HEADER TRANSFERASE/TRANSFERASE INHIBITOR 09-MAR-11 3R0T TITLE CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT IN COMPLEX TITLE 2 WITH THE INHIBITOR CX-5279 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 1-337; COMPND 5 SYNONYM: CK II ALPHA; COMPND 6 EC: 2.7.11.1; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CSNK2A1, CK2A1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT7-7 KEYWDS KINASE, CK2-INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR KEYWDS 2 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR R.BATTISTUTTA,E.PAPINUTTO,G.LOLLI,F.PIERRE,M.HADDACH,D.M.RYCKMAN REVDAT 2 29-OCT-14 3R0T 1 AUTHOR REVDAT 1 07-DEC-11 3R0T 0 JRNL AUTH R.BATTISTUTTA,G.COZZA,F.PIERRE,E.PAPINUTTO,G.LOLLI,S.SARNO, JRNL AUTH 2 S.E.O'BRIEN,A.SIDDIQUI-JAIN,M.HADDACH,K.ANDERES,D.M.RYCKMAN, JRNL AUTH 3 F.MEGGIO,L.A.PINNA JRNL TITL UNPRECEDENTED SELECTIVITY AND STRUCTURAL DETERMINANTS OF A JRNL TITL 2 NEW CLASS OF PROTEIN KINASE CK2 INHIBITORS IN CLINICAL JRNL TITL 3 TRIALS FOR THE TREATMENT OF CANCER. JRNL REF BIOCHEMISTRY V. 50 8478 2011 JRNL REFN ISSN 0006-2960 JRNL PMID 21870818 JRNL DOI 10.1021/BI2008382 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH G.COZZA,M.MAZZORANA,E.PAPINUTTO,J.BAIN,M.ELLIOTT,G.DI MAIRA, REMARK 1 AUTH 2 A.GIANONCELLI,M.A.PAGANO,S.SARNO,M.RUZZENE,R.BATTISTUTTA, REMARK 1 AUTH 3 F.MEGGIO,S.MORO,G.ZAGOTTO,L.A.PINNA REMARK 1 TITL QUINALIZARIN AS A POTENT, SELECTIVE AND CELL-PERMEABLE REMARK 1 TITL 2 INHIBITOR OF PROTEIN KINASE CK2. REMARK 1 REF BIOCHEM.J. V. 421 387 2009 REMARK 1 REFN ISSN 0264-6021 REMARK 1 PMID 19432557 REMARK 1 DOI 10.1042/BJ20090069 REMARK 2 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.18 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 89.4 REMARK 3 NUMBER OF REFLECTIONS : 28526 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.163 REMARK 3 R VALUE (WORKING SET) : 0.160 REMARK 3 FREE R VALUE : 0.211 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 1420 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 35.1842 - 3.7690 0.99 3103 165 0.1437 0.1687 REMARK 3 2 3.7690 - 2.9920 0.99 3026 162 0.1456 0.1894 REMARK 3 3 2.9920 - 2.6140 1.00 3033 153 0.1662 0.2429 REMARK 3 4 2.6140 - 2.3750 0.99 2975 179 0.1725 0.2541 REMARK 3 5 2.3750 - 2.2048 0.99 3009 152 0.1654 0.2217 REMARK 3 6 2.2048 - 2.0749 0.97 2927 145 0.1638 0.2257 REMARK 3 7 2.0749 - 1.9710 0.92 2782 140 0.1662 0.2278 REMARK 3 8 1.9710 - 1.8852 0.85 2580 129 0.1825 0.2350 REMARK 3 9 1.8852 - 1.8126 0.71 2123 113 0.2041 0.2279 REMARK 3 10 1.8126 - 1.7500 0.51 1548 82 0.2385 0.3005 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.83 REMARK 3 K_SOL : 0.37 REMARK 3 B_SOL : 38.79 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.080 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 17.83 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.07 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -6.30980 REMARK 3 B22 (A**2) : 3.47990 REMARK 3 B33 (A**2) : 2.82990 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.16510 REMARK 3 B23 (A**2) : -0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 2946 REMARK 3 ANGLE : 1.036 3976 REMARK 3 CHIRALITY : 0.075 406 REMARK 3 PLANARITY : 0.005 501 REMARK 3 DIHEDRAL : 13.608 1109 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (chain A and resid 3:13) REMARK 3 ORIGIN FOR THE GROUP (A): 1.4641 -55.6146 14.6268 REMARK 3 T TENSOR REMARK 3 T11: 0.1667 T22: 0.1553 REMARK 3 T33: 0.2001 T12: -0.0541 REMARK 3 T13: 0.0353 T23: -0.0565 REMARK 3 L TENSOR REMARK 3 L11: 0.0564 L22: 0.0078 REMARK 3 L33: 0.0150 L12: 0.0243 REMARK 3 L13: 0.0083 L23: -0.0003 REMARK 3 S TENSOR REMARK 3 S11: -0.0120 S12: 0.0526 S13: -0.0471 REMARK 3 S21: -0.0062 S22: 0.0860 S23: -0.0703 REMARK 3 S31: -0.0106 S32: -0.0466 S33: 0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (chain A and resid 14:32) REMARK 3 ORIGIN FOR THE GROUP (A): 20.9593 -56.5547 8.8193 REMARK 3 T TENSOR REMARK 3 T11: 0.2184 T22: 0.1470 REMARK 3 T33: 0.3446 T12: 0.0235 REMARK 3 T13: 0.0536 T23: -0.0858 REMARK 3 L TENSOR REMARK 3 L11: 0.0139 L22: 0.0999 REMARK 3 L33: 0.0686 L12: -0.0127 REMARK 3 L13: 0.0311 L23: -0.0074 REMARK 3 S TENSOR REMARK 3 S11: -0.2488 S12: 0.1931 S13: -0.1999 REMARK 3 S21: -0.0211 S22: 0.0957 S23: -0.1243 REMARK 3 S31: 0.1808 S32: 0.1616 S33: -0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (chain A and resid 33:51) REMARK 3 ORIGIN FOR THE GROUP (A): 33.0192 -34.0681 15.6464 REMARK 3 T TENSOR REMARK 3 T11: 0.1317 T22: 0.2292 REMARK 3 T33: 0.2319 T12: -0.0256 REMARK 3 T13: 0.0088 T23: -0.0750 REMARK 3 L TENSOR REMARK 3 L11: 0.0751 L22: 0.1045 REMARK 3 L33: 0.1087 L12: -0.0117 REMARK 3 L13: 0.0879 L23: 0.0255 REMARK 3 S TENSOR REMARK 3 S11: -0.0732 S12: 0.0348 S13: -0.0756 REMARK 3 S21: -0.0804 S22: -0.1905 S23: 0.2135 REMARK 3 S31: -0.0276 S32: 0.0701 S33: -0.0001 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (chain A and resid 52:71) REMARK 3 ORIGIN FOR THE GROUP (A): 32.1118 -31.5914 11.3104 REMARK 3 T TENSOR REMARK 3 T11: 0.1156 T22: 0.2072 REMARK 3 T33: 0.1295 T12: -0.0180 REMARK 3 T13: -0.0353 T23: -0.0043 REMARK 3 L TENSOR REMARK 3 L11: 0.0728 L22: 0.0127 REMARK 3 L33: 0.0385 L12: -0.0320 REMARK 3 L13: -0.0050 L23: 0.0035 REMARK 3 S TENSOR REMARK 3 S11: -0.0461 S12: 0.1432 S13: 0.2397 REMARK 3 S21: -0.1383 S22: 0.0626 S23: 0.0589 REMARK 3 S31: 0.0279 S32: -0.0798 S33: 0.0007 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (chain A and resid 72:102) REMARK 3 ORIGIN FOR THE GROUP (A): 24.7116 -44.4796 11.8194 REMARK 3 T TENSOR REMARK 3 T11: 0.1217 T22: 0.1772 REMARK 3 T33: 0.1597 T12: 0.0066 REMARK 3 T13: -0.0140 T23: -0.0266 REMARK 3 L TENSOR REMARK 3 L11: 0.1791 L22: 0.2326 REMARK 3 L33: 0.1170 L12: 0.1641 REMARK 3 L13: 0.0026 L23: 0.1089 REMARK 3 S TENSOR REMARK 3 S11: -0.0039 S12: -0.1009 S13: -0.1852 REMARK 3 S21: 0.0915 S22: 0.0280 S23: -0.1044 REMARK 3 S31: 0.0618 S32: 0.0149 S33: -0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (chain A and resid 103:139) REMARK 3 ORIGIN FOR THE GROUP (A): 15.9998 -29.1819 10.8388 REMARK 3 T TENSOR REMARK 3 T11: 0.1312 T22: 0.1502 REMARK 3 T33: 0.1780 T12: 0.0178 REMARK 3 T13: -0.0068 T23: -0.0057 REMARK 3 L TENSOR REMARK 3 L11: 0.0500 L22: 0.0814 REMARK 3 L33: 0.2482 L12: -0.0064 REMARK 3 L13: -0.0006 L23: -0.1427 REMARK 3 S TENSOR REMARK 3 S11: -0.0048 S12: 0.0020 S13: 0.2493 REMARK 3 S21: 0.0802 S22: 0.0149 S23: -0.1391 REMARK 3 S31: -0.0785 S32: -0.0440 S33: 0.0000 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (chain A and resid 140:224) REMARK 3 ORIGIN FOR THE GROUP (A): 9.9353 -41.3947 15.1453 REMARK 3 T TENSOR REMARK 3 T11: 0.0934 T22: 0.0745 REMARK 3 T33: 0.1054 T12: -0.0020 REMARK 3 T13: -0.0027 T23: -0.0197 REMARK 3 L TENSOR REMARK 3 L11: 0.5752 L22: 0.4700 REMARK 3 L33: 0.2096 L12: 0.0653 REMARK 3 L13: -0.1833 L23: -0.2846 REMARK 3 S TENSOR REMARK 3 S11: -0.0428 S12: 0.1121 S13: -0.0482 REMARK 3 S21: 0.0253 S22: 0.0386 S23: -0.1052 REMARK 3 S31: 0.0006 S32: -0.0174 S33: 0.0000 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (chain A and resid 225:247) REMARK 3 ORIGIN FOR THE GROUP (A): 0.7560 -31.9870 26.3692 REMARK 3 T TENSOR REMARK 3 T11: 0.1549 T22: 0.0805 REMARK 3 T33: 0.1055 T12: 0.0151 REMARK 3 T13: -0.0151 T23: 0.0012 REMARK 3 L TENSOR REMARK 3 L11: 0.1356 L22: 0.0378 REMARK 3 L33: 0.0555 L12: -0.0798 REMARK 3 L13: 0.0674 L23: -0.0466 REMARK 3 S TENSOR REMARK 3 S11: -0.0772 S12: 0.0027 S13: 0.1597 REMARK 3 S21: 0.1155 S22: 0.0023 S23: -0.1846 REMARK 3 S31: -0.0997 S32: -0.0487 S33: -0.0003 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (chain A and resid 248:329) REMARK 3 ORIGIN FOR THE GROUP (A): -5.9085 -37.9654 18.3039 REMARK 3 T TENSOR REMARK 3 T11: 0.0920 T22: 0.1009 REMARK 3 T33: 0.0675 T12: -0.0082 REMARK 3 T13: -0.0036 T23: 0.0107 REMARK 3 L TENSOR REMARK 3 L11: 0.4401 L22: 0.2274 REMARK 3 L33: 0.3372 L12: -0.1399 REMARK 3 L13: -0.2005 L23: -0.0276 REMARK 3 S TENSOR REMARK 3 S11: -0.0103 S12: 0.1025 S13: -0.0126 REMARK 3 S21: 0.0164 S22: 0.0378 S23: -0.0172 REMARK 3 S31: 0.0227 S32: -0.1320 S33: 0.0000 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 3R0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-11. REMARK 100 THE RCSB ID CODE IS RCSB064346. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-OCT-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ELETTRA REMARK 200 BEAMLINE : 5.2R REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI111 REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28551 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 46.180 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 89.6 REMARK 200 DATA REDUNDANCY : 2.800 REMARK 200 R MERGE (I) : 0.08300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84 REMARK 200 COMPLETENESS FOR SHELL (%) : 57.4 REMARK 200 DATA REDUNDANCY IN SHELL : 1.60 REMARK 200 R MERGE FOR SHELL (I) : 0.46200 REMARK 200 R SYM FOR SHELL (I) : 0.46200 REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 2PVR REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 37.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 4000, 0.2M LI2SO4, 0.1M TRIS REMARK 280 PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 23.09200 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 ASP A 330 REMARK 465 GLN A 331 REMARK 465 ALA A 332 REMARK 465 ARG A 333 REMARK 465 MET A 334 REMARK 465 GLY A 335 REMARK 465 SER A 336 REMARK 465 SER A 337 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 VAL A 66 CA CB CG1 CG2 REMARK 480 MET A 137 CA CB CG SD CE REMARK 480 MET A 150 CA CB CG SD CE REMARK 480 SER A 194 CA CB OG 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 PRO A 72 7.31 -63.10 REMARK 500 LYS A 74 171.94 77.25 REMARK 500 LYS A 75 -94.80 -122.48 REMARK 500 ASP A 156 41.13 -151.35 REMARK 500 ASP A 175 76.09 53.05 REMARK 500 ALA A 193 155.33 68.87 REMARK 500 MET A 208 54.56 -92.13 REMARK 500 HIS A 234 73.11 -103.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 630 DISTANCE = 5.37 ANGSTROMS REMARK 525 HOH A 658 DISTANCE = 5.17 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FU9 A 338 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 339 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 340 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 341 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 342 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 343 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 344 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 345 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 346 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 347 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 348 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 349 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 350 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 351 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 352 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3PE1 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT REMARK 900 IN COMPLEX WITH THE INHIBITOR CX-4945 REMARK 900 RELATED ID: 3PE2 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT REMARK 900 IN COMPLEX WITH THE INHIBITOR CX-5011 DBREF 3R0T A 1 337 UNP P68400 CSK21_HUMAN 1 337 SEQRES 1 A 337 MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR SEQRES 2 A 337 ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR SEQRES 3 A 337 GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR SEQRES 4 A 337 GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU SEQRES 5 A 337 VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL SEQRES 6 A 337 VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE SEQRES 7 A 337 LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY SEQRES 8 A 337 PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO SEQRES 9 A 337 VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN SEQRES 10 A 337 ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP SEQRES 11 A 337 TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA SEQRES 12 A 337 LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP SEQRES 13 A 337 VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG SEQRES 14 A 337 LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR SEQRES 15 A 337 HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG SEQRES 16 A 337 TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET SEQRES 17 A 337 TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET SEQRES 18 A 337 LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS SEQRES 19 A 337 GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS SEQRES 20 A 337 VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS SEQRES 21 A 337 TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU SEQRES 22 A 337 GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS SEQRES 23 A 337 SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP SEQRES 24 A 337 PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG SEQRES 25 A 337 LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR SEQRES 26 A 337 THR VAL VAL LYS ASP GLN ALA ARG MET GLY SER SER HET FU9 A 338 32 HET SO4 A 339 5 HET SO4 A 340 5 HET SO4 A 341 5 HET SO4 A 342 5 HET PEG A 343 7 HET EDO A 344 4 HET EDO A 345 4 HET EDO A 346 4 HET EDO A 347 4 HET EDO A 348 4 HET EDO A 349 4 HET EDO A 350 4 HET EDO A 351 4 HET EDO A 352 4 HETNAM FU9 3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL) HETNAM 2 FU9 PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC HETNAM 3 FU9 ACID HETNAM SO4 SULFATE ION HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM EDO 1,2-ETHANEDIOL HETSYN FU9 CX-5279 HETSYN EDO ETHYLENE GLYCOL FORMUL 2 FU9 C22 H16 F3 N5 O2 FORMUL 3 SO4 4(O4 S 2-) FORMUL 7 PEG C4 H10 O3 FORMUL 8 EDO 9(C2 H6 O2) FORMUL 17 HOH *334(H2 O) HELIX 1 1 PRO A 20 ASP A 25 1 6 HELIX 2 2 TYR A 26 HIS A 29 5 4 HELIX 3 3 ASN A 35 ASP A 37 5 3 HELIX 4 4 LYS A 76 ARG A 89 1 14 HELIX 5 5 ASP A 120 TYR A 125 1 6 HELIX 6 6 THR A 129 MET A 150 1 22 HELIX 7 7 LYS A 158 HIS A 160 5 3 HELIX 8 8 ASP A 175 ALA A 179 5 5 HELIX 9 9 SER A 194 LYS A 198 5 5 HELIX 10 10 GLY A 199 VAL A 204 1 6 HELIX 11 11 TYR A 211 ARG A 228 1 18 HELIX 12 12 ASP A 237 GLY A 250 1 14 HELIX 13 13 GLY A 250 TYR A 261 1 12 HELIX 14 14 ASP A 266 ILE A 272 5 7 HELIX 15 15 ARG A 280 VAL A 285 5 6 HELIX 16 16 ASN A 289 VAL A 293 5 5 HELIX 17 17 SER A 294 LEU A 305 1 12 HELIX 18 18 ASP A 308 ARG A 312 5 5 HELIX 19 19 THR A 314 GLU A 320 1 7 HELIX 20 20 HIS A 321 TYR A 325 5 5 SHEET 1 A 5 TYR A 39 ARG A 47 0 SHEET 2 A 5 SER A 51 ASN A 58 -1 O VAL A 53 N LEU A 45 SHEET 3 A 5 LYS A 64 LEU A 70 -1 O VAL A 65 N ALA A 56 SHEET 4 A 5 THR A 108 GLU A 114 -1 O LEU A 111 N LYS A 68 SHEET 5 A 5 LEU A 97 ASP A 103 -1 N VAL A 101 O ALA A 110 SHEET 1 B 2 ILE A 152 MET A 153 0 SHEET 2 B 2 GLU A 180 PHE A 181 -1 O GLU A 180 N MET A 153 SHEET 1 C 2 VAL A 162 ASP A 165 0 SHEET 2 C 2 LYS A 170 LEU A 173 -1 O LYS A 170 N ASP A 165 CISPEP 1 GLU A 230 PRO A 231 0 1.13 SITE 1 AC1 20 LEU A 45 GLY A 46 ARG A 47 VAL A 53 SITE 2 AC1 20 VAL A 66 LYS A 68 PHE A 113 GLU A 114 SITE 3 AC1 20 HIS A 115 VAL A 116 ASN A 118 MET A 163 SITE 4 AC1 20 ILE A 174 ASP A 175 EDO A 345 EDO A 351 SITE 5 AC1 20 HOH A 370 HOH A 381 HOH A 616 HOH A 636 SITE 1 AC2 6 ARG A 80 ARG A 155 ASN A 189 VAL A 192 SITE 2 AC2 6 HOH A 369 HOH A 677 SITE 1 AC3 4 ARG A 191 LYS A 198 ASN A 238 PEG A 343 SITE 1 AC4 8 ASP A 253 ARG A 278 ARG A 306 TYR A 307 SITE 2 AC4 8 ASP A 308 HOH A 397 HOH A 442 HOH A 465 SITE 1 AC5 5 LYS A 170 ARG A 172 HOH A 428 HOH A 463 SITE 2 AC5 5 HOH A 649 SITE 1 AC6 6 SER A 194 ARG A 195 TYR A 196 SO4 A 340 SITE 2 AC6 6 HOH A 433 HOH A 619 SITE 1 AC7 6 GLN A 36 TYR A 39 VAL A 101 ASP A 103 SITE 2 AC7 6 PRO A 104 ARG A 280 SITE 1 AC8 6 ASN A 118 ASP A 120 HIS A 160 FU9 A 338 SITE 2 AC8 6 EDO A 348 EDO A 351 SITE 1 AC9 4 ASP A 37 PRO A 295 HIS A 321 HOH A 620 SITE 1 BC1 5 PHE A 232 HOH A 372 HOH A 573 HOH A 621 SITE 2 BC1 5 HOH A 668 SITE 1 BC2 9 ASN A 118 THR A 119 ASP A 120 PHE A 121 SITE 2 BC2 9 PRO A 159 VAL A 162 MET A 163 ILE A 164 SITE 3 BC2 9 EDO A 345 SITE 1 BC3 6 LYS A 158 HIS A 160 SER A 194 EDO A 350 SITE 2 BC3 6 HOH A 618 HOH A 619 SITE 1 BC4 5 PRO A 159 PHE A 197 GLU A 230 EDO A 349 SITE 2 BC4 5 HOH A 618 SITE 1 BC5 5 ASN A 118 FU9 A 338 EDO A 345 HOH A 455 SITE 2 BC5 5 HOH A 575 SITE 1 BC6 7 PRO A 104 ARG A 278 LYS A 279 ASP A 302 SITE 2 BC6 7 HOH A 531 HOH A 642 HOH A 679 CRYST1 58.352 46.184 63.300 90.00 111.51 90.00 P 1 21 1 2 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017137 0.000000 0.006753 0.00000 SCALE2 0.000000 0.021653 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016980 0.00000 ATOM 1 N GLY A 3 -1.502 -62.453 29.985 1.00 40.82 N ANISOU 1 N GLY A 3 5111 4857 5540 -349 80 -403 N ATOM 2 CA GLY A 3 -0.651 -61.305 29.715 1.00 44.52 C ANISOU 2 CA GLY A 3 5587 5318 6013 -345 98 -421 C ATOM 3 C GLY A 3 -1.188 -60.418 28.604 1.00 39.81 C ANISOU 3 C GLY A 3 4994 4745 5387 -353 122 -411 C ATOM 4 O GLY A 3 -2.322 -60.588 28.164 1.00 36.32 O ANISOU 4 O GLY A 3 4552 4328 4919 -359 125 -385 O ATOM 5 N PRO A 4 -0.368 -59.467 28.133 1.00 38.43 N ANISOU 5 N PRO A 4 4823 4562 5216 -353 140 -431 N ATOM 6 CA PRO A 4 -0.839 -58.542 27.100 1.00 28.04 C ANISOU 6 CA PRO A 4 3512 3269 3872 -360 164 -421 C ATOM 7 C PRO A 4 -1.077 -59.249 25.772 1.00 26.24 C ANISOU 7 C PRO A 4 3274 3054 3640 -386 172 -431 C ATOM 8 O PRO A 4 -0.480 -60.287 25.482 1.00 29.56 O ANISOU 8 O PRO A 4 3684 3461 4086 -400 164 -457 O ATOM 9 CB PRO A 4 0.313 -57.540 26.978 1.00 34.55 C ANISOU 9 CB PRO A 4 4342 4077 4709 -355 178 -446 C ATOM 10 CG PRO A 4 1.524 -58.326 27.371 1.00 39.33 C ANISOU 10 CG PRO A 4 4939 4652 5354 -358 165 -481 C ATOM 11 CD PRO A 4 1.055 -59.258 28.461 1.00 39.89 C ANISOU 11 CD PRO A 4 5007 4717 5431 -349 140 -465 C ATOM 12 N VAL A 5 -1.971 -58.679 24.977 1.00 21.32 N ANISOU 12 N VAL A 5 2656 2459 2987 -392 188 -409 N ATOM 13 CA VAL A 5 -2.286 -59.191 23.656 1.00 25.36 C ANISOU 13 CA VAL A 5 3158 2986 3490 -416 198 -415 C ATOM 14 C VAL A 5 -1.179 -58.723 22.726 1.00 20.62 C ANISOU 14 C VAL A 5 2556 2376 2904 -429 216 -450 C ATOM 15 O VAL A 5 -0.725 -57.591 22.846 1.00 22.01 O ANISOU 15 O VAL A 5 2740 2547 3076 -418 228 -453 O ATOM 16 CB VAL A 5 -3.629 -58.612 23.180 1.00 14.07 C ANISOU 16 CB VAL A 5 1735 1590 2021 -416 209 -378 C ATOM 17 CG1 VAL A 5 -3.854 -58.886 21.709 1.00 17.54 C ANISOU 17 CG1 VAL A 5 2167 2047 2450 -442 224 -386 C ATOM 18 CG2 VAL A 5 -4.773 -59.147 24.037 1.00 23.46 C ANISOU 18 CG2 VAL A 5 2926 2792 3196 -405 192 -344 C ATOM 19 N PRO A 6 -0.720 -59.591 21.809 1.00 19.05 N ANISOU 19 N PRO A 6 2345 2173 2721 -451 218 -477 N ATOM 20 CA PRO A 6 0.332 -59.161 20.879 1.00 22.26 C ANISOU 20 CA PRO A 6 2749 2571 3140 -464 235 -511 C ATOM 21 C PRO A 6 -0.180 -58.203 19.796 1.00 19.43 C ANISOU 21 C PRO A 6 2395 2237 2751 -473 259 -498 C ATOM 22 O PRO A 6 -1.380 -58.098 19.579 1.00 23.70 O ANISOU 22 O PRO A 6 2938 2804 3262 -474 262 -466 O ATOM 23 CB PRO A 6 0.816 -60.479 20.258 1.00 22.71 C ANISOU 23 CB PRO A 6 2791 2618 3221 -486 229 -541 C ATOM 24 CG PRO A 6 -0.334 -61.414 20.398 1.00 24.95 C ANISOU 24 CG PRO A 6 3071 2918 3492 -490 215 -515 C ATOM 25 CD PRO A 6 -1.050 -61.022 21.661 1.00 24.62 C ANISOU 25 CD PRO A 6 3039 2879 3436 -465 203 -481 C ATOM 26 N SER A 7 0.745 -57.506 19.142 1.00 17.65 N ANISOU 26 N SER A 7 2170 2004 2534 -480 276 -524 N ATOM 27 CA SER A 7 0.417 -56.544 18.097 1.00 16.35 C ANISOU 27 CA SER A 7 2008 1861 2343 -488 300 -515 C ATOM 28 C SER A 7 1.444 -56.657 16.984 1.00 20.63 C ANISOU 28 C SER A 7 2542 2394 2901 -510 313 -554 C ATOM 29 O SER A 7 2.597 -57.000 17.244 1.00 20.28 O ANISOU 29 O SER A 7 2493 2324 2888 -510 307 -587 O ATOM 30 CB SER A 7 0.466 -55.121 18.661 1.00 17.57 C ANISOU 30 CB SER A 7 2177 2015 2485 -467 308 -500 C ATOM 31 OG SER A 7 0.286 -54.152 17.636 1.00 19.00 O ANISOU 31 OG SER A 7 2361 2214 2643 -476 331 -495 O ATOM 32 N ARG A 8 1.025 -56.363 15.754 1.00 20.45 N ANISOU 32 N ARG A 8 2517 2395 2857 -527 331 -550 N ATOM 33 CA ARG A 8 1.917 -56.328 14.585 1.00 21.97 C ANISOU 33 CA ARG A 8 2703 2585 3062 -548 347 -584 C ATOM 34 C ARG A 8 1.691 -55.027 13.836 1.00 21.54 C ANISOU 34 C ARG A 8 2655 2548 2981 -550 370 -572 C ATOM 35 O ARG A 8 0.571 -54.501 13.838 1.00 18.25 O ANISOU 35 O ARG A 8 2246 2155 2534 -544 374 -536 O ATOM 36 CB ARG A 8 1.572 -57.455 13.608 1.00 29.94 C ANISOU 36 CB ARG A 8 3698 3606 4070 -574 346 -593 C ATOM 37 CG ARG A 8 1.835 -58.846 14.104 1.00 37.53 C ANISOU 37 CG ARG A 8 4651 4551 5059 -577 325 -610 C ATOM 38 CD ARG A 8 3.325 -59.102 14.202 1.00 40.04 C ANISOU 38 CD ARG A 8 4963 4838 5414 -580 323 -653 C ATOM 39 NE ARG A 8 3.601 -60.471 14.624 1.00 40.22 N ANISOU 39 NE ARG A 8 4975 4844 5464 -584 303 -669 N ATOM 40 CZ ARG A 8 3.575 -60.878 15.889 1.00 42.42 C ANISOU 40 CZ ARG A 8 5256 5106 5755 -566 282 -661 C ATOM 41 NH1 ARG A 8 3.283 -60.018 16.864 1.00 33.21 N ANISOU 41 NH1 ARG A 8 4102 3938 4577 -542 279 -636 N ATOM 42 NH2 ARG A 8 3.841 -62.146 16.180 1.00 45.87 N ANISOU 42 NH2 ARG A 8 5683 5528 6218 -572 264 -677 N ATOM 43 N ALA A 9 2.731 -54.532 13.165 1.00 15.62 N ANISOU 43 N ALA A 9 1904 1789 2243 -560 384 -602 N ATOM 44 CA ALA A 9 2.572 -53.402 12.257 1.00 18.46 C ANISOU 44 CA ALA A 9 2267 2166 2579 -566 407 -594 C ATOM 45 C ALA A 9 1.606 -53.796 11.137 1.00 21.46 C ANISOU 45 C ALA A 9 2642 2578 2936 -587 416 -580 C ATOM 46 O ALA A 9 1.625 -54.930 10.662 1.00 21.38 O ANISOU 46 O ALA A 9 2621 2568 2936 -605 409 -595 O ATOM 47 CB ALA A 9 3.914 -52.996 11.673 1.00 14.16 C ANISOU 47 CB ALA A 9 1720 1606 2055 -576 420 -633 C ATOM 48 N ARG A 10 0.762 -52.862 10.709 1.00 13.86 N ANISOU 48 N ARG A 10 1687 1639 1940 -586 429 -550 N ATOM 49 CA ARG A 10 -0.195 -53.164 9.653 1.00 16.17 C ANISOU 49 CA ARG A 10 1974 1962 2208 -605 438 -534 C ATOM 50 C ARG A 10 0.395 -52.974 8.263 1.00 16.19 C ANISOU 50 C ARG A 10 1970 1972 2210 -630 457 -560 C ATOM 51 O ARG A 10 -0.245 -53.311 7.260 1.00 20.93 O ANISOU 51 O ARG A 10 2563 2595 2793 -649 465 -553 O ATOM 52 CB ARG A 10 -1.463 -52.325 9.813 1.00 20.15 C ANISOU 52 CB ARG A 10 2489 2491 2677 -593 443 -489 C ATOM 53 CG ARG A 10 -2.278 -52.639 11.048 1.00 33.68 C ANISOU 53 CG ARG A 10 4208 4204 4385 -572 424 -460 C ATOM 54 CD ARG A 10 -3.552 -51.806 11.037 1.00 41.52 C ANISOU 54 CD ARG A 10 5211 5224 5342 -563 431 -416 C ATOM 55 NE ARG A 10 -3.245 -50.409 10.738 1.00 55.14 N ANISOU 55 NE ARG A 10 6944 6952 7056 -557 450 -413 N ATOM 56 CZ ARG A 10 -4.138 -49.512 10.325 1.00 57.27 C ANISOU 56 CZ ARG A 10 7221 7246 7295 -555 463 -382 C ATOM 57 NH1 ARG A 10 -5.406 -49.859 10.157 1.00 51.33 N ANISOU 57 NH1 ARG A 10 6468 6519 6518 -558 460 -351 N ATOM 58 NH2 ARG A 10 -3.756 -48.265 10.082 1.00 58.40 N ANISOU 58 NH2 ARG A 10 7370 7388 7430 -550 479 -382 N ATOM 59 N VAL A 11 1.614 -52.434 8.208 1.00 17.69 N ANISOU 59 N VAL A 11 2160 2142 2420 -629 465 -589 N ATOM 60 CA VAL A 11 2.346 -52.276 6.954 1.00 18.09 C ANISOU 60 CA VAL A 11 2203 2196 2474 -652 483 -618 C ATOM 61 C VAL A 11 3.819 -52.578 7.179 1.00 22.01 C ANISOU 61 C VAL A 11 2695 2661 3008 -653 479 -661 C ATOM 62 O VAL A 11 4.294 -52.538 8.311 1.00 20.68 O ANISOU 62 O VAL A 11 2531 2469 2858 -633 466 -665 O ATOM 63 CB VAL A 11 2.206 -50.858 6.352 1.00 17.11 C ANISOU 63 CB VAL A 11 2088 2088 2327 -652 504 -604 C ATOM 64 CG1 VAL A 11 0.766 -50.601 5.959 1.00 21.02 C ANISOU 64 CG1 VAL A 11 2586 2615 2785 -654 509 -563 C ATOM 65 CG2 VAL A 11 2.716 -49.791 7.320 1.00 21.76 C ANISOU 65 CG2 VAL A 11 2689 2658 2922 -626 504 -600 C ATOM 66 N TYR A 12 4.526 -52.889 6.097 1.00 17.12 N ANISOU 66 N TYR A 12 2064 2041 2398 -677 490 -693 N ATOM 67 CA TYR A 12 5.951 -53.168 6.155 1.00 19.55 C ANISOU 67 CA TYR A 12 2367 2322 2741 -681 488 -736 C ATOM 68 C TYR A 12 6.273 -54.144 7.269 1.00 21.70 C ANISOU 68 C TYR A 12 2636 2568 3041 -668 465 -747 C ATOM 69 O TYR A 12 7.320 -54.030 7.919 1.00 22.08 O ANISOU 69 O TYR A 12 2686 2589 3115 -658 459 -770 O ATOM 70 CB TYR A 12 6.708 -51.872 6.405 1.00 15.19 C ANISOU 70 CB TYR A 12 1824 1757 2191 -668 499 -742 C ATOM 71 CG TYR A 12 6.436 -50.806 5.380 1.00 18.71 C ANISOU 71 CG TYR A 12 2273 2225 2610 -678 522 -731 C ATOM 72 CD1 TYR A 12 6.473 -51.100 4.028 1.00 19.73 C ANISOU 72 CD1 TYR A 12 2393 2372 2733 -706 535 -746 C ATOM 73 CD2 TYR A 12 6.138 -49.507 5.764 1.00 17.74 C ANISOU 73 CD2 TYR A 12 2163 2107 2469 -660 529 -705 C ATOM 74 CE1 TYR A 12 6.241 -50.128 3.081 1.00 18.96 C ANISOU 74 CE1 TYR A 12 2298 2296 2611 -716 556 -735 C ATOM 75 CE2 TYR A 12 5.887 -48.528 4.829 1.00 21.09 C ANISOU 75 CE2 TYR A 12 2591 2553 2869 -670 550 -694 C ATOM 76 CZ TYR A 12 5.938 -48.849 3.485 1.00 16.76 C ANISOU 76 CZ TYR A 12 2033 2022 2315 -697 563 -709 C ATOM 77 OH TYR A 12 5.705 -47.877 2.541 1.00 22.86 O ANISOU 77 OH TYR A 12 2808 2815 3064 -707 583 -699 O ATOM 78 N THR A 13 5.373 -55.095 7.495 1.00 19.83 N ANISOU 78 N THR A 13 2396 2342 2799 -670 451 -729 N ATOM 79 CA THR A 13 5.482 -55.969 8.655 1.00 22.60 C ANISOU 79 CA THR A 13 2745 2671 3172 -656 428 -732 C ATOM 80 C THR A 13 6.719 -56.847 8.586 1.00 25.56 C ANISOU 80 C THR A 13 3108 3019 3583 -666 421 -776 C ATOM 81 O THR A 13 7.417 -57.034 9.587 1.00 24.25 O ANISOU 81 O THR A 13 2944 2827 3443 -651 408 -789 O ATOM 82 CB THR A 13 4.245 -56.876 8.814 1.00 20.97 C ANISOU 82 CB THR A 13 2535 2481 2950 -658 415 -704 C ATOM 83 OG1 THR A 13 3.054 -56.090 8.692 1.00 26.40 O ANISOU 83 OG1 THR A 13 3232 3196 3601 -652 423 -664 O ATOM 84 CG2 THR A 13 4.268 -57.546 10.168 1.00 18.64 C ANISOU 84 CG2 THR A 13 2241 2165 2674 -639 391 -700 C ATOM 85 N ASP A 14 7.000 -57.363 7.393 1.00 25.50 N ANISOU 85 N ASP A 14 3469 2039 4180 -271 566 -1070 N ATOM 86 CA ASP A 14 8.052 -58.358 7.223 1.00 28.16 C ANISOU 86 CA ASP A 14 3792 2362 4546 -223 643 -1099 C ATOM 87 C ASP A 14 9.233 -57.872 6.392 1.00 23.39 C ANISOU 87 C ASP A 14 3131 1840 3917 -248 629 -1101 C ATOM 88 O ASP A 14 9.986 -58.690 5.854 1.00 20.94 O ANISOU 88 O ASP A 14 2805 1531 3619 -234 699 -1140 O ATOM 89 CB ASP A 14 7.484 -59.634 6.594 1.00 38.57 C ANISOU 89 CB ASP A 14 5141 3635 5878 -246 740 -1168 C ATOM 90 CG ASP A 14 6.515 -60.358 7.517 1.00 43.55 C ANISOU 90 CG ASP A 14 5828 4175 6545 -204 770 -1167 C ATOM 91 OD1 ASP A 14 6.987 -61.012 8.472 1.00 44.76 O ANISOU 91 OD1 ASP A 14 5996 4269 6740 -114 800 -1150 O ATOM 92 OD2 ASP A 14 5.290 -60.274 7.284 1.00 38.57 O ANISOU 92 OD2 ASP A 14 5227 3530 5899 -259 763 -1184 O ATOM 93 N VAL A 15 9.409 -56.558 6.296 1.00 22.43 N ANISOU 93 N VAL A 15 2978 1785 3760 -282 540 -1060 N ATOM 94 CA VAL A 15 10.496 -56.020 5.487 1.00 22.29 C ANISOU 94 CA VAL A 15 2906 1849 3715 -310 522 -1060 C ATOM 95 C VAL A 15 11.853 -56.585 5.890 1.00 24.88 C ANISOU 95 C VAL A 15 3210 2167 4078 -228 560 -1052 C ATOM 96 O VAL A 15 12.652 -56.938 5.027 1.00 26.13 O ANISOU 96 O VAL A 15 3337 2362 4230 -245 605 -1086 O ATOM 97 CB VAL A 15 10.549 -54.476 5.535 1.00 24.94 C ANISOU 97 CB VAL A 15 3212 2252 4012 -347 413 -1007 C ATOM 98 CG1 VAL A 15 9.453 -53.872 4.667 1.00 18.51 C ANISOU 98 CG1 VAL A 15 2406 1475 3153 -449 382 -1029 C ATOM 99 CG2 VAL A 15 10.416 -54.002 6.957 1.00 35.48 C ANISOU 99 CG2 VAL A 15 4565 3547 5369 -277 353 -943 C ATOM 100 N ASN A 16 12.122 -56.667 7.190 1.00 24.52 N ANISOU 100 N ASN A 16 3178 2070 4069 -139 543 -1006 N ATOM 101 CA ASN A 16 13.408 -57.186 7.659 1.00 27.34 C ANISOU 101 CA ASN A 16 3513 2413 4461 -57 575 -994 C ATOM 102 C ASN A 16 13.463 -58.705 7.613 1.00 29.82 C ANISOU 102 C ASN A 16 3853 2662 4813 -17 682 -1045 C ATOM 103 O ASN A 16 14.539 -59.292 7.465 1.00 31.81 O ANISOU 103 O ASN A 16 4082 2919 5086 24 730 -1060 O ATOM 104 CB ASN A 16 13.731 -56.692 9.072 1.00 23.17 C ANISOU 104 CB ASN A 16 2990 1856 3958 25 514 -925 C ATOM 105 CG ASN A 16 14.065 -55.224 9.109 1.00 22.63 C ANISOU 105 CG ASN A 16 2885 1858 3854 -1 412 -872 C ATOM 106 OD1 ASN A 16 14.844 -54.740 8.294 1.00 24.80 O ANISOU 106 OD1 ASN A 16 3113 2207 4104 -39 397 -877 O ATOM 107 ND2 ASN A 16 13.463 -54.498 10.043 1.00 17.96 N ANISOU 107 ND2 ASN A 16 2315 1246 3262 17 340 -821 N ATOM 108 N THR A 17 12.298 -59.332 7.744 1.00 34.34 N ANISOU 108 N THR A 17 4476 3175 5396 -30 718 -1072 N ATOM 109 CA THR A 17 12.194 -60.784 7.694 1.00 33.88 C ANISOU 109 CA THR A 17 4448 3050 5373 2 819 -1123 C ATOM 110 C THR A 17 12.802 -61.307 6.399 1.00 34.28 C ANISOU 110 C THR A 17 4470 3144 5409 -42 883 -1180 C ATOM 111 O THR A 17 13.375 -62.394 6.363 1.00 41.50 O ANISOU 111 O THR A 17 5388 4024 6355 4 961 -1212 O ATOM 112 CB THR A 17 10.718 -61.231 7.783 1.00 30.25 C ANISOU 112 CB THR A 17 4043 2534 4916 -29 843 -1148 C ATOM 113 OG1 THR A 17 10.090 -60.625 8.924 1.00 39.37 O ANISOU 113 OG1 THR A 17 5224 3655 6079 3 777 -1093 O ATOM 114 CG2 THR A 17 10.617 -62.750 7.882 1.00 31.13 C ANISOU 114 CG2 THR A 17 4189 2569 5068 14 945 -1195 C ATOM 115 N HIS A 18 12.694 -60.512 5.342 1.00 32.28 N ANISOU 115 N HIS A 18 4187 2968 5108 -129 847 -1193 N ATOM 116 CA HIS A 18 13.097 -60.948 4.008 1.00 36.98 C ANISOU 116 CA HIS A 18 4759 3608 5684 -184 905 -1250 C ATOM 117 C HIS A 18 14.301 -60.203 3.431 1.00 35.82 C ANISOU 117 C HIS A 18 4552 3547 5513 -200 871 -1235 C ATOM 118 O HIS A 18 14.665 -60.401 2.272 1.00 33.08 O ANISOU 118 O HIS A 18 4179 3246 5143 -251 909 -1279 O ATOM 119 CB HIS A 18 11.904 -60.867 3.061 1.00 37.24 C ANISOU 119 CB HIS A 18 4813 3656 5682 -282 911 -1292 C ATOM 120 CG HIS A 18 10.808 -61.825 3.409 1.00 38.02 C ANISOU 120 CG HIS A 18 4968 3670 5806 -271 964 -1322 C ATOM 121 ND1 HIS A 18 9.590 -61.419 3.913 1.00 34.86 N ANISOU 121 ND1 HIS A 18 4605 3241 5401 -292 921 -1302 N ATOM 122 CD2 HIS A 18 10.758 -63.177 3.347 1.00 35.48 C ANISOU 122 CD2 HIS A 18 4674 3288 5517 -240 1058 -1369 C ATOM 123 CE1 HIS A 18 8.830 -62.480 4.128 1.00 35.92 C ANISOU 123 CE1 HIS A 18 4785 3301 5563 -276 986 -1336 C ATOM 124 NE2 HIS A 18 9.516 -63.558 3.791 1.00 35.59 N ANISOU 124 NE2 HIS A 18 4740 3239 5545 -245 1069 -1377 N ATOM 125 N ARG A 19 14.903 -59.344 4.247 1.00 36.48 N ANISOU 125 N ARG A 19 4611 3649 5600 -155 799 -1171 N ATOM 126 CA ARG A 19 16.174 -58.707 3.911 1.00 32.17 C ANISOU 126 CA ARG A 19 4007 3175 5040 -152 768 -1150 C ATOM 127 C ARG A 19 17.295 -59.661 4.277 1.00 34.10 C ANISOU 127 C ARG A 19 4240 3388 5327 -67 832 -1158 C ATOM 128 O ARG A 19 17.129 -60.485 5.172 1.00 32.12 O ANISOU 128 O ARG A 19 4025 3059 5119 4 870 -1155 O ATOM 129 CB ARG A 19 16.353 -57.415 4.714 1.00 27.42 C ANISOU 129 CB ARG A 19 3388 2603 4428 -134 663 -1076 C ATOM 130 CG ARG A 19 15.479 -56.258 4.275 1.00 33.58 C ANISOU 130 CG ARG A 19 4167 3432 5159 -220 586 -1062 C ATOM 131 CD ARG A 19 16.222 -55.352 3.330 1.00 38.85 C ANISOU 131 CD ARG A 19 4780 4196 5786 -278 546 -1057 C ATOM 132 NE ARG A 19 15.389 -54.281 2.794 1.00 42.19 N ANISOU 132 NE ARG A 19 5201 4668 6159 -366 477 -1049 N ATOM 133 CZ ARG A 19 15.812 -53.412 1.882 1.00 44.31 C ANISOU 133 CZ ARG A 19 5427 5023 6385 -431 437 -1047 C ATOM 134 NH1 ARG A 19 17.053 -53.494 1.411 1.00 41.81 N ANISOU 134 NH1 ARG A 19 5065 4751 6069 -419 459 -1053 N ATOM 135 NH2 ARG A 19 15.001 -52.469 1.432 1.00 40.28 N ANISOU 135 NH2 ARG A 19 4919 4553 5832 -510 375 -1040 N ATOM 136 N PRO A 20 18.455 -59.541 3.603 1.00 34.02 N ANISOU 136 N PRO A 20 4181 3439 5308 -73 844 -1166 N ATOM 137 CA PRO A 20 19.609 -60.329 4.042 1.00 34.71 C ANISOU 137 CA PRO A 20 4252 3500 5436 12 896 -1166 C ATOM 138 C PRO A 20 19.906 -60.020 5.504 1.00 37.28 C ANISOU 138 C PRO A 20 4585 3786 5795 100 845 -1101 C ATOM 139 O PRO A 20 19.670 -58.899 5.955 1.00 30.21 O ANISOU 139 O PRO A 20 3682 2916 4880 88 756 -1050 O ATOM 140 CB PRO A 20 20.755 -59.812 3.162 1.00 33.68 C ANISOU 140 CB PRO A 20 4059 3457 5281 -17 885 -1168 C ATOM 141 CG PRO A 20 20.107 -59.121 2.020 1.00 36.39 C ANISOU 141 CG PRO A 20 4394 3863 5571 -126 857 -1191 C ATOM 142 CD PRO A 20 18.797 -58.598 2.524 1.00 31.96 C ANISOU 142 CD PRO A 20 3873 3273 4998 -153 803 -1169 C ATOM 143 N ARG A 21 20.419 -61.005 6.230 1.00 37.42 N ANISOU 143 N ARG A 21 4617 3741 5861 188 900 -1104 N ATOM 144 CA ARG A 21 20.750 -60.838 7.641 1.00 36.04 C ANISOU 144 CA ARG A 21 4451 3521 5720 278 859 -1046 C ATOM 145 C ARG A 21 21.672 -59.640 7.898 1.00 32.18 C ANISOU 145 C ARG A 21 3912 3097 5217 289 775 -987 C ATOM 146 O ARG A 21 21.509 -58.937 8.888 1.00 30.57 O ANISOU 146 O ARG A 21 3718 2879 5019 323 703 -930 O ATOM 147 CB ARG A 21 21.373 -62.126 8.183 1.00 40.30 C ANISOU 147 CB ARG A 21 5005 3995 6313 367 939 -1064 C ATOM 148 CG ARG A 21 21.677 -62.128 9.669 1.00 42.05 C ANISOU 148 CG ARG A 21 5242 4160 6574 466 909 -1009 C ATOM 149 CD ARG A 21 21.910 -63.551 10.157 1.00 50.92 C ANISOU 149 CD ARG A 21 6395 5203 7747 543 997 -1038 C ATOM 150 NE ARG A 21 22.545 -63.597 11.472 1.00 59.73 N ANISOU 150 NE ARG A 21 7516 6276 8904 643 974 -987 N ATOM 151 CZ ARG A 21 21.925 -63.936 12.599 1.00 65.53 C ANISOU 151 CZ ARG A 21 8299 6932 9668 700 971 -965 C ATOM 152 NH1 ARG A 21 20.638 -64.264 12.586 1.00 68.26 N ANISOU 152 NH1 ARG A 21 8693 7234 10008 666 990 -988 N ATOM 153 NH2 ARG A 21 22.597 -63.951 13.743 1.00 65.89 N ANISOU 153 NH2 ARG A 21 8344 6943 9748 791 948 -919 N ATOM 154 N GLU A 22 22.639 -59.413 7.011 1.00 26.59 N ANISOU 154 N GLU A 22 3152 2459 4491 261 782 -1001 N ATOM 155 CA GLU A 22 23.559 -58.283 7.140 1.00 27.88 C ANISOU 155 CA GLU A 22 3264 2689 4639 266 705 -949 C ATOM 156 C GLU A 22 22.824 -56.942 7.224 1.00 26.97 C ANISOU 156 C GLU A 22 3149 2613 4484 209 606 -908 C ATOM 157 O GLU A 22 23.340 -55.981 7.798 1.00 29.49 O ANISOU 157 O GLU A 22 3443 2962 4799 232 528 -850 O ATOM 158 CB GLU A 22 24.540 -58.252 5.963 1.00 29.37 C ANISOU 158 CB GLU A 22 3399 2953 4807 226 733 -979 C ATOM 159 CG GLU A 22 23.853 -58.257 4.602 1.00 47.78 C ANISOU 159 CG GLU A 22 5732 5326 7096 123 761 -1034 C ATOM 160 CD GLU A 22 24.822 -58.191 3.430 1.00 62.08 C ANISOU 160 CD GLU A 22 7489 7212 8885 82 788 -1062 C ATOM 161 OE1 GLU A 22 26.051 -58.129 3.664 1.00 61.20 O ANISOU 161 OE1 GLU A 22 7337 7123 8791 134 785 -1039 O ATOM 162 OE2 GLU A 22 24.347 -58.200 2.270 1.00 65.47 O ANISOU 162 OE2 GLU A 22 7917 7678 9278 -2 812 -1108 O ATOM 163 N TYR A 23 21.627 -56.875 6.644 1.00 24.08 N ANISOU 163 N TYR A 23 2814 2247 4090 134 609 -938 N ATOM 164 CA TYR A 23 20.863 -55.632 6.635 1.00 18.77 C ANISOU 164 CA TYR A 23 2143 1612 3378 74 518 -904 C ATOM 165 C TYR A 23 20.475 -55.171 8.042 1.00 22.62 C ANISOU 165 C TYR A 23 2658 2051 3884 134 454 -843 C ATOM 166 O TYR A 23 20.655 -54.005 8.389 1.00 21.90 O ANISOU 166 O TYR A 23 2546 2000 3774 127 365 -790 O ATOM 167 CB TYR A 23 19.615 -55.749 5.751 1.00 19.50 C ANISOU 167 CB TYR A 23 2264 1707 3438 -15 540 -951 C ATOM 168 CG TYR A 23 18.807 -54.468 5.689 1.00 20.47 C ANISOU 168 CG TYR A 23 2389 1870 3518 -80 448 -919 C ATOM 169 CD1 TYR A 23 19.171 -53.446 4.831 1.00 24.15 C ANISOU 169 CD1 TYR A 23 2811 2426 3940 -149 396 -911 C ATOM 170 CD2 TYR A 23 17.690 -54.278 6.500 1.00 19.19 C ANISOU 170 CD2 TYR A 23 2273 1656 3361 -71 412 -895 C ATOM 171 CE1 TYR A 23 18.454 -52.260 4.772 1.00 18.81 C ANISOU 171 CE1 TYR A 23 2136 1786 3224 -208 310 -880 C ATOM 172 CE2 TYR A 23 16.961 -53.090 6.454 1.00 17.09 C ANISOU 172 CE2 TYR A 23 2008 1427 3057 -129 326 -865 C ATOM 173 CZ TYR A 23 17.351 -52.083 5.582 1.00 17.84 C ANISOU 173 CZ TYR A 23 2059 1612 3108 -198 275 -857 C ATOM 174 OH TYR A 23 16.655 -50.893 5.497 1.00 17.48 O ANISOU 174 OH TYR A 23 2013 1606 3022 -257 189 -828 O ATOM 175 N TRP A 24 19.940 -56.087 8.844 1.00 21.93 N ANISOU 175 N TRP A 24 2620 1877 3835 191 499 -852 N ATOM 176 CA TRP A 24 19.401 -55.725 10.162 1.00 21.58 C ANISOU 176 CA TRP A 24 2610 1780 3809 243 444 -799 C ATOM 177 C TRP A 24 20.253 -56.195 11.353 1.00 22.11 C ANISOU 177 C TRP A 24 2679 1795 3925 355 454 -765 C ATOM 178 O TRP A 24 20.078 -55.721 12.479 1.00 19.22 O ANISOU 178 O TRP A 24 2332 1398 3573 404 396 -711 O ATOM 179 CB TRP A 24 17.965 -56.241 10.304 1.00 20.96 C ANISOU 179 CB TRP A 24 2590 1640 3734 221 472 -825 C ATOM 180 CG TRP A 24 17.844 -57.693 10.030 1.00 20.25 C ANISOU 180 CG TRP A 24 2526 1494 3673 240 579 -885 C ATOM 181 CD1 TRP A 24 17.385 -58.281 8.882 1.00 27.80 C ANISOU 181 CD1 TRP A 24 3489 2463 4612 173 642 -949 C ATOM 182 CD2 TRP A 24 18.205 -58.760 10.910 1.00 21.59 C ANISOU 182 CD2 TRP A 24 2721 1587 3894 334 637 -886 C ATOM 183 NE1 TRP A 24 17.437 -59.651 9.000 1.00 28.10 N ANISOU 183 NE1 TRP A 24 3553 2435 4688 219 736 -990 N ATOM 184 CE2 TRP A 24 17.932 -59.969 10.238 1.00 25.70 C ANISOU 184 CE2 TRP A 24 3262 2077 4427 318 734 -952 C ATOM 185 CE3 TRP A 24 18.724 -58.812 12.205 1.00 21.98 C ANISOU 185 CE3 TRP A 24 2779 1592 3982 430 615 -837 C ATOM 186 CZ2 TRP A 24 18.166 -61.215 10.819 1.00 32.78 C ANISOU 186 CZ2 TRP A 24 4186 2898 5372 395 809 -971 C ATOM 187 CZ3 TRP A 24 18.957 -60.051 12.780 1.00 23.29 C ANISOU 187 CZ3 TRP A 24 2972 1683 4195 506 690 -856 C ATOM 188 CH2 TRP A 24 18.673 -61.234 12.088 1.00 32.48 C ANISOU 188 CH2 TRP A 24 4155 2817 5370 488 786 -922 C ATOM 189 N ASP A 25 21.167 -57.130 11.108 1.00 25.51 N ANISOU 189 N ASP A 25 3094 2216 4384 395 528 -795 N ATOM 190 CA ASP A 25 22.022 -57.664 12.168 1.00 23.59 C ANISOU 190 CA ASP A 25 2852 1924 4189 501 544 -768 C ATOM 191 C ASP A 25 23.178 -56.701 12.412 1.00 21.98 C ANISOU 191 C ASP A 25 2595 1778 3979 525 474 -716 C ATOM 192 O ASP A 25 24.328 -56.996 12.075 1.00 25.57 O ANISOU 192 O ASP A 25 3010 2260 4445 549 506 -726 O ATOM 193 CB ASP A 25 22.538 -59.051 11.778 1.00 26.72 C ANISOU 193 CB ASP A 25 3250 2287 4617 533 651 -823 C ATOM 194 CG ASP A 25 23.374 -59.709 12.871 1.00 29.58 C ANISOU 194 CG ASP A 25 3618 2591 5031 644 675 -799 C ATOM 195 OD1 ASP A 25 23.339 -59.260 14.035 1.00 34.11 O ANISOU 195 OD1 ASP A 25 4207 3134 5621 700 618 -744 O ATOM 196 OD2 ASP A 25 24.069 -60.696 12.560 1.00 39.64 O ANISOU 196 OD2 ASP A 25 4882 3851 6330 676 753 -837 O ATOM 197 N TYR A 26 22.863 -55.547 12.991 1.00 19.11 N ANISOU 197 N TYR A 26 2232 1433 3597 518 379 -660 N ATOM 198 CA TYR A 26 23.839 -54.474 13.156 1.00 24.13 C ANISOU 198 CA TYR A 26 2819 2131 4220 528 302 -608 C ATOM 199 C TYR A 26 24.998 -54.829 14.081 1.00 26.18 C ANISOU 199 C TYR A 26 3063 2361 4524 630 309 -576 C ATOM 200 O TYR A 26 26.073 -54.239 13.984 1.00 25.78 O ANISOU 200 O TYR A 26 2962 2365 4468 640 271 -548 O ATOM 201 CB TYR A 26 23.165 -53.187 13.635 1.00 25.24 C ANISOU 201 CB TYR A 26 2968 2291 4331 499 199 -555 C ATOM 202 CG TYR A 26 22.463 -53.309 14.971 1.00 29.33 C ANISOU 202 CG TYR A 26 3537 2730 4875 562 176 -520 C ATOM 203 CD1 TYR A 26 23.164 -53.170 16.161 1.00 25.55 C ANISOU 203 CD1 TYR A 26 3057 2221 4429 653 141 -467 C ATOM 204 CD2 TYR A 26 21.096 -53.553 15.039 1.00 28.83 C ANISOU 204 CD2 TYR A 26 3526 2622 4806 531 189 -539 C ATOM 205 CE1 TYR A 26 22.523 -53.272 17.385 1.00 30.86 C ANISOU 205 CE1 TYR A 26 3779 2821 5126 711 120 -434 C ATOM 206 CE2 TYR A 26 20.447 -53.655 16.261 1.00 31.11 C ANISOU 206 CE2 TYR A 26 3862 2839 5119 589 169 -507 C ATOM 207 CZ TYR A 26 21.169 -53.517 17.427 1.00 32.80 C ANISOU 207 CZ TYR A 26 4074 3024 5363 678 135 -454 C ATOM 208 OH TYR A 26 20.534 -53.616 18.640 1.00 46.14 O ANISOU 208 OH TYR A 26 5813 4643 7077 736 115 -422 O ATOM 209 N GLU A 27 24.781 -55.787 14.975 1.00 30.09 N ANISOU 209 N GLU A 27 3601 2769 5062 704 355 -580 N ATOM 210 CA GLU A 27 25.817 -56.172 15.926 1.00 33.50 C ANISOU 210 CA GLU A 27 4024 3166 5539 805 362 -549 C ATOM 211 C GLU A 27 27.064 -56.717 15.227 1.00 34.74 C ANISOU 211 C GLU A 27 4134 3359 5708 818 419 -579 C ATOM 212 O GLU A 27 28.171 -56.640 15.770 1.00 31.43 O ANISOU 212 O GLU A 27 3686 2944 5314 883 403 -547 O ATOM 213 CB GLU A 27 25.273 -57.172 16.952 1.00 39.01 C ANISOU 213 CB GLU A 27 4781 3763 6280 879 409 -553 C ATOM 214 CG GLU A 27 24.503 -56.523 18.096 1.00 41.96 C ANISOU 214 CG GLU A 27 5192 4096 6653 906 336 -499 C ATOM 215 CD GLU A 27 23.580 -57.496 18.817 1.00 51.75 C ANISOU 215 CD GLU A 27 6497 5241 7924 948 387 -515 C ATOM 216 OE1 GLU A 27 22.369 -57.520 18.497 1.00 59.76 O ANISOU 216 OE1 GLU A 27 7545 6242 8918 891 395 -539 O ATOM 217 OE2 GLU A 27 24.059 -58.232 19.705 1.00 53.70 O ANISOU 217 OE2 GLU A 27 6761 5427 8216 1037 419 -504 O ATOM 218 N SER A 28 26.886 -57.236 14.014 1.00 30.96 N ANISOU 218 N SER A 28 3646 2906 5211 754 484 -641 N ATOM 219 CA SER A 28 27.990 -57.828 13.269 1.00 36.58 C ANISOU 219 CA SER A 28 4316 3650 5933 761 546 -676 C ATOM 220 C SER A 28 28.534 -56.868 12.216 1.00 30.71 C ANISOU 220 C SER A 28 3514 3008 5146 687 505 -674 C ATOM 221 O SER A 28 29.439 -57.215 11.458 1.00 32.55 O ANISOU 221 O SER A 28 3707 3280 5380 680 550 -703 O ATOM 222 CB SER A 28 27.553 -59.137 12.608 1.00 44.54 C ANISOU 222 CB SER A 28 5352 4619 6952 746 652 -748 C ATOM 223 OG SER A 28 26.789 -58.886 11.439 1.00 53.21 O ANISOU 223 OG SER A 28 6449 5761 8006 644 660 -788 O ATOM 224 N HIS A 29 27.977 -55.663 12.173 1.00 25.16 N ANISOU 224 N HIS A 29 2807 2347 4404 631 419 -640 N ATOM 225 CA HIS A 29 28.439 -54.637 11.241 1.00 21.69 C ANISOU 225 CA HIS A 29 2315 2004 3922 559 370 -632 C ATOM 226 C HIS A 29 29.912 -54.280 11.461 1.00 26.62 C ANISOU 226 C HIS A 29 2884 2669 4561 608 344 -597 C ATOM 227 O HIS A 29 30.346 -54.020 12.583 1.00 27.29 O ANISOU 227 O HIS A 29 2971 2726 4674 681 299 -545 O ATOM 228 CB HIS A 29 27.585 -53.373 11.353 1.00 23.44 C ANISOU 228 CB HIS A 29 2546 2256 4104 502 276 -594 C ATOM 229 CG HIS A 29 27.979 -52.301 10.384 1.00 27.70 C ANISOU 229 CG HIS A 29 3034 2894 4598 424 224 -587 C ATOM 230 ND1 HIS A 29 27.807 -52.433 9.024 1.00 25.50 N ANISOU 230 ND1 HIS A 29 2739 2665 4285 341 265 -640 N ATOM 231 CD2 HIS A 29 28.567 -51.096 10.575 1.00 29.49 C ANISOU 231 CD2 HIS A 29 3222 3178 4805 418 135 -532 C ATOM 232 CE1 HIS A 29 28.260 -51.350 8.417 1.00 32.65 C ANISOU 232 CE1 HIS A 29 3598 3655 5154 286 204 -618 C ATOM 233 NE2 HIS A 29 28.725 -50.521 9.336 1.00 30.23 N ANISOU 233 NE2 HIS A 29 3277 3354 4855 331 125 -553 N ATOM 234 N VAL A 30 30.679 -54.267 10.380 1.00 25.27 N ANISOU 234 N VAL A 30 2664 2564 4373 566 372 -626 N ATOM 235 CA VAL A 30 32.069 -53.837 10.449 1.00 27.58 C ANISOU 235 CA VAL A 30 2899 2905 4675 600 344 -594 C ATOM 236 C VAL A 30 32.195 -52.409 9.928 1.00 31.06 C ANISOU 236 C VAL A 30 3299 3434 5068 529 256 -560 C ATOM 237 O VAL A 30 31.979 -52.142 8.742 1.00 31.42 O ANISOU 237 O VAL A 30 3326 3538 5074 443 266 -594 O ATOM 238 CB VAL A 30 32.991 -54.763 9.647 1.00 32.05 C ANISOU 238 CB VAL A 30 3433 3488 5256 609 433 -643 C ATOM 239 CG1 VAL A 30 34.410 -54.192 9.598 1.00 37.88 C ANISOU 239 CG1 VAL A 30 4107 4288 5999 632 399 -610 C ATOM 240 CG2 VAL A 30 32.992 -56.153 10.259 1.00 36.74 C ANISOU 240 CG2 VAL A 30 4064 3994 5900 688 516 -671 C ATOM 241 N VAL A 31 32.548 -51.492 10.821 1.00 26.69 N ANISOU 241 N VAL A 31 2733 2889 4519 566 169 -494 N ATOM 242 CA VAL A 31 32.630 -50.086 10.462 1.00 29.93 C ANISOU 242 CA VAL A 31 3109 3377 4885 504 78 -457 C ATOM 243 C VAL A 31 33.782 -49.805 9.501 1.00 29.17 C ANISOU 243 C VAL A 31 2946 3363 4773 472 86 -467 C ATOM 244 O VAL A 31 34.892 -50.299 9.690 1.00 32.69 O ANISOU 244 O VAL A 31 3363 3807 5253 532 120 -465 O ATOM 245 CB VAL A 31 32.763 -49.203 11.714 1.00 29.72 C ANISOU 245 CB VAL A 31 3086 3336 4869 557 -17 -382 C ATOM 246 CG1 VAL A 31 33.047 -47.759 11.324 1.00 31.63 C ANISOU 246 CG1 VAL A 31 3285 3664 5068 498 -110 -342 C ATOM 247 CG2 VAL A 31 31.494 -49.294 12.554 1.00 31.17 C ANISOU 247 CG2 VAL A 31 3336 3449 5059 573 -35 -370 C ATOM 248 N GLU A 32 33.506 -49.022 8.463 1.00 30.99 N ANISOU 248 N GLU A 32 3154 3667 4954 377 56 -478 N ATOM 249 CA GLU A 32 34.537 -48.569 7.534 1.00 35.78 C ANISOU 249 CA GLU A 32 3697 4359 5539 337 51 -482 C ATOM 250 C GLU A 32 34.983 -47.149 7.904 1.00 36.55 C ANISOU 250 C GLU A 32 3760 4511 5616 329 -59 -415 C ATOM 251 O GLU A 32 34.229 -46.180 7.732 1.00 28.88 O ANISOU 251 O GLU A 32 2798 3569 4605 266 -128 -395 O ATOM 252 CB GLU A 32 34.016 -48.616 6.095 1.00 44.73 C ANISOU 252 CB GLU A 32 4826 5541 6630 236 90 -539 C ATOM 253 CG GLU A 32 35.001 -48.118 5.044 1.00 58.64 C ANISOU 253 CG GLU A 32 6522 7393 8364 187 86 -546 C ATOM 254 CD GLU A 32 34.422 -48.158 3.636 1.00 68.68 C ANISOU 254 CD GLU A 32 7793 8710 9591 86 123 -602 C ATOM 255 OE1 GLU A 32 33.430 -48.891 3.422 1.00 69.49 O ANISOU 255 OE1 GLU A 32 7943 8767 9693 66 176 -646 O ATOM 256 OE2 GLU A 32 34.954 -47.454 2.748 1.00 71.27 O ANISOU 256 OE2 GLU A 32 8074 9121 9885 26 98 -601 O ATOM 257 N TRP A 33 36.207 -47.033 8.415 1.00 28.21 N ANISOU 257 N TRP A 33 2892 3925 3902 74 582 -704 N ATOM 258 CA TRP A 33 36.697 -45.766 8.962 1.00 29.78 C ANISOU 258 CA TRP A 33 3106 4157 4053 41 544 -647 C ATOM 259 C TRP A 33 37.291 -44.837 7.913 1.00 27.70 C ANISOU 259 C TRP A 33 2878 3930 3717 50 466 -611 C ATOM 260 O TRP A 33 38.052 -45.266 7.039 1.00 25.31 O ANISOU 260 O TRP A 33 2593 3660 3365 77 469 -570 O ATOM 261 CB TRP A 33 37.739 -46.023 10.055 1.00 27.02 C ANISOU 261 CB TRP A 33 2751 3849 3664 18 613 -554 C ATOM 262 CG TRP A 33 37.227 -46.906 11.145 1.00 27.32 C ANISOU 262 CG TRP A 33 2756 3855 3768 5 690 -582 C ATOM 263 CD1 TRP A 33 37.440 -48.251 11.282 1.00 28.91 C ANISOU 263 CD1 TRP A 33 2944 4052 3990 22 767 -575 C ATOM 264 CD2 TRP A 33 36.401 -46.516 12.243 1.00 28.69 C ANISOU 264 CD2 TRP A 33 2908 3995 3998 -26 698 -624 C ATOM 265 NE1 TRP A 33 36.798 -48.717 12.404 1.00 28.81 N ANISOU 265 NE1 TRP A 33 2902 4005 4041 2 822 -609 N ATOM 266 CE2 TRP A 33 36.150 -47.673 13.011 1.00 31.32 C ANISOU 266 CE2 TRP A 33 3214 4305 4383 -28 783 -639 C ATOM 267 CE3 TRP A 33 35.839 -45.301 12.650 1.00 27.14 C ANISOU 267 CE3 TRP A 33 2712 3786 3814 -52 642 -651 C ATOM 268 CZ2 TRP A 33 35.365 -47.649 14.163 1.00 37.21 C ANISOU 268 CZ2 TRP A 33 3932 5017 5190 -55 813 -680 C ATOM 269 CZ3 TRP A 33 35.060 -45.281 13.801 1.00 31.89 C ANISOU 269 CZ3 TRP A 33 3286 4354 4477 -78 673 -692 C ATOM 270 CH2 TRP A 33 34.834 -46.446 14.543 1.00 36.40 C ANISOU 270 CH2 TRP A 33 3830 4904 5097 -80 758 -705 C ATOM 271 N GLY A 34 36.958 -43.557 8.018 1.00 19.32 N ANISOU 271 N GLY A 34 1826 2865 2648 29 397 -623 N ATOM 272 CA GLY A 34 37.572 -42.551 7.175 1.00 20.89 C ANISOU 272 CA GLY A 34 2061 3102 2776 31 323 -580 C ATOM 273 C GLY A 34 38.796 -41.952 7.849 1.00 20.68 C ANISOU 273 C GLY A 34 2047 3134 2675 2 334 -470 C ATOM 274 O GLY A 34 39.281 -42.471 8.855 1.00 19.71 O ANISOU 274 O GLY A 34 1909 3027 2552 -13 406 -423 O ATOM 275 N ASN A 35 39.285 -40.850 7.297 1.00 21.08 N ANISOU 275 N ASN A 35 2129 3217 2665 -5 263 -430 N ATOM 276 CA ASN A 35 40.481 -40.203 7.827 1.00 21.01 C ANISOU 276 CA ASN A 35 2135 3266 2581 -31 266 -325 C ATOM 277 C ASN A 35 40.111 -39.067 8.755 1.00 19.67 C ANISOU 277 C ASN A 35 1964 3086 2425 -69 230 -329 C ATOM 278 O ASN A 35 39.546 -38.064 8.329 1.00 19.55 O ANISOU 278 O ASN A 35 1963 3053 2414 -74 150 -369 O ATOM 279 CB ASN A 35 41.362 -39.685 6.696 1.00 31.70 C ANISOU 279 CB ASN A 35 3524 4667 3853 -18 212 -268 C ATOM 280 CG ASN A 35 41.922 -40.801 5.852 1.00 45.33 C ANISOU 280 CG ASN A 35 5254 6415 5556 18 253 -249 C ATOM 281 OD1 ASN A 35 42.064 -41.930 6.320 1.00 43.96 O ANISOU 281 OD1 ASN A 35 5058 6237 5406 27 332 -243 O ATOM 282 ND2 ASN A 35 42.243 -40.498 4.598 1.00 56.99 N ANISOU 282 ND2 ASN A 35 6758 7913 6985 39 198 -239 N ATOM 283 N GLN A 36 40.437 -39.226 10.032 1.00 19.13 N ANISOU 283 N GLN A 36 1878 3028 2362 -95 289 -287 N ATOM 284 CA GLN A 36 40.078 -38.230 11.033 1.00 15.71 C ANISOU 284 CA GLN A 36 1441 2584 1945 -132 263 -292 C ATOM 285 C GLN A 36 40.659 -36.855 10.698 1.00 19.46 C ANISOU 285 C GLN A 36 1948 3095 2353 -149 183 -239 C ATOM 286 O GLN A 36 40.077 -35.830 11.049 1.00 17.88 O ANISOU 286 O GLN A 36 1750 2873 2170 -170 128 -270 O ATOM 287 CB GLN A 36 40.530 -38.708 12.416 1.00 21.17 C ANISOU 287 CB GLN A 36 2112 3289 2642 -155 345 -242 C ATOM 288 CG GLN A 36 40.075 -37.832 13.577 1.00 21.47 C ANISOU 288 CG GLN A 36 2141 3311 2706 -192 330 -253 C ATOM 289 CD GLN A 36 41.051 -36.700 13.877 1.00 21.25 C ANISOU 289 CD GLN A 36 2137 3332 2603 -219 291 -164 C ATOM 290 OE1 GLN A 36 42.212 -36.745 13.473 1.00 23.76 O ANISOU 290 OE1 GLN A 36 2475 3702 2851 -215 296 -80 O ATOM 291 NE2 GLN A 36 40.574 -35.676 14.584 1.00 19.55 N ANISOU 291 NE2 GLN A 36 1921 3102 2405 -247 250 -183 N ATOM 292 N ASP A 37 41.806 -36.835 10.021 1.00 18.94 N ANISOU 292 N ASP A 37 1906 3082 2209 -140 176 -159 N ATOM 293 CA ASP A 37 42.446 -35.578 9.656 1.00 17.14 C ANISOU 293 CA ASP A 37 1709 2891 1912 -156 102 -102 C ATOM 294 C ASP A 37 41.708 -34.792 8.571 1.00 23.36 C ANISOU 294 C ASP A 37 2517 3652 2707 -144 8 -166 C ATOM 295 O ASP A 37 42.053 -33.642 8.309 1.00 24.20 O ANISOU 295 O ASP A 37 2649 3780 2765 -160 -62 -130 O ATOM 296 CB ASP A 37 43.906 -35.808 9.250 1.00 25.11 C ANISOU 296 CB ASP A 37 2738 3967 2836 -151 125 4 C ATOM 297 CG ASP A 37 44.052 -36.918 8.238 1.00 40.71 C ANISOU 297 CG ASP A 37 4713 5946 4809 -111 155 -10 C ATOM 298 OD1 ASP A 37 43.788 -38.085 8.603 1.00 45.25 O ANISOU 298 OD1 ASP A 37 5263 6501 5430 -97 229 -38 O ATOM 299 OD2 ASP A 37 44.420 -36.624 7.078 1.00 50.04 O ANISOU 299 OD2 ASP A 37 5919 7151 5942 -94 106 6 O ATOM 300 N ASP A 38 40.684 -35.392 7.957 1.00 18.40 N ANISOU 300 N ASP A 38 1876 2975 2140 -116 4 -260 N ATOM 301 CA ASP A 38 39.933 -34.694 6.916 1.00 17.82 C ANISOU 301 CA ASP A 38 1821 2874 2077 -102 -85 -325 C ATOM 302 C ASP A 38 39.051 -33.588 7.483 1.00 19.39 C ANISOU 302 C ASP A 38 2017 3036 2313 -127 -144 -376 C ATOM 303 O ASP A 38 38.601 -32.706 6.745 1.00 20.59 O ANISOU 303 O ASP A 38 2190 3174 2461 -124 -229 -413 O ATOM 304 CB ASP A 38 39.047 -35.657 6.124 1.00 21.36 C ANISOU 304 CB ASP A 38 2255 3277 2582 -65 -72 -414 C ATOM 305 CG ASP A 38 39.822 -36.499 5.148 1.00 20.81 C ANISOU 305 CG ASP A 38 2198 3241 2468 -33 -46 -375 C ATOM 306 OD1 ASP A 38 41.054 -36.289 5.012 1.00 19.37 O ANISOU 306 OD1 ASP A 38 2035 3118 2207 -40 -41 -279 O ATOM 307 OD2 ASP A 38 39.193 -37.374 4.512 1.00 22.14 O ANISOU 307 OD2 ASP A 38 2356 3376 2680 -2 -29 -442 O ATOM 308 N TYR A 39 38.792 -33.639 8.788 1.00 17.12 N ANISOU 308 N TYR A 39 1705 2735 2064 -152 -99 -380 N ATOM 309 CA TYR A 39 37.806 -32.746 9.401 1.00 21.33 C ANISOU 309 CA TYR A 39 2230 3228 2646 -173 -145 -442 C ATOM 310 C TYR A 39 38.407 -31.895 10.505 1.00 25.65 C ANISOU 310 C TYR A 39 2783 3805 3160 -211 -147 -373 C ATOM 311 O TYR A 39 39.029 -32.407 11.441 1.00 26.89 O ANISOU 311 O TYR A 39 2925 3985 3306 -226 -73 -317 O ATOM 312 CB TYR A 39 36.600 -33.553 9.906 1.00 17.99 C ANISOU 312 CB TYR A 39 1769 2747 2318 -164 -99 -538 C ATOM 313 CG TYR A 39 36.103 -34.481 8.839 1.00 22.60 C ANISOU 313 CG TYR A 39 2349 3305 2933 -125 -91 -599 C ATOM 314 CD1 TYR A 39 35.264 -34.016 7.829 1.00 17.51 C ANISOU 314 CD1 TYR A 39 1715 2625 2311 -107 -169 -675 C ATOM 315 CD2 TYR A 39 36.515 -35.808 8.797 1.00 22.55 C ANISOU 315 CD2 TYR A 39 2329 3310 2931 -106 -10 -578 C ATOM 316 CE1 TYR A 39 34.838 -34.852 6.825 1.00 18.86 C ANISOU 316 CE1 TYR A 39 1884 2773 2508 -71 -164 -729 C ATOM 317 CE2 TYR A 39 36.089 -36.654 7.794 1.00 17.79 C ANISOU 317 CE2 TYR A 39 1723 2684 2354 -70 -5 -633 C ATOM 318 CZ TYR A 39 35.244 -36.168 6.815 1.00 19.20 C ANISOU 318 CZ TYR A 39 1912 2828 2555 -53 -82 -708 C ATOM 319 OH TYR A 39 34.814 -37.000 5.816 1.00 19.34 O ANISOU 319 OH TYR A 39 1927 2821 2599 -16 -78 -763 O ATOM 320 N GLN A 40 38.242 -30.585 10.364 1.00 20.44 N ANISOU 320 N GLN A 40 2144 3143 2480 -228 -233 -377 N ATOM 321 CA GLN A 40 38.687 -29.645 11.379 1.00 23.33 C ANISOU 321 CA GLN A 40 2516 3531 2818 -265 -246 -321 C ATOM 322 C GLN A 40 37.490 -29.054 12.116 1.00 25.44 C ANISOU 322 C GLN A 40 2765 3747 3153 -280 -275 -403 C ATOM 323 O GLN A 40 36.630 -28.428 11.501 1.00 18.67 O ANISOU 323 O GLN A 40 1916 2855 2322 -271 -349 -474 O ATOM 324 CB GLN A 40 39.509 -28.527 10.738 1.00 34.83 C ANISOU 324 CB GLN A 40 4012 5028 4194 -275 -324 -253 C ATOM 325 CG GLN A 40 40.746 -29.031 10.015 1.00 50.56 C ANISOU 325 CG GLN A 40 6023 7075 6114 -262 -298 -167 C ATOM 326 CD GLN A 40 41.760 -27.934 9.734 1.00 59.10 C ANISOU 326 CD GLN A 40 7140 8206 7111 -282 -358 -79 C ATOM 327 OE1 GLN A 40 42.964 -28.138 9.879 1.00 55.16 O ANISOU 327 OE1 GLN A 40 6648 7760 6550 -290 -321 16 O ATOM 328 NE2 GLN A 40 41.275 -26.766 9.325 1.00 65.49 N ANISOU 328 NE2 GLN A 40 7970 8997 7917 -291 -452 -111 N ATOM 329 N LEU A 41 37.441 -29.246 13.431 1.00 23.57 N ANISOU 329 N LEU A 41 2504 3507 2943 -301 -217 -393 N ATOM 330 CA LEU A 41 36.349 -28.700 14.241 1.00 20.98 C ANISOU 330 CA LEU A 41 2158 3135 2679 -317 -238 -466 C ATOM 331 C LEU A 41 36.390 -27.164 14.297 1.00 19.58 C ANISOU 331 C LEU A 41 2006 2964 2469 -340 -330 -451 C ATOM 332 O LEU A 41 37.447 -26.569 14.485 1.00 19.99 O ANISOU 332 O LEU A 41 2081 3062 2451 -359 -344 -359 O ATOM 333 CB LEU A 41 36.379 -29.295 15.648 1.00 22.01 C ANISOU 333 CB LEU A 41 2258 3265 2840 -336 -150 -451 C ATOM 334 CG LEU A 41 36.328 -30.822 15.735 1.00 16.83 C ANISOU 334 CG LEU A 41 1575 2601 2219 -317 -55 -465 C ATOM 335 CD1 LEU A 41 36.442 -31.290 17.182 1.00 21.71 C ANISOU 335 CD1 LEU A 41 2167 3222 2860 -340 27 -441 C ATOM 336 CD2 LEU A 41 35.065 -31.354 15.093 1.00 21.48 C ANISOU 336 CD2 LEU A 41 2145 3134 2882 -290 -64 -577 C ATOM 337 N VAL A 42 35.236 -26.533 14.102 1.00 19.54 N ANISOU 337 N VAL A 42 1998 2912 2514 -336 -394 -542 N ATOM 338 CA VAL A 42 35.135 -25.075 14.052 1.00 20.83 C ANISOU 338 CA VAL A 42 2187 3075 2654 -354 -489 -541 C ATOM 339 C VAL A 42 34.472 -24.500 15.310 1.00 21.04 C ANISOU 339 C VAL A 42 2194 3076 2725 -379 -490 -577 C ATOM 340 O VAL A 42 34.941 -23.519 15.876 1.00 23.99 O ANISOU 340 O VAL A 42 2584 3472 3060 -405 -525 -526 O ATOM 341 CB VAL A 42 34.335 -24.623 12.808 1.00 23.88 C ANISOU 341 CB VAL A 42 2589 3427 3058 -331 -575 -617 C ATOM 342 CG1 VAL A 42 34.177 -23.108 12.793 1.00 31.16 C ANISOU 342 CG1 VAL A 42 3537 4345 3959 -350 -675 -619 C ATOM 343 CG2 VAL A 42 35.024 -25.100 11.544 1.00 26.27 C ANISOU 343 CG2 VAL A 42 2913 3757 3311 -307 -580 -578 C ATOM 344 N ARG A 43 33.359 -25.094 15.729 1.00 22.92 N ANISOU 344 N ARG A 43 2396 3267 3044 -370 -453 -667 N ATOM 345 CA ARG A 43 32.715 -24.661 16.959 1.00 24.76 C ANISOU 345 CA ARG A 43 2608 3477 3322 -392 -445 -704 C ATOM 346 C ARG A 43 31.737 -25.689 17.493 1.00 21.65 C ANISOU 346 C ARG A 43 2171 3044 3012 -383 -373 -783 C ATOM 347 O ARG A 43 31.151 -26.448 16.732 1.00 22.81 O ANISOU 347 O ARG A 43 2306 3163 3198 -356 -362 -844 O ATOM 348 CB ARG A 43 32.010 -23.318 16.766 1.00 27.32 C ANISOU 348 CB ARG A 43 2947 3775 3657 -399 -548 -756 C ATOM 349 CG ARG A 43 30.981 -23.300 15.662 1.00 34.69 C ANISOU 349 CG ARG A 43 3881 4665 4635 -371 -606 -852 C ATOM 350 CD ARG A 43 30.017 -22.147 15.890 1.00 42.48 C ANISOU 350 CD ARG A 43 4868 5614 5657 -380 -687 -924 C ATOM 351 NE ARG A 43 29.701 -21.445 14.653 1.00 56.71 N ANISOU 351 NE ARG A 43 6699 7401 7447 -363 -784 -959 N ATOM 352 CZ ARG A 43 28.484 -21.368 14.124 1.00 63.47 C ANISOU 352 CZ ARG A 43 7544 8207 8366 -344 -828 -1066 C ATOM 353 NH1 ARG A 43 27.453 -21.950 14.728 1.00 58.93 N ANISOU 353 NH1 ARG A 43 6929 7593 7871 -339 -783 -1148 N ATOM 354 NH2 ARG A 43 28.296 -20.702 12.993 1.00 69.65 N ANISOU 354 NH2 ARG A 43 8356 8979 9130 -330 -918 -1090 N ATOM 355 N LYS A 44 31.572 -25.709 18.812 1.00 17.42 N ANISOU 355 N LYS A 44 1612 2504 2502 -405 -325 -782 N ATOM 356 CA LYS A 44 30.643 -26.631 19.444 1.00 21.28 C ANISOU 356 CA LYS A 44 2059 2956 3071 -400 -255 -855 C ATOM 357 C LYS A 44 29.227 -26.110 19.235 1.00 21.78 C ANISOU 357 C LYS A 44 2108 2964 3202 -392 -315 -971 C ATOM 358 O LYS A 44 28.940 -24.967 19.552 1.00 23.47 O ANISOU 358 O LYS A 44 2332 3172 3414 -407 -380 -986 O ATOM 359 CB LYS A 44 30.944 -26.746 20.947 1.00 21.45 C ANISOU 359 CB LYS A 44 2062 2992 3095 -429 -187 -813 C ATOM 360 CG LYS A 44 30.318 -27.960 21.615 1.00 21.19 C ANISOU 360 CG LYS A 44 1988 2934 3130 -425 -94 -861 C ATOM 361 CD LYS A 44 30.501 -27.949 23.131 1.00 35.38 C ANISOU 361 CD LYS A 44 3768 4742 4933 -454 -35 -828 C ATOM 362 CE LYS A 44 31.946 -28.202 23.520 1.00 45.21 C ANISOU 362 CE LYS A 44 5030 6042 6105 -468 13 -708 C ATOM 363 NZ LYS A 44 32.201 -28.024 24.985 1.00 48.12 N ANISOU 363 NZ LYS A 44 5387 6425 6471 -498 59 -669 N ATOM 364 N LEU A 45 28.342 -26.939 18.695 1.00 18.06 N ANISOU 364 N LEU A 45 1614 2454 2792 -367 -295 -1053 N ATOM 365 CA LEU A 45 26.960 -26.503 18.506 1.00 21.60 C ANISOU 365 CA LEU A 45 2047 2850 3311 -358 -349 -1166 C ATOM 366 C LEU A 45 26.112 -26.868 19.720 1.00 23.72 C ANISOU 366 C LEU A 45 2273 3091 3650 -371 -290 -1223 C ATOM 367 O LEU A 45 25.174 -26.149 20.086 1.00 26.91 O ANISOU 367 O LEU A 45 2664 3463 4097 -378 -334 -1294 O ATOM 368 CB LEU A 45 26.374 -27.107 17.242 1.00 18.66 C ANISOU 368 CB LEU A 45 1672 2448 2970 -324 -369 -1232 C ATOM 369 CG LEU A 45 27.060 -26.735 15.927 1.00 21.04 C ANISOU 369 CG LEU A 45 2015 2773 3208 -308 -434 -1189 C ATOM 370 CD1 LEU A 45 26.280 -27.303 14.759 1.00 25.65 C ANISOU 370 CD1 LEU A 45 2593 3319 3834 -274 -455 -1270 C ATOM 371 CD2 LEU A 45 27.182 -25.232 15.792 1.00 25.51 C ANISOU 371 CD2 LEU A 45 2612 3347 3734 -322 -533 -1174 C ATOM 372 N GLY A 46 26.450 -27.981 20.357 1.00 25.86 N ANISOU 372 N GLY A 46 2522 3373 3930 -376 -191 -1192 N ATOM 373 CA GLY A 46 25.697 -28.415 21.512 1.00 29.67 C ANISOU 373 CA GLY A 46 2964 3831 4477 -390 -128 -1240 C ATOM 374 C GLY A 46 26.109 -29.772 22.036 1.00 27.87 C ANISOU 374 C GLY A 46 2716 3615 4259 -391 -17 -1204 C ATOM 375 O GLY A 46 26.994 -30.427 21.499 1.00 24.72 O ANISOU 375 O GLY A 46 2332 3243 3816 -380 13 -1141 O ATOM 376 N ARG A 47 25.423 -30.196 23.088 1.00 29.31 N ANISOU 376 N ARG A 47 2862 3775 4501 -404 42 -1248 N ATOM 377 CA ARG A 47 25.749 -31.420 23.783 1.00 33.06 C ANISOU 377 CA ARG A 47 3314 4259 4987 -410 148 -1215 C ATOM 378 C ARG A 47 24.461 -32.132 24.150 1.00 36.27 C ANISOU 378 C ARG A 47 3677 4617 5486 -406 191 -1316 C ATOM 379 O ARG A 47 23.528 -31.508 24.652 1.00 37.40 O ANISOU 379 O ARG A 47 3802 4732 5675 -416 163 -1384 O ATOM 380 CB ARG A 47 26.542 -31.090 25.050 1.00 32.66 C ANISOU 380 CB ARG A 47 3268 4244 4896 -442 187 -1134 C ATOM 381 CG ARG A 47 26.839 -32.287 25.915 1.00 41.28 C ANISOU 381 CG ARG A 47 4337 5345 6004 -451 297 -1102 C ATOM 382 CD ARG A 47 28.247 -32.213 26.464 1.00 50.96 C ANISOU 382 CD ARG A 47 5586 6625 7152 -469 329 -982 C ATOM 383 NE ARG A 47 28.286 -31.582 27.774 1.00 57.17 N ANISOU 383 NE ARG A 47 6366 7422 7935 -499 342 -960 N ATOM 384 CZ ARG A 47 29.381 -31.070 28.330 1.00 55.87 C ANISOU 384 CZ ARG A 47 6225 7301 7703 -519 344 -864 C ATOM 385 NH1 ARG A 47 30.544 -31.094 27.688 1.00 47.52 N ANISOU 385 NH1 ARG A 47 5199 6283 6575 -512 332 -779 N ATOM 386 NH2 ARG A 47 29.307 -30.525 29.533 1.00 60.60 N ANISOU 386 NH2 ARG A 47 6816 7904 8304 -545 355 -854 N ATOM 387 N GLY A 48 24.407 -33.430 23.879 1.00 36.61 N ANISOU 387 N GLY A 48 3704 4649 5558 -391 258 -1327 N ATOM 388 CA GLY A 48 23.269 -34.246 24.253 1.00 43.19 C ANISOU 388 CA GLY A 48 4495 5439 6478 -388 309 -1414 C ATOM 389 C GLY A 48 23.695 -35.271 25.280 1.00 43.23 C ANISOU 389 C GLY A 48 4480 5458 6487 -404 417 -1368 C ATOM 390 O GLY A 48 24.866 -35.337 25.638 1.00 43.65 O ANISOU 390 O GLY A 48 4553 5554 6477 -415 448 -1269 O ATOM 391 N LYS A 49 22.750 -36.074 25.756 1.00 47.80 N ANISOU 391 N LYS A 49 5020 6000 7142 -406 473 -1438 N ATOM 392 CA LYS A 49 23.079 -37.111 26.722 1.00 45.40 C ANISOU 392 CA LYS A 49 4697 5706 6848 -421 577 -1399 C ATOM 393 C LYS A 49 24.058 -38.100 26.109 1.00 35.92 C ANISOU 393 C LYS A 49 3512 4528 5606 -404 619 -1331 C ATOM 394 O LYS A 49 24.841 -38.728 26.817 1.00 41.93 O ANISOU 394 O LYS A 49 4275 5316 6341 -418 692 -1260 O ATOM 395 CB LYS A 49 21.813 -37.830 27.215 1.00 51.88 C ANISOU 395 CB LYS A 49 5472 6480 7761 -424 626 -1493 C ATOM 396 CG LYS A 49 20.568 -37.561 26.373 1.00 54.96 C ANISOU 396 CG LYS A 49 5847 6824 8212 -404 563 -1604 C ATOM 397 CD LYS A 49 19.284 -38.049 27.060 1.00 63.39 C ANISOU 397 CD LYS A 49 6868 7849 9370 -413 606 -1697 C ATOM 398 CE LYS A 49 19.201 -39.569 27.129 1.00 66.56 C ANISOU 398 CE LYS A 49 7247 8235 9810 -407 696 -1702 C ATOM 399 NZ LYS A 49 17.842 -40.044 27.535 1.00 67.59 N ANISOU 399 NZ LYS A 49 7330 8317 10032 -411 727 -1804 N ATOM 400 N TYR A 50 24.038 -38.206 24.784 1.00 34.83 N ANISOU 400 N TYR A 50 3390 4382 5461 -375 572 -1352 N ATOM 401 CA TYR A 50 24.788 -39.255 24.100 1.00 35.43 C ANISOU 401 CA TYR A 50 3478 4473 5510 -355 613 -1304 C ATOM 402 C TYR A 50 25.979 -38.786 23.272 1.00 28.57 C ANISOU 402 C TYR A 50 2652 3648 4554 -343 566 -1221 C ATOM 403 O TYR A 50 26.767 -39.608 22.816 1.00 28.32 O ANISOU 403 O TYR A 50 2633 3638 4490 -329 604 -1168 O ATOM 404 CB TYR A 50 23.855 -40.049 23.191 1.00 43.16 C ANISOU 404 CB TYR A 50 4438 5407 6552 -327 611 -1393 C ATOM 405 CG TYR A 50 22.747 -40.756 23.925 1.00 54.97 C ANISOU 405 CG TYR A 50 5890 6861 8134 -336 668 -1470 C ATOM 406 CD1 TYR A 50 23.027 -41.750 24.852 1.00 56.71 C ANISOU 406 CD1 TYR A 50 6093 7087 8367 -351 765 -1436 C ATOM 407 CD2 TYR A 50 21.416 -40.437 23.682 1.00 61.84 C ANISOU 407 CD2 TYR A 50 6737 7684 9074 -330 626 -1579 C ATOM 408 CE1 TYR A 50 22.012 -42.403 25.522 1.00 64.71 C ANISOU 408 CE1 TYR A 50 7066 8062 9459 -361 818 -1506 C ATOM 409 CE2 TYR A 50 20.395 -41.085 24.347 1.00 66.52 C ANISOU 409 CE2 TYR A 50 7289 8240 9747 -339 679 -1650 C ATOM 410 CZ TYR A 50 20.698 -42.068 25.265 1.00 69.94 C ANISOU 410 CZ TYR A 50 7704 8680 10190 -355 775 -1613 C ATOM 411 OH TYR A 50 19.681 -42.716 25.929 1.00 76.85 O ANISOU 411 OH TYR A 50 8539 9518 11144 -365 829 -1682 O ATOM 412 N SER A 51 26.097 -37.481 23.062 1.00 26.64 N ANISOU 412 N SER A 51 2430 3417 4273 -349 484 -1212 N ATOM 413 CA SER A 51 27.116 -36.963 22.159 1.00 21.41 C ANISOU 413 CA SER A 51 1809 2793 3533 -338 430 -1142 C ATOM 414 C SER A 51 27.318 -35.465 22.302 1.00 20.30 C ANISOU 414 C SER A 51 1692 2671 3351 -354 351 -1120 C ATOM 415 O SER A 51 26.550 -34.772 22.982 1.00 24.16 O ANISOU 415 O SER A 51 2165 3138 3875 -371 328 -1170 O ATOM 416 CB SER A 51 26.716 -37.240 20.715 1.00 32.43 C ANISOU 416 CB SER A 51 3213 4167 4944 -303 385 -1195 C ATOM 417 OG SER A 51 25.740 -36.300 20.289 1.00 34.14 O ANISOU 417 OG SER A 51 3429 4351 5193 -299 301 -1276 O ATOM 418 N GLU A 52 28.372 -34.982 21.655 1.00 16.13 N ANISOU 418 N GLU A 52 1581 2569 1979 -40 -314 -497 N ATOM 419 CA GLU A 52 28.588 -33.560 21.444 1.00 23.57 C ANISOU 419 CA GLU A 52 2481 3477 2996 -23 -320 -459 C ATOM 420 C GLU A 52 28.637 -33.333 19.949 1.00 20.74 C ANISOU 420 C GLU A 52 2140 3135 2604 -51 -336 -394 C ATOM 421 O GLU A 52 29.212 -34.133 19.223 1.00 18.50 O ANISOU 421 O GLU A 52 1906 2875 2249 -74 -325 -391 O ATOM 422 CB GLU A 52 29.909 -33.105 22.062 1.00 28.68 C ANISOU 422 CB GLU A 52 3125 4090 3683 3 -285 -494 C ATOM 423 CG GLU A 52 29.905 -33.045 23.568 1.00 38.23 C ANISOU 423 CG GLU A 52 4307 5276 4942 36 -270 -555 C ATOM 424 CD GLU A 52 31.054 -32.226 24.100 1.00 38.03 C ANISOU 424 CD GLU A 52 4263 5210 4976 65 -242 -576 C ATOM 425 OE1 GLU A 52 32.138 -32.267 23.489 1.00 34.57 O ANISOU 425 OE1 GLU A 52 3854 4769 4512 56 -223 -568 O ATOM 426 OE2 GLU A 52 30.868 -31.529 25.113 1.00 41.69 O ANISOU 426 OE2 GLU A 52 4683 5645 5513 95 -241 -600 O ATOM 427 N VAL A 53 28.049 -32.235 19.495 1.00 13.76 N ANISOU 427 N VAL A 53 1217 2239 1773 -47 -362 -341 N ATOM 428 CA VAL A 53 27.943 -31.958 18.074 1.00 13.64 C ANISOU 428 CA VAL A 53 1213 2240 1730 -73 -381 -274 C ATOM 429 C VAL A 53 28.707 -30.679 17.736 1.00 16.95 C ANISOU 429 C VAL A 53 1607 2624 2210 -58 -373 -241 C ATOM 430 O VAL A 53 28.517 -29.641 18.380 1.00 22.10 O ANISOU 430 O VAL A 53 2210 3243 2944 -31 -377 -241 O ATOM 431 CB VAL A 53 26.460 -31.816 17.660 1.00 18.78 C ANISOU 431 CB VAL A 53 1842 2912 2382 -87 -421 -232 C ATOM 432 CG1 VAL A 53 26.342 -31.425 16.200 1.00 21.71 C ANISOU 432 CG1 VAL A 53 2220 3297 2730 -111 -442 -161 C ATOM 433 CG2 VAL A 53 25.710 -33.115 17.919 1.00 17.35 C ANISOU 433 CG2 VAL A 53 1688 2768 2138 -104 -429 -263 C ATOM 434 N PHE A 54 29.553 -30.761 16.711 1.00 15.01 N ANISOU 434 N PHE A 54 1395 2387 1923 -75 -363 -212 N ATOM 435 CA PHE A 54 30.391 -29.648 16.297 1.00 17.97 C ANISOU 435 CA PHE A 54 1751 2729 2346 -64 -354 -180 C ATOM 436 C PHE A 54 30.131 -29.255 14.846 1.00 24.44 C ANISOU 436 C PHE A 54 2576 3566 3145 -88 -377 -106 C ATOM 437 O PHE A 54 29.832 -30.102 14.000 1.00 25.40 O ANISOU 437 O PHE A 54 2735 3726 3189 -118 -388 -87 O ATOM 438 CB PHE A 54 31.869 -30.031 16.448 1.00 18.44 C ANISOU 438 CB PHE A 54 1845 2779 2382 -59 -315 -217 C ATOM 439 CG PHE A 54 32.284 -30.353 17.857 1.00 19.95 C ANISOU 439 CG PHE A 54 2031 2951 2597 -34 -289 -290 C ATOM 440 CD1 PHE A 54 32.931 -29.402 18.634 1.00 18.78 C ANISOU 440 CD1 PHE A 54 1848 2760 2528 -2 -271 -310 C ATOM 441 CD2 PHE A 54 32.055 -31.607 18.399 1.00 18.57 C ANISOU 441 CD2 PHE A 54 1887 2802 2366 -41 -281 -339 C ATOM 442 CE1 PHE A 54 33.339 -29.687 19.936 1.00 24.13 C ANISOU 442 CE1 PHE A 54 2521 3420 3227 23 -246 -378 C ATOM 443 CE2 PHE A 54 32.464 -31.908 19.707 1.00 17.56 C ANISOU 443 CE2 PHE A 54 1756 2657 2260 -16 -256 -406 C ATOM 444 CZ PHE A 54 33.104 -30.942 20.475 1.00 23.65 C ANISOU 444 CZ PHE A 54 2491 3386 3110 16 -239 -426 C ATOM 445 N GLU A 55 30.227 -27.968 14.548 1.00 22.30 N ANISOU 445 N GLU A 55 2266 3266 2939 -76 -385 -63 N ATOM 446 CA GLU A 55 30.323 -27.556 13.158 1.00 20.33 C ANISOU 446 CA GLU A 55 2027 3028 2669 -96 -398 4 C ATOM 447 C GLU A 55 31.766 -27.797 12.768 1.00 22.63 C ANISOU 447 C GLU A 55 2355 3314 2927 -101 -366 -5 C ATOM 448 O GLU A 55 32.651 -27.626 13.588 1.00 19.13 O ANISOU 448 O GLU A 55 1907 2843 2518 -79 -338 -48 O ATOM 449 CB GLU A 55 29.979 -26.083 13.007 1.00 20.72 C ANISOU 449 CB GLU A 55 2023 3046 2803 -80 -416 52 C ATOM 450 CG GLU A 55 30.209 -25.530 11.613 1.00 27.79 C ANISOU 450 CG GLU A 55 2925 3949 3686 -98 -427 122 C ATOM 451 CD GLU A 55 29.842 -24.061 11.504 1.00 33.49 C ANISOU 451 CD GLU A 55 3592 4638 4493 -80 -444 169 C ATOM 452 OE1 GLU A 55 28.641 -23.745 11.593 1.00 46.55 O ANISOU 452 OE1 GLU A 55 5216 6299 6174 -79 -474 189 O ATOM 453 OE2 GLU A 55 30.749 -23.229 11.322 1.00 43.53 O ANISOU 453 OE2 GLU A 55 4853 5880 5807 -68 -428 185 O ATOM 454 N ALA A 56 32.013 -28.205 11.531 1.00 21.27 N ANISOU 454 N ALA A 56 2221 3171 2690 -129 -370 34 N ATOM 455 CA ALA A 56 33.384 -28.450 11.106 1.00 19.79 C ANISOU 455 CA ALA A 56 2070 2981 2469 -134 -340 27 C ATOM 456 C ALA A 56 33.534 -28.207 9.623 1.00 17.35 C ANISOU 456 C ALA A 56 1778 2690 2125 -158 -352 94 C ATOM 457 O ALA A 56 32.558 -27.981 8.923 1.00 19.31 O ANISOU 457 O ALA A 56 2014 2956 2367 -172 -384 143 O ATOM 458 CB ALA A 56 33.823 -29.867 11.462 1.00 17.19 C ANISOU 458 CB ALA A 56 1792 2677 2065 -145 -319 -30 C ATOM 459 N ILE A 57 34.773 -28.241 9.154 1.00 14.84 N ANISOU 459 N ILE A 57 1488 2366 1784 -162 -327 97 N ATOM 460 CA ILE A 57 35.046 -28.091 7.739 1.00 18.59 C ANISOU 460 CA ILE A 57 1984 2860 2220 -184 -335 157 C ATOM 461 C ILE A 57 35.735 -29.359 7.265 1.00 21.03 C ANISOU 461 C ILE A 57 2354 3201 2434 -207 -317 136 C ATOM 462 O ILE A 57 36.643 -29.877 7.920 1.00 20.95 O ANISOU 462 O ILE A 57 2367 3183 2411 -198 -286 82 O ATOM 463 CB ILE A 57 35.917 -26.844 7.456 1.00 25.09 C ANISOU 463 CB ILE A 57 2781 3645 3105 -169 -322 190 C ATOM 464 CG1 ILE A 57 36.276 -26.768 5.974 1.00 30.10 C ANISOU 464 CG1 ILE A 57 3441 4301 3693 -193 -328 251 C ATOM 465 CG2 ILE A 57 37.184 -26.883 8.282 1.00 33.95 C ANISOU 465 CG2 ILE A 57 3912 4740 4248 -149 -283 136 C ATOM 466 CD1 ILE A 57 37.222 -25.638 5.630 1.00 39.51 C ANISOU 466 CD1 ILE A 57 4614 5459 4939 -180 -313 283 C ATOM 467 N ASN A 58 35.261 -29.891 6.152 1.00 18.95 N ANISOU 467 N ASN A 58 2119 2978 2104 -237 -337 176 N ATOM 468 CA ASN A 58 35.931 -30.997 5.501 1.00 19.65 C ANISOU 468 CA ASN A 58 2266 3099 2102 -260 -322 165 C ATOM 469 C ASN A 58 37.007 -30.377 4.627 1.00 20.12 C ANISOU 469 C ASN A 58 2334 3147 2163 -262 -308 204 C ATOM 470 O ASN A 58 36.698 -29.790 3.598 1.00 24.45 O ANISOU 470 O ASN A 58 2873 3704 2714 -274 -328 268 O ATOM 471 CB ASN A 58 34.920 -31.765 4.643 1.00 20.67 C ANISOU 471 CB ASN A 58 2418 3274 2160 -291 -352 195 C ATOM 472 CG ASN A 58 35.549 -32.901 3.851 1.00 26.18 C ANISOU 472 CG ASN A 58 3177 4008 2761 -317 -340 190 C ATOM 473 OD1 ASN A 58 36.765 -32.968 3.688 1.00 20.69 O ANISOU 473 OD1 ASN A 58 2506 3304 2050 -315 -312 179 O ATOM 474 ND2 ASN A 58 34.705 -33.791 3.333 1.00 25.62 N ANISOU 474 ND2 ASN A 58 3131 3980 2624 -343 -362 199 N ATOM 475 N ILE A 59 38.267 -30.492 5.030 1.00 23.02 N ANISOU 475 N ILE A 59 2718 3495 2532 -251 -272 168 N ATOM 476 CA ILE A 59 39.337 -29.794 4.321 1.00 18.90 C ANISOU 476 CA ILE A 59 2199 2957 2023 -249 -256 202 C ATOM 477 C ILE A 59 39.719 -30.421 2.976 1.00 25.46 C ANISOU 477 C ILE A 59 3078 3825 2769 -279 -258 238 C ATOM 478 O ILE A 59 40.600 -29.913 2.289 1.00 28.14 O ANISOU 478 O ILE A 59 3423 4155 3112 -280 -245 270 O ATOM 479 CB ILE A 59 40.601 -29.638 5.194 1.00 19.71 C ANISOU 479 CB ILE A 59 2304 3026 2160 -226 -218 152 C ATOM 480 CG1 ILE A 59 41.247 -30.989 5.474 1.00 23.83 C ANISOU 480 CG1 ILE A 59 2877 3569 2606 -235 -193 96 C ATOM 481 CG2 ILE A 59 40.274 -28.943 6.495 1.00 24.78 C ANISOU 481 CG2 ILE A 59 2896 3629 2889 -195 -216 118 C ATOM 482 CD1 ILE A 59 42.601 -30.869 6.181 1.00 27.74 C ANISOU 482 CD1 ILE A 59 3379 4035 3127 -215 -154 50 C ATOM 483 N THR A 60 39.070 -31.520 2.602 1.00 23.15 N ANISOU 483 N THR A 60 2820 3576 2402 -303 -272 233 N ATOM 484 CA THR A 60 39.301 -32.108 1.281 1.00 28.27 C ANISOU 484 CA THR A 60 3511 4262 2968 -333 -278 270 C ATOM 485 C THR A 60 38.400 -31.484 0.206 1.00 33.71 C ANISOU 485 C THR A 60 4180 4966 3661 -347 -313 345 C ATOM 486 O THR A 60 38.637 -31.673 -0.991 1.00 35.69 O ANISOU 486 O THR A 60 4458 5244 3858 -368 -318 387 O ATOM 487 CB THR A 60 39.124 -33.643 1.272 1.00 28.82 C ANISOU 487 CB THR A 60 3632 4373 2947 -354 -276 231 C ATOM 488 OG1 THR A 60 37.726 -33.972 1.282 1.00 33.21 O ANISOU 488 OG1 THR A 60 4177 4951 3490 -365 -308 240 O ATOM 489 CG2 THR A 60 39.824 -34.272 2.470 1.00 34.17 C ANISOU 489 CG2 THR A 60 4324 5033 3624 -338 -244 155 C ATOM 490 N ASN A 61 37.372 -30.750 0.632 1.00 32.24 N ANISOU 490 N ASN A 61 3946 4765 3538 -335 -337 360 N ATOM 491 CA ASN A 61 36.517 -30.011 -0.301 1.00 23.44 C ANISOU 491 CA ASN A 61 2807 3660 2439 -344 -370 431 C ATOM 492 C ASN A 61 36.170 -28.609 0.202 1.00 26.12 C ANISOU 492 C ASN A 61 3085 3958 2881 -318 -379 452 C ATOM 493 O ASN A 61 35.462 -27.857 -0.460 1.00 32.10 O ANISOU 493 O ASN A 61 3815 4717 3664 -322 -406 510 O ATOM 494 CB ASN A 61 35.249 -30.802 -0.648 1.00 24.84 C ANISOU 494 CB ASN A 61 2997 3880 2563 -367 -402 440 C ATOM 495 CG ASN A 61 34.439 -31.177 0.578 1.00 24.36 C ANISOU 495 CG ASN A 61 2918 3812 2525 -355 -408 388 C ATOM 496 OD1 ASN A 61 34.612 -30.603 1.655 1.00 21.81 O ANISOU 496 OD1 ASN A 61 2562 3452 2273 -328 -395 356 O ATOM 497 ND2 ASN A 61 33.533 -32.135 0.417 1.00 28.38 N ANISOU 497 ND2 ASN A 61 3447 4359 2976 -376 -428 380 N ATOM 498 N ASN A 62 36.702 -28.257 1.367 1.00 28.34 N ANISOU 498 N ASN A 62 3345 4200 3222 -292 -356 405 N ATOM 499 CA ASN A 62 36.363 -27.004 2.041 1.00 21.69 C ANISOU 499 CA ASN A 62 2444 3316 2479 -265 -363 414 C ATOM 500 C ASN A 62 34.861 -26.833 2.269 1.00 26.87 C ANISOU 500 C ASN A 62 3068 3981 3160 -265 -398 428 C ATOM 501 O ASN A 62 34.375 -25.710 2.369 1.00 36.30 O ANISOU 501 O ASN A 62 4214 5150 4427 -250 -414 461 O ATOM 502 CB ASN A 62 36.946 -25.785 1.305 1.00 24.88 C ANISOU 502 CB ASN A 62 2826 3696 2930 -258 -361 471 C ATOM 503 CG ASN A 62 38.452 -25.672 1.464 1.00 36.50 C ANISOU 503 CG ASN A 62 4315 5144 4409 -248 -323 448 C ATOM 504 OD1 ASN A 62 39.053 -26.363 2.291 1.00 36.83 O ANISOU 504 OD1 ASN A 62 4377 5181 4434 -240 -297 385 O ATOM 505 ND2 ASN A 62 39.071 -24.797 0.676 1.00 36.86 N ANISOU 505 ND2 ASN A 62 4352 5176 4479 -247 -318 498 N ATOM 506 N GLU A 63 34.137 -27.947 2.364 1.00 20.47 N ANISOU 506 N GLU A 63 2283 3206 2288 -282 -411 404 N ATOM 507 CA GLU A 63 32.700 -27.902 2.646 1.00 27.40 C ANISOU 507 CA GLU A 63 3132 4094 3184 -282 -443 412 C ATOM 508 C GLU A 63 32.417 -27.958 4.145 1.00 26.20 C ANISOU 508 C GLU A 63 2955 3918 3081 -258 -435 350 C ATOM 509 O GLU A 63 33.075 -28.670 4.900 1.00 25.93 O ANISOU 509 O GLU A 63 2945 3880 3027 -252 -408 290 O ATOM 510 CB GLU A 63 31.973 -29.062 1.966 1.00 28.11 C ANISOU 510 CB GLU A 63 3261 4236 3184 -313 -463 419 C ATOM 511 CG GLU A 63 32.280 -29.215 0.497 1.00 42.84 C ANISOU 511 CG GLU A 63 5158 6131 4989 -339 -470 473 C ATOM 512 CD GLU A 63 31.424 -28.342 -0.383 1.00 58.90 C ANISOU 512 CD GLU A 63 7160 8171 7047 -345 -503 545 C ATOM 513 OE1 GLU A 63 30.940 -27.294 0.099 1.00 64.41 O ANISOU 513 OE1 GLU A 63 7808 8839 7827 -325 -514 559 O ATOM 514 OE2 GLU A 63 31.233 -28.715 -1.561 1.00 60.51 O ANISOU 514 OE2 GLU A 63 7391 8411 7189 -371 -518 587 O ATOM 515 N LYS A 64 31.414 -27.208 4.570 1.00 26.31 N ANISOU 515 N LYS A 64 2921 3917 3158 -245 -459 365 N ATOM 516 CA LYS A 64 30.963 -27.268 5.942 1.00 26.31 C ANISOU 516 CA LYS A 64 2895 3898 3202 -223 -456 311 C ATOM 517 C LYS A 64 30.304 -28.625 6.204 1.00 22.12 C ANISOU 517 C LYS A 64 2397 3405 2602 -241 -463 273 C ATOM 518 O LYS A 64 29.598 -29.153 5.355 1.00 20.96 O ANISOU 518 O LYS A 64 2270 3297 2399 -266 -486 304 O ATOM 519 CB LYS A 64 29.981 -26.130 6.190 1.00 37.02 C ANISOU 519 CB LYS A 64 4194 5233 4639 -207 -482 343 C ATOM 520 CG LYS A 64 29.812 -25.747 7.630 1.00 47.84 C ANISOU 520 CG LYS A 64 5527 6570 6082 -176 -474 293 C ATOM 521 CD LYS A 64 29.031 -24.452 7.729 1.00 54.69 C ANISOU 521 CD LYS A 64 6336 7411 7033 -159 -498 333 C ATOM 522 CE LYS A 64 29.715 -23.340 6.953 1.00 52.07 C ANISOU 522 CE LYS A 64 5988 7055 6739 -154 -494 386 C ATOM 523 NZ LYS A 64 28.918 -22.082 7.015 1.00 50.83 N ANISOU 523 NZ LYS A 64 5775 6874 6663 -138 -519 427 N ATOM 524 N VAL A 65 30.565 -29.195 7.373 1.00 18.69 N ANISOU 524 N VAL A 65 1969 2961 2173 -226 -442 205 N ATOM 525 CA VAL A 65 29.913 -30.418 7.802 1.00 21.64 C ANISOU 525 CA VAL A 65 2366 3364 2490 -239 -448 164 C ATOM 526 C VAL A 65 29.625 -30.341 9.292 1.00 17.68 C ANISOU 526 C VAL A 65 1836 2838 2045 -212 -440 107 C ATOM 527 O VAL A 65 29.958 -29.361 9.950 1.00 18.67 O ANISOU 527 O VAL A 65 1923 2923 2248 -184 -430 100 O ATOM 528 CB VAL A 65 30.784 -31.672 7.542 1.00 13.04 C ANISOU 528 CB VAL A 65 1339 2301 1316 -257 -423 131 C ATOM 529 CG1 VAL A 65 31.057 -31.825 6.059 1.00 21.10 C ANISOU 529 CG1 VAL A 65 2391 3349 2276 -285 -431 185 C ATOM 530 CG2 VAL A 65 32.090 -31.603 8.344 1.00 15.99 C ANISOU 530 CG2 VAL A 65 1719 2643 1714 -235 -384 81 C ATOM 531 N VAL A 66 29.005 -31.385 9.820 1.00 16.59 N ANISOU 531 N VAL A 66 1715 2724 1866 -220 -444 67 N ATOM 532 CA AVAL A 66 28.745 -31.475 11.250 1.00 14.78 C ANISOU 532 CA AVAL A 66 1462 2475 1679 -196 -435 9 C ATOM 533 CA BVAL A 66 28.758 -31.463 11.250 0.00 18.02 C ANISOU 533 CA BVAL A 66 1872 2884 2089 -195 -435 9 C ATOM 534 C VAL A 66 29.320 -32.773 11.792 1.00 20.05 C ANISOU 534 C VAL A 66 2175 3158 2286 -201 -409 -54 C ATOM 535 O VAL A 66 29.225 -33.822 11.148 1.00 20.95 O ANISOU 535 O VAL A 66 2333 3308 2317 -229 -413 -52 O ATOM 536 CB AVAL A 66 27.225 -31.384 11.528 1.00 20.20 C ANISOU 536 CB AVAL A 66 2116 3173 2386 -197 -470 21 C ATOM 537 CB BVAL A 66 27.258 -31.332 11.580 0.00 20.85 C ANISOU 537 CB BVAL A 66 2197 3253 2474 -195 -469 19 C ATOM 538 CG1AVAL A 66 26.895 -31.928 12.903 1.00 25.84 C ANISOU 538 CG1AVAL A 66 2823 3881 3116 -180 -460 -45 C ATOM 539 CG1BVAL A 66 26.533 -32.634 11.299 0.00 20.48 C ANISOU 539 CG1BVAL A 66 2186 3251 2344 -222 -482 8 C ATOM 540 CG2AVAL A 66 26.771 -29.942 11.392 1.00 22.92 C ANISOU 540 CG2AVAL A 66 2406 3490 2812 -180 -489 69 C ATOM 541 CG2BVAL A 66 27.069 -30.918 13.024 0.00 23.51 C ANISOU 541 CG2BVAL A 66 2493 3557 2882 -162 -460 -28 C ATOM 542 N VAL A 67 29.937 -32.703 12.969 1.00 16.83 N ANISOU 542 N VAL A 67 1757 2720 1917 -174 -382 -109 N ATOM 543 CA VAL A 67 30.561 -33.870 13.556 1.00 14.61 C ANISOU 543 CA VAL A 67 1517 2450 1584 -176 -355 -171 C ATOM 544 C VAL A 67 29.936 -34.202 14.892 1.00 14.30 C ANISOU 544 C VAL A 67 1457 2404 1571 -158 -354 -225 C ATOM 545 O VAL A 67 29.940 -33.386 15.812 1.00 15.49 O ANISOU 545 O VAL A 67 1566 2521 1800 -129 -348 -243 O ATOM 546 CB VAL A 67 32.074 -33.641 13.773 1.00 15.21 C ANISOU 546 CB VAL A 67 1606 2499 1673 -161 -317 -195 C ATOM 547 CG1 VAL A 67 32.709 -34.844 14.458 1.00 21.55 C ANISOU 547 CG1 VAL A 67 2451 3313 2426 -161 -288 -262 C ATOM 548 CG2 VAL A 67 32.750 -33.332 12.450 1.00 16.51 C ANISOU 548 CG2 VAL A 67 1792 2671 1810 -179 -317 -142 C ATOM 549 N LYS A 68 29.420 -35.421 15.000 1.00 12.79 N ANISOU 549 N LYS A 68 1297 2246 1315 -176 -358 -252 N ATOM 550 CA LYS A 68 28.808 -35.906 16.223 1.00 12.64 C ANISOU 550 CA LYS A 68 1266 2226 1311 -162 -357 -304 C ATOM 551 C LYS A 68 29.741 -36.897 16.913 1.00 15.60 C ANISOU 551 C LYS A 68 1679 2602 1646 -157 -321 -369 C ATOM 552 O LYS A 68 29.842 -38.066 16.509 1.00 15.67 O ANISOU 552 O LYS A 68 1737 2644 1575 -181 -316 -382 O ATOM 553 CB LYS A 68 27.469 -36.574 15.880 1.00 12.17 C ANISOU 553 CB LYS A 68 1212 2203 1208 -186 -389 -288 C ATOM 554 CG LYS A 68 26.699 -37.135 17.048 1.00 11.49 C ANISOU 554 CG LYS A 68 1114 2121 1131 -175 -391 -337 C ATOM 555 CD LYS A 68 25.333 -37.603 16.526 1.00 15.60 C ANISOU 555 CD LYS A 68 1635 2677 1615 -200 -426 -308 C ATOM 556 CE LYS A 68 24.525 -38.341 17.552 1.00 20.22 C ANISOU 556 CE LYS A 68 2216 3273 2196 -194 -430 -355 C ATOM 557 NZ LYS A 68 23.236 -38.802 16.909 1.00 15.69 N ANISOU 557 NZ LYS A 68 1645 2735 1582 -222 -465 -323 N ATOM 558 N ILE A 69 30.439 -36.419 17.942 1.00 14.89 N ANISOU 558 N ILE A 69 1567 2476 1612 -126 -296 -410 N ATOM 559 CA ILE A 69 31.349 -37.253 18.713 1.00 15.90 C ANISOU 559 CA ILE A 69 1727 2602 1712 -117 -261 -474 C ATOM 560 C ILE A 69 30.558 -37.973 19.790 1.00 21.50 C ANISOU 560 C ILE A 69 2432 3321 2418 -109 -264 -522 C ATOM 561 O ILE A 69 30.034 -37.349 20.720 1.00 21.01 O ANISOU 561 O ILE A 69 2324 3236 2423 -84 -270 -538 O ATOM 562 CB ILE A 69 32.492 -36.413 19.323 1.00 16.71 C ANISOU 562 CB ILE A 69 1810 2663 1877 -86 -232 -495 C ATOM 563 CG1 ILE A 69 33.206 -35.654 18.198 1.00 19.76 C ANISOU 563 CG1 ILE A 69 2200 3040 2268 -95 -232 -442 C ATOM 564 CG2 ILE A 69 33.432 -37.300 20.123 1.00 20.64 C ANISOU 564 CG2 ILE A 69 2341 3159 2343 -76 -196 -562 C ATOM 565 CD1 ILE A 69 34.332 -34.779 18.649 1.00 24.56 C ANISOU 565 CD1 ILE A 69 2788 3608 2936 -68 -206 -456 C ATOM 566 N LEU A 70 30.444 -39.289 19.641 1.00 20.37 N ANISOU 566 N LEU A 70 2333 3211 2195 -131 -260 -545 N ATOM 567 CA LEU A 70 29.596 -40.076 20.519 1.00 23.96 C ANISOU 567 CA LEU A 70 2787 3680 2637 -129 -265 -586 C ATOM 568 C LEU A 70 30.206 -40.202 21.906 1.00 30.96 C ANISOU 568 C LEU A 70 3665 4542 3555 -98 -234 -653 C ATOM 569 O LEU A 70 31.381 -40.549 22.052 1.00 33.58 O ANISOU 569 O LEU A 70 4027 4867 3866 -93 -203 -684 O ATOM 570 CB LEU A 70 29.350 -41.464 19.925 1.00 25.15 C ANISOU 570 CB LEU A 70 2991 3874 2692 -162 -269 -591 C ATOM 571 CG LEU A 70 28.742 -41.467 18.522 1.00 22.89 C ANISOU 571 CG LEU A 70 2716 3615 2364 -195 -299 -527 C ATOM 572 CD1 LEU A 70 28.592 -42.887 17.996 1.00 31.22 C ANISOU 572 CD1 LEU A 70 3826 4711 3323 -227 -300 -538 C ATOM 573 CD2 LEU A 70 27.395 -40.752 18.544 1.00 29.44 C ANISOU 573 CD2 LEU A 70 3499 4445 3243 -193 -335 -492 C ATOM 574 N LYS A 71 29.411 -39.913 22.930 1.00 37.86 N ANISOU 574 N LYS A 71 4499 5404 4482 -77 -244 -675 N ATOM 575 CA LYS A 71 29.855 -40.160 24.294 1.00 38.35 C ANISOU 575 CA LYS A 71 4555 5448 4569 -48 -216 -742 C ATOM 576 C LYS A 71 29.957 -41.665 24.456 1.00 43.80 C ANISOU 576 C LYS A 71 5296 6168 5178 -65 -202 -783 C ATOM 577 O LYS A 71 29.251 -42.411 23.770 1.00 43.64 O ANISOU 577 O LYS A 71 5301 6181 5099 -95 -221 -762 O ATOM 578 CB LYS A 71 28.876 -39.583 25.320 1.00 35.82 C ANISOU 578 CB LYS A 71 4181 5111 4318 -24 -232 -755 C ATOM 579 CG LYS A 71 28.901 -38.067 25.439 1.00 37.30 C ANISOU 579 CG LYS A 71 4315 5262 4596 0 -240 -727 C ATOM 580 CD LYS A 71 28.454 -37.637 26.827 1.00 44.12 C ANISOU 580 CD LYS A 71 5132 6102 5528 34 -238 -767 C ATOM 581 CE LYS A 71 28.532 -36.129 27.001 1.00 47.17 C ANISOU 581 CE LYS A 71 5466 6451 6007 60 -245 -742 C ATOM 582 NZ LYS A 71 27.389 -35.452 26.344 1.00 49.58 N ANISOU 582 NZ LYS A 71 5740 6763 6337 48 -283 -684 N ATOM 583 N PRO A 72 30.854 -42.122 25.342 1.00 59.77 N ANISOU 583 N PRO A 72 7350 8035 7326 133 -514 86 N ATOM 584 CA PRO A 72 31.000 -43.556 25.608 1.00 66.40 C ANISOU 584 CA PRO A 72 8186 8830 8212 140 -541 130 C ATOM 585 C PRO A 72 29.719 -44.126 26.201 1.00 74.42 C ANISOU 585 C PRO A 72 9234 9848 9195 119 -528 172 C ATOM 586 O PRO A 72 29.688 -45.283 26.621 1.00 77.36 O ANISOU 586 O PRO A 72 9611 10188 9593 120 -551 217 O ATOM 587 CB PRO A 72 32.137 -43.608 26.634 1.00 63.60 C ANISOU 587 CB PRO A 72 7829 8481 7855 151 -594 160 C ATOM 588 CG PRO A 72 32.902 -42.343 26.418 1.00 62.79 C ANISOU 588 CG PRO A 72 7713 8412 7734 157 -592 115 C ATOM 589 CD PRO A 72 31.867 -41.322 26.051 1.00 60.90 C ANISOU 589 CD PRO A 72 7490 8208 7443 139 -544 83 C ATOM 590 N VAL A 73 28.672 -43.308 26.235 1.00 80.09 N ANISOU 590 N VAL A 73 9972 10603 9857 99 -492 158 N ATOM 591 CA VAL A 73 27.368 -43.753 26.698 1.00 85.73 C ANISOU 591 CA VAL A 73 10714 11321 10538 77 -473 190 C ATOM 592 C VAL A 73 26.847 -44.868 25.792 1.00 85.27 C ANISOU 592 C VAL A 73 10646 11216 10537 80 -454 190 C ATOM 593 O VAL A 73 26.482 -44.634 24.636 1.00 81.60 O ANISOU 593 O VAL A 73 10167 10743 10094 82 -419 147 O ATOM 594 CB VAL A 73 26.351 -42.588 26.752 1.00 87.64 C ANISOU 594 CB VAL A 73 10974 11609 10716 58 -433 165 C ATOM 595 CG1 VAL A 73 25.018 -43.066 27.310 1.00 88.21 C ANISOU 595 CG1 VAL A 73 11074 11687 10754 33 -414 198 C ATOM 596 CG2 VAL A 73 26.900 -41.440 27.590 1.00 86.39 C ANISOU 596 CG2 VAL A 73 10823 11497 10503 55 -450 160 C ATOM 597 N LYS A 74 26.846 -46.084 26.328 1.00 85.27 N ANISOU 597 N LYS A 74 10654 11185 10561 80 -478 239 N ATOM 598 CA LYS A 74 26.312 -47.260 25.640 1.00 80.27 C ANISOU 598 CA LYS A 74 10015 10505 9979 81 -463 247 C ATOM 599 C LYS A 74 27.237 -47.829 24.560 1.00 74.78 C ANISOU 599 C LYS A 74 9283 9764 9365 105 -471 219 C ATOM 600 O LYS A 74 28.262 -47.236 24.224 1.00 69.76 O ANISOU 600 O LYS A 74 8625 9134 8746 121 -484 188 O ATOM 601 CB LYS A 74 24.892 -47.010 25.124 1.00 78.26 C ANISOU 601 CB LYS A 74 9773 10265 9698 61 -413 227 C ATOM 602 CG LYS A 74 23.899 -46.635 26.227 1.00 75.70 C ANISOU 602 CG LYS A 74 9484 9980 9299 35 -403 256 C ATOM 603 CD LYS A 74 23.861 -47.672 27.352 1.00 78.20 C ANISOU 603 CD LYS A 74 9822 10280 9609 25 -435 321 C ATOM 604 CE LYS A 74 24.887 -47.391 28.456 1.00 81.00 C ANISOU 604 CE LYS A 74 10184 10652 9939 31 -482 350 C ATOM 605 NZ LYS A 74 24.695 -46.065 29.108 1.00 80.63 N ANISOU 605 NZ LYS A 74 10153 10664 9820 16 -473 336 N ATOM 606 N LYS A 75 26.861 -48.990 24.032 1.00 72.99 N ANISOU 606 N LYS A 75 9051 9494 9188 106 -462 231 N ATOM 607 CA LYS A 75 27.791 -49.848 23.306 1.00 70.54 C ANISOU 607 CA LYS A 75 8708 9132 8960 128 -479 220 C ATOM 608 C LYS A 75 27.358 -50.162 21.875 1.00 62.81 C ANISOU 608 C LYS A 75 7711 8127 8028 129 -438 177 C ATOM 609 O LYS A 75 27.637 -49.396 20.953 1.00 63.31 O ANISOU 609 O LYS A 75 7755 8201 8099 133 -416 125 O ATOM 610 CB LYS A 75 27.980 -51.147 24.090 1.00 78.55 C ANISOU 610 CB LYS A 75 9732 10110 10004 132 -516 280 C ATOM 611 CG LYS A 75 26.970 -51.333 25.220 1.00 82.31 C ANISOU 611 CG LYS A 75 10248 10606 10418 108 -517 331 C ATOM 612 CD LYS A 75 27.632 -51.236 26.591 1.00 84.14 C ANISOU 612 CD LYS A 75 10497 10855 10617 109 -567 377 C ATOM 613 CE LYS A 75 28.239 -49.860 26.835 1.00 85.27 C ANISOU 613 CE LYS A 75 10636 11046 10717 113 -573 349 C ATOM 614 NZ LYS A 75 27.428 -49.015 27.763 1.00 83.83 N ANISOU 614 NZ LYS A 75 10488 10918 10447 87 -561 363 N ATOM 615 N LYS A 76 26.689 -51.299 21.695 1.00 55.57 N ANISOU 615 N LYS A 76 6799 7174 7141 122 -428 201 N ATOM 616 CA LYS A 76 26.199 -51.711 20.378 1.00 48.97 C ANISOU 616 CA LYS A 76 5946 6311 6348 120 -389 164 C ATOM 617 C LYS A 76 25.136 -50.752 19.843 1.00 37.27 C ANISOU 617 C LYS A 76 4477 4868 4818 101 -343 129 C ATOM 618 O LYS A 76 24.669 -50.886 18.709 1.00 35.16 O ANISOU 618 O LYS A 76 4198 4586 4577 96 -309 94 O ATOM 619 CB LYS A 76 25.621 -53.126 20.432 1.00 50.58 C ANISOU 619 CB LYS A 76 6158 6472 6589 114 -388 201 C ATOM 620 CG LYS A 76 24.477 -53.287 21.420 1.00 52.97 C ANISOU 620 CG LYS A 76 6498 6795 6834 92 -382 247 C ATOM 621 CD LYS A 76 23.565 -54.439 21.020 1.00 58.69 C ANISOU 621 CD LYS A 76 7227 7483 7589 80 -359 262 C ATOM 622 CE LYS A 76 22.619 -54.808 22.149 1.00 62.81 C ANISOU 622 CE LYS A 76 7786 8017 8060 59 -363 315 C ATOM 623 NZ LYS A 76 23.363 -55.336 23.330 1.00 64.57 N ANISOU 623 NZ LYS A 76 8021 8227 8284 66 -414 370 N ATOM 624 N LYS A 77 24.733 -49.800 20.673 1.00 33.14 N ANISOU 624 N LYS A 77 3977 4393 4223 90 -344 140 N ATOM 625 CA LYS A 77 23.899 -48.711 20.196 1.00 35.10 C ANISOU 625 CA LYS A 77 4232 4679 4425 76 -306 103 C ATOM 626 C LYS A 77 24.641 -47.953 19.092 1.00 28.18 C ANISOU 626 C LYS A 77 3330 3804 3573 88 -296 45 C ATOM 627 O LYS A 77 24.024 -47.397 18.181 1.00 23.31 O ANISOU 627 O LYS A 77 2710 3198 2947 79 -260 5 O ATOM 628 CB LYS A 77 23.535 -47.763 21.341 1.00 43.08 C ANISOU 628 CB LYS A 77 5269 5741 5359 64 -312 122 C ATOM 629 CG LYS A 77 23.018 -46.413 20.860 1.00 52.46 C ANISOU 629 CG LYS A 77 6460 6969 6503 56 -281 77 C ATOM 630 CD LYS A 77 22.330 -45.622 21.958 1.00 51.14 C ANISOU 630 CD LYS A 77 6320 6849 6260 39 -278 96 C ATOM 631 CE LYS A 77 21.900 -44.270 21.421 1.00 55.61 C ANISOU 631 CE LYS A 77 6886 7453 6791 34 -249 49 C ATOM 632 NZ LYS A 77 21.019 -43.540 22.368 1.00 60.18 N ANISOU 632 NZ LYS A 77 7490 8075 7300 15 -238 63 N ATOM 633 N ILE A 78 25.971 -47.935 19.174 1.00 21.48 N ANISOU 633 N ILE A 78 2462 2945 2755 107 -327 39 N ATOM 634 CA ILE A 78 26.763 -47.212 18.190 1.00 18.93 C ANISOU 634 CA ILE A 78 2115 2624 2455 117 -318 -16 C ATOM 635 C ILE A 78 26.637 -47.851 16.817 1.00 20.90 C ANISOU 635 C ILE A 78 2344 2835 2763 116 -291 -49 C ATOM 636 O ILE A 78 26.399 -47.163 15.826 1.00 19.77 O ANISOU 636 O ILE A 78 2195 2703 2614 109 -261 -96 O ATOM 637 CB ILE A 78 28.245 -47.140 18.591 1.00 25.23 C ANISOU 637 CB ILE A 78 2895 3416 3277 137 -358 -14 C ATOM 638 CG1 ILE A 78 28.405 -46.317 19.867 1.00 31.47 C ANISOU 638 CG1 ILE A 78 3705 4250 4004 135 -382 12 C ATOM 639 CG2 ILE A 78 29.061 -46.532 17.467 1.00 31.51 C ANISOU 639 CG2 ILE A 78 3663 4207 4103 145 -345 -74 C ATOM 640 CD1 ILE A 78 29.842 -46.246 20.373 1.00 36.61 C ANISOU 640 CD1 ILE A 78 4338 4896 4675 155 -425 17 C ATOM 641 N LYS A 79 26.811 -49.168 16.753 1.00 21.64 N ANISOU 641 N LYS A 79 2427 2883 2913 123 -302 -26 N ATOM 642 CA LYS A 79 26.642 -49.882 15.495 1.00 22.44 C ANISOU 642 CA LYS A 79 2509 2945 3071 121 -275 -56 C ATOM 643 C LYS A 79 25.212 -49.773 14.965 1.00 16.37 C ANISOU 643 C LYS A 79 1757 2189 2274 99 -234 -65 C ATOM 644 O LYS A 79 25.000 -49.703 13.758 1.00 17.17 O ANISOU 644 O LYS A 79 1847 2280 2398 92 -204 -108 O ATOM 645 CB LYS A 79 27.017 -51.352 15.654 1.00 21.41 C ANISOU 645 CB LYS A 79 2367 2764 3006 131 -296 -25 C ATOM 646 CG LYS A 79 28.496 -51.580 15.905 1.00 27.16 C ANISOU 646 CG LYS A 79 3070 3470 3779 154 -334 -24 C ATOM 647 CD LYS A 79 28.923 -52.933 15.393 1.00 33.52 C ANISOU 647 CD LYS A 79 3851 4216 4668 164 -340 -22 C ATOM 648 CE LYS A 79 30.415 -53.148 15.565 1.00 38.03 C ANISOU 648 CE LYS A 79 4394 4765 5291 188 -378 -26 C ATOM 649 NZ LYS A 79 30.792 -54.506 15.089 1.00 37.33 N ANISOU 649 NZ LYS A 79 4281 4616 5287 199 -383 -23 N ATOM 650 N ARG A 80 24.229 -49.789 15.859 1.00 17.21 N ANISOU 650 N ARG A 80 1891 2316 2331 87 -233 -26 N ATOM 651 CA ARG A 80 22.837 -49.686 15.435 1.00 20.64 C ANISOU 651 CA ARG A 80 2340 2763 2737 67 -196 -34 C ATOM 652 C ARG A 80 22.621 -48.387 14.681 1.00 19.09 C ANISOU 652 C ARG A 80 2143 2600 2509 61 -171 -84 C ATOM 653 O ARG A 80 22.065 -48.391 13.586 1.00 13.78 O ANISOU 653 O ARG A 80 1464 1920 1851 51 -140 -116 O ATOM 654 CB ARG A 80 21.897 -49.749 16.638 1.00 17.29 C ANISOU 654 CB ARG A 80 1947 2363 2261 55 -199 13 C ATOM 655 CG ARG A 80 20.432 -49.773 16.279 1.00 18.45 C ANISOU 655 CG ARG A 80 2108 2519 2384 34 -162 8 C ATOM 656 CD ARG A 80 19.594 -49.895 17.542 1.00 18.00 C ANISOU 656 CD ARG A 80 2080 2484 2277 21 -167 55 C ATOM 657 NE ARG A 80 19.612 -48.661 18.322 1.00 20.32 N ANISOU 657 NE ARG A 80 2387 2826 2507 18 -175 54 N ATOM 658 CZ ARG A 80 19.137 -48.553 19.562 1.00 27.70 C ANISOU 658 CZ ARG A 80 3347 3786 3392 7 -184 93 C ATOM 659 NH1 ARG A 80 18.636 -49.614 20.177 1.00 28.92 N ANISOU 659 NH1 ARG A 80 3516 3922 3552 -3 -188 136 N ATOM 660 NH2 ARG A 80 19.174 -47.385 20.192 1.00 24.51 N ANISOU 660 NH2 ARG A 80 2954 3427 2932 4 -188 87 N ATOM 661 N GLU A 81 23.067 -47.271 15.258 1.00 17.61 N ANISOU 661 N GLU A 81 1963 2451 2278 65 -185 -89 N ATOM 662 CA GLU A 81 22.856 -45.980 14.616 1.00 14.79 C ANISOU 662 CA GLU A 81 1607 2126 1887 59 -164 -133 C ATOM 663 C GLU A 81 23.611 -45.938 13.288 1.00 15.07 C ANISOU 663 C GLU A 81 1617 2138 1970 64 -153 -182 C ATOM 664 O GLU A 81 23.076 -45.504 12.277 1.00 12.64 O ANISOU 664 O GLU A 81 1309 1835 1659 53 -125 -219 O ATOM 665 CB GLU A 81 23.263 -44.819 15.530 1.00 13.15 C ANISOU 665 CB GLU A 81 1411 1962 1625 63 -182 -129 C ATOM 666 CG GLU A 81 23.170 -43.451 14.858 1.00 16.14 C ANISOU 666 CG GLU A 81 1790 2370 1972 58 -162 -176 C ATOM 667 CD GLU A 81 23.466 -42.292 15.800 1.00 15.49 C ANISOU 667 CD GLU A 81 1720 2331 1833 61 -178 -172 C ATOM 668 OE1 GLU A 81 23.835 -42.538 16.966 1.00 17.69 O ANISOU 668 OE1 GLU A 81 2006 2617 2098 66 -205 -133 O ATOM 669 OE2 GLU A 81 23.326 -41.132 15.373 1.00 17.23 O ANISOU 669 OE2 GLU A 81 1944 2579 2024 56 -163 -207 O ATOM 670 N ILE A 82 24.860 -46.399 13.293 1.00 14.70 N ANISOU 670 N ILE A 82 1550 2066 1969 80 -177 -184 N ATOM 671 CA ILE A 82 25.650 -46.429 12.065 1.00 16.94 C ANISOU 671 CA ILE A 82 1809 2327 2303 83 -167 -232 C ATOM 672 C ILE A 82 25.022 -47.246 10.945 1.00 14.45 C ANISOU 672 C ILE A 82 1484 1978 2027 72 -137 -249 C ATOM 673 O ILE A 82 24.960 -46.791 9.808 1.00 17.47 O ANISOU 673 O ILE A 82 1861 2362 2416 62 -113 -295 O ATOM 674 CB ILE A 82 27.076 -46.943 12.315 1.00 17.93 C ANISOU 674 CB ILE A 82 1910 2425 2477 103 -199 -228 C ATOM 675 CG1 ILE A 82 27.860 -45.916 13.140 1.00 19.47 C ANISOU 675 CG1 ILE A 82 2109 2656 2634 113 -224 -226 C ATOM 676 CG2 ILE A 82 27.736 -47.211 10.986 1.00 18.58 C ANISOU 676 CG2 ILE A 82 1965 2476 2617 103 -182 -277 C ATOM 677 CD1 ILE A 82 29.275 -46.375 13.546 1.00 19.46 C ANISOU 677 CD1 ILE A 82 2085 2632 2678 134 -261 -219 C ATOM 678 N LYS A 83 24.574 -48.461 11.257 1.00 16.91 N ANISOU 678 N LYS A 83 1798 2261 2367 72 -140 -214 N ATOM 679 CA LYS A 83 23.957 -49.340 10.267 1.00 15.88 C ANISOU 679 CA LYS A 83 1660 2098 2277 60 -112 -227 C ATOM 680 C LYS A 83 22.671 -48.732 9.705 1.00 15.01 C ANISOU 680 C LYS A 83 1566 2012 2123 40 -79 -245 C ATOM 681 O LYS A 83 22.418 -48.753 8.494 1.00 14.41 O ANISOU 681 O LYS A 83 1482 1926 2069 28 -53 -283 O ATOM 682 CB LYS A 83 23.666 -50.715 10.880 1.00 15.92 C ANISOU 682 CB LYS A 83 1667 2069 2312 63 -124 -180 C ATOM 683 CG LYS A 83 23.158 -51.746 9.891 1.00 20.59 C ANISOU 683 CG LYS A 83 2248 2623 2953 53 -97 -193 C ATOM 684 CD LYS A 83 24.091 -51.880 8.710 1.00 28.36 C ANISOU 684 CD LYS A 83 3203 3579 3993 56 -88 -242 C ATOM 685 CE LYS A 83 23.485 -52.752 7.630 1.00 29.59 C ANISOU 685 CE LYS A 83 3350 3703 4190 41 -56 -261 C ATOM 686 NZ LYS A 83 24.445 -52.981 6.521 1.00 31.14 N ANISOU 686 NZ LYS A 83 3517 3870 4445 42 -47 -309 N ATOM 687 N ILE A 84 21.862 -48.174 10.593 1.00 13.52 N ANISOU 687 N ILE A 84 1402 1859 1876 35 -82 -218 N ATOM 688 CA ILE A 84 20.628 -47.524 10.169 1.00 14.53 C ANISOU 688 CA ILE A 84 1545 2013 1963 17 -53 -233 C ATOM 689 C ILE A 84 20.924 -46.357 9.222 1.00 14.65 C ANISOU 689 C ILE A 84 1556 2048 1964 13 -41 -285 C ATOM 690 O ILE A 84 20.294 -46.227 8.174 1.00 17.01 O ANISOU 690 O ILE A 84 1854 2344 2267 -1 -15 -314 O ATOM 691 CB ILE A 84 19.787 -47.068 11.388 1.00 15.22 C ANISOU 691 CB ILE A 84 1657 2136 1990 13 -59 -197 C ATOM 692 CG1 ILE A 84 19.137 -48.292 12.054 1.00 18.48 C ANISOU 692 CG1 ILE A 84 2078 2528 2415 9 -61 -151 C ATOM 693 CG2 ILE A 84 18.709 -46.077 10.968 1.00 16.82 C ANISOU 693 CG2 ILE A 84 1872 2371 2146 -1 -34 -220 C ATOM 694 CD1 ILE A 84 18.420 -47.998 13.358 1.00 20.30 C ANISOU 694 CD1 ILE A 84 2333 2791 2590 4 -68 -112 C ATOM 695 N LEU A 85 21.880 -45.505 9.590 1.00 13.95 N ANISOU 695 N LEU A 85 1464 1978 1858 24 -60 -295 N ATOM 696 CA LEU A 85 22.262 -44.380 8.732 1.00 12.39 C ANISOU 696 CA LEU A 85 1263 1798 1646 20 -50 -343 C ATOM 697 C LEU A 85 22.742 -44.859 7.367 1.00 13.72 C ANISOU 697 C LEU A 85 1412 1933 1868 14 -34 -383 C ATOM 698 O LEU A 85 22.444 -44.247 6.344 1.00 15.24 O ANISOU 698 O LEU A 85 1607 2133 2051 0 -12 -421 O ATOM 699 CB LEU A 85 23.346 -43.523 9.403 1.00 11.31 C ANISOU 699 CB LEU A 85 1125 1684 1489 34 -74 -346 C ATOM 700 CG LEU A 85 22.857 -42.634 10.560 1.00 13.05 C ANISOU 700 CG LEU A 85 1368 1947 1645 35 -85 -321 C ATOM 701 CD1 LEU A 85 24.032 -42.138 11.415 1.00 14.85 C ANISOU 701 CD1 LEU A 85 1591 2190 1861 51 -114 -313 C ATOM 702 CD2 LEU A 85 22.024 -41.465 10.033 1.00 13.00 C ANISOU 702 CD2 LEU A 85 1374 1970 1593 22 -62 -349 C ATOM 703 N GLU A 86 23.509 -45.945 7.351 1.00 18.52 N ANISOU 703 N GLU A 86 2001 2504 2533 23 -44 -375 N ATOM 704 CA GLU A 86 23.985 -46.489 6.081 1.00 20.17 C ANISOU 704 CA GLU A 86 2189 2679 2797 16 -27 -413 C ATOM 705 C GLU A 86 22.861 -47.113 5.255 1.00 19.39 C ANISOU 705 C GLU A 86 2094 2564 2710 -3 2 -419 C ATOM 706 O GLU A 86 22.788 -46.897 4.047 1.00 16.08 O ANISOU 706 O GLU A 86 1670 2139 2302 -18 24 -461 O ATOM 707 CB GLU A 86 25.144 -47.460 6.291 1.00 16.99 C ANISOU 707 CB GLU A 86 1761 2239 2455 32 -47 -406 C ATOM 708 CG GLU A 86 26.458 -46.722 6.514 1.00 19.51 C ANISOU 708 CG GLU A 86 2068 2570 2773 46 -68 -426 C ATOM 709 CD GLU A 86 27.627 -47.636 6.802 1.00 28.89 C ANISOU 709 CD GLU A 86 3230 3723 4023 64 -91 -417 C ATOM 710 OE1 GLU A 86 27.481 -48.876 6.684 1.00 29.59 O ANISOU 710 OE1 GLU A 86 3309 3773 4161 66 -89 -401 O ATOM 711 OE2 GLU A 86 28.694 -47.095 7.168 1.00 29.86 O ANISOU 711 OE2 GLU A 86 3343 3856 4146 77 -112 -427 O ATOM 712 N ASN A 87 21.985 -47.874 5.905 1.00 19.41 N ANISOU 712 N ASN A 87 2106 2560 2709 -3 1 -377 N ATOM 713 CA ASN A 87 20.816 -48.424 5.213 1.00 20.98 C ANISOU 713 CA ASN A 87 2310 2748 2914 -21 29 -380 C ATOM 714 C ASN A 87 19.945 -47.357 4.556 1.00 19.21 C ANISOU 714 C ASN A 87 2100 2554 2643 -38 49 -408 C ATOM 715 O ASN A 87 19.450 -47.546 3.449 1.00 17.41 O ANISOU 715 O ASN A 87 1870 2315 2431 -55 73 -435 O ATOM 716 CB ASN A 87 19.955 -49.263 6.160 1.00 19.87 C ANISOU 716 CB ASN A 87 2181 2602 2768 -19 24 -330 C ATOM 717 CG ASN A 87 20.600 -50.577 6.524 1.00 21.93 C ANISOU 717 CG ASN A 87 2427 2821 3085 -7 10 -304 C ATOM 718 OD1 ASN A 87 21.596 -50.980 5.920 1.00 21.18 O ANISOU 718 OD1 ASN A 87 2310 2697 3040 -2 7 -328 O ATOM 719 ND2 ASN A 87 20.030 -51.261 7.518 1.00 17.18 N ANISOU 719 ND2 ASN A 87 1838 2216 2476 -4 0 -255 N ATOM 720 N LEU A 88 19.778 -46.228 5.233 1.00 15.95 N ANISOU 720 N LEU A 88 1703 2181 2176 -33 39 -401 N ATOM 721 CA LEU A 88 18.824 -45.208 4.808 1.00 12.77 C ANISOU 721 CA LEU A 88 1317 1809 1727 -47 54 -420 C ATOM 722 C LEU A 88 19.453 -44.119 3.939 1.00 15.70 C ANISOU 722 C LEU A 88 1686 2193 2087 -52 58 -466 C ATOM 723 O LEU A 88 18.756 -43.245 3.430 1.00 15.46 O ANISOU 723 O LEU A 88 1668 2184 2022 -64 70 -486 O ATOM 724 CB LEU A 88 18.159 -44.556 6.029 1.00 17.62 C ANISOU 724 CB LEU A 88 1949 2459 2286 -41 44 -387 C ATOM 725 CG LEU A 88 17.305 -45.438 6.947 1.00 18.61 C ANISOU 725 CG LEU A 88 2082 2580 2408 -41 43 -342 C ATOM 726 CD1 LEU A 88 16.814 -44.645 8.155 1.00 19.32 C ANISOU 726 CD1 LEU A 88 2191 2709 2441 -37 33 -316 C ATOM 727 CD2 LEU A 88 16.123 -46.027 6.190 1.00 16.43 C ANISOU 727 CD2 LEU A 88 1808 2292 2145 -58 69 -347 C ATOM 728 N ARG A 89 20.764 -44.185 3.750 1.00 14.49 N ANISOU 728 N ARG A 89 1518 2025 1964 -44 47 -484 N ATOM 729 CA ARG A 89 21.484 -43.102 3.091 1.00 17.92 C ANISOU 729 CA ARG A 89 1951 2473 2383 -48 48 -525 C ATOM 730 C ARG A 89 21.001 -42.898 1.665 1.00 20.43 C ANISOU 730 C ARG A 89 2273 2785 2706 -72 74 -565 C ATOM 731 O ARG A 89 20.855 -43.854 0.903 1.00 15.60 O ANISOU 731 O ARG A 89 1649 2142 2135 -83 89 -575 O ATOM 732 CB ARG A 89 22.997 -43.363 3.132 1.00 20.16 C ANISOU 732 CB ARG A 89 2215 2738 2707 -36 34 -539 C ATOM 733 CG ARG A 89 23.854 -42.207 2.630 1.00 24.12 C ANISOU 733 CG ARG A 89 2717 3257 3192 -39 33 -580 C ATOM 734 CD ARG A 89 25.283 -42.291 3.187 1.00 21.61 C ANISOU 734 CD ARG A 89 2381 2932 2898 -21 11 -581 C ATOM 735 NE ARG A 89 25.871 -43.608 2.952 1.00 17.86 N ANISOU 735 NE ARG A 89 1882 2415 2489 -16 10 -579 N ATOM 736 CZ ARG A 89 26.865 -44.131 3.664 1.00 29.70 C ANISOU 736 CZ ARG A 89 3364 3900 4022 4 -13 -564 C ATOM 737 NH1 ARG A 89 27.404 -43.449 4.672 1.00 28.08 N ANISOU 737 NH1 ARG A 89 3163 3721 3787 20 -38 -547 N ATOM 738 NH2 ARG A 89 27.324 -45.343 3.365 1.00 27.34 N ANISOU 738 NH2 ARG A 89 3041 3560 3786 7 -12 -565 N ATOM 739 N GLY A 90 20.750 -41.643 1.313 1.00 18.08 N ANISOU 739 N GLY A 90 1990 2515 2365 -80 77 -587 N ATOM 740 CA GLY A 90 20.262 -41.307 -0.013 1.00 15.39 C ANISOU 740 CA GLY A 90 1655 2172 2021 -104 97 -623 C ATOM 741 C GLY A 90 18.742 -41.294 -0.103 1.00 20.97 C ANISOU 741 C GLY A 90 2376 2890 2703 -114 108 -608 C ATOM 742 O GLY A 90 18.181 -40.884 -1.117 1.00 23.78 O ANISOU 742 O GLY A 90 2740 3248 3048 -133 122 -634 O ATOM 743 N GLY A 91 18.073 -41.754 0.950 1.00 18.29 N ANISOU 743 N GLY A 91 2039 2556 2355 -102 102 -567 N ATOM 744 CA GLY A 91 16.612 -41.768 0.975 1.00 15.75 C ANISOU 744 CA GLY A 91 1728 2245 2010 -111 113 -552 C ATOM 745 C GLY A 91 16.058 -40.359 1.088 1.00 16.34 C ANISOU 745 C GLY A 91 1821 2355 2032 -112 109 -561 C ATOM 746 O GLY A 91 16.758 -39.454 1.522 1.00 15.24 O ANISOU 746 O GLY A 91 1686 2235 1869 -102 95 -567 O ATOM 747 N PRO A 92 14.797 -40.152 0.677 1.00 13.63 N ANISOU 747 N PRO A 92 1487 2021 1671 -125 120 -563 N ATOM 748 CA PRO A 92 14.239 -38.790 0.685 1.00 10.85 C ANISOU 748 CA PRO A 92 1150 1701 1273 -126 116 -575 C ATOM 749 C PRO A 92 14.276 -38.131 2.061 1.00 12.49 C ANISOU 749 C PRO A 92 1364 1936 1445 -108 102 -550 C ATOM 750 O PRO A 92 13.742 -38.676 3.018 1.00 14.51 O ANISOU 750 O PRO A 92 1619 2196 1697 -101 101 -517 O ATOM 751 CB PRO A 92 12.789 -38.992 0.213 1.00 15.75 C ANISOU 751 CB PRO A 92 1774 2321 1889 -140 130 -573 C ATOM 752 CG PRO A 92 12.524 -40.431 0.318 1.00 22.20 C ANISOU 752 CG PRO A 92 2580 3113 2742 -142 140 -552 C ATOM 753 CD PRO A 92 13.825 -41.155 0.223 1.00 18.05 C ANISOU 753 CD PRO A 92 2041 2562 2254 -137 136 -556 C ATOM 754 N ASN A 93 14.931 -36.974 2.156 1.00 15.60 N ANISOU 754 N ASN A 93 1766 2349 1813 -102 91 -567 N ATOM 755 CA ASN A 93 14.928 -36.189 3.391 1.00 16.13 C ANISOU 755 CA ASN A 93 1841 2447 1842 -88 79 -548 C ATOM 756 C ASN A 93 15.581 -36.863 4.605 1.00 17.10 C ANISOU 756 C ASN A 93 1957 2568 1973 -72 67 -515 C ATOM 757 O ASN A 93 15.361 -36.460 5.735 1.00 15.52 O ANISOU 757 O ASN A 93 1763 2391 1742 -63 59 -493 O ATOM 758 CB ASN A 93 13.493 -35.719 3.694 1.00 16.21 C ANISOU 758 CB ASN A 93 1860 2477 1822 -91 85 -539 C ATOM 759 CG ASN A 93 12.975 -34.770 2.630 1.00 19.04 C ANISOU 759 CG ASN A 93 2228 2842 2166 -103 90 -571 C ATOM 760 OD1 ASN A 93 13.764 -34.182 1.890 1.00 15.66 O ANISOU 760 OD1 ASN A 93 1802 2409 1737 -108 86 -599 O ATOM 761 ND2 ASN A 93 11.648 -34.609 2.550 1.00 15.29 N ANISOU 761 ND2 ASN A 93 1756 2375 1678 -110 98 -568 N ATOM 762 N ILE A 94 16.389 -37.889 4.370 1.00 14.72 N ANISOU 762 N ILE A 94 1642 2238 1713 -70 65 -513 N ATOM 763 CA ILE A 94 17.151 -38.512 5.458 1.00 11.60 C ANISOU 763 CA ILE A 94 1239 1838 1329 -55 50 -482 C ATOM 764 C ILE A 94 18.513 -37.817 5.534 1.00 11.64 C ANISOU 764 C ILE A 94 1241 1851 1331 -46 35 -501 C ATOM 765 O ILE A 94 19.142 -37.618 4.517 1.00 11.72 O ANISOU 765 O ILE A 94 1246 1848 1360 -52 40 -535 O ATOM 766 CB ILE A 94 17.398 -40.017 5.164 1.00 17.52 C ANISOU 766 CB ILE A 94 1974 2550 2132 -56 54 -470 C ATOM 767 CG1 ILE A 94 16.071 -40.746 4.877 1.00 15.03 C ANISOU 767 CG1 ILE A 94 1661 2225 1824 -68 72 -458 C ATOM 768 CG2 ILE A 94 18.211 -40.673 6.287 1.00 18.80 C ANISOU 768 CG2 ILE A 94 2130 2706 2309 -39 34 -437 C ATOM 769 CD1 ILE A 94 15.070 -40.683 6.012 1.00 15.09 C ANISOU 769 CD1 ILE A 94 1681 2256 1798 -65 71 -424 C ATOM 770 N ILE A 95 18.963 -37.449 6.729 1.00 11.55 N ANISOU 770 N ILE A 95 1234 1860 1296 -32 17 -479 N ATOM 771 CA ILE A 95 20.273 -36.826 6.849 1.00 11.13 C ANISOU 771 CA ILE A 95 1176 1814 1240 -23 2 -496 C ATOM 772 C ILE A 95 21.332 -37.781 6.289 1.00 12.75 C ANISOU 772 C ILE A 95 1361 1984 1500 -20 -1 -506 C ATOM 773 O ILE A 95 21.238 -39.009 6.461 1.00 12.96 O ANISOU 773 O ILE A 95 1378 1985 1561 -17 -2 -482 O ATOM 774 CB ILE A 95 20.597 -36.440 8.316 1.00 11.01 C ANISOU 774 CB ILE A 95 1166 1824 1192 -8 -18 -466 C ATOM 775 CG1 ILE A 95 21.732 -35.409 8.345 1.00 12.93 C ANISOU 775 CG1 ILE A 95 1408 2083 1420 -2 -29 -491 C ATOM 776 CG2 ILE A 95 20.946 -37.676 9.154 1.00 12.19 C ANISOU 776 CG2 ILE A 95 1306 1955 1369 2 -32 -427 C ATOM 777 CD1 ILE A 95 21.335 -34.035 7.849 1.00 14.05 C ANISOU 777 CD1 ILE A 95 1564 2249 1524 -11 -19 -522 C ATOM 778 N THR A 96 22.320 -37.220 5.597 1.00 15.31 N ANISOU 778 N THR A 96 1679 2304 1832 -22 -2 -543 N ATOM 779 CA THR A 96 23.376 -38.007 4.991 1.00 11.90 C ANISOU 779 CA THR A 96 1227 1841 1454 -21 -3 -560 C ATOM 780 C THR A 96 24.583 -38.136 5.907 1.00 14.24 C ANISOU 780 C THR A 96 1511 2138 1761 -2 -27 -546 C ATOM 781 O THR A 96 25.209 -37.147 6.294 1.00 18.06 O ANISOU 781 O THR A 96 1999 2646 2216 4 -39 -557 O ATOM 782 CB THR A 96 23.843 -37.402 3.650 1.00 16.26 C ANISOU 782 CB THR A 96 1777 2387 2013 -36 12 -612 C ATOM 783 OG1 THR A 96 22.788 -37.499 2.694 1.00 18.45 O ANISOU 783 OG1 THR A 96 2064 2658 2290 -55 33 -624 O ATOM 784 CG2 THR A 96 25.057 -38.150 3.111 1.00 21.88 C ANISOU 784 CG2 THR A 96 2466 3068 2780 -35 11 -633 C ATOM 785 N LEU A 97 24.894 -39.373 6.244 1.00 14.79 N ANISOU 785 N LEU A 97 1565 2180 1873 7 -36 -522 N ATOM 786 CA LEU A 97 26.129 -39.680 6.941 1.00 16.95 C ANISOU 786 CA LEU A 97 1823 2446 2171 25 -61 -512 C ATOM 787 C LEU A 97 27.234 -39.676 5.910 1.00 15.10 C ANISOU 787 C LEU A 97 1569 2192 1977 21 -55 -558 C ATOM 788 O LEU A 97 27.267 -40.522 5.022 1.00 16.78 O ANISOU 788 O LEU A 97 1768 2372 2236 13 -41 -574 O ATOM 789 CB LEU A 97 26.042 -41.055 7.595 1.00 19.71 C ANISOU 789 CB LEU A 97 2164 2770 2557 36 -74 -470 C ATOM 790 CG LEU A 97 27.300 -41.519 8.340 1.00 15.61 C ANISOU 790 CG LEU A 97 1626 2238 2068 55 -103 -455 C ATOM 791 CD1 LEU A 97 27.589 -40.640 9.545 1.00 14.71 C ANISOU 791 CD1 LEU A 97 1523 2160 1904 66 -127 -434 C ATOM 792 CD2 LEU A 97 27.125 -42.960 8.777 1.00 16.73 C ANISOU 792 CD2 LEU A 97 1760 2347 2251 63 -113 -416 C ATOM 793 N ALA A 98 28.141 -38.717 6.022 1.00 13.74 N ANISOU 793 N ALA A 98 1395 2038 1786 25 -65 -581 N ATOM 794 CA ALA A 98 29.205 -38.567 5.038 1.00 17.45 C ANISOU 794 CA ALA A 98 1848 2493 2289 19 -57 -630 C ATOM 795 C ALA A 98 30.426 -39.427 5.344 1.00 16.81 C ANISOU 795 C ALA A 98 1739 2386 2264 35 -76 -627 C ATOM 796 O ALA A 98 31.154 -39.845 4.436 1.00 17.32 O ANISOU 796 O ALA A 98 1781 2422 2375 29 -65 -663 O ATOM 797 CB ALA A 98 29.607 -37.117 4.930 1.00 19.68 C ANISOU 797 CB ALA A 98 2142 2808 2528 13 -56 -659 C ATOM 798 N ASP A 99 30.661 -39.699 6.621 1.00 14.01 N ANISOU 798 N ASP A 99 1381 2038 1904 55 -104 -585 N ATOM 799 CA ASP A 99 31.871 -40.404 7.001 1.00 16.23 C ANISOU 799 CA ASP A 99 1635 2296 2235 72 -128 -581 C ATOM 800 C ASP A 99 31.774 -40.806 8.464 1.00 18.17 C ANISOU 800 C ASP A 99 1886 2550 2469 91 -159 -524 C ATOM 801 O ASP A 99 30.901 -40.337 9.193 1.00 15.16 O ANISOU 801 O ASP A 99 1529 2197 2033 89 -162 -494 O ATOM 802 CB ASP A 99 33.071 -39.476 6.802 1.00 18.00 C ANISOU 802 CB ASP A 99 1848 2534 2456 74 -133 -622 C ATOM 803 CG ASP A 99 34.365 -40.223 6.489 1.00 17.41 C ANISOU 803 CG ASP A 99 1738 2426 2450 83 -143 -644 C ATOM 804 OD1 ASP A 99 34.409 -41.468 6.574 1.00 18.50 O ANISOU 804 OD1 ASP A 99 1860 2530 2641 93 -151 -624 O ATOM 805 OD2 ASP A 99 35.345 -39.540 6.140 1.00 19.56 O ANISOU 805 OD2 ASP A 99 1999 2706 2726 81 -143 -685 O ATOM 806 N ILE A 100 32.673 -41.688 8.887 1.00 17.05 N ANISOU 806 N ILE A 100 1720 2381 2377 108 -184 -510 N ATOM 807 CA ILE A 100 32.795 -42.056 10.288 1.00 13.66 C ANISOU 807 CA ILE A 100 1294 1958 1938 126 -219 -457 C ATOM 808 C ILE A 100 34.291 -42.111 10.553 1.00 14.50 C ANISOU 808 C ILE A 100 1373 2054 2082 143 -247 -470 C ATOM 809 O ILE A 100 35.022 -42.741 9.793 1.00 18.43 O ANISOU 809 O ILE A 100 1843 2518 2642 146 -242 -499 O ATOM 810 CB ILE A 100 32.230 -43.455 10.560 1.00 17.79 C ANISOU 810 CB ILE A 100 1815 2447 2496 131 -225 -415 C ATOM 811 CG1 ILE A 100 30.811 -43.592 10.009 1.00 21.92 C ANISOU 811 CG1 ILE A 100 2358 2970 2998 112 -192 -412 C ATOM 812 CG2 ILE A 100 32.272 -43.743 12.057 1.00 18.94 C ANISOU 812 CG2 ILE A 100 1971 2603 2623 146 -261 -358 C ATOM 813 CD1 ILE A 100 30.397 -45.041 9.730 1.00 22.93 C ANISOU 813 CD1 ILE A 100 2477 3055 3180 112 -186 -392 C ATOM 814 N VAL A 101 34.743 -41.435 11.601 1.00 12.67 N ANISOU 814 N VAL A 101 1148 1853 1812 154 -274 -451 N ATOM 815 CA VAL A 101 36.164 -41.418 11.940 1.00 12.95 C ANISOU 815 CA VAL A 101 1158 1883 1880 170 -303 -462 C ATOM 816 C VAL A 101 36.305 -41.701 13.429 1.00 19.18 C ANISOU 816 C VAL A 101 1954 2682 2652 186 -345 -405 C ATOM 817 O VAL A 101 35.346 -41.553 14.190 1.00 19.93 O ANISOU 817 O VAL A 101 2078 2800 2695 181 -346 -366 O ATOM 818 CB VAL A 101 36.833 -40.062 11.632 1.00 17.75 C ANISOU 818 CB VAL A 101 1765 2523 2457 164 -295 -509 C ATOM 819 CG1 VAL A 101 36.673 -39.683 10.143 1.00 17.91 C ANISOU 819 CG1 VAL A 101 1783 2536 2487 145 -254 -566 C ATOM 820 CG2 VAL A 101 36.281 -38.968 12.545 1.00 18.27 C ANISOU 820 CG2 VAL A 101 1861 2638 2442 160 -301 -486 C ATOM 821 N LYS A 102 37.501 -42.114 13.840 1.00 16.87 N ANISOU 821 N LYS A 102 1635 2373 2402 205 -378 -402 N ATOM 822 CA LYS A 102 37.788 -42.335 15.250 1.00 16.94 C ANISOU 822 CA LYS A 102 1650 2392 2395 220 -422 -349 C ATOM 823 C LYS A 102 38.310 -41.036 15.830 1.00 21.09 C ANISOU 823 C LYS A 102 2183 2964 2867 220 -434 -361 C ATOM 824 O LYS A 102 39.368 -40.550 15.421 1.00 22.12 O ANISOU 824 O LYS A 102 2290 3096 3018 225 -437 -404 O ATOM 825 CB LYS A 102 38.858 -43.425 15.418 1.00 19.34 C ANISOU 825 CB LYS A 102 1919 2654 2775 241 -457 -339 C ATOM 826 CG LYS A 102 38.492 -44.754 14.770 1.00 29.98 C ANISOU 826 CG LYS A 102 3254 3950 4186 242 -445 -333 C ATOM 827 CD LYS A 102 39.469 -45.859 15.165 1.00 44.03 C ANISOU 827 CD LYS A 102 5003 5688 6038 265 -485 -312 C ATOM 828 CE LYS A 102 39.078 -47.185 14.531 1.00 45.45 C ANISOU 828 CE LYS A 102 5171 5816 6281 266 -472 -306 C ATOM 829 NZ LYS A 102 39.629 -48.348 15.281 1.00 50.62 N ANISOU 829 NZ LYS A 102 5809 6433 6990 288 -517 -262 N ATOM 830 N ASP A 103 37.599 -40.469 16.791 1.00 15.74 N ANISOU 830 N ASP A 103 1638 1947 2394 -55 -449 -203 N ATOM 831 CA ASP A 103 38.127 -39.275 17.428 1.00 16.68 C ANISOU 831 CA ASP A 103 1733 2018 2587 -73 -484 -223 C ATOM 832 C ASP A 103 39.247 -39.661 18.407 1.00 19.33 C ANISOU 832 C ASP A 103 2059 2352 2932 -86 -522 -247 C ATOM 833 O ASP A 103 39.066 -40.527 19.260 1.00 19.43 O ANISOU 833 O ASP A 103 2103 2390 2888 -81 -538 -286 O ATOM 834 CB ASP A 103 37.035 -38.463 18.117 1.00 13.90 C ANISOU 834 CB ASP A 103 1406 1643 2234 -74 -499 -269 C ATOM 835 CG ASP A 103 37.561 -37.160 18.663 1.00 22.96 C ANISOU 835 CG ASP A 103 2529 2735 3459 -93 -532 -286 C ATOM 836 OD1 ASP A 103 37.670 -36.192 17.884 1.00 23.60 O ANISOU 836 OD1 ASP A 103 2582 2786 3598 -99 -519 -252 O ATOM 837 OD2 ASP A 103 37.881 -37.098 19.867 1.00 24.50 O ANISOU 837 OD2 ASP A 103 2735 2917 3657 -104 -572 -333 O ATOM 838 N PRO A 104 40.417 -39.021 18.279 1.00 21.38 N ANISOU 838 N PRO A 104 2275 2584 3264 -102 -538 -224 N ATOM 839 CA PRO A 104 41.566 -39.448 19.084 1.00 20.53 C ANISOU 839 CA PRO A 104 2154 2479 3166 -114 -571 -238 C ATOM 840 C PRO A 104 41.509 -38.921 20.523 1.00 20.26 C ANISOU 840 C PRO A 104 2137 2418 3145 -130 -620 -300 C ATOM 841 O PRO A 104 42.218 -39.426 21.399 1.00 23.15 O ANISOU 841 O PRO A 104 2502 2793 3500 -138 -650 -324 O ATOM 842 CB PRO A 104 42.746 -38.820 18.338 1.00 22.97 C ANISOU 842 CB PRO A 104 2409 2766 3551 -127 -569 -185 C ATOM 843 CG PRO A 104 42.186 -37.543 17.813 1.00 21.03 C ANISOU 843 CG PRO A 104 2152 2481 3356 -134 -560 -174 C ATOM 844 CD PRO A 104 40.742 -37.862 17.425 1.00 16.97 C ANISOU 844 CD PRO A 104 1677 1988 2781 -112 -527 -183 C ATOM 845 N VAL A 105 40.686 -37.905 20.756 1.00 14.93 N ANISOU 845 N VAL A 105 1474 1710 2490 -134 -627 -326 N ATOM 846 CA VAL A 105 40.521 -37.351 22.096 1.00 14.93 C ANISOU 846 CA VAL A 105 1493 1681 2499 -148 -671 -386 C ATOM 847 C VAL A 105 39.449 -38.097 22.887 1.00 19.26 C ANISOU 847 C VAL A 105 2093 2258 2968 -132 -673 -436 C ATOM 848 O VAL A 105 39.673 -38.473 24.034 1.00 21.24 O ANISOU 848 O VAL A 105 2360 2513 3196 -138 -707 -481 O ATOM 849 CB VAL A 105 40.196 -35.831 22.062 1.00 18.21 C ANISOU 849 CB VAL A 105 1899 2042 2978 -160 -681 -392 C ATOM 850 CG1 VAL A 105 39.957 -35.311 23.474 1.00 18.50 C ANISOU 850 CG1 VAL A 105 1963 2050 3017 -171 -725 -458 C ATOM 851 CG2 VAL A 105 41.335 -35.052 21.407 1.00 18.80 C ANISOU 851 CG2 VAL A 105 1924 2086 3135 -179 -684 -346 C ATOM 852 N SER A 106 38.283 -38.316 22.279 1.00 20.03 N ANISOU 852 N SER A 106 2214 2376 3022 -112 -638 -428 N ATOM 853 CA SER A 106 37.201 -38.978 22.995 1.00 20.51 C ANISOU 853 CA SER A 106 2322 2464 3007 -98 -639 -473 C ATOM 854 C SER A 106 37.412 -40.488 23.038 1.00 26.82 C ANISOU 854 C SER A 106 3137 3315 3739 -87 -630 -470 C ATOM 855 O SER A 106 36.862 -41.174 23.908 1.00 27.67 O ANISOU 855 O SER A 106 3280 3445 3786 -80 -643 -513 O ATOM 856 CB SER A 106 35.854 -38.684 22.337 1.00 15.10 C ANISOU 856 CB SER A 106 1655 1784 2297 -81 -606 -463 C ATOM 857 OG SER A 106 35.819 -39.254 21.046 1.00 15.77 O ANISOU 857 OG SER A 106 1729 1898 2365 -70 -563 -408 O ATOM 858 N ARG A 107 38.199 -40.999 22.089 1.00 20.61 N ANISOU 858 N ARG A 107 2323 2545 2962 -85 -607 -417 N ATOM 859 CA ARG A 107 38.417 -42.435 21.952 1.00 22.22 C ANISOU 859 CA ARG A 107 2543 2797 3102 -73 -593 -406 C ATOM 860 C ARG A 107 37.098 -43.122 21.613 1.00 27.32 C ANISOU 860 C ARG A 107 3229 3478 3672 -55 -562 -410 C ATOM 861 O ARG A 107 36.841 -44.248 22.036 1.00 31.57 O ANISOU 861 O ARG A 107 3799 4053 4141 -46 -563 -430 O ATOM 862 CB ARG A 107 39.023 -43.010 23.240 1.00 27.91 C ANISOU 862 CB ARG A 107 3274 3526 3803 -81 -632 -450 C ATOM 863 CG ARG A 107 40.292 -42.276 23.706 1.00 33.68 C ANISOU 863 CG ARG A 107 3967 4222 4609 -103 -668 -451 C ATOM 864 CD ARG A 107 40.730 -42.707 25.107 1.00 35.10 C ANISOU 864 CD ARG A 107 4161 4406 4769 -112 -710 -502 C ATOM 865 NE ARG A 107 41.056 -44.130 25.149 1.00 27.37 N ANISOU 865 NE ARG A 107 3196 3474 3730 -99 -701 -495 N ATOM 866 CZ ARG A 107 42.144 -44.646 24.603 1.00 29.03 C ANISOU 866 CZ ARG A 107 3377 3699 3954 -98 -691 -452 C ATOM 867 NH1 ARG A 107 43.000 -43.850 23.983 1.00 30.32 N ANISOU 867 NH1 ARG A 107 3493 3835 4190 -110 -690 -412 N ATOM 868 NH2 ARG A 107 42.375 -45.948 24.673 1.00 28.45 N ANISOU 868 NH2 ARG A 107 3320 3666 3822 -84 -681 -448 N ATOM 869 N THR A 108 36.265 -42.426 20.844 1.00 22.72 N ANISOU 869 N THR A 108 2646 2885 3104 -50 -537 -390 N ATOM 870 CA THR A 108 34.984 -42.957 20.399 1.00 19.54 C ANISOU 870 CA THR A 108 2276 2514 2633 -34 -506 -387 C ATOM 871 C THR A 108 34.765 -42.583 18.938 1.00 20.95 C ANISOU 871 C THR A 108 2435 2691 2835 -28 -465 -329 C ATOM 872 O THR A 108 35.482 -41.740 18.393 1.00 17.29 O ANISOU 872 O THR A 108 1932 2196 2443 -37 -463 -298 O ATOM 873 CB THR A 108 33.813 -42.387 21.226 1.00 21.06 C ANISOU 873 CB THR A 108 2498 2696 2810 -32 -522 -436 C ATOM 874 OG1 THR A 108 33.752 -40.969 21.050 1.00 19.03 O ANISOU 874 OG1 THR A 108 2217 2393 2623 -39 -526 -431 O ATOM 875 CG2 THR A 108 33.996 -42.696 22.701 1.00 26.62 C ANISOU 875 CG2 THR A 108 3222 3400 3491 -37 -564 -495 C ATOM 876 N PRO A 109 33.764 -43.197 18.300 1.00 21.75 N ANISOU 876 N PRO A 109 2562 2826 2876 -15 -432 -313 N ATOM 877 CA PRO A 109 33.491 -42.855 16.903 1.00 18.62 C ANISOU 877 CA PRO A 109 2148 2429 2497 -10 -393 -258 C ATOM 878 C PRO A 109 32.887 -41.470 16.793 1.00 16.15 C ANISOU 878 C PRO A 109 1821 2080 2236 -13 -393 -261 C ATOM 879 O PRO A 109 32.127 -41.038 17.676 1.00 20.30 O ANISOU 879 O PRO A 109 2367 2596 2751 -13 -413 -305 O ATOM 880 CB PRO A 109 32.468 -43.915 16.470 1.00 18.07 C ANISOU 880 CB PRO A 109 2118 2408 2341 3 -364 -250 C ATOM 881 CG PRO A 109 32.593 -45.009 17.486 1.00 23.41 C ANISOU 881 CG PRO A 109 2826 3111 2957 4 -386 -290 C ATOM 882 CD PRO A 109 32.919 -44.307 18.769 1.00 17.86 C ANISOU 882 CD PRO A 109 2116 2376 2293 -6 -430 -341 C ATOM 883 N ALA A 110 33.225 -40.789 15.705 1.00 14.15 N ANISOU 883 N ALA A 110 1533 1807 2037 -15 -370 -212 N ATOM 884 CA ALA A 110 32.703 -39.468 15.404 1.00 13.72 C ANISOU 884 CA ALA A 110 1462 1717 2034 -17 -365 -205 C ATOM 885 C ALA A 110 31.998 -39.555 14.059 1.00 18.00 C ANISOU 885 C ALA A 110 2002 2279 2557 -6 -319 -155 C ATOM 886 O ALA A 110 32.630 -39.800 13.039 1.00 14.93 O ANISOU 886 O ALA A 110 1591 1897 2184 -6 -295 -106 O ATOM 887 CB ALA A 110 33.820 -38.443 15.352 1.00 15.53 C ANISOU 887 CB ALA A 110 1648 1899 2354 -31 -382 -191 C ATOM 888 N LEU A 111 30.683 -39.369 14.063 1.00 16.18 N ANISOU 888 N LEU A 111 1797 2061 2291 3 -307 -167 N ATOM 889 CA LEU A 111 29.911 -39.402 12.827 1.00 17.34 C ANISOU 889 CA LEU A 111 1943 2228 2418 12 -264 -121 C ATOM 890 C LEU A 111 29.906 -38.036 12.157 1.00 18.10 C ANISOU 890 C LEU A 111 2005 2284 2589 10 -253 -93 C ATOM 891 O LEU A 111 29.638 -37.012 12.804 1.00 17.83 O ANISOU 891 O LEU A 111 1968 2214 2594 7 -273 -122 O ATOM 892 CB LEU A 111 28.462 -39.835 13.092 1.00 16.33 C ANISOU 892 CB LEU A 111 1855 2134 2215 22 -255 -142 C ATOM 893 CG LEU A 111 28.202 -41.069 13.959 1.00 17.60 C ANISOU 893 CG LEU A 111 2057 2334 2297 24 -270 -180 C ATOM 894 CD1 LEU A 111 26.707 -41.375 13.972 1.00 14.61 C ANISOU 894 CD1 LEU A 111 1713 1989 1850 33 -255 -189 C ATOM 895 CD2 LEU A 111 28.984 -42.265 13.487 1.00 19.53 C ANISOU 895 CD2 LEU A 111 2304 2606 2509 23 -259 -155 C ATOM 896 N VAL A 112 30.169 -38.024 10.853 1.00 13.13 N ANISOU 896 N VAL A 112 1352 1660 1978 11 -220 -35 N ATOM 897 CA VAL A 112 30.215 -36.786 10.081 1.00 15.18 C ANISOU 897 CA VAL A 112 1577 1883 2309 9 -205 -1 C ATOM 898 C VAL A 112 28.989 -36.714 9.183 1.00 15.06 C ANISOU 898 C VAL A 112 1571 1890 2260 20 -168 28 C ATOM 899 O VAL A 112 28.768 -37.600 8.355 1.00 16.67 O ANISOU 899 O VAL A 112 1785 2132 2415 25 -139 61 O ATOM 900 CB VAL A 112 31.479 -36.734 9.217 1.00 14.05 C ANISOU 900 CB VAL A 112 1394 1727 2218 2 -195 46 C ATOM 901 CG1 VAL A 112 31.563 -35.402 8.457 1.00 18.45 C ANISOU 901 CG1 VAL A 112 1914 2244 2852 -1 -182 80 C ATOM 902 CG2 VAL A 112 32.707 -36.953 10.085 1.00 12.94 C ANISOU 902 CG2 VAL A 112 1244 1572 2103 -9 -231 21 C ATOM 903 N PHE A 113 28.193 -35.667 9.358 1.00 12.23 N ANISOU 903 N PHE A 113 1213 1508 1927 24 -169 16 N ATOM 904 CA PHE A 113 26.921 -35.514 8.624 1.00 13.54 C ANISOU 904 CA PHE A 113 1388 1695 2060 35 -137 40 C ATOM 905 C PHE A 113 26.944 -34.299 7.712 1.00 19.03 C ANISOU 905 C PHE A 113 2048 2356 2825 36 -117 80 C ATOM 906 O PHE A 113 27.703 -33.339 7.932 1.00 13.98 O ANISOU 906 O PHE A 113 1382 1669 2261 28 -135 75 O ATOM 907 CB PHE A 113 25.746 -35.309 9.586 1.00 13.58 C ANISOU 907 CB PHE A 113 1425 1707 2028 44 -150 -7 C ATOM 908 CG PHE A 113 25.487 -36.461 10.493 1.00 14.71 C ANISOU 908 CG PHE A 113 1606 1886 2096 45 -168 -47 C ATOM 909 CD1 PHE A 113 24.661 -37.501 10.092 1.00 16.37 C ANISOU 909 CD1 PHE A 113 1845 2150 2227 51 -145 -33 C ATOM 910 CD2 PHE A 113 26.023 -36.485 11.769 1.00 16.63 C ANISOU 910 CD2 PHE A 113 1860 2111 2349 39 -207 -99 C ATOM 911 CE1 PHE A 113 24.390 -38.552 10.943 1.00 17.88 C ANISOU 911 CE1 PHE A 113 2071 2374 2347 51 -162 -71 C ATOM 912 CE2 PHE A 113 25.770 -37.542 12.622 1.00 12.89 C ANISOU 912 CE2 PHE A 113 1421 1671 1806 41 -224 -137 C ATOM 913 CZ PHE A 113 24.953 -38.577 12.209 1.00 16.56 C ANISOU 913 CZ PHE A 113 1913 2189 2191 47 -201 -122 C ATOM 914 N GLU A 114 26.082 -34.324 6.704 1.00 13.90 N ANISOU 914 N GLU A 114 1400 1731 2151 44 -81 119 N ATOM 915 CA GLU A 114 25.899 -33.160 5.865 1.00 16.51 C ANISOU 915 CA GLU A 114 1700 2032 2540 47 -60 155 C ATOM 916 C GLU A 114 25.475 -31.998 6.758 1.00 18.96 C ANISOU 916 C GLU A 114 2013 2302 2890 50 -83 116 C ATOM 917 O GLU A 114 24.819 -32.187 7.791 1.00 18.28 O ANISOU 917 O GLU A 114 1958 2225 2763 56 -102 69 O ATOM 918 CB GLU A 114 24.819 -33.440 4.803 1.00 24.79 C ANISOU 918 CB GLU A 114 2756 3120 3543 56 -19 197 C ATOM 919 CG GLU A 114 23.413 -33.146 5.268 1.00 20.07 C ANISOU 919 CG GLU A 114 2183 2535 2907 68 -17 173 C ATOM 920 CD GLU A 114 22.336 -33.527 4.250 1.00 25.31 C ANISOU 920 CD GLU A 114 2855 3243 3518 75 21 214 C ATOM 921 OE1 GLU A 114 21.939 -32.672 3.433 1.00 30.42 O ANISOU 921 OE1 GLU A 114 3480 3877 4201 81 45 250 O ATOM 922 OE2 GLU A 114 21.859 -34.678 4.296 1.00 18.47 O ANISOU 922 OE2 GLU A 114 2019 2425 2574 75 27 210 O ATOM 923 N HIS A 115 25.849 -30.790 6.370 1.00 18.34 N ANISOU 923 N HIS A 115 1902 2177 2888 47 -81 136 N ATOM 924 CA HIS A 115 25.497 -29.610 7.140 1.00 20.92 C ANISOU 924 CA HIS A 115 2232 2459 3256 51 -101 102 C ATOM 925 C HIS A 115 24.212 -29.019 6.579 1.00 16.44 C ANISOU 925 C HIS A 115 1668 1900 2677 67 -71 123 C ATOM 926 O HIS A 115 24.087 -28.840 5.365 1.00 20.12 O ANISOU 926 O HIS A 115 2112 2374 3157 69 -38 175 O ATOM 927 CB HIS A 115 26.632 -28.588 7.052 1.00 24.21 C ANISOU 927 CB HIS A 115 2614 2819 3766 37 -117 112 C ATOM 928 CG HIS A 115 26.359 -27.307 7.776 1.00 25.64 C ANISOU 928 CG HIS A 115 2798 2949 3995 40 -137 80 C ATOM 929 ND1 HIS A 115 25.636 -26.276 7.212 1.00 21.34 N ANISOU 929 ND1 HIS A 115 2245 2383 3480 51 -115 102 N ATOM 930 CD2 HIS A 115 26.727 -26.879 9.007 1.00 24.97 C ANISOU 930 CD2 HIS A 115 2727 2828 3933 33 -177 28 C ATOM 931 CE1 HIS A 115 25.561 -25.273 8.068 1.00 21.73 C ANISOU 931 CE1 HIS A 115 2303 2385 3568 51 -140 65 C ATOM 932 NE2 HIS A 115 26.204 -25.617 9.170 1.00 21.36 N ANISOU 932 NE2 HIS A 115 2271 2329 3518 40 -178 19 N ATOM 933 N VAL A 116 23.257 -28.731 7.461 1.00 16.11 N ANISOU 933 N VAL A 116 1654 1858 2608 79 -82 82 N ATOM 934 CA VAL A 116 22.003 -28.097 7.069 1.00 18.56 C ANISOU 934 CA VAL A 116 1970 2175 2908 97 -56 98 C ATOM 935 C VAL A 116 21.928 -26.671 7.612 1.00 22.46 C ANISOU 935 C VAL A 116 2460 2611 3465 103 -71 75 C ATOM 936 O VAL A 116 21.982 -26.449 8.819 1.00 26.60 O ANISOU 936 O VAL A 116 3005 3112 3991 103 -104 22 O ATOM 937 CB VAL A 116 20.777 -28.902 7.567 1.00 21.44 C ANISOU 937 CB VAL A 116 2371 2591 3183 110 -51 75 C ATOM 938 CG1 VAL A 116 19.478 -28.216 7.149 1.00 22.86 C ANISOU 938 CG1 VAL A 116 2553 2780 3353 129 -24 95 C ATOM 939 CG2 VAL A 116 20.815 -30.314 7.019 1.00 23.08 C ANISOU 939 CG2 VAL A 116 2587 2856 3326 103 -36 97 C ATOM 940 N ASN A 117 21.828 -25.699 6.718 1.00 22.55 N ANISOU 940 N ASN A 117 2445 2596 3529 107 -48 115 N ATOM 941 CA ASN A 117 21.680 -24.314 7.146 1.00 19.94 C ANISOU 941 CA ASN A 117 2112 2208 3256 114 -59 98 C ATOM 942 C ASN A 117 20.259 -24.063 7.631 1.00 24.70 C ANISOU 942 C ASN A 117 2744 2828 3815 138 -50 76 C ATOM 943 O ASN A 117 19.460 -23.442 6.932 1.00 26.34 O ANISOU 943 O ASN A 117 2942 3036 4029 153 -21 109 O ATOM 944 CB ASN A 117 22.031 -23.366 6.001 1.00 28.30 C ANISOU 944 CB ASN A 117 3133 3234 4385 110 -37 150 C ATOM 945 CG ASN A 117 21.966 -21.913 6.414 1.00 36.42 C ANISOU 945 CG ASN A 117 4160 4200 5477 116 -49 133 C ATOM 946 OD1 ASN A 117 22.095 -21.589 7.596 1.00 43.08 O ANISOU 946 OD1 ASN A 117 5026 5013 6329 116 -82 80 O ATOM 947 ND2 ASN A 117 21.762 -21.025 5.444 1.00 41.10 N ANISOU 947 ND2 ASN A 117 4729 4772 6115 122 -21 177 N ATOM 948 N ASN A 118 19.935 -24.553 8.825 1.00 20.82 N ANISOU 948 N ASN A 118 2285 2349 3275 143 -75 23 N ATOM 949 CA ASN A 118 18.545 -24.502 9.284 1.00 30.46 C ANISOU 949 CA ASN A 118 3534 3596 4443 167 -65 5 C ATOM 950 C ASN A 118 18.199 -23.254 10.089 1.00 31.03 C ANISOU 950 C ASN A 118 3620 3617 4553 182 -80 -29 C ATOM 951 O ASN A 118 19.075 -22.466 10.452 1.00 30.53 O ANISOU 951 O ASN A 118 3549 3494 4556 171 -104 -47 O ATOM 952 CB ASN A 118 18.182 -25.756 10.090 1.00 23.22 C ANISOU 952 CB ASN A 118 2648 2730 3444 167 -80 -30 C ATOM 953 CG ASN A 118 18.701 -25.700 11.503 1.00 25.83 C ANISOU 953 CG ASN A 118 3001 3030 3782 163 -123 -94 C ATOM 954 OD1 ASN A 118 19.862 -25.363 11.731 1.00 26.50 O ANISOU 954 OD1 ASN A 118 3074 3072 3924 145 -147 -106 O ATOM 955 ND2 ASN A 118 17.838 -26.003 12.468 1.00 26.57 N ANISOU 955 ND2 ASN A 118 3128 3147 3819 178 -133 -134 N ATOM 956 N THR A 119 16.904 -23.081 10.346 1.00 25.53 N ANISOU 956 N THR A 119 2945 2943 3814 207 -65 -37 N ATOM 957 CA THR A 119 16.417 -22.084 11.282 1.00 23.06 C ANISOU 957 CA THR A 119 2654 2590 3520 226 -79 -76 C ATOM 958 C THR A 119 15.829 -22.852 12.459 1.00 23.83 C ANISOU 958 C THR A 119 2788 2722 3546 236 -98 -126 C ATOM 959 O THR A 119 14.883 -23.628 12.279 1.00 30.50 O ANISOU 959 O THR A 119 3642 3627 4321 247 -79 -114 O ATOM 960 CB THR A 119 15.299 -21.213 10.648 1.00 37.02 C ANISOU 960 CB THR A 119 4415 4357 5293 253 -43 -43 C ATOM 961 OG1 THR A 119 15.808 -20.513 9.502 1.00 31.49 O ANISOU 961 OG1 THR A 119 3680 3628 4658 244 -23 7 O ATOM 962 CG2 THR A 119 14.760 -20.211 11.660 1.00 34.55 C ANISOU 962 CG2 THR A 119 4129 4003 4994 276 -57 -85 C ATOM 963 N ASP A 120 16.379 -22.658 13.655 1.00 23.65 N ANISOU 963 N ASP A 120 2786 2662 3539 231 -137 -182 N ATOM 964 CA ASP A 120 15.913 -23.410 14.820 1.00 26.93 C ANISOU 964 CA ASP A 120 3236 3109 3889 238 -158 -231 C ATOM 965 C ASP A 120 14.393 -23.348 14.945 1.00 26.22 C ANISOU 965 C ASP A 120 3165 3056 3743 270 -134 -229 C ATOM 966 O ASP A 120 13.772 -22.328 14.645 1.00 30.45 O ANISOU 966 O ASP A 120 3696 3568 4304 290 -114 -212 O ATOM 967 CB ASP A 120 16.557 -22.922 16.117 1.00 28.82 C ANISOU 967 CB ASP A 120 3497 3295 4158 234 -201 -292 C ATOM 968 CG ASP A 120 16.245 -23.838 17.296 1.00 33.04 C ANISOU 968 CG ASP A 120 4064 3864 4624 237 -224 -343 C ATOM 969 OD1 ASP A 120 16.764 -24.977 17.315 1.00 33.53 O ANISOU 969 OD1 ASP A 120 4125 3962 4655 219 -235 -345 O ATOM 970 OD2 ASP A 120 15.483 -23.424 18.198 1.00 34.32 O ANISOU 970 OD2 ASP A 120 4256 4018 4766 260 -232 -379 O ATOM 971 N PHE A 121 13.797 -24.444 15.399 1.00 24.15 N ANISOU 971 N PHE A 121 2923 2852 3402 273 -136 -245 N ATOM 972 CA PHE A 121 12.345 -24.525 15.436 1.00 21.75 C ANISOU 972 CA PHE A 121 2633 2593 3038 301 -113 -237 C ATOM 973 C PHE A 121 11.775 -23.470 16.378 1.00 23.66 C ANISOU 973 C PHE A 121 2898 2797 3295 328 -122 -274 C ATOM 974 O PHE A 121 10.662 -22.990 16.179 1.00 27.82 O ANISOU 974 O PHE A 121 3428 3339 3804 355 -96 -256 O ATOM 975 CB PHE A 121 11.876 -25.931 15.814 1.00 23.07 C ANISOU 975 CB PHE A 121 2819 2829 3118 297 -117 -249 C ATOM 976 CG PHE A 121 12.101 -26.289 17.254 1.00 25.13 C ANISOU 976 CG PHE A 121 3111 3083 3355 296 -155 -314 C ATOM 977 CD1 PHE A 121 11.094 -26.106 18.194 1.00 23.30 C ANISOU 977 CD1 PHE A 121 2908 2864 3082 323 -160 -347 C ATOM 978 CD2 PHE A 121 13.311 -26.830 17.670 1.00 28.69 C ANISOU 978 CD2 PHE A 121 3563 3517 3822 270 -187 -341 C ATOM 979 CE1 PHE A 121 11.296 -26.439 19.526 1.00 23.90 C ANISOU 979 CE1 PHE A 121 3012 2934 3133 323 -195 -407 C ATOM 980 CE2 PHE A 121 13.513 -27.167 19.002 1.00 26.79 C ANISOU 980 CE2 PHE A 121 3351 3271 3558 270 -222 -400 C ATOM 981 CZ PHE A 121 12.498 -26.967 19.927 1.00 25.78 C ANISOU 981 CZ PHE A 121 3252 3155 3389 296 -226 -434 C ATOM 982 N LYS A 122 12.555 -23.088 17.383 1.00 30.38 N ANISOU 982 N LYS A 122 3766 3597 4181 321 -159 -325 N ATOM 983 CA LYS A 122 12.132 -22.049 18.319 1.00 32.67 C ANISOU 983 CA LYS A 122 4082 3843 4490 346 -170 -364 C ATOM 984 C LYS A 122 11.921 -20.682 17.664 1.00 41.90 C ANISOU 984 C LYS A 122 5236 4964 5719 362 -147 -334 C ATOM 985 O LYS A 122 11.182 -19.851 18.194 1.00 45.71 O ANISOU 985 O LYS A 122 5740 5424 6202 392 -143 -352 O ATOM 986 CB LYS A 122 13.126 -21.926 19.467 1.00 37.99 C ANISOU 986 CB LYS A 122 4775 4468 5191 331 -216 -423 C ATOM 987 CG LYS A 122 13.076 -23.079 20.447 1.00 44.58 C ANISOU 987 CG LYS A 122 5634 5345 5960 326 -241 -465 C ATOM 988 CD LYS A 122 11.936 -22.923 21.438 1.00 55.39 C ANISOU 988 CD LYS A 122 7038 6729 7279 359 -242 -500 C ATOM 989 CE LYS A 122 12.174 -23.821 22.635 1.00 61.85 C ANISOU 989 CE LYS A 122 7883 7568 8050 350 -276 -554 C ATOM 990 NZ LYS A 122 13.628 -23.838 22.973 1.00 63.05 N ANISOU 990 NZ LYS A 122 8030 7674 8252 319 -313 -580 N ATOM 991 N GLN A 123 12.574 -20.442 16.528 1.00 40.19 N ANISOU 991 N GLN A 123 4986 4732 5554 344 -133 -289 N ATOM 992 CA GLN A 123 12.338 -19.217 15.756 1.00 42.13 C ANISOU 992 CA GLN A 123 5215 4937 5855 358 -107 -253 C ATOM 993 C GLN A 123 11.438 -19.467 14.549 1.00 34.13 C ANISOU 993 C GLN A 123 4178 3978 4812 369 -62 -191 C ATOM 994 O GLN A 123 10.647 -18.611 14.166 1.00 41.66 O ANISOU 994 O GLN A 123 5129 4922 5778 395 -35 -167 O ATOM 995 CB GLN A 123 13.657 -18.592 15.287 1.00 53.75 C ANISOU 995 CB GLN A 123 6663 6348 7411 331 -120 -241 C ATOM 996 CG GLN A 123 13.475 -17.520 14.203 1.00 64.11 C ANISOU 996 CG GLN A 123 7950 7630 8778 340 -89 -191 C ATOM 997 CD GLN A 123 14.786 -16.886 13.747 1.00 71.16 C ANISOU 997 CD GLN A 123 8819 8462 9755 312 -103 -179 C ATOM 998 OE1 GLN A 123 15.835 -17.076 14.370 1.00 74.87 O ANISOU 998 OE1 GLN A 123 9294 8904 10248 288 -139 -212 O ATOM 999 NE2 GLN A 123 14.729 -16.127 12.653 1.00 65.45 N ANISOU 999 NE2 GLN A 123 8069 7720 9078 316 -74 -129 N ATOM 1000 N LEU A 124 11.559 -20.650 13.953 1.00 26.63 N ANISOU 1000 N LEU A 124 3213 3085 3821 350 -54 -165 N ATOM 1001 CA LEU A 124 10.862 -20.961 12.710 1.00 22.62 C ANISOU 1001 CA LEU A 124 2680 2626 3287 355 -13 -104 C ATOM 1002 C LEU A 124 9.352 -21.164 12.855 1.00 24.56 C ANISOU 1002 C LEU A 124 2942 2927 3464 384 10 -96 C ATOM 1003 O LEU A 124 8.578 -20.676 12.037 1.00 25.63 O ANISOU 1003 O LEU A 124 3062 3077 3601 401 45 -51 O ATOM 1004 CB LEU A 124 11.475 -22.198 12.058 1.00 22.93 C ANISOU 1004 CB LEU A 124 2704 2708 3301 325 -12 -80 C ATOM 1005 CG LEU A 124 10.905 -22.567 10.690 1.00 25.19 C ANISOU 1005 CG LEU A 124 2965 3044 3563 324 28 -15 C ATOM 1006 CD1 LEU A 124 11.267 -21.499 9.679 1.00 25.67 C ANISOU 1006 CD1 LEU A 124 2994 3060 3698 323 49 28 C ATOM 1007 CD2 LEU A 124 11.437 -23.922 10.244 1.00 27.28 C ANISOU 1007 CD2 LEU A 124 3222 3353 3789 296 25 0 C ATOM 1008 N TYR A 125 8.931 -21.888 13.884 1.00 25.83 N ANISOU 1008 N TYR A 125 3131 3120 3562 390 -8 -137 N ATOM 1009 CA TYR A 125 7.527 -22.269 13.993 1.00 24.24 C ANISOU 1009 CA TYR A 125 2942 2981 3288 415 13 -126 C ATOM 1010 C TYR A 125 6.575 -21.076 14.050 1.00 28.43 C ANISOU 1010 C TYR A 125 3477 3491 3835 452 34 -118 C ATOM 1011 O TYR A 125 5.461 -21.146 13.539 1.00 26.99 O ANISOU 1011 O TYR A 125 3286 3357 3611 470 65 -80 O ATOM 1012 CB TYR A 125 7.299 -23.210 15.177 1.00 28.48 C ANISOU 1012 CB TYR A 125 3511 3553 3759 414 -14 -176 C ATOM 1013 CG TYR A 125 7.733 -24.638 14.914 1.00 24.19 C ANISOU 1013 CG TYR A 125 2963 3057 3169 384 -22 -169 C ATOM 1014 CD1 TYR A 125 8.639 -24.937 13.905 1.00 29.65 C ANISOU 1014 CD1 TYR A 125 3629 3743 3894 356 -16 -135 C ATOM 1015 CD2 TYR A 125 7.214 -25.685 15.664 1.00 22.39 C ANISOU 1015 CD2 TYR A 125 2759 2883 2865 384 -35 -196 C ATOM 1016 CE1 TYR A 125 9.033 -26.246 13.663 1.00 26.87 C ANISOU 1016 CE1 TYR A 125 3276 3434 3498 330 -22 -128 C ATOM 1017 CE2 TYR A 125 7.593 -26.992 15.431 1.00 22.20 C ANISOU 1017 CE2 TYR A 125 2736 2903 2798 357 -42 -189 C ATOM 1018 CZ TYR A 125 8.506 -27.268 14.431 1.00 21.99 C ANISOU 1018 CZ TYR A 125 2684 2867 2804 331 -35 -156 C ATOM 1019 OH TYR A 125 8.884 -28.571 14.196 1.00 26.49 O ANISOU 1019 OH TYR A 125 3256 3478 3329 306 -41 -150 O ATOM 1020 N GLN A 126 7.001 -19.974 14.651 1.00 26.10 N ANISOU 1020 N GLN A 126 3194 3126 3599 463 18 -150 N ATOM 1021 CA GLN A 126 6.097 -18.830 14.741 1.00 33.26 C ANISOU 1021 CA GLN A 126 4108 4011 4520 502 39 -143 C ATOM 1022 C GLN A 126 6.057 -17.980 13.469 1.00 29.17 C ANISOU 1022 C GLN A 126 3557 3471 4054 505 73 -85 C ATOM 1023 O GLN A 126 5.333 -16.989 13.401 1.00 29.39 O ANISOU 1023 O GLN A 126 3588 3481 4098 537 94 -72 O ATOM 1024 CB GLN A 126 6.431 -17.966 15.950 1.00 44.05 C ANISOU 1024 CB GLN A 126 5505 5311 5921 516 11 -202 C ATOM 1025 CG GLN A 126 7.863 -17.509 15.994 1.00 47.35 C ANISOU 1025 CG GLN A 126 5919 5658 6415 488 -17 -221 C ATOM 1026 CD GLN A 126 8.249 -17.032 17.371 1.00 53.71 C ANISOU 1026 CD GLN A 126 6761 6410 7236 494 -54 -288 C ATOM 1027 OE1 GLN A 126 7.478 -17.178 18.322 1.00 58.27 O ANISOU 1027 OE1 GLN A 126 7368 7008 7764 519 -60 -322 O ATOM 1028 NE2 GLN A 126 9.439 -16.455 17.492 1.00 49.81 N ANISOU 1028 NE2 GLN A 126 6266 5849 6813 472 -80 -307 N ATOM 1029 N THR A 127 6.831 -18.369 12.462 1.00 30.64 N ANISOU 1029 N THR A 127 3714 3662 4267 474 78 -50 N ATOM 1030 CA THR A 127 6.793 -17.687 11.174 1.00 34.89 C ANISOU 1030 CA THR A 127 4219 4188 4850 475 111 9 C ATOM 1031 C THR A 127 6.149 -18.541 10.069 1.00 33.67 C ANISOU 1031 C THR A 127 4041 4108 4645 469 143 67 C ATOM 1032 O THR A 127 5.854 -18.034 8.989 1.00 36.13 O ANISOU 1032 O THR A 127 4326 4421 4981 474 175 119 O ATOM 1033 CB THR A 127 8.199 -17.225 10.733 1.00 41.61 C ANISOU 1033 CB THR A 127 5051 4975 5782 447 96 13 C ATOM 1034 OG1 THR A 127 8.992 -18.360 10.359 1.00 44.49 O ANISOU 1034 OG1 THR A 127 5402 5370 6131 412 85 20 O ATOM 1035 CG2 THR A 127 8.889 -16.482 11.867 1.00 40.35 C ANISOU 1035 CG2 THR A 127 4917 4744 5669 448 60 -46 C ATOM 1036 N LEU A 128 5.910 -19.824 10.341 1.00 27.96 N ANISOU 1036 N LEU A 128 3328 3446 3851 456 134 57 N ATOM 1037 CA LEU A 128 5.367 -20.718 9.316 1.00 25.47 C ANISOU 1037 CA LEU A 128 2993 3201 3484 445 161 109 C ATOM 1038 C LEU A 128 3.936 -20.357 8.941 1.00 23.54 C ANISOU 1038 C LEU A 128 2744 2998 3204 476 197 147 C ATOM 1039 O LEU A 128 3.091 -20.105 9.799 1.00 18.72 O ANISOU 1039 O LEU A 128 2154 2396 2561 504 195 121 O ATOM 1040 CB LEU A 128 5.424 -22.184 9.746 1.00 25.58 C ANISOU 1040 CB LEU A 128 3023 3270 3427 424 143 89 C ATOM 1041 CG LEU A 128 6.786 -22.867 9.916 1.00 27.72 C ANISOU 1041 CG LEU A 128 3295 3520 3718 390 113 63 C ATOM 1042 CD1 LEU A 128 6.568 -24.314 10.316 1.00 31.40 C ANISOU 1042 CD1 LEU A 128 3780 4048 4103 376 100 48 C ATOM 1043 CD2 LEU A 128 7.636 -22.779 8.646 1.00 22.75 C ANISOU 1043 CD2 LEU A 128 2632 2872 3139 367 128 109 C ATOM 1044 N THR A 129 3.672 -20.329 7.642 1.00 20.65 N ANISOU 1044 N THR A 129 2348 2656 2843 470 229 209 N ATOM 1045 CA THR A 129 2.322 -20.082 7.171 1.00 19.47 C ANISOU 1045 CA THR A 129 2190 2553 2656 496 264 251 C ATOM 1046 C THR A 129 1.583 -21.408 7.075 1.00 14.21 C ANISOU 1046 C THR A 129 1528 1971 1898 484 269 266 C ATOM 1047 O THR A 129 2.178 -22.475 7.260 1.00 21.10 O ANISOU 1047 O THR A 129 2411 2863 2742 456 247 247 O ATOM 1048 CB THR A 129 2.327 -19.442 5.779 1.00 19.10 C ANISOU 1048 CB THR A 129 2107 2496 2654 494 297 314 C ATOM 1049 OG1 THR A 129 2.928 -20.354 4.863 1.00 18.37 O ANISOU 1049 OG1 THR A 129 1997 2430 2551 459 301 344 O ATOM 1050 CG2 THR A 129 3.098 -18.121 5.779 1.00 18.42 C ANISOU 1050 CG2 THR A 129 2014 2324 2661 503 293 303 C ATOM 1051 N ASP A 130 0.280 -21.333 6.805 1.00 15.32 N ANISOU 1051 N ASP A 130 1665 2164 1993 506 296 301 N ATOM 1052 CA ASP A 130 -0.526 -22.526 6.555 1.00 15.53 C ANISOU 1052 CA ASP A 130 1693 2275 1933 494 305 326 C ATOM 1053 C ASP A 130 0.128 -23.367 5.463 1.00 19.62 C ANISOU 1053 C ASP A 130 2195 2814 2448 455 310 361 C ATOM 1054 O ASP A 130 0.277 -24.588 5.598 1.00 17.26 O ANISOU 1054 O ASP A 130 1909 2555 2094 431 295 351 O ATOM 1055 CB ASP A 130 -1.955 -22.139 6.156 1.00 18.05 C ANISOU 1055 CB ASP A 130 2000 2641 2216 522 339 371 C ATOM 1056 CG ASP A 130 -2.829 -23.349 5.827 1.00 28.92 C ANISOU 1056 CG ASP A 130 3379 4108 3503 507 348 402 C ATOM 1057 OD1 ASP A 130 -2.609 -24.435 6.409 1.00 22.80 O ANISOU 1057 OD1 ASP A 130 2624 3359 2678 486 323 371 O ATOM 1058 OD2 ASP A 130 -3.757 -23.205 4.997 1.00 27.70 O ANISOU 1058 OD2 ASP A 130 3204 3997 3325 515 380 458 O ATOM 1059 N TYR A 131 0.535 -22.713 4.382 1.00 14.64 N ANISOU 1059 N TYR A 131 1535 2153 1875 451 331 402 N ATOM 1060 CA TYR A 131 1.156 -23.441 3.282 1.00 13.86 C ANISOU 1060 CA TYR A 131 1419 2071 1775 417 339 439 C ATOM 1061 C TYR A 131 2.455 -24.118 3.740 1.00 15.86 C ANISOU 1061 C TYR A 131 1687 2297 2044 390 306 396 C ATOM 1062 O TYR A 131 2.677 -25.311 3.472 1.00 14.57 O ANISOU 1062 O TYR A 131 1531 2174 1833 363 300 403 O ATOM 1063 CB TYR A 131 1.384 -22.536 2.071 1.00 15.37 C ANISOU 1063 CB TYR A 131 1576 2233 2031 419 368 490 C ATOM 1064 CG TYR A 131 1.843 -23.309 0.861 1.00 21.42 C ANISOU 1064 CG TYR A 131 2325 3026 2787 387 380 534 C ATOM 1065 CD1 TYR A 131 0.934 -23.957 0.044 1.00 19.87 C ANISOU 1065 CD1 TYR A 131 2122 2900 2529 379 405 584 C ATOM 1066 CD2 TYR A 131 3.200 -23.422 0.557 1.00 22.65 C ANISOU 1066 CD2 TYR A 131 2474 3139 2995 363 367 526 C ATOM 1067 CE1 TYR A 131 1.356 -24.680 -1.065 1.00 24.62 C ANISOU 1067 CE1 TYR A 131 2710 3524 3119 350 417 624 C ATOM 1068 CE2 TYR A 131 3.631 -24.146 -0.538 1.00 26.18 C ANISOU 1068 CE2 TYR A 131 2906 3610 3430 336 380 566 C ATOM 1069 CZ TYR A 131 2.704 -24.773 -1.345 1.00 28.95 C ANISOU 1069 CZ TYR A 131 3253 4029 3719 329 405 615 C ATOM 1070 OH TYR A 131 3.120 -25.493 -2.437 1.00 28.68 O ANISOU 1070 OH TYR A 131 3208 4017 3672 303 418 654 O ATOM 1071 N ASP A 132 3.310 -23.369 4.433 1.00 15.64 N ANISOU 1071 N ASP A 132 1664 2199 2080 396 284 353 N ATOM 1072 CA ASP A 132 4.568 -23.953 4.912 1.00 16.36 C ANISOU 1072 CA ASP A 132 1766 2261 2188 371 251 313 C ATOM 1073 C ASP A 132 4.327 -25.233 5.736 1.00 16.52 C ANISOU 1073 C ASP A 132 1817 2331 2130 361 229 278 C ATOM 1074 O ASP A 132 5.054 -26.225 5.588 1.00 17.77 O ANISOU 1074 O ASP A 132 1980 2503 2270 333 216 274 O ATOM 1075 CB ASP A 132 5.359 -22.964 5.774 1.00 16.16 C ANISOU 1075 CB ASP A 132 1747 2158 2234 382 226 265 C ATOM 1076 CG ASP A 132 5.853 -21.751 5.005 1.00 24.34 C ANISOU 1076 CG ASP A 132 2756 3137 3356 387 242 294 C ATOM 1077 OD1 ASP A 132 6.131 -21.847 3.786 1.00 19.87 O ANISOU 1077 OD1 ASP A 132 2163 2580 2808 371 264 344 O ATOM 1078 OD2 ASP A 132 5.980 -20.686 5.651 1.00 32.84 O ANISOU 1078 OD2 ASP A 132 3839 4157 4482 406 232 265 O ATOM 1079 N ILE A 133 3.324 -25.208 6.613 1.00 15.85 N ANISOU 1079 N ILE A 133 1752 2272 1998 383 225 255 N ATOM 1080 CA ILE A 133 3.093 -26.341 7.508 1.00 15.83 C ANISOU 1080 CA ILE A 133 1778 2312 1923 375 202 218 C ATOM 1081 C ILE A 133 2.749 -27.580 6.693 1.00 18.20 C ANISOU 1081 C ILE A 133 2077 2682 2156 351 216 258 C ATOM 1082 O ILE A 133 3.313 -28.648 6.906 1.00 16.34 O ANISOU 1082 O ILE A 133 1858 2463 1889 327 197 239 O ATOM 1083 CB ILE A 133 1.996 -26.064 8.554 1.00 18.98 C ANISOU 1083 CB ILE A 133 2199 2731 2283 406 198 190 C ATOM 1084 CG1 ILE A 133 2.408 -24.933 9.494 1.00 19.17 C ANISOU 1084 CG1 ILE A 133 2232 2684 2368 428 180 143 C ATOM 1085 CG2 ILE A 133 1.692 -27.329 9.374 1.00 19.15 C ANISOU 1085 CG2 ILE A 133 2249 2805 2223 395 176 159 C ATOM 1086 CD1 ILE A 133 1.238 -24.411 10.344 1.00 19.40 C ANISOU 1086 CD1 ILE A 133 2278 2728 2367 466 184 126 C ATOM 1087 N ARG A 134 1.842 -27.434 5.733 1.00 18.06 N ANISOU 1087 N ARG A 134 2042 2703 2118 356 249 315 N ATOM 1088 CA ARG A 134 1.459 -28.566 4.900 1.00 19.42 C ANISOU 1088 CA ARG A 134 2213 2940 2225 332 263 356 C ATOM 1089 C ARG A 134 2.666 -29.056 4.105 1.00 14.78 C ANISOU 1089 C ARG A 134 1616 2332 1666 302 261 370 C ATOM 1090 O ARG A 134 2.908 -30.260 3.988 1.00 13.62 O ANISOU 1090 O ARG A 134 1486 2221 1470 277 252 369 O ATOM 1091 CB ARG A 134 0.338 -28.158 3.955 1.00 18.51 C ANISOU 1091 CB ARG A 134 2077 2864 2092 343 300 417 C ATOM 1092 CG ARG A 134 -0.812 -27.440 4.653 1.00 11.47 C ANISOU 1092 CG ARG A 134 1189 1985 1185 379 307 409 C ATOM 1093 CD ARG A 134 -2.009 -27.410 3.747 1.00 17.63 C ANISOU 1093 CD ARG A 134 1951 2823 1925 384 341 471 C ATOM 1094 NE ARG A 134 -3.040 -26.491 4.228 1.00 14.71 N ANISOU 1094 NE ARG A 134 1578 2457 1555 422 353 473 N ATOM 1095 CZ ARG A 134 -4.331 -26.635 3.950 1.00 19.25 C ANISOU 1095 CZ ARG A 134 2146 3096 2072 432 375 512 C ATOM 1096 NH1 ARG A 134 -4.736 -27.673 3.227 1.00 18.04 N ANISOU 1096 NH1 ARG A 134 1992 3006 1856 404 383 551 N ATOM 1097 NH2 ARG A 134 -5.207 -25.754 4.404 1.00 16.76 N ANISOU 1097 NH2 ARG A 134 1827 2781 1761 470 387 513 N ATOM 1098 N PHE A 135 3.409 -28.112 3.540 1.00 17.70 N ANISOU 1098 N PHE A 135 1962 2647 2118 305 270 384 N ATOM 1099 CA PHE A 135 4.584 -28.444 2.737 1.00 14.43 C ANISOU 1099 CA PHE A 135 1534 2210 1739 280 270 401 C ATOM 1100 C PHE A 135 5.599 -29.274 3.531 1.00 13.48 C ANISOU 1100 C PHE A 135 1436 2075 1612 262 236 352 C ATOM 1101 O PHE A 135 6.045 -30.343 3.091 1.00 17.50 O ANISOU 1101 O PHE A 135 1952 2610 2086 238 234 363 O ATOM 1102 CB PHE A 135 5.235 -27.171 2.205 1.00 13.99 C ANISOU 1102 CB PHE A 135 1449 2090 1778 289 281 417 C ATOM 1103 CG PHE A 135 6.443 -27.427 1.347 1.00 23.47 C ANISOU 1103 CG PHE A 135 2632 3267 3019 265 283 439 C ATOM 1104 CD1 PHE A 135 6.326 -27.524 -0.034 1.00 21.84 C ANISOU 1104 CD1 PHE A 135 2404 3083 2812 255 314 500 C ATOM 1105 CD2 PHE A 135 7.700 -27.584 1.925 1.00 22.43 C ANISOU 1105 CD2 PHE A 135 2507 3092 2924 253 254 398 C ATOM 1106 CE1 PHE A 135 7.454 -27.765 -0.823 1.00 20.28 C ANISOU 1106 CE1 PHE A 135 2191 2864 2652 235 317 520 C ATOM 1107 CE2 PHE A 135 8.813 -27.823 1.146 1.00 23.94 C ANISOU 1107 CE2 PHE A 135 2681 3264 3152 233 257 420 C ATOM 1108 CZ PHE A 135 8.690 -27.914 -0.229 1.00 22.75 C ANISOU 1108 CZ PHE A 135 2508 3134 3000 225 289 481 C ATOM 1109 N TYR A 136 5.956 -28.785 4.710 1.00 13.25 N ANISOU 1109 N TYR A 136 1419 2004 1612 275 209 297 N ATOM 1110 CA TYR A 136 6.996 -29.432 5.496 1.00 14.94 C ANISOU 1110 CA TYR A 136 1651 2197 1828 259 175 249 C ATOM 1111 C TYR A 136 6.495 -30.735 6.113 1.00 15.14 C ANISOU 1111 C TYR A 136 1708 2281 1764 250 161 227 C ATOM 1112 O TYR A 136 7.247 -31.697 6.250 1.00 17.40 O ANISOU 1112 O TYR A 136 2008 2575 2030 230 144 211 O ATOM 1113 CB TYR A 136 7.576 -28.465 6.538 1.00 17.09 C ANISOU 1113 CB TYR A 136 1926 2404 2163 274 149 198 C ATOM 1114 CG TYR A 136 8.453 -27.364 5.957 1.00 16.63 C ANISOU 1114 CG TYR A 136 1838 2281 2198 274 155 214 C ATOM 1115 CD1 TYR A 136 9.543 -27.667 5.139 1.00 19.48 C ANISOU 1115 CD1 TYR A 136 2180 2626 2593 251 158 238 C ATOM 1116 CD2 TYR A 136 8.193 -26.026 6.226 1.00 18.56 C ANISOU 1116 CD2 TYR A 136 2075 2481 2497 297 159 207 C ATOM 1117 CE1 TYR A 136 10.350 -26.666 4.622 1.00 21.51 C ANISOU 1117 CE1 TYR A 136 2411 2827 2936 250 162 255 C ATOM 1118 CE2 TYR A 136 8.990 -25.014 5.703 1.00 16.97 C ANISOU 1118 CE2 TYR A 136 1848 2220 2381 296 163 222 C ATOM 1119 CZ TYR A 136 10.065 -25.337 4.903 1.00 14.72 C ANISOU 1119 CZ TYR A 136 1543 1922 2128 272 165 247 C ATOM 1120 OH TYR A 136 10.874 -24.355 4.378 1.00 22.04 O ANISOU 1120 OH TYR A 136 2443 2791 3139 269 169 264 O ATOM 1121 N MET A 137 5.215 -30.781 6.477 1.00 16.57 N ANISOU 1121 N MET A 137 1901 2505 1890 266 168 228 N ATOM 1122 CA AMET A 137 4.618 -32.029 6.940 1.00 15.26 C ANISOU 1122 CA AMET A 137 1765 2401 1635 256 158 215 C ATOM 1123 CA BMET A 137 4.612 -32.026 6.941 0.00 15.30 C ANISOU 1123 CA BMET A 137 1769 2405 1639 256 158 215 C ATOM 1124 C MET A 137 4.739 -33.107 5.868 1.00 15.98 C ANISOU 1124 C MET A 137 1855 2533 1682 228 174 258 C ATOM 1125 O MET A 137 5.108 -34.241 6.155 1.00 16.30 O ANISOU 1125 O MET A 137 1919 2597 1678 209 157 239 O ATOM 1126 CB AMET A 137 3.148 -31.814 7.328 1.00 13.48 C ANISOU 1126 CB AMET A 137 1547 2218 1359 277 169 220 C ATOM 1127 CB BMET A 137 3.143 -31.811 7.320 0.00 14.47 C ANISOU 1127 CB BMET A 137 1671 2343 1484 277 169 221 C ATOM 1128 CG AMET A 137 2.971 -31.251 8.723 1.00 14.23 C ANISOU 1128 CG AMET A 137 1657 2286 1464 302 146 164 C ATOM 1129 CG BMET A 137 2.937 -31.528 8.800 0.00 14.00 C ANISOU 1129 CG BMET A 137 1633 2268 1420 298 143 161 C ATOM 1130 SD AMET A 137 3.362 -32.472 10.003 1.00 20.34 S ANISOU 1130 SD AMET A 137 2468 3077 2182 287 106 102 S ATOM 1131 SD BMET A 137 3.329 -32.976 9.799 0.00 21.63 S ANISOU 1131 SD BMET A 137 2635 3261 2321 277 107 111 S ATOM 1132 CE AMET A 137 1.836 -33.425 10.069 1.00 46.14 C ANISOU 1132 CE AMET A 137 5753 6435 5341 287 117 123 C ATOM 1133 CE BMET A 137 3.564 -32.239 11.415 0.00 20.62 C ANISOU 1133 CE BMET A 137 2524 3084 2225 302 75 39 C ATOM 1134 N TYR A 138 4.445 -32.743 4.627 1.00 12.97 N ANISOU 1134 N TYR A 138 1449 2162 1316 226 206 316 N ATOM 1135 CA TYR A 138 4.554 -33.690 3.530 1.00 11.88 C ANISOU 1135 CA TYR A 138 1311 2061 1140 201 222 360 C ATOM 1136 C TYR A 138 6.006 -34.147 3.401 1.00 11.80 C ANISOU 1136 C TYR A 138 1303 2016 1164 183 208 345 C ATOM 1137 O TYR A 138 6.280 -35.316 3.161 1.00 15.91 O ANISOU 1137 O TYR A 138 1842 2567 1635 162 204 350 O ATOM 1138 CB TYR A 138 4.108 -33.040 2.234 1.00 15.92 C ANISOU 1138 CB TYR A 138 1793 2579 1675 204 258 422 C ATOM 1139 CG TYR A 138 3.774 -34.023 1.140 1.00 17.92 C ANISOU 1139 CG TYR A 138 2052 2887 1870 181 278 472 C ATOM 1140 CD1 TYR A 138 2.588 -34.748 1.169 1.00 16.94 C ANISOU 1140 CD1 TYR A 138 1946 2830 1660 175 284 488 C ATOM 1141 CD2 TYR A 138 4.631 -34.205 0.068 1.00 22.10 C ANISOU 1141 CD2 TYR A 138 2567 3400 2429 164 292 505 C ATOM 1142 CE1 TYR A 138 2.277 -35.645 0.158 1.00 21.08 C ANISOU 1142 CE1 TYR A 138 2477 3403 2129 151 302 534 C ATOM 1143 CE2 TYR A 138 4.334 -35.086 -0.939 1.00 27.38 C ANISOU 1143 CE2 TYR A 138 3244 4116 3043 143 311 550 C ATOM 1144 CZ TYR A 138 3.160 -35.807 -0.894 1.00 19.30 C ANISOU 1144 CZ TYR A 138 2241 3158 1935 136 315 564 C ATOM 1145 OH TYR A 138 2.881 -36.684 -1.920 1.00 22.96 O ANISOU 1145 OH TYR A 138 2714 3667 2344 112 333 609 O ATOM 1146 N GLU A 139 6.937 -33.223 3.573 1.00 14.75 N ANISOU 1146 N GLU A 139 1658 2326 1621 191 199 327 N ATOM 1147 CA GLU A 139 8.349 -33.573 3.478 1.00 16.15 C ANISOU 1147 CA GLU A 139 1832 2469 1836 175 185 314 C ATOM 1148 C GLU A 139 8.779 -34.534 4.591 1.00 13.10 C ANISOU 1148 C GLU A 139 1478 2090 1409 167 152 261 C ATOM 1149 O GLU A 139 9.571 -35.448 4.356 1.00 13.07 O ANISOU 1149 O GLU A 139 1484 2093 1390 148 145 262 O ATOM 1150 CB GLU A 139 9.216 -32.311 3.454 1.00 14.66 C ANISOU 1150 CB GLU A 139 1615 2210 1747 185 182 308 C ATOM 1151 CG GLU A 139 8.999 -31.461 2.196 1.00 13.28 C ANISOU 1151 CG GLU A 139 1407 2024 1615 190 216 366 C ATOM 1152 CD GLU A 139 9.424 -32.176 0.931 1.00 20.95 C ANISOU 1152 CD GLU A 139 2369 3018 2573 170 237 415 C ATOM 1153 OE1 GLU A 139 10.524 -32.754 0.908 1.00 22.45 O ANISOU 1153 OE1 GLU A 139 2562 3192 2774 155 224 404 O ATOM 1154 OE2 GLU A 139 8.672 -32.160 -0.053 1.00 20.40 O ANISOU 1154 OE2 GLU A 139 2289 2981 2480 170 267 465 O ATOM 1155 N ILE A 140 8.270 -34.331 5.806 1.00 12.25 N ANISOU 1155 N ILE A 140 1393 1793 1470 -117 97 1 N ATOM 1156 CA ILE A 140 8.551 -35.271 6.901 1.00 14.01 C ANISOU 1156 CA ILE A 140 1643 1958 1720 -108 82 -41 C ATOM 1157 C ILE A 140 7.971 -36.656 6.577 1.00 17.14 C ANISOU 1157 C ILE A 140 2045 2381 2089 -128 89 -81 C ATOM 1158 O ILE A 140 8.593 -37.693 6.817 1.00 12.90 O ANISOU 1158 O ILE A 140 1515 1814 1571 -130 92 -126 O ATOM 1159 CB ILE A 140 7.958 -34.780 8.242 1.00 13.59 C ANISOU 1159 CB ILE A 140 1618 1858 1687 -85 62 -20 C ATOM 1160 CG1 ILE A 140 8.579 -33.438 8.639 1.00 18.92 C ANISOU 1160 CG1 ILE A 140 2293 2500 2394 -68 55 12 C ATOM 1161 CG2 ILE A 140 8.198 -35.806 9.345 1.00 14.03 C ANISOU 1161 CG2 ILE A 140 1702 1863 1767 -76 47 -59 C ATOM 1162 CD1 ILE A 140 7.880 -32.761 9.816 1.00 13.79 C ANISOU 1162 CD1 ILE A 140 1674 1811 1757 -47 41 36 C ATOM 1163 N LEU A 141 6.765 -36.666 6.025 1.00 13.18 N ANISOU 1163 N LEU A 141 1536 1930 1542 -143 91 -63 N ATOM 1164 CA LEU A 141 6.122 -37.916 5.672 1.00 11.84 C ANISOU 1164 CA LEU A 141 1370 1787 1343 -166 95 -101 C ATOM 1165 C LEU A 141 6.939 -38.706 4.646 1.00 12.40 C ANISOU 1165 C LEU A 141 1429 1882 1401 -189 118 -146 C ATOM 1166 O LEU A 141 6.977 -39.930 4.705 1.00 14.53 O ANISOU 1166 O LEU A 141 1708 2138 1674 -201 124 -195 O ATOM 1167 CB LEU A 141 4.708 -37.647 5.158 1.00 12.23 C ANISOU 1167 CB LEU A 141 1407 1893 1345 -182 92 -65 C ATOM 1168 CG LEU A 141 3.670 -37.372 6.248 1.00 16.86 C ANISOU 1168 CG LEU A 141 2010 2451 1944 -162 75 -33 C ATOM 1169 CD1 LEU A 141 2.324 -36.944 5.621 1.00 13.42 C ANISOU 1169 CD1 LEU A 141 1555 2078 1467 -178 73 14 C ATOM 1170 CD2 LEU A 141 3.480 -38.596 7.132 1.00 16.36 C ANISOU 1170 CD2 LEU A 141 1971 2345 1900 -159 67 -75 C ATOM 1171 N LYS A 142 7.602 -38.016 3.718 1.00 17.86 N ANISOU 1171 N LYS A 142 2098 2606 2080 -194 133 -131 N ATOM 1172 CA LYS A 142 8.466 -38.709 2.757 1.00 13.81 C ANISOU 1172 CA LYS A 142 1575 2114 1556 -213 160 -174 C ATOM 1173 C LYS A 142 9.566 -39.452 3.502 1.00 20.53 C ANISOU 1173 C LYS A 142 2440 2897 2466 -197 165 -213 C ATOM 1174 O LYS A 142 9.814 -40.631 3.254 1.00 16.81 O ANISOU 1174 O LYS A 142 1974 2418 1995 -210 182 -265 O ATOM 1175 CB LYS A 142 9.093 -37.735 1.760 1.00 18.22 C ANISOU 1175 CB LYS A 142 2108 2714 2099 -215 177 -142 C ATOM 1176 CG LYS A 142 8.122 -37.187 0.729 1.00 24.39 C ANISOU 1176 CG LYS A 142 2872 3578 2817 -237 178 -106 C ATOM 1177 CD LYS A 142 8.860 -36.236 -0.209 1.00 26.64 C ANISOU 1177 CD LYS A 142 3129 3899 3092 -236 198 -72 C ATOM 1178 CE LYS A 142 7.892 -35.483 -1.100 1.00 28.97 C ANISOU 1178 CE LYS A 142 3403 4275 3331 -253 195 -20 C ATOM 1179 NZ LYS A 142 8.615 -34.486 -1.930 1.00 31.54 N ANISOU 1179 NZ LYS A 142 3700 4633 3653 -247 215 21 N ATOM 1180 N ALA A 143 10.214 -38.750 4.426 1.00 13.04 N ANISOU 1180 N ALA A 143 1493 1895 1566 -169 149 -188 N ATOM 1181 CA ALA A 143 11.256 -39.342 5.252 1.00 13.66 C ANISOU 1181 CA ALA A 143 1580 1908 1703 -152 147 -215 C ATOM 1182 C ALA A 143 10.717 -40.512 6.079 1.00 14.94 C ANISOU 1182 C ALA A 143 1763 2037 1875 -152 137 -248 C ATOM 1183 O ALA A 143 11.360 -41.556 6.172 1.00 10.45 O ANISOU 1183 O ALA A 143 1196 1439 1335 -153 152 -287 O ATOM 1184 CB ALA A 143 11.864 -38.281 6.165 1.00 11.33 C ANISOU 1184 CB ALA A 143 1286 1568 1451 -127 124 -177 C ATOM 1185 N LEU A 144 9.536 -40.350 6.681 1.00 12.32 N ANISOU 1185 N LEU A 144 1448 1709 1525 -149 116 -228 N ATOM 1186 CA LEU A 144 8.990 -41.416 7.518 1.00 11.38 C ANISOU 1186 CA LEU A 144 1349 1558 1419 -146 107 -254 C ATOM 1187 C LEU A 144 8.525 -42.629 6.704 1.00 16.13 C ANISOU 1187 C LEU A 144 1946 2189 1993 -175 129 -298 C ATOM 1188 O LEU A 144 8.819 -43.773 7.056 1.00 14.52 O ANISOU 1188 O LEU A 144 1749 1949 1818 -175 138 -337 O ATOM 1189 CB LEU A 144 7.879 -40.906 8.440 1.00 10.75 C ANISOU 1189 CB LEU A 144 1286 1469 1329 -132 82 -218 C ATOM 1190 CG LEU A 144 8.342 -39.991 9.582 1.00 11.83 C ANISOU 1190 CG LEU A 144 1437 1559 1500 -103 60 -188 C ATOM 1191 CD1 LEU A 144 7.128 -39.512 10.385 1.00 14.17 C ANISOU 1191 CD1 LEU A 144 1754 1851 1781 -90 43 -155 C ATOM 1192 CD2 LEU A 144 9.362 -40.705 10.486 1.00 13.43 C ANISOU 1192 CD2 LEU A 144 1648 1702 1752 -88 52 -212 C ATOM 1193 N ASP A 145 7.819 -42.406 5.606 1.00 13.85 N ANISOU 1193 N ASP A 145 1647 1966 1650 -201 138 -294 N ATOM 1194 CA ASP A 145 7.465 -43.553 4.785 1.00 18.17 C ANISOU 1194 CA ASP A 145 2193 2541 2168 -233 158 -343 C ATOM 1195 C ASP A 145 8.721 -44.283 4.316 1.00 19.38 C ANISOU 1195 C ASP A 145 2343 2673 2349 -237 190 -390 C ATOM 1196 O ASP A 145 8.752 -45.516 4.275 1.00 15.27 O ANISOU 1196 O ASP A 145 1829 2132 1842 -249 208 -439 O ATOM 1197 CB ASP A 145 6.656 -43.160 3.568 1.00 15.59 C ANISOU 1197 CB ASP A 145 1854 2295 1774 -264 161 -331 C ATOM 1198 CG ASP A 145 6.184 -44.376 2.800 1.00 27.73 C ANISOU 1198 CG ASP A 145 3396 3861 3280 -303 177 -386 C ATOM 1199 OD1 ASP A 145 5.660 -45.311 3.449 1.00 22.16 O ANISOU 1199 OD1 ASP A 145 2703 3122 2595 -305 171 -410 O ATOM 1200 OD2 ASP A 145 6.373 -44.413 1.570 1.00 27.69 O ANISOU 1200 OD2 ASP A 145 3382 3909 3230 -330 198 -406 O ATOM 1201 N TYR A 146 9.754 -43.528 3.944 1.00 16.75 N ANISOU 1201 N TYR A 146 1996 2343 2027 -226 201 -373 N ATOM 1202 CA TYR A 146 10.993 -44.173 3.526 1.00 15.93 C ANISOU 1202 CA TYR A 146 1885 2215 1954 -225 236 -411 C ATOM 1203 C TYR A 146 11.571 -45.081 4.617 1.00 15.23 C ANISOU 1203 C TYR A 146 1804 2051 1933 -205 235 -433 C ATOM 1204 O TYR A 146 11.769 -46.276 4.388 1.00 15.96 O ANISOU 1204 O TYR A 146 1899 2125 2040 -217 263 -482 O ATOM 1205 CB TYR A 146 12.038 -43.165 3.034 1.00 13.74 C ANISOU 1205 CB TYR A 146 1587 1948 1685 -213 247 -382 C ATOM 1206 CG TYR A 146 13.252 -43.866 2.464 1.00 13.07 C ANISOU 1206 CG TYR A 146 1492 1844 1628 -215 289 -421 C ATOM 1207 CD1 TYR A 146 13.171 -44.535 1.243 1.00 19.16 C ANISOU 1207 CD1 TYR A 146 2265 2659 2356 -244 327 -465 C ATOM 1208 CD2 TYR A 146 14.465 -43.884 3.144 1.00 14.64 C ANISOU 1208 CD2 TYR A 146 1681 1983 1897 -188 291 -413 C ATOM 1209 CE1 TYR A 146 14.263 -45.194 0.711 1.00 21.98 C ANISOU 1209 CE1 TYR A 146 2615 2996 2740 -243 373 -501 C ATOM 1210 CE2 TYR A 146 15.573 -44.544 2.610 1.00 18.44 C ANISOU 1210 CE2 TYR A 146 2151 2445 2411 -187 334 -443 C ATOM 1211 CZ TYR A 146 15.457 -45.195 1.390 1.00 22.28 C ANISOU 1211 CZ TYR A 146 2641 2972 2854 -214 378 -488 C ATOM 1212 OH TYR A 146 16.522 -45.857 0.828 1.00 22.86 O ANISOU 1212 OH TYR A 146 2704 3025 2958 -212 428 -521 O ATOM 1213 N CYS A 147 11.832 -44.546 5.808 1.00 16.57 N ANISOU 1213 N CYS A 147 1977 2177 2144 -176 204 -397 N ATOM 1214 CA CYS A 147 12.454 -45.388 6.826 1.00 15.40 C ANISOU 1214 CA CYS A 147 1832 1961 2058 -157 202 -411 C ATOM 1215 C CYS A 147 11.556 -46.558 7.244 1.00 15.69 C ANISOU 1215 C CYS A 147 1884 1982 2095 -166 202 -441 C ATOM 1216 O CYS A 147 12.034 -47.682 7.390 1.00 14.85 O ANISOU 1216 O CYS A 147 1775 1838 2029 -165 225 -475 O ATOM 1217 CB CYS A 147 13.008 -44.592 8.018 1.00 16.91 C ANISOU 1217 CB CYS A 147 2025 2110 2290 -128 167 -368 C ATOM 1218 SG CYS A 147 11.806 -43.821 9.129 1.00 14.85 S ANISOU 1218 SG CYS A 147 1788 1848 2006 -115 122 -328 S ATOM 1219 N HIS A 148 10.253 -46.313 7.380 1.00 11.14 N ANISOU 1219 N HIS A 148 1321 1436 1477 -175 181 -427 N ATOM 1220 CA HIS A 148 9.321 -47.409 7.652 1.00 12.23 C ANISOU 1220 CA HIS A 148 1470 1565 1613 -187 182 -453 C ATOM 1221 C HIS A 148 9.364 -48.475 6.543 1.00 12.35 C ANISOU 1221 C HIS A 148 1480 1597 1615 -219 221 -512 C ATOM 1222 O HIS A 148 9.404 -49.674 6.823 1.00 18.03 O ANISOU 1222 O HIS A 148 2202 2278 2370 -222 238 -547 O ATOM 1223 CB HIS A 148 7.896 -46.880 7.835 1.00 12.31 C ANISOU 1223 CB HIS A 148 1490 1610 1579 -193 155 -423 C ATOM 1224 CG HIS A 148 7.739 -45.949 8.997 1.00 12.14 C ANISOU 1224 CG HIS A 148 1479 1565 1571 -162 122 -372 C ATOM 1225 ND1 HIS A 148 6.604 -45.192 9.194 1.00 12.53 N ANISOU 1225 ND1 HIS A 148 1535 1642 1584 -161 102 -334 N ATOM 1226 CD2 HIS A 148 8.572 -45.655 10.026 1.00 13.72 C ANISOU 1226 CD2 HIS A 148 1683 1715 1814 -133 108 -353 C ATOM 1227 CE1 HIS A 148 6.743 -44.475 10.296 1.00 17.68 C ANISOU 1227 CE1 HIS A 148 2200 2262 2258 -131 79 -298 C ATOM 1228 NE2 HIS A 148 7.933 -44.726 10.810 1.00 16.70 N ANISOU 1228 NE2 HIS A 148 2075 2092 2178 -115 80 -310 N ATOM 1229 N SER A 149 9.385 -48.047 5.285 1.00 17.95 N ANISOU 1229 N SER A 149 2182 2363 2274 -243 238 -522 N ATOM 1230 CA SER A 149 9.414 -48.999 4.167 1.00 14.90 C ANISOU 1230 CA SER A 149 1797 1999 1866 -277 277 -582 C ATOM 1231 C SER A 149 10.722 -49.777 4.188 1.00 14.78 C ANISOU 1231 C SER A 149 1775 1930 1910 -264 315 -616 C ATOM 1232 O SER A 149 10.831 -50.864 3.608 1.00 14.99 O ANISOU 1232 O SER A 149 1806 1947 1942 -285 353 -672 O ATOM 1233 CB SER A 149 9.262 -48.279 2.821 1.00 19.65 C ANISOU 1233 CB SER A 149 2392 2677 2396 -303 287 -580 C ATOM 1234 OG SER A 149 10.431 -47.536 2.487 1.00 18.10 O ANISOU 1234 OG SER A 149 2182 2482 2213 -286 302 -562 O ATOM 1235 N MET A 150 11.709 -49.215 4.875 1.00 15.91 N ANISOU 1235 N MET A 150 1908 2037 2101 -230 306 -581 N ATOM 1236 CA AMET A 150 13.019 -49.846 4.968 1.00 16.51 C ANISOU 1236 CA AMET A 150 1972 2060 2241 -214 340 -600 C ATOM 1237 CA BMET A 150 13.028 -49.828 4.985 0.00 17.16 C ANISOU 1237 CA BMET A 150 2054 2142 2324 -214 340 -599 C ATOM 1238 C MET A 150 13.207 -50.571 6.303 1.00 20.08 C ANISOU 1238 C MET A 150 2424 2442 2763 -189 327 -592 C ATOM 1239 O MET A 150 14.330 -50.894 6.690 1.00 20.12 O ANISOU 1239 O MET A 150 2415 2400 2831 -168 343 -588 O ATOM 1240 CB AMET A 150 14.111 -48.788 4.739 1.00 15.94 C ANISOU 1240 CB AMET A 150 1883 1995 2180 -197 341 -565 C ATOM 1241 CB BMET A 150 14.120 -48.767 4.829 0.00 16.51 C ANISOU 1241 CB BMET A 150 1955 2064 2255 -195 339 -562 C ATOM 1242 CG AMET A 150 14.020 -48.152 3.335 1.00 17.08 C ANISOU 1242 CG AMET A 150 2023 2208 2257 -220 362 -572 C ATOM 1243 CG BMET A 150 14.348 -48.356 3.385 0.00 16.72 C ANISOU 1243 CG BMET A 150 1974 2147 2230 -216 371 -578 C ATOM 1244 SD AMET A 150 14.813 -49.218 2.078 1.00 22.26 S ANISOU 1244 SD AMET A 150 2676 2865 2916 -240 435 -639 S ATOM 1245 SD BMET A 150 14.886 -49.761 2.393 0.00 22.35 S ANISOU 1245 SD BMET A 150 2690 2848 2954 -236 441 -652 S ATOM 1246 CE AMET A 150 16.541 -48.929 2.507 1.00 20.02 C ANISOU 1246 CE AMET A 150 2365 2525 2715 -202 451 -608 C ATOM 1247 CE BMET A 150 14.897 -49.055 0.749 0.00 22.77 C ANISOU 1247 CE BMET A 150 2742 2985 2926 -263 469 -662 C ATOM 1248 N GLY A 151 12.099 -50.832 6.992 1.00 16.45 N ANISOU 1248 N GLY A 151 1978 1980 2292 -192 299 -586 N ATOM 1249 CA GLY A 151 12.109 -51.622 8.215 1.00 16.97 C ANISOU 1249 CA GLY A 151 2045 1985 2416 -171 288 -579 C ATOM 1250 C GLY A 151 12.600 -50.939 9.481 1.00 17.90 C ANISOU 1250 C GLY A 151 2160 2071 2568 -136 249 -524 C ATOM 1251 O GLY A 151 13.004 -51.595 10.436 1.00 15.22 O ANISOU 1251 O GLY A 151 1817 1680 2287 -116 245 -516 O ATOM 1252 N ILE A 152 12.548 -49.617 9.502 1.00 15.74 N ANISOU 1252 N ILE A 152 1891 1830 2261 -130 220 -487 N ATOM 1253 CA ILE A 152 13.138 -48.868 10.603 1.00 9.20 C ANISOU 1253 CA ILE A 152 1062 972 1461 -102 183 -440 C ATOM 1254 C ILE A 152 12.165 -47.861 11.186 1.00 15.13 C ANISOU 1254 C ILE A 152 1833 1746 2170 -96 143 -404 C ATOM 1255 O ILE A 152 11.490 -47.139 10.455 1.00 15.32 O ANISOU 1255 O ILE A 152 1861 1819 2140 -111 142 -399 O ATOM 1256 CB ILE A 152 14.417 -48.150 10.118 1.00 15.76 C ANISOU 1256 CB ILE A 152 1873 1804 2310 -96 192 -428 C ATOM 1257 CG1 ILE A 152 15.510 -49.191 9.804 1.00 15.32 C ANISOU 1257 CG1 ILE A 152 1796 1713 2314 -94 233 -455 C ATOM 1258 CG2 ILE A 152 14.858 -47.078 11.129 1.00 12.81 C ANISOU 1258 CG2 ILE A 152 1502 1413 1951 -74 147 -378 C ATOM 1259 CD1 ILE A 152 16.546 -48.713 8.811 1.00 21.51 C ANISOU 1259 CD1 ILE A 152 2559 2511 3102 -98 261 -457 C ATOM 1260 N MET A 153 12.094 -47.818 12.514 1.00 10.93 N ANISOU 1260 N MET A 153 1313 1179 1661 -73 111 -376 N ATOM 1261 CA MET A 153 11.347 -46.769 13.187 1.00 13.52 C ANISOU 1261 CA MET A 153 1662 1520 1954 -63 76 -340 C ATOM 1262 C MET A 153 12.308 -45.759 13.812 1.00 14.47 C ANISOU 1262 C MET A 153 1782 1620 2094 -46 48 -308 C ATOM 1263 O MET A 153 13.354 -46.128 14.353 1.00 13.67 O ANISOU 1263 O MET A 153 1671 1482 2042 -34 43 -304 O ATOM 1264 CB MET A 153 10.367 -47.338 14.220 1.00 22.03 C ANISOU 1264 CB MET A 153 2760 2579 3032 -52 61 -331 C ATOM 1265 CG MET A 153 10.887 -48.463 15.062 1.00 22.27 C ANISOU 1265 CG MET A 153 2785 2560 3116 -38 63 -338 C ATOM 1266 SD MET A 153 9.599 -49.211 16.102 1.00 19.07 S ANISOU 1266 SD MET A 153 2399 2139 2707 -27 52 -328 S ATOM 1267 CE MET A 153 10.502 -50.655 16.656 1.00 16.75 C ANISOU 1267 CE MET A 153 2087 1791 2486 -16 67 -341 C ATOM 1268 N HIS A 154 11.954 -44.482 13.720 1.00 11.92 N ANISOU 1268 N HIS A 154 1470 1323 1736 -45 32 -282 N ATOM 1269 CA HIS A 154 12.844 -43.426 14.182 1.00 12.51 C ANISOU 1269 CA HIS A 154 1545 1381 1828 -34 7 -255 C ATOM 1270 C HIS A 154 12.829 -43.338 15.711 1.00 17.35 C ANISOU 1270 C HIS A 154 2182 1955 2455 -15 -30 -235 C ATOM 1271 O HIS A 154 13.884 -43.313 16.342 1.00 14.50 O ANISOU 1271 O HIS A 154 1815 1562 2132 -6 -49 -225 O ATOM 1272 CB HIS A 154 12.468 -42.089 13.536 1.00 13.29 C ANISOU 1272 CB HIS A 154 1645 1515 1888 -41 5 -235 C ATOM 1273 CG HIS A 154 13.413 -40.975 13.865 1.00 13.72 C ANISOU 1273 CG HIS A 154 1697 1553 1964 -33 -17 -210 C ATOM 1274 ND1 HIS A 154 13.393 -40.326 15.079 1.00 12.40 N ANISOU 1274 ND1 HIS A 154 1555 1355 1801 -19 -52 -189 N ATOM 1275 CD2 HIS A 154 14.407 -40.398 13.146 1.00 14.06 C ANISOU 1275 CD2 HIS A 154 1715 1601 2025 -39 -9 -204 C ATOM 1276 CE1 HIS A 154 14.334 -39.397 15.096 1.00 10.88 C ANISOU 1276 CE1 HIS A 154 1353 1150 1630 -19 -67 -172 C ATOM 1277 NE2 HIS A 154 14.963 -39.417 13.936 1.00 9.44 N ANISOU 1277 NE2 HIS A 154 1138 989 1459 -30 -41 -179 N ATOM 1278 N ARG A 155 11.624 -43.304 16.285 1.00 14.40 N ANISOU 1278 N ARG A 155 1835 1587 2050 -8 -38 -226 N ATOM 1279 CA ARG A 155 11.394 -43.304 17.744 1.00 11.74 C ANISOU 1279 CA ARG A 155 1526 1217 1715 11 -67 -208 C ATOM 1280 C ARG A 155 11.813 -42.032 18.495 1.00 11.12 C ANISOU 1280 C ARG A 155 1469 1124 1632 20 -100 -183 C ATOM 1281 O ARG A 155 11.818 -42.007 19.724 1.00 14.32 O ANISOU 1281 O ARG A 155 1899 1502 2038 34 -126 -171 O ATOM 1282 CB ARG A 155 11.978 -44.553 18.438 1.00 9.72 C ANISOU 1282 CB ARG A 155 1263 928 1503 20 -71 -216 C ATOM 1283 CG ARG A 155 11.563 -45.892 17.800 1.00 12.71 C ANISOU 1283 CG ARG A 155 1623 1312 1893 11 -37 -244 C ATOM 1284 CD ARG A 155 11.858 -47.089 18.722 1.00 10.60 C ANISOU 1284 CD ARG A 155 1353 1008 1669 24 -40 -243 C ATOM 1285 NE ARG A 155 13.268 -47.150 19.119 1.00 12.13 N ANISOU 1285 NE ARG A 155 1528 1172 1908 30 -56 -233 N ATOM 1286 CZ ARG A 155 13.792 -48.056 19.948 1.00 16.69 C ANISOU 1286 CZ ARG A 155 2096 1716 2529 42 -63 -223 C ATOM 1287 NH1 ARG A 155 13.029 -48.995 20.501 1.00 12.23 N ANISOU 1287 NH1 ARG A 155 1539 1140 1968 51 -56 -223 N ATOM 1288 NH2 ARG A 155 15.096 -48.012 20.239 1.00 13.85 N ANISOU 1288 NH2 ARG A 155 1716 1335 2212 46 -79 -208 N ATOM 1289 N ASP A 156 12.134 -40.970 17.771 1.00 13.28 N ANISOU 1289 N ASP A 156 1734 1415 1898 12 -97 -177 N ATOM 1290 CA ASP A 156 12.465 -39.714 18.440 1.00 8.89 C ANISOU 1290 CA ASP A 156 1198 841 1339 17 -125 -156 C ATOM 1291 C ASP A 156 12.108 -38.554 17.536 1.00 11.31 C ANISOU 1291 C ASP A 156 1499 1176 1623 10 -111 -144 C ATOM 1292 O ASP A 156 12.850 -37.582 17.427 1.00 13.86 O ANISOU 1292 O ASP A 156 1815 1490 1960 6 -122 -133 O ATOM 1293 CB ASP A 156 13.953 -39.679 18.823 1.00 10.43 C ANISOU 1293 CB ASP A 156 1378 1007 1578 15 -150 -154 C ATOM 1294 CG ASP A 156 14.268 -38.609 19.858 1.00 16.50 C ANISOU 1294 CG ASP A 156 2176 1749 2343 19 -188 -138 C ATOM 1295 OD1 ASP A 156 13.337 -38.125 20.552 1.00 13.46 O ANISOU 1295 OD1 ASP A 156 1830 1361 1923 29 -194 -131 O ATOM 1296 OD2 ASP A 156 15.461 -38.269 19.990 1.00 17.62 O ANISOU 1296 OD2 ASP A 156 2303 1873 2518 12 -211 -132 O ATOM 1297 N VAL A 157 10.956 -38.668 16.877 1.00 12.85 N ANISOU 1297 N VAL A 157 1693 1406 1785 7 -85 -143 N ATOM 1298 CA VAL A 157 10.463 -37.579 16.050 1.00 11.54 C ANISOU 1298 CA VAL A 157 1520 1271 1596 1 -71 -124 C ATOM 1299 C VAL A 157 10.029 -36.429 16.970 1.00 16.56 C ANISOU 1299 C VAL A 157 2189 1883 2220 15 -87 -101 C ATOM 1300 O VAL A 157 9.233 -36.625 17.894 1.00 14.25 O ANISOU 1300 O VAL A 157 1928 1575 1912 29 -92 -97 O ATOM 1301 CB VAL A 157 9.280 -38.042 15.153 1.00 13.30 C ANISOU 1301 CB VAL A 157 1731 1539 1784 -8 -43 -125 C ATOM 1302 CG1 VAL A 157 8.639 -36.848 14.452 1.00 12.02 C ANISOU 1302 CG1 VAL A 157 1562 1409 1597 -11 -31 -95 C ATOM 1303 CG2 VAL A 157 9.743 -39.081 14.133 1.00 14.95 C ANISOU 1303 CG2 VAL A 157 1908 1771 2000 -26 -24 -154 C ATOM 1304 N LYS A 158 10.572 -35.242 16.722 1.00 10.05 N ANISOU 1304 N LYS A 158 1359 1053 1406 12 -91 -85 N ATOM 1305 CA LYS A 158 10.285 -34.036 17.497 1.00 11.22 C ANISOU 1305 CA LYS A 158 1539 1175 1550 23 -102 -66 C ATOM 1306 C LYS A 158 10.892 -32.866 16.729 1.00 15.25 C ANISOU 1306 C LYS A 158 2026 1690 2077 14 -96 -49 C ATOM 1307 O LYS A 158 11.758 -33.074 15.870 1.00 10.97 O ANISOU 1307 O LYS A 158 1449 1164 1555 2 -92 -55 O ATOM 1308 CB LYS A 158 10.896 -34.128 18.910 1.00 10.10 C ANISOU 1308 CB LYS A 158 1432 986 1422 30 -136 -79 C ATOM 1309 CG LYS A 158 12.418 -34.210 18.932 1.00 14.66 C ANISOU 1309 CG LYS A 158 1989 1543 2038 19 -161 -89 C ATOM 1310 CD LYS A 158 12.933 -34.388 20.350 1.00 13.63 C ANISOU 1310 CD LYS A 158 1890 1372 1915 23 -199 -98 C ATOM 1311 CE LYS A 158 14.451 -34.454 20.379 1.00 13.01 C ANISOU 1311 CE LYS A 158 1788 1276 1880 10 -227 -103 C ATOM 1312 NZ LYS A 158 14.956 -34.412 21.806 1.00 20.64 N ANISOU 1312 NZ LYS A 158 2787 2205 2848 10 -270 -107 N ATOM 1313 N PRO A 159 10.437 -31.633 17.014 1.00 14.30 N ANISOU 1313 N PRO A 159 1926 1556 1953 22 -92 -27 N ATOM 1314 CA PRO A 159 10.897 -30.457 16.271 1.00 14.87 C ANISOU 1314 CA PRO A 159 1975 1632 2045 15 -83 -5 C ATOM 1315 C PRO A 159 12.424 -30.373 16.146 1.00 15.21 C ANISOU 1315 C PRO A 159 1996 1656 2127 2 -104 -16 C ATOM 1316 O PRO A 159 12.932 -30.092 15.064 1.00 13.78 O ANISOU 1316 O PRO A 159 1775 1500 1961 -7 -89 -4 O ATOM 1317 CB PRO A 159 10.351 -29.296 17.099 1.00 17.02 C ANISOU 1317 CB PRO A 159 2284 1869 2315 27 -83 10 C ATOM 1318 CG PRO A 159 9.043 -29.840 17.639 1.00 14.16 C ANISOU 1318 CG PRO A 159 1949 1513 1917 42 -71 11 C ATOM 1319 CD PRO A 159 9.361 -31.287 17.972 1.00 15.38 C ANISOU 1319 CD PRO A 159 2105 1672 2066 39 -89 -19 C ATOM 1320 N HIS A 160 13.145 -30.617 17.232 1.00 15.98 N ANISOU 1320 N HIS A 160 2117 1713 2242 2 -138 -36 N ATOM 1321 CA HIS A 160 14.604 -30.509 17.168 1.00 15.65 C ANISOU 1321 CA HIS A 160 2052 1652 2243 -11 -161 -41 C ATOM 1322 C HIS A 160 15.214 -31.430 16.119 1.00 16.29 C ANISOU 1322 C HIS A 160 2087 1765 2338 -19 -145 -46 C ATOM 1323 O HIS A 160 16.220 -31.087 15.495 1.00 19.06 O ANISOU 1323 O HIS A 160 2404 2116 2723 -28 -145 -37 O ATOM 1324 CB HIS A 160 15.234 -30.779 18.525 1.00 12.87 C ANISOU 1324 CB HIS A 160 1730 1256 1903 -13 -204 -59 C ATOM 1325 CG HIS A 160 16.734 -30.748 18.499 1.00 21.38 C ANISOU 1325 CG HIS A 160 2780 2315 3028 -27 -231 -59 C ATOM 1326 ND1 HIS A 160 17.465 -29.655 18.913 1.00 27.93 N ANISOU 1326 ND1 HIS A 160 3616 3111 3886 -38 -257 -52 N ATOM 1327 CD2 HIS A 160 17.636 -31.672 18.094 1.00 23.52 C ANISOU 1327 CD2 HIS A 160 3014 2595 3327 -33 -234 -64 C ATOM 1328 CE1 HIS A 160 18.754 -29.911 18.774 1.00 28.54 C ANISOU 1328 CE1 HIS A 160 3660 3179 4007 -51 -278 -50 C ATOM 1329 NE2 HIS A 160 18.886 -31.129 18.282 1.00 25.70 N ANISOU 1329 NE2 HIS A 160 3272 2843 3648 -46 -263 -56 N ATOM 1330 N ASN A 161 14.605 -32.593 15.903 1.00 15.14 N ANISOU 1330 N ASN A 161 1941 1646 2168 -15 -130 -61 N ATOM 1331 CA ASN A 161 15.190 -33.579 14.979 1.00 13.20 C ANISOU 1331 CA ASN A 161 1656 1425 1934 -22 -112 -73 C ATOM 1332 C ASN A 161 14.753 -33.427 13.523 1.00 14.47 C ANISOU 1332 C ASN A 161 1787 1637 2073 -29 -73 -63 C ATOM 1333 O ASN A 161 15.113 -34.228 12.663 1.00 14.47 O ANISOU 1333 O ASN A 161 1760 1663 2075 -36 -52 -77 O ATOM 1334 CB ASN A 161 14.914 -34.997 15.473 1.00 9.02 C ANISOU 1334 CB ASN A 161 1139 893 1397 -18 -114 -98 C ATOM 1335 CG ASN A 161 15.740 -35.340 16.688 1.00 11.33 C ANISOU 1335 CG ASN A 161 1446 1141 1720 -15 -151 -105 C ATOM 1336 OD1 ASN A 161 16.776 -34.708 16.932 1.00 14.17 O ANISOU 1336 OD1 ASN A 161 1796 1476 2113 -20 -175 -95 O ATOM 1337 ND2 ASN A 161 15.303 -36.329 17.455 1.00 12.48 N ANISOU 1337 ND2 ASN A 161 1611 1277 1854 -7 -159 -118 N ATOM 1338 N VAL A 162 13.958 -32.406 13.244 1.00 12.18 N ANISOU 1338 N VAL A 162 1503 1363 1761 -27 -62 -39 N ATOM 1339 CA VAL A 162 13.563 -32.140 11.866 1.00 13.50 C ANISOU 1339 CA VAL A 162 1640 1584 1906 -34 -29 -21 C ATOM 1340 C VAL A 162 14.177 -30.822 11.454 1.00 20.08 C ANISOU 1340 C VAL A 162 2453 2412 2765 -36 -26 10 C ATOM 1341 O VAL A 162 13.610 -29.757 11.727 1.00 25.06 O ANISOU 1341 O VAL A 162 3097 3032 3393 -29 -27 35 O ATOM 1342 CB VAL A 162 12.022 -32.045 11.726 1.00 17.56 C ANISOU 1342 CB VAL A 162 2168 2130 2373 -30 -14 -7 C ATOM 1343 CG1 VAL A 162 11.635 -31.684 10.289 1.00 15.46 C ANISOU 1343 CG1 VAL A 162 1868 1925 2082 -41 16 17 C ATOM 1344 CG2 VAL A 162 11.378 -33.355 12.126 1.00 15.58 C ANISOU 1344 CG2 VAL A 162 1935 1884 2100 -30 -16 -36 C ATOM 1345 N MET A 163 15.332 -30.891 10.796 1.00 13.91 N ANISOU 1345 N MET A 163 1637 1633 2013 -43 -20 9 N ATOM 1346 CA MET A 163 16.071 -29.698 10.415 1.00 11.33 C ANISOU 1346 CA MET A 163 1287 1298 1721 -45 -18 39 C ATOM 1347 C MET A 163 15.541 -29.122 9.116 1.00 16.36 C ANISOU 1347 C MET A 163 1894 1989 2331 -48 17 71 C ATOM 1348 O MET A 163 15.379 -29.836 8.129 1.00 18.29 O ANISOU 1348 O MET A 163 2120 2284 2546 -55 42 63 O ATOM 1349 CB MET A 163 17.565 -29.991 10.292 1.00 15.54 C ANISOU 1349 CB MET A 163 1793 1809 2302 -50 -26 31 C ATOM 1350 CG MET A 163 18.112 -30.646 11.532 1.00 19.96 C ANISOU 1350 CG MET A 163 2376 2320 2887 -49 -62 5 C ATOM 1351 SD MET A 163 19.863 -30.348 11.670 1.00 25.32 S ANISOU 1351 SD MET A 163 3024 2960 3638 -56 -83 15 S ATOM 1352 CE MET A 163 19.861 -28.569 11.719 1.00 19.94 C ANISOU 1352 CE MET A 163 2342 2259 2976 -58 -92 51 C ATOM 1353 N ILE A 164 15.275 -27.821 9.125 1.00 17.72 N ANISOU 1353 N ILE A 164 2065 2153 2515 -43 19 107 N ATOM 1354 CA ILE A 164 14.683 -27.161 7.971 1.00 19.38 C ANISOU 1354 CA ILE A 164 2246 2416 2701 -45 50 147 C ATOM 1355 C ILE A 164 15.505 -25.963 7.518 1.00 23.77 C ANISOU 1355 C ILE A 164 2770 2959 3301 -44 58 184 C ATOM 1356 O ILE A 164 15.735 -25.021 8.284 1.00 23.42 O ANISOU 1356 O ILE A 164 2739 2862 3296 -40 41 196 O ATOM 1357 CB ILE A 164 13.259 -26.675 8.287 1.00 18.16 C ANISOU 1357 CB ILE A 164 2113 2269 2516 -36 55 168 C ATOM 1358 CG1 ILE A 164 12.343 -27.858 8.580 1.00 17.33 C ANISOU 1358 CG1 ILE A 164 2034 2185 2367 -38 51 138 C ATOM 1359 CG2 ILE A 164 12.705 -25.841 7.146 1.00 23.44 C ANISOU 1359 CG2 ILE A 164 2747 2990 3168 -37 85 220 C ATOM 1360 CD1 ILE A 164 10.974 -27.438 9.130 1.00 23.01 C ANISOU 1360 CD1 ILE A 164 2778 2901 3064 -27 53 158 C ATOM 1361 N ASP A 165 15.961 -26.022 6.273 1.00 17.35 N ANISOU 1361 N ASP A 165 1917 2194 2483 -51 84 202 N ATOM 1362 CA ASP A 165 16.530 -24.869 5.607 1.00 22.07 C ANISOU 1362 CA ASP A 165 2477 2794 3114 -49 100 248 C ATOM 1363 C ASP A 165 15.374 -24.153 4.926 1.00 25.66 C ANISOU 1363 C ASP A 165 2920 3297 3535 -46 125 293 C ATOM 1364 O ASP A 165 14.928 -24.542 3.851 1.00 25.26 O ANISOU 1364 O ASP A 165 2847 3315 3435 -52 149 305 O ATOM 1365 CB ASP A 165 17.592 -25.289 4.585 1.00 25.30 C ANISOU 1365 CB ASP A 165 2847 3233 3532 -56 121 248 C ATOM 1366 CG ASP A 165 18.216 -24.103 3.872 1.00 29.53 C ANISOU 1366 CG ASP A 165 3340 3772 4106 -53 139 300 C ATOM 1367 OD1 ASP A 165 17.567 -23.037 3.798 1.00 31.11 O ANISOU 1367 OD1 ASP A 165 3535 3975 4309 -48 146 341 O ATOM 1368 OD2 ASP A 165 19.356 -24.237 3.389 1.00 31.96 O ANISOU 1368 OD2 ASP A 165 3619 4079 4445 -56 149 302 O ATOM 1369 N HIS A 166 14.895 -23.104 5.574 1.00 23.93 N ANISOU 1369 N HIS A 166 2714 3040 3340 -37 118 319 N ATOM 1370 CA HIS A 166 13.725 -22.377 5.107 1.00 21.26 C ANISOU 1370 CA HIS A 166 2364 2736 2977 -31 141 367 C ATOM 1371 C HIS A 166 14.007 -21.559 3.843 1.00 26.37 C ANISOU 1371 C HIS A 166 2958 3428 3633 -31 171 425 C ATOM 1372 O HIS A 166 13.080 -21.183 3.127 1.00 29.81 O ANISOU 1372 O HIS A 166 3374 3917 4037 -30 193 470 O ATOM 1373 CB HIS A 166 13.202 -21.477 6.233 1.00 18.53 C ANISOU 1373 CB HIS A 166 2051 2327 2663 -18 130 377 C ATOM 1374 CG HIS A 166 11.777 -21.053 6.060 1.00 22.64 C ANISOU 1374 CG HIS A 166 2571 2877 3153 -9 151 416 C ATOM 1375 ND1 HIS A 166 10.802 -21.896 5.571 1.00 23.89 N ANISOU 1375 ND1 HIS A 166 2729 3099 3251 -14 157 416 N ATOM 1376 CD2 HIS A 166 11.157 -19.880 6.334 1.00 25.06 C ANISOU 1376 CD2 HIS A 166 2878 3155 3487 4 166 460 C ATOM 1377 CE1 HIS A 166 9.645 -21.260 5.548 1.00 24.81 C ANISOU 1377 CE1 HIS A 166 2841 3227 3357 -4 174 461 C ATOM 1378 NE2 HIS A 166 9.832 -20.034 6.001 1.00 26.08 N ANISOU 1378 NE2 HIS A 166 3004 3333 3573 8 183 489 N ATOM 1379 N GLU A 167 15.278 -21.282 3.567 1.00 25.68 N ANISOU 1379 N GLU A 167 2846 3321 3590 -34 172 428 N ATOM 1380 CA GLU A 167 15.637 -20.567 2.344 1.00 27.70 C ANISOU 1380 CA GLU A 167 3049 3620 3854 -34 203 484 C ATOM 1381 C GLU A 167 15.410 -21.417 1.098 1.00 31.17 C ANISOU 1381 C GLU A 167 3466 4150 4226 -44 225 485 C ATOM 1382 O GLU A 167 14.751 -20.984 0.152 1.00 31.17 O ANISOU 1382 O GLU A 167 3437 4212 4193 -44 250 535 O ATOM 1383 CB GLU A 167 17.088 -20.072 2.396 1.00 34.72 C ANISOU 1383 CB GLU A 167 3915 4462 4813 -34 199 488 C ATOM 1384 CG GLU A 167 17.542 -19.360 1.126 1.00 45.22 C ANISOU 1384 CG GLU A 167 5189 5837 6156 -32 233 548 C ATOM 1385 CD GLU A 167 18.980 -18.868 1.207 1.00 55.68 C ANISOU 1385 CD GLU A 167 6489 7112 7556 -32 229 555 C ATOM 1386 OE1 GLU A 167 19.626 -19.064 2.259 1.00 55.80 O ANISOU 1386 OE1 GLU A 167 6530 7058 7613 -36 196 514 O ATOM 1387 OE2 GLU A 167 19.465 -18.282 0.216 1.00 61.72 O ANISOU 1387 OE2 GLU A 167 7206 7907 8339 -29 258 605 O ATOM 1388 N HIS A 168 15.945 -22.633 1.099 1.00 32.98 N ANISOU 1388 N HIS A 168 3709 4385 4435 -52 218 430 N ATOM 1389 CA HIS A 168 15.806 -23.523 -0.051 1.00 31.81 C ANISOU 1389 CA HIS A 168 3547 4318 4223 -64 241 419 C ATOM 1390 C HIS A 168 14.678 -24.531 0.122 1.00 29.42 C ANISOU 1390 C HIS A 168 3276 4047 3856 -74 231 383 C ATOM 1391 O HIS A 168 14.554 -25.464 -0.668 1.00 28.61 O ANISOU 1391 O HIS A 168 3171 4002 3698 -88 245 359 O ATOM 1392 CB HIS A 168 17.111 -24.266 -0.307 1.00 31.94 C ANISOU 1392 CB HIS A 168 3554 4323 4257 -68 248 383 C ATOM 1393 CG HIS A 168 18.295 -23.362 -0.463 1.00 35.89 C ANISOU 1393 CG HIS A 168 4020 4790 4826 -60 257 418 C ATOM 1394 ND1 HIS A 168 18.507 -22.604 -1.594 1.00 36.99 N ANISOU 1394 ND1 HIS A 168 4115 4977 4964 -58 289 475 N ATOM 1395 CD2 HIS A 168 19.326 -23.092 0.372 1.00 38.98 C ANISOU 1395 CD2 HIS A 168 4413 5106 5291 -55 236 408 C ATOM 1396 CE1 HIS A 168 19.622 -21.908 -1.451 1.00 42.46 C ANISOU 1396 CE1 HIS A 168 4783 5622 5729 -50 289 498 C ATOM 1397 NE2 HIS A 168 20.139 -22.186 -0.267 1.00 42.60 N ANISOU 1397 NE2 HIS A 168 4828 5565 5794 -50 256 457 N ATOM 1398 N ARG A 169 13.870 -24.345 1.162 1.00 22.57 N ANISOU 1398 N ARG A 169 2440 3140 2996 -67 208 379 N ATOM 1399 CA ARG A 169 12.726 -25.212 1.413 1.00 24.39 C ANISOU 1399 CA ARG A 169 2698 3395 3173 -74 198 351 C ATOM 1400 C ARG A 169 13.147 -26.674 1.487 1.00 25.91 C ANISOU 1400 C ARG A 169 2912 3589 3344 -86 192 283 C ATOM 1401 O ARG A 169 12.495 -27.546 0.911 1.00 30.85 O ANISOU 1401 O ARG A 169 3542 4270 3911 -101 199 263 O ATOM 1402 CB ARG A 169 11.678 -25.043 0.307 1.00 28.73 C ANISOU 1402 CB ARG A 169 3223 4032 3662 -85 217 395 C ATOM 1403 CG ARG A 169 11.495 -23.610 -0.180 1.00 36.09 C ANISOU 1403 CG ARG A 169 4118 4978 4615 -75 234 473 C ATOM 1404 CD ARG A 169 10.464 -22.862 0.632 1.00 41.23 C ANISOU 1404 CD ARG A 169 4782 5596 5285 -61 226 505 C ATOM 1405 NE ARG A 169 9.157 -23.518 0.621 1.00 45.50 N ANISOU 1405 NE ARG A 169 5338 6181 5770 -70 219 501 N ATOM 1406 CZ ARG A 169 8.135 -23.140 1.385 1.00 42.51 C ANISOU 1406 CZ ARG A 169 4976 5775 5401 -58 213 522 C ATOM 1407 NH1 ARG A 169 8.278 -22.109 2.209 1.00 43.44 N ANISOU 1407 NH1 ARG A 169 5104 5823 5580 -37 215 543 N ATOM 1408 NH2 ARG A 169 6.980 -23.787 1.337 1.00 35.17 N ANISOU 1408 NH2 ARG A 169 4055 4886 4422 -67 207 520 N ATOM 1409 N LYS A 170 14.229 -26.933 2.213 1.00 22.91 N ANISOU 1409 N LYS A 170 2544 3146 3014 -79 178 250 N ATOM 1410 CA LYS A 170 14.824 -28.261 2.299 1.00 28.35 C ANISOU 1410 CA LYS A 170 3247 3828 3698 -87 177 191 C ATOM 1411 C LYS A 170 14.737 -28.810 3.729 1.00 24.85 C ANISOU 1411 C LYS A 170 2844 3319 3279 -80 144 152 C ATOM 1412 O LYS A 170 14.959 -28.085 4.699 1.00 22.26 O ANISOU 1412 O LYS A 170 2529 2933 2995 -68 122 164 O ATOM 1413 CB LYS A 170 16.286 -28.186 1.844 1.00 29.58 C ANISOU 1413 CB LYS A 170 3375 3970 3896 -85 192 191 C ATOM 1414 CG LYS A 170 17.041 -29.505 1.885 1.00 39.56 C ANISOU 1414 CG LYS A 170 4647 5220 5165 -90 197 136 C ATOM 1415 CD LYS A 170 18.475 -29.358 1.350 1.00 45.79 C ANISOU 1415 CD LYS A 170 5403 5998 5998 -87 217 145 C ATOM 1416 CE LYS A 170 19.434 -28.787 2.395 1.00 43.65 C ANISOU 1416 CE LYS A 170 5129 5648 5805 -75 188 155 C ATOM 1417 NZ LYS A 170 20.823 -28.675 1.862 1.00 45.77 N ANISOU 1417 NZ LYS A 170 5362 5907 6122 -72 208 168 N ATOM 1418 N LEU A 171 14.432 -30.095 3.857 1.00 16.14 N ANISOU 1418 N LEU A 171 1760 2224 2146 -88 142 105 N ATOM 1419 CA LEU A 171 14.193 -30.683 5.171 1.00 17.78 C ANISOU 1419 CA LEU A 171 2006 2380 2370 -81 114 73 C ATOM 1420 C LEU A 171 14.986 -31.973 5.361 1.00 19.01 C ANISOU 1420 C LEU A 171 2168 2514 2542 -85 114 22 C ATOM 1421 O LEU A 171 15.107 -32.769 4.428 1.00 17.55 O ANISOU 1421 O LEU A 171 1969 2369 2329 -97 140 0 O ATOM 1422 CB LEU A 171 12.689 -30.964 5.327 1.00 14.16 C ANISOU 1422 CB LEU A 171 1568 1949 1862 -84 110 73 C ATOM 1423 CG LEU A 171 12.188 -31.498 6.668 1.00 21.01 C ANISOU 1423 CG LEU A 171 2476 2769 2738 -75 84 47 C ATOM 1424 CD1 LEU A 171 10.774 -30.977 6.939 1.00 18.92 C ANISOU 1424 CD1 LEU A 171 2225 2520 2445 -70 81 77 C ATOM 1425 CD2 LEU A 171 12.236 -33.022 6.671 1.00 17.94 C ANISOU 1425 CD2 LEU A 171 2097 2384 2334 -84 86 -4 C ATOM 1426 N ARG A 172 15.530 -32.175 6.565 1.00 15.49 N ANISOU 1426 N ARG A 172 1741 2005 2140 -75 86 5 N ATOM 1427 CA ARG A 172 16.263 -33.398 6.882 1.00 8.69 C ANISOU 1427 CA ARG A 172 884 1117 1301 -76 85 -36 C ATOM 1428 C ARG A 172 15.857 -33.940 8.252 1.00 9.85 C ANISOU 1428 C ARG A 172 1067 1219 1456 -68 53 -57 C ATOM 1429 O ARG A 172 15.859 -33.202 9.249 1.00 14.38 O ANISOU 1429 O ARG A 172 1659 1754 2052 -59 24 -40 O ATOM 1430 CB ARG A 172 17.791 -33.164 6.859 1.00 12.87 C ANISOU 1430 CB ARG A 172 1387 1613 1890 -72 85 -28 C ATOM 1431 CG ARG A 172 18.349 -32.738 5.490 1.00 12.76 C ANISOU 1431 CG ARG A 172 1335 1641 1872 -78 121 -8 C ATOM 1432 CD ARG A 172 18.351 -33.886 4.507 1.00 16.06 C ANISOU 1432 CD ARG A 172 1744 2100 2257 -88 159 -41 C ATOM 1433 NE ARG A 172 18.917 -33.507 3.211 1.00 17.01 N ANISOU 1433 NE ARG A 172 1831 2262 2370 -92 196 -22 N ATOM 1434 CZ ARG A 172 18.201 -33.106 2.164 1.00 24.72 C ANISOU 1434 CZ ARG A 172 2799 3304 3291 -102 218 -5 C ATOM 1435 NH1 ARG A 172 16.877 -33.016 2.241 1.00 20.57 N ANISOU 1435 NH1 ARG A 172 2293 2809 2715 -109 206 -2 N ATOM 1436 NH2 ARG A 172 18.808 -32.791 1.031 1.00 28.67 N ANISOU 1436 NH2 ARG A 172 3268 3841 3785 -105 253 13 N ATOM 1437 N LEU A 173 15.525 -35.229 8.306 1.00 10.07 N ANISOU 1437 N LEU A 173 1106 1253 1468 -72 61 -93 N ATOM 1438 CA LEU A 173 15.258 -35.898 9.578 1.00 10.24 C ANISOU 1438 CA LEU A 173 1157 1232 1501 -64 35 -112 C ATOM 1439 C LEU A 173 16.592 -36.409 10.147 1.00 13.44 C ANISOU 1439 C LEU A 173 1552 1590 1963 -58 22 -124 C ATOM 1440 O LEU A 173 17.284 -37.206 9.507 1.00 15.81 O ANISOU 1440 O LEU A 173 1831 1896 2280 -63 48 -143 O ATOM 1441 CB LEU A 173 14.293 -37.065 9.377 1.00 10.25 C ANISOU 1441 CB LEU A 173 1170 1258 1465 -71 49 -142 C ATOM 1442 CG LEU A 173 13.771 -37.860 10.581 1.00 16.27 C ANISOU 1442 CG LEU A 173 1963 1986 2232 -62 28 -159 C ATOM 1443 CD1 LEU A 173 13.079 -36.961 11.620 1.00 16.89 C ANISOU 1443 CD1 LEU A 173 2070 2045 2303 -49 -1 -132 C ATOM 1444 CD2 LEU A 173 12.817 -38.962 10.116 1.00 16.63 C ANISOU 1444 CD2 LEU A 173 2013 2063 2243 -74 48 -187 C ATOM 1445 N ILE A 174 16.933 -35.962 11.350 1.00 13.88 N ANISOU 1445 N ILE A 174 1625 1600 2048 -49 -15 -112 N ATOM 1446 CA ILE A 174 18.231 -36.271 11.936 1.00 16.84 C ANISOU 1446 CA ILE A 174 1987 1932 2479 -46 -34 -114 C ATOM 1447 C ILE A 174 18.133 -37.093 13.221 1.00 16.21 C ANISOU 1447 C ILE A 174 1933 1816 2410 -38 -62 -128 C ATOM 1448 O ILE A 174 17.030 -37.453 13.662 1.00 15.92 O ANISOU 1448 O ILE A 174 1925 1786 2338 -34 -65 -138 O ATOM 1449 CB ILE A 174 18.991 -34.981 12.265 1.00 15.01 C ANISOU 1449 CB ILE A 174 1748 1675 2279 -46 -60 -84 C ATOM 1450 CG1 ILE A 174 18.254 -34.179 13.346 1.00 13.87 C ANISOU 1450 CG1 ILE A 174 1644 1510 2116 -41 -94 -74 C ATOM 1451 CG2 ILE A 174 19.207 -34.142 10.997 1.00 14.38 C ANISOU 1451 CG2 ILE A 174 1638 1629 2196 -52 -31 -63 C ATOM 1452 CD1 ILE A 174 19.139 -33.101 14.005 1.00 17.54 C ANISOU 1452 CD1 ILE A 174 2109 1935 2620 -44 -129 -54 C ATOM 1453 N ASP A 175 19.303 -37.373 13.799 1.00 13.87 N ANISOU 1453 N ASP A 175 1621 1482 2165 -36 -83 -123 N ATOM 1454 CA ASP A 175 19.466 -38.091 15.068 1.00 15.55 C ANISOU 1454 CA ASP A 175 1851 1659 2397 -29 -115 -128 C ATOM 1455 C ASP A 175 18.743 -39.432 15.112 1.00 11.90 C ANISOU 1455 C ASP A 175 1399 1205 1918 -24 -94 -154 C ATOM 1456 O ASP A 175 17.702 -39.577 15.760 1.00 14.24 O ANISOU 1456 O ASP A 175 1728 1503 2179 -18 -104 -159 O ATOM 1457 CB ASP A 175 19.065 -37.238 16.271 1.00 13.77 C ANISOU 1457 CB ASP A 175 1665 1414 2155 -26 -159 -116 C ATOM 1458 CG ASP A 175 19.668 -37.758 17.577 1.00 18.09 C ANISOU 1458 CG ASP A 175 2222 1923 2729 -22 -200 -112 C ATOM 1459 OD1 ASP A 175 19.685 -37.009 18.566 1.00 25.06 O ANISOU 1459 OD1 ASP A 175 3132 2784 3604 -24 -240 -102 O ATOM 1460 OD2 ASP A 175 20.138 -38.913 17.612 1.00 17.02 O ANISOU 1460 OD2 ASP A 175 2066 1779 2624 -19 -191 -118 O ATOM 1461 N TRP A 176 19.340 -40.404 14.436 1.00 10.44 N ANISOU 1461 N TRP A 176 1183 1021 1762 -26 -62 -168 N ATOM 1462 CA TRP A 176 18.835 -41.764 14.373 1.00 12.13 C ANISOU 1462 CA TRP A 176 1400 1236 1972 -23 -36 -195 C ATOM 1463 C TRP A 176 19.374 -42.616 15.510 1.00 14.74 C ANISOU 1463 C TRP A 176 1729 1526 2347 -13 -59 -189 C ATOM 1464 O TRP A 176 19.362 -43.848 15.441 1.00 16.33 O ANISOU 1464 O TRP A 176 1920 1716 2568 -9 -34 -207 O ATOM 1465 CB TRP A 176 19.167 -42.350 12.996 1.00 9.25 C ANISOU 1465 CB TRP A 176 1006 893 1616 -31 17 -217 C ATOM 1466 CG TRP A 176 18.482 -41.546 11.946 1.00 14.39 C ANISOU 1466 CG TRP A 176 1661 1592 2215 -42 36 -220 C ATOM 1467 CD1 TRP A 176 18.866 -40.318 11.460 1.00 17.23 C ANISOU 1467 CD1 TRP A 176 2010 1968 2571 -46 31 -196 C ATOM 1468 CD2 TRP A 176 17.227 -41.849 11.323 1.00 15.90 C ANISOU 1468 CD2 TRP A 176 1868 1822 2350 -52 58 -242 C ATOM 1469 NE1 TRP A 176 17.936 -39.867 10.542 1.00 14.24 N ANISOU 1469 NE1 TRP A 176 1636 1637 2136 -56 52 -200 N ATOM 1470 CE2 TRP A 176 16.926 -40.788 10.441 1.00 14.83 C ANISOU 1470 CE2 TRP A 176 1728 1728 2178 -61 67 -228 C ATOM 1471 CE3 TRP A 176 16.346 -42.931 11.400 1.00 14.06 C ANISOU 1471 CE3 TRP A 176 1650 1594 2099 -56 72 -270 C ATOM 1472 CZ2 TRP A 176 15.770 -40.775 9.649 1.00 13.45 C ANISOU 1472 CZ2 TRP A 176 1562 1602 1944 -74 86 -239 C ATOM 1473 CZ3 TRP A 176 15.193 -42.915 10.614 1.00 18.70 C ANISOU 1473 CZ3 TRP A 176 2247 2227 2629 -70 89 -284 C ATOM 1474 CH2 TRP A 176 14.921 -41.848 9.750 1.00 17.10 C ANISOU 1474 CH2 TRP A 176 2039 2069 2388 -80 95 -268 C ATOM 1475 N GLY A 177 19.826 -41.949 16.570 1.00 17.31 N ANISOU 1475 N GLY A 177 2065 1827 2685 -9 -107 -163 N ATOM 1476 CA GLY A 177 20.432 -42.618 17.708 1.00 16.98 C ANISOU 1476 CA GLY A 177 2019 1750 2683 -1 -137 -148 C ATOM 1477 C GLY A 177 19.475 -43.454 18.545 1.00 18.84 C ANISOU 1477 C GLY A 177 2283 1980 2896 9 -143 -157 C ATOM 1478 O GLY A 177 19.911 -44.324 19.301 1.00 18.10 O ANISOU 1478 O GLY A 177 2179 1861 2837 18 -155 -147 O ATOM 1479 N LEU A 178 18.176 -43.188 18.429 1.00 17.53 N ANISOU 1479 N LEU A 178 2149 1837 2673 9 -134 -171 N ATOM 1480 CA LEU A 178 17.176 -44.027 19.082 1.00 14.17 C ANISOU 1480 CA LEU A 178 1747 1409 2228 19 -132 -178 C ATOM 1481 C LEU A 178 16.451 -44.951 18.098 1.00 16.85 C ANISOU 1481 C LEU A 178 2077 1767 2559 14 -83 -208 C ATOM 1482 O LEU A 178 15.591 -45.722 18.500 1.00 16.89 O ANISOU 1482 O LEU A 178 2096 1769 2551 20 -76 -216 O ATOM 1483 CB LEU A 178 16.140 -43.183 19.843 1.00 12.31 C ANISOU 1483 CB LEU A 178 1557 1181 1938 24 -158 -169 C ATOM 1484 CG LEU A 178 16.645 -42.387 21.050 1.00 20.05 C ANISOU 1484 CG LEU A 178 2560 2140 2918 28 -208 -146 C ATOM 1485 CD1 LEU A 178 15.481 -41.717 21.790 1.00 20.05 C ANISOU 1485 CD1 LEU A 178 2609 2146 2864 36 -222 -141 C ATOM 1486 CD2 LEU A 178 17.422 -43.291 21.978 1.00 26.37 C ANISOU 1486 CD2 LEU A 178 3347 2913 3759 35 -231 -132 C ATOM 1487 N ALA A 179 16.798 -44.873 16.817 1.00 17.60 N ANISOU 1487 N ALA A 179 2148 1882 2659 2 -49 -225 N ATOM 1488 CA ALA A 179 16.089 -45.653 15.801 1.00 14.08 C ANISOU 1488 CA ALA A 179 1696 1460 2196 -8 -4 -258 C ATOM 1489 C ALA A 179 16.336 -47.147 15.967 1.00 18.29 C ANISOU 1489 C ALA A 179 2213 1963 2773 -3 19 -275 C ATOM 1490 O ALA A 179 17.405 -47.553 16.434 1.00 16.14 O ANISOU 1490 O ALA A 179 1919 1658 2556 6 13 -261 O ATOM 1491 CB ALA A 179 16.472 -45.189 14.394 1.00 12.10 C ANISOU 1491 CB ALA A 179 1424 1238 1935 -23 26 -271 C ATOM 1492 N GLU A 180 15.346 -47.962 15.602 1.00 12.77 N ANISOU 1492 N GLU A 180 1522 1276 2054 -10 46 -303 N ATOM 1493 CA GLU A 180 15.467 -49.428 15.702 1.00 16.10 C ANISOU 1493 CA GLU A 180 1929 1668 2521 -7 74 -322 C ATOM 1494 C GLU A 180 14.892 -50.126 14.483 1.00 16.88 C ANISOU 1494 C GLU A 180 2023 1787 2602 -28 121 -368 C ATOM 1495 O GLU A 180 14.079 -49.555 13.758 1.00 20.07 O ANISOU 1495 O GLU A 180 2441 2235 2951 -44 124 -380 O ATOM 1496 CB GLU A 180 14.714 -49.965 16.919 1.00 17.20 C ANISOU 1496 CB GLU A 180 2087 1786 2661 7 51 -307 C ATOM 1497 CG GLU A 180 15.579 -50.424 18.072 1.00 20.57 C ANISOU 1497 CG GLU A 180 2502 2172 3143 26 30 -277 C ATOM 1498 CD GLU A 180 16.343 -51.715 17.797 1.00 22.60 C ANISOU 1498 CD GLU A 180 2724 2394 3468 29 68 -291 C ATOM 1499 OE1 GLU A 180 16.844 -52.301 18.774 1.00 27.51 O ANISOU 1499 OE1 GLU A 180 3334 2982 4137 45 54 -263 O ATOM 1500 OE2 GLU A 180 16.467 -52.142 16.629 1.00 21.15 O ANISOU 1500 OE2 GLU A 180 2526 2217 3293 14 114 -327 O ATOM 1501 N PHE A 181 15.294 -51.378 14.284 1.00 15.58 N ANISOU 1501 N PHE A 181 1840 1592 2487 -28 158 -392 N ATOM 1502 CA PHE A 181 14.721 -52.217 13.242 1.00 14.19 C ANISOU 1502 CA PHE A 181 1663 1429 2298 -50 203 -442 C ATOM 1503 C PHE A 181 13.410 -52.827 13.748 1.00 14.12 C ANISOU 1503 C PHE A 181 1673 1420 2271 -54 195 -449 C ATOM 1504 O PHE A 181 13.343 -53.300 14.885 1.00 18.49 O ANISOU 1504 O PHE A 181 2228 1939 2858 -34 177 -425 O ATOM 1505 CB PHE A 181 15.702 -53.333 12.877 1.00 20.31 C ANISOU 1505 CB PHE A 181 2412 2165 3141 -48 251 -467 C ATOM 1506 CG PHE A 181 16.925 -52.851 12.149 1.00 15.72 C ANISOU 1506 CG PHE A 181 1810 1587 2578 -48 271 -465 C ATOM 1507 CD1 PHE A 181 16.944 -52.809 10.760 1.00 14.82 C ANISOU 1507 CD1 PHE A 181 1694 1503 2432 -70 313 -505 C ATOM 1508 CD2 PHE A 181 18.051 -52.441 12.851 1.00 16.40 C ANISOU 1508 CD2 PHE A 181 1875 1645 2711 -27 248 -422 C ATOM 1509 CE1 PHE A 181 18.073 -52.365 10.077 1.00 18.59 C ANISOU 1509 CE1 PHE A 181 2151 1985 2928 -68 335 -501 C ATOM 1510 CE2 PHE A 181 19.184 -51.995 12.181 1.00 19.46 C ANISOU 1510 CE2 PHE A 181 2239 2034 3120 -26 267 -416 C ATOM 1511 CZ PHE A 181 19.190 -51.964 10.783 1.00 17.85 C ANISOU 1511 CZ PHE A 181 2034 1860 2886 -45 313 -455 C ATOM 1512 N TYR A 182 12.377 -52.812 12.909 1.00 15.91 N ANISOU 1512 N TYR A 182 1913 1686 2445 -79 207 -479 N ATOM 1513 CA TYR A 182 11.121 -53.453 13.270 1.00 15.25 C ANISOU 1513 CA TYR A 182 1844 1602 2349 -85 203 -486 C ATOM 1514 C TYR A 182 11.122 -54.933 12.900 1.00 17.20 C ANISOU 1514 C TYR A 182 2078 1817 2639 -98 247 -531 C ATOM 1515 O TYR A 182 11.323 -55.307 11.737 1.00 16.00 O ANISOU 1515 O TYR A 182 1921 1678 2480 -123 285 -577 O ATOM 1516 CB TYR A 182 9.887 -52.753 12.672 1.00 18.00 C ANISOU 1516 CB TYR A 182 2209 2007 2623 -107 189 -489 C ATOM 1517 CG TYR A 182 8.618 -53.520 13.013 1.00 16.76 C ANISOU 1517 CG TYR A 182 2061 1846 2461 -115 187 -496 C ATOM 1518 CD1 TYR A 182 8.076 -53.478 14.293 1.00 18.70 C ANISOU 1518 CD1 TYR A 182 2317 2071 2716 -90 158 -456 C ATOM 1519 CD2 TYR A 182 8.008 -54.340 12.076 1.00 19.91 C ANISOU 1519 CD2 TYR A 182 2457 2260 2847 -148 216 -543 C ATOM 1520 CE1 TYR A 182 6.926 -54.212 14.616 1.00 18.94 C ANISOU 1520 CE1 TYR A 182 2353 2096 2748 -96 159 -459 C ATOM 1521 CE2 TYR A 182 6.873 -55.068 12.388 1.00 19.00 C ANISOU 1521 CE2 TYR A 182 2347 2139 2734 -157 213 -549 C ATOM 1522 CZ TYR A 182 6.342 -55.009 13.656 1.00 15.86 C ANISOU 1522 CZ TYR A 182 1956 1719 2350 -130 186 -505 C ATOM 1523 OH TYR A 182 5.210 -55.755 13.948 1.00 16.36 O ANISOU 1523 OH TYR A 182 2022 1775 2420 -139 186 -507 O ATOM 1524 N HIS A 183 10.895 -55.764 13.913 1.00 13.33 N ANISOU 1524 N HIS A 183 1586 1284 2194 -81 242 -517 N ATOM 1525 CA HIS A 183 10.777 -57.203 13.740 1.00 16.68 C ANISOU 1525 CA HIS A 183 1999 1671 2668 -91 282 -554 C ATOM 1526 C HIS A 183 9.438 -57.638 14.349 1.00 17.75 C ANISOU 1526 C HIS A 183 2146 1805 2792 -93 266 -545 C ATOM 1527 O HIS A 183 9.170 -57.366 15.526 1.00 19.91 O ANISOU 1527 O HIS A 183 2427 2068 3070 -67 232 -497 O ATOM 1528 CB HIS A 183 11.932 -57.925 14.429 1.00 19.80 C ANISOU 1528 CB HIS A 183 2371 2007 3147 -64 299 -537 C ATOM 1529 CG HIS A 183 13.278 -57.644 13.826 1.00 23.30 C ANISOU 1529 CG HIS A 183 2796 2444 3612 -61 321 -544 C ATOM 1530 ND1 HIS A 183 13.671 -58.154 12.606 1.00 26.13 N ANISOU 1530 ND1 HIS A 183 3148 2802 3980 -83 374 -598 N ATOM 1531 CD2 HIS A 183 14.328 -56.924 14.288 1.00 23.44 C ANISOU 1531 CD2 HIS A 183 2802 2455 3648 -39 299 -503 C ATOM 1532 CE1 HIS A 183 14.900 -57.750 12.338 1.00 26.26 C ANISOU 1532 CE1 HIS A 183 3147 2811 4020 -72 386 -586 C ATOM 1533 NE2 HIS A 183 15.323 -57.004 13.343 1.00 23.62 N ANISOU 1533 NE2 HIS A 183 2807 2473 3693 -46 339 -529 N ATOM 1534 N PRO A 184 8.596 -58.312 13.555 1.00 18.36 N ANISOU 1534 N PRO A 184 2228 1894 2855 -126 290 -591 N ATOM 1535 CA PRO A 184 7.261 -58.658 14.067 1.00 20.60 C ANISOU 1535 CA PRO A 184 2519 2180 3127 -130 273 -579 C ATOM 1536 C PRO A 184 7.382 -59.436 15.373 1.00 19.16 C ANISOU 1536 C PRO A 184 2327 1942 3011 -98 270 -545 C ATOM 1537 O PRO A 184 8.157 -60.394 15.429 1.00 17.53 O ANISOU 1537 O PRO A 184 2102 1687 2872 -92 304 -562 O ATOM 1538 CB PRO A 184 6.688 -59.564 12.972 1.00 21.55 C ANISOU 1538 CB PRO A 184 2638 2306 3243 -173 308 -643 C ATOM 1539 CG PRO A 184 7.460 -59.235 11.744 1.00 27.23 C ANISOU 1539 CG PRO A 184 3358 3052 3937 -194 333 -683 C ATOM 1540 CD PRO A 184 8.839 -58.861 12.209 1.00 20.53 C ANISOU 1540 CD PRO A 184 2498 2176 3126 -160 335 -655 C ATOM 1541 N GLY A 185 6.657 -59.016 16.406 1.00 20.23 N ANISOU 1541 N GLY A 185 2474 2084 3130 -77 234 -496 N ATOM 1542 CA GLY A 185 6.621 -59.738 17.664 1.00 22.19 C ANISOU 1542 CA GLY A 185 2714 2285 3432 -47 230 -460 C ATOM 1543 C GLY A 185 7.681 -59.319 18.661 1.00 23.51 C ANISOU 1543 C GLY A 185 2877 2432 3622 -11 209 -414 C ATOM 1544 O GLY A 185 7.686 -59.763 19.807 1.00 21.28 O ANISOU 1544 O GLY A 185 2591 2120 3376 17 199 -374 O ATOM 1545 N GLN A 186 8.587 -58.453 18.232 1.00 18.73 N ANISOU 1545 N GLN A 186 2274 1846 2995 -11 201 -416 N ATOM 1546 CA GLN A 186 9.681 -58.035 19.095 1.00 19.73 C ANISOU 1546 CA GLN A 186 2395 1956 3145 18 178 -375 C ATOM 1547 C GLN A 186 9.188 -57.026 20.131 1.00 21.94 C ANISOU 1547 C GLN A 186 2701 2257 3376 38 130 -326 C ATOM 1548 O GLN A 186 8.395 -56.136 19.816 1.00 21.24 O ANISOU 1548 O GLN A 186 2635 2210 3226 28 114 -328 O ATOM 1549 CB GLN A 186 10.816 -57.448 18.254 1.00 19.54 C ANISOU 1549 CB GLN A 186 2361 1943 3119 8 186 -393 C ATOM 1550 CG GLN A 186 12.121 -57.280 19.003 1.00 28.53 C ANISOU 1550 CG GLN A 186 3484 3055 4300 33 170 -355 C ATOM 1551 CD GLN A 186 13.309 -57.145 18.062 1.00 33.03 C ANISOU 1551 CD GLN A 186 4033 3623 4894 24 196 -378 C ATOM 1552 OE1 GLN A 186 13.556 -58.021 17.227 1.00 36.94 O ANISOU 1552 OE1 GLN A 186 4511 4098 5426 10 244 -419 O ATOM 1553 NE2 GLN A 186 14.039 -56.042 18.182 1.00 31.62 N ANISOU 1553 NE2 GLN A 186 3858 3463 4695 30 165 -354 N ATOM 1554 N GLU A 187 9.638 -57.182 21.371 1.00 18.90 N ANISOU 1554 N GLU A 187 2313 1846 3020 67 108 -282 N ATOM 1555 CA GLU A 187 9.313 -56.226 22.420 1.00 20.08 C ANISOU 1555 CA GLU A 187 2492 2014 3124 86 64 -239 C ATOM 1556 C GLU A 187 10.428 -55.194 22.529 1.00 21.68 C ANISOU 1556 C GLU A 187 2698 2225 3313 91 36 -224 C ATOM 1557 O GLU A 187 11.603 -55.555 22.590 1.00 23.77 O ANISOU 1557 O GLU A 187 2937 2466 3627 95 39 -218 O ATOM 1558 CB GLU A 187 9.109 -56.943 23.754 1.00 20.03 C ANISOU 1558 CB GLU A 187 2484 1978 3147 113 54 -197 C ATOM 1559 CG GLU A 187 7.947 -57.944 23.721 1.00 24.92 C ANISOU 1559 CG GLU A 187 3099 2586 3784 110 81 -206 C ATOM 1560 CD GLU A 187 7.559 -58.446 25.099 1.00 37.68 C ANISOU 1560 CD GLU A 187 4719 4181 5415 139 68 -157 C ATOM 1561 OE1 GLU A 187 8.460 -58.672 25.935 1.00 39.16 O ANISOU 1561 OE1 GLU A 187 4895 4348 5634 159 54 -124 O ATOM 1562 OE2 GLU A 187 6.348 -58.617 25.345 1.00 41.74 O ANISOU 1562 OE2 GLU A 187 5246 4702 5910 142 73 -149 O ATOM 1563 N TYR A 188 10.058 -53.914 22.539 1.00 15.11 N ANISOU 1563 N TYR A 188 1895 1427 2419 88 9 -217 N ATOM 1564 CA TYR A 188 11.038 -52.823 22.537 1.00 16.20 C ANISOU 1564 CA TYR A 188 2038 1575 2543 88 -18 -207 C ATOM 1565 C TYR A 188 11.037 -52.054 23.843 1.00 20.21 C ANISOU 1565 C TYR A 188 2575 2083 3020 107 -62 -167 C ATOM 1566 O TYR A 188 10.068 -52.094 24.586 1.00 20.21 O ANISOU 1566 O TYR A 188 2599 2086 2993 120 -70 -149 O ATOM 1567 CB TYR A 188 10.774 -51.860 21.379 1.00 20.55 C ANISOU 1567 CB TYR A 188 2596 2163 3049 67 -11 -233 C ATOM 1568 CG TYR A 188 10.938 -52.538 20.054 1.00 17.41 C ANISOU 1568 CG TYR A 188 2172 1769 2675 45 31 -275 C ATOM 1569 CD1 TYR A 188 12.189 -52.652 19.486 1.00 20.03 C ANISOU 1569 CD1 TYR A 188 2478 2088 3045 39 45 -288 C ATOM 1570 CD2 TYR A 188 9.851 -53.117 19.397 1.00 14.15 C ANISOU 1570 CD2 TYR A 188 1760 1369 2247 29 58 -303 C ATOM 1571 CE1 TYR A 188 12.374 -53.289 18.296 1.00 22.63 C ANISOU 1571 CE1 TYR A 188 2786 2418 3393 20 88 -329 C ATOM 1572 CE2 TYR A 188 10.026 -53.767 18.182 1.00 16.03 C ANISOU 1572 CE2 TYR A 188 1978 1611 2503 5 97 -347 C ATOM 1573 CZ TYR A 188 11.306 -53.845 17.646 1.00 16.47 C ANISOU 1573 CZ TYR A 188 2011 1654 2593 2 114 -361 C ATOM 1574 OH TYR A 188 11.541 -54.479 16.454 1.00 20.28 O ANISOU 1574 OH TYR A 188 2477 2138 3091 -20 157 -407 O ATOM 1575 N ASN A 189 12.133 -51.353 24.109 1.00 17.19 N ANISOU 1575 N ASN A 189 2191 1699 2643 108 -91 -152 N ATOM 1576 CA ASN A 189 12.237 -50.467 25.263 1.00 16.32 C ANISOU 1576 CA ASN A 189 2113 1591 2498 121 -136 -121 C ATOM 1577 C ASN A 189 11.219 -49.337 25.126 1.00 13.85 C ANISOU 1577 C ASN A 189 1837 1305 2119 118 -141 -127 C ATOM 1578 O ASN A 189 11.091 -48.747 24.054 1.00 19.45 O ANISOU 1578 O ASN A 189 2543 2035 2813 102 -125 -150 O ATOM 1579 CB ASN A 189 13.664 -49.901 25.305 1.00 21.42 C ANISOU 1579 CB ASN A 189 2742 2229 3165 114 -163 -111 C ATOM 1580 CG ASN A 189 13.932 -49.018 26.518 1.00 29.77 C ANISOU 1580 CG ASN A 189 3833 3289 4191 122 -214 -82 C ATOM 1581 OD1 ASN A 189 13.101 -48.873 27.414 1.00 21.50 O ANISOU 1581 OD1 ASN A 189 2821 2244 3102 135 -227 -68 O ATOM 1582 ND2 ASN A 189 15.126 -48.436 26.556 1.00 36.70 N ANISOU 1582 ND2 ASN A 189 4697 4161 5085 112 -243 -73 N ATOM 1583 N VAL A 190 10.485 -49.029 26.191 1.00 16.54 N ANISOU 1583 N VAL A 190 2215 1647 2423 134 -159 -105 N ATOM 1584 CA VAL A 190 9.501 -47.942 26.108 1.00 12.06 C ANISOU 1584 CA VAL A 190 1684 1101 1799 135 -158 -106 C ATOM 1585 C VAL A 190 10.115 -46.579 26.443 1.00 15.38 C ANISOU 1585 C VAL A 190 2130 1524 2191 131 -191 -100 C ATOM 1586 O VAL A 190 9.466 -45.544 26.304 1.00 20.86 O ANISOU 1586 O VAL A 190 2851 2232 2844 131 -189 -102 O ATOM 1587 CB VAL A 190 8.233 -48.208 26.976 1.00 15.67 C ANISOU 1587 CB VAL A 190 2170 1557 2226 155 -152 -87 C ATOM 1588 CG1 VAL A 190 7.517 -49.486 26.524 1.00 17.61 C ANISOU 1588 CG1 VAL A 190 2390 1800 2502 154 -118 -95 C ATOM 1589 CG2 VAL A 190 8.596 -48.271 28.458 1.00 16.86 C ANISOU 1589 CG2 VAL A 190 2345 1691 2369 174 -183 -58 C ATOM 1590 N ARG A 191 11.381 -46.586 26.864 1.00 16.73 N ANISOU 1590 N ARG A 191 2288 1680 2389 128 -221 -92 N ATOM 1591 CA ARG A 191 12.080 -45.351 27.209 1.00 22.31 C ANISOU 1591 CA ARG A 191 3016 2386 3075 121 -256 -88 C ATOM 1592 C ARG A 191 12.767 -44.729 25.995 1.00 21.88 C ANISOU 1592 C ARG A 191 2934 2340 3039 101 -248 -106 C ATOM 1593 O ARG A 191 14.004 -44.608 25.941 1.00 20.27 O ANISOU 1593 O ARG A 191 2707 2126 2868 91 -269 -102 O ATOM 1594 CB ARG A 191 13.085 -45.591 28.343 1.00 23.22 C ANISOU 1594 CB ARG A 191 3132 2484 3206 124 -298 -65 C ATOM 1595 CG ARG A 191 12.454 -46.138 29.620 1.00 29.76 C ANISOU 1595 CG ARG A 191 3990 3307 4011 144 -308 -43 C ATOM 1596 CD ARG A 191 13.455 -46.172 30.759 1.00 41.24 C ANISOU 1596 CD ARG A 191 5450 4752 5470 144 -356 -18 C ATOM 1597 NE ARG A 191 13.795 -44.826 31.209 1.00 51.04 N ANISOU 1597 NE ARG A 191 6728 5994 6671 133 -392 -22 N ATOM 1598 CZ ARG A 191 14.845 -44.533 31.970 1.00 59.55 C ANISOU 1598 CZ ARG A 191 7809 7066 7751 122 -442 -7 C ATOM 1599 NH1 ARG A 191 15.671 -45.493 32.365 1.00 59.53 N ANISOU 1599 NH1 ARG A 191 7771 7058 7790 123 -460 19 N ATOM 1600 NH2 ARG A 191 15.075 -43.278 32.330 1.00 62.27 N ANISOU 1600 NH2 ARG A 191 8191 7410 8058 108 -472 -17 N ATOM 1601 N VAL A 192 11.943 -44.335 25.029 1.00 17.93 N ANISOU 1601 N VAL A 192 2435 1860 2518 95 -217 -121 N ATOM 1602 CA VAL A 192 12.375 -43.648 23.830 1.00 17.11 C ANISOU 1602 CA VAL A 192 2309 1770 2421 78 -205 -136 C ATOM 1603 C VAL A 192 11.491 -42.413 23.645 1.00 19.79 C ANISOU 1603 C VAL A 192 2679 2127 2714 78 -200 -134 C ATOM 1604 O VAL A 192 10.457 -42.270 24.326 1.00 16.33 O ANISOU 1604 O VAL A 192 2275 1688 2242 92 -198 -124 O ATOM 1605 CB VAL A 192 12.229 -44.550 22.583 1.00 13.70 C ANISOU 1605 CB VAL A 192 1839 1353 2012 69 -165 -156 C ATOM 1606 CG1 VAL A 192 13.139 -45.794 22.691 1.00 12.50 C ANISOU 1606 CG1 VAL A 192 1654 1179 1915 70 -162 -159 C ATOM 1607 CG2 VAL A 192 10.759 -44.966 22.400 1.00 16.11 C ANISOU 1607 CG2 VAL A 192 2158 1676 2289 73 -138 -162 C ATOM 1608 N ALA A 193 11.899 -41.536 22.725 1.00 19.02 N ANISOU 1608 N ALA A 193 2566 2041 2618 64 -195 -139 N ATOM 1609 CA ALA A 193 11.188 -40.292 22.418 1.00 16.89 C ANISOU 1609 CA ALA A 193 2317 1785 2313 63 -187 -133 C ATOM 1610 C ALA A 193 11.255 -39.273 23.554 1.00 15.43 C ANISOU 1610 C ALA A 193 2176 1578 2109 71 -217 -121 C ATOM 1611 O ALA A 193 11.463 -39.619 24.724 1.00 19.31 O ANISOU 1611 O ALA A 193 2691 2049 2597 80 -242 -117 O ATOM 1612 CB ALA A 193 9.720 -40.582 22.037 1.00 18.06 C ANISOU 1612 CB ALA A 193 2472 1957 2432 69 -155 -131 C ATOM 1613 N SER A 194 11.107 -38.003 23.210 1.00 13.79 N ANISOU 1613 N SER A 194 1979 1374 1886 66 -213 -117 N ATOM 1614 CA ASER A 194 11.015 -36.968 24.220 1.00 15.19 C ANISOU 1614 CA ASER A 194 2202 1528 2041 72 -234 -110 C ATOM 1615 CA BSER A 194 11.012 -36.959 24.217 0.00 17.17 C ANISOU 1615 CA BSER A 194 2453 1779 2293 72 -234 -110 C ATOM 1616 C SER A 194 9.630 -37.015 24.851 1.00 17.31 C ANISOU 1616 C SER A 194 2508 1797 2271 92 -215 -102 C ATOM 1617 O SER A 194 8.655 -37.342 24.182 1.00 14.94 O ANISOU 1617 O SER A 194 2194 1521 1962 97 -183 -96 O ATOM 1618 CB ASER A 194 11.242 -35.596 23.593 1.00 19.69 C ANISOU 1618 CB ASER A 194 2769 2098 2615 62 -229 -106 C ATOM 1619 CB BSER A 194 11.247 -35.583 23.594 0.00 19.96 C ANISOU 1619 CB BSER A 194 2803 2132 2649 62 -229 -106 C ATOM 1620 OG ASER A 194 10.557 -34.596 24.333 1.00 27.84 O ANISOU 1620 OG ASER A 194 3849 3112 3618 72 -228 -100 O ATOM 1621 OG BSER A 194 12.605 -35.405 23.235 0.00 19.92 O ANISOU 1621 OG BSER A 194 2768 2119 2681 45 -251 -111 O ATOM 1622 N ARG A 195 9.553 -36.690 26.139 1.00 16.00 N ANISOU 1622 N ARG A 195 2390 1608 2083 103 -235 -100 N ATOM 1623 CA ARG A 195 8.296 -36.756 26.887 1.00 18.85 C ANISOU 1623 CA ARG A 195 2790 1965 2407 125 -216 -90 C ATOM 1624 C ARG A 195 7.057 -36.308 26.103 1.00 13.43 C ANISOU 1624 C ARG A 195 2098 1297 1708 133 -174 -76 C ATOM 1625 O ARG A 195 6.065 -37.027 26.056 1.00 13.56 O ANISOU 1625 O ARG A 195 2110 1327 1714 145 -151 -66 O ATOM 1626 CB ARG A 195 8.384 -35.945 28.184 1.00 19.55 C ANISOU 1626 CB ARG A 195 2937 2025 2467 131 -237 -93 C ATOM 1627 CG ARG A 195 7.106 -35.990 29.023 1.00 19.35 C ANISOU 1627 CG ARG A 195 2955 1993 2403 157 -213 -81 C ATOM 1628 CD ARG A 195 7.168 -34.972 30.155 1.00 23.67 C ANISOU 1628 CD ARG A 195 3565 2512 2918 161 -226 -89 C ATOM 1629 NE ARG A 195 8.430 -35.070 30.875 1.00 28.80 N ANISOU 1629 NE ARG A 195 4224 3148 3569 145 -277 -103 N ATOM 1630 CZ ARG A 195 9.040 -34.049 31.465 1.00 28.67 C ANISOU 1630 CZ ARG A 195 4245 3108 3541 131 -302 -119 C ATOM 1631 NH1 ARG A 195 8.502 -32.833 31.440 1.00 23.38 N ANISOU 1631 NH1 ARG A 195 3608 2420 2856 135 -277 -124 N ATOM 1632 NH2 ARG A 195 10.188 -34.251 32.091 1.00 34.26 N ANISOU 1632 NH2 ARG A 195 4956 3809 4252 113 -353 -128 N ATOM 1633 N TYR A 196 7.109 -35.119 25.508 1.00 16.27 N ANISOU 1633 N TYR A 196 2455 1657 2071 125 -164 -73 N ATOM 1634 CA TYR A 196 5.908 -34.519 24.903 1.00 15.08 C ANISOU 1634 CA TYR A 196 2302 1522 1908 135 -125 -52 C ATOM 1635 C TYR A 196 5.446 -35.275 23.656 1.00 14.31 C ANISOU 1635 C TYR A 196 2154 1464 1819 126 -104 -44 C ATOM 1636 O TYR A 196 4.301 -35.118 23.204 1.00 12.73 O ANISOU 1636 O TYR A 196 1946 1284 1606 134 -74 -23 O ATOM 1637 CB TYR A 196 6.151 -33.048 24.575 1.00 17.38 C ANISOU 1637 CB TYR A 196 2599 1799 2204 129 -119 -46 C ATOM 1638 CG TYR A 196 6.797 -32.313 25.717 1.00 21.19 C ANISOU 1638 CG TYR A 196 3129 2240 2680 129 -144 -62 C ATOM 1639 CD1 TYR A 196 6.242 -32.350 26.990 1.00 20.98 C ANISOU 1639 CD1 TYR A 196 3157 2191 2623 147 -144 -64 C ATOM 1640 CD2 TYR A 196 7.989 -31.624 25.537 1.00 28.95 C ANISOU 1640 CD2 TYR A 196 4105 3209 3687 109 -170 -74 C ATOM 1641 CE1 TYR A 196 6.841 -31.693 28.048 1.00 24.20 C ANISOU 1641 CE1 TYR A 196 3613 2564 3019 143 -169 -82 C ATOM 1642 CE2 TYR A 196 8.600 -30.965 26.592 1.00 30.64 C ANISOU 1642 CE2 TYR A 196 4363 3385 3893 104 -198 -91 C ATOM 1643 CZ TYR A 196 8.019 -31.003 27.843 1.00 30.86 C ANISOU 1643 CZ TYR A 196 4447 3392 3885 120 -198 -97 C ATOM 1644 OH TYR A 196 8.622 -30.349 28.895 1.00 32.91 O ANISOU 1644 OH TYR A 196 4756 3618 4132 112 -227 -117 O ATOM 1645 N PHE A 197 6.313 -36.145 23.150 1.00 9.74 N ANISOU 1645 N PHE A 197 1541 897 1262 111 -119 -62 N ATOM 1646 CA PHE A 197 6.071 -36.815 21.877 1.00 16.08 C ANISOU 1646 CA PHE A 197 2298 1739 2073 97 -101 -64 C ATOM 1647 C PHE A 197 5.928 -38.330 22.044 1.00 13.97 C ANISOU 1647 C PHE A 197 2020 1477 1813 98 -101 -76 C ATOM 1648 O PHE A 197 5.819 -39.057 21.064 1.00 11.77 O ANISOU 1648 O PHE A 197 1705 1225 1543 84 -87 -85 O ATOM 1649 CB PHE A 197 7.192 -36.445 20.897 1.00 15.93 C ANISOU 1649 CB PHE A 197 2245 1731 2077 77 -107 -74 C ATOM 1650 CG PHE A 197 7.339 -34.967 20.720 1.00 14.48 C ANISOU 1650 CG PHE A 197 2069 1540 1893 76 -105 -59 C ATOM 1651 CD1 PHE A 197 6.569 -34.297 19.791 1.00 10.51 C ANISOU 1651 CD1 PHE A 197 1549 1066 1379 74 -78 -36 C ATOM 1652 CD2 PHE A 197 8.198 -34.234 21.536 1.00 14.96 C ANISOU 1652 CD2 PHE A 197 2156 1563 1964 77 -131 -65 C ATOM 1653 CE1 PHE A 197 6.665 -32.923 19.640 1.00 16.33 C ANISOU 1653 CE1 PHE A 197 2291 1793 2121 75 -72 -18 C ATOM 1654 CE2 PHE A 197 8.307 -32.865 21.398 1.00 14.59 C ANISOU 1654 CE2 PHE A 197 2117 1504 1922 75 -127 -53 C ATOM 1655 CZ PHE A 197 7.528 -32.205 20.445 1.00 12.99 C ANISOU 1655 CZ PHE A 197 1895 1328 1712 76 -95 -28 C ATOM 1656 N LYS A 198 5.924 -38.797 23.296 1.00 13.64 N ANISOU 1656 N LYS A 198 2008 1407 1768 114 -116 -77 N ATOM 1657 CA LYS A 198 5.833 -40.229 23.578 1.00 13.40 C ANISOU 1657 CA LYS A 198 1966 1375 1750 117 -117 -85 C ATOM 1658 C LYS A 198 4.433 -40.683 23.244 1.00 16.42 C ANISOU 1658 C LYS A 198 2343 1779 2118 122 -88 -72 C ATOM 1659 O LYS A 198 3.488 -40.016 23.642 1.00 13.01 O ANISOU 1659 O LYS A 198 1936 1346 1663 137 -76 -50 O ATOM 1660 CB LYS A 198 6.083 -40.501 25.068 1.00 13.19 C ANISOU 1660 CB LYS A 198 1976 1317 1718 134 -139 -81 C ATOM 1661 CG LYS A 198 7.565 -40.506 25.478 1.00 10.01 C ANISOU 1661 CG LYS A 198 1571 895 1339 126 -174 -93 C ATOM 1662 CD LYS A 198 7.681 -40.482 26.992 1.00 8.55 C ANISOU 1662 CD LYS A 198 1429 684 1135 142 -199 -84 C ATOM 1663 CE LYS A 198 9.133 -40.252 27.434 1.00 10.62 C ANISOU 1663 CE LYS A 198 1690 929 1415 129 -240 -92 C ATOM 1664 NZ LYS A 198 9.975 -41.450 27.150 1.00 14.76 N ANISOU 1664 NZ LYS A 198 2171 1454 1982 122 -248 -96 N ATOM 1665 N GLY A 199 4.302 -41.803 22.530 1.00 12.98 N ANISOU 1665 N GLY A 199 1873 1361 1699 109 -77 -86 N ATOM 1666 CA GLY A 199 2.982 -42.349 22.208 1.00 11.79 C ANISOU 1666 CA GLY A 199 1712 1230 1538 109 -54 -74 C ATOM 1667 C GLY A 199 2.319 -42.946 23.440 1.00 14.45 C ANISOU 1667 C GLY A 199 2075 1543 1872 133 -54 -58 C ATOM 1668 O GLY A 199 2.987 -43.298 24.399 1.00 16.53 O ANISOU 1668 O GLY A 199 2356 1780 2146 145 -71 -62 O ATOM 1669 N PRO A 200 0.980 -43.048 23.433 1.00 10.74 N ANISOU 1669 N PRO A 200 1606 1086 1388 141 -34 -35 N ATOM 1670 CA PRO A 200 0.311 -43.720 24.549 1.00 12.28 C ANISOU 1670 CA PRO A 200 1821 1260 1583 165 -29 -17 C ATOM 1671 C PRO A 200 0.882 -45.125 24.802 1.00 13.89 C ANISOU 1671 C PRO A 200 2009 1449 1821 161 -37 -36 C ATOM 1672 O PRO A 200 0.897 -45.581 25.950 1.00 15.84 O ANISOU 1672 O PRO A 200 2277 1672 2071 183 -43 -24 O ATOM 1673 CB PRO A 200 -1.144 -43.797 24.074 1.00 8.24 C ANISOU 1673 CB PRO A 200 1296 772 1064 164 -5 7 C ATOM 1674 CG PRO A 200 -1.313 -42.571 23.242 1.00 14.32 C ANISOU 1674 CG PRO A 200 2060 1567 1815 153 2 17 C ATOM 1675 CD PRO A 200 0.028 -42.401 22.518 1.00 15.01 C ANISOU 1675 CD PRO A 200 2132 1660 1912 131 -15 -17 C ATOM 1676 N GLU A 201 1.371 -45.795 23.758 1.00 10.11 N ANISOU 1676 N GLU A 201 1493 984 1366 135 -35 -65 N ATOM 1677 CA GLU A 201 1.900 -47.140 23.944 1.00 12.28 C ANISOU 1677 CA GLU A 201 1749 1239 1679 132 -36 -82 C ATOM 1678 C GLU A 201 3.086 -47.133 24.921 1.00 14.93 C ANISOU 1678 C GLU A 201 2101 1545 2026 146 -60 -82 C ATOM 1679 O GLU A 201 3.215 -48.024 25.770 1.00 13.14 O ANISOU 1679 O GLU A 201 1876 1296 1821 161 -64 -73 O ATOM 1680 CB GLU A 201 2.281 -47.803 22.605 1.00 15.02 C ANISOU 1680 CB GLU A 201 2056 1602 2048 100 -25 -118 C ATOM 1681 CG GLU A 201 3.278 -47.031 21.735 1.00 12.17 C ANISOU 1681 CG GLU A 201 1686 1257 1682 82 -31 -138 C ATOM 1682 CD GLU A 201 2.589 -46.095 20.760 1.00 16.55 C ANISOU 1682 CD GLU A 201 2235 1850 2202 67 -23 -132 C ATOM 1683 OE1 GLU A 201 1.789 -45.257 21.212 1.00 13.16 O ANISOU 1683 OE1 GLU A 201 1828 1427 1746 82 -23 -101 O ATOM 1684 OE2 GLU A 201 2.846 -46.196 19.545 1.00 13.80 O ANISOU 1684 OE2 GLU A 201 1861 1528 1854 41 -13 -156 O ATOM 1685 N LEU A 202 3.943 -46.123 24.803 1.00 14.58 N ANISOU 1685 N LEU A 202 2066 1503 1970 142 -77 -88 N ATOM 1686 CA LEU A 202 5.064 -45.991 25.714 1.00 14.40 C ANISOU 1686 CA LEU A 202 2059 1456 1955 151 -105 -86 C ATOM 1687 C LEU A 202 4.571 -45.641 27.113 1.00 13.86 C ANISOU 1687 C LEU A 202 2035 1373 1858 178 -116 -58 C ATOM 1688 O LEU A 202 5.108 -46.120 28.111 1.00 14.22 O ANISOU 1688 O LEU A 202 2091 1400 1912 190 -135 -49 O ATOM 1689 CB LEU A 202 6.035 -44.909 25.226 1.00 14.75 C ANISOU 1689 CB LEU A 202 2103 1506 1995 137 -122 -97 C ATOM 1690 CG LEU A 202 6.452 -44.972 23.756 1.00 11.63 C ANISOU 1690 CG LEU A 202 1670 1131 1619 112 -107 -122 C ATOM 1691 CD1 LEU A 202 7.373 -43.803 23.446 1.00 13.79 C ANISOU 1691 CD1 LEU A 202 1945 1407 1887 103 -124 -126 C ATOM 1692 CD2 LEU A 202 7.136 -46.309 23.442 1.00 14.66 C ANISOU 1692 CD2 LEU A 202 2018 1504 2048 103 -100 -140 C ATOM 1693 N LEU A 203 3.552 -44.789 27.180 1.00 10.65 N ANISOU 1693 N LEU A 203 1654 976 1415 187 -102 -44 N ATOM 1694 CA LEU A 203 3.105 -44.252 28.458 1.00 11.46 C ANISOU 1694 CA LEU A 203 1806 1065 1485 212 -107 -22 C ATOM 1695 C LEU A 203 2.335 -45.294 29.267 1.00 14.34 C ANISOU 1695 C LEU A 203 2175 1421 1853 233 -95 0 C ATOM 1696 O LEU A 203 2.190 -45.172 30.482 1.00 13.07 O ANISOU 1696 O LEU A 203 2052 1246 1668 256 -102 18 O ATOM 1697 CB LEU A 203 2.260 -42.997 28.224 1.00 10.73 C ANISOU 1697 CB LEU A 203 1737 982 1359 217 -90 -11 C ATOM 1698 CG LEU A 203 3.019 -41.862 27.516 1.00 16.30 C ANISOU 1698 CG LEU A 203 2439 1693 2061 199 -101 -27 C ATOM 1699 CD1 LEU A 203 2.074 -40.750 27.109 1.00 15.99 C ANISOU 1699 CD1 LEU A 203 2413 1665 2000 203 -76 -12 C ATOM 1700 CD2 LEU A 203 4.158 -41.327 28.381 1.00 16.19 C ANISOU 1700 CD2 LEU A 203 2455 1657 2040 199 -135 -37 C ATOM 1701 N VAL A 204 1.835 -46.319 28.589 1.00 18.39 N ANISOU 1701 N VAL A 204 2650 1942 2396 225 -76 -2 N ATOM 1702 CA VAL A 204 1.150 -47.409 29.271 1.00 16.36 C ANISOU 1702 CA VAL A 204 2389 1673 2152 243 -63 19 C ATOM 1703 C VAL A 204 2.034 -48.646 29.348 1.00 18.17 C ANISOU 1703 C VAL A 204 2588 1888 2427 237 -73 9 C ATOM 1704 O VAL A 204 1.582 -49.712 29.772 1.00 17.81 O ANISOU 1704 O VAL A 204 2530 1832 2405 249 -61 24 O ATOM 1705 CB VAL A 204 -0.215 -47.756 28.610 1.00 10.98 C ANISOU 1705 CB VAL A 204 1687 1007 1476 240 -32 29 C ATOM 1706 CG1 VAL A 204 -1.130 -46.542 28.617 1.00 16.54 C ANISOU 1706 CG1 VAL A 204 2420 1724 2142 250 -18 48 C ATOM 1707 CG2 VAL A 204 -0.022 -48.272 27.191 1.00 12.50 C ANISOU 1707 CG2 VAL A 204 1834 1216 1699 207 -25 -1 C ATOM 1708 N ASP A 205 3.294 -48.494 28.938 1.00 14.79 N ANISOU 1708 N ASP A 205 2145 1458 2015 220 -94 -14 N ATOM 1709 CA ASP A 205 4.294 -49.546 29.095 1.00 15.82 C ANISOU 1709 CA ASP A 205 2248 1572 2192 217 -104 -19 C ATOM 1710 C ASP A 205 4.026 -50.758 28.190 1.00 22.82 C ANISOU 1710 C ASP A 205 3089 2455 3125 202 -76 -37 C ATOM 1711 O ASP A 205 4.309 -51.892 28.570 1.00 25.55 O ANISOU 1711 O ASP A 205 3414 2781 3513 209 -72 -29 O ATOM 1712 CB ASP A 205 4.357 -49.970 30.573 1.00 24.18 C ANISOU 1712 CB ASP A 205 3328 2613 3245 243 -119 14 C ATOM 1713 CG ASP A 205 5.636 -50.713 30.931 1.00 37.88 C ANISOU 1713 CG ASP A 205 5039 4333 5022 242 -139 18 C ATOM 1714 OD1 ASP A 205 6.628 -50.624 30.171 1.00 36.53 O ANISOU 1714 OD1 ASP A 205 4842 4160 4876 221 -148 -5 O ATOM 1715 OD2 ASP A 205 5.647 -51.383 31.992 1.00 36.60 O ANISOU 1715 OD2 ASP A 205 4882 4159 4867 262 -147 48 O ATOM 1716 N TYR A 206 3.491 -50.516 26.993 1.00 14.96 N ANISOU 1716 N TYR A 206 2079 1480 2124 181 -58 -59 N ATOM 1717 CA TYR A 206 3.277 -51.581 26.007 1.00 14.72 C ANISOU 1717 CA TYR A 206 2011 1450 2134 161 -33 -85 C ATOM 1718 C TYR A 206 4.460 -51.685 25.057 1.00 14.68 C ANISOU 1718 C TYR A 206 1978 1444 2154 138 -32 -119 C ATOM 1719 O TYR A 206 4.713 -50.761 24.293 1.00 15.31 O ANISOU 1719 O TYR A 206 2061 1546 2209 123 -37 -135 O ATOM 1720 CB TYR A 206 2.013 -51.320 25.182 1.00 15.52 C ANISOU 1720 CB TYR A 206 2108 1577 2210 146 -14 -90 C ATOM 1721 CG TYR A 206 1.659 -52.485 24.279 1.00 14.67 C ANISOU 1721 CG TYR A 206 1965 1469 2139 122 10 -117 C ATOM 1722 CD1 TYR A 206 1.137 -53.666 24.806 1.00 18.65 C ANISOU 1722 CD1 TYR A 206 2457 1950 2680 132 24 -105 C ATOM 1723 CD2 TYR A 206 1.854 -52.412 22.905 1.00 15.70 C ANISOU 1723 CD2 TYR A 206 2075 1622 2267 89 20 -154 C ATOM 1724 CE1 TYR A 206 0.810 -54.738 23.983 1.00 16.60 C ANISOU 1724 CE1 TYR A 206 2166 1685 2456 107 47 -134 C ATOM 1725 CE2 TYR A 206 1.542 -53.477 22.078 1.00 13.49 C ANISOU 1725 CE2 TYR A 206 1767 1342 2018 64 42 -185 C ATOM 1726 CZ TYR A 206 1.013 -54.634 22.621 1.00 15.11 C ANISOU 1726 CZ TYR A 206 1962 1520 2261 72 55 -176 C ATOM 1727 OH TYR A 206 0.697 -55.688 21.793 1.00 16.04 O ANISOU 1727 OH TYR A 206 2052 1632 2410 44 78 -210 O ATOM 1728 N GLN A 207 5.159 -52.820 25.077 1.00 15.08 N ANISOU 1728 N GLN A 207 2001 1469 2259 136 -23 -129 N ATOM 1729 CA GLN A 207 6.453 -52.926 24.396 1.00 18.49 C ANISOU 1729 CA GLN A 207 2408 1894 2722 121 -22 -155 C ATOM 1730 C GLN A 207 6.423 -53.393 22.943 1.00 18.69 C ANISOU 1730 C GLN A 207 2407 1930 2764 91 9 -199 C ATOM 1731 O GLN A 207 7.420 -53.232 22.225 1.00 16.10 O ANISOU 1731 O GLN A 207 2063 1603 2451 78 13 -221 O ATOM 1732 CB GLN A 207 7.391 -53.850 25.183 1.00 16.62 C ANISOU 1732 CB GLN A 207 2154 1622 2540 136 -27 -139 C ATOM 1733 CG GLN A 207 7.692 -53.387 26.591 1.00 18.90 C ANISOU 1733 CG GLN A 207 2468 1904 2810 162 -62 -97 C ATOM 1734 CD GLN A 207 8.671 -54.310 27.280 1.00 24.07 C ANISOU 1734 CD GLN A 207 3097 2527 3520 174 -68 -76 C ATOM 1735 OE1 GLN A 207 8.278 -55.136 28.097 1.00 26.32 O ANISOU 1735 OE1 GLN A 207 3379 2795 3825 192 -63 -49 O ATOM 1736 NE2 GLN A 207 9.955 -54.196 26.928 1.00 20.65 N ANISOU 1736 NE2 GLN A 207 2642 2087 3116 165 -77 -84 N ATOM 1737 N MET A 208 5.316 -53.989 22.503 1.00 15.20 N ANISOU 1737 N MET A 208 1960 1496 2321 79 30 -212 N ATOM 1738 CA MET A 208 5.269 -54.565 21.153 1.00 13.79 C ANISOU 1738 CA MET A 208 1757 1326 2156 47 60 -258 C ATOM 1739 C MET A 208 4.736 -53.552 20.140 1.00 14.19 C ANISOU 1739 C MET A 208 1817 1425 2151 25 57 -272 C ATOM 1740 O MET A 208 3.758 -53.813 19.417 1.00 15.06 O ANISOU 1740 O MET A 208 1922 1557 2245 2 71 -289 O ATOM 1741 CB MET A 208 4.452 -55.867 21.152 1.00 15.06 C ANISOU 1741 CB MET A 208 1903 1467 2353 40 84 -269 C ATOM 1742 CG MET A 208 4.778 -56.815 20.007 1.00 18.48 C ANISOU 1742 CG MET A 208 2310 1891 2821 10 118 -321 C ATOM 1743 SD MET A 208 3.933 -58.428 20.086 1.00 20.80 S ANISOU 1743 SD MET A 208 2584 2150 3168 1 148 -337 S ATOM 1744 CE MET A 208 4.650 -59.091 21.589 1.00 36.70 C ANISOU 1744 CE MET A 208 4590 4111 5243 43 143 -292 C ATOM 1745 N TYR A 209 5.378 -52.386 20.102 1.00 14.68 N ANISOU 1745 N TYR A 209 1890 1502 2185 30 38 -262 N ATOM 1746 CA TYR A 209 4.928 -51.287 19.249 1.00 15.47 C ANISOU 1746 CA TYR A 209 1998 1647 2233 14 34 -265 C ATOM 1747 C TYR A 209 5.668 -51.312 17.920 1.00 16.22 C ANISOU 1747 C TYR A 209 2072 1760 2331 -14 52 -304 C ATOM 1748 O TYR A 209 6.423 -52.245 17.657 1.00 13.40 O ANISOU 1748 O TYR A 209 1696 1378 2017 -20 72 -331 O ATOM 1749 CB TYR A 209 5.095 -49.934 19.959 1.00 11.07 C ANISOU 1749 CB TYR A 209 1466 1095 1644 34 6 -230 C ATOM 1750 CG TYR A 209 6.518 -49.567 20.373 1.00 13.55 C ANISOU 1750 CG TYR A 209 1781 1388 1980 45 -10 -226 C ATOM 1751 CD1 TYR A 209 7.403 -49.025 19.461 1.00 14.76 C ANISOU 1751 CD1 TYR A 209 1920 1556 2132 30 -7 -244 C ATOM 1752 CD2 TYR A 209 6.945 -49.725 21.692 1.00 10.71 C ANISOU 1752 CD2 TYR A 209 1434 996 1638 71 -31 -201 C ATOM 1753 CE1 TYR A 209 8.693 -48.669 19.829 1.00 18.96 C ANISOU 1753 CE1 TYR A 209 2448 2067 2687 39 -24 -237 C ATOM 1754 CE2 TYR A 209 8.238 -49.362 22.079 1.00 16.38 C ANISOU 1754 CE2 TYR A 209 2150 1697 2375 77 -52 -195 C ATOM 1755 CZ TYR A 209 9.109 -48.843 21.139 1.00 17.04 C ANISOU 1755 CZ TYR A 209 2217 1793 2463 61 -48 -213 C ATOM 1756 OH TYR A 209 10.390 -48.479 21.503 1.00 15.81 O ANISOU 1756 OH TYR A 209 2056 1620 2331 66 -70 -203 O ATOM 1757 N ASP A 210 5.446 -50.303 17.078 1.00 12.80 N ANISOU 1757 N ASP A 210 1641 1368 1853 -29 49 -304 N ATOM 1758 CA ASP A 210 5.954 -50.345 15.701 1.00 10.01 C ANISOU 1758 CA ASP A 210 1270 1042 1493 -58 70 -341 C ATOM 1759 C ASP A 210 6.120 -48.956 15.095 1.00 11.19 C ANISOU 1759 C ASP A 210 1422 1229 1600 -63 60 -326 C ATOM 1760 O ASP A 210 6.145 -47.958 15.816 1.00 12.61 O ANISOU 1760 O ASP A 210 1619 1406 1768 -42 37 -291 O ATOM 1761 CB ASP A 210 5.084 -51.258 14.813 1.00 10.75 C ANISOU 1761 CB ASP A 210 1352 1155 1577 -89 93 -375 C ATOM 1762 CG ASP A 210 3.615 -50.829 14.764 1.00 15.03 C ANISOU 1762 CG ASP A 210 1902 1732 2075 -97 81 -351 C ATOM 1763 OD1 ASP A 210 3.333 -49.779 14.153 1.00 17.79 O ANISOU 1763 OD1 ASP A 210 2253 2126 2381 -106 73 -336 O ATOM 1764 OD2 ASP A 210 2.731 -51.551 15.298 1.00 15.69 O ANISOU 1764 OD2 ASP A 210 1988 1802 2173 -94 81 -344 O ATOM 1765 N TYR A 211 6.242 -48.885 13.771 1.00 10.85 N ANISOU 1765 N TYR A 211 1364 1223 1535 -91 78 -353 N ATOM 1766 CA TYR A 211 6.354 -47.607 13.075 1.00 10.39 C ANISOU 1766 CA TYR A 211 1304 1206 1437 -97 72 -337 C ATOM 1767 C TYR A 211 5.315 -46.577 13.500 1.00 14.59 C ANISOU 1767 C TYR A 211 1850 1758 1933 -86 51 -292 C ATOM 1768 O TYR A 211 5.556 -45.372 13.441 1.00 10.36 O ANISOU 1768 O TYR A 211 1319 1237 1381 -78 41 -266 O ATOM 1769 CB TYR A 211 6.202 -47.816 11.562 1.00 11.86 C ANISOU 1769 CB TYR A 211 1474 1440 1593 -133 96 -369 C ATOM 1770 CG TYR A 211 6.921 -49.015 10.988 1.00 9.21 C ANISOU 1770 CG TYR A 211 1126 1086 1287 -149 126 -421 C ATOM 1771 CD1 TYR A 211 8.311 -49.018 10.846 1.00 13.55 C ANISOU 1771 CD1 TYR A 211 1665 1612 1870 -140 140 -433 C ATOM 1772 CD2 TYR A 211 6.211 -50.139 10.560 1.00 11.36 C ANISOU 1772 CD2 TYR A 211 1396 1364 1557 -174 144 -457 C ATOM 1773 CE1 TYR A 211 8.967 -50.106 10.313 1.00 15.78 C ANISOU 1773 CE1 TYR A 211 1937 1875 2184 -152 175 -479 C ATOM 1774 CE2 TYR A 211 6.865 -51.238 10.017 1.00 14.27 C ANISOU 1774 CE2 TYR A 211 1755 1711 1955 -189 177 -508 C ATOM 1775 CZ TYR A 211 8.247 -51.209 9.892 1.00 13.96 C ANISOU 1775 CZ TYR A 211 1707 1648 1950 -177 195 -518 C ATOM 1776 OH TYR A 211 8.917 -52.279 9.350 1.00 14.37 O ANISOU 1776 OH TYR A 211 1749 1675 2035 -189 234 -567 O ATOM 1777 N SER A 212 4.140 -47.054 13.888 1.00 11.20 N ANISOU 1777 N SER A 212 1428 1331 1496 -87 49 -283 N ATOM 1778 CA SER A 212 3.035 -46.160 14.224 1.00 12.21 C ANISOU 1778 CA SER A 212 1567 1479 1592 -77 36 -240 C ATOM 1779 C SER A 212 3.364 -45.212 15.393 1.00 8.63 C ANISOU 1779 C SER A 212 1138 995 1147 -43 18 -205 C ATOM 1780 O SER A 212 2.763 -44.149 15.512 1.00 11.13 O ANISOU 1780 O SER A 212 1464 1327 1438 -33 11 -170 O ATOM 1781 CB SER A 212 1.762 -46.964 14.481 1.00 12.26 C ANISOU 1781 CB SER A 212 1574 1488 1597 -83 38 -235 C ATOM 1782 OG SER A 212 1.961 -47.941 15.491 1.00 12.60 O ANISOU 1782 OG SER A 212 1626 1482 1680 -65 38 -245 O ATOM 1783 N LEU A 213 4.334 -45.573 16.233 1.00 11.37 N ANISOU 1783 N LEU A 213 1494 1296 1529 -25 10 -215 N ATOM 1784 CA LEU A 213 4.826 -44.625 17.252 1.00 10.76 C ANISOU 1784 CA LEU A 213 1441 1192 1455 2 -11 -188 C ATOM 1785 C LEU A 213 5.200 -43.272 16.632 1.00 14.81 C ANISOU 1785 C LEU A 213 1951 1728 1948 -3 -14 -175 C ATOM 1786 O LEU A 213 4.847 -42.213 17.162 1.00 11.80 O ANISOU 1786 O LEU A 213 1590 1343 1551 12 -23 -144 O ATOM 1787 CB LEU A 213 6.051 -45.190 17.975 1.00 11.77 C ANISOU 1787 CB LEU A 213 1571 1278 1625 13 -22 -202 C ATOM 1788 CG LEU A 213 6.723 -44.207 18.928 1.00 15.92 C ANISOU 1788 CG LEU A 213 2119 1779 2152 33 -47 -180 C ATOM 1789 CD1 LEU A 213 5.835 -43.946 20.149 1.00 17.71 C ANISOU 1789 CD1 LEU A 213 2379 1988 2360 56 -58 -153 C ATOM 1790 CD2 LEU A 213 8.092 -44.747 19.354 1.00 14.74 C ANISOU 1790 CD2 LEU A 213 1960 1596 2044 37 -59 -193 C ATOM 1791 N ASP A 214 5.927 -43.309 15.515 1.00 12.40 N ANISOU 1791 N ASP A 214 1620 1445 1646 -24 -3 -196 N ATOM 1792 CA ASP A 214 6.403 -42.087 14.861 1.00 13.58 C ANISOU 1792 CA ASP A 214 1761 1616 1782 -29 -4 -182 C ATOM 1793 C ASP A 214 5.228 -41.224 14.408 1.00 11.99 C ANISOU 1793 C ASP A 214 1560 1453 1541 -33 2 -151 C ATOM 1794 O ASP A 214 5.343 -40.003 14.304 1.00 11.26 O ANISOU 1794 O ASP A 214 1470 1368 1441 -27 -2 -124 O ATOM 1795 CB ASP A 214 7.278 -42.419 13.647 1.00 13.08 C ANISOU 1795 CB ASP A 214 1670 1575 1726 -51 14 -211 C ATOM 1796 CG ASP A 214 8.605 -43.068 14.031 1.00 15.36 C ANISOU 1796 CG ASP A 214 1953 1823 2060 -45 11 -233 C ATOM 1797 OD1 ASP A 214 9.071 -42.892 15.179 1.00 14.00 O ANISOU 1797 OD1 ASP A 214 1797 1610 1912 -25 -11 -220 O ATOM 1798 OD2 ASP A 214 9.184 -43.755 13.163 1.00 14.88 O ANISOU 1798 OD2 ASP A 214 1871 1773 2012 -61 33 -263 O ATOM 1799 N MET A 215 4.105 -41.866 14.120 1.00 11.39 N ANISOU 1799 N MET A 215 1479 1402 1447 -44 11 -151 N ATOM 1800 CA MET A 215 2.942 -41.139 13.630 1.00 10.59 C ANISOU 1800 CA MET A 215 1371 1341 1311 -49 16 -116 C ATOM 1801 C MET A 215 2.242 -40.373 14.764 1.00 11.69 C ANISOU 1801 C MET A 215 1537 1454 1449 -20 9 -77 C ATOM 1802 O MET A 215 1.737 -39.267 14.552 1.00 13.02 O ANISOU 1802 O MET A 215 1704 1641 1602 -15 13 -40 O ATOM 1803 CB MET A 215 1.988 -42.084 12.888 1.00 11.39 C ANISOU 1803 CB MET A 215 1454 1481 1392 -76 26 -129 C ATOM 1804 CG MET A 215 2.641 -42.790 11.694 1.00 16.78 C ANISOU 1804 CG MET A 215 2114 2191 2068 -107 37 -172 C ATOM 1805 SD MET A 215 3.507 -41.675 10.551 1.00 14.79 S ANISOU 1805 SD MET A 215 1844 1978 1798 -118 45 -164 S ATOM 1806 CE MET A 215 2.120 -40.845 9.765 1.00 15.01 C ANISOU 1806 CE MET A 215 1854 2071 1778 -133 45 -115 C ATOM 1807 N TRP A 216 2.221 -40.948 15.967 1.00 11.33 N ANISOU 1807 N TRP A 216 1517 1366 1424 0 1 -83 N ATOM 1808 CA TRP A 216 1.779 -40.193 17.130 1.00 11.21 C ANISOU 1808 CA TRP A 216 1533 1319 1407 29 -4 -52 C ATOM 1809 C TRP A 216 2.648 -38.945 17.312 1.00 12.59 C ANISOU 1809 C TRP A 216 1720 1476 1586 39 -12 -43 C ATOM 1810 O TRP A 216 2.144 -37.830 17.439 1.00 14.33 O ANISOU 1810 O TRP A 216 1951 1699 1796 51 -5 -11 O ATOM 1811 CB TRP A 216 1.812 -41.028 18.418 1.00 6.73 C ANISOU 1811 CB TRP A 216 992 709 857 49 -13 -62 C ATOM 1812 CG TRP A 216 1.405 -40.200 19.609 1.00 13.29 C ANISOU 1812 CG TRP A 216 1860 1509 1679 79 -16 -33 C ATOM 1813 CD1 TRP A 216 2.226 -39.447 20.407 1.00 9.88 C ANISOU 1813 CD1 TRP A 216 1457 1044 1252 94 -30 -34 C ATOM 1814 CD2 TRP A 216 0.062 -39.969 20.087 1.00 13.28 C ANISOU 1814 CD2 TRP A 216 1873 1509 1663 96 -1 2 C ATOM 1815 NE1 TRP A 216 1.479 -38.794 21.368 1.00 14.93 N ANISOU 1815 NE1 TRP A 216 2131 1663 1877 119 -24 -7 N ATOM 1816 CE2 TRP A 216 0.153 -39.096 21.189 1.00 13.99 C ANISOU 1816 CE2 TRP A 216 2004 1564 1748 123 -4 17 C ATOM 1817 CE3 TRP A 216 -1.197 -40.434 19.701 1.00 11.54 C ANISOU 1817 CE3 TRP A 216 1634 1316 1434 91 14 23 C ATOM 1818 CZ2 TRP A 216 -0.972 -38.680 21.914 1.00 14.73 C ANISOU 1818 CZ2 TRP A 216 2122 1647 1829 147 14 52 C ATOM 1819 CZ3 TRP A 216 -2.320 -40.005 20.415 1.00 12.21 C ANISOU 1819 CZ3 TRP A 216 1739 1391 1510 115 29 62 C ATOM 1820 CH2 TRP A 216 -2.195 -39.146 21.511 1.00 16.29 C ANISOU 1820 CH2 TRP A 216 2298 1870 2022 145 31 76 C ATOM 1821 N SER A 217 3.966 -39.147 17.330 1.00 10.21 N ANISOU 1821 N SER A 217 1417 1157 1307 34 -25 -71 N ATOM 1822 CA SER A 217 4.913 -38.038 17.478 1.00 8.02 C ANISOU 1822 CA SER A 217 1147 861 1040 39 -36 -66 C ATOM 1823 C SER A 217 4.679 -36.954 16.437 1.00 10.36 C ANISOU 1823 C SER A 217 1423 1192 1322 29 -22 -42 C ATOM 1824 O SER A 217 4.692 -35.769 16.758 1.00 10.59 O ANISOU 1824 O SER A 217 1466 1205 1352 40 -22 -19 O ATOM 1825 CB SER A 217 6.350 -38.561 17.383 1.00 7.89 C ANISOU 1825 CB SER A 217 1118 829 1052 29 -49 -97 C ATOM 1826 OG SER A 217 6.576 -39.521 18.396 1.00 12.32 O ANISOU 1826 OG SER A 217 1695 1357 1628 40 -63 -112 O ATOM 1827 N LEU A 218 4.455 -37.361 15.189 1.00 10.19 N ANISOU 1827 N LEU A 218 1367 1218 1287 7 -8 -47 N ATOM 1828 CA LEU A 218 4.193 -36.403 14.132 1.00 9.10 C ANISOU 1828 CA LEU A 218 1204 1120 1132 -4 6 -19 C ATOM 1829 C LEU A 218 2.903 -35.642 14.397 1.00 12.87 C ANISOU 1829 C LEU A 218 1691 1606 1593 10 16 26 C ATOM 1830 O LEU A 218 2.821 -34.441 14.126 1.00 12.97 O ANISOU 1830 O LEU A 218 1698 1625 1607 15 24 59 O ATOM 1831 CB LEU A 218 4.110 -37.091 12.767 1.00 11.20 C ANISOU 1831 CB LEU A 218 1436 1442 1379 -32 17 -33 C ATOM 1832 CG LEU A 218 3.924 -36.171 11.554 1.00 13.16 C ANISOU 1832 CG LEU A 218 1654 1741 1606 -46 31 -3 C ATOM 1833 CD1 LEU A 218 5.199 -35.411 11.225 1.00 13.89 C ANISOU 1833 CD1 LEU A 218 1736 1823 1719 -46 30 -4 C ATOM 1834 CD2 LEU A 218 3.467 -36.973 10.342 1.00 11.86 C ANISOU 1834 CD2 LEU A 218 1462 1636 1409 -77 41 -16 C ATOM 1835 N GLY A 219 1.898 -36.337 14.926 1.00 10.33 N ANISOU 1835 N GLY A 219 1381 1282 1263 17 18 30 N ATOM 1836 CA GLY A 219 0.635 -35.690 15.243 1.00 10.36 C ANISOU 1836 CA GLY A 219 1392 1288 1254 32 31 75 C ATOM 1837 C GLY A 219 0.850 -34.643 16.323 1.00 16.41 C ANISOU 1837 C GLY A 219 2195 2004 2036 60 32 90 C ATOM 1838 O GLY A 219 0.261 -33.563 16.273 1.00 15.04 O ANISOU 1838 O GLY A 219 2021 1832 1861 72 48 130 O ATOM 1839 N CYS A 220 1.695 -34.955 17.305 1.00 14.35 N ANISOU 1839 N CYS A 220 1965 1698 1790 70 14 57 N ATOM 1840 CA CYS A 220 2.011 -33.977 18.352 1.00 14.61 C ANISOU 1840 CA CYS A 220 2037 1682 1832 92 11 63 C ATOM 1841 C CYS A 220 2.660 -32.726 17.759 1.00 17.41 C ANISOU 1841 C CYS A 220 2379 2038 2199 86 15 76 C ATOM 1842 O CYS A 220 2.312 -31.603 18.148 1.00 12.24 O ANISOU 1842 O CYS A 220 1742 1360 1548 101 28 102 O ATOM 1843 CB CYS A 220 2.921 -34.577 19.430 1.00 12.75 C ANISOU 1843 CB CYS A 220 1832 1405 1607 98 -14 27 C ATOM 1844 SG CYS A 220 2.153 -35.883 20.408 1.00 14.03 S ANISOU 1844 SG CYS A 220 2016 1555 1759 112 -16 20 S ATOM 1845 N MET A 221 3.586 -32.925 16.816 1.00 11.13 N ANISOU 1845 N MET A 221 1551 1267 1412 64 6 59 N ATOM 1846 CA MET A 221 4.206 -31.805 16.102 1.00 12.81 C ANISOU 1846 CA MET A 221 1743 1486 1638 57 11 75 C ATOM 1847 C MET A 221 3.153 -30.992 15.338 1.00 15.26 C ANISOU 1847 C MET A 221 2030 1830 1936 59 38 125 C ATOM 1848 O MET A 221 3.132 -29.764 15.418 1.00 14.88 O ANISOU 1848 O MET A 221 1986 1763 1903 69 50 152 O ATOM 1849 CB MET A 221 5.305 -32.292 15.145 1.00 11.62 C ANISOU 1849 CB MET A 221 1559 1360 1496 34 2 51 C ATOM 1850 CG MET A 221 6.523 -32.873 15.863 1.00 12.35 C ANISOU 1850 CG MET A 221 1668 1414 1611 33 -24 12 C ATOM 1851 SD MET A 221 7.872 -33.232 14.701 1.00 18.58 S ANISOU 1851 SD MET A 221 2414 2228 2419 11 -27 -9 S ATOM 1852 CE MET A 221 8.013 -31.674 13.847 1.00 10.91 C ANISOU 1852 CE MET A 221 1419 1273 1455 8 -11 30 C ATOM 1853 N LEU A 222 2.299 -31.678 14.586 1.00 13.02 N ANISOU 1853 N LEU A 222 1720 1598 1630 48 47 137 N ATOM 1854 CA LEU A 222 1.253 -31.001 13.836 1.00 10.60 C ANISOU 1854 CA LEU A 222 1386 1330 1310 47 70 190 C ATOM 1855 C LEU A 222 0.375 -30.150 14.750 1.00 11.17 C ANISOU 1855 C LEU A 222 1486 1366 1393 76 88 225 C ATOM 1856 O LEU A 222 0.137 -28.973 14.469 1.00 14.19 O ANISOU 1856 O LEU A 222 1857 1747 1788 84 107 267 O ATOM 1857 CB LEU A 222 0.412 -31.998 13.039 1.00 13.21 C ANISOU 1857 CB LEU A 222 1688 1719 1611 28 71 194 C ATOM 1858 CG LEU A 222 -0.696 -31.382 12.184 1.00 10.03 C ANISOU 1858 CG LEU A 222 1251 1368 1194 23 90 254 C ATOM 1859 CD1 LEU A 222 -0.140 -30.508 11.056 1.00 12.56 C ANISOU 1859 CD1 LEU A 222 1535 1723 1513 10 97 278 C ATOM 1860 CD2 LEU A 222 -1.555 -32.497 11.622 1.00 12.24 C ANISOU 1860 CD2 LEU A 222 1509 1698 1444 1 84 251 C ATOM 1861 N ALA A 223 -0.100 -30.737 15.845 1.00 10.39 N ANISOU 1861 N ALA A 223 1423 1235 1290 92 85 210 N ATOM 1862 CA ALA A 223 -0.955 -30.004 16.772 1.00 11.50 C ANISOU 1862 CA ALA A 223 1594 1337 1437 121 107 241 C ATOM 1863 C ALA A 223 -0.255 -28.740 17.268 1.00 17.44 C ANISOU 1863 C ALA A 223 2372 2040 2213 133 113 240 C ATOM 1864 O ALA A 223 -0.869 -27.681 17.331 1.00 12.42 O ANISOU 1864 O ALA A 223 1739 1391 1591 149 141 281 O ATOM 1865 CB ALA A 223 -1.359 -30.880 17.938 1.00 11.81 C ANISOU 1865 CB ALA A 223 1672 1347 1468 136 101 219 C ATOM 1866 N SER A 224 1.032 -28.847 17.610 1.00 15.01 N ANISOU 1866 N SER A 224 2082 1705 1915 124 87 195 N ATOM 1867 CA SER A 224 1.777 -27.685 18.103 1.00 11.85 C ANISOU 1867 CA SER A 224 1707 1256 1539 131 87 190 C ATOM 1868 C SER A 224 1.906 -26.601 17.028 1.00 14.62 C ANISOU 1868 C SER A 224 2017 1627 1909 124 105 227 C ATOM 1869 O SER A 224 1.892 -25.410 17.334 1.00 19.99 O ANISOU 1869 O SER A 224 2713 2271 2613 136 124 246 O ATOM 1870 CB SER A 224 3.168 -28.090 18.637 1.00 14.67 C ANISOU 1870 CB SER A 224 2085 1585 1904 119 50 137 C ATOM 1871 OG SER A 224 4.081 -28.342 17.583 1.00 15.88 O ANISOU 1871 OG SER A 224 2195 1771 2066 96 35 128 O ATOM 1872 N MET A 225 2.008 -27.004 15.767 1.00 14.19 N ANISOU 1872 N MET A 225 1905 1453 2035 42 41 352 N ATOM 1873 CA MET A 225 2.169 -26.027 14.695 1.00 14.12 C ANISOU 1873 CA MET A 225 1863 1430 2072 35 49 392 C ATOM 1874 C MET A 225 0.835 -25.351 14.319 1.00 15.20 C ANISOU 1874 C MET A 225 2014 1593 2167 58 70 385 C ATOM 1875 O MET A 225 0.747 -24.119 14.290 1.00 17.67 O ANISOU 1875 O MET A 225 2331 1871 2513 66 40 391 O ATOM 1876 CB MET A 225 2.801 -26.675 13.457 1.00 14.89 C ANISOU 1876 CB MET A 225 1910 1555 2193 10 95 437 C ATOM 1877 CG MET A 225 4.240 -27.172 13.649 1.00 22.12 C ANISOU 1877 CG MET A 225 2804 2439 3162 -15 74 454 C ATOM 1878 SD MET A 225 4.731 -28.223 12.259 1.00 33.16 S ANISOU 1878 SD MET A 225 4149 3886 4564 -39 138 498 S ATOM 1879 CE MET A 225 6.376 -28.710 12.724 1.00 48.15 C ANISOU 1879 CE MET A 225 6030 5742 6524 -65 103 510 C ATOM 1880 N ILE A 226 -0.197 -26.141 14.042 1.00 15.33 N ANISOU 1880 N ILE A 226 2040 1672 2113 67 120 372 N ATOM 1881 CA ILE A 226 -1.472 -25.542 13.606 1.00 16.81 C ANISOU 1881 CA ILE A 226 2238 1888 2259 88 144 367 C ATOM 1882 C ILE A 226 -2.176 -24.755 14.713 1.00 16.32 C ANISOU 1882 C ILE A 226 2224 1802 2175 116 100 326 C ATOM 1883 O ILE A 226 -2.868 -23.782 14.427 1.00 20.69 O ANISOU 1883 O ILE A 226 2784 2352 2725 131 98 328 O ATOM 1884 CB ILE A 226 -2.440 -26.548 12.927 1.00 14.15 C ANISOU 1884 CB ILE A 226 1897 1626 1853 92 211 366 C ATOM 1885 CG1 ILE A 226 -2.939 -27.603 13.922 1.00 14.27 C ANISOU 1885 CG1 ILE A 226 1948 1669 1806 102 214 324 C ATOM 1886 CG2 ILE A 226 -1.771 -27.188 11.710 1.00 15.37 C ANISOU 1886 CG2 ILE A 226 2002 1805 2033 67 255 409 C ATOM 1887 CD1 ILE A 226 -4.035 -28.491 13.350 1.00 13.53 C ANISOU 1887 CD1 ILE A 226 1854 1647 1641 109 276 319 C ATOM 1888 N PHE A 227 -1.965 -25.153 15.966 1.00 13.74 N ANISOU 1888 N PHE A 227 1930 1458 1834 123 65 290 N ATOM 1889 CA PHE A 227 -2.565 -24.489 17.119 1.00 13.81 C ANISOU 1889 CA PHE A 227 1985 1443 1820 150 20 248 C ATOM 1890 C PHE A 227 -1.641 -23.462 17.771 1.00 19.51 C ANISOU 1890 C PHE A 227 2713 2090 2611 149 -49 247 C ATOM 1891 O PHE A 227 -2.064 -22.699 18.641 1.00 19.54 O ANISOU 1891 O PHE A 227 2751 2067 2605 173 -91 216 O ATOM 1892 CB PHE A 227 -2.999 -25.527 18.162 1.00 11.50 C ANISOU 1892 CB PHE A 227 1726 1177 1464 162 22 207 C ATOM 1893 CG PHE A 227 -4.121 -26.426 17.696 1.00 14.02 C ANISOU 1893 CG PHE A 227 2048 1569 1709 170 83 202 C ATOM 1894 CD1 PHE A 227 -5.170 -25.916 16.952 1.00 13.31 C ANISOU 1894 CD1 PHE A 227 1958 1511 1590 183 116 209 C ATOM 1895 CD2 PHE A 227 -4.119 -27.778 18.001 1.00 12.26 C ANISOU 1895 CD2 PHE A 227 1830 1382 1446 163 108 189 C ATOM 1896 CE1 PHE A 227 -6.208 -26.746 16.519 1.00 14.19 C ANISOU 1896 CE1 PHE A 227 2071 1688 1634 189 172 204 C ATOM 1897 CE2 PHE A 227 -5.149 -28.608 17.578 1.00 14.53 C ANISOU 1897 CE2 PHE A 227 2120 1735 1668 169 163 184 C ATOM 1898 CZ PHE A 227 -6.192 -28.086 16.837 1.00 16.01 C ANISOU 1898 CZ PHE A 227 2305 1953 1826 182 195 192 C ATOM 1899 N ARG A 228 -0.370 -23.464 17.385 1.00 20.12 N ANISOU 1899 N ARG A 228 2755 2133 2755 122 -61 279 N ATOM 1900 CA ARG A 228 0.575 -22.509 17.958 1.00 20.90 C ANISOU 1900 CA ARG A 228 2857 2161 2925 119 -127 280 C ATOM 1901 C ARG A 228 0.688 -22.704 19.461 1.00 17.92 C ANISOU 1901 C ARG A 228 2522 1758 2530 134 -176 234 C ATOM 1902 O ARG A 228 0.559 -21.758 20.242 1.00 21.09 O ANISOU 1902 O ARG A 228 2951 2118 2944 153 -227 210 O ATOM 1903 CB ARG A 228 0.147 -21.075 17.629 1.00 25.45 C ANISOU 1903 CB ARG A 228 3434 2709 3526 132 -148 289 C ATOM 1904 CG ARG A 228 0.269 -20.733 16.157 1.00 33.26 C ANISOU 1904 CG ARG A 228 4377 3711 4548 115 -109 340 C ATOM 1905 CD ARG A 228 1.722 -20.488 15.760 1.00 48.78 C ANISOU 1905 CD ARG A 228 6304 5631 6601 86 -132 380 C ATOM 1906 NE ARG A 228 1.849 -20.068 14.363 1.00 61.30 N ANISOU 1906 NE ARG A 228 7845 7227 8220 72 -97 431 N ATOM 1907 CZ ARG A 228 1.787 -18.804 13.947 1.00 62.73 C ANISOU 1907 CZ ARG A 228 8015 7375 8443 76 -118 451 C ATOM 1908 NH1 ARG A 228 1.598 -17.820 14.819 1.00 64.73 N ANISOU 1908 NH1 ARG A 228 8301 7582 8710 95 -174 423 N ATOM 1909 NH2 ARG A 228 1.912 -18.521 12.656 1.00 57.33 N ANISOU 1909 NH2 ARG A 228 7289 6707 7788 62 -83 498 N ATOM 1910 N LYS A 229 0.925 -23.947 19.862 1.00 17.11 N ANISOU 1910 N LYS A 229 2423 1681 2397 125 -159 221 N ATOM 1911 CA LYS A 229 1.167 -24.287 21.251 1.00 20.15 C ANISOU 1911 CA LYS A 229 2843 2045 2768 136 -202 181 C ATOM 1912 C LYS A 229 2.247 -25.366 21.267 1.00 22.32 C ANISOU 1912 C LYS A 229 3096 2320 3065 109 -194 194 C ATOM 1913 O LYS A 229 1.987 -26.513 20.920 1.00 18.46 O ANISOU 1913 O LYS A 229 2598 1882 2534 101 -145 197 O ATOM 1914 CB LYS A 229 -0.117 -24.779 21.925 1.00 20.49 C ANISOU 1914 CB LYS A 229 2927 2135 2724 164 -184 139 C ATOM 1915 CG LYS A 229 0.053 -25.099 23.410 1.00 21.54 C ANISOU 1915 CG LYS A 229 3099 2249 2838 179 -229 95 C ATOM 1916 CD LYS A 229 -1.237 -25.594 24.052 1.00 23.14 C ANISOU 1916 CD LYS A 229 3340 2501 2953 208 -210 57 C ATOM 1917 CE LYS A 229 -1.012 -25.933 25.523 1.00 27.67 C ANISOU 1917 CE LYS A 229 3949 3055 3508 222 -254 16 C ATOM 1918 NZ LYS A 229 0.195 -26.799 25.752 1.00 24.08 N ANISOU 1918 NZ LYS A 229 3478 2584 3088 196 -262 25 N ATOM 1919 N GLU A 230 3.467 -25.001 21.651 1.00 20.77 N ANISOU 1919 N GLU A 230 2890 2066 2937 95 -242 202 N ATOM 1920 CA GLU A 230 4.595 -25.935 21.553 1.00 23.03 C ANISOU 1920 CA GLU A 230 3150 2347 3252 67 -236 221 C ATOM 1921 C GLU A 230 5.279 -26.085 22.900 1.00 28.82 C ANISOU 1921 C GLU A 230 3910 3040 4000 71 -291 189 C ATOM 1922 O GLU A 230 5.840 -25.118 23.408 1.00 25.95 O ANISOU 1922 O GLU A 230 3554 2617 3687 74 -348 185 O ATOM 1923 CB GLU A 230 5.605 -25.452 20.496 1.00 30.20 C ANISOU 1923 CB GLU A 230 4009 3227 4237 40 -234 272 C ATOM 1924 CG GLU A 230 6.444 -26.562 19.819 1.00 30.77 C ANISOU 1924 CG GLU A 230 4043 3322 4325 10 -196 303 C ATOM 1925 CD GLU A 230 7.524 -27.142 20.731 1.00 30.89 C ANISOU 1925 CD GLU A 230 4064 3306 4367 -2 -233 291 C ATOM 1926 OE1 GLU A 230 8.225 -26.363 21.408 1.00 33.35 O ANISOU 1926 OE1 GLU A 230 4385 3557 4730 -2 -292 284 O ATOM 1927 OE2 GLU A 230 7.673 -28.380 20.780 1.00 25.65 O ANISOU 1927 OE2 GLU A 230 3397 2677 3673 -12 -203 286 O ATOM 1928 N PRO A 231 5.239 -27.302 23.481 1.00 27.48 N ANISOU 1928 N PRO A 231 3754 2901 3785 70 -275 167 N ATOM 1929 CA PRO A 231 4.599 -28.478 22.877 1.00 24.36 C ANISOU 1929 CA PRO A 231 3350 2575 3332 65 -209 172 C ATOM 1930 C PRO A 231 3.102 -28.487 23.165 1.00 20.10 C ANISOU 1930 C PRO A 231 2844 2078 2714 95 -188 141 C ATOM 1931 O PRO A 231 2.646 -27.744 24.036 1.00 20.97 O ANISOU 1931 O PRO A 231 2990 2166 2812 120 -229 110 O ATOM 1932 CB PRO A 231 5.279 -29.637 23.603 1.00 19.75 C ANISOU 1932 CB PRO A 231 2770 1993 2739 54 -215 158 C ATOM 1933 CG PRO A 231 5.509 -29.097 24.980 1.00 25.62 C ANISOU 1933 CG PRO A 231 3551 2689 3492 72 -281 121 C ATOM 1934 CD PRO A 231 5.831 -27.621 24.792 1.00 34.45 C ANISOU 1934 CD PRO A 231 4663 3753 4672 74 -323 135 C ATOM 1935 N PHE A 232 2.350 -29.324 22.453 1.00 14.29 N ANISOU 1935 N PHE A 232 2099 1405 1927 93 -127 149 N ATOM 1936 CA PHE A 232 0.908 -29.368 22.613 1.00 12.68 C ANISOU 1936 CA PHE A 232 1924 1247 1649 120 -102 124 C ATOM 1937 C PHE A 232 0.501 -30.085 23.912 1.00 16.65 C ANISOU 1937 C PHE A 232 2466 1764 2096 138 -117 79 C ATOM 1938 O PHE A 232 -0.226 -29.525 24.740 1.00 16.27 O ANISOU 1938 O PHE A 232 2455 1710 2017 166 -144 47 O ATOM 1939 CB PHE A 232 0.257 -30.016 21.377 1.00 14.34 C ANISOU 1939 CB PHE A 232 2107 1517 1824 111 -31 149 C ATOM 1940 CG PHE A 232 -1.254 -29.980 21.399 1.00 10.54 C ANISOU 1940 CG PHE A 232 1651 1083 1270 137 -3 127 C ATOM 1941 CD1 PHE A 232 -1.927 -28.788 21.245 1.00 15.80 C ANISOU 1941 CD1 PHE A 232 2329 1737 1937 156 -15 125 C ATOM 1942 CD2 PHE A 232 -1.986 -31.137 21.582 1.00 15.46 C ANISOU 1942 CD2 PHE A 232 2287 1761 1826 143 36 110 C ATOM 1943 CE1 PHE A 232 -3.306 -28.746 21.277 1.00 14.01 C ANISOU 1943 CE1 PHE A 232 2126 1553 1644 181 10 105 C ATOM 1944 CE2 PHE A 232 -3.377 -31.101 21.613 1.00 21.47 C ANISOU 1944 CE2 PHE A 232 3072 2566 2521 167 61 91 C ATOM 1945 CZ PHE A 232 -4.031 -29.904 21.464 1.00 20.03 C ANISOU 1945 CZ PHE A 232 2900 2371 2338 186 48 88 C ATOM 1946 N PHE A 233 0.969 -31.318 24.096 1.00 13.15 N ANISOU 1946 N PHE A 233 2016 1340 1642 122 -100 79 N ATOM 1947 CA PHE A 233 0.723 -32.031 25.340 1.00 10.24 C ANISOU 1947 CA PHE A 233 1681 982 1226 137 -116 40 C ATOM 1948 C PHE A 233 1.920 -31.792 26.249 1.00 17.59 C ANISOU 1948 C PHE A 233 2619 1854 2210 131 -176 30 C ATOM 1949 O PHE A 233 2.962 -32.425 26.099 1.00 15.32 O ANISOU 1949 O PHE A 233 2308 1554 1959 105 -175 47 O ATOM 1950 CB PHE A 233 0.546 -33.536 25.095 1.00 8.84 C ANISOU 1950 CB PHE A 233 1494 859 1005 124 -66 43 C ATOM 1951 CG PHE A 233 -0.637 -33.896 24.209 1.00 12.81 C ANISOU 1951 CG PHE A 233 1990 1423 1454 130 -5 52 C ATOM 1952 CD1 PHE A 233 -1.951 -33.676 24.628 1.00 15.01 C ANISOU 1952 CD1 PHE A 233 2301 1732 1670 159 2 25 C ATOM 1953 CD2 PHE A 233 -0.426 -34.494 22.980 1.00 8.64 C ANISOU 1953 CD2 PHE A 233 1423 924 937 106 44 86 C ATOM 1954 CE1 PHE A 233 -3.034 -34.033 23.820 1.00 15.28 C ANISOU 1954 CE1 PHE A 233 2328 1823 1655 164 57 33 C ATOM 1955 CE2 PHE A 233 -1.495 -34.851 22.162 1.00 11.04 C ANISOU 1955 CE2 PHE A 233 1720 1285 1191 112 99 94 C ATOM 1956 CZ PHE A 233 -2.807 -34.612 22.581 1.00 14.96 C ANISOU 1956 CZ PHE A 233 2249 1810 1627 140 106 67 C ATOM 1957 N HIS A 234 1.758 -30.871 27.191 1.00 19.36 N ANISOU 1957 N HIS A 234 2876 2041 2438 154 -228 2 N ATOM 1958 CA HIS A 234 2.869 -30.352 27.983 1.00 16.77 C ANISOU 1958 CA HIS A 234 2554 1650 2168 150 -291 -6 C ATOM 1959 C HIS A 234 2.868 -30.973 29.384 1.00 19.59 C ANISOU 1959 C HIS A 234 2948 2008 2490 166 -320 -47 C ATOM 1960 O HIS A 234 2.524 -30.311 30.368 1.00 20.42 O ANISOU 1960 O HIS A 234 3088 2090 2581 194 -364 -80 O ATOM 1961 CB HIS A 234 2.719 -28.831 28.068 1.00 25.39 C ANISOU 1961 CB HIS A 234 3657 2697 3292 167 -334 -11 C ATOM 1962 CG HIS A 234 3.993 -28.100 28.362 1.00 32.21 C ANISOU 1962 CG HIS A 234 4512 3491 4237 155 -391 -2 C ATOM 1963 ND1 HIS A 234 5.040 -28.668 29.055 1.00 40.96 N ANISOU 1963 ND1 HIS A 234 5620 4572 5372 141 -420 -8 N ATOM 1964 CD2 HIS A 234 4.387 -26.841 28.053 1.00 35.70 C ANISOU 1964 CD2 HIS A 234 4943 3882 4738 153 -426 14 C ATOM 1965 CE1 HIS A 234 6.021 -27.789 29.167 1.00 38.12 C ANISOU 1965 CE1 HIS A 234 5250 4149 5084 132 -470 2 C ATOM 1966 NE2 HIS A 234 5.649 -26.672 28.568 1.00 36.86 N ANISOU 1966 NE2 HIS A 234 5084 3974 4947 139 -475 16 N ATOM 1967 N GLY A 235 3.249 -32.246 29.476 1.00 16.45 N ANISOU 1967 N GLY A 235 2540 1635 2076 150 -295 -44 N ATOM 1968 CA GLY A 235 3.246 -32.942 30.750 1.00 14.75 C ANISOU 1968 CA GLY A 235 2356 1425 1825 163 -317 -80 C ATOM 1969 C GLY A 235 4.442 -32.601 31.621 1.00 16.45 C ANISOU 1969 C GLY A 235 2577 1578 2095 158 -379 -90 C ATOM 1970 O GLY A 235 5.509 -32.280 31.110 1.00 16.97 O ANISOU 1970 O GLY A 235 2613 1604 2229 134 -394 -62 O ATOM 1971 N HIS A 236 4.270 -32.701 32.934 1.00 15.67 N ANISOU 1971 N HIS A 236 2516 1473 1966 181 -416 -130 N ATOM 1972 CA HIS A 236 5.350 -32.390 33.873 1.00 22.36 C ANISOU 1972 CA HIS A 236 3373 2263 2861 180 -478 -144 C ATOM 1973 C HIS A 236 6.243 -33.596 34.155 1.00 22.53 C ANISOU 1973 C HIS A 236 3381 2287 2890 157 -471 -139 C ATOM 1974 O HIS A 236 7.393 -33.449 34.608 1.00 22.88 O ANISOU 1974 O HIS A 236 3421 2283 2989 145 -514 -139 O ATOM 1975 CB HIS A 236 4.771 -31.824 35.169 1.00 29.40 C ANISOU 1975 CB HIS A 236 4311 3141 3718 218 -524 -189 C ATOM 1976 CG HIS A 236 4.039 -30.531 34.974 1.00 51.58 C ANISOU 1976 CG HIS A 236 7134 5937 6528 241 -541 -195 C ATOM 1977 ND1 HIS A 236 4.618 -29.435 34.370 1.00 62.08 N ANISOU 1977 ND1 HIS A 236 8444 7217 7925 230 -566 -173 N ATOM 1978 CD2 HIS A 236 2.774 -30.162 35.291 1.00 55.16 C ANISOU 1978 CD2 HIS A 236 7617 6419 6922 275 -535 -220 C ATOM 1979 CE1 HIS A 236 3.744 -28.444 34.328 1.00 61.33 C ANISOU 1979 CE1 HIS A 236 8368 7122 7814 255 -576 -185 C ATOM 1980 NE2 HIS A 236 2.618 -28.859 34.881 1.00 58.45 N ANISOU 1980 NE2 HIS A 236 8033 6804 7372 283 -557 -214 N ATOM 1981 N ASP A 237 5.694 -34.782 33.894 1.00 17.22 N ANISOU 1981 N ASP A 237 2705 1674 2165 152 -418 -137 N ATOM 1982 CA ASP A 237 6.420 -36.047 33.944 1.00 20.94 C ANISOU 1982 CA ASP A 237 3159 2158 2639 128 -399 -128 C ATOM 1983 C ASP A 237 5.661 -37.052 33.071 1.00 16.97 C ANISOU 1983 C ASP A 237 2640 1721 2088 119 -329 -111 C ATOM 1984 O ASP A 237 4.667 -36.691 32.458 1.00 19.66 O ANISOU 1984 O ASP A 237 2980 2090 2397 130 -299 -106 O ATOM 1985 CB ASP A 237 6.572 -36.560 35.387 1.00 22.73 C ANISOU 1985 CB ASP A 237 3418 2379 2839 144 -434 -165 C ATOM 1986 CG ASP A 237 5.234 -36.767 36.090 1.00 28.60 C ANISOU 1986 CG ASP A 237 4199 3167 3502 178 -423 -198 C ATOM 1987 OD1 ASP A 237 4.278 -37.248 35.447 1.00 22.27 O ANISOU 1987 OD1 ASP A 237 3391 2418 2652 180 -370 -189 O ATOM 1988 OD2 ASP A 237 5.143 -36.458 37.298 1.00 28.84 O ANISOU 1988 OD2 ASP A 237 4264 3179 3516 204 -468 -232 O ATOM 1989 N ASN A 238 6.113 -38.303 33.021 1.00 13.50 N ANISOU 1989 N ASN A 238 2185 1304 1640 99 -303 -103 N ATOM 1990 CA ASN A 238 5.502 -39.277 32.106 1.00 16.39 C ANISOU 1990 CA ASN A 238 2532 1730 1968 87 -237 -85 C ATOM 1991 C ASN A 238 4.082 -39.683 32.496 1.00 14.78 C ANISOU 1991 C ASN A 238 2356 1578 1681 113 -211 -110 C ATOM 1992 O ASN A 238 3.308 -40.145 31.651 1.00 16.78 O ANISOU 1992 O ASN A 238 2596 1880 1899 110 -158 -96 O ATOM 1993 CB ASN A 238 6.392 -40.515 31.925 1.00 20.71 C ANISOU 1993 CB ASN A 238 3055 2285 2530 59 -217 -69 C ATOM 1994 CG ASN A 238 7.712 -40.188 31.236 1.00 18.83 C ANISOU 1994 CG ASN A 238 2781 2004 2370 30 -230 -36 C ATOM 1995 OD1 ASN A 238 7.833 -39.172 30.551 1.00 20.39 O ANISOU 1995 OD1 ASN A 238 2963 2177 2606 27 -237 -17 O ATOM 1996 ND2 ASN A 238 8.710 -41.050 31.420 1.00 21.74 N ANISOU 1996 ND2 ASN A 238 3135 2363 2763 9 -234 -29 N ATOM 1997 N TYR A 239 3.742 -39.518 33.770 1.00 17.18 N ANISOU 1997 N TYR A 239 2698 1875 1955 140 -247 -146 N ATOM 1998 CA TYR A 239 2.401 -39.842 34.241 1.00 16.32 C ANISOU 1998 CA TYR A 239 2618 1815 1768 167 -227 -171 C ATOM 1999 C TYR A 239 1.461 -38.710 33.863 1.00 15.05 C ANISOU 1999 C TYR A 239 2468 1657 1593 189 -225 -173 C ATOM 2000 O TYR A 239 0.414 -38.932 33.245 1.00 14.74 O ANISOU 2000 O TYR A 239 2426 1666 1509 195 -180 -167 O ATOM 2001 CB TYR A 239 2.409 -40.089 35.747 1.00 15.78 C ANISOU 2001 CB TYR A 239 2585 1739 1672 189 -266 -207 C ATOM 2002 CG TYR A 239 3.456 -41.106 36.118 1.00 27.93 C ANISOU 2002 CG TYR A 239 4112 3267 3232 167 -273 -204 C ATOM 2003 CD1 TYR A 239 3.340 -42.421 35.703 1.00 29.10 C ANISOU 2003 CD1 TYR A 239 4244 3460 3354 149 -225 -191 C ATOM 2004 CD2 TYR A 239 4.581 -40.744 36.839 1.00 31.18 C ANISOU 2004 CD2 TYR A 239 4529 3624 3694 163 -326 -213 C ATOM 2005 CE1 TYR A 239 4.306 -43.359 36.015 1.00 32.55 C ANISOU 2005 CE1 TYR A 239 4669 3888 3811 128 -230 -187 C ATOM 2006 CE2 TYR A 239 5.554 -41.674 37.155 1.00 36.96 C ANISOU 2006 CE2 TYR A 239 5250 4348 4447 142 -331 -208 C ATOM 2007 CZ TYR A 239 5.408 -42.983 36.740 1.00 36.84 C ANISOU 2007 CZ TYR A 239 5218 4378 4403 125 -282 -196 C ATOM 2008 OH TYR A 239 6.367 -43.924 37.048 1.00 35.98 O ANISOU 2008 OH TYR A 239 5097 4259 4313 104 -287 -192 O ATOM 2009 N ASP A 240 1.868 -37.489 34.192 1.00 14.82 N ANISOU 2009 N ASP A 240 2448 1576 1606 199 -275 -180 N ATOM 2010 CA ASP A 240 1.081 -36.325 33.845 1.00 12.58 C ANISOU 2010 CA ASP A 240 2174 1289 1316 219 -279 -182 C ATOM 2011 C ASP A 240 0.957 -36.226 32.324 1.00 12.39 C ANISOU 2011 C ASP A 240 2114 1282 1312 197 -232 -144 C ATOM 2012 O ASP A 240 -0.039 -35.736 31.814 1.00 16.24 O ANISOU 2012 O ASP A 240 2606 1795 1770 211 -209 -142 O ATOM 2013 CB ASP A 240 1.707 -35.058 34.429 1.00 16.75 C ANISOU 2013 CB ASP A 240 2717 1753 1896 230 -345 -195 C ATOM 2014 CG ASP A 240 0.847 -33.831 34.232 1.00 19.21 C ANISOU 2014 CG ASP A 240 3043 2058 2197 255 -355 -201 C ATOM 2015 OD1 ASP A 240 -0.329 -33.830 34.655 1.00 19.42 O ANISOU 2015 OD1 ASP A 240 3097 2122 2160 284 -343 -225 O ATOM 2016 OD2 ASP A 240 1.344 -32.856 33.644 1.00 20.11 O ANISOU 2016 OD2 ASP A 240 3141 2132 2369 245 -373 -183 O ATOM 2017 N GLN A 241 1.957 -36.710 31.602 1.00 8.86 N ANISOU 2017 N GLN A 241 1631 824 912 164 -217 -114 N ATOM 2018 CA GLN A 241 1.888 -36.689 30.144 1.00 11.71 C ANISOU 2018 CA GLN A 241 1956 1204 1291 144 -171 -76 C ATOM 2019 C GLN A 241 0.636 -37.455 29.689 1.00 15.44 C ANISOU 2019 C GLN A 241 2430 1745 1692 151 -112 -77 C ATOM 2020 O GLN A 241 -0.116 -36.980 28.842 1.00 16.94 O ANISOU 2020 O GLN A 241 2611 1956 1869 156 -83 -64 O ATOM 2021 CB GLN A 241 3.156 -37.281 29.527 1.00 11.55 C ANISOU 2021 CB GLN A 241 1897 1166 1325 108 -161 -45 C ATOM 2022 CG GLN A 241 3.224 -37.165 27.999 1.00 10.08 C ANISOU 2022 CG GLN A 241 1670 995 1164 87 -118 -4 C ATOM 2023 CD GLN A 241 3.294 -35.719 27.517 1.00 15.13 C ANISOU 2023 CD GLN A 241 2302 1596 1848 91 -141 10 C ATOM 2024 OE1 GLN A 241 3.742 -34.843 28.238 1.00 14.33 O ANISOU 2024 OE1 GLN A 241 2218 1445 1781 101 -195 -4 O ATOM 2025 NE2 GLN A 241 2.866 -35.477 26.283 1.00 15.43 N ANISOU 2025 NE2 GLN A 241 2315 1659 1888 85 -100 38 N ATOM 2026 N LEU A 242 0.400 -38.633 30.263 1.00 10.57 N ANISOU 2026 N LEU A 242 1825 1162 1030 153 -96 -93 N ATOM 2027 CA LEU A 242 -0.772 -39.412 29.856 1.00 11.92 C ANISOU 2027 CA LEU A 242 1998 1398 1135 159 -42 -94 C ATOM 2028 C LEU A 242 -2.058 -38.715 30.280 1.00 14.50 C ANISOU 2028 C LEU A 242 2356 1743 1409 194 -46 -118 C ATOM 2029 O LEU A 242 -3.060 -38.769 29.557 1.00 13.00 O ANISOU 2029 O LEU A 242 2162 1596 1182 199 -3 -110 O ATOM 2030 CB LEU A 242 -0.719 -40.847 30.377 1.00 13.43 C ANISOU 2030 CB LEU A 242 2193 1621 1291 152 -24 -104 C ATOM 2031 CG LEU A 242 -1.835 -41.758 29.846 1.00 9.80 C ANISOU 2031 CG LEU A 242 1728 1227 768 154 35 -100 C ATOM 2032 CD1 LEU A 242 -1.836 -41.826 28.313 1.00 11.99 C ANISOU 2032 CD1 LEU A 242 1968 1524 1065 133 81 -65 C ATOM 2033 CD2 LEU A 242 -1.733 -43.158 30.455 1.00 12.60 C ANISOU 2033 CD2 LEU A 242 2088 1608 1091 147 47 -111 C ATOM 2034 N VAL A 243 -2.046 -38.061 31.443 1.00 12.11 N ANISOU 2034 N VAL A 243 2087 1410 1105 217 -98 -147 N ATOM 2035 CA VAL A 243 -3.229 -37.316 31.884 1.00 11.31 C ANISOU 2035 CA VAL A 243 2017 1323 957 252 -106 -171 C ATOM 2036 C VAL A 243 -3.546 -36.177 30.914 1.00 14.80 C ANISOU 2036 C VAL A 243 2447 1754 1423 254 -99 -153 C ATOM 2037 O VAL A 243 -4.704 -35.967 30.553 1.00 15.92 O ANISOU 2037 O VAL A 243 2597 1933 1520 270 -70 -155 O ATOM 2038 CB VAL A 243 -3.102 -36.776 33.329 1.00 11.56 C ANISOU 2038 CB VAL A 243 2086 1321 984 279 -167 -207 C ATOM 2039 CG1 VAL A 243 -4.403 -36.048 33.741 1.00 12.86 C ANISOU 2039 CG1 VAL A 243 2284 1507 1095 317 -172 -231 C ATOM 2040 CG2 VAL A 243 -2.769 -37.915 34.315 1.00 16.59 C ANISOU 2040 CG2 VAL A 243 2736 1970 1597 278 -174 -225 C ATOM 2041 N ARG A 244 -2.517 -35.458 30.476 1.00 13.14 N ANISOU 2041 N ARG A 244 2215 1493 1285 236 -124 -133 N ATOM 2042 CA ARG A 244 -2.696 -34.367 29.511 1.00 15.63 C ANISOU 2042 CA ARG A 244 2516 1794 1631 235 -119 -112 C ATOM 2043 C ARG A 244 -3.362 -34.881 28.252 1.00 15.75 C ANISOU 2043 C ARG A 244 2504 1860 1620 223 -53 -85 C ATOM 2044 O ARG A 244 -4.261 -34.246 27.707 1.00 12.85 O ANISOU 2044 O ARG A 244 2139 1512 1232 236 -34 -82 O ATOM 2045 CB ARG A 244 -1.350 -33.747 29.119 1.00 14.77 C ANISOU 2045 CB ARG A 244 2380 1626 1607 212 -150 -88 C ATOM 2046 CG ARG A 244 -0.552 -33.194 30.276 1.00 22.38 C ANISOU 2046 CG ARG A 244 3366 2533 2606 221 -217 -111 C ATOM 2047 CD ARG A 244 -1.248 -32.014 30.900 1.00 25.82 C ANISOU 2047 CD ARG A 244 3835 2950 3027 255 -255 -137 C ATOM 2048 NE ARG A 244 -0.450 -31.397 31.960 1.00 28.99 N ANISOU 2048 NE ARG A 244 4256 3292 3467 264 -323 -159 N ATOM 2049 CZ ARG A 244 -0.382 -30.084 32.165 1.00 36.40 C ANISOU 2049 CZ ARG A 244 5207 4186 4439 279 -368 -167 C ATOM 2050 NH1 ARG A 244 -1.042 -29.255 31.362 1.00 37.52 N ANISOU 2050 NH1 ARG A 244 5342 4334 4582 286 -351 -153 N ATOM 2051 NH2 ARG A 244 0.350 -29.596 33.158 1.00 34.32 N ANISOU 2051 NH2 ARG A 244 4961 3869 4208 288 -430 -188 N ATOM 2052 N ILE A 245 -2.894 -36.026 27.778 1.00 11.77 N ANISOU 2052 N ILE A 245 1975 1379 1119 197 -19 -67 N ATOM 2053 CA ILE A 245 -3.462 -36.637 26.580 1.00 12.87 C ANISOU 2053 CA ILE A 245 2088 1569 1234 184 44 -43 C ATOM 2054 C ILE A 245 -4.917 -37.034 26.838 1.00 14.62 C ANISOU 2054 C ILE A 245 2335 1846 1375 208 74 -64 C ATOM 2055 O ILE A 245 -5.809 -36.724 26.046 1.00 13.51 O ANISOU 2055 O ILE A 245 2188 1735 1210 215 108 -53 O ATOM 2056 CB ILE A 245 -2.660 -37.873 26.148 1.00 11.09 C ANISOU 2056 CB ILE A 245 1833 1356 1024 154 71 -23 C ATOM 2057 CG1 ILE A 245 -1.258 -37.443 25.660 1.00 11.82 C ANISOU 2057 CG1 ILE A 245 1895 1398 1198 128 48 4 C ATOM 2058 CG2 ILE A 245 -3.423 -38.636 25.069 1.00 11.12 C ANISOU 2058 CG2 ILE A 245 1816 1419 990 146 136 -5 C ATOM 2059 CD1 ILE A 245 -0.274 -38.585 25.437 1.00 12.57 C ANISOU 2059 CD1 ILE A 245 1964 1497 1316 100 63 20 C ATOM 2060 N ALA A 246 -5.154 -37.697 27.963 1.00 12.06 N ANISOU 2060 N ALA A 246 2038 1534 1010 222 60 -92 N ATOM 2061 CA ALA A 246 -6.508 -38.149 28.310 1.00 15.56 C ANISOU 2061 CA ALA A 246 2504 2031 1376 245 87 -112 C ATOM 2062 C ALA A 246 -7.532 -37.007 28.470 1.00 15.93 C ANISOU 2062 C ALA A 246 2577 2081 1396 276 75 -127 C ATOM 2063 O ALA A 246 -8.740 -37.196 28.245 1.00 13.93 O ANISOU 2063 O ALA A 246 2333 1876 1086 291 110 -132 O ATOM 2064 CB ALA A 246 -6.471 -39.007 29.552 1.00 11.17 C ANISOU 2064 CB ALA A 246 1973 1484 786 254 69 -139 C ATOM 2065 N LYS A 247 -7.062 -35.827 28.849 1.00 11.66 N ANISOU 2065 N LYS A 247 2046 1487 896 286 26 -135 N ATOM 2066 CA LYS A 247 -7.934 -34.645 28.914 1.00 12.20 C ANISOU 2066 CA LYS A 247 2136 1552 947 314 12 -147 C ATOM 2067 C LYS A 247 -8.454 -34.169 27.543 1.00 16.76 C ANISOU 2067 C LYS A 247 2689 2148 1531 307 53 -119 C ATOM 2068 O LYS A 247 -9.404 -33.388 27.463 1.00 17.83 O ANISOU 2068 O LYS A 247 2841 2296 1639 330 55 -127 O ATOM 2069 CB LYS A 247 -7.256 -33.496 29.671 1.00 17.22 C ANISOU 2069 CB LYS A 247 2790 2125 1630 327 -54 -163 C ATOM 2070 CG LYS A 247 -7.139 -33.748 31.176 1.00 16.66 C ANISOU 2070 CG LYS A 247 2754 2042 1535 347 -96 -199 C ATOM 2071 CD LYS A 247 -6.543 -32.566 31.918 1.00 21.58 C ANISOU 2071 CD LYS A 247 3396 2603 2202 362 -163 -216 C ATOM 2072 CE LYS A 247 -6.719 -32.738 33.424 1.00 30.61 C ANISOU 2072 CE LYS A 247 4579 3744 3309 390 -201 -256 C ATOM 2073 NZ LYS A 247 -5.992 -31.700 34.203 1.00 36.89 N ANISOU 2073 NZ LYS A 247 5391 4476 4150 403 -269 -274 N ATOM 2074 N VAL A 248 -7.840 -34.656 26.475 1.00 12.09 N ANISOU 2074 N VAL A 248 1686 1563 1344 75 -38 181 N ATOM 2075 CA VAL A 248 -8.200 -34.271 25.123 1.00 12.93 C ANISOU 2075 CA VAL A 248 1765 1704 1445 66 -29 193 C ATOM 2076 C VAL A 248 -8.879 -35.426 24.401 1.00 14.51 C ANISOU 2076 C VAL A 248 1945 1939 1630 32 -27 192 C ATOM 2077 O VAL A 248 -9.956 -35.253 23.824 1.00 15.30 O ANISOU 2077 O VAL A 248 2019 2086 1709 28 -18 211 O ATOM 2078 CB VAL A 248 -6.965 -33.818 24.318 1.00 14.10 C ANISOU 2078 CB VAL A 248 1914 1829 1616 65 -34 179 C ATOM 2079 CG1 VAL A 248 -7.336 -33.536 22.865 1.00 11.84 C ANISOU 2079 CG1 VAL A 248 1599 1583 1319 57 -23 192 C ATOM 2080 CG2 VAL A 248 -6.328 -32.579 24.956 1.00 13.22 C ANISOU 2080 CG2 VAL A 248 1819 1683 1523 96 -34 177 C ATOM 2081 N LEU A 249 -8.252 -36.598 24.427 1.00 10.40 N ANISOU 2081 N LEU A 249 1435 1397 1120 7 -35 169 N ATOM 2082 CA LEU A 249 -8.800 -37.773 23.752 1.00 11.45 C ANISOU 2082 CA LEU A 249 1551 1557 1243 -29 -33 162 C ATOM 2083 C LEU A 249 -9.828 -38.490 24.616 1.00 13.95 C ANISOU 2083 C LEU A 249 1869 1883 1547 -37 -26 171 C ATOM 2084 O LEU A 249 -10.607 -39.311 24.124 1.00 11.89 O ANISOU 2084 O LEU A 249 1589 1652 1277 -67 -21 169 O ATOM 2085 CB LEU A 249 -7.681 -38.755 23.370 1.00 14.12 C ANISOU 2085 CB LEU A 249 1901 1864 1600 -52 -40 133 C ATOM 2086 CG LEU A 249 -6.827 -38.430 22.142 1.00 15.35 C ANISOU 2086 CG LEU A 249 2047 2021 1764 -56 -43 121 C ATOM 2087 CD1 LEU A 249 -6.036 -37.140 22.301 1.00 16.15 C ANISOU 2087 CD1 LEU A 249 2156 2100 1879 -25 -45 128 C ATOM 2088 CD2 LEU A 249 -5.871 -39.576 21.829 1.00 16.02 C ANISOU 2088 CD2 LEU A 249 2143 2078 1866 -80 -47 93 C ATOM 2089 N GLY A 250 -9.820 -38.185 25.903 1.00 11.25 N ANISOU 2089 N GLY A 250 1549 1518 1208 -11 -27 180 N ATOM 2090 CA GLY A 250 -10.807 -38.741 26.815 1.00 12.99 C ANISOU 2090 CA GLY A 250 1771 1747 1417 -13 -18 194 C ATOM 2091 C GLY A 250 -10.363 -40.033 27.466 1.00 15.00 C ANISOU 2091 C GLY A 250 2047 1968 1684 -29 -18 180 C ATOM 2092 O GLY A 250 -9.541 -40.782 26.919 1.00 14.67 O ANISOU 2092 O GLY A 250 2011 1906 1658 -50 -23 158 O ATOM 2093 N THR A 251 -10.913 -40.307 28.643 1.00 14.90 N ANISOU 2093 N THR A 251 2048 1949 1664 -16 -11 194 N ATOM 2094 CA THR A 251 -10.521 -41.503 29.371 1.00 13.15 C ANISOU 2094 CA THR A 251 1848 1695 1454 -25 -8 187 C ATOM 2095 C THR A 251 -11.213 -42.780 28.884 1.00 8.74 C ANISOU 2095 C THR A 251 1274 1147 899 -67 6 184 C ATOM 2096 O THR A 251 -10.643 -43.864 28.999 1.00 14.97 O ANISOU 2096 O THR A 251 2078 1904 1704 -84 9 170 O ATOM 2097 CB THR A 251 -10.739 -41.352 30.888 1.00 14.93 C ANISOU 2097 CB THR A 251 2097 1907 1670 9 -4 204 C ATOM 2098 OG1 THR A 251 -12.054 -40.846 31.128 1.00 12.69 O ANISOU 2098 OG1 THR A 251 1796 1660 1367 17 9 229 O ATOM 2099 CG2 THR A 251 -9.721 -40.383 31.483 1.00 16.79 C ANISOU 2099 CG2 THR A 251 2355 2118 1908 47 -20 196 C ATOM 2100 N GLU A 252 -12.441 -42.687 28.371 1.00 12.44 N ANISOU 2100 N GLU A 252 1712 1661 1354 -86 16 196 N ATOM 2101 CA GLU A 252 -13.116 -43.925 27.956 1.00 12.07 C ANISOU 2101 CA GLU A 252 1649 1624 1313 -130 29 189 C ATOM 2102 C GLU A 252 -12.375 -44.625 26.814 1.00 14.45 C ANISOU 2102 C GLU A 252 1946 1914 1629 -163 23 157 C ATOM 2103 O GLU A 252 -12.242 -45.855 26.799 1.00 15.38 O ANISOU 2103 O GLU A 252 2072 2007 1764 -192 33 142 O ATOM 2104 CB GLU A 252 -14.589 -43.683 27.611 1.00 16.76 C ANISOU 2104 CB GLU A 252 2206 2273 1889 -144 39 206 C ATOM 2105 CG GLU A 252 -15.444 -43.419 28.844 1.00 24.41 C ANISOU 2105 CG GLU A 252 3179 3248 2847 -119 52 237 C ATOM 2106 CD GLU A 252 -15.562 -44.640 29.737 1.00 37.97 C ANISOU 2106 CD GLU A 252 4915 4934 4579 -132 69 241 C ATOM 2107 OE1 GLU A 252 -16.125 -45.661 29.284 1.00 46.30 O ANISOU 2107 OE1 GLU A 252 5951 5996 5644 -175 81 232 O ATOM 2108 OE2 GLU A 252 -15.084 -44.585 30.890 1.00 37.25 O ANISOU 2108 OE2 GLU A 252 4855 4809 4488 -99 70 252 O ATOM 2109 N ASP A 253 -11.865 -43.848 25.867 1.00 12.71 N ANISOU 2109 N ASP A 253 1716 1709 1404 -158 10 147 N ATOM 2110 CA ASP A 253 -11.094 -44.438 24.779 1.00 14.01 C ANISOU 2110 CA ASP A 253 1878 1863 1580 -185 4 117 C ATOM 2111 C ASP A 253 -9.712 -44.927 25.211 1.00 13.90 C ANISOU 2111 C ASP A 253 1898 1792 1589 -174 0 102 C ATOM 2112 O ASP A 253 -9.160 -45.855 24.610 1.00 15.55 O ANISOU 2112 O ASP A 253 2112 1982 1813 -201 2 77 O ATOM 2113 CB ASP A 253 -11.026 -43.498 23.582 1.00 12.33 C ANISOU 2113 CB ASP A 253 1642 1689 1355 -182 -6 114 C ATOM 2114 CG ASP A 253 -12.383 -43.335 22.908 1.00 17.70 C ANISOU 2114 CG ASP A 253 2283 2431 2011 -201 -1 123 C ATOM 2115 OD1 ASP A 253 -13.127 -44.333 22.818 1.00 21.86 O ANISOU 2115 OD1 ASP A 253 2796 2970 2538 -237 8 114 O ATOM 2116 OD2 ASP A 253 -12.707 -42.208 22.503 1.00 18.37 O ANISOU 2116 OD2 ASP A 253 2350 2553 2078 -180 -5 140 O ATOM 2117 N LEU A 254 -9.172 -44.327 26.266 1.00 14.24 N ANISOU 2117 N LEU A 254 1965 1810 1635 -135 -7 115 N ATOM 2118 CA LEU A 254 -7.936 -44.831 26.858 1.00 17.65 C ANISOU 2118 CA LEU A 254 2428 2193 2086 -122 -11 104 C ATOM 2119 C LEU A 254 -8.210 -46.203 27.447 1.00 17.43 C ANISOU 2119 C LEU A 254 2413 2140 2069 -140 5 105 C ATOM 2120 O LEU A 254 -7.431 -47.139 27.248 1.00 17.70 O ANISOU 2120 O LEU A 254 2462 2141 2122 -153 9 87 O ATOM 2121 CB LEU A 254 -7.403 -43.889 27.936 1.00 13.92 C ANISOU 2121 CB LEU A 254 1975 1704 1610 -77 -23 117 C ATOM 2122 CG LEU A 254 -6.195 -44.374 28.745 1.00 16.16 C ANISOU 2122 CG LEU A 254 2289 1943 1910 -57 -30 109 C ATOM 2123 CD1 LEU A 254 -5.041 -44.737 27.821 1.00 17.48 C ANISOU 2123 CD1 LEU A 254 2456 2090 2096 -71 -37 83 C ATOM 2124 CD2 LEU A 254 -5.801 -43.286 29.707 1.00 15.23 C ANISOU 2124 CD2 LEU A 254 2183 1818 1784 -15 -44 117 C ATOM 2125 N TYR A 255 -9.322 -46.337 28.165 1.00 15.47 N ANISOU 2125 N TYR A 255 2161 1907 1810 -140 18 126 N ATOM 2126 CA TYR A 255 -9.672 -47.645 28.704 1.00 14.01 C ANISOU 2126 CA TYR A 255 1988 1699 1639 -159 39 130 C ATOM 2127 C TYR A 255 -9.949 -48.666 27.596 1.00 15.80 C ANISOU 2127 C TYR A 255 2198 1928 1878 -210 51 106 C ATOM 2128 O TYR A 255 -9.550 -49.825 27.714 1.00 17.25 O ANISOU 2128 O TYR A 255 2398 2073 2083 -226 65 96 O ATOM 2129 CB TYR A 255 -10.823 -47.563 29.713 1.00 11.64 C ANISOU 2129 CB TYR A 255 1684 1414 1324 -148 53 160 C ATOM 2130 CG TYR A 255 -10.342 -47.244 31.116 1.00 14.69 C ANISOU 2130 CG TYR A 255 2101 1777 1705 -100 50 180 C ATOM 2131 CD1 TYR A 255 -9.822 -48.239 31.925 1.00 19.00 C ANISOU 2131 CD1 TYR A 255 2674 2282 2264 -92 62 185 C ATOM 2132 CD2 TYR A 255 -10.398 -45.949 31.629 1.00 21.03 C ANISOU 2132 CD2 TYR A 255 2905 2599 2488 -62 36 193 C ATOM 2133 CE1 TYR A 255 -9.373 -47.966 33.202 1.00 21.87 C ANISOU 2133 CE1 TYR A 255 3064 2630 2618 -46 57 202 C ATOM 2134 CE2 TYR A 255 -9.951 -45.669 32.916 1.00 19.68 C ANISOU 2134 CE2 TYR A 255 2761 2409 2308 -20 32 206 C ATOM 2135 CZ TYR A 255 -9.441 -46.687 33.694 1.00 23.45 C ANISOU 2135 CZ TYR A 255 3263 2851 2796 -11 41 210 C ATOM 2136 OH TYR A 255 -8.991 -46.440 34.979 1.00 28.51 O ANISOU 2136 OH TYR A 255 3930 3478 3423 33 35 223 O ATOM 2137 N ASP A 256 -10.613 -48.245 26.519 1.00 14.06 N ANISOU 2137 N ASP A 256 1944 1752 1645 -234 46 97 N ATOM 2138 CA ASP A 256 -10.837 -49.147 25.387 1.00 12.60 C ANISOU 2138 CA ASP A 256 1743 1576 1470 -283 54 68 C ATOM 2139 C ASP A 256 -9.503 -49.667 24.829 1.00 15.19 C ANISOU 2139 C ASP A 256 2090 1866 1816 -287 49 41 C ATOM 2140 O ASP A 256 -9.389 -50.829 24.451 1.00 16.15 O ANISOU 2140 O ASP A 256 2217 1964 1957 -320 63 19 O ATOM 2141 CB ASP A 256 -11.585 -48.454 24.254 1.00 15.74 C ANISOU 2141 CB ASP A 256 2101 2034 1845 -301 44 62 C ATOM 2142 CG ASP A 256 -13.069 -48.238 24.549 1.00 19.83 C ANISOU 2142 CG ASP A 256 2592 2596 2348 -310 52 83 C ATOM 2143 OD1 ASP A 256 -13.626 -48.836 25.501 1.00 17.04 O ANISOU 2143 OD1 ASP A 256 2247 2225 2004 -314 69 99 O ATOM 2144 OD2 ASP A 256 -13.683 -47.461 23.788 1.00 24.75 O ANISOU 2144 OD2 ASP A 256 3183 3273 2948 -313 42 86 O ATOM 2145 N TYR A 257 -8.517 -48.774 24.752 1.00 15.49 N ANISOU 2145 N TYR A 257 2138 1898 1850 -254 31 42 N ATOM 2146 CA TYR A 257 -7.181 -49.080 24.248 1.00 16.94 C ANISOU 2146 CA TYR A 257 2337 2049 2050 -251 25 19 C ATOM 2147 C TYR A 257 -6.490 -50.118 25.116 1.00 16.68 C ANISOU 2147 C TYR A 257 2336 1960 2040 -243 37 20 C ATOM 2148 O TYR A 257 -6.088 -51.176 24.634 1.00 17.14 O ANISOU 2148 O TYR A 257 2403 1992 2117 -268 49 -2 O ATOM 2149 CB TYR A 257 -6.340 -47.803 24.199 1.00 15.96 C ANISOU 2149 CB TYR A 257 2215 1931 1919 -214 4 25 C ATOM 2150 CG TYR A 257 -4.899 -47.994 23.768 1.00 19.32 C ANISOU 2150 CG TYR A 257 2654 2323 2361 -207 -3 6 C ATOM 2151 CD1 TYR A 257 -4.584 -48.768 22.650 1.00 15.97 C ANISOU 2151 CD1 TYR A 257 2225 1896 1945 -238 4 -22 C ATOM 2152 CD2 TYR A 257 -3.855 -47.373 24.451 1.00 16.61 C ANISOU 2152 CD2 TYR A 257 2329 1957 2026 -168 -16 13 C ATOM 2153 CE1 TYR A 257 -3.263 -48.936 22.234 1.00 17.06 C ANISOU 2153 CE1 TYR A 257 2376 2007 2100 -229 -1 -39 C ATOM 2154 CE2 TYR A 257 -2.520 -47.542 24.039 1.00 19.24 C ANISOU 2154 CE2 TYR A 257 2672 2263 2377 -161 -22 -4 C ATOM 2155 CZ TYR A 257 -2.245 -48.326 22.923 1.00 20.90 C ANISOU 2155 CZ TYR A 257 2877 2470 2595 -191 -13 -29 C ATOM 2156 OH TYR A 257 -0.956 -48.510 22.463 1.00 17.11 O ANISOU 2156 OH TYR A 257 2405 1965 2132 -184 -17 -45 O ATOM 2157 N ILE A 258 -6.349 -49.829 26.403 1.00 14.21 N ANISOU 2157 N ILE A 258 2042 1631 1726 -207 35 45 N ATOM 2158 CA ILE A 258 -5.643 -50.769 27.263 1.00 10.14 C ANISOU 2158 CA ILE A 258 1557 1066 1229 -193 46 49 C ATOM 2159 C ILE A 258 -6.434 -52.077 27.368 1.00 18.57 C ANISOU 2159 C ILE A 258 2627 2117 2311 -227 75 49 C ATOM 2160 O ILE A 258 -5.855 -53.152 27.504 1.00 17.83 O ANISOU 2160 O ILE A 258 2554 1980 2239 -232 91 43 O ATOM 2161 CB ILE A 258 -5.315 -50.188 28.660 1.00 17.19 C ANISOU 2161 CB ILE A 258 2469 1949 2113 -144 37 76 C ATOM 2162 CG1 ILE A 258 -6.582 -49.899 29.460 1.00 18.49 C ANISOU 2162 CG1 ILE A 258 2627 2137 2260 -139 45 103 C ATOM 2163 CG2 ILE A 258 -4.441 -48.930 28.538 1.00 16.83 C ANISOU 2163 CG2 ILE A 258 2421 1914 2060 -114 9 71 C ATOM 2164 CD1 ILE A 258 -6.303 -49.615 30.911 1.00 21.81 C ANISOU 2164 CD1 ILE A 258 3071 2544 2671 -93 41 127 C ATOM 2165 N ASP A 259 -7.759 -51.985 27.293 1.00 14.49 N ANISOU 2165 N ASP A 259 2089 1634 1784 -250 84 58 N ATOM 2166 CA ASP A 259 -8.585 -53.190 27.362 1.00 10.77 C ANISOU 2166 CA ASP A 259 1616 1148 1329 -287 113 56 C ATOM 2167 C ASP A 259 -8.388 -54.069 26.135 1.00 15.75 C ANISOU 2167 C ASP A 259 2240 1767 1977 -333 122 18 C ATOM 2168 O ASP A 259 -8.349 -55.295 26.241 1.00 16.39 O ANISOU 2168 O ASP A 259 2336 1809 2084 -355 148 10 O ATOM 2169 CB ASP A 259 -10.071 -52.841 27.510 1.00 13.74 C ANISOU 2169 CB ASP A 259 1965 1567 1688 -304 119 72 C ATOM 2170 CG ASP A 259 -10.432 -52.398 28.912 1.00 17.44 C ANISOU 2170 CG ASP A 259 2446 2036 2146 -264 123 111 C ATOM 2171 OD1 ASP A 259 -9.578 -52.489 29.819 1.00 17.27 O ANISOU 2171 OD1 ASP A 259 2455 1979 2128 -227 122 125 O ATOM 2172 OD2 ASP A 259 -11.594 -51.989 29.114 1.00 20.10 O ANISOU 2172 OD2 ASP A 259 2761 2409 2467 -271 127 128 O ATOM 2173 N LYS A 260 -8.288 -53.441 24.970 1.00 16.45 N ANISOU 2173 N LYS A 260 2307 1893 2052 -346 103 -5 N ATOM 2174 CA LYS A 260 -8.050 -54.174 23.730 1.00 18.59 C ANISOU 2174 CA LYS A 260 2571 2159 2334 -386 109 -45 C ATOM 2175 C LYS A 260 -6.789 -55.020 23.795 1.00 18.35 C ANISOU 2175 C LYS A 260 2573 2070 2330 -377 119 -58 C ATOM 2176 O LYS A 260 -6.776 -56.145 23.307 1.00 20.25 O ANISOU 2176 O LYS A 260 2818 2283 2591 -411 140 -83 O ATOM 2177 CB LYS A 260 -7.973 -53.228 22.528 1.00 22.54 C ANISOU 2177 CB LYS A 260 3044 2709 2810 -391 85 -62 C ATOM 2178 CG LYS A 260 -7.436 -53.912 21.284 1.00 18.05 C ANISOU 2178 CG LYS A 260 2475 2133 2251 -422 89 -103 C ATOM 2179 CD LYS A 260 -7.580 -53.048 20.041 1.00 24.81 C ANISOU 2179 CD LYS A 260 3301 3047 3080 -429 69 -119 C ATOM 2180 CE LYS A 260 -6.770 -53.635 18.886 1.00 24.53 C ANISOU 2180 CE LYS A 260 3269 2999 3051 -449 71 -158 C ATOM 2181 NZ LYS A 260 -6.780 -52.754 17.696 1.00 25.15 N ANISOU 2181 NZ LYS A 260 3321 3134 3101 -449 53 -169 N ATOM 2182 N TYR A 261 -5.734 -54.476 24.401 1.00 15.81 N ANISOU 2182 N TYR A 261 2271 1730 2008 -330 105 -41 N ATOM 2183 CA TYR A 261 -4.447 -55.171 24.486 1.00 16.61 C ANISOU 2183 CA TYR A 261 2400 1780 2132 -314 112 -50 C ATOM 2184 C TYR A 261 -4.249 -55.887 25.819 1.00 18.36 C ANISOU 2184 C TYR A 261 2650 1956 2370 -289 131 -22 C ATOM 2185 O TYR A 261 -3.162 -56.416 26.104 1.00 18.74 O ANISOU 2185 O TYR A 261 2723 1963 2436 -266 137 -22 O ATOM 2186 CB TYR A 261 -3.311 -54.191 24.198 1.00 13.37 C ANISOU 2186 CB TYR A 261 1989 1378 1712 -280 85 -52 C ATOM 2187 CG TYR A 261 -3.402 -53.696 22.780 1.00 12.86 C ANISOU 2187 CG TYR A 261 1899 1353 1635 -305 73 -79 C ATOM 2188 CD1 TYR A 261 -2.903 -54.460 21.727 1.00 16.26 C ANISOU 2188 CD1 TYR A 261 2332 1769 2078 -331 83 -112 C ATOM 2189 CD2 TYR A 261 -4.033 -52.488 22.482 1.00 13.21 C ANISOU 2189 CD2 TYR A 261 1917 1449 1652 -302 55 -70 C ATOM 2190 CE1 TYR A 261 -3.015 -54.031 20.421 1.00 17.30 C ANISOU 2190 CE1 TYR A 261 2440 1940 2193 -353 74 -137 C ATOM 2191 CE2 TYR A 261 -4.139 -52.044 21.176 1.00 14.91 C ANISOU 2191 CE2 TYR A 261 2109 1704 1853 -321 46 -91 C ATOM 2192 CZ TYR A 261 -3.628 -52.818 20.150 1.00 18.46 C ANISOU 2192 CZ TYR A 261 2561 2141 2313 -347 54 -125 C ATOM 2193 OH TYR A 261 -3.734 -52.382 18.848 1.00 16.58 O ANISOU 2193 OH TYR A 261 2298 1945 2056 -364 46 -145 O ATOM 2194 N ASN A 262 -5.318 -55.924 26.614 1.00 20.95 N ANISOU 2194 N ASN A 262 2974 2293 2691 -292 142 2 N ATOM 2195 CA ASN A 262 -5.294 -56.560 27.925 1.00 20.67 C ANISOU 2195 CA ASN A 262 2965 2221 2668 -267 162 33 C ATOM 2196 C ASN A 262 -4.110 -56.040 28.749 1.00 22.84 C ANISOU 2196 C ASN A 262 3260 2482 2936 -210 144 51 C ATOM 2197 O ASN A 262 -3.388 -56.816 29.369 1.00 24.99 O ANISOU 2197 O ASN A 262 3559 2713 3225 -187 158 63 O ATOM 2198 CB ASN A 262 -5.244 -58.090 27.790 1.00 19.62 C ANISOU 2198 CB ASN A 262 2849 2036 2568 -295 199 22 C ATOM 2199 CG ASN A 262 -6.526 -58.687 27.205 1.00 24.72 C ANISOU 2199 CG ASN A 262 3475 2693 3224 -353 221 5 C ATOM 2200 OD1 ASN A 262 -7.435 -57.976 26.769 1.00 31.16 O ANISOU 2200 OD1 ASN A 262 4261 3560 4020 -374 207 -1 O ATOM 2201 ND2 ASN A 262 -6.593 -60.010 27.190 1.00 30.97 N ANISOU 2201 ND2 ASN A 262 4283 3437 4049 -379 257 -4 N ATOM 2202 N ILE A 263 -3.931 -54.717 28.717 1.00 24.17 N ANISOU 2202 N ILE A 263 3415 2688 3080 -187 112 53 N ATOM 2203 CA ILE A 263 -2.900 -53.986 29.450 1.00 21.22 C ANISOU 2203 CA ILE A 263 3054 2311 2696 -136 88 66 C ATOM 2204 C ILE A 263 -3.539 -53.438 30.719 1.00 25.67 C ANISOU 2204 C ILE A 263 3623 2892 3240 -106 85 98 C ATOM 2205 O ILE A 263 -4.717 -53.070 30.720 1.00 29.14 O ANISOU 2205 O ILE A 263 4046 3361 3666 -123 89 107 O ATOM 2206 CB ILE A 263 -2.423 -52.744 28.657 1.00 25.79 C ANISOU 2206 CB ILE A 263 3614 2923 3263 -132 57 48 C ATOM 2207 CG1 ILE A 263 -1.774 -53.120 27.324 1.00 28.90 C ANISOU 2207 CG1 ILE A 263 4000 3307 3672 -159 58 16 C ATOM 2208 CG2 ILE A 263 -1.459 -51.899 29.479 1.00 29.30 C ANISOU 2208 CG2 ILE A 263 4068 3366 3698 -83 32 59 C ATOM 2209 CD1 ILE A 263 -1.470 -51.903 26.465 1.00 27.83 C ANISOU 2209 CD1 ILE A 263 3843 3206 3524 -158 33 2 C ATOM 2210 N GLU A 264 -2.765 -53.361 31.793 1.00 17.83 N ANISOU 2210 N GLU A 264 2650 1883 2241 -60 77 116 N ATOM 2211 CA GLU A 264 -3.236 -52.734 33.013 1.00 24.93 C ANISOU 2211 CA GLU A 264 3555 2801 3116 -26 70 144 C ATOM 2212 C GLU A 264 -2.507 -51.410 33.238 1.00 24.75 C ANISOU 2212 C GLU A 264 3528 2800 3076 8 34 137 C ATOM 2213 O GLU A 264 -1.284 -51.359 33.152 1.00 25.73 O ANISOU 2213 O GLU A 264 3658 2909 3208 26 19 124 O ATOM 2214 CB GLU A 264 -2.981 -53.680 34.180 1.00 29.60 C ANISOU 2214 CB GLU A 264 4174 3361 3712 4 90 171 C ATOM 2215 CG GLU A 264 -3.625 -53.267 35.462 1.00 34.03 C ANISOU 2215 CG GLU A 264 4742 3940 4246 37 91 202 C ATOM 2216 CD GLU A 264 -3.897 -54.454 36.355 1.00 37.05 C ANISOU 2216 CD GLU A 264 5147 4293 4637 50 126 233 C ATOM 2217 OE1 GLU A 264 -3.001 -55.323 36.490 1.00 36.76 O ANISOU 2217 OE1 GLU A 264 5129 4222 4617 64 136 236 O ATOM 2218 OE2 GLU A 264 -5.017 -54.520 36.902 1.00 38.19 O ANISOU 2218 OE2 GLU A 264 5290 4450 4771 46 145 256 O ATOM 2219 N LEU A 265 -3.252 -50.339 33.509 1.00 21.44 N ANISOU 2219 N LEU A 265 3097 2415 2634 15 23 145 N ATOM 2220 CA LEU A 265 -2.634 -49.062 33.845 1.00 23.13 C ANISOU 2220 CA LEU A 265 3309 2646 2832 48 -8 138 C ATOM 2221 C LEU A 265 -1.882 -49.174 35.170 1.00 22.61 C ANISOU 2221 C LEU A 265 3266 2567 2756 95 -17 151 C ATOM 2222 O LEU A 265 -2.321 -49.869 36.080 1.00 28.20 O ANISOU 2222 O LEU A 265 3991 3268 3457 110 1 176 O ATOM 2223 CB LEU A 265 -3.680 -47.945 33.981 1.00 25.27 C ANISOU 2223 CB LEU A 265 3566 2953 3081 49 -14 146 C ATOM 2224 CG LEU A 265 -4.121 -47.107 32.785 1.00 21.23 C ANISOU 2224 CG LEU A 265 3028 2468 2570 21 -21 132 C ATOM 2225 CD1 LEU A 265 -4.877 -45.903 33.296 1.00 22.47 C ANISOU 2225 CD1 LEU A 265 3179 2656 2704 41 -28 144 C ATOM 2226 CD2 LEU A 265 -2.928 -46.678 31.935 1.00 24.36 C ANISOU 2226 CD2 LEU A 265 3418 2855 2981 19 -40 106 C ATOM 2227 N ASP A 266 -0.755 -48.481 35.268 1.00 20.39 N ANISOU 2227 N ASP A 266 2986 2286 2475 119 -45 135 N ATOM 2228 CA ASP A 266 -0.071 -48.294 36.542 1.00 23.03 C ANISOU 2228 CA ASP A 266 3337 2620 2793 167 -61 143 C ATOM 2229 C ASP A 266 -1.109 -47.812 37.556 1.00 24.91 C ANISOU 2229 C ASP A 266 3581 2880 3001 187 -57 164 C ATOM 2230 O ASP A 266 -1.856 -46.870 37.277 1.00 22.29 O ANISOU 2230 O ASP A 266 3237 2572 2661 176 -61 160 O ATOM 2231 CB ASP A 266 1.025 -47.243 36.367 1.00 22.24 C ANISOU 2231 CB ASP A 266 3228 2527 2696 181 -95 116 C ATOM 2232 CG ASP A 266 1.930 -47.117 37.573 1.00 23.26 C ANISOU 2232 CG ASP A 266 3371 2658 2811 227 -116 117 C ATOM 2233 OD1 ASP A 266 1.467 -47.301 38.716 1.00 23.74 O ANISOU 2233 OD1 ASP A 266 3447 2726 2846 256 -110 139 O ATOM 2234 OD2 ASP A 266 3.114 -46.797 37.376 1.00 27.48 O ANISOU 2234 OD2 ASP A 266 3898 3187 3356 236 -138 96 O ATOM 2235 N PRO A 267 -1.178 -48.462 38.733 1.00 22.66 N ANISOU 2235 N PRO A 267 3317 2591 2702 219 -46 189 N ATOM 2236 CA PRO A 267 -2.197 -48.064 39.712 1.00 21.53 C ANISOU 2236 CA PRO A 267 3182 2470 2529 239 -38 211 C ATOM 2237 C PRO A 267 -2.005 -46.636 40.219 1.00 24.28 C ANISOU 2237 C PRO A 267 3527 2843 2854 267 -68 196 C ATOM 2238 O PRO A 267 -2.919 -46.071 40.826 1.00 24.50 O ANISOU 2238 O PRO A 267 3558 2893 2859 280 -63 209 O ATOM 2239 CB PRO A 267 -2.010 -49.076 40.855 1.00 20.50 C ANISOU 2239 CB PRO A 267 3075 2328 2387 274 -23 240 C ATOM 2240 CG PRO A 267 -0.622 -49.587 40.685 1.00 23.66 C ANISOU 2240 CG PRO A 267 3480 2707 2804 285 -36 226 C ATOM 2241 CD PRO A 267 -0.386 -49.610 39.198 1.00 21.88 C ANISOU 2241 CD PRO A 267 3236 2467 2611 239 -37 201 C ATOM 2242 N ARG A 268 -0.839 -46.047 39.979 1.00 20.69 N ANISOU 2242 N ARG A 268 3067 2386 2407 274 -97 168 N ATOM 2243 CA ARG A 268 -0.633 -44.675 40.429 1.00 25.72 C ANISOU 2243 CA ARG A 268 3701 3042 3027 296 -124 149 C ATOM 2244 C ARG A 268 -1.552 -43.691 39.690 1.00 26.54 C ANISOU 2244 C ARG A 268 3789 3161 3134 271 -120 143 C ATOM 2245 O ARG A 268 -1.749 -42.565 40.143 1.00 27.62 O ANISOU 2245 O ARG A 268 3926 3313 3254 289 -132 135 O ATOM 2246 CB ARG A 268 0.836 -44.256 40.327 1.00 34.61 C ANISOU 2246 CB ARG A 268 4823 4162 4166 308 -156 118 C ATOM 2247 CG ARG A 268 1.291 -43.847 38.947 1.00 40.62 C ANISOU 2247 CG ARG A 268 5564 4913 4959 272 -162 95 C ATOM 2248 CD ARG A 268 2.733 -43.367 38.992 1.00 44.75 C ANISOU 2248 CD ARG A 268 6080 5430 5493 286 -193 66 C ATOM 2249 NE ARG A 268 3.676 -44.479 39.065 1.00 46.97 N ANISOU 2249 NE ARG A 268 6366 5695 5785 294 -194 69 N ATOM 2250 CZ ARG A 268 4.838 -44.428 39.704 1.00 47.02 C ANISOU 2250 CZ ARG A 268 6373 5704 5787 323 -219 56 C ATOM 2251 NH1 ARG A 268 5.200 -43.322 40.345 1.00 46.62 N ANISOU 2251 NH1 ARG A 268 6320 5670 5724 344 -246 34 N ATOM 2252 NH2 ARG A 268 5.635 -45.487 39.710 1.00 45.27 N ANISOU 2252 NH2 ARG A 268 6156 5469 5577 333 -216 63 N ATOM 2253 N PHE A 269 -2.116 -44.126 38.564 1.00 23.57 N ANISOU 2253 N PHE A 269 3398 2779 2777 230 -101 148 N ATOM 2254 CA PHE A 269 -3.081 -43.310 37.827 1.00 16.00 C ANISOU 2254 CA PHE A 269 2422 1838 1818 208 -93 148 C ATOM 2255 C PHE A 269 -4.441 -43.243 38.515 1.00 24.46 C ANISOU 2255 C PHE A 269 3498 2931 2866 217 -74 176 C ATOM 2256 O PHE A 269 -5.276 -42.417 38.153 1.00 27.65 O ANISOU 2256 O PHE A 269 3888 3354 3264 209 -69 179 O ATOM 2257 CB PHE A 269 -3.252 -43.815 36.394 1.00 20.28 C ANISOU 2257 CB PHE A 269 2946 2375 2386 162 -81 143 C ATOM 2258 CG PHE A 269 -2.112 -43.453 35.480 1.00 21.32 C ANISOU 2258 CG PHE A 269 3067 2494 2540 151 -99 116 C ATOM 2259 CD1 PHE A 269 -2.002 -42.175 34.964 1.00 20.05 C ANISOU 2259 CD1 PHE A 269 2892 2344 2382 149 -112 101 C ATOM 2260 CD2 PHE A 269 -1.173 -44.403 35.110 1.00 20.43 C ANISOU 2260 CD2 PHE A 269 2957 2358 2447 141 -100 107 C ATOM 2261 CE1 PHE A 269 -0.964 -41.835 34.107 1.00 19.32 C ANISOU 2261 CE1 PHE A 269 2789 2240 2312 138 -126 79 C ATOM 2262 CE2 PHE A 269 -0.128 -44.074 34.254 1.00 22.16 C ANISOU 2262 CE2 PHE A 269 3165 2566 2687 131 -115 83 C ATOM 2263 CZ PHE A 269 -0.026 -42.781 33.753 1.00 18.43 C ANISOU 2263 CZ PHE A 269 2679 2107 2218 129 -128 69 C ATOM 2264 N ASN A 270 -4.663 -44.102 39.506 1.00 22.09 N ANISOU 2264 N ASN A 270 3215 2626 2552 237 -60 198 N ATOM 2265 CA ASN A 270 -5.940 -44.125 40.223 1.00 22.61 C ANISOU 2265 CA ASN A 270 3286 2711 2595 248 -39 227 C ATOM 2266 C ASN A 270 -6.310 -42.791 40.865 1.00 29.10 C ANISOU 2266 C ASN A 270 4110 3556 3391 277 -50 224 C ATOM 2267 O ASN A 270 -7.489 -42.437 40.933 1.00 28.26 O ANISOU 2267 O ASN A 270 3995 3469 3272 275 -33 242 O ATOM 2268 CB ASN A 270 -5.948 -45.221 41.296 1.00 31.94 C ANISOU 2268 CB ASN A 270 4489 3883 3765 271 -22 252 C ATOM 2269 CG ASN A 270 -6.036 -46.623 40.710 1.00 36.06 C ANISOU 2269 CG ASN A 270 5008 4381 4313 238 2 263 C ATOM 2270 OD1 ASN A 270 -6.577 -46.824 39.624 1.00 34.58 O ANISOU 2270 OD1 ASN A 270 4801 4194 4145 195 14 259 O ATOM 2271 ND2 ASN A 270 -5.509 -47.602 41.441 1.00 39.76 N ANISOU 2271 ND2 ASN A 270 5496 4830 4780 260 11 278 N ATOM 2272 N ASP A 271 -5.307 -42.057 41.344 1.00 23.41 N ANISOU 2272 N ASP A 271 3399 2831 2663 305 -78 200 N ATOM 2273 CA ASP A 271 -5.547 -40.795 42.042 1.00 31.26 C ANISOU 2273 CA ASP A 271 4400 3843 3634 336 -89 192 C ATOM 2274 C ASP A 271 -5.306 -39.549 41.195 1.00 30.11 C ANISOU 2274 C ASP A 271 4239 3697 3504 322 -103 166 C ATOM 2275 O ASP A 271 -5.473 -38.429 41.685 1.00 32.25 O ANISOU 2275 O ASP A 271 4515 3978 3760 345 -111 156 O ATOM 2276 CB ASP A 271 -4.685 -40.708 43.303 1.00 44.70 C ANISOU 2276 CB ASP A 271 6125 5545 5314 379 -109 180 C ATOM 2277 CG ASP A 271 -5.034 -41.774 44.321 1.00 57.48 C ANISOU 2277 CG ASP A 271 7762 7169 6910 403 -92 211 C ATOM 2278 OD1 ASP A 271 -6.134 -42.362 44.220 1.00 57.84 O ANISOU 2278 OD1 ASP A 271 7804 7220 6955 389 -62 243 O ATOM 2279 OD2 ASP A 271 -4.206 -42.019 45.224 1.00 65.78 O ANISOU 2279 OD2 ASP A 271 8830 8220 7944 437 -108 206 O ATOM 2280 N ILE A 272 -4.902 -39.729 39.939 1.00 25.96 N ANISOU 2280 N ILE A 272 3695 3160 3009 286 -105 155 N ATOM 2281 CA ILE A 272 -4.565 -38.577 39.100 1.00 17.07 C ANISOU 2281 CA ILE A 272 2555 2031 1900 275 -117 132 C ATOM 2282 C ILE A 272 -5.295 -38.494 37.754 1.00 20.17 C ANISOU 2282 C ILE A 272 2923 2433 2308 239 -101 142 C ATOM 2283 O ILE A 272 -5.351 -37.417 37.153 1.00 19.32 O ANISOU 2283 O ILE A 272 2803 2329 2208 235 -104 134 O ATOM 2284 CB ILE A 272 -3.029 -38.463 38.847 1.00 19.50 C ANISOU 2284 CB ILE A 272 2862 2317 2229 274 -143 101 C ATOM 2285 CG1 ILE A 272 -2.500 -39.706 38.128 1.00 16.43 C ANISOU 2285 CG1 ILE A 272 2468 1915 1861 247 -140 103 C ATOM 2286 CG2 ILE A 272 -2.294 -38.231 40.142 1.00 23.80 C ANISOU 2286 CG2 ILE A 272 3427 2860 2756 311 -164 85 C ATOM 2287 CD1 ILE A 272 -1.009 -39.619 37.744 1.00 20.48 C ANISOU 2287 CD1 ILE A 272 2977 2408 2398 244 -163 74 C ATOM 2288 N LEU A 273 -5.855 -39.609 37.284 1.00 16.40 N ANISOU 2288 N LEU A 273 2438 1960 1835 213 -83 160 N ATOM 2289 CA LEU A 273 -6.372 -39.661 35.915 1.00 16.26 C ANISOU 2289 CA LEU A 273 2394 1952 1831 176 -72 164 C ATOM 2290 C LEU A 273 -7.742 -39.003 35.733 1.00 24.10 C ANISOU 2290 C LEU A 273 3371 2976 2809 175 -55 185 C ATOM 2291 O LEU A 273 -7.988 -38.357 34.716 1.00 26.12 O ANISOU 2291 O LEU A 273 3607 3245 3072 160 -54 183 O ATOM 2292 CB LEU A 273 -6.406 -41.099 35.399 1.00 22.71 C ANISOU 2292 CB LEU A 273 3207 2762 2661 144 -60 169 C ATOM 2293 CG LEU A 273 -6.874 -41.316 33.961 1.00 23.94 C ANISOU 2293 CG LEU A 273 3336 2931 2830 103 -50 167 C ATOM 2294 CD1 LEU A 273 -6.095 -40.435 32.990 1.00 23.68 C ANISOU 2294 CD1 LEU A 273 3290 2895 2811 98 -65 147 C ATOM 2295 CD2 LEU A 273 -6.763 -42.787 33.566 1.00 26.06 C ANISOU 2295 CD2 LEU A 273 3605 3185 3113 73 -39 166 C ATOM 2296 N GLY A 274 -8.637 -39.192 36.695 1.00 19.27 N ANISOU 2296 N GLY A 274 2769 2378 2176 193 -42 207 N ATOM 2297 CA GLY A 274 -9.977 -38.625 36.611 1.00 19.77 C ANISOU 2297 CA GLY A 274 2816 2471 2223 195 -24 230 C ATOM 2298 C GLY A 274 -10.826 -39.215 35.499 1.00 18.33 C ANISOU 2298 C GLY A 274 2605 2311 2049 155 -9 242 C ATOM 2299 O GLY A 274 -10.466 -40.235 34.914 1.00 19.30 O ANISOU 2299 O GLY A 274 2723 2423 2188 124 -8 233 O ATOM 2300 N ARG A 275 -11.973 -38.583 35.234 1.00 16.23 N ANISOU 2300 N ARG A 275 2319 2079 1770 156 5 261 N ATOM 2301 CA ARG A 275 -12.822 -38.918 34.090 1.00 15.31 C ANISOU 2301 CA ARG A 275 2168 1991 1656 120 16 270 C ATOM 2302 C ARG A 275 -12.916 -37.718 33.164 1.00 15.98 C ANISOU 2302 C ARG A 275 2234 2096 1742 124 11 269 C ATOM 2303 O ARG A 275 -13.203 -36.606 33.607 1.00 21.43 O ANISOU 2303 O ARG A 275 2928 2793 2420 156 14 278 O ATOM 2304 CB ARG A 275 -14.229 -39.337 34.542 1.00 18.34 C ANISOU 2304 CB ARG A 275 2538 2404 2025 116 39 299 C ATOM 2305 CG ARG A 275 -14.277 -40.674 35.268 1.00 23.99 C ANISOU 2305 CG ARG A 275 3268 3102 2745 105 50 305 C ATOM 2306 CD ARG A 275 -15.717 -41.203 35.330 1.00 24.86 C ANISOU 2306 CD ARG A 275 3355 3244 2847 87 75 332 C ATOM 2307 NE ARG A 275 -16.572 -40.403 36.204 1.00 20.86 N ANISOU 2307 NE ARG A 275 2849 2759 2317 123 86 358 N ATOM 2308 CZ ARG A 275 -17.884 -40.590 36.326 1.00 24.59 C ANISOU 2308 CZ ARG A 275 3299 3265 2781 115 108 384 C ATOM 2309 NH1 ARG A 275 -18.472 -41.552 35.632 1.00 24.74 N ANISOU 2309 NH1 ARG A 275 3290 3298 2812 70 119 386 N ATOM 2310 NH2 ARG A 275 -18.605 -39.829 37.144 1.00 17.81 N ANISOU 2310 NH2 ARG A 275 2442 2424 1899 152 119 408 N ATOM 2311 N HIS A 276 -12.696 -37.953 31.873 1.00 11.87 N ANISOU 2311 N HIS A 276 1692 1585 1233 92 7 257 N ATOM 2312 CA HIS A 276 -12.668 -36.889 30.885 1.00 12.28 C ANISOU 2312 CA HIS A 276 1725 1654 1285 96 4 257 C ATOM 2313 C HIS A 276 -13.342 -37.310 29.598 1.00 15.62 C ANISOU 2313 C HIS A 276 2113 2116 1706 61 9 262 C ATOM 2314 O HIS A 276 -13.107 -38.402 29.073 1.00 11.30 O ANISOU 2314 O HIS A 276 1560 1564 1168 26 7 247 O ATOM 2315 CB HIS A 276 -11.224 -36.498 30.577 1.00 16.69 C ANISOU 2315 CB HIS A 276 2300 2178 1864 101 -13 232 C ATOM 2316 CG HIS A 276 -10.451 -36.093 31.785 1.00 18.23 C ANISOU 2316 CG HIS A 276 2527 2337 2062 133 -23 221 C ATOM 2317 ND1 HIS A 276 -10.579 -34.848 32.361 1.00 15.88 N ANISOU 2317 ND1 HIS A 276 2240 2037 1758 168 -21 227 N ATOM 2318 CD2 HIS A 276 -9.541 -36.764 32.529 1.00 19.78 C ANISOU 2318 CD2 HIS A 276 2749 2501 2267 136 -35 204 C ATOM 2319 CE1 HIS A 276 -9.777 -34.768 33.407 1.00 18.06 C ANISOU 2319 CE1 HIS A 276 2543 2281 2036 189 -33 211 C ATOM 2320 NE2 HIS A 276 -9.137 -35.918 33.530 1.00 23.89 N ANISOU 2320 NE2 HIS A 276 3291 3003 2783 171 -42 198 N ATOM 2321 N SER A 277 -14.192 -36.431 29.092 1.00 11.47 N ANISOU 2321 N SER A 277 1563 1629 1165 72 18 282 N ATOM 2322 CA SER A 277 -14.809 -36.653 27.795 1.00 12.21 C ANISOU 2322 CA SER A 277 1620 1768 1253 43 21 286 C ATOM 2323 C SER A 277 -13.795 -36.429 26.685 1.00 16.92 C ANISOU 2323 C SER A 277 2213 2353 1861 33 9 266 C ATOM 2324 O SER A 277 -12.798 -35.710 26.871 1.00 17.78 O ANISOU 2324 O SER A 277 2344 2428 1983 55 2 258 O ATOM 2325 CB SER A 277 -15.974 -35.677 27.622 1.00 16.67 C ANISOU 2325 CB SER A 277 2159 2380 1797 65 33 317 C ATOM 2326 OG SER A 277 -15.486 -34.357 27.784 1.00 21.24 O ANISOU 2326 OG SER A 277 2753 2940 2379 104 33 323 O ATOM 2327 N ARG A 278 -14.032 -37.035 25.523 1.00 12.32 N ANISOU 2327 N ARG A 278 1604 1802 1274 -1 8 258 N ATOM 2328 CA ARG A 278 -13.207 -36.729 24.361 1.00 12.55 C ANISOU 2328 CA ARG A 278 1627 1832 1310 -7 0 244 C ATOM 2329 C ARG A 278 -13.596 -35.337 23.892 1.00 16.68 C ANISOU 2329 C ARG A 278 2134 2384 1821 24 7 270 C ATOM 2330 O ARG A 278 -14.783 -35.001 23.876 1.00 15.61 O ANISOU 2330 O ARG A 278 1973 2292 1664 33 17 295 O ATOM 2331 CB ARG A 278 -13.429 -37.754 23.248 1.00 15.01 C ANISOU 2331 CB ARG A 278 1913 2173 1616 -50 -3 228 C ATOM 2332 CG ARG A 278 -12.469 -37.612 22.065 1.00 15.25 C ANISOU 2332 CG ARG A 278 1940 2201 1653 -58 -10 210 C ATOM 2333 CD ARG A 278 -12.190 -38.990 21.457 1.00 15.79 C ANISOU 2333 CD ARG A 278 2005 2266 1727 -102 -15 179 C ATOM 2334 NE ARG A 278 -10.979 -39.019 20.633 1.00 22.77 N ANISOU 2334 NE ARG A 278 2897 3129 2624 -107 -22 158 N ATOM 2335 CZ ARG A 278 -10.279 -40.124 20.394 1.00 19.51 C ANISOU 2335 CZ ARG A 278 2496 2690 2226 -135 -25 129 C ATOM 2336 NH1 ARG A 278 -10.669 -41.274 20.929 1.00 17.53 N ANISOU 2336 NH1 ARG A 278 2252 2427 1981 -162 -22 117 N ATOM 2337 NH2 ARG A 278 -9.193 -40.087 19.630 1.00 16.75 N ANISOU 2337 NH2 ARG A 278 2153 2324 1887 -137 -30 112 N ATOM 2338 N LYS A 279 -12.614 -34.520 23.527 1.00 15.90 N ANISOU 2338 N LYS A 279 2046 2260 1736 42 4 265 N ATOM 2339 CA LYS A 279 -12.898 -33.142 23.113 1.00 19.66 C ANISOU 2339 CA LYS A 279 2509 2755 2204 75 15 292 C ATOM 2340 C LYS A 279 -12.930 -33.009 21.592 1.00 25.53 C ANISOU 2340 C LYS A 279 3224 3540 2937 65 17 296 C ATOM 2341 O LYS A 279 -12.280 -33.774 20.887 1.00 25.94 O ANISOU 2341 O LYS A 279 3273 3587 2994 36 7 273 O ATOM 2342 CB LYS A 279 -11.838 -32.188 23.666 1.00 12.05 C ANISOU 2342 CB LYS A 279 1576 1738 1266 104 15 286 C ATOM 2343 CG LYS A 279 -11.649 -32.222 25.171 1.00 11.59 C ANISOU 2343 CG LYS A 279 1549 1638 1216 119 11 277 C ATOM 2344 CD LYS A 279 -12.963 -32.139 25.954 1.00 16.74 C ANISOU 2344 CD LYS A 279 2195 2318 1846 133 22 301 C ATOM 2345 CE LYS A 279 -12.727 -32.098 27.472 1.00 17.42 C ANISOU 2345 CE LYS A 279 2315 2365 1939 153 19 293 C ATOM 2346 NZ LYS A 279 -12.103 -33.344 28.060 1.00 11.69 N ANISOU 2346 NZ LYS A 279 1609 1612 1222 130 5 268 N ATOM 2347 N ARG A 280 -13.671 -32.030 21.082 1.00 18.34 N ANISOU 2347 N ARG A 280 2290 2670 2009 90 29 328 N ATOM 2348 CA ARG A 280 -13.604 -31.723 19.654 1.00 17.01 C ANISOU 2348 CA ARG A 280 2095 2540 1828 89 33 337 C ATOM 2349 C ARG A 280 -12.442 -30.759 19.408 1.00 19.11 C ANISOU 2349 C ARG A 280 2380 2762 2118 112 39 338 C ATOM 2350 O ARG A 280 -12.166 -29.882 20.228 1.00 17.85 O ANISOU 2350 O ARG A 280 2243 2562 1977 141 47 346 O ATOM 2351 CB ARG A 280 -14.918 -31.132 19.154 1.00 19.93 C ANISOU 2351 CB ARG A 280 2429 2977 2166 108 45 374 C ATOM 2352 CG ARG A 280 -16.122 -32.016 19.469 1.00 19.67 C ANISOU 2352 CG ARG A 280 2374 2988 2111 85 40 374 C ATOM 2353 CD ARG A 280 -17.388 -31.493 18.852 1.00 21.61 C ANISOU 2353 CD ARG A 280 2578 3308 2324 101 50 409 C ATOM 2354 NE ARG A 280 -18.544 -32.185 19.405 1.00 22.34 N ANISOU 2354 NE ARG A 280 2651 3434 2401 84 48 412 N ATOM 2355 CZ ARG A 280 -19.076 -33.297 18.904 1.00 21.65 C ANISOU 2355 CZ ARG A 280 2537 3390 2300 41 37 394 C ATOM 2356 NH1 ARG A 280 -20.130 -33.844 19.500 1.00 24.34 N ANISOU 2356 NH1 ARG A 280 2861 3757 2632 26 39 399 N ATOM 2357 NH2 ARG A 280 -18.557 -33.859 17.817 1.00 20.23 N ANISOU 2357 NH2 ARG A 280 2346 3225 2114 13 26 369 N ATOM 2358 N TRP A 281 -11.771 -30.915 18.275 1.00 14.12 N ANISOU 2358 N TRP A 281 1739 2139 1488 100 36 328 N ATOM 2359 CA TRP A 281 -10.521 -30.183 18.049 1.00 16.44 C ANISOU 2359 CA TRP A 281 2050 2385 1810 115 42 324 C ATOM 2360 C TRP A 281 -10.728 -28.682 17.919 1.00 18.79 C ANISOU 2360 C TRP A 281 2345 2683 2111 158 64 361 C ATOM 2361 O TRP A 281 -9.796 -27.897 18.115 1.00 17.10 O ANISOU 2361 O TRP A 281 2150 2418 1928 175 72 359 O ATOM 2362 CB TRP A 281 -9.802 -30.721 16.814 1.00 17.65 C ANISOU 2362 CB TRP A 281 2193 2552 1962 93 37 308 C ATOM 2363 CG TRP A 281 -9.271 -32.078 17.027 1.00 17.73 C ANISOU 2363 CG TRP A 281 2215 2542 1980 55 19 269 C ATOM 2364 CD1 TRP A 281 -9.752 -33.240 16.498 1.00 16.72 C ANISOU 2364 CD1 TRP A 281 2070 2453 1830 22 9 252 C ATOM 2365 CD2 TRP A 281 -8.169 -32.438 17.865 1.00 15.93 C ANISOU 2365 CD2 TRP A 281 2018 2249 1784 47 9 242 C ATOM 2366 NE1 TRP A 281 -9.002 -34.304 16.945 1.00 21.00 N ANISOU 2366 NE1 TRP A 281 2634 2954 2392 -6 -3 217 N ATOM 2367 CE2 TRP A 281 -8.022 -33.835 17.784 1.00 17.81 C ANISOU 2367 CE2 TRP A 281 2259 2488 2020 11 -4 212 C ATOM 2368 CE3 TRP A 281 -7.283 -31.710 18.673 1.00 20.27 C ANISOU 2368 CE3 TRP A 281 2595 2742 2367 68 10 238 C ATOM 2369 CZ2 TRP A 281 -7.029 -34.520 18.475 1.00 14.31 C ANISOU 2369 CZ2 TRP A 281 1842 1992 1603 -2 -15 184 C ATOM 2370 CZ3 TRP A 281 -6.299 -32.394 19.362 1.00 20.78 C ANISOU 2370 CZ3 TRP A 281 2683 2757 2456 53 -4 207 C ATOM 2371 CH2 TRP A 281 -6.183 -33.788 19.261 1.00 20.51 C ANISOU 2371 CH2 TRP A 281 2650 2726 2416 21 -16 183 C ATOM 2372 N GLU A 282 -11.950 -28.294 17.577 1.00 17.72 N ANISOU 2372 N GLU A 282 2182 2605 1945 175 75 394 N ATOM 2373 CA GLU A 282 -12.283 -26.891 17.372 1.00 22.08 C ANISOU 2373 CA GLU A 282 2729 3163 2497 219 100 434 C ATOM 2374 C GLU A 282 -12.059 -26.035 18.619 1.00 18.02 C ANISOU 2374 C GLU A 282 2246 2590 2012 245 110 435 C ATOM 2375 O GLU A 282 -11.806 -24.835 18.523 1.00 21.37 O ANISOU 2375 O GLU A 282 2678 2989 2454 277 131 457 O ATOM 2376 CB GLU A 282 -13.731 -26.749 16.868 1.00 23.89 C ANISOU 2376 CB GLU A 282 2921 3470 2685 234 108 469 C ATOM 2377 CG GLU A 282 -13.923 -27.113 15.393 1.00 24.12 C ANISOU 2377 CG GLU A 282 2915 3564 2684 223 105 477 C ATOM 2378 CD GLU A 282 -14.131 -28.611 15.143 1.00 32.25 C ANISOU 2378 CD GLU A 282 3931 4627 3695 174 80 442 C ATOM 2379 OE1 GLU A 282 -14.075 -29.414 16.104 1.00 26.65 O ANISOU 2379 OE1 GLU A 282 3240 3886 2998 148 66 414 O ATOM 2380 OE2 GLU A 282 -14.355 -28.988 13.967 1.00 35.47 O ANISOU 2380 OE2 GLU A 282 4309 5092 4074 162 75 443 O ATOM 2381 N ARG A 283 -12.135 -26.635 19.794 1.00 18.51 N ANISOU 2381 N ARG A 283 2328 2627 2080 231 95 412 N ATOM 2382 CA ARG A 283 -11.917 -25.849 21.007 1.00 23.86 C ANISOU 2382 CA ARG A 283 3035 3250 2780 256 103 409 C ATOM 2383 C ARG A 283 -10.508 -25.245 21.094 1.00 19.13 C ANISOU 2383 C ARG A 283 2461 2585 2221 260 105 389 C ATOM 2384 O ARG A 283 -10.306 -24.280 21.810 1.00 17.24 O ANISOU 2384 O ARG A 283 2242 2305 2003 285 117 390 O ATOM 2385 CB ARG A 283 -12.217 -26.658 22.273 1.00 24.15 C ANISOU 2385 CB ARG A 283 3089 3274 2811 242 87 387 C ATOM 2386 CG ARG A 283 -11.326 -27.869 22.474 1.00 23.06 C ANISOU 2386 CG ARG A 283 2964 3112 2685 204 62 348 C ATOM 2387 CD ARG A 283 -10.992 -28.066 23.958 1.00 33.52 C ANISOU 2387 CD ARG A 283 4322 4390 4023 207 52 325 C ATOM 2388 NE ARG A 283 -12.183 -28.252 24.784 1.00 44.40 N ANISOU 2388 NE ARG A 283 5698 5794 5378 217 56 340 N ATOM 2389 CZ ARG A 283 -12.171 -28.318 26.114 1.00 40.28 C ANISOU 2389 CZ ARG A 283 5202 5243 4859 228 51 328 C ATOM 2390 NH1 ARG A 283 -11.033 -28.203 26.788 1.00 40.36 N ANISOU 2390 NH1 ARG A 283 5241 5200 4893 229 40 299 N ATOM 2391 NH2 ARG A 283 -13.303 -28.493 26.770 1.00 38.76 N ANISOU 2391 NH2 ARG A 283 5006 5079 4644 237 58 346 N ATOM 2392 N PHE A 284 -9.545 -25.808 20.370 1.00 18.17 N ANISOU 2392 N PHE A 284 2337 2454 2111 234 94 368 N ATOM 2393 CA PHE A 284 -8.174 -25.305 20.427 1.00 14.05 C ANISOU 2393 CA PHE A 284 1835 1874 1631 234 95 348 C ATOM 2394 C PHE A 284 -7.924 -24.208 19.401 1.00 16.47 C ANISOU 2394 C PHE A 284 2129 2179 1949 257 121 377 C ATOM 2395 O PHE A 284 -6.839 -23.639 19.340 1.00 20.06 O ANISOU 2395 O PHE A 284 2596 2585 2440 259 128 365 O ATOM 2396 CB PHE A 284 -7.194 -26.453 20.236 1.00 12.75 C ANISOU 2396 CB PHE A 284 1675 1695 1475 198 71 312 C ATOM 2397 CG PHE A 284 -7.348 -27.514 21.273 1.00 15.57 C ANISOU 2397 CG PHE A 284 2046 2045 1823 179 49 287 C ATOM 2398 CD1 PHE A 284 -6.951 -27.273 22.581 1.00 19.39 C ANISOU 2398 CD1 PHE A 284 2558 2484 2326 188 41 267 C ATOM 2399 CD2 PHE A 284 -7.938 -28.723 20.966 1.00 14.48 C ANISOU 2399 CD2 PHE A 284 1894 1949 1658 153 37 283 C ATOM 2400 CE1 PHE A 284 -7.109 -28.233 23.553 1.00 17.92 C ANISOU 2400 CE1 PHE A 284 2385 2294 2130 175 23 248 C ATOM 2401 CE2 PHE A 284 -8.094 -29.693 21.936 1.00 20.28 C ANISOU 2401 CE2 PHE A 284 2642 2675 2388 137 21 263 C ATOM 2402 CZ PHE A 284 -7.686 -29.449 23.232 1.00 19.51 C ANISOU 2402 CZ PHE A 284 2573 2533 2307 150 14 248 C ATOM 2403 N VAL A 285 -8.939 -23.919 18.598 1.00 17.01 N ANISOU 2403 N VAL A 285 2172 2304 1988 274 137 415 N ATOM 2404 CA VAL A 285 -8.831 -22.883 17.575 1.00 15.13 C ANISOU 2404 CA VAL A 285 1920 2073 1756 300 166 450 C ATOM 2405 C VAL A 285 -9.205 -21.525 18.144 1.00 19.44 C ANISOU 2405 C VAL A 285 2478 2590 2318 340 194 476 C ATOM 2406 O VAL A 285 -10.203 -21.396 18.843 1.00 25.56 O ANISOU 2406 O VAL A 285 3254 3382 3075 356 196 488 O ATOM 2407 CB VAL A 285 -9.760 -23.184 16.392 1.00 17.36 C ANISOU 2407 CB VAL A 285 2167 2436 1994 304 171 482 C ATOM 2408 CG1 VAL A 285 -9.635 -22.095 15.331 1.00 15.97 C ANISOU 2408 CG1 VAL A 285 1977 2269 1822 337 203 523 C ATOM 2409 CG2 VAL A 285 -9.456 -24.549 15.821 1.00 15.22 C ANISOU 2409 CG2 VAL A 285 1885 2194 1706 264 144 453 C ATOM 2410 N HIS A 286 -8.400 -20.510 17.848 1.00 15.71 N ANISOU 2410 N HIS A 286 2015 2072 1883 356 218 484 N ATOM 2411 CA HIS A 286 -8.680 -19.159 18.321 1.00 16.81 C ANISOU 2411 CA HIS A 286 2168 2177 2044 394 249 507 C ATOM 2412 C HIS A 286 -8.181 -18.144 17.297 1.00 18.14 C ANISOU 2412 C HIS A 286 2328 2328 2235 416 284 539 C ATOM 2413 O HIS A 286 -7.607 -18.528 16.274 1.00 21.26 O ANISOU 2413 O HIS A 286 2708 2741 2628 402 282 542 O ATOM 2414 CB HIS A 286 -8.066 -18.927 19.704 1.00 19.10 C ANISOU 2414 CB HIS A 286 2492 2398 2369 387 239 467 C ATOM 2415 CG HIS A 286 -6.617 -19.291 19.790 1.00 19.90 C ANISOU 2415 CG HIS A 286 2605 2450 2505 356 221 424 C ATOM 2416 ND1 HIS A 286 -5.653 -18.681 19.021 1.00 15.99 N ANISOU 2416 ND1 HIS A 286 2107 1923 2045 356 240 429 N ATOM 2417 CD2 HIS A 286 -5.969 -20.191 20.568 1.00 15.79 C ANISOU 2417 CD2 HIS A 286 2099 1909 1991 325 187 378 C ATOM 2418 CE1 HIS A 286 -4.471 -19.201 19.306 1.00 15.81 C ANISOU 2418 CE1 HIS A 286 2094 1863 2049 326 217 387 C ATOM 2419 NE2 HIS A 286 -4.636 -20.116 20.244 1.00 19.04 N ANISOU 2419 NE2 HIS A 286 2515 2280 2441 308 185 355 N ATOM 2420 N SER A 287 -8.404 -16.857 17.552 1.00 16.89 N ANISOU 2420 N SER A 287 2180 2136 2100 452 319 565 N ATOM 2421 CA SER A 287 -8.170 -15.850 16.518 1.00 20.35 C ANISOU 2421 CA SER A 287 2608 2567 2556 480 359 607 C ATOM 2422 C SER A 287 -6.711 -15.770 16.066 1.00 21.62 C ANISOU 2422 C SER A 287 2776 2678 2761 458 362 585 C ATOM 2423 O SER A 287 -6.420 -15.305 14.962 1.00 21.89 O ANISOU 2423 O SER A 287 2796 2721 2803 473 389 619 O ATOM 2424 CB SER A 287 -8.684 -14.483 16.969 1.00 32.23 C ANISOU 2424 CB SER A 287 4126 4037 4081 524 400 637 C ATOM 2425 OG SER A 287 -8.160 -14.143 18.238 1.00 46.24 O ANISOU 2425 OG SER A 287 5934 5740 5895 514 394 594 O ATOM 2426 N GLU A 288 -5.804 -16.247 16.911 1.00 17.86 N ANISOU 2426 N GLU A 288 2319 2155 2313 424 334 531 N ATOM 2427 CA GLU A 288 -4.370 -16.171 16.624 1.00 20.78 C ANISOU 2427 CA GLU A 288 2694 2473 2728 402 335 506 C ATOM 2428 C GLU A 288 -3.795 -17.389 15.907 1.00 22.45 C ANISOU 2428 C GLU A 288 2890 2720 2921 369 307 488 C ATOM 2429 O GLU A 288 -2.641 -17.354 15.475 1.00 25.72 O ANISOU 2429 O GLU A 288 3304 3101 3370 353 310 474 O ATOM 2430 CB GLU A 288 -3.574 -15.896 17.896 1.00 19.55 C ANISOU 2430 CB GLU A 288 2567 2245 2618 385 323 456 C ATOM 2431 CG GLU A 288 -3.702 -14.474 18.401 1.00 25.22 C ANISOU 2431 CG GLU A 288 3302 2909 3372 414 360 468 C ATOM 2432 CD GLU A 288 -5.077 -14.186 18.980 1.00 28.04 C ANISOU 2432 CD GLU A 288 3665 3294 3696 445 368 491 C ATOM 2433 OE1 GLU A 288 -5.539 -14.977 19.839 1.00 28.20 O ANISOU 2433 OE1 GLU A 288 3692 3335 3687 433 334 465 O ATOM 2434 OE2 GLU A 288 -5.690 -13.170 18.577 1.00 32.21 O ANISOU 2434 OE2 GLU A 288 4190 3821 4228 483 409 537 O ATOM 2435 N ASN A 289 -4.574 -18.463 15.789 1.00 17.01 N ANISOU 2435 N ASN A 289 2188 2093 2180 358 280 487 N ATOM 2436 CA ASN A 289 -4.109 -19.631 15.040 1.00 14.65 C ANISOU 2436 CA ASN A 289 1875 1829 1862 328 256 470 C ATOM 2437 C ASN A 289 -5.053 -20.086 13.921 1.00 17.87 C ANISOU 2437 C ASN A 289 2254 2320 2216 338 259 505 C ATOM 2438 O ASN A 289 -4.719 -20.995 13.165 1.00 20.11 O ANISOU 2438 O ASN A 289 2524 2636 2480 315 243 493 O ATOM 2439 CB ASN A 289 -3.796 -20.808 15.983 1.00 13.48 C ANISOU 2439 CB ASN A 289 1740 1670 1711 292 214 419 C ATOM 2440 CG ASN A 289 -5.048 -21.359 16.686 1.00 13.63 C ANISOU 2440 CG ASN A 289 1760 1730 1690 294 196 419 C ATOM 2441 OD1 ASN A 289 -6.176 -21.196 16.210 1.00 14.95 O ANISOU 2441 OD1 ASN A 289 1909 1951 1821 314 208 455 O ATOM 2442 ND2 ASN A 289 -4.841 -22.036 17.816 1.00 14.30 N ANISOU 2442 ND2 ASN A 289 1863 1790 1779 273 168 379 N ATOM 2443 N GLN A 290 -6.217 -19.447 13.798 1.00 16.88 N ANISOU 2443 N GLN A 290 2118 2232 2065 371 279 547 N ATOM 2444 CA GLN A 290 -7.253 -19.927 12.870 1.00 17.56 C ANISOU 2444 CA GLN A 290 2174 2405 2094 380 276 577 C ATOM 2445 C GLN A 290 -6.783 -19.966 11.405 1.00 19.52 C ANISOU 2445 C GLN A 290 2400 2685 2330 383 290 598 C ATOM 2446 O GLN A 290 -7.243 -20.786 10.606 1.00 20.97 O ANISOU 2446 O GLN A 290 2561 2939 2468 373 274 600 O ATOM 2447 CB GLN A 290 -8.534 -19.091 13.006 1.00 18.94 C ANISOU 2447 CB GLN A 290 2339 2612 2247 421 299 622 C ATOM 2448 CG GLN A 290 -8.395 -17.681 12.463 1.00 28.56 C ANISOU 2448 CG GLN A 290 3557 3806 3488 464 346 670 C ATOM 2449 CD GLN A 290 -9.456 -16.725 12.985 1.00 44.27 C ANISOU 2449 CD GLN A 290 5548 5799 5472 506 371 706 C ATOM 2450 OE1 GLN A 290 -10.498 -17.144 13.491 1.00 48.16 O ANISOU 2450 OE1 GLN A 290 6033 6333 5931 507 355 706 O ATOM 2451 NE2 GLN A 290 -9.186 -15.424 12.871 1.00 46.74 N ANISOU 2451 NE2 GLN A 290 5872 6066 5822 541 414 739 N ATOM 2452 N HIS A 291 -5.878 -19.069 11.049 1.00 22.27 N ANISOU 2452 N HIS A 291 2757 2986 2720 398 319 613 N ATOM 2453 CA HIS A 291 -5.339 -19.049 9.692 1.00 21.04 C ANISOU 2453 CA HIS A 291 2583 2855 2555 405 336 634 C ATOM 2454 C HIS A 291 -4.492 -20.299 9.375 1.00 22.80 C ANISOU 2454 C HIS A 291 2805 3084 2774 362 305 589 C ATOM 2455 O HIS A 291 -4.117 -20.524 8.221 1.00 21.85 O ANISOU 2455 O HIS A 291 2669 2996 2637 363 312 601 O ATOM 2456 CB HIS A 291 -4.511 -17.780 9.473 1.00 22.46 C ANISOU 2456 CB HIS A 291 2773 2972 2787 429 378 660 C ATOM 2457 CG HIS A 291 -3.267 -17.723 10.303 1.00 18.36 C ANISOU 2457 CG HIS A 291 2279 2367 2328 401 371 616 C ATOM 2458 ND1 HIS A 291 -3.288 -17.477 11.659 1.00 20.87 N ANISOU 2458 ND1 HIS A 291 2621 2633 2676 393 360 587 N ATOM 2459 CD2 HIS A 291 -1.967 -17.912 9.976 1.00 23.04 C ANISOU 2459 CD2 HIS A 291 2875 2922 2956 379 371 594 C ATOM 2460 CE1 HIS A 291 -2.054 -17.500 12.128 1.00 25.00 C ANISOU 2460 CE1 HIS A 291 3159 3090 3248 368 353 549 C ATOM 2461 NE2 HIS A 291 -1.232 -17.765 11.126 1.00 24.33 N ANISOU 2461 NE2 HIS A 291 3061 3013 3169 358 359 552 N ATOM 2462 N LEU A 292 -4.186 -21.097 10.396 1.00 18.11 N ANISOU 2462 N LEU A 292 2230 2458 2195 327 271 539 N ATOM 2463 CA LEU A 292 -3.398 -22.322 10.213 1.00 20.91 C ANISOU 2463 CA LEU A 292 2586 2812 2548 287 243 496 C ATOM 2464 C LEU A 292 -4.297 -23.557 10.264 1.00 22.19 C ANISOU 2464 C LEU A 292 2737 3034 2660 265 210 476 C ATOM 2465 O LEU A 292 -3.842 -24.690 10.064 1.00 18.70 O ANISOU 2465 O LEU A 292 2295 2600 2209 232 187 441 O ATOM 2466 CB LEU A 292 -2.331 -22.431 11.299 1.00 18.13 C ANISOU 2466 CB LEU A 292 2260 2382 2247 264 228 453 C ATOM 2467 CG LEU A 292 -1.379 -21.236 11.400 1.00 20.31 C ANISOU 2467 CG LEU A 292 2547 2592 2580 279 258 463 C ATOM 2468 CD1 LEU A 292 -0.432 -21.394 12.571 1.00 16.41 C ANISOU 2468 CD1 LEU A 292 2076 2029 2132 255 238 417 C ATOM 2469 CD2 LEU A 292 -0.606 -21.064 10.098 1.00 21.98 C ANISOU 2469 CD2 LEU A 292 2743 2811 2799 285 281 483 C ATOM 2470 N VAL A 293 -5.577 -23.332 10.528 1.00 17.53 N ANISOU 2470 N VAL A 293 2137 2484 2039 282 211 499 N ATOM 2471 CA VAL A 293 -6.515 -24.428 10.739 1.00 15.85 C ANISOU 2471 CA VAL A 293 1914 2324 1784 259 183 480 C ATOM 2472 C VAL A 293 -7.551 -24.489 9.629 1.00 17.89 C ANISOU 2472 C VAL A 293 2138 2671 1988 274 188 512 C ATOM 2473 O VAL A 293 -8.038 -23.473 9.146 1.00 25.60 O ANISOU 2473 O VAL A 293 3101 3672 2953 314 215 559 O ATOM 2474 CB VAL A 293 -7.238 -24.317 12.112 1.00 18.48 C ANISOU 2474 CB VAL A 293 2261 2636 2124 261 173 474 C ATOM 2475 CG1 VAL A 293 -8.172 -25.501 12.336 1.00 25.32 C ANISOU 2475 CG1 VAL A 293 3117 3554 2952 235 146 454 C ATOM 2476 CG2 VAL A 293 -6.238 -24.232 13.244 1.00 19.51 C ANISOU 2476 CG2 VAL A 293 2425 2684 2304 249 166 441 C ATOM 2477 N SER A 294 -7.879 -25.702 9.231 1.00 20.35 N ANISOU 2477 N SER A 294 2436 3032 2265 243 163 486 N ATOM 2478 CA SER A 294 -8.859 -25.933 8.198 1.00 21.02 C ANISOU 2478 CA SER A 294 2485 3208 2293 251 162 507 C ATOM 2479 C SER A 294 -9.530 -27.226 8.589 1.00 20.12 C ANISOU 2479 C SER A 294 2365 3125 2155 211 130 469 C ATOM 2480 O SER A 294 -8.993 -27.968 9.403 1.00 17.73 O ANISOU 2480 O SER A 294 2085 2772 1880 179 113 429 O ATOM 2481 CB SER A 294 -8.160 -26.082 6.841 1.00 21.16 C ANISOU 2481 CB SER A 294 2491 3253 2297 251 170 509 C ATOM 2482 OG SER A 294 -7.153 -27.082 6.890 1.00 18.82 O ANISOU 2482 OG SER A 294 2212 2920 2020 212 152 460 O ATOM 2483 N PRO A 295 -10.704 -27.511 8.017 1.00 21.46 N ANISOU 2483 N PRO A 295 2501 3379 2275 212 123 482 N ATOM 2484 CA PRO A 295 -11.323 -28.808 8.297 1.00 18.83 C ANISOU 2484 CA PRO A 295 2159 3076 1921 169 94 443 C ATOM 2485 C PRO A 295 -10.376 -29.955 7.936 1.00 20.45 C ANISOU 2485 C PRO A 295 2376 3259 2134 128 78 394 C ATOM 2486 O PRO A 295 -10.314 -30.946 8.660 1.00 14.43 O ANISOU 2486 O PRO A 295 1628 2469 1386 91 59 355 O ATOM 2487 CB PRO A 295 -12.551 -28.812 7.380 1.00 22.58 C ANISOU 2487 CB PRO A 295 2590 3652 2339 180 92 467 C ATOM 2488 CG PRO A 295 -12.860 -27.352 7.173 1.00 26.98 C ANISOU 2488 CG PRO A 295 3137 4221 2891 236 121 526 C ATOM 2489 CD PRO A 295 -11.528 -26.673 7.123 1.00 23.95 C ANISOU 2489 CD PRO A 295 2783 3765 2551 253 141 533 C ATOM 2490 N GLU A 296 -9.656 -29.816 6.826 1.00 18.47 N ANISOU 2490 N GLU A 296 2120 3023 1876 136 87 397 N ATOM 2491 CA GLU A 296 -8.674 -30.821 6.409 1.00 15.13 C ANISOU 2491 CA GLU A 296 1709 2577 1461 102 76 353 C ATOM 2492 C GLU A 296 -7.577 -31.050 7.450 1.00 13.28 C ANISOU 2492 C GLU A 296 1514 2250 1283 86 72 326 C ATOM 2493 O GLU A 296 -7.228 -32.197 7.727 1.00 16.78 O ANISOU 2493 O GLU A 296 1970 2672 1736 49 55 283 O ATOM 2494 CB GLU A 296 -8.040 -30.457 5.067 1.00 19.47 C ANISOU 2494 CB GLU A 296 2248 3155 1995 121 91 368 C ATOM 2495 CG GLU A 296 -8.990 -30.591 3.886 1.00 19.29 C ANISOU 2495 CG GLU A 296 2186 3235 1909 128 88 381 C ATOM 2496 CD GLU A 296 -9.898 -29.395 3.724 1.00 31.25 C ANISOU 2496 CD GLU A 296 3677 4794 3401 175 106 439 C ATOM 2497 OE1 GLU A 296 -9.616 -28.335 4.327 1.00 25.80 O ANISOU 2497 OE1 GLU A 296 3005 4052 2747 206 127 472 O ATOM 2498 OE2 GLU A 296 -10.900 -29.522 2.985 1.00 30.89 O ANISOU 2498 OE2 GLU A 296 3596 4837 3302 180 99 450 O ATOM 2499 N ALA A 297 -7.042 -29.972 8.027 1.00 16.22 N ANISOU 2499 N ALA A 297 1903 2566 1692 115 89 351 N ATOM 2500 CA ALA A 297 -6.010 -30.101 9.067 1.00 15.01 C ANISOU 2500 CA ALA A 297 1784 2328 1591 103 84 326 C ATOM 2501 C ALA A 297 -6.546 -30.827 10.295 1.00 16.97 C ANISOU 2501 C ALA A 297 2045 2558 1845 80 64 302 C ATOM 2502 O ALA A 297 -5.874 -31.700 10.841 1.00 14.90 O ANISOU 2502 O ALA A 297 1803 2253 1605 52 50 265 O ATOM 2503 CB ALA A 297 -5.459 -28.741 9.470 1.00 10.57 C ANISOU 2503 CB ALA A 297 1235 1715 1066 138 106 356 C ATOM 2504 N LEU A 298 -7.753 -30.467 10.734 1.00 17.46 N ANISOU 2504 N LEU A 298 2095 2652 1887 92 65 325 N ATOM 2505 CA LEU A 298 -8.337 -31.094 11.918 1.00 15.81 C ANISOU 2505 CA LEU A 298 1897 2428 1682 73 49 307 C ATOM 2506 C LEU A 298 -8.621 -32.578 11.694 1.00 20.87 C ANISOU 2506 C LEU A 298 2531 3096 2304 30 30 270 C ATOM 2507 O LEU A 298 -8.366 -33.406 12.573 1.00 18.70 O ANISOU 2507 O LEU A 298 2276 2780 2048 6 17 240 O ATOM 2508 CB LEU A 298 -9.582 -30.348 12.392 1.00 15.69 C ANISOU 2508 CB LEU A 298 1869 2444 1650 99 58 342 C ATOM 2509 CG LEU A 298 -9.293 -28.912 12.841 1.00 17.81 C ANISOU 2509 CG LEU A 298 2152 2673 1945 141 79 374 C ATOM 2510 CD1 LEU A 298 -10.552 -28.260 13.397 1.00 17.28 C ANISOU 2510 CD1 LEU A 298 2073 2633 1860 166 87 406 C ATOM 2511 CD2 LEU A 298 -8.190 -28.912 13.876 1.00 21.82 C ANISOU 2511 CD2 LEU A 298 2695 3098 2499 134 73 348 C ATOM 2512 N ASP A 299 -9.107 -32.930 10.512 1.00 15.45 N ANISOU 2512 N ASP A 299 1816 2476 1580 21 28 269 N ATOM 2513 CA ASP A 299 -9.361 -34.332 10.236 1.00 17.28 C ANISOU 2513 CA ASP A 299 2040 2732 1795 -23 12 230 C ATOM 2514 C ASP A 299 -8.050 -35.116 10.185 1.00 20.94 C ANISOU 2514 C ASP A 299 2530 3141 2287 -46 7 192 C ATOM 2515 O ASP A 299 -7.965 -36.223 10.689 1.00 16.04 O ANISOU 2515 O ASP A 299 1922 2495 1677 -78 -5 159 O ATOM 2516 CB ASP A 299 -10.146 -34.524 8.940 1.00 20.75 C ANISOU 2516 CB ASP A 299 2441 3258 2184 -29 10 233 C ATOM 2517 CG ASP A 299 -10.443 -35.986 8.665 1.00 24.08 C ANISOU 2517 CG ASP A 299 2856 3703 2592 -78 -7 187 C ATOM 2518 OD1 ASP A 299 -11.171 -36.611 9.464 1.00 24.36 O ANISOU 2518 OD1 ASP A 299 2890 3735 2631 -101 -15 175 O ATOM 2519 OD2 ASP A 299 -9.942 -36.520 7.664 1.00 18.58 O ANISOU 2519 OD2 ASP A 299 2153 3024 1881 -94 -9 163 O ATOM 2520 N PHE A 300 -7.029 -34.531 9.572 1.00 13.76 N ANISOU 2520 N PHE A 300 1626 2212 1390 -26 18 201 N ATOM 2521 CA PHE A 300 -5.727 -35.197 9.463 1.00 12.88 C ANISOU 2521 CA PHE A 300 1537 2051 1306 -43 15 168 C ATOM 2522 C PHE A 300 -5.151 -35.408 10.852 1.00 13.21 C ANISOU 2522 C PHE A 300 1610 2020 1390 -48 8 155 C ATOM 2523 O PHE A 300 -4.756 -36.511 11.189 1.00 12.95 O ANISOU 2523 O PHE A 300 1592 1958 1369 -76 -2 121 O ATOM 2524 CB PHE A 300 -4.785 -34.367 8.607 1.00 13.01 C ANISOU 2524 CB PHE A 300 1551 2061 1330 -18 31 186 C ATOM 2525 CG PHE A 300 -3.400 -34.936 8.494 1.00 14.47 C ANISOU 2525 CG PHE A 300 1757 2196 1546 -31 31 157 C ATOM 2526 CD1 PHE A 300 -3.216 -36.289 8.269 1.00 13.16 C ANISOU 2526 CD1 PHE A 300 1596 2030 1374 -66 19 116 C ATOM 2527 CD2 PHE A 300 -2.289 -34.116 8.604 1.00 16.21 C ANISOU 2527 CD2 PHE A 300 1990 2367 1802 -9 43 171 C ATOM 2528 CE1 PHE A 300 -1.939 -36.818 8.150 1.00 18.29 C ANISOU 2528 CE1 PHE A 300 2265 2635 2051 -75 20 91 C ATOM 2529 CE2 PHE A 300 -1.004 -34.645 8.491 1.00 16.16 C ANISOU 2529 CE2 PHE A 300 1999 2317 1824 -20 42 145 C ATOM 2530 CZ PHE A 300 -0.837 -35.988 8.272 1.00 15.65 C ANISOU 2530 CZ PHE A 300 1940 2256 1751 -51 31 107 C ATOM 2531 N LEU A 301 -5.119 -34.352 11.659 1.00 13.73 N ANISOU 2531 N LEU A 301 1686 2056 1477 -20 15 181 N ATOM 2532 CA LEU A 301 -4.614 -34.454 13.029 1.00 12.83 C ANISOU 2532 CA LEU A 301 1600 1878 1398 -21 7 169 C ATOM 2533 C LEU A 301 -5.380 -35.517 13.809 1.00 14.49 C ANISOU 2533 C LEU A 301 1816 2092 1599 -47 -6 150 C ATOM 2534 O LEU A 301 -4.781 -36.352 14.497 1.00 13.42 O ANISOU 2534 O LEU A 301 1701 1913 1485 -64 -15 124 O ATOM 2535 CB LEU A 301 -4.721 -33.109 13.746 1.00 13.19 C ANISOU 2535 CB LEU A 301 1651 1901 1459 14 16 199 C ATOM 2536 CG LEU A 301 -4.337 -33.111 15.227 1.00 15.24 C ANISOU 2536 CG LEU A 301 1938 2102 1749 16 7 187 C ATOM 2537 CD1 LEU A 301 -2.839 -33.453 15.417 1.00 11.44 C ANISOU 2537 CD1 LEU A 301 1477 1565 1304 8 1 160 C ATOM 2538 CD2 LEU A 301 -4.686 -31.755 15.867 1.00 16.30 C ANISOU 2538 CD2 LEU A 301 2077 2224 1893 50 18 216 C ATOM 2539 N ASP A 302 -6.709 -35.476 13.696 1.00 11.08 N ANISOU 2539 N ASP A 302 1361 1712 1135 -48 -6 166 N ATOM 2540 CA ASP A 302 -7.570 -36.438 14.370 1.00 12.93 C ANISOU 2540 CA ASP A 302 1596 1956 1360 -74 -15 152 C ATOM 2541 C ASP A 302 -7.205 -37.876 14.023 1.00 14.36 C ANISOU 2541 C ASP A 302 1783 2130 1543 -113 -22 112 C ATOM 2542 O ASP A 302 -7.375 -38.778 14.838 1.00 14.26 O ANISOU 2542 O ASP A 302 1784 2093 1541 -133 -28 95 O ATOM 2543 CB ASP A 302 -9.031 -36.198 13.981 1.00 16.89 C ANISOU 2543 CB ASP A 302 2065 2528 1824 -72 -12 173 C ATOM 2544 CG ASP A 302 -9.992 -36.992 14.840 1.00 23.97 C ANISOU 2544 CG ASP A 302 2961 3431 2715 -94 -18 166 C ATOM 2545 OD1 ASP A 302 -9.848 -36.948 16.076 1.00 18.24 O ANISOU 2545 OD1 ASP A 302 2259 2659 2011 -86 -19 168 O ATOM 2546 OD2 ASP A 302 -10.873 -37.676 14.276 1.00 22.53 O ANISOU 2546 OD2 ASP A 302 2753 3300 2507 -121 -22 156 O ATOM 2547 N LYS A 303 -6.727 -38.090 12.798 1.00 13.25 N ANISOU 2547 N LYS A 303 1631 2011 1392 -122 -20 99 N ATOM 2548 CA LYS A 303 -6.422 -39.432 12.327 1.00 7.65 C ANISOU 2548 CA LYS A 303 926 1298 682 -159 -25 60 C ATOM 2549 C LYS A 303 -4.999 -39.873 12.681 1.00 10.87 C ANISOU 2549 C LYS A 303 1364 1639 1127 -160 -26 39 C ATOM 2550 O LYS A 303 -4.669 -41.047 12.555 1.00 12.84 O ANISOU 2550 O LYS A 303 1624 1871 1383 -188 -28 7 O ATOM 2551 CB LYS A 303 -6.667 -39.535 10.817 1.00 9.15 C ANISOU 2551 CB LYS A 303 1089 1550 838 -169 -23 52 C ATOM 2552 CG LYS A 303 -8.162 -39.570 10.453 1.00 15.23 C ANISOU 2552 CG LYS A 303 1826 2394 1569 -180 -27 61 C ATOM 2553 CD LYS A 303 -8.372 -39.403 8.956 1.00 24.26 C ANISOU 2553 CD LYS A 303 2940 3605 2674 -180 -25 59 C ATOM 2554 CE LYS A 303 -9.761 -39.859 8.543 1.00 23.95 C ANISOU 2554 CE LYS A 303 2866 3638 2595 -204 -33 52 C ATOM 2555 NZ LYS A 303 -10.780 -39.395 9.526 1.00 25.12 N ANISOU 2555 NZ LYS A 303 3006 3794 2744 -193 -34 80 N ATOM 2556 N LEU A 304 -4.166 -38.936 13.132 1.00 14.49 N ANISOU 2556 N LEU A 304 1836 2059 1609 -130 -23 57 N ATOM 2557 CA LEU A 304 -2.828 -39.277 13.625 1.00 14.62 C ANISOU 2557 CA LEU A 304 1880 2014 1663 -128 -25 39 C ATOM 2558 C LEU A 304 -2.880 -39.565 15.129 1.00 15.95 C ANISOU 2558 C LEU A 304 2070 2139 1851 -126 -33 38 C ATOM 2559 O LEU A 304 -2.313 -40.546 15.612 1.00 11.66 O ANISOU 2559 O LEU A 304 1546 1558 1326 -140 -37 16 O ATOM 2560 CB LEU A 304 -1.850 -38.131 13.367 1.00 11.76 C ANISOU 2560 CB LEU A 304 1518 1631 1319 -99 -19 56 C ATOM 2561 CG LEU A 304 -1.496 -37.772 11.918 1.00 12.22 C ANISOU 2561 CG LEU A 304 1558 1723 1363 -94 -8 61 C ATOM 2562 CD1 LEU A 304 -0.530 -36.593 11.885 1.00 14.93 C ANISOU 2562 CD1 LEU A 304 1903 2035 1732 -64 1 81 C ATOM 2563 CD2 LEU A 304 -0.901 -38.969 11.197 1.00 16.97 C ANISOU 2563 CD2 LEU A 304 2164 2322 1963 -119 -9 27 C ATOM 2564 N LEU A 305 -3.570 -38.698 15.863 1.00 9.26 N ANISOU 2564 N LEU A 305 1220 1298 999 -106 -33 64 N ATOM 2565 CA LEU A 305 -3.639 -38.809 17.314 1.00 8.11 C ANISOU 2565 CA LEU A 305 1096 1117 869 -98 -40 65 C ATOM 2566 C LEU A 305 -4.734 -39.772 17.778 1.00 13.02 C ANISOU 2566 C LEU A 305 1717 1756 1475 -121 -41 61 C ATOM 2567 O LEU A 305 -5.809 -39.345 18.230 1.00 14.69 O ANISOU 2567 O LEU A 305 1918 1992 1670 -114 -39 81 O ATOM 2568 CB LEU A 305 -3.798 -37.424 17.948 1.00 13.54 C ANISOU 2568 CB LEU A 305 1785 1799 1561 -65 -38 92 C ATOM 2569 CG LEU A 305 -2.624 -36.455 17.713 1.00 13.78 C ANISOU 2569 CG LEU A 305 1820 1801 1616 -43 -36 95 C ATOM 2570 CD1 LEU A 305 -2.843 -35.123 18.411 1.00 14.01 C ANISOU 2570 CD1 LEU A 305 1852 1819 1651 -12 -32 118 C ATOM 2571 CD2 LEU A 305 -1.271 -37.086 18.148 1.00 11.71 C ANISOU 2571 CD2 LEU A 305 1578 1487 1383 -48 -45 69 C ATOM 2572 N ARG A 306 -4.460 -41.066 17.633 1.00 11.77 N ANISOU 2572 N ARG A 306 1567 1583 1324 -149 -41 34 N ATOM 2573 CA ARG A 306 -5.316 -42.134 18.165 1.00 16.22 C ANISOU 2573 CA ARG A 306 2132 2149 1880 -174 -39 26 C ATOM 2574 C ARG A 306 -4.569 -42.875 19.267 1.00 15.18 C ANISOU 2574 C ARG A 306 2032 1960 1776 -171 -41 16 C ATOM 2575 O ARG A 306 -3.367 -43.138 19.130 1.00 12.13 O ANISOU 2575 O ARG A 306 1660 1539 1409 -168 -43 1 O ATOM 2576 CB ARG A 306 -5.685 -43.156 17.079 1.00 16.18 C ANISOU 2576 CB ARG A 306 2113 2173 1863 -213 -34 1 C ATOM 2577 CG ARG A 306 -5.997 -42.602 15.698 1.00 20.67 C ANISOU 2577 CG ARG A 306 2652 2797 2405 -216 -34 3 C ATOM 2578 CD ARG A 306 -7.187 -41.648 15.685 1.00 14.86 C ANISOU 2578 CD ARG A 306 1891 2113 1643 -202 -34 33 C ATOM 2579 NE ARG A 306 -8.367 -42.186 16.360 1.00 16.74 N ANISOU 2579 NE ARG A 306 2121 2366 1873 -219 -32 36 N ATOM 2580 CZ ARG A 306 -9.517 -41.524 16.470 1.00 23.86 C ANISOU 2580 CZ ARG A 306 3001 3313 2753 -210 -31 62 C ATOM 2581 NH1 ARG A 306 -9.652 -40.307 15.949 1.00 19.50 N ANISOU 2581 NH1 ARG A 306 2431 2794 2183 -181 -31 87 N ATOM 2582 NH2 ARG A 306 -10.539 -42.074 17.105 1.00 23.47 N ANISOU 2582 NH2 ARG A 306 2945 3276 2699 -227 -28 65 N ATOM 2583 N TYR A 307 -5.257 -43.228 20.356 1.00 15.70 N ANISOU 2583 N TYR A 307 2107 2017 1841 -171 -38 26 N ATOM 2584 CA TYR A 307 -4.615 -44.043 21.391 1.00 13.78 C ANISOU 2584 CA TYR A 307 1893 1724 1619 -167 -38 19 C ATOM 2585 C TYR A 307 -4.084 -45.320 20.743 1.00 16.10 C ANISOU 2585 C TYR A 307 2193 1998 1926 -196 -31 -9 C ATOM 2586 O TYR A 307 -2.914 -45.666 20.883 1.00 14.00 O ANISOU 2586 O TYR A 307 1946 1694 1681 -188 -34 -21 O ATOM 2587 CB TYR A 307 -5.608 -44.448 22.482 1.00 14.89 C ANISOU 2587 CB TYR A 307 2040 1865 1754 -169 -32 34 C ATOM 2588 CG TYR A 307 -5.969 -43.379 23.492 1.00 9.87 C ANISOU 2588 CG TYR A 307 1407 1232 1109 -135 -37 60 C ATOM 2589 CD1 TYR A 307 -4.993 -42.796 24.299 1.00 9.86 C ANISOU 2589 CD1 TYR A 307 1427 1198 1121 -102 -47 63 C ATOM 2590 CD2 TYR A 307 -7.291 -42.988 23.670 1.00 11.28 C ANISOU 2590 CD2 TYR A 307 1570 1450 1268 -135 -31 80 C ATOM 2591 CE1 TYR A 307 -5.319 -41.839 25.243 1.00 10.50 C ANISOU 2591 CE1 TYR A 307 1514 1283 1194 -71 -52 82 C ATOM 2592 CE2 TYR A 307 -7.634 -42.031 24.620 1.00 12.82 C ANISOU 2592 CE2 TYR A 307 1770 1647 1454 -103 -34 103 C ATOM 2593 CZ TYR A 307 -6.642 -41.463 25.399 1.00 11.41 C ANISOU 2593 CZ TYR A 307 1614 1433 1287 -71 -44 102 C ATOM 2594 OH TYR A 307 -6.962 -40.519 26.329 1.00 14.50 O ANISOU 2594 OH TYR A 307 2013 1826 1670 -39 -46 121 O ATOM 2595 N ASP A 308 -4.967 -46.017 20.031 1.00 11.03 N ANISOU 2595 N ASP A 308 1534 1385 1271 -231 -22 -21 N ATOM 2596 CA ASP A 308 -4.633 -47.309 19.425 1.00 9.46 C ANISOU 2596 CA ASP A 308 1342 1168 1084 -263 -13 -51 C ATOM 2597 C ASP A 308 -3.653 -47.133 18.271 1.00 10.89 C ANISOU 2597 C ASP A 308 1519 1351 1267 -263 -16 -70 C ATOM 2598 O ASP A 308 -4.006 -46.597 17.222 1.00 14.36 O ANISOU 2598 O ASP A 308 1934 1836 1686 -270 -19 -73 O ATOM 2599 CB ASP A 308 -5.909 -48.009 18.928 1.00 11.30 C ANISOU 2599 CB ASP A 308 1554 1435 1303 -304 -3 -63 C ATOM 2600 CG ASP A 308 -5.679 -49.471 18.592 1.00 19.77 C ANISOU 2600 CG ASP A 308 2640 2479 2394 -339 11 -95 C ATOM 2601 OD1 ASP A 308 -4.509 -49.861 18.416 1.00 16.78 O ANISOU 2601 OD1 ASP A 308 2280 2063 2033 -331 13 -109 O ATOM 2602 OD2 ASP A 308 -6.665 -50.237 18.523 1.00 17.40 O ANISOU 2602 OD2 ASP A 308 2329 2193 2091 -373 22 -105 O ATOM 2603 N HIS A 309 -2.412 -47.571 18.477 1.00 13.38 N ANISOU 2603 N HIS A 309 1857 1620 1607 -252 -15 -81 N ATOM 2604 CA HIS A 309 -1.360 -47.394 17.481 1.00 11.12 C ANISOU 2604 CA HIS A 309 1568 1331 1326 -248 -17 -96 C ATOM 2605 C HIS A 309 -1.730 -48.055 16.154 1.00 11.53 C ANISOU 2605 C HIS A 309 1605 1412 1363 -283 -9 -124 C ATOM 2606 O HIS A 309 -1.319 -47.593 15.094 1.00 16.33 O ANISOU 2606 O HIS A 309 2200 2045 1961 -280 -10 -131 O ATOM 2607 CB HIS A 309 -0.036 -47.950 17.998 1.00 10.39 C ANISOU 2607 CB HIS A 309 1501 1184 1263 -232 -16 -104 C ATOM 2608 CG HIS A 309 -0.130 -49.357 18.522 1.00 13.59 C ANISOU 2608 CG HIS A 309 1927 1553 1683 -250 -2 -116 C ATOM 2609 ND1 HIS A 309 -0.571 -49.655 19.796 1.00 12.91 N ANISOU 2609 ND1 HIS A 309 1855 1447 1604 -242 0 -99 N ATOM 2610 CD2 HIS A 309 0.165 -50.547 17.944 1.00 12.13 C ANISOU 2610 CD2 HIS A 309 1751 1347 1510 -274 13 -143 C ATOM 2611 CE1 HIS A 309 -0.528 -50.961 19.983 1.00 15.80 C ANISOU 2611 CE1 HIS A 309 2238 1779 1985 -260 17 -113 C ATOM 2612 NE2 HIS A 309 -0.077 -51.526 18.875 1.00 12.85 N ANISOU 2612 NE2 HIS A 309 1863 1404 1617 -280 25 -141 N ATOM 2613 N GLN A 310 -2.534 -49.116 16.221 1.00 12.00 N ANISOU 2613 N GLN A 310 1666 1472 1422 -316 2 -140 N ATOM 2614 CA GLN A 310 -2.998 -49.806 15.021 1.00 13.71 C ANISOU 2614 CA GLN A 310 1868 1719 1624 -353 9 -171 C ATOM 2615 C GLN A 310 -4.025 -48.983 14.230 1.00 17.52 C ANISOU 2615 C GLN A 310 2316 2272 2070 -361 0 -164 C ATOM 2616 O GLN A 310 -4.256 -49.246 13.056 1.00 21.80 O ANISOU 2616 O GLN A 310 2840 2851 2592 -384 2 -189 O ATOM 2617 CB GLN A 310 -3.604 -51.169 15.378 1.00 16.55 C ANISOU 2617 CB GLN A 310 2238 2055 1997 -389 24 -192 C ATOM 2618 CG GLN A 310 -2.585 -52.221 15.828 1.00 16.02 C ANISOU 2618 CG GLN A 310 2204 1920 1964 -387 38 -205 C ATOM 2619 CD GLN A 310 -3.238 -53.565 16.137 1.00 22.15 C ANISOU 2619 CD GLN A 310 2990 2670 2755 -424 58 -224 C ATOM 2620 OE1 GLN A 310 -4.403 -53.792 15.807 1.00 23.71 O ANISOU 2620 OE1 GLN A 310 3168 2903 2939 -458 61 -235 O ATOM 2621 NE2 GLN A 310 -2.486 -54.464 16.768 1.00 20.70 N ANISOU 2621 NE2 GLN A 310 2837 2425 2603 -417 74 -227 N ATOM 2622 N SER A 311 -4.638 -47.996 14.871 1.00 16.22 N ANISOU 2622 N SER A 311 2141 2129 1895 -339 -8 -131 N ATOM 2623 CA SER A 311 -5.673 -47.184 14.217 1.00 17.81 C ANISOU 2623 CA SER A 311 2308 2398 2062 -341 -15 -118 C ATOM 2624 C SER A 311 -5.134 -45.910 13.556 1.00 15.40 C ANISOU 2624 C SER A 311 1991 2118 1743 -308 -22 -100 C ATOM 2625 O SER A 311 -5.857 -45.220 12.819 1.00 16.17 O ANISOU 2625 O SER A 311 2060 2275 1809 -306 -25 -88 O ATOM 2626 CB SER A 311 -6.769 -46.814 15.222 1.00 19.97 C ANISOU 2626 CB SER A 311 2574 2685 2330 -335 -17 -91 C ATOM 2627 OG SER A 311 -7.411 -47.976 15.708 1.00 20.18 O ANISOU 2627 OG SER A 311 2604 2695 2367 -369 -7 -106 O ATOM 2628 N ARG A 312 -3.875 -45.584 13.820 1.00 11.53 N ANISOU 2628 N ARG A 312 1521 1583 1275 -282 -22 -94 N ATOM 2629 CA ARG A 312 -3.304 -44.364 13.260 1.00 17.36 C ANISOU 2629 CA ARG A 312 2250 2338 2007 -252 -25 -75 C ATOM 2630 C ARG A 312 -3.084 -44.494 11.766 1.00 12.80 C ANISOU 2630 C ARG A 312 1657 1798 1410 -263 -21 -94 C ATOM 2631 O ARG A 312 -2.858 -45.599 11.272 1.00 15.63 O ANISOU 2631 O ARG A 312 2022 2148 1770 -290 -16 -128 O ATOM 2632 CB ARG A 312 -1.983 -44.033 13.953 1.00 12.82 C ANISOU 2632 CB ARG A 312 1700 1705 1466 -225 -27 -68 C ATOM 2633 CG ARG A 312 -2.184 -43.790 15.439 1.00 12.41 C ANISOU 2633 CG ARG A 312 1664 1622 1430 -209 -32 -49 C ATOM 2634 CD ARG A 312 -0.857 -43.645 16.168 1.00 13.88 C ANISOU 2634 CD ARG A 312 1873 1754 1649 -186 -36 -49 C ATOM 2635 NE ARG A 312 -1.078 -43.857 17.599 1.00 12.13 N ANISOU 2635 NE ARG A 312 1669 1501 1438 -177 -41 -40 N ATOM 2636 CZ ARG A 312 -0.173 -44.318 18.446 1.00 11.88 C ANISOU 2636 CZ ARG A 312 1660 1422 1431 -166 -44 -46 C ATOM 2637 NH1 ARG A 312 1.061 -44.602 18.028 1.00 9.98 N ANISOU 2637 NH1 ARG A 312 1427 1155 1210 -163 -43 -61 N ATOM 2638 NH2 ARG A 312 -0.504 -44.481 19.718 1.00 11.43 N ANISOU 2638 NH2 ARG A 312 1618 1346 1378 -156 -47 -35 N ATOM 2639 N LEU A 313 -3.175 -43.369 11.050 1.00 14.10 N ANISOU 2639 N LEU A 313 1800 2003 1553 -241 -22 -71 N ATOM 2640 CA LEU A 313 -2.753 -43.316 9.651 1.00 13.97 C ANISOU 2640 CA LEU A 313 1771 2020 1518 -242 -16 -83 C ATOM 2641 C LEU A 313 -1.297 -43.773 9.547 1.00 14.85 C ANISOU 2641 C LEU A 313 1905 2078 1659 -238 -11 -101 C ATOM 2642 O LEU A 313 -0.465 -43.434 10.398 1.00 14.51 O ANISOU 2642 O LEU A 313 1880 1984 1648 -218 -12 -89 O ATOM 2643 CB LEU A 313 -2.831 -41.886 9.106 1.00 13.10 C ANISOU 2643 CB LEU A 313 1641 1947 1390 -208 -14 -46 C ATOM 2644 CG LEU A 313 -4.215 -41.294 8.842 1.00 17.71 C ANISOU 2644 CG LEU A 313 2195 2597 1936 -205 -17 -24 C ATOM 2645 CD1 LEU A 313 -4.074 -39.872 8.380 1.00 17.18 C ANISOU 2645 CD1 LEU A 313 2115 2554 1860 -166 -10 15 C ATOM 2646 CD2 LEU A 313 -4.961 -42.117 7.817 1.00 18.11 C ANISOU 2646 CD2 LEU A 313 2224 2707 1950 -236 -20 -53 C ATOM 2647 N THR A 314 -0.998 -44.537 8.503 1.00 12.49 N ANISOU 2647 N THR A 314 1604 1794 1347 -257 -5 -132 N ATOM 2648 CA THR A 314 0.385 -44.839 8.167 1.00 15.26 C ANISOU 2648 CA THR A 314 1972 2106 1721 -249 3 -146 C ATOM 2649 C THR A 314 0.949 -43.624 7.446 1.00 16.88 C ANISOU 2649 C THR A 314 2163 2332 1919 -217 9 -119 C ATOM 2650 O THR A 314 0.201 -42.717 7.059 1.00 11.64 O ANISOU 2650 O THR A 314 1478 1718 1229 -204 8 -94 O ATOM 2651 CB THR A 314 0.529 -46.097 7.268 1.00 16.89 C ANISOU 2651 CB THR A 314 2182 2319 1915 -279 11 -191 C ATOM 2652 OG1 THR A 314 -0.054 -45.862 5.979 1.00 15.50 O ANISOU 2652 OG1 THR A 314 1980 2213 1695 -285 12 -197 O ATOM 2653 CG2 THR A 314 -0.121 -47.312 7.914 1.00 12.26 C ANISOU 2653 CG2 THR A 314 1608 1713 1338 -314 9 -218 C ATOM 2654 N ALA A 315 2.263 -43.597 7.262 1.00 14.41 N ANISOU 2654 N ALA A 315 1862 1982 1632 -203 17 -122 N ATOM 2655 CA ALA A 315 2.883 -42.479 6.577 1.00 11.71 C ANISOU 2655 CA ALA A 315 1507 1654 1288 -174 26 -96 C ATOM 2656 C ALA A 315 2.349 -42.389 5.148 1.00 13.77 C ANISOU 2656 C ALA A 315 1746 1985 1503 -176 33 -99 C ATOM 2657 O ALA A 315 2.072 -41.307 4.662 1.00 14.51 O ANISOU 2657 O ALA A 315 1820 2115 1578 -154 38 -67 O ATOM 2658 CB ALA A 315 4.406 -42.618 6.578 1.00 10.32 C ANISOU 2658 CB ALA A 315 1345 1428 1148 -162 34 -103 C ATOM 2659 N ARG A 316 2.217 -43.531 4.478 1.00 14.39 N ANISOU 2659 N ARG A 316 1826 2080 1561 -203 34 -138 N ATOM 2660 CA ARG A 316 1.766 -43.531 3.102 1.00 18.76 C ANISOU 2660 CA ARG A 316 2358 2702 2067 -207 39 -146 C ATOM 2661 C ARG A 316 0.317 -43.045 3.017 1.00 17.86 C ANISOU 2661 C ARG A 316 2220 2652 1915 -210 29 -129 C ATOM 2662 O ARG A 316 0.001 -42.189 2.195 1.00 16.65 O ANISOU 2662 O ARG A 316 2043 2553 1728 -188 33 -104 O ATOM 2663 CB ARG A 316 1.921 -44.913 2.482 1.00 25.06 C ANISOU 2663 CB ARG A 316 3167 3502 2854 -238 42 -197 C ATOM 2664 CG ARG A 316 1.825 -44.912 0.976 1.00 32.68 C ANISOU 2664 CG ARG A 316 4112 4532 3771 -236 49 -210 C ATOM 2665 CD ARG A 316 3.045 -44.242 0.368 1.00 33.59 C ANISOU 2665 CD ARG A 316 4229 4636 3897 -202 66 -188 C ATOM 2666 NE ARG A 316 2.842 -43.924 -1.040 1.00 37.24 N ANISOU 2666 NE ARG A 316 4671 5171 4309 -190 74 -186 N ATOM 2667 CZ ARG A 316 3.233 -44.702 -2.043 1.00 39.95 C ANISOU 2667 CZ ARG A 316 5017 5533 4629 -200 83 -222 C ATOM 2668 NH1 ARG A 316 3.857 -45.844 -1.792 1.00 36.37 N ANISOU 2668 NH1 ARG A 316 4588 5028 4202 -222 86 -263 N ATOM 2669 NH2 ARG A 316 3.009 -44.330 -3.295 1.00 46.64 N ANISOU 2669 NH2 ARG A 316 5843 6452 5426 -185 89 -217 N ATOM 2670 N GLU A 317 -0.552 -43.563 3.883 1.00 20.72 N ANISOU 2670 N GLU A 317 2586 3006 2282 -234 16 -140 N ATOM 2671 CA GLU A 317 -1.939 -43.089 3.938 1.00 19.64 C ANISOU 2671 CA GLU A 317 2423 2926 2113 -236 7 -122 C ATOM 2672 C GLU A 317 -2.000 -41.611 4.239 1.00 15.69 C ANISOU 2672 C GLU A 317 1914 2432 1617 -196 10 -69 C ATOM 2673 O GLU A 317 -2.847 -40.895 3.708 1.00 19.26 O ANISOU 2673 O GLU A 317 2339 2946 2032 -182 10 -44 O ATOM 2674 CB GLU A 317 -2.733 -43.789 5.037 1.00 19.38 C ANISOU 2674 CB GLU A 317 2398 2870 2094 -264 -4 -136 C ATOM 2675 CG GLU A 317 -2.967 -45.256 4.850 1.00 18.62 C ANISOU 2675 CG GLU A 317 2310 2770 1996 -308 -5 -187 C ATOM 2676 CD GLU A 317 -3.789 -45.824 5.983 1.00 24.97 C ANISOU 2676 CD GLU A 317 3119 3551 2817 -333 -12 -193 C ATOM 2677 OE1 GLU A 317 -3.367 -45.717 7.160 1.00 16.99 O ANISOU 2677 OE1 GLU A 317 2131 2480 1844 -321 -11 -176 O ATOM 2678 OE2 GLU A 317 -4.874 -46.364 5.698 1.00 21.41 O ANISOU 2678 OE2 GLU A 317 2649 3145 2341 -364 -18 -214 O ATOM 2679 N ALA A 318 -1.136 -41.153 5.142 1.00 13.91 N ANISOU 2679 N ALA A 318 1709 2140 1436 -178 14 -52 N ATOM 2680 CA ALA A 318 -1.126 -39.745 5.506 1.00 12.13 C ANISOU 2680 CA ALA A 318 1478 1911 1221 -141 19 -5 C ATOM 2681 C ALA A 318 -0.857 -38.898 4.258 1.00 16.66 C ANISOU 2681 C ALA A 318 2032 2528 1770 -114 34 20 C ATOM 2682 O ALA A 318 -1.473 -37.841 4.053 1.00 18.18 O ANISOU 2682 O ALA A 318 2206 2758 1944 -89 39 58 O ATOM 2683 CB ALA A 318 -0.082 -39.474 6.606 1.00 13.18 C ANISOU 2683 CB ALA A 318 1636 1965 1407 -129 20 2 C ATOM 2684 N MET A 319 0.042 -39.376 3.402 1.00 13.28 N ANISOU 2684 N MET A 319 1609 2097 1340 -118 42 -1 N ATOM 2685 CA MET A 319 0.398 -38.630 2.205 1.00 15.25 C ANISOU 2685 CA MET A 319 1842 2386 1568 -90 59 23 C ATOM 2686 C MET A 319 -0.755 -38.553 1.207 1.00 16.72 C ANISOU 2686 C MET A 319 1998 2662 1692 -89 57 28 C ATOM 2687 O MET A 319 -0.764 -37.683 0.340 1.00 17.25 O ANISOU 2687 O MET A 319 2048 2772 1735 -59 71 62 O ATOM 2688 CB MET A 319 1.658 -39.205 1.554 1.00 16.77 C ANISOU 2688 CB MET A 319 2046 2553 1773 -94 70 -1 C ATOM 2689 CG MET A 319 2.863 -39.060 2.459 1.00 19.83 C ANISOU 2689 CG MET A 319 2457 2859 2220 -87 74 1 C ATOM 2690 SD MET A 319 4.299 -39.836 1.733 1.00 21.15 S ANISOU 2690 SD MET A 319 2636 2997 2402 -92 87 -28 S ATOM 2691 CE MET A 319 4.618 -38.655 0.434 1.00 20.13 C ANISOU 2691 CE MET A 319 2485 2914 2251 -54 112 13 C ATOM 2692 N GLU A 320 -1.739 -39.434 1.360 1.00 18.27 N ANISOU 2692 N GLU A 320 2188 2888 1865 -122 39 -2 N ATOM 2693 CA GLU A 320 -2.947 -39.395 0.526 1.00 21.93 C ANISOU 2693 CA GLU A 320 2621 3443 2270 -124 32 0 C ATOM 2694 C GLU A 320 -4.002 -38.417 1.050 1.00 20.65 C ANISOU 2694 C GLU A 320 2439 3308 2097 -104 29 44 C ATOM 2695 O GLU A 320 -5.022 -38.195 0.394 1.00 22.25 O ANISOU 2695 O GLU A 320 2613 3591 2252 -98 24 55 O ATOM 2696 CB GLU A 320 -3.581 -40.791 0.410 1.00 19.95 C ANISOU 2696 CB GLU A 320 2367 3214 1999 -172 16 -55 C ATOM 2697 CG GLU A 320 -2.645 -41.900 -0.076 1.00 21.28 C ANISOU 2697 CG GLU A 320 2555 3354 2176 -196 20 -104 C ATOM 2698 CD GLU A 320 -2.428 -41.879 -1.574 1.00 25.98 C ANISOU 2698 CD GLU A 320 3135 4013 2725 -184 28 -112 C ATOM 2699 OE1 GLU A 320 -3.383 -42.179 -2.317 1.00 26.11 O ANISOU 2699 OE1 GLU A 320 3125 4106 2690 -198 17 -130 O ATOM 2700 OE2 GLU A 320 -1.300 -41.574 -2.018 1.00 25.28 O ANISOU 2700 OE2 GLU A 320 3057 3898 2650 -161 45 -101 O ATOM 2701 N HIS A 321 -3.790 -37.843 2.231 1.00 16.18 N ANISOU 2701 N HIS A 321 1891 2681 1576 -91 31 67 N ATOM 2702 CA HIS A 321 -4.855 -37.050 2.866 1.00 16.84 C ANISOU 2702 CA HIS A 321 1960 2786 1652 -75 28 103 C ATOM 2703 C HIS A 321 -5.165 -35.716 2.170 1.00 15.40 C ANISOU 2703 C HIS A 321 1755 2652 1444 -30 44 156 C ATOM 2704 O HIS A 321 -4.260 -35.033 1.703 1.00 17.60 O ANISOU 2704 O HIS A 321 2040 2912 1736 -2 63 179 O ATOM 2705 CB HIS A 321 -4.550 -36.815 4.355 1.00 20.12 C ANISOU 2705 CB HIS A 321 2402 3122 2120 -74 27 110 C ATOM 2706 CG HIS A 321 -5.740 -36.367 5.147 1.00 22.62 C ANISOU 2706 CG HIS A 321 2707 3457 2429 -68 20 134 C ATOM 2707 ND1 HIS A 321 -6.159 -35.056 5.184 1.00 20.36 N ANISOU 2707 ND1 HIS A 321 2408 3190 2136 -29 33 183 N ATOM 2708 CD2 HIS A 321 -6.608 -37.059 5.924 1.00 15.63 C ANISOU 2708 CD2 HIS A 321 1822 2575 1542 -95 6 116 C ATOM 2709 CE1 HIS A 321 -7.231 -34.957 5.951 1.00 17.67 C ANISOU 2709 CE1 HIS A 321 2060 2864 1789 -31 25 194 C ATOM 2710 NE2 HIS A 321 -7.526 -36.159 6.410 1.00 16.05 N ANISOU 2710 NE2 HIS A 321 1861 2651 1587 -72 8 154 N ATOM 2711 N PRO A 322 -6.464 -35.339 2.099 1.00 15.12 N ANISOU 2711 N PRO A 322 1692 2681 1372 -21 39 179 N ATOM 2712 CA PRO A 322 -6.861 -34.059 1.493 1.00 17.97 C ANISOU 2712 CA PRO A 322 2030 3091 1707 26 56 234 C ATOM 2713 C PRO A 322 -6.088 -32.819 1.991 1.00 16.23 C ANISOU 2713 C PRO A 322 1828 2806 1531 65 79 277 C ATOM 2714 O PRO A 322 -5.974 -31.831 1.255 1.00 16.40 O ANISOU 2714 O PRO A 322 1838 2855 1540 104 101 320 O ATOM 2715 CB PRO A 322 -8.358 -33.961 1.843 1.00 17.98 C ANISOU 2715 CB PRO A 322 2006 3148 1679 25 44 248 C ATOM 2716 CG PRO A 322 -8.810 -35.382 1.890 1.00 19.75 C ANISOU 2716 CG PRO A 322 2225 3391 1887 -27 20 192 C ATOM 2717 CD PRO A 322 -7.634 -36.159 2.471 1.00 19.58 C ANISOU 2717 CD PRO A 322 2242 3282 1915 -55 18 153 C ATOM 2718 N TYR A 323 -5.571 -32.863 3.215 1.00 16.49 N ANISOU 2718 N TYR A 323 1891 2758 1617 53 76 266 N ATOM 2719 CA TYR A 323 -4.765 -31.771 3.760 1.00 19.60 C ANISOU 2719 CA TYR A 323 2303 3086 2058 83 96 297 C ATOM 2720 C TYR A 323 -3.636 -31.382 2.793 1.00 14.72 C ANISOU 2720 C TYR A 323 1687 2458 1449 101 117 308 C ATOM 2721 O TYR A 323 -3.253 -30.216 2.691 1.00 20.48 O ANISOU 2721 O TYR A 323 2418 3167 2198 136 142 349 O ATOM 2722 CB TYR A 323 -4.192 -32.201 5.125 1.00 20.93 C ANISOU 2722 CB TYR A 323 2503 3172 2277 59 84 267 C ATOM 2723 CG TYR A 323 -3.380 -31.170 5.892 1.00 15.71 C ANISOU 2723 CG TYR A 323 1862 2438 1668 83 99 289 C ATOM 2724 CD1 TYR A 323 -3.919 -29.938 6.247 1.00 17.09 C ANISOU 2724 CD1 TYR A 323 2033 2613 1849 117 115 332 C ATOM 2725 CD2 TYR A 323 -2.086 -31.461 6.319 1.00 13.12 C ANISOU 2725 CD2 TYR A 323 1558 2042 1386 70 98 264 C ATOM 2726 CE1 TYR A 323 -3.190 -29.012 6.976 1.00 11.61 C ANISOU 2726 CE1 TYR A 323 1357 1849 1204 134 129 346 C ATOM 2727 CE2 TYR A 323 -1.345 -30.546 7.037 1.00 14.16 C ANISOU 2727 CE2 TYR A 323 1706 2110 1566 87 109 278 C ATOM 2728 CZ TYR A 323 -1.894 -29.330 7.362 1.00 14.72 C ANISOU 2728 CZ TYR A 323 1772 2179 1642 118 125 317 C ATOM 2729 OH TYR A 323 -1.155 -28.436 8.087 1.00 20.27 O ANISOU 2729 OH TYR A 323 2491 2815 2394 132 137 326 O ATOM 2730 N PHE A 324 -3.130 -32.357 2.053 1.00 16.82 N ANISOU 2730 N PHE A 324 1952 2739 1698 78 110 273 N ATOM 2731 CA PHE A 324 -1.978 -32.112 1.191 1.00 15.81 C ANISOU 2731 CA PHE A 324 1829 2599 1581 93 130 280 C ATOM 2732 C PHE A 324 -2.346 -31.802 -0.260 1.00 18.98 C ANISOU 2732 C PHE A 324 2203 3083 1927 118 144 305 C ATOM 2733 O PHE A 324 -1.474 -31.587 -1.091 1.00 16.21 O ANISOU 2733 O PHE A 324 1852 2730 1578 134 164 315 O ATOM 2734 CB PHE A 324 -1.002 -33.283 1.274 1.00 16.75 C ANISOU 2734 CB PHE A 324 1968 2676 1722 58 119 228 C ATOM 2735 CG PHE A 324 -0.463 -33.499 2.651 1.00 20.78 C ANISOU 2735 CG PHE A 324 2504 3104 2287 41 108 208 C ATOM 2736 CD1 PHE A 324 0.399 -32.571 3.222 1.00 16.26 C ANISOU 2736 CD1 PHE A 324 1945 2468 1765 61 123 231 C ATOM 2737 CD2 PHE A 324 -0.835 -34.611 3.389 1.00 17.22 C ANISOU 2737 CD2 PHE A 324 2065 2641 1838 5 84 168 C ATOM 2738 CE1 PHE A 324 0.892 -32.759 4.513 1.00 16.20 C ANISOU 2738 CE1 PHE A 324 1961 2390 1805 46 111 211 C ATOM 2739 CE2 PHE A 324 -0.345 -34.809 4.679 1.00 18.85 C ANISOU 2739 CE2 PHE A 324 2295 2775 2091 -8 74 152 C ATOM 2740 CZ PHE A 324 0.518 -33.880 5.239 1.00 14.78 C ANISOU 2740 CZ PHE A 324 1792 2201 1621 14 86 173 C ATOM 2741 N TYR A 325 -3.640 -31.739 -0.563 1.00 17.95 N ANISOU 2741 N TYR A 325 2046 3027 1746 125 136 319 N ATOM 2742 CA TYR A 325 -4.043 -31.424 -1.931 1.00 15.72 C ANISOU 2742 CA TYR A 325 1735 2831 1405 153 147 345 C ATOM 2743 C TYR A 325 -3.513 -30.063 -2.388 1.00 12.87 C ANISOU 2743 C TYR A 325 1373 2459 1059 203 184 405 C ATOM 2744 O TYR A 325 -3.205 -29.881 -3.565 1.00 16.53 O ANISOU 2744 O TYR A 325 1823 2967 1490 226 201 422 O ATOM 2745 CB TYR A 325 -5.573 -31.458 -2.087 1.00 14.31 C ANISOU 2745 CB TYR A 325 1526 2738 1173 155 131 354 C ATOM 2746 CG TYR A 325 -6.212 -32.828 -2.011 1.00 20.03 C ANISOU 2746 CG TYR A 325 2244 3497 1871 106 98 296 C ATOM 2747 CD1 TYR A 325 -5.448 -33.994 -2.001 1.00 19.25 C ANISOU 2747 CD1 TYR A 325 2165 3360 1788 65 86 239 C ATOM 2748 CD2 TYR A 325 -7.596 -32.953 -1.962 1.00 22.59 C ANISOU 2748 CD2 TYR A 325 2540 3890 2154 100 81 298 C ATOM 2749 CE1 TYR A 325 -6.046 -35.240 -1.933 1.00 20.90 C ANISOU 2749 CE1 TYR A 325 2369 3596 1976 19 60 186 C ATOM 2750 CE2 TYR A 325 -8.199 -34.184 -1.891 1.00 27.87 C ANISOU 2750 CE2 TYR A 325 3201 4588 2802 52 53 245 C ATOM 2751 CZ TYR A 325 -7.429 -35.321 -1.881 1.00 26.19 C ANISOU 2751 CZ TYR A 325 3010 4334 2608 12 44 188 C ATOM 2752 OH TYR A 325 -8.061 -36.536 -1.807 1.00 27.33 O ANISOU 2752 OH TYR A 325 3146 4503 2734 -37 19 135 O ATOM 2753 N THR A 326 -3.391 -29.112 -1.460 1.00 15.82 N ANISOU 2753 N THR A 326 1759 2771 1481 221 198 436 N ATOM 2754 CA THR A 326 -2.988 -27.758 -1.836 1.00 16.96 C ANISOU 2754 CA THR A 326 1901 2899 1642 269 237 495 C ATOM 2755 C THR A 326 -1.467 -27.636 -2.033 1.00 18.62 C ANISOU 2755 C THR A 326 2131 3045 1900 268 257 490 C ATOM 2756 O THR A 326 -0.991 -26.698 -2.669 1.00 21.52 O ANISOU 2756 O THR A 326 2492 3408 2275 305 292 536 O ATOM 2757 CB THR A 326 -3.486 -26.697 -0.831 1.00 29.18 C ANISOU 2757 CB THR A 326 3456 4409 3224 290 248 532 C ATOM 2758 OG1 THR A 326 -3.153 -25.386 -1.308 1.00 35.24 O ANISOU 2758 OG1 THR A 326 4219 5164 4006 338 289 591 O ATOM 2759 CG2 THR A 326 -2.859 -26.906 0.515 1.00 29.96 C ANISOU 2759 CG2 THR A 326 3584 4414 3386 261 236 498 C ATOM 2760 N VAL A 327 -0.729 -28.608 -1.516 1.00 15.81 N ANISOU 2760 N VAL A 327 1794 2639 1573 228 237 437 N ATOM 2761 CA VAL A 327 0.736 -28.637 -1.653 1.00 15.17 C ANISOU 2761 CA VAL A 327 1730 2498 1538 223 252 426 C ATOM 2762 C VAL A 327 1.175 -28.987 -3.077 1.00 17.69 C ANISOU 2762 C VAL A 327 2035 2869 1817 233 266 427 C ATOM 2763 O VAL A 327 0.740 -29.990 -3.643 1.00 20.21 O ANISOU 2763 O VAL A 327 2346 3246 2086 214 245 394 O ATOM 2764 CB VAL A 327 1.344 -29.628 -0.666 1.00 17.41 C ANISOU 2764 CB VAL A 327 2036 2718 1860 179 226 370 C ATOM 2765 CG1 VAL A 327 2.856 -29.734 -0.874 1.00 19.37 C ANISOU 2765 CG1 VAL A 327 2296 2912 2151 175 241 358 C ATOM 2766 CG2 VAL A 327 1.035 -29.193 0.754 1.00 19.91 C ANISOU 2766 CG2 VAL A 327 2366 2980 2217 174 216 372 C ATOM 2767 N VAL A 328 2.033 -28.154 -3.662 1.00 15.51 N ANISOU 2767 N VAL A 328 1758 2572 1563 263 302 465 N ATOM 2768 CA VAL A 328 2.514 -28.395 -5.019 1.00 20.21 C ANISOU 2768 CA VAL A 328 2342 3216 2122 278 319 471 C ATOM 2769 C VAL A 328 3.404 -29.626 -5.074 1.00 24.03 C ANISOU 2769 C VAL A 328 2840 3675 2617 242 303 413 C ATOM 2770 O VAL A 328 4.365 -29.737 -4.311 1.00 19.02 O ANISOU 2770 O VAL A 328 2223 2961 2042 223 302 393 O ATOM 2771 CB VAL A 328 3.305 -27.190 -5.582 1.00 25.81 C ANISOU 2771 CB VAL A 328 3047 3900 2860 319 367 528 C ATOM 2772 CG1 VAL A 328 4.060 -27.595 -6.842 1.00 29.17 C ANISOU 2772 CG1 VAL A 328 3465 4360 3257 329 384 526 C ATOM 2773 CG2 VAL A 328 2.381 -26.013 -5.863 1.00 23.63 C ANISOU 2773 CG2 VAL A 328 2754 3665 2560 364 390 591 C ATOM 2774 N LYS A 329 3.092 -30.536 -5.991 1.00 24.47 N ANISOU 2774 N LYS A 329 2886 3800 2612 233 290 385 N ATOM 2775 CA LYS A 329 3.924 -31.719 -6.204 1.00 36.96 C ANISOU 2775 CA LYS A 329 4481 5363 4199 202 279 332 C ATOM 2776 C LYS A 329 4.956 -31.494 -7.318 1.00 37.65 C ANISOU 2776 C LYS A 329 4564 5459 4282 228 313 351 C ATOM 2777 O LYS A 329 6.148 -31.770 -7.146 1.00 41.50 O ANISOU 2777 O LYS A 329 5066 5887 4816 217 322 333 O ATOM 2778 CB LYS A 329 3.054 -32.936 -6.528 1.00 43.00 C ANISOU 2778 CB LYS A 329 5240 6192 4905 173 248 282 C ATOM 2779 CG LYS A 329 1.943 -33.186 -5.519 1.00 44.23 C ANISOU 2779 CG LYS A 329 5397 6349 5060 148 217 265 C ATOM 2780 CD LYS A 329 2.471 -33.174 -4.088 1.00 41.48 C ANISOU 2780 CD LYS A 329 5072 5904 4783 128 208 253 C ATOM 2781 CE LYS A 329 1.384 -33.590 -3.102 1.00 39.67 C ANISOU 2781 CE LYS A 329 4845 5678 4551 101 178 232 C ATOM 2782 NZ LYS A 329 0.137 -32.776 -3.236 1.00 36.68 N ANISOU 2782 NZ LYS A 329 4443 5359 4134 126 179 273 N TER 2783 LYS A 329 HETATM 2784 N1 FU9 A 338 23.421 -29.478 10.420 1.00 19.97 N HETATM 2785 C2 FU9 A 338 23.434 -28.488 11.339 1.00 19.82 C HETATM 2786 N3 FU9 A 338 23.310 -28.750 12.649 1.00 16.65 N HETATM 2787 C4 FU9 A 338 23.185 -30.006 13.072 1.00 14.99 C HETATM 2788 C5 FU9 A 338 23.147 -31.045 12.151 1.00 13.79 C HETATM 2789 C6 FU9 A 338 23.287 -30.744 10.797 1.00 17.01 C HETATM 2790 OAA FU9 A 338 22.464 -36.547 15.342 1.00 13.61 O HETATM 2791 OAB FU9 A 338 22.086 -37.214 13.268 1.00 16.32 O HETATM 2792 FAC FU9 A 338 24.116 -31.123 20.289 1.00 37.04 F HETATM 2793 FAD FU9 A 338 22.009 -30.950 20.696 1.00 39.25 F HETATM 2794 FAE FU9 A 338 22.714 -32.258 19.128 1.00 40.80 F HETATM 2795 CAF FU9 A 338 22.594 -27.556 18.409 1.00 18.66 C HETATM 2796 CAG FU9 A 338 22.777 -27.761 17.049 1.00 19.72 C HETATM 2797 CAH FU9 A 338 22.658 -28.643 19.269 1.00 16.31 C HETATM 2798 CAI FU9 A 338 22.800 -34.725 12.202 1.00 10.51 C HETATM 2799 CAJ FU9 A 338 22.968 -33.433 11.721 1.00 13.22 C HETATM 2800 CAL FU9 A 338 22.973 -30.130 17.400 1.00 17.88 C HETATM 2801 CAM FU9 A 338 22.708 -33.870 14.448 1.00 13.89 C HETATM 2802 CAN FU9 A 338 23.500 -24.762 11.531 1.00 23.65 C HETATM 2803 CAO FU9 A 338 24.834 -25.307 12.063 1.00 31.24 C HETATM 2804 NAQ FU9 A 338 22.885 -31.520 14.849 1.00 14.98 N HETATM 2805 NAS FU9 A 338 22.985 -29.154 15.196 1.00 14.12 N HETATM 2806 NAT FU9 A 338 23.580 -27.216 10.980 1.00 21.94 N HETATM 2807 CAU FU9 A 338 22.486 -36.365 14.101 1.00 15.99 C HETATM 2808 CAV FU9 A 338 22.877 -29.044 16.527 1.00 14.02 C HETATM 2809 CAW FU9 A 338 22.708 -34.950 13.574 1.00 15.52 C HETATM 2810 CAX FU9 A 338 22.843 -29.925 18.771 1.00 18.91 C HETATM 2811 CAZ FU9 A 338 23.093 -30.247 14.432 1.00 14.63 C HETATM 2812 CBA FU9 A 338 22.874 -32.568 13.978 1.00 14.78 C HETATM 2813 CBB FU9 A 338 22.996 -32.352 12.609 1.00 12.09 C HETATM 2814 CBE FU9 A 338 23.598 -26.197 12.040 1.00 24.43 C HETATM 2815 CBF FU9 A 338 22.914 -31.103 19.747 1.00 33.36 C HETATM 2816 S SO4 A 339 16.994 -48.427 23.467 1.00 56.37 S HETATM 2817 O1 SO4 A 339 18.081 -47.592 22.948 1.00 54.07 O HETATM 2818 O2 SO4 A 339 16.573 -49.386 22.452 1.00 44.10 O HETATM 2819 O3 SO4 A 339 17.449 -49.155 24.652 1.00 62.33 O HETATM 2820 O4 SO4 A 339 15.862 -47.573 23.827 1.00 55.64 O HETATM 2821 S SO4 A 340 12.335 -41.463 29.821 1.00 55.41 S HETATM 2822 O1 SO4 A 340 12.524 -41.505 28.365 1.00 49.11 O HETATM 2823 O2 SO4 A 340 11.605 -42.648 30.264 1.00 51.42 O HETATM 2824 O3 SO4 A 340 13.642 -41.420 30.480 1.00 56.91 O HETATM 2825 O4 SO4 A 340 11.578 -40.268 30.194 1.00 53.41 O HETATM 2826 S SO4 A 341 -8.673 -44.194 19.555 1.00 20.92 S HETATM 2827 O1 SO4 A 341 -8.890 -44.407 18.118 1.00 26.24 O HETATM 2828 O2 SO4 A 341 -9.987 -44.244 20.203 1.00 24.61 O HETATM 2829 O3 SO4 A 341 -7.781 -45.264 20.045 1.00 17.72 O HETATM 2830 O4 SO4 A 341 -8.117 -42.851 19.768 1.00 12.17 O HETATM 2831 S SO4 A 342 16.660 -32.532 -1.544 1.00 60.53 S HETATM 2832 O1 SO4 A 342 18.092 -32.240 -1.608 1.00 60.37 O HETATM 2833 O2 SO4 A 342 16.008 -31.860 -2.665 1.00 66.82 O HETATM 2834 O3 SO4 A 342 16.445 -33.972 -1.635 1.00 60.76 O HETATM 2835 O4 SO4 A 342 16.083 -32.057 -0.290 1.00 56.69 O HETATM 2836 C1 PEG A 343 11.944 -32.966 28.991 1.00 56.31 C HETATM 2837 O1 PEG A 343 11.298 -31.707 29.225 1.00 56.67 O HETATM 2838 C2 PEG A 343 11.484 -33.531 27.650 1.00 53.96 C HETATM 2839 O2 PEG A 343 12.178 -34.752 27.413 1.00 55.88 O HETATM 2840 C3 PEG A 343 11.570 -35.803 28.154 1.00 52.84 C HETATM 2841 C4 PEG A 343 12.333 -37.112 28.003 1.00 49.96 C HETATM 2842 O4 PEG A 343 11.995 -37.950 29.120 1.00 53.07 O HETATM 2843 C1 EDO A 344 36.720 -34.839 14.137 1.00 36.42 C HETATM 2844 O1 EDO A 344 37.874 -34.042 13.843 1.00 41.78 O HETATM 2845 C2 EDO A 344 37.172 -36.201 14.636 1.00 35.03 C HETATM 2846 O2 EDO A 344 38.187 -36.015 15.626 1.00 42.78 O HETATM 2847 C1 EDO A 345 19.415 -27.579 15.641 1.00 36.05 C HETATM 2848 O1 EDO A 345 18.612 -26.416 15.884 1.00 36.30 O HETATM 2849 C2 EDO A 345 18.554 -28.838 15.673 1.00 30.48 C HETATM 2850 O2 EDO A 345 17.199 -28.530 15.316 1.00 26.54 O HETATM 2851 C1 EDO A 346 46.096 -32.820 6.362 1.00 34.89 C HETATM 2852 O1 EDO A 346 45.187 -33.876 6.713 1.00 41.33 O HETATM 2853 C2 EDO A 346 46.688 -33.074 4.975 1.00 39.51 C HETATM 2854 O2 EDO A 346 47.830 -33.946 5.050 1.00 29.68 O HETATM 2855 C1 EDO A 347 -3.512 -28.782 24.927 1.00 31.45 C HETATM 2856 O1 EDO A 347 -4.315 -28.235 25.980 1.00 34.75 O HETATM 2857 C2 EDO A 347 -3.161 -30.226 25.258 1.00 23.02 C HETATM 2858 O2 EDO A 347 -2.455 -30.258 26.501 1.00 28.27 O HETATM 2859 C1 EDO A 348 13.925 -26.745 12.537 1.00 30.67 C HETATM 2860 O1 EDO A 348 15.064 -26.455 11.710 1.00 27.06 O HETATM 2861 C2 EDO A 348 14.326 -27.670 13.686 1.00 28.04 C HETATM 2862 O2 EDO A 348 15.184 -26.970 14.593 1.00 34.93 O HETATM 2863 C1 EDO A 349 13.940 -31.689 22.311 1.00 39.56 C HETATM 2864 O1 EDO A 349 14.512 -30.521 21.707 1.00 45.99 O HETATM 2865 C2 EDO A 349 13.327 -31.365 23.668 1.00 44.54 C HETATM 2866 O2 EDO A 349 12.614 -32.504 24.166 1.00 44.84 O HETATM 2867 C1 EDO A 350 10.835 -28.583 23.200 1.00 32.95 C HETATM 2868 O1 EDO A 350 9.779 -27.664 23.502 1.00 33.08 O HETATM 2869 C2 EDO A 350 10.240 -29.859 22.616 1.00 31.46 C HETATM 2870 O2 EDO A 350 9.881 -29.645 21.243 1.00 32.80 O HETATM 2871 C1 EDO A 351 20.986 -23.426 13.465 1.00 52.38 C HETATM 2872 O1 EDO A 351 20.721 -22.062 13.812 1.00 57.95 O HETATM 2873 C2 EDO A 351 20.228 -24.368 14.395 1.00 49.78 C HETATM 2874 O2 EDO A 351 20.793 -24.356 15.712 1.00 46.66 O HETATM 2875 C1 EDO A 352 -13.220 -35.583 18.281 1.00 37.90 C HETATM 2876 O1 EDO A 352 -13.664 -35.017 17.031 1.00 39.89 O HETATM 2877 C2 EDO A 352 -11.932 -36.382 18.091 1.00 40.36 C HETATM 2878 O2 EDO A 352 -12.190 -37.673 17.506 1.00 34.29 O HETATM 2879 O HOH A 353 8.987 -40.871 17.285 1.00 11.54 O HETATM 2880 O HOH A 354 19.887 -46.447 16.454 1.00 14.49 O HETATM 2881 O HOH A 355 2.911 -32.739 22.505 1.00 12.91 O HETATM 2882 O HOH A 356 17.796 -55.912 14.153 1.00 18.39 O HETATM 2883 O HOH A 357 3.501 -48.348 17.810 1.00 12.78 O HETATM 2884 O HOH A 358 4.072 -45.639 8.010 1.00 15.13 O HETATM 2885 O HOH A 359 5.129 -56.420 16.508 1.00 14.96 O HETATM 2886 O HOH A 360 2.642 -49.571 11.395 1.00 16.54 O HETATM 2887 O HOH A 361 6.648 -54.967 18.038 1.00 14.45 O HETATM 2888 O HOH A 362 2.678 -37.208 23.829 1.00 13.76 O HETATM 2889 O HOH A 363 -12.542 -41.011 25.190 1.00 13.06 O HETATM 2890 O HOH A 364 3.806 -30.836 20.403 1.00 14.14 O HETATM 2891 O HOH A 365 3.656 -45.923 5.361 1.00 14.29 O HETATM 2892 O HOH A 366 22.685 -41.517 5.775 1.00 15.45 O HETATM 2893 O HOH A 367 10.733 -37.427 20.575 1.00 19.09 O HETATM 2894 O HOH A 368 2.780 -53.781 16.835 1.00 14.74 O HETATM 2895 O HOH A 369 14.426 -50.921 22.150 1.00 20.60 O HETATM 2896 O HOH A 370 21.855 -39.865 13.360 1.00 13.76 O HETATM 2897 O HOH A 371 42.009 -38.747 25.405 1.00 17.57 O HETATM 2898 O HOH A 372 -4.465 -31.544 28.119 1.00 19.13 O HETATM 2899 O HOH A 373 4.265 -54.914 26.848 1.00 23.39 O HETATM 2900 O HOH A 374 17.533 -39.711 18.780 1.00 16.97 O HETATM 2901 O HOH A 375 0.699 -45.713 11.723 1.00 17.36 O HETATM 2902 O HOH A 376 2.793 -46.915 10.393 1.00 16.79 O HETATM 2903 O HOH A 377 -14.155 -40.349 27.563 1.00 15.62 O HETATM 2904 O HOH A 378 20.975 -39.402 2.890 1.00 21.54 O HETATM 2905 O HOH A 379 9.134 -41.397 0.598 1.00 19.48 O HETATM 2906 O HOH A 380 -4.935 -25.756 7.552 1.00 18.32 O HETATM 2907 O HOH A 381 21.984 -35.285 17.697 1.00 18.29 O HETATM 2908 O HOH A 382 0.274 -51.267 14.343 1.00 18.60 O HETATM 2909 O HOH A 383 -1.149 -47.631 12.399 1.00 21.52 O HETATM 2910 O HOH A 384 0.018 -50.293 11.987 1.00 20.34 O HETATM 2911 O HOH A 385 39.348 -42.611 11.751 1.00 16.81 O HETATM 2912 O HOH A 386 -7.995 -37.924 17.848 1.00 14.71 O HETATM 2913 O HOH A 387 37.834 -39.677 5.231 1.00 20.11 O HETATM 2914 O HOH A 388 -6.813 -42.787 11.904 1.00 13.63 O HETATM 2915 O HOH A 389 11.369 -28.600 13.194 1.00 21.39 O HETATM 2916 O HOH A 390 -3.234 -56.930 17.914 1.00 24.53 O HETATM 2917 O HOH A 391 -1.347 -35.492 36.694 1.00 18.42 O HETATM 2918 O HOH A 392 1.543 -47.653 4.618 1.00 22.24 O HETATM 2919 O HOH A 393 22.234 -57.364 15.694 1.00 32.79 O HETATM 2920 O HOH A 394 16.303 -42.005 16.506 1.00 16.12 O HETATM 2921 O HOH A 395 14.367 -37.035 22.773 1.00 24.20 O HETATM 2922 O HOH A 396 5.423 -24.868 -3.326 1.00 20.38 O HETATM 2923 O HOH A 397 -9.125 -46.712 21.995 1.00 19.61 O HETATM 2924 O HOH A 398 -1.139 -18.620 6.435 1.00 21.33 O HETATM 2925 O HOH A 399 -11.422 -52.354 23.775 1.00 22.96 O HETATM 2926 O HOH A 400 -7.604 -26.782 3.277 1.00 21.94 O HETATM 2927 O HOH A 401 -13.582 -42.892 31.940 1.00 19.54 O HETATM 2928 O HOH A 402 21.093 -26.219 3.957 1.00 23.45 O HETATM 2929 O HOH A 403 43.640 -41.818 21.066 1.00 21.26 O HETATM 2930 O HOH A 404 6.222 -31.065 0.101 1.00 21.88 O HETATM 2931 O HOH A 405 5.926 -29.808 19.127 1.00 25.17 O HETATM 2932 O HOH A 406 10.860 -50.969 28.444 1.00 23.36 O HETATM 2933 O HOH A 407 23.244 -54.092 4.147 1.00 23.70 O HETATM 2934 O HOH A 408 26.114 -50.905 5.506 1.00 23.66 O HETATM 2935 O HOH A 409 -2.706 -21.923 21.212 1.00 21.27 O HETATM 2936 O HOH A 410 0.774 -42.278 -0.412 1.00 29.93 O HETATM 2937 O HOH A 411 23.379 -41.136 19.237 1.00 27.98 O HETATM 2938 O HOH A 412 -10.318 -16.170 19.802 1.00 21.17 O HETATM 2939 O HOH A 413 -7.632 -14.724 21.421 1.00 24.65 O HETATM 2940 O HOH A 414 -15.121 -30.129 22.991 1.00 31.12 O HETATM 2941 O HOH A 415 5.720 -44.137 32.363 1.00 32.89 O HETATM 2942 O HOH A 416 -1.666 -25.760 8.506 1.00 20.16 O HETATM 2943 O HOH A 417 17.143 -26.886 19.125 1.00 29.81 O HETATM 2944 O HOH A 418 -4.114 -29.928 30.383 1.00 26.31 O HETATM 2945 O HOH A 419 4.413 -46.642 34.675 1.00 32.14 O HETATM 2946 O HOH A 420 10.164 -56.549 9.469 1.00 21.53 O HETATM 2947 O HOH A 421 41.959 -41.303 14.987 1.00 24.00 O HETATM 2948 O HOH A 422 -5.506 -28.983 0.729 1.00 24.63 O HETATM 2949 O HOH A 423 -4.991 -46.372 9.146 1.00 30.81 O HETATM 2950 O HOH A 424 27.660 -30.729 4.215 1.00 29.30 O HETATM 2951 O HOH A 425 -21.404 -41.199 36.611 1.00 27.34 O HETATM 2952 O HOH A 426 -2.740 -35.777 -0.544 1.00 20.22 O HETATM 2953 O HOH A 427 -8.719 -49.412 21.249 1.00 29.92 O HETATM 2954 O HOH A 428 16.577 -35.947 0.068 1.00 21.27 O HETATM 2955 O HOH A 429 3.162 -42.870 31.959 1.00 22.42 O HETATM 2956 O HOH A 430 -8.147 -43.271 9.276 1.00 29.09 O HETATM 2957 O HOH A 431 31.321 -36.279 22.820 1.00 34.85 O HETATM 2958 O HOH A 432 23.663 -61.490 5.037 1.00 37.50 O HETATM 2959 O HOH A 433 9.789 -37.458 31.225 1.00 36.24 O HETATM 2960 O HOH A 434 2.995 -25.731 25.757 1.00 31.26 O HETATM 2961 O HOH A 435 -7.586 -40.501 5.760 1.00 22.37 O HETATM 2962 O HOH A 436 -13.460 -28.763 3.650 1.00 41.17 O HETATM 2963 O HOH A 437 -14.286 -47.573 28.134 1.00 28.78 O HETATM 2964 O HOH A 438 8.992 -23.871 21.291 1.00 31.83 O HETATM 2965 O HOH A 439 -11.063 -51.070 21.222 1.00 32.01 O HETATM 2966 O HOH A 440 40.192 -26.924 14.795 1.00 25.66 O HETATM 2967 O HOH A 441 8.846 -52.049 29.945 1.00 35.68 O HETATM 2968 O HOH A 442 -9.323 -46.912 17.430 1.00 22.12 O HETATM 2969 O HOH A 443 24.442 -44.374 18.580 1.00 28.11 O HETATM 2970 O HOH A 444 -4.785 -23.809 21.307 1.00 23.80 O HETATM 2971 O HOH A 445 0.403 -42.968 -3.612 1.00 25.15 O HETATM 2972 O HOH A 446 -7.421 -35.680 36.038 1.00 23.99 O HETATM 2973 O HOH A 447 30.472 -48.622 8.290 1.00 27.71 O HETATM 2974 O HOH A 448 24.588 -23.891 18.696 1.00 39.99 O HETATM 2975 O HOH A 449 -4.227 -19.079 5.923 1.00 25.82 O HETATM 2976 O HOH A 450 -16.376 -33.756 16.087 1.00 26.91 O HETATM 2977 O HOH A 451 -5.542 -40.836 3.692 1.00 26.34 O HETATM 2978 O HOH A 452 -13.062 -33.825 34.162 1.00 25.66 O HETATM 2979 O HOH A 453 2.877 -40.653 -2.024 1.00 36.34 O HETATM 2980 O HOH A 454 8.408 -43.660 28.127 1.00 26.95 O HETATM 2981 O HOH A 455 23.336 -24.450 16.087 1.00 23.85 O HETATM 2982 O HOH A 456 -6.877 -38.794 -1.320 1.00 29.85 O HETATM 2983 O HOH A 457 6.574 -42.217 0.161 1.00 32.59 O HETATM 2984 O HOH A 458 4.250 -56.808 24.850 1.00 29.79 O HETATM 2985 O HOH A 459 18.670 -36.527 1.628 1.00 41.68 O HETATM 2986 O HOH A 460 2.731 -37.384 38.612 1.00 40.20 O HETATM 2987 O HOH A 461 -8.272 -42.805 6.840 1.00 21.73 O HETATM 2988 O HOH A 462 29.512 -44.707 6.245 1.00 30.57 O HETATM 2989 O HOH A 463 13.783 -31.554 1.480 1.00 26.91 O HETATM 2990 O HOH A 464 19.473 -40.454 20.444 1.00 32.00 O HETATM 2991 O HOH A 465 -12.156 -44.554 18.915 1.00 26.17 O HETATM 2992 O HOH A 466 33.404 -34.346 22.535 1.00 40.28 O HETATM 2993 O HOH A 467 24.614 -42.885 20.996 1.00 27.93 O HETATM 2994 O HOH A 468 0.554 -47.234 33.162 1.00 31.37 O HETATM 2995 O HOH A 469 -9.790 -34.492 20.818 1.00 32.61 O HETATM 2996 O HOH A 470 2.873 -47.067 32.777 1.00 36.55 O HETATM 2997 O HOH A 471 -5.167 -15.793 12.654 1.00 33.66 O HETATM 2998 O HOH A 472 22.380 -51.519 3.454 1.00 30.05 O HETATM 2999 O HOH A 473 -4.059 -51.031 37.829 1.00 36.69 O HETATM 3000 O HOH A 474 -4.934 -46.758 37.318 1.00 29.20 O HETATM 3001 O HOH A 475 -3.943 -35.056 37.565 1.00 26.44 O HETATM 3002 O HOH A 476 42.444 -43.224 16.922 1.00 30.61 O HETATM 3003 O HOH A 477 -1.280 -39.304 -3.392 1.00 28.50 O HETATM 3004 O HOH A 478 -13.624 -53.509 28.381 1.00 31.89 O HETATM 3005 O HOH A 479 36.688 -36.539 3.451 1.00 40.64 O HETATM 3006 O HOH A 480 -11.940 -46.797 21.061 1.00 26.59 O HETATM 3007 O HOH A 481 39.690 -30.436 14.892 1.00 22.81 O HETATM 3008 O HOH A 482 -12.156 -35.922 36.712 1.00 31.35 O HETATM 3009 O HOH A 483 11.129 -59.699 22.041 1.00 28.91 O HETATM 3010 O HOH A 484 -12.156 -36.058 12.025 1.00 31.53 O HETATM 3011 O HOH A 485 0.691 -35.685 38.432 1.00 29.26 O HETATM 3012 O HOH A 486 -15.249 -28.824 25.276 1.00 33.35 O HETATM 3013 O HOH A 487 -17.117 -32.681 26.885 1.00 29.66 O HETATM 3014 O HOH A 488 16.588 -54.905 16.453 1.00 26.49 O HETATM 3015 O HOH A 489 25.439 -56.069 9.491 1.00 29.14 O HETATM 3016 O HOH A 490 45.408 -39.758 7.676 1.00 36.57 O HETATM 3017 O HOH A 491 31.016 -52.455 6.147 1.00 49.61 O HETATM 3018 O HOH A 492 -11.225 -39.951 12.195 1.00 30.54 O HETATM 3019 O HOH A 493 -8.669 -30.348 26.891 1.00 32.98 O HETATM 3020 O HOH A 494 -8.812 -56.960 28.616 1.00 38.66 O HETATM 3021 O HOH A 495 5.944 -56.460 28.158 1.00 42.20 O HETATM 3022 O HOH A 496 -6.596 -51.753 8.705 1.00 41.18 O HETATM 3023 O HOH A 497 -11.037 -26.208 3.618 1.00 44.65 O HETATM 3024 O HOH A 498 -3.234 -43.681 42.897 1.00 42.07 O HETATM 3025 O HOH A 499 42.432 -41.227 10.656 1.00 32.84 O HETATM 3026 O HOH A 500 31.718 -33.575 2.882 1.00 31.86 O HETATM 3027 O HOH A 501 -9.625 -34.728 37.096 1.00 31.70 O HETATM 3028 O HOH A 502 9.199 -52.110 1.314 1.00 40.53 O HETATM 3029 O HOH A 503 20.046 -49.891 1.955 1.00 31.41 O HETATM 3030 O HOH A 504 41.837 -42.981 12.600 1.00 27.78 O HETATM 3031 O HOH A 505 -7.323 -50.590 14.907 1.00 28.55 O HETATM 3032 O HOH A 506 -7.186 -53.302 30.877 1.00 26.87 O HETATM 3033 O HOH A 507 9.388 -39.697 -1.489 1.00 30.55 O HETATM 3034 O HOH A 508 -13.871 -42.218 18.577 1.00 29.56 O HETATM 3035 O HOH A 509 -1.937 -55.736 13.465 1.00 31.56 O HETATM 3036 O HOH A 510 -12.295 -43.120 34.267 1.00 42.79 O HETATM 3037 O HOH A 511 15.669 -52.821 21.172 1.00 28.09 O HETATM 3038 O HOH A 512 -3.645 -30.545 32.931 1.00 29.39 O HETATM 3039 O HOH A 513 10.723 -61.471 14.569 1.00 35.50 O HETATM 3040 O HOH A 514 43.133 -41.011 23.974 1.00 24.97 O HETATM 3041 O HOH A 515 12.327 -58.376 -0.032 1.00 33.37 O HETATM 3042 O HOH A 516 13.442 -35.011 -1.078 1.00 51.72 O HETATM 3043 O HOH A 517 -11.705 -27.740 1.000 1.00 36.49 O HETATM 3044 O HOH A 518 -5.860 -42.693 -1.803 1.00 34.88 O HETATM 3045 O HOH A 519 17.950 -53.316 22.670 1.00 34.24 O HETATM 3046 O HOH A 520 19.622 -57.566 15.677 1.00 37.57 O HETATM 3047 O HOH A 521 -8.882 -41.271 44.550 1.00 47.56 O HETATM 3048 O HOH A 522 -13.228 -50.239 28.060 1.00 33.31 O HETATM 3049 O HOH A 523 0.028 -51.910 36.102 1.00 34.92 O HETATM 3050 O HOH A 524 -1.579 -21.597 23.731 1.00 34.19 O HETATM 3051 O HOH A 525 11.834 -60.657 -0.713 1.00 33.81 O HETATM 3052 O HOH A 526 22.340 -29.992 3.535 1.00 33.35 O HETATM 3053 O HOH A 527 -6.869 -48.041 6.855 1.00 44.06 O HETATM 3054 O HOH A 528 25.428 -25.634 4.585 1.00 36.24 O HETATM 3055 O HOH A 529 5.592 -46.281 30.843 1.00 37.42 O HETATM 3056 O HOH A 530 34.118 -44.081 5.974 1.00 42.31 O HETATM 3057 O HOH A 531 -9.727 -36.677 19.920 1.00 29.57 O HETATM 3058 O HOH A 532 41.958 -44.391 20.994 1.00 32.80 O HETATM 3059 O HOH A 533 29.946 -25.609 2.803 1.00 31.26 O HETATM 3060 O HOH A 534 -16.297 -31.170 13.532 1.00 36.73 O HETATM 3061 O HOH A 535 20.135 -21.628 3.369 1.00 36.24 O HETATM 3062 O HOH A 536 -5.726 -12.160 15.693 1.00 35.86 O HETATM 3063 O HOH A 537 15.438 -64.473 6.272 1.00 47.94 O HETATM 3064 O HOH A 538 25.336 -60.721 15.449 1.00 44.65 O HETATM 3065 O HOH A 539 36.246 -51.381 12.114 1.00 43.19 O HETATM 3066 O HOH A 540 -10.406 -12.657 12.914 1.00 44.14 O HETATM 3067 O HOH A 541 -4.024 -57.459 32.035 1.00 29.96 O HETATM 3068 O HOH A 542 -9.628 -39.050 4.423 1.00 40.58 O HETATM 3069 O HOH A 543 -11.825 -18.407 15.845 1.00 43.15 O HETATM 3070 O HOH A 544 29.965 -49.690 5.661 1.00 36.88 O HETATM 3071 O HOH A 545 1.589 -17.726 10.004 1.00 34.66 O HETATM 3072 O HOH A 546 24.998 -45.095 0.252 1.00 45.15 O HETATM 3073 O HOH A 547 40.331 -25.921 4.480 1.00 43.50 O HETATM 3074 O HOH A 548 -9.017 -49.318 18.607 1.00 42.10 O HETATM 3075 O HOH A 549 -17.098 -27.192 24.175 1.00 24.07 O HETATM 3076 O HOH A 550 -11.582 -32.895 30.824 1.00 37.29 O HETATM 3077 O HOH A 551 -13.016 -49.345 20.451 1.00 33.16 O HETATM 3078 O HOH A 552 14.318 -55.182 21.070 1.00 30.29 O HETATM 3079 O HOH A 553 -2.595 -32.555 34.139 1.00 32.88 O HETATM 3080 O HOH A 554 11.397 -33.436 -1.627 1.00 36.25 O HETATM 3081 O HOH A 555 18.931 -45.870 1.296 1.00 29.31 O HETATM 3082 O HOH A 556 -8.316 -12.231 22.397 1.00 34.91 O HETATM 3083 O HOH A 557 4.166 -56.597 4.985 1.00 33.50 O HETATM 3084 O HOH A 558 0.796 -49.582 32.362 1.00 41.85 O HETATM 3085 O HOH A 559 -11.599 -18.937 20.443 1.00 44.26 O HETATM 3086 O HOH A 560 1.785 -52.390 30.681 1.00 27.95 O HETATM 3087 O HOH A 561 4.156 -23.647 16.847 1.00 36.00 O HETATM 3088 O HOH A 562 18.500 -51.548 0.573 1.00 33.29 O HETATM 3089 O HOH A 563 -14.599 -49.080 30.299 1.00 37.03 O HETATM 3090 O HOH A 564 33.863 -30.493 24.531 1.00 34.27 O HETATM 3091 O HOH A 565 19.680 -40.421 -3.506 1.00 41.55 O HETATM 3092 O HOH A 566 -7.157 -47.993 35.960 1.00 30.89 O HETATM 3093 O HOH A 567 -5.034 -24.078 23.853 1.00 41.10 O HETATM 3094 O HOH A 568 29.486 -55.523 7.750 1.00 38.26 O HETATM 3095 O HOH A 569 -7.865 -50.118 38.360 1.00 46.08 O HETATM 3096 O HOH A 570 25.449 -60.897 9.766 1.00 50.64 O HETATM 3097 O HOH A 571 5.339 -41.809 -1.955 1.00 41.56 O HETATM 3098 O HOH A 572 10.026 -51.195 32.720 1.00 36.14 O HETATM 3099 O HOH A 573 -3.816 -27.684 28.935 1.00 48.98 O HETATM 3100 O HOH A 574 -3.764 -62.391 26.213 1.00 54.21 O HETATM 3101 O HOH A 575 18.609 -20.792 13.803 1.00 29.57 O HETATM 3102 O HOH A 576 -5.911 -50.429 39.984 1.00 31.27 O HETATM 3103 O HOH A 577 10.886 -54.346 1.006 1.00 27.43 O HETATM 3104 O HOH A 578 7.886 -43.712 33.472 1.00 40.79 O HETATM 3105 O HOH A 579 21.565 -56.109 3.123 1.00 31.07 O HETATM 3106 O HOH A 580 26.921 -54.949 7.785 1.00 38.95 O HETATM 3107 O HOH A 581 5.219 -37.752 -3.409 1.00 31.63 O HETATM 3108 O HOH A 582 23.543 -26.288 2.871 1.00 38.05 O HETATM 3109 O HOH A 583 -3.752 -37.691 -3.065 1.00 35.09 O HETATM 3110 O HOH A 584 33.644 -52.199 13.564 1.00 32.43 O HETATM 3111 O HOH A 585 12.975 -52.583 28.329 1.00 38.29 O HETATM 3112 O HOH A 586 -7.329 -46.771 9.945 1.00 38.33 O HETATM 3113 O HOH A 587 15.709 -24.026 20.958 1.00 37.85 O HETATM 3114 O HOH A 588 -6.695 -29.987 28.212 1.00 41.24 O HETATM 3115 O HOH A 589 2.114 -60.305 23.873 1.00 41.47 O HETATM 3116 O HOH A 590 -12.107 -36.412 39.559 1.00 33.57 O HETATM 3117 O HOH A 591 0.659 -37.607 -2.181 1.00 38.27 O HETATM 3118 O HOH A 592 -7.474 -11.257 19.867 1.00 38.67 O HETATM 3119 O HOH A 593 -0.958 -57.855 30.505 1.00 37.24 O HETATM 3120 O HOH A 594 8.309 -39.434 34.616 1.00 28.39 O HETATM 3121 O HOH A 595 7.165 -48.266 31.823 1.00 40.15 O HETATM 3122 O HOH A 596 9.210 -44.839 30.298 1.00 42.43 O HETATM 3123 O HOH A 597 38.333 -41.802 3.751 1.00 44.38 O HETATM 3124 O HOH A 598 11.855 -49.430 30.513 1.00 44.09 O HETATM 3125 O HOH A 599 -13.199 -49.022 17.846 1.00 43.38 O HETATM 3126 O HOH A 600 -12.130 -33.036 13.150 1.00 41.24 O HETATM 3127 O HOH A 601 2.030 -54.408 28.689 1.00 33.15 O HETATM 3128 O HOH A 602 12.591 -52.701 2.190 1.00 31.39 O HETATM 3129 O HOH A 603 -22.838 -42.228 38.659 1.00 41.52 O HETATM 3130 O HOH A 604 43.553 -46.577 21.223 1.00 39.70 O HETATM 3131 O HOH A 605 21.818 -33.439 0.661 1.00 34.62 O HETATM 3132 O HOH A 606 6.823 -39.637 -2.417 1.00 38.12 O HETATM 3133 O HOH A 607 -2.702 -45.750 44.276 1.00 48.77 O HETATM 3134 O HOH A 608 -11.272 -31.729 1.446 1.00 39.82 O HETATM 3135 O HOH A 609 32.326 -24.884 9.038 1.00 38.28 O HETATM 3136 O HOH A 610 35.295 -25.089 -1.615 1.00 49.23 O HETATM 3137 O HOH A 611 7.698 -50.635 34.147 1.00 44.01 O HETATM 3138 O HOH A 612 9.908 -34.472 35.583 1.00 42.93 O HETATM 3139 O HOH A 613 37.928 -49.254 7.995 1.00 33.32 O HETATM 3140 O HOH A 614 23.152 -26.273 22.215 1.00 41.20 O HETATM 3141 O HOH A 615 41.285 -28.672 16.660 1.00 35.58 O HETATM 3142 O HOH A 616 20.942 -32.581 17.029 1.00 26.57 O HETATM 3143 O HOH A 617 22.035 -38.838 19.645 1.00 32.26 O HETATM 3144 O HOH A 618 12.202 -30.676 19.997 1.00 14.82 O HETATM 3145 O HOH A 619 14.373 -33.985 25.464 1.00 38.59 O HETATM 3146 O HOH A 620 43.061 -34.427 4.985 1.00 35.88 O HETATM 3147 O HOH A 621 -0.776 -29.421 28.143 1.00 20.64 O HETATM 3148 O HOH A 622 3.095 -22.818 13.914 1.00 27.75 O HETATM 3149 O HOH A 623 9.209 -20.408 16.731 1.00 38.23 O HETATM 3150 O HOH A 624 3.905 -62.107 18.929 1.00 27.78 O HETATM 3151 O HOH A 625 -0.182 -59.831 16.492 1.00 25.49 O HETATM 3152 O HOH A 626 19.234 -38.595 0.745 1.00 35.60 O HETATM 3153 O HOH A 627 9.452 -30.821 34.123 1.00 45.46 O HETATM 3154 O HOH A 628 -12.153 -25.558 0.203 1.00 36.58 O HETATM 3155 O HOH A 629 12.513 -56.905 2.268 1.00 32.28 O HETATM 3156 O HOH A 630 12.552 -43.701 -2.672 1.00 39.41 O HETATM 3157 O HOH A 631 24.894 -50.854 2.690 1.00 47.58 O HETATM 3158 O HOH A 632 16.843 -21.855 7.294 1.00 31.74 O HETATM 3159 O HOH A 633 6.043 -30.978 -2.727 1.00 40.43 O HETATM 3160 O HOH A 634 44.817 -28.772 11.400 1.00 34.20 O HETATM 3161 O HOH A 635 23.360 -38.250 -0.120 1.00 35.95 O HETATM 3162 O HOH A 636 23.070 -35.013 20.269 1.00 37.93 O HETATM 3163 O HOH A 637 -1.905 -57.581 15.499 1.00 37.08 O HETATM 3164 O HOH A 638 -7.143 -62.724 28.374 1.00 43.76 O HETATM 3165 O HOH A 639 -6.909 -22.965 3.883 1.00 36.99 O HETATM 3166 O HOH A 640 35.774 -34.414 23.348 1.00 45.32 O HETATM 3167 O HOH A 641 -12.621 -31.610 10.278 1.00 33.08 O HETATM 3168 O HOH A 642 -13.569 -36.962 14.949 1.00 39.45 O HETATM 3169 O HOH A 643 40.843 -44.553 18.615 1.00 34.61 O HETATM 3170 O HOH A 644 15.373 -14.592 15.843 1.00 43.78 O HETATM 3171 O HOH A 645 -6.338 -22.228 6.340 1.00 37.51 O HETATM 3172 O HOH A 646 -8.097 -20.886 7.364 1.00 46.49 O HETATM 3173 O HOH A 647 -1.390 -14.623 14.431 1.00 40.72 O HETATM 3174 O HOH A 648 12.668 -60.723 16.841 1.00 38.81 O HETATM 3175 O HOH A 649 19.780 -34.799 -1.808 1.00 38.64 O HETATM 3176 O HOH A 650 4.401 -40.543 40.978 1.00 43.07 O HETATM 3177 O HOH A 651 9.323 -46.983 31.784 1.00 53.17 O HETATM 3178 O HOH A 652 -17.525 -43.561 33.887 1.00 35.48 O HETATM 3179 O HOH A 653 25.803 -54.363 3.372 1.00 35.60 O HETATM 3180 O HOH A 654 42.827 -26.398 5.086 1.00 36.77 O HETATM 3181 O HOH A 655 15.340 -43.345 -2.787 1.00 43.07 O HETATM 3182 O HOH A 656 42.969 -31.562 10.198 1.00 36.97 O HETATM 3183 O HOH A 657 33.204 -51.226 16.085 1.00 54.54 O HETATM 3184 O HOH A 658 -5.037 -26.627 34.398 1.00 49.78 O HETATM 3185 O HOH A 659 -1.910 -34.521 -2.811 1.00 41.69 O HETATM 3186 O HOH A 660 32.752 -37.926 24.216 1.00 43.13 O HETATM 3187 O HOH A 661 17.955 -18.788 10.146 1.00 40.71 O HETATM 3188 O HOH A 662 41.125 -44.687 9.088 1.00 40.62 O HETATM 3189 O HOH A 663 14.143 -18.449 8.697 1.00 44.61 O HETATM 3190 O HOH A 664 32.632 -23.638 3.736 1.00 42.30 O HETATM 3191 O HOH A 665 43.601 -34.187 12.677 1.00 38.07 O HETATM 3192 O HOH A 666 44.029 -39.282 13.971 1.00 36.52 O HETATM 3193 O HOH A 667 4.442 -61.705 9.312 1.00 43.23 O HETATM 3194 O HOH A 668 -6.223 -27.476 27.565 1.00 57.32 O HETATM 3195 O HOH A 669 25.591 -23.039 3.959 1.00 49.88 O HETATM 3196 O HOH A 670 10.349 -47.112 -0.137 1.00 39.41 O HETATM 3197 O HOH A 671 16.192 -62.081 7.266 1.00 49.49 O HETATM 3198 O HOH A 672 11.988 -17.990 10.583 1.00 43.35 O HETATM 3199 O HOH A 673 33.949 -53.866 15.617 1.00 53.72 O HETATM 3200 O HOH A 674 -4.454 -28.624 36.023 1.00 55.78 O HETATM 3201 O HOH A 675 -13.092 -20.997 17.495 1.00 45.73 O HETATM 3202 O HOH A 676 38.424 -43.378 18.884 1.00 48.49 O HETATM 3203 O HOH A 677 17.663 -51.580 24.458 1.00 49.03 O HETATM 3204 O HOH A 678 -0.956 -26.433 28.785 1.00 40.13 O HETATM 3205 O HOH A 679 -12.680 -40.260 17.294 1.00 35.21 O HETATM 3206 O HOH A 680 11.973 -60.029 11.207 1.00 40.14 O HETATM 3207 O HOH A 681 10.583 -20.475 2.116 1.00 36.94 O HETATM 3208 O HOH A 682 -16.460 -32.838 24.455 1.00 31.74 O HETATM 3209 O HOH A 683 11.946 -31.462 32.508 1.00 41.88 O HETATM 3210 O HOH A 684 17.725 -33.871 21.326 1.00 31.82 O HETATM 3211 O HOH A 685 17.274 -36.842 20.894 1.00 39.21 O HETATM 3212 O HOH A 686 18.354 -35.010 19.012 1.00 27.88 O CONECT 2784 2785 2789 CONECT 2785 2784 2786 2806 CONECT 2786 2785 2787 CONECT 2787 2786 2788 2811 CONECT 2788 2787 2789 2813 CONECT 2789 2784 2788 CONECT 2790 2807 CONECT 2791 2807 CONECT 2792 2815 CONECT 2793 2815 CONECT 2794 2815 CONECT 2795 2796 2797 CONECT 2796 2795 2808 CONECT 2797 2795 2810 CONECT 2798 2799 2809 CONECT 2799 2798 2813 CONECT 2800 2808 2810 CONECT 2801 2809 2812 CONECT 2802 2803 2814 CONECT 2803 2802 2814 CONECT 2804 2811 2812 CONECT 2805 2808 2811 CONECT 2806 2785 2814 CONECT 2807 2790 2791 2809 CONECT 2808 2796 2800 2805 CONECT 2809 2798 2801 2807 CONECT 2810 2797 2800 2815 CONECT 2811 2787 2804 2805 CONECT 2812 2801 2804 2813 CONECT 2813 2788 2799 2812 CONECT 2814 2802 2803 2806 CONECT 2815 2792 2793 2794 2810 CONECT 2816 2817 2818 2819 2820 CONECT 2817 2816 CONECT 2818 2816 CONECT 2819 2816 CONECT 2820 2816 CONECT 2821 2822 2823 2824 2825 CONECT 2822 2821 CONECT 2823 2821 CONECT 2824 2821 CONECT 2825 2821 CONECT 2826 2827 2828 2829 2830 CONECT 2827 2826 CONECT 2828 2826 CONECT 2829 2826 CONECT 2830 2826 CONECT 2831 2832 2833 2834 2835 CONECT 2832 2831 CONECT 2833 2831 CONECT 2834 2831 CONECT 2835 2831 CONECT 2836 2837 2838 CONECT 2837 2836 CONECT 2838 2836 2839 CONECT 2839 2838 2840 CONECT 2840 2839 2841 CONECT 2841 2840 2842 CONECT 2842 2841 CONECT 2843 2844 2845 CONECT 2844 2843 CONECT 2845 2843 2846 CONECT 2846 2845 CONECT 2847 2848 2849 CONECT 2848 2847 CONECT 2849 2847 2850 CONECT 2850 2849 CONECT 2851 2852 2853 CONECT 2852 2851 CONECT 2853 2851 2854 CONECT 2854 2853 CONECT 2855 2856 2857 CONECT 2856 2855 CONECT 2857 2855 2858 CONECT 2858 2857 CONECT 2859 2860 2861 CONECT 2860 2859 CONECT 2861 2859 2862 CONECT 2862 2861 CONECT 2863 2864 2865 CONECT 2864 2863 CONECT 2865 2863 2866 CONECT 2866 2865 CONECT 2867 2868 2869 CONECT 2868 2867 CONECT 2869 2867 2870 CONECT 2870 2869 CONECT 2871 2872 2873 CONECT 2872 2871 CONECT 2873 2871 2874 CONECT 2874 2873 CONECT 2875 2876 2877 CONECT 2876 2875 CONECT 2877 2875 2878 CONECT 2878 2877 MASTER 473 0 15 20 9 0 32 6 3194 1 95 26 END