 -3.141 -4.833 37.647 1.00 15.13 C ANISOU 3018 C SER B 57 2053 1817 1877 13 -159 -221 C ATOM 3019 O SER B 57 -4.158 -5.384 37.236 1.00 15.70 O ANISOU 3019 O SER B 57 2159 1627 2176 -99 -235 -144 O ATOM 3020 CB SER B 57 -3.381 -2.972 39.320 1.00 16.76 C ANISOU 3020 CB SER B 57 2311 1931 2127 445 -410 -448 C ATOM 3021 OG SER B 57 -4.685 -2.670 38.835 1.00 20.15 O ANISOU 3021 OG SER B 57 1993 2379 3282 -177 -438 -153 O ATOM 3022 N ASP B 58 -2.098 -4.554 36.858 1.00 15.73 N ANISOU 3022 N ASP B 58 2316 1941 1719 -103 -156 23 N ATOM 3023 CA ASP B 58 -2.090 -4.888 35.413 1.00 16.25 C ANISOU 3023 CA ASP B 58 2251 2146 1776 -57 -122 -161 C ATOM 3024 C ASP B 58 -2.334 -6.369 35.139 1.00 15.99 C ANISOU 3024 C ASP B 58 2143 2092 1838 53 -249 14 C ATOM 3025 O ASP B 58 -2.844 -6.739 34.077 1.00 18.66 O ANISOU 3025 O ASP B 58 2994 2081 2011 111 -564 -83 O ATOM 3026 CB ASP B 58 -0.761 -4.490 34.755 1.00 16.36 C ANISOU 3026 CB ASP B 58 2477 2121 1618 -2 -36 276 C ATOM 3027 CG ASP B 58 -0.605 -2.996 34.600 1.00 19.98 C ANISOU 3027 CG ASP B 58 2876 2136 2578 56 -143 300 C ATOM 3028 OD1 ASP B 58 0.524 -2.497 34.811 1.00 19.63 O ANISOU 3028 OD1 ASP B 58 2644 2198 2614 320 -162 224 O ATOM 3029 OD2 ASP B 58 -1.602 -2.326 34.253 1.00 23.16 O ANISOU 3029 OD2 ASP B 58 2758 2759 3280 125 -22 643 O ATOM 3030 N TYR B 59 -1.930 -7.200 36.097 1.00 13.98 N ANISOU 3030 N TYR B 59 1784 1683 1842 51 207 81 N ATOM 3031 CA TYR B 59 -2.037 -8.645 35.989 1.00 13.35 C ANISOU 3031 CA TYR B 59 1832 1752 1487 37 0 -90 C ATOM 3032 C TYR B 59 -3.212 -9.228 36.769 1.00 14.05 C ANISOU 3032 C TYR B 59 1897 2054 1386 -127 55 -326 C ATOM 3033 O TYR B 59 -3.369 -10.444 36.835 1.00 15.37 O ANISOU 3033 O TYR B 59 1999 2003 1835 -44 203 -364 O ATOM 3034 CB TYR B 59 -0.724 -9.301 36.415 1.00 14.68 C ANISOU 3034 CB TYR B 59 1824 1917 1837 150 178 85 C ATOM 3035 CG TYR B 59 0.448 -8.919 35.552 1.00 14.26 C ANISOU 3035 CG TYR B 59 1984 1668 1765 34 160 113 C ATOM 3036 CD1 TYR B 59 0.552 -9.385 34.237 1.00 15.42 C ANISOU 3036 CD1 TYR B 59 2276 1733 1848 141 234 50 C ATOM 3037 CD2 TYR B 59 1.453 -8.088 36.043 1.00 15.57 C ANISOU 3037 CD2 TYR B 59 1920 1561 2431 116 192 36 C ATOM 3038 CE1 TYR B 59 1.630 -9.036 33.444 1.00 15.91 C ANISOU 3038 CE1 TYR B 59 2319 1702 2021 241 310 271 C ATOM 3039 CE2 TYR B 59 2.536 -7.739 35.260 1.00 15.87 C ANISOU 3039 CE2 TYR B 59 2198 1575 2257 166 330 110 C ATOM 3040 CZ TYR B 59 2.614 -8.201 33.960 1.00 15.37 C ANISOU 3040 CZ TYR B 59 2071 1562 2206 412 319 212 C ATOM 3041 OH TYR B 59 3.704 -7.864 33.187 1.00 17.55 O ANISOU 3041 OH TYR B 59 2223 1972 2472 383 502 341 O ATOM 3042 N ASN B 60 -4.035 -8.353 37.346 1.00 14.14 N ANISOU 3042 N ASN B 60 1679 2161 1531 12 2 -175 N ATOM 3043 CA ASN B 60 -5.154 -8.757 38.205 1.00 16.34 C ANISOU 3043 CA ASN B 60 1842 2287 2076 -299 190 -364 C ATOM 3044 C ASN B 60 -4.670 -9.634 39.362 1.00 16.38 C ANISOU 3044 C ASN B 60 2037 2345 1842 -392 190 -364 C ATOM 3045 O ASN B 60 -5.309 -10.627 39.743 1.00 17.83 O ANISOU 3045 O ASN B 60 2392 2547 1835 -497 337 -154 O ATOM 3046 CB ASN B 60 -6.277 -9.441 37.405 1.00 18.03 C ANISOU 3046 CB ASN B 60 2118 2627 2105 -364 46 -573 C ATOM 3047 CG ASN B 60 -7.555 -9.578 38.205 1.00 20.03 C ANISOU 3047 CG ASN B 60 2366 2748 2497 -348 331 -586 C ATOM 3048 OD1 ASN B 60 -7.860 -8.746 39.070 1.00 21.59 O ANISOU 3048 OD1 ASN B 60 2407 2956 2838 -181 314 -752 O ATOM 3049 ND2 ASN B 60 -8.303 -10.641 37.939 1.00 24.34 N ANISOU 3049 ND2 ASN B 60 2786 3232 3227 -872 28 -420 N ATOM 3050 N ILE B 61 -3.524 -9.261 39.922 1.00 14.49 N ANISOU 3050 N ILE B 61 1922 2198 1381 41 136 -346 N ATOM 3051 CA ILE B 61 -3.004 -9.957 41.077 1.00 14.84 C ANISOU 3051 CA ILE B 61 2012 2186 1437 48 347 -110 C ATOM 3052 C ILE B 61 -3.667 -9.333 42.296 1.00 14.76 C ANISOU 3052 C ILE B 61 2071 1884 1653 79 272 -317 C ATOM 3053 O ILE B 61 -3.405 -8.176 42.634 1.00 16.00 O ANISOU 3053 O ILE B 61 2344 1844 1889 152 234 -367 O ATOM 3054 CB ILE B 61 -1.472 -9.885 41.139 1.00 14.29 C ANISOU 3054 CB ILE B 61 2005 2015 1409 196 265 -54 C ATOM 3055 CG1 ILE B 61 -0.880 -10.681 39.963 1.00 15.81 C ANISOU 3055 CG1 ILE B 61 2210 2097 1698 143 564 -119 C ATOM 3056 CG2 ILE B 61 -0.963 -10.411 42.477 1.00 15.63 C ANISOU 3056 CG2 ILE B 61 2471 1917 1549 -12 133 135 C ATOM 3057 CD1 ILE B 61 0.575 -10.395 39.676 1.00 16.51 C ANISOU 3057 CD1 ILE B 61 2091 1923 2257 242 489 -266 C ATOM 3058 N GLN B 62 -4.567 -10.097 42.906 1.00 15.93 N ANISOU 3058 N GLN B 62 2321 2098 1632 184 395 7 N ATOM 3059 CA GLN B 62 -5.350 -9.630 44.040 1.00 16.30 C ANISOU 3059 CA GLN B 62 2114 2135 1944 222 371 -228 C ATOM 3060 C GLN B 62 -4.881 -10.278 45.338 1.00 15.85 C ANISOU 3060 C GLN B 62 1845 2116 2061 269 283 -163 C ATOM 3061 O GLN B 62 -3.931 -11.062 45.347 1.00 15.96 O ANISOU 3061 O GLN B 62 1971 1965 2126 313 435 105 O ATOM 3062 CB GLN B 62 -6.838 -9.909 43.803 1.00 18.31 C ANISOU 3062 CB GLN B 62 2278 2703 1974 74 -20 -279 C ATOM 3063 CG GLN B 62 -7.392 -9.213 42.568 1.00 21.05 C ANISOU 3063 CG GLN B 62 3173 2860 1962 201 -176 -312 C ATOM 3064 CD GLN B 62 -8.848 -9.544 42.309 1.00 25.00 C ANISOU 3064 CD GLN B 62 3344 3325 2829 -137 -239 -95 C ATOM 3065 OE1 GLN B 62 -9.216 -10.706 42.158 1.00 27.98 O ANISOU 3065 OE1 GLN B 62 3584 3413 3633 -182 -159 -399 O ATOM 3066 NE2 GLN B 62 -9.680 -8.518 42.242 1.00 32.83 N ANISOU 3066 NE2 GLN B 62 4178 3899 4395 511 -74 -246 N ATOM 3067 N LYS B 63 -5.555 -9.959 46.439 1.00 15.67 N ANISOU 3067 N LYS B 63 1963 2009 1982 203 263 -143 N ATOM 3068 CA LYS B 63 -5.128 -10.447 47.746 1.00 14.36 C ANISOU 3068 CA LYS B 63 1783 1820 1851 27 346 -141 C ATOM 3069 C LYS B 63 -5.051 -11.970 47.795 1.00 14.73 C ANISOU 3069 C LYS B 63 1854 1881 1860 178 48 -92 C ATOM 3070 O LYS B 63 -5.894 -12.674 47.218 1.00 14.82 O ANISOU 3070 O LYS B 63 1927 1862 1840 200 37 -63 O ATOM 3071 CB LYS B 63 -6.046 -9.914 48.848 1.00 17.72 C ANISOU 3071 CB LYS B 63 2144 2468 2122 310 387 -541 C ATOM 3072 CG LYS B 63 -7.493 -10.361 48.722 1.00 18.42 C ANISOU 3072 CG LYS B 63 2185 2658 2154 294 273 -343 C ATOM 3073 CD LYS B 63 -8.362 -9.645 49.740 1.00 21.01 C ANISOU 3073 CD LYS B 63 2669 2922 2390 317 371 -731 C ATOM 3074 CE LYS B 63 -9.772 -10.218 49.730 1.00 27.21 C ANISOU 3074 CE LYS B 63 2838 4184 3318 -124 417 -688 C ATOM 3075 NZ LYS B 63 -10.516 -9.891 48.483 1.00 35.85 N ANISOU 3075 NZ LYS B 63 4510 5281 3829 -115 -298 -465 N ATOM 3076 N GLU B 64 -4.012 -12.461 48.472 1.00 13.48 N ANISOU 3076 N GLU B 64 1796 1693 1630 224 225 99 N ATOM 3077 CA GLU B 64 -3.772 -13.898 48.672 1.00 14.07 C ANISOU 3077 CA GLU B 64 2025 1689 1632 248 72 -58 C ATOM 3078 C GLU B 64 -3.352 -14.655 47.410 1.00 13.36 C ANISOU 3078 C GLU B 64 1785 1689 1600 167 -54 -94 C ATOM 3079 O GLU B 64 -3.263 -15.875 47.438 1.00 14.66 O ANISOU 3079 O GLU B 64 1997 1686 1888 55 -27 50 O ATOM 3080 CB GLU B 64 -4.949 -14.593 49.375 1.00 17.46 C ANISOU 3080 CB GLU B 64 2339 2030 2263 37 306 -31 C ATOM 3081 CG GLU B 64 -4.934 -14.415 50.885 1.00 21.95 C ANISOU 3081 CG GLU B 64 2991 3044 2304 28 593 85 C ATOM 3082 CD GLU B 64 -5.371 -13.028 51.314 1.00 21.62 C ANISOU 3082 CD GLU B 64 2807 2833 2574 -62 569 352 C ATOM 3083 OE1 GLU B 64 -6.489 -12.617 50.948 1.00 25.65 O ANISOU 3083 OE1 GLU B 64 2721 3634 3391 -39 363 322 O ATOM 3084 OE2 GLU B 64 -4.605 -12.353 52.028 1.00 25.90 O ANISOU 3084 OE2 GLU B 64 3718 3617 2506 -302 268 132 O ATOM 3085 N SER B 65 -3.077 -13.933 46.322 1.00 13.10 N ANISOU 3085 N SER B 65 1674 1869 1434 147 105 -232 N ATOM 3086 CA SER B 65 -2.476 -14.542 45.130 1.00 13.02 C ANISOU 3086 CA SER B 65 1814 1742 1390 385 87 -85 C ATOM 3087 C SER B 65 -1.110 -15.139 45.442 1.00 12.58 C ANISOU 3087 C SER B 65 1651 1683 1445 178 64 -7 C ATOM 3088 O SER B 65 -0.382 -14.644 46.303 1.00 12.92 O ANISOU 3088 O SER B 65 1719 1640 1549 248 -27 -32 O ATOM 3089 CB SER B 65 -2.283 -13.508 44.022 1.00 13.93 C ANISOU 3089 CB SER B 65 1823 1839 1631 297 27 100 C ATOM 3090 OG SER B 65 -3.514 -13.010 43.546 1.00 15.54 O ANISOU 3090 OG SER B 65 2077 2037 1788 631 -109 -58 O ATOM 3091 N THR B 66 -0.766 -16.201 44.720 1.00 12.70 N ANISOU 3091 N THR B 66 1695 1659 1469 335 29 46 N ATOM 3092 CA THR B 66 0.568 -16.775 44.777 1.00 12.47 C ANISOU 3092 CA THR B 66 1695 1560 1481 307 136 107 C ATOM 3093 C THR B 66 1.257 -16.593 43.437 1.00 12.23 C ANISOU 3093 C THR B 66 1575 1617 1455 154 91 -39 C ATOM 3094 O THR B 66 0.712 -16.987 42.397 1.00 13.98 O ANISOU 3094 O THR B 66 1624 1956 1729 206 -107 -192 O ATOM 3095 CB THR B 66 0.512 -18.278 45.114 1.00 13.23 C ANISOU 3095 CB THR B 66 1858 1549 1618 103 267 83 C ATOM 3096 OG1 THR B 66 -0.162 -18.460 46.370 1.00 13.98 O ANISOU 3096 OG1 THR B 66 2183 1685 1443 72 179 238 O ATOM 3097 CG2 THR B 66 1.909 -18.856 45.215 1.00 14.85 C ANISOU 3097 CG2 THR B 66 1880 1925 1835 261 269 25 C ATOM 3098 N LEU B 67 2.446 -15.991 43.480 1.00 12.63 N ANISOU 3098 N LEU B 67 1679 1504 1615 129 214 -3 N ATOM 3099 CA LEU B 67 3.334 -15.902 42.323 1.00 12.21 C ANISOU 3099 CA LEU B 67 1656 1376 1607 66 212 -159 C ATOM 3100 C LEU B 67 4.398 -16.965 42.457 1.00 12.33 C ANISOU 3100 C LEU B 67 1727 1556 1403 182 62 -176 C ATOM 3101 O LEU B 67 4.619 -17.478 43.552 1.00 13.70 O ANISOU 3101 O LEU B 67 2010 1818 1375 253 59 -86 O ATOM 3102 CB LEU B 67 4.023 -14.540 42.290 1.00 12.55 C ANISOU 3102 CB LEU B 67 1855 1265 1646 104 12 -7 C ATOM 3103 CG LEU B 67 3.150 -13.303 42.481 1.00 13.97 C ANISOU 3103 CG LEU B 67 1803 1401 2103 141 89 -224 C ATOM 3104 CD1 LEU B 67 3.994 -12.057 42.307 1.00 14.86 C ANISOU 3104 CD1 LEU B 67 2090 1299 2254 104 161 -40 C ATOM 3105 CD2 LEU B 67 1.967 -13.273 41.531 1.00 16.29 C ANISOU 3105 CD2 LEU B 67 2231 1633 2323 102 -243 -212 C ATOM 3106 N HIS B 68 5.044 -17.302 41.348 1.00 12.29 N ANISOU 3106 N HIS B 68 1664 1554 1452 253 100 -141 N ATOM 3107 CA HIS B 68 6.203 -18.195 41.377 1.00 12.06 C ANISOU 3107 CA HIS B 68 1480 1455 1646 106 16 -308 C ATOM 3108 C HIS B 68 7.424 -17.444 40.981 1.00 11.60 C ANISOU 3108 C HIS B 68 1529 1536 1342 60 -29 -124 C ATOM 3109 O HIS B 68 7.429 -16.705 39.983 1.00 13.52 O ANISOU 3109 O HIS B 68 1796 1685 1656 -56 -177 115 O ATOM 3110 CB HIS B 68 5.998 -19.398 40.465 1.00 13.97 C ANISOU 3110 CB HIS B 68 1922 1476 1910 -40 32 -381 C ATOM 3111 CG HIS B 68 4.901 -20.299 40.941 1.00 14.40 C ANISOU 3111 CG HIS B 68 1661 1570 2239 19 6 -272 C ATOM 3112 ND1 HIS B 68 5.127 -21.456 41.598 1.00 19.31 N ANISOU 3112 ND1 HIS B 68 2407 2073 2856 -73 -103 247 N ATOM 3113 CD2 HIS B 68 3.527 -20.129 40.908 1.00 13.41 C ANISOU 3113 CD2 HIS B 68 1645 1514 1934 266 -141 -87 C ATOM 3114 CE1 HIS B 68 3.942 -22.011 41.927 1.00 16.59 C ANISOU 3114 CE1 HIS B 68 2374 1620 2307 -109 -175 -76 C ATOM 3115 NE2 HIS B 68 2.971 -21.198 41.508 1.00 18.92 N ANISOU 3115 NE2 HIS B 68 2573 2017 2596 -51 6 290 N ATOM 3116 N LEU B 69 8.474 -17.626 41.766 1.00 13.12 N ANISOU 3116 N LEU B 69 1617 1698 1669 145 -184 -280 N ATOM 3117 CA LEU B 69 9.744 -17.022 41.462 1.00 13.27 C ANISOU 3117 CA LEU B 69 1671 1939 1432 114 -241 -195 C ATOM 3118 C LEU B 69 10.622 -18.064 40.805 1.00 12.66 C ANISOU 3118 C LEU B 69 1563 1650 1595 110 -226 27 C ATOM 3119 O LEU B 69 10.965 -19.078 41.415 1.00 15.24 O ANISOU 3119 O LEU B 69 2062 1865 1861 524 -142 117 O ATOM 3120 CB LEU B 69 10.391 -16.498 42.747 1.00 13.53 C ANISOU 3120 CB LEU B 69 1950 1879 1310 34 -245 -102 C ATOM 3121 CG LEU B 69 11.793 -15.916 42.597 1.00 14.46 C ANISOU 3121 CG LEU B 69 1964 1917 1613 -39 -336 -10 C ATOM 3122 CD1 LEU B 69 11.737 -14.627 41.795 1.00 15.31 C ANISOU 3122 CD1 LEU B 69 2120 1929 1768 66 -215 44 C ATOM 3123 CD2 LEU B 69 12.427 -15.677 43.959 1.00 17.07 C ANISOU 3123 CD2 LEU B 69 2566 2240 1680 83 -580 8 C ATOM 3124 N VAL B 70 10.925 -17.841 39.535 1.00 13.06 N ANISOU 3124 N VAL B 70 1649 1799 1515 147 -111 -344 N ATOM 3125 CA VAL B 70 11.871 -18.683 38.809 1.00 12.60 C ANISOU 3125 CA VAL B 70 1446 1768 1572 143 -92 -203 C ATOM 3126 C VAL B 70 13.105 -17.825 38.562 1.00 13.71 C ANISOU 3126 C VAL B 70 1608 1731 1867 33 -191 -250 C ATOM 3127 O VAL B 70 13.130 -16.651 38.946 1.00 14.98 O ANISOU 3127 O VAL B 70 1847 1562 2281 -18 -263 -78 O ATOM 3128 CB VAL B 70 11.261 -19.290 37.517 1.00 13.50 C ANISOU 3128 CB VAL B 70 1514 1777 1835 39 -219 -269 C ATOM 3129 CG1 VAL B 70 9.993 -20.056 37.869 1.00 15.00 C ANISOU 3129 CG1 VAL B 70 1639 1864 2194 -106 -144 -372 C ATOM 3130 CG2 VAL B 70 11.001 -18.233 36.445 1.00 14.80 C ANISOU 3130 CG2 VAL B 70 1848 2120 1654 37 -204 -198 C ATOM 3131 N LEU B 71 14.133 -18.399 37.953 1.00 13.73 N ANISOU 3131 N LEU B 71 1477 1949 1788 -66 -81 -91 N ATOM 3132 CA LEU B 71 15.393 -17.679 37.812 1.00 14.43 C ANISOU 3132 CA LEU B 71 1444 2120 1919 -49 28 -44 C ATOM 3133 C LEU B 71 15.801 -17.630 36.356 1.00 13.37 C ANISOU 3133 C LEU B 71 1558 1749 1773 -104 -21 -342 C ATOM 3134 O LEU B 71 15.524 -18.559 35.591 1.00 16.89 O ANISOU 3134 O LEU B 71 2212 2175 2028 -505 414 -685 O ATOM 3135 CB LEU B 71 16.494 -18.313 38.672 1.00 15.05 C ANISOU 3135 CB LEU B 71 1797 2105 1813 191 13 -54 C ATOM 3136 CG LEU B 71 16.260 -18.321 40.189 1.00 16.75 C ANISOU 3136 CG LEU B 71 2274 2318 1771 229 -223 -68 C ATOM 3137 CD1 LEU B 71 17.321 -19.185 40.844 1.00 19.89 C ANISOU 3137 CD1 LEU B 71 2095 2887 2575 164 -503 210 C ATOM 3138 CD2 LEU B 71 16.247 -16.925 40.809 1.00 19.97 C ANISOU 3138 CD2 LEU B 71 2606 2350 2628 -68 -547 -289 C ATOM 3139 N ARG B 72 16.448 -16.539 35.960 1.00 12.79 N ANISOU 3139 N ARG B 72 1743 1571 1543 68 108 -301 N ATOM 3140 CA ARG B 72 16.943 -16.440 34.596 1.00 13.09 C ANISOU 3140 CA ARG B 72 1631 1777 1564 148 102 -136 C ATOM 3141 C ARG B 72 17.997 -17.529 34.364 1.00 13.24 C ANISOU 3141 C ARG B 72 1722 1799 1508 182 26 -296 C ATOM 3142 O ARG B 72 18.818 -17.827 35.244 1.00 16.12 O ANISOU 3142 O ARG B 72 1915 2440 1767 228 -111 -177 O ATOM 3143 CB ARG B 72 17.518 -15.054 34.311 1.00 15.44 C ANISOU 3143 CB ARG B 72 2017 1803 2045 -52 -127 -148 C ATOM 3144 CG ARG B 72 18.813 -14.746 35.026 1.00 16.03 C ANISOU 3144 CG ARG B 72 2046 1777 2265 -47 -153 -214 C ATOM 3145 CD ARG B 72 19.327 -13.374 34.660 1.00 17.88 C ANISOU 3145 CD ARG B 72 2593 1866 2335 -258 -104 -166 C ATOM 3146 NE ARG B 72 20.532 -13.060 35.417 1.00 19.52 N ANISOU 3146 NE ARG B 72 2383 2390 2643 -572 203 -609 N ATOM 3147 CZ ARG B 72 21.245 -11.944 35.277 1.00 21.43 C ANISOU 3147 CZ ARG B 72 2447 2101 3592 -300 245 -325 C ATOM 3148 NH1 ARG B 72 20.886 -11.018 34.397 1.00 25.68 N ANISOU 3148 NH1 ARG B 72 3247 2650 3858 -64 156 -41 N ATOM 3149 NH2 ARG B 72 22.327 -11.763 36.017 1.00 28.51 N ANISOU 3149 NH2 ARG B 72 2796 3580 4455 -643 -200 -675 N ATOM 3150 N LEU B 73 17.954 -18.150 33.193 1.00 11.52 N ANISOU 3150 N LEU B 73 1338 1620 1419 127 102 -185 N ATOM 3151 CA LEU B 73 18.972 -19.119 32.849 1.00 11.46 C ANISOU 3151 CA LEU B 73 1297 1547 1508 133 -17 -172 C ATOM 3152 C LEU B 73 20.207 -18.407 32.327 1.00 11.60 C ANISOU 3152 C LEU B 73 1361 1527 1519 -4 -199 -73 C ATOM 3153 O LEU B 73 20.121 -17.311 31.773 1.00 13.42 O ANISOU 3153 O LEU B 73 1500 1798 1799 -16 -15 238 O ATOM 3154 CB LEU B 73 18.440 -20.140 31.844 1.00 11.99 C ANISOU 3154 CB LEU B 73 1359 1505 1690 -13 -28 -184 C ATOM 3155 CG LEU B 73 17.312 -21.023 32.399 1.00 11.51 C ANISOU 3155 CG LEU B 73 1326 1444 1603 25 -98 -57 C ATOM 3156 CD1 LEU B 73 16.723 -21.929 31.334 1.00 12.66 C ANISOU 3156 CD1 LEU B 73 1345 2000 1461 -213 30 -161 C ATOM 3157 CD2 LEU B 73 17.803 -21.868 33.573 1.00 14.35 C ANISOU 3157 CD2 LEU B 73 2199 1663 1590 -37 7 198 C ATOM 3158 N ARG B 74 21.352 -19.047 32.503 1.00 12.20 N ANISOU 3158 N ARG B 74 1304 1740 1591 30 -140 -35 N ATOM 3159 CA ARG B 74 22.642 -18.437 32.197 1.00 12.99 C ANISOU 3159 CA ARG B 74 1356 1776 1803 -17 -40 -85 C ATOM 3160 C ARG B 74 23.395 -19.332 31.223 1.00 12.76 C ANISOU 3160 C ARG B 74 1343 1805 1700 -61 -48 -77 C ATOM 3161 O ARG B 74 24.462 -19.855 31.526 1.00 12.93 O ANISOU 3161 O ARG B 74 1476 1771 1663 49 -103 -55 O ATOM 3162 CB ARG B 74 23.424 -18.188 33.491 1.00 14.91 C ANISOU 3162 CB ARG B 74 1594 2250 1821 -130 -62 -228 C ATOM 3163 CG ARG B 74 22.717 -17.250 34.460 1.00 17.09 C ANISOU 3163 CG ARG B 74 1966 2312 2212 -202 121 -419 C ATOM 3164 CD ARG B 74 22.530 -15.861 33.875 1.00 19.47 C ANISOU 3164 CD ARG B 74 2381 2327 2687 -167 165 -401 C ATOM 3165 NE ARG B 74 23.749 -15.065 33.953 1.00 22.82 N ANISOU 3165 NE ARG B 74 2660 2781 3229 -503 34 -48 N ATOM 3166 CZ ARG B 74 23.913 -13.895 33.338 1.00 23.85 C ANISOU 3166 CZ ARG B 74 2904 2896 3261 -365 147 177 C ATOM 3167 NH1 ARG B 74 22.941 -13.396 32.584 1.00 23.56 N ANISOU 3167 NH1 ARG B 74 3296 2847 2809 236 267 -273 N ATOM 3168 NH2 ARG B 74 25.055 -13.231 33.466 1.00 27.56 N ANISOU 3168 NH2 ARG B 74 3377 3260 3833 -768 51 -372 N ATOM 3169 N GLY B 75 22.810 -19.506 30.044 1.00 12.28 N ANISOU 3169 N GLY B 75 1432 1576 1655 25 -16 -67 N ATOM 3170 CA GLY B 75 23.389 -20.374 29.038 1.00 12.46 C ANISOU 3170 CA GLY B 75 1369 1851 1513 -73 67 -120 C ATOM 3171 C GLY B 75 24.507 -19.695 28.275 1.00 13.30 C ANISOU 3171 C GLY B 75 1504 1802 1747 -82 40 193 C ATOM 3172 O GLY B 75 24.391 -18.526 27.857 1.00 13.99 O ANISOU 3172 O GLY B 75 1537 1822 1956 -20 142 132 O ATOM 3173 N GLY B 76 25.599 -20.432 28.104 1.00 13.91 N ANISOU 3173 N GLY B 76 1550 1947 1789 -72 52 108 N ATOM 3174 CA GLY B 76 26.622 -20.059 27.144 1.00 14.92 C ANISOU 3174 CA GLY B 76 1737 2208 1722 -156 193 -149 C ATOM 3175 C GLY B 76 26.146 -20.539 25.794 1.00 15.73 C ANISOU 3175 C GLY B 76 2007 2060 1910 -56 -119 10 C ATOM 3176 O GLY B 76 26.962 -20.930 24.965 1.00 15.61 O ANISOU 3176 O GLY B 76 1897 2110 1921 71 -170 -130 O ATOM 3177 OXT GLY B 76 24.931 -20.570 25.547 1.00 16.78 O ANISOU 3177 OXT GLY B 76 2012 2231 2130 96 -89 105 O TER 3178 GLY B 76 HETATM 3179 ZN ZN A 401 -10.667 -21.556 45.650 1.00 26.34 ZN ANISOU 3179 ZN ZN A 401 3624 3962 2422 -839 657 -783 ZN HETATM 3180 NA NA A 402 22.096 -24.645 21.379 1.00 17.73 NA ANISOU 3180 NA NA A 402 2138 2278 2319 76 189 -29 NA HETATM 3181 C3' NHE A 403 31.075 -25.544 24.717 1.00 16.62 C ANISOU 3181 C3' NHE A 403 2075 2337 1902 307 -281 612 C HETATM 3182 C2' NHE A 403 30.926 -26.140 23.317 1.00 17.81 C ANISOU 3182 C2' NHE A 403 2329 2414 2021 468 -77 391 C HETATM 3183 C1' NHE A 403 30.606 -27.640 23.211 1.00 22.90 C ANISOU 3183 C1' NHE A 403 3801 2892 2005 -593 -207 418 C HETATM 3184 C6' NHE A 403 29.876 -28.273 24.407 1.00 18.15 C ANISOU 3184 C6' NHE A 403 2459 2388 2047 -70 -304 447 C HETATM 3185 N NHE A 403 29.933 -28.027 21.971 1.00 15.93 N ANISOU 3185 N NHE A 403 1779 2289 1984 250 -270 925 N HETATM 3186 C1 NHE A 403 30.001 -27.213 20.750 1.00 15.21 C ANISOU 3186 C1 NHE A 403 2192 1978 1609 372 -208 544 C HETATM 3187 C2 NHE A 403 29.790 -27.980 19.440 1.00 15.62 C ANISOU 3187 C2 NHE A 403 2224 2017 1691 69 -169 546 C HETATM 3188 S NHE A 403 30.495 -27.329 18.097 1.00 15.61 S ANISOU 3188 S NHE A 403 1862 2142 1925 171 50 450 S HETATM 3189 O1 NHE A 403 31.689 -26.614 18.313 1.00 16.95 O ANISOU 3189 O1 NHE A 403 2171 2192 2075 -14 133 213 O HETATM 3190 O2 NHE A 403 30.301 -28.126 16.952 1.00 17.59 O ANISOU 3190 O2 NHE A 403 2186 2536 1958 179 -132 311 O HETATM 3191 O3 NHE A 403 29.484 -26.103 17.839 1.00 15.29 O ANISOU 3191 O3 NHE A 403 2044 2064 1701 155 74 355 O HETATM 3192 C5' NHE A 403 29.837 -27.476 25.708 1.00 17.57 C ANISOU 3192 C5' NHE A 403 2048 2368 2260 16 -242 245 C HETATM 3193 C4' NHE A 403 31.034 -26.557 25.858 1.00 16.81 C ANISOU 3193 C4' NHE A 403 1799 2398 2188 131 -239 775 C HETATM 3194 C3' NHE A 404 7.308 -23.617 9.156 1.00 27.08 C ANISOU 3194 C3' NHE A 404 4483 3392 2414 1 71 263 C HETATM 3195 C2' NHE A 404 7.936 -22.457 8.380 1.00 29.14 C ANISOU 3195 C2' NHE A 404 4498 3239 3334 31 349 265 C HETATM 3196 C1' NHE A 404 8.968 -22.916 7.338 1.00 29.39 C ANISOU 3196 C1' NHE A 404 4925 3369 2870 -162 392 64 C HETATM 3197 C6' NHE A 404 8.682 -24.322 6.799 1.00 32.00 C ANISOU 3197 C6' NHE A 404 5217 3190 3752 -39 417 153 C HETATM 3198 N NHE A 404 9.096 -21.987 6.226 1.00 30.63 N ANISOU 3198 N NHE A 404 4937 2875 3824 -26 571 403 N HETATM 3199 C1 NHE A 404 8.687 -20.593 6.249 1.00 29.38 C ANISOU 3199 C1 NHE A 404 5215 2937 3009 162 463 -119 C HETATM 3200 C2 NHE A 404 8.598 -20.101 4.810 1.00 32.20 C ANISOU 3200 C2 NHE A 404 4835 4146 3251 387 567 343 C HETATM 3201 S NHE A 404 8.025 -18.538 4.701 1.00 38.79 S ANISOU 3201 S NHE A 404 5171 4451 5115 754 503 45 S HETATM 3202 O1 NHE A 404 6.925 -18.143 5.552 1.00 43.33 O ANISOU 3202 O1 NHE A 404 5206 5767 5489 909 727 -219 O HETATM 3203 O2 NHE A 404 8.380 -17.711 3.565 1.00 41.84 O ANISOU 3203 O2 NHE A 404 5884 5474 4537 275 684 -62 O HETATM 3204 O3 NHE A 404 6.894 -19.167 3.702 1.00 36.10 O ANISOU 3204 O3 NHE A 404 3872 4691 5150 1230 995 -449 O HETATM 3205 C5' NHE A 404 8.652 -25.388 7.895 1.00 29.47 C ANISOU 3205 C5' NHE A 404 4705 3590 2901 311 162 -47 C HETATM 3206 C4' NHE A 404 8.234 -24.832 9.259 1.00 28.35 C ANISOU 3206 C4' NHE A 404 4302 3806 2662 221 198 131 C HETATM 3207 C1 GOL A 405 20.577 13.603 5.659 1.00 36.93 C ANISOU 3207 C1 GOL A 405 4333 5391 4306 286 -74 -242 C HETATM 3208 O1 GOL A 405 19.509 13.072 6.437 1.00 38.11 O ANISOU 3208 O1 GOL A 405 4592 5117 4770 103 250 -475 O HETATM 3209 C2 GOL A 405 21.640 12.525 5.498 1.00 34.05 C ANISOU 3209 C2 GOL A 405 4534 5018 3385 173 52 -419 C HETATM 3210 O2 GOL A 405 22.219 12.195 6.776 1.00 26.27 O ANISOU 3210 O2 GOL A 405 3344 3013 3622 -55 544 265 O HETATM 3211 C3 GOL A 405 22.682 13.056 4.517 1.00 34.59 C ANISOU 3211 C3 GOL A 405 4422 4488 4233 -410 -96 -41 C HETATM 3212 O3 GOL A 405 23.772 13.691 5.199 1.00 33.96 O ANISOU 3212 O3 GOL A 405 4068 4089 4745 -326 173 -270 O HETATM 3213 C1 GOL A 406 6.656 -33.943 24.583 1.00 20.19 C ANISOU 3213 C1 GOL A 406 3224 2157 2288 374 -410 -28 C HETATM 3214 O1 GOL A 406 6.282 -33.077 25.651 1.00 19.66 O ANISOU 3214 O1 GOL A 406 3173 2040 2255 587 -284 80 O HETATM 3215 C2 GOL A 406 7.075 -35.270 25.183 1.00 19.86 C ANISOU 3215 C2 GOL A 406 2981 1766 2797 315 57 -183 C HETATM 3216 O2 GOL A 406 7.617 -36.058 24.131 1.00 20.23 O ANISOU 3216 O2 GOL A 406 2583 2501 2601 108 -134 -583 O HETATM 3217 C3 GOL A 406 5.886 -35.991 25.821 1.00 22.06 C ANISOU 3217 C3 GOL A 406 2825 2385 3171 199 71 -53 C HETATM 3218 O3 GOL A 406 4.876 -36.244 24.838 1.00 23.01 O ANISOU 3218 O3 GOL A 406 2932 2741 3066 -179 273 -402 O HETATM 3219 C1 GOL B 101 10.949 0.730 42.480 1.00 29.91 C ANISOU 3219 C1 GOL B 101 3542 4074 3748 311 -64 -262 C HETATM 3220 O1 GOL B 101 10.304 1.840 43.125 1.00 29.44 O ANISOU 3220 O1 GOL B 101 2893 4656 3635 1310 -227 331 O HETATM 3221 C2 GOL B 101 12.056 0.179 43.370 1.00 28.03 C ANISOU 3221 C2 GOL B 101 3785 3507 3357 442 339 168 C HETATM 3222 O2 GOL B 101 11.432 -0.635 44.357 1.00 25.96 O ANISOU 3222 O2 GOL B 101 3309 2896 3658 -44 309 -208 O HETATM 3223 C3 GOL B 101 13.033 -0.695 42.584 1.00 26.08 C ANISOU 3223 C3 GOL B 101 3250 3458 3201 -194 370 -134 C HETATM 3224 O3 GOL B 101 13.757 0.079 41.611 1.00 32.47 O ANISOU 3224 O3 GOL B 101 4537 3535 4262 -1324 572 -60 O HETATM 3225 O HOH A 501 2.523 -21.847 25.676 1.00 10.79 O ANISOU 3225 O HOH A 501 1369 1354 1374 41 -144 -98 O HETATM 3226 O HOH A 502 26.298 -22.731 19.361 1.00 13.77 O ANISOU 3226 O HOH A 502 1436 1783 2010 -6 45 63 O HETATM 3227 O HOH A 503 26.823 -25.004 21.091 1.00 15.45 O ANISOU 3227 O HOH A 503 1990 2170 1708 -69 -13 99 O HETATM 3228 O HOH A 504 19.580 5.115 5.876 1.00 19.50 O ANISOU 3228 O HOH A 504 2398 2860 2150 341 216 621 O HETATM 3229 O HOH A 505 15.417 -24.537 20.515 1.00 13.92 O ANISOU 3229 O HOH A 505 1633 1542 2112 -76 194 38 O HETATM 3230 O HOH A 506 27.145 -14.148 22.316 1.00 15.66 O ANISOU 3230 O HOH A 506 1644 2050 2256 15 -364 335 O HETATM 3231 O HOH A 507 -3.105 -28.892 19.471 1.00 14.92 O ANISOU 3231 O HOH A 507 2283 1868 1518 -430 -153 353 O HETATM 3232 O HOH A 508 -1.224 -9.705 30.865 1.00 28.33 O ANISOU 3232 O HOH A 508 4625 3497 2641 1164 748 15 O HETATM 3233 O HOH A 509 1.679 -8.976 17.320 1.00 25.37 O ANISOU 3233 O HOH A 509 2313 3492 3833 68 29 -1152 O HETATM 3234 O HOH A 510 -8.332 -28.556 27.083 1.00 11.29 O ANISOU 3234 O HOH A 510 1242 1567 1479 -117 -127 98 O HETATM 3235 O HOH A 511 2.300 -32.514 25.261 1.00 15.88 O ANISOU 3235 O HOH A 511 1859 1660 2512 -161 605 -203 O HETATM 3236 O HOH A 512 15.200 -21.296 28.093 1.00 11.45 O ANISOU 3236 O HOH A 512 1228 1240 1882 93 -92 234 O HETATM 3237 O HOH A 513 5.620 -25.455 12.361 1.00 21.48 O ANISOU 3237 O HOH A 513 1789 2743 3627 -21 -57 -473 O HETATM 3238 O HOH A 514 -14.645 -15.502 34.099 1.00 35.94 O ANISOU 3238 O HOH A 514 4038 3356 6258 1605 1945 442 O HETATM 3239 O HOH A 515 13.140 -22.043 29.832 1.00 12.26 O ANISOU 3239 O HOH A 515 1445 1800 1413 -36 -30 71 O HETATM 3240 O HOH A 516 21.937 -34.616 28.162 1.00 22.31 O ANISOU 3240 O HOH A 516 2427 2826 3221 752 107 833 O HETATM 3241 O HOH A 517 4.026 -30.339 17.555 1.00 17.00 O ANISOU 3241 O HOH A 517 2228 1750 2480 202 -189 43 O HETATM 3242 O HOH A 518 21.213 -12.441 8.955 1.00 16.09 O ANISOU 3242 O HOH A 518 2220 2184 1708 300 222 -63 O HETATM 3243 O HOH A 519 7.446 -17.949 29.130 1.00 12.01 O ANISOU 3243 O HOH A 519 1487 1561 1512 103 -141 53 O HETATM 3244 O HOH A 520 32.381 -29.519 21.825 1.00 19.81 O ANISOU 3244 O HOH A 520 2449 2380 2695 605 -798 -29 O HETATM 3245 O HOH A 521 26.945 -29.663 8.803 1.00 28.03 O ANISOU 3245 O HOH A 521 3414 4212 3023 884 93 -869 O HETATM 3246 O HOH A 522 30.971 -19.799 15.149 1.00 16.31 O ANISOU 3246 O HOH A 522 2157 2391 1648 -223 198 510 O HETATM 3247 O HOH A 523 -9.894 -31.012 21.260 1.00 13.98 O ANISOU 3247 O HOH A 523 1880 1519 1912 112 -264 328 O HETATM 3248 O HOH A 524 24.076 -29.185 26.891 1.00 16.26 O ANISOU 3248 O HOH A 524 2686 1914 1578 -197 32 211 O HETATM 3249 O HOH A 525 -16.115 -33.634 28.280 1.00 19.84 O ANISOU 3249 O HOH A 525 2397 1668 3474 -134 784 452 O HETATM 3250 O HOH A 526 24.915 -33.325 19.047 1.00 17.91 O ANISOU 3250 O HOH A 526 2151 2195 2458 358 48 -162 O HETATM 3251 O HOH A 527 7.871 -15.232 28.341 1.00 16.18 O ANISOU 3251 O HOH A 527 2279 1867 2002 37 213 250 O HETATM 3252 O HOH A 528 25.285 -13.179 24.344 1.00 15.05 O ANISOU 3252 O HOH A 528 1656 1887 2172 -31 -159 31 O HETATM 3253 O HOH A 529 17.469 16.992 11.480 1.00 36.53 O ANISOU 3253 O HOH A 529 5258 1663 6956 -55 964 -341 O HETATM 3254 O HOH A 530 7.480 -19.980 27.241 1.00 11.96 O ANISOU 3254 O HOH A 530 1273 1566 1702 69 -56 -177 O HETATM 3255 O HOH A 531 -9.776 -28.526 18.385 1.00 21.99 O ANISOU 3255 O HOH A 531 2870 2920 2563 -1008 371 -888 O HETATM 3256 O HOH A 532 11.588 -6.562 21.899 1.00 28.45 O ANISOU 3256 O HOH A 532 4987 2098 3722 -226 -516 234 O HETATM 3257 O HOH A 533 -3.702 -28.574 14.637 1.00 33.80 O ANISOU 3257 O HOH A 533 4360 3951 4531 505 -506 149 O HETATM 3258 O HOH A 534 -12.019 -32.040 19.874 1.00 24.09 O ANISOU 3258 O HOH A 534 3158 3924 2071 489 -162 334 O HETATM 3259 O HOH A 535 26.403 -14.685 8.013 1.00 23.86 O ANISOU 3259 O HOH A 535 2943 3293 2830 -15 785 -104 O HETATM 3260 O HOH A 536 -0.416 -18.607 29.250 1.00 16.50 O ANISOU 3260 O HOH A 536 2382 1917 1970 -87 -440 -5 O HETATM 3261 O HOH A 537 32.873 -13.426 23.972 1.00 29.69 O ANISOU 3261 O HOH A 537 4112 3572 3596 -764 41 -705 O HETATM 3262 O HOH A 538 -10.159 -31.643 25.714 1.00 12.47 O ANISOU 3262 O HOH A 538 1459 1515 1764 -73 -112 224 O HETATM 3263 O HOH A 539 33.139 16.750 6.507 1.00 27.94 O ANISOU 3263 O HOH A 539 3891 3940 2782 365 60 21 O HETATM 3264 O HOH A 540 -8.531 -27.391 14.427 1.00 28.65 O ANISOU 3264 O HOH A 540 3575 4408 2902 -19 -835 -587 O HETATM 3265 O HOH A 541 20.336 -28.594 34.223 1.00 26.06 O ANISOU 3265 O HOH A 541 4451 3470 1978 -864 -648 942 O HETATM 3266 O HOH A 542 -5.073 -18.503 34.437 1.00 14.74 O ANISOU 3266 O HOH A 542 1635 1921 2042 -74 71 -89 O HETATM 3267 O HOH A 543 31.115 -8.207 23.924 1.00 27.58 O ANISOU 3267 O HOH A 543 3139 2755 4583 -663 -876 793 O HETATM 3268 O HOH A 544 13.655 -19.771 31.415 1.00 13.94 O ANISOU 3268 O HOH A 544 1652 2007 1638 83 -200 -36 O HETATM 3269 O HOH A 545 27.964 -7.097 21.471 1.00 19.47 O ANISOU 3269 O HOH A 545 2507 1962 2928 -412 46 558 O HETATM 3270 O HOH A 546 -14.711 -27.347 33.843 1.00 20.62 O ANISOU 3270 O HOH A 546 2225 3075 2532 -66 158 24 O HETATM 3271 O HOH A 547 11.624 -28.761 32.776 1.00 13.49 O ANISOU 3271 O HOH A 547 1701 2050 1374 26 90 24 O HETATM 3272 O HOH A 548 29.070 -0.840 6.152 1.00 18.99 O ANISOU 3272 O HOH A 548 2700 1975 2537 76 74 4 O HETATM 3273 O HOH A 549 13.944 -21.228 36.842 1.00 15.21 O ANISOU 3273 O HOH A 549 2048 1868 1863 8 -102 -180 O HETATM 3274 O HOH A 550 17.648 -31.290 5.145 1.00 31.04 O ANISOU 3274 O HOH A 550 5502 3261 3030 -211 330 -135 O HETATM 3275 O HOH A 551 14.581 -1.746 21.097 1.00 34.09 O ANISOU 3275 O HOH A 551 4468 4629 3854 -1303 -372 -14 O HETATM 3276 O HOH A 552 1.553 -16.467 28.846 1.00 13.59 O ANISOU 3276 O HOH A 552 1639 1935 1589 -79 14 -148 O HETATM 3277 O HOH A 553 29.173 -19.752 7.812 1.00 22.07 O ANISOU 3277 O HOH A 553 2938 3356 2091 -50 540 474 O HETATM 3278 O HOH A 554 -2.682 -10.887 26.731 1.00 18.86 O ANISOU 3278 O HOH A 554 2386 1930 2848 -67 65 -440 O HETATM 3279 O HOH A 555 -9.401 -11.863 30.042 1.00 25.71 O ANISOU 3279 O HOH A 555 4307 1979 3482 171 852 -161 O HETATM 3280 O HOH A 556 -1.894 -34.439 30.375 1.00 20.41 O ANISOU 3280 O HOH A 556 2361 2120 3273 348 -207 -21 O HETATM 3281 O HOH A 557 4.405 -23.236 13.309 1.00 19.06 O ANISOU 3281 O HOH A 557 2214 2142 2883 4 959 394 O HETATM 3282 O HOH A 558 5.551 -5.620 15.867 1.00 35.51 O ANISOU 3282 O HOH A 558 3741 4859 4890 -876 -10 -569 O HETATM 3283 O HOH A 559 3.912 -14.538 12.782 1.00 20.89 O ANISOU 3283 O HOH A 559 2597 2462 2876 80 295 10 O HETATM 3284 O HOH A 560 28.532 -29.044 10.948 1.00 21.83 O ANISOU 3284 O HOH A 560 3124 2852 2315 50 639 177 O HETATM 3285 O HOH A 561 33.223 -24.441 18.256 1.00 15.04 O ANISOU 3285 O HOH A 561 1525 2387 1800 473 -215 266 O HETATM 3286 O HOH A 562 13.989 2.830 6.743 1.00 18.05 O ANISOU 3286 O HOH A 562 2171 1898 2786 -258 -70 505 O HETATM 3287 O HOH A 563 -12.884 -17.852 22.393 1.00 17.50 O ANISOU 3287 O HOH A 563 1354 2624 2670 282 -236 -3 O HETATM 3288 O HOH A 564 -7.050 -17.829 42.669 1.00 27.07 O ANISOU 3288 O HOH A 564 3594 3695 2996 407 -384 33 O HETATM 3289 O HOH A 565 9.727 -12.375 8.637 1.00 21.95 O ANISOU 3289 O HOH A 565 2853 3178 2307 -303 293 -61 O HETATM 3290 O HOH A 566 3.652 -10.585 30.163 1.00 18.64 O ANISOU 3290 O HOH A 566 2508 2027 2547 99 85 317 O HETATM 3291 O HOH A 567 43.387 10.148 5.295 1.00 31.61 O ANISOU 3291 O HOH A 567 3499 3802 4707 198 408 472 O HETATM 3292 O HOH A 568 30.772 -27.511 10.571 1.00 25.31 O ANISOU 3292 O HOH A 568 2922 3497 3197 256 905 575 O HETATM 3293 O HOH A 569 28.780 -1.548 8.912 1.00 22.01 O ANISOU 3293 O HOH A 569 3073 3181 2108 -240 -15 328 O HETATM 3294 O HOH A 570 -14.564 -25.864 29.452 1.00 20.96 O ANISOU 3294 O HOH A 570 2672 2057 3235 -29 -769 -173 O HETATM 3295 O HOH A 571 9.481 -31.458 14.106 1.00 18.58 O ANISOU 3295 O HOH A 571 2501 2080 2476 -156 -173 -245 O HETATM 3296 O HOH A 572 26.994 -26.468 6.179 1.00 25.98 O ANISOU 3296 O HOH A 572 2903 3947 3021 256 1221 -804 O HETATM 3297 O HOH A 573 -0.947 -31.432 22.939 1.00 15.43 O ANISOU 3297 O HOH A 573 1725 1893 2245 -36 -60 45 O HETATM 3298 O HOH A 574 -5.375 -12.110 19.123 1.00 24.89 O ANISOU 3298 O HOH A 574 3070 2767 3619 747 329 821 O HETATM 3299 O HOH A 575 10.737 -27.784 36.595 1.00 21.93 O ANISOU 3299 O HOH A 575 2622 2926 2782 -191 523 163 O HETATM 3300 O HOH A 576 -5.176 -32.096 21.412 1.00 15.99 O ANISOU 3300 O HOH A 576 2407 1768 1898 -374 370 -366 O HETATM 3301 O HOH A 577 1.135 -10.348 24.820 1.00 23.55 O ANISOU 3301 O HOH A 577 4367 2073 2505 668 -250 155 O HETATM 3302 O HOH A 578 9.126 -37.142 31.050 1.00 24.79 O ANISOU 3302 O HOH A 578 2869 3229 3320 -506 882 444 O HETATM 3303 O HOH A 579 -7.583 -31.674 19.782 1.00 21.81 O ANISOU 3303 O HOH A 579 2868 2430 2988 -84 -145 -622 O HETATM 3304 O HOH A 580 14.020 -16.820 32.781 1.00 25.26 O ANISOU 3304 O HOH A 580 1833 4346 3418 283 -335 -1650 O HETATM 3305 O HOH A 581 -15.795 -32.575 30.948 1.00 19.62 O ANISOU 3305 O HOH A 581 3209 2057 2189 230 248 270 O HETATM 3306 O HOH A 582 18.798 -13.749 28.333 1.00 19.91 O ANISOU 3306 O HOH A 582 2101 1558 3904 -211 -74 462 O HETATM 3307 O HOH A 583 10.376 -29.205 12.832 1.00 18.60 O ANISOU 3307 O HOH A 583 2606 2267 2192 -73 -463 -268 O HETATM 3308 O HOH A 584 12.456 0.418 6.422 1.00 21.94 O ANISOU 3308 O HOH A 584 2878 2210 3246 -366 -529 464 O HETATM 3309 O HOH A 585 10.393 -19.636 10.128 1.00 18.35 O ANISOU 3309 O HOH A 585 2232 2805 1933 -364 -269 189 O HETATM 3310 O HOH A 586 7.563 -37.004 28.619 1.00 25.84 O ANISOU 3310 O HOH A 586 2761 3510 3545 200 520 565 O HETATM 3311 O HOH A 587 -8.694 -16.950 35.826 1.00 29.70 O ANISOU 3311 O HOH A 587 4732 2880 3673 22 1825 -164 O HETATM 3312 O HOH A 588 22.933 12.162 -3.750 1.00 27.14 O ANISOU 3312 O HOH A 588 3742 3189 3380 -193 -315 735 O HETATM 3313 O HOH A 589 24.033 -11.766 7.787 1.00 21.00 O ANISOU 3313 O HOH A 589 3133 3132 1712 908 447 603 O HETATM 3314 O HOH A 590 1.447 -24.379 40.310 1.00 29.20 O ANISOU 3314 O HOH A 590 3335 3898 3861 -285 -429 305 O HETATM 3315 O HOH A 591 2.947 -34.760 28.153 1.00 27.37 O ANISOU 3315 O HOH A 591 3120 2925 4354 722 -762 -870 O HETATM 3316 O HOH A 592 0.910 -17.712 15.592 1.00 19.56 O ANISOU 3316 O HOH A 592 2531 2061 2839 -440 818 55 O HETATM 3317 O HOH A 593 23.155 -10.594 31.900 1.00 35.58 O ANISOU 3317 O HOH A 593 5406 2615 5498 372 1347 626 O HETATM 3318 O HOH A 594 30.345 -1.032 0.880 1.00 38.31 O ANISOU 3318 O HOH A 594 4663 2188 7704 280 710 116 O HETATM 3319 O HOH A 595 32.587 -4.972 18.365 1.00 31.07 O ANISOU 3319 O HOH A 595 2857 3253 5693 -596 -609 572 O HETATM 3320 O HOH A 596 42.135 17.179 3.165 1.00 29.95 O ANISOU 3320 O HOH A 596 3847 4512 3017 -1476 73 -26 O HETATM 3321 O HOH A 597 8.877 -27.435 11.434 1.00 20.42 O ANISOU 3321 O HOH A 597 2667 2684 2406 -268 -59 81 O HETATM 3322 O HOH A 598 11.860 -15.522 5.976 1.00 26.89 O ANISOU 3322 O HOH A 598 3558 3065 3593 -55 65 -44 O HETATM 3323 O HOH A 599 22.188 11.557 -0.807 1.00 26.09 O ANISOU 3323 O HOH A 599 3512 3921 2477 424 249 1217 O HETATM 3324 O HOH A 600 -2.590 -19.232 41.087 1.00 16.26 O ANISOU 3324 O HOH A 600 2296 2122 1759 174 -202 -327 O HETATM 3325 O HOH A 601 8.478 -37.109 15.471 1.00 28.19 O ANISOU 3325 O HOH A 601 3862 3340 3509 -593 687 -174 O HETATM 3326 O HOH A 602 25.595 -26.938 40.769 1.00 33.55 O ANISOU 3326 O HOH A 602 4428 4433 3885 1855 -563 -533 O HETATM 3327 O HOH A 603 10.606 -41.738 20.809 1.00 21.92 O ANISOU 3327 O HOH A 603 2788 2230 3308 -258 292 -449 O HETATM 3328 O HOH A 604 16.430 8.348 0.902 1.00 41.95 O ANISOU 3328 O HOH A 604 4516 4561 6862 -652 60 1704 O HETATM 3329 O HOH A 605 25.926 -5.023 21.627 1.00 21.24 O ANISOU 3329 O HOH A 605 2771 1908 3391 -140 -404 184 O HETATM 3330 O HOH A 606 31.605 10.748 -7.662 1.00 28.46 O ANISOU 3330 O HOH A 606 3594 5195 2024 206 37 1473 O HETATM 3331 O HOH A 607 22.494 -32.970 30.973 1.00 25.15 O ANISOU 3331 O HOH A 607 2537 2139 4881 229 212 1022 O HETATM 3332 O HOH A 608 32.818 -18.907 27.280 1.00 23.16 O ANISOU 3332 O HOH A 608 1985 4114 2698 654 -335 -313 O HETATM 3333 O HOH A 609 25.852 -16.194 35.788 1.00 24.95 O ANISOU 3333 O HOH A 609 3607 2678 3194 90 -100 -209 O HETATM 3334 O HOH A 610 15.243 -33.423 37.415 1.00 32.52 O ANISOU 3334 O HOH A 610 6047 4086 2223 1371 -771 259 O HETATM 3335 O HOH A 611 30.472 -6.197 22.219 1.00 27.40 O ANISOU 3335 O HOH A 611 2972 2622 4814 -681 -578 687 O HETATM 3336 O HOH A 612 24.224 -32.531 28.199 1.00 22.63 O ANISOU 3336 O HOH A 612 2899 2657 3041 833 -287 -377 O HETATM 3337 O HOH A 613 30.144 -20.276 29.487 1.00 25.76 O ANISOU 3337 O HOH A 613 3454 3286 3045 458 273 360 O HETATM 3338 O HOH A 614 11.757 -21.340 8.239 1.00 24.89 O ANISOU 3338 O HOH A 614 4279 3158 2020 71 117 606 O HETATM 3339 O HOH A 615 28.891 -14.298 33.066 1.00 39.19 O ANISOU 3339 O HOH A 615 4244 5096 5549 846 -1489 -906 O HETATM 3340 O HOH A 616 1.253 -30.183 17.990 1.00 26.48 O ANISOU 3340 O HOH A 616 2861 3128 4072 0 -53 -327 O HETATM 3341 O HOH A 617 -7.437 -29.771 17.636 1.00 26.61 O ANISOU 3341 O HOH A 617 2756 3847 3506 -165 102 -379 O HETATM 3342 O HOH A 618 24.690 -35.421 26.998 1.00 28.20 O ANISOU 3342 O HOH A 618 4143 3654 2917 916 -221 167 O HETATM 3343 O HOH A 619 -7.733 -17.962 33.585 1.00 19.56 O ANISOU 3343 O HOH A 619 2106 2570 2755 60 -587 -315 O HETATM 3344 O HOH A 620 -11.787 -14.330 28.906 1.00 25.75 O ANISOU 3344 O HOH A 620 2372 4335 3076 313 251 -185 O HETATM 3345 O HOH A 621 4.724 -31.815 15.340 1.00 29.06 O ANISOU 3345 O HOH A 621 2955 4018 4067 -115 149 -1872 O HETATM 3346 O HOH A 622 24.914 -21.867 6.216 1.00 28.43 O ANISOU 3346 O HOH A 622 3226 4848 2726 -517 -318 1312 O HETATM 3347 O HOH A 623 18.934 -32.761 1.662 1.00 26.50 O ANISOU 3347 O HOH A 623 4132 3417 2518 1027 753 68 O HETATM 3348 O HOH A 624 19.803 -12.438 23.343 1.00 30.65 O ANISOU 3348 O HOH A 624 3979 3730 3934 41 7 -339 O HETATM 3349 O HOH A 625 -3.805 -20.206 13.869 1.00 27.03 O ANISOU 3349 O HOH A 625 3902 3282 3084 -892 -566 1255 O HETATM 3350 O HOH A 626 19.497 5.389 -1.767 1.00 32.30 O ANISOU 3350 O HOH A 626 4064 5622 2584 50 -1356 453 O HETATM 3351 O HOH A 627 36.831 -25.544 17.298 1.00 20.86 O ANISOU 3351 O HOH A 627 1663 3997 2266 367 -18 158 O HETATM 3352 O HOH A 628 28.828 -23.355 38.148 1.00 23.85 O ANISOU 3352 O HOH A 628 2267 3871 2922 36 -66 842 O HETATM 3353 O HOH A 629 28.841 -31.994 20.708 1.00 21.67 O ANISOU 3353 O HOH A 629 2726 2638 2869 529 254 86 O HETATM 3354 O HOH A 630 -3.283 -16.646 33.264 1.00 18.49 O ANISOU 3354 O HOH A 630 2089 2422 2515 -163 -91 -120 O HETATM 3355 O HOH A 631 3.294 -16.940 14.332 1.00 22.38 O ANISOU 3355 O HOH A 631 2841 2470 3189 -668 1125 -80 O HETATM 3356 O HOH A 632 24.420 -15.534 38.220 1.00 37.43 O ANISOU 3356 O HOH A 632 5309 4860 4053 -528 -66 -1055 O HETATM 3357 O HOH A 633 -5.063 -28.477 17.260 1.00 22.11 O ANISOU 3357 O HOH A 633 3340 2205 2854 -438 -404 108 O HETATM 3358 O HOH A 634 -0.935 -13.568 14.221 1.00 25.72 O ANISOU 3358 O HOH A 634 3301 3210 3260 12 -344 378 O HETATM 3359 O HOH A 635 15.749 -9.234 29.287 1.00 30.40 O ANISOU 3359 O HOH A 635 4006 3425 4120 453 -18 -208 O HETATM 3360 O HOH A 636 5.309 -21.334 37.080 1.00 19.22 O ANISOU 3360 O HOH A 636 3062 2646 1594 790 -277 -562 O HETATM 3361 O HOH A 637 3.967 -9.549 18.987 1.00 23.91 O ANISOU 3361 O HOH A 637 2163 3266 3655 296 49 856 O HETATM 3362 O HOH A 638 8.980 -29.639 36.095 1.00 24.51 O ANISOU 3362 O HOH A 638 2956 3278 3077 -716 819 -172 O HETATM 3363 O HOH A 639 24.571 10.621 6.973 1.00 21.63 O ANISOU 3363 O HOH A 639 3008 2868 2341 240 80 23 O HETATM 3364 O HOH A 640 37.467 3.502 15.596 1.00 31.54 O ANISOU 3364 O HOH A 640 4321 2742 4921 -525 -1793 1381 O HETATM 3365 O HOH A 641 8.679 -18.156 8.740 1.00 29.83 O ANISOU 3365 O HOH A 641 4309 3537 3485 288 -522 521 O HETATM 3366 O HOH A 642 6.426 -28.673 10.628 1.00 40.77 O ANISOU 3366 O HOH A 642 6295 5100 4093 -1622 -2351 -101 O HETATM 3367 O HOH A 643 23.408 3.953 18.553 1.00 35.39 O ANISOU 3367 O HOH A 643 4272 2037 7138 -686 -671 -186 O HETATM 3368 O HOH A 644 2.023 -23.347 36.265 1.00 27.12 O ANISOU 3368 O HOH A 644 2779 4356 3169 -393 -499 572 O HETATM 3369 O HOH A 645 33.592 -18.987 15.581 1.00 29.84 O ANISOU 3369 O HOH A 645 3063 4791 3483 -378 154 473 O HETATM 3370 O HOH A 646 17.059 -10.294 3.018 1.00 27.99 O ANISOU 3370 O HOH A 646 5228 2845 2560 607 935 161 O HETATM 3371 O HOH A 647 20.617 12.308 1.379 1.00 32.79 O ANISOU 3371 O HOH A 647 4497 3894 4066 -317 584 1282 O HETATM 3372 O HOH A 648 11.790 -10.910 27.274 1.00 24.28 O ANISOU 3372 O HOH A 648 3073 2825 3325 -191 324 -45 O HETATM 3373 O HOH A 649 18.564 -6.428 8.408 1.00 19.31 O ANISOU 3373 O HOH A 649 2391 2362 2582 -7 570 466 O HETATM 3374 O HOH A 650 -14.341 -20.818 29.199 1.00 28.73 O ANISOU 3374 O HOH A 650 3774 3943 3199 948 487 189 O HETATM 3375 O HOH A 651 -7.377 -15.485 16.497 1.00 25.04 O ANISOU 3375 O HOH A 651 2127 3444 3940 -370 -994 1072 O HETATM 3376 O HOH A 652 -5.476 -8.917 25.040 1.00 33.02 O ANISOU 3376 O HOH A 652 4689 3248 4608 650 620 -298 O HETATM 3377 O HOH A 653 -11.471 -20.450 40.000 1.00 25.11 O ANISOU 3377 O HOH A 653 3038 3770 2732 382 -53 -28 O HETATM 3378 O HOH A 654 -3.473 -32.819 33.776 1.00 23.11 O ANISOU 3378 O HOH A 654 3630 2712 2439 -17 -485 282 O HETATM 3379 O HOH A 655 26.404 -31.664 23.448 1.00 18.82 O ANISOU 3379 O HOH A 655 2270 2434 2444 150 149 298 O HETATM 3380 O HOH A 656 25.053 -35.760 21.812 1.00 24.17 O ANISOU 3380 O HOH A 656 3861 1987 3332 270 -685 5 O HETATM 3381 O HOH A 657 31.124 -24.727 10.964 1.00 24.93 O ANISOU 3381 O HOH A 657 3507 2898 3066 51 337 138 O HETATM 3382 O HOH A 658 12.197 4.668 5.656 1.00 23.81 O ANISOU 3382 O HOH A 658 3210 3049 2786 131 -544 894 O HETATM 3383 O HOH A 659 22.817 8.333 -2.410 1.00 23.45 O ANISOU 3383 O HOH A 659 3215 3296 2397 -652 233 103 O HETATM 3384 O HOH A 660 6.974 -32.507 13.958 1.00 31.43 O ANISOU 3384 O HOH A 660 2515 4149 5277 -823 565 -1868 O HETATM 3385 O HOH A 661 -11.802 -17.688 18.905 1.00 25.03 O ANISOU 3385 O HOH A 661 2283 3261 3964 433 -572 317 O HETATM 3386 O HOH A 662 23.227 -4.893 22.964 1.00 21.95 O ANISOU 3386 O HOH A 662 2977 1922 3438 -336 67 514 O HETATM 3387 O HOH A 663 10.500 -14.388 29.484 1.00 25.59 O ANISOU 3387 O HOH A 663 3627 3511 2585 378 828 -6 O HETATM 3388 O HOH A 664 17.101 -12.432 26.651 1.00 20.11 O ANISOU 3388 O HOH A 664 2609 2304 2724 -162 60 -131 O HETATM 3389 O HOH A 665 27.012 -32.361 12.308 1.00 33.49 O ANISOU 3389 O HOH A 665 4484 4686 3554 -766 1002 -1133 O HETATM 3390 O HOH A 666 27.758 -24.611 35.864 1.00 20.86 O ANISOU 3390 O HOH A 666 2231 3009 2685 470 -114 128 O HETATM 3391 O HOH A 667 -8.705 -31.760 28.049 1.00 21.80 O ANISOU 3391 O HOH A 667 2524 2580 3177 55 -767 -215 O HETATM 3392 O HOH A 668 7.650 -22.867 37.583 1.00 28.41 O ANISOU 3392 O HOH A 668 3094 4040 3660 144 -462 -767 O HETATM 3393 O HOH A 669 -4.796 -14.513 32.665 1.00 24.51 O ANISOU 3393 O HOH A 669 2663 3226 3423 -151 99 193 O HETATM 3394 O HOH A 670 26.472 4.781 17.517 1.00 34.88 O ANISOU 3394 O HOH A 670 4242 4722 4287 -780 664 -361 O HETATM 3395 O HOH A 671 0.652 -31.431 20.462 1.00 27.73 O ANISOU 3395 O HOH A 671 3063 3780 3692 76 -233 -653 O HETATM 3396 O HOH A 672 19.747 11.284 17.532 1.00 41.63 O ANISOU 3396 O HOH A 672 6200 4829 4786 304 275 -869 O HETATM 3397 O HOH A 673 43.489 7.065 10.196 1.00 36.25 O ANISOU 3397 O HOH A 673 3154 4430 6190 34 -366 236 O HETATM 3398 O HOH A 674 12.520 11.983 12.647 1.00 31.65 O ANISOU 3398 O HOH A 674 3052 3012 5958 331 -564 -701 O HETATM 3399 O HOH A 675 1.920 -33.233 22.284 1.00 24.37 O ANISOU 3399 O HOH A 675 2922 3358 2980 -304 180 -593 O HETATM 3400 O HOH A 676 11.742 7.310 6.726 1.00 30.60 O ANISOU 3400 O HOH A 676 4007 3695 3921 257 -533 436 O HETATM 3401 O HOH A 677 1.312 -27.701 38.831 1.00 30.51 O ANISOU 3401 O HOH A 677 3722 3585 4285 1163 -341 -687 O HETATM 3402 O HOH A 678 11.835 -12.934 6.771 1.00 25.04 O ANISOU 3402 O HOH A 678 2598 2831 4083 -528 504 -350 O HETATM 3403 O HOH A 679 23.551 14.133 10.582 1.00 31.41 O ANISOU 3403 O HOH A 679 3737 3396 4798 288 478 521 O HETATM 3404 O HOH A 680 35.392 11.497 -5.471 1.00 31.19 O ANISOU 3404 O HOH A 680 4812 3421 3616 -677 870 -437 O HETATM 3405 O HOH A 681 10.061 -33.195 34.236 1.00 20.75 O ANISOU 3405 O HOH A 681 2563 2706 2615 76 417 648 O HETATM 3406 O HOH A 682 26.803 12.379 14.923 1.00 27.00 O ANISOU 3406 O HOH A 682 3224 3962 3071 29 57 -1027 O HETATM 3407 O HOH A 683 15.538 -5.487 25.486 1.00 32.78 O ANISOU 3407 O HOH A 683 3642 4240 4571 385 706 -100 O HETATM 3408 O HOH A 684 18.459 -11.724 0.935 1.00 36.02 O ANISOU 3408 O HOH A 684 5200 4357 4128 532 242 143 O HETATM 3409 O HOH A 685 18.589 -39.751 26.215 1.00 30.60 O ANISOU 3409 O HOH A 685 3943 4321 3360 1844 -384 -560 O HETATM 3410 O HOH A 686 -16.377 -18.038 30.667 1.00 30.29 O ANISOU 3410 O HOH A 686 2642 5481 3386 424 139 -1099 O HETATM 3411 O HOH A 687 41.122 9.300 16.400 1.00 29.62 O ANISOU 3411 O HOH A 687 3931 4467 2855 -370 -96 820 O HETATM 3412 O HOH A 688 20.695 -43.194 17.434 1.00 28.65 O ANISOU 3412 O HOH A 688 3824 1934 5127 577 -293 102 O HETATM 3413 O HOH A 689 -16.461 -31.798 22.386 1.00 23.80 O ANISOU 3413 O HOH A 689 2307 3488 3246 332 19 307 O HETATM 3414 O HOH A 690 24.688 -33.036 21.832 1.00 21.03 O ANISOU 3414 O HOH A 690 2469 2734 2787 91 -112 26 O HETATM 3415 O HOH A 691 25.552 10.168 11.846 1.00 20.93 O ANISOU 3415 O HOH A 691 3112 2449 2388 -284 -111 126 O HETATM 3416 O HOH A 692 12.223 -25.920 9.116 1.00 26.42 O ANISOU 3416 O HOH A 692 3414 3852 2769 57 33 -833 O HETATM 3417 O HOH A 693 34.989 -18.952 13.275 1.00 33.58 O ANISOU 3417 O HOH A 693 3974 4293 4489 -398 286 658 O HETATM 3418 O HOH A 694 15.138 -29.473 9.159 1.00 35.87 O ANISOU 3418 O HOH A 694 3973 5507 4148 184 -315 -729 O HETATM 3419 O HOH A 695 17.624 4.052 16.855 1.00 32.73 O ANISOU 3419 O HOH A 695 3616 4128 4689 300 -32 1432 O HETATM 3420 O HOH A 696 15.426 4.028 15.514 1.00 29.58 O ANISOU 3420 O HOH A 696 3894 3976 3366 -280 187 396 O HETATM 3421 O HOH A 697 11.140 -37.823 15.063 1.00 28.32 O ANISOU 3421 O HOH A 697 3858 2651 4251 -509 557 -575 O HETATM 3422 O HOH A 698 38.088 12.215 16.316 1.00 29.84 O ANISOU 3422 O HOH A 698 5016 4101 2220 -519 -103 376 O HETATM 3423 O HOH A 699 14.128 -29.738 6.509 1.00 36.77 O ANISOU 3423 O HOH A 699 5866 4555 3548 -870 -310 -568 O HETATM 3424 O HOH A 700 12.478 -14.224 31.475 1.00 31.15 O ANISOU 3424 O HOH A 700 5266 3770 2798 -695 825 608 O HETATM 3425 O HOH A 701 9.504 -15.297 8.206 1.00 31.20 O ANISOU 3425 O HOH A 701 3858 3521 4473 -311 98 746 O HETATM 3426 O HOH A 702 22.775 -25.763 18.942 1.00 13.20 O ANISOU 3426 O HOH A 702 1590 1768 1654 151 127 -125 O HETATM 3427 O HOH A 703 6.267 -18.756 8.235 1.00 30.84 O ANISOU 3427 O HOH A 703 4784 3965 2966 243 38 420 O HETATM 3428 O HOH A 704 12.563 -9.819 3.823 1.00 35.38 O ANISOU 3428 O HOH A 704 5034 5185 3222 805 -272 754 O HETATM 3429 O HOH A 705 -4.636 -17.922 39.636 1.00 21.63 O ANISOU 3429 O HOH A 705 2815 3342 2061 472 67 544 O HETATM 3430 O HOH A 706 -5.228 -17.312 36.962 1.00 18.52 O ANISOU 3430 O HOH A 706 2932 2485 1617 -111 -60 -247 O HETATM 3431 O HOH A 707 7.052 -30.175 32.698 1.00 15.43 O ANISOU 3431 O HOH A 707 1698 2173 1991 179 -141 584 O HETATM 3432 O HOH A 708 22.188 -34.510 0.081 1.00 33.23 O ANISOU 3432 O HOH A 708 4786 2726 5112 816 -462 924 O HETATM 3433 O HOH A 709 16.206 -6.328 28.208 1.00 41.55 O ANISOU 3433 O HOH A 709 4935 4368 6482 -1167 318 -1524 O HETATM 3434 O HOH A 710 33.435 -17.521 24.969 1.00 26.64 O ANISOU 3434 O HOH A 710 3479 3818 2822 855 -515 149 O HETATM 3435 O HOH A 711 19.832 -8.240 6.631 1.00 25.98 O ANISOU 3435 O HOH A 711 3200 2736 3936 -543 877 -103 O HETATM 3436 O HOH A 712 -8.009 -11.760 19.518 1.00 30.25 O ANISOU 3436 O HOH A 712 3047 4686 3758 412 315 141 O HETATM 3437 O HOH A 713 0.235 -17.566 12.132 1.00 35.35 O ANISOU 3437 O HOH A 713 4854 4104 4471 467 92 209 O HETATM 3438 O HOH A 714 27.310 -3.021 23.011 1.00 28.51 O ANISOU 3438 O HOH A 714 3831 2554 4447 -512 -315 -348 O HETATM 3439 O HOH A 715 23.740 -4.340 25.731 1.00 26.88 O ANISOU 3439 O HOH A 715 3671 2944 3597 -44 -60 25 O HETATM 3440 O HOH A 716 3.204 -25.863 37.077 1.00 35.37 O ANISOU 3440 O HOH A 716 2690 6779 3967 126 -258 1502 O HETATM 3441 O HOH A 717 34.414 -16.409 16.605 1.00 28.58 O ANISOU 3441 O HOH A 717 3515 3838 3504 -127 3 83 O HETATM 3442 O HOH A 718 26.462 13.583 9.955 1.00 36.89 O ANISOU 3442 O HOH A 718 3934 4367 5713 -92 -299 829 O HETATM 3443 O HOH A 719 27.171 8.253 13.671 1.00 25.85 O ANISOU 3443 O HOH A 719 3618 3395 2808 -868 163 -467 O HETATM 3444 O HOH A 720 26.420 1.714 -3.601 1.00 42.40 O ANISOU 3444 O HOH A 720 6639 6890 2579 -1923 -181 -8 O HETATM 3445 O HOH A 721 -16.267 -24.738 38.138 1.00 25.85 O ANISOU 3445 O HOH A 721 2825 4056 2940 -609 -287 99 O HETATM 3446 O HOH A 722 35.266 6.381 19.012 1.00 34.81 O ANISOU 3446 O HOH A 722 5315 3813 4096 -615 -1249 900 O HETATM 3447 O HOH A 723 -1.032 -28.616 14.366 1.00 35.82 O ANISOU 3447 O HOH A 723 4665 3953 4990 32 -180 -1896 O HETATM 3448 O HOH A 724 -3.111 -33.852 20.590 1.00 25.10 O ANISOU 3448 O HOH A 724 4049 2447 3040 -377 980 -484 O HETATM 3449 O HOH A 725 30.366 -31.929 13.608 1.00 37.94 O ANISOU 3449 O HOH A 725 4069 4191 6155 719 1264 -286 O HETATM 3450 O HOH A 726 25.942 10.841 9.192 1.00 26.55 O ANISOU 3450 O HOH A 726 3123 3461 3501 -648 -157 254 O HETATM 3451 O HOH A 727 32.091 18.644 10.608 1.00 52.05 O ANISOU 3451 O HOH A 727 7907 6697 5170 155 -104 76 O HETATM 3452 O HOH A 728 20.812 -34.174 8.087 1.00 51.43 O ANISOU 3452 O HOH A 728 10066 5710 3763 -616 1317 -432 O HETATM 3453 O HOH A 729 15.482 -27.462 5.618 1.00 26.41 O ANISOU 3453 O HOH A 729 3095 4158 2779 -117 -630 -401 O HETATM 3454 O HOH A 730 22.115 -30.233 6.893 1.00 23.89 O ANISOU 3454 O HOH A 730 2920 2812 3344 373 410 -547 O HETATM 3455 O HOH A 731 23.352 -32.397 8.814 1.00 26.06 O ANISOU 3455 O HOH A 731 3557 2832 3513 410 219 -693 O HETATM 3456 O HOH A 732 -3.670 -17.367 15.045 1.00 27.75 O ANISOU 3456 O HOH A 732 3434 3648 3460 471 262 1463 O HETATM 3457 O HOH A 733 26.144 10.028 15.635 1.00 33.78 O ANISOU 3457 O HOH A 733 4793 4293 3748 -364 91 -654 O HETATM 3458 O HOH A 734 29.235 0.761 18.768 1.00 29.89 O ANISOU 3458 O HOH A 734 3650 4163 3543 -645 247 376 O HETATM 3459 O HOH A 735 20.309 3.829 16.853 1.00 25.24 O ANISOU 3459 O HOH A 735 3373 2317 3898 196 169 677 O HETATM 3460 O HOH A 736 17.686 -9.902 27.449 1.00 24.59 O ANISOU 3460 O HOH A 736 3286 2898 3157 -276 93 -227 O HETATM 3461 O HOH A 737 9.686 -30.504 33.597 1.00 15.77 O ANISOU 3461 O HOH A 737 1603 2367 2023 14 -11 507 O HETATM 3462 O HOH A 738 8.077 -4.781 15.062 1.00 29.28 O ANISOU 3462 O HOH A 738 3556 2722 4845 -686 -972 1483 O HETATM 3463 O HOH A 739 14.440 -9.967 1.947 1.00 34.83 O ANISOU 3463 O HOH A 739 5604 5024 2604 1139 -478 690 O HETATM 3464 O HOH A 740 27.338 -13.015 31.101 1.00 24.05 O ANISOU 3464 O HOH A 740 3493 2765 2880 -411 -1226 -186 O HETATM 3465 O HOH A 741 32.733 -28.035 12.734 1.00 34.38 O ANISOU 3465 O HOH A 741 3981 5733 3346 830 137 613 O HETATM 3466 O HOH A 742 34.065 -28.146 17.740 1.00 31.64 O ANISOU 3466 O HOH A 742 3351 4085 4585 870 -286 -477 O HETATM 3467 O HOH B 201 20.442 -17.390 37.321 1.00 19.12 O ANISOU 3467 O HOH B 201 2302 2913 2047 308 -354 -569 O HETATM 3468 O HOH B 202 13.701 -4.759 41.186 1.00 27.31 O ANISOU 3468 O HOH B 202 2964 2970 4443 305 760 238 O HETATM 3469 O HOH B 203 1.580 -18.254 40.209 1.00 13.71 O ANISOU 3469 O HOH B 203 1905 1848 1454 5 -185 37 O HETATM 3470 O HOH B 204 2.371 1.502 44.751 1.00 13.20 O ANISOU 3470 O HOH B 204 1802 1441 1770 71 29 -104 O HETATM 3471 O HOH B 205 -1.085 -17.948 32.031 1.00 18.60 O ANISOU 3471 O HOH B 205 1988 3064 2013 -467 36 147 O HETATM 3472 O HOH B 206 11.773 -9.847 34.826 1.00 26.66 O ANISOU 3472 O HOH B 206 3355 2641 4132 522 641 620 O HETATM 3473 O HOH B 207 2.806 -2.406 51.253 1.00 34.90 O ANISOU 3473 O HOH B 207 5835 2968 4455 744 474 -551 O HETATM 3474 O HOH B 208 3.763 -15.041 29.514 1.00 12.21 O ANISOU 3474 O HOH B 208 1580 1803 1256 186 -30 -138 O HETATM 3475 O HOH B 209 5.402 -13.868 27.741 1.00 13.50 O ANISOU 3475 O HOH B 209 1692 1875 1561 39 142 111 O HETATM 3476 O HOH B 210 9.688 -10.869 36.426 1.00 17.69 O ANISOU 3476 O HOH B 210 2089 1771 2859 99 -175 164 O HETATM 3477 O HOH B 211 5.018 -17.440 30.171 1.00 12.33 O ANISOU 3477 O HOH B 211 1752 1606 1323 103 113 -189 O HETATM 3478 O HOH B 212 0.638 -20.354 48.194 1.00 25.68 O ANISOU 3478 O HOH B 212 3119 3166 3471 916 453 1366 O HETATM 3479 O HOH B 213 -2.900 -17.451 43.341 1.00 16.15 O ANISOU 3479 O HOH B 213 1982 2127 2025 176 -190 -231 O HETATM 3480 O HOH B 214 9.155 -21.086 41.818 1.00 17.26 O ANISOU 3480 O HOH B 214 2770 1792 1996 450 -188 -41 O HETATM 3481 O HOH B 215 -3.061 0.120 44.888 1.00 16.06 O ANISOU 3481 O HOH B 215 1966 1705 2429 446 -115 -199 O HETATM 3482 O HOH B 216 -8.306 -12.539 45.943 1.00 20.02 O ANISOU 3482 O HOH B 216 2271 2660 2674 16 -262 300 O HETATM 3483 O HOH B 217 6.800 -16.270 54.335 1.00 22.17 O ANISOU 3483 O HOH B 217 3164 2841 2418 540 -345 199 O HETATM 3484 O HOH B 218 -5.058 -6.012 42.195 1.00 19.75 O ANISOU 3484 O HOH B 218 2648 1845 3011 82 23 -360 O HETATM 3485 O HOH B 219 -2.908 -18.304 46.149 1.00 16.53 O ANISOU 3485 O HOH B 219 2101 1924 2255 10 8 242 O HETATM 3486 O HOH B 220 19.962 -2.553 38.505 1.00 32.39 O ANISOU 3486 O HOH B 220 3208 2686 6413 -168 -365 -1141 O HETATM 3487 O HOH B 221 -7.261 -7.594 46.441 1.00 19.94 O ANISOU 3487 O HOH B 221 2647 2348 2581 613 164 161 O HETATM 3488 O HOH B 222 28.350 -22.859 26.638 1.00 27.48 O ANISOU 3488 O HOH B 222 3623 3393 3423 -378 -319 455 O HETATM 3489 O HOH B 223 5.685 -11.112 28.432 1.00 20.92 O ANISOU 3489 O HOH B 223 2880 2036 3029 317 662 108 O HETATM 3490 O HOH B 224 2.998 -19.987 37.757 1.00 18.83 O ANISOU 3490 O HOH B 224 2389 2894 1869 696 -128 22 O HETATM 3491 O HOH B 225 -0.298 -20.227 40.005 1.00 17.30 O ANISOU 3491 O HOH B 225 2253 2045 2274 -313 -55 13 O HETATM 3492 O HOH B 226 5.752 -4.252 46.493 1.00 22.24 O ANISOU 3492 O HOH B 226 2961 2581 2907 374 203 16 O HETATM 3493 O HOH B 227 20.553 -14.624 31.304 1.00 19.99 O ANISOU 3493 O HOH B 227 3221 2081 2290 -168 119 -228 O HETATM 3494 O HOH B 228 10.281 -11.633 29.405 1.00 25.43 O ANISOU 3494 O HOH B 228 3419 2913 3327 6 187 -159 O HETATM 3495 O HOH B 229 -2.129 -12.159 35.020 1.00 17.17 O ANISOU 3495 O HOH B 229 2480 2191 1854 187 84 -302 O HETATM 3496 O HOH B 230 -2.992 -13.617 53.981 1.00 28.84 O ANISOU 3496 O HOH B 230 5241 2804 2910 379 139 389 O HETATM 3497 O HOH B 231 -4.468 -9.591 52.175 1.00 21.17 O ANISOU 3497 O HOH B 231 2478 3028 2537 -26 480 105 O HETATM 3498 O HOH B 232 16.157 -3.862 44.619 1.00 27.44 O ANISOU 3498 O HOH B 232 3910 3483 3031 -51 -233 -107 O HETATM 3499 O HOH B 233 13.100 -19.265 43.349 1.00 20.43 O ANISOU 3499 O HOH B 233 3583 2371 1807 308 -184 -84 O HETATM 3500 O HOH B 234 -8.166 -13.206 43.123 1.00 23.82 O ANISOU 3500 O HOH B 234 2713 3148 3187 14 -65 -217 O HETATM 3501 O HOH B 235 -6.850 -5.972 44.257 1.00 21.94 O ANISOU 3501 O HOH B 235 2804 2261 3269 -197 -371 -353 O HETATM 3502 O HOH B 236 -6.876 -6.335 40.173 1.00 25.32 O ANISOU 3502 O HOH B 236 2983 3398 3238 431 -459 210 O HETATM 3503 O HOH B 237 6.850 1.417 35.506 1.00 23.57 O ANISOU 3503 O HOH B 237 3440 2213 3301 44 6 -575 O HETATM 3504 O HOH B 238 0.263 -2.448 52.267 1.00 31.41 O ANISOU 3504 O HOH B 238 4444 4114 3376 182 -384 -82 O HETATM 3505 O HOH B 239 -1.891 -14.953 35.042 1.00 17.76 O ANISOU 3505 O HOH B 239 1986 2332 2429 425 -380 -166 O HETATM 3506 O HOH B 240 8.396 -23.271 40.359 1.00 29.12 O ANISOU 3506 O HOH B 240 3020 3401 4641 -72 -290 -1188 O HETATM 3507 O HOH B 241 -5.627 -12.891 42.053 1.00 22.27 O ANISOU 3507 O HOH B 241 2352 3424 2686 27 -120 -278 O HETATM 3508 O HOH B 242 6.664 -7.271 52.457 1.00 21.42 O ANISOU 3508 O HOH B 242 2943 2423 2769 43 -540 -328 O HETATM 3509 O HOH B 243 15.349 -6.698 56.303 1.00 47.20 O ANISOU 3509 O HOH B 243 6617 6148 5168 47 911 216 O HETATM 3510 O HOH B 244 3.551 -7.941 30.693 1.00 23.25 O ANISOU 3510 O HOH B 244 3323 2770 2741 341 233 88 O HETATM 3511 O HOH B 245 -6.097 -13.146 39.317 1.00 23.92 O ANISOU 3511 O HOH B 245 3621 2424 3041 -196 -375 130 O HETATM 3512 O HOH B 246 -9.873 -13.755 48.001 1.00 28.06 O ANISOU 3512 O HOH B 246 2775 3903 3983 -32 203 -49 O HETATM 3513 O HOH B 247 14.195 -20.516 34.205 1.00 17.44 O ANISOU 3513 O HOH B 247 2003 2638 1985 -126 -215 -61 O HETATM 3514 O HOH B 248 -8.567 -14.387 39.175 1.00 32.40 O ANISOU 3514 O HOH B 248 4907 4526 2876 -1759 -498 650 O HETATM 3515 O HOH B 249 6.033 -23.385 50.737 1.00 23.99 O ANISOU 3515 O HOH B 249 4090 2504 2521 390 -854 133 O HETATM 3516 O HOH B 250 10.820 -7.487 33.002 1.00 28.68 O ANISOU 3516 O HOH B 250 2713 4364 3818 336 796 -529 O HETATM 3517 O HOH B 251 21.682 -14.938 37.212 1.00 22.83 O ANISOU 3517 O HOH B 251 3283 3413 1977 -251 179 -300 O HETATM 3518 O HOH B 252 1.471 0.219 34.721 1.00 32.54 O ANISOU 3518 O HOH B 252 4907 3289 4166 647 636 42 O HETATM 3519 O HOH B 253 3.384 -21.168 47.885 1.00 24.68 O ANISOU 3519 O HOH B 253 3531 3535 2308 605 82 381 O HETATM 3520 O HOH B 254 -6.738 -4.776 37.832 1.00 28.21 O ANISOU 3520 O HOH B 254 3440 3260 4016 235 -141 -306 O HETATM 3521 O HOH B 255 0.150 -15.410 55.986 1.00 27.81 O ANISOU 3521 O HOH B 255 3661 4209 2696 1971 769 599 O HETATM 3522 O HOH B 256 5.996 -0.448 47.926 1.00 29.27 O ANISOU 3522 O HOH B 256 4161 2979 3978 -194 610 -250 O HETATM 3523 O HOH B 257 8.489 -14.166 53.869 1.00 23.96 O ANISOU 3523 O HOH B 257 3652 3154 2295 104 -880 375 O HETATM 3524 O HOH B 258 18.920 -3.583 43.781 1.00 27.51 O ANISOU 3524 O HOH B 258 3240 3170 4040 -1217 -76 -59 O HETATM 3525 O HOH B 259 8.527 -24.808 43.922 1.00 36.06 O ANISOU 3525 O HOH B 259 4938 3847 4914 -892 1271 -580 O HETATM 3526 O HOH B 260 -1.253 -0.020 32.832 1.00 36.43 O ANISOU 3526 O HOH B 260 4912 3870 5058 1249 -177 41 O HETATM 3527 O HOH B 261 18.281 -3.254 40.984 1.00 31.88 O ANISOU 3527 O HOH B 261 3502 4778 3832 -674 -419 682 O HETATM 3528 O HOH B 262 9.859 -27.347 44.793 1.00 49.12 O ANISOU 3528 O HOH B 262 7974 6285 4404 -1569 -180 -930 O HETATM 3529 O HOH B 263 10.156 -25.549 40.331 1.00 33.20 O ANISOU 3529 O HOH B 263 4100 3304 5208 -565 -1140 -546 O HETATM 3530 O HOH B 264 -11.010 -6.955 48.978 1.00 33.31 O ANISOU 3530 O HOH B 264 4396 3064 5195 1176 850 227 O HETATM 3531 O HOH B 265 11.008 -2.538 47.909 1.00 27.88 O ANISOU 3531 O HOH B 265 4229 2296 4068 -241 632 -504 O HETATM 3532 O HOH B 266 9.074 -0.617 48.722 1.00 32.15 O ANISOU 3532 O HOH B 266 3599 5418 3198 746 -498 261 O HETATM 3533 O HOH B 267 3.877 -1.712 49.030 1.00 25.30 O ANISOU 3533 O HOH B 267 3553 3228 2829 -280 -30 -848 O HETATM 3534 O HOH B 268 -4.016 -3.602 50.048 1.00 28.19 O ANISOU 3534 O HOH B 268 3707 2730 4271 1047 552 608 O HETATM 3535 O HOH B 269 15.689 -3.805 40.083 1.00 32.43 O ANISOU 3535 O HOH B 269 3909 4642 3770 -738 -621 729 O HETATM 3536 O HOH B 270 19.799 -6.866 40.581 1.00 29.87 O ANISOU 3536 O HOH B 270 3624 3310 4412 -45 -496 -1254 O HETATM 3537 O HOH B 271 1.239 -22.032 38.726 1.00 26.62 O ANISOU 3537 O HOH B 271 2987 3543 3586 -584 -248 -821 O CONECT 894 3180 CONECT 924 3180 CONECT 931 3180 CONECT 1527 3179 CONECT 1552 3179 CONECT 1790 3179 CONECT 1803 3179 CONECT 2167 3180 CONECT 3179 1527 1552 1790 1803 CONECT 3180 894 924 931 2167 CONECT 3180 3426 CONECT 3181 3182 3193 CONECT 3182 3181 3183 CONECT 3183 3182 3184 3185 CONECT 3184 3183 3192 CONECT 3185 3183 3186 CONECT 3186 3185 3187 CONECT 3187 3186 3188 CONECT 3188 3187 3189 3190 3191 CONECT 3189 3188 CONECT 3190 3188 CONECT 3191 3188 CONECT 3192 3184 3193 CONECT 3193 3181 3192 CONECT 3194 3195 3206 CONECT 3195 3194 3196 CONECT 3196 3195 3197 3198 CONECT 3197 3196 3205 CONECT 3198 3196 3199 CONECT 3199 3198 3200 CONECT 3200 3199 3201 CONECT 3201 3200 3202 3203 3204 CONECT 3202 3201 CONECT 3203 3201 CONECT 3204 3201 CONECT 3205 3197 3206 CONECT 3206 3194 3205 CONECT 3207 3208 3209 CONECT 3208 3207 CONECT 3209 3207 3210 3211 CONECT 3210 3209 CONECT 3211 3209 3212 CONECT 3212 3211 CONECT 3213 3214 3215 CONECT 3214 3213 CONECT 3215 3213 3216 3217 CONECT 3216 3215 CONECT 3217 3215 3218 CONECT 3218 3217 CONECT 3219 3220 3221 CONECT 3220 3219 CONECT 3221 3219 3222 3223 CONECT 3222 3221 CONECT 3223 3221 3224 CONECT 3224 3223 CONECT 3426 3180 MASTER 332 0 7 12 27 0 13 6 3454 2 56 32 END
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RCSB PDB
PDBbind
79aa, >3OLM_2|Chain... at 92%
3rul
RCSB PDB
PDBbind
79aa, >3RUL_1|Chains... at 94%
3znz
RCSB PDB
PDBbind
152aa, >3ZNZ_2|Chain... at 100%
4i6l
RCSB PDB
PDBbind
76aa, >4I6L_2|Chain... at 90%
5e6j
RCSB PDB
PDBbind
76aa, >5E6J_2|Chains... at 97%
5gvi
RCSB PDB
PDBbind
72aa, >5GVI_3|Chain... at 100%
5l6h
RCSB PDB
PDBbind
76aa, >5L6H_2|Chains... at 96%
5l6i
RCSB PDB
PDBbind
76aa, >5L6I_2|Chains... at 96%
5l6j
RCSB PDB
PDBbind
76aa, >5L6J_2|Chains... at 96%
5lrw
RCSB PDB
PDBbind
76aa, >5LRW_2|Chains... at 98%
5ohp
RCSB PDB
PDBbind
76aa, >5OHP_2|Chains... at 100%
5ydr
RCSB PDB
PDBbind
75aa, >5YDR_1|Chains... at 97%
5yij
RCSB PDB
PDBbind
78aa, >5YIJ_2|Chains... at 97%
6isu
RCSB PDB
PDBbind
76aa, >6ISU_3|Chain... at 100%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
1otr
RCSB PDB
PDBbind
ubiquitin
1p3q
RCSB PDB
PDBbind
ubiquitin
1q0w
RCSB PDB
PDBbind
ubiquitin
1s1q
RCSB PDB
PDBbind
Ubiquitin
1wr1
RCSB PDB
PDBbind
ubiquitin
1wr6
RCSB PDB
PDBbind
ubiquitin
1wrd
RCSB PDB
PDBbind
ubiquitin
1yx5
RCSB PDB
PDBbind
Ubiquitin
1yx6
RCSB PDB
PDBbind
Ubiquitin
2c7m
RCSB PDB
PDBbind
ubiquitin
2c7n
RCSB PDB
PDBbind
ubiquitin
2den
RCSB PDB
PDBbind
Ubiquitin
2dx5
RCSB PDB
PDBbind
Ubiquitin
2fuh
RCSB PDB
PDBbind
Ubiquitin
2g45
RCSB PDB
PDBbind
ubiquitin
2hd5
RCSB PDB
PDBbind
ubiquitin
2hth
RCSB PDB
PDBbind
ubiquitin
2jt4
RCSB PDB
PDBbind
Ubiquitin
2k6d
RCSB PDB
PDBbind
ubiquitin
2kwu
RCSB PDB
PDBbind
Ubiquitin
2kwv
RCSB PDB
PDBbind
Ubiquitin
2lvo
RCSB PDB
PDBbind
ubiquitin
2mbb
RCSB PDB
PDBbind
Ubiquitin
2mcn
RCSB PDB
PDBbind
Ubiquitin
2mj5
RCSB PDB
PDBbind
Ubiquitin
2mur
RCSB PDB
PDBbind
Ubiquitin
2oob
RCSB PDB
PDBbind
ubiquitin
2qho
RCSB PDB
PDBbind
ubiquitin
2xbb
RCSB PDB
PDBbind
UBIQUITIN
3olm
RCSB PDB
PDBbind
Ubiquitin
4hcn
RCSB PDB
PDBbind
ubiquitin
4i6l
RCSB PDB
PDBbind
Ubiquitin
4k1r
RCSB PDB
PDBbind
Ubiquitin
4msm
RCSB PDB
PDBbind
Ubiquitin
Entry Information
PDB ID
4m0w
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
SARS-CoV papain-like protease C112S mutant
Ligand Name
ubiquitin
EC.Number
E.C.3.4.19.12 ;3.4.22.69
Resolution
1.4(Å)
Affinity (Kd/Ki/IC50)
Kd=6.7uM
Release Year
2014
Protein/NA Sequence
Check fasta file
Primary Reference
(2014) Acta Crystallogr.,Sect.D Vol. 70: pp. 572-581
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):
P0C6U8
P62992
Entrez Gene ID
NCBI Entrez Gene ID:
286839
ASD
Information of known allosteric effects of PDB entries
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times since Nov 2007.
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