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*** ZNP_ZNC_only ***elNémo ID: 24012300063776725Job options:ID = 24012300063776725 JOBID = ZNP_ZNC_only USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER ZNP_ZNC_only HEADER SIGNALING PROTEIN 03-FEB-16 5HZV TITLE CRYSTAL STRUCTURE OF THE ZONA PELLUCIDA MODULE OF HUMAN ENDOGLIN/CD105 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MALTOSE-BINDING PERIPLASMIC PROTEIN,ENDOGLIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MBP,MMBP,MALTODEXTRIN-BINDING PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: THIS PROTEIN IS A CHIMERA. RESIDUES 368-734 ARE FROM COMPND 8 E. COLI MALTOSE BINDING PROTEIN (MBP), CORRESPOND TO RESIDUES 27-393 COMPND 9 OF SWISS-PROT DATABASE ENTRY P0AEX9 AND CONTAIN MUTATIONS D449A, COMPND 10 K450A, E539A, N540A, A582H, K586H, K606A, A679V, I684V, E726A, E729A, COMPND 11 D730A AND R734N (CORRESPONDING TO D108A, K109A, E198A, N199A, A241H, COMPND 12 K245H, K265A, A338V, I343V, E385A, E388A, D389A AND R393N IN P0AEX9). COMPND 13 RESIDUES 738-981 ARE FROM HUMAN ENDOGLIN PROTEIN AND CORRESPOND TO COMPND 14 RESIDUES 338-581 OF SWISS-PROT DATABASE ENTRY P17813. SUBTRACTING 400 COMPND 15 FROM THE PDB ENTRY RESIDUE NUMBERING RESULTS IN THE NUMBERING COMPND 16 ACCORDING TO UNIPROT ENTRY P17813. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12), HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 83333, 9606; SOURCE 5 STRAIN: K12; SOURCE 6 CELL: ENDOTHELIAL; SOURCE 7 GENE: MALE, B4034, JW3994, ENG, END; SOURCE 8 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 9 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 12 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3216; SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PHLSEC KEYWDS ZONA PELLUCIDA DOMAIN, ANGIOGENESIS, GLYCOPROTEIN, RECEPTOR, KEYWDS 2 SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR M.BOKHOVE,T.SAITO,L.JOVINE REVDAT 5 29-JUL-20 5HZV 1 COMPND REMARK HET HETNAM REVDAT 5 2 1 HETSYN FORMUL LINK SITE REVDAT 5 3 1 ATOM REVDAT 4 06-SEP-17 5HZV 1 REMARK REVDAT 3 23-AUG-17 5HZV 1 COMPND SOURCE DBREF SEQADV REVDAT 2 14-JUN-17 5HZV 1 JRNL REVDAT 1 07-JUN-17 5HZV 0 JRNL AUTH T.SAITO,M.BOKHOVE,R.CROCI,S.ZAMORA-CABALLERO,L.HAN, JRNL AUTH 2 M.LETARTE,D.DE SANCTIS,L.JOVINE JRNL TITL STRUCTURAL BASIS OF THE HUMAN ENDOGLIN-BMP9 INTERACTION: JRNL TITL 2 INSIGHTS INTO BMP SIGNALING AND HHT1. JRNL REF CELL REP V. 19 1917 2017 JRNL REFN ESSN 2211-1247 JRNL PMID 28564608 JRNL DOI 10.1016/J.CELREP.2017.05.011 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.GOUGOS,M.LETARTE REMARK 1 TITL PRIMARY STRUCTURE OF ENDOGLIN, AN RGD-CONTAINING REMARK 1 TITL 2 GLYCOPROTEIN OF HUMAN ENDOTHELIAL CELLS. REMARK 1 REF J. BIOL. CHEM. V. 265 8361 1990 REMARK 1 REFN ISSN 0021-9258 REMARK 1 PMID 1692830 REMARK 1 REFERENCE 2 REMARK 1 AUTH P.BORK,C.SANDER REMARK 1 TITL A LARGE DOMAIN COMMON TO SPERM RECEPTORS (ZP2 AND ZP3) AND REMARK 1 TITL 2 TGF-BETA TYPE III RECEPTOR. REMARK 1 REF FEBS LETT. V. 300 237 1992 REMARK 1 REFN ISSN 0014-5793 REMARK 1 PMID 1313375 REMARK 1 REFERENCE 3 REMARK 1 AUTH L.JOVINE,C.C.DARIE,E.S.LITSCHER,P.M.WASSARMAN REMARK 1 TITL ZONA PELLUCIDA DOMAIN PROTEINS. REMARK 1 REF ANNU. REV. BIOCHEM. V. 74 83 2005 REMARK 1 REFN ISSN 0066-4154 REMARK 1 PMID 15952882 REMARK 1 DOI 10.1146/ANNUREV.BIOCHEM.74.082803.133039 REMARK 1 REFERENCE 4 REMARK 1 AUTH L.HAN,M.MONNE,H.OKUMURA,T.SCHWEND,A.L.CHERRY,D.FLOT, REMARK 1 AUTH 2 T.MATSUDA,L.JOVINE REMARK 1 TITL INSIGHTS INTO EGG COAT ASSEMBLY AND EGG-SPERM INTERACTION REMARK 1 TITL 2 FROM THE X-RAY STRUCTURE OF FULL-LENGTH ZP3. REMARK 1 REF CELL V. 143 404 2010 REMARK 1 REFN ISSN 1097-4172 REMARK 1 PMID 20970175 REMARK 1 DOI 10.1016/J.CELL.2010.09.041 REMARK 1 REFERENCE 5 REMARK 1 AUTH M.BOKHOVE,K.NISHIMURA,M.BRUNATI,L.HAN,D.DE SANCTIS, REMARK 1 AUTH 2 L.RAMPOLDI,L.JOVINE REMARK 1 TITL A STRUCTURED INTERDOMAIN LINKER DIRECTS SELF-POLYMERIZATION REMARK 1 TITL 2 OF HUMAN UROMODULIN. REMARK 1 REF PROC. NATL. ACAD. SCI. V. 113 1552 2016 REMARK 1 REF 2 U.S.A. REMARK 1 REFN ESSN 1091-6490 REMARK 1 PMID 26811476 REMARK 1 DOI 10.1073/PNAS.1519803113 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 3 NUMBER OF REFLECTIONS : 21429 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.234 REMARK 3 R VALUE (WORKING SET) : 0.232 REMARK 3 FREE R VALUE : 0.272 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.310 REMARK 3 FREE R VALUE TEST SET COUNT : 1138 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 29.5037 - 5.3915 0.97 2551 153 0.1829 0.2483 REMARK 3 2 5.3915 - 4.2836 0.98 2516 152 0.1832 0.2172 REMARK 3 3 4.2836 - 3.7433 0.99 2550 146 0.2187 0.2365 REMARK 3 4 3.7433 - 3.4016 0.99 2513 157 0.2516 0.2891 REMARK 3 5 3.4016 - 3.1581 0.99 2582 113 0.2837 0.3406 REMARK 3 6 3.1581 - 2.9721 0.99 2534 149 0.3246 0.3668 REMARK 3 7 2.9721 - 2.8234 0.99 2553 143 0.3637 0.4035 REMARK 3 8 2.8234 - 2.7005 0.97 2492 125 0.4031 0.4429 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.510 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.220 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 72.17 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 4719 REMARK 3 ANGLE : 0.534 6414 REMARK 3 CHIRALITY : 0.041 727 REMARK 3 PLANARITY : 0.004 823 REMARK 3 DIHEDRAL : 10.633 2844 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A AND (RESID 844:976) REMARK 3 ORIGIN FOR THE GROUP (A): 10.5078 83.7513 56.5438 REMARK 3 T TENSOR REMARK 3 T11: 0.8027 T22: 0.5983 REMARK 3 T33: 0.7139 T12: -0.0504 REMARK 3 T13: -0.0145 T23: -0.0006 REMARK 3 L TENSOR REMARK 3 L11: 1.2148 L22: 2.9213 REMARK 3 L33: 3.2530 L12: -0.7364 REMARK 3 L13: -1.0954 L23: 1.8018 REMARK 3 S TENSOR REMARK 3 S11: -0.1450 S12: 0.1242 S13: -0.0373 REMARK 3 S21: 0.2215 S22: -0.0513 S23: -0.0776 REMARK 3 S31: 0.2670 S32: 0.1346 S33: -0.0039 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN A AND (RESID 743:843) REMARK 3 ORIGIN FOR THE GROUP (A): 40.9911 50.1162 72.0674 REMARK 3 T TENSOR REMARK 3 T11: 0.7846 T22: 0.9756 REMARK 3 T33: 0.7623 T12: 0.1771 REMARK 3 T13: -0.0616 T23: 0.0067 REMARK 3 L TENSOR REMARK 3 L11: 1.4810 L22: 1.5077 REMARK 3 L33: 1.2673 L12: -0.7179 REMARK 3 L13: -0.8837 L23: 0.5289 REMARK 3 S TENSOR REMARK 3 S11: 0.0158 S12: 0.2571 S13: 0.1353 REMARK 3 S21: 0.0940 S22: -0.1567 S23: 0.2022 REMARK 3 S31: -0.6051 S32: -0.1340 S33: -0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN A AND (RESID 844:976) REMARK 3 ORIGIN FOR THE GROUP (A): 39.3244 15.2567 63.0870 REMARK 3 T TENSOR REMARK 3 T11: 0.9802 T22: 0.9352 REMARK 3 T33: 1.1300 T12: 0.0858 REMARK 3 T13: -0.0087 T23: -0.0490 REMARK 3 L TENSOR REMARK 3 L11: 0.4743 L22: 1.1965 REMARK 3 L33: 0.8632 L12: -0.0459 REMARK 3 L13: 0.0554 L23: 0.4637 REMARK 3 S TENSOR REMARK 3 S11: 0.0511 S12: 0.2044 S13: -0.4300 REMARK 3 S21: -0.4137 S22: 0.0081 S23: 0.7261 REMARK 3 S31: 0.1789 S32: 0.1638 S33: -0.0001 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5HZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-16. REMARK 100 THE DEPOSITION ID IS D_1000215849. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-SEP-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5-7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : SI SINGLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS (JUN 17, 2015) REMARK 200 DATA SCALING SOFTWARE : XSCALE (JUN 17, 2015) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21583 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690 REMARK 200 RESOLUTION RANGE LOW (A) : 29.510 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06200 REMARK 200 FOR THE DATA SET : 9.4300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76 REMARK 200 COMPLETENESS FOR SHELL (%) : 85.4 REMARK 200 DATA REDUNDANCY IN SHELL : 2.80 REMARK 200 R MERGE FOR SHELL (I) : 0.67500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.990 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER (2.5.6) REMARK 200 STARTING MODEL: 3SEX REMARK 200 REMARK 200 REMARK: HEXAGONAL ROD REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 11.5% EQUAL MIXTURE OF MPD, PEG 1000 REMARK 280 AND PEG 3350 (1:1:1), MES/IMIDAZOLE MIX, PH 6.5, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.02667 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.51333 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.27000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 14.75667 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 73.78333 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 900 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27770 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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 GLU A 364 REMARK 465 THR A 365 REMARK 465 GLY A 366 REMARK 465 THR A 367 REMARK 465 PRO A 738 REMARK 465 ALA A 739 REMARK 465 PRO A 740 REMARK 465 ILE A 741 REMARK 465 GLN A 742 REMARK 465 THR A 743 REMARK 465 THR A 744 REMARK 465 PRO A 745 REMARK 465 PRO A 746 REMARK 465 LYS A 747 REMARK 465 ASP A 748 REMARK 465 PRO A 977 REMARK 465 ASP A 978 REMARK 465 LEU A 979 REMARK 465 SER A 980 REMARK 465 GLY A 981 REMARK 465 LEU A 982 REMARK 465 GLU A 983 REMARK 465 HIS A 984 REMARK 465 HIS A 985 REMARK 465 HIS A 986 REMARK 465 HIS A 987 REMARK 465 HIS A 988 REMARK 465 HIS A 989 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 VAL A 548 NE2 GLN A 732 2.18 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 NZ LYS A 401 O GLN A 692 3565 2.12 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 ILE A 475 -61.18 -108.21 REMARK 500 LYS A 569 -1.96 84.76 REMARK 500 TYR A 650 -64.14 -109.98 REMARK 500 PRO A 858 53.88 -68.92 REMARK 500 GLU A 900 -16.36 77.95 REMARK 500 ARG A 910 -4.05 78.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3D4G RELATED DB: PDB REMARK 900 ZP-N DOMAIN OF MAMMALIAN SPERM RECEPTOR ZP3 (CRYSTAL FORM II) REMARK 900 RELATED ID: 3NK4 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FULL-LENGTH SPERM RECEPTOR ZP3 AT 2.0 A REMARK 900 RESOLUTION REMARK 900 RELATED ID: 4WRN RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A ZP DOMAIN POLYMERIZATION INTERMEDIATE REMARK 900 RELATED ID: 5I04 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE ORPHAN REGION OF HUMAN ENDOGLIN/CD105 REMARK 900 RELATED ID: 5HZW RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE ORPHAN REGION OF HUMAN ENDOGLIN/CD105 IN REMARK 900 COMPLEX WITH BMP9 REMARK 900 RELATED ID: 5I05 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN BMP9 AT 1.87 A RESOLUTION DBREF 5HZV A 368 734 UNP P0AEX9 MALE_ECOLI 27 393 DBREF 5HZV A 738 981 UNP P17813 EGLN_HUMAN 338 581 SEQADV 5HZV GLU A 364 UNP P0AEX9 EXPRESSION TAG SEQADV 5HZV THR A 365 UNP P0AEX9 EXPRESSION TAG SEQADV 5HZV GLY A 366 UNP P0AEX9 EXPRESSION TAG SEQADV 5HZV THR A 367 UNP P0AEX9 EXPRESSION TAG SEQADV 5HZV ALA A 449 UNP P0AEX9 ASP 108 ENGINEERED MUTATION SEQADV 5HZV ALA A 450 UNP P0AEX9 LYS 109 ENGINEERED MUTATION SEQADV 5HZV ALA A 539 UNP P0AEX9 GLU 198 ENGINEERED MUTATION SEQADV 5HZV ALA A 540 UNP P0AEX9 ASN 199 ENGINEERED MUTATION SEQADV 5HZV HIS A 582 UNP P0AEX9 ALA 241 ENGINEERED MUTATION SEQADV 5HZV HIS A 586 UNP P0AEX9 LYS 245 ENGINEERED MUTATION SEQADV 5HZV ALA A 606 UNP P0AEX9 LYS 265 ENGINEERED MUTATION SEQADV 5HZV VAL A 679 UNP P0AEX9 ALA 338 ENGINEERED MUTATION SEQADV 5HZV VAL A 684 UNP P0AEX9 ILE 343 ENGINEERED MUTATION SEQADV 5HZV ALA A 726 UNP P0AEX9 GLU 385 ENGINEERED MUTATION SEQADV 5HZV ALA A 729 UNP P0AEX9 LYS 388 ENGINEERED MUTATION SEQADV 5HZV ALA A 730 UNP P0AEX9 ASP 389 ENGINEERED MUTATION SEQADV 5HZV ASN A 734 UNP P0AEX9 ARG 393 ENGINEERED MUTATION SEQADV 5HZV ALA A 735 UNP P0AEX9 LINKER SEQADV 5HZV ALA A 736 UNP P0AEX9 LINKER SEQADV 5HZV ALA A 737 UNP P0AEX9 LINKER SEQADV 5HZV LEU A 982 UNP P17813 EXPRESSION TAG SEQADV 5HZV GLU A 983 UNP P17813 EXPRESSION TAG SEQADV 5HZV HIS A 984 UNP P17813 EXPRESSION TAG SEQADV 5HZV HIS A 985 UNP P17813 EXPRESSION TAG SEQADV 5HZV HIS A 986 UNP P17813 EXPRESSION TAG SEQADV 5HZV HIS A 987 UNP P17813 EXPRESSION TAG SEQADV 5HZV HIS A 988 UNP P17813 EXPRESSION TAG SEQADV 5HZV HIS A 989 UNP P17813 EXPRESSION TAG SEQRES 1 A 626 GLU THR GLY THR LYS ILE GLU GLU GLY LYS LEU VAL ILE SEQRES 2 A 626 TRP ILE ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU SEQRES 3 A 626 VAL GLY LYS LYS PHE GLU LYS ASP THR GLY ILE LYS VAL SEQRES 4 A 626 THR VAL GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO SEQRES 5 A 626 GLN VAL ALA ALA THR GLY ASP GLY PRO ASP ILE ILE PHE SEQRES 6 A 626 TRP ALA HIS ASP ARG PHE GLY GLY TYR ALA GLN SER GLY SEQRES 7 A 626 LEU LEU ALA GLU ILE THR PRO ALA ALA ALA PHE GLN ASP SEQRES 8 A 626 LYS LEU TYR PRO PHE THR TRP ASP ALA VAL ARG TYR ASN SEQRES 9 A 626 GLY LYS LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SEQRES 10 A 626 SER LEU ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO SEQRES 11 A 626 LYS THR TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU SEQRES 12 A 626 LYS ALA LYS GLY LYS SER ALA LEU MET PHE ASN LEU GLN SEQRES 13 A 626 GLU PRO TYR PHE THR TRP PRO LEU ILE ALA ALA ASP GLY SEQRES 14 A 626 GLY TYR ALA PHE LYS TYR ALA ALA GLY LYS TYR ASP ILE SEQRES 15 A 626 LYS ASP VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY SEQRES 16 A 626 LEU THR PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS MET SEQRES 17 A 626 ASN ALA ASP THR ASP TYR SER ILE ALA GLU HIS ALA PHE SEQRES 18 A 626 ASN HIS GLY GLU THR ALA MET THR ILE ASN GLY PRO TRP SEQRES 19 A 626 ALA TRP SER ASN ILE ASP THR SER ALA VAL ASN TYR GLY SEQRES 20 A 626 VAL THR VAL LEU PRO THR PHE LYS GLY GLN PRO SER LYS SEQRES 21 A 626 PRO PHE VAL GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SEQRES 22 A 626 SER PRO ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN SEQRES 23 A 626 TYR LEU LEU THR ASP GLU GLY LEU GLU ALA VAL ASN LYS SEQRES 24 A 626 ASP LYS PRO LEU GLY ALA VAL ALA LEU LYS SER TYR GLU SEQRES 25 A 626 GLU GLU LEU VAL LYS ASP PRO ARG VAL ALA ALA THR MET SEQRES 26 A 626 GLU ASN ALA GLN LYS GLY GLU ILE MET PRO ASN ILE PRO SEQRES 27 A 626 GLN MET SER ALA PHE TRP TYR ALA VAL ARG THR ALA VAL SEQRES 28 A 626 ILE ASN ALA ALA SER GLY ARG GLN THR VAL ASP ALA ALA SEQRES 29 A 626 LEU ALA ALA ALA GLN THR ASN ALA ALA ALA PRO ALA PRO SEQRES 30 A 626 ILE GLN THR THR PRO PRO LYS ASP THR CYS SER PRO GLU SEQRES 31 A 626 LEU LEU MET SER LEU ILE GLN THR LYS CYS ALA ASP ASP SEQRES 32 A 626 ALA MET THR LEU VAL LEU LYS LYS GLU LEU VAL ALA HIS SEQRES 33 A 626 LEU LYS CYS THR ILE THR GLY LEU THR PHE TRP ASP PRO SEQRES 34 A 626 SER CYS GLU ALA GLU ASP ARG GLY ASP LYS PHE VAL LEU SEQRES 35 A 626 ARG SER ALA TYR SER SER CYS GLY MET GLN VAL SER ALA SEQRES 36 A 626 SER MET ILE SER ASN GLU ALA VAL VAL ASN ILE LEU SER SEQRES 37 A 626 SER SER SER PRO GLN ARG LYS LYS VAL HIS CYS LEU ASN SEQRES 38 A 626 MET ASP SER LEU SER PHE GLN LEU GLY LEU TYR LEU SER SEQRES 39 A 626 PRO HIS PHE LEU GLN ALA SER ASN THR ILE GLU PRO GLY SEQRES 40 A 626 GLN GLN SER PHE VAL GLN VAL ARG VAL SER PRO SER VAL SEQRES 41 A 626 SER GLU PHE LEU LEU GLN LEU ASP SER CYS HIS LEU ASP SEQRES 42 A 626 LEU GLY PRO GLU GLY GLY THR VAL GLU LEU ILE GLN GLY SEQRES 43 A 626 ARG ALA ALA LYS GLY ASN CYS VAL SER LEU LEU SER PRO SEQRES 44 A 626 SER PRO GLU GLY ASP PRO ARG PHE SER PHE LEU LEU HIS SEQRES 45 A 626 PHE TYR THR VAL PRO ILE PRO LYS THR GLY THR LEU SER SEQRES 46 A 626 CYS THR VAL ALA LEU ARG PRO LYS THR GLY SER GLN ASP SEQRES 47 A 626 GLN GLU VAL HIS ARG THR VAL PHE MET ARG LEU ASN ILE SEQRES 48 A 626 ILE SER PRO ASP LEU SER GLY LEU GLU HIS HIS HIS HIS SEQRES 49 A 626 HIS HIS HET GLC B 1 12 HET GLC B 2 11 HET GOL A1002 6 HETNAM GLC ALPHA-D-GLUCOPYRANOSE HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 2 GLC 2(C6 H12 O6) FORMUL 3 GOL C3 H8 O3 FORMUL 4 HOH *15(H2 O) HELIX 1 1 PRO A 752 LEU A 758 1 7 HELIX 2 2 LYS A 774 LEU A 780 1 7 HELIX 3 3 MET A 845 SER A 847 1 3 HELIX 4 4 GLN A 960 GLN A 962 1 3 SHEET 1 1 1 ILE A 759 CYS A 763 0 SHEET 2 2 1 ALA A 767 LYS A 773 0 SHEET 3 3 1 ILE A 784 THR A 788 0 SHEET 4 4 1 GLU A 797 ASP A 798 0 SHEET 5 5 1 LYS A 802 ALA A 808 0 SHEET 6 6 1 GLN A 815 SER A 817 0 SHEET 7 7 1 MET A 820 ILE A 829 0 SHEET 8 8 1 SER A 832 LEU A 843 0 SHEET 9 9 1 SER A 849 TYR A 855 0 SHEET 10 10 1 THR A 866 ILE A 867 0 SHEET 11 11 1 GLN A 871 SER A 880 0 SHEET 12 12 1 PHE A 886 ASP A 896 0 SHEET 13 13 1 THR A 903 GLN A 908 0 SHEET 14 14 1 ALA A 911 ALA A 912 0 SHEET 15 15 1 VAL A 917 LEU A 919 0 SHEET 16 16 1 ARG A 929 LEU A 934 0 SHEET 17 17 1 THR A 944 PRO A 955 0 SHEET 18 18 1 VAL A 964 ILE A 974 0 SSBOND 1 CYS A 750 CYS A 782 1555 1555 2.04 SSBOND 2 CYS A 763 CYS A 842 1555 1555 2.04 SSBOND 3 CYS A 794 CYS A 812 1555 1555 2.03 SSBOND 4 CYS A 893 CYS A 949 1555 1555 2.03 LINK O4 GLC B 1 C1 GLC B 2 1555 1555 1.41 CISPEP 1 SER A 880 PRO A 881 0 -10.40 CISPEP 2 VAL A 939 PRO A 940 0 4.54 CRYST1 125.160 125.160 88.540 90.00 90.00 120.00 P 65 6 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 0.007990 0.004613 0.000000 0.00000 SCALE2 0.000000 0.009226 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011294 0.00000 ATOM 1 N THR A 749 43.473 67.883 61.092 1.00 94.14 N ANISOU 1 N THR A 749 14023 11429 10316 2829 40 2063 N ATOM 2 CA THR A 749 44.893 67.573 61.224 1.00 94.67 C ANISOU 2 CA THR A 749 14052 11456 10463 2529 95 2048 C ATOM 3 C THR A 749 45.092 66.246 61.952 1.00 92.60 C ANISOU 3 C THR A 749 13539 11393 10254 2360 -38 1864 C ATOM 4 O THR A 749 46.123 65.592 61.790 1.00 92.19 O ANISOU 4 O THR A 749 13385 11417 10225 2168 -38 1848 O ATOM 5 CB THR A 749 45.646 68.689 61.979 1.00 94.38 C ANISOU 5 CB THR A 749 14201 11094 10566 2335 239 2061 C ATOM 6 OG1 THR A 749 45.457 69.936 61.299 1.00 96.80 O ANISOU 6 OG1 THR A 749 14753 11192 10832 2496 386 2240 O ATOM 7 CG2 THR A 749 47.141 68.391 62.063 1.00 92.85 C ANISOU 7 CG2 THR A 749 13951 10868 10460 2028 294 2039 C ATOM 8 N CYS A 750 44.115 65.854 62.773 1.00 91.83 N ANISOU 8 N CYS A 750 13345 11370 10178 2435 -140 1731 N ATOM 9 CA CYS A 750 44.205 64.562 63.441 1.00 88.59 C ANISOU 9 CA CYS A 750 12704 11147 9811 2303 -252 1567 C ATOM 10 C CYS A 750 43.761 63.419 62.532 1.00 88.45 C ANISOU 10 C CYS A 750 12493 11420 9692 2432 -354 1552 C ATOM 11 O CYS A 750 44.431 62.384 62.464 1.00 87.93 O ANISOU 11 O CYS A 750 12268 11502 9639 2286 -397 1494 O ATOM 12 CB CYS A 750 43.374 64.570 64.725 1.00 86.65 C ANISOU 12 CB CYS A 750 12434 10854 9636 2321 -299 1428 C ATOM 13 SG CYS A 750 43.272 62.953 65.543 1.00 89.82 S ANISOU 13 SG CYS A 750 12563 11484 10081 2208 -422 1239 S ATOM 14 N SER A 751 42.654 63.589 61.815 1.00105.14 N ANISOU 14 N SER A 751 14617 13625 11705 2707 -394 1596 N ATOM 15 CA SER A 751 42.090 62.501 61.023 1.00103.67 C ANISOU 15 CA SER A 751 14235 13727 11430 2840 -504 1546 C ATOM 16 C SER A 751 41.812 61.309 61.931 1.00100.61 C ANISOU 16 C SER A 751 13624 13474 11128 2732 -593 1356 C ATOM 17 O SER A 751 42.417 60.242 61.765 1.00 99.70 O ANISOU 17 O SER A 751 13352 13507 11022 2601 -629 1300 O ATOM 18 CB SER A 751 43.034 62.103 59.886 1.00104.39 C ANISOU 18 CB SER A 751 14303 13923 11438 2785 -481 1639 C ATOM 19 OG SER A 751 42.472 61.069 59.095 1.00104.83 O ANISOU 19 OG SER A 751 14171 14258 11401 2918 -589 1578 O ATOM 20 N PRO A 752 40.910 61.453 62.906 1.00 92.87 N ANISOU 20 N PRO A 752 12632 12440 10215 2788 -617 1257 N ATOM 21 CA PRO A 752 40.653 60.341 63.836 1.00 92.76 C ANISOU 21 CA PRO A 752 12424 12533 10289 2686 -677 1086 C ATOM 22 C PRO A 752 40.000 59.132 63.190 1.00 89.81 C ANISOU 22 C PRO A 752 11818 12431 9876 2790 -771 994 C ATOM 23 O PRO A 752 40.127 58.025 63.729 1.00 88.24 O ANISOU 23 O PRO A 752 11448 12332 9745 2666 -800 873 O ATOM 24 CB PRO A 752 39.738 60.973 64.893 1.00 92.62 C ANISOU 24 CB PRO A 752 12478 12377 10335 2762 -661 1024 C ATOM 25 CG PRO A 752 39.114 62.147 64.213 1.00 96.15 C ANISOU 25 CG PRO A 752 13090 12734 10708 2987 -633 1144 C ATOM 26 CD PRO A 752 40.150 62.663 63.261 1.00 95.98 C ANISOU 26 CD PRO A 752 13201 12652 10616 2938 -573 1304 C ATOM 27 N GLU A 753 39.304 59.297 62.063 1.00 89.76 N ANISOU 27 N GLU A 753 11798 12546 9761 3018 -816 1042 N ATOM 28 CA GLU A 753 38.700 58.144 61.401 1.00 88.59 C ANISOU 28 CA GLU A 753 11418 12665 9578 3111 -911 934 C ATOM 29 C GLU A 753 39.753 57.094 61.069 1.00 85.71 C ANISOU 29 C GLU A 753 10936 12412 9215 2922 -914 913 C ATOM 30 O GLU A 753 39.506 55.890 61.207 1.00 82.37 O ANISOU 30 O GLU A 753 10302 12148 8844 2875 -962 773 O ATOM 31 CB GLU A 753 37.962 58.591 60.139 1.00 90.26 C ANISOU 31 CB GLU A 753 11655 12994 9645 3389 -965 1003 C ATOM 32 CG GLU A 753 36.814 59.557 60.402 1.00 92.17 C ANISOU 32 CG GLU A 753 11989 13149 9881 3609 -972 1018 C ATOM 33 CD GLU A 753 35.980 59.824 59.159 1.00 97.53 C ANISOU 33 CD GLU A 753 12653 13993 10410 3910 -1049 1062 C ATOM 34 OE1 GLU A 753 36.446 59.500 58.044 1.00 93.97 O ANISOU 34 OE1 GLU A 753 12181 13684 9839 3944 -1078 1119 O ATOM 35 OE2 GLU A 753 34.856 60.355 59.297 1.00 99.99 O ANISOU 35 OE2 GLU A 753 12973 14300 10719 4120 -1082 1036 O ATOM 36 N LEU A 754 40.935 57.532 60.629 1.00 80.14 N ANISOU 36 N LEU A 754 10365 11620 8465 2812 -851 1050 N ATOM 37 CA LEU A 754 42.039 56.602 60.418 1.00 78.95 C ANISOU 37 CA LEU A 754 10114 11554 8331 2617 -840 1035 C ATOM 38 C LEU A 754 42.529 56.009 61.730 1.00 77.48 C ANISOU 38 C LEU A 754 9855 11300 8282 2395 -820 937 C ATOM 39 O LEU A 754 42.971 54.854 61.761 1.00 77.16 O ANISOU 39 O LEU A 754 9653 11385 8280 2278 -840 859 O ATOM 40 CB LEU A 754 43.197 57.305 59.704 1.00 80.58 C ANISOU 40 CB LEU A 754 10485 11662 8470 2547 -761 1206 C ATOM 41 CG LEU A 754 43.099 57.528 58.193 1.00 81.33 C ANISOU 41 CG LEU A 754 10626 11872 8403 2730 -770 1316 C ATOM 42 CD1 LEU A 754 44.300 58.325 57.705 1.00 82.20 C ANISOU 42 CD1 LEU A 754 10922 11833 8477 2633 -655 1492 C ATOM 43 CD2 LEU A 754 43.008 56.205 57.453 1.00 80.59 C ANISOU 43 CD2 LEU A 754 10315 12045 8259 2752 -848 1217 C ATOM 44 N LEU A 755 42.457 56.778 62.818 1.00 75.37 N ANISOU 44 N LEU A 755 9712 10839 8087 2344 -780 939 N ATOM 45 CA LEU A 755 42.982 56.310 64.096 1.00 73.97 C ANISOU 45 CA LEU A 755 9492 10595 8020 2144 -761 855 C ATOM 46 C LEU A 755 42.335 54.995 64.507 1.00 72.60 C ANISOU 46 C LEU A 755 9102 10582 7903 2153 -809 703 C ATOM 47 O LEU A 755 43.026 54.036 64.869 1.00 71.30 O ANISOU 47 O LEU A 755 8826 10478 7788 1999 -806 650 O ATOM 48 CB LEU A 755 42.766 57.381 65.166 1.00 74.59 C ANISOU 48 CB LEU A 755 9738 10453 8150 2131 -718 862 C ATOM 49 CG LEU A 755 43.342 57.114 66.558 1.00 73.51 C ANISOU 49 CG LEU A 755 9596 10229 8106 1938 -700 783 C ATOM 50 CD1 LEU A 755 44.853 56.955 66.511 1.00 73.11 C ANISOU 50 CD1 LEU A 755 9553 10155 8069 1723 -675 829 C ATOM 51 CD2 LEU A 755 42.951 58.241 67.495 1.00 74.41 C ANISOU 51 CD2 LEU A 755 9883 10136 8254 1961 -661 780 C ATOM 52 N MET A 756 41.005 54.925 64.446 1.00 73.01 N ANISOU 52 N MET A 756 9086 10701 7954 2337 -847 629 N ATOM 53 CA MET A 756 40.319 53.717 64.889 1.00 71.91 C ANISOU 53 CA MET A 756 8741 10692 7891 2342 -871 475 C ATOM 54 C MET A 756 40.771 52.493 64.105 1.00 71.09 C ANISOU 54 C MET A 756 8461 10776 7774 2284 -897 433 C ATOM 55 O MET A 756 40.737 51.375 64.630 1.00 69.90 O ANISOU 55 O MET A 756 8158 10695 7707 2201 -886 325 O ATOM 56 CB MET A 756 38.807 53.899 64.768 1.00 72.80 C ANISOU 56 CB MET A 756 8795 10858 8006 2558 -908 400 C ATOM 57 CG MET A 756 38.241 55.035 65.619 1.00 73.61 C ANISOU 57 CG MET A 756 9060 10776 8134 2628 -874 426 C ATOM 58 SD MET A 756 38.672 54.938 67.377 1.00 72.47 S ANISOU 58 SD MET A 756 8974 10464 8095 2439 -805 374 S ATOM 59 CE MET A 756 40.140 55.964 67.430 1.00 72.84 C ANISOU 59 CE MET A 756 9247 10333 8095 2283 -768 521 C ATOM 60 N SER A 757 41.203 52.680 62.857 1.00 93.13 N ANISOU 60 N SER A 757 11278 13646 10463 2330 -921 520 N ATOM 61 CA SER A 757 41.664 51.551 62.057 1.00 90.15 C ANISOU 61 CA SER A 757 10741 13446 10065 2278 -942 479 C ATOM 62 C SER A 757 42.924 50.923 62.638 1.00 87.77 C ANISOU 62 C SER A 757 10418 13105 9827 2049 -893 491 C ATOM 63 O SER A 757 43.151 49.719 62.473 1.00 85.89 O ANISOU 63 O SER A 757 10015 12994 9627 1983 -895 411 O ATOM 64 CB SER A 757 41.918 51.999 60.620 1.00 88.02 C ANISOU 64 CB SER A 757 10532 13256 9653 2382 -968 585 C ATOM 65 OG SER A 757 42.748 51.075 59.945 1.00 91.82 O ANISOU 65 OG SER A 757 10909 13864 10113 2284 -965 577 O ATOM 66 N LEU A 758 43.751 51.715 63.320 1.00 69.82 N ANISOU 66 N LEU A 758 8303 10656 7570 1929 -849 581 N ATOM 67 CA LEU A 758 45.000 51.203 63.867 1.00 68.77 C ANISOU 67 CA LEU A 758 8149 10493 7490 1721 -814 592 C ATOM 68 C LEU A 758 44.785 50.309 65.085 1.00 67.53 C ANISOU 68 C LEU A 758 7886 10338 7434 1650 -803 477 C ATOM 69 O LEU A 758 45.696 49.559 65.453 1.00 66.59 O ANISOU 69 O LEU A 758 7702 10245 7356 1506 -783 466 O ATOM 70 CB LEU A 758 45.909 52.370 64.246 1.00 69.42 C ANISOU 70 CB LEU A 758 8423 10390 7565 1616 -775 703 C ATOM 71 CG LEU A 758 46.135 53.452 63.194 1.00 70.92 C ANISOU 71 CG LEU A 758 8759 10523 7664 1685 -754 838 C ATOM 72 CD1 LEU A 758 47.029 54.538 63.768 1.00 71.58 C ANISOU 72 CD1 LEU A 758 9018 10400 7778 1552 -698 920 C ATOM 73 CD2 LEU A 758 46.736 52.871 61.933 1.00 70.96 C ANISOU 73 CD2 LEU A 758 8687 10674 7603 1678 -754 886 C ATOM 74 N ILE A 759 43.617 50.381 65.725 1.00 67.61 N ANISOU 74 N ILE A 759 7884 10321 7485 1754 -807 396 N ATOM 75 CA ILE A 759 43.367 49.589 66.925 1.00 66.62 C ANISOU 75 CA ILE A 759 7680 10182 7452 1698 -776 297 C ATOM 76 C ILE A 759 43.185 48.130 66.531 1.00 65.80 C ANISOU 76 C ILE A 759 7365 10242 7395 1694 -769 204 C ATOM 77 O ILE A 759 42.270 47.784 65.777 1.00 66.18 O ANISOU 77 O ILE A 759 7302 10402 7442 1816 -793 134 O ATOM 78 CB ILE A 759 42.134 50.100 67.680 1.00 67.10 C ANISOU 78 CB ILE A 759 7787 10161 7548 1816 -766 238 C ATOM 79 CG1 ILE A 759 42.284 51.582 68.027 1.00 68.07 C ANISOU 79 CG1 ILE A 759 8126 10110 7627 1826 -766 326 C ATOM 80 CG2 ILE A 759 41.929 49.286 68.955 1.00 66.20 C ANISOU 80 CG2 ILE A 759 7608 10023 7521 1759 -715 148 C ATOM 81 CD1 ILE A 759 40.999 52.225 68.500 1.00 68.82 C ANISOU 81 CD1 ILE A 759 8274 10133 7742 1975 -759 281 C ATOM 82 N GLN A 760 44.016 47.264 67.097 1.00 64.80 N ANISOU 82 N GLN A 760 7180 10126 7316 1559 -733 191 N ATOM 83 CA GLN A 760 43.999 45.843 66.791 1.00 64.05 C ANISOU 83 CA GLN A 760 6896 10164 7277 1536 -706 109 C ATOM 84 C GLN A 760 43.315 45.093 67.923 1.00 63.52 C ANISOU 84 C GLN A 760 6758 10066 7309 1544 -643 10 C ATOM 85 O GLN A 760 43.496 45.423 69.098 1.00 63.35 O ANISOU 85 O GLN A 760 6838 9929 7301 1501 -615 32 O ATOM 86 CB GLN A 760 45.423 45.317 66.594 1.00 63.43 C ANISOU 86 CB GLN A 760 6795 10120 7185 1393 -695 172 C ATOM 87 CG GLN A 760 46.330 46.254 65.796 1.00 64.04 C ANISOU 87 CG GLN A 760 6985 10176 7172 1352 -733 293 C ATOM 88 CD GLN A 760 47.789 45.852 65.856 1.00 63.52 C ANISOU 88 CD GLN A 760 6904 10121 7109 1197 -715 352 C ATOM 89 OE1 GLN A 760 48.671 46.703 65.969 1.00 63.93 O ANISOU 89 OE1 GLN A 760 7074 10087 7129 1114 -724 441 O ATOM 90 NE2 GLN A 760 48.053 44.553 65.780 1.00 62.73 N ANISOU 90 NE2 GLN A 760 6653 10122 7059 1157 -685 298 N ATOM 91 N THR A 761 42.522 44.089 67.565 1.00 68.89 N ANISOU 91 N THR A 761 7267 10848 8061 1599 -613 -104 N ATOM 92 CA THR A 761 41.804 43.271 68.537 1.00 66.60 C ANISOU 92 CA THR A 761 6895 10528 7883 1610 -527 -203 C ATOM 93 C THR A 761 42.461 41.899 68.594 1.00 66.63 C ANISOU 93 C THR A 761 6776 10590 7949 1516 -460 -232 C ATOM 94 O THR A 761 42.419 41.142 67.619 1.00 72.50 O ANISOU 94 O THR A 761 7378 11452 8716 1519 -462 -291 O ATOM 95 CB THR A 761 40.327 43.147 68.173 1.00 69.44 C ANISOU 95 CB THR A 761 7138 10942 8304 1742 -523 -329 C ATOM 96 OG1 THR A 761 39.771 44.452 67.970 1.00 74.10 O ANISOU 96 OG1 THR A 761 7841 11489 8823 1846 -593 -290 O ATOM 97 CG2 THR A 761 39.564 42.455 69.286 1.00 69.60 C ANISOU 97 CG2 THR A 761 7095 10901 8449 1750 -412 -422 C ATOM 98 N LYS A 762 43.062 41.583 69.735 1.00 74.53 N ANISOU 98 N LYS A 762 7836 11510 8971 1441 -400 -191 N ATOM 99 CA LYS A 762 43.634 40.269 69.987 1.00 73.38 C ANISOU 99 CA LYS A 762 7590 11400 8891 1370 -318 -210 C ATOM 100 C LYS A 762 42.634 39.461 70.801 1.00 72.77 C ANISOU 100 C LYS A 762 7436 11279 8932 1418 -197 -309 C ATOM 101 O LYS A 762 42.126 39.942 71.820 1.00 76.29 O ANISOU 101 O LYS A 762 7978 11626 9382 1458 -165 -306 O ATOM 102 CB LYS A 762 44.960 40.382 70.742 1.00 74.86 C ANISOU 102 CB LYS A 762 7886 11536 9021 1274 -326 -100 C ATOM 103 CG LYS A 762 45.991 41.307 70.101 1.00 73.89 C ANISOU 103 CG LYS A 762 7851 11429 8795 1212 -430 0 C ATOM 104 CD LYS A 762 46.877 40.566 69.119 1.00 76.33 C ANISOU 104 CD LYS A 762 8054 11845 9102 1147 -435 21 C ATOM 105 CE LYS A 762 48.012 41.442 68.624 1.00 76.79 C ANISOU 105 CE LYS A 762 8203 11903 9070 1072 -513 127 C ATOM 106 NZ LYS A 762 49.088 41.577 69.639 1.00 74.63 N ANISOU 106 NZ LYS A 762 8007 11572 8779 981 -518 192 N ATOM 107 N CYS A 763 42.342 38.246 70.349 1.00 61.77 N ANISOU 107 N CYS A 763 5874 9954 7640 1412 -120 -401 N ATOM 108 CA CYS A 763 41.417 37.360 71.046 1.00 61.95 C ANISOU 108 CA CYS A 763 5808 9930 7801 1446 23 -502 C ATOM 109 C CYS A 763 42.217 36.202 71.626 1.00 62.92 C ANISOU 109 C CYS A 763 5907 10028 7971 1378 135 -466 C ATOM 110 O CYS A 763 42.710 35.345 70.885 1.00 62.89 O ANISOU 110 O CYS A 763 5792 10100 8003 1330 154 -489 O ATOM 111 CB CYS A 763 40.319 36.856 70.112 1.00 63.95 C ANISOU 111 CB CYS A 763 5873 10268 8158 1497 41 -661 C ATOM 112 SG CYS A 763 39.290 38.165 69.395 1.00 68.84 S ANISOU 112 SG CYS A 763 6506 10934 8716 1610 -95 -708 S ATOM 113 N ALA A 764 42.347 36.185 72.951 1.00 60.60 N ANISOU 113 N ALA A 764 5725 9630 7671 1385 211 -407 N ATOM 114 CA ALA A 764 42.917 35.053 73.654 1.00 60.37 C ANISOU 114 CA ALA A 764 5681 9566 7690 1354 340 -373 C ATOM 115 C ALA A 764 41.800 34.068 73.988 1.00 60.85 C ANISOU 115 C ALA A 764 5630 9573 7916 1396 522 -487 C ATOM 116 O ALA A 764 40.637 34.264 73.627 1.00 61.35 O ANISOU 116 O ALA A 764 5610 9641 8058 1440 533 -602 O ATOM 117 CB ALA A 764 43.651 35.519 74.909 1.00 60.27 C ANISOU 117 CB ALA A 764 5849 9481 7570 1354 327 -253 C ATOM 118 N ASP A 765 42.151 32.991 74.689 1.00 86.79 N ANISOU 118 N ASP A 765 8909 12805 11261 1386 673 -456 N ATOM 119 CA ASP A 765 41.142 32.008 75.064 1.00 86.87 C ANISOU 119 CA ASP A 765 8820 12742 11443 1418 878 -557 C ATOM 120 C ASP A 765 40.205 32.564 76.131 1.00 85.84 C ANISOU 120 C ASP A 765 8787 12508 11323 1491 946 -566 C ATOM 121 O ASP A 765 38.981 32.438 76.018 1.00 87.61 O ANISOU 121 O ASP A 765 8908 12702 11677 1523 1030 -693 O ATOM 122 CB ASP A 765 41.812 30.720 75.548 1.00 85.57 C ANISOU 122 CB ASP A 765 8644 12533 11335 1400 1039 -502 C ATOM 123 CG ASP A 765 42.499 29.956 74.424 1.00 89.52 C ANISOU 123 CG ASP A 765 9012 13126 11875 1332 1016 -530 C ATOM 124 OD1 ASP A 765 41.987 29.973 73.283 1.00 91.39 O ANISOU 124 OD1 ASP A 765 9108 13442 12174 1306 959 -653 O ATOM 125 OD2 ASP A 765 43.551 29.333 74.682 1.00 90.10 O ANISOU 125 OD2 ASP A 765 9122 13200 11913 1313 1054 -431 O ATOM 126 N ASP A 766 40.761 33.132 77.201 1.00 79.11 N ANISOU 126 N ASP A 766 8123 11600 10337 1519 919 -443 N ATOM 127 CA ASP A 766 39.968 33.706 78.284 1.00 82.07 C ANISOU 127 CA ASP A 766 8612 11873 10696 1592 983 -442 C ATOM 128 C ASP A 766 39.866 35.230 78.256 1.00 80.77 C ANISOU 128 C ASP A 766 8561 11722 10406 1611 803 -421 C ATOM 129 O ASP A 766 39.166 35.795 79.103 1.00 76.87 O ANISOU 129 O ASP A 766 8164 11145 9899 1675 849 -429 O ATOM 130 CB ASP A 766 40.544 33.266 79.631 1.00 80.67 C ANISOU 130 CB ASP A 766 8582 11617 10451 1630 1097 -329 C ATOM 131 CG ASP A 766 41.997 33.655 79.792 1.00 82.00 C ANISOU 131 CG ASP A 766 8867 11845 10444 1596 945 -202 C ATOM 132 OD1 ASP A 766 42.634 33.995 78.771 1.00 80.38 O ANISOU 132 OD1 ASP A 766 8605 11736 10201 1527 789 -199 O ATOM 133 OD2 ASP A 766 42.504 33.612 80.932 1.00 84.28 O ANISOU 133 OD2 ASP A 766 9300 12090 10632 1642 984 -110 O ATOM 134 N ALA A 767 40.531 35.915 77.325 1.00 75.73 N ANISOU 134 N ALA A 767 7921 11174 9680 1561 615 -394 N ATOM 135 CA ALA A 767 40.638 37.366 77.429 1.00 72.79 C ANISOU 135 CA ALA A 767 7687 10790 9178 1575 461 -349 C ATOM 136 C ALA A 767 40.716 38.017 76.055 1.00 73.30 C ANISOU 136 C ALA A 767 7685 10947 9217 1547 304 -373 C ATOM 137 O ALA A 767 41.047 37.380 75.051 1.00 69.86 O ANISOU 137 O ALA A 767 7119 10602 8822 1502 285 -399 O ATOM 138 CB ALA A 767 41.861 37.773 78.259 1.00 71.71 C ANISOU 138 CB ALA A 767 7722 10634 8892 1543 393 -227 C ATOM 139 N MET A 768 40.410 39.315 76.042 1.00 71.69 N ANISOU 139 N MET A 768 7585 10715 8938 1582 199 -360 N ATOM 140 CA MET A 768 40.541 40.176 74.872 1.00 68.06 C ANISOU 140 CA MET A 768 7115 10324 8421 1574 48 -352 C ATOM 141 C MET A 768 41.552 41.268 75.189 1.00 68.70 C ANISOU 141 C MET A 768 7377 10366 8360 1528 -66 -241 C ATOM 142 O MET A 768 41.508 41.865 76.271 1.00 71.79 O ANISOU 142 O MET A 768 7912 10662 8702 1549 -53 -213 O ATOM 143 CB MET A 768 39.193 40.803 74.490 1.00 68.23 C ANISOU 143 CB MET A 768 7094 10340 8491 1672 32 -440 C ATOM 144 CG MET A 768 39.262 41.820 73.346 1.00 69.48 C ANISOU 144 CG MET A 768 7272 10558 8570 1694 -119 -416 C ATOM 145 SD MET A 768 37.765 42.816 73.165 1.00 72.35 S ANISOU 145 SD MET A 768 7637 10895 8957 1835 -149 -490 S ATOM 146 CE MET A 768 36.527 41.556 72.860 1.00 74.59 C ANISOU 146 CE MET A 768 7668 11251 9420 1885 -38 -664 C ATOM 147 N THR A 769 42.452 41.535 74.245 1.00 61.62 N ANISOU 147 N THR A 769 6471 9539 7402 1464 -171 -186 N ATOM 148 CA THR A 769 43.472 42.565 74.403 1.00 61.68 C ANISOU 148 CA THR A 769 6630 9510 7295 1403 -274 -90 C ATOM 149 C THR A 769 43.477 43.465 73.178 1.00 61.98 C ANISOU 149 C THR A 769 6678 9584 7289 1410 -376 -66 C ATOM 150 O THR A 769 43.485 42.977 72.043 1.00 61.82 O ANISOU 150 O THR A 769 6534 9665 7291 1409 -393 -86 O ATOM 151 CB THR A 769 44.860 41.950 74.601 1.00 61.17 C ANISOU 151 CB THR A 769 6558 9487 7196 1302 -283 -25 C ATOM 152 OG1 THR A 769 44.833 41.067 75.729 1.00 61.03 O ANISOU 152 OG1 THR A 769 6539 9441 7210 1318 -180 -37 O ATOM 153 CG2 THR A 769 45.909 43.035 74.837 1.00 61.42 C ANISOU 153 CG2 THR A 769 6733 9479 7127 1228 -385 53 C ATOM 154 N LEU A 770 43.485 44.774 73.413 1.00 62.55 N ANISOU 154 N LEU A 770 6903 9569 7294 1422 -437 -24 N ATOM 155 CA LEU A 770 43.569 45.770 72.356 1.00 63.05 C ANISOU 155 CA LEU A 770 7015 9640 7303 1436 -521 23 C ATOM 156 C LEU A 770 44.971 46.359 72.339 1.00 63.08 C ANISOU 156 C LEU A 770 7120 9613 7236 1317 -578 116 C ATOM 157 O LEU A 770 45.526 46.679 73.395 1.00 63.16 O ANISOU 157 O LEU A 770 7232 9545 7220 1257 -579 134 O ATOM 158 CB LEU A 770 42.532 46.877 72.559 1.00 63.89 C ANISOU 158 CB LEU A 770 7225 9654 7398 1543 -533 6 C ATOM 159 CG LEU A 770 41.062 46.454 72.533 1.00 64.12 C ANISOU 159 CG LEU A 770 7146 9712 7505 1670 -481 -96 C ATOM 160 CD1 LEU A 770 40.166 47.682 72.526 1.00 65.10 C ANISOU 160 CD1 LEU A 770 7374 9755 7605 1782 -510 -96 C ATOM 161 CD2 LEU A 770 40.749 45.564 71.338 1.00 63.94 C ANISOU 161 CD2 LEU A 770 6932 9836 7524 1700 -489 -151 C ATOM 162 N VAL A 771 45.537 46.495 71.143 1.00 72.98 N ANISOU 162 N VAL A 771 8340 10933 8458 1283 -623 168 N ATOM 163 CA VAL A 771 46.887 47.014 70.963 1.00 72.94 C ANISOU 163 CA VAL A 771 8406 10904 8404 1162 -665 253 C ATOM 164 C VAL A 771 46.848 48.108 69.906 1.00 71.79 C ANISOU 164 C VAL A 771 8342 10729 8207 1194 -704 317 C ATOM 165 O VAL A 771 46.208 47.948 68.862 1.00 71.95 O ANISOU 165 O VAL A 771 8293 10829 8217 1286 -711 309 O ATOM 166 CB VAL A 771 47.879 45.907 70.559 1.00 73.35 C ANISOU 166 CB VAL A 771 8328 11069 8471 1073 -655 268 C ATOM 167 CG1 VAL A 771 49.293 46.466 70.470 1.00 74.30 C ANISOU 167 CG1 VAL A 771 8513 11163 8554 942 -693 346 C ATOM 168 CG2 VAL A 771 47.824 44.757 71.553 1.00 74.44 C ANISOU 168 CG2 VAL A 771 8390 11235 8661 1068 -601 213 C ATOM 169 N LEU A 772 47.526 49.219 70.186 1.00 64.84 N ANISOU 169 N LEU A 772 7609 9734 7294 1122 -724 377 N ATOM 170 CA LEU A 772 47.637 50.342 69.265 1.00 65.84 C ANISOU 170 CA LEU A 772 7840 9802 7374 1142 -739 457 C ATOM 171 C LEU A 772 49.108 50.705 69.141 1.00 66.13 C ANISOU 171 C LEU A 772 7921 9804 7403 982 -744 525 C ATOM 172 O LEU A 772 49.725 51.139 70.119 1.00 66.37 O ANISOU 172 O LEU A 772 8026 9742 7449 883 -751 512 O ATOM 173 CB LEU A 772 46.826 51.542 69.759 1.00 66.77 C ANISOU 173 CB LEU A 772 8115 9773 7481 1224 -736 456 C ATOM 174 CG LEU A 772 46.854 52.793 68.879 1.00 68.03 C ANISOU 174 CG LEU A 772 8409 9846 7595 1265 -734 549 C ATOM 175 CD1 LEU A 772 46.213 52.524 67.530 1.00 68.22 C ANISOU 175 CD1 LEU A 772 8358 9989 7575 1400 -746 577 C ATOM 176 CD2 LEU A 772 46.157 53.954 69.576 1.00 68.97 C ANISOU 176 CD2 LEU A 772 8691 9800 7715 1332 -721 542 C ATOM 177 N LYS A 773 49.663 50.538 67.943 1.00 78.35 N ANISOU 177 N LYS A 773 9417 11428 8926 959 -738 589 N ATOM 178 CA LYS A 773 51.081 50.799 67.734 1.00 77.54 C ANISOU 178 CA LYS A 773 9332 11301 8829 804 -730 651 C ATOM 179 C LYS A 773 51.349 52.299 67.771 1.00 79.00 C ANISOU 179 C LYS A 773 9697 11312 9006 764 -711 711 C ATOM 180 O LYS A 773 50.638 53.085 67.139 1.00 79.25 O ANISOU 180 O LYS A 773 9828 11284 8999 875 -693 761 O ATOM 181 CB LYS A 773 51.535 50.211 66.401 1.00 76.50 C ANISOU 181 CB LYS A 773 9102 11296 8671 802 -714 704 C ATOM 182 CG LYS A 773 51.379 48.700 66.302 1.00 76.54 C ANISOU 182 CG LYS A 773 8923 11463 8695 825 -720 639 C ATOM 183 CD LYS A 773 51.854 48.184 64.949 1.00 82.67 C ANISOU 183 CD LYS A 773 9613 12360 9437 823 -702 687 C ATOM 184 CE LYS A 773 51.708 46.672 64.819 1.00 80.53 C ANISOU 184 CE LYS A 773 9161 12241 9197 842 -698 612 C ATOM 185 NZ LYS A 773 52.609 45.933 65.747 1.00 79.46 N ANISOU 185 NZ LYS A 773 8952 12116 9123 722 -690 587 N ATOM 186 N LYS A 774 52.384 52.694 68.516 1.00 85.54 N ANISOU 186 N LYS A 774 10566 12061 9874 608 -713 700 N ATOM 187 CA LYS A 774 52.704 54.112 68.642 1.00 86.94 C ANISOU 187 CA LYS A 774 10912 12056 10066 548 -684 738 C ATOM 188 C LYS A 774 53.172 54.696 67.316 1.00 87.83 C ANISOU 188 C LYS A 774 11074 12137 10161 534 -624 853 C ATOM 189 O LYS A 774 52.786 55.814 66.954 1.00 91.61 O ANISOU 189 O LYS A 774 11706 12478 10624 591 -578 915 O ATOM 190 CB LYS A 774 53.770 54.317 69.719 1.00 88.05 C ANISOU 190 CB LYS A 774 11057 12138 10259 373 -707 678 C ATOM 191 CG LYS A 774 53.221 54.459 71.127 1.00 85.68 C ANISOU 191 CG LYS A 774 10814 11779 9960 398 -746 579 C ATOM 192 CD LYS A 774 54.311 54.910 72.083 1.00 88.60 C ANISOU 192 CD LYS A 774 11211 12081 10371 229 -775 516 C ATOM 193 CE LYS A 774 53.765 55.210 73.467 1.00 90.75 C ANISOU 193 CE LYS A 774 11569 12283 10628 261 -810 417 C ATOM 194 NZ LYS A 774 54.792 55.840 74.343 1.00 90.83 N ANISOU 194 NZ LYS A 774 11622 12218 10671 100 -844 340 N ATOM 195 N GLU A 775 54.005 53.957 66.579 1.00100.47 N ANISOU 195 N GLU A 775 12554 13859 11762 466 -613 889 N ATOM 196 CA GLU A 775 54.518 54.461 65.308 1.00103.63 C ANISOU 196 CA GLU A 775 13002 14233 12139 452 -542 1004 C ATOM 197 C GLU A 775 53.380 54.888 64.390 1.00106.51 C ANISOU 197 C GLU A 775 13458 14591 12419 651 -521 1073 C ATOM 198 O GLU A 775 53.400 55.985 63.820 1.00109.77 O ANISOU 198 O GLU A 775 14023 14873 12812 679 -453 1168 O ATOM 199 CB GLU A 775 55.382 53.394 64.635 1.00101.73 C ANISOU 199 CB GLU A 775 12599 14154 11899 383 -536 1021 C ATOM 200 CG GLU A 775 55.900 53.776 63.250 1.00105.03 C ANISOU 200 CG GLU A 775 13059 14567 12280 382 -453 1142 C ATOM 201 CD GLU A 775 56.478 52.593 62.498 1.00107.94 C ANISOU 201 CD GLU A 775 13262 15118 12630 358 -451 1150 C ATOM 202 OE1 GLU A 775 56.771 51.563 63.140 1.00105.82 O ANISOU 202 OE1 GLU A 775 12849 14955 12404 301 -504 1067 O ATOM 203 OE2 GLU A 775 56.636 52.694 61.263 1.00106.31 O ANISOU 203 OE2 GLU A 775 13080 14948 12363 406 -390 1243 O ATOM 204 N LEU A 776 52.373 54.027 64.236 1.00 70.91 N ANISOU 204 N LEU A 776 8855 10223 7863 797 -575 1024 N ATOM 205 CA LEU A 776 51.248 54.353 63.366 1.00 71.51 C ANISOU 205 CA LEU A 776 8991 10324 7853 1002 -575 1071 C ATOM 206 C LEU A 776 50.548 55.624 63.830 1.00 72.62 C ANISOU 206 C LEU A 776 9314 10283 7995 1079 -556 1093 C ATOM 207 O LEU A 776 50.140 56.453 63.007 1.00 73.93 O ANISOU 207 O LEU A 776 9604 10388 8096 1202 -516 1190 O ATOM 208 CB LEU A 776 50.267 53.181 63.325 1.00 70.28 C ANISOU 208 CB LEU A 776 8680 10347 7675 1125 -641 976 C ATOM 209 CG LEU A 776 50.863 51.828 62.927 1.00 69.16 C ANISOU 209 CG LEU A 776 8353 10382 7542 1058 -654 938 C ATOM 210 CD1 LEU A 776 49.829 50.722 63.063 1.00 68.09 C ANISOU 210 CD1 LEU A 776 8070 10389 7412 1166 -705 825 C ATOM 211 CD2 LEU A 776 51.412 51.865 61.510 1.00 69.90 C ANISOU 211 CD2 LEU A 776 8452 10546 7562 1075 -614 1036 C ATOM 212 N VAL A 777 50.409 55.799 65.147 1.00 72.24 N ANISOU 212 N VAL A 777 9291 10144 8014 1016 -580 1008 N ATOM 213 CA VAL A 777 49.766 56.997 65.682 1.00 73.32 C ANISOU 213 CA VAL A 777 9602 10098 8160 1081 -557 1017 C ATOM 214 C VAL A 777 50.541 58.243 65.276 1.00 75.02 C ANISOU 214 C VAL A 777 9984 10130 8389 1002 -468 1123 C ATOM 215 O VAL A 777 49.954 59.297 65.002 1.00 76.36 O ANISOU 215 O VAL A 777 10317 10165 8533 1116 -421 1192 O ATOM 216 CB VAL A 777 49.634 56.889 67.213 1.00 72.65 C ANISOU 216 CB VAL A 777 9509 9956 8139 1009 -595 897 C ATOM 217 CG1 VAL A 777 49.072 58.177 67.808 1.00 73.89 C ANISOU 217 CG1 VAL A 777 9854 9909 8311 1059 -562 899 C ATOM 218 CG2 VAL A 777 48.749 55.710 67.588 1.00 71.20 C ANISOU 218 CG2 VAL A 777 9174 9931 7947 1105 -655 802 C ATOM 219 N ALA A 778 51.872 58.144 65.235 1.00 75.10 N ANISOU 219 N ALA A 778 9958 10127 8451 808 -435 1138 N ATOM 220 CA ALA A 778 52.691 59.301 64.887 1.00 76.84 C ANISOU 220 CA ALA A 778 10325 10162 8710 706 -332 1228 C ATOM 221 C ALA A 778 52.348 59.828 63.497 1.00 78.08 C ANISOU 221 C ALA A 778 10586 10299 8780 859 -256 1379 C ATOM 222 O ALA A 778 52.329 61.045 63.276 1.00 79.81 O ANISOU 222 O ALA A 778 10992 10323 9010 882 -162 1465 O ATOM 223 CB ALA A 778 54.173 58.936 64.976 1.00 76.71 C ANISOU 223 CB ALA A 778 10209 10170 8767 477 -312 1209 C ATOM 224 N HIS A 779 52.074 58.930 62.546 1.00 77.51 N ANISOU 224 N HIS A 779 10403 10428 8620 970 -292 1412 N ATOM 225 CA HIS A 779 51.719 59.372 61.199 1.00 78.81 C ANISOU 225 CA HIS A 779 10665 10602 8676 1139 -232 1553 C ATOM 226 C HIS A 779 50.455 60.222 61.197 1.00 79.78 C ANISOU 226 C HIS A 779 10936 10634 8743 1354 -234 1588 C ATOM 227 O HIS A 779 50.300 61.102 60.342 1.00 81.51 O ANISOU 227 O HIS A 779 11315 10761 8895 1474 -150 1726 O ATOM 228 CB HIS A 779 51.527 58.170 60.274 1.00 78.89 C ANISOU 228 CB HIS A 779 10514 10867 8592 1234 -291 1547 C ATOM 229 CG HIS A 779 52.776 57.383 60.033 1.00 78.09 C ANISOU 229 CG HIS A 779 10282 10856 8531 1052 -270 1540 C ATOM 230 ND1 HIS A 779 53.037 56.189 60.671 1.00 75.68 N ANISOU 230 ND1 HIS A 779 9784 10690 8280 951 -349 1416 N ATOM 231 CD2 HIS A 779 53.835 57.616 59.222 1.00 78.06 C ANISOU 231 CD2 HIS A 779 10315 10822 8524 959 -169 1645 C ATOM 232 CE1 HIS A 779 54.204 55.722 60.264 1.00 75.17 C ANISOU 232 CE1 HIS A 779 9638 10681 8243 807 -307 1443 C ATOM 233 NE2 HIS A 779 54.708 56.569 59.385 1.00 76.83 N ANISOU 233 NE2 HIS A 779 9979 10791 8422 805 -197 1577 N ATOM 234 N LEU A 780 49.538 59.970 62.135 1.00 78.67 N ANISOU 234 N LEU A 780 10745 10517 8627 1415 -321 1471 N ATOM 235 CA LEU A 780 48.254 60.659 62.151 1.00 79.53 C ANISOU 235 CA LEU A 780 10965 10566 8687 1634 -333 1490 C ATOM 236 C LEU A 780 48.320 62.042 62.786 1.00 81.00 C ANISOU 236 C LEU A 780 11362 10476 8940 1595 -246 1529 C ATOM 237 O LEU A 780 47.396 62.840 62.590 1.00 82.22 O ANISOU 237 O LEU A 780 11649 10544 9047 1786 -224 1586 O ATOM 238 CB LEU A 780 47.218 59.820 62.900 1.00 78.03 C ANISOU 238 CB LEU A 780 10631 10509 8509 1714 -446 1344 C ATOM 239 CG LEU A 780 46.859 58.469 62.287 1.00 76.76 C ANISOU 239 CG LEU A 780 10261 10615 8291 1788 -531 1285 C ATOM 240 CD1 LEU A 780 45.986 57.684 63.252 1.00 75.37 C ANISOU 240 CD1 LEU A 780 9948 10523 8166 1818 -611 1130 C ATOM 241 CD2 LEU A 780 46.150 58.648 60.955 1.00 77.92 C ANISOU 241 CD2 LEU A 780 10437 10863 8305 2023 -542 1372 C ATOM 242 N LYS A 781 49.373 62.343 63.542 1.00 96.64 N ANISOU 242 N LYS A 781 13370 12318 11029 1357 -198 1490 N ATOM 243 CA LYS A 781 49.514 63.647 64.189 1.00100.84 C ANISOU 243 CA LYS A 781 14096 12578 11639 1294 -109 1503 C ATOM 244 C LYS A 781 48.405 63.883 65.216 1.00100.51 C ANISOU 244 C LYS A 781 14090 12484 11614 1397 -166 1405 C ATOM 245 O LYS A 781 47.887 64.994 65.353 1.00103.01 O ANISOU 245 O LYS A 781 14587 12609 11940 1489 -99 1451 O ATOM 246 CB LYS A 781 49.541 64.776 63.153 1.00101.79 C ANISOU 246 CB LYS A 781 14419 12539 11718 1398 25 1681 C ATOM 247 CG LYS A 781 50.676 64.667 62.146 1.00102.07 C ANISOU 247 CG LYS A 781 14442 12596 11743 1292 111 1789 C ATOM 248 CD LYS A 781 52.031 64.833 62.815 1.00102.68 C ANISOU 248 CD LYS A 781 14496 12553 11963 990 167 1724 C ATOM 249 CE LYS A 781 53.166 64.691 61.820 1.00103.47 C ANISOU 249 CE LYS A 781 14569 12678 12065 880 262 1826 C ATOM 250 NZ LYS A 781 54.489 64.869 62.476 1.00103.76 N ANISOU 250 NZ LYS A 781 14565 12605 12255 584 313 1749 N ATOM 251 N CYS A 782 48.039 62.832 65.946 1.00 89.27 N ANISOU 251 N CYS A 782 12498 11224 10195 1384 -277 1273 N ATOM 252 CA CYS A 782 47.060 62.932 67.018 1.00 90.07 C ANISOU 252 CA CYS A 782 12617 11287 10320 1462 -324 1167 C ATOM 253 C CYS A 782 47.716 62.610 68.352 1.00 92.82 C ANISOU 253 C CYS A 782 12909 11608 10748 1255 -358 1030 C ATOM 254 O CYS A 782 48.634 61.788 68.431 1.00 92.41 O ANISOU 254 O CYS A 782 12724 11669 10717 1100 -394 992 O ATOM 255 CB CYS A 782 45.877 61.980 66.811 1.00 87.39 C ANISOU 255 CB CYS A 782 12131 11158 9917 1654 -414 1121 C ATOM 256 SG CYS A 782 45.082 62.084 65.209 1.00 93.26 S ANISOU 256 SG CYS A 782 12886 12009 10540 1915 -414 1252 S ATOM 257 N THR A 783 47.228 63.265 69.401 1.00 88.17 N ANISOU 257 N THR A 783 12427 10874 10199 1266 -349 955 N ATOM 258 CA THR A 783 47.596 62.948 70.774 1.00 85.24 C ANISOU 258 CA THR A 783 12013 10495 9879 1120 -395 812 C ATOM 259 C THR A 783 46.388 62.312 71.446 1.00 84.29 C ANISOU 259 C THR A 783 11822 10475 9730 1267 -454 727 C ATOM 260 O THR A 783 45.323 62.933 71.535 1.00 84.79 O ANISOU 260 O THR A 783 11983 10452 9782 1430 -428 736 O ATOM 261 CB THR A 783 48.044 64.199 71.531 1.00 89.23 C ANISOU 261 CB THR A 783 12699 10752 10453 1003 -330 773 C ATOM 262 OG1 THR A 783 49.209 64.745 70.900 1.00 90.68 O ANISOU 262 OG1 THR A 783 12933 10839 10683 850 -260 844 O ATOM 263 CG2 THR A 783 48.371 63.868 72.984 1.00 87.07 C ANISOU 263 CG2 THR A 783 12385 10490 10209 872 -391 613 C ATOM 264 N ILE A 784 46.553 61.079 71.910 1.00 84.43 N ANISOU 264 N ILE A 784 11670 10668 9743 1212 -522 648 N ATOM 265 CA ILE A 784 45.463 60.332 72.523 1.00 83.39 C ANISOU 265 CA ILE A 784 11451 10639 9596 1339 -561 567 C ATOM 266 C ILE A 784 45.439 60.658 74.010 1.00 83.85 C ANISOU 266 C ILE A 784 11592 10588 9679 1275 -560 456 C ATOM 267 O ILE A 784 46.414 60.406 74.726 1.00 84.88 O ANISOU 267 O ILE A 784 11700 10727 9823 1108 -587 395 O ATOM 268 CB ILE A 784 45.622 58.822 72.289 1.00 81.70 C ANISOU 268 CB ILE A 784 11022 10652 9368 1320 -614 539 C ATOM 269 CG1 ILE A 784 45.754 58.537 70.789 1.00 81.65 C ANISOU 269 CG1 ILE A 784 10942 10754 9328 1371 -616 640 C ATOM 270 CG2 ILE A 784 44.436 58.070 72.886 1.00 80.83 C ANISOU 270 CG2 ILE A 784 10823 10629 9259 1451 -630 455 C ATOM 271 CD1 ILE A 784 45.942 57.078 70.441 1.00 80.13 C ANISOU 271 CD1 ILE A 784 10543 10777 9128 1350 -659 612 C ATOM 272 N THR A 785 44.324 61.225 74.476 1.00 82.63 N ANISOU 272 N THR A 785 11531 10339 9525 1417 -532 426 N ATOM 273 CA THR A 785 44.183 61.524 75.897 1.00 81.84 C ANISOU 273 CA THR A 785 11517 10141 9436 1379 -525 316 C ATOM 274 C THR A 785 43.845 60.274 76.701 1.00 81.77 C ANISOU 274 C THR A 785 11370 10287 9412 1397 -560 229 C ATOM 275 O THR A 785 44.345 60.103 77.818 1.00 84.16 O ANISOU 275 O THR A 785 11694 10578 9704 1296 -578 144 O ATOM 276 CB THR A 785 43.111 62.594 76.110 1.00 84.20 C ANISOU 276 CB THR A 785 11972 10275 9746 1529 -468 317 C ATOM 277 OG1 THR A 785 41.967 62.298 75.302 1.00 86.42 O ANISOU 277 OG1 THR A 785 12177 10645 10013 1731 -466 370 O ATOM 278 CG2 THR A 785 43.644 63.973 75.754 1.00 84.68 C ANISOU 278 CG2 THR A 785 12217 10126 9833 1470 -412 378 C ATOM 279 N GLY A 786 43.004 59.391 76.165 1.00 78.85 N ANISOU 279 N GLY A 786 10858 10062 9039 1527 -566 245 N ATOM 280 CA GLY A 786 42.671 58.172 76.870 1.00 77.61 C ANISOU 280 CA GLY A 786 10569 10037 8882 1544 -575 169 C ATOM 281 C GLY A 786 42.122 57.101 75.937 1.00 76.59 C ANISOU 281 C GLY A 786 10251 10084 8766 1635 -585 193 C ATOM 282 O GLY A 786 41.558 57.409 74.890 1.00 77.01 O ANISOU 282 O GLY A 786 10287 10154 8819 1745 -587 249 O ATOM 283 N LEU A 787 42.298 55.852 76.353 1.00 70.41 N ANISOU 283 N LEU A 787 9331 9430 7991 1592 -590 145 N ATOM 284 CA LEU A 787 41.750 54.694 75.648 1.00 69.45 C ANISOU 284 CA LEU A 787 9017 9474 7898 1665 -588 137 C ATOM 285 C LEU A 787 41.229 53.717 76.691 1.00 68.76 C ANISOU 285 C LEU A 787 8853 9433 7839 1691 -540 52 C ATOM 286 O LEU A 787 41.981 53.299 77.577 1.00 68.36 O ANISOU 286 O LEU A 787 8821 9385 7768 1591 -538 30 O ATOM 287 CB LEU A 787 42.811 54.025 74.764 1.00 68.73 C ANISOU 287 CB LEU A 787 8819 9501 7795 1557 -629 191 C ATOM 288 CG LEU A 787 42.543 52.582 74.316 1.00 67.61 C ANISOU 288 CG LEU A 787 8470 9533 7685 1584 -621 159 C ATOM 289 CD1 LEU A 787 41.291 52.489 73.471 1.00 67.86 C ANISOU 289 CD1 LEU A 787 8414 9628 7743 1746 -616 138 C ATOM 290 CD2 LEU A 787 43.731 52.031 73.551 1.00 67.02 C ANISOU 290 CD2 LEU A 787 8314 9556 7594 1465 -657 213 C ATOM 291 N THR A 788 39.955 53.343 76.584 1.00 68.74 N ANISOU 291 N THR A 788 8763 9470 7886 1830 -498 3 N ATOM 292 CA THR A 788 39.330 52.484 77.580 1.00 68.32 C ANISOU 292 CA THR A 788 8646 9438 7873 1867 -423 -76 C ATOM 293 C THR A 788 38.333 51.553 76.902 1.00 67.94 C ANISOU 293 C THR A 788 8401 9510 7904 1966 -390 -125 C ATOM 294 O THR A 788 38.096 51.629 75.693 1.00 68.08 O ANISOU 294 O THR A 788 8336 9601 7929 2017 -438 -104 O ATOM 295 CB THR A 788 38.620 53.311 78.659 1.00 69.21 C ANISOU 295 CB THR A 788 8908 9409 7980 1940 -373 -118 C ATOM 296 OG1 THR A 788 37.465 53.950 78.099 1.00 70.00 O ANISOU 296 OG1 THR A 788 9003 9477 8117 2086 -364 -128 O ATOM 297 CG2 THR A 788 39.549 54.365 79.225 1.00 69.85 C ANISOU 297 CG2 THR A 788 9185 9365 7990 1844 -413 -88 C ATOM 298 N PHE A 789 37.749 50.669 77.706 1.00 67.62 N ANISOU 298 N PHE A 789 8285 9487 7920 1995 -301 -196 N ATOM 299 CA PHE A 789 36.577 49.903 77.317 1.00 67.61 C ANISOU 299 CA PHE A 789 8104 9566 8019 2096 -243 -274 C ATOM 300 C PHE A 789 35.331 50.675 77.749 1.00 68.64 C ANISOU 300 C PHE A 789 8290 9607 8184 2233 -198 -323 C ATOM 301 O PHE A 789 35.406 51.839 78.151 1.00 69.34 O ANISOU 301 O PHE A 789 8557 9576 8213 2253 -221 -287 O ATOM 302 CB PHE A 789 36.611 48.507 77.938 1.00 66.88 C ANISOU 302 CB PHE A 789 7898 9525 7987 2051 -145 -322 C ATOM 303 CG PHE A 789 37.521 47.544 77.237 1.00 65.95 C ANISOU 303 CG PHE A 789 7664 9525 7871 1952 -177 -295 C ATOM 304 CD1 PHE A 789 37.289 47.176 75.923 1.00 65.83 C ANISOU 304 CD1 PHE A 789 7490 9626 7895 1975 -224 -317 C ATOM 305 CD2 PHE A 789 38.590 46.980 77.904 1.00 65.33 C ANISOU 305 CD2 PHE A 789 7629 9445 7748 1847 -159 -252 C ATOM 306 CE1 PHE A 789 38.123 46.280 75.286 1.00 65.04 C ANISOU 306 CE1 PHE A 789 7286 9630 7797 1886 -245 -297 C ATOM 307 CE2 PHE A 789 39.420 46.083 77.274 1.00 64.55 C ANISOU 307 CE2 PHE A 789 7420 9450 7656 1764 -181 -227 C ATOM 308 CZ PHE A 789 39.189 45.733 75.964 1.00 64.38 C ANISOU 308 CZ PHE A 789 7247 9534 7679 1779 -219 -249 C ATOM 309 N TRP A 790 34.164 50.031 77.664 1.00 74.14 N ANISOU 309 N TRP A 790 8826 10357 8986 2327 -127 -414 N ATOM 310 CA TRP A 790 32.952 50.628 78.214 1.00 73.46 C ANISOU 310 CA TRP A 790 8774 10188 8948 2457 -64 -472 C ATOM 311 C TRP A 790 33.147 51.009 79.673 1.00 78.19 C ANISOU 311 C TRP A 790 9560 10646 9503 2430 12 -460 C ATOM 312 O TRP A 790 32.705 52.079 80.111 1.00 79.01 O ANISOU 312 O TRP A 790 9803 10637 9579 2504 17 -457 O ATOM 313 CB TRP A 790 31.778 49.660 78.079 1.00 74.24 C ANISOU 313 CB TRP A 790 8650 10368 9189 2533 25 -588 C ATOM 314 CG TRP A 790 31.123 49.666 76.732 1.00 80.41 C ANISOU 314 CG TRP A 790 9262 11275 10016 2624 -56 -634 C ATOM 315 CD1 TRP A 790 30.929 50.743 75.915 1.00 78.24 C ANISOU 315 CD1 TRP A 790 9043 11007 9678 2720 -165 -591 C ATOM 316 CD2 TRP A 790 30.575 48.536 76.044 1.00 78.76 C ANISOU 316 CD2 TRP A 790 8800 11208 9919 2635 -33 -739 C ATOM 317 NE1 TRP A 790 30.290 50.352 74.764 1.00 75.93 N ANISOU 317 NE1 TRP A 790 8547 10865 9436 2803 -223 -659 N ATOM 318 CE2 TRP A 790 30.064 49.002 74.817 1.00 76.09 C ANISOU 318 CE2 TRP A 790 8369 10973 9568 2745 -147 -761 C ATOM 319 CE3 TRP A 790 30.471 47.175 76.346 1.00 76.87 C ANISOU 319 CE3 TRP A 790 8404 11012 9790 2566 79 -819 C ATOM 320 CZ2 TRP A 790 29.453 48.157 73.895 1.00 78.44 C ANISOU 320 CZ2 TRP A 790 8417 11430 9956 2784 -168 -876 C ATOM 321 CZ3 TRP A 790 29.857 46.340 75.434 1.00 78.00 C ANISOU 321 CZ3 TRP A 790 8299 11295 10041 2593 74 -934 C ATOM 322 CH2 TRP A 790 29.363 46.832 74.218 1.00 78.69 C ANISOU 322 CH2 TRP A 790 8291 11498 10108 2699 -56 -969 C ATOM 323 N ASP A 791 33.804 50.150 80.435 1.00 73.28 N ANISOU 323 N ASP A 791 8947 10031 8866 2335 72 -455 N ATOM 324 CA ASP A 791 34.120 50.446 81.822 1.00 70.47 C ANISOU 324 CA ASP A 791 8772 9562 8440 2311 131 -443 C ATOM 325 C ASP A 791 35.256 51.460 81.858 1.00 69.68 C ANISOU 325 C ASP A 791 8856 9403 8217 2227 16 -370 C ATOM 326 O ASP A 791 36.384 51.116 81.478 1.00 69.65 O ANISOU 326 O ASP A 791 8835 9464 8166 2114 -56 -319 O ATOM 327 CB ASP A 791 34.528 49.165 82.553 1.00 73.33 C ANISOU 327 CB ASP A 791 9085 9965 8812 2250 227 -449 C ATOM 328 CG ASP A 791 34.588 49.335 84.065 1.00 73.82 C ANISOU 328 CG ASP A 791 9320 9925 8803 2264 313 -453 C ATOM 329 OD1 ASP A 791 34.614 50.489 84.543 1.00 75.53 O ANISOU 329 OD1 ASP A 791 9711 10042 8944 2286 273 -448 O ATOM 330 OD2 ASP A 791 34.618 48.307 84.775 1.00 69.85 O ANISOU 330 OD2 ASP A 791 8785 9439 8315 2259 426 -461 O ATOM 331 N PRO A 792 35.026 52.699 82.300 1.00 70.64 N ANISOU 331 N PRO A 792 9149 9398 8292 2272 2 -370 N ATOM 332 CA PRO A 792 36.143 53.655 82.382 1.00 70.88 C ANISOU 332 CA PRO A 792 9351 9359 8222 2175 -94 -316 C ATOM 333 C PRO A 792 37.257 53.188 83.297 1.00 70.47 C ANISOU 333 C PRO A 792 9368 9320 8088 2058 -101 -310 C ATOM 334 O PRO A 792 38.406 53.613 83.121 1.00 70.42 O ANISOU 334 O PRO A 792 9431 9308 8017 1945 -195 -269 O ATOM 335 CB PRO A 792 35.479 54.936 82.909 1.00 72.16 C ANISOU 335 CB PRO A 792 9681 9367 8368 2262 -68 -341 C ATOM 336 CG PRO A 792 34.195 54.490 83.520 1.00 72.47 C ANISOU 336 CG PRO A 792 9661 9397 8478 2387 56 -410 C ATOM 337 CD PRO A 792 33.757 53.299 82.739 1.00 71.66 C ANISOU 337 CD PRO A 792 9321 9437 8469 2410 80 -424 C ATOM 338 N SER A 793 36.950 52.317 84.262 1.00 70.31 N ANISOU 338 N SER A 793 9326 9319 8070 2090 -1 -348 N ATOM 339 CA SER A 793 37.977 51.778 85.146 1.00 70.05 C ANISOU 339 CA SER A 793 9353 9318 7947 2006 -8 -337 C ATOM 340 C SER A 793 39.109 51.123 84.368 1.00 69.09 C ANISOU 340 C SER A 793 9121 9312 7816 1890 -94 -282 C ATOM 341 O SER A 793 40.264 51.160 84.807 1.00 69.09 O ANISOU 341 O SER A 793 9192 9331 7728 1795 -162 -263 O ATOM 342 CB SER A 793 37.354 50.765 86.105 1.00 70.05 C ANISOU 342 CB SER A 793 9321 9332 7963 2081 137 -368 C ATOM 343 OG SER A 793 38.342 49.899 86.630 1.00 69.60 O ANISOU 343 OG SER A 793 9263 9349 7835 2015 132 -338 O ATOM 344 N CYS A 794 38.808 50.526 83.216 1.00 74.56 N ANISOU 344 N CYS A 794 9640 10090 8600 1899 -95 -264 N ATOM 345 CA CYS A 794 39.805 49.797 82.440 1.00 72.98 C ANISOU 345 CA CYS A 794 9324 10006 8401 1799 -159 -215 C ATOM 346 C CYS A 794 40.418 50.758 81.430 1.00 72.03 C ANISOU 346 C CYS A 794 9237 9874 8259 1733 -278 -170 C ATOM 347 O CYS A 794 39.765 51.154 80.460 1.00 72.23 O ANISOU 347 O CYS A 794 9211 9899 8336 1791 -293 -164 O ATOM 348 CB CYS A 794 39.167 48.589 81.756 1.00 70.65 C ANISOU 348 CB CYS A 794 8824 9808 8212 1842 -86 -232 C ATOM 349 SG CYS A 794 38.170 47.577 82.889 1.00 73.72 S ANISOU 349 SG CYS A 794 9177 10172 8660 1937 97 -290 S ATOM 350 N GLU A 795 41.679 51.120 81.653 1.00 79.53 N ANISOU 350 N GLU A 795 10269 10817 9133 1616 -358 -139 N ATOM 351 CA GLU A 795 42.382 52.088 80.827 1.00 80.10 C ANISOU 351 CA GLU A 795 10393 10855 9187 1537 -451 -94 C ATOM 352 C GLU A 795 43.598 51.433 80.191 1.00 80.44 C ANISOU 352 C GLU A 795 10332 11009 9222 1418 -511 -45 C ATOM 353 O GLU A 795 44.242 50.566 80.789 1.00 80.53 O ANISOU 353 O GLU A 795 10300 11093 9206 1371 -507 -50 O ATOM 354 CB GLU A 795 42.820 53.313 81.644 1.00 79.11 C ANISOU 354 CB GLU A 795 10464 10598 8998 1488 -488 -118 C ATOM 355 CG GLU A 795 41.673 54.163 82.174 1.00 82.85 C ANISOU 355 CG GLU A 795 11058 10942 9479 1603 -431 -162 C ATOM 356 CD GLU A 795 42.158 55.374 82.948 1.00 88.77 C ANISOU 356 CD GLU A 795 12003 11556 10170 1544 -465 -198 C ATOM 357 OE1 GLU A 795 43.389 55.553 83.059 1.00 89.63 O ANISOU 357 OE1 GLU A 795 12141 11676 10237 1409 -537 -195 O ATOM 358 OE2 GLU A 795 41.311 56.145 83.448 1.00 89.92 O ANISOU 358 OE2 GLU A 795 12266 11583 10317 1632 -417 -237 O ATOM 359 N ALA A 796 43.901 51.853 78.967 1.00 67.28 N ANISOU 359 N ALA A 796 8631 9356 7574 1381 -560 8 N ATOM 360 CA ALA A 796 45.055 51.316 78.266 1.00 66.69 C ANISOU 360 CA ALA A 796 8461 9382 7497 1269 -610 58 C ATOM 361 C ALA A 796 46.335 51.659 79.015 1.00 67.12 C ANISOU 361 C ALA A 796 8596 9411 7497 1138 -666 52 C ATOM 362 O ALA A 796 46.448 52.705 79.659 1.00 68.10 O ANISOU 362 O ALA A 796 8869 9418 7589 1112 -686 22 O ATOM 363 CB ALA A 796 45.117 51.863 76.840 1.00 66.87 C ANISOU 363 CB ALA A 796 8461 9409 7538 1263 -642 120 C ATOM 364 N GLU A 797 47.304 50.755 78.930 1.00 72.54 N ANISOU 364 N GLU A 797 9176 10211 8176 1058 -692 72 N ATOM 365 CA GLU A 797 48.607 50.932 79.549 1.00 72.33 C ANISOU 365 CA GLU A 797 9186 10194 8103 934 -758 61 C ATOM 366 C GLU A 797 49.652 51.177 78.469 1.00 72.80 C ANISOU 366 C GLU A 797 9187 10286 8188 813 -807 116 C ATOM 367 O GLU A 797 49.645 50.522 77.422 1.00 73.10 O ANISOU 367 O GLU A 797 9103 10409 8261 823 -789 167 O ATOM 368 CB GLU A 797 48.982 49.707 80.386 1.00 70.78 C ANISOU 368 CB GLU A 797 8916 10106 7873 947 -747 44 C ATOM 369 CG GLU A 797 50.327 49.831 81.085 1.00 73.91 C ANISOU 369 CG GLU A 797 9335 10538 8211 837 -830 21 C ATOM 370 CD GLU A 797 50.501 48.830 82.212 1.00 75.51 C ANISOU 370 CD GLU A 797 9518 10823 8350 894 -816 -1 C ATOM 371 OE1 GLU A 797 49.501 48.203 82.623 1.00 74.83 O ANISOU 371 OE1 GLU A 797 9435 10732 8265 1015 -726 -4 O ATOM 372 OE2 GLU A 797 51.644 48.671 82.691 1.00 74.74 O ANISOU 372 OE2 GLU A 797 9401 10797 8202 822 -889 -15 O ATOM 373 N ASP A 798 50.546 52.126 78.730 1.00 69.37 N ANISOU 373 N ASP A 798 8838 9779 7738 697 -861 98 N ATOM 374 CA ASP A 798 51.580 52.506 77.776 1.00 68.61 C ANISOU 374 CA ASP A 798 8702 9690 7676 571 -892 147 C ATOM 375 C ASP A 798 52.828 51.673 78.037 1.00 69.19 C ANISOU 375 C ASP A 798 8658 9893 7740 473 -942 139 C ATOM 376 O ASP A 798 53.478 51.822 79.077 1.00 74.63 O ANISOU 376 O ASP A 798 9381 10584 8391 415 -997 73 O ATOM 377 CB ASP A 798 51.883 53.997 77.887 1.00 71.32 C ANISOU 377 CB ASP A 798 9194 9873 8032 488 -906 124 C ATOM 378 CG ASP A 798 53.171 54.386 77.185 1.00 77.27 C ANISOU 378 CG ASP A 798 9908 10625 8827 328 -930 157 C ATOM 379 OD1 ASP A 798 53.551 53.707 76.208 1.00 81.66 O ANISOU 379 OD1 ASP A 798 10340 11282 9405 311 -918 227 O ATOM 380 OD2 ASP A 798 53.807 55.374 77.610 1.00 78.30 O ANISOU 380 OD2 ASP A 798 10127 10648 8975 216 -952 105 O ATOM 381 N ARG A 799 53.171 50.808 77.087 1.00 81.77 N ANISOU 381 N ARG A 799 10109 11597 9362 461 -927 202 N ATOM 382 CA ARG A 799 54.397 50.026 77.147 1.00 83.43 C ANISOU 382 CA ARG A 799 10195 11931 9574 372 -968 207 C ATOM 383 C ARG A 799 55.547 50.704 76.416 1.00 84.55 C ANISOU 383 C ARG A 799 10316 12052 9759 220 -996 233 C ATOM 384 O ARG A 799 56.641 50.136 76.336 1.00 84.11 O ANISOU 384 O ARG A 799 10144 12098 9716 136 -1029 239 O ATOM 385 CB ARG A 799 54.155 48.633 76.566 1.00 81.76 C ANISOU 385 CB ARG A 799 9837 11849 9378 443 -924 252 C ATOM 386 CG ARG A 799 52.849 48.003 77.037 1.00 81.29 C ANISOU 386 CG ARG A 799 9791 11791 9306 593 -865 231 C ATOM 387 CD ARG A 799 53.062 46.603 77.577 1.00 81.29 C ANISOU 387 CD ARG A 799 9685 11906 9296 637 -841 228 C ATOM 388 NE ARG A 799 53.902 46.600 78.769 1.00 82.02 N ANISOU 388 NE ARG A 799 9813 12022 9328 599 -900 193 N ATOM 389 CZ ARG A 799 54.325 45.501 79.384 1.00 81.05 C ANISOU 389 CZ ARG A 799 9618 11999 9177 637 -892 198 C ATOM 390 NH1 ARG A 799 53.989 44.303 78.923 1.00 82.69 N ANISOU 390 NH1 ARG A 799 9716 12275 9427 701 -813 236 N ATOM 391 NH2 ARG A 799 55.087 45.599 80.463 1.00 79.15 N ANISOU 391 NH2 ARG A 799 9418 11791 8866 616 -960 162 N ATOM 392 N GLY A 800 55.309 51.893 75.868 1.00 92.87 N ANISOU 392 N GLY A 800 11479 12970 10839 189 -971 253 N ATOM 393 CA GLY A 800 56.320 52.745 75.298 1.00 92.84 C ANISOU 393 CA GLY A 800 11488 12903 10885 40 -973 272 C ATOM 394 C GLY A 800 56.572 52.539 73.818 1.00 89.37 C ANISOU 394 C GLY A 800 10974 12504 10480 23 -921 373 C ATOM 395 O GLY A 800 56.974 53.488 73.138 1.00 91.44 O ANISOU 395 O GLY A 800 11299 12663 10782 -58 -883 413 O ATOM 396 N ASP A 801 56.351 51.331 73.297 1.00118.11 N ANISOU 396 N ASP A 801 14488 16284 14106 98 -907 412 N ATOM 397 CA ASP A 801 56.248 51.131 71.857 1.00116.69 C ANISOU 397 CA ASP A 801 14258 16143 13935 125 -853 502 C ATOM 398 C ASP A 801 54.814 50.946 71.378 1.00114.37 C ANISOU 398 C ASP A 801 13996 15850 13608 294 -820 524 C ATOM 399 O ASP A 801 54.577 50.956 70.166 1.00116.36 O ANISOU 399 O ASP A 801 14233 16128 13852 339 -782 591 O ATOM 400 CB ASP A 801 57.081 49.914 71.433 1.00115.38 C ANISOU 400 CB ASP A 801 13916 16139 13785 82 -856 523 C ATOM 401 CG ASP A 801 56.547 48.615 72.001 1.00122.09 C ANISOU 401 CG ASP A 801 14674 17101 14612 183 -868 485 C ATOM 402 OD1 ASP A 801 55.780 48.666 72.987 1.00125.82 O ANISOU 402 OD1 ASP A 801 15215 17531 15059 257 -883 431 O ATOM 403 OD2 ASP A 801 56.899 47.543 71.466 1.00122.91 O ANISOU 403 OD2 ASP A 801 14641 17329 14728 188 -849 509 O ATOM 404 N LYS A 802 53.860 50.780 72.290 1.00 78.60 N ANISOU 404 N LYS A 802 9506 11300 9057 392 -832 464 N ATOM 405 CA LYS A 802 52.473 50.534 71.922 1.00 74.90 C ANISOU 405 CA LYS A 802 9043 10844 8572 551 -802 465 C ATOM 406 C LYS A 802 51.596 50.800 73.135 1.00 76.46 C ANISOU 406 C LYS A 802 9330 10964 8757 625 -808 395 C ATOM 407 O LYS A 802 52.079 50.880 74.267 1.00 76.34 O ANISOU 407 O LYS A 802 9352 10921 8734 564 -837 344 O ATOM 408 CB LYS A 802 52.277 49.106 71.405 1.00 73.80 C ANISOU 408 CB LYS A 802 8736 10862 8440 606 -785 463 C ATOM 409 CG LYS A 802 52.457 48.036 72.463 1.00 74.43 C ANISOU 409 CG LYS A 802 8736 11013 8531 601 -790 407 C ATOM 410 CD LYS A 802 52.725 46.676 71.841 1.00 76.45 C ANISOU 410 CD LYS A 802 8824 11413 8810 607 -764 417 C ATOM 411 CE LYS A 802 52.932 45.611 72.908 1.00 75.85 C ANISOU 411 CE LYS A 802 8681 11395 8744 614 -754 376 C ATOM 412 NZ LYS A 802 53.439 44.329 72.339 1.00 75.02 N ANISOU 412 NZ LYS A 802 8418 11416 8669 600 -722 392 N ATOM 413 N PHE A 803 50.299 50.942 72.883 1.00 68.87 N ANISOU 413 N PHE A 803 8401 9976 7790 765 -780 389 N ATOM 414 CA PHE A 803 49.296 51.034 73.937 1.00 68.87 C ANISOU 414 CA PHE A 803 8466 9916 7785 857 -767 322 C ATOM 415 C PHE A 803 48.524 49.723 73.983 1.00 67.81 C ANISOU 415 C PHE A 803 8196 9896 7672 953 -732 284 C ATOM 416 O PHE A 803 47.934 49.313 72.977 1.00 67.47 O ANISOU 416 O PHE A 803 8066 9924 7646 1027 -715 297 O ATOM 417 CB PHE A 803 48.348 52.207 73.694 1.00 69.75 C ANISOU 417 CB PHE A 803 8710 9902 7889 950 -751 335 C ATOM 418 CG PHE A 803 49.035 53.539 73.661 1.00 70.97 C ANISOU 418 CG PHE A 803 9011 9918 8038 859 -761 370 C ATOM 419 CD1 PHE A 803 49.537 54.098 74.822 1.00 71.60 C ANISOU 419 CD1 PHE A 803 9189 9903 8114 772 -780 315 C ATOM 420 CD2 PHE A 803 49.175 54.234 72.472 1.00 71.66 C ANISOU 420 CD2 PHE A 803 9141 9965 8122 862 -745 454 C ATOM 421 CE1 PHE A 803 50.171 55.323 74.800 1.00 72.89 C ANISOU 421 CE1 PHE A 803 9479 9926 8290 675 -780 330 C ATOM 422 CE2 PHE A 803 49.808 55.463 72.446 1.00 72.95 C ANISOU 422 CE2 PHE A 803 9443 9979 8296 772 -731 488 C ATOM 423 CZ PHE A 803 50.304 56.008 73.613 1.00 73.57 C ANISOU 423 CZ PHE A 803 9608 9955 8389 671 -747 419 C ATOM 424 N VAL A 804 48.528 49.069 75.143 1.00 68.08 N ANISOU 424 N VAL A 804 8216 9946 7705 955 -717 233 N ATOM 425 CA VAL A 804 47.867 47.783 75.320 1.00 66.69 C ANISOU 425 CA VAL A 804 7919 9858 7564 1034 -660 195 C ATOM 426 C VAL A 804 46.767 47.931 76.362 1.00 67.58 C ANISOU 426 C VAL A 804 8106 9893 7678 1135 -612 136 C ATOM 427 O VAL A 804 46.954 48.594 77.388 1.00 69.61 O ANISOU 427 O VAL A 804 8492 10063 7892 1115 -629 117 O ATOM 428 CB VAL A 804 48.867 46.681 75.729 1.00 65.51 C ANISOU 428 CB VAL A 804 7676 9802 7412 962 -658 202 C ATOM 429 CG1 VAL A 804 49.446 46.960 77.106 1.00 69.90 C ANISOU 429 CG1 VAL A 804 8333 10310 7916 922 -685 181 C ATOM 430 CG2 VAL A 804 48.201 45.315 75.680 1.00 67.51 C ANISOU 430 CG2 VAL A 804 7796 10135 7719 1039 -577 172 C ATOM 431 N LEU A 805 45.613 47.328 76.082 1.00 63.71 N ANISOU 431 N LEU A 805 7529 9435 7242 1242 -550 98 N ATOM 432 CA LEU A 805 44.488 47.290 77.012 1.00 63.93 C ANISOU 432 CA LEU A 805 7600 9399 7292 1344 -480 38 C ATOM 433 C LEU A 805 43.937 45.871 77.042 1.00 63.27 C ANISOU 433 C LEU A 805 7364 9396 7281 1393 -389 -5 C ATOM 434 O LEU A 805 43.381 45.398 76.047 1.00 63.01 O ANISOU 434 O LEU A 805 7199 9432 7309 1432 -372 -29 O ATOM 435 CB LEU A 805 43.409 48.288 76.594 1.00 64.59 C ANISOU 435 CB LEU A 805 7742 9411 7389 1438 -486 20 C ATOM 436 CG LEU A 805 42.059 48.183 77.299 1.00 64.87 C ANISOU 436 CG LEU A 805 7782 9395 7469 1559 -403 -50 C ATOM 437 CD1 LEU A 805 42.200 48.372 78.800 1.00 65.20 C ANISOU 437 CD1 LEU A 805 7957 9349 7467 1551 -367 -69 C ATOM 438 CD2 LEU A 805 41.076 49.194 76.720 1.00 65.62 C ANISOU 438 CD2 LEU A 805 7921 9434 7577 1660 -423 -61 C ATOM 439 N ARG A 806 44.056 45.208 78.188 1.00 63.17 N ANISOU 439 N ARG A 806 7372 9370 7261 1399 -323 -18 N ATOM 440 CA ARG A 806 43.617 43.829 78.343 1.00 62.71 C ANISOU 440 CA ARG A 806 7185 9363 7279 1440 -210 -51 C ATOM 441 C ARG A 806 42.456 43.759 79.325 1.00 63.16 C ANISOU 441 C ARG A 806 7288 9339 7371 1541 -99 -107 C ATOM 442 O ARG A 806 42.465 44.426 80.366 1.00 63.71 O ANISOU 442 O ARG A 806 7510 9327 7370 1562 -102 -102 O ATOM 443 CB ARG A 806 44.759 42.931 78.830 1.00 62.34 C ANISOU 443 CB ARG A 806 7116 9371 7197 1377 -197 -6 C ATOM 444 CG ARG A 806 44.367 41.464 78.985 1.00 61.98 C ANISOU 444 CG ARG A 806 6947 9363 7238 1420 -60 -30 C ATOM 445 CD ARG A 806 45.432 40.667 79.713 1.00 61.86 C ANISOU 445 CD ARG A 806 6947 9385 7173 1389 -38 26 C ATOM 446 NE ARG A 806 44.961 39.327 80.054 1.00 61.76 N ANISOU 446 NE ARG A 806 6849 9373 7243 1446 124 10 N ATOM 447 CZ ARG A 806 44.090 39.064 81.025 1.00 62.24 C ANISOU 447 CZ ARG A 806 6965 9356 7328 1534 254 -16 C ATOM 448 NH1 ARG A 806 43.579 40.049 81.754 1.00 62.80 N ANISOU 448 NH1 ARG A 806 7174 9350 7339 1579 233 -34 N ATOM 449 NH2 ARG A 806 43.720 37.813 81.266 1.00 62.26 N ANISOU 449 NH2 ARG A 806 6887 9349 7420 1578 418 -26 N ATOM 450 N SER A 807 41.464 42.941 78.989 1.00 63.04 N ANISOU 450 N SER A 807 7136 9347 7469 1601 4 -168 N ATOM 451 CA SER A 807 40.310 42.722 79.843 1.00 63.54 C ANISOU 451 CA SER A 807 7214 9336 7593 1695 137 -227 C ATOM 452 C SER A 807 39.885 41.267 79.749 1.00 63.30 C ANISOU 452 C SER A 807 7021 9344 7685 1710 281 -272 C ATOM 453 O SER A 807 39.891 40.678 78.664 1.00 62.90 O ANISOU 453 O SER A 807 6813 9377 7708 1678 267 -302 O ATOM 454 CB SER A 807 39.138 43.623 79.444 1.00 64.10 C ANISOU 454 CB SER A 807 7284 9366 7706 1772 117 -286 C ATOM 455 OG SER A 807 37.914 43.103 79.931 1.00 64.54 O ANISOU 455 OG SER A 807 7274 9380 7869 1856 264 -365 O ATOM 456 N ALA A 808 39.523 40.695 80.892 1.00 70.19 N ANISOU 456 N ALA A 808 7941 10150 8580 1760 428 -277 N ATOM 457 CA ALA A 808 38.927 39.371 80.901 1.00 68.19 C ANISOU 457 CA ALA A 808 7545 9898 8467 1783 602 -329 C ATOM 458 C ALA A 808 37.543 39.427 80.270 1.00 70.37 C ANISOU 458 C ALA A 808 7683 10171 8885 1833 652 -446 C ATOM 459 O ALA A 808 36.848 40.446 80.329 1.00 71.33 O ANISOU 459 O ALA A 808 7861 10253 8989 1888 603 -477 O ATOM 460 CB ALA A 808 38.832 38.830 82.327 1.00 68.58 C ANISOU 460 CB ALA A 808 7699 9862 8497 1838 765 -296 C ATOM 461 N TYR A 809 37.144 38.312 79.660 1.00 74.58 N ANISOU 461 N TYR A 809 8026 10747 9565 1817 751 -519 N ATOM 462 CA TYR A 809 35.845 38.253 79.001 1.00 72.69 C ANISOU 462 CA TYR A 809 7621 10525 9473 1861 793 -654 C ATOM 463 C TYR A 809 34.705 38.568 79.959 1.00 76.53 C ANISOU 463 C TYR A 809 8156 10904 10018 1948 921 -703 C ATOM 464 O TYR A 809 33.638 39.016 79.526 1.00 78.10 O ANISOU 464 O TYR A 809 8263 11114 10298 2004 907 -802 O ATOM 465 CB TYR A 809 35.651 36.871 78.383 1.00 71.86 C ANISOU 465 CB TYR A 809 7307 10468 9527 1820 908 -739 C ATOM 466 CG TYR A 809 36.509 36.606 77.164 1.00 73.41 C ANISOU 466 CG TYR A 809 7414 10788 9690 1746 777 -727 C ATOM 467 CD1 TYR A 809 36.868 37.633 76.297 1.00 74.02 C ANISOU 467 CD1 TYR A 809 7525 10944 9653 1741 572 -697 C ATOM 468 CD2 TYR A 809 36.963 35.325 76.880 1.00 72.42 C ANISOU 468 CD2 TYR A 809 7176 10692 9647 1686 873 -742 C ATOM 469 CE1 TYR A 809 37.654 37.390 75.187 1.00 71.38 C ANISOU 469 CE1 TYR A 809 7116 10721 9283 1679 466 -681 C ATOM 470 CE2 TYR A 809 37.749 35.077 75.770 1.00 71.30 C ANISOU 470 CE2 TYR A 809 6955 10662 9472 1622 761 -734 C ATOM 471 CZ TYR A 809 38.091 36.111 74.929 1.00 70.66 C ANISOU 471 CZ TYR A 809 6911 10665 9273 1619 558 -703 C ATOM 472 OH TYR A 809 38.873 35.863 73.825 1.00 72.65 O ANISOU 472 OH TYR A 809 7091 11027 9487 1560 460 -691 O ATOM 473 N SER A 810 34.900 38.325 81.251 1.00 90.60 N ANISOU 473 N SER A 810 10078 12588 11756 1970 1050 -637 N ATOM 474 CA SER A 810 33.889 38.599 82.261 1.00 89.04 C ANISOU 474 CA SER A 810 9949 12281 11602 2055 1190 -673 C ATOM 475 C SER A 810 34.089 39.944 82.951 1.00 91.12 C ANISOU 475 C SER A 810 10431 12492 11699 2099 1082 -607 C ATOM 476 O SER A 810 33.357 40.257 83.895 1.00 95.05 O ANISOU 476 O SER A 810 11017 12894 12204 2174 1195 -624 O ATOM 477 CB SER A 810 33.878 37.472 83.291 1.00 93.59 C ANISOU 477 CB SER A 810 10554 12773 12232 2070 1425 -643 C ATOM 478 OG SER A 810 35.201 37.092 83.623 1.00 94.71 O ANISOU 478 OG SER A 810 10804 12938 12243 2028 1386 -522 O ATOM 479 N SER A 811 35.057 40.742 82.507 1.00 66.94 N ANISOU 479 N SER A 811 7457 9484 8494 2051 879 -538 N ATOM 480 CA SER A 811 35.431 41.981 83.175 1.00 67.16 C ANISOU 480 CA SER A 811 7699 9456 8363 2072 777 -478 C ATOM 481 C SER A 811 35.302 43.160 82.218 1.00 67.12 C ANISOU 481 C SER A 811 7691 9483 8329 2073 601 -494 C ATOM 482 O SER A 811 35.156 42.999 81.006 1.00 66.99 O ANISOU 482 O SER A 811 7519 9553 8381 2053 533 -532 O ATOM 483 CB SER A 811 36.865 41.907 83.719 1.00 67.00 C ANISOU 483 CB SER A 811 7817 9454 8188 2010 708 -373 C ATOM 484 OG SER A 811 36.949 41.036 84.833 1.00 67.05 O ANISOU 484 OG SER A 811 7880 9413 8180 2044 871 -341 O ATOM 485 N CYS A 812 35.329 44.362 82.796 1.00 66.86 N ANISOU 485 N CYS A 812 7838 9374 8190 2105 537 -466 N ATOM 486 CA CYS A 812 35.341 45.609 82.030 1.00 66.99 C ANISOU 486 CA CYS A 812 7900 9394 8159 2111 379 -458 C ATOM 487 C CYS A 812 34.066 45.774 81.207 1.00 67.48 C ANISOU 487 C CYS A 812 7813 9481 8344 2197 392 -544 C ATOM 488 O CYS A 812 34.083 46.311 80.099 1.00 67.43 O ANISOU 488 O CYS A 812 7757 9535 8331 2202 267 -540 O ATOM 489 CB CYS A 812 36.580 45.691 81.137 1.00 66.22 C ANISOU 489 CB CYS A 812 7792 9379 7989 2008 229 -390 C ATOM 490 SG CYS A 812 38.127 45.720 82.065 1.00 65.90 S ANISOU 490 SG CYS A 812 7921 9321 7798 1911 180 -301 S ATOM 491 N GLY A 813 32.945 45.322 81.762 1.00 84.17 N ANISOU 491 N GLY A 813 9858 11553 10571 2272 547 -623 N ATOM 492 CA GLY A 813 31.667 45.498 81.097 1.00 85.20 C ANISOU 492 CA GLY A 813 9837 11711 10826 2364 561 -721 C ATOM 493 C GLY A 813 31.557 44.773 79.777 1.00 84.23 C ANISOU 493 C GLY A 813 9485 11725 10794 2339 510 -779 C ATOM 494 O GLY A 813 30.788 45.194 78.906 1.00 83.10 O ANISOU 494 O GLY A 813 9231 11640 10701 2414 441 -844 O ATOM 495 N MET A 814 32.307 43.688 79.603 1.00 73.55 N ANISOU 495 N MET A 814 8060 10429 9457 2244 541 -760 N ATOM 496 CA MET A 814 32.180 42.879 78.401 1.00 72.51 C ANISOU 496 CA MET A 814 7704 10425 9420 2216 511 -833 C ATOM 497 C MET A 814 30.751 42.373 78.263 1.00 73.44 C ANISOU 497 C MET A 814 7621 10560 9724 2289 625 -986 C ATOM 498 O MET A 814 30.045 42.155 79.251 1.00 74.04 O ANISOU 498 O MET A 814 7711 10540 9882 2328 788 -1026 O ATOM 499 CB MET A 814 33.150 41.700 78.449 1.00 71.63 C ANISOU 499 CB MET A 814 7556 10347 9315 2108 566 -793 C ATOM 500 CG MET A 814 34.607 42.081 78.237 1.00 70.76 C ANISOU 500 CG MET A 814 7580 10263 9042 2026 428 -665 C ATOM 501 SD MET A 814 35.019 42.411 76.517 1.00 70.44 S ANISOU 501 SD MET A 814 7440 10365 8959 2002 239 -662 S ATOM 502 CE MET A 814 36.689 43.030 76.688 1.00 69.67 C ANISOU 502 CE MET A 814 7543 10248 8682 1905 120 -504 C ATOM 503 N GLN A 815 30.321 42.197 77.017 1.00 95.41 N ANISOU 503 N GLN A 815 10210 13470 12571 2311 540 -1078 N ATOM 504 CA GLN A 815 28.962 41.780 76.700 1.00 96.71 C ANISOU 504 CA GLN A 815 10149 13679 12916 2381 616 -1248 C ATOM 505 C GLN A 815 29.023 40.436 75.991 1.00 97.60 C ANISOU 505 C GLN A 815 10040 13889 13153 2303 668 -1350 C ATOM 506 O GLN A 815 29.694 40.305 74.962 1.00 97.63 O ANISOU 506 O GLN A 815 9998 14007 13091 2261 536 -1333 O ATOM 507 CB GLN A 815 28.270 42.831 75.831 1.00 97.61 C ANISOU 507 CB GLN A 815 10219 13874 12995 2500 457 -1291 C ATOM 508 CG GLN A 815 26.759 42.758 75.840 1.00101.79 C ANISOU 508 CG GLN A 815 10560 14421 13693 2603 533 -1457 C ATOM 509 CD GLN A 815 26.122 44.016 75.286 1.00105.72 C ANISOU 509 CD GLN A 815 11077 14965 14124 2750 384 -1462 C ATOM 510 OE1 GLN A 815 26.759 45.066 75.209 1.00106.65 O ANISOU 510 OE1 GLN A 815 11400 15049 14072 2776 263 -1323 O ATOM 511 NE2 GLN A 815 24.860 43.918 74.898 1.00107.22 N ANISOU 511 NE2 GLN A 815 11051 15231 14455 2849 397 -1625 N ATOM 512 N VAL A 816 28.331 39.443 76.542 1.00 92.05 N ANISOU 512 N VAL A 816 9206 13132 12635 2283 872 -1458 N ATOM 513 CA VAL A 816 28.295 38.096 75.984 1.00 91.10 C ANISOU 513 CA VAL A 816 8871 13078 12667 2204 959 -1574 C ATOM 514 C VAL A 816 26.928 37.906 75.344 1.00 91.99 C ANISOU 514 C VAL A 816 8718 13273 12961 2266 974 -1788 C ATOM 515 O VAL A 816 25.912 37.802 76.043 1.00 92.71 O ANISOU 515 O VAL A 816 8744 13284 13199 2308 1131 -1877 O ATOM 516 CB VAL A 816 28.556 37.027 77.054 1.00 92.83 C ANISOU 516 CB VAL A 816 9130 13165 12977 2130 1201 -1541 C ATOM 517 CG1 VAL A 816 28.519 35.630 76.439 1.00 92.65 C ANISOU 517 CG1 VAL A 816 8886 13194 13125 2044 1304 -1666 C ATOM 518 CG2 VAL A 816 29.893 37.273 77.745 1.00 92.56 C ANISOU 518 CG2 VAL A 816 9355 13063 12749 2087 1170 -1335 C ATOM 519 N SER A 817 26.897 37.863 74.015 1.00106.26 N ANISOU 519 N SER A 817 10368 15249 14756 2276 813 -1878 N ATOM 520 CA SER A 817 25.660 37.605 73.293 1.00108.90 C ANISOU 520 CA SER A 817 10424 15696 15258 2334 803 -2104 C ATOM 521 C SER A 817 26.001 37.125 71.892 1.00109.73 C ANISOU 521 C SER A 817 10368 15982 15340 2302 659 -2193 C ATOM 522 O SER A 817 27.112 37.330 71.398 1.00110.69 O ANISOU 522 O SER A 817 10620 16152 15288 2265 532 -2059 O ATOM 523 CB SER A 817 24.772 38.851 73.233 1.00111.29 C ANISOU 523 CB SER A 817 10742 16029 15514 2488 689 -2123 C ATOM 524 OG SER A 817 23.542 38.562 72.588 1.00113.90 O ANISOU 524 OG SER A 817 10783 16478 16016 2551 680 -2356 O ATOM 525 N ALA A 818 25.020 36.482 71.259 1.00120.06 N ANISOU 525 N ALA A 818 11389 17397 16833 2315 683 -2430 N ATOM 526 CA ALA A 818 25.144 36.038 69.871 1.00120.51 C ANISOU 526 CA ALA A 818 11263 17648 16875 2303 540 -2557 C ATOM 527 C ALA A 818 26.423 35.232 69.660 1.00119.57 C ANISOU 527 C ALA A 818 11217 17515 16699 2169 570 -2465 C ATOM 528 O ALA A 818 27.077 35.322 68.618 1.00119.83 O ANISOU 528 O ALA A 818 11253 17685 16593 2169 403 -2439 O ATOM 529 CB ALA A 818 25.088 37.230 68.915 1.00120.03 C ANISOU 529 CB ALA A 818 11247 17744 16614 2446 273 -2515 C ATOM 530 N SER A 819 26.787 34.437 70.666 1.00105.00 N ANISOU 530 N SER A 819 9437 15503 14957 2064 791 -2408 N ATOM 531 CA SER A 819 27.974 33.585 70.599 1.00104.62 C ANISOU 531 CA SER A 819 9453 15423 14873 1943 849 -2320 C ATOM 532 C SER A 819 29.242 34.406 70.382 1.00103.27 C ANISOU 532 C SER A 819 9523 15279 14436 1949 673 -2090 C ATOM 533 O SER A 819 30.235 33.906 69.848 1.00103.15 O ANISOU 533 O SER A 819 9527 15312 14353 1874 636 -2037 O ATOM 534 CB SER A 819 27.834 32.530 69.499 1.00104.46 C ANISOU 534 CB SER A 819 9179 15535 14977 1880 845 -2524 C ATOM 535 OG SER A 819 28.900 31.599 69.551 1.00103.29 O ANISOU 535 OG SER A 819 9084 15333 14829 1763 940 -2447 O ATOM 536 N MET A 820 29.217 35.671 70.794 1.00 91.02 N ANISOU 536 N MET A 820 8152 13690 12740 2036 575 -1959 N ATOM 537 CA MET A 820 30.346 36.573 70.628 1.00 88.36 C ANISOU 537 CA MET A 820 8044 13364 12165 2042 417 -1752 C ATOM 538 C MET A 820 30.490 37.426 71.878 1.00 89.36 C ANISOU 538 C MET A 820 8406 13334 12214 2071 461 -1595 C ATOM 539 O MET A 820 29.518 37.671 72.597 1.00 90.02 O ANISOU 539 O MET A 820 8473 13339 12391 2133 552 -1653 O ATOM 540 CB MET A 820 30.170 37.480 69.401 1.00 88.16 C ANISOU 540 CB MET A 820 7990 13500 12006 2142 187 -1771 C ATOM 541 CG MET A 820 30.130 36.746 68.068 1.00 90.53 C ANISOU 541 CG MET A 820 8078 13981 12338 2126 112 -1920 C ATOM 542 SD MET A 820 31.766 36.326 67.434 1.00 91.03 S ANISOU 542 SD MET A 820 8239 14090 12259 2015 54 -1783 S ATOM 543 CE MET A 820 32.393 37.945 66.995 1.00 87.64 C ANISOU 543 CE MET A 820 8043 13693 11564 2103 -156 -1580 C ATOM 544 N ILE A 821 31.715 37.876 72.131 1.00 91.04 N ANISOU 544 N ILE A 821 8833 13503 12257 2025 397 -1405 N ATOM 545 CA ILE A 821 32.016 38.777 73.238 1.00 88.92 C ANISOU 545 CA ILE A 821 8803 13100 11884 2047 408 -1256 C ATOM 546 C ILE A 821 32.345 40.131 72.633 1.00 88.44 C ANISOU 546 C ILE A 821 8873 13086 11645 2108 206 -1160 C ATOM 547 O ILE A 821 33.370 40.289 71.959 1.00 90.58 O ANISOU 547 O ILE A 821 9203 13418 11794 2058 95 -1069 O ATOM 548 CB ILE A 821 33.170 38.257 74.104 1.00 87.45 C ANISOU 548 CB ILE A 821 8759 12819 11647 1948 497 -1124 C ATOM 549 CG1 ILE A 821 32.878 36.818 74.524 1.00 87.71 C ANISOU 549 CG1 ILE A 821 8654 12810 11860 1895 707 -1214 C ATOM 550 CG2 ILE A 821 33.379 39.177 75.309 1.00 86.92 C ANISOU 550 CG2 ILE A 821 8928 12621 11476 1978 510 -999 C ATOM 551 CD1 ILE A 821 33.938 36.195 75.376 1.00 87.93 C ANISOU 551 CD1 ILE A 821 8810 12754 11845 1822 809 -1088 C ATOM 552 N SER A 822 31.483 41.111 72.880 1.00 69.19 N ANISOU 552 N SER A 822 6482 10610 9196 2218 173 -1176 N ATOM 553 CA SER A 822 31.587 42.418 72.256 1.00 69.68 C ANISOU 553 CA SER A 822 6656 10707 9110 2300 1 -1098 C ATOM 554 C SER A 822 31.837 43.488 73.309 1.00 70.53 C ANISOU 554 C SER A 822 7010 10663 9125 2318 9 -971 C ATOM 555 O SER A 822 31.300 43.428 74.420 1.00 69.25 O ANISOU 555 O SER A 822 6886 10390 9035 2334 136 -997 O ATOM 556 CB SER A 822 30.318 42.750 71.464 1.00 70.53 C ANISOU 556 CB SER A 822 6602 10920 9275 2440 -68 -1233 C ATOM 557 OG SER A 822 29.166 42.649 72.283 1.00 76.05 O ANISOU 557 OG SER A 822 7229 11549 10118 2498 57 -1337 O ATOM 558 N ASN A 823 32.675 44.452 72.947 1.00 75.18 N ANISOU 558 N ASN A 823 7767 11242 9556 2312 -118 -839 N ATOM 559 CA ASN A 823 32.888 45.655 73.733 1.00 72.35 C ANISOU 559 CA ASN A 823 7641 10748 9103 2337 -137 -733 C ATOM 560 C ASN A 823 33.159 46.786 72.750 1.00 71.91 C ANISOU 560 C ASN A 823 7674 10727 8921 2397 -289 -652 C ATOM 561 O ASN A 823 33.127 46.593 71.532 1.00 75.42 O ANISOU 561 O ASN A 823 8002 11309 9347 2430 -374 -679 O ATOM 562 CB ASN A 823 34.030 45.464 74.736 1.00 72.59 C ANISOU 562 CB ASN A 823 7826 10680 9076 2211 -83 -635 C ATOM 563 CG ASN A 823 33.861 46.309 75.989 1.00 74.89 C ANISOU 563 CG ASN A 823 8309 10817 9328 2241 -33 -593 C ATOM 564 OD1 ASN A 823 33.492 47.481 75.922 1.00 75.94 O ANISOU 564 OD1 ASN A 823 8549 10895 9409 2322 -94 -566 O ATOM 565 ND2 ASN A 823 34.126 45.707 77.146 1.00 70.58 N ANISOU 565 ND2 ASN A 823 7815 10200 8804 2183 83 -587 N ATOM 566 N GLU A 824 33.412 47.975 73.282 1.00 81.50 N ANISOU 566 N GLU A 824 9103 11817 10049 2417 -315 -556 N ATOM 567 CA GLU A 824 33.770 49.120 72.458 1.00 84.86 C ANISOU 567 CA GLU A 824 9648 12239 10355 2467 -434 -457 C ATOM 568 C GLU A 824 35.013 49.783 73.024 1.00 84.99 C ANISOU 568 C GLU A 824 9884 12133 10274 2351 -446 -330 C ATOM 569 O GLU A 824 35.155 49.928 74.243 1.00 86.16 O ANISOU 569 O GLU A 824 10145 12162 10431 2304 -378 -324 O ATOM 570 CB GLU A 824 32.629 50.139 72.372 1.00 87.68 C ANISOU 570 CB GLU A 824 10042 12557 10715 2642 -457 -480 C ATOM 571 CG GLU A 824 31.499 49.717 71.445 1.00 89.56 C ANISOU 571 CG GLU A 824 10057 12951 11020 2778 -494 -598 C ATOM 572 CD GLU A 824 30.517 50.835 71.157 1.00 93.05 C ANISOU 572 CD GLU A 824 10543 13373 11437 2969 -545 -598 C ATOM 573 OE1 GLU A 824 30.803 51.992 71.529 1.00 93.72 O ANISOU 573 OE1 GLU A 824 10848 13318 11445 2993 -553 -488 O ATOM 574 OE2 GLU A 824 29.459 50.557 70.553 1.00 92.56 O ANISOU 574 OE2 GLU A 824 10292 13438 11437 3099 -576 -712 O ATOM 575 N ALA A 825 35.907 50.191 72.128 1.00 68.57 N ANISOU 575 N ALA A 825 7864 10087 8103 2309 -531 -235 N ATOM 576 CA ALA A 825 37.112 50.915 72.507 1.00 68.36 C ANISOU 576 CA ALA A 825 8031 9948 7993 2195 -550 -123 C ATOM 577 C ALA A 825 36.783 52.400 72.494 1.00 69.55 C ANISOU 577 C ALA A 825 8360 9974 8091 2288 -577 -62 C ATOM 578 O ALA A 825 36.523 52.976 71.432 1.00 70.35 O ANISOU 578 O ALA A 825 8469 10116 8146 2388 -635 -17 O ATOM 579 CB ALA A 825 38.258 50.596 71.551 1.00 67.82 C ANISOU 579 CB ALA A 825 7933 9968 7868 2095 -607 -52 C ATOM 580 N VAL A 826 36.791 53.020 73.670 1.00 69.79 N ANISOU 580 N VAL A 826 8541 9852 8122 2263 -530 -60 N ATOM 581 CA VAL A 826 36.467 54.434 73.799 1.00 71.00 C ANISOU 581 CA VAL A 826 8877 9863 8239 2347 -536 -12 C ATOM 582 C VAL A 826 37.778 55.207 73.773 1.00 71.12 C ANISOU 582 C VAL A 826 9063 9777 8183 2215 -564 89 C ATOM 583 O VAL A 826 38.586 55.117 74.702 1.00 70.65 O ANISOU 583 O VAL A 826 9075 9652 8116 2078 -544 82 O ATOM 584 CB VAL A 826 35.673 54.720 75.077 1.00 71.40 C ANISOU 584 CB VAL A 826 8996 9799 8334 2401 -462 -81 C ATOM 585 CG1 VAL A 826 35.287 56.193 75.142 1.00 72.78 C ANISOU 585 CG1 VAL A 826 9356 9821 8477 2499 -463 -34 C ATOM 586 CG2 VAL A 826 34.435 53.840 75.139 1.00 71.31 C ANISOU 586 CG2 VAL A 826 8793 9887 8415 2509 -416 -190 C ATOM 587 N VAL A 827 37.983 55.972 72.707 1.00 77.01 N ANISOU 587 N VAL A 827 9872 10511 8877 2262 -607 179 N ATOM 588 CA VAL A 827 39.201 56.740 72.498 1.00 75.74 C ANISOU 588 CA VAL A 827 9862 10252 8665 2139 -620 277 C ATOM 589 C VAL A 827 38.867 58.215 72.647 1.00 79.25 C ANISOU 589 C VAL A 827 10510 10510 9092 2220 -593 327 C ATOM 590 O VAL A 827 37.845 58.688 72.135 1.00 83.71 O ANISOU 590 O VAL A 827 11082 11075 9650 2404 -595 341 O ATOM 591 CB VAL A 827 39.816 56.452 71.115 1.00 74.33 C ANISOU 591 CB VAL A 827 9611 10191 8439 2120 -664 356 C ATOM 592 CG1 VAL A 827 41.115 57.227 70.931 1.00 76.84 C ANISOU 592 CG1 VAL A 827 10078 10397 8722 1979 -657 454 C ATOM 593 CG2 VAL A 827 40.060 54.967 70.963 1.00 73.75 C ANISOU 593 CG2 VAL A 827 9332 10297 8392 2052 -682 295 C ATOM 594 N ASN A 828 39.723 58.934 73.363 1.00 74.13 N ANISOU 594 N ASN A 828 10022 9704 8438 2085 -568 346 N ATOM 595 CA ASN A 828 39.596 60.373 73.531 1.00 75.67 C ANISOU 595 CA ASN A 828 10428 9696 8627 2130 -529 393 C ATOM 596 C ASN A 828 40.852 61.036 72.991 1.00 76.27 C ANISOU 596 C ASN A 828 10615 9683 8680 1993 -522 487 C ATOM 597 O ASN A 828 41.967 60.682 73.386 1.00 75.62 O ANISOU 597 O ASN A 828 10515 9611 8606 1804 -535 466 O ATOM 598 CB ASN A 828 39.379 60.744 74.999 1.00 75.90 C ANISOU 598 CB ASN A 828 10562 9592 8685 2095 -488 303 C ATOM 599 CG ASN A 828 37.971 60.450 75.469 1.00 75.87 C ANISOU 599 CG ASN A 828 10493 9624 8712 2264 -464 227 C ATOM 600 OD1 ASN A 828 37.050 61.235 75.239 1.00 77.03 O ANISOU 600 OD1 ASN A 828 10709 9694 8864 2428 -440 248 O ATOM 601 ND2 ASN A 828 37.795 59.315 76.135 1.00 74.67 N ANISOU 601 ND2 ASN A 828 10205 9585 8583 2229 -462 140 N ATOM 602 N ILE A 829 40.662 61.994 72.089 1.00 91.93 N ANISOU 602 N ILE A 829 12711 11581 10638 2097 -496 592 N ATOM 603 CA ILE A 829 41.751 62.693 71.423 1.00 89.47 C ANISOU 603 CA ILE A 829 12512 11171 10313 1989 -465 697 C ATOM 604 C ILE A 829 41.735 64.146 71.865 1.00 92.03 C ANISOU 604 C ILE A 829 13067 11236 10664 1994 -388 724 C ATOM 605 O ILE A 829 40.666 64.739 72.050 1.00 95.54 O ANISOU 605 O ILE A 829 13590 11602 11110 2167 -362 721 O ATOM 606 CB ILE A 829 41.636 62.591 69.890 1.00 93.32 C ANISOU 606 CB ILE A 829 12952 11769 10738 2110 -478 815 C ATOM 607 CG1 ILE A 829 40.190 62.845 69.446 1.00 95.50 C ANISOU 607 CG1 ILE A 829 13223 12083 10980 2380 -490 831 C ATOM 608 CG2 ILE A 829 42.139 61.238 69.415 1.00 90.83 C ANISOU 608 CG2 ILE A 829 12430 11678 10404 2030 -539 792 C ATOM 609 CD1 ILE A 829 40.016 62.963 67.950 1.00 94.72 C ANISOU 609 CD1 ILE A 829 13115 12077 10797 2533 -504 952 C ATOM 610 N LEU A 830 42.927 64.720 72.027 1.00 80.84 N ANISOU 610 N LEU A 830 11755 9683 9279 1801 -347 745 N ATOM 611 CA LEU A 830 43.026 66.112 72.449 1.00 82.65 C ANISOU 611 CA LEU A 830 12206 9647 9551 1778 -261 758 C ATOM 612 C LEU A 830 42.301 67.046 71.487 1.00 84.96 C ANISOU 612 C LEU A 830 12629 9838 9815 1986 -195 892 C ATOM 613 O LEU A 830 41.797 68.096 71.902 1.00 87.61 O ANISOU 613 O LEU A 830 13135 9974 10179 2063 -127 893 O ATOM 614 CB LEU A 830 44.495 66.514 72.566 1.00 83.21 C ANISOU 614 CB LEU A 830 12339 9605 9671 1529 -223 758 C ATOM 615 CG LEU A 830 44.778 67.890 73.169 1.00 85.12 C ANISOU 615 CG LEU A 830 12799 9563 9981 1450 -130 734 C ATOM 616 CD1 LEU A 830 44.339 67.946 74.626 1.00 86.43 C ANISOU 616 CD1 LEU A 830 12996 9678 10165 1432 -157 577 C ATOM 617 CD2 LEU A 830 46.253 68.223 73.038 1.00 85.82 C ANISOU 617 CD2 LEU A 830 12916 9561 10130 1205 -89 739 C ATOM 618 N SER A 831 42.236 66.686 70.205 1.00115.43 N ANISOU 618 N SER A 831 16417 13831 13611 2090 -213 1006 N ATOM 619 CA SER A 831 41.628 67.573 69.219 1.00117.18 C ANISOU 619 CA SER A 831 16771 13968 13785 2303 -153 1149 C ATOM 620 C SER A 831 40.118 67.665 69.405 1.00118.84 C ANISOU 620 C SER A 831 16968 14214 13970 2558 -183 1118 C ATOM 621 O SER A 831 39.541 68.754 69.304 1.00121.93 O ANISOU 621 O SER A 831 17532 14434 14362 2709 -111 1186 O ATOM 622 CB SER A 831 41.965 67.087 67.813 1.00117.32 C ANISOU 622 CB SER A 831 16709 14145 13722 2356 -174 1269 C ATOM 623 OG SER A 831 43.366 66.958 67.659 1.00119.64 O ANISOU 623 OG SER A 831 16999 14410 14048 2118 -140 1292 O ATOM 624 N SER A 832 39.464 66.540 69.680 1.00110.64 N ANISOU 624 N SER A 832 15726 13391 12920 2609 -279 1014 N ATOM 625 CA SER A 832 38.011 66.470 69.751 1.00110.83 C ANISOU 625 CA SER A 832 15693 13489 12930 2851 -313 974 C ATOM 626 C SER A 832 37.578 66.146 71.173 1.00109.69 C ANISOU 626 C SER A 832 15504 13320 12854 2790 -321 817 C ATOM 627 O SER A 832 38.109 65.219 71.793 1.00107.44 O ANISOU 627 O SER A 832 15099 13129 12594 2617 -359 722 O ATOM 628 CB SER A 832 37.469 65.417 68.782 1.00110.68 C ANISOU 628 CB SER A 832 15459 13748 12846 2985 -408 975 C ATOM 629 OG SER A 832 36.061 65.312 68.885 1.00111.91 O ANISOU 629 OG SER A 832 15533 13984 13003 3210 -445 914 O ATOM 630 N SER A 833 36.603 66.906 71.678 1.00135.98 N ANISOU 630 N SER A 833 18934 16525 16208 2944 -278 795 N ATOM 631 CA SER A 833 36.084 66.660 73.018 1.00135.22 C ANISOU 631 CA SER A 833 18809 16400 16169 2913 -270 651 C ATOM 632 C SER A 833 35.286 65.364 73.073 1.00134.96 C ANISOU 632 C SER A 833 18530 16609 16141 2987 -341 556 C ATOM 633 O SER A 833 35.309 64.656 74.086 1.00133.83 O ANISOU 633 O SER A 833 18307 16505 16035 2881 -344 440 O ATOM 634 CB SER A 833 35.215 67.834 73.467 1.00136.34 C ANISOU 634 CB SER A 833 19123 16343 16337 3073 -195 657 C ATOM 635 OG SER A 833 35.966 69.033 73.537 1.00138.85 O ANISOU 635 OG SER A 833 19676 16411 16670 2985 -111 726 O ATOM 636 N SER A 834 34.574 65.035 71.996 1.00119.99 N ANISOU 636 N SER A 834 16509 14875 14206 3173 -394 600 N ATOM 637 CA SER A 834 33.702 63.868 72.010 1.00117.54 C ANISOU 637 CA SER A 834 15956 14783 13920 3254 -451 494 C ATOM 638 C SER A 834 34.528 62.585 71.903 1.00114.63 C ANISOU 638 C SER A 834 15422 14581 13550 3068 -500 451 C ATOM 639 O SER A 834 35.531 62.550 71.183 1.00112.74 O ANISOU 639 O SER A 834 15209 14365 13263 2966 -520 536 O ATOM 640 CB SER A 834 32.698 63.937 70.863 1.00117.43 C ANISOU 640 CB SER A 834 15850 14904 13864 3513 -504 536 C ATOM 641 OG SER A 834 31.841 65.056 71.010 1.00119.89 O ANISOU 641 OG SER A 834 16298 15072 14181 3707 -459 570 O ATOM 642 N PRO A 835 34.136 61.522 72.605 1.00 79.10 N ANISOU 642 N PRO A 835 10757 10191 9106 3025 -506 325 N ATOM 643 CA PRO A 835 34.887 60.265 72.516 1.00 77.42 C ANISOU 643 CA PRO A 835 10388 10131 8898 2862 -541 287 C ATOM 644 C PRO A 835 34.656 59.546 71.195 1.00 77.22 C ANISOU 644 C PRO A 835 10183 10319 8840 2950 -613 303 C ATOM 645 O PRO A 835 33.593 59.645 70.577 1.00 78.12 O ANISOU 645 O PRO A 835 10216 10517 8948 3153 -644 287 O ATOM 646 CB PRO A 835 34.343 59.446 73.693 1.00 76.52 C ANISOU 646 CB PRO A 835 10169 10046 8857 2829 -502 153 C ATOM 647 CG PRO A 835 32.968 59.975 73.907 1.00 77.68 C ANISOU 647 CG PRO A 835 10321 10151 9043 3033 -472 109 C ATOM 648 CD PRO A 835 33.040 61.440 73.584 1.00 79.26 C ANISOU 648 CD PRO A 835 10738 10181 9194 3117 -461 216 C ATOM 649 N GLN A 836 35.680 58.808 70.769 1.00106.23 N ANISOU 649 N GLN A 836 13787 14087 12489 2797 -642 327 N ATOM 650 CA GLN A 836 35.618 57.972 69.577 1.00103.30 C ANISOU 650 CA GLN A 836 13238 13927 12085 2848 -708 326 C ATOM 651 C GLN A 836 35.383 56.527 69.993 1.00101.83 C ANISOU 651 C GLN A 836 12831 13886 11972 2778 -709 193 C ATOM 652 O GLN A 836 36.085 56.007 70.866 1.00102.79 O ANISOU 652 O GLN A 836 12957 13967 12131 2606 -671 163 O ATOM 653 CB GLN A 836 36.908 58.082 68.765 1.00102.66 C ANISOU 653 CB GLN A 836 13223 13852 11931 2730 -725 440 C ATOM 654 CG GLN A 836 36.955 59.277 67.829 1.00104.95 C ANISOU 654 CG GLN A 836 13676 14064 12135 2853 -727 580 C ATOM 655 CD GLN A 836 36.021 59.127 66.641 1.00107.37 C ANISOU 655 CD GLN A 836 13873 14544 12379 3082 -793 584 C ATOM 656 OE1 GLN A 836 35.988 58.080 65.992 1.00104.79 O ANISOU 656 OE1 GLN A 836 13358 14421 12038 3082 -849 527 O ATOM 657 NE2 GLN A 836 35.253 60.172 66.354 1.00109.06 N ANISOU 657 NE2 GLN A 836 14203 14683 12553 3286 -789 645 N ATOM 658 N ARG A 837 34.404 55.883 69.363 1.00 77.93 N ANISOU 658 N ARG A 837 9613 11028 8969 2916 -748 111 N ATOM 659 CA ARG A 837 33.991 54.534 69.724 1.00 77.35 C ANISOU 659 CA ARG A 837 9321 11081 8989 2870 -730 -28 C ATOM 660 C ARG A 837 34.193 53.603 68.538 1.00 76.35 C ANISOU 660 C ARG A 837 9016 11160 8836 2867 -794 -54 C ATOM 661 O ARG A 837 33.737 53.896 67.428 1.00 76.88 O ANISOU 661 O ARG A 837 9042 11332 8839 3019 -865 -36 O ATOM 662 CB ARG A 837 32.526 54.509 70.173 1.00 77.65 C ANISOU 662 CB ARG A 837 9260 11132 9112 3024 -703 -144 C ATOM 663 CG ARG A 837 32.244 55.361 71.395 1.00 77.34 C ANISOU 663 CG ARG A 837 9390 10893 9102 3035 -630 -133 C ATOM 664 CD ARG A 837 30.777 55.321 71.789 1.00 78.16 C ANISOU 664 CD ARG A 837 9385 11016 9298 3194 -594 -248 C ATOM 665 NE ARG A 837 30.549 55.995 73.066 1.00 78.83 N ANISOU 665 NE ARG A 837 9627 10911 9413 3188 -508 -249 N ATOM 666 CZ ARG A 837 30.555 55.399 74.255 1.00 80.10 C ANISOU 666 CZ ARG A 837 9775 11016 9643 3086 -417 -319 C ATOM 667 NH1 ARG A 837 30.765 54.095 74.360 1.00 80.30 N ANISOU 667 NH1 ARG A 837 9636 11148 9725 2981 -389 -388 N ATOM 668 NH2 ARG A 837 30.344 56.115 75.352 1.00 81.85 N ANISOU 668 NH2 ARG A 837 10158 11069 9874 3097 -345 -317 N ATOM 669 N LYS A 838 34.874 52.485 68.781 1.00 73.00 N ANISOU 669 N LYS A 838 8489 10792 8454 2704 -767 -97 N ATOM 670 CA LYS A 838 35.048 51.429 67.794 1.00 72.01 C ANISOU 670 CA LYS A 838 8176 10858 8325 2684 -810 -148 C ATOM 671 C LYS A 838 34.572 50.119 68.401 1.00 71.30 C ANISOU 671 C LYS A 838 7890 10833 8367 2627 -748 -297 C ATOM 672 O LYS A 838 35.008 49.745 69.494 1.00 70.23 O ANISOU 672 O LYS A 838 7796 10603 8287 2500 -669 -301 O ATOM 673 CB LYS A 838 36.511 51.301 67.355 1.00 71.25 C ANISOU 673 CB LYS A 838 8152 10764 8155 2532 -824 -40 C ATOM 674 CG LYS A 838 36.776 50.126 66.420 1.00 70.71 C ANISOU 674 CG LYS A 838 7894 10885 8087 2495 -855 -98 C ATOM 675 CD LYS A 838 38.246 50.007 66.075 1.00 72.41 C ANISOU 675 CD LYS A 838 8180 11093 8239 2341 -856 9 C ATOM 676 CE LYS A 838 38.501 48.821 65.158 1.00 71.98 C ANISOU 676 CE LYS A 838 7941 11222 8186 2307 -879 -54 C ATOM 677 NZ LYS A 838 39.923 48.742 64.718 1.00 72.76 N ANISOU 677 NZ LYS A 838 8103 11321 8219 2171 -878 55 N ATOM 678 N LYS A 839 33.690 49.423 67.691 1.00 77.60 N ANISOU 678 N LYS A 839 8475 11794 9214 2723 -779 -423 N ATOM 679 CA LYS A 839 33.161 48.158 68.177 1.00 76.28 C ANISOU 679 CA LYS A 839 8108 11684 9193 2671 -703 -577 C ATOM 680 C LYS A 839 34.188 47.049 67.991 1.00 75.53 C ANISOU 680 C LYS A 839 7941 11647 9109 2507 -677 -575 C ATOM 681 O LYS A 839 34.691 46.832 66.884 1.00 75.54 O ANISOU 681 O LYS A 839 7896 11770 9038 2501 -749 -553 O ATOM 682 CB LYS A 839 31.865 47.804 67.451 1.00 76.74 C ANISOU 682 CB LYS A 839 7946 11898 9313 2824 -747 -733 C ATOM 683 CG LYS A 839 30.698 48.715 67.802 1.00 82.23 C ANISOU 683 CG LYS A 839 8673 12539 10033 2992 -753 -762 C ATOM 684 CD LYS A 839 29.347 48.095 67.452 1.00 83.73 C ANISOU 684 CD LYS A 839 8599 12871 10341 3109 -762 -961 C ATOM 685 CE LYS A 839 29.036 46.858 68.301 1.00 85.02 C ANISOU 685 CE LYS A 839 8602 13013 10689 2991 -624 -1100 C ATOM 686 NZ LYS A 839 29.166 47.099 69.775 1.00 80.62 N ANISOU 686 NZ LYS A 839 8198 12252 10182 2917 -494 -1040 N ATOM 687 N VAL A 840 34.493 46.348 69.077 1.00 72.85 N ANISOU 687 N VAL A 840 7599 11224 8857 2385 -569 -596 N ATOM 688 CA VAL A 840 35.409 45.216 69.050 1.00 72.59 C ANISOU 688 CA VAL A 840 7494 11235 8852 2238 -525 -599 C ATOM 689 C VAL A 840 34.634 43.965 69.435 1.00 71.51 C ANISOU 689 C VAL A 840 7156 11136 8878 2225 -418 -757 C ATOM 690 O VAL A 840 33.705 44.013 70.246 1.00 73.50 O ANISOU 690 O VAL A 840 7386 11318 9221 2279 -341 -827 O ATOM 691 CB VAL A 840 36.618 45.426 69.990 1.00 71.15 C ANISOU 691 CB VAL A 840 7493 10922 8620 2104 -486 -471 C ATOM 692 CG1 VAL A 840 37.407 46.658 69.570 1.00 72.75 C ANISOU 692 CG1 VAL A 840 7884 11077 8683 2100 -577 -328 C ATOM 693 CG2 VAL A 840 36.164 45.551 71.442 1.00 72.26 C ANISOU 693 CG2 VAL A 840 7710 10922 8822 2106 -387 -490 C ATOM 694 N HIS A 841 35.016 42.839 68.837 1.00 84.15 N ANISOU 694 N HIS A 841 8608 12842 10522 2152 -400 -816 N ATOM 695 CA HIS A 841 34.349 41.571 69.086 1.00 83.62 C ANISOU 695 CA HIS A 841 8340 12808 10625 2126 -284 -973 C ATOM 696 C HIS A 841 35.381 40.457 69.152 1.00 82.73 C ANISOU 696 C HIS A 841 8193 12702 10540 1985 -214 -948 C ATOM 697 O HIS A 841 36.411 40.498 68.475 1.00 85.65 O ANISOU 697 O HIS A 841 8610 13128 10806 1929 -289 -862 O ATOM 698 CB HIS A 841 33.314 41.243 67.997 1.00 86.73 C ANISOU 698 CB HIS A 841 8513 13362 11080 2223 -340 -1143 C ATOM 699 CG HIS A 841 32.545 42.431 67.512 1.00 88.92 C ANISOU 699 CG HIS A 841 8827 13679 11278 2383 -460 -1141 C ATOM 700 ND1 HIS A 841 32.817 43.057 66.314 1.00 87.39 N ANISOU 700 ND1 HIS A 841 8666 13602 10937 2458 -608 -1087 N ATOM 701 CD2 HIS A 841 31.507 43.106 68.061 1.00 91.83 C ANISOU 701 CD2 HIS A 841 9212 13988 11692 2493 -445 -1179 C ATOM 702 CE1 HIS A 841 31.981 44.066 66.147 1.00 89.82 C ANISOU 702 CE1 HIS A 841 9011 13918 11200 2615 -682 -1088 C ATOM 703 NE2 HIS A 841 31.176 44.118 67.192 1.00 92.72 N ANISOU 703 NE2 HIS A 841 9364 14180 11686 2637 -588 -1147 N ATOM 704 N CYS A 842 35.097 39.463 69.989 1.00 65.36 N ANISOU 704 N CYS A 842 5914 10438 8482 1934 -58 -1019 N ATOM 705 CA CYS A 842 35.857 38.225 70.028 1.00 64.64 C ANISOU 705 CA CYS A 842 5754 10356 8450 1821 34 -1024 C ATOM 706 C CYS A 842 34.877 37.067 70.108 1.00 65.24 C ANISOU 706 C CYS A 842 5618 10444 8727 1821 176 -1206 C ATOM 707 O CYS A 842 33.790 37.192 70.678 1.00 65.97 O ANISOU 707 O CYS A 842 5667 10480 8920 1884 250 -1291 O ATOM 708 CB CYS A 842 36.830 38.174 71.215 1.00 63.76 C ANISOU 708 CB CYS A 842 5817 10116 8293 1745 109 -880 C ATOM 709 SG CYS A 842 38.382 39.074 70.973 1.00 63.80 S ANISOU 709 SG CYS A 842 6018 10127 8096 1684 -35 -687 S ATOM 710 N LEU A 843 35.261 35.943 69.513 1.00 72.02 N ANISOU 710 N LEU A 843 6340 11371 9653 1748 223 -1273 N ATOM 711 CA LEU A 843 34.405 34.768 69.518 1.00 72.71 C ANISOU 711 CA LEU A 843 6216 11462 9950 1730 372 -1459 C ATOM 712 C LEU A 843 34.439 34.084 70.879 1.00 72.46 C ANISOU 712 C LEU A 843 6240 11265 10027 1682 584 -1419 C ATOM 713 O LEU A 843 35.500 33.931 71.491 1.00 71.57 O ANISOU 713 O LEU A 843 6273 11082 9837 1627 621 -1267 O ATOM 714 CB LEU A 843 34.843 33.792 68.430 1.00 72.69 C ANISOU 714 CB LEU A 843 6059 11578 9983 1665 360 -1546 C ATOM 715 CG LEU A 843 34.034 32.499 68.304 1.00 73.56 C ANISOU 715 CG LEU A 843 5933 11693 10323 1628 518 -1760 C ATOM 716 CD1 LEU A 843 32.596 32.791 67.906 1.00 74.94 C ANISOU 716 CD1 LEU A 843 5938 11943 10594 1716 478 -1955 C ATOM 717 CD2 LEU A 843 34.679 31.562 67.306 1.00 73.44 C ANISOU 717 CD2 LEU A 843 5801 11779 10323 1555 509 -1824 C ATOM 718 N ASN A 844 33.267 33.663 71.347 1.00 94.33 N ANISOU 718 N ASN A 844 10963 11421 13458 339 823 575 N ATOM 719 CA ASN A 844 33.148 32.917 72.593 1.00 93.19 C ANISOU 719 CA ASN A 844 10688 11258 13461 334 996 619 C ATOM 720 C ASN A 844 32.992 31.445 72.241 1.00 95.86 C ANISOU 720 C ASN A 844 10985 11523 13912 353 929 569 C ATOM 721 O ASN A 844 31.940 31.026 71.747 1.00 97.93 O ANISOU 721 O ASN A 844 11170 11647 14393 361 788 524 O ATOM 722 CB ASN A 844 31.959 33.404 73.415 1.00 91.19 C ANISOU 722 CB ASN A 844 10286 10900 13463 323 1046 660 C ATOM 723 CG ASN A 844 31.909 32.773 74.785 1.00 94.02 C ANISOU 723 CG ASN A 844 10530 11249 13943 311 1250 717 C ATOM 724 OD1 ASN A 844 32.942 32.519 75.403 1.00 95.45 O ANISOU 724 OD1 ASN A 844 10765 11544 13959 309 1396 753 O ATOM 725 ND2 ASN A 844 30.702 32.503 75.265 1.00 96.83 N ANISOU 725 ND2 ASN A 844 10730 11469 14591 303 1259 722 N ATOM 726 N MET A 845 34.034 30.658 72.512 1.00 95.38 N ANISOU 726 N MET A 845 10976 11555 13711 363 1028 573 N ATOM 727 CA MET A 845 34.004 29.245 72.159 1.00 96.64 C ANISOU 727 CA MET A 845 11115 11650 13955 385 968 523 C ATOM 728 C MET A 845 33.185 28.427 73.147 1.00 97.53 C ANISOU 728 C MET A 845 11073 11644 14340 376 1061 557 C ATOM 729 O MET A 845 32.648 27.377 72.778 1.00101.35 O ANISOU 729 O MET A 845 11505 12016 14988 385 973 511 O ATOM 730 CB MET A 845 35.430 28.703 72.070 1.00 93.34 C ANISOU 730 CB MET A 845 10808 11371 13286 405 1035 510 C ATOM 731 CG MET A 845 36.106 29.005 70.742 1.00 92.11 C ANISOU 731 CG MET A 845 10803 11293 12902 415 896 442 C ATOM 732 SD MET A 845 37.888 28.746 70.772 1.00 96.17 S ANISOU 732 SD MET A 845 11440 12005 13095 431 1011 431 S ATOM 733 CE MET A 845 38.403 30.036 71.904 1.00 95.70 C ANISOU 733 CE MET A 845 11378 12070 12913 398 1204 519 C ATOM 734 N ASP A 846 33.076 28.882 74.397 1.00 89.15 N ANISOU 734 N ASP A 846 9941 10603 13330 357 1242 636 N ATOM 735 CA ASP A 846 32.221 28.192 75.356 1.00 89.32 C ANISOU 735 CA ASP A 846 9817 10505 13614 341 1342 672 C ATOM 736 C ASP A 846 30.780 28.116 74.866 1.00 91.44 C ANISOU 736 C ASP A 846 9969 10608 14169 327 1199 627 C ATOM 737 O ASP A 846 30.082 27.134 75.141 1.00 92.98 O ANISOU 737 O ASP A 846 10060 10680 14590 315 1209 617 O ATOM 738 CB ASP A 846 32.282 28.892 76.712 1.00 88.26 C ANISOU 738 CB ASP A 846 9638 10423 13476 321 1550 761 C ATOM 739 CG ASP A 846 33.617 28.706 77.403 1.00 87.42 C ANISOU 739 CG ASP A 846 9621 10461 13135 336 1706 806 C ATOM 740 OD1 ASP A 846 34.121 27.567 77.421 1.00 87.35 O ANISOU 740 OD1 ASP A 846 9639 10452 13099 358 1722 793 O ATOM 741 OD2 ASP A 846 34.160 29.700 77.928 1.00 87.24 O ANISOU 741 OD2 ASP A 846 9641 10550 12958 328 1808 851 O ATOM 742 N SER A 847 30.314 29.142 74.149 1.00 85.14 N ANISOU 742 N SER A 847 9184 9799 13368 328 1064 598 N ATOM 743 CA SER A 847 28.970 29.101 73.579 1.00 86.50 C ANISOU 743 CA SER A 847 9245 9817 13802 324 903 543 C ATOM 744 C SER A 847 28.851 28.010 72.524 1.00 87.40 C ANISOU 744 C SER A 847 9383 9858 13966 340 726 459 C ATOM 745 O SER A 847 27.804 27.362 72.402 1.00 88.61 O ANISOU 745 O SER A 847 9412 9867 14388 329 648 418 O ATOM 746 CB SER A 847 28.618 30.462 72.976 1.00 86.58 C ANISOU 746 CB SER A 847 9292 9841 13766 333 782 529 C ATOM 747 OG SER A 847 27.415 30.396 72.229 1.00 87.98 O ANISOU 747 OG SER A 847 9381 9877 14172 340 587 461 O ATOM 748 N LEU A 848 29.911 27.793 71.754 1.00103.53 N ANISOU 748 N LEU A 848 11583 11999 15757 365 662 428 N ATOM 749 CA LEU A 848 29.881 26.818 70.677 1.00103.45 C ANISOU 749 CA LEU A 848 11614 11929 15763 385 488 342 C ATOM 750 C LEU A 848 30.042 25.404 71.220 1.00102.86 C ANISOU 750 C LEU A 848 11491 11807 15785 381 582 345 C ATOM 751 O LEU A 848 30.662 25.180 72.264 1.00101.79 O ANISOU 751 O LEU A 848 11354 11736 15587 376 781 414 O ATOM 752 CB LEU A 848 30.986 27.115 69.663 1.00102.10 C ANISOU 752 CB LEU A 848 11633 11884 15277 411 398 305 C ATOM 753 CG LEU A 848 31.044 28.557 69.155 1.00101.61 C ANISOU 753 CG LEU A 848 11655 11884 15066 411 327 312 C ATOM 754 CD1 LEU A 848 32.202 28.735 68.190 1.00101.35 C ANISOU 754 CD1 LEU A 848 11815 11977 14716 428 262 276 C ATOM 755 CD2 LEU A 848 29.732 28.956 68.496 1.00103.65 C ANISOU 755 CD2 LEU A 848 11844 12007 15533 415 131 266 C ATOM 756 N SER A 849 29.468 24.447 70.496 1.00 97.02 N ANISOU 756 N SER A 849 10717 10948 15199 386 432 269 N ATOM 757 CA SER A 849 29.572 23.031 70.821 1.00 97.42 C ANISOU 757 CA SER A 849 10735 10933 15347 385 488 259 C ATOM 758 C SER A 849 30.294 22.323 69.686 1.00 98.07 C ANISOU 758 C SER A 849 10950 11046 15264 422 346 179 C ATOM 759 O SER A 849 29.874 22.413 68.529 1.00 98.67 O ANISOU 759 O SER A 849 11058 11075 15359 434 136 98 O ATOM 760 CB SER A 849 28.192 22.410 71.040 1.00 98.81 C ANISOU 760 CB SER A 849 10740 10924 15880 349 449 235 C ATOM 761 OG SER A 849 27.523 23.031 72.123 1.00100.05 O ANISOU 761 OG SER A 849 10769 11052 16193 314 595 306 O ATOM 762 N PHE A 850 31.372 21.621 70.021 1.00101.66 N ANISOU 762 N PHE A 850 11485 11581 15560 445 457 197 N ATOM 763 CA PHE A 850 32.216 20.952 69.040 1.00101.11 C ANISOU 763 CA PHE A 850 11547 11561 15309 486 351 122 C ATOM 764 C PHE A 850 32.038 19.446 69.154 1.00101.67 C ANISOU 764 C PHE A 850 11579 11517 15535 493 348 90 C ATOM 765 O PHE A 850 32.066 18.894 70.260 1.00101.06 O ANISOU 765 O PHE A 850 11440 11408 15551 481 515 154 O ATOM 766 CB PHE A 850 33.684 21.331 69.239 1.00 98.94 C ANISOU 766 CB PHE A 850 11401 11477 14715 515 469 155 C ATOM 767 CG PHE A 850 33.968 22.782 68.997 1.00 97.72 C ANISOU 767 CG PHE A 850 11308 11439 14383 505 463 178 C ATOM 768 CD1 PHE A 850 34.590 23.193 67.832 1.00 95.69 C ANISOU 768 CD1 PHE A 850 11190 11270 13899 524 338 116 C ATOM 769 CD2 PHE A 850 33.604 23.736 69.930 1.00 99.34 C ANISOU 769 CD2 PHE A 850 11438 11662 14646 474 585 261 C ATOM 770 CE1 PHE A 850 34.847 24.530 67.606 1.00 96.32 C ANISOU 770 CE1 PHE A 850 11337 11447 13814 510 336 140 C ATOM 771 CE2 PHE A 850 33.855 25.073 69.708 1.00 98.38 C ANISOU 771 CE2 PHE A 850 11379 11638 14364 464 577 281 C ATOM 772 CZ PHE A 850 34.479 25.470 68.547 1.00 97.56 C ANISOU 772 CZ PHE A 850 11418 11616 14035 480 453 223 C ATOM 773 N GLN A 851 31.857 18.790 68.010 1.00101.82 N ANISOU 773 N GLN A 851 11642 11467 15576 511 158 -10 N ATOM 774 CA GLN A 851 31.701 17.346 67.951 1.00102.96 C ANISOU 774 CA GLN A 851 11765 11495 15859 518 130 -55 C ATOM 775 C GLN A 851 32.536 16.805 66.800 1.00102.64 C ANISOU 775 C GLN A 851 11871 11510 15619 569 -1 -148 C ATOM 776 O GLN A 851 32.760 17.493 65.800 1.00102.24 O ANISOU 776 O GLN A 851 11911 11530 15406 584 -131 -199 O ATOM 777 CB GLN A 851 30.229 16.948 67.774 1.00105.16 C ANISOU 777 CB GLN A 851 11904 11580 16473 475 15 -96 C ATOM 778 CG GLN A 851 29.990 15.447 67.707 1.00106.48 C ANISOU 778 CG GLN A 851 12045 11610 16802 473 -17 -145 C ATOM 779 CD GLN A 851 28.520 15.087 67.803 1.00107.07 C ANISOU 779 CD GLN A 851 11955 11494 17231 416 -84 -171 C ATOM 780 OE1 GLN A 851 27.656 15.963 67.832 1.00106.40 O ANISOU 780 OE1 GLN A 851 11773 11382 17273 385 -125 -162 O ATOM 781 NE2 GLN A 851 28.229 13.791 67.854 1.00107.56 N ANISOU 781 NE2 GLN A 851 11984 11423 17460 402 -96 -208 N ATOM 782 N LEU A 852 32.999 15.568 66.954 1.00102.48 N ANISOU 782 N LEU A 852 11879 11453 15606 596 39 -169 N ATOM 783 CA LEU A 852 33.824 14.900 65.954 1.00102.76 C ANISOU 783 CA LEU A 852 12047 11533 15463 649 -67 -261 C ATOM 784 C LEU A 852 33.005 13.816 65.271 1.00104.33 C ANISOU 784 C LEU A 852 12212 11555 15873 642 -231 -351 C ATOM 785 O LEU A 852 32.587 12.849 65.915 1.00106.33 O ANISOU 785 O LEU A 852 12388 11683 16328 626 -169 -333 O ATOM 786 CB LEU A 852 35.079 14.297 66.587 1.00101.97 C ANISOU 786 CB LEU A 852 12017 11533 15192 696 92 -229 C ATOM 787 CG LEU A 852 36.288 15.215 66.774 1.00100.55 C ANISOU 787 CG LEU A 852 11926 11567 14714 723 202 -190 C ATOM 788 CD1 LEU A 852 37.402 14.479 67.502 1.00 99.99 C ANISOU 788 CD1 LEU A 852 11899 11571 14523 773 352 -162 C ATOM 789 CD2 LEU A 852 36.795 15.742 65.440 1.00100.59 C ANISOU 789 CD2 LEU A 852 12053 11670 14496 743 58 -276 C ATOM 790 N GLY A 853 32.765 13.983 63.976 1.00137.60 N ANISOU 790 N GLY A 853 16488 15754 20040 653 -439 -448 N ATOM 791 CA GLY A 853 32.155 12.937 63.184 1.00141.56 C ANISOU 791 CA GLY A 853 16981 16104 20699 655 -612 -550 C ATOM 792 C GLY A 853 33.197 12.075 62.494 1.00142.93 C ANISOU 792 C GLY A 853 17298 16331 20677 716 -653 -629 C ATOM 793 O GLY A 853 34.296 12.524 62.187 1.00143.96 O ANISOU 793 O GLY A 853 17550 16626 20524 757 -615 -633 O ATOM 794 N LEU A 854 32.825 10.823 62.243 1.00120.53 N ANISOU 794 N LEU A 854 14444 13350 18003 721 -731 -696 N ATOM 795 CA LEU A 854 33.658 9.884 61.504 1.00120.35 C ANISOU 795 CA LEU A 854 14548 13347 17831 781 -796 -787 C ATOM 796 C LEU A 854 32.765 9.144 60.526 1.00121.58 C ANISOU 796 C LEU A 854 14693 13337 18164 769 -1016 -902 C ATOM 797 O LEU A 854 31.688 8.675 60.904 1.00121.75 O ANISOU 797 O LEU A 854 14586 13193 18481 719 -1040 -896 O ATOM 798 CB LEU A 854 34.375 8.882 62.417 1.00118.52 C ANISOU 798 CB LEU A 854 14324 13111 17599 813 -627 -745 C ATOM 799 CG LEU A 854 35.692 9.312 63.063 1.00118.50 C ANISOU 799 CG LEU A 854 14388 13299 17337 858 -442 -676 C ATOM 800 CD1 LEU A 854 35.480 10.272 64.226 1.00118.65 C ANISOU 800 CD1 LEU A 854 14313 13372 17397 815 -276 -546 C ATOM 801 CD2 LEU A 854 36.444 8.083 63.524 1.00119.56 C ANISOU 801 CD2 LEU A 854 14565 13411 17450 913 -352 -682 C ATOM 802 N TYR A 855 33.211 9.034 59.278 1.00137.03 N ANISOU 802 N TYR A 855 16783 15340 19942 812 -1171 -1010 N ATOM 803 CA TYR A 855 32.389 8.475 58.217 1.00140.71 C ANISOU 803 CA TYR A 855 17256 15665 20544 805 -1404 -1128 C ATOM 804 C TYR A 855 33.165 7.406 57.465 1.00142.07 C ANISOU 804 C TYR A 855 17560 15838 20584 866 -1469 -1233 C ATOM 805 O TYR A 855 34.363 7.553 57.206 1.00142.20 O ANISOU 805 O TYR A 855 17703 16009 20317 921 -1407 -1245 O ATOM 806 CB TYR A 855 31.917 9.578 57.264 1.00141.34 C ANISOU 806 CB TYR A 855 17372 15782 20548 793 -1576 -1166 C ATOM 807 CG TYR A 855 31.166 10.680 57.977 1.00139.66 C ANISOU 807 CG TYR A 855 17032 15571 20461 741 -1517 -1068 C ATOM 808 CD1 TYR A 855 30.054 10.392 58.756 1.00138.23 C ANISOU 808 CD1 TYR A 855 16671 15239 20609 684 -1488 -1029 C ATOM 809 CD2 TYR A 855 31.571 12.003 57.877 1.00139.06 C ANISOU 809 CD2 TYR A 855 17017 15644 20176 745 -1485 -1016 C ATOM 810 CE1 TYR A 855 29.365 11.392 59.415 1.00137.18 C ANISOU 810 CE1 TYR A 855 16419 15109 20596 640 -1429 -945 C ATOM 811 CE2 TYR A 855 30.886 13.010 58.532 1.00138.96 C ANISOU 811 CE2 TYR A 855 16890 15629 20279 702 -1432 -930 C ATOM 812 CZ TYR A 855 29.784 12.698 59.299 1.00137.96 C ANISOU 812 CZ TYR A 855 16581 15355 20481 652 -1404 -897 C ATOM 813 OH TYR A 855 29.098 13.694 59.953 1.00137.33 O ANISOU 813 OH TYR A 855 16386 15274 20521 612 -1348 -817 O ATOM 814 N LEU A 856 32.464 6.324 57.126 1.00144.20 N ANISOU 814 N LEU A 856 17793 15929 21067 854 -1593 -1314 N ATOM 815 CA LEU A 856 33.094 5.183 56.471 1.00144.87 C ANISOU 815 CA LEU A 856 17993 15987 21066 912 -1657 -1419 C ATOM 816 C LEU A 856 33.421 5.472 55.010 1.00144.32 C ANISOU 816 C LEU A 856 18073 15988 20775 952 -1844 -1536 C ATOM 817 O LEU A 856 34.378 4.906 54.468 1.00142.80 O ANISOU 817 O LEU A 856 18013 15861 20386 1015 -1849 -1608 O ATOM 818 CB LEU A 856 32.179 3.959 56.579 1.00145.27 C ANISOU 818 CB LEU A 856 17956 15813 21426 878 -1732 -1468 C ATOM 819 CG LEU A 856 31.955 3.319 57.957 1.00143.93 C ANISOU 819 CG LEU A 856 17669 15547 21471 844 -1545 -1370 C ATOM 820 CD1 LEU A 856 32.042 4.311 59.114 1.00141.53 C ANISOU 820 CD1 LEU A 856 17282 15344 21151 814 -1346 -1221 C ATOM 821 CD2 LEU A 856 30.611 2.601 57.985 1.00144.76 C ANISOU 821 CD2 LEU A 856 17646 15424 21931 773 -1648 -1410 C ATOM 822 N SER A 857 32.645 6.330 54.359 1.00142.99 N ANISOU 822 N SER A 857 17892 15805 20632 919 -1999 -1558 N ATOM 823 CA SER A 857 32.831 6.703 52.968 1.00144.03 C ANISOU 823 CA SER A 857 18173 15993 20559 951 -2188 -1662 C ATOM 824 C SER A 857 32.845 8.223 52.857 1.00143.45 C ANISOU 824 C SER A 857 18124 16047 20332 934 -2182 -1597 C ATOM 825 O SER A 857 32.441 8.918 53.792 1.00142.63 O ANISOU 825 O SER A 857 17898 15952 20343 892 -2070 -1486 O ATOM 826 CB SER A 857 31.713 6.133 52.082 1.00146.18 C ANISOU 826 CB SER A 857 18423 16086 21035 933 -2442 -1779 C ATOM 827 OG SER A 857 30.449 6.659 52.450 1.00145.19 O ANISOU 827 OG SER A 857 18138 15856 21170 870 -2502 -1734 O ATOM 828 N PRO A 858 33.303 8.767 51.716 1.00120.71 N ANISOU 828 N PRO A 858 15409 13264 17191 965 -2299 -1665 N ATOM 829 CA PRO A 858 33.228 10.227 51.532 1.00119.65 C ANISOU 829 CA PRO A 858 15311 13231 16918 945 -2314 -1606 C ATOM 830 C PRO A 858 31.795 10.714 51.378 1.00119.14 C ANISOU 830 C PRO A 858 15139 13032 17095 903 -2486 -1606 C ATOM 831 O PRO A 858 31.464 11.422 50.422 1.00120.01 O ANISOU 831 O PRO A 858 15341 13151 17108 909 -2663 -1651 O ATOM 832 CB PRO A 858 34.043 10.464 50.250 1.00118.44 C ANISOU 832 CB PRO A 858 15378 13190 16436 989 -2411 -1695 C ATOM 833 CG PRO A 858 34.920 9.280 50.123 1.00117.72 C ANISOU 833 CG PRO A 858 15352 13117 16261 1037 -2350 -1767 C ATOM 834 CD PRO A 858 34.141 8.130 50.690 1.00119.48 C ANISOU 834 CD PRO A 858 15427 13157 16811 1023 -2372 -1782 C ATOM 835 N HIS A 859 30.945 10.359 52.339 1.00135.02 N ANISOU 835 N HIS A 859 16956 14921 19422 861 -2430 -1553 N ATOM 836 CA HIS A 859 29.535 10.719 52.327 1.00135.71 C ANISOU 836 CA HIS A 859 16908 14873 19784 819 -2576 -1557 C ATOM 837 C HIS A 859 29.054 10.699 53.769 1.00135.36 C ANISOU 837 C HIS A 859 16661 14777 19992 769 -2389 -1447 C ATOM 838 O HIS A 859 29.678 10.085 54.639 1.00133.58 O ANISOU 838 O HIS A 859 16408 14579 19769 769 -2190 -1392 O ATOM 839 CB HIS A 859 28.700 9.759 51.462 1.00137.29 C ANISOU 839 CB HIS A 859 17093 14902 20167 821 -2814 -1693 C ATOM 840 CG HIS A 859 29.293 9.476 50.115 1.00139.10 C ANISOU 840 CG HIS A 859 17531 15173 20147 875 -2975 -1810 C ATOM 841 ND1 HIS A 859 29.074 10.282 49.018 1.00139.61 N ANISOU 841 ND1 HIS A 859 17717 15267 20062 895 -3173 -1864 N ATOM 842 CD2 HIS A 859 30.103 8.476 49.690 1.00139.13 C ANISOU 842 CD2 HIS A 859 17650 15193 20021 915 -2963 -1887 C ATOM 843 CE1 HIS A 859 29.721 9.790 47.976 1.00139.29 C ANISOU 843 CE1 HIS A 859 17858 15260 19804 940 -3272 -1967 C ATOM 844 NE2 HIS A 859 30.353 8.695 48.357 1.00138.98 N ANISOU 844 NE2 HIS A 859 17815 15215 19776 954 -3147 -1986 N ATOM 845 N PHE A 860 27.939 11.378 54.017 1.00135.87 N ANISOU 845 N PHE A 860 16588 14767 20269 729 -2454 -1416 N ATOM 846 CA PHE A 860 27.390 11.422 55.366 1.00134.54 C ANISOU 846 CA PHE A 860 16225 14546 20350 676 -2278 -1315 C ATOM 847 C PHE A 860 26.946 10.032 55.806 1.00135.99 C ANISOU 847 C PHE A 860 16298 14573 20799 647 -2251 -1350 C ATOM 848 O PHE A 860 26.273 9.315 55.059 1.00135.42 O ANISOU 848 O PHE A 860 16208 14367 20877 642 -2446 -1462 O ATOM 849 CB PHE A 860 26.220 12.402 55.431 1.00134.89 C ANISOU 849 CB PHE A 860 16141 14533 20580 643 -2375 -1294 C ATOM 850 CG PHE A 860 26.614 13.782 55.876 1.00134.65 C ANISOU 850 CG PHE A 860 16137 14645 20377 647 -2256 -1187 C ATOM 851 CD1 PHE A 860 26.345 14.209 57.167 1.00134.43 C ANISOU 851 CD1 PHE A 860 15960 14624 20491 606 -2056 -1074 C ATOM 852 CD2 PHE A 860 27.264 14.647 55.011 1.00134.67 C ANISOU 852 CD2 PHE A 860 16323 14774 20073 688 -2338 -1201 C ATOM 853 CE1 PHE A 860 26.710 15.476 57.584 1.00132.55 C ANISOU 853 CE1 PHE A 860 15750 14515 20097 608 -1947 -980 C ATOM 854 CE2 PHE A 860 27.632 15.916 55.422 1.00133.25 C ANISOU 854 CE2 PHE A 860 16173 14720 19738 686 -2226 -1104 C ATOM 855 CZ PHE A 860 27.354 16.331 56.711 1.00131.86 C ANISOU 855 CZ PHE A 860 15843 14549 19710 648 -2034 -995 C ATOM 856 N LEU A 861 27.333 9.653 57.023 1.00155.08 N ANISOU 856 N LEU A 861 18648 17005 23269 626 -2009 -1255 N ATOM 857 CA LEU A 861 27.003 8.344 57.568 1.00155.41 C ANISOU 857 CA LEU A 861 18599 16901 23547 595 -1950 -1270 C ATOM 858 C LEU A 861 26.778 8.472 59.068 1.00154.69 C ANISOU 858 C LEU A 861 18363 16795 23617 545 -1708 -1140 C ATOM 859 O LEU A 861 27.302 9.380 59.716 1.00152.67 O ANISOU 859 O LEU A 861 18119 16674 23213 552 -1552 -1038 O ATOM 860 CB LEU A 861 28.104 7.319 57.268 1.00155.41 C ANISOU 860 CB LEU A 861 18749 16936 23363 649 -1916 -1316 C ATOM 861 CG LEU A 861 28.267 6.971 55.786 1.00157.61 C ANISOU 861 CG LEU A 861 19170 17204 23509 695 -2155 -1459 C ATOM 862 CD1 LEU A 861 29.473 6.084 55.585 1.00156.83 C ANISOU 862 CD1 LEU A 861 19220 17165 23204 755 -2091 -1496 C ATOM 863 CD2 LEU A 861 27.020 6.295 55.232 1.00158.21 C ANISOU 863 CD2 LEU A 861 19151 17081 23881 656 -2363 -1565 C ATOM 864 N GLN A 862 25.992 7.544 59.610 1.00164.18 N ANISOU 864 N GLN A 862 19432 17828 25121 490 -1676 -1148 N ATOM 865 CA GLN A 862 25.443 7.689 60.952 1.00164.23 C ANISOU 865 CA GLN A 862 19276 17785 25340 426 -1477 -1039 C ATOM 866 C GLN A 862 26.297 7.064 62.051 1.00163.09 C ANISOU 866 C GLN A 862 19168 17672 25125 433 -1227 -943 C ATOM 867 O GLN A 862 26.026 7.316 63.230 1.00161.78 O ANISOU 867 O GLN A 862 18896 17496 25077 388 -1036 -836 O ATOM 868 CB GLN A 862 24.039 7.073 61.000 1.00165.11 C ANISOU 868 CB GLN A 862 19209 17688 25837 350 -1566 -1097 C ATOM 869 CG GLN A 862 23.126 7.526 59.869 1.00166.03 C ANISOU 869 CG GLN A 862 19282 17751 26052 347 -1840 -1209 C ATOM 870 CD GLN A 862 21.741 6.914 59.953 1.00168.09 C ANISOU 870 CD GLN A 862 19351 17809 26708 269 -1923 -1273 C ATOM 871 OE1 GLN A 862 21.461 6.097 60.830 1.00168.06 O ANISOU 871 OE1 GLN A 862 19253 17697 26905 210 -1772 -1235 O ATOM 872 NE2 GLN A 862 20.867 7.307 59.033 1.00169.55 N ANISOU 872 NE2 GLN A 862 19478 17939 27005 267 -2167 -1374 N ATOM 873 N ALA A 863 27.313 6.266 61.716 1.00148.63 N ANISOU 873 N ALA A 863 17486 15879 23107 492 -1224 -978 N ATOM 874 CA ALA A 863 28.123 5.577 62.720 1.00147.20 C ANISOU 874 CA ALA A 863 17346 15716 22865 509 -1006 -896 C ATOM 875 C ALA A 863 29.549 6.114 62.676 1.00145.23 C ANISOU 875 C ALA A 863 17249 15679 22251 589 -924 -858 C ATOM 876 O ALA A 863 30.312 5.794 61.757 1.00143.81 O ANISOU 876 O ALA A 863 17209 15561 21872 652 -1028 -941 O ATOM 877 CB ALA A 863 28.097 4.068 62.487 1.00147.16 C ANISOU 877 CB ALA A 863 17376 15560 22978 512 -1058 -969 C ATOM 878 N SER A 864 29.902 6.926 63.672 1.00161.91 N ANISOU 878 N SER A 864 19333 17904 24282 583 -733 -737 N ATOM 879 CA SER A 864 31.258 7.425 63.854 1.00161.44 C ANISOU 879 CA SER A 864 19396 18045 23899 649 -620 -688 C ATOM 880 C SER A 864 32.040 6.691 64.936 1.00161.43 C ANISOU 880 C SER A 864 19425 18057 23854 676 -416 -611 C ATOM 881 O SER A 864 33.235 6.956 65.101 1.00161.73 O ANISOU 881 O SER A 864 19563 18257 23628 738 -324 -581 O ATOM 882 CB SER A 864 31.211 8.921 64.188 1.00160.30 C ANISOU 882 CB SER A 864 19212 18031 23664 629 -556 -611 C ATOM 883 OG SER A 864 30.538 9.157 65.411 1.00160.27 O ANISOU 883 OG SER A 864 19070 17967 23859 569 -398 -506 O ATOM 884 N ASN A 865 31.412 5.767 65.665 1.00133.97 N ANISOU 884 N ASN A 865 15867 14411 20624 633 -345 -579 N ATOM 885 CA ASN A 865 32.032 5.241 66.877 1.00132.85 C ANISOU 885 CA ASN A 865 15745 14276 20453 653 -133 -481 C ATOM 886 C ASN A 865 33.088 4.186 66.588 1.00133.07 C ANISOU 886 C ASN A 865 15912 14321 20329 736 -144 -533 C ATOM 887 O ASN A 865 34.062 4.073 67.341 1.00131.98 O ANISOU 887 O ASN A 865 15838 14277 20033 790 8 -465 O ATOM 888 CB ASN A 865 30.966 4.657 67.804 1.00133.25 C ANISOU 888 CB ASN A 865 15670 14137 20822 571 -39 -422 C ATOM 889 CG ASN A 865 30.516 5.639 68.867 1.00133.43 C ANISOU 889 CG ASN A 865 15585 14200 20911 515 122 -303 C ATOM 890 OD1 ASN A 865 30.839 6.826 68.813 1.00131.85 O ANISOU 890 OD1 ASN A 865 15391 14158 20549 531 137 -274 O ATOM 891 ND2 ASN A 865 29.764 5.146 69.843 1.00133.98 N ANISOU 891 ND2 ASN A 865 15560 14125 21223 447 249 -236 N ATOM 892 N THR A 866 32.921 3.412 65.524 1.00117.89 N ANISOU 892 N THR A 866 14036 12308 18449 753 -324 -655 N ATOM 893 CA THR A 866 33.801 2.294 65.228 1.00119.36 C ANISOU 893 CA THR A 866 14346 12481 18527 831 -344 -716 C ATOM 894 C THR A 866 34.730 2.652 64.077 1.00118.92 C ANISOU 894 C THR A 866 14411 12585 18188 907 -462 -812 C ATOM 895 O THR A 866 34.317 3.293 63.105 1.00118.45 O ANISOU 895 O THR A 866 14347 12554 18104 886 -615 -881 O ATOM 896 CB THR A 866 32.994 1.041 64.882 1.00121.99 C ANISOU 896 CB THR A 866 14655 12585 19111 797 -452 -791 C ATOM 897 OG1 THR A 866 32.065 0.765 65.939 1.00122.71 O ANISOU 897 OG1 THR A 866 14627 12524 19474 712 -334 -701 O ATOM 898 CG2 THR A 866 33.908 -0.160 64.706 1.00122.90 C ANISOU 898 CG2 THR A 866 14899 12674 19125 882 -456 -845 C ATOM 899 N ILE A 867 35.985 2.235 64.204 1.00118.89 N ANISOU 899 N ILE A 867 14517 12686 17971 996 -388 -818 N ATOM 900 CA ILE A 867 37.009 2.439 63.189 1.00117.18 C ANISOU 900 CA ILE A 867 14423 12625 17476 1073 -472 -913 C ATOM 901 C ILE A 867 37.630 1.084 62.882 1.00117.57 C ANISOU 901 C ILE A 867 14568 12608 17496 1150 -509 -995 C ATOM 902 O ILE A 867 37.794 0.252 63.781 1.00117.94 O ANISOU 902 O ILE A 867 14611 12571 17630 1170 -398 -939 O ATOM 903 CB ILE A 867 38.080 3.446 63.662 1.00115.17 C ANISOU 903 CB ILE A 867 14200 12601 16957 1112 -330 -843 C ATOM 904 CG1 ILE A 867 39.132 3.668 62.576 1.00115.40 C ANISOU 904 CG1 ILE A 867 14353 12794 16700 1182 -409 -947 C ATOM 905 CG2 ILE A 867 38.741 2.960 64.939 1.00115.73 C ANISOU 905 CG2 ILE A 867 14272 12688 17011 1154 -139 -749 C ATOM 906 CD1 ILE A 867 40.067 4.829 62.860 1.00113.42 C ANISOU 906 CD1 ILE A 867 14126 12773 16195 1201 -291 -893 C ATOM 907 N GLU A 868 37.970 0.857 61.614 1.00114.34 N ANISOU 907 N GLU A 868 14252 12231 16961 1194 -666 -1128 N ATOM 908 CA GLU A 868 38.570 -0.409 61.235 1.00115.13 C ANISOU 908 CA GLU A 868 14447 12270 17026 1272 -711 -1220 C ATOM 909 C GLU A 868 39.919 -0.176 60.563 1.00114.94 C ANISOU 909 C GLU A 868 14541 12448 16681 1366 -714 -1295 C ATOM 910 O GLU A 868 40.052 0.751 59.756 1.00112.99 O ANISOU 910 O GLU A 868 14326 12329 16276 1354 -784 -1338 O ATOM 911 CB GLU A 868 37.653 -1.188 60.283 1.00116.89 C ANISOU 911 CB GLU A 868 14675 12305 17433 1240 -909 -1334 C ATOM 912 CG GLU A 868 36.403 -1.729 60.953 1.00117.86 C ANISOU 912 CG GLU A 868 14684 12205 17893 1153 -901 -1278 C ATOM 913 CD GLU A 868 35.609 -2.654 60.054 1.00121.72 C ANISOU 913 CD GLU A 868 15182 12502 18563 1128 -1093 -1401 C ATOM 914 OE1 GLU A 868 35.848 -2.641 58.829 1.00120.71 O ANISOU 914 OE1 GLU A 868 15140 12422 18304 1166 -1252 -1526 O ATOM 915 OE2 GLU A 868 34.751 -3.399 60.576 1.00124.28 O ANISOU 915 OE2 GLU A 868 15433 12628 19161 1068 -1081 -1374 O ATOM 916 N PRO A 869 40.932 -0.992 60.863 1.00104.08 N ANISOU 916 N PRO A 869 13237 11106 15204 1460 -639 -1315 N ATOM 917 CA PRO A 869 42.223 -0.834 60.183 1.00102.75 C ANISOU 917 CA PRO A 869 13172 11128 14739 1550 -640 -1402 C ATOM 918 C PRO A 869 42.159 -1.285 58.733 1.00104.44 C ANISOU 918 C PRO A 869 13476 11304 14904 1573 -830 -1561 C ATOM 919 O PRO A 869 41.377 -2.164 58.362 1.00105.12 O ANISOU 919 O PRO A 869 13562 11196 15182 1553 -950 -1619 O ATOM 920 CB PRO A 869 43.170 -1.724 60.998 1.00101.60 C ANISOU 920 CB PRO A 869 13061 10991 14550 1646 -517 -1379 C ATOM 921 CG PRO A 869 42.497 -1.904 62.311 1.00102.06 C ANISOU 921 CG PRO A 869 13031 10923 14825 1595 -406 -1240 C ATOM 922 CD PRO A 869 41.037 -1.899 62.019 1.00103.91 C ANISOU 922 CD PRO A 869 13194 10976 15310 1488 -516 -1237 C ATOM 923 N GLY A 870 43.004 -0.667 57.909 1.00114.20 N ANISOU 923 N GLY A 870 14791 12728 15873 1612 -851 -1635 N ATOM 924 CA GLY A 870 43.072 -0.980 56.498 1.00113.76 C ANISOU 924 CA GLY A 870 14837 12664 15723 1638 -1019 -1789 C ATOM 925 C GLY A 870 41.938 -0.429 55.663 1.00113.67 C ANISOU 925 C GLY A 870 14813 12576 15802 1551 -1185 -1819 C ATOM 926 O GLY A 870 41.963 -0.589 54.437 1.00115.17 O ANISOU 926 O GLY A 870 15097 12765 15897 1569 -1335 -1947 O ATOM 927 N GLN A 871 40.950 0.214 56.280 1.00116.43 N ANISOU 927 N GLN A 871 15051 12860 16328 1462 -1168 -1711 N ATOM 928 CA GLN A 871 39.811 0.784 55.574 1.00116.46 C ANISOU 928 CA GLN A 871 15027 12785 16437 1383 -1329 -1734 C ATOM 929 C GLN A 871 39.812 2.291 55.782 1.00115.77 C ANISOU 929 C GLN A 871 14905 12849 16234 1334 -1264 -1644 C ATOM 930 O GLN A 871 39.960 2.764 56.914 1.00116.13 O ANISOU 930 O GLN A 871 14870 12950 16304 1315 -1097 -1519 O ATOM 931 CB GLN A 871 38.496 0.175 56.070 1.00118.79 C ANISOU 931 CB GLN A 871 15207 12847 17080 1316 -1383 -1697 C ATOM 932 CG GLN A 871 37.402 0.108 55.017 1.00119.57 C ANISOU 932 CG GLN A 871 15306 12813 17311 1267 -1611 -1792 C ATOM 933 CD GLN A 871 37.699 -0.913 53.936 1.00119.42 C ANISOU 933 CD GLN A 871 15408 12734 17234 1327 -1757 -1949 C ATOM 934 OE1 GLN A 871 38.725 -1.592 53.972 1.00118.88 O ANISOU 934 OE1 GLN A 871 15420 12721 17029 1408 -1684 -1989 O ATOM 935 NE2 GLN A 871 36.798 -1.030 52.968 1.00121.22 N ANISOU 935 NE2 GLN A 871 15647 12847 17565 1291 -1968 -2044 N ATOM 936 N GLN A 872 39.646 3.038 54.693 1.00129.36 N ANISOU 936 N GLN A 872 16695 14630 17826 1314 -1397 -1708 N ATOM 937 CA GLN A 872 39.706 4.491 54.768 1.00129.01 C ANISOU 937 CA GLN A 872 16641 14730 17648 1271 -1347 -1632 C ATOM 938 C GLN A 872 38.655 5.026 55.733 1.00128.30 C ANISOU 938 C GLN A 872 16399 14552 17797 1194 -1300 -1508 C ATOM 939 O GLN A 872 37.496 4.601 55.717 1.00128.80 O ANISOU 939 O GLN A 872 16384 14433 18123 1149 -1409 -1518 O ATOM 940 CB GLN A 872 39.504 5.100 53.381 1.00129.53 C ANISOU 940 CB GLN A 872 16815 14832 17569 1259 -1527 -1725 C ATOM 941 CG GLN A 872 40.556 4.686 52.367 1.00131.32 C ANISOU 941 CG GLN A 872 17200 15159 17536 1330 -1565 -1852 C ATOM 942 CD GLN A 872 40.257 5.200 50.971 1.00132.75 C ANISOU 942 CD GLN A 872 17501 15353 17585 1315 -1754 -1946 C ATOM 943 OE1 GLN A 872 39.328 5.983 50.771 1.00132.14 O ANISOU 943 OE1 GLN A 872 17391 15225 17591 1256 -1856 -1910 O ATOM 944 NE2 GLN A 872 41.042 4.757 49.997 1.00132.00 N ANISOU 944 NE2 GLN A 872 17550 15322 17281 1373 -1805 -2069 N ATOM 945 N SER A 873 39.072 5.967 56.577 1.00 91.00 N ANISOU 945 N SER A 873 11631 9961 12983 1177 -1134 -1394 N ATOM 946 CA SER A 873 38.202 6.603 57.556 1.00 90.37 C ANISOU 946 CA SER A 873 11413 9826 13098 1107 -1063 -1270 C ATOM 947 C SER A 873 38.204 8.108 57.332 1.00 89.48 C ANISOU 947 C SER A 873 11317 9846 12837 1070 -1061 -1224 C ATOM 948 O SER A 873 39.257 8.708 57.087 1.00 88.69 O ANISOU 948 O SER A 873 11309 9926 12461 1099 -991 -1230 O ATOM 949 CB SER A 873 38.652 6.279 58.985 1.00 89.46 C ANISOU 949 CB SER A 873 11223 9729 13037 1121 -848 -1163 C ATOM 950 OG SER A 873 38.633 4.881 59.219 1.00 90.36 O ANISOU 950 OG SER A 873 11331 9709 13291 1156 -850 -1200 O ATOM 951 N PHE A 874 37.021 8.712 57.417 1.00 90.29 N ANISOU 951 N PHE A 874 11327 9853 13125 1005 -1136 -1182 N ATOM 952 CA PHE A 874 36.823 10.120 57.098 1.00 89.72 C ANISOU 952 CA PHE A 874 11274 9872 12943 969 -1170 -1146 C ATOM 953 C PHE A 874 36.263 10.841 58.313 1.00 90.60 C ANISOU 953 C PHE A 874 11245 9973 13208 916 -1038 -1013 C ATOM 954 O PHE A 874 35.307 10.367 58.936 1.00 92.40 O ANISOU 954 O PHE A 874 11343 10047 13719 881 -1037 -980 O ATOM 955 CB PHE A 874 35.887 10.268 55.898 1.00 91.04 C ANISOU 955 CB PHE A 874 11477 9938 13177 950 -1417 -1236 C ATOM 956 CG PHE A 874 36.406 9.605 54.660 1.00 92.12 C ANISOU 956 CG PHE A 874 11763 10086 13153 1001 -1552 -1371 C ATOM 957 CD1 PHE A 874 37.224 10.298 53.788 1.00 91.80 C ANISOU 957 CD1 PHE A 874 11877 10198 12804 1024 -1579 -1414 C ATOM 958 CD2 PHE A 874 36.101 8.284 54.381 1.00 93.27 C ANISOU 958 CD2 PHE A 874 11900 10089 13451 1023 -1644 -1456 C ATOM 959 CE1 PHE A 874 37.718 9.694 52.651 1.00 92.78 C ANISOU 959 CE1 PHE A 874 12143 10336 12772 1070 -1694 -1541 C ATOM 960 CE2 PHE A 874 36.594 7.671 53.246 1.00 94.23 C ANISOU 960 CE2 PHE A 874 12163 10221 13420 1073 -1766 -1585 C ATOM 961 CZ PHE A 874 37.406 8.377 52.381 1.00 94.15 C ANISOU 961 CZ PHE A 874 12306 10368 13099 1098 -1789 -1628 C ATOM 962 N VAL A 875 36.854 11.989 58.638 1.00 99.78 N ANISOU 962 N VAL A 875 12434 11295 14183 907 -924 -941 N ATOM 963 CA VAL A 875 36.540 12.734 59.849 1.00 97.71 C ANISOU 963 CA VAL A 875 12054 11051 14019 865 -772 -813 C ATOM 964 C VAL A 875 35.980 14.094 59.455 1.00 95.08 C ANISOU 964 C VAL A 875 11725 10750 13653 824 -850 -787 C ATOM 965 O VAL A 875 36.502 14.753 58.550 1.00 94.23 O ANISOU 965 O VAL A 875 11746 10749 13309 836 -920 -831 O ATOM 966 CB VAL A 875 37.785 12.900 60.744 1.00 95.56 C ANISOU 966 CB VAL A 875 11805 10943 13561 892 -550 -743 C ATOM 967 CG1 VAL A 875 37.409 13.509 62.089 1.00 95.66 C ANISOU 967 CG1 VAL A 875 11693 10955 13698 850 -388 -612 C ATOM 968 CG2 VAL A 875 38.496 11.564 60.935 1.00 96.26 C ANISOU 968 CG2 VAL A 875 11923 11015 13637 950 -496 -785 C ATOM 969 N GLN A 876 34.918 14.511 60.142 1.00 96.33 N ANISOU 969 N GLN A 876 11744 10812 14045 775 -835 -717 N ATOM 970 CA GLN A 876 34.312 15.820 59.938 1.00 96.93 C ANISOU 970 CA GLN A 876 11804 10905 14118 740 -898 -683 C ATOM 971 C GLN A 876 34.074 16.472 61.290 1.00 96.57 C ANISOU 971 C GLN A 876 11635 10881 14177 703 -713 -558 C ATOM 972 O GLN A 876 33.545 15.835 62.207 1.00 96.91 O ANISOU 972 O GLN A 876 11549 10822 14451 684 -628 -515 O ATOM 973 CB GLN A 876 32.993 15.710 59.168 1.00100.07 C ANISOU 973 CB GLN A 876 12151 11138 14732 721 -1126 -751 C ATOM 974 CG GLN A 876 32.188 17.000 59.141 1.00100.09 C ANISOU 974 CG GLN A 876 12106 11131 14792 688 -1188 -708 C ATOM 975 CD GLN A 876 31.148 17.021 58.039 1.00101.21 C ANISOU 975 CD GLN A 876 12252 11148 15057 688 -1453 -799 C ATOM 976 OE1 GLN A 876 31.009 16.061 57.281 1.00101.64 O ANISOU 976 OE1 GLN A 876 12343 11120 15154 709 -1592 -898 O ATOM 977 NE2 GLN A 876 30.412 18.122 57.942 1.00102.55 N ANISOU 977 NE2 GLN A 876 12383 11299 15281 670 -1530 -771 N ATOM 978 N VAL A 877 34.462 17.739 61.407 1.00108.59 N ANISOU 978 N VAL A 877 13202 12532 15527 691 -650 -501 N ATOM 979 CA VAL A 877 34.283 18.514 62.629 1.00107.37 C ANISOU 979 CA VAL A 877 12945 12410 15440 657 -479 -386 C ATOM 980 C VAL A 877 33.043 19.377 62.456 1.00108.37 C ANISOU 980 C VAL A 877 12993 12444 15739 622 -594 -373 C ATOM 981 O VAL A 877 32.989 20.231 61.562 1.00110.53 O ANISOU 981 O VAL A 877 13357 12755 15884 625 -724 -405 O ATOM 982 CB VAL A 877 35.515 19.381 62.932 1.00106.16 C ANISOU 982 CB VAL A 877 12887 12456 14994 664 -329 -332 C ATOM 983 CG1 VAL A 877 35.364 20.056 64.287 1.00105.19 C ANISOU 983 CG1 VAL A 877 12657 12363 14947 633 -142 -215 C ATOM 984 CG2 VAL A 877 36.786 18.546 62.882 1.00105.75 C ANISOU 984 CG2 VAL A 877 12923 12504 14753 709 -248 -368 C ATOM 985 N ARG A 878 32.051 19.167 63.315 1.00 99.07 N ANISOU 985 N ARG A 878 11648 11145 14849 590 -545 -328 N ATOM 986 CA ARG A 878 30.788 19.885 63.249 1.00100.23 C ANISOU 986 CA ARG A 878 11690 11191 15201 560 -648 -323 C ATOM 987 C ARG A 878 30.629 20.740 64.496 1.00100.02 C ANISOU 987 C ARG A 878 11566 11205 15232 529 -459 -211 C ATOM 988 O ARG A 878 30.873 20.271 65.613 1.00 98.83 O ANISOU 988 O ARG A 878 11347 11062 15144 516 -268 -145 O ATOM 989 CB ARG A 878 29.614 18.918 63.117 1.00101.06 C ANISOU 989 CB ARG A 878 11666 11105 15627 543 -765 -382 C ATOM 990 CG ARG A 878 29.515 18.248 61.752 1.00101.72 C ANISOU 990 CG ARG A 878 11839 11127 15683 571 -997 -505 C ATOM 991 CD ARG A 878 28.140 17.644 61.539 1.00103.34 C ANISOU 991 CD ARG A 878 11901 11139 16223 547 -1146 -568 C ATOM 992 NE ARG A 878 27.090 18.641 61.722 1.00103.67 N ANISOU 992 NE ARG A 878 11828 11130 16434 521 -1198 -542 N ATOM 993 CZ ARG A 878 25.810 18.358 61.942 1.00106.11 C ANISOU 993 CZ ARG A 878 11960 11284 17074 488 -1265 -568 C ATOM 994 NH1 ARG A 878 25.403 17.098 62.012 1.00108.13 N ANISOU 994 NH1 ARG A 878 12137 11415 17533 467 -1284 -619 N ATOM 995 NH2 ARG A 878 24.935 19.342 62.101 1.00106.82 N ANISOU 995 NH2 ARG A 878 11949 11341 17298 473 -1309 -548 N ATOM 996 N VAL A 879 30.212 21.988 64.303 1.00104.12 N ANISOU 996 N VAL A 879 12085 11746 15728 519 -516 -189 N ATOM 997 CA VAL A 879 30.031 22.942 65.390 1.00104.08 C ANISOU 997 CA VAL A 879 11998 11782 15766 492 -353 -90 C ATOM 998 C VAL A 879 28.593 23.434 65.361 1.00104.03 C ANISOU 998 C VAL A 879 11852 11642 16032 472 -465 -102 C ATOM 999 O VAL A 879 28.083 23.811 64.299 1.00104.22 O ANISOU 999 O VAL A 879 11919 11619 16062 489 -680 -169 O ATOM 1000 CB VAL A 879 31.011 24.124 65.277 1.00101.46 C ANISOU 1000 CB VAL A 879 11805 11619 15125 501 -293 -47 C ATOM 1001 CG1 VAL A 879 30.805 25.112 66.423 1.00100.62 C ANISOU 1001 CG1 VAL A 879 11613 11549 15067 473 -125 52 C ATOM 1002 CG2 VAL A 879 32.438 23.614 65.266 1.00100.67 C ANISOU 1002 CG2 VAL A 879 11831 11655 14765 522 -188 -48 C ATOM 1003 N SER A 880 27.942 23.424 66.519 1.00106.58 N ANISOU 1003 N SER A 880 12012 11903 16579 439 -321 -41 N ATOM 1004 CA SER A 880 26.608 23.995 66.636 1.00106.15 C ANISOU 1004 CA SER A 880 11809 11736 16786 420 -397 -48 C ATOM 1005 C SER A 880 26.579 25.035 67.762 1.00105.68 C ANISOU 1005 C SER A 880 11687 11738 16728 400 -208 51 C ATOM 1006 O SER A 880 27.177 24.809 68.809 1.00105.29 O ANISOU 1006 O SER A 880 11628 11752 16627 384 12 126 O ATOM 1007 CB SER A 880 25.570 22.906 66.900 1.00107.53 C ANISOU 1007 CB SER A 880 11814 11745 17299 391 -421 -89 C ATOM 1008 OG SER A 880 25.490 22.004 65.811 1.00110.02 O ANISOU 1008 OG SER A 880 12180 11991 17629 409 -615 -189 O ATOM 1009 N PRO A 881 25.898 26.180 67.553 1.00118.75 N ANISOU 1009 N PRO A 881 13309 13374 18438 405 -296 51 N ATOM 1010 CA PRO A 881 25.340 26.657 66.283 1.00121.01 C ANISOU 1010 CA PRO A 881 13643 13606 18728 435 -561 -28 C ATOM 1011 C PRO A 881 26.422 26.834 65.225 1.00120.52 C ANISOU 1011 C PRO A 881 13808 13654 18330 467 -661 -57 C ATOM 1012 O PRO A 881 27.460 27.430 65.516 1.00118.69 O ANISOU 1012 O PRO A 881 13693 13563 17842 466 -530 4 O ATOM 1013 CB PRO A 881 24.718 28.010 66.652 1.00120.85 C ANISOU 1013 CB PRO A 881 13560 13583 18772 436 -551 13 C ATOM 1014 CG PRO A 881 24.476 27.944 68.107 1.00119.45 C ANISOU 1014 CG PRO A 881 13233 13399 18756 399 -309 89 C ATOM 1015 CD PRO A 881 25.580 27.096 68.664 1.00117.64 C ANISOU 1015 CD PRO A 881 13072 13255 18372 384 -128 134 C ATOM 1016 N SER A 882 26.186 26.309 64.024 1.00133.29 N ANISOU 1016 N SER A 882 15486 15207 19951 491 -886 -152 N ATOM 1017 CA SER A 882 27.172 26.409 62.957 1.00134.28 C ANISOU 1017 CA SER A 882 15830 15428 19761 519 -984 -189 C ATOM 1018 C SER A 882 27.595 27.857 62.780 1.00131.84 C ANISOU 1018 C SER A 882 15645 15220 19228 527 -978 -140 C ATOM 1019 O SER A 882 26.755 28.755 62.679 1.00130.38 O ANISOU 1019 O SER A 882 15413 14976 19151 535 -1075 -136 O ATOM 1020 CB SER A 882 26.595 25.864 61.648 1.00134.70 C ANISOU 1020 CB SER A 882 15922 15378 19879 547 -1258 -302 C ATOM 1021 OG SER A 882 26.149 24.528 61.799 1.00136.87 O ANISOU 1021 OG SER A 882 16079 15548 20375 535 -1270 -352 O ATOM 1022 N VAL A 883 28.903 28.082 62.744 1.00107.34 N ANISOU 1022 N VAL A 883 12699 12268 15816 524 -865 -106 N ATOM 1023 CA VAL A 883 29.452 29.415 62.551 1.00106.38 C ANISOU 1023 CA VAL A 883 12715 12251 15454 523 -844 -60 C ATOM 1024 C VAL A 883 29.855 29.490 61.084 1.00106.08 C ANISOU 1024 C VAL A 883 12878 12236 15193 547 -1040 -132 C ATOM 1025 O VAL A 883 30.878 28.934 60.672 1.00103.42 O ANISOU 1025 O VAL A 883 12661 11988 14644 549 -1004 -159 O ATOM 1026 CB VAL A 883 30.636 29.681 63.486 1.00103.75 C ANISOU 1026 CB VAL A 883 12421 12073 14925 497 -586 21 C ATOM 1027 CG1 VAL A 883 30.999 31.151 63.478 1.00103.77 C ANISOU 1027 CG1 VAL A 883 12531 12162 14736 485 -551 76 C ATOM 1028 CG2 VAL A 883 30.320 29.223 64.908 1.00104.00 C ANISOU 1028 CG2 VAL A 883 12266 12076 15174 476 -392 81 C ATOM 1029 N SER A 884 29.042 30.187 60.290 1.00120.15 N ANISOU 1029 N SER A 884 14697 13934 17021 570 -1250 -165 N ATOM 1030 CA SER A 884 29.366 30.403 58.887 1.00122.68 C ANISOU 1030 CA SER A 884 15226 14270 17117 593 -1442 -227 C ATOM 1031 C SER A 884 30.302 31.589 58.708 1.00123.52 C ANISOU 1031 C SER A 884 15518 14507 16907 576 -1366 -172 C ATOM 1032 O SER A 884 31.082 31.619 57.752 1.00125.00 O ANISOU 1032 O SER A 884 15903 14764 16828 579 -1427 -208 O ATOM 1033 CB SER A 884 28.086 30.613 58.078 1.00122.98 C ANISOU 1033 CB SER A 884 15234 14155 17336 630 -1715 -290 C ATOM 1034 OG SER A 884 27.440 31.813 58.460 1.00123.96 O ANISOU 1034 OG SER A 884 15311 14245 17542 634 -1727 -237 O ATOM 1035 N GLU A 885 30.237 32.566 59.616 1.00114.44 N ANISOU 1035 N GLU A 885 14310 13390 15782 555 -1229 -87 N ATOM 1036 CA GLU A 885 31.033 33.778 59.468 1.00112.14 C ANISOU 1036 CA GLU A 885 14191 13209 15209 534 -1162 -34 C ATOM 1037 C GLU A 885 32.517 33.494 59.659 1.00112.60 C ANISOU 1037 C GLU A 885 14348 13434 15000 500 -970 -16 C ATOM 1038 O GLU A 885 33.357 34.159 59.045 1.00113.87 O ANISOU 1038 O GLU A 885 14702 13690 14872 482 -963 -11 O ATOM 1039 CB GLU A 885 30.572 34.841 60.467 1.00110.53 C ANISOU 1039 CB GLU A 885 13888 12993 15116 520 -1057 49 C ATOM 1040 CG GLU A 885 29.063 34.914 60.669 1.00112.93 C ANISOU 1040 CG GLU A 885 14015 13134 15757 552 -1190 33 C ATOM 1041 CD GLU A 885 28.582 34.066 61.835 1.00114.62 C ANISOU 1041 CD GLU A 885 13989 13307 16254 541 -1050 48 C ATOM 1042 OE1 GLU A 885 29.322 33.943 62.835 1.00111.81 O ANISOU 1042 OE1 GLU A 885 13594 13051 15838 508 -813 109 O ATOM 1043 OE2 GLU A 885 27.464 33.517 61.751 1.00117.39 O ANISOU 1043 OE2 GLU A 885 14193 13522 16886 564 -1178 -2 O ATOM 1044 N PHE A 886 32.854 32.531 60.510 1.00 91.68 N ANISOU 1044 N PHE A 886 11572 10821 12442 492 -811 -7 N ATOM 1045 CA PHE A 886 34.238 32.214 60.827 1.00 90.96 C ANISOU 1045 CA PHE A 886 11547 10888 12125 469 -621 8 C ATOM 1046 C PHE A 886 34.808 31.167 59.879 1.00 89.07 C ANISOU 1046 C PHE A 886 11405 10672 11763 488 -703 -79 C ATOM 1047 O PHE A 886 34.097 30.286 59.390 1.00 89.84 O ANISOU 1047 O PHE A 886 11452 10655 12027 519 -855 -144 O ATOM 1048 CB PHE A 886 34.356 31.732 62.270 1.00 89.85 C ANISOU 1048 CB PHE A 886 11232 10777 12132 457 -406 65 C ATOM 1049 CG PHE A 886 34.294 32.842 63.271 1.00 88.08 C ANISOU 1049 CG PHE A 886 10953 10590 11922 429 -262 155 C ATOM 1050 CD1 PHE A 886 35.415 33.198 63.999 1.00 87.58 C ANISOU 1050 CD1 PHE A 886 10926 10679 11673 399 -51 208 C ATOM 1051 CD2 PHE A 886 33.121 33.550 63.462 1.00 86.92 C ANISOU 1051 CD2 PHE A 886 10722 10328 11974 435 -344 181 C ATOM 1052 CE1 PHE A 886 35.359 34.225 64.912 1.00 87.19 C ANISOU 1052 CE1 PHE A 886 10833 10662 11634 372 78 287 C ATOM 1053 CE2 PHE A 886 33.059 34.578 64.371 1.00 87.70 C ANISOU 1053 CE2 PHE A 886 10777 10459 12086 412 -213 259 C ATOM 1054 CZ PHE A 886 34.179 34.920 65.096 1.00 88.62 C ANISOU 1054 CZ PHE A 886 10936 10725 12012 379 -1 313 C ATOM 1055 N LEU A 887 36.101 31.302 59.599 1.00 88.38 N ANISOU 1055 N LEU A 887 11462 10736 11383 469 -602 -85 N ATOM 1056 CA LEU A 887 36.847 30.321 58.826 1.00 88.74 C ANISOU 1056 CA LEU A 887 11600 10831 11286 487 -636 -167 C ATOM 1057 C LEU A 887 37.400 29.256 59.765 1.00 87.93 C ANISOU 1057 C LEU A 887 11373 10781 11255 496 -465 -161 C ATOM 1058 O LEU A 887 37.981 29.580 60.806 1.00 86.76 O ANISOU 1058 O LEU A 887 11167 10728 11069 474 -265 -93 O ATOM 1059 CB LEU A 887 37.986 31.000 58.063 1.00 88.58 C ANISOU 1059 CB LEU A 887 11790 10951 10914 459 -602 -182 C ATOM 1060 CG LEU A 887 39.020 30.095 57.388 1.00 88.76 C ANISOU 1060 CG LEU A 887 11913 11066 10746 472 -583 -264 C ATOM 1061 CD1 LEU A 887 38.367 29.219 56.333 1.00 91.28 C ANISOU 1061 CD1 LEU A 887 12270 11264 11148 514 -805 -356 C ATOM 1062 CD2 LEU A 887 40.129 30.937 56.781 1.00 88.57 C ANISOU 1062 CD2 LEU A 887 12083 11187 10383 431 -517 -268 C ATOM 1063 N LEU A 888 37.226 27.990 59.392 1.00 81.67 N ANISOU 1063 N LEU A 888 10548 9922 10562 531 -548 -232 N ATOM 1064 CA LEU A 888 37.670 26.863 60.202 1.00 81.13 C ANISOU 1064 CA LEU A 888 10371 9879 10575 549 -411 -232 C ATOM 1065 C LEU A 888 38.870 26.195 59.547 1.00 81.16 C ANISOU 1065 C LEU A 888 10498 9995 10344 568 -385 -305 C ATOM 1066 O LEU A 888 38.863 25.933 58.339 1.00 82.16 O ANISOU 1066 O LEU A 888 10744 10095 10377 585 -543 -388 O ATOM 1067 CB LEU A 888 36.546 25.842 60.398 1.00 81.95 C ANISOU 1067 CB LEU A 888 10329 9811 10996 573 -508 -257 C ATOM 1068 CG LEU A 888 35.556 26.163 61.518 1.00 81.67 C ANISOU 1068 CG LEU A 888 10116 9685 11229 554 -445 -177 C ATOM 1069 CD1 LEU A 888 34.636 27.310 61.124 1.00 82.19 C ANISOU 1069 CD1 LEU A 888 10194 9682 11352 540 -577 -160 C ATOM 1070 CD2 LEU A 888 34.754 24.928 61.905 1.00 82.33 C ANISOU 1070 CD2 LEU A 888 10050 9628 11605 570 -477 -201 C ATOM 1071 N GLN A 889 39.894 25.923 60.351 1.00 91.56 N ANISOU 1071 N GLN A 889 11784 11436 11567 569 -188 -278 N ATOM 1072 CA GLN A 889 41.078 25.206 59.909 1.00 90.48 C ANISOU 1072 CA GLN A 889 11735 11413 11231 594 -139 -349 C ATOM 1073 C GLN A 889 41.570 24.328 61.049 1.00 89.09 C ANISOU 1073 C GLN A 889 11439 11272 11139 622 26 -322 C ATOM 1074 O GLN A 889 41.359 24.637 62.225 1.00 88.03 O ANISOU 1074 O GLN A 889 11192 11136 11119 606 151 -234 O ATOM 1075 CB GLN A 889 42.189 26.163 59.463 1.00 89.21 C ANISOU 1075 CB GLN A 889 11721 11423 10753 561 -62 -354 C ATOM 1076 CG GLN A 889 41.929 26.855 58.133 1.00 89.54 C ANISOU 1076 CG GLN A 889 11927 11440 10655 541 -228 -398 C ATOM 1077 CD GLN A 889 42.987 27.887 57.800 1.00 90.52 C ANISOU 1077 CD GLN A 889 12192 11726 10474 495 -131 -391 C ATOM 1078 OE1 GLN A 889 43.337 28.724 58.632 1.00 90.12 O ANISOU 1078 OE1 GLN A 889 12104 11757 10379 457 17 -315 O ATOM 1079 NE2 GLN A 889 43.514 27.825 56.583 1.00 95.75 N ANISOU 1079 NE2 GLN A 889 13021 12435 10923 493 -208 -473 N ATOM 1080 N LEU A 890 42.225 23.227 60.692 1.00 76.62 N ANISOU 1080 N LEU A 890 9892 9721 9498 666 23 -399 N ATOM 1081 CA LEU A 890 42.731 22.265 61.664 1.00 76.12 C ANISOU 1081 CA LEU A 890 9734 9683 9505 704 158 -384 C ATOM 1082 C LEU A 890 44.232 22.475 61.820 1.00 75.38 C ANISOU 1082 C LEU A 890 9703 9790 9146 711 311 -399 C ATOM 1083 O LEU A 890 45.010 22.146 60.920 1.00 75.85 O ANISOU 1083 O LEU A 890 9869 9927 9023 733 276 -489 O ATOM 1084 CB LEU A 890 42.412 20.838 61.223 1.00 77.13 C ANISOU 1084 CB LEU A 890 9847 9693 9765 754 49 -462 C ATOM 1085 CG LEU A 890 40.926 20.520 61.044 1.00 78.03 C ANISOU 1085 CG LEU A 890 9887 9603 10156 745 -108 -460 C ATOM 1086 CD1 LEU A 890 40.735 19.104 60.528 1.00 79.08 C ANISOU 1086 CD1 LEU A 890 10022 9631 10396 791 -215 -548 C ATOM 1087 CD2 LEU A 890 40.171 20.710 62.347 1.00 77.46 C ANISOU 1087 CD2 LEU A 890 9660 9456 10314 720 -10 -355 C ATOM 1088 N ASP A 891 44.635 23.010 62.974 1.00 76.02 N ANISOU 1088 N ASP A 891 9714 9958 9212 694 482 -316 N ATOM 1089 CA ASP A 891 46.052 23.238 63.236 1.00 75.32 C ANISOU 1089 CA ASP A 891 9666 10064 8889 699 633 -330 C ATOM 1090 C ASP A 891 46.779 21.919 63.460 1.00 75.51 C ANISOU 1090 C ASP A 891 9662 10116 8912 771 679 -386 C ATOM 1091 O ASP A 891 47.862 21.692 62.907 1.00 75.68 O ANISOU 1091 O ASP A 891 9758 10265 8732 795 707 -466 O ATOM 1092 CB ASP A 891 46.223 24.150 64.454 1.00 74.18 C ANISOU 1092 CB ASP A 891 9450 9993 8742 663 793 -227 C ATOM 1093 CG ASP A 891 45.568 25.506 64.271 1.00 74.00 C ANISOU 1093 CG ASP A 891 9458 9946 8711 596 755 -171 C ATOM 1094 OD1 ASP A 891 45.488 25.988 63.120 1.00 74.59 O ANISOU 1094 OD1 ASP A 891 9649 10021 8671 570 642 -220 O ATOM 1095 OD2 ASP A 891 45.134 26.092 65.286 1.00 73.32 O ANISOU 1095 OD2 ASP A 891 9287 9838 8732 570 839 -80 O ATOM 1096 N SER A 892 46.194 21.036 64.264 1.00 77.81 N ANISOU 1096 N SER A 892 9849 10288 9427 807 690 -347 N ATOM 1097 CA SER A 892 46.827 19.775 64.618 1.00 76.83 C ANISOU 1097 CA SER A 892 9697 10175 9321 880 738 -387 C ATOM 1098 C SER A 892 45.750 18.724 64.823 1.00 77.43 C ANISOU 1098 C SER A 892 9704 10048 9669 905 652 -376 C ATOM 1099 O SER A 892 44.658 19.029 65.309 1.00 80.02 O ANISOU 1099 O SER A 892 9957 10256 10192 866 634 -302 O ATOM 1100 CB SER A 892 47.671 19.900 65.895 1.00 75.76 C ANISOU 1100 CB SER A 892 9499 10159 9128 899 925 -325 C ATOM 1101 OG SER A 892 48.448 21.085 65.898 1.00 75.76 O ANISOU 1101 OG SER A 892 9539 10330 8916 855 1014 -314 O ATOM 1102 N CYS A 893 46.063 17.490 64.439 1.00 75.46 N ANISOU 1102 N CYS A 893 9478 9759 9434 968 601 -455 N ATOM 1103 CA CYS A 893 45.232 16.344 64.766 1.00 76.15 C ANISOU 1103 CA CYS A 893 9500 9662 9771 997 546 -447 C ATOM 1104 C CYS A 893 46.132 15.197 65.190 1.00 76.29 C ANISOU 1104 C CYS A 893 9518 9714 9753 1078 618 -481 C ATOM 1105 O CYS A 893 47.238 15.028 64.670 1.00 76.35 O ANISOU 1105 O CYS A 893 9598 9855 9557 1122 633 -562 O ATOM 1106 CB CYS A 893 44.345 15.907 63.596 1.00 77.33 C ANISOU 1106 CB CYS A 893 9689 9668 10024 987 348 -523 C ATOM 1107 SG CYS A 893 42.912 16.964 63.285 1.00 77.48 S ANISOU 1107 SG CYS A 893 9674 9576 10188 905 236 -474 S ATOM 1108 N HIS A 894 45.648 14.416 66.152 1.00 79.11 N ANISOU 1108 N HIS A 894 9797 9949 10311 1099 664 -420 N ATOM 1109 CA HIS A 894 46.383 13.275 66.670 1.00 76.91 C ANISOU 1109 CA HIS A 894 9520 9675 10027 1181 727 -440 C ATOM 1110 C HIS A 894 45.392 12.174 67.008 1.00 77.49 C ANISOU 1110 C HIS A 894 9543 9530 10368 1189 676 -418 C ATOM 1111 O HIS A 894 44.222 12.438 67.299 1.00 77.75 O ANISOU 1111 O HIS A 894 9510 9434 10599 1126 652 -354 O ATOM 1112 CB HIS A 894 47.205 13.638 67.916 1.00 76.99 C ANISOU 1112 CB HIS A 894 9493 9815 9946 1203 907 -362 C ATOM 1113 CG HIS A 894 48.287 14.642 67.662 1.00 77.45 C ANISOU 1113 CG HIS A 894 9593 10093 9741 1196 972 -390 C ATOM 1114 ND1 HIS A 894 48.061 16.001 67.690 1.00 78.51 N ANISOU 1114 ND1 HIS A 894 9718 10299 9813 1118 1004 -338 N ATOM 1115 CD2 HIS A 894 49.602 14.484 67.381 1.00 77.08 C ANISOU 1115 CD2 HIS A 894 9595 10209 9482 1254 1013 -468 C ATOM 1116 CE1 HIS A 894 49.190 16.638 67.434 1.00 77.68 C ANISOU 1116 CE1 HIS A 894 9659 10388 9468 1122 1065 -380 C ATOM 1117 NE2 HIS A 894 50.141 15.741 67.243 1.00 77.26 N ANISOU 1117 NE2 HIS A 894 9636 10398 9321 1203 1074 -461 N ATOM 1118 N LEU A 895 45.872 10.937 66.956 1.00 81.58 N ANISOU 1118 N LEU A 895 10095 10007 10896 1266 660 -475 N ATOM 1119 CA LEU A 895 45.111 9.772 67.389 1.00 82.44 C ANISOU 1119 CA LEU A 895 10167 9913 11245 1280 633 -453 C ATOM 1120 C LEU A 895 45.918 9.056 68.457 1.00 82.27 C ANISOU 1120 C LEU A 895 10145 9920 11194 1357 762 -411 C ATOM 1121 O LEU A 895 47.042 8.614 68.196 1.00 82.37 O ANISOU 1121 O LEU A 895 10217 10040 11039 1439 771 -483 O ATOM 1122 CB LEU A 895 44.809 8.838 66.217 1.00 83.71 C ANISOU 1122 CB LEU A 895 10382 9960 11464 1304 466 -570 C ATOM 1123 CG LEU A 895 44.270 7.449 66.566 1.00 84.77 C ANISOU 1123 CG LEU A 895 10499 9893 11816 1332 437 -570 C ATOM 1124 CD1 LEU A 895 42.965 7.553 67.335 1.00 84.88 C ANISOU 1124 CD1 LEU A 895 10415 9743 12091 1253 465 -467 C ATOM 1125 CD2 LEU A 895 44.094 6.624 65.303 1.00 86.00 C ANISOU 1125 CD2 LEU A 895 10720 9961 11997 1358 266 -700 C ATOM 1126 N ASP A 896 45.342 8.937 69.651 1.00 78.70 N ANISOU 1126 N ASP A 896 9628 9372 10903 1332 859 -296 N ATOM 1127 CA ASP A 896 46.035 8.402 70.816 1.00 78.49 C ANISOU 1127 CA ASP A 896 9605 9371 10848 1399 991 -235 C ATOM 1128 C ASP A 896 45.540 6.984 71.063 1.00 79.67 C ANISOU 1128 C ASP A 896 9765 9315 11192 1432 958 -234 C ATOM 1129 O ASP A 896 44.366 6.777 71.387 1.00 80.15 O ANISOU 1129 O ASP A 896 9772 9200 11480 1365 951 -176 O ATOM 1130 CB ASP A 896 45.802 9.290 72.036 1.00 77.53 C ANISOU 1130 CB ASP A 896 9418 9290 10748 1349 1136 -104 C ATOM 1131 CG ASP A 896 46.586 8.835 73.246 1.00 77.30 C ANISOU 1131 CG ASP A 896 9405 9305 10663 1422 1269 -40 C ATOM 1132 OD1 ASP A 896 47.637 8.181 73.068 1.00 77.57 O ANISOU 1132 OD1 ASP A 896 9497 9412 10563 1519 1258 -108 O ATOM 1133 OD2 ASP A 896 46.150 9.132 74.378 1.00 76.93 O ANISOU 1133 OD2 ASP A 896 9312 9217 10702 1386 1383 75 O ATOM 1134 N LEU A 897 46.437 6.014 70.910 1.00 96.15 N ANISOU 1134 N LEU A 897 11919 11421 13192 1533 940 -302 N ATOM 1135 CA LEU A 897 46.131 4.614 71.158 1.00 97.90 C ANISOU 1135 CA LEU A 897 12169 11452 13575 1577 913 -305 C ATOM 1136 C LEU A 897 46.392 4.208 72.603 1.00 96.92 C ANISOU 1136 C LEU A 897 12045 11296 13483 1618 1056 -194 C ATOM 1137 O LEU A 897 46.242 3.028 72.939 1.00 96.47 O ANISOU 1137 O LEU A 897 12026 11084 13546 1662 1050 -185 O ATOM 1138 CB LEU A 897 46.945 3.729 70.207 1.00 98.38 C ANISOU 1138 CB LEU A 897 12311 11539 13530 1673 811 -442 C ATOM 1139 CG LEU A 897 46.845 4.119 68.727 1.00 97.88 C ANISOU 1139 CG LEU A 897 12269 11526 13394 1643 672 -561 C ATOM 1140 CD1 LEU A 897 47.781 3.283 67.864 1.00 99.10 C ANISOU 1140 CD1 LEU A 897 12507 11727 13419 1745 592 -699 C ATOM 1141 CD2 LEU A 897 45.411 4.002 68.225 1.00 95.33 C ANISOU 1141 CD2 LEU A 897 11909 11011 13299 1549 563 -562 C ATOM 1142 N GLY A 898 46.780 5.152 73.457 1.00126.75 N ANISOU 1142 N GLY A 898 15791 15213 17156 1607 1181 -110 N ATOM 1143 CA GLY A 898 47.001 4.880 74.855 1.00126.89 C ANISOU 1143 CA GLY A 898 15815 15207 17192 1642 1316 0 C ATOM 1144 C GLY A 898 48.358 4.260 75.106 1.00125.76 C ANISOU 1144 C GLY A 898 15741 15167 16876 1777 1339 -42 C ATOM 1145 O GLY A 898 49.165 4.078 74.188 1.00123.61 O ANISOU 1145 O GLY A 898 15503 14996 16465 1841 1258 -162 O ATOM 1146 N PRO A 899 48.642 3.935 76.366 1.00 99.43 N ANISOU 1146 N PRO A 899 12427 11810 13542 1824 1450 53 N ATOM 1147 CA PRO A 899 49.898 3.245 76.676 1.00 99.95 C ANISOU 1147 CA PRO A 899 12560 11956 13461 1965 1463 14 C ATOM 1148 C PRO A 899 50.008 1.939 75.905 1.00101.55 C ANISOU 1148 C PRO A 899 12827 12036 13721 2038 1347 -86 C ATOM 1149 O PRO A 899 49.024 1.218 75.727 1.00101.89 O ANISOU 1149 O PRO A 899 12881 11868 13965 1991 1298 -73 O ATOM 1150 CB PRO A 899 49.811 3.011 78.188 1.00 99.70 C ANISOU 1150 CB PRO A 899 12549 11855 13478 1984 1591 152 C ATOM 1151 CG PRO A 899 48.879 4.063 78.679 1.00 99.32 C ANISOU 1151 CG PRO A 899 12428 11797 13513 1856 1673 253 C ATOM 1152 CD PRO A 899 47.876 4.260 77.582 1.00 97.97 C ANISOU 1152 CD PRO A 899 12208 11539 13477 1756 1573 199 C ATOM 1153 N GLU A 900 51.222 1.655 75.432 1.00115.40 N ANISOU 1153 N GLU A 900 14620 13929 15300 2152 1303 -193 N ATOM 1154 CA GLU A 900 51.530 0.451 74.666 1.00116.91 C ANISOU 1154 CA GLU A 900 14876 14033 15511 2240 1194 -305 C ATOM 1155 C GLU A 900 51.065 0.572 73.217 1.00118.74 C ANISOU 1155 C GLU A 900 15095 14249 15773 2179 1070 -417 C ATOM 1156 O GLU A 900 51.503 -0.206 72.362 1.00118.92 O ANISOU 1156 O GLU A 900 15169 14256 15761 2253 973 -538 O ATOM 1157 CB GLU A 900 50.893 -0.784 75.319 1.00118.18 C ANISOU 1157 CB GLU A 900 15096 13943 15866 2262 1196 -237 C ATOM 1158 CG GLU A 900 51.431 -2.110 74.810 1.00121.39 C ANISOU 1158 CG GLU A 900 15585 14266 16273 2383 1102 -340 C ATOM 1159 CD GLU A 900 50.583 -3.286 75.253 1.00121.88 C ANISOU 1159 CD GLU A 900 15706 14051 16553 2373 1091 -278 C ATOM 1160 OE1 GLU A 900 51.141 -4.246 75.827 1.00120.28 O ANISOU 1160 OE1 GLU A 900 15584 13780 16338 2488 1102 -266 O ATOM 1161 OE2 GLU A 900 49.354 -3.246 75.033 1.00121.18 O ANISOU 1161 OE2 GLU A 900 15583 13809 16651 2250 1070 -242 O ATOM 1162 N GLY A 901 50.187 1.533 72.924 1.00108.66 N ANISOU 1162 N GLY A 901 13756 12973 14556 2049 1067 -380 N ATOM 1163 CA GLY A 901 49.739 1.744 71.562 1.00106.36 C ANISOU 1163 CA GLY A 901 13458 12672 14280 1991 944 -482 C ATOM 1164 C GLY A 901 50.458 2.872 70.851 1.00104.74 C ANISOU 1164 C GLY A 901 13235 12704 13859 1978 941 -551 C ATOM 1165 O GLY A 901 50.468 2.927 69.617 1.00105.61 O ANISOU 1165 O GLY A 901 13367 12842 13916 1966 835 -663 O ATOM 1166 N GLY A 902 51.062 3.778 71.612 1.00116.19 N ANISOU 1166 N GLY A 902 14649 14322 15177 1978 1057 -487 N ATOM 1167 CA GLY A 902 51.701 4.943 71.033 1.00116.04 C ANISOU 1167 CA GLY A 902 14609 14522 14957 1949 1070 -540 C ATOM 1168 C GLY A 902 50.686 5.931 70.477 1.00116.41 C ANISOU 1168 C GLY A 902 14619 14544 15067 1817 1030 -514 C ATOM 1169 O GLY A 902 49.472 5.739 70.535 1.00116.77 O ANISOU 1169 O GLY A 902 14642 14407 15317 1748 990 -459 O ATOM 1170 N THR A 903 51.218 7.018 69.923 1.00 97.54 N ANISOU 1170 N THR A 903 12223 12342 12495 1783 1042 -557 N ATOM 1171 CA THR A 903 50.417 8.069 69.309 1.00 95.46 C ANISOU 1171 CA THR A 903 11938 12081 12252 1668 998 -542 C ATOM 1172 C THR A 903 50.829 8.237 67.853 1.00 96.11 C ANISOU 1172 C THR A 903 12078 12250 12188 1669 895 -678 C ATOM 1173 O THR A 903 52.022 8.267 67.535 1.00 96.17 O ANISOU 1173 O THR A 903 12117 12427 11998 1731 924 -760 O ATOM 1174 CB THR A 903 50.581 9.406 70.046 1.00 94.62 C ANISOU 1174 CB THR A 903 11782 12113 12056 1608 1117 -451 C ATOM 1175 OG1 THR A 903 50.197 9.252 71.418 1.00 96.78 O ANISOU 1175 OG1 THR A 903 12009 12306 12457 1608 1217 -325 O ATOM 1176 CG2 THR A 903 49.721 10.493 69.407 1.00 95.47 C ANISOU 1176 CG2 THR A 903 11874 12212 12190 1495 1064 -434 C ATOM 1177 N VAL A 904 49.835 8.348 66.976 1.00 85.26 N ANISOU 1177 N VAL A 904 10718 10763 10914 1601 776 -703 N ATOM 1178 CA VAL A 904 50.052 8.625 65.561 1.00 85.65 C ANISOU 1178 CA VAL A 904 10832 10880 10829 1587 672 -821 C ATOM 1179 C VAL A 904 49.629 10.062 65.299 1.00 84.85 C ANISOU 1179 C VAL A 904 10718 10851 10669 1483 676 -776 C ATOM 1180 O VAL A 904 48.581 10.508 65.783 1.00 84.52 O ANISOU 1180 O VAL A 904 10620 10705 10789 1412 677 -679 O ATOM 1181 CB VAL A 904 49.283 7.642 64.659 1.00 86.92 C ANISOU 1181 CB VAL A 904 11035 10857 11133 1595 513 -898 C ATOM 1182 CG1 VAL A 904 47.803 7.693 64.944 1.00 87.07 C ANISOU 1182 CG1 VAL A 904 10998 10682 11403 1514 460 -814 C ATOM 1183 CG2 VAL A 904 49.537 7.947 63.190 1.00 87.38 C ANISOU 1183 CG2 VAL A 904 11176 10991 11035 1583 405 -1022 C ATOM 1184 N GLU A 905 50.451 10.788 64.549 1.00 98.76 N ANISOU 1184 N GLU A 905 12533 12790 12201 1475 684 -846 N ATOM 1185 CA GLU A 905 50.185 12.180 64.209 1.00 98.40 C ANISOU 1185 CA GLU A 905 12495 12824 12068 1381 688 -812 C ATOM 1186 C GLU A 905 49.503 12.211 62.846 1.00 98.28 C ANISOU 1186 C GLU A 905 12553 12727 12063 1343 523 -888 C ATOM 1187 O GLU A 905 50.137 11.944 61.820 1.00101.99 O ANISOU 1187 O GLU A 905 13106 13266 12381 1376 467 -1005 O ATOM 1188 CB GLU A 905 51.488 12.976 64.206 1.00 99.52 C ANISOU 1188 CB GLU A 905 12659 13204 11949 1386 800 -842 C ATOM 1189 CG GLU A 905 51.326 14.479 64.109 1.00101.11 C ANISOU 1189 CG GLU A 905 12866 13496 12054 1289 837 -787 C ATOM 1190 CD GLU A 905 52.643 15.205 64.308 1.00102.64 C ANISOU 1190 CD GLU A 905 13067 13922 12011 1291 969 -809 C ATOM 1191 OE1 GLU A 905 53.701 14.594 64.049 1.00104.11 O ANISOU 1191 OE1 GLU A 905 13275 14210 12072 1363 997 -905 O ATOM 1192 OE2 GLU A 905 52.624 16.378 64.735 1.00101.26 O ANISOU 1192 OE2 GLU A 905 12870 13824 11780 1221 1045 -735 O ATOM 1193 N LEU A 906 48.211 12.540 62.837 1.00 78.59 N ANISOU 1193 N LEU A 906 10025 10086 9748 1275 444 -826 N ATOM 1194 CA LEU A 906 47.458 12.567 61.589 1.00 79.47 C ANISOU 1194 CA LEU A 906 10202 10105 9888 1241 271 -895 C ATOM 1195 C LEU A 906 47.696 13.864 60.827 1.00 79.12 C ANISOU 1195 C LEU A 906 10230 10190 9643 1181 256 -910 C ATOM 1196 O LEU A 906 47.881 13.845 59.605 1.00 79.87 O ANISOU 1196 O LEU A 906 10428 10309 9610 1184 153 -1010 O ATOM 1197 CB LEU A 906 45.966 12.380 61.873 1.00 79.82 C ANISOU 1197 CB LEU A 906 10174 9939 10216 1196 184 -831 C ATOM 1198 CG LEU A 906 45.582 11.155 62.707 1.00 80.23 C ANISOU 1198 CG LEU A 906 10153 9840 10490 1238 208 -800 C ATOM 1199 CD1 LEU A 906 44.093 11.164 63.018 1.00 80.56 C ANISOU 1199 CD1 LEU A 906 10111 9689 10808 1175 141 -733 C ATOM 1200 CD2 LEU A 906 45.969 9.865 62.002 1.00 81.34 C ANISOU 1200 CD2 LEU A 906 10359 9929 10619 1313 122 -917 C ATOM 1201 N ILE A 907 47.706 14.994 61.528 1.00 79.60 N ANISOU 1201 N ILE A 907 10247 10330 9667 1127 360 -813 N ATOM 1202 CA ILE A 907 47.898 16.301 60.914 1.00 79.25 C ANISOU 1202 CA ILE A 907 10273 10399 9439 1063 358 -813 C ATOM 1203 C ILE A 907 48.799 17.124 61.818 1.00 78.06 C ANISOU 1203 C ILE A 907 10086 10422 9152 1046 541 -748 C ATOM 1204 O ILE A 907 48.736 17.010 63.046 1.00 77.39 O ANISOU 1204 O ILE A 907 9902 10321 9180 1058 646 -663 O ATOM 1205 CB ILE A 907 46.556 17.029 60.678 1.00 79.37 C ANISOU 1205 CB ILE A 907 10276 10284 9596 993 246 -755 C ATOM 1206 CG1 ILE A 907 45.667 16.207 59.741 1.00 80.66 C ANISOU 1206 CG1 ILE A 907 10474 10278 9896 1009 52 -830 C ATOM 1207 CG2 ILE A 907 46.793 18.432 60.116 1.00 79.00 C ANISOU 1207 CG2 ILE A 907 10314 10353 9351 929 251 -745 C ATOM 1208 CD1 ILE A 907 44.293 16.802 59.504 1.00 80.97 C ANISOU 1208 CD1 ILE A 907 10487 10177 10100 951 -76 -785 C ATOM 1209 N GLN A 908 49.644 17.951 61.209 1.00 89.21 N ANISOU 1209 N GLN A 908 11581 11998 10317 1016 582 -791 N ATOM 1210 CA GLN A 908 50.471 18.872 61.970 1.00 88.32 C ANISOU 1210 CA GLN A 908 11439 12053 10067 987 747 -737 C ATOM 1211 C GLN A 908 50.818 20.065 61.095 1.00 88.40 C ANISOU 1211 C GLN A 908 11554 12174 9859 916 742 -763 C ATOM 1212 O GLN A 908 50.833 19.976 59.866 1.00 93.55 O ANISOU 1212 O GLN A 908 12316 12820 10410 910 637 -849 O ATOM 1213 CB GLN A 908 51.748 18.196 62.482 1.00 88.88 C ANISOU 1213 CB GLN A 908 11477 12256 10038 1060 868 -785 C ATOM 1214 CG GLN A 908 52.514 19.022 63.509 1.00 89.61 C ANISOU 1214 CG GLN A 908 11511 12503 10032 1037 1039 -719 C ATOM 1215 CD GLN A 908 51.688 19.342 64.743 1.00 90.41 C ANISOU 1215 CD GLN A 908 11516 12513 10323 1012 1088 -585 C ATOM 1216 OE1 GLN A 908 51.617 20.493 65.175 1.00 89.80 O ANISOU 1216 OE1 GLN A 908 11424 12494 10201 946 1158 -513 O ATOM 1217 NE2 GLN A 908 51.061 18.321 65.319 1.00 90.73 N ANISOU 1217 NE2 GLN A 908 11494 12406 10574 1064 1055 -553 N ATOM 1218 N GLY A 909 51.097 21.188 61.750 1.00 80.04 N ANISOU 1218 N GLY A 909 10469 11216 8725 859 859 -687 N ATOM 1219 CA GLY A 909 51.488 22.390 61.039 1.00 81.30 C ANISOU 1219 CA GLY A 909 10732 11486 8673 784 876 -702 C ATOM 1220 C GLY A 909 50.468 22.864 60.030 1.00 82.81 C ANISOU 1220 C GLY A 909 11018 11556 8892 738 715 -701 C ATOM 1221 O GLY A 909 50.839 23.496 59.034 1.00 82.79 O ANISOU 1221 O GLY A 909 11142 11624 8690 694 687 -752 O ATOM 1222 N ARG A 910 49.191 22.567 60.254 1.00 84.25 N ANISOU 1222 N ARG A 910 11143 11555 9315 747 605 -649 N ATOM 1223 CA ARG A 910 48.082 22.981 59.402 1.00 83.24 C ANISOU 1223 CA ARG A 910 11084 11293 9252 712 434 -645 C ATOM 1224 C ARG A 910 47.979 22.097 58.159 1.00 83.69 C ANISOU 1224 C ARG A 910 11234 11285 9278 751 281 -758 C ATOM 1225 O ARG A 910 47.034 22.267 57.380 1.00 84.45 O ANISOU 1225 O ARG A 910 11390 11259 9438 735 116 -769 O ATOM 1226 CB ARG A 910 48.194 24.455 58.974 1.00 83.65 C ANISOU 1226 CB ARG A 910 11236 11419 9127 633 449 -612 C ATOM 1227 CG ARG A 910 46.885 25.114 58.567 1.00 85.57 C ANISOU 1227 CG ARG A 910 11510 11513 9489 597 296 -565 C ATOM 1228 CD ARG A 910 45.939 25.301 59.743 1.00 84.80 C ANISOU 1228 CD ARG A 910 11263 11312 9645 592 323 -459 C ATOM 1229 NE ARG A 910 46.420 26.268 60.730 1.00 83.29 N ANISOU 1229 NE ARG A 910 11026 11230 9389 550 493 -375 N ATOM 1230 CZ ARG A 910 46.125 27.566 60.727 1.00 82.82 C ANISOU 1230 CZ ARG A 910 11011 11180 9277 489 497 -315 C ATOM 1231 NH1 ARG A 910 46.607 28.359 61.672 1.00 79.47 N ANISOU 1231 NH1 ARG A 910 10540 10856 8797 453 658 -245 N ATOM 1232 NH2 ARG A 910 45.353 28.080 59.780 1.00 88.07 N ANISOU 1232 NH2 ARG A 910 11771 11751 9940 467 336 -326 N ATOM 1233 N ALA A 911 48.903 21.158 57.952 1.00 77.37 N ANISOU 1233 N ALA A 911 10448 10562 8388 807 325 -847 N ATOM 1234 CA ALA A 911 48.922 20.318 56.763 1.00 78.61 C ANISOU 1234 CA ALA A 911 10703 10672 8495 847 192 -964 C ATOM 1235 C ALA A 911 48.978 18.849 57.157 1.00 78.91 C ANISOU 1235 C ALA A 911 10656 10642 8683 930 187 -1007 C ATOM 1236 O ALA A 911 49.491 18.492 58.220 1.00 78.18 O ANISOU 1236 O ALA A 911 10461 10603 8639 964 320 -970 O ATOM 1237 CB ALA A 911 50.119 20.653 55.865 1.00 78.99 C ANISOU 1237 CB ALA A 911 10885 10892 8238 832 249 -1054 C ATOM 1238 N ALA A 912 48.453 17.998 56.277 1.00 92.85 N ANISOU 1238 N ALA A 912 12475 12286 10517 965 26 -1088 N ATOM 1239 CA ALA A 912 48.460 16.564 56.527 1.00 93.52 C ANISOU 1239 CA ALA A 912 12500 12290 10745 1044 3 -1138 C ATOM 1240 C ALA A 912 49.891 16.043 56.610 1.00 93.60 C ANISOU 1240 C ALA A 912 12523 12461 10581 1100 133 -1211 C ATOM 1241 O ALA A 912 50.787 16.521 55.908 1.00 94.33 O ANISOU 1241 O ALA A 912 12712 12702 10426 1085 177 -1277 O ATOM 1242 CB ALA A 912 47.695 15.832 55.425 1.00 92.03 C ANISOU 1242 CB ALA A 912 12383 11950 10633 1065 -201 -1225 C ATOM 1243 N LYS A 913 50.102 15.057 57.477 1.00104.54 N ANISOU 1243 N LYS A 913 13811 13814 12097 1167 194 -1202 N ATOM 1244 CA LYS A 913 51.419 14.474 57.708 1.00103.93 C ANISOU 1244 CA LYS A 913 13725 13877 11886 1236 313 -1269 C ATOM 1245 C LYS A 913 51.407 13.014 57.272 1.00105.52 C ANISOU 1245 C LYS A 913 13946 13978 12171 1322 221 -1368 C ATOM 1246 O LYS A 913 50.657 12.203 57.827 1.00106.24 O ANISOU 1246 O LYS A 913 13967 13907 12493 1352 171 -1329 O ATOM 1247 CB LYS A 913 51.816 14.590 59.180 1.00100.65 C ANISOU 1247 CB LYS A 913 13187 13523 11531 1252 473 -1172 C ATOM 1248 CG LYS A 913 53.165 13.966 59.503 1.00101.84 C ANISOU 1248 CG LYS A 913 13317 13816 11561 1333 588 -1241 C ATOM 1249 CD LYS A 913 53.598 14.254 60.931 1.00102.81 C ANISOU 1249 CD LYS A 913 13331 14016 11715 1344 743 -1144 C ATOM 1250 CE LYS A 913 55.007 13.740 61.186 1.00101.74 C ANISOU 1250 CE LYS A 913 13177 14040 11441 1427 850 -1222 C ATOM 1251 NZ LYS A 913 55.487 14.034 62.563 1.00 99.48 N ANISOU 1251 NZ LYS A 913 12791 13837 11170 1442 993 -1135 N ATOM 1252 N GLY A 914 52.236 12.686 56.288 1.00104.64 N ANISOU 1252 N GLY A 914 13929 13958 11870 1358 204 -1497 N ATOM 1253 CA GLY A 914 52.424 11.318 55.856 1.00106.37 C ANISOU 1253 CA GLY A 914 14174 14106 12135 1448 133 -1606 C ATOM 1254 C GLY A 914 51.557 10.959 54.659 1.00108.75 C ANISOU 1254 C GLY A 914 14573 14264 12483 1435 -61 -1677 C ATOM 1255 O GLY A 914 50.592 11.645 54.318 1.00107.76 O ANISOU 1255 O GLY A 914 14475 14056 12413 1362 -158 -1627 O ATOM 1256 N ASN A 915 51.924 9.850 54.008 1.00104.45 N ANISOU 1256 N ASN A 915 14083 13688 11914 1511 -122 -1803 N ATOM 1257 CA ASN A 915 51.156 9.363 52.866 1.00103.26 C ANISOU 1257 CA ASN A 915 14028 13397 11807 1510 -313 -1886 C ATOM 1258 C ASN A 915 49.779 8.861 53.281 1.00102.73 C ANISOU 1258 C ASN A 915 13890 13101 12041 1496 -434 -1818 C ATOM 1259 O ASN A 915 48.834 8.917 52.485 1.00102.56 O ANISOU 1259 O ASN A 915 13926 12957 12084 1459 -599 -1844 O ATOM 1260 CB ASN A 915 51.916 8.241 52.156 1.00105.91 C ANISOU 1260 CB ASN A 915 14433 13754 12053 1601 -340 -2039 C ATOM 1261 CG ASN A 915 53.158 8.735 51.434 1.00108.16 C ANISOU 1261 CG ASN A 915 14809 14253 12032 1605 -248 -2132 C ATOM 1262 OD1 ASN A 915 53.301 9.927 51.161 1.00109.83 O ANISOU 1262 OD1 ASN A 915 15069 14575 12088 1527 -203 -2096 O ATOM 1263 ND2 ASN A 915 54.061 7.812 51.109 1.00104.79 N ANISOU 1263 ND2 ASN A 915 14411 13884 11522 1695 -217 -2257 N ATOM 1264 N CYS A 916 49.645 8.363 54.511 1.00117.19 N ANISOU 1264 N CYS A 916 15598 14871 14058 1524 -355 -1736 N ATOM 1265 CA CYS A 916 48.397 7.753 54.954 1.00118.06 C ANISOU 1265 CA CYS A 916 15635 14760 14463 1511 -452 -1680 C ATOM 1266 C CYS A 916 47.302 8.772 55.248 1.00117.06 C ANISOU 1266 C CYS A 916 15454 14569 14455 1416 -488 -1566 C ATOM 1267 O CYS A 916 46.166 8.366 55.519 1.00116.69 O ANISOU 1267 O CYS A 916 15343 14337 14658 1393 -577 -1526 O ATOM 1268 CB CYS A 916 48.649 6.903 56.201 1.00116.91 C ANISOU 1268 CB CYS A 916 15388 14571 14463 1570 -342 -1624 C ATOM 1269 SG CYS A 916 49.797 5.526 55.949 1.00115.92 S ANISOU 1269 SG CYS A 916 15314 14482 14250 1698 -319 -1758 S ATOM 1270 N VAL A 917 47.606 10.068 55.204 1.00 85.23 N ANISOU 1270 N VAL A 917 11446 10680 10257 1360 -420 -1518 N ATOM 1271 CA VAL A 917 46.644 11.117 55.519 1.00 84.61 C ANISOU 1271 CA VAL A 917 11319 10552 10278 1276 -445 -1410 C ATOM 1272 C VAL A 917 46.577 12.089 54.351 1.00 84.97 C ANISOU 1272 C VAL A 917 11488 10660 10138 1227 -538 -1453 C ATOM 1273 O VAL A 917 47.601 12.408 53.737 1.00 85.02 O ANISOU 1273 O VAL A 917 11595 10824 9885 1237 -485 -1519 O ATOM 1274 CB VAL A 917 47.019 11.863 56.819 1.00 83.13 C ANISOU 1274 CB VAL A 917 11032 10467 10085 1252 -257 -1284 C ATOM 1275 CG1 VAL A 917 45.971 12.915 57.155 1.00 82.58 C ANISOU 1275 CG1 VAL A 917 10908 10335 10132 1169 -285 -1176 C ATOM 1276 CG2 VAL A 917 47.177 10.883 57.971 1.00 82.86 C ANISOU 1276 CG2 VAL A 917 10896 10379 10209 1308 -160 -1242 C ATOM 1277 N SER A 918 45.368 12.556 54.046 1.00102.20 N ANISOU 1277 N SER A 918 13664 12714 12453 1173 -676 -1418 N ATOM 1278 CA SER A 918 45.166 13.564 53.015 1.00104.06 C ANISOU 1278 CA SER A 918 14021 12990 12529 1124 -776 -1441 C ATOM 1279 C SER A 918 43.994 14.449 53.412 1.00103.63 C ANISOU 1279 C SER A 918 13893 12840 12641 1060 -833 -1336 C ATOM 1280 O SER A 918 42.992 13.963 53.944 1.00102.57 O ANISOU 1280 O SER A 918 13644 12547 12781 1057 -892 -1297 O ATOM 1281 CB SER A 918 44.906 12.922 51.646 1.00102.78 C ANISOU 1281 CB SER A 918 13983 12747 12322 1152 -969 -1573 C ATOM 1282 OG SER A 918 43.751 12.103 51.680 1.00104.15 O ANISOU 1282 OG SER A 918 14085 12715 12774 1161 -1116 -1585 O ATOM 1283 N LEU A 919 44.128 15.746 53.150 1.00 88.38 N ANISOU 1283 N LEU A 919 12031 11005 10545 1008 -812 -1293 N ATOM 1284 CA LEU A 919 43.068 16.699 53.443 1.00 86.63 C ANISOU 1284 CA LEU A 919 11755 10703 10457 951 -870 -1200 C ATOM 1285 C LEU A 919 42.004 16.670 52.353 1.00 88.46 C ANISOU 1285 C LEU A 919 12056 10790 10763 945 -1114 -1260 C ATOM 1286 O LEU A 919 42.288 16.405 51.181 1.00 88.86 O ANISOU 1286 O LEU A 919 12252 10854 10656 966 -1224 -1364 O ATOM 1287 CB LEU A 919 43.637 18.113 53.574 1.00 86.66 C ANISOU 1287 CB LEU A 919 11815 10860 10251 900 -756 -1132 C ATOM 1288 CG LEU A 919 44.411 18.430 54.856 1.00 85.55 C ANISOU 1288 CG LEU A 919 11575 10845 10084 891 -524 -1044 C ATOM 1289 CD1 LEU A 919 45.156 19.750 54.719 1.00 84.03 C ANISOU 1289 CD1 LEU A 919 11473 10818 9638 840 -423 -1008 C ATOM 1290 CD2 LEU A 919 43.475 18.471 56.058 1.00 84.07 C ANISOU 1290 CD2 LEU A 919 11217 10547 10177 875 -489 -937 C ATOM 1291 N LEU A 920 40.767 16.944 52.755 1.00 90.09 N ANISOU 1291 N LEU A 920 12156 10858 11215 917 -1200 -1197 N ATOM 1292 CA LEU A 920 39.624 16.968 51.853 1.00 91.69 C ANISOU 1292 CA LEU A 920 12396 10911 11529 911 -1440 -1247 C ATOM 1293 C LEU A 920 39.048 18.378 51.787 1.00 91.18 C ANISOU 1293 C LEU A 920 12353 10849 11440 863 -1488 -1173 C ATOM 1294 O LEU A 920 39.521 19.303 52.452 1.00 89.80 O ANISOU 1294 O LEU A 920 12163 10787 11168 832 -1330 -1083 O ATOM 1295 CB LEU A 920 38.554 15.971 52.304 1.00 91.07 C ANISOU 1295 CB LEU A 920 12164 10646 11794 922 -1525 -1255 C ATOM 1296 CG LEU A 920 39.006 14.522 52.465 1.00 91.19 C ANISOU 1296 CG LEU A 920 12148 10629 11869 970 -1483 -1321 C ATOM 1297 CD1 LEU A 920 37.832 13.664 52.883 1.00 92.12 C ANISOU 1297 CD1 LEU A 920 12118 10548 12333 966 -1573 -1323 C ATOM 1298 CD2 LEU A 920 39.625 13.988 51.185 1.00 94.14 C ANISOU 1298 CD2 LEU A 920 12695 11041 12034 1011 -1587 -1453 C ATOM 1299 N SER A 921 37.994 18.532 50.966 1.00105.60 N ANISOU 1299 N SER A 921 14217 12545 13360 862 -1717 -1215 N ATOM 1300 CA SER A 921 37.337 19.823 50.821 1.00105.60 C ANISOU 1300 CA SER A 921 14243 12526 13354 827 -1794 -1154 C ATOM 1301 C SER A 921 36.260 19.990 51.892 1.00105.19 C ANISOU 1301 C SER A 921 13982 12363 13622 806 -1777 -1069 C ATOM 1302 O SER A 921 35.603 19.014 52.268 1.00105.64 O ANISOU 1302 O SER A 921 13902 12296 13940 819 -1817 -1093 O ATOM 1303 CB SER A 921 36.705 19.956 49.440 1.00107.22 C ANISOU 1303 CB SER A 921 14591 12644 13506 842 -2057 -1240 C ATOM 1304 OG SER A 921 35.640 19.037 49.275 1.00109.22 O ANISOU 1304 OG SER A 921 14742 12722 14034 865 -2231 -1301 O ATOM 1305 N PRO A 922 36.053 21.204 52.396 1.00 90.86 N ANISOU 1305 N PRO A 922 12140 10585 11798 772 -1715 -973 N ATOM 1306 CA PRO A 922 35.073 21.404 53.469 1.00 90.46 C ANISOU 1306 CA PRO A 922 11887 10438 12045 751 -1678 -893 C ATOM 1307 C PRO A 922 33.651 21.135 52.995 1.00 92.14 C ANISOU 1307 C PRO A 922 12026 10464 12518 761 -1915 -944 C ATOM 1308 O PRO A 922 33.354 21.053 51.801 1.00 93.22 O ANISOU 1308 O PRO A 922 12283 10547 12589 783 -2128 -1031 O ATOM 1309 CB PRO A 922 35.264 22.871 53.865 1.00 89.48 C ANISOU 1309 CB PRO A 922 11795 10407 11798 717 -1582 -795 C ATOM 1310 CG PRO A 922 35.893 23.511 52.679 1.00 90.22 C ANISOU 1310 CG PRO A 922 12118 10585 11576 718 -1664 -838 C ATOM 1311 CD PRO A 922 36.741 22.456 52.038 1.00 90.35 C ANISOU 1311 CD PRO A 922 12230 10652 11445 747 -1663 -933 C ATOM 1312 N SER A 923 32.763 20.992 53.976 1.00122.89 N ANISOU 1312 N SER A 923 15716 14259 16716 744 -1874 -892 N ATOM 1313 CA SER A 923 31.356 20.741 53.726 1.00125.03 C ANISOU 1313 CA SER A 923 15874 14352 17279 746 -2074 -936 C ATOM 1314 C SER A 923 30.706 22.000 53.161 1.00126.02 C ANISOU 1314 C SER A 923 16059 14453 17370 747 -2229 -923 C ATOM 1315 O SER A 923 31.310 23.076 53.162 1.00125.06 O ANISOU 1315 O SER A 923 16047 14446 17023 736 -2151 -862 O ATOM 1316 CB SER A 923 30.675 20.316 55.025 1.00125.02 C ANISOU 1316 CB SER A 923 15638 14267 17598 720 -1950 -877 C ATOM 1317 OG SER A 923 30.503 21.424 55.889 1.00125.22 O ANISOU 1317 OG SER A 923 15589 14337 17652 693 -1826 -770 O ATOM 1318 N PRO A 924 29.478 21.900 52.639 1.00122.82 N ANISOU 1318 N PRO A 924 15589 13895 17181 760 -2459 -983 N ATOM 1319 CA PRO A 924 28.754 23.138 52.307 1.00122.49 C ANISOU 1319 CA PRO A 924 15572 13818 17149 765 -2596 -958 C ATOM 1320 C PRO A 924 28.678 24.076 53.496 1.00121.43 C ANISOU 1320 C PRO A 924 15323 13732 17083 735 -2407 -838 C ATOM 1321 O PRO A 924 28.837 25.293 53.347 1.00119.73 O ANISOU 1321 O PRO A 924 15208 13578 16708 735 -2409 -786 O ATOM 1322 CB PRO A 924 27.372 22.633 51.864 1.00123.51 C ANISOU 1322 CB PRO A 924 15582 13765 17581 783 -2841 -1044 C ATOM 1323 CG PRO A 924 27.264 21.254 52.431 1.00123.99 C ANISOU 1323 CG PRO A 924 15492 13762 17856 767 -2760 -1077 C ATOM 1324 CD PRO A 924 28.651 20.708 52.387 1.00123.28 C ANISOU 1324 CD PRO A 924 15538 13802 17500 770 -2604 -1075 C ATOM 1325 N GLU A 925 28.440 23.526 54.681 1.00137.69 N ANISOU 1325 N GLU A 925 17182 15761 19372 709 -2241 -793 N ATOM 1326 CA GLU A 925 28.685 24.245 55.917 1.00136.51 C ANISOU 1326 CA GLU A 925 16944 15687 19236 678 -2008 -676 C ATOM 1327 C GLU A 925 30.190 24.370 56.146 1.00134.61 C ANISOU 1327 C GLU A 925 16840 15624 18681 669 -1804 -628 C ATOM 1328 O GLU A 925 30.996 23.643 55.561 1.00135.14 O ANISOU 1328 O GLU A 925 17025 15745 18577 684 -1810 -685 O ATOM 1329 CB GLU A 925 28.025 23.529 57.097 1.00137.30 C ANISOU 1329 CB GLU A 925 16804 15701 19663 652 -1886 -645 C ATOM 1330 CG GLU A 925 26.588 23.094 56.838 1.00139.70 C ANISOU 1330 CG GLU A 925 16954 15822 20301 655 -2082 -716 C ATOM 1331 CD GLU A 925 25.963 22.415 58.039 1.00139.85 C ANISOU 1331 CD GLU A 925 16741 15758 20638 618 -1938 -682 C ATOM 1332 OE1 GLU A 925 26.673 22.217 59.046 1.00138.36 O ANISOU 1332 OE1 GLU A 925 16523 15650 20397 596 -1693 -604 O ATOM 1333 OE2 GLU A 925 24.762 22.079 57.975 1.00140.25 O ANISOU 1333 OE2 GLU A 925 16639 15663 20988 611 -2069 -735 O ATOM 1334 N GLY A 926 30.568 25.303 57.018 1.00119.03 N ANISOU 1334 N GLY A 926 14846 13744 16635 644 -1621 -526 N ATOM 1335 CA GLY A 926 31.978 25.566 57.262 1.00118.81 C ANISOU 1335 CA GLY A 926 14940 13892 16312 632 -1429 -481 C ATOM 1336 C GLY A 926 32.756 24.383 57.810 1.00117.87 C ANISOU 1336 C GLY A 926 14779 13823 16185 634 -1272 -489 C ATOM 1337 O GLY A 926 33.985 24.473 57.919 1.00116.93 O ANISOU 1337 O GLY A 926 14760 13852 15816 631 -1128 -470 O ATOM 1338 N ASP A 927 32.084 23.288 58.151 1.00120.75 N ANISOU 1338 N ASP A 927 15000 14067 16814 639 -1298 -520 N ATOM 1339 CA ASP A 927 32.724 22.143 58.779 1.00119.74 C ANISOU 1339 CA ASP A 927 14822 13966 16706 645 -1148 -520 C ATOM 1340 C ASP A 927 33.942 21.685 57.969 1.00118.89 C ANISOU 1340 C ASP A 927 14892 13969 16310 673 -1152 -584 C ATOM 1341 O ASP A 927 33.803 21.384 56.774 1.00119.34 O ANISOU 1341 O ASP A 927 15054 13982 16306 695 -1343 -678 O ATOM 1342 CB ASP A 927 31.725 20.996 58.903 1.00120.57 C ANISOU 1342 CB ASP A 927 14784 13900 17128 646 -1235 -568 C ATOM 1343 CG ASP A 927 30.502 21.371 59.716 1.00122.33 C ANISOU 1343 CG ASP A 927 14817 14011 17653 615 -1221 -514 C ATOM 1344 OD1 ASP A 927 30.628 22.220 60.622 1.00121.27 O ANISOU 1344 OD1 ASP A 927 14633 13943 17500 593 -1062 -419 O ATOM 1345 OD2 ASP A 927 29.415 20.816 59.448 1.00123.71 O ANISOU 1345 OD2 ASP A 927 14888 14031 18086 611 -1368 -572 O ATOM 1346 N PRO A 928 35.129 21.616 58.569 1.00103.35 N ANISOU 1346 N PRO A 928 12959 12144 14165 674 -949 -543 N ATOM 1347 CA PRO A 928 36.292 21.074 57.857 1.00103.67 C ANISOU 1347 CA PRO A 928 13148 12289 13953 704 -941 -613 C ATOM 1348 C PRO A 928 36.250 19.554 57.783 1.00103.04 C ANISOU 1348 C PRO A 928 13025 12124 14002 737 -976 -683 C ATOM 1349 O PRO A 928 35.516 18.886 58.513 1.00103.41 O ANISOU 1349 O PRO A 928 12922 12051 14318 731 -954 -660 O ATOM 1350 CB PRO A 928 37.476 21.555 58.702 1.00101.43 C ANISOU 1350 CB PRO A 928 12881 12179 13477 693 -703 -540 C ATOM 1351 CG PRO A 928 36.928 21.625 60.080 1.00 99.92 C ANISOU 1351 CG PRO A 928 12516 11939 13511 672 -570 -444 C ATOM 1352 CD PRO A 928 35.473 22.013 59.946 1.00100.35 C ANISOU 1352 CD PRO A 928 12483 11838 13808 651 -718 -436 C ATOM 1353 N ARG A 929 37.062 19.010 56.876 1.00 99.84 N ANISOU 1353 N ARG A 929 12758 11779 13397 770 -1027 -772 N ATOM 1354 CA ARG A 929 37.110 17.570 56.670 1.00100.61 C ANISOU 1354 CA ARG A 929 12840 11800 13588 808 -1073 -851 C ATOM 1355 C ARG A 929 38.531 17.142 56.337 1.00100.27 C ANISOU 1355 C ARG A 929 12920 11903 13275 846 -983 -903 C ATOM 1356 O ARG A 929 39.314 17.910 55.772 1.00101.08 O ANISOU 1356 O ARG A 929 13154 12143 13108 841 -962 -916 O ATOM 1357 CB ARG A 929 36.169 17.123 55.543 1.00102.25 C ANISOU 1357 CB ARG A 929 13081 11859 13909 817 -1328 -950 C ATOM 1358 CG ARG A 929 34.697 17.344 55.820 1.00103.20 C ANISOU 1358 CG ARG A 929 13060 11818 14333 786 -1436 -921 C ATOM 1359 CD ARG A 929 33.859 16.374 55.010 1.00104.52 C ANISOU 1359 CD ARG A 929 13215 11823 14676 802 -1652 -1028 C ATOM 1360 NE ARG A 929 32.429 16.653 55.096 1.00105.34 N ANISOU 1360 NE ARG A 929 13188 11776 15061 773 -1783 -1019 N ATOM 1361 CZ ARG A 929 31.693 17.210 54.138 1.00106.40 C ANISOU 1361 CZ ARG A 929 13373 11849 15205 775 -2002 -1071 C ATOM 1362 NH1 ARG A 929 32.230 17.563 52.979 1.00106.80 N ANISOU 1362 NH1 ARG A 929 13619 11972 14988 801 -2118 -1133 N ATOM 1363 NH2 ARG A 929 30.398 17.408 54.343 1.00107.15 N ANISOU 1363 NH2 ARG A 929 13324 11808 15581 752 -2108 -1064 N ATOM 1364 N PHE A 930 38.853 15.900 56.695 1.00100.77 N ANISOU 1364 N PHE A 930 12939 11932 13417 883 -929 -936 N ATOM 1365 CA PHE A 930 40.108 15.281 56.295 1.00100.76 C ANISOU 1365 CA PHE A 930 13044 12045 13194 932 -871 -1008 C ATOM 1366 C PHE A 930 39.938 13.770 56.361 1.00101.74 C ANISOU 1366 C PHE A 930 13123 12048 13487 975 -911 -1069 C ATOM 1367 O PHE A 930 38.995 13.260 56.972 1.00103.25 O ANISOU 1367 O PHE A 930 13187 12088 13955 959 -932 -1034 O ATOM 1368 CB PHE A 930 41.278 15.746 57.171 1.00101.16 C ANISOU 1368 CB PHE A 930 13089 12276 13073 935 -642 -939 C ATOM 1369 CG PHE A 930 41.362 15.056 58.504 1.00 98.55 C ANISOU 1369 CG PHE A 930 12625 11914 12904 953 -491 -871 C ATOM 1370 CD1 PHE A 930 42.243 14.002 58.697 1.00 98.82 C ANISOU 1370 CD1 PHE A 930 12675 11988 12883 1013 -416 -917 C ATOM 1371 CD2 PHE A 930 40.576 15.467 59.568 1.00 96.66 C ANISOU 1371 CD2 PHE A 930 12254 11607 12867 912 -422 -762 C ATOM 1372 CE1 PHE A 930 42.332 13.367 59.921 1.00 98.57 C ANISOU 1372 CE1 PHE A 930 12538 11923 12991 1034 -282 -851 C ATOM 1373 CE2 PHE A 930 40.663 14.836 60.797 1.00 96.05 C ANISOU 1373 CE2 PHE A 930 12070 11499 12925 927 -278 -696 C ATOM 1374 CZ PHE A 930 41.540 13.784 60.972 1.00 97.16 C ANISOU 1374 CZ PHE A 930 12238 11675 13005 988 -211 -738 C ATOM 1375 N SER A 931 40.858 13.061 55.710 1.00 85.48 N ANISOU 1375 N SER A 931 11170 10054 11256 1027 -919 -1165 N ATOM 1376 CA SER A 931 40.843 11.606 55.667 1.00 86.35 C ANISOU 1376 CA SER A 931 11261 10057 11489 1076 -960 -1236 C ATOM 1377 C SER A 931 42.178 11.064 56.156 1.00 85.72 C ANISOU 1377 C SER A 931 11204 10107 11258 1134 -791 -1246 C ATOM 1378 O SER A 931 43.218 11.713 56.016 1.00 85.02 O ANISOU 1378 O SER A 931 11189 10200 10915 1142 -694 -1249 O ATOM 1379 CB SER A 931 40.568 11.093 54.249 1.00 87.85 C ANISOU 1379 CB SER A 931 11565 10174 11639 1097 -1172 -1371 C ATOM 1380 OG SER A 931 40.509 9.678 54.224 1.00 88.74 O ANISOU 1380 OG SER A 931 11659 10172 11886 1143 -1215 -1441 O ATOM 1381 N PHE A 932 42.141 9.862 56.730 1.00 86.06 N ANISOU 1381 N PHE A 932 11184 10052 11463 1174 -759 -1253 N ATOM 1382 CA PHE A 932 43.350 9.211 57.211 1.00 85.65 C ANISOU 1382 CA PHE A 932 11150 10101 11293 1242 -616 -1269 C ATOM 1383 C PHE A 932 43.184 7.703 57.102 1.00 86.78 C ANISOU 1383 C PHE A 932 11291 10098 11585 1296 -685 -1342 C ATOM 1384 O PHE A 932 42.076 7.174 57.225 1.00 87.51 O ANISOU 1384 O PHE A 932 11316 10002 11932 1267 -777 -1331 O ATOM 1385 CB PHE A 932 43.669 9.606 58.661 1.00 84.31 C ANISOU 1385 CB PHE A 932 10879 10000 11155 1233 -416 -1139 C ATOM 1386 CG PHE A 932 42.774 8.961 59.678 1.00 84.44 C ANISOU 1386 CG PHE A 932 10773 9844 11466 1217 -388 -1060 C ATOM 1387 CD1 PHE A 932 43.183 7.823 60.353 1.00 84.64 C ANISOU 1387 CD1 PHE A 932 10776 9821 11564 1276 -312 -1059 C ATOM 1388 CD2 PHE A 932 41.526 9.490 59.963 1.00 84.44 C ANISOU 1388 CD2 PHE A 932 10685 9730 11670 1143 -436 -990 C ATOM 1389 CE1 PHE A 932 42.366 7.224 61.291 1.00 84.86 C ANISOU 1389 CE1 PHE A 932 10704 9685 11855 1255 -277 -984 C ATOM 1390 CE2 PHE A 932 40.704 8.894 60.901 1.00 84.66 C ANISOU 1390 CE2 PHE A 932 10600 9599 11969 1121 -397 -921 C ATOM 1391 CZ PHE A 932 41.124 7.761 61.565 1.00 84.87 C ANISOU 1391 CZ PHE A 932 10614 9576 12059 1174 -314 -915 C ATOM 1392 N LEU A 933 44.302 7.018 56.868 1.00 98.27 N ANISOU 1392 N LEU A 933 12818 11640 12881 1374 -638 -1420 N ATOM 1393 CA LEU A 933 44.343 5.564 56.783 1.00100.27 C ANISOU 1393 CA LEU A 933 13084 11770 13244 1438 -687 -1495 C ATOM 1394 C LEU A 933 45.216 5.033 57.911 1.00 98.38 C ANISOU 1394 C LEU A 933 12800 11587 12992 1501 -513 -1443 C ATOM 1395 O LEU A 933 46.344 5.498 58.097 1.00 98.37 O ANISOU 1395 O LEU A 933 12826 11777 12774 1536 -392 -1441 O ATOM 1396 CB LEU A 933 44.886 5.105 55.426 1.00102.21 C ANISOU 1396 CB LEU A 933 13464 12054 13317 1489 -804 -1652 C ATOM 1397 CG LEU A 933 44.933 3.593 55.188 1.00103.22 C ANISOU 1397 CG LEU A 933 13621 12049 13548 1559 -874 -1747 C ATOM 1398 CD1 LEU A 933 43.531 2.999 55.160 1.00102.82 C ANISOU 1398 CD1 LEU A 933 13514 11759 13794 1513 -1014 -1741 C ATOM 1399 CD2 LEU A 933 45.674 3.281 53.897 1.00103.59 C ANISOU 1399 CD2 LEU A 933 13808 12175 13378 1615 -957 -1902 C ATOM 1400 N LEU A 934 44.695 4.061 58.655 1.00 87.85 N ANISOU 1400 N LEU A 934 11402 10087 11889 1515 -502 -1404 N ATOM 1401 CA LEU A 934 45.351 3.547 59.851 1.00 87.32 C ANISOU 1401 CA LEU A 934 11292 10044 11841 1571 -344 -1336 C ATOM 1402 C LEU A 934 45.830 2.126 59.590 1.00 88.45 C ANISOU 1402 C LEU A 934 11495 10110 12002 1665 -386 -1434 C ATOM 1403 O LEU A 934 45.018 1.233 59.323 1.00 89.59 O ANISOU 1403 O LEU A 934 11641 10059 12342 1655 -498 -1472 O ATOM 1404 CB LEU A 934 44.397 3.584 61.045 1.00 86.95 C ANISOU 1404 CB LEU A 934 11132 9865 12041 1511 -276 -1198 C ATOM 1405 CG LEU A 934 44.986 3.249 62.416 1.00 86.30 C ANISOU 1405 CG LEU A 934 11007 9809 11974 1558 -101 -1103 C ATOM 1406 CD1 LEU A 934 46.030 4.275 62.832 1.00 84.94 C ANISOU 1406 CD1 LEU A 934 10834 9872 11567 1575 35 -1059 C ATOM 1407 CD2 LEU A 934 43.874 3.170 63.448 1.00 86.26 C ANISOU 1407 CD2 LEU A 934 10901 9640 12233 1489 -53 -980 C ATOM 1408 N HIS A 935 47.141 1.919 59.677 1.00 97.81 N ANISOU 1408 N HIS A 935 12727 11446 12989 1755 -297 -1479 N ATOM 1409 CA HIS A 935 47.757 0.619 59.442 1.00100.22 C ANISOU 1409 CA HIS A 935 13093 11700 13284 1859 -327 -1579 C ATOM 1410 C HIS A 935 48.354 0.089 60.737 1.00100.31 C ANISOU 1410 C HIS A 935 13064 11716 13331 1928 -184 -1500 C ATOM 1411 O HIS A 935 49.050 0.819 61.450 1.00101.26 O ANISOU 1411 O HIS A 935 13149 12000 13327 1938 -48 -1431 O ATOM 1412 CB HIS A 935 48.847 0.711 58.371 1.00103.26 C ANISOU 1412 CB HIS A 935 13573 12257 13406 1922 -354 -1719 C ATOM 1413 CG HIS A 935 49.716 -0.506 58.295 1.00105.05 C ANISOU 1413 CG HIS A 935 13853 12472 13590 2045 -349 -1816 C ATOM 1414 ND1 HIS A 935 49.207 -1.775 58.121 1.00105.91 N ANISOU 1414 ND1 HIS A 935 13991 12375 13875 2082 -450 -1868 N ATOM 1415 CD2 HIS A 935 51.060 -0.649 58.378 1.00104.94 C ANISOU 1415 CD2 HIS A 935 13864 12626 13383 2143 -257 -1875 C ATOM 1416 CE1 HIS A 935 50.199 -2.647 58.097 1.00104.88 C ANISOU 1416 CE1 HIS A 935 13909 12282 13659 2201 -422 -1952 C ATOM 1417 NE2 HIS A 935 51.334 -1.989 58.251 1.00105.63 N ANISOU 1417 NE2 HIS A 935 13998 12605 13532 2242 -307 -1960 N ATOM 1418 N PHE A 936 48.084 -1.181 61.031 1.00 98.14 N ANISOU 1418 N PHE A 936 12804 11261 13225 1976 -219 -1512 N ATOM 1419 CA PHE A 936 48.665 -1.873 62.174 1.00 99.20 C ANISOU 1419 CA PHE A 936 12925 11375 13392 2057 -104 -1451 C ATOM 1420 C PHE A 936 49.439 -3.083 61.677 1.00 99.46 C ANISOU 1420 C PHE A 936 13042 11380 13369 2181 -158 -1580 C ATOM 1421 O PHE A 936 48.911 -3.887 60.901 1.00 99.56 O ANISOU 1421 O PHE A 936 13104 11239 13485 2182 -290 -1668 O ATOM 1422 CB PHE A 936 47.591 -2.316 63.171 1.00 96.97 C ANISOU 1422 CB PHE A 936 12585 10880 13380 2000 -77 -1326 C ATOM 1423 CG PHE A 936 47.036 -1.200 64.003 1.00 95.87 C ANISOU 1423 CG PHE A 936 12355 10782 13288 1904 21 -1183 C ATOM 1424 CD1 PHE A 936 47.781 -0.653 65.035 1.00 96.03 C ANISOU 1424 CD1 PHE A 936 12343 10947 13196 1934 176 -1092 C ATOM 1425 CD2 PHE A 936 45.765 -0.706 63.764 1.00 96.47 C ANISOU 1425 CD2 PHE A 936 12375 10752 13526 1785 -45 -1145 C ATOM 1426 CE1 PHE A 936 47.270 0.374 65.809 1.00 94.35 C ANISOU 1426 CE1 PHE A 936 12051 10770 13027 1847 268 -963 C ATOM 1427 CE2 PHE A 936 45.249 0.319 64.535 1.00 96.34 C ANISOU 1427 CE2 PHE A 936 12273 10772 13559 1701 46 -1018 C ATOM 1428 CZ PHE A 936 46.002 0.860 65.559 1.00 94.32 C ANISOU 1428 CZ PHE A 936 11993 10659 13185 1730 206 -926 C ATOM 1429 N TYR A 937 50.688 -3.208 62.124 1.00 90.68 N ANISOU 1429 N TYR A 937 11944 10415 12096 2287 -60 -1596 N ATOM 1430 CA TYR A 937 51.504 -4.349 61.732 1.00 91.83 C ANISOU 1430 CA TYR A 937 12164 10543 12185 2418 -102 -1720 C ATOM 1431 C TYR A 937 51.177 -5.601 62.533 1.00 92.74 C ANISOU 1431 C TYR A 937 12297 10441 12498 2471 -103 -1670 C ATOM 1432 O TYR A 937 51.292 -6.712 62.004 1.00 94.07 O ANISOU 1432 O TYR A 937 12536 10496 12710 2545 -191 -1774 O ATOM 1433 CB TYR A 937 52.988 -4.019 61.894 1.00 91.29 C ANISOU 1433 CB TYR A 937 12095 10716 11874 2518 -1 -1766 C ATOM 1434 CG TYR A 937 53.590 -3.270 60.726 1.00 91.11 C ANISOU 1434 CG TYR A 937 12099 10890 11629 2506 -27 -1886 C ATOM 1435 CD1 TYR A 937 54.027 -3.947 59.593 1.00 92.31 C ANISOU 1435 CD1 TYR A 937 12330 11045 11698 2575 -120 -2052 C ATOM 1436 CD2 TYR A 937 53.731 -1.888 60.757 1.00 89.83 C ANISOU 1436 CD2 TYR A 937 11889 10906 11334 2425 47 -1833 C ATOM 1437 CE1 TYR A 937 54.582 -3.269 58.521 1.00 92.25 C ANISOU 1437 CE1 TYR A 937 12358 11215 11479 2560 -135 -2161 C ATOM 1438 CE2 TYR A 937 54.285 -1.201 59.691 1.00 89.76 C ANISOU 1438 CE2 TYR A 937 11916 11072 11117 2408 30 -1939 C ATOM 1439 CZ TYR A 937 54.708 -1.897 58.575 1.00 90.99 C ANISOU 1439 CZ TYR A 937 12154 11228 11190 2474 -58 -2102 C ATOM 1440 OH TYR A 937 55.261 -1.223 57.509 1.00 91.03 O ANISOU 1440 OH TYR A 937 12204 11403 10980 2453 -66 -2207 O ATOM 1441 N THR A 938 50.764 -5.455 63.790 1.00 92.12 N ANISOU 1441 N THR A 938 12165 10298 12540 2434 -4 -1515 N ATOM 1442 CA THR A 938 50.738 -6.574 64.720 1.00 92.90 C ANISOU 1442 CA THR A 938 12293 10228 12778 2502 29 -1457 C ATOM 1443 C THR A 938 49.431 -6.614 65.501 1.00 92.90 C ANISOU 1443 C THR A 938 12247 10026 13023 2388 54 -1316 C ATOM 1444 O THR A 938 48.633 -5.673 65.493 1.00 92.10 O ANISOU 1444 O THR A 938 12076 9941 12977 2265 64 -1251 O ATOM 1445 CB THR A 938 51.924 -6.507 65.690 1.00 92.32 C ANISOU 1445 CB THR A 938 12215 10302 12560 2613 155 -1412 C ATOM 1446 OG1 THR A 938 51.924 -5.243 66.364 1.00 90.79 O ANISOU 1446 OG1 THR A 938 11943 10257 12298 2540 267 -1300 O ATOM 1447 CG2 THR A 938 53.230 -6.681 64.931 1.00 92.65 C ANISOU 1447 CG2 THR A 938 12298 10520 12384 2737 129 -1567 C ATOM 1448 N VAL A 939 49.234 -7.743 66.176 1.00105.90 N ANISOU 1448 N VAL A 939 13938 11479 14819 2434 65 -1274 N ATOM 1449 CA VAL A 939 48.043 -8.025 66.966 1.00106.23 C ANISOU 1449 CA VAL A 939 13951 11303 15109 2335 98 -1147 C ATOM 1450 C VAL A 939 48.516 -8.361 68.383 1.00106.09 C ANISOU 1450 C VAL A 939 13954 11265 15089 2403 233 -1025 C ATOM 1451 O VAL A 939 49.570 -8.969 68.545 1.00106.49 O ANISOU 1451 O VAL A 939 14071 11368 15021 2543 244 -1072 O ATOM 1452 CB VAL A 939 47.236 -9.179 66.326 1.00107.90 C ANISOU 1452 CB VAL A 939 14212 11264 15520 2312 -31 -1222 C ATOM 1453 CG1 VAL A 939 46.038 -9.582 67.169 1.00108.45 C ANISOU 1453 CG1 VAL A 939 14253 11097 15856 2209 12 -1097 C ATOM 1454 CG2 VAL A 939 46.778 -8.788 64.932 1.00108.05 C ANISOU 1454 CG2 VAL A 939 14215 11312 15528 2248 -172 -1343 C ATOM 1455 N PRO A 940 47.757 -7.966 69.424 1.00 98.59 N ANISOU 1455 N PRO A 940 12951 10243 14267 2309 337 -870 N ATOM 1456 CA PRO A 940 46.445 -7.308 69.480 1.00 98.23 C ANISOU 1456 CA PRO A 940 12817 10114 14392 2146 345 -795 C ATOM 1457 C PRO A 940 46.438 -5.857 69.020 1.00 96.80 C ANISOU 1457 C PRO A 940 12552 10139 14087 2077 349 -803 C ATOM 1458 O PRO A 940 47.380 -5.106 69.264 1.00 95.68 O ANISOU 1458 O PRO A 940 12400 10215 13739 2131 421 -792 O ATOM 1459 CB PRO A 940 46.075 -7.402 70.961 1.00 98.13 C ANISOU 1459 CB PRO A 940 12794 10002 14490 2113 491 -626 C ATOM 1460 CG PRO A 940 47.359 -7.440 71.669 1.00 97.66 C ANISOU 1460 CG PRO A 940 12787 10086 14234 2248 576 -600 C ATOM 1461 CD PRO A 940 48.300 -8.194 70.775 1.00 98.42 C ANISOU 1461 CD PRO A 940 12961 10225 14209 2380 468 -753 C ATOM 1462 N ILE A 941 45.350 -5.482 68.355 1.00112.11 N ANISOU 1462 N ILE A 941 14433 12002 16161 1958 267 -824 N ATOM 1463 CA ILE A 941 45.122 -4.108 67.922 1.00110.29 C ANISOU 1463 CA ILE A 941 14126 11929 15848 1879 261 -821 C ATOM 1464 C ILE A 941 44.645 -3.331 69.142 1.00109.82 C ANISOU 1464 C ILE A 941 13989 11881 15857 1802 408 -659 C ATOM 1465 O ILE A 941 43.914 -3.890 69.974 1.00111.43 O ANISOU 1465 O ILE A 941 14177 11901 16258 1757 466 -568 O ATOM 1466 CB ILE A 941 44.089 -4.039 66.785 1.00110.11 C ANISOU 1466 CB ILE A 941 14076 11806 15956 1787 108 -903 C ATOM 1467 CG1 ILE A 941 44.397 -5.080 65.699 1.00112.71 C ANISOU 1467 CG1 ILE A 941 14494 12065 16266 1860 -37 -1058 C ATOM 1468 CG2 ILE A 941 44.064 -2.641 66.186 1.00108.79 C ANISOU 1468 CG2 ILE A 941 13857 11820 15657 1730 84 -919 C ATOM 1469 CD1 ILE A 941 43.294 -5.241 64.669 1.00114.40 C ANISOU 1469 CD1 ILE A 941 14688 12138 16641 1774 -198 -1139 C ATOM 1470 N PRO A 942 45.022 -2.065 69.307 1.00 91.48 N ANISOU 1470 N PRO A 942 11618 9761 13379 1781 476 -620 N ATOM 1471 CA PRO A 942 44.460 -1.280 70.411 1.00 90.63 C ANISOU 1471 CA PRO A 942 11432 9655 13347 1700 608 -472 C ATOM 1472 C PRO A 942 42.941 -1.322 70.379 1.00 91.27 C ANISOU 1472 C PRO A 942 11441 9539 13699 1572 569 -434 C ATOM 1473 O PRO A 942 42.317 -1.092 69.343 1.00 91.59 O ANISOU 1473 O PRO A 942 11452 9549 13799 1515 440 -514 O ATOM 1474 CB PRO A 942 45.001 0.128 70.150 1.00 89.17 C ANISOU 1474 CB PRO A 942 11210 9714 12955 1686 636 -477 C ATOM 1475 CG PRO A 942 46.275 -0.095 69.416 1.00 89.17 C ANISOU 1475 CG PRO A 942 11285 9866 12728 1798 585 -596 C ATOM 1476 CD PRO A 942 46.054 -1.316 68.568 1.00 90.64 C ANISOU 1476 CD PRO A 942 11532 9894 13011 1835 449 -705 C ATOM 1477 N LYS A 943 42.341 -1.634 71.529 1.00107.45 N ANISOU 1477 N LYS A 943 13462 11452 15914 1528 683 -313 N ATOM 1478 CA LYS A 943 40.887 -1.744 71.598 1.00108.50 C ANISOU 1478 CA LYS A 943 13515 11388 16323 1403 663 -277 C ATOM 1479 C LYS A 943 40.227 -0.401 71.323 1.00106.97 C ANISOU 1479 C LYS A 943 13216 11283 16145 1307 650 -259 C ATOM 1480 O LYS A 943 39.332 -0.294 70.476 1.00105.67 O ANISOU 1480 O LYS A 943 12998 11036 16115 1236 526 -324 O ATOM 1481 CB LYS A 943 40.464 -2.269 72.969 1.00108.19 C ANISOU 1481 CB LYS A 943 13471 11202 16434 1373 814 -143 C ATOM 1482 CG LYS A 943 40.928 -3.678 73.275 1.00109.71 C ANISOU 1482 CG LYS A 943 13773 11262 16649 1458 820 -152 C ATOM 1483 CD LYS A 943 40.548 -4.075 74.692 1.00110.29 C ANISOU 1483 CD LYS A 943 13856 11203 16846 1425 983 -7 C ATOM 1484 CE LYS A 943 40.795 -5.550 74.941 1.00111.46 C ANISOU 1484 CE LYS A 943 14119 11175 17057 1493 976 -14 C ATOM 1485 NZ LYS A 943 40.545 -5.935 76.360 1.00111.75 N ANISOU 1485 NZ LYS A 943 14189 11091 17182 1470 1144 134 N ATOM 1486 N THR A 944 40.660 0.637 72.031 1.00 95.35 N ANISOU 1486 N THR A 944 11717 9977 14537 1308 773 -174 N ATOM 1487 CA THR A 944 40.041 1.949 71.966 1.00 93.96 C ANISOU 1487 CA THR A 944 11443 9878 14377 1219 784 -139 C ATOM 1488 C THR A 944 41.110 3.004 71.729 1.00 92.23 C ANISOU 1488 C THR A 944 11251 9915 13876 1271 804 -157 C ATOM 1489 O THR A 944 42.271 2.837 72.112 1.00 91.66 O ANISOU 1489 O THR A 944 11248 9962 13616 1364 872 -150 O ATOM 1490 CB THR A 944 39.272 2.257 73.261 1.00 93.64 C ANISOU 1490 CB THR A 944 11325 9758 14495 1141 942 2 C ATOM 1491 OG1 THR A 944 38.382 1.173 73.556 1.00 96.39 O ANISOU 1491 OG1 THR A 944 11658 9866 15098 1094 943 20 O ATOM 1492 CG2 THR A 944 38.461 3.536 73.137 1.00 94.19 C ANISOU 1492 CG2 THR A 944 11286 9878 14624 1046 938 29 C ATOM 1493 N GLY A 945 40.703 4.091 71.083 1.00 84.01 N ANISOU 1493 N GLY A 945 10157 8954 12810 1210 741 -182 N ATOM 1494 CA GLY A 945 41.579 5.227 70.880 1.00 82.70 C ANISOU 1494 CA GLY A 945 10009 9020 12392 1236 769 -190 C ATOM 1495 C GLY A 945 40.761 6.497 70.875 1.00 82.04 C ANISOU 1495 C GLY A 945 9840 8967 12366 1141 773 -143 C ATOM 1496 O GLY A 945 39.532 6.466 70.750 1.00 82.72 O ANISOU 1496 O GLY A 945 9852 8901 12678 1062 718 -134 O ATOM 1497 N THR A 946 41.455 7.620 71.025 1.00 90.28 N ANISOU 1497 N THR A 946 10889 10207 13205 1149 840 -115 N ATOM 1498 CA THR A 946 40.806 8.921 71.063 1.00 89.96 C ANISOU 1498 CA THR A 946 10778 10213 13191 1067 853 -68 C ATOM 1499 C THR A 946 41.396 9.821 69.989 1.00 91.28 C ANISOU 1499 C THR A 946 10995 10546 13140 1076 765 -146 C ATOM 1500 O THR A 946 42.620 9.939 69.879 1.00 90.42 O ANISOU 1500 O THR A 946 10956 10602 12797 1140 804 -178 O ATOM 1501 CB THR A 946 40.947 9.581 72.440 1.00 87.99 C ANISOU 1501 CB THR A 946 10484 10030 12919 1050 1040 60 C ATOM 1502 OG1 THR A 946 42.334 9.744 72.758 1.00 88.48 O ANISOU 1502 OG1 THR A 946 10613 10275 12729 1126 1123 61 O ATOM 1503 CG2 THR A 946 40.274 8.740 73.510 1.00 90.15 C ANISOU 1503 CG2 THR A 946 10713 10128 13410 1030 1135 143 C ATOM 1504 N LEU A 947 40.522 10.449 69.201 1.00 83.24 N ANISOU 1504 N LEU A 947 9944 9484 12200 1013 648 -178 N ATOM 1505 CA LEU A 947 40.941 11.382 68.161 1.00 82.80 C ANISOU 1505 CA LEU A 947 9945 9568 11947 1010 560 -244 C ATOM 1506 C LEU A 947 40.976 12.796 68.723 1.00 81.61 C ANISOU 1506 C LEU A 947 9757 9539 11713 964 661 -160 C ATOM 1507 O LEU A 947 39.956 13.311 69.194 1.00 81.59 O ANISOU 1507 O LEU A 947 9666 9450 11884 899 681 -92 O ATOM 1508 CB LEU A 947 40.006 11.322 66.953 1.00 83.80 C ANISOU 1508 CB LEU A 947 10072 9581 12186 973 363 -327 C ATOM 1509 CG LEU A 947 40.301 10.304 65.848 1.00 84.84 C ANISOU 1509 CG LEU A 947 10288 9668 12278 1025 220 -453 C ATOM 1510 CD1 LEU A 947 39.346 10.514 64.687 1.00 85.73 C ANISOU 1510 CD1 LEU A 947 10402 9687 12484 982 23 -528 C ATOM 1511 CD2 LEU A 947 41.736 10.397 65.364 1.00 84.33 C ANISOU 1511 CD2 LEU A 947 10333 9793 11915 1093 244 -515 C ATOM 1512 N SER A 948 42.144 13.424 68.653 1.00 79.71 N ANISOU 1512 N SER A 948 9581 9494 11211 995 723 -170 N ATOM 1513 CA SER A 948 42.348 14.785 69.128 1.00 78.29 C ANISOU 1513 CA SER A 948 9381 9445 10919 955 820 -100 C ATOM 1514 C SER A 948 42.621 15.682 67.930 1.00 77.69 C ANISOU 1514 C SER A 948 9379 9475 10664 935 717 -170 C ATOM 1515 O SER A 948 43.532 15.410 67.142 1.00 79.93 O ANISOU 1515 O SER A 948 9752 9854 10762 979 673 -258 O ATOM 1516 CB SER A 948 43.507 14.847 70.122 1.00 77.01 C ANISOU 1516 CB SER A 948 9234 9430 10599 1000 990 -51 C ATOM 1517 OG SER A 948 43.814 16.188 70.454 1.00 77.33 O ANISOU 1517 OG SER A 948 9267 9610 10506 961 1073 1 O ATOM 1518 N CYS A 949 41.825 16.739 67.790 1.00 76.33 N ANISOU 1518 N CYS A 949 9174 9281 10549 870 679 -133 N ATOM 1519 CA CYS A 949 42.001 17.712 66.722 1.00 76.23 C ANISOU 1519 CA CYS A 949 9240 9357 10368 844 586 -184 C ATOM 1520 C CYS A 949 41.837 19.112 67.286 1.00 75.30 C ANISOU 1520 C CYS A 949 9090 9312 10210 789 672 -99 C ATOM 1521 O CYS A 949 40.846 19.401 67.963 1.00 75.28 O ANISOU 1521 O CYS A 949 8991 9206 10405 751 697 -26 O ATOM 1522 CB CYS A 949 40.997 17.483 65.590 1.00 77.37 C ANISOU 1522 CB CYS A 949 9399 9361 10638 826 383 -254 C ATOM 1523 SG CYS A 949 41.443 16.162 64.440 1.00 78.49 S ANISOU 1523 SG CYS A 949 9633 9467 10723 888 247 -389 S ATOM 1524 N THR A 950 42.806 19.974 67.001 1.00 74.00 N ANISOU 1524 N THR A 950 9004 9321 9791 784 719 -112 N ATOM 1525 CA THR A 950 42.781 21.363 67.439 1.00 73.13 C ANISOU 1525 CA THR A 950 8884 9293 9611 732 797 -40 C ATOM 1526 C THR A 950 42.305 22.233 66.283 1.00 73.54 C ANISOU 1526 C THR A 950 9007 9329 9607 692 651 -79 C ATOM 1527 O THR A 950 42.952 22.283 65.231 1.00 73.84 O ANISOU 1527 O THR A 950 9158 9445 9453 702 579 -158 O ATOM 1528 CB THR A 950 44.165 21.803 67.913 1.00 72.18 C ANISOU 1528 CB THR A 950 8805 9371 9247 744 948 -28 C ATOM 1529 OG1 THR A 950 44.603 20.937 68.967 1.00 71.92 O ANISOU 1529 OG1 THR A 950 8715 9347 9267 792 1068 5 O ATOM 1530 CG2 THR A 950 44.135 23.244 68.413 1.00 71.31 C ANISOU 1530 CG2 THR A 950 8685 9340 9070 686 1034 47 C ATOM 1531 N VAL A 951 41.182 22.921 66.483 1.00 73.63 N ANISOU 1531 N VAL A 951 8956 9239 9781 649 609 -24 N ATOM 1532 CA VAL A 951 40.573 23.751 65.450 1.00 74.14 C ANISOU 1532 CA VAL A 951 9084 9266 9822 617 456 -54 C ATOM 1533 C VAL A 951 40.937 25.203 65.709 1.00 73.28 C ANISOU 1533 C VAL A 951 9014 9272 9556 574 540 4 C ATOM 1534 O VAL A 951 41.031 25.637 66.863 1.00 72.43 O ANISOU 1534 O VAL A 951 8833 9206 9481 557 693 85 O ATOM 1535 CB VAL A 951 39.042 23.573 65.414 1.00 75.00 C ANISOU 1535 CB VAL A 951 9093 9178 10224 603 333 -44 C ATOM 1536 CG1 VAL A 951 38.673 22.099 65.369 1.00 75.83 C ANISOU 1536 CG1 VAL A 951 9143 9161 10506 638 276 -90 C ATOM 1537 CG2 VAL A 951 38.379 24.251 66.610 1.00 74.42 C ANISOU 1537 CG2 VAL A 951 8900 9068 10308 570 447 59 C ATOM 1538 N ALA A 952 41.142 25.958 64.633 1.00 73.55 N ANISOU 1538 N ALA A 952 9174 9356 9417 553 442 -39 N ATOM 1539 CA ALA A 952 41.354 27.395 64.706 1.00 72.95 C ANISOU 1539 CA ALA A 952 9152 9366 9199 506 494 10 C ATOM 1540 C ALA A 952 40.147 28.107 64.111 1.00 73.66 C ANISOU 1540 C ALA A 952 9252 9329 9407 484 332 18 C ATOM 1541 O ALA A 952 39.641 27.713 63.056 1.00 74.71 O ANISOU 1541 O ALA A 952 9438 9372 9576 502 151 -50 O ATOM 1542 CB ALA A 952 42.627 27.808 63.965 1.00 72.75 C ANISOU 1542 CB ALA A 952 9277 9507 8859 493 524 -40 C ATOM 1543 N LEU A 953 39.683 29.149 64.797 1.00 73.16 N ANISOU 1543 N LEU A 953 9139 9254 9405 451 392 96 N ATOM 1544 CA LEU A 953 38.499 29.903 64.391 1.00 73.83 C ANISOU 1544 CA LEU A 953 9215 9216 9620 438 249 110 C ATOM 1545 C LEU A 953 38.901 31.353 64.166 1.00 73.42 C ANISOU 1545 C LEU A 953 9278 9253 9365 397 275 144 C ATOM 1546 O LEU A 953 39.280 32.049 65.113 1.00 72.46 O ANISOU 1546 O LEU A 953 9121 9211 9199 370 437 213 O ATOM 1547 CB LEU A 953 37.398 29.805 65.448 1.00 73.80 C ANISOU 1547 CB LEU A 953 9032 9092 9917 438 290 170 C ATOM 1548 CG LEU A 953 36.956 28.395 65.840 1.00 74.22 C ANISOU 1548 CG LEU A 953 8963 9048 10190 468 290 149 C ATOM 1549 CD1 LEU A 953 35.952 28.456 66.961 1.00 74.17 C ANISOU 1549 CD1 LEU A 953 8787 8938 10455 456 363 216 C ATOM 1550 CD2 LEU A 953 36.361 27.667 64.655 1.00 75.51 C ANISOU 1550 CD2 LEU A 953 9160 9099 10433 493 73 59 C ATOM 1551 N ARG A 954 38.808 31.811 62.917 1.00 82.19 N ANISOU 1551 N ARG A 954 10531 10345 10351 392 115 96 N ATOM 1552 CA ARG A 954 39.081 33.200 62.597 1.00 81.55 C ANISOU 1552 CA ARG A 954 10577 10325 10085 351 119 128 C ATOM 1553 C ARG A 954 37.872 33.822 61.907 1.00 81.64 C ANISOU 1553 C ARG A 954 10617 10191 10211 361 -83 125 C ATOM 1554 O ARG A 954 37.232 33.163 61.080 1.00 84.67 O ANISOU 1554 O ARG A 954 11011 10469 10690 395 -265 62 O ATOM 1555 CB ARG A 954 40.310 33.333 61.683 1.00 79.79 C ANISOU 1555 CB ARG A 954 10538 10238 9542 330 133 77 C ATOM 1556 CG ARG A 954 40.667 34.770 61.335 1.00 80.00 C ANISOU 1556 CG ARG A 954 10709 10327 9359 278 150 111 C ATOM 1557 CD ARG A 954 41.976 34.861 60.564 1.00 82.57 C ANISOU 1557 CD ARG A 954 11203 10800 9369 246 202 60 C ATOM 1558 NE ARG A 954 41.913 34.191 59.266 1.00 82.02 N ANISOU 1558 NE ARG A 954 11244 10687 9231 273 35 -27 N ATOM 1559 CZ ARG A 954 41.285 34.674 58.198 1.00 82.64 C ANISOU 1559 CZ ARG A 954 11455 10673 9272 274 -153 -48 C ATOM 1560 NH1 ARG A 954 40.645 35.834 58.262 1.00 81.69 N ANISOU 1560 NH1 ARG A 954 11370 10489 9180 253 -203 13 N ATOM 1561 NH2 ARG A 954 41.289 33.989 57.063 1.00 85.37 N ANISOU 1561 NH2 ARG A 954 11902 10986 9548 302 -296 -131 N ATOM 1562 N PRO A 955 37.531 35.074 62.213 1.00 78.02 N ANISOU 1562 N PRO A 955 10175 9720 9750 335 -65 187 N ATOM 1563 CA PRO A 955 36.422 35.716 61.497 1.00 79.71 C ANISOU 1563 CA PRO A 955 10429 9797 10058 352 -271 179 C ATOM 1564 C PRO A 955 36.779 35.974 60.043 1.00 79.41 C ANISOU 1564 C PRO A 955 10611 9774 9788 349 -424 123 C ATOM 1565 O PRO A 955 37.880 36.434 59.728 1.00 79.92 O ANISOU 1565 O PRO A 955 10825 9968 9574 310 -336 125 O ATOM 1566 CB PRO A 955 36.209 37.032 62.259 1.00 80.43 C ANISOU 1566 CB PRO A 955 10501 9897 10162 324 -180 262 C ATOM 1567 CG PRO A 955 36.927 36.884 63.542 1.00 77.11 C ANISOU 1567 CG PRO A 955 9978 9587 9734 298 65 313 C ATOM 1568 CD PRO A 955 38.037 35.914 63.312 1.00 77.64 C ANISOU 1568 CD PRO A 955 10090 9768 9643 296 137 266 C ATOM 1569 N LYS A 956 35.830 35.676 59.151 1.00 78.18 N ANISOU 1569 N LYS A 956 10475 9483 9748 390 -655 69 N ATOM 1570 CA LYS A 956 36.026 36.002 57.742 1.00 79.22 C ANISOU 1570 CA LYS A 956 10827 9608 9665 392 -821 19 C ATOM 1571 C LYS A 956 36.307 37.485 57.556 1.00 79.13 C ANISOU 1571 C LYS A 956 10971 9636 9457 353 -799 75 C ATOM 1572 O LYS A 956 37.033 37.870 56.632 1.00 79.51 O ANISOU 1572 O LYS A 956 11231 9750 9231 327 -828 52 O ATOM 1573 CB LYS A 956 34.799 35.592 56.930 1.00 80.73 C ANISOU 1573 CB LYS A 956 11001 9631 10042 447 -1086 -41 C ATOM 1574 CG LYS A 956 34.741 34.110 56.597 1.00 81.20 C ANISOU 1574 CG LYS A 956 10996 9659 10198 479 -1151 -122 C ATOM 1575 CD LYS A 956 33.370 33.713 56.064 1.00 82.64 C ANISOU 1575 CD LYS A 956 11105 9663 10630 530 -1398 -176 C ATOM 1576 CE LYS A 956 33.209 32.201 55.987 1.00 83.02 C ANISOU 1576 CE LYS A 956 11048 9665 10829 556 -1438 -249 C ATOM 1577 NZ LYS A 956 34.156 31.568 55.032 1.00 83.31 N ANISOU 1577 NZ LYS A 956 11254 9781 10620 558 -1464 -320 N ATOM 1578 N THR A 957 35.748 38.325 58.423 1.00 96.29 N ANISOU 1578 N THR A 957 13049 11770 11768 347 -744 146 N ATOM 1579 CA THR A 957 35.968 39.762 58.375 1.00 96.75 C ANISOU 1579 CA THR A 957 13242 11856 11662 310 -714 205 C ATOM 1580 C THR A 957 37.142 40.214 59.237 1.00 97.74 C ANISOU 1580 C THR A 957 13373 12143 11620 246 -451 259 C ATOM 1581 O THR A 957 37.553 41.375 59.138 1.00 99.66 O ANISOU 1581 O THR A 957 13753 12430 11683 202 -404 302 O ATOM 1582 CB THR A 957 34.691 40.486 58.819 1.00 98.55 C ANISOU 1582 CB THR A 957 13366 11946 12132 344 -806 247 C ATOM 1583 OG1 THR A 957 33.579 39.997 58.060 1.00101.06 O ANISOU 1583 OG1 THR A 957 13655 12115 12628 406 -1055 188 O ATOM 1584 CG2 THR A 957 34.803 41.992 58.629 1.00 99.71 C ANISOU 1584 CG2 THR A 957 13674 12096 12116 315 -812 303 C ATOM 1585 N GLY A 958 37.705 39.327 60.057 1.00 90.39 N ANISOU 1585 N GLY A 958 12305 11300 10740 241 -285 255 N ATOM 1586 CA GLY A 958 38.738 39.695 60.999 1.00 89.51 C ANISOU 1586 CA GLY A 958 12170 11336 10503 188 -42 303 C ATOM 1587 C GLY A 958 40.130 39.273 60.551 1.00 88.76 C ANISOU 1587 C GLY A 958 12187 11397 10139 153 58 258 C ATOM 1588 O GLY A 958 40.311 38.523 59.597 1.00 90.12 O ANISOU 1588 O GLY A 958 12438 11566 10239 173 -45 187 O ATOM 1589 N SER A 959 41.123 39.777 61.280 1.00 85.13 N ANISOU 1589 N SER A 959 11730 11078 9537 99 265 296 N ATOM 1590 CA SER A 959 42.510 39.418 61.046 1.00 84.17 C ANISOU 1590 CA SER A 959 11685 11121 9176 63 390 252 C ATOM 1591 C SER A 959 42.863 38.159 61.834 1.00 81.44 C ANISOU 1591 C SER A 959 11169 10830 8943 99 497 230 C ATOM 1592 O SER A 959 42.024 37.549 62.502 1.00 79.08 O ANISOU 1592 O SER A 959 10709 10437 8901 147 472 249 O ATOM 1593 CB SER A 959 43.436 40.568 61.434 1.00 84.18 C ANISOU 1593 CB SER A 959 11767 11249 8969 -15 557 296 C ATOM 1594 OG SER A 959 43.446 40.773 62.836 1.00 83.66 O ANISOU 1594 OG SER A 959 11543 11218 9026 -20 713 356 O ATOM 1595 N GLN A 960 44.136 37.767 61.760 1.00 71.98 N ANISOU 1595 N GLN A 960 10011 9787 7549 76 621 187 N ATOM 1596 CA GLN A 960 44.590 36.588 62.485 1.00 71.36 C ANISOU 1596 CA GLN A 960 9791 9770 7554 115 723 163 C ATOM 1597 C GLN A 960 44.600 36.829 63.990 1.00 70.24 C ANISOU 1597 C GLN A 960 9496 9662 7531 110 886 237 C ATOM 1598 O GLN A 960 44.406 35.889 64.768 1.00 69.87 O ANISOU 1598 O GLN A 960 9302 9591 7654 157 931 243 O ATOM 1599 CB GLN A 960 45.980 36.187 61.997 1.00 71.35 C ANISOU 1599 CB GLN A 960 9873 9930 7306 95 811 92 C ATOM 1600 CG GLN A 960 46.352 34.753 62.292 1.00 71.19 C ANISOU 1600 CG GLN A 960 9745 9943 7361 155 847 40 C ATOM 1601 CD GLN A 960 47.804 34.473 61.988 1.00 71.10 C ANISOU 1601 CD GLN A 960 9796 10109 7108 137 961 -29 C ATOM 1602 OE1 GLN A 960 48.630 35.386 61.962 1.00 70.83 O ANISOU 1602 OE1 GLN A 960 9841 10197 6874 71 1068 -22 O ATOM 1603 NE2 GLN A 960 48.126 33.209 61.745 1.00 71.39 N ANISOU 1603 NE2 GLN A 960 9797 10161 7168 194 940 -100 N ATOM 1604 N ASP A 961 44.818 38.078 64.416 1.00 75.16 N ANISOU 1604 N ASP A 961 10159 10334 8064 53 976 293 N ATOM 1605 CA ASP A 961 44.805 38.399 65.840 1.00 73.04 C ANISOU 1605 CA ASP A 961 9758 10096 7899 47 1128 363 C ATOM 1606 C ASP A 961 43.562 37.846 66.520 1.00 73.12 C ANISOU 1606 C ASP A 961 9611 9958 8215 102 1074 401 C ATOM 1607 O ASP A 961 43.629 37.329 67.641 1.00 71.17 O ANISOU 1607 O ASP A 961 9227 9733 8083 125 1193 431 O ATOM 1608 CB ASP A 961 44.869 39.913 66.032 1.00 71.08 C ANISOU 1608 CB ASP A 961 9588 9872 7549 -19 1182 418 C ATOM 1609 CG ASP A 961 46.168 40.512 65.533 1.00 75.07 C ANISOU 1609 CG ASP A 961 10235 10534 7755 -88 1270 386 C ATOM 1610 OD1 ASP A 961 47.128 39.743 65.314 1.00 78.39 O ANISOU 1610 OD1 ASP A 961 10660 11069 8057 -83 1328 324 O ATOM 1611 OD2 ASP A 961 46.230 41.750 65.360 1.00 72.94 O ANISOU 1611 OD2 ASP A 961 10073 10271 7372 -149 1284 419 O ATOM 1612 N GLN A 962 42.422 37.930 65.845 1.00 69.66 N ANISOU 1612 N GLN A 962 9191 9365 7910 125 895 396 N ATOM 1613 CA GLN A 962 41.149 37.493 66.394 1.00 69.87 C ANISOU 1613 CA GLN A 962 9068 9243 8239 170 834 425 C ATOM 1614 C GLN A 962 40.917 36.002 66.208 1.00 70.28 C ANISOU 1614 C GLN A 962 9040 9239 8424 224 770 373 C ATOM 1615 O GLN A 962 39.829 35.514 66.529 1.00 70.66 O ANISOU 1615 O GLN A 962 8965 9152 8729 258 705 386 O ATOM 1616 CB GLN A 962 40.018 38.292 65.748 1.00 70.75 C ANISOU 1616 CB GLN A 962 9227 9212 8440 173 662 437 C ATOM 1617 CG GLN A 962 40.185 39.803 65.908 1.00 70.45 C ANISOU 1617 CG GLN A 962 9280 9212 8277 123 715 490 C ATOM 1618 CD GLN A 962 39.564 40.602 64.780 1.00 71.50 C ANISOU 1618 CD GLN A 962 9553 9249 8366 121 526 477 C ATOM 1619 OE1 GLN A 962 40.063 41.669 64.423 1.00 71.50 O ANISOU 1619 OE1 GLN A 962 9701 9302 8165 72 545 495 O ATOM 1620 NE2 GLN A 962 38.471 40.098 64.218 1.00 72.48 N ANISOU 1620 NE2 GLN A 962 9635 9226 8677 172 338 446 N ATOM 1621 N GLU A 963 41.898 35.283 65.673 1.00 84.44 N ANISOU 1621 N GLU A 963 10902 11131 10052 230 786 312 N ATOM 1622 CA GLU A 963 41.794 33.838 65.552 1.00 86.19 C ANISOU 1622 CA GLU A 963 11054 11307 10387 282 739 261 C ATOM 1623 C GLU A 963 41.932 33.178 66.917 1.00 86.80 C ANISOU 1623 C GLU A 963 10978 11407 10596 303 898 304 C ATOM 1624 O GLU A 963 42.822 33.516 67.703 1.00 86.88 O ANISOU 1624 O GLU A 963 10978 11547 10485 283 1066 336 O ATOM 1625 CB GLU A 963 42.871 33.313 64.606 1.00 89.80 C ANISOU 1625 CB GLU A 963 11634 11871 10617 285 721 179 C ATOM 1626 CG GLU A 963 42.724 31.849 64.230 1.00 91.01 C ANISOU 1626 CG GLU A 963 11743 11963 10872 342 639 113 C ATOM 1627 CD GLU A 963 43.780 31.406 63.235 1.00 92.15 C ANISOU 1627 CD GLU A 963 12017 12213 10782 347 620 26 C ATOM 1628 OE1 GLU A 963 44.813 32.099 63.119 1.00 91.95 O ANISOU 1628 OE1 GLU A 963 12082 12335 10520 305 720 21 O ATOM 1629 OE2 GLU A 963 43.577 30.373 62.563 1.00 93.27 O ANISOU 1629 OE2 GLU A 963 12169 12292 10979 389 506 -43 O ATOM 1630 N VAL A 964 41.049 32.220 67.191 1.00 75.22 N ANISOU 1630 N VAL A 964 9394 9810 9375 343 842 302 N ATOM 1631 CA VAL A 964 41.052 31.477 68.443 1.00 75.56 C ANISOU 1631 CA VAL A 964 9300 9848 9561 366 978 344 C ATOM 1632 C VAL A 964 41.128 29.991 68.127 1.00 77.01 C ANISOU 1632 C VAL A 964 9457 9987 9815 414 923 284 C ATOM 1633 O VAL A 964 40.727 29.543 67.049 1.00 75.88 O ANISOU 1633 O VAL A 964 9364 9767 9700 431 757 219 O ATOM 1634 CB VAL A 964 39.809 31.785 69.304 1.00 75.14 C ANISOU 1634 CB VAL A 964 9115 9665 9768 360 994 413 C ATOM 1635 CG1 VAL A 964 39.799 33.247 69.717 1.00 73.32 C ANISOU 1635 CG1 VAL A 964 8910 9483 9465 317 1063 472 C ATOM 1636 CG2 VAL A 964 38.528 31.424 68.559 1.00 78.20 C ANISOU 1636 CG2 VAL A 964 9465 9878 10368 377 802 377 C ATOM 1637 N HIS A 965 41.641 29.223 69.086 1.00 90.18 N ANISOU 1637 N HIS A 965 11053 11700 11510 440 1060 306 N ATOM 1638 CA HIS A 965 41.897 27.803 68.897 1.00 87.57 C ANISOU 1638 CA HIS A 965 10707 11342 11222 489 1031 252 C ATOM 1639 C HIS A 965 41.244 27.007 70.015 1.00 84.96 C ANISOU 1639 C HIS A 965 10240 10906 11134 510 1105 306 C ATOM 1640 O HIS A 965 41.245 27.432 71.174 1.00 83.66 O ANISOU 1640 O HIS A 965 10010 10769 11006 496 1249 383 O ATOM 1641 CB HIS A 965 43.401 27.519 68.863 1.00 85.53 C ANISOU 1641 CB HIS A 965 10520 11258 10720 510 1125 213 C ATOM 1642 CG HIS A 965 44.204 28.625 68.255 1.00 84.91 C ANISOU 1642 CG HIS A 965 10558 11319 10385 469 1138 192 C ATOM 1643 ND1 HIS A 965 44.432 28.721 66.900 1.00 90.00 N ANISOU 1643 ND1 HIS A 965 11324 11983 10890 461 1013 115 N ATOM 1644 CD2 HIS A 965 44.826 29.688 68.817 1.00 85.01 C ANISOU 1644 CD2 HIS A 965 10589 11456 10256 429 1265 237 C ATOM 1645 CE1 HIS A 965 45.164 29.793 66.653 1.00 88.91 C ANISOU 1645 CE1 HIS A 965 11276 11973 10533 415 1068 116 C ATOM 1646 NE2 HIS A 965 45.416 30.398 67.799 1.00 86.03 N ANISOU 1646 NE2 HIS A 965 10847 11673 10166 393 1219 188 N ATOM 1647 N ARG A 966 40.684 25.853 69.658 1.00 91.78 N ANISOU 1647 N ARG A 966 11067 11645 12159 541 1007 263 N ATOM 1648 CA ARG A 966 40.106 24.929 70.621 1.00 92.11 C ANISOU 1648 CA ARG A 966 10993 11577 12427 558 1074 306 C ATOM 1649 C ARG A 966 40.433 23.505 70.201 1.00 92.49 C ANISOU 1649 C ARG A 966 11062 11586 12492 608 1018 239 C ATOM 1650 O ARG A 966 40.618 23.217 69.016 1.00 95.71 O ANISOU 1650 O ARG A 966 11551 11996 12819 623 881 154 O ATOM 1651 CB ARG A 966 38.586 25.101 70.741 1.00 92.85 C ANISOU 1651 CB ARG A 966 10984 11498 12797 528 1003 334 C ATOM 1652 CG ARG A 966 37.939 24.174 71.761 1.00 93.73 C ANISOU 1652 CG ARG A 966 10975 11489 13149 534 1086 381 C ATOM 1653 CD ARG A 966 36.477 24.523 71.981 1.00 95.94 C ANISOU 1653 CD ARG A 966 11139 11617 13696 496 1042 410 C ATOM 1654 NE ARG A 966 35.792 23.541 72.820 1.00 98.79 N ANISOU 1654 NE ARG A 966 11388 11848 14300 493 1112 443 N ATOM 1655 CZ ARG A 966 34.532 23.653 73.235 1.00 98.98 C ANISOU 1655 CZ ARG A 966 11288 11735 14585 458 1112 472 C ATOM 1656 NH1 ARG A 966 33.805 24.711 72.900 1.00 98.10 N ANISOU 1656 NH1 ARG A 966 11144 11599 14532 432 1036 470 N ATOM 1657 NH2 ARG A 966 33.997 22.706 73.994 1.00 98.11 N ANISOU 1657 NH2 ARG A 966 11087 11510 14680 450 1189 501 N ATOM 1658 N THR A 967 40.496 22.614 71.187 1.00 71.87 N ANISOU 1658 N THR A 967 8386 8936 9985 634 1126 279 N ATOM 1659 CA THR A 967 40.817 21.211 70.970 1.00 72.47 C ANISOU 1659 CA THR A 967 8479 8966 10090 685 1092 226 C ATOM 1660 C THR A 967 39.583 20.357 71.223 1.00 73.40 C ANISOU 1660 C THR A 967 8501 8881 10508 675 1045 240 C ATOM 1661 O THR A 967 38.857 20.571 72.198 1.00 73.31 O ANISOU 1661 O THR A 967 8394 8797 10662 644 1137 319 O ATOM 1662 CB THR A 967 41.957 20.758 71.886 1.00 71.82 C ANISOU 1662 CB THR A 967 8413 8997 9881 731 1248 255 C ATOM 1663 OG1 THR A 967 43.061 21.663 71.763 1.00 70.97 O ANISOU 1663 OG1 THR A 967 8374 9081 9509 729 1307 245 O ATOM 1664 CG2 THR A 967 42.418 19.355 71.516 1.00 72.49 C ANISOU 1664 CG2 THR A 967 8534 9046 9964 794 1199 188 C ATOM 1665 N VAL A 968 39.354 19.388 70.341 1.00 74.37 N ANISOU 1665 N VAL A 968 8648 8912 10698 699 907 158 N ATOM 1666 CA VAL A 968 38.208 18.494 70.424 1.00 75.43 C ANISOU 1666 CA VAL A 968 8697 8848 11116 685 844 154 C ATOM 1667 C VAL A 968 38.721 17.072 70.595 1.00 75.88 C ANISOU 1667 C VAL A 968 8780 8865 11187 738 869 126 C ATOM 1668 O VAL A 968 39.684 16.664 69.935 1.00 75.87 O ANISOU 1668 O VAL A 968 8874 8951 11002 788 824 56 O ATOM 1669 CB VAL A 968 37.306 18.598 69.176 1.00 76.41 C ANISOU 1669 CB VAL A 968 8821 8870 11340 663 634 76 C ATOM 1670 CG1 VAL A 968 35.947 17.973 69.451 1.00 77.46 C ANISOU 1670 CG1 VAL A 968 8831 8800 11799 630 590 85 C ATOM 1671 CG2 VAL A 968 37.150 20.049 68.737 1.00 75.94 C ANISOU 1671 CG2 VAL A 968 8787 8887 11180 630 587 85 C ATOM 1672 N PHE A 969 38.078 16.324 71.487 1.00 77.20 N ANISOU 1672 N PHE A 969 8864 8898 11570 726 943 179 N ATOM 1673 CA PHE A 969 38.438 14.945 71.774 1.00 77.75 C ANISOU 1673 CA PHE A 969 8957 8902 11682 773 973 165 C ATOM 1674 C PHE A 969 37.238 14.045 71.522 1.00 79.10 C ANISOU 1674 C PHE A 969 9058 8858 12137 741 877 136 C ATOM 1675 O PHE A 969 36.086 14.453 71.700 1.00 79.48 O ANISOU 1675 O PHE A 969 9007 8803 12389 678 862 166 O ATOM 1676 CB PHE A 969 38.911 14.778 73.230 1.00 77.14 C ANISOU 1676 CB PHE A 969 8863 8862 11585 790 1176 267 C ATOM 1677 CG PHE A 969 40.081 15.647 73.597 1.00 75.87 C ANISOU 1677 CG PHE A 969 8758 8910 11159 818 1278 296 C ATOM 1678 CD1 PHE A 969 41.379 15.183 73.454 1.00 75.59 C ANISOU 1678 CD1 PHE A 969 8810 8996 10913 892 1296 254 C ATOM 1679 CD2 PHE A 969 39.885 16.926 74.092 1.00 75.04 C ANISOU 1679 CD2 PHE A 969 8612 8879 11020 772 1356 361 C ATOM 1680 CE1 PHE A 969 42.457 15.980 73.791 1.00 74.57 C ANISOU 1680 CE1 PHE A 969 8723 9062 10550 914 1390 273 C ATOM 1681 CE2 PHE A 969 40.961 17.727 74.432 1.00 73.94 C ANISOU 1681 CE2 PHE A 969 8522 8930 10642 792 1450 384 C ATOM 1682 CZ PHE A 969 42.247 17.253 74.282 1.00 73.68 C ANISOU 1682 CZ PHE A 969 8572 9019 10406 860 1467 339 C ATOM 1683 N MET A 970 37.516 12.819 71.088 1.00 99.47 N ANISOU 1683 N MET A 970 11689 11370 14733 785 810 71 N ATOM 1684 CA MET A 970 36.485 11.805 70.940 1.00100.59 C ANISOU 1684 CA MET A 970 11772 11303 15144 756 734 42 C ATOM 1685 C MET A 970 37.122 10.439 71.126 1.00102.05 C ANISOU 1685 C MET A 970 12023 11439 15311 816 761 21 C ATOM 1686 O MET A 970 38.269 10.223 70.734 1.00103.83 O ANISOU 1686 O MET A 970 12350 11785 15315 888 747 -27 O ATOM 1687 CB MET A 970 35.806 11.879 69.572 1.00102.19 C ANISOU 1687 CB MET A 970 11972 11440 15415 735 517 -63 C ATOM 1688 CG MET A 970 34.540 11.054 69.483 1.00103.98 C ANISOU 1688 CG MET A 970 12108 11447 15954 686 438 -89 C ATOM 1689 SD MET A 970 33.783 11.139 67.857 1.00108.50 S ANISOU 1689 SD MET A 970 12683 11946 16595 669 167 -221 S ATOM 1690 CE MET A 970 32.129 10.558 68.220 1.00107.44 C ANISOU 1690 CE MET A 970 12385 11569 16868 588 136 -215 C ATOM 1691 N ARG A 971 36.361 9.514 71.705 1.00104.66 N ANISOU 1691 N ARG A 971 12296 11590 15881 786 799 53 N ATOM 1692 CA ARG A 971 36.827 8.161 71.980 1.00105.13 C ANISOU 1692 CA ARG A 971 12417 11570 15956 839 830 42 C ATOM 1693 C ARG A 971 36.123 7.193 71.039 1.00107.70 C ANISOU 1693 C ARG A 971 12737 11726 16458 823 662 -57 C ATOM 1694 O ARG A 971 34.904 7.278 70.853 1.00109.17 O ANISOU 1694 O ARG A 971 12825 11779 16876 747 598 -67 O ATOM 1695 CB ARG A 971 36.566 7.784 73.440 1.00105.33 C ANISOU 1695 CB ARG A 971 12401 11512 16107 815 1017 162 C ATOM 1696 CG ARG A 971 37.346 6.575 73.917 1.00106.36 C ANISOU 1696 CG ARG A 971 12622 11604 16184 888 1079 173 C ATOM 1697 CD ARG A 971 37.266 6.420 75.428 1.00106.88 C ANISOU 1697 CD ARG A 971 12671 11624 16313 873 1279 304 C ATOM 1698 NE ARG A 971 38.092 5.314 75.908 1.00108.11 N ANISOU 1698 NE ARG A 971 12929 11753 16396 955 1334 319 N ATOM 1699 CZ ARG A 971 39.380 5.411 76.229 1.00107.37 C ANISOU 1699 CZ ARG A 971 12920 11818 16056 1047 1392 331 C ATOM 1700 NH1 ARG A 971 40.018 6.569 76.132 1.00104.33 N ANISOU 1700 NH1 ARG A 971 12532 11638 15471 1064 1411 332 N ATOM 1701 NH2 ARG A 971 40.035 4.338 76.652 1.00108.48 N ANISOU 1701 NH2 ARG A 971 13151 11912 16155 1125 1428 341 N ATOM 1702 N LEU A 972 36.890 6.273 70.451 1.00 86.99 N ANISOU 1702 N LEU A 972 10216 9107 13730 897 590 -136 N ATOM 1703 CA LEU A 972 36.400 5.429 69.370 1.00 88.32 C ANISOU 1703 CA LEU A 972 10400 9142 14015 894 409 -250 C ATOM 1704 C LEU A 972 36.904 4.005 69.547 1.00 89.14 C ANISOU 1704 C LEU A 972 10582 9153 14134 956 425 -274 C ATOM 1705 O LEU A 972 37.961 3.772 70.139 1.00 88.53 O ANISOU 1705 O LEU A 972 10577 9170 13891 1029 534 -236 O ATOM 1706 CB LEU A 972 36.854 5.961 68.008 1.00 88.08 C ANISOU 1706 CB LEU A 972 10436 9234 13795 928 248 -360 C ATOM 1707 CG LEU A 972 36.851 7.482 67.851 1.00 86.95 C ANISOU 1707 CG LEU A 972 10265 9243 13529 897 254 -331 C ATOM 1708 CD1 LEU A 972 37.700 7.853 66.661 1.00 86.64 C ANISOU 1708 CD1 LEU A 972 10333 9351 13235 950 139 -429 C ATOM 1709 CD2 LEU A 972 35.435 8.011 67.695 1.00 87.50 C ANISOU 1709 CD2 LEU A 972 10219 9197 13832 807 178 -323 C ATOM 1710 N ASN A 973 36.149 3.056 68.999 1.00108.78 N ANISOU 1710 N ASN A 973 13055 11455 16822 928 307 -345 N ATOM 1711 CA ASN A 973 36.461 1.636 69.106 1.00110.92 C ANISOU 1711 CA ASN A 973 13398 11602 17143 977 305 -374 C ATOM 1712 C ASN A 973 37.168 1.158 67.846 1.00110.18 C ANISOU 1712 C ASN A 973 13410 11558 16896 1055 146 -513 C ATOM 1713 O ASN A 973 36.654 1.332 66.736 1.00109.26 O ANISOU 1713 O ASN A 973 13281 11415 16818 1027 -23 -610 O ATOM 1714 CB ASN A 973 35.189 0.816 69.327 1.00112.44 C ANISOU 1714 CB ASN A 973 13513 11546 17662 892 283 -368 C ATOM 1715 CG ASN A 973 34.491 1.162 70.623 1.00112.53 C ANISOU 1715 CG ASN A 973 13425 11495 17834 813 458 -233 C ATOM 1716 OD1 ASN A 973 34.897 0.719 71.697 1.00113.15 O ANISOU 1716 OD1 ASN A 973 13543 11553 17896 837 617 -141 O ATOM 1717 ND2 ASN A 973 33.427 1.952 70.530 1.00111.79 N ANISOU 1717 ND2 ASN A 973 13207 11372 17898 721 429 -223 N ATOM 1718 N ILE A 974 38.335 0.541 68.025 1.00105.62 N ANISOU 1718 N ILE A 974 12937 11048 16146 1157 196 -526 N ATOM 1719 CA ILE A 974 39.091 -0.059 66.932 1.00107.10 C ANISOU 1719 CA ILE A 974 13229 11275 16188 1241 66 -659 C ATOM 1720 C ILE A 974 38.842 -1.560 66.956 1.00108.66 C ANISOU 1720 C ILE A 974 13469 11265 16553 1262 25 -698 C ATOM 1721 O ILE A 974 38.983 -2.202 68.005 1.00107.73 O ANISOU 1721 O ILE A 974 13365 11068 16500 1280 151 -614 O ATOM 1722 CB ILE A 974 40.596 0.243 67.053 1.00105.95 C ANISOU 1722 CB ILE A 974 13167 11349 15740 1347 144 -663 C ATOM 1723 CG1 ILE A 974 40.845 1.727 67.351 1.00104.06 C ANISOU 1723 CG1 ILE A 974 12881 11304 15352 1316 228 -594 C ATOM 1724 CG2 ILE A 974 41.320 -0.187 65.778 1.00106.20 C ANISOU 1724 CG2 ILE A 974 13298 11442 15612 1424 4 -814 C ATOM 1725 CD1 ILE A 974 42.291 2.071 67.644 1.00103.62 C ANISOU 1725 CD1 ILE A 974 12888 11463 15018 1408 326 -587 C ATOM 1726 N ILE A 975 38.484 -2.125 65.800 1.00131.06 N ANISOU 1726 N ILE A 975 16336 14010 19452 1260 -153 -826 N ATOM 1727 CA ILE A 975 38.215 -3.553 65.680 1.00133.17 C ANISOU 1727 CA ILE A 975 16647 14070 19879 1275 -213 -880 C ATOM 1728 C ILE A 975 38.605 -4.009 64.282 1.00133.82 C ANISOU 1728 C ILE A 975 16819 14169 19857 1336 -395 -1044 C ATOM 1729 O ILE A 975 38.742 -3.206 63.358 1.00134.35 O ANISOU 1729 O ILE A 975 16894 14368 19784 1336 -491 -1113 O ATOM 1730 CB ILE A 975 36.732 -3.896 65.961 1.00134.87 C ANISOU 1730 CB ILE A 975 16760 14058 20428 1154 -235 -847 C ATOM 1731 CG1 ILE A 975 35.807 -3.072 65.059 1.00135.44 C ANISOU 1731 CG1 ILE A 975 16747 14136 20577 1072 -379 -908 C ATOM 1732 CG2 ILE A 975 36.400 -3.661 67.430 1.00134.78 C ANISOU 1732 CG2 ILE A 975 16678 14009 20525 1100 -36 -687 C ATOM 1733 CD1 ILE A 975 34.376 -3.565 65.051 1.00138.06 C ANISOU 1733 CD1 ILE A 975 16978 14237 21241 963 -445 -920 C ATOM 1734 N SER A 976 38.782 -5.319 64.134 1.00112.70 N ANISOU 1734 N SER A 976 14219 11354 17248 1388 -440 -1106 N ATOM 1735 CA SER A 976 39.109 -5.912 62.842 1.00113.74 C ANISOU 1735 CA SER A 976 14441 11475 17299 1447 -611 -1267 C ATOM 1736 C SER A 976 38.559 -7.332 62.749 1.00114.41 C ANISOU 1736 C SER A 976 14557 11309 17604 1438 -683 -1321 C ATOM 1737 O SER A 976 39.280 -8.268 62.402 1.00114.92 O ANISOU 1737 O SER A 976 14728 11346 17589 1534 -724 -1403 O ATOM 1738 CB SER A 976 40.624 -5.919 62.620 1.00113.14 C ANISOU 1738 CB SER A 976 14472 11593 16924 1581 -573 -1317 C ATOM 1739 OG SER A 976 40.953 -6.452 61.347 1.00112.94 O ANISOU 1739 OG SER A 976 14536 11565 16811 1638 -732 -1478 O CONECT 13 12 256 CONECT 112 111 709 CONECT 256 13 255 CONECT 349 348 490 CONECT 490 349 489 CONECT 709 112 708 CONECT 1107 1106 1523 CONECT 1523 1107 1522 END If you find results from this site helpful for your 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