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*** TRANSCRIPTION 19-MAR-18 6G0Q ***elNémo ID: 2401031933183680449Job options:ID = 2401031933183680449 JOBID = TRANSCRIPTION 19-MAR-18 6G0Q USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -65 DQMAX = 65 DQSTEP = 5 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER TRANSCRIPTION 19-MAR-18 6G0Q TITLE CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX TITLE 2 WITH AN ACETYLATED GATA1 PEPTIDE (K312AC/K315AC) COMPND MOL_ID: 1; COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PROTEIN HUNK1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ERYTHROID TRANSCRIPTION FACTOR; COMPND 8 CHAIN: B; COMPND 9 SYNONYM: ERYF1,GATA-BINDING FACTOR 1,GF-1,NF-E1 DNA-BINDING PROTEIN; COMPND 10 ENGINEERED: YES; COMPND 11 OTHER_DETAILS: GATA1 PEPTIDE ACETYLATED AT K312 AND K315 C-TERMINAL COMPND 12 TYR ADDED FOR UV DETECTION SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: BRD4, HUNK1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606 KEYWDS BROMODOMAIN, TRANSCRIPTION, COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR P.FILIPPAKOPOULOS,S.PICAUD,J.NEWMAN,F.SORRELL,F.VON DELFT, AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA REVDAT 3 20-FEB-19 6G0Q 1 JRNL REVDAT 2 26-DEC-18 6G0Q 1 JRNL REVDAT 1 28-NOV-18 6G0Q 0 JRNL AUTH J.P.LAMBERT,S.PICAUD,T.FUJISAWA,H.HOU,P.SAVITSKY, JRNL AUTH 2 L.UUSKULA-REIMAND,G.D.GUPTA,H.ABDOUNI,Z.Y.LIN,M.TUCHOLSKA, JRNL AUTH 3 J.D.R.KNIGHT,B.GONZALEZ-BADILLO,N.ST-DENIS,J.A.NEWMAN, JRNL AUTH 4 M.STUCKI,L.PELLETIER,N.BANDEIRA,M.D.WILSON, JRNL AUTH 5 P.FILIPPAKOPOULOS,A.C.GINGRAS JRNL TITL INTERACTOME REWIRING FOLLOWING PHARMACOLOGICAL TARGETING OF JRNL TITL 2 BET BROMODOMAINS. JRNL REF MOL. CELL V. 73 621 2019 JRNL REFN ISSN 1097-4164 JRNL PMID 30554943 JRNL DOI 10.1016/J.MOLCEL.2018.11.006 REMARK 2 REMARK 2 RESOLUTION. 1.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.17 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 3 NUMBER OF REFLECTIONS : 26788 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) : 0.143 REMARK 3 R VALUE (WORKING SET) : 0.141 REMARK 3 FREE R VALUE : 0.178 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1384 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1130 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 4 REMARK 3 SOLVENT ATOMS : 234 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.03 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.11000 REMARK 3 B22 (A**2) : 0.04000 REMARK 3 B33 (A**2) : -0.15000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.063 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.058 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.023 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.231 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY REMARK 4 REMARK 4 6G0Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAR-18. REMARK 100 THE DEPOSITION ID IS D_1200009241. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-APR-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I02 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28201 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400 REMARK 200 RESOLUTION RANGE LOW (A) : 43.855 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 200 DATA REDUNDANCY : 6.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.07100 REMARK 200 FOR THE DATA SET : 24.4000 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) : 1.48 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3 REMARK 200 DATA REDUNDANCY IN SHELL : 6.40 REMARK 200 R MERGE FOR SHELL (I) : 0.06300 REMARK 200 R SYM FOR SHELL (I) : 0.06300 REMARK 200 FOR SHELL : 9.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.5.7 REMARK 200 STARTING MODEL: ENSEMBLE OF 2OSS, 2OUO, 2GRC, 2OO1, 3DAI, 3D7C, REMARK 200 3DWY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.24 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30.0% PEG 1K 0.1M SPG PH 8.0, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 19.64200 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.17200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.92750 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.17200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.64200 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.92750 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 8400 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 SER A 42 REMARK 465 GLU A 168 REMARK 465 ALA B 309 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O SER B 310 O HOH B 401 1.87 REMARK 500 O HOH A 476 O HOH A 503 2.02 REMARK 500 O HOH A 377 O HOH A 476 2.11 REMARK 500 O HOH A 332 O HOH A 416 2.11 REMARK 500 O HOH A 439 O HOH A 496 2.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 302 O HOH A 505 2765 2.09 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 MET A 43 CG - SD - CE ANGL. DEV. = -22.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 94 74.96 -119.32 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 505 DISTANCE = 6.31 ANGSTROMS REMARK 525 HOH A 506 DISTANCE = 6.34 ANGSTROMS REMARK 525 HOH A 507 DISTANCE = 6.62 ANGSTROMS REMARK 525 HOH A 508 DISTANCE = 6.97 ANGSTROMS REMARK 525 HOH A 509 DISTANCE = 10.24 ANGSTROMS REMARK 525 HOH A 510 DISTANCE = 10.48 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 201 DBREF 6G0Q A 42 168 UNP O60885 BRD4_HUMAN 42 168 DBREF 6G0Q B 309 319 UNP P15976 GATA1_HUMAN 309 319 SEQADV 6G0Q MET A 43 UNP O60885 THR 43 CONFLICT SEQADV 6G0Q TYR B 319 UNP P15976 SER 319 CONFLICT SEQRES 1 A 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN SEQRES 2 A 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU SEQRES 3 A 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA SEQRES 4 A 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN SEQRES 5 A 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP SEQRES 6 A 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR SEQRES 7 A 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET SEQRES 8 A 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP SEQRES 9 A 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU SEQRES 10 A 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU SEQRES 1 B 11 ALA SER GLY ALY GLY LYS ALY LYS ARG GLY TYR MODRES 6G0Q ALY B 312 LYS MODIFIED RESIDUE MODRES 6G0Q ALY B 315 LYS MODIFIED RESIDUE HET ALY B 312 12 HET ALY B 315 12 HET EDO A 201 4 HETNAM ALY N(6)-ACETYLLYSINE HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 2 ALY 2(C8 H16 N2 O3) FORMUL 3 EDO C2 H6 O2 FORMUL 4 HOH *234(H2 O) HELIX 1 AA1 THR A 60 VAL A 69 1 10 HELIX 2 AA2 VAL A 69 HIS A 77 1 9 HELIX 3 AA3 ALA A 80 GLN A 84 5 5 HELIX 4 AA4 ASP A 96 ILE A 101 1 6 HELIX 5 AA5 ASP A 106 ASN A 116 1 11 HELIX 6 AA6 ASN A 121 ASN A 140 1 20 HELIX 7 AA7 ASP A 144 ASN A 162 1 19 LINK C GLY B 311 N ALY B 312 1555 1555 1.32 LINK C ALY B 312 N GLY B 313 1555 1555 1.34 LINK C LYS B 314 N ALY B 315 1555 1555 1.32 LINK C ALY B 315 N LYS B 316 1555 1555 1.33 SITE 1 AC1 6 MET A 43 ASN A 54 ASN A 130 HOH A 328 SITE 2 AC1 6 HOH A 397 HOH A 398 CRYST1 39.284 43.855 82.344 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.025456 0.000000 0.000000 0.00000 SCALE2 0.000000 0.022802 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012144 0.00000 ATOM 1 N MET A 43 21.052 27.701 12.354 1.00 11.85 N ANISOU 1 N MET A 43 1262 1528 1712 16 513 -151 N ATOM 2 CA MET A 43 21.389 26.916 11.132 1.00 9.22 C ANISOU 2 CA MET A 43 914 1282 1305 -104 192 80 C ATOM 3 C MET A 43 22.897 26.948 10.903 1.00 6.79 C ANISOU 3 C MET A 43 930 941 709 -78 234 -34 C ATOM 4 O MET A 43 23.601 27.832 11.377 1.00 8.37 O ANISOU 4 O MET A 43 916 1051 1214 -105 194 -187 O ATOM 5 CB MET A 43 20.734 27.583 9.930 1.00 12.21 C ANISOU 5 CB MET A 43 1137 1850 1650 9 152 488 C ATOM 6 CG MET A 43 19.219 27.841 10.147 1.00 16.13 C ANISOU 6 CG MET A 43 1104 2986 2037 -62 144 120 C ATOM 7 SD MET A 43 18.534 29.129 9.080 1.00 20.73 S ANISOU 7 SD MET A 43 2573 2196 3106 193 57 -275 S ATOM 8 CE MET A 43 18.342 27.711 8.114 1.00 8.49 C ANISOU 8 CE MET A 43 556 1342 1326 330 -226 458 C ATOM 9 N ASN A 44 23.397 26.003 10.133 1.00 4.95 N ANISOU 9 N ASN A 44 564 601 713 -107 1 101 N ATOM 10 CA ASN A 44 24.759 26.075 9.638 1.00 4.88 C ANISOU 10 CA ASN A 44 629 625 600 -11 87 52 C ATOM 11 C ASN A 44 24.823 27.144 8.563 1.00 4.53 C ANISOU 11 C ASN A 44 516 693 510 70 -3 53 C ATOM 12 O ASN A 44 23.860 27.345 7.822 1.00 5.25 O ANISOU 12 O ASN A 44 554 626 814 -36 -131 343 O ATOM 13 CB ASN A 44 25.188 24.769 9.027 1.00 5.38 C ANISOU 13 CB ASN A 44 639 605 799 29 0 52 C ATOM 14 CG ASN A 44 25.291 23.652 9.997 1.00 6.04 C ANISOU 14 CG ASN A 44 825 726 741 131 -22 79 C ATOM 15 OD1 ASN A 44 25.986 23.771 11.014 1.00 7.36 O ANISOU 15 OD1 ASN A 44 1411 669 714 186 -156 -32 O ATOM 16 ND2 ASN A 44 24.658 22.533 9.654 1.00 6.47 N ANISOU 16 ND2 ASN A 44 661 892 906 -23 -13 171 N ATOM 17 N PRO A 45 25.972 27.794 8.413 1.00 4.23 N ANISOU 17 N PRO A 45 527 618 459 43 -80 -19 N ATOM 18 CA PRO A 45 26.218 28.636 7.269 1.00 4.75 C ANISOU 18 CA PRO A 45 527 619 656 54 0 94 C ATOM 19 C PRO A 45 26.449 27.773 6.047 1.00 4.77 C ANISOU 19 C PRO A 45 590 539 683 -70 -40 69 C ATOM 20 O PRO A 45 26.724 26.587 6.168 1.00 4.38 O ANISOU 20 O PRO A 45 499 597 566 59 -79 73 O ATOM 21 CB PRO A 45 27.511 29.356 7.662 1.00 5.61 C ANISOU 21 CB PRO A 45 639 748 741 -99 92 -9 C ATOM 22 CG PRO A 45 28.252 28.345 8.454 1.00 6.22 C ANISOU 22 CG PRO A 45 707 820 834 -62 -56 -71 C ATOM 23 CD PRO A 45 27.192 27.642 9.241 1.00 5.16 C ANISOU 23 CD PRO A 45 575 776 608 103 -147 5 C ATOM 24 N PRO A 46 26.393 28.337 4.845 1.00 5.00 N ANISOU 24 N PRO A 46 458 753 689 113 2 105 N ATOM 25 CA PRO A 46 26.930 27.619 3.693 1.00 4.91 C ANISOU 25 CA PRO A 46 593 694 577 -6 -67 81 C ATOM 26 C PRO A 46 28.401 27.314 3.901 1.00 5.53 C ANISOU 26 C PRO A 46 579 712 807 22 -7 -12 C ATOM 27 O PRO A 46 29.054 28.041 4.660 1.00 5.55 O ANISOU 27 O PRO A 46 502 889 716 172 -58 -94 O ATOM 28 CB PRO A 46 26.789 28.641 2.560 1.00 6.06 C ANISOU 28 CB PRO A 46 680 1009 612 10 -132 233 C ATOM 29 CG PRO A 46 26.806 29.947 3.225 1.00 7.69 C ANISOU 29 CG PRO A 46 1055 1009 857 105 -54 231 C ATOM 30 CD PRO A 46 26.104 29.754 4.537 1.00 5.92 C ANISOU 30 CD PRO A 46 644 668 937 81 -29 -30 C ATOM 31 N PRO A 47 28.909 26.245 3.279 1.00 5.46 N ANISOU 31 N PRO A 47 585 807 681 61 -41 -19 N ATOM 32 CA PRO A 47 30.324 25.947 3.460 1.00 5.33 C ANISOU 32 CA PRO A 47 620 732 672 97 -58 86 C ATOM 33 C PRO A 47 31.187 27.005 2.807 1.00 5.27 C ANISOU 33 C PRO A 47 639 660 702 -3 -148 6 C ATOM 34 O PRO A 47 30.719 27.790 1.999 1.00 5.54 O ANISOU 34 O PRO A 47 636 689 778 100 -48 66 O ATOM 35 CB PRO A 47 30.458 24.590 2.760 1.00 7.35 C ANISOU 35 CB PRO A 47 947 745 1100 87 112 -14 C ATOM 36 CG PRO A 47 29.426 24.671 1.653 1.00 7.80 C ANISOU 36 CG PRO A 47 1215 822 924 73 73 -92 C ATOM 37 CD PRO A 47 28.263 25.332 2.318 1.00 6.66 C ANISOU 37 CD PRO A 47 804 875 849 -79 -115 -12 C ATOM 38 N PRO A 48 32.481 27.046 3.111 1.00 4.63 N ANISOU 38 N PRO A 48 607 633 518 104 -88 88 N ATOM 39 CA PRO A 48 33.350 27.997 2.425 1.00 4.95 C ANISOU 39 CA PRO A 48 556 638 684 41 -24 -21 C ATOM 40 C PRO A 48 33.397 27.707 0.903 1.00 4.95 C ANISOU 40 C PRO A 48 547 676 656 248 11 55 C ATOM 41 O PRO A 48 33.269 26.569 0.475 1.00 5.53 O ANISOU 41 O PRO A 48 619 721 761 156 -74 39 O ATOM 42 CB PRO A 48 34.729 27.743 3.078 1.00 5.62 C ANISOU 42 CB PRO A 48 632 659 844 170 -62 58 C ATOM 43 CG PRO A 48 34.399 27.048 4.393 1.00 5.94 C ANISOU 43 CG PRO A 48 665 904 689 212 -32 -12 C ATOM 44 CD PRO A 48 33.241 26.185 4.009 1.00 5.56 C ANISOU 44 CD PRO A 48 761 662 688 212 -84 154 C ATOM 45 N GLU A 49 33.580 28.742 0.104 1.00 4.60 N ANISOU 45 N GLU A 49 422 598 725 191 118 -2 N ATOM 46 CA GLU A 49 33.751 28.597 -1.321 1.00 5.29 C ANISOU 46 CA GLU A 49 625 728 654 108 -124 23 C ATOM 47 C GLU A 49 34.970 27.746 -1.625 1.00 5.22 C ANISOU 47 C GLU A 49 588 720 672 23 -9 -6 C ATOM 48 O GLU A 49 35.959 27.797 -0.897 1.00 6.25 O ANISOU 48 O GLU A 49 632 860 882 197 -129 -150 O ATOM 49 CB GLU A 49 33.896 29.942 -1.966 1.00 7.29 C ANISOU 49 CB GLU A 49 995 815 957 9 121 132 C ATOM 50 CG GLU A 49 32.571 30.720 -1.919 1.00 9.64 C ANISOU 50 CG GLU A 49 1139 1144 1379 207 71 340 C ATOM 51 CD GLU A 49 31.483 30.227 -2.843 1.00 12.07 C ANISOU 51 CD GLU A 49 1332 1633 1622 477 -248 90 C ATOM 52 OE1 GLU A 49 31.717 29.970 -4.029 1.00 14.48 O ANISOU 52 OE1 GLU A 49 1910 1896 1694 292 194 375 O ATOM 53 OE2 GLU A 49 30.363 30.132 -2.342 1.00 21.74 O ANISOU 53 OE2 GLU A 49 1578 4486 2193 -429 16 35 O ATOM 54 N THR A 50 34.881 26.940 -2.675 1.00 4.89 N ANISOU 54 N THR A 50 580 631 644 94 -50 44 N ATOM 55 CA THR A 50 35.973 26.073 -3.068 1.00 5.42 C ANISOU 55 CA THR A 50 609 714 733 77 -10 -92 C ATOM 56 C THR A 50 36.408 26.209 -4.513 1.00 6.31 C ANISOU 56 C THR A 50 889 726 781 187 81 26 C ATOM 57 O THR A 50 37.456 25.686 -4.858 1.00 6.83 O ANISOU 57 O THR A 50 809 1040 743 240 57 99 O ATOM 58 CB THR A 50 35.577 24.608 -2.832 1.00 7.11 C ANISOU 58 CB THR A 50 978 784 938 122 25 287 C ATOM 59 OG1 THR A 50 34.325 24.301 -3.455 1.00 10.10 O ANISOU 59 OG1 THR A 50 1370 1121 1344 -225 -289 275 O ATOM 60 CG2 THR A 50 35.517 24.301 -1.331 1.00 7.49 C ANISOU 60 CG2 THR A 50 993 937 914 167 160 215 C ATOM 61 N SER A 51 35.661 26.952 -5.342 1.00 5.94 N ANISOU 61 N SER A 51 728 727 799 -7 95 152 N ATOM 62 CA SER A 51 36.033 27.131 -6.757 1.00 6.83 C ANISOU 62 CA SER A 51 861 905 829 60 212 84 C ATOM 63 C SER A 51 35.588 28.501 -7.155 1.00 8.10 C ANISOU 63 C SER A 51 1008 1019 1049 30 167 322 C ATOM 64 O SER A 51 34.465 28.913 -6.829 1.00 12.22 O ANISOU 64 O SER A 51 1306 1300 2036 264 732 781 O ATOM 65 CB SER A 51 35.323 26.068 -7.591 1.00 12.16 C ANISOU 65 CB SER A 51 2092 1152 1375 -23 -333 -158 C ATOM 66 OG SER A 51 35.779 26.014 -8.932 1.00 20.65 O ANISOU 66 OG SER A 51 3269 2855 1721 -369 346 184 O ATOM 67 N ASN A 52 36.419 29.199 -7.902 1.00 5.72 N ANISOU 67 N ASN A 52 706 676 788 -29 -35 -19 N ATOM 68 CA ASN A 52 36.051 30.479 -8.437 1.00 6.84 C ANISOU 68 CA ASN A 52 883 785 928 5 -19 130 C ATOM 69 C ASN A 52 36.732 30.585 -9.795 1.00 6.42 C ANISOU 69 C ASN A 52 835 555 1049 84 79 94 C ATOM 70 O ASN A 52 37.943 30.799 -9.833 1.00 7.14 O ANISOU 70 O ASN A 52 816 901 994 22 157 309 O ATOM 71 CB ASN A 52 36.481 31.591 -7.491 1.00 7.65 C ANISOU 71 CB ASN A 52 923 1021 962 121 96 -92 C ATOM 72 CG ASN A 52 36.061 32.963 -7.977 1.00 8.04 C ANISOU 72 CG ASN A 52 769 1065 1218 99 337 86 C ATOM 73 OD1 ASN A 52 35.855 33.198 -9.177 1.00 9.72 O ANISOU 73 OD1 ASN A 52 1310 1087 1294 274 338 163 O ATOM 74 ND2 ASN A 52 35.909 33.871 -7.043 1.00 10.39 N ANISOU 74 ND2 ASN A 52 1527 1061 1357 145 116 -13 N ATOM 75 N PRO A 53 35.988 30.459 -10.886 1.00 8.16 N ANISOU 75 N PRO A 53 824 1082 1194 -160 4 83 N ATOM 76 CA PRO A 53 36.594 30.479 -12.229 1.00 8.54 C ANISOU 76 CA PRO A 53 1190 917 1134 -13 -8 -28 C ATOM 77 C PRO A 53 37.226 31.796 -12.620 1.00 8.11 C ANISOU 77 C PRO A 53 1175 899 1006 180 66 174 C ATOM 78 O PRO A 53 37.981 31.829 -13.584 1.00 10.66 O ANISOU 78 O PRO A 53 1411 1433 1206 -205 325 -83 O ATOM 79 CB PRO A 53 35.434 30.124 -13.154 1.00 12.42 C ANISOU 79 CB PRO A 53 1914 1648 1157 -449 -333 -23 C ATOM 80 CG PRO A 53 34.245 30.554 -12.416 1.00 15.39 C ANISOU 80 CG PRO A 53 1558 2551 1735 -202 -513 -63 C ATOM 81 CD PRO A 53 34.512 30.307 -10.962 1.00 10.27 C ANISOU 81 CD PRO A 53 864 1521 1516 -370 6 -54 C ATOM 82 N ASN A 54 36.964 32.860 -11.888 1.00 7.34 N ANISOU 82 N ASN A 54 939 968 882 -226 17 17 N ATOM 83 CA ASN A 54 37.591 34.139 -12.180 1.00 7.29 C ANISOU 83 CA ASN A 54 831 872 1064 -8 -15 294 C ATOM 84 C ASN A 54 38.931 34.328 -11.510 1.00 7.48 C ANISOU 84 C ASN A 54 737 844 1259 3 67 202 C ATOM 85 O ASN A 54 39.645 35.280 -11.860 1.00 9.53 O ANISOU 85 O ASN A 54 897 952 1770 -133 14 302 O ATOM 86 CB ASN A 54 36.630 35.278 -11.789 1.00 7.39 C ANISOU 86 CB ASN A 54 894 878 1034 14 -109 198 C ATOM 87 CG ASN A 54 35.400 35.322 -12.646 1.00 9.54 C ANISOU 87 CG ASN A 54 1148 1143 1332 44 -380 149 C ATOM 88 OD1 ASN A 54 35.352 34.789 -13.740 1.00 13.56 O ANISOU 88 OD1 ASN A 54 1469 2221 1461 589 -391 -179 O ATOM 89 ND2 ASN A 54 34.416 36.036 -12.162 1.00 11.62 N ANISOU 89 ND2 ASN A 54 1125 1819 1471 90 -53 89 N ATOM 90 N LYS A 55 39.284 33.465 -10.560 1.00 6.12 N ANISOU 90 N LYS A 55 612 707 1006 -63 -32 -23 N ATOM 91 CA LYS A 55 40.598 33.602 -9.954 1.00 7.24 C ANISOU 91 CA LYS A 55 755 942 1054 -44 -198 -108 C ATOM 92 C LYS A 55 41.657 33.118 -10.961 1.00 8.31 C ANISOU 92 C LYS A 55 846 930 1379 -11 -11 -72 C ATOM 93 O LYS A 55 41.462 32.118 -11.630 1.00 8.88 O ANISOU 93 O LYS A 55 551 1245 1575 14 -90 -367 O ATOM 94 CB LYS A 55 40.720 32.770 -8.700 1.00 8.18 C ANISOU 94 CB LYS A 55 889 1069 1150 97 -244 12 C ATOM 95 CG LYS A 55 40.009 33.318 -7.467 1.00 8.54 C ANISOU 95 CG LYS A 55 1093 954 1198 -266 -99 -103 C ATOM 96 CD LYS A 55 40.319 32.449 -6.238 1.00 13.65 C ANISOU 96 CD LYS A 55 1871 1808 1504 -39 -91 358 C ATOM 97 CE LYS A 55 39.747 32.961 -4.936 1.00 19.51 C ANISOU 97 CE LYS A 55 2624 2741 2047 324 576 430 C ATOM 98 NZ LYS A 55 40.643 32.452 -3.880 1.00 21.11 N ANISOU 98 NZ LYS A 55 2430 2690 2898 -199 -146 384 N ATOM 99 N PRO A 56 42.837 33.751 -10.992 1.00 6.93 N ANISOU 99 N PRO A 56 755 748 1129 116 -94 -38 N ATOM 100 CA PRO A 56 43.937 33.244 -11.779 1.00 6.16 C ANISOU 100 CA PRO A 56 759 774 805 -18 -116 -73 C ATOM 101 C PRO A 56 44.433 31.911 -11.193 1.00 6.39 C ANISOU 101 C PRO A 56 662 800 965 -31 -33 2 C ATOM 102 O PRO A 56 44.185 31.637 -10.032 1.00 10.07 O ANISOU 102 O PRO A 56 1411 1339 1076 385 294 203 O ATOM 103 CB PRO A 56 44.978 34.342 -11.649 1.00 6.96 C ANISOU 103 CB PRO A 56 679 817 1147 -40 -32 235 C ATOM 104 CG PRO A 56 44.727 34.869 -10.273 1.00 7.96 C ANISOU 104 CG PRO A 56 779 957 1287 -25 -209 -69 C ATOM 105 CD PRO A 56 43.258 34.820 -10.082 1.00 7.88 C ANISOU 105 CD PRO A 56 867 1058 1067 -78 9 -131 C ATOM 106 N LYS A 57 45.064 31.098 -12.009 1.00 5.21 N ANISOU 106 N LYS A 57 607 755 618 33 -76 220 N ATOM 107 CA LYS A 57 45.466 29.760 -11.645 1.00 6.75 C ANISOU 107 CA LYS A 57 738 769 1056 154 125 250 C ATOM 108 C LYS A 57 46.967 29.592 -11.870 1.00 5.06 C ANISOU 108 C LYS A 57 668 668 586 -37 54 58 C ATOM 109 O LYS A 57 47.498 30.023 -12.899 1.00 5.84 O ANISOU 109 O LYS A 57 666 780 770 -25 126 226 O ATOM 110 CB LYS A 57 44.744 28.711 -12.506 1.00 10.34 C ANISOU 110 CB LYS A 57 1220 1126 1581 -98 25 -15 C ATOM 111 CG LYS A 57 43.217 28.719 -12.428 1.00 14.04 C ANISOU 111 CG LYS A 57 1277 1831 2227 30 117 136 C ATOM 112 CD LYS A 57 42.628 27.479 -13.047 1.00 20.30 C ANISOU 112 CD LYS A 57 2311 2501 2898 -384 -528 -269 C ATOM 113 CE LYS A 57 43.078 27.234 -14.467 1.00 27.36 C ANISOU 113 CE LYS A 57 3064 4174 3155 -651 -194 -374 C ATOM 114 NZ LYS A 57 42.786 28.405 -15.321 1.00 32.97 N ANISOU 114 NZ LYS A 57 4008 4353 4165 -532 428 192 N ATOM 115 N ARG A 58 47.653 28.944 -10.950 1.00 4.26 N ANISOU 115 N ARG A 58 540 520 557 -8 163 26 N ATOM 116 CA ARG A 58 49.035 28.514 -11.153 1.00 4.52 C ANISOU 116 CA ARG A 58 554 591 569 22 135 -19 C ATOM 117 C ARG A 58 49.254 27.177 -10.485 1.00 4.78 C ANISOU 117 C ARG A 58 599 573 643 -31 35 -18 C ATOM 118 O ARG A 58 48.702 26.895 -9.430 1.00 6.53 O ANISOU 118 O ARG A 58 903 723 852 48 263 132 O ATOM 119 CB ARG A 58 50.067 29.554 -10.687 1.00 4.46 C ANISOU 119 CB ARG A 58 513 646 534 -14 70 108 C ATOM 120 CG ARG A 58 50.097 29.773 -9.175 1.00 4.38 C ANISOU 120 CG ARG A 58 562 546 556 59 46 43 C ATOM 121 CD ARG A 58 51.166 30.800 -8.874 1.00 5.04 C ANISOU 121 CD ARG A 58 618 653 644 21 -27 -16 C ATOM 122 NE ARG A 58 51.292 31.081 -7.448 1.00 4.51 N ANISOU 122 NE ARG A 58 516 611 587 14 5 54 N ATOM 123 CZ ARG A 58 52.195 31.889 -6.909 1.00 7.94 C ANISOU 123 CZ ARG A 58 774 1313 929 -393 66 -196 C ATOM 124 NH1 ARG A 58 53.069 32.506 -7.682 1.00 11.51 N ANISOU 124 NH1 ARG A 58 1013 2175 1185 -869 100 -72 N ATOM 125 NH2 ARG A 58 52.204 32.089 -5.596 1.00 10.00 N ANISOU 125 NH2 ARG A 58 976 1913 910 -727 31 -112 N ATOM 126 N GLN A 59 50.122 26.407 -11.108 1.00 6.03 N ANISOU 126 N GLN A 59 704 754 830 125 182 96 N ATOM 127 CA GLN A 59 50.682 25.216 -10.530 1.00 6.35 C ANISOU 127 CA GLN A 59 785 823 802 -27 66 278 C ATOM 128 C GLN A 59 52.025 25.565 -9.949 1.00 6.16 C ANISOU 128 C GLN A 59 633 817 889 189 82 248 C ATOM 129 O GLN A 59 52.826 26.236 -10.587 1.00 8.20 O ANISOU 129 O GLN A 59 921 1148 1044 -33 137 385 O ATOM 130 CB GLN A 59 50.885 24.187 -11.639 1.00 8.58 C ANISOU 130 CB GLN A 59 1037 949 1271 33 -77 -45 C ATOM 131 CG GLN A 59 51.517 22.891 -11.154 1.00 10.97 C ANISOU 131 CG GLN A 59 1403 1185 1578 200 18 230 C ATOM 132 CD GLN A 59 51.758 21.896 -12.266 1.00 13.88 C ANISOU 132 CD GLN A 59 1600 1826 1848 259 36 -190 C ATOM 133 OE1 GLN A 59 50.832 21.447 -12.944 1.00 17.18 O ANISOU 133 OE1 GLN A 59 2011 2183 2332 109 -125 -510 O ATOM 134 NE2 GLN A 59 52.991 21.523 -12.435 1.00 11.61 N ANISOU 134 NE2 GLN A 59 1571 1404 1436 163 160 -302 N ATOM 135 N THR A 60 52.293 25.144 -8.734 1.00 6.02 N ANISOU 135 N THR A 60 587 927 773 121 125 118 N ATOM 136 CA THR A 60 53.600 25.322 -8.135 1.00 5.88 C ANISOU 136 CA THR A 60 749 696 787 45 -3 162 C ATOM 137 C THR A 60 53.977 24.066 -7.360 1.00 4.56 C ANISOU 137 C THR A 60 547 643 541 16 206 106 C ATOM 138 O THR A 60 53.104 23.269 -6.944 1.00 4.68 O ANISOU 138 O THR A 60 654 473 652 -41 105 103 O ATOM 139 CB THR A 60 53.671 26.499 -7.181 1.00 6.62 C ANISOU 139 CB THR A 60 851 825 838 43 116 75 C ATOM 140 OG1 THR A 60 52.908 26.217 -5.996 1.00 6.93 O ANISOU 140 OG1 THR A 60 1043 682 907 -39 253 55 O ATOM 141 CG2 THR A 60 53.166 27.808 -7.803 1.00 8.44 C ANISOU 141 CG2 THR A 60 1068 851 1287 100 205 237 C ATOM 142 N ASN A 61 55.276 23.877 -7.182 1.00 4.38 N ANISOU 142 N ASN A 61 579 585 500 16 135 70 N ATOM 143 CA ASN A 61 55.729 22.724 -6.403 1.00 4.76 C ANISOU 143 CA ASN A 61 651 607 551 163 111 20 C ATOM 144 C ASN A 61 55.114 22.780 -4.983 1.00 4.15 C ANISOU 144 C ASN A 61 442 557 578 10 98 -49 C ATOM 145 O ASN A 61 54.722 21.768 -4.425 1.00 5.10 O ANISOU 145 O ASN A 61 763 587 587 86 236 15 O ATOM 146 CB ASN A 61 57.257 22.710 -6.401 1.00 5.74 C ANISOU 146 CB ASN A 61 662 909 610 217 262 -179 C ATOM 147 CG ASN A 61 57.843 21.398 -5.945 1.00 6.35 C ANISOU 147 CG ASN A 61 917 945 548 242 232 -141 C ATOM 148 OD1 ASN A 61 57.157 20.379 -5.801 1.00 8.68 O ANISOU 148 OD1 ASN A 61 1319 881 1095 324 225 180 O ATOM 149 ND2 ASN A 61 59.147 21.440 -5.750 1.00 8.82 N ANISOU 149 ND2 ASN A 61 1019 1371 960 134 -38 -134 N ATOM 150 N GLN A 62 55.092 23.963 -4.372 1.00 4.21 N ANISOU 150 N GLN A 62 529 453 615 -86 218 32 N ATOM 151 CA GLN A 62 54.492 24.114 -3.036 1.00 4.47 C ANISOU 151 CA GLN A 62 483 644 571 51 127 -1 C ATOM 152 C GLN A 62 53.028 23.654 -3.005 1.00 3.90 C ANISOU 152 C GLN A 62 547 518 415 -39 42 -2 C ATOM 153 O GLN A 62 52.641 22.903 -2.128 1.00 3.87 O ANISOU 153 O GLN A 62 557 461 453 27 161 -31 O ATOM 154 CB GLN A 62 54.583 25.552 -2.545 1.00 4.76 C ANISOU 154 CB GLN A 62 561 677 569 98 52 -75 C ATOM 155 CG GLN A 62 55.984 26.071 -2.222 1.00 5.63 C ANISOU 155 CG GLN A 62 571 789 776 80 29 -60 C ATOM 156 CD GLN A 62 55.925 27.473 -1.640 1.00 6.85 C ANISOU 156 CD GLN A 62 938 741 923 -95 99 -34 C ATOM 157 OE1 GLN A 62 55.276 28.397 -2.205 1.00 8.04 O ANISOU 157 OE1 GLN A 62 953 872 1228 116 91 -146 O ATOM 158 NE2 GLN A 62 56.622 27.669 -0.546 1.00 9.51 N ANISOU 158 NE2 GLN A 62 1313 1190 1109 -113 -129 72 N ATOM 159 N LEU A 63 52.226 24.093 -3.969 1.00 3.90 N ANISOU 159 N LEU A 63 462 384 635 84 37 30 N ATOM 160 CA LEU A 63 50.838 23.697 -3.998 1.00 4.28 C ANISOU 160 CA LEU A 63 523 533 567 -51 42 -115 C ATOM 161 C LEU A 63 50.663 22.209 -4.265 1.00 4.19 C ANISOU 161 C LEU A 63 522 506 562 -18 48 -27 C ATOM 162 O LEU A 63 49.793 21.565 -3.647 1.00 4.44 O ANISOU 162 O LEU A 63 639 584 461 -12 109 22 O ATOM 163 CB LEU A 63 50.019 24.569 -4.979 1.00 4.52 C ANISOU 163 CB LEU A 63 481 599 636 38 30 -160 C ATOM 164 CG LEU A 63 49.836 26.035 -4.580 1.00 5.27 C ANISOU 164 CG LEU A 63 729 512 760 -45 -10 -45 C ATOM 165 CD1 LEU A 63 49.271 26.795 -5.777 1.00 6.25 C ANISOU 165 CD1 LEU A 63 793 746 835 51 80 113 C ATOM 166 CD2 LEU A 63 48.900 26.126 -3.405 1.00 5.92 C ANISOU 166 CD2 LEU A 63 750 743 756 51 -39 -61 C ATOM 167 N GLN A 64 51.477 21.641 -5.152 1.00 3.99 N ANISOU 167 N GLN A 64 508 461 545 -36 141 89 N ATOM 168 CA GLN A 64 51.417 20.219 -5.394 1.00 4.87 C ANISOU 168 CA GLN A 64 676 550 621 -63 -34 -136 C ATOM 169 C GLN A 64 51.754 19.431 -4.138 1.00 4.17 C ANISOU 169 C GLN A 64 482 516 586 -9 154 -106 C ATOM 170 O GLN A 64 51.055 18.468 -3.796 1.00 4.71 O ANISOU 170 O GLN A 64 655 458 675 -69 174 -162 O ATOM 171 CB GLN A 64 52.320 19.866 -6.564 1.00 6.83 C ANISOU 171 CB GLN A 64 898 767 929 0 265 -76 C ATOM 172 CG GLN A 64 51.735 20.337 -7.896 1.00 10.98 C ANISOU 172 CG GLN A 64 1497 1344 1329 228 0 248 C ATOM 173 CD GLN A 64 52.198 19.552 -9.098 1.00 15.54 C ANISOU 173 CD GLN A 64 2216 2095 1593 391 48 -167 C ATOM 174 OE1 GLN A 64 51.449 19.412 -10.088 1.00 22.64 O ANISOU 174 OE1 GLN A 64 3196 3554 1849 47 -607 239 O ATOM 175 NE2 GLN A 64 53.410 19.050 -9.053 1.00 14.83 N ANISOU 175 NE2 GLN A 64 2080 2422 1131 467 158 -678 N ATOM 176 N TYR A 65 52.797 19.848 -3.442 1.00 3.39 N ANISOU 176 N TYR A 65 494 385 407 75 114 -11 N ATOM 177 CA TYR A 65 53.185 19.187 -2.201 1.00 3.92 C ANISOU 177 CA TYR A 65 541 454 494 66 60 60 C ATOM 178 C TYR A 65 52.060 19.286 -1.160 1.00 3.83 C ANISOU 178 C TYR A 65 527 434 493 -41 59 28 C ATOM 179 O TYR A 65 51.784 18.323 -0.435 1.00 3.94 O ANISOU 179 O TYR A 65 515 431 549 -17 105 37 O ATOM 180 CB TYR A 65 54.476 19.820 -1.685 1.00 5.12 C ANISOU 180 CB TYR A 65 572 675 698 15 80 -61 C ATOM 181 CG TYR A 65 55.040 19.228 -0.447 1.00 5.50 C ANISOU 181 CG TYR A 65 656 747 687 -47 16 -51 C ATOM 182 CD1 TYR A 65 54.653 19.691 0.815 1.00 5.63 C ANISOU 182 CD1 TYR A 65 693 728 717 27 220 96 C ATOM 183 CD2 TYR A 65 55.951 18.220 -0.508 1.00 6.25 C ANISOU 183 CD2 TYR A 65 841 835 697 78 4 -147 C ATOM 184 CE1 TYR A 65 55.177 19.169 1.975 1.00 5.27 C ANISOU 184 CE1 TYR A 65 592 702 707 -80 142 32 C ATOM 185 CE2 TYR A 65 56.505 17.691 0.634 1.00 7.12 C ANISOU 185 CE2 TYR A 65 1042 844 818 213 16 -2 C ATOM 186 CZ TYR A 65 56.090 18.139 1.878 1.00 6.00 C ANISOU 186 CZ TYR A 65 778 727 775 46 11 50 C ATOM 187 OH TYR A 65 56.634 17.591 3.014 1.00 7.47 O ANISOU 187 OH TYR A 65 967 1121 747 255 -120 -94 O ATOM 188 N LEU A 66 51.441 20.455 -1.075 1.00 3.31 N ANISOU 188 N LEU A 66 409 468 378 -36 93 60 N ATOM 189 CA LEU A 66 50.360 20.633 -0.094 1.00 3.72 C ANISOU 189 CA LEU A 66 385 568 461 16 88 -42 C ATOM 190 C LEU A 66 49.236 19.626 -0.355 1.00 3.91 C ANISOU 190 C LEU A 66 577 390 518 -32 110 -10 C ATOM 191 O LEU A 66 48.623 19.155 0.613 1.00 4.99 O ANISOU 191 O LEU A 66 601 731 564 -189 123 21 O ATOM 192 CB LEU A 66 49.842 22.065 -0.080 1.00 4.33 C ANISOU 192 CB LEU A 66 588 536 518 4 216 -6 C ATOM 193 CG LEU A 66 50.742 23.038 0.673 1.00 5.25 C ANISOU 193 CG LEU A 66 692 688 611 -56 135 -43 C ATOM 194 CD1 LEU A 66 50.491 24.473 0.234 1.00 6.83 C ANISOU 194 CD1 LEU A 66 938 777 877 -21 118 123 C ATOM 195 CD2 LEU A 66 50.564 22.878 2.185 1.00 5.92 C ANISOU 195 CD2 LEU A 66 860 768 621 -97 52 50 C ATOM 196 N LEU A 67 48.904 19.323 -1.598 1.00 3.70 N ANISOU 196 N LEU A 67 377 524 503 -21 99 59 N ATOM 197 CA LEU A 67 47.865 18.333 -1.905 1.00 4.63 C ANISOU 197 CA LEU A 67 462 584 711 -32 18 -81 C ATOM 198 C LEU A 67 48.377 16.905 -1.772 1.00 4.85 C ANISOU 198 C LEU A 67 677 526 637 -80 103 -87 C ATOM 199 O LEU A 67 47.750 16.087 -1.065 1.00 6.78 O ANISOU 199 O LEU A 67 1060 520 993 -96 272 60 O ATOM 200 CB LEU A 67 47.273 18.548 -3.280 1.00 5.11 C ANISOU 200 CB LEU A 67 772 564 606 -17 48 -207 C ATOM 201 CG LEU A 67 46.120 17.587 -3.694 1.00 6.48 C ANISOU 201 CG LEU A 67 846 725 890 -94 -82 -171 C ATOM 202 CD1 LEU A 67 44.987 17.646 -2.683 1.00 7.62 C ANISOU 202 CD1 LEU A 67 897 918 1079 -342 38 12 C ATOM 203 CD2 LEU A 67 45.652 17.982 -5.099 1.00 9.25 C ANISOU 203 CD2 LEU A 67 1436 1175 902 -112 -90 14 C ATOM 204 N ARG A 68 49.497 16.604 -2.425 1.00 5.03 N ANISOU 204 N ARG A 68 696 543 672 -47 104 -103 N ATOM 205 CA ARG A 68 49.907 15.215 -2.603 1.00 6.34 C ANISOU 205 CA ARG A 68 991 531 886 -54 -41 -200 C ATOM 206 C ARG A 68 50.580 14.665 -1.385 1.00 6.68 C ANISOU 206 C ARG A 68 1025 724 787 -29 144 11 C ATOM 207 O ARG A 68 50.576 13.456 -1.187 1.00 9.08 O ANISOU 207 O ARG A 68 1417 726 1305 20 -38 153 O ATOM 208 CB ARG A 68 50.843 15.145 -3.813 1.00 8.75 C ANISOU 208 CB ARG A 68 1410 722 1192 74 320 -227 C ATOM 209 CG ARG A 68 50.092 15.473 -5.098 1.00 13.69 C ANISOU 209 CG ARG A 68 2170 1741 1288 153 152 -83 C ATOM 210 CD ARG A 68 49.231 14.336 -5.586 1.00 24.37 C ANISOU 210 CD ARG A 68 3340 3007 2913 -833 -464 -240 C ATOM 211 NE ARG A 68 47.806 14.502 -5.315 1.00 30.99 N ANISOU 211 NE ARG A 68 3690 4511 3571 403 136 -1412 N ATOM 212 CZ ARG A 68 46.833 14.585 -6.234 1.00 35.94 C ANISOU 212 CZ ARG A 68 4133 5597 3923 1045 -103 -907 C ATOM 213 NH1 ARG A 68 47.093 14.553 -7.543 1.00 44.60 N ANISOU 213 NH1 ARG A 68 5205 7700 4040 -640 334 -337 N ATOM 214 NH2 ARG A 68 45.556 14.704 -5.838 1.00 35.03 N ANISOU 214 NH2 ARG A 68 3870 4735 4703 -797 77 -1047 N ATOM 215 N VAL A 69 51.178 15.512 -0.552 1.00 5.37 N ANISOU 215 N VAL A 69 755 647 637 96 155 78 N ATOM 216 CA VAL A 69 51.876 15.065 0.660 1.00 5.51 C ANISOU 216 CA VAL A 69 677 660 756 20 -10 -22 C ATOM 217 C VAL A 69 51.108 15.521 1.899 1.00 5.77 C ANISOU 217 C VAL A 69 795 700 697 54 51 88 C ATOM 218 O VAL A 69 50.737 14.717 2.739 1.00 7.94 O ANISOU 218 O VAL A 69 1367 635 1015 39 304 179 O ATOM 219 CB VAL A 69 53.322 15.568 0.703 1.00 5.61 C ANISOU 219 CB VAL A 69 687 695 749 7 141 39 C ATOM 220 CG1 VAL A 69 53.959 15.187 2.004 1.00 7.04 C ANISOU 220 CG1 VAL A 69 884 890 901 176 -105 -95 C ATOM 221 CG2 VAL A 69 54.087 14.976 -0.497 1.00 6.64 C ANISOU 221 CG2 VAL A 69 889 781 852 100 147 -77 C ATOM 222 N VAL A 70 50.862 16.809 2.080 1.00 5.72 N ANISOU 222 N VAL A 70 771 720 679 107 181 82 N ATOM 223 CA VAL A 70 50.319 17.285 3.364 1.00 5.10 C ANISOU 223 CA VAL A 70 624 683 628 68 109 94 C ATOM 224 C VAL A 70 48.863 16.857 3.529 1.00 4.73 C ANISOU 224 C VAL A 70 650 537 607 39 100 74 C ATOM 225 O VAL A 70 48.528 16.108 4.459 1.00 6.28 O ANISOU 225 O VAL A 70 864 849 671 -21 228 194 O ATOM 226 CB VAL A 70 50.455 18.800 3.544 1.00 5.65 C ANISOU 226 CB VAL A 70 745 724 676 -66 107 37 C ATOM 227 CG1 VAL A 70 49.897 19.225 4.884 1.00 6.17 C ANISOU 227 CG1 VAL A 70 851 791 702 0 170 65 C ATOM 228 CG2 VAL A 70 51.907 19.194 3.400 1.00 6.06 C ANISOU 228 CG2 VAL A 70 732 763 808 -54 43 -28 C ATOM 229 N LEU A 71 48.001 17.273 2.614 1.00 4.89 N ANISOU 229 N LEU A 71 510 662 685 -84 99 185 N ATOM 230 CA LEU A 71 46.578 16.910 2.700 1.00 4.70 C ANISOU 230 CA LEU A 71 482 694 609 0 243 81 C ATOM 231 C LEU A 71 46.405 15.420 2.674 1.00 5.54 C ANISOU 231 C LEU A 71 620 713 769 -79 155 95 C ATOM 232 O LEU A 71 45.707 14.866 3.524 1.00 6.03 O ANISOU 232 O LEU A 71 718 784 790 3 196 194 O ATOM 233 CB LEU A 71 45.793 17.569 1.580 1.00 5.88 C ANISOU 233 CB LEU A 71 655 755 823 -35 64 154 C ATOM 234 CG LEU A 71 44.279 17.450 1.569 1.00 7.10 C ANISOU 234 CG LEU A 71 647 1052 998 -38 116 72 C ATOM 235 CD1 LEU A 71 43.787 16.114 1.070 1.00 8.14 C ANISOU 235 CD1 LEU A 71 1041 1041 1008 -81 -52 153 C ATOM 236 CD2 LEU A 71 43.623 17.796 2.874 1.00 7.90 C ANISOU 236 CD2 LEU A 71 926 1187 888 -198 -41 -176 C ATOM 237 N LYS A 72 47.041 14.747 1.721 1.00 5.99 N ANISOU 237 N LYS A 72 821 664 787 -165 200 32 N ATOM 238 CA LYS A 72 46.865 13.288 1.601 1.00 7.47 C ANISOU 238 CA LYS A 72 1159 648 1029 -66 43 6 C ATOM 239 C LYS A 72 47.263 12.562 2.877 1.00 6.42 C ANISOU 239 C LYS A 72 723 660 1055 -3 79 -8 C ATOM 240 O LYS A 72 46.568 11.608 3.295 1.00 8.40 O ANISOU 240 O LYS A 72 1201 682 1307 -155 122 133 O ATOM 241 CB LYS A 72 47.712 12.748 0.437 1.00 11.19 C ANISOU 241 CB LYS A 72 1769 1356 1124 14 323 -85 C ATOM 242 CG LYS A 72 47.708 11.234 0.233 1.00 16.15 C ANISOU 242 CG LYS A 72 2154 1413 2568 -105 -223 -211 C ATOM 243 CD LYS A 72 47.920 10.859 -1.241 1.00 25.40 C ANISOU 243 CD LYS A 72 3893 3210 2546 -54 133 -104 C ATOM 244 CE LYS A 72 49.383 10.733 -1.663 1.00 30.17 C ANISOU 244 CE LYS A 72 3802 3847 3811 -472 145 115 C ATOM 245 NZ LYS A 72 49.725 11.480 -2.928 1.00 25.55 N ANISOU 245 NZ LYS A 72 3749 2732 3224 -590 -265 -483 N ATOM 246 N THR A 73 48.372 12.953 3.487 1.00 5.44 N ANISOU 246 N THR A 73 727 602 738 -58 158 65 N ATOM 247 CA THR A 73 48.837 12.275 4.701 1.00 6.38 C ANISOU 247 CA THR A 73 933 718 774 91 70 35 C ATOM 248 C THR A 73 47.832 12.481 5.840 1.00 6.42 C ANISOU 248 C THR A 73 944 555 938 -88 220 63 C ATOM 249 O THR A 73 47.479 11.541 6.568 1.00 7.02 O ANISOU 249 O THR A 73 926 744 997 -82 272 202 O ATOM 250 CB THR A 73 50.222 12.791 5.133 1.00 7.97 C ANISOU 250 CB THR A 73 889 1005 1132 4 101 299 C ATOM 251 OG1 THR A 73 51.151 12.453 4.114 1.00 10.74 O ANISOU 251 OG1 THR A 73 1122 1431 1527 189 447 469 O ATOM 252 CG2 THR A 73 50.653 12.143 6.413 1.00 10.54 C ANISOU 252 CG2 THR A 73 1303 1548 1150 118 22 393 C ATOM 253 N LEU A 74 47.348 13.705 6.029 1.00 5.27 N ANISOU 253 N LEU A 74 655 582 765 -63 186 133 N ATOM 254 CA LEU A 74 46.386 13.955 7.112 1.00 5.61 C ANISOU 254 CA LEU A 74 705 694 732 65 135 85 C ATOM 255 C LEU A 74 45.058 13.262 6.824 1.00 5.42 C ANISOU 255 C LEU A 74 772 620 666 13 84 132 C ATOM 256 O LEU A 74 44.436 12.721 7.733 1.00 6.14 O ANISOU 256 O LEU A 74 944 639 749 -115 234 32 O ATOM 257 CB LEU A 74 46.163 15.451 7.331 1.00 6.32 C ANISOU 257 CB LEU A 74 784 669 947 91 150 88 C ATOM 258 CG LEU A 74 47.111 16.130 8.323 1.00 10.52 C ANISOU 258 CG LEU A 74 1386 888 1722 -334 -212 55 C ATOM 259 CD1 LEU A 74 48.539 16.117 7.872 1.00 12.59 C ANISOU 259 CD1 LEU A 74 1721 1168 1895 8 252 -1 C ATOM 260 CD2 LEU A 74 46.640 17.563 8.592 1.00 12.21 C ANISOU 260 CD2 LEU A 74 1403 1281 1951 -14 -215 -342 C ATOM 261 N TRP A 75 44.628 13.281 5.570 1.00 5.74 N ANISOU 261 N TRP A 75 623 862 695 -163 40 102 N ATOM 262 CA TRP A 75 43.333 12.721 5.175 1.00 5.70 C ANISOU 262 CA TRP A 75 621 747 795 -54 -17 5 C ATOM 263 C TRP A 75 43.210 11.238 5.516 1.00 6.21 C ANISOU 263 C TRP A 75 744 783 833 -114 156 45 C ATOM 264 O TRP A 75 42.121 10.790 5.918 1.00 7.31 O ANISOU 264 O TRP A 75 868 730 1178 -207 352 -85 O ATOM 265 CB TRP A 75 43.103 12.949 3.682 1.00 6.12 C ANISOU 265 CB TRP A 75 760 788 777 67 75 0 C ATOM 266 CG TRP A 75 41.735 12.618 3.207 1.00 6.64 C ANISOU 266 CG TRP A 75 825 865 832 65 -6 -205 C ATOM 267 CD1 TRP A 75 41.259 11.413 2.789 1.00 9.18 C ANISOU 267 CD1 TRP A 75 1148 835 1503 98 55 -381 C ATOM 268 CD2 TRP A 75 40.648 13.518 3.146 1.00 5.74 C ANISOU 268 CD2 TRP A 75 819 724 638 10 102 39 C ATOM 269 NE1 TRP A 75 39.950 11.524 2.450 1.00 10.20 N ANISOU 269 NE1 TRP A 75 1158 904 1812 26 -119 -559 N ATOM 270 CE2 TRP A 75 39.545 12.819 2.659 1.00 7.35 C ANISOU 270 CE2 TRP A 75 957 937 896 64 20 -403 C ATOM 271 CE3 TRP A 75 40.500 14.858 3.492 1.00 5.93 C ANISOU 271 CE3 TRP A 75 700 710 841 -122 62 -30 C ATOM 272 CZ2 TRP A 75 38.297 13.428 2.463 1.00 7.13 C ANISOU 272 CZ2 TRP A 75 894 772 1039 -179 -259 -162 C ATOM 273 CZ3 TRP A 75 39.289 15.478 3.289 1.00 6.24 C ANISOU 273 CZ3 TRP A 75 835 687 848 13 65 0 C ATOM 274 CH2 TRP A 75 38.202 14.779 2.772 1.00 6.31 C ANISOU 274 CH2 TRP A 75 814 788 795 93 -43 -51 C ATOM 275 N LYS A 76 44.315 10.506 5.366 1.00 5.90 N ANISOU 275 N LYS A 76 824 679 736 -91 231 93 N ATOM 276 CA LYS A 76 44.305 9.048 5.552 1.00 7.28 C ANISOU 276 CA LYS A 76 1162 617 984 14 16 -71 C ATOM 277 C LYS A 76 44.508 8.642 6.997 1.00 7.46 C ANISOU 277 C LYS A 76 1211 779 842 -40 188 -177 C ATOM 278 O LYS A 76 44.364 7.470 7.341 1.00 10.54 O ANISOU 278 O LYS A 76 1844 838 1322 -44 270 33 O ATOM 279 CB LYS A 76 45.320 8.370 4.624 1.00 11.33 C ANISOU 279 CB LYS A 76 1923 1042 1336 491 273 -114 C ATOM 280 CG LYS A 76 46.747 8.539 5.005 1.00 15.25 C ANISOU 280 CG LYS A 76 1992 1950 1852 111 346 85 C ATOM 281 CD LYS A 76 47.625 7.657 4.121 1.00 20.89 C ANISOU 281 CD LYS A 76 2851 2811 2273 523 459 -436 C ATOM 282 CE LYS A 76 49.036 8.188 4.004 1.00 24.52 C ANISOU 282 CE LYS A 76 2982 3074 3259 233 245 -344 C ATOM 283 NZ LYS A 76 49.864 8.158 5.236 1.00 28.51 N ANISOU 283 NZ LYS A 76 3801 3983 3046 255 170 -56 N ATOM 284 N HIS A 77 44.827 9.600 7.854 1.00 5.47 N ANISOU 284 N HIS A 77 868 649 558 -45 391 -13 N ATOM 285 CA HIS A 77 45.111 9.308 9.262 1.00 5.63 C ANISOU 285 CA HIS A 77 814 691 632 96 265 -59 C ATOM 286 C HIS A 77 43.832 8.817 9.996 1.00 5.40 C ANISOU 286 C HIS A 77 679 602 770 41 68 92 C ATOM 287 O HIS A 77 42.724 9.213 9.666 1.00 5.43 O ANISOU 287 O HIS A 77 670 713 680 69 152 60 O ATOM 288 CB HIS A 77 45.664 10.573 9.937 1.00 5.92 C ANISOU 288 CB HIS A 77 637 740 870 -23 292 -52 C ATOM 289 CG HIS A 77 46.276 10.319 11.253 1.00 6.39 C ANISOU 289 CG HIS A 77 809 786 830 -215 152 -210 C ATOM 290 ND1 HIS A 77 45.555 10.258 12.417 1.00 6.96 N ANISOU 290 ND1 HIS A 77 757 1026 859 -17 152 78 N ATOM 291 CD2 HIS A 77 47.566 10.115 11.611 1.00 10.06 C ANISOU 291 CD2 HIS A 77 884 1436 1502 99 123 220 C ATOM 292 CE1 HIS A 77 46.367 10.036 13.435 1.00 8.94 C ANISOU 292 CE1 HIS A 77 1129 1251 1015 297 -12 87 C ATOM 293 NE2 HIS A 77 47.597 9.952 12.969 1.00 12.25 N ANISOU 293 NE2 HIS A 77 995 2211 1446 148 -81 -66 N ATOM 294 N GLN A 78 44.036 7.921 10.965 1.00 4.94 N ANISOU 294 N GLN A 78 750 332 795 161 247 3 N ATOM 295 CA GLN A 78 42.912 7.371 11.705 1.00 5.78 C ANISOU 295 CA GLN A 78 838 503 853 -109 154 12 C ATOM 296 C GLN A 78 42.114 8.374 12.513 1.00 5.51 C ANISOU 296 C GLN A 78 732 614 745 -118 169 32 C ATOM 297 O GLN A 78 40.982 8.107 12.853 1.00 6.33 O ANISOU 297 O GLN A 78 775 429 1199 -118 293 -12 O ATOM 298 CB GLN A 78 43.390 6.251 12.621 1.00 8.38 C ANISOU 298 CB GLN A 78 1309 859 1014 249 221 194 C ATOM 299 CG GLN A 78 44.283 6.719 13.742 1.00 10.28 C ANISOU 299 CG GLN A 78 1779 1024 1100 408 -215 384 C ATOM 300 CD GLN A 78 45.639 6.295 13.464 1.00 19.00 C ANISOU 300 CD GLN A 78 1815 2084 3319 308 54 351 C ATOM 301 OE1 GLN A 78 46.256 6.815 12.541 1.00 19.22 O ANISOU 301 OE1 GLN A 78 2448 1974 2881 859 126 629 O ATOM 302 NE2 GLN A 78 46.042 5.203 14.098 1.00 20.08 N ANISOU 302 NE2 GLN A 78 2294 2484 2851 440 158 609 N ATOM 303 N PHE A 79 42.679 9.562 12.746 1.00 4.43 N ANISOU 303 N PHE A 79 683 528 470 -12 88 64 N ATOM 304 CA PHE A 79 41.958 10.635 13.442 1.00 4.82 C ANISOU 304 CA PHE A 79 599 639 592 31 99 38 C ATOM 305 C PHE A 79 41.367 11.683 12.498 1.00 4.54 C ANISOU 305 C PHE A 79 614 465 644 -6 67 -34 C ATOM 306 O PHE A 79 40.822 12.694 12.976 1.00 5.19 O ANISOU 306 O PHE A 79 776 491 701 48 230 6 O ATOM 307 CB PHE A 79 42.834 11.322 14.480 1.00 5.23 C ANISOU 307 CB PHE A 79 780 466 738 -7 93 -89 C ATOM 308 CG PHE A 79 43.361 10.441 15.599 1.00 5.38 C ANISOU 308 CG PHE A 79 644 689 709 -13 129 -25 C ATOM 309 CD1 PHE A 79 42.735 9.257 16.019 1.00 5.91 C ANISOU 309 CD1 PHE A 79 893 781 570 -85 86 86 C ATOM 310 CD2 PHE A 79 44.496 10.831 16.260 1.00 6.73 C ANISOU 310 CD2 PHE A 79 1064 722 771 -202 -78 -171 C ATOM 311 CE1 PHE A 79 43.264 8.536 17.068 1.00 7.08 C ANISOU 311 CE1 PHE A 79 1095 952 641 -78 -25 129 C ATOM 312 CE2 PHE A 79 45.024 10.106 17.292 1.00 9.64 C ANISOU 312 CE2 PHE A 79 1299 1234 1130 -200 -292 115 C ATOM 313 CZ PHE A 79 44.428 8.950 17.688 1.00 8.82 C ANISOU 313 CZ PHE A 79 1438 1226 685 -191 -335 171 C ATOM 314 N ALA A 80 41.407 11.448 11.193 1.00 4.07 N ANISOU 314 N ALA A 80 440 498 607 44 108 43 N ATOM 315 CA ALA A 80 41.005 12.481 10.247 1.00 4.83 C ANISOU 315 CA ALA A 80 558 502 773 47 70 117 C ATOM 316 C ALA A 80 39.501 12.681 10.147 1.00 3.86 C ANISOU 316 C ALA A 80 530 390 546 10 120 82 C ATOM 317 O ALA A 80 39.045 13.776 9.808 1.00 3.87 O ANISOU 317 O ALA A 80 519 473 479 71 184 168 O ATOM 318 CB ALA A 80 41.516 12.162 8.852 1.00 6.50 C ANISOU 318 CB ALA A 80 844 843 781 74 159 135 C ATOM 319 N TRP A 81 38.690 11.645 10.340 1.00 3.74 N ANISOU 319 N TRP A 81 464 409 544 19 135 81 N ATOM 320 CA TRP A 81 37.281 11.734 9.917 1.00 3.73 C ANISOU 320 CA TRP A 81 550 399 469 -22 18 55 C ATOM 321 C TRP A 81 36.498 12.899 10.462 1.00 3.86 C ANISOU 321 C TRP A 81 483 424 556 -22 23 46 C ATOM 322 O TRP A 81 35.676 13.444 9.727 1.00 5.15 O ANISOU 322 O TRP A 81 700 647 608 22 -60 186 O ATOM 323 CB TRP A 81 36.545 10.375 10.056 1.00 4.29 C ANISOU 323 CB TRP A 81 575 429 625 -53 -5 109 C ATOM 324 CG TRP A 81 36.302 9.956 11.487 1.00 4.33 C ANISOU 324 CG TRP A 81 706 350 586 -81 69 2 C ATOM 325 CD1 TRP A 81 37.097 9.160 12.268 1.00 5.68 C ANISOU 325 CD1 TRP A 81 775 696 686 84 103 102 C ATOM 326 CD2 TRP A 81 35.213 10.380 12.310 1.00 4.17 C ANISOU 326 CD2 TRP A 81 643 321 620 -69 51 70 C ATOM 327 NE1 TRP A 81 36.557 9.068 13.539 1.00 5.48 N ANISOU 327 NE1 TRP A 81 817 564 699 41 107 313 N ATOM 328 CE2 TRP A 81 35.401 9.786 13.588 1.00 4.49 C ANISOU 328 CE2 TRP A 81 672 381 651 -136 95 146 C ATOM 329 CE3 TRP A 81 34.100 11.209 12.094 1.00 5.01 C ANISOU 329 CE3 TRP A 81 532 700 672 -40 29 193 C ATOM 330 CZ2 TRP A 81 34.520 9.996 14.650 1.00 6.36 C ANISOU 330 CZ2 TRP A 81 849 812 752 39 190 175 C ATOM 331 CZ3 TRP A 81 33.193 11.392 13.146 1.00 6.96 C ANISOU 331 CZ3 TRP A 81 777 947 918 157 247 189 C ATOM 332 CH2 TRP A 81 33.450 10.820 14.429 1.00 7.55 C ANISOU 332 CH2 TRP A 81 825 1053 989 124 263 299 C ATOM 333 N PRO A 82 36.706 13.334 11.733 1.00 3.62 N ANISOU 333 N PRO A 82 445 448 481 -63 59 140 N ATOM 334 CA PRO A 82 35.902 14.471 12.210 1.00 4.75 C ANISOU 334 CA PRO A 82 572 568 665 39 125 123 C ATOM 335 C PRO A 82 36.224 15.794 11.520 1.00 4.16 C ANISOU 335 C PRO A 82 505 538 534 -22 175 22 C ATOM 336 O PRO A 82 35.512 16.772 11.742 1.00 5.23 O ANISOU 336 O PRO A 82 676 530 781 63 312 189 O ATOM 337 CB PRO A 82 36.290 14.592 13.696 1.00 4.51 C ANISOU 337 CB PRO A 82 531 542 638 -11 197 64 C ATOM 338 CG PRO A 82 36.773 13.237 14.066 1.00 4.73 C ANISOU 338 CG PRO A 82 649 563 584 38 -22 -14 C ATOM 339 CD PRO A 82 37.525 12.788 12.834 1.00 3.97 C ANISOU 339 CD PRO A 82 506 451 548 -18 -15 90 C ATOM 340 N PHE A 83 37.322 15.815 10.749 1.00 3.14 N ANISOU 340 N PHE A 83 460 371 362 -7 93 8 N ATOM 341 CA PHE A 83 37.848 17.012 10.085 1.00 3.52 C ANISOU 341 CA PHE A 83 493 436 409 -10 108 78 C ATOM 342 C PHE A 83 37.711 16.941 8.574 1.00 3.14 C ANISOU 342 C PHE A 83 356 382 455 -32 -114 113 C ATOM 343 O PHE A 83 38.177 17.866 7.881 1.00 4.72 O ANISOU 343 O PHE A 83 686 511 593 -103 77 177 O ATOM 344 CB PHE A 83 39.324 17.201 10.469 1.00 4.29 C ANISOU 344 CB PHE A 83 532 500 598 -82 66 -22 C ATOM 345 CG PHE A 83 39.537 17.250 11.952 1.00 4.34 C ANISOU 345 CG PHE A 83 350 653 645 -71 -86 33 C ATOM 346 CD1 PHE A 83 39.389 18.435 12.652 1.00 5.57 C ANISOU 346 CD1 PHE A 83 698 622 794 -124 15 32 C ATOM 347 CD2 PHE A 83 39.868 16.097 12.672 1.00 5.06 C ANISOU 347 CD2 PHE A 83 729 573 617 -168 0 55 C ATOM 348 CE1 PHE A 83 39.577 18.491 13.999 1.00 6.20 C ANISOU 348 CE1 PHE A 83 720 847 787 -93 146 -178 C ATOM 349 CE2 PHE A 83 40.035 16.158 14.053 1.00 6.26 C ANISOU 349 CE2 PHE A 83 834 899 646 -171 -88 107 C ATOM 350 CZ PHE A 83 39.893 17.355 14.685 1.00 5.83 C ANISOU 350 CZ PHE A 83 552 1027 633 -257 151 1 C ATOM 351 N GLN A 84 37.013 15.952 8.050 1.00 3.35 N ANISOU 351 N GLN A 84 530 309 431 -55 8 41 N ATOM 352 CA GLN A 84 36.933 15.767 6.589 1.00 3.42 C ANISOU 352 CA GLN A 84 429 420 450 -91 5 -38 C ATOM 353 C GLN A 84 35.793 16.499 5.927 1.00 4.04 C ANISOU 353 C GLN A 84 510 454 570 50 113 73 C ATOM 354 O GLN A 84 35.619 16.440 4.708 1.00 5.53 O ANISOU 354 O GLN A 84 820 705 576 167 138 55 O ATOM 355 CB GLN A 84 36.852 14.259 6.252 1.00 4.19 C ANISOU 355 CB GLN A 84 572 459 560 -66 67 -146 C ATOM 356 CG GLN A 84 38.195 13.546 6.438 1.00 4.97 C ANISOU 356 CG GLN A 84 688 559 639 15 -6 33 C ATOM 357 CD GLN A 84 38.104 12.058 6.200 1.00 5.44 C ANISOU 357 CD GLN A 84 806 517 743 -4 -22 155 C ATOM 358 OE1 GLN A 84 37.030 11.479 6.333 1.00 7.69 O ANISOU 358 OE1 GLN A 84 840 681 1399 -53 174 -165 O ATOM 359 NE2 GLN A 84 39.218 11.454 5.848 1.00 8.78 N ANISOU 359 NE2 GLN A 84 1001 778 1555 61 215 -134 N ATOM 360 N GLN A 85 34.988 17.194 6.728 1.00 4.05 N ANISOU 360 N GLN A 85 549 469 520 112 22 20 N ATOM 361 CA GLN A 85 33.824 17.930 6.205 1.00 4.41 C ANISOU 361 CA GLN A 85 636 532 507 51 -197 -10 C ATOM 362 C GLN A 85 33.531 19.060 7.184 1.00 3.79 C ANISOU 362 C GLN A 85 457 487 494 -71 0 30 C ATOM 363 O GLN A 85 33.955 18.984 8.340 1.00 3.69 O ANISOU 363 O GLN A 85 484 401 515 26 -32 -6 O ATOM 364 CB GLN A 85 32.584 16.992 6.092 1.00 5.19 C ANISOU 364 CB GLN A 85 662 600 707 33 -213 -128 C ATOM 365 CG GLN A 85 32.155 16.339 7.392 1.00 5.65 C ANISOU 365 CG GLN A 85 622 554 969 -70 -54 -15 C ATOM 366 CD GLN A 85 33.085 15.234 7.844 1.00 5.31 C ANISOU 366 CD GLN A 85 719 530 768 -77 168 170 C ATOM 367 OE1 GLN A 85 33.422 14.373 7.037 1.00 7.69 O ANISOU 367 OE1 GLN A 85 1053 751 1117 1 115 -135 O ATOM 368 NE2 GLN A 85 33.512 15.260 9.097 1.00 6.10 N ANISOU 368 NE2 GLN A 85 780 691 844 61 117 4 N ATOM 369 N PRO A 86 32.723 20.056 6.805 1.00 4.25 N ANISOU 369 N PRO A 86 648 517 449 12 -77 -37 N ATOM 370 CA PRO A 86 32.349 21.083 7.738 1.00 3.87 C ANISOU 370 CA PRO A 86 440 493 537 -47 -82 -79 C ATOM 371 C PRO A 86 31.704 20.534 8.982 1.00 4.14 C ANISOU 371 C PRO A 86 527 457 589 35 -23 -34 C ATOM 372 O PRO A 86 30.959 19.569 8.924 1.00 5.22 O ANISOU 372 O PRO A 86 735 485 761 -69 8 -23 O ATOM 373 CB PRO A 86 31.352 21.934 6.918 1.00 4.88 C ANISOU 373 CB PRO A 86 580 507 765 97 -114 -77 C ATOM 374 CG PRO A 86 31.791 21.771 5.496 1.00 5.95 C ANISOU 374 CG PRO A 86 843 729 688 86 -137 91 C ATOM 375 CD PRO A 86 32.294 20.339 5.422 1.00 5.30 C ANISOU 375 CD PRO A 86 716 745 551 83 -178 75 C ATOM 376 N VAL A 87 31.912 21.187 10.111 1.00 3.96 N ANISOU 376 N VAL A 87 489 439 575 9 73 -40 N ATOM 377 CA VAL A 87 31.222 20.836 11.348 1.00 5.03 C ANISOU 377 CA VAL A 87 643 621 645 39 143 45 C ATOM 378 C VAL A 87 29.734 21.143 11.137 1.00 5.07 C ANISOU 378 C VAL A 87 710 625 589 54 -86 13 C ATOM 379 O VAL A 87 29.368 22.260 10.747 1.00 6.37 O ANISOU 379 O VAL A 87 798 681 940 167 45 93 O ATOM 380 CB VAL A 87 31.755 21.682 12.505 1.00 5.84 C ANISOU 380 CB VAL A 87 790 801 627 227 -1 -25 C ATOM 381 CG1 VAL A 87 30.908 21.509 13.751 1.00 6.85 C ANISOU 381 CG1 VAL A 87 881 950 769 11 82 56 C ATOM 382 CG2 VAL A 87 33.211 21.344 12.790 1.00 6.24 C ANISOU 382 CG2 VAL A 87 781 780 810 98 -79 111 C ATOM 383 N ASP A 88 28.900 20.156 11.373 1.00 6.69 N ANISOU 383 N ASP A 88 741 877 922 -5 124 217 N ATOM 384 CA ASP A 88 27.451 20.294 11.210 1.00 7.66 C ANISOU 384 CA ASP A 88 775 1110 1022 74 94 117 C ATOM 385 C ASP A 88 26.874 20.496 12.610 1.00 7.59 C ANISOU 385 C ASP A 88 933 994 955 -41 77 185 C ATOM 386 O ASP A 88 26.641 19.537 13.359 1.00 8.07 O ANISOU 386 O ASP A 88 916 965 1186 293 310 325 O ATOM 387 CB ASP A 88 26.898 19.061 10.486 1.00 7.86 C ANISOU 387 CB ASP A 88 928 1085 972 205 102 76 C ATOM 388 CG ASP A 88 25.400 19.183 10.205 1.00 8.16 C ANISOU 388 CG ASP A 88 839 1117 1141 86 345 240 C ATOM 389 OD1 ASP A 88 24.724 19.945 10.911 1.00 8.28 O ANISOU 389 OD1 ASP A 88 856 1050 1237 146 435 322 O ATOM 390 OD2 ASP A 88 24.971 18.530 9.280 1.00 12.32 O ANISOU 390 OD2 ASP A 88 920 1990 1771 -35 -49 -88 O ATOM 391 N ALA A 89 26.726 21.744 13.017 1.00 9.35 N ANISOU 391 N ALA A 89 1562 1020 969 -71 250 165 N ATOM 392 CA ALA A 89 26.324 22.062 14.379 1.00 9.46 C ANISOU 392 CA ALA A 89 1533 1255 804 481 -98 267 C ATOM 393 C ALA A 89 24.873 21.662 14.612 1.00 10.84 C ANISOU 393 C ALA A 89 1455 1548 1114 769 187 355 C ATOM 394 O ALA A 89 24.458 21.531 15.768 1.00 16.36 O ANISOU 394 O ALA A 89 2780 2390 1044 820 401 575 O ATOM 395 CB ALA A 89 26.520 23.543 14.605 1.00 12.88 C ANISOU 395 CB ALA A 89 2269 1348 1277 33 160 239 C ATOM 396 N VAL A 90 24.068 21.496 13.555 1.00 9.57 N ANISOU 396 N VAL A 90 1332 1218 1087 463 259 320 N ATOM 397 CA VAL A 90 22.665 21.074 13.691 1.00 10.96 C ANISOU 397 CA VAL A 90 1265 1669 1229 510 185 111 C ATOM 398 C VAL A 90 22.656 19.595 14.003 1.00 12.87 C ANISOU 398 C VAL A 90 1818 1736 1337 397 665 313 C ATOM 399 O VAL A 90 22.087 19.168 15.032 1.00 15.21 O ANISOU 399 O VAL A 90 1393 2708 1676 757 766 922 O ATOM 400 CB VAL A 90 21.805 21.401 12.442 1.00 13.40 C ANISOU 400 CB VAL A 90 1788 2043 1258 414 -50 86 C ATOM 401 CG1 VAL A 90 20.403 20.843 12.583 1.00 14.11 C ANISOU 401 CG1 VAL A 90 1731 2000 1628 575 61 351 C ATOM 402 CG2 VAL A 90 21.798 22.908 12.228 1.00 15.19 C ANISOU 402 CG2 VAL A 90 2101 2017 1651 662 359 -19 C ATOM 403 N LYS A 91 23.351 18.797 13.215 1.00 9.09 N ANISOU 403 N LYS A 91 1131 1304 1019 147 302 376 N ATOM 404 CA LYS A 91 23.387 17.358 13.449 1.00 10.52 C ANISOU 404 CA LYS A 91 1099 1385 1511 -36 0 547 C ATOM 405 C LYS A 91 24.048 17.013 14.783 1.00 9.88 C ANISOU 405 C LYS A 91 1141 1366 1244 2 51 176 C ATOM 406 O LYS A 91 23.610 16.098 15.484 1.00 15.60 O ANISOU 406 O LYS A 91 1841 1842 2244 -74 258 860 O ATOM 407 CB LYS A 91 24.146 16.666 12.323 1.00 14.59 C ANISOU 407 CB LYS A 91 1859 1834 1847 165 298 283 C ATOM 408 CG LYS A 91 24.060 15.161 12.380 1.00 19.53 C ANISOU 408 CG LYS A 91 2553 1962 2903 -69 69 590 C ATOM 409 CD LYS A 91 24.623 14.547 11.114 1.00 24.42 C ANISOU 409 CD LYS A 91 3530 2584 3161 78 138 -18 C ATOM 410 CE LYS A 91 23.662 14.645 9.954 1.00 27.37 C ANISOU 410 CE LYS A 91 3194 3586 3616 768 -64 -61 C ATOM 411 NZ LYS A 91 24.028 13.747 8.820 1.00 33.89 N ANISOU 411 NZ LYS A 91 4531 3956 4389 663 -140 -809 N ATOM 412 N LEU A 92 25.055 17.771 15.143 1.00 9.38 N ANISOU 412 N LEU A 92 1007 1246 1311 25 102 452 N ATOM 413 CA LEU A 92 25.866 17.490 16.316 1.00 9.37 C ANISOU 413 CA LEU A 92 1299 1156 1105 -54 177 698 C ATOM 414 C LEU A 92 25.361 18.191 17.585 1.00 11.94 C ANISOU 414 C LEU A 92 1160 1840 1534 183 202 299 C ATOM 415 O LEU A 92 25.935 18.066 18.665 1.00 15.60 O ANISOU 415 O LEU A 92 1929 2309 1689 -315 -106 706 O ATOM 416 CB LEU A 92 27.337 17.790 16.015 1.00 9.70 C ANISOU 416 CB LEU A 92 1159 1202 1323 168 52 514 C ATOM 417 CG LEU A 92 28.019 17.034 14.850 1.00 9.59 C ANISOU 417 CG LEU A 92 1255 1116 1273 227 -52 464 C ATOM 418 CD1 LEU A 92 29.463 17.460 14.693 1.00 11.53 C ANISOU 418 CD1 LEU A 92 1460 1299 1619 11 269 223 C ATOM 419 CD2 LEU A 92 27.924 15.530 15.018 1.00 9.60 C ANISOU 419 CD2 LEU A 92 1306 1073 1269 109 -97 30 C ATOM 420 N ASN A 93 24.262 18.931 17.446 1.00 11.30 N ANISOU 420 N ASN A 93 1330 1411 1550 140 129 590 N ATOM 421 CA ASN A 93 23.665 19.657 18.550 1.00 12.88 C ANISOU 421 CA ASN A 93 1996 1597 1300 6 163 476 C ATOM 422 C ASN A 93 24.657 20.550 19.287 1.00 14.97 C ANISOU 422 C ASN A 93 2038 2021 1628 -282 -16 631 C ATOM 423 O ASN A 93 24.873 20.438 20.491 1.00 14.22 O ANISOU 423 O ASN A 93 2039 1993 1368 -376 244 247 O ATOM 424 CB ASN A 93 22.956 18.662 19.482 1.00 15.36 C ANISOU 424 CB ASN A 93 2130 1692 2013 -335 284 552 C ATOM 425 CG ASN A 93 22.160 19.337 20.574 1.00 21.50 C ANISOU 425 CG ASN A 93 3045 2669 2454 -176 844 325 C ATOM 426 OD1 ASN A 93 21.674 20.441 20.419 1.00 27.10 O ANISOU 426 OD1 ASN A 93 2743 3515 4039 619 596 472 O ATOM 427 ND2 ASN A 93 22.054 18.667 21.705 1.00 29.16 N ANISOU 427 ND2 ASN A 93 4455 3771 2851 -1068 1703 788 N ATOM 428 N LEU A 94 25.265 21.461 18.534 1.00 11.58 N ANISOU 428 N LEU A 94 1614 1596 1189 440 253 544 N ATOM 429 CA LEU A 94 26.178 22.461 19.053 1.00 12.90 C ANISOU 429 CA LEU A 94 1678 1897 1326 320 284 501 C ATOM 430 C LEU A 94 25.586 23.842 18.737 1.00 14.02 C ANISOU 430 C LEU A 94 1786 1681 1859 269 505 450 C ATOM 431 O LEU A 94 26.073 24.554 17.853 1.00 11.51 O ANISOU 431 O LEU A 94 982 1696 1695 464 435 404 O ATOM 432 CB LEU A 94 27.548 22.315 18.369 1.00 11.97 C ANISOU 432 CB LEU A 94 1323 1807 1418 305 -58 151 C ATOM 433 CG LEU A 94 28.130 20.901 18.317 1.00 11.65 C ANISOU 433 CG LEU A 94 1442 1667 1315 146 -4 123 C ATOM 434 CD1 LEU A 94 29.423 20.890 17.484 1.00 11.49 C ANISOU 434 CD1 LEU A 94 1268 1541 1557 207 -86 250 C ATOM 435 CD2 LEU A 94 28.376 20.380 19.734 1.00 13.36 C ANISOU 435 CD2 LEU A 94 1743 1842 1488 -206 -8 458 C ATOM 436 N PRO A 95 24.545 24.263 19.472 1.00 12.66 N ANISOU 436 N PRO A 95 1206 1925 1677 373 127 807 N ATOM 437 CA PRO A 95 23.912 25.532 19.105 1.00 12.75 C ANISOU 437 CA PRO A 95 1081 1806 1955 490 391 557 C ATOM 438 C PRO A 95 24.743 26.825 19.210 1.00 14.52 C ANISOU 438 C PRO A 95 1310 1991 2212 357 521 453 C ATOM 439 O PRO A 95 24.393 27.824 18.579 1.00 17.94 O ANISOU 439 O PRO A 95 1842 2362 2610 467 359 832 O ATOM 440 CB PRO A 95 22.697 25.605 20.073 1.00 15.31 C ANISOU 440 CB PRO A 95 1362 2283 2169 106 645 139 C ATOM 441 CG PRO A 95 23.009 24.637 21.160 1.00 17.55 C ANISOU 441 CG PRO A 95 2066 2330 2272 387 635 166 C ATOM 442 CD PRO A 95 23.787 23.547 20.517 1.00 14.23 C ANISOU 442 CD PRO A 95 1901 1796 1707 -33 570 295 C ATOM 443 N ASP A 96 25.854 26.800 19.950 1.00 11.91 N ANISOU 443 N ASP A 96 1148 1776 1599 355 795 324 N ATOM 444 CA ASP A 96 26.709 27.945 20.184 1.00 12.19 C ANISOU 444 CA ASP A 96 1345 1724 1561 446 433 -57 C ATOM 445 C ASP A 96 27.961 27.969 19.248 1.00 10.08 C ANISOU 445 C ASP A 96 1128 1485 1213 372 157 160 C ATOM 446 O ASP A 96 28.791 28.826 19.375 1.00 10.84 O ANISOU 446 O ASP A 96 1447 1500 1171 326 468 197 O ATOM 447 CB ASP A 96 27.178 27.988 21.652 1.00 16.20 C ANISOU 447 CB ASP A 96 2119 2551 1482 80 490 279 C ATOM 448 CG ASP A 96 27.814 26.652 22.124 1.00 18.79 C ANISOU 448 CG ASP A 96 2267 2224 2647 -6 842 381 C ATOM 449 OD1 ASP A 96 27.682 25.606 21.426 1.00 18.33 O ANISOU 449 OD1 ASP A 96 1825 3074 2062 569 -265 -67 O ATOM 450 OD2 ASP A 96 28.452 26.647 23.201 1.00 31.43 O ANISOU 450 OD2 ASP A 96 5376 3401 3165 77 -362 267 O ATOM 451 N TYR A 97 28.061 26.997 18.367 1.00 8.99 N ANISOU 451 N TYR A 97 842 1611 963 441 355 299 N ATOM 452 CA TYR A 97 29.302 26.817 17.588 1.00 6.79 C ANISOU 452 CA TYR A 97 519 1139 919 165 122 162 C ATOM 453 C TYR A 97 29.713 28.075 16.788 1.00 7.53 C ANISOU 453 C TYR A 97 916 1143 802 136 -91 256 C ATOM 454 O TYR A 97 30.832 28.557 16.901 1.00 7.75 O ANISOU 454 O TYR A 97 812 1128 1005 197 208 341 O ATOM 455 CB TYR A 97 29.181 25.579 16.714 1.00 6.11 C ANISOU 455 CB TYR A 97 479 1046 796 85 104 246 C ATOM 456 CG TYR A 97 30.480 25.230 16.008 1.00 5.31 C ANISOU 456 CG TYR A 97 418 963 637 -23 53 225 C ATOM 457 CD1 TYR A 97 31.484 24.548 16.663 1.00 5.32 C ANISOU 457 CD1 TYR A 97 579 917 523 33 -84 57 C ATOM 458 CD2 TYR A 97 30.707 25.616 14.678 1.00 5.67 C ANISOU 458 CD2 TYR A 97 581 1031 539 -28 -19 111 C ATOM 459 CE1 TYR A 97 32.689 24.243 16.030 1.00 4.91 C ANISOU 459 CE1 TYR A 97 513 807 543 121 -129 171 C ATOM 460 CE2 TYR A 97 31.893 25.292 14.029 1.00 5.07 C ANISOU 460 CE2 TYR A 97 623 759 545 41 -18 110 C ATOM 461 CZ TYR A 97 32.904 24.659 14.725 1.00 4.47 C ANISOU 461 CZ TYR A 97 462 654 580 25 69 46 C ATOM 462 OH TYR A 97 34.094 24.450 14.073 1.00 3.99 O ANISOU 462 OH TYR A 97 446 549 518 52 33 105 O ATOM 463 N TYR A 98 28.753 28.712 16.117 1.00 8.15 N ANISOU 463 N TYR A 98 775 1031 1292 299 27 241 N ATOM 464 CA TYR A 98 29.028 29.900 15.291 1.00 9.07 C ANISOU 464 CA TYR A 98 1212 1309 922 59 297 217 C ATOM 465 C TYR A 98 29.065 31.237 16.064 1.00 9.88 C ANISOU 465 C TYR A 98 1360 1281 1113 -34 320 210 C ATOM 466 O TYR A 98 29.330 32.259 15.460 1.00 9.41 O ANISOU 466 O TYR A 98 1437 979 1160 -27 46 37 O ATOM 467 CB TYR A 98 28.079 29.975 14.071 1.00 10.12 C ANISOU 467 CB TYR A 98 1092 1558 1195 82 237 -67 C ATOM 468 CG TYR A 98 28.169 28.712 13.276 1.00 7.52 C ANISOU 468 CG TYR A 98 897 1197 760 -58 -203 224 C ATOM 469 CD1 TYR A 98 29.343 28.448 12.474 1.00 7.77 C ANISOU 469 CD1 TYR A 98 1017 1309 623 55 -248 40 C ATOM 470 CD2 TYR A 98 27.169 27.771 13.313 1.00 8.60 C ANISOU 470 CD2 TYR A 98 1232 1063 972 -113 -50 59 C ATOM 471 CE1 TYR A 98 29.472 27.289 11.788 1.00 6.71 C ANISOU 471 CE1 TYR A 98 938 897 711 -62 -344 330 C ATOM 472 CE2 TYR A 98 27.298 26.581 12.615 1.00 7.37 C ANISOU 472 CE2 TYR A 98 1050 931 819 -151 -168 129 C ATOM 473 CZ TYR A 98 28.386 26.341 11.879 1.00 7.40 C ANISOU 473 CZ TYR A 98 935 981 894 -91 -262 -6 C ATOM 474 OH TYR A 98 28.459 25.187 11.178 1.00 8.71 O ANISOU 474 OH TYR A 98 1231 747 1330 270 -126 15 O ATOM 475 N LYS A 99 28.743 31.245 17.364 1.00 8.54 N ANISOU 475 N LYS A 99 1211 1020 1012 42 119 177 N ATOM 476 CA LYS A 99 29.014 32.388 18.212 1.00 9.23 C ANISOU 476 CA LYS A 99 1400 1181 924 387 -60 99 C ATOM 477 C LYS A 99 30.445 32.679 18.417 1.00 8.10 C ANISOU 477 C LYS A 99 1398 907 771 233 151 -92 C ATOM 478 O LYS A 99 30.852 33.831 18.580 1.00 10.99 O ANISOU 478 O LYS A 99 1718 1058 1398 90 -53 -177 O ATOM 479 CB LYS A 99 28.236 32.248 19.516 1.00 9.97 C ANISOU 479 CB LYS A 99 1491 1309 987 158 33 -93 C ATOM 480 CG LYS A 99 26.718 32.075 19.322 1.00 14.41 C ANISOU 480 CG LYS A 99 1569 2236 1668 -133 -143 107 C ATOM 481 CD LYS A 99 25.915 31.968 20.619 1.00 21.32 C ANISOU 481 CD LYS A 99 2615 3209 2274 374 676 -392 C ATOM 482 CE LYS A 99 24.419 32.003 20.344 1.00 30.63 C ANISOU 482 CE LYS A 99 2781 4482 4372 -1195 -43 -62 C ATOM 483 NZ LYS A 99 23.945 30.716 19.762 1.00 33.92 N ANISOU 483 NZ LYS A 99 4480 3723 4683 506 118 -848 N ATOM 484 N ILE A 100 31.301 31.629 18.356 1.00 7.85 N ANISOU 484 N ILE A 100 1067 1009 904 188 19 45 N ATOM 485 CA ILE A 100 32.756 31.798 18.478 1.00 7.52 C ANISOU 485 CA ILE A 100 1121 976 757 222 -68 -154 C ATOM 486 C ILE A 100 33.452 31.423 17.180 1.00 5.23 C ANISOU 486 C ILE A 100 744 629 613 253 -162 117 C ATOM 487 O ILE A 100 34.487 32.025 16.888 1.00 7.91 O ANISOU 487 O ILE A 100 1100 853 1051 -50 -56 -205 O ATOM 488 CB ILE A 100 33.284 31.037 19.705 1.00 6.28 C ANISOU 488 CB ILE A 100 950 652 782 -67 49 -32 C ATOM 489 CG1 ILE A 100 34.733 31.409 20.035 1.00 7.47 C ANISOU 489 CG1 ILE A 100 879 933 1026 137 -76 -41 C ATOM 490 CG2 ILE A 100 33.254 29.535 19.606 1.00 5.51 C ANISOU 490 CG2 ILE A 100 742 655 696 -11 -90 -86 C ATOM 491 CD1 ILE A 100 34.953 32.889 20.376 1.00 9.40 C ANISOU 491 CD1 ILE A 100 1158 1002 1409 111 -180 -195 C ATOM 492 N ILE A 101 32.909 30.437 16.388 1.00 5.97 N ANISOU 492 N ILE A 101 764 902 601 253 -108 -18 N ATOM 493 CA ILE A 101 33.578 30.025 15.115 1.00 4.66 C ANISOU 493 CA ILE A 101 632 581 556 32 -107 -28 C ATOM 494 C ILE A 101 33.017 30.853 13.961 1.00 4.42 C ANISOU 494 C ILE A 101 591 534 552 170 14 -50 C ATOM 495 O ILE A 101 32.024 30.486 13.327 1.00 6.70 O ANISOU 495 O ILE A 101 781 784 979 -35 -245 175 O ATOM 496 CB ILE A 101 33.511 28.518 14.848 1.00 3.80 C ANISOU 496 CB ILE A 101 468 531 442 36 44 90 C ATOM 497 CG1 ILE A 101 34.106 27.682 16.000 1.00 3.81 C ANISOU 497 CG1 ILE A 101 533 480 434 50 -41 3 C ATOM 498 CG2 ILE A 101 34.247 28.213 13.524 1.00 4.01 C ANISOU 498 CG2 ILE A 101 490 574 458 -2 40 36 C ATOM 499 CD1 ILE A 101 35.462 28.166 16.450 1.00 3.96 C ANISOU 499 CD1 ILE A 101 472 566 466 55 19 10 C ATOM 500 N LYS A 102 33.663 31.972 13.735 1.00 4.71 N ANISOU 500 N LYS A 102 565 668 556 130 -26 114 N ATOM 501 CA LYS A 102 33.294 32.880 12.643 1.00 5.29 C ANISOU 501 CA LYS A 102 714 752 545 116 -101 135 C ATOM 502 C LYS A 102 34.063 32.622 11.366 1.00 5.16 C ANISOU 502 C LYS A 102 653 618 689 101 2 165 C ATOM 503 O LYS A 102 33.690 33.144 10.340 1.00 6.65 O ANISOU 503 O LYS A 102 888 855 783 368 40 293 O ATOM 504 CB LYS A 102 33.441 34.330 13.075 1.00 6.87 C ANISOU 504 CB LYS A 102 971 711 928 361 -180 101 C ATOM 505 CG LYS A 102 32.704 34.743 14.311 1.00 9.06 C ANISOU 505 CG LYS A 102 1306 1112 1021 336 -34 52 C ATOM 506 CD LYS A 102 31.252 34.572 14.178 1.00 9.84 C ANISOU 506 CD LYS A 102 1241 1484 1012 452 95 262 C ATOM 507 CE LYS A 102 30.552 35.312 15.297 1.00 10.50 C ANISOU 507 CE LYS A 102 1643 1208 1137 315 120 79 C ATOM 508 NZ LYS A 102 29.100 35.017 15.276 1.00 10.89 N ANISOU 508 NZ LYS A 102 1727 1451 956 82 -51 -95 N ATOM 509 N THR A 103 35.081 31.755 11.390 1.00 4.46 N ANISOU 509 N THR A 103 656 450 586 39 -18 11 N ATOM 510 CA THR A 103 35.846 31.368 10.208 1.00 4.93 C ANISOU 510 CA THR A 103 641 557 675 102 67 84 C ATOM 511 C THR A 103 35.925 29.841 10.146 1.00 3.43 C ANISOU 511 C THR A 103 407 539 355 53 -26 152 C ATOM 512 O THR A 103 36.987 29.230 10.395 1.00 3.62 O ANISOU 512 O THR A 103 426 512 437 49 -84 163 O ATOM 513 CB THR A 103 37.277 31.982 10.174 1.00 7.28 C ANISOU 513 CB THR A 103 836 729 1199 -150 214 214 C ATOM 514 OG1 THR A 103 37.195 33.385 10.466 1.00 12.12 O ANISOU 514 OG1 THR A 103 1603 916 2085 -156 144 -275 O ATOM 515 CG2 THR A 103 37.854 31.821 8.812 1.00 9.18 C ANISOU 515 CG2 THR A 103 1301 1118 1070 30 99 296 C ATOM 516 N PRO A 104 34.805 29.170 9.845 1.00 3.67 N ANISOU 516 N PRO A 104 443 437 512 110 -118 42 N ATOM 517 CA PRO A 104 34.837 27.713 9.754 1.00 3.91 C ANISOU 517 CA PRO A 104 507 443 533 28 1 25 C ATOM 518 C PRO A 104 35.790 27.209 8.693 1.00 3.19 C ANISOU 518 C PRO A 104 329 456 424 -10 -113 36 C ATOM 519 O PRO A 104 35.984 27.838 7.660 1.00 3.93 O ANISOU 519 O PRO A 104 500 503 491 87 -44 107 O ATOM 520 CB PRO A 104 33.399 27.349 9.394 1.00 5.25 C ANISOU 520 CB PRO A 104 525 683 787 -76 84 -208 C ATOM 521 CG PRO A 104 32.599 28.574 9.514 1.00 6.46 C ANISOU 521 CG PRO A 104 687 711 1053 53 -130 40 C ATOM 522 CD PRO A 104 33.474 29.736 9.538 1.00 4.80 C ANISOU 522 CD PRO A 104 445 601 776 204 -45 23 C ATOM 523 N MET A 105 36.417 26.061 8.959 1.00 3.01 N ANISOU 523 N MET A 105 420 385 336 3 48 12 N ATOM 524 CA MET A 105 37.286 25.446 7.961 1.00 3.11 C ANISOU 524 CA MET A 105 365 412 405 15 16 -45 C ATOM 525 C MET A 105 37.389 23.978 8.254 1.00 3.15 C ANISOU 525 C MET A 105 331 429 436 51 31 -3 C ATOM 526 O MET A 105 37.298 23.572 9.420 1.00 4.60 O ANISOU 526 O MET A 105 822 462 461 24 73 29 O ATOM 527 CB MET A 105 38.666 26.124 7.955 1.00 3.47 C ANISOU 527 CB MET A 105 401 446 471 -25 -10 63 C ATOM 528 CG MET A 105 39.596 25.719 6.827 1.00 4.89 C ANISOU 528 CG MET A 105 559 653 642 3 117 -23 C ATOM 529 SD MET A 105 38.893 25.760 5.166 1.00 5.13 S ANISOU 529 SD MET A 105 658 694 595 -43 150 33 S ATOM 530 CE MET A 105 38.322 27.464 5.039 1.00 5.54 C ANISOU 530 CE MET A 105 687 690 726 -50 75 33 C ATOM 531 N ASP A 106 37.658 23.172 7.226 1.00 3.46 N ANISOU 531 N ASP A 106 535 387 390 -23 90 28 N ATOM 532 CA ASP A 106 37.787 21.721 7.366 1.00 3.57 C ANISOU 532 CA ASP A 106 543 402 411 10 61 52 C ATOM 533 C ASP A 106 38.619 21.211 6.202 1.00 3.39 C ANISOU 533 C ASP A 106 458 404 424 15 74 103 C ATOM 534 O ASP A 106 38.836 21.914 5.210 1.00 3.08 O ANISOU 534 O ASP A 106 421 370 377 -6 71 60 O ATOM 535 CB ASP A 106 36.407 21.063 7.311 1.00 4.11 C ANISOU 535 CB ASP A 106 546 475 538 -9 167 74 C ATOM 536 CG ASP A 106 35.735 21.300 5.959 1.00 4.31 C ANISOU 536 CG ASP A 106 431 589 616 -8 107 55 C ATOM 537 OD1 ASP A 106 35.215 22.434 5.683 1.00 5.09 O ANISOU 537 OD1 ASP A 106 616 627 687 51 117 92 O ATOM 538 OD2 ASP A 106 35.820 20.402 5.094 1.00 5.83 O ANISOU 538 OD2 ASP A 106 831 648 733 -16 224 -12 O ATOM 539 N MET A 107 39.070 19.964 6.288 1.00 3.17 N ANISOU 539 N MET A 107 421 370 414 -8 138 35 N ATOM 540 CA MET A 107 39.939 19.410 5.249 1.00 3.26 C ANISOU 540 CA MET A 107 419 381 436 -16 133 0 C ATOM 541 C MET A 107 39.231 19.109 3.959 1.00 3.21 C ANISOU 541 C MET A 107 454 288 475 59 76 13 C ATOM 542 O MET A 107 39.878 19.088 2.894 1.00 3.56 O ANISOU 542 O MET A 107 496 371 486 -82 108 61 O ATOM 543 CB MET A 107 40.659 18.148 5.709 1.00 4.69 C ANISOU 543 CB MET A 107 613 515 651 40 62 149 C ATOM 544 CG MET A 107 41.623 18.366 6.849 1.00 5.33 C ANISOU 544 CG MET A 107 670 635 719 2 21 91 C ATOM 545 SD MET A 107 42.907 17.128 7.030 1.00 7.99 S ANISOU 545 SD MET A 107 991 786 1255 199 -92 237 S ATOM 546 CE MET A 107 41.870 15.795 7.501 1.00 7.36 C ANISOU 546 CE MET A 107 925 732 1138 144 -2 -48 C ATOM 547 N GLY A 108 37.936 18.838 3.998 1.00 3.56 N ANISOU 547 N GLY A 108 508 327 515 -82 -12 115 N ATOM 548 CA GLY A 108 37.209 18.655 2.739 1.00 3.64 C ANISOU 548 CA GLY A 108 454 398 530 -70 23 -22 C ATOM 549 C GLY A 108 37.252 19.910 1.879 1.00 3.38 C ANISOU 549 C GLY A 108 379 428 476 37 26 -14 C ATOM 550 O GLY A 108 37.501 19.848 0.671 1.00 4.76 O ANISOU 550 O GLY A 108 777 568 462 -97 50 24 O ATOM 551 N THR A 109 37.055 21.052 2.523 1.00 3.43 N ANISOU 551 N THR A 109 492 394 416 -3 20 10 N ATOM 552 CA THR A 109 37.126 22.332 1.875 1.00 3.37 C ANISOU 552 CA THR A 109 405 483 389 39 8 95 C ATOM 553 C THR A 109 38.549 22.574 1.350 1.00 2.89 C ANISOU 553 C THR A 109 387 346 364 94 12 59 C ATOM 554 O THR A 109 38.722 23.012 0.199 1.00 3.49 O ANISOU 554 O THR A 109 448 485 392 -73 47 90 O ATOM 555 CB THR A 109 36.728 23.425 2.856 1.00 3.77 C ANISOU 555 CB THR A 109 487 465 480 -9 -5 31 C ATOM 556 OG1 THR A 109 35.337 23.283 3.169 1.00 5.13 O ANISOU 556 OG1 THR A 109 538 613 795 -38 121 122 O ATOM 557 CG2 THR A 109 36.983 24.803 2.316 1.00 4.17 C ANISOU 557 CG2 THR A 109 558 447 579 85 28 59 C ATOM 558 N ILE A 110 39.577 22.300 2.164 1.00 2.72 N ANISOU 558 N ILE A 110 352 342 340 -17 -6 20 N ATOM 559 CA ILE A 110 40.962 22.526 1.739 1.00 2.84 C ANISOU 559 CA ILE A 110 361 353 363 -65 -18 2 C ATOM 560 C ILE A 110 41.283 21.646 0.532 1.00 2.92 C ANISOU 560 C ILE A 110 331 369 406 31 70 28 C ATOM 561 O ILE A 110 41.900 22.129 -0.442 1.00 3.63 O ANISOU 561 O ILE A 110 475 555 348 9 83 49 O ATOM 562 CB ILE A 110 41.936 22.241 2.908 1.00 3.07 C ANISOU 562 CB ILE A 110 451 354 358 -18 -36 17 C ATOM 563 CG1 ILE A 110 41.726 23.247 4.023 1.00 3.05 C ANISOU 563 CG1 ILE A 110 374 395 388 -62 62 -4 C ATOM 564 CG2 ILE A 110 43.384 22.274 2.418 1.00 4.46 C ANISOU 564 CG2 ILE A 110 471 636 586 79 24 -3 C ATOM 565 CD1 ILE A 110 42.450 22.927 5.341 1.00 3.95 C ANISOU 565 CD1 ILE A 110 534 485 480 -62 -33 46 C ATOM 566 N LYS A 111 40.884 20.376 0.578 1.00 3.20 N ANISOU 566 N LYS A 111 385 382 447 0 82 30 N ATOM 567 CA LYS A 111 41.126 19.464 -0.532 1.00 4.17 C ANISOU 567 CA LYS A 111 510 596 475 141 69 -45 C ATOM 568 C LYS A 111 40.519 20.022 -1.841 1.00 3.87 C ANISOU 568 C LYS A 111 468 520 480 -40 14 -40 C ATOM 569 O LYS A 111 41.183 20.063 -2.885 1.00 5.22 O ANISOU 569 O LYS A 111 750 697 535 -10 154 -84 O ATOM 570 CB LYS A 111 40.556 18.109 -0.168 1.00 4.82 C ANISOU 570 CB LYS A 111 657 681 493 47 97 -15 C ATOM 571 CG LYS A 111 40.730 17.026 -1.205 1.00 6.76 C ANISOU 571 CG LYS A 111 998 867 703 -34 136 -215 C ATOM 572 CD LYS A 111 40.276 15.683 -0.637 1.00 9.32 C ANISOU 572 CD LYS A 111 1306 951 1283 -221 53 -72 C ATOM 573 CE LYS A 111 40.585 14.486 -1.494 1.00 15.25 C ANISOU 573 CE LYS A 111 2180 1479 2134 -34 370 -558 C ATOM 574 NZ LYS A 111 39.780 14.544 -2.724 1.00 19.91 N ANISOU 574 NZ LYS A 111 3021 2238 2305 -677 -77 -38 N ATOM 575 N LYS A 112 39.255 20.423 -1.777 1.00 4.29 N ANISOU 575 N LYS A 112 508 594 528 30 39 -35 N ATOM 576 CA LYS A 112 38.575 20.972 -2.940 1.00 4.72 C ANISOU 576 CA LYS A 112 695 565 531 -14 -50 -64 C ATOM 577 C LYS A 112 39.248 22.244 -3.404 1.00 4.67 C ANISOU 577 C LYS A 112 577 645 552 -4 91 -54 C ATOM 578 O LYS A 112 39.401 22.444 -4.619 1.00 5.68 O ANISOU 578 O LYS A 112 880 743 535 -131 33 12 O ATOM 579 CB LYS A 112 37.104 21.195 -2.658 1.00 6.05 C ANISOU 579 CB LYS A 112 724 813 759 99 -54 53 C ATOM 580 CG LYS A 112 36.288 19.901 -2.613 1.00 9.00 C ANISOU 580 CG LYS A 112 1292 935 1190 -160 -208 64 C ATOM 581 CD LYS A 112 34.902 20.208 -2.114 1.00 14.56 C ANISOU 581 CD LYS A 112 1411 2175 1946 -140 0 0 C ATOM 582 CE LYS A 112 34.110 18.966 -1.828 1.00 19.96 C ANISOU 582 CE LYS A 112 2368 2166 3049 -475 -472 74 C ATOM 583 NZ LYS A 112 32.817 19.372 -1.229 1.00 27.14 N ANISOU 583 NZ LYS A 112 2594 3966 3751 -201 -86 -26 N ATOM 584 N ARG A 113 39.651 23.123 -2.497 1.00 3.93 N ANISOU 584 N ARG A 113 500 506 487 3 115 38 N ATOM 585 CA ARG A 113 40.349 24.338 -2.895 1.00 4.33 C ANISOU 585 CA ARG A 113 615 467 563 -30 34 26 C ATOM 586 C ARG A 113 41.622 24.022 -3.674 1.00 4.46 C ANISOU 586 C ARG A 113 531 603 559 -71 -2 80 C ATOM 587 O ARG A 113 41.888 24.631 -4.713 1.00 5.46 O ANISOU 587 O ARG A 113 689 890 493 -21 83 98 O ATOM 588 CB ARG A 113 40.625 25.186 -1.679 1.00 3.71 C ANISOU 588 CB ARG A 113 513 446 448 -26 91 93 C ATOM 589 CG ARG A 113 39.390 25.899 -1.147 1.00 3.67 C ANISOU 589 CG ARG A 113 487 464 441 -29 62 78 C ATOM 590 CD ARG A 113 39.626 26.729 0.087 1.00 4.03 C ANISOU 590 CD ARG A 113 553 452 526 2 91 5 C ATOM 591 NE ARG A 113 38.442 27.525 0.359 1.00 3.68 N ANISOU 591 NE ARG A 113 440 402 556 -62 11 -10 N ATOM 592 CZ ARG A 113 38.416 28.646 1.085 1.00 3.88 C ANISOU 592 CZ ARG A 113 503 536 434 -13 57 -68 C ATOM 593 NH1 ARG A 113 39.442 29.039 1.822 1.00 4.81 N ANISOU 593 NH1 ARG A 113 568 699 557 -40 -39 -23 N ATOM 594 NH2 ARG A 113 37.299 29.328 1.112 1.00 5.31 N ANISOU 594 NH2 ARG A 113 551 564 899 40 -22 -80 N ATOM 595 N LEU A 114 42.406 23.072 -3.185 1.00 4.16 N ANISOU 595 N LEU A 114 493 556 530 -16 64 -35 N ATOM 596 CA LEU A 114 43.626 22.652 -3.890 1.00 4.59 C ANISOU 596 CA LEU A 114 505 652 584 -34 93 -85 C ATOM 597 C LEU A 114 43.290 22.098 -5.247 1.00 5.39 C ANISOU 597 C LEU A 114 707 745 594 -123 54 -87 C ATOM 598 O LEU A 114 43.939 22.437 -6.253 1.00 6.74 O ANISOU 598 O LEU A 114 754 1117 690 -222 170 -112 O ATOM 599 CB LEU A 114 44.446 21.672 -3.111 1.00 4.80 C ANISOU 599 CB LEU A 114 568 706 546 -5 117 -30 C ATOM 600 CG LEU A 114 45.178 22.276 -1.874 1.00 4.85 C ANISOU 600 CG LEU A 114 512 660 671 -21 38 -1 C ATOM 601 CD1 LEU A 114 45.489 21.225 -0.820 1.00 5.10 C ANISOU 601 CD1 LEU A 114 633 650 653 71 58 -35 C ATOM 602 CD2 LEU A 114 46.414 23.041 -2.284 1.00 4.72 C ANISOU 602 CD2 LEU A 114 450 684 659 -1 -2 -21 C ATOM 603 N GLU A 115 42.292 21.226 -5.300 1.00 5.52 N ANISOU 603 N GLU A 115 595 939 563 -152 169 -208 N ATOM 604 CA GLU A 115 41.927 20.584 -6.561 1.00 6.16 C ANISOU 604 CA GLU A 115 809 789 742 39 -45 -305 C ATOM 605 C GLU A 115 41.396 21.558 -7.603 1.00 6.71 C ANISOU 605 C GLU A 115 886 872 789 -41 -23 -157 C ATOM 606 O GLU A 115 41.555 21.340 -8.824 1.00 9.84 O ANISOU 606 O GLU A 115 1542 1406 790 28 -51 -316 O ATOM 607 CB GLU A 115 40.884 19.497 -6.320 1.00 7.83 C ANISOU 607 CB GLU A 115 1160 1126 689 -184 150 -109 C ATOM 608 CG GLU A 115 41.428 18.297 -5.578 1.00 9.02 C ANISOU 608 CG GLU A 115 1373 1093 958 -137 64 -120 C ATOM 609 CD GLU A 115 40.351 17.398 -4.984 1.00 13.26 C ANISOU 609 CD GLU A 115 1740 1734 1560 -385 423 17 C ATOM 610 OE1 GLU A 115 39.151 17.787 -4.889 1.00 14.22 O ANISOU 610 OE1 GLU A 115 1853 1538 2008 -319 220 -108 O ATOM 611 OE2 GLU A 115 40.752 16.285 -4.625 1.00 18.40 O ANISOU 611 OE2 GLU A 115 3207 1546 2236 -232 -1 -199 O ATOM 612 N ASN A 116 40.784 22.652 -7.167 1.00 6.20 N ANISOU 612 N ASN A 116 811 808 735 -134 -17 -131 N ATOM 613 CA ASN A 116 40.207 23.658 -8.056 1.00 6.68 C ANISOU 613 CA ASN A 116 802 994 740 -126 -76 -69 C ATOM 614 C ASN A 116 41.076 24.903 -8.235 1.00 7.30 C ANISOU 614 C ASN A 116 884 967 919 -86 17 50 C ATOM 615 O ASN A 116 40.590 25.922 -8.732 1.00 7.91 O ANISOU 615 O ASN A 116 1164 1093 749 -305 -181 258 O ATOM 616 CB ASN A 116 38.850 24.066 -7.528 1.00 7.58 C ANISOU 616 CB ASN A 116 925 1094 861 19 58 35 C ATOM 617 CG ASN A 116 37.822 22.989 -7.645 1.00 10.55 C ANISOU 617 CG ASN A 116 1031 1678 1299 -275 -185 -163 C ATOM 618 OD1 ASN A 116 37.568 22.474 -8.729 1.00 17.14 O ANISOU 618 OD1 ASN A 116 2263 2299 1950 -1052 247 -971 O ATOM 619 ND2 ASN A 116 37.140 22.748 -6.566 1.00 13.08 N ANISOU 619 ND2 ASN A 116 1427 2069 1472 -1047 -287 181 N ATOM 620 N ASN A 117 42.337 24.826 -7.795 1.00 6.50 N ANISOU 620 N ASN A 117 912 1100 455 -181 47 21 N ATOM 621 CA ASN A 117 43.277 25.971 -7.976 1.00 7.25 C ANISOU 621 CA ASN A 117 840 1143 771 -155 73 140 C ATOM 622 C ASN A 117 42.765 27.234 -7.356 1.00 7.01 C ANISOU 622 C ASN A 117 880 949 834 -317 28 116 C ATOM 623 O ASN A 117 42.978 28.343 -7.830 1.00 9.19 O ANISOU 623 O ASN A 117 1301 1289 898 -533 -178 473 O ATOM 624 CB ASN A 117 43.557 26.192 -9.481 1.00 9.85 C ANISOU 624 CB ASN A 117 1267 1596 879 -459 236 313 C ATOM 625 CG ASN A 117 43.928 24.915 -10.184 1.00 12.67 C ANISOU 625 CG ASN A 117 1676 2145 990 22 356 19 C ATOM 626 OD1 ASN A 117 43.181 24.459 -11.056 1.00 20.06 O ANISOU 626 OD1 ASN A 117 2797 3406 1417 -812 39 -337 O ATOM 627 ND2 ASN A 117 45.017 24.302 -9.806 1.00 12.95 N ANISOU 627 ND2 ASN A 117 1756 2080 1084 -73 45 -368 N ATOM 628 N TYR A 118 42.083 27.112 -6.217 1.00 5.84 N ANISOU 628 N TYR A 118 752 820 647 -139 -96 150 N ATOM 629 CA TYR A 118 41.548 28.258 -5.511 1.00 5.29 C ANISOU 629 CA TYR A 118 568 763 676 -137 -46 219 C ATOM 630 C TYR A 118 42.663 29.069 -4.859 1.00 5.43 C ANISOU 630 C TYR A 118 615 765 682 -10 -125 45 C ATOM 631 O TYR A 118 42.526 30.273 -4.670 1.00 7.72 O ANISOU 631 O TYR A 118 834 693 1405 -140 -519 154 O ATOM 632 CB TYR A 118 40.551 27.753 -4.442 1.00 4.82 C ANISOU 632 CB TYR A 118 509 717 603 -166 -65 81 C ATOM 633 CG TYR A 118 39.686 28.746 -3.738 1.00 5.13 C ANISOU 633 CG TYR A 118 699 503 746 -210 42 144 C ATOM 634 CD1 TYR A 118 38.469 29.141 -4.283 1.00 7.50 C ANISOU 634 CD1 TYR A 118 897 925 1027 26 -209 -96 C ATOM 635 CD2 TYR A 118 40.039 29.315 -2.516 1.00 5.80 C ANISOU 635 CD2 TYR A 118 861 597 743 -138 -117 199 C ATOM 636 CE1 TYR A 118 37.638 30.021 -3.631 1.00 7.73 C ANISOU 636 CE1 TYR A 118 876 1075 984 115 -216 -44 C ATOM 637 CE2 TYR A 118 39.197 30.211 -1.857 1.00 6.47 C ANISOU 637 CE2 TYR A 118 984 658 815 -236 0 81 C ATOM 638 CZ TYR A 118 37.983 30.571 -2.416 1.00 8.08 C ANISOU 638 CZ TYR A 118 1007 1045 1015 -53 -51 -130 C ATOM 639 OH TYR A 118 37.118 31.442 -1.777 1.00 10.92 O ANISOU 639 OH TYR A 118 1088 1201 1857 56 -133 -458 O ATOM 640 N TYR A 119 43.715 28.410 -4.412 1.00 4.48 N ANISOU 640 N TYR A 119 510 537 652 -156 32 253 N ATOM 641 CA TYR A 119 44.828 29.057 -3.728 1.00 4.05 C ANISOU 641 CA TYR A 119 429 502 607 24 84 18 C ATOM 642 C TYR A 119 45.883 29.471 -4.762 1.00 4.29 C ANISOU 642 C TYR A 119 552 510 564 -45 67 94 C ATOM 643 O TYR A 119 46.235 28.706 -5.634 1.00 5.70 O ANISOU 643 O TYR A 119 846 650 668 -220 322 40 O ATOM 644 CB TYR A 119 45.482 28.116 -2.745 1.00 3.86 C ANISOU 644 CB TYR A 119 391 584 489 -54 68 31 C ATOM 645 CG TYR A 119 44.621 27.547 -1.668 1.00 3.43 C ANISOU 645 CG TYR A 119 389 507 407 -34 11 35 C ATOM 646 CD1 TYR A 119 43.996 28.355 -0.762 1.00 3.50 C ANISOU 646 CD1 TYR A 119 443 439 445 -105 14 -12 C ATOM 647 CD2 TYR A 119 44.554 26.169 -1.468 1.00 3.74 C ANISOU 647 CD2 TYR A 119 420 501 496 -7 21 40 C ATOM 648 CE1 TYR A 119 43.275 27.803 0.327 1.00 3.56 C ANISOU 648 CE1 TYR A 119 480 457 414 -77 45 -36 C ATOM 649 CE2 TYR A 119 43.846 25.613 -0.406 1.00 4.26 C ANISOU 649 CE2 TYR A 119 591 545 482 23 101 26 C ATOM 650 CZ TYR A 119 43.242 26.448 0.512 1.00 3.28 C ANISOU 650 CZ TYR A 119 359 466 420 -86 15 4 C ATOM 651 OH TYR A 119 42.581 25.847 1.565 1.00 4.79 O ANISOU 651 OH TYR A 119 701 630 486 -245 66 77 O ATOM 652 N TRP A 120 46.414 30.658 -4.560 1.00 3.35 N ANISOU 652 N TRP A 120 356 522 395 -11 115 46 N ATOM 653 CA TRP A 120 47.538 31.180 -5.335 1.00 3.13 C ANISOU 653 CA TRP A 120 340 434 415 -70 82 8 C ATOM 654 C TRP A 120 48.828 31.044 -4.527 1.00 3.11 C ANISOU 654 C TRP A 120 441 280 458 -37 -5 0 C ATOM 655 O TRP A 120 49.820 30.498 -5.034 1.00 4.49 O ANISOU 655 O TRP A 120 535 545 623 76 71 -28 O ATOM 656 CB TRP A 120 47.277 32.624 -5.719 1.00 3.69 C ANISOU 656 CB TRP A 120 474 558 367 27 -20 152 C ATOM 657 CG TRP A 120 48.327 33.266 -6.594 1.00 4.07 C ANISOU 657 CG TRP A 120 434 603 510 -99 -44 108 C ATOM 658 CD1 TRP A 120 49.336 34.043 -6.168 1.00 4.41 C ANISOU 658 CD1 TRP A 120 453 731 489 -140 -128 198 C ATOM 659 CD2 TRP A 120 48.425 33.194 -8.011 1.00 3.24 C ANISOU 659 CD2 TRP A 120 315 422 494 1 -60 173 C ATOM 660 NE1 TRP A 120 50.044 34.512 -7.236 1.00 4.94 N ANISOU 660 NE1 TRP A 120 592 718 567 -224 -73 237 N ATOM 661 CE2 TRP A 120 49.516 34.023 -8.394 1.00 4.29 C ANISOU 661 CE2 TRP A 120 425 588 616 -122 -47 188 C ATOM 662 CE3 TRP A 120 47.665 32.593 -9.014 1.00 3.96 C ANISOU 662 CE3 TRP A 120 454 485 563 -94 0 35 C ATOM 663 CZ2 TRP A 120 49.888 34.206 -9.729 1.00 5.11 C ANISOU 663 CZ2 TRP A 120 629 720 590 -151 -120 233 C ATOM 664 CZ3 TRP A 120 48.050 32.768 -10.341 1.00 3.98 C ANISOU 664 CZ3 TRP A 120 462 523 525 -75 -38 -74 C ATOM 665 CH2 TRP A 120 49.136 33.584 -10.682 1.00 4.53 C ANISOU 665 CH2 TRP A 120 589 606 526 -97 -74 246 C ATOM 666 N ASN A 121 48.835 31.551 -3.305 1.00 3.78 N ANISOU 666 N ASN A 121 370 691 373 72 18 21 N ATOM 667 CA ASN A 121 49.969 31.469 -2.398 1.00 3.67 C ANISOU 667 CA ASN A 121 391 550 452 121 -23 33 C ATOM 668 C ASN A 121 49.819 30.251 -1.495 1.00 4.01 C ANISOU 668 C ASN A 121 531 502 489 8 17 -14 C ATOM 669 O ASN A 121 48.735 29.966 -0.983 1.00 4.81 O ANISOU 669 O ASN A 121 576 699 553 -29 59 85 O ATOM 670 CB ASN A 121 50.084 32.718 -1.535 1.00 4.10 C ANISOU 670 CB ASN A 121 505 499 553 -47 -21 63 C ATOM 671 CG ASN A 121 50.479 33.946 -2.297 1.00 4.73 C ANISOU 671 CG ASN A 121 576 602 619 -5 -15 193 C ATOM 672 OD1 ASN A 121 51.302 33.892 -3.206 1.00 7.01 O ANISOU 672 OD1 ASN A 121 893 1005 764 -7 212 232 O ATOM 673 ND2 ASN A 121 49.905 35.047 -1.935 1.00 6.35 N ANISOU 673 ND2 ASN A 121 796 720 896 0 239 43 N ATOM 674 N ALA A 122 50.918 29.528 -1.311 1.00 3.92 N ANISOU 674 N ALA A 122 574 487 425 59 128 31 N ATOM 675 CA ALA A 122 50.938 28.408 -0.371 1.00 4.23 C ANISOU 675 CA ALA A 122 603 441 562 14 118 66 C ATOM 676 C ALA A 122 50.426 28.794 0.998 1.00 3.88 C ANISOU 676 C ALA A 122 422 555 497 -24 44 113 C ATOM 677 O ALA A 122 49.744 27.979 1.654 1.00 4.35 O ANISOU 677 O ALA A 122 538 525 586 -98 56 109 O ATOM 678 CB ALA A 122 52.339 27.842 -0.276 1.00 6.00 C ANISOU 678 CB ALA A 122 714 690 876 173 62 106 C ATOM 679 N GLN A 123 50.749 29.998 1.448 1.00 3.97 N ANISOU 679 N GLN A 123 516 549 441 -38 0 143 N ATOM 680 CA GLN A 123 50.325 30.418 2.756 1.00 4.62 C ANISOU 680 CA GLN A 123 625 577 551 -51 -14 -75 C ATOM 681 C GLN A 123 48.836 30.451 2.919 1.00 4.21 C ANISOU 681 C GLN A 123 614 545 440 -177 -20 -30 C ATOM 682 O GLN A 123 48.343 30.309 4.058 1.00 5.00 O ANISOU 682 O GLN A 123 691 668 539 -279 111 22 O ATOM 683 CB GLN A 123 50.942 31.760 3.170 1.00 6.13 C ANISOU 683 CB GLN A 123 839 635 856 -238 174 -94 C ATOM 684 CG GLN A 123 50.762 32.094 4.654 1.00 6.62 C ANISOU 684 CG GLN A 123 945 786 783 -280 -32 -73 C ATOM 685 CD GLN A 123 51.354 31.082 5.615 1.00 7.44 C ANISOU 685 CD GLN A 123 938 947 940 -164 -23 -2 C ATOM 686 OE1 GLN A 123 52.359 30.472 5.332 1.00 10.67 O ANISOU 686 OE1 GLN A 123 1108 1659 1286 338 -360 -67 O ATOM 687 NE2 GLN A 123 50.735 30.942 6.789 1.00 10.57 N ANISOU 687 NE2 GLN A 123 1316 1540 1160 -75 271 156 N ATOM 688 N GLU A 124 48.071 30.668 1.837 1.00 3.65 N ANISOU 688 N GLU A 124 482 427 475 -15 42 46 N ATOM 689 CA GLU A 124 46.605 30.622 1.946 1.00 4.61 C ANISOU 689 CA GLU A 124 496 602 654 -40 138 47 C ATOM 690 C GLU A 124 46.109 29.276 2.424 1.00 3.89 C ANISOU 690 C GLU A 124 528 540 408 -21 59 -30 C ATOM 691 O GLU A 124 45.159 29.169 3.210 1.00 5.06 O ANISOU 691 O GLU A 124 571 680 672 -22 179 136 O ATOM 692 CB GLU A 124 45.937 30.954 0.609 1.00 5.36 C ANISOU 692 CB GLU A 124 626 779 631 91 186 108 C ATOM 693 CG GLU A 124 46.163 32.350 0.094 1.00 6.41 C ANISOU 693 CG GLU A 124 859 779 796 107 203 134 C ATOM 694 CD GLU A 124 45.611 32.532 -1.310 1.00 8.55 C ANISOU 694 CD GLU A 124 1054 1300 893 137 59 256 C ATOM 695 OE1 GLU A 124 46.320 32.366 -2.296 1.00 8.57 O ANISOU 695 OE1 GLU A 124 1067 1306 883 320 18 136 O ATOM 696 OE2 GLU A 124 44.440 32.879 -1.444 1.00 12.14 O ANISOU 696 OE2 GLU A 124 1005 2263 1341 218 62 47 O ATOM 697 N CYS A 125 46.734 28.230 1.925 1.00 3.50 N ANISOU 697 N CYS A 125 420 443 464 -31 69 91 N ATOM 698 CA CYS A 125 46.375 26.862 2.310 1.00 3.64 C ANISOU 698 CA CYS A 125 472 439 470 -78 45 62 C ATOM 699 C CYS A 125 46.840 26.533 3.728 1.00 3.28 C ANISOU 699 C CYS A 125 401 396 448 -51 42 -28 C ATOM 700 O CYS A 125 46.091 25.983 4.538 1.00 3.70 O ANISOU 700 O CYS A 125 462 487 455 -102 122 -101 O ATOM 701 CB CYS A 125 47.000 25.927 1.289 1.00 4.60 C ANISOU 701 CB CYS A 125 582 632 532 -114 11 -121 C ATOM 702 SG CYS A 125 46.776 24.166 1.661 1.00 5.92 S ANISOU 702 SG CYS A 125 836 626 788 -118 175 -139 S ATOM 703 N ILE A 126 48.081 26.899 4.053 1.00 3.49 N ANISOU 703 N ILE A 126 383 528 413 -52 49 -40 N ATOM 704 CA ILE A 126 48.609 26.701 5.395 1.00 3.68 C ANISOU 704 CA ILE A 126 466 467 464 0 4 -3 C ATOM 705 C ILE A 126 47.716 27.431 6.408 1.00 3.17 C ANISOU 705 C ILE A 126 293 490 418 -86 20 47 C ATOM 706 O ILE A 126 47.381 26.886 7.479 1.00 3.83 O ANISOU 706 O ILE A 126 393 653 410 -124 8 100 O ATOM 707 CB ILE A 126 50.071 27.200 5.455 1.00 4.39 C ANISOU 707 CB ILE A 126 508 561 597 -58 -55 64 C ATOM 708 CG1 ILE A 126 50.928 26.263 4.583 1.00 5.64 C ANISOU 708 CG1 ILE A 126 691 710 739 7 -11 -60 C ATOM 709 CG2 ILE A 126 50.573 27.235 6.896 1.00 4.74 C ANISOU 709 CG2 ILE A 126 574 627 600 -83 -83 -7 C ATOM 710 CD1 ILE A 126 52.347 26.734 4.318 1.00 7.36 C ANISOU 710 CD1 ILE A 126 716 1033 1047 6 106 55 C ATOM 711 N GLN A 127 47.290 28.642 6.070 1.00 3.03 N ANISOU 711 N GLN A 127 319 457 373 -99 42 4 N ATOM 712 CA GLN A 127 46.409 29.407 6.955 1.00 3.84 C ANISOU 712 CA GLN A 127 424 549 485 -58 60 -92 C ATOM 713 C GLN A 127 45.108 28.632 7.210 1.00 3.22 C ANISOU 713 C GLN A 127 430 412 381 -28 21 -57 C ATOM 714 O GLN A 127 44.594 28.630 8.337 1.00 3.54 O ANISOU 714 O GLN A 127 453 479 412 -99 61 3 O ATOM 715 CB GLN A 127 46.092 30.753 6.337 1.00 5.22 C ANISOU 715 CB GLN A 127 756 549 677 -106 159 -13 C ATOM 716 CG GLN A 127 45.175 31.646 7.174 1.00 8.53 C ANISOU 716 CG GLN A 127 1176 938 1124 125 391 -175 C ATOM 717 CD GLN A 127 45.165 33.071 6.740 1.00 14.09 C ANISOU 717 CD GLN A 127 1811 1262 2278 50 358 489 C ATOM 718 OE1 GLN A 127 46.208 33.726 6.731 1.00 19.32 O ANISOU 718 OE1 GLN A 127 2212 1643 3486 -409 478 484 O ATOM 719 NE2 GLN A 127 43.994 33.577 6.428 1.00 22.17 N ANISOU 719 NE2 GLN A 127 1949 2754 3721 348 75 712 N ATOM 720 N ASP A 128 44.548 28.030 6.169 1.00 2.84 N ANISOU 720 N ASP A 128 368 397 313 -68 26 30 N ATOM 721 CA ASP A 128 43.319 27.240 6.325 1.00 2.85 C ANISOU 721 CA ASP A 128 334 369 378 -26 83 12 C ATOM 722 C ASP A 128 43.505 26.030 7.235 1.00 2.93 C ANISOU 722 C ASP A 128 336 421 354 17 27 17 C ATOM 723 O ASP A 128 42.665 25.764 8.105 1.00 2.60 O ANISOU 723 O ASP A 128 324 404 260 23 -16 16 O ATOM 724 CB ASP A 128 42.743 26.817 4.978 1.00 3.29 C ANISOU 724 CB ASP A 128 414 437 399 -87 48 33 C ATOM 725 CG ASP A 128 41.962 27.921 4.276 1.00 4.21 C ANISOU 725 CG ASP A 128 435 608 555 -10 -46 70 C ATOM 726 OD1 ASP A 128 41.615 28.941 4.892 1.00 5.92 O ANISOU 726 OD1 ASP A 128 994 685 568 124 9 86 O ATOM 727 OD2 ASP A 128 41.620 27.733 3.073 1.00 4.76 O ANISOU 727 OD2 ASP A 128 522 757 530 85 -68 127 O ATOM 728 N PHE A 129 44.602 25.286 7.070 1.00 2.75 N ANISOU 728 N PHE A 129 348 359 336 3 61 2 N ATOM 729 CA PHE A 129 44.870 24.232 8.031 1.00 3.06 C ANISOU 729 CA PHE A 129 352 349 459 42 -30 15 C ATOM 730 C PHE A 129 44.947 24.761 9.431 1.00 3.22 C ANISOU 730 C PHE A 129 372 455 395 -8 -17 79 C ATOM 731 O PHE A 129 44.372 24.171 10.359 1.00 3.46 O ANISOU 731 O PHE A 129 350 553 412 31 25 107 O ATOM 732 CB PHE A 129 46.194 23.495 7.711 1.00 3.68 C ANISOU 732 CB PHE A 129 414 433 549 74 106 43 C ATOM 733 CG PHE A 129 46.105 22.437 6.624 1.00 4.02 C ANISOU 733 CG PHE A 129 444 537 545 108 -80 13 C ATOM 734 CD1 PHE A 129 45.560 21.190 6.916 1.00 5.41 C ANISOU 734 CD1 PHE A 129 741 625 687 36 119 61 C ATOM 735 CD2 PHE A 129 46.558 22.659 5.335 1.00 4.47 C ANISOU 735 CD2 PHE A 129 551 539 607 139 16 42 C ATOM 736 CE1 PHE A 129 45.510 20.192 5.965 1.00 6.73 C ANISOU 736 CE1 PHE A 129 981 643 933 59 -29 -50 C ATOM 737 CE2 PHE A 129 46.526 21.654 4.388 1.00 5.73 C ANISOU 737 CE2 PHE A 129 745 811 619 122 -50 -77 C ATOM 738 CZ PHE A 129 46.018 20.424 4.721 1.00 6.31 C ANISOU 738 CZ PHE A 129 800 721 876 186 -33 -127 C ATOM 739 N ASN A 130 45.699 25.837 9.625 1.00 2.92 N ANISOU 739 N ASN A 130 275 461 371 18 2 53 N ATOM 740 CA ASN A 130 45.844 26.390 10.972 1.00 3.51 C ANISOU 740 CA ASN A 130 445 436 452 -1 26 -39 C ATOM 741 C ASN A 130 44.513 26.845 11.568 1.00 3.06 C ANISOU 741 C ASN A 130 389 345 428 -50 17 39 C ATOM 742 O ASN A 130 44.245 26.555 12.742 1.00 3.80 O ANISOU 742 O ASN A 130 505 527 410 -171 14 -19 O ATOM 743 CB ASN A 130 46.878 27.517 10.957 1.00 4.38 C ANISOU 743 CB ASN A 130 642 533 486 -141 -50 -75 C ATOM 744 CG ASN A 130 48.293 26.960 10.847 1.00 7.32 C ANISOU 744 CG ASN A 130 693 1087 1001 65 -362 -86 C ATOM 745 OD1 ASN A 130 48.559 25.865 11.322 1.00 10.50 O ANISOU 745 OD1 ASN A 130 851 1242 1896 196 -119 155 O ATOM 746 ND2 ASN A 130 49.143 27.690 10.268 1.00 12.44 N ANISOU 746 ND2 ASN A 130 1194 2327 1203 -148 181 104 N ATOM 747 N THR A 131 43.668 27.451 10.753 1.00 2.78 N ANISOU 747 N THR A 131 329 373 355 -50 66 17 N ATOM 748 CA THR A 131 42.331 27.876 11.185 1.00 3.11 C ANISOU 748 CA THR A 131 360 367 453 4 54 -45 C ATOM 749 C THR A 131 41.511 26.675 11.637 1.00 2.52 C ANISOU 749 C THR A 131 290 375 292 29 11 -31 C ATOM 750 O THR A 131 40.803 26.732 12.656 1.00 2.79 O ANISOU 750 O THR A 131 269 470 320 54 29 70 O ATOM 751 CB THR A 131 41.604 28.626 10.069 1.00 3.56 C ANISOU 751 CB THR A 131 420 471 460 -35 68 37 C ATOM 752 OG1 THR A 131 42.329 29.831 9.809 1.00 4.90 O ANISOU 752 OG1 THR A 131 570 454 838 -30 180 150 O ATOM 753 CG2 THR A 131 40.183 28.962 10.441 1.00 3.83 C ANISOU 753 CG2 THR A 131 442 501 512 24 77 85 C ATOM 754 N MET A 132 41.580 25.579 10.899 1.00 2.46 N ANISOU 754 N MET A 132 337 288 307 0 53 26 N ATOM 755 CA MET A 132 40.855 24.375 11.300 1.00 2.76 C ANISOU 755 CA MET A 132 331 358 359 -61 53 21 C ATOM 756 C MET A 132 41.279 23.955 12.722 1.00 2.77 C ANISOU 756 C MET A 132 320 365 364 -31 20 -10 C ATOM 757 O MET A 132 40.439 23.631 13.583 1.00 3.55 O ANISOU 757 O MET A 132 479 424 444 -47 95 120 O ATOM 758 CB MET A 132 41.131 23.274 10.278 1.00 3.30 C ANISOU 758 CB MET A 132 423 400 430 23 44 -4 C ATOM 759 CG MET A 132 40.513 21.953 10.623 1.00 3.97 C ANISOU 759 CG MET A 132 482 493 534 -91 48 13 C ATOM 760 SD MET A 132 40.874 20.679 9.421 1.00 5.27 S ANISOU 760 SD MET A 132 812 502 689 -94 65 -72 S ATOM 761 CE MET A 132 42.535 20.307 9.885 1.00 8.30 C ANISOU 761 CE MET A 132 1044 964 1143 176 -221 -149 C ATOM 762 N PHE A 133 42.581 23.901 12.975 1.00 2.56 N ANISOU 762 N PHE A 133 329 311 330 59 13 -18 N ATOM 763 CA PHE A 133 43.063 23.521 14.293 1.00 2.98 C ANISOU 763 CA PHE A 133 437 335 360 23 -11 40 C ATOM 764 C PHE A 133 42.633 24.507 15.376 1.00 2.50 C ANISOU 764 C PHE A 133 285 362 300 -58 -24 34 C ATOM 765 O PHE A 133 42.130 24.119 16.438 1.00 2.74 O ANISOU 765 O PHE A 133 423 330 288 -7 23 20 O ATOM 766 CB PHE A 133 44.592 23.322 14.302 1.00 4.08 C ANISOU 766 CB PHE A 133 456 566 529 86 -50 79 C ATOM 767 CG PHE A 133 45.101 22.250 13.384 1.00 4.32 C ANISOU 767 CG PHE A 133 517 589 535 66 6 83 C ATOM 768 CD1 PHE A 133 44.600 20.960 13.433 1.00 6.41 C ANISOU 768 CD1 PHE A 133 852 658 925 -83 104 -126 C ATOM 769 CD2 PHE A 133 46.094 22.536 12.472 1.00 4.58 C ANISOU 769 CD2 PHE A 133 560 587 592 44 20 180 C ATOM 770 CE1 PHE A 133 45.046 19.979 12.586 1.00 6.78 C ANISOU 770 CE1 PHE A 133 760 686 1128 106 24 -133 C ATOM 771 CE2 PHE A 133 46.562 21.538 11.597 1.00 6.28 C ANISOU 771 CE2 PHE A 133 769 877 740 272 49 81 C ATOM 772 CZ PHE A 133 46.008 20.282 11.659 1.00 6.28 C ANISOU 772 CZ PHE A 133 907 819 658 250 -34 -171 C ATOM 773 N THR A 134 42.847 25.781 15.131 1.00 2.36 N ANISOU 773 N THR A 134 296 335 262 8 -12 18 N ATOM 774 CA THR A 134 42.578 26.754 16.155 1.00 2.61 C ANISOU 774 CA THR A 134 351 320 317 11 1 -2 C ATOM 775 C THR A 134 41.072 26.909 16.422 1.00 2.36 C ANISOU 775 C THR A 134 345 271 278 -39 10 0 C ATOM 776 O THR A 134 40.661 27.181 17.562 1.00 2.75 O ANISOU 776 O THR A 134 361 382 302 -64 35 -52 O ATOM 777 CB THR A 134 43.267 28.115 15.884 1.00 3.00 C ANISOU 777 CB THR A 134 414 366 358 -46 36 -8 C ATOM 778 OG1 THR A 134 42.885 28.618 14.596 1.00 3.67 O ANISOU 778 OG1 THR A 134 592 394 408 -90 20 74 O ATOM 779 CG2 THR A 134 44.731 27.985 16.007 1.00 3.28 C ANISOU 779 CG2 THR A 134 409 463 374 -36 63 41 C ATOM 780 N ASN A 135 40.230 26.669 15.445 1.00 2.65 N ANISOU 780 N ASN A 135 344 366 296 -85 -3 40 N ATOM 781 CA ASN A 135 38.789 26.619 15.676 1.00 2.58 C ANISOU 781 CA ASN A 135 330 337 311 -43 -37 -9 C ATOM 782 C ASN A 135 38.501 25.547 16.704 1.00 2.36 C ANISOU 782 C ASN A 135 275 312 310 18 -32 -10 C ATOM 783 O ASN A 135 37.718 25.729 17.628 1.00 2.47 O ANISOU 783 O ASN A 135 360 307 269 -14 -3 29 O ATOM 784 CB ASN A 135 38.022 26.277 14.381 1.00 2.34 C ANISOU 784 CB ASN A 135 277 317 293 -31 2 -34 C ATOM 785 CG ASN A 135 37.955 27.402 13.389 1.00 2.46 C ANISOU 785 CG ASN A 135 263 345 326 27 -3 -15 C ATOM 786 OD1 ASN A 135 38.282 28.524 13.687 1.00 3.14 O ANISOU 786 OD1 ASN A 135 405 339 448 46 -104 -31 O ATOM 787 ND2 ASN A 135 37.466 27.095 12.202 1.00 2.83 N ANISOU 787 ND2 ASN A 135 354 407 314 60 -46 30 N ATOM 788 N CYS A 136 39.094 24.382 16.503 1.00 2.14 N ANISOU 788 N CYS A 136 267 280 263 -14 2 -13 N ATOM 789 CA CYS A 136 38.840 23.263 17.412 1.00 2.57 C ANISOU 789 CA CYS A 136 334 356 287 -31 5 35 C ATOM 790 C CYS A 136 39.227 23.601 18.836 1.00 2.48 C ANISOU 790 C CYS A 136 331 293 318 -33 -22 15 C ATOM 791 O CYS A 136 38.493 23.258 19.772 1.00 3.00 O ANISOU 791 O CYS A 136 419 386 335 -47 -13 102 O ATOM 792 CB CYS A 136 39.623 22.056 16.882 1.00 3.09 C ANISOU 792 CB CYS A 136 417 357 398 0 -98 -49 C ATOM 793 SG CYS A 136 39.293 20.510 17.721 1.00 5.26 S ANISOU 793 SG CYS A 136 872 411 713 79 144 86 S ATOM 794 N TYR A 137 40.357 24.283 19.019 1.00 2.33 N ANISOU 794 N TYR A 137 294 325 267 -23 -13 31 N ATOM 795 CA TYR A 137 40.848 24.587 20.357 1.00 2.48 C ANISOU 795 CA TYR A 137 346 298 298 4 -26 -36 C ATOM 796 C TYR A 137 40.105 25.702 21.075 1.00 2.41 C ANISOU 796 C TYR A 137 355 265 296 16 -28 -3 C ATOM 797 O TYR A 137 40.228 25.811 22.300 1.00 2.58 O ANISOU 797 O TYR A 137 427 256 294 12 -30 -9 O ATOM 798 CB TYR A 137 42.356 24.882 20.369 1.00 3.08 C ANISOU 798 CB TYR A 137 336 461 372 19 -71 31 C ATOM 799 CG TYR A 137 43.221 23.925 19.644 1.00 3.09 C ANISOU 799 CG TYR A 137 407 442 323 44 -48 84 C ATOM 800 CD1 TYR A 137 42.935 22.565 19.623 1.00 3.89 C ANISOU 800 CD1 TYR A 137 479 445 551 33 15 -9 C ATOM 801 CD2 TYR A 137 44.343 24.374 18.953 1.00 3.79 C ANISOU 801 CD2 TYR A 137 431 460 547 30 41 66 C ATOM 802 CE1 TYR A 137 43.773 21.672 18.958 1.00 4.11 C ANISOU 802 CE1 TYR A 137 521 453 586 27 38 -38 C ATOM 803 CE2 TYR A 137 45.181 23.501 18.269 1.00 3.97 C ANISOU 803 CE2 TYR A 137 444 518 546 -16 32 -43 C ATOM 804 CZ TYR A 137 44.890 22.136 18.268 1.00 4.09 C ANISOU 804 CZ TYR A 137 496 485 570 47 47 -52 C ATOM 805 OH TYR A 137 45.699 21.216 17.616 1.00 7.02 O ANISOU 805 OH TYR A 137 1099 615 951 306 256 -106 O ATOM 806 N ILE A 138 39.397 26.575 20.341 1.00 2.14 N ANISOU 806 N ILE A 138 259 278 273 -7 -8 0 N ATOM 807 CA ILE A 138 38.591 27.614 20.992 1.00 2.38 C ANISOU 807 CA ILE A 138 298 287 317 8 -22 -28 C ATOM 808 C ILE A 138 37.205 27.156 21.318 1.00 2.41 C ANISOU 808 C ILE A 138 324 261 328 -3 -10 24 C ATOM 809 O ILE A 138 36.620 27.632 22.276 1.00 3.41 O ANISOU 809 O ILE A 138 456 505 335 3 -6 -83 O ATOM 810 CB ILE A 138 38.607 28.952 20.226 1.00 2.67 C ANISOU 810 CB ILE A 138 352 312 348 -12 19 -4 C ATOM 811 CG1 ILE A 138 38.263 30.130 21.143 1.00 3.19 C ANISOU 811 CG1 ILE A 138 453 379 379 0 0 -65 C ATOM 812 CG2 ILE A 138 37.748 28.901 19.006 1.00 2.74 C ANISOU 812 CG2 ILE A 138 327 353 358 6 21 45 C ATOM 813 CD1 ILE A 138 38.532 31.493 20.542 1.00 4.22 C ANISOU 813 CD1 ILE A 138 595 460 547 -11 24 50 C ATOM 814 N TYR A 139 36.673 26.195 20.559 1.00 2.69 N ANISOU 814 N TYR A 139 337 318 366 -12 14 -37 N ATOM 815 CA TYR A 139 35.307 25.731 20.813 1.00 3.26 C ANISOU 815 CA TYR A 139 323 376 538 -7 -15 41 C ATOM 816 C TYR A 139 35.269 24.610 21.847 1.00 3.00 C ANISOU 816 C TYR A 139 348 466 325 -23 -62 -6 C ATOM 817 O TYR A 139 34.411 24.622 22.733 1.00 3.62 O ANISOU 817 O TYR A 139 321 578 475 3 3 79 O ATOM 818 CB TYR A 139 34.622 25.273 19.513 1.00 3.93 C ANISOU 818 CB TYR A 139 451 550 490 70 -53 36 C ATOM 819 CG TYR A 139 33.205 24.806 19.787 1.00 4.10 C ANISOU 819 CG TYR A 139 495 586 476 -16 -99 66 C ATOM 820 CD1 TYR A 139 32.233 25.747 20.112 1.00 4.30 C ANISOU 820 CD1 TYR A 139 495 557 580 11 -166 101 C ATOM 821 CD2 TYR A 139 32.906 23.461 19.890 1.00 5.12 C ANISOU 821 CD2 TYR A 139 566 614 762 -3 -172 253 C ATOM 822 CE1 TYR A 139 30.980 25.348 20.532 1.00 5.51 C ANISOU 822 CE1 TYR A 139 553 796 743 49 8 75 C ATOM 823 CE2 TYR A 139 31.639 23.070 20.272 1.00 5.88 C ANISOU 823 CE2 TYR A 139 649 785 800 -152 -174 339 C ATOM 824 CZ TYR A 139 30.705 24.034 20.606 1.00 6.63 C ANISOU 824 CZ TYR A 139 656 899 961 -180 -48 298 C ATOM 825 OH TYR A 139 29.444 23.626 21.028 1.00 11.62 O ANISOU 825 OH TYR A 139 728 2104 1581 -345 222 358 O ATOM 826 N ASN A 140 36.150 23.628 21.699 1.00 2.76 N ANISOU 826 N ASN A 140 357 359 330 -78 17 46 N ATOM 827 CA ASN A 140 36.070 22.393 22.472 1.00 2.85 C ANISOU 827 CA ASN A 140 368 309 403 -34 53 29 C ATOM 828 C ASN A 140 36.957 22.460 23.720 1.00 3.45 C ANISOU 828 C ASN A 140 528 389 393 28 12 -17 C ATOM 829 O ASN A 140 38.048 23.006 23.673 1.00 4.38 O ANISOU 829 O ASN A 140 474 681 508 22 -153 48 O ATOM 830 CB ASN A 140 36.512 21.214 21.604 1.00 2.67 C ANISOU 830 CB ASN A 140 360 302 352 -36 37 40 C ATOM 831 CG ASN A 140 35.618 21.005 20.418 1.00 2.78 C ANISOU 831 CG ASN A 140 381 309 365 -3 37 -33 C ATOM 832 OD1 ASN A 140 34.522 20.461 20.502 1.00 3.71 O ANISOU 832 OD1 ASN A 140 447 483 480 -107 16 65 O ATOM 833 ND2 ASN A 140 36.097 21.458 19.265 1.00 3.40 N ANISOU 833 ND2 ASN A 140 458 465 367 -87 -3 32 N ATOM 834 N LYS A 141 36.438 21.908 24.814 1.00 4.42 N ANISOU 834 N LYS A 141 591 620 467 6 12 117 N ATOM 835 CA LYS A 141 37.151 21.900 26.061 1.00 5.09 C ANISOU 835 CA LYS A 141 653 632 648 49 -154 25 C ATOM 836 C LYS A 141 38.524 21.243 25.898 1.00 3.73 C ANISOU 836 C LYS A 141 702 456 259 32 2 34 C ATOM 837 O LYS A 141 38.635 20.169 25.266 1.00 4.85 O ANISOU 837 O LYS A 141 917 569 356 141 -167 -103 O ATOM 838 CB LYS A 141 36.312 21.120 27.099 1.00 6.93 C ANISOU 838 CB LYS A 141 904 940 786 -26 119 -43 C ATOM 839 CG LYS A 141 36.892 21.141 28.516 1.00 9.20 C ANISOU 839 CG LYS A 141 1294 1283 919 55 -130 64 C ATOM 840 CD LYS A 141 36.004 20.320 29.475 1.00 14.36 C ANISOU 840 CD LYS A 141 2059 2057 1338 -556 55 264 C ATOM 841 CE LYS A 141 34.767 21.061 29.879 1.00 18.82 C ANISOU 841 CE LYS A 141 2470 2314 2365 -100 -76 341 C ATOM 842 NZ LYS A 141 33.871 20.250 30.766 1.00 29.92 N ANISOU 842 NZ LYS A 141 3857 3531 3978 -885 508 1064 N ATOM 843 N PRO A 142 39.587 21.800 26.512 1.00 4.57 N ANISOU 843 N PRO A 142 722 536 478 64 -77 -63 N ATOM 844 CA PRO A 142 40.875 21.129 26.488 1.00 5.17 C ANISOU 844 CA PRO A 142 641 801 520 56 -74 4 C ATOM 845 C PRO A 142 40.753 19.711 26.985 1.00 6.56 C ANISOU 845 C PRO A 142 814 768 910 56 -168 -3 C ATOM 846 O PRO A 142 39.989 19.446 27.930 1.00 7.23 O ANISOU 846 O PRO A 142 1141 787 819 55 -154 157 O ATOM 847 CB PRO A 142 41.751 21.980 27.421 1.00 5.88 C ANISOU 847 CB PRO A 142 852 673 708 -64 -170 73 C ATOM 848 CG PRO A 142 41.099 23.328 27.370 1.00 6.67 C ANISOU 848 CG PRO A 142 1029 689 814 -19 -225 -19 C ATOM 849 CD PRO A 142 39.661 23.105 27.198 1.00 5.68 C ANISOU 849 CD PRO A 142 981 490 686 -12 -99 -71 C ATOM 850 N GLY A 143 41.429 18.811 26.299 1.00 6.71 N ANISOU 850 N GLY A 143 1121 756 669 25 -203 -77 N ATOM 851 CA GLY A 143 41.377 17.402 26.730 1.00 7.43 C ANISOU 851 CA GLY A 143 1111 838 874 220 -366 115 C ATOM 852 C GLY A 143 40.230 16.579 26.148 1.00 6.69 C ANISOU 852 C GLY A 143 1043 776 723 191 -157 -24 C ATOM 853 O GLY A 143 40.214 15.357 26.291 1.00 9.15 O ANISOU 853 O GLY A 143 1588 743 1145 191 -248 -48 O ATOM 854 N ASP A 144 39.223 17.211 25.536 1.00 5.21 N ANISOU 854 N ASP A 144 947 526 505 103 -101 -84 N ATOM 855 CA ASP A 144 38.195 16.485 24.841 1.00 5.41 C ANISOU 855 CA ASP A 144 855 578 621 -12 13 -23 C ATOM 856 C ASP A 144 38.856 15.669 23.717 1.00 4.57 C ANISOU 856 C ASP A 144 598 541 596 -72 29 37 C ATOM 857 O ASP A 144 39.890 16.047 23.162 1.00 4.61 O ANISOU 857 O ASP A 144 680 513 556 -122 37 90 O ATOM 858 CB ASP A 144 37.120 17.411 24.199 1.00 5.83 C ANISOU 858 CB ASP A 144 924 652 638 14 -68 -51 C ATOM 859 CG ASP A 144 35.957 17.772 25.141 1.00 8.58 C ANISOU 859 CG ASP A 144 1096 1088 1075 13 227 15 C ATOM 860 OD1 ASP A 144 36.048 17.514 26.356 1.00 11.76 O ANISOU 860 OD1 ASP A 144 1975 1486 1005 84 521 54 O ATOM 861 OD2 ASP A 144 34.952 18.321 24.661 1.00 10.89 O ANISOU 861 OD2 ASP A 144 1320 1434 1383 290 115 -190 O ATOM 862 N ASP A 145 38.205 14.573 23.351 1.00 3.71 N ANISOU 862 N ASP A 145 634 416 360 -24 57 122 N ATOM 863 CA ASP A 145 38.768 13.703 22.326 1.00 4.04 C ANISOU 863 CA ASP A 145 505 509 520 29 100 64 C ATOM 864 C ASP A 145 39.044 14.428 20.999 1.00 3.51 C ANISOU 864 C ASP A 145 415 368 551 -28 96 43 C ATOM 865 O ASP A 145 40.087 14.230 20.386 1.00 4.58 O ANISOU 865 O ASP A 145 529 525 685 74 204 28 O ATOM 866 CB ASP A 145 37.867 12.488 22.058 1.00 4.68 C ANISOU 866 CB ASP A 145 657 544 577 -39 127 1 C ATOM 867 CG ASP A 145 38.093 11.356 23.009 1.00 6.17 C ANISOU 867 CG ASP A 145 849 597 897 58 -91 94 C ATOM 868 OD1 ASP A 145 38.977 11.439 23.910 1.00 7.41 O ANISOU 868 OD1 ASP A 145 1255 608 953 -156 -255 118 O ATOM 869 OD2 ASP A 145 37.345 10.345 22.818 1.00 6.91 O ANISOU 869 OD2 ASP A 145 846 891 888 -159 -59 144 O ATOM 870 N ILE A 146 38.137 15.292 20.569 1.00 3.20 N ANISOU 870 N ILE A 146 439 388 387 -49 55 42 N ATOM 871 CA ILE A 146 38.334 15.996 19.307 1.00 3.16 C ANISOU 871 CA ILE A 146 472 329 399 -86 84 25 C ATOM 872 C ILE A 146 39.599 16.860 19.366 1.00 3.16 C ANISOU 872 C ILE A 146 405 365 428 -46 14 -7 C ATOM 873 O ILE A 146 40.312 16.989 18.375 1.00 3.92 O ANISOU 873 O ILE A 146 571 458 458 -9 105 -62 O ATOM 874 CB ILE A 146 37.107 16.832 18.909 1.00 3.60 C ANISOU 874 CB ILE A 146 420 467 480 -57 115 15 C ATOM 875 CG1 ILE A 146 37.174 17.354 17.464 1.00 4.89 C ANISOU 875 CG1 ILE A 146 709 589 559 -79 332 85 C ATOM 876 CG2 ILE A 146 36.868 18.001 19.845 1.00 3.53 C ANISOU 876 CG2 ILE A 146 461 401 476 12 24 53 C ATOM 877 CD1 ILE A 146 36.932 16.293 16.440 1.00 5.88 C ANISOU 877 CD1 ILE A 146 777 766 689 -125 200 -12 C ATOM 878 N VAL A 147 39.876 17.431 20.540 1.00 3.40 N ANISOU 878 N VAL A 147 424 452 415 -10 38 -39 N ATOM 879 CA VAL A 147 41.065 18.256 20.729 1.00 3.52 C ANISOU 879 CA VAL A 147 443 452 440 -20 31 -25 C ATOM 880 C VAL A 147 42.332 17.433 20.684 1.00 3.56 C ANISOU 880 C VAL A 147 476 466 410 7 62 55 C ATOM 881 O VAL A 147 43.309 17.795 20.017 1.00 3.99 O ANISOU 881 O VAL A 147 424 513 580 -55 64 40 O ATOM 882 CB VAL A 147 40.977 19.068 22.045 1.00 3.58 C ANISOU 882 CB VAL A 147 517 441 402 16 7 5 C ATOM 883 CG1 VAL A 147 42.265 19.801 22.337 1.00 4.34 C ANISOU 883 CG1 VAL A 147 541 574 531 -3 -76 29 C ATOM 884 CG2 VAL A 147 39.808 20.042 21.986 1.00 3.98 C ANISOU 884 CG2 VAL A 147 531 456 525 18 -101 -44 C ATOM 885 N LEU A 148 42.317 16.258 21.326 1.00 3.72 N ANISOU 885 N LEU A 148 472 457 484 31 69 74 N ATOM 886 CA LEU A 148 43.503 15.387 21.277 1.00 4.31 C ANISOU 886 CA LEU A 148 500 466 671 38 97 43 C ATOM 887 C LEU A 148 43.741 14.875 19.872 1.00 4.18 C ANISOU 887 C LEU A 148 469 483 635 13 8 16 C ATOM 888 O LEU A 148 44.903 14.764 19.442 1.00 4.93 O ANISOU 888 O LEU A 148 501 544 826 -3 81 -40 O ATOM 889 CB LEU A 148 43.359 14.261 22.308 1.00 5.74 C ANISOU 889 CB LEU A 148 875 515 788 140 254 127 C ATOM 890 CG LEU A 148 43.204 14.696 23.781 1.00 8.49 C ANISOU 890 CG LEU A 148 1292 1230 701 220 77 171 C ATOM 891 CD1 LEU A 148 42.852 13.485 24.623 1.00 10.39 C ANISOU 891 CD1 LEU A 148 1477 1177 1294 128 66 291 C ATOM 892 CD2 LEU A 148 44.423 15.436 24.292 1.00 10.41 C ANISOU 892 CD2 LEU A 148 1634 1262 1058 -65 88 221 C ATOM 893 N MET A 149 42.677 14.600 19.126 1.00 3.57 N ANISOU 893 N MET A 149 467 431 456 16 72 6 N ATOM 894 CA MET A 149 42.787 14.228 17.722 1.00 4.09 C ANISOU 894 CA MET A 149 673 422 459 1 48 -22 C ATOM 895 C MET A 149 43.382 15.354 16.893 1.00 4.20 C ANISOU 895 C MET A 149 505 478 609 4 112 -3 C ATOM 896 O MET A 149 44.342 15.129 16.118 1.00 4.78 O ANISOU 896 O MET A 149 612 532 668 -45 189 -116 O ATOM 897 CB MET A 149 41.425 13.816 17.174 1.00 4.27 C ANISOU 897 CB MET A 149 558 553 509 -3 169 66 C ATOM 898 CG MET A 149 40.910 12.528 17.809 1.00 4.73 C ANISOU 898 CG MET A 149 745 466 585 -36 150 3 C ATOM 899 SD MET A 149 39.167 12.211 17.498 1.00 6.70 S ANISOU 899 SD MET A 149 805 663 1078 -134 148 71 S ATOM 900 CE MET A 149 39.288 11.303 16.040 1.00 6.02 C ANISOU 900 CE MET A 149 667 890 727 73 151 271 C ATOM 901 N ALA A 150 42.864 16.565 17.050 1.00 3.94 N ANISOU 901 N ALA A 150 521 455 520 -40 125 -72 N ATOM 902 CA ALA A 150 43.409 17.731 16.341 1.00 4.06 C ANISOU 902 CA ALA A 150 552 496 492 -22 151 -43 C ATOM 903 C ALA A 150 44.865 17.958 16.690 1.00 3.90 C ANISOU 903 C ALA A 150 576 379 527 -15 96 -16 C ATOM 904 O ALA A 150 45.665 18.267 15.774 1.00 5.01 O ANISOU 904 O ALA A 150 673 561 667 -122 222 -68 O ATOM 905 CB ALA A 150 42.602 18.970 16.691 1.00 4.13 C ANISOU 905 CB ALA A 150 531 482 554 -23 138 -22 C ATOM 906 N GLU A 151 45.253 17.794 17.957 1.00 3.93 N ANISOU 906 N GLU A 151 489 418 586 -14 46 55 N ATOM 907 CA GLU A 151 46.665 17.989 18.347 1.00 4.58 C ANISOU 907 CA GLU A 151 510 560 668 45 -21 -1 C ATOM 908 C GLU A 151 47.559 16.966 17.639 1.00 5.10 C ANISOU 908 C GLU A 151 549 562 824 43 181 93 C ATOM 909 O GLU A 151 48.672 17.321 17.198 1.00 5.62 O ANISOU 909 O GLU A 151 488 691 956 103 173 181 O ATOM 910 CB GLU A 151 46.850 17.923 19.866 1.00 4.99 C ANISOU 910 CB GLU A 151 577 654 664 -4 -25 -13 C ATOM 911 CG GLU A 151 46.231 19.099 20.625 1.00 6.25 C ANISOU 911 CG GLU A 151 743 567 1061 -31 -139 -202 C ATOM 912 CD GLU A 151 46.264 19.001 22.140 1.00 10.78 C ANISOU 912 CD GLU A 151 1689 1329 1076 384 -373 -326 C ATOM 913 OE1 GLU A 151 46.607 17.960 22.691 1.00 15.57 O ANISOU 913 OE1 GLU A 151 3145 1467 1303 272 -265 57 O ATOM 914 OE2 GLU A 151 45.915 19.990 22.806 1.00 13.88 O ANISOU 914 OE2 GLU A 151 2249 1548 1476 532 -8 -476 O ATOM 915 N ALA A 152 47.106 15.725 17.516 1.00 5.15 N ANISOU 915 N ALA A 152 511 626 817 7 148 -22 N ATOM 916 CA ALA A 152 47.916 14.722 16.813 1.00 5.21 C ANISOU 916 CA ALA A 152 625 627 727 79 122 25 C ATOM 917 C ALA A 152 48.006 15.047 15.348 1.00 5.11 C ANISOU 917 C ALA A 152 564 675 699 12 126 -17 C ATOM 918 O ALA A 152 49.090 14.940 14.743 1.00 6.57 O ANISOU 918 O ALA A 152 560 820 1115 157 239 14 O ATOM 919 CB ALA A 152 47.319 13.340 17.010 1.00 5.91 C ANISOU 919 CB ALA A 152 760 644 839 49 115 61 C ATOM 920 N LEU A 153 46.929 15.504 14.731 1.00 4.50 N ANISOU 920 N LEU A 153 573 494 642 -4 155 31 N ATOM 921 CA LEU A 153 46.949 15.898 13.348 1.00 4.64 C ANISOU 921 CA LEU A 153 689 454 618 0 58 -30 C ATOM 922 C LEU A 153 47.833 17.117 13.126 1.00 4.44 C ANISOU 922 C LEU A 153 560 599 526 -38 155 -32 C ATOM 923 O LEU A 153 48.528 17.191 12.099 1.00 4.67 O ANISOU 923 O LEU A 153 475 765 532 -25 129 95 O ATOM 924 CB LEU A 153 45.546 16.162 12.812 1.00 4.96 C ANISOU 924 CB LEU A 153 692 590 601 -2 49 -39 C ATOM 925 CG LEU A 153 44.650 14.918 12.714 1.00 6.53 C ANISOU 925 CG LEU A 153 1004 624 853 -134 141 -27 C ATOM 926 CD1 LEU A 153 43.230 15.321 12.381 1.00 9.12 C ANISOU 926 CD1 LEU A 153 1022 1106 1336 -123 35 -204 C ATOM 927 CD2 LEU A 153 45.146 13.926 11.663 1.00 7.30 C ANISOU 927 CD2 LEU A 153 1069 824 880 -59 68 -147 C ATOM 928 N GLU A 154 47.794 18.061 14.037 1.00 4.29 N ANISOU 928 N GLU A 154 518 513 597 -92 122 -31 N ATOM 929 CA GLU A 154 48.623 19.259 13.905 1.00 4.37 C ANISOU 929 CA GLU A 154 467 602 591 -137 15 44 C ATOM 930 C GLU A 154 50.102 18.902 14.013 1.00 4.49 C ANISOU 930 C GLU A 154 505 650 550 -50 28 33 C ATOM 931 O GLU A 154 50.915 19.448 13.271 1.00 5.01 O ANISOU 931 O GLU A 154 499 739 663 -64 106 15 O ATOM 932 CB GLU A 154 48.238 20.292 14.954 1.00 5.14 C ANISOU 932 CB GLU A 154 623 692 636 -36 200 70 C ATOM 933 CG GLU A 154 49.002 21.584 14.824 1.00 6.36 C ANISOU 933 CG GLU A 154 799 749 865 -163 68 14 C ATOM 934 CD GLU A 154 48.646 22.665 15.800 1.00 9.45 C ANISOU 934 CD GLU A 154 1382 1004 1204 42 331 -147 C ATOM 935 OE1 GLU A 154 48.022 22.394 16.804 1.00 11.40 O ANISOU 935 OE1 GLU A 154 1471 1237 1622 -233 679 -346 O ATOM 936 OE2 GLU A 154 49.080 23.806 15.540 1.00 13.95 O ANISOU 936 OE2 GLU A 154 2121 1145 2033 -179 679 -23 O ATOM 937 N LYS A 155 50.463 17.995 14.909 1.00 4.78 N ANISOU 937 N LYS A 155 570 638 608 25 128 51 N ATOM 938 CA LYS A 155 51.861 17.548 14.987 1.00 5.43 C ANISOU 938 CA LYS A 155 530 846 686 -31 -7 -89 C ATOM 939 C LYS A 155 52.285 16.948 13.653 1.00 5.11 C ANISOU 939 C LYS A 155 616 603 721 72 86 9 C ATOM 940 O LYS A 155 53.408 17.255 13.158 1.00 6.33 O ANISOU 940 O LYS A 155 535 771 1097 101 120 102 O ATOM 941 CB LYS A 155 52.020 16.599 16.156 1.00 7.81 C ANISOU 941 CB LYS A 155 745 1004 1217 122 -2 276 C ATOM 942 CG LYS A 155 52.097 17.329 17.484 1.00 12.80 C ANISOU 942 CG LYS A 155 1471 1793 1598 131 -249 -137 C ATOM 943 CD LYS A 155 52.121 16.362 18.668 1.00 19.61 C ANISOU 943 CD LYS A 155 2842 2464 2143 -348 -311 403 C ATOM 944 CE LYS A 155 51.526 17.001 19.926 1.00 22.65 C ANISOU 944 CE LYS A 155 3005 2926 2673 -168 -208 -105 C ATOM 945 NZ LYS A 155 51.507 16.051 21.059 1.00 26.45 N ANISOU 945 NZ LYS A 155 3695 4016 2337 -228 -233 44 N ATOM 946 N LEU A 156 51.458 16.118 13.070 1.00 5.26 N ANISOU 946 N LEU A 156 548 710 739 24 148 14 N ATOM 947 CA LEU A 156 51.767 15.511 11.796 1.00 4.90 C ANISOU 947 CA LEU A 156 652 577 634 138 -83 61 C ATOM 948 C LEU A 156 51.869 16.587 10.680 1.00 5.09 C ANISOU 948 C LEU A 156 688 660 584 176 105 65 C ATOM 949 O LEU A 156 52.781 16.582 9.839 1.00 5.29 O ANISOU 949 O LEU A 156 541 625 844 87 151 71 O ATOM 950 CB LEU A 156 50.720 14.490 11.504 1.00 7.12 C ANISOU 950 CB LEU A 156 871 771 1060 -119 25 107 C ATOM 951 CG LEU A 156 50.871 13.699 10.223 1.00 8.19 C ANISOU 951 CG LEU A 156 1090 961 1058 0 -43 19 C ATOM 952 CD1 LEU A 156 52.227 12.994 10.131 1.00 10.30 C ANISOU 952 CD1 LEU A 156 1286 1248 1379 218 90 -161 C ATOM 953 CD2 LEU A 156 49.731 12.683 10.147 1.00 10.72 C ANISOU 953 CD2 LEU A 156 1540 1183 1348 -329 15 -139 C ATOM 954 N PHE A 157 50.917 17.531 10.660 1.00 4.57 N ANISOU 954 N PHE A 157 460 553 721 11 159 96 N ATOM 955 CA PHE A 157 50.943 18.660 9.733 1.00 4.41 C ANISOU 955 CA PHE A 157 566 546 560 10 -6 21 C ATOM 956 C PHE A 157 52.273 19.377 9.843 1.00 4.23 C ANISOU 956 C PHE A 157 517 534 556 46 77 47 C ATOM 957 O PHE A 157 52.898 19.650 8.794 1.00 4.97 O ANISOU 957 O PHE A 157 536 639 712 41 183 116 O ATOM 958 CB PHE A 157 49.791 19.602 10.101 1.00 4.85 C ANISOU 958 CB PHE A 157 522 658 660 32 9 22 C ATOM 959 CG PHE A 157 49.809 20.917 9.376 1.00 4.50 C ANISOU 959 CG PHE A 157 314 775 617 -30 134 121 C ATOM 960 CD1 PHE A 157 49.463 20.985 8.040 1.00 4.65 C ANISOU 960 CD1 PHE A 157 519 629 619 28 67 -91 C ATOM 961 CD2 PHE A 157 50.160 22.095 10.031 1.00 5.84 C ANISOU 961 CD2 PHE A 157 628 805 786 37 3 76 C ATOM 962 CE1 PHE A 157 49.472 22.192 7.372 1.00 6.31 C ANISOU 962 CE1 PHE A 157 803 857 737 182 38 133 C ATOM 963 CE2 PHE A 157 50.124 23.303 9.374 1.00 7.79 C ANISOU 963 CE2 PHE A 157 1270 651 1037 -31 -33 -12 C ATOM 964 CZ PHE A 157 49.809 23.335 8.047 1.00 7.59 C ANISOU 964 CZ PHE A 157 1186 715 982 165 44 172 C ATOM 965 N LEU A 158 52.733 19.673 11.053 1.00 4.37 N ANISOU 965 N LEU A 158 455 567 637 -31 102 -61 N ATOM 966 CA LEU A 158 54.000 20.409 11.171 1.00 4.92 C ANISOU 966 CA LEU A 158 516 598 755 -81 -40 68 C ATOM 967 C LEU A 158 55.178 19.592 10.683 1.00 5.27 C ANISOU 967 C LEU A 158 690 665 646 -33 0 -49 C ATOM 968 O LEU A 158 56.123 20.161 10.082 1.00 5.91 O ANISOU 968 O LEU A 158 702 748 794 40 39 141 O ATOM 969 CB LEU A 158 54.227 20.885 12.597 1.00 6.16 C ANISOU 969 CB LEU A 158 671 873 796 -71 43 -78 C ATOM 970 CG LEU A 158 53.224 21.972 13.023 1.00 7.80 C ANISOU 970 CG LEU A 158 845 973 1144 18 235 -98 C ATOM 971 CD1 LEU A 158 53.325 22.218 14.521 1.00 10.25 C ANISOU 971 CD1 LEU A 158 1281 1370 1241 -39 274 -438 C ATOM 972 CD2 LEU A 158 53.428 23.258 12.254 1.00 9.80 C ANISOU 972 CD2 LEU A 158 1197 1021 1504 96 352 35 C ATOM 973 N GLN A 159 55.156 18.274 10.895 1.00 4.70 N ANISOU 973 N GLN A 159 503 689 590 -13 198 62 N ATOM 974 CA GLN A 159 56.233 17.429 10.368 1.00 5.83 C ANISOU 974 CA GLN A 159 650 837 728 90 41 -241 C ATOM 975 C GLN A 159 56.234 17.472 8.851 1.00 5.72 C ANISOU 975 C GLN A 159 636 817 720 81 38 -74 C ATOM 976 O GLN A 159 57.307 17.503 8.238 1.00 7.32 O ANISOU 976 O GLN A 159 722 1096 963 30 197 -12 O ATOM 977 CB AGLN A 159 56.207 16.026 10.920 0.50 6.53 C ANISOU 977 CB AGLN A 159 768 856 856 402 303 -113 C ATOM 978 CB BGLN A 159 56.036 15.985 10.837 0.50 6.48 C ANISOU 978 CB BGLN A 159 698 836 928 382 299 -89 C ATOM 979 CG AGLN A 159 56.674 15.934 12.387 0.50 9.96 C ANISOU 979 CG AGLN A 159 1291 1382 1111 256 -66 112 C ATOM 980 CG BGLN A 159 56.203 15.798 12.351 0.50 9.32 C ANISOU 980 CG BGLN A 159 1126 1366 1048 361 -188 -58 C ATOM 981 CD AGLN A 159 58.079 16.539 12.715 0.50 10.07 C ANISOU 981 CD AGLN A 159 1391 1255 1180 54 110 66 C ATOM 982 CD BGLN A 159 55.861 14.413 12.864 0.50 12.93 C ANISOU 982 CD BGLN A 159 1524 1679 1709 -164 -84 128 C ATOM 983 OE1AGLN A 159 59.107 16.320 12.009 0.50 15.53 O ANISOU 983 OE1AGLN A 159 1833 3012 1054 374 571 1166 O ATOM 984 OE1BGLN A 159 54.866 13.814 12.474 0.50 15.52 O ANISOU 984 OE1BGLN A 159 1720 1752 2425 -360 -498 608 O ATOM 985 NE2AGLN A 159 58.126 17.307 13.812 0.50 13.13 N ANISOU 985 NE2AGLN A 159 1819 1692 1476 8 218 -279 N ATOM 986 NE2BGLN A 159 56.685 13.905 13.777 0.50 18.85 N ANISOU 986 NE2BGLN A 159 2154 2561 2448 146 -571 403 N ATOM 987 N LYS A 160 55.071 17.479 8.209 1.00 5.01 N ANISOU 987 N LYS A 160 647 605 649 46 30 -53 N ATOM 988 CA LYS A 160 55.045 17.511 6.719 1.00 5.49 C ANISOU 988 CA LYS A 160 664 765 654 37 99 -184 C ATOM 989 C LYS A 160 55.340 18.876 6.156 1.00 5.53 C ANISOU 989 C LYS A 160 528 864 706 96 20 24 C ATOM 990 O LYS A 160 56.071 19.018 5.175 1.00 8.35 O ANISOU 990 O LYS A 160 932 1405 835 87 276 -31 O ATOM 991 CB LYS A 160 53.716 16.980 6.202 1.00 6.56 C ANISOU 991 CB LYS A 160 756 899 838 3 -64 -173 C ATOM 992 CG LYS A 160 53.461 15.518 6.597 1.00 8.18 C ANISOU 992 CG LYS A 160 1086 1058 963 -144 -238 60 C ATOM 993 CD LYS A 160 54.586 14.566 6.173 1.00 13.45 C ANISOU 993 CD LYS A 160 1501 1641 1967 185 -34 -277 C ATOM 994 CE LYS A 160 54.298 13.113 6.483 1.00 19.09 C ANISOU 994 CE LYS A 160 2230 1961 3059 -167 115 -61 C ATOM 995 NZ LYS A 160 55.469 12.328 6.008 1.00 23.96 N ANISOU 995 NZ LYS A 160 2550 2992 3561 363 121 -482 N ATOM 996 N ILE A 161 54.857 19.908 6.810 1.00 5.32 N ANISOU 996 N ILE A 161 562 807 651 -6 69 2 N ATOM 997 CA ILE A 161 55.096 21.281 6.357 1.00 6.70 C ANISOU 997 CA ILE A 161 798 882 866 -137 1 106 C ATOM 998 C ILE A 161 56.584 21.651 6.480 1.00 5.96 C ANISOU 998 C ILE A 161 806 780 678 -148 1 164 C ATOM 999 O ILE A 161 57.074 22.462 5.700 1.00 5.97 O ANISOU 999 O ILE A 161 759 782 728 -130 154 104 O ATOM 1000 CB ILE A 161 54.221 22.321 7.133 1.00 10.73 C ANISOU 1000 CB ILE A 161 1056 1238 1782 497 318 360 C ATOM 1001 CG1 ILE A 161 52.769 22.204 6.659 1.00 13.30 C ANISOU 1001 CG1 ILE A 161 1469 1787 1794 -141 12 -44 C ATOM 1002 CG2 ILE A 161 54.785 23.764 7.087 1.00 16.96 C ANISOU 1002 CG2 ILE A 161 2419 1749 2273 -218 -254 -89 C ATOM 1003 CD1 ILE A 161 52.573 22.688 5.214 1.00 12.61 C ANISOU 1003 CD1 ILE A 161 1417 1708 1666 605 -584 -477 C ATOM 1004 N ASN A 162 57.305 20.997 7.384 1.00 5.92 N ANISOU 1004 N ASN A 162 642 833 773 -102 6 156 N ATOM 1005 CA ASN A 162 58.729 21.225 7.551 1.00 6.76 C ANISOU 1005 CA ASN A 162 682 992 894 -129 -80 -19 C ATOM 1006 C ASN A 162 59.472 21.047 6.220 1.00 7.38 C ANISOU 1006 C ASN A 162 727 1086 992 -208 18 -65 C ATOM 1007 O ASN A 162 60.453 21.769 5.951 1.00 9.78 O ANISOU 1007 O ASN A 162 750 1650 1314 -417 189 -130 O ATOM 1008 CB ASN A 162 59.217 20.285 8.631 1.00 7.77 C ANISOU 1008 CB ASN A 162 822 1122 1007 -122 -21 153 C ATOM 1009 CG ASN A 162 60.697 20.450 8.941 1.00 8.33 C ANISOU 1009 CG ASN A 162 815 1096 1251 -199 23 229 C ATOM 1010 OD1 ASN A 162 61.203 21.582 9.023 1.00 8.50 O ANISOU 1010 OD1 ASN A 162 770 1135 1323 -173 -177 245 O ATOM 1011 ND2 ASN A 162 61.368 19.321 9.179 1.00 9.52 N ANISOU 1011 ND2 ASN A 162 932 1131 1551 -47 169 121 N ATOM 1012 N GLU A 163 59.004 20.114 5.404 1.00 7.08 N ANISOU 1012 N GLU A 163 788 957 944 1 -4 -64 N ATOM 1013 CA GLU A 163 59.671 19.829 4.143 1.00 8.04 C ANISOU 1013 CA GLU A 163 818 1292 942 121 -72 -210 C ATOM 1014 C GLU A 163 58.955 20.450 2.920 1.00 7.08 C ANISOU 1014 C GLU A 163 802 855 1033 -25 -125 -208 C ATOM 1015 O GLU A 163 59.166 20.054 1.775 1.00 9.45 O ANISOU 1015 O GLU A 163 1099 1311 1180 153 -2 -391 O ATOM 1016 CB GLU A 163 59.822 18.324 4.020 1.00 11.95 C ANISOU 1016 CB GLU A 163 1491 1358 1690 344 87 -94 C ATOM 1017 CG GLU A 163 60.917 17.760 4.938 1.00 19.94 C ANISOU 1017 CG GLU A 163 2568 2947 2061 836 -496 194 C ATOM 1018 CD GLU A 163 60.723 16.307 5.367 1.00 33.72 C ANISOU 1018 CD GLU A 163 4914 3368 4529 201 -571 757 C ATOM 1019 OE1 GLU A 163 60.180 15.497 4.590 1.00 33.98 O ANISOU 1019 OE1 GLU A 163 4540 3218 5154 1322 -810 -34 O ATOM 1020 OE2 GLU A 163 61.130 15.972 6.502 1.00 43.06 O ANISOU 1020 OE2 GLU A 163 7138 4744 4477 193 -1033 454 O ATOM 1021 N LEU A 164 58.104 21.441 3.137 1.00 6.17 N ANISOU 1021 N LEU A 164 618 924 802 -63 156 87 N ATOM 1022 CA LEU A 164 57.527 22.196 2.023 1.00 6.57 C ANISOU 1022 CA LEU A 164 744 845 907 -25 34 70 C ATOM 1023 C LEU A 164 58.617 22.745 1.065 1.00 6.20 C ANISOU 1023 C LEU A 164 553 955 846 -117 -64 -84 C ATOM 1024 O LEU A 164 59.595 23.323 1.549 1.00 7.55 O ANISOU 1024 O LEU A 164 806 1061 1000 -338 -113 -125 O ATOM 1025 CB LEU A 164 56.764 23.393 2.594 1.00 5.97 C ANISOU 1025 CB LEU A 164 766 965 538 -88 140 3 C ATOM 1026 CG LEU A 164 55.966 24.241 1.618 1.00 6.70 C ANISOU 1026 CG LEU A 164 701 930 914 -1 116 88 C ATOM 1027 CD1 LEU A 164 54.741 23.486 1.090 1.00 8.24 C ANISOU 1027 CD1 LEU A 164 919 1196 1015 -159 -13 85 C ATOM 1028 CD2 LEU A 164 55.598 25.566 2.268 1.00 8.83 C ANISOU 1028 CD2 LEU A 164 975 1218 1162 137 32 -188 C ATOM 1029 N PRO A 165 58.431 22.625 -0.250 1.00 6.42 N ANISOU 1029 N PRO A 165 638 974 826 -128 139 -86 N ATOM 1030 CA PRO A 165 59.361 23.258 -1.205 1.00 7.24 C ANISOU 1030 CA PRO A 165 819 1009 922 -128 200 30 C ATOM 1031 C PRO A 165 59.498 24.740 -0.986 1.00 7.69 C ANISOU 1031 C PRO A 165 919 1019 980 -76 -35 -96 C ATOM 1032 O PRO A 165 58.584 25.390 -0.467 1.00 8.46 O ANISOU 1032 O PRO A 165 960 1094 1158 -89 5 -44 O ATOM 1033 CB PRO A 165 58.700 22.979 -2.577 1.00 8.76 C ANISOU 1033 CB PRO A 165 1167 1168 991 -96 76 -119 C ATOM 1034 CG PRO A 165 57.990 21.670 -2.352 1.00 8.11 C ANISOU 1034 CG PRO A 165 1106 1151 823 -90 57 -177 C ATOM 1035 CD PRO A 165 57.440 21.767 -0.952 1.00 6.59 C ANISOU 1035 CD PRO A 165 784 858 861 -145 65 -55 C ATOM 1036 N THR A 166 60.649 25.303 -1.387 1.00 9.30 N ANISOU 1036 N THR A 166 1126 1150 1255 -59 288 81 N ATOM 1037 CA THR A 166 60.837 26.750 -1.286 1.00 10.77 C ANISOU 1037 CA THR A 166 1494 1208 1389 -226 193 5 C ATOM 1038 C THR A 166 59.930 27.520 -2.247 1.00 11.16 C ANISOU 1038 C THR A 166 1279 1090 1868 -169 232 78 C ATOM 1039 O THR A 166 59.414 26.994 -3.249 1.00 12.94 O ANISOU 1039 O THR A 166 1950 1416 1548 31 158 260 O ATOM 1040 CB THR A 166 62.314 27.152 -1.460 1.00 13.97 C ANISOU 1040 CB THR A 166 1543 1619 2145 -206 145 247 C ATOM 1041 OG1 THR A 166 62.730 26.697 -2.725 1.00 21.05 O ANISOU 1041 OG1 THR A 166 2513 2856 2626 -144 938 -138 O ATOM 1042 CG2 THR A 166 63.144 26.514 -0.384 1.00 15.17 C ANISOU 1042 CG2 THR A 166 1526 2091 2146 -196 -4 165 C ATOM 1043 N GLU A 167 59.679 28.773 -1.875 1.00 10.01 N ANISOU 1043 N GLU A 167 973 1269 1560 -118 40 -207 N ATOM 1044 CA GLU A 167 58.866 29.670 -2.675 1.00 11.44 C ANISOU 1044 CA GLU A 167 1336 1448 1562 0 44 -26 C ATOM 1045 C GLU A 167 59.594 30.090 -3.960 1.00 14.20 C ANISOU 1045 C GLU A 167 1584 1878 1933 224 434 183 C ATOM 1046 O GLU A 167 60.781 30.462 -3.853 1.00 16.24 O ANISOU 1046 O GLU A 167 2087 2044 2038 -361 342 246 O ATOM 1047 CB GLU A 167 58.541 30.897 -1.824 1.00 12.64 C ANISOU 1047 CB GLU A 167 1828 1379 1593 -93 44 -80 C ATOM 1048 CG GLU A 167 57.543 31.823 -2.471 1.00 12.84 C ANISOU 1048 CG GLU A 167 1733 1717 1428 -144 -19 95 C ATOM 1049 CD GLU A 167 57.151 33.001 -1.611 1.00 15.50 C ANISOU 1049 CD GLU A 167 2077 1641 2170 -9 -603 -316 C ATOM 1050 OE1 GLU A 167 56.346 33.822 -2.121 1.00 15.01 O ANISOU 1050 OE1 GLU A 167 1816 1669 2216 -262 -591 -99 O ATOM 1051 OE2 GLU A 167 57.599 33.094 -0.436 1.00 14.07 O ANISOU 1051 OE2 GLU A 167 1588 1678 2079 180 -382 -319 O TER 1052 GLU A 167 ATOM 1053 N SER B 310 27.331 21.142 24.689 1.00 32.41 N ANISOU 1053 N SER B 310 3972 3527 4813 -510 474 -29 N ATOM 1054 CA SER B 310 28.532 22.036 24.610 1.00 27.21 C ANISOU 1054 CA SER B 310 3110 3858 3370 -67 26 -130 C ATOM 1055 C SER B 310 29.785 21.358 24.101 1.00 28.95 C ANISOU 1055 C SER B 310 3642 2579 4777 -173 401 -293 C ATOM 1056 O SER B 310 30.766 22.037 23.882 1.00 38.76 O ANISOU 1056 O SER B 310 4772 4450 5503 -1710 789 -897 O ATOM 1057 CB SER B 310 28.826 22.640 25.974 1.00 25.23 C ANISOU 1057 CB SER B 310 3212 2500 3873 -88 195 -523 C ATOM 1058 OG SER B 310 29.014 21.627 26.945 1.00 33.26 O ANISOU 1058 OG SER B 310 5802 3287 3548 254 824 -27 O ATOM 1059 N GLY B 311 29.789 20.039 23.945 1.00 19.71 N ANISOU 1059 N GLY B 311 2104 2503 2879 40 899 -498 N ATOM 1060 CA GLY B 311 30.866 19.359 23.248 1.00 13.74 C ANISOU 1060 CA GLY B 311 2118 1503 1597 144 277 -250 C ATOM 1061 C GLY B 311 30.384 18.246 22.354 1.00 9.11 C ANISOU 1061 C GLY B 311 1211 971 1278 330 264 206 C ATOM 1062 O GLY B 311 29.219 17.914 22.262 1.00 11.88 O ANISOU 1062 O GLY B 311 1111 1565 1834 332 540 201 O HETATM 1063 OH ALY B 312 35.346 20.937 16.487 1.00 4.79 O ANISOU 1063 OH ALY B 312 929 460 430 -132 80 92 O HETATM 1064 CH ALY B 312 35.110 20.042 15.666 1.00 4.95 C ANISOU 1064 CH ALY B 312 737 537 606 -53 11 -16 C HETATM 1065 CH3 ALY B 312 35.982 19.791 14.491 1.00 5.56 C ANISOU 1065 CH3 ALY B 312 736 780 595 -67 76 162 C HETATM 1066 NZ ALY B 312 34.034 19.262 15.726 1.00 4.48 N ANISOU 1066 NZ ALY B 312 608 549 542 15 -97 -59 N HETATM 1067 CE ALY B 312 33.041 19.342 16.810 1.00 5.07 C ANISOU 1067 CE ALY B 312 630 640 655 15 -7 150 C HETATM 1068 CD ALY B 312 33.148 18.106 17.689 1.00 4.73 C ANISOU 1068 CD ALY B 312 668 576 550 32 19 62 C HETATM 1069 CG ALY B 312 32.084 18.082 18.786 1.00 4.78 C ANISOU 1069 CG ALY B 312 581 589 645 38 21 43 C HETATM 1070 CB ALY B 312 32.154 16.736 19.522 1.00 5.14 C ANISOU 1070 CB ALY B 312 634 644 674 195 2 92 C HETATM 1071 CA ALY B 312 31.107 16.656 20.648 1.00 6.08 C ANISOU 1071 CA ALY B 312 600 839 870 -141 62 209 C HETATM 1072 N ALY B 312 31.359 17.679 21.660 1.00 6.29 N ANISOU 1072 N ALY B 312 876 803 708 -14 168 270 N HETATM 1073 C ALY B 312 31.142 15.234 21.187 1.00 5.92 C ANISOU 1073 C ALY B 312 590 798 860 61 20 113 C HETATM 1074 O ALY B 312 30.784 14.312 20.477 1.00 7.98 O ANISOU 1074 O ALY B 312 1150 800 1081 -168 -78 173 O ATOM 1075 N GLY B 313 31.597 15.059 22.430 1.00 5.58 N ANISOU 1075 N GLY B 313 762 552 804 65 128 213 N ATOM 1076 CA GLY B 313 31.621 13.734 23.046 1.00 5.42 C ANISOU 1076 CA GLY B 313 802 578 678 -20 267 215 C ATOM 1077 C GLY B 313 32.861 12.958 22.691 1.00 5.03 C ANISOU 1077 C GLY B 313 738 562 610 -28 131 89 C ATOM 1078 O GLY B 313 33.754 13.398 21.991 1.00 5.83 O ANISOU 1078 O GLY B 313 688 532 991 -29 215 102 O ATOM 1079 N LYS B 314 32.924 11.738 23.197 1.00 4.80 N ANISOU 1079 N LYS B 314 630 567 624 -24 232 132 N ATOM 1080 CA LYS B 314 34.033 10.847 22.944 1.00 4.89 C ANISOU 1080 CA LYS B 314 729 493 635 -3 154 32 C ATOM 1081 C LYS B 314 33.983 10.399 21.498 1.00 4.08 C ANISOU 1081 C LYS B 314 659 311 580 62 101 136 C ATOM 1082 O LYS B 314 32.909 10.326 20.864 1.00 5.44 O ANISOU 1082 O LYS B 314 636 644 786 -32 108 -10 O ATOM 1083 CB LYS B 314 33.992 9.660 23.895 1.00 6.85 C ANISOU 1083 CB LYS B 314 1085 657 860 7 225 221 C ATOM 1084 CG LYS B 314 34.231 10.032 25.372 1.00 8.24 C ANISOU 1084 CG LYS B 314 1319 954 855 97 295 101 C ATOM 1085 CD LYS B 314 35.673 10.349 25.728 1.00 8.79 C ANISOU 1085 CD LYS B 314 1376 968 996 123 180 191 C ATOM 1086 CE LYS B 314 35.869 10.507 27.245 1.00 10.63 C ANISOU 1086 CE LYS B 314 1720 1147 1171 92 -100 -252 C ATOM 1087 NZ LYS B 314 37.328 10.667 27.529 1.00 12.17 N ANISOU 1087 NZ LYS B 314 1750 1439 1434 25 88 77 N HETATM 1088 OH ALY B 315 33.550 15.274 15.660 1.00 6.41 O ANISOU 1088 OH ALY B 315 863 870 699 54 6 136 O HETATM 1089 CH ALY B 315 32.689 14.449 15.906 1.00 7.17 C ANISOU 1089 CH ALY B 315 1063 599 1061 76 145 -46 C HETATM 1090 CH3 ALY B 315 31.529 14.221 15.016 1.00 8.29 C ANISOU 1090 CH3 ALY B 315 1016 901 1229 113 46 233 C HETATM 1091 NZ ALY B 315 32.712 13.725 17.009 1.00 7.88 N ANISOU 1091 NZ ALY B 315 927 915 1151 -19 51 118 N HETATM 1092 CE ALY B 315 33.763 13.728 17.980 1.00 7.19 C ANISOU 1092 CE ALY B 315 943 825 963 214 122 -17 C HETATM 1093 CD ALY B 315 34.508 12.400 17.861 1.00 6.62 C ANISOU 1093 CD ALY B 315 876 701 938 87 124 7 C HETATM 1094 CG ALY B 315 35.644 12.276 18.873 1.00 5.82 C ANISOU 1094 CG ALY B 315 847 566 797 6 203 93 C HETATM 1095 CB ALY B 315 36.199 10.859 18.881 1.00 4.31 C ANISOU 1095 CB ALY B 315 529 547 560 -64 74 21 C HETATM 1096 CA ALY B 315 35.296 9.795 19.536 1.00 4.11 C ANISOU 1096 CA ALY B 315 577 517 467 -6 18 116 C HETATM 1097 N ALY B 315 35.155 10.124 20.949 1.00 3.96 N ANISOU 1097 N ALY B 315 547 459 495 -4 -15 52 N HETATM 1098 C ALY B 315 35.938 8.457 19.343 1.00 4.10 C ANISOU 1098 C ALY B 315 593 485 478 -66 68 38 C HETATM 1099 O ALY B 315 36.871 8.109 20.047 1.00 5.61 O ANISOU 1099 O ALY B 315 658 654 816 -15 -97 43 O ATOM 1100 N LYS B 316 35.466 7.729 18.335 1.00 3.83 N ANISOU 1100 N LYS B 316 436 502 516 55 10 -4 N ATOM 1101 CA LYS B 316 36.131 6.522 17.864 1.00 4.42 C ANISOU 1101 CA LYS B 316 630 509 538 133 57 50 C ATOM 1102 C LYS B 316 37.116 6.874 16.771 1.00 5.21 C ANISOU 1102 C LYS B 316 645 667 665 133 112 131 C ATOM 1103 O LYS B 316 36.877 7.792 16.003 1.00 7.64 O ANISOU 1103 O LYS B 316 1004 874 1025 495 288 369 O ATOM 1104 CB LYS B 316 35.120 5.521 17.351 1.00 5.86 C ANISOU 1104 CB LYS B 316 818 674 735 41 43 -162 C ATOM 1105 CG LYS B 316 34.078 5.145 18.382 1.00 6.39 C ANISOU 1105 CG LYS B 316 770 816 842 69 21 5 C ATOM 1106 CD LYS B 316 33.194 3.995 18.010 1.00 9.52 C ANISOU 1106 CD LYS B 316 1286 890 1439 -84 -12 -250 C ATOM 1107 CE LYS B 316 32.178 3.701 19.109 1.00 11.49 C ANISOU 1107 CE LYS B 316 1263 1349 1751 -37 153 -201 C ATOM 1108 NZ LYS B 316 31.403 2.452 18.868 1.00 16.34 N ANISOU 1108 NZ LYS B 316 1916 1732 2558 -449 180 -249 N ATOM 1109 N ARG B 317 38.224 6.163 16.696 1.00 3.50 N ANISOU 1109 N ARG B 317 452 437 439 -82 4 33 N ATOM 1110 CA ARG B 317 39.115 6.333 15.566 1.00 3.79 C ANISOU 1110 CA ARG B 317 501 462 476 -135 47 55 C ATOM 1111 C ARG B 317 38.566 5.662 14.314 1.00 4.29 C ANISOU 1111 C ARG B 317 561 562 505 -116 -75 94 C ATOM 1112 O ARG B 317 37.735 4.753 14.393 1.00 5.00 O ANISOU 1112 O ARG B 317 647 655 597 -210 -176 43 O ATOM 1113 CB ARG B 317 40.507 5.814 15.868 1.00 4.02 C ANISOU 1113 CB ARG B 317 526 472 526 -94 58 -29 C ATOM 1114 CG ARG B 317 40.574 4.339 16.212 1.00 4.13 C ANISOU 1114 CG ARG B 317 567 497 504 -87 40 37 C ATOM 1115 CD ARG B 317 41.993 3.791 16.164 1.00 4.88 C ANISOU 1115 CD ARG B 317 644 646 561 36 0 -11 C ATOM 1116 NE ARG B 317 42.336 3.519 14.760 1.00 4.13 N ANISOU 1116 NE ARG B 317 754 278 535 -110 -15 15 N ATOM 1117 CZ ARG B 317 43.427 2.907 14.390 1.00 5.78 C ANISOU 1117 CZ ARG B 317 734 618 844 -61 3 -90 C ATOM 1118 NH1 ARG B 317 43.619 2.688 13.100 1.00 7.19 N ANISOU 1118 NH1 ARG B 317 930 876 922 186 265 -77 N ATOM 1119 NH2 ARG B 317 44.322 2.540 15.276 1.00 7.33 N ANISOU 1119 NH2 ARG B 317 884 1029 868 120 -122 -302 N ATOM 1120 N GLY B 318 39.073 6.098 13.168 1.00 4.25 N ANISOU 1120 N GLY B 318 626 507 481 -71 1 4 N ATOM 1121 CA GLY B 318 38.814 5.415 11.900 1.00 4.87 C ANISOU 1121 CA GLY B 318 689 625 535 -107 -210 20 C ATOM 1122 C GLY B 318 39.762 4.240 11.701 1.00 4.75 C ANISOU 1122 C GLY B 318 735 509 560 -152 -77 94 C ATOM 1123 O GLY B 318 40.635 3.927 12.512 1.00 5.41 O ANISOU 1123 O GLY B 318 725 660 670 -17 -91 61 O ATOM 1124 N TYR B 319 39.611 3.602 10.550 1.00 6.41 N ANISOU 1124 N TYR B 319 1085 764 586 -74 -120 -18 N ATOM 1125 CA TYR B 319 40.531 2.568 10.153 1.00 8.20 C ANISOU 1125 CA TYR B 319 1209 957 949 -5 -38 -187 C ATOM 1126 C TYR B 319 41.914 3.131 9.839 1.00 10.22 C ANISOU 1126 C TYR B 319 1334 1391 1156 88 493 -42 C ATOM 1127 O TYR B 319 42.003 4.259 9.368 1.00 14.62 O ANISOU 1127 O TYR B 319 1976 1720 1858 -391 127 387 O ATOM 1128 CB TYR B 319 39.934 1.802 8.967 1.00 7.57 C ANISOU 1128 CB TYR B 319 1184 858 833 -48 2 -79 C ATOM 1129 CG TYR B 319 38.709 0.983 9.351 1.00 6.92 C ANISOU 1129 CG TYR B 319 1194 925 509 -171 -110 -374 C ATOM 1130 CD1 TYR B 319 38.823 -0.300 9.889 1.00 8.59 C ANISOU 1130 CD1 TYR B 319 1138 1254 869 -126 -311 42 C ATOM 1131 CD2 TYR B 319 37.445 1.519 9.227 1.00 8.10 C ANISOU 1131 CD2 TYR B 319 1329 932 817 -45 -110 -214 C ATOM 1132 CE1 TYR B 319 37.699 -1.015 10.266 1.00 8.34 C ANISOU 1132 CE1 TYR B 319 1314 1225 629 -272 -305 -77 C ATOM 1133 CE2 TYR B 319 36.320 0.835 9.615 1.00 10.27 C ANISOU 1133 CE2 TYR B 319 1190 1533 1178 -174 -322 -147 C ATOM 1134 CZ TYR B 319 36.450 -0.419 10.151 1.00 9.36 C ANISOU 1134 CZ TYR B 319 1357 1436 762 -186 -250 -244 C ATOM 1135 OH TYR B 319 35.321 -1.101 10.512 1.00 12.64 O ANISOU 1135 OH TYR B 319 1326 2099 1377 -383 -42 -331 O ATOM 1136 OXT TYR B 319 42.914 2.465 10.183 1.00 19.04 O ANISOU 1136 OXT TYR B 319 1752 2331 3150 604 268 536 O TER 1137 TYR B 319 HETATM 1138 C1 EDO A 201 53.159 26.249 9.712 1.00 18.23 C ANISOU 1138 C1 EDO A 201 1902 2457 2565 540 35 -405 C HETATM 1139 O1 EDO A 201 52.160 27.051 10.381 1.00 14.29 O ANISOU 1139 O1 EDO A 201 1183 2285 1962 211 -147 -71 O HETATM 1140 C2 EDO A 201 54.581 26.716 10.057 1.00 18.75 C ANISOU 1140 C2 EDO A 201 1749 2894 2480 338 515 -119 C HETATM 1141 O2 EDO A 201 54.663 28.120 9.768 1.00 20.60 O ANISOU 1141 O2 EDO A 201 2475 3049 2302 -589 686 -593 O HETATM 1142 O HOH A 301 22.842 31.345 17.626 1.00 40.50 O ANISOU 1142 O HOH A 301 4733 6108 4547 402 1319 -493 O HETATM 1143 O HOH A 302 37.430 17.203 28.428 1.00 32.34 O ANISOU 1143 O HOH A 302 4734 7245 307 2368 275 608 O HETATM 1144 O HOH A 303 43.322 33.112 -3.754 1.00 16.77 O ANISOU 1144 O HOH A 303 1777 2787 1807 -376 -163 981 O HETATM 1145 O HOH A 304 19.930 19.780 16.375 1.00 21.23 O ANISOU 1145 O HOH A 304 2192 3887 1984 565 594 131 O HETATM 1146 O HOH A 305 36.095 23.314 15.355 1.00 3.76 O ANISOU 1146 O HOH A 305 481 429 518 -70 -129 -7 O HETATM 1147 O HOH A 306 38.234 8.224 24.117 1.00 9.38 O ANISOU 1147 O HOH A 306 1800 645 1117 91 330 -7 O HETATM 1148 O HOH A 307 39.069 12.768 26.192 1.00 16.51 O ANISOU 1148 O HOH A 307 3366 1165 1741 -154 96 68 O HETATM 1149 O HOH A 308 35.752 35.114 9.074 1.00 20.34 O ANISOU 1149 O HOH A 308 2202 2883 2640 -342 -570 780 O HETATM 1150 O HOH A 309 44.080 31.376 -7.385 1.00 10.55 O ANISOU 1150 O HOH A 309 1303 1684 1019 -473 -134 397 O HETATM 1151 O HOH A 310 47.371 25.825 15.890 1.00 23.95 O ANISOU 1151 O HOH A 310 3315 2401 3383 718 206 -190 O HETATM 1152 O HOH A 311 28.658 30.711 -0.353 1.00 14.04 O ANISOU 1152 O HOH A 311 1525 2080 1727 478 -379 -75 O HETATM 1153 O HOH A 312 60.837 23.528 -5.724 1.00 24.01 O ANISOU 1153 O HOH A 312 2237 2916 3970 -214 920 -725 O HETATM 1154 O HOH A 313 34.173 18.246 22.089 1.00 5.63 O ANISOU 1154 O HOH A 313 793 587 758 -97 222 152 O HETATM 1155 O HOH A 314 48.332 15.903 22.488 1.00 21.76 O ANISOU 1155 O HOH A 314 4093 1911 2262 -104 -1638 -255 O HETATM 1156 O HOH A 315 48.688 9.354 7.574 1.00 21.16 O ANISOU 1156 O HOH A 315 2340 1686 4013 330 298 1109 O HETATM 1157 O HOH A 316 33.399 23.837 1.372 1.00 11.84 O ANISOU 1157 O HOH A 316 1474 1292 1730 86 -78 162 O HETATM 1158 O HOH A 317 61.057 23.409 3.823 1.00 24.80 O ANISOU 1158 O HOH A 317 3038 4045 2341 -1781 -1225 820 O HETATM 1159 O HOH A 318 26.185 16.344 8.242 1.00 29.90 O ANISOU 1159 O HOH A 318 4026 3654 3680 1468 -1385 -1417 O HETATM 1160 O HOH A 319 60.292 18.585 -0.208 1.00 24.18 O ANISOU 1160 O HOH A 319 2278 4349 2561 922 416 -1413 O HETATM 1161 O HOH A 320 47.405 24.747 -8.390 1.00 13.24 O ANISOU 1161 O HOH A 320 1608 2112 1309 -451 381 355 O HETATM 1162 O HOH A 321 53.438 30.383 -2.479 1.00 10.88 O ANISOU 1162 O HOH A 321 882 1527 1721 232 394 638 O HETATM 1163 O HOH A 322 40.504 29.932 14.442 1.00 5.39 O ANISOU 1163 O HOH A 322 633 520 896 0 -123 0 O HETATM 1164 O HOH A 323 40.187 30.996 3.809 1.00 15.03 O ANISOU 1164 O HOH A 323 2632 1230 1849 212 -968 -376 O HETATM 1165 O HOH A 324 29.948 27.703 -0.616 1.00 15.64 O ANISOU 1165 O HOH A 324 2963 1615 1363 -204 -925 77 O HETATM 1166 O HOH A 325 31.253 28.247 6.261 1.00 5.33 O ANISOU 1166 O HOH A 325 566 767 692 183 5 22 O HETATM 1167 O HOH A 326 33.760 31.265 -5.291 1.00 17.09 O ANISOU 1167 O HOH A 326 1576 2423 2494 160 765 696 O HETATM 1168 O HOH A 327 46.375 23.656 -6.090 1.00 6.62 O ANISOU 1168 O HOH A 327 801 849 865 14 240 -49 O HETATM 1169 O HOH A 328 52.016 26.582 13.067 1.00 14.90 O ANISOU 1169 O HOH A 328 2081 1803 1776 -297 276 -285 O HETATM 1170 O HOH A 329 29.244 18.660 7.002 1.00 9.26 O ANISOU 1170 O HOH A 329 1094 1108 1316 -67 -387 -66 O HETATM 1171 O HOH A 330 33.785 20.792 24.823 1.00 11.84 O ANISOU 1171 O HOH A 330 1180 1492 1825 -489 310 32 O HETATM 1172 O HOH A 331 41.768 31.545 -14.292 1.00 28.01 O ANISOU 1172 O HOH A 331 4241 4062 2336 -200 -32 -13 O HETATM 1173 O HOH A 332 32.263 26.038 23.677 1.00 24.06 O ANISOU 1173 O HOH A 332 2723 3799 2620 1275 395 -198 O HETATM 1174 O HOH A 333 37.103 27.342 -10.931 1.00 20.80 O ANISOU 1174 O HOH A 333 2807 2791 2302 18 -447 246 O HETATM 1175 O HOH A 334 25.851 28.870 16.503 1.00 17.48 O ANISOU 1175 O HOH A 334 1317 2765 2558 370 -51 760 O HETATM 1176 O HOH A 335 33.886 16.995 2.651 1.00 22.40 O ANISOU 1176 O HOH A 335 3016 3018 2477 -744 -470 637 O HETATM 1177 O HOH A 336 36.958 21.473 11.174 1.00 9.85 O ANISOU 1177 O HOH A 336 1331 1525 886 -1004 -407 525 O HETATM 1178 O HOH A 337 50.918 19.600 -14.993 1.00 31.75 O ANISOU 1178 O HOH A 337 1529 4255 6280 349 108 -1655 O HETATM 1179 O HOH A 338 50.806 12.848 15.306 1.00 11.26 O ANISOU 1179 O HOH A 338 1427 1551 1297 559 83 216 O HETATM 1180 O HOH A 339 22.311 25.518 6.438 1.00 12.41 O ANISOU 1180 O HOH A 339 1644 1399 1670 -344 -186 162 O HETATM 1181 O HOH A 340 41.782 30.497 7.180 1.00 10.22 O ANISOU 1181 O HOH A 340 1755 1192 936 66 -69 25 O HETATM 1182 O HOH A 341 59.769 16.835 9.311 1.00 11.64 O ANISOU 1182 O HOH A 341 983 1275 2164 -146 -89 253 O HETATM 1183 O HOH A 342 37.438 33.622 13.214 1.00 23.53 O ANISOU 1183 O HOH A 342 4211 2292 2437 -541 -821 375 O HETATM 1184 O HOH A 343 37.815 22.808 13.252 1.00 10.10 O ANISOU 1184 O HOH A 343 922 1481 1431 -658 869 -766 O HETATM 1185 O HOH A 344 47.213 14.073 20.818 1.00 9.96 O ANISOU 1185 O HOH A 344 1092 1238 1452 -44 20 -231 O HETATM 1186 O HOH A 345 43.792 35.239 -0.127 1.00 22.14 O ANISOU 1186 O HOH A 345 1945 2187 4280 377 55 -882 O HETATM 1187 O HOH A 346 35.599 24.676 11.743 1.00 5.63 O ANISOU 1187 O HOH A 346 1017 541 580 39 86 7 O HETATM 1188 O HOH A 347 50.060 10.392 14.192 1.00 23.46 O ANISOU 1188 O HOH A 347 2914 2842 3157 435 -1128 0 O HETATM 1189 O HOH A 348 36.673 8.719 6.492 1.00 19.13 O ANISOU 1189 O HOH A 348 2800 1546 2919 -623 -351 -376 O HETATM 1190 O HOH A 349 36.849 30.915 13.664 1.00 8.28 O ANISOU 1190 O HOH A 349 807 964 1374 229 -280 183 O HETATM 1191 O HOH A 350 40.809 23.515 23.775 1.00 4.50 O ANISOU 1191 O HOH A 350 616 481 611 173 -45 159 O HETATM 1192 O HOH A 351 50.237 24.488 13.092 1.00 14.43 O ANISOU 1192 O HOH A 351 1307 1930 2243 101 7 316 O HETATM 1193 O HOH A 352 57.787 15.049 2.892 1.00 22.07 O ANISOU 1193 O HOH A 352 2869 2691 2824 583 -364 -76 O HETATM 1194 O HOH A 353 28.018 36.148 17.593 1.00 31.92 O ANISOU 1194 O HOH A 353 2844 6694 2588 933 719 -2560 O HETATM 1195 O HOH A 354 35.269 19.401 10.778 1.00 5.92 O ANISOU 1195 O HOH A 354 930 511 806 10 -170 -9 O HETATM 1196 O HOH A 355 54.191 15.259 21.178 1.00 37.24 O ANISOU 1196 O HOH A 355 4461 7320 2367 -204 611 309 O HETATM 1197 O HOH A 356 22.608 29.718 6.999 1.00 8.84 O ANISOU 1197 O HOH A 356 894 1018 1444 190 -138 114 O HETATM 1198 O HOH A 357 34.052 24.399 7.316 1.00 5.09 O ANISOU 1198 O HOH A 357 754 514 665 -159 82 94 O HETATM 1199 O HOH A 358 42.045 14.410 28.197 1.00 20.75 O ANISOU 1199 O HOH A 358 2756 2827 2299 1134 -489 195 O HETATM 1200 O HOH A 359 46.114 28.663 -8.439 1.00 10.35 O ANISOU 1200 O HOH A 359 1236 1852 843 -76 432 250 O HETATM 1201 O HOH A 360 38.328 29.559 -15.205 1.00 35.85 O ANISOU 1201 O HOH A 360 5177 4029 4414 -206 1732 -1888 O HETATM 1202 O HOH A 361 47.679 21.296 -5.484 1.00 11.12 O ANISOU 1202 O HOH A 361 1746 950 1526 120 -603 -343 O HETATM 1203 O HOH A 362 34.316 11.696 7.044 1.00 16.11 O ANISOU 1203 O HOH A 362 1495 1441 3182 5 -489 -51 O HETATM 1204 O HOH A 363 33.179 33.683 -9.915 1.00 15.15 O ANISOU 1204 O HOH A 363 2162 1509 2085 6 158 -14 O HETATM 1205 O HOH A 364 22.447 23.044 17.039 1.00 28.18 O ANISOU 1205 O HOH A 364 3634 4182 2889 1151 464 877 O HETATM 1206 O HOH A 365 27.972 22.938 8.392 1.00 6.14 O ANISOU 1206 O HOH A 365 609 779 942 10 67 267 O HETATM 1207 O HOH A 366 57.126 18.269 -3.928 1.00 26.16 O ANISOU 1207 O HOH A 366 4038 2741 3159 -226 -787 980 O HETATM 1208 O HOH A 367 46.942 18.228 25.481 1.00 26.38 O ANISOU 1208 O HOH A 367 3702 4100 2219 -293 -263 167 O HETATM 1209 O HOH A 368 57.237 25.247 6.145 1.00 13.35 O ANISOU 1209 O HOH A 368 1738 1467 1866 140 -214 -462 O HETATM 1210 O HOH A 369 56.885 22.836 10.590 1.00 12.15 O ANISOU 1210 O HOH A 369 1751 1379 1484 -580 357 -151 O HETATM 1211 O HOH A 370 32.108 25.111 -1.652 1.00 18.30 O ANISOU 1211 O HOH A 370 2567 2134 2249 170 -97 -189 O HETATM 1212 O HOH A 371 57.086 25.768 -8.254 1.00 11.96 O ANISOU 1212 O HOH A 371 1639 1122 1779 -606 345 -54 O HETATM 1213 O HOH A 372 39.111 28.352 -8.106 1.00 11.43 O ANISOU 1213 O HOH A 372 1111 1822 1408 201 128 598 O HETATM 1214 O HOH A 373 33.667 17.832 27.855 1.00 23.01 O ANISOU 1214 O HOH A 373 2708 3976 2058 -419 451 -102 O HETATM 1215 O HOH A 374 45.253 26.068 -5.320 1.00 7.34 O ANISOU 1215 O HOH A 374 882 843 1063 -185 66 19 O HETATM 1216 O HOH A 375 25.238 24.381 5.190 1.00 17.65 O ANISOU 1216 O HOH A 375 2771 2200 1735 -1390 157 -165 O HETATM 1217 O HOH A 376 35.814 13.838 24.685 1.00 13.66 O ANISOU 1217 O HOH A 376 1591 1327 2271 -671 712 -154 O HETATM 1218 O HOH A 377 54.124 29.655 3.267 1.00 33.73 O ANISOU 1218 O HOH A 377 3107 5475 4232 538 216 116 O HETATM 1219 O HOH A 378 41.025 8.548 7.492 1.00 18.71 O ANISOU 1219 O HOH A 378 2569 1918 2620 10 256 -594 O HETATM 1220 O HOH A 379 52.459 35.555 -5.204 1.00 9.50 O ANISOU 1220 O HOH A 379 896 1006 1706 -230 233 275 O HETATM 1221 O HOH A 380 32.666 27.324 -4.477 1.00 11.12 O ANISOU 1221 O HOH A 380 1191 1664 1367 144 -345 46 O HETATM 1222 O HOH A 381 28.845 24.710 6.486 1.00 5.30 O ANISOU 1222 O HOH A 381 675 640 698 21 -45 106 O HETATM 1223 O HOH A 382 48.710 32.596 7.926 1.00 19.67 O ANISOU 1223 O HOH A 382 2574 2335 2565 -305 -129 -456 O HETATM 1224 O HOH A 383 63.119 22.412 6.733 1.00 11.70 O ANISOU 1224 O HOH A 383 1148 1775 1519 -440 -112 115 O HETATM 1225 O HOH A 384 37.395 16.486 -3.052 1.00 18.62 O ANISOU 1225 O HOH A 384 2850 2028 2195 -131 401 -304 O HETATM 1226 O HOH A 385 55.450 18.229 14.906 1.00 14.35 O ANISOU 1226 O HOH A 385 1353 2317 1779 77 66 385 O HETATM 1227 O HOH A 386 41.308 32.308 10.807 1.00 16.74 O ANISOU 1227 O HOH A 386 3093 1405 1863 353 -43 -122 O HETATM 1228 O HOH A 387 42.156 31.600 -0.294 1.00 21.18 O ANISOU 1228 O HOH A 387 2207 2206 3635 14 -86 -114 O HETATM 1229 O HOH A 388 52.098 28.596 -4.630 1.00 12.03 O ANISOU 1229 O HOH A 388 1286 1505 1778 50 66 -279 O HETATM 1230 O HOH A 389 54.409 32.586 -3.828 1.00 17.02 O ANISOU 1230 O HOH A 389 2287 1725 2454 -245 -1058 466 O HETATM 1231 O HOH A 390 33.150 33.313 -14.820 1.00 30.02 O ANISOU 1231 O HOH A 390 4005 4553 2846 400 -692 -365 O HETATM 1232 O HOH A 391 53.644 28.139 -12.565 1.00 24.57 O ANISOU 1232 O HOH A 391 4550 1827 2955 -135 -128 1104 O HETATM 1233 O HOH A 392 49.076 20.944 -9.608 1.00 26.52 O ANISOU 1233 O HOH A 392 4337 2811 2929 -439 926 -131 O HETATM 1234 O HOH A 393 29.873 17.520 10.809 1.00 13.41 O ANISOU 1234 O HOH A 393 1783 1590 1719 380 -317 -7 O HETATM 1235 O HOH A 394 37.297 31.802 16.370 1.00 13.24 O ANISOU 1235 O HOH A 394 1941 1393 1695 -59 215 -414 O HETATM 1236 O HOH A 395 55.247 25.303 -11.807 1.00 17.83 O ANISOU 1236 O HOH A 395 2247 2256 2271 564 549 968 O HETATM 1237 O HOH A 396 35.193 30.394 6.629 1.00 9.62 O ANISOU 1237 O HOH A 396 1162 1139 1354 -103 -108 313 O HETATM 1238 O HOH A 397 51.728 29.680 9.308 1.00 15.93 O ANISOU 1238 O HOH A 397 2402 1668 1981 -376 -388 404 O HETATM 1239 O HOH A 398 54.284 29.218 7.059 1.00 10.66 O ANISOU 1239 O HOH A 398 1313 1225 1512 -153 -268 186 O HETATM 1240 O HOH A 399 63.241 29.187 -4.620 1.00 36.67 O ANISOU 1240 O HOH A 399 5192 5261 3477 411 344 -724 O HETATM 1241 O HOH A 400 47.998 21.824 -12.639 1.00 42.35 O ANISOU 1241 O HOH A 400 5979 4959 5151 1381 -720 -2527 O HETATM 1242 O HOH A 401 36.932 17.254 -0.432 1.00 13.29 O ANISOU 1242 O HOH A 401 2013 1204 1830 -273 -226 -197 O HETATM 1243 O HOH A 402 31.011 24.832 9.900 1.00 10.65 O ANISOU 1243 O HOH A 402 1676 1119 1252 364 -237 -256 O HETATM 1244 O HOH A 403 59.859 26.064 2.381 1.00 18.51 O ANISOU 1244 O HOH A 403 2602 2281 2148 -813 -217 -167 O HETATM 1245 O HOH A 404 40.521 25.168 -11.899 1.00 19.56 O ANISOU 1245 O HOH A 404 2855 2832 1744 -106 -249 -133 O HETATM 1246 O HOH A 405 38.328 23.658 -11.243 1.00 25.91 O ANISOU 1246 O HOH A 405 3561 4190 2094 -1247 -563 232 O HETATM 1247 O HOH A 406 24.927 19.923 6.756 1.00 14.55 O ANISOU 1247 O HOH A 406 1282 1826 2420 95 34 -27 O HETATM 1248 O HOH A 407 49.794 14.118 19.772 1.00 18.80 O ANISOU 1248 O HOH A 407 1469 2976 2695 -104 -49 223 O HETATM 1249 O HOH A 408 49.785 19.711 18.391 1.00 22.15 O ANISOU 1249 O HOH A 408 2394 3776 2245 -1303 150 -355 O HETATM 1250 O HOH A 409 45.094 29.695 13.061 1.00 8.29 O ANISOU 1250 O HOH A 409 1312 948 890 -276 286 -385 O HETATM 1251 O HOH A 410 51.288 27.464 -13.542 1.00 15.73 O ANISOU 1251 O HOH A 410 2489 2104 1381 403 947 453 O HETATM 1252 O HOH A 411 34.563 23.623 -10.033 1.00 35.21 O ANISOU 1252 O HOH A 411 3643 5659 4075 -1330 -651 -1128 O HETATM 1253 O HOH A 412 60.764 29.813 0.606 1.00 17.94 O ANISOU 1253 O HOH A 412 2402 2277 2134 327 -633 -163 O HETATM 1254 O HOH A 413 48.778 6.686 11.108 1.00 36.17 O ANISOU 1254 O HOH A 413 2508 4955 6277 860 1354 804 O HETATM 1255 O HOH A 414 56.196 28.846 -4.923 1.00 16.65 O ANISOU 1255 O HOH A 414 2174 2174 1976 401 -108 -491 O HETATM 1256 O HOH A 415 41.147 29.482 -9.791 1.00 13.22 O ANISOU 1256 O HOH A 415 1412 1394 2214 226 170 270 O HETATM 1257 O HOH A 416 33.877 27.392 23.505 1.00 18.94 O ANISOU 1257 O HOH A 416 2757 2138 2302 134 -392 -482 O HETATM 1258 O HOH A 417 21.495 24.226 8.791 1.00 8.00 O ANISOU 1258 O HOH A 417 766 1066 1206 -231 -15 80 O HETATM 1259 O HOH A 418 34.083 31.382 1.271 1.00 13.10 O ANISOU 1259 O HOH A 418 1590 1235 2152 63 38 -399 O HETATM 1260 O HOH A 419 44.701 10.246 1.480 1.00 25.71 O ANISOU 1260 O HOH A 419 2863 3006 3897 -431 23 224 O HETATM 1261 O HOH A 420 33.602 23.589 9.905 1.00 7.87 O ANISOU 1261 O HOH A 420 1386 857 745 -355 138 126 O HETATM 1262 O HOH A 421 42.934 31.067 2.711 1.00 21.10 O ANISOU 1262 O HOH A 421 2283 2169 3563 826 1123 -258 O HETATM 1263 O HOH A 422 37.572 35.385 -15.635 1.00 35.44 O ANISOU 1263 O HOH A 422 4466 4591 4406 303 354 -874 O HETATM 1264 O HOH A 423 51.090 17.656 -12.470 1.00 27.60 O ANISOU 1264 O HOH A 423 2941 4080 3464 488 322 -892 O HETATM 1265 O HOH A 424 52.967 31.694 0.341 1.00 8.57 O ANISOU 1265 O HOH A 424 969 920 1366 -55 235 -31 O HETATM 1266 O HOH A 425 45.567 14.262 -2.049 1.00 25.99 O ANISOU 1266 O HOH A 425 2847 2913 4114 -543 -395 -67 O HETATM 1267 O HOH A 426 35.574 32.770 -4.002 1.00 20.23 O ANISOU 1267 O HOH A 426 2508 2347 2830 272 277 26 O HETATM 1268 O HOH A 427 45.117 30.712 10.560 1.00 11.65 O ANISOU 1268 O HOH A 427 1621 1386 1418 -547 -84 67 O HETATM 1269 O HOH A 428 45.723 32.253 -14.722 1.00 16.11 O ANISOU 1269 O HOH A 428 2166 2503 1452 -31 424 385 O HETATM 1270 O HOH A 429 39.675 8.792 10.144 1.00 8.47 O ANISOU 1270 O HOH A 429 1238 563 1415 169 57 -79 O HETATM 1271 O HOH A 430 39.271 8.557 4.977 1.00 24.45 O ANISOU 1271 O HOH A 430 4159 1699 3430 332 82 -414 O HETATM 1272 O HOH A 431 31.696 36.558 -13.402 1.00 18.21 O ANISOU 1272 O HOH A 431 1545 2603 2771 393 -277 231 O HETATM 1273 O HOH A 432 43.943 20.076 25.117 1.00 16.13 O ANISOU 1273 O HOH A 432 2059 2160 1910 237 -575 -125 O HETATM 1274 O HOH A 433 40.092 33.527 -1.085 1.00 18.10 O ANISOU 1274 O HOH A 433 2675 1829 2373 -536 165 3 O HETATM 1275 O HOH A 434 62.320 23.348 -3.040 1.00 23.71 O ANISOU 1275 O HOH A 434 2253 2567 4186 212 1645 -493 O HETATM 1276 O HOH A 435 32.087 16.245 11.619 1.00 11.86 O ANISOU 1276 O HOH A 435 1501 1776 1226 426 -173 -69 O HETATM 1277 O HOH A 436 30.480 30.155 21.558 1.00 19.56 O ANISOU 1277 O HOH A 436 2125 2723 2582 -438 -648 -537 O HETATM 1278 O HOH A 437 55.776 30.185 0.987 1.00 29.21 O ANISOU 1278 O HOH A 437 5576 2453 3068 822 -980 -1052 O HETATM 1279 O HOH A 438 56.905 26.213 -5.510 1.00 10.67 O ANISOU 1279 O HOH A 438 1610 931 1511 -184 191 137 O HETATM 1280 O HOH A 439 40.937 33.129 6.857 1.00 19.83 O ANISOU 1280 O HOH A 439 3547 1863 2123 -31 437 -348 O HETATM 1281 O HOH A 440 56.339 12.757 3.015 1.00 30.25 O ANISOU 1281 O HOH A 440 4238 1939 5314 1133 704 44 O HETATM 1282 O HOH A 441 31.100 28.343 23.433 1.00 20.96 O ANISOU 1282 O HOH A 441 3434 2026 2500 294 -242 -175 O HETATM 1283 O HOH A 442 53.730 10.381 7.897 1.00 35.68 O ANISOU 1283 O HOH A 442 4668 3611 5277 1799 975 399 O HETATM 1284 O HOH A 443 49.806 23.188 -8.106 1.00 12.72 O ANISOU 1284 O HOH A 443 1780 1756 1297 131 243 177 O HETATM 1285 O HOH A 444 45.308 20.792 -8.706 1.00 40.77 O ANISOU 1285 O HOH A 444 4193 7636 3661 -152 1108 -2279 O HETATM 1286 O HOH A 445 31.898 22.454 -0.490 1.00 23.58 O ANISOU 1286 O HOH A 445 3385 2264 3308 -141 342 -673 O HETATM 1287 O HOH A 446 34.897 12.073 3.883 1.00 26.30 O ANISOU 1287 O HOH A 446 3482 3680 2828 -15 144 -703 O HETATM 1288 O HOH A 447 34.919 7.145 11.397 1.00 75.43 O ANISOU 1288 O HOH A 447 9919 9046 9693 -3155 -2767 -160 O HETATM 1289 O HOH A 448 47.887 30.773 9.994 1.00 13.82 O ANISOU 1289 O HOH A 448 1632 1991 1628 -640 -210 -88 O HETATM 1290 O HOH A 449 39.717 27.818 -11.490 1.00 20.12 O ANISOU 1290 O HOH A 449 2928 2183 2533 260 -202 -128 O HETATM 1291 O HOH A 450 32.802 31.749 -7.973 1.00 23.94 O ANISOU 1291 O HOH A 450 2986 3270 2837 155 558 214 O HETATM 1292 O HOH A 451 47.810 6.918 8.245 1.00 24.85 O ANISOU 1292 O HOH A 451 2843 2318 4281 202 1349 772 O HETATM 1293 O HOH A 452 60.205 28.106 -7.923 1.00 32.77 O ANISOU 1293 O HOH A 452 4773 4509 3165 -1964 -541 -1370 O HETATM 1294 O HOH A 453 45.525 35.163 3.459 1.00 30.34 O ANISOU 1294 O HOH A 453 3350 5050 3125 -375 1337 452 O HETATM 1295 O HOH A 454 53.515 25.020 -14.105 1.00 27.73 O ANISOU 1295 O HOH A 454 3538 3106 3892 425 447 592 O HETATM 1296 O HOH A 455 56.490 27.262 -10.464 1.00 27.27 O ANISOU 1296 O HOH A 455 3798 4181 2382 -1393 -526 436 O HETATM 1297 O HOH A 456 54.337 16.591 -4.742 1.00 32.83 O ANISOU 1297 O HOH A 456 4120 2218 6133 -287 2840 -678 O HETATM 1298 O HOH A 457 57.967 24.534 8.803 1.00 10.30 O ANISOU 1298 O HOH A 457 1186 1186 1541 -314 35 -148 O HETATM 1299 O HOH A 458 49.295 30.915 12.451 1.00 16.36 O ANISOU 1299 O HOH A 458 2001 2476 1736 -648 475 -312 O HETATM 1300 O HOH A 459 30.945 13.634 11.549 1.00 20.25 O ANISOU 1300 O HOH A 459 3162 1992 2537 -226 -1125 460 O HETATM 1301 O HOH A 460 34.562 39.146 -14.563 1.00 26.97 O ANISOU 1301 O HOH A 460 3088 3745 3413 655 799 -537 O HETATM 1302 O HOH A 461 43.146 33.983 2.607 1.00 29.59 O ANISOU 1302 O HOH A 461 3313 3755 4174 143 -30 -551 O HETATM 1303 O HOH A 462 33.493 14.419 26.146 1.00 27.67 O ANISOU 1303 O HOH A 462 3018 4564 2929 -215 366 -249 O HETATM 1304 O HOH A 463 57.036 20.894 15.277 1.00 30.21 O ANISOU 1304 O HOH A 463 2957 4542 3979 1144 -438 -1736 O HETATM 1305 O HOH A 464 44.373 33.385 10.441 1.00 21.29 O ANISOU 1305 O HOH A 464 3256 2163 2671 507 -39 116 O HETATM 1306 O HOH A 465 31.661 33.046 -12.185 1.00 27.27 O ANISOU 1306 O HOH A 465 2888 3827 3642 -261 -430 -302 O HETATM 1307 O HOH A 466 51.515 9.467 11.956 1.00 36.83 O ANISOU 1307 O HOH A 466 4776 4190 5026 1608 1876 1224 O HETATM 1308 O HOH A 467 43.760 17.910 -8.711 1.00 40.03 O ANISOU 1308 O HOH A 467 5575 6059 3576 1051 335 -2173 O HETATM 1309 O HOH A 468 28.151 22.525 4.802 1.00 11.36 O ANISOU 1309 O HOH A 468 1405 1415 1495 -304 -176 217 O HETATM 1310 O HOH A 469 27.499 20.749 6.810 1.00 9.71 O ANISOU 1310 O HOH A 469 1104 1114 1469 -118 -234 8 O HETATM 1311 O HOH A 470 43.318 36.698 -13.911 1.00 19.70 O ANISOU 1311 O HOH A 470 3028 2828 1629 1017 -432 -465 O HETATM 1312 O HOH A 471 51.150 9.400 9.032 1.00 27.68 O ANISOU 1312 O HOH A 471 3224 2164 5126 526 -718 332 O HETATM 1313 O HOH A 472 31.364 25.633 7.230 1.00 6.05 O ANISOU 1313 O HOH A 472 565 802 930 -54 1 133 O HETATM 1314 O HOH A 473 40.652 36.542 -4.907 1.00 17.16 O ANISOU 1314 O HOH A 473 2071 2410 2039 389 318 -181 O HETATM 1315 O HOH A 474 66.566 27.047 -0.979 1.00 21.34 O ANISOU 1315 O HOH A 474 2364 3179 2565 90 -405 -268 O HETATM 1316 O HOH A 475 55.036 14.497 17.645 1.00 37.21 O ANISOU 1316 O HOH A 475 2350 4702 7084 635 -583 243 O HETATM 1317 O HOH A 476 56.033 28.938 3.803 1.00 38.29 O ANISOU 1317 O HOH A 476 5123 3075 6350 516 617 -887 O HETATM 1318 O HOH A 477 37.303 31.269 4.911 1.00 27.80 O ANISOU 1318 O HOH A 477 3614 3865 3081 -105 1099 1043 O HETATM 1319 O HOH A 478 33.359 6.219 13.662 1.00 29.83 O ANISOU 1319 O HOH A 478 3415 3562 4357 1374 616 1337 O HETATM 1320 O HOH A 479 28.301 15.779 9.533 1.00 36.32 O ANISOU 1320 O HOH A 479 2913 2516 8369 -28 -2058 -1451 O HETATM 1321 O HOH A 480 24.272 31.832 6.332 1.00 10.43 O ANISOU 1321 O HOH A 480 1178 1401 1381 -76 3 402 O HETATM 1322 O HOH A 481 26.261 29.612 -0.960 1.00 16.81 O ANISOU 1322 O HOH A 481 2022 1909 2455 -48 -470 97 O HETATM 1323 O HOH A 482 47.893 19.558 -7.521 1.00 20.11 O ANISOU 1323 O HOH A 482 2981 2832 1825 -331 429 -617 O HETATM 1324 O HOH A 483 48.439 28.168 15.726 1.00 24.62 O ANISOU 1324 O HOH A 483 3156 3066 3131 -75 490 -220 O HETATM 1325 O HOH A 484 18.001 19.313 13.345 1.00 30.46 O ANISOU 1325 O HOH A 484 2080 4795 4698 -163 -87 422 O HETATM 1326 O HOH A 485 66.026 24.402 -0.864 1.00 32.05 O ANISOU 1326 O HOH A 485 3979 3845 4354 -442 -1185 -165 O HETATM 1327 O HOH A 486 35.076 15.446 0.373 1.00 25.89 O ANISOU 1327 O HOH A 486 3327 4643 1867 -1903 -780 426 O HETATM 1328 O HOH A 487 24.693 31.134 15.357 1.00 21.55 O ANISOU 1328 O HOH A 487 3112 2616 2460 726 545 1080 O HETATM 1329 O HOH A 488 55.711 27.487 5.427 1.00 20.83 O ANISOU 1329 O HOH A 488 2314 3133 2467 914 -1060 -1034 O HETATM 1330 O HOH A 489 59.498 26.309 4.925 1.00 16.19 O ANISOU 1330 O HOH A 489 1669 2255 2226 -119 290 -67 O HETATM 1331 O HOH A 490 38.521 18.535 32.133 1.00 17.98 O ANISOU 1331 O HOH A 490 1978 2084 2769 -336 -523 624 O HETATM 1332 O HOH A 491 62.021 20.629 -2.204 1.00 30.46 O ANISOU 1332 O HOH A 491 3779 3356 4436 729 1306 -686 O HETATM 1333 O HOH A 492 29.409 18.203 4.255 1.00 25.19 O ANISOU 1333 O HOH A 492 2840 4381 2348 567 -867 -1463 O HETATM 1334 O HOH A 493 50.776 12.264 18.081 1.00 17.81 O ANISOU 1334 O HOH A 493 2080 2918 1768 258 89 392 O HETATM 1335 O HOH A 494 31.534 35.674 -16.162 1.00 32.44 O ANISOU 1335 O HOH A 494 4591 3671 4063 47 139 -810 O HETATM 1336 O HOH A 495 62.730 26.480 2.801 1.00 27.21 O ANISOU 1336 O HOH A 495 2272 4796 3268 -1394 -478 70 O HETATM 1337 O HOH A 496 39.348 32.937 5.470 1.00 20.46 O ANISOU 1337 O HOH A 496 3274 2578 1922 -121 526 637 O HETATM 1338 O HOH A 497 27.431 13.700 11.971 1.00 36.98 O ANISOU 1338 O HOH A 497 5949 4126 3974 615 -1264 -917 O HETATM 1339 O HOH A 498 45.256 7.817 0.574 1.00 34.03 O ANISOU 1339 O HOH A 498 3976 5050 3900 -177 -400 86 O HETATM 1340 O HOH A 499 29.581 32.262 22.996 1.00 32.59 O ANISOU 1340 O HOH A 499 5993 3967 2421 1842 -670 -1189 O HETATM 1341 O HOH A 500 47.351 30.523 14.466 1.00 18.17 O ANISOU 1341 O HOH A 500 1500 2893 2509 -313 485 -20 O HETATM 1342 O HOH A 501 54.568 19.802 17.161 1.00 29.43 O ANISOU 1342 O HOH A 501 3219 4543 3419 -385 36 -441 O HETATM 1343 O HOH A 502 57.307 23.953 13.007 1.00 22.99 O ANISOU 1343 O HOH A 502 2368 4049 2318 519 -250 -1764 O HETATM 1344 O HOH A 503 57.969 29.402 4.148 1.00 30.00 O ANISOU 1344 O HOH A 503 3715 4758 2923 -565 444 -281 O HETATM 1345 O HOH A 504 29.263 21.042 2.722 1.00 27.84 O ANISOU 1345 O HOH A 504 4805 2886 2885 -772 -499 78 O HETATM 1346 O HOH A 505 59.057 26.298 -11.617 1.00 23.24 O ANISOU 1346 O HOH A 505 3626 2402 2802 -11 -200 -479 O HETATM 1347 O HOH A 506 50.970 9.929 -9.494 1.00 31.27 O ANISOU 1347 O HOH A 506 2657 4723 4500 -636 1254 -570 O HETATM 1348 O HOH A 507 47.806 32.713 16.289 1.00 18.41 O ANISOU 1348 O HOH A 507 1823 2376 2796 -138 1113 -688 O HETATM 1349 O HOH A 508 57.473 12.409 -1.566 1.00 28.03 O ANISOU 1349 O HOH A 508 2959 3322 4369 970 850 -480 O HETATM 1350 O HOH A 509 43.224 37.538 19.609 1.00 5.32 O ANISOU 1350 O HOH A 509 592 599 828 93 108 -130 O HETATM 1351 O HOH A 510 45.889 38.478 16.493 1.00 17.18 O ANISOU 1351 O HOH A 510 3008 1938 1582 606 -115 -79 O HETATM 1352 O HOH B 401 32.510 22.664 23.599 1.00 22.41 O ANISOU 1352 O HOH B 401 2715 3375 2423 -1162 -65 158 O HETATM 1353 O HOH B 402 26.147 21.883 22.926 1.00 29.40 O ANISOU 1353 O HOH B 402 3430 3973 3766 470 -237 -1913 O HETATM 1354 O HOH B 403 30.754 11.649 20.174 1.00 10.99 O ANISOU 1354 O HOH B 403 1200 1118 1858 80 -394 -39 O HETATM 1355 O HOH B 404 33.574 17.148 13.753 1.00 4.98 O ANISOU 1355 O HOH B 404 644 607 638 20 124 25 O HETATM 1356 O HOH B 405 35.204 4.287 13.610 1.00 12.36 O ANISOU 1356 O HOH B 405 1118 1659 1918 121 -518 -114 O HETATM 1357 O HOH B 406 29.255 14.628 18.220 1.00 19.42 O ANISOU 1357 O HOH B 406 2801 2258 2318 -228 -845 646 O HETATM 1358 O HOH B 407 35.935 6.304 21.938 1.00 6.03 O ANISOU 1358 O HOH B 407 783 858 647 129 1 133 O HETATM 1359 O HOH B 408 44.611 5.212 9.010 1.00 23.38 O ANISOU 1359 O HOH B 408 2671 2668 3544 -921 336 -158 O HETATM 1360 O HOH B 409 31.989 7.868 19.875 1.00 9.22 O ANISOU 1360 O HOH B 409 1059 1167 1277 134 -2 254 O HETATM 1361 O HOH B 410 33.480 0.474 19.093 1.00 11.28 O ANISOU 1361 O HOH B 410 1326 1587 1372 -219 24 278 O HETATM 1362 O HOH B 411 46.211 1.282 13.271 1.00 32.75 O ANISOU 1362 O HOH B 411 3531 4591 4320 2317 1202 692 O HETATM 1363 O HOH B 412 37.824 4.920 8.597 1.00 17.86 O ANISOU 1363 O HOH B 412 3001 1702 2082 -20 -1662 95 O HETATM 1364 O HOH B 413 32.774 8.608 17.348 1.00 8.15 O ANISOU 1364 O HOH B 413 815 1259 1020 -97 -128 300 O HETATM 1365 O HOH B 414 31.236 11.086 17.435 1.00 12.11 O ANISOU 1365 O HOH B 414 1456 1288 1857 -325 104 354 O HETATM 1366 O HOH B 415 30.026 2.268 22.007 1.00 28.09 O ANISOU 1366 O HOH B 415 1806 5319 3546 67 146 375 O HETATM 1367 O HOH B 416 31.214 12.713 26.875 1.00 30.70 O ANISOU 1367 O HOH B 416 4052 3285 4325 -187 496 -57 O HETATM 1368 O HOH B 417 33.225 6.066 21.602 1.00 9.79 O ANISOU 1368 O HOH B 417 1038 1531 1149 -263 -326 369 O HETATM 1369 O HOH B 418 35.304 4.241 10.856 1.00 21.81 O ANISOU 1369 O HOH B 418 2567 3094 2626 -578 -487 -12 O HETATM 1370 O HOH B 419 28.439 10.668 21.042 1.00 29.86 O ANISOU 1370 O HOH B 419 2440 3649 5257 97 907 1896 O HETATM 1371 O HOH B 420 35.181 0.839 16.902 1.00 8.06 O ANISOU 1371 O HOH B 420 934 976 1151 -153 -252 73 O HETATM 1372 O HOH B 421 31.189 4.889 22.781 1.00 21.29 O ANISOU 1372 O HOH B 421 1840 4142 2106 -786 -99 1542 O HETATM 1373 O HOH B 422 33.918 2.079 14.755 1.00 12.14 O ANISOU 1373 O HOH B 422 1771 1590 1248 69 -622 -204 O HETATM 1374 O HOH B 423 31.610 7.040 15.537 1.00 23.21 O ANISOU 1374 O HOH B 423 2792 3472 2553 587 -707 -1202 O HETATM 1375 O HOH B 424 35.710 3.507 7.117 1.00 18.45 O ANISOU 1375 O HOH B 424 2268 2710 2028 -638 -825 341 O CONECT 1061 1072 CONECT 1063 1064 CONECT 1064 1063 1065 1066 CONECT 1065 1064 CONECT 1066 1064 1067 CONECT 1067 1066 1068 CONECT 1068 1067 1069 CONECT 1069 1068 1070 CONECT 1070 1069 1071 CONECT 1071 1070 1072 1073 CONECT 1072 1061 1071 CONECT 1073 1071 1074 1075 CONECT 1074 1073 CONECT 1075 1073 CONECT 1081 1097 CONECT 1088 1089 CONECT 1089 1088 1090 1091 CONECT 1090 1089 CONECT 1091 1089 1092 CONECT 1092 1091 1093 CONECT 1093 1092 1094 CONECT 1094 1093 1095 CONECT 1095 1094 1096 CONECT 1096 1095 1097 1098 CONECT 1097 1081 1096 CONECT 1098 1096 1099 1100 CONECT 1099 1098 CONECT 1100 1098 CONECT 1138 1139 1140 CONECT 1139 1138 CONECT 1140 1138 1141 CONECT 1141 1140 MASTER 298 0 3 7 0 0 2 6 1368 2 32 11 END If you find results from this site helpful for your research, please cite one of our papers:
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