Browse entries in the PDBbind-CN Database
HEADER RNA/RNA BINDING PROTEIN 08-OCT-09 3K64 TITLE CRYSTAL STRUCTURE OF FBF-2/FEM-3 PME COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: FEM-3 MRNA-BINDING FACTOR 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 164-575, RNA-BINDING DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 5'-R(*UP*GP*UP*GP*UP*CP*AP*UP*U)-3'; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS; SOURCE 3 ORGANISM_COMMON: NEMATODE; SOURCE 4 ORGANISM_TAXID: 6239; SOURCE 5 GENE: F21H12.5, FBF-2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES KEYWDS FBF, FEM-3 BINDING FACTOR, PUF, RNA-BINDING SPECIFICITY, KEYWDS 2 BASE FLIPPING, BASE STACKING EXPDTA X-RAY DIFFRACTION AUTHOR Y.WANG,L.OPPERMAN,M.WICKENS,T.M.T.HALL REVDAT 2 22-DEC-09 3K64 1 JRNL REVDAT 1 03-NOV-09 3K64 0 JRNL AUTH Y.WANG,L.OPPERMAN,M.WICKENS,T.M.HALL JRNL TITL STRUCTURAL BASIS FOR SPECIFIC RECOGNITION OF JRNL TITL 2 MULTIPLE MRNA TARGETS BY A PUF REGULATORY PROTEIN. JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 20186 2009 JRNL REFN ISSN 0027-8424 JRNL PMID 19901328 JRNL DOI 10.1073/PNAS.0812076106 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX.REFINE REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.32 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 36362 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.152 REMARK 3 FREE R VALUE : 0.191 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1845 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.92 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A AND RESID 168:193 REMARK 3 ORIGIN FOR THE GROUP (A): 22.0054 -2.5161 -30.5641 REMARK 3 T TENSOR REMARK 3 T11: 0.4280 T22: 0.3313 REMARK 3 T33: 0.3258 T12: 0.0124 REMARK 3 T13: -0.1219 T23: 0.2209 REMARK 3 L TENSOR REMARK 3 L11: 0.3875 L22: 0.3803 REMARK 3 L33: 2.8032 L12: -0.6079 REMARK 3 L13: 0.1868 L23: 0.4400 REMARK 3 S TENSOR REMARK 3 S11: 0.2327 S12: 0.7077 S13: 0.5420 REMARK 3 S21: -1.0606 S22: 0.3211 S23: 0.4880 REMARK 3 S31: -0.4049 S32: -0.0479 S33: 1.1938 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN A AND RESID 194:229 REMARK 3 ORIGIN FOR THE GROUP (A): 28.6507 -7.7959 -21.0556 REMARK 3 T TENSOR REMARK 3 T11: 0.1381 T22: 0.1253 REMARK 3 T33: 0.1627 T12: -0.0272 REMARK 3 T13: 0.0198 T23: 0.0169 REMARK 3 L TENSOR REMARK 3 L11: 0.2438 L22: 0.2861 REMARK 3 L33: 0.3417 L12: -0.0442 REMARK 3 L13: -0.2392 L23: -0.3094 REMARK 3 S TENSOR REMARK 3 S11: 0.1091 S12: 0.2024 S13: 0.0881 REMARK 3 S21: -0.1071 S22: 0.1228 S23: 0.1007 REMARK 3 S31: -0.0513 S32: -0.0000 S33: 0.0001 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN A AND RESID 230:276 REMARK 3 ORIGIN FOR THE GROUP (A): 30.6284 -8.8459 -9.1541 REMARK 3 T TENSOR REMARK 3 T11: 0.1437 T22: 0.1232 REMARK 3 T33: 0.1523 T12: -0.0124 REMARK 3 T13: 0.0333 T23: -0.0163 REMARK 3 L TENSOR REMARK 3 L11: 0.0341 L22: 0.5443 REMARK 3 L33: 1.7640 L12: 0.0324 REMARK 3 L13: -0.7492 L23: -0.7242 REMARK 3 S TENSOR REMARK 3 S11: 0.0997 S12: 0.0058 S13: 0.1817 REMARK 3 S21: 0.1052 S22: 0.0291 S23: 0.0656 REMARK 3 S31: -0.1025 S32: 0.1284 S33: -0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN A AND RESID 277:313 REMARK 3 ORIGIN FOR THE GROUP (A): 26.8079 -15.7635 0.0810 REMARK 3 T TENSOR REMARK 3 T11: 0.1454 T22: 0.1644 REMARK 3 T33: 0.1583 T12: -0.0453 REMARK 3 T13: 0.0372 T23: -0.0139 REMARK 3 L TENSOR REMARK 3 L11: 0.2697 L22: 0.2763 REMARK 3 L33: 0.2880 L12: 0.4716 REMARK 3 L13: -0.3106 L23: -1.0099 REMARK 3 S TENSOR REMARK 3 S11: 0.1114 S12: 0.0628 S13: 0.1098 REMARK 3 S21: 0.1324 S22: 0.0522 S23: 0.0571 REMARK 3 S31: -0.1606 S32: 0.1194 S33: -0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN A AND RESID 314:349 REMARK 3 ORIGIN FOR THE GROUP (A): 23.9834 -22.5183 7.2297 REMARK 3 T TENSOR REMARK 3 T11: 0.1118 T22: 0.1537 REMARK 3 T33: 0.1463 T12: -0.0250 REMARK 3 T13: 0.0237 T23: 0.0026 REMARK 3 L TENSOR REMARK 3 L11: 0.7077 L22: 0.4285 REMARK 3 L33: 0.4082 L12: 0.6220 REMARK 3 L13: -0.6193 L23: -0.6878 REMARK 3 S TENSOR REMARK 3 S11: 0.2017 S12: -0.0562 S13: 0.2268 REMARK 3 S21: 0.0872 S22: -0.0000 S23: 0.1312 REMARK 3 S31: -0.0206 S32: 0.0976 S33: 0.0035 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN A AND RESID 350:404 REMARK 3 ORIGIN FOR THE GROUP (A): 25.0293 -32.0301 12.0864 REMARK 3 T TENSOR REMARK 3 T11: 0.1123 T22: 0.1889 REMARK 3 T33: 0.0945 T12: -0.0405 REMARK 3 T13: -0.0122 T23: 0.0235 REMARK 3 L TENSOR REMARK 3 L11: 1.0406 L22: 0.9744 REMARK 3 L33: 0.2733 L12: 0.8903 REMARK 3 L13: -0.3328 L23: -0.7676 REMARK 3 S TENSOR REMARK 3 S11: 0.1745 S12: -0.2767 S13: -0.0256 REMARK 3 S21: 0.0897 S22: -0.0705 S23: 0.1179 REMARK 3 S31: -0.0198 S32: 0.0553 S33: 0.0001 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN A AND RESID 405:441 REMARK 3 ORIGIN FOR THE GROUP (A): 16.5577 -41.2116 15.4695 REMARK 3 T TENSOR REMARK 3 T11: 0.1184 T22: 0.1749 REMARK 3 T33: 0.1562 T12: -0.0441 REMARK 3 T13: -0.0281 T23: 0.0413 REMARK 3 L TENSOR REMARK 3 L11: 0.4373 L22: 0.8752 REMARK 3 L33: -0.1898 L12: 0.8979 REMARK 3 L13: 0.0490 L23: -0.5801 REMARK 3 S TENSOR REMARK 3 S11: 0.1330 S12: -0.0354 S13: 0.1339 REMARK 3 S21: 0.1881 S22: -0.1000 S23: -0.0421 REMARK 3 S31: -0.0005 S32: 0.0485 S33: -0.0000 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN A AND RESID 442:487 REMARK 3 ORIGIN FOR THE GROUP (A): 7.5585 -52.0851 18.8387 REMARK 3 T TENSOR REMARK 3 T11: 0.1921 T22: 0.1449 REMARK 3 T33: 0.1450 T12: -0.0314 REMARK 3 T13: -0.0394 T23: 0.0431 REMARK 3 L TENSOR REMARK 3 L11: 0.6139 L22: 1.4509 REMARK 3 L33: -0.0075 L12: 0.6583 REMARK 3 L13: 0.4341 L23: -0.1336 REMARK 3 S TENSOR REMARK 3 S11: 0.0620 S12: -0.0812 S13: -0.0309 REMARK 3 S21: 0.3723 S22: -0.0430 S23: -0.0003 REMARK 3 S31: -0.0779 S32: 0.0813 S33: -0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN A AND RESID 488:545 REMARK 3 ORIGIN FOR THE GROUP (A): 9.9184 -61.2620 12.8197 REMARK 3 T TENSOR REMARK 3 T11: 0.1227 T22: 0.1446 REMARK 3 T33: 0.1101 T12: 0.0103 REMARK 3 T13: -0.0064 T23: 0.0203 REMARK 3 L TENSOR REMARK 3 L11: 0.6958 L22: 1.1956 REMARK 3 L33: 0.8817 L12: 0.3819 REMARK 3 L13: 0.0376 L23: -0.5009 REMARK 3 S TENSOR REMARK 3 S11: -0.0342 S12: 0.0836 S13: -0.1121 REMARK 3 S21: 0.0218 S22: -0.0444 S23: -0.0470 REMARK 3 S31: 0.0923 S32: 0.2135 S33: -0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN A AND RESID 546:567 REMARK 3 ORIGIN FOR THE GROUP (A): -0.1385 -64.1194 4.5358 REMARK 3 T TENSOR REMARK 3 T11: 0.2161 T22: 0.1902 REMARK 3 T33: 0.0863 T12: 0.0034 REMARK 3 T13: -0.0038 T23: -0.0150 REMARK 3 L TENSOR REMARK 3 L11: 0.5736 L22: 0.3288 REMARK 3 L33: 0.3867 L12: 0.0326 REMARK 3 L13: 0.1416 L23: -0.2414 REMARK 3 S TENSOR REMARK 3 S11: -0.0414 S12: 0.4973 S13: -0.0102 REMARK 3 S21: -0.1747 S22: 0.0724 S23: 0.1752 REMARK 3 S31: 0.3852 S32: -0.0771 S33: 0.0078 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): 10.1506 -33.2661 -3.3772 REMARK 3 T TENSOR REMARK 3 T11: 0.3169 T22: 0.2600 REMARK 3 T33: 0.2121 T12: -0.1296 REMARK 3 T13: -0.0516 T23: 0.0936 REMARK 3 L TENSOR REMARK 3 L11: 0.0585 L22: -0.1746 REMARK 3 L33: -0.6751 L12: 0.4104 REMARK 3 L13: -0.3064 L23: -0.1909 REMARK 3 S TENSOR REMARK 3 S11: -0.1411 S12: 0.0844 S13: 0.1861 REMARK 3 S21: -0.3441 S22: 0.1538 S23: 0.2577 REMARK 3 S31: 0.1402 S32: 0.1028 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 3K64 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-09. REMARK 100 THE RCSB ID CODE IS RCSB055593. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-OCT-07 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36362 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 26.320 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 11.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.11800 REMARK 200
FOR THE DATA SET : 23.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 11.40 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.83800 REMARK 200
FOR SHELL : 3.700 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 3K5Q REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.31 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 7.5, 10% REMARK 280 POLYETHYLENE GLYCOL 8000, AND 8% ETHYLENE GLYCOL, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.84733 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 67.69467 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 50.77100 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 84.61833 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 16.92367 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19780 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 164 REMARK 465 ASN A 165 REMARK 465 ASN A 166 REMARK 465 VAL A 167 REMARK 465 THR A 568 REMARK 465 HIS A 569 REMARK 465 PRO A 570 REMARK 465 ILE A 571 REMARK 465 TYR A 572 REMARK 465 GLU A 573 REMARK 465 LEU A 574 REMARK 465 GLN A 575 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 312 -153.96 -113.75 REMARK 500 ARG A 441 -3.14 75.28 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 727 DISTANCE = 5.08 ANGSTROMS REMARK 525 HOH A 790 DISTANCE = 5.27 ANGSTROMS REMARK 525 HOH A 806 DISTANCE = 6.00 ANGSTROMS REMARK 525 HOH A 812 DISTANCE = 5.27 ANGSTROMS REMARK 525 HOH A 855 DISTANCE = 5.23 ANGSTROMS REMARK 525 HOH A 870 DISTANCE = 6.46 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3K5Q RELATED DB: PDB REMARK 900 RELATED ID: 3K5Y RELATED DB: PDB REMARK 900 RELATED ID: 3K5Z RELATED DB: PDB REMARK 900 RELATED ID: 3K61 RELATED DB: PDB REMARK 900 RELATED ID: 3K62 RELATED DB: PDB DBREF 3K64 A 164 575 UNP Q09312 FBF2_CAEEL 164 575 DBREF 3K64 B 1 9 PDB 3K64 3K64 1 9 SEQRES 1 A 412 SER ASN ASN VAL LEU PRO THR TRP SER LEU ASP SER ASN SEQRES 2 A 412 GLY GLU MET ARG SER ARG LEU SER LEU SER GLU VAL LEU SEQRES 3 A 412 ASP SER GLY ASP LEU MET LYS PHE ALA VAL ASP LYS THR SEQRES 4 A 412 GLY CYS GLN PHE LEU GLU LYS ALA VAL LYS GLY SER LEU SEQRES 5 A 412 THR SER TYR GLN LYS PHE GLN LEU PHE GLU GLN VAL ILE SEQRES 6 A 412 GLY ARG LYS ASP ASP PHE LEU LYS LEU SER THR ASN ILE SEQRES 7 A 412 PHE GLY ASN TYR LEU VAL GLN SER VAL ILE GLY ILE SER SEQRES 8 A 412 LEU ALA THR ASN ASP ASP GLY TYR THR LYS ARG GLN GLU SEQRES 9 A 412 LYS LEU LYS ASN PHE ILE SER SER GLN MET THR ASP MET SEQRES 10 A 412 CYS LEU ASP LYS PHE ALA CYS ARG VAL ILE GLN SER SER SEQRES 11 A 412 LEU GLN ASN MET ASP LEU SER LEU ALA CYS LYS LEU VAL SEQRES 12 A 412 GLN ALA LEU PRO ARG ASP ALA ARG LEU ILE ALA ILE CYS SEQRES 13 A 412 VAL ASP GLN ASN ALA ASN HIS VAL ILE GLN LYS VAL VAL SEQRES 14 A 412 ALA VAL ILE PRO LEU LYS ASN TRP GLU PHE ILE VAL ASP SEQRES 15 A 412 PHE VAL ALA THR PRO GLU HIS LEU ARG GLN ILE CYS SER SEQRES 16 A 412 ASP LYS TYR GLY CYS ARG VAL VAL GLN THR ILE ILE GLU SEQRES 17 A 412 LYS LEU THR ALA ASP SER MET ASN VAL ASP LEU THR SER SEQRES 18 A 412 ALA ALA GLN ASN LEU ARG GLU ARG ALA LEU GLN ARG LEU SEQRES 19 A 412 MET THR SER VAL THR ASN ARG CYS GLN GLU LEU ALA THR SEQRES 20 A 412 ASN GLU TYR ALA ASN TYR ILE ILE GLN HIS ILE VAL SER SEQRES 21 A 412 ASN ASP ASP LEU ALA VAL TYR ARG GLU CYS ILE ILE GLU SEQRES 22 A 412 LYS CYS LEU MET ARG ASN LEU LEU SER LEU SER GLN GLU SEQRES 23 A 412 LYS PHE ALA SER HIS VAL VAL GLU LYS ALA PHE LEU HIS SEQRES 24 A 412 ALA PRO LEU GLU LEU LEU ALA GLU MET MET ASP GLU ILE SEQRES 25 A 412 PHE ASP GLY TYR ILE PRO HIS PRO ASP THR GLY LYS ASP SEQRES 26 A 412 ALA LEU ASP ILE MET MET PHE HIS GLN PHE GLY ASN TYR SEQRES 27 A 412 VAL VAL GLN CYS MET LEU THR ILE CYS CYS ASP ALA VAL SEQRES 28 A 412 SER GLY ARG ARG GLN THR LYS GLU GLY GLY TYR ASP HIS SEQRES 29 A 412 ALA ILE SER PHE GLN ASP TRP LEU LYS LYS LEU HIS SER SEQRES 30 A 412 ARG VAL THR LYS GLU ARG HIS ARG LEU SER ARG PHE SER SEQRES 31 A 412 SER GLY LYS LYS MET ILE GLU THR LEU ALA ASN LEU ARG SEQRES 32 A 412 SER THR HIS PRO ILE TYR GLU LEU GLN SEQRES 1 B 9 U G U G U C A U U FORMUL 3 HOH *495(H2 O) HELIX 1 1 PRO A 169 LEU A 173 5 5 HELIX 2 2 SER A 184 GLY A 192 1 9 HELIX 3 3 ASP A 193 VAL A 199 1 7 HELIX 4 4 ASP A 200 VAL A 211 1 12 HELIX 5 5 THR A 216 GLY A 229 1 14 HELIX 6 6 ARG A 230 THR A 239 1 10 HELIX 7 7 PHE A 242 THR A 257 1 16 HELIX 8 8 GLY A 261 GLN A 276 1 16 HELIX 9 9 GLN A 276 ASP A 283 1 8 HELIX 10 10 PHE A 285 MET A 297 1 13 HELIX 11 11 ASP A 298 ALA A 308 1 11 HELIX 12 12 ASP A 312 VAL A 320 1 9 HELIX 13 13 ALA A 324 ILE A 335 1 12 HELIX 14 14 PRO A 336 THR A 349 1 14 HELIX 15 15 THR A 349 SER A 358 1 10 HELIX 16 16 ASP A 359 LEU A 373 1 15 HELIX 17 17 ASP A 376 VAL A 380 5 5 HELIX 18 18 THR A 383 ARG A 404 1 22 HELIX 19 19 ARG A 404 THR A 410 1 7 HELIX 20 20 ALA A 414 ASN A 424 1 11 HELIX 21 21 LEU A 427 LEU A 439 1 13 HELIX 22 22 ASN A 442 GLN A 448 1 7 HELIX 23 23 PHE A 451 ALA A 463 1 13 HELIX 24 24 PRO A 464 GLY A 478 1 15 HELIX 25 25 ASP A 488 PHE A 495 1 8 HELIX 26 26 PHE A 498 SER A 515 1 18 HELIX 27 27 HIS A 527 GLU A 545 1 19 HELIX 28 28 GLU A 545 SER A 550 1 6 HELIX 29 29 PHE A 552 SER A 567 1 16 SHEET 1 A 2 LYS A 521 GLU A 522 0 SHEET 2 A 2 TYR A 525 ASP A 526 -1 O TYR A 525 N GLU A 522 CRYST1 96.675 96.675 101.542 90.00 90.00 120.00 P 61 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010344 0.005972 0.000000 0.00000 SCALE2 0.000000 0.011944 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009848 0.00000 ATOM 1 N LEU A 168 14.954 -1.633 -24.887 1.00 47.82 N ANISOU 1 N LEU A 168 5188 5460 7523 593 -1733 2665 N ATOM 2 CA LEU A 168 16.304 -1.454 -25.412 1.00 46.97 C ANISOU 2 CA LEU A 168 5312 5302 7231 585 -1595 2616 C ATOM 3 C LEU A 168 16.483 -0.068 -26.029 1.00 45.76 C ANISOU 3 C LEU A 168 5348 5007 7032 677 -1489 2841 C ATOM 4 O LEU A 168 15.512 0.562 -26.445 1.00 49.22 O ANISOU 4 O LEU A 168 5785 5421 7494 765 -1607 3053 O ATOM 5 CB LEU A 168 16.611 -2.525 -26.461 1.00 44.75 C ANISOU 5 CB LEU A 168 5206 5142 6656 510 -1788 2574 C ATOM 6 CG LEU A 168 16.611 -3.989 -26.018 1.00 41.27 C ANISOU 6 CG LEU A 168 4665 4816 6198 404 -1890 2337 C ATOM 7 CD1 LEU A 168 16.772 -4.911 -27.218 1.00 48.59 C ANISOU 7 CD1 LEU A 168 5794 5856 6814 342 -2106 2327 C ATOM 8 CD2 LEU A 168 17.708 -4.249 -24.998 1.00 35.99 C ANISOU 8 CD2 LEU A 168 3945 4128 5603 379 -1652 2081 C ATOM 9 N PRO A 169 17.735 0.410 -26.093 1.00 42.48 N ANISOU 9 N PRO A 169 5112 4493 6536 645 -1251 2788 N ATOM 10 CA PRO A 169 18.054 1.673 -26.768 1.00 46.01 C ANISOU 10 CA PRO A 169 5785 4802 6895 654 -1096 2949 C ATOM 11 C PRO A 169 17.646 1.611 -28.234 1.00 45.68 C ANISOU 11 C PRO A 169 5954 4817 6584 658 -1301 3136 C ATOM 12 O PRO A 169 17.828 0.581 -28.880 1.00 48.11 O ANISOU 12 O PRO A 169 6315 5276 6688 581 -1448 3046 O ATOM 13 CB PRO A 169 19.582 1.750 -26.676 1.00 46.06 C ANISOU 13 CB PRO A 169 5902 4801 6798 504 -795 2722 C ATOM 14 CG PRO A 169 19.959 0.848 -25.578 1.00 36.18 C ANISOU 14 CG PRO A 169 4434 3635 5679 475 -746 2455 C ATOM 15 CD PRO A 169 18.928 -0.237 -25.528 1.00 37.64 C ANISOU 15 CD PRO A 169 4471 3938 5894 531 -1062 2483 C ATOM 16 N THR A 170 17.106 2.702 -28.755 1.00 46.91 N ANISOU 16 N THR A 170 6244 4851 6730 760 -1312 3389 N ATOM 17 CA THR A 170 16.649 2.719 -30.137 1.00 56.08 C ANISOU 17 CA THR A 170 7607 6061 7639 791 -1510 3580 C ATOM 18 C THR A 170 17.786 2.479 -31.143 1.00 56.95 C ANISOU 18 C THR A 170 7971 6225 7443 637 -1403 3488 C ATOM 19 O THR A 170 17.572 1.862 -32.183 1.00 59.33 O ANISOU 19 O THR A 170 8382 6647 7513 625 -1609 3538 O ATOM 20 CB THR A 170 15.875 4.016 -30.455 1.00 60.16 C ANISOU 20 CB THR A 170 8238 6422 8196 955 -1526 3869 C ATOM 21 OG1 THR A 170 15.716 4.154 -31.873 1.00 67.02 O ANISOU 21 OG1 THR A 170 9361 7320 8783 972 -1654 4035 O ATOM 22 CG2 THR A 170 16.613 5.221 -29.905 1.00 62.32 C ANISOU 22 CG2 THR A 170 8617 6482 8579 935 -1194 3863 C ATOM 23 N TRP A 171 18.995 2.939 -30.827 1.00 51.29 N ANISOU 23 N TRP A 171 7337 5435 6718 519 -1087 3346 N ATOM 24 CA TRP A 171 20.137 2.721 -31.716 1.00 48.94 C ANISOU 24 CA TRP A 171 7256 5215 6125 368 -964 3243 C ATOM 25 C TRP A 171 20.408 1.239 -31.957 1.00 47.19 C ANISOU 25 C TRP A 171 6972 5213 5746 302 -1127 3044 C ATOM 26 O TRP A 171 21.042 0.869 -32.943 1.00 49.22 O ANISOU 26 O TRP A 171 7413 5575 5712 221 -1134 3001 O ATOM 27 CB TRP A 171 21.407 3.401 -31.186 1.00 45.39 C ANISOU 27 CB TRP A 171 6857 4680 5708 236 -589 3091 C ATOM 28 CG TRP A 171 21.944 2.847 -29.883 1.00 39.36 C ANISOU 28 CG TRP A 171 5846 3970 5140 190 -460 2812 C ATOM 29 CD1 TRP A 171 21.791 3.391 -28.641 1.00 38.23 C ANISOU 29 CD1 TRP A 171 5528 3699 5301 242 -326 2776 C ATOM 30 CD2 TRP A 171 22.735 1.658 -29.701 1.00 41.06 C ANISOU 30 CD2 TRP A 171 5978 4379 5243 99 -451 2527 C ATOM 31 NE1 TRP A 171 22.427 2.616 -27.699 1.00 36.18 N ANISOU 31 NE1 TRP A 171 5074 3542 5130 188 -233 2489 N ATOM 32 CE2 TRP A 171 23.013 1.547 -28.324 1.00 40.09 C ANISOU 32 CE2 TRP A 171 5628 4234 5371 104 -307 2331 C ATOM 33 CE3 TRP A 171 23.231 0.678 -30.567 1.00 45.12 C ANISOU 33 CE3 TRP A 171 6599 5085 5461 31 -554 2417 C ATOM 34 CZ2 TRP A 171 23.760 0.491 -27.791 1.00 39.49 C ANISOU 34 CZ2 TRP A 171 5434 4319 5253 49 -264 2030 C ATOM 35 CZ3 TRP A 171 23.971 -0.369 -30.036 1.00 40.63 C ANISOU 35 CZ3 TRP A 171 5917 4673 4846 -22 -516 2118 C ATOM 36 CH2 TRP A 171 24.230 -0.452 -28.663 1.00 38.78 C ANISOU 36 CH2 TRP A 171 5462 4411 4861 -11 -370 1928 C ATOM 37 N SER A 172 19.926 0.398 -31.049 1.00 50.31 N ANISOU 37 N SER A 172 7117 5672 6325 341 -1257 2923 N ATOM 38 CA SER A 172 20.184 -1.033 -31.115 1.00 46.12 C ANISOU 38 CA SER A 172 6534 5325 5664 281 -1404 2716 C ATOM 39 C SER A 172 18.996 -1.781 -31.708 1.00 47.94 C ANISOU 39 C SER A 172 6738 5642 5834 351 -1778 2849 C ATOM 40 O SER A 172 18.936 -3.007 -31.649 1.00 45.41 O ANISOU 40 O SER A 172 6356 5451 5446 314 -1950 2701 O ATOM 41 CB SER A 172 20.468 -1.578 -29.717 1.00 43.76 C ANISOU 41 CB SER A 172 5997 5043 5587 266 -1305 2477 C ATOM 42 OG SER A 172 19.257 -1.799 -29.012 1.00 35.10 O ANISOU 42 OG SER A 172 4683 3919 4735 365 -1497 2566 O ATOM 43 N LEU A 173 18.052 -1.043 -32.279 1.00 54.12 N ANISOU 43 N LEU A 173 7576 6355 6633 452 -1907 3123 N ATOM 44 CA LEU A 173 16.816 -1.642 -32.774 1.00 58.64 C ANISOU 44 CA LEU A 173 8090 7018 7173 526 -2264 3261 C ATOM 45 C LEU A 173 16.680 -1.575 -34.292 1.00 63.01 C ANISOU 45 C LEU A 173 8893 7625 7425 544 -2417 3418 C ATOM 46 O LEU A 173 17.248 -0.699 -34.942 1.00 62.10 O ANISOU 46 O LEU A 173 8992 7428 7173 541 -2246 3510 O ATOM 47 CB LEU A 173 15.606 -0.968 -32.122 1.00 56.10 C ANISOU 47 CB LEU A 173 7576 6615 7124 666 -2345 3449 C ATOM 48 CG LEU A 173 15.481 -1.195 -30.616 1.00 53.96 C ANISOU 48 CG LEU A 173 7017 6322 7164 659 -2252 3294 C ATOM 49 CD1 LEU A 173 14.283 -0.449 -30.054 1.00 56.06 C ANISOU 49 CD1 LEU A 173 7081 6536 7684 772 -2288 3433 C ATOM 50 CD2 LEU A 173 15.390 -2.684 -30.311 1.00 45.50 C ANISOU 50 CD2 LEU A 173 5807 5400 6081 548 -2403 3069 C ATOM 51 N ASP A 174 15.922 -2.517 -34.842 1.00 67.78 N ANISOU 51 N ASP A 174 9469 8363 7921 557 -2740 3445 N ATOM 52 CA ASP A 174 15.577 -2.520 -36.257 1.00 77.58 C ANISOU 52 CA ASP A 174 10916 9667 8892 599 -2937 3606 C ATOM 53 C ASP A 174 14.422 -1.568 -36.506 1.00 86.50 C ANISOU 53 C ASP A 174 12021 10732 10114 759 -3049 3887 C ATOM 54 O ASP A 174 13.965 -0.879 -35.595 1.00 81.46 O ANISOU 54 O ASP A 174 11213 9997 9743 829 -2951 3940 O ATOM 55 CB ASP A 174 15.159 -3.923 -36.701 1.00 81.94 C ANISOU 55 CB ASP A 174 11430 10386 9316 535 -3233 3488 C ATOM 56 CG ASP A 174 16.303 -4.713 -37.298 1.00 90.54 C ANISOU 56 CG ASP A 174 12722 11565 10114 439 -3203 3315 C ATOM 57 OD1 ASP A 174 17.297 -4.089 -37.729 1.00 92.43 O ANISOU 57 OD1 ASP A 174 13150 11762 10208 417 -2968 3310 O ATOM 58 OD2 ASP A 174 16.201 -5.958 -37.346 1.00 93.56 O ANISOU 58 OD2 ASP A 174 13059 12050 10440 354 -3368 3128 O ATOM 59 N SER A 175 13.948 -1.542 -37.747 1.00 99.80 N ANISOU 59 N SER A 175 13866 12478 11576 819 -3244 4035 N ATOM 60 CA SER A 175 12.741 -0.806 -38.090 1.00111.28 C ANISOU 60 CA SER A 175 15280 13911 13090 978 -3388 4263 C ATOM 61 C SER A 175 11.529 -1.601 -37.621 1.00113.91 C ANISOU 61 C SER A 175 15306 14376 13599 966 -3634 4198 C ATOM 62 O SER A 175 10.397 -1.123 -37.669 1.00116.14 O ANISOU 62 O SER A 175 15476 14681 13972 1094 -3767 4355 O ATOM 63 CB SER A 175 12.668 -0.576 -39.597 1.00117.92 C ANISOU 63 CB SER A 175 16402 14788 13616 1051 -3517 4431 C ATOM 64 OG SER A 175 12.771 -1.803 -40.299 1.00120.38 O ANISOU 64 OG SER A 175 16751 15260 13729 950 -3718 4296 O ATOM 65 N ASN A 176 11.785 -2.824 -37.166 1.00112.26 N ANISOU 65 N ASN A 176 14975 14253 13424 808 -3686 3965 N ATOM 66 CA ASN A 176 10.739 -3.707 -36.673 1.00111.46 C ANISOU 66 CA ASN A 176 14605 14266 13481 747 -3895 3885 C ATOM 67 C ASN A 176 10.588 -3.586 -35.163 1.00100.23 C ANISOU 67 C ASN A 176 12913 12786 12385 723 -3740 3793 C ATOM 68 O ASN A 176 9.719 -4.219 -34.565 1.00 94.27 O ANISOU 68 O ASN A 176 11917 12109 11791 664 -3868 3735 O ATOM 69 CB ASN A 176 11.061 -5.157 -37.033 1.00119.24 C ANISOU 69 CB ASN A 176 15642 15353 14310 582 -4040 3681 C ATOM 70 CG ASN A 176 11.665 -5.294 -38.416 1.00126.49 C ANISOU 70 CG ASN A 176 16866 16309 14884 590 -4110 3713 C ATOM 71 OD1 ASN A 176 11.242 -4.628 -39.360 1.00131.25 O ANISOU 71 OD1 ASN A 176 17595 16923 15351 712 -4203 3916 O ATOM 72 ND2 ASN A 176 12.661 -6.164 -38.542 1.00126.74 N ANISOU 72 ND2 ASN A 176 17026 16366 14764 472 -4062 3507 N ATOM 73 N GLY A 177 11.445 -2.773 -34.552 1.00 96.45 N ANISOU 73 N GLY A 177 12481 12167 11997 760 -3455 3782 N ATOM 74 CA GLY A 177 11.472 -2.638 -33.107 1.00 90.73 C ANISOU 74 CA GLY A 177 11522 11379 11572 740 -3278 3673 C ATOM 75 C GLY A 177 12.145 -3.841 -32.476 1.00 83.50 C ANISOU 75 C GLY A 177 10544 10505 10678 574 -3235 3399 C ATOM 76 O GLY A 177 12.008 -4.101 -31.280 1.00 77.27 O ANISOU 76 O GLY A 177 9536 9698 10126 528 -3144 3273 O ATOM 77 N GLU A 178 12.879 -4.581 -33.298 1.00 81.98 N ANISOU 77 N GLU A 178 10559 10368 10221 493 -3297 3303 N ATOM 78 CA GLU A 178 13.537 -5.797 -32.856 1.00 81.83 C ANISOU 78 CA GLU A 178 10530 10395 10168 352 -3279 3037 C ATOM 79 C GLU A 178 15.038 -5.562 -32.769 1.00 75.54 C ANISOU 79 C GLU A 178 9901 9549 9253 345 -3031 2922 C ATOM 80 O GLU A 178 15.628 -4.970 -33.671 1.00 76.57 O ANISOU 80 O GLU A 178 10261 9666 9169 390 -2977 3032 O ATOM 81 CB GLU A 178 13.231 -6.928 -33.838 1.00 91.13 C ANISOU 81 CB GLU A 178 11821 11685 11119 266 -3547 2987 C ATOM 82 CG GLU A 178 13.406 -8.323 -33.271 1.00 97.03 C ANISOU 82 CG GLU A 178 12517 12465 11886 122 -3594 2732 C ATOM 83 CD GLU A 178 12.777 -9.386 -34.152 1.00103.99 C ANISOU 83 CD GLU A 178 13481 13432 12598 37 -3885 2716 C ATOM 84 OE1 GLU A 178 12.974 -10.589 -33.873 1.00104.01 O ANISOU 84 OE1 GLU A 178 13512 13440 12567 -82 -3935 2514 O ATOM 85 OE2 GLU A 178 12.083 -9.018 -35.123 1.00106.66 O ANISOU 85 OE2 GLU A 178 13869 13823 12833 95 -4064 2907 O ATOM 86 N MET A 179 15.653 -6.019 -31.682 1.00 68.63 N ANISOU 86 N MET A 179 8916 8654 8505 287 -2874 2703 N ATOM 87 CA MET A 179 17.093 -5.857 -31.503 1.00 61.55 C ANISOU 87 CA MET A 179 8153 7740 7495 280 -2637 2573 C ATOM 88 C MET A 179 17.848 -6.286 -32.755 1.00 58.98 C ANISOU 88 C MET A 179 8107 7510 6792 244 -2705 2544 C ATOM 89 O MET A 179 17.641 -7.384 -33.269 1.00 57.97 O ANISOU 89 O MET A 179 8034 7474 6518 178 -2902 2435 O ATOM 90 CB MET A 179 17.600 -6.650 -30.294 1.00 52.82 C ANISOU 90 CB MET A 179 6904 6644 6522 221 -2522 2296 C ATOM 91 CG MET A 179 19.047 -6.334 -29.938 1.00 48.57 C ANISOU 91 CG MET A 179 6448 6092 5916 211 -2224 2131 C ATOM 92 SD MET A 179 19.729 -7.333 -28.602 1.00 45.45 S ANISOU 92 SD MET A 179 5914 5733 5622 177 -2110 1795 S ATOM 93 CE MET A 179 20.283 -8.785 -29.492 1.00 45.43 C ANISOU 93 CE MET A 179 6134 5885 5244 109 -2291 1603 C ATOM 94 N ARG A 180 18.718 -5.409 -33.243 1.00 53.52 N ANISOU 94 N ARG A 180 7578 6775 5984 239 -2469 2573 N ATOM 95 CA ARG A 180 19.478 -5.678 -34.454 1.00 54.52 C ANISOU 95 CA ARG A 180 7962 6995 5758 196 -2481 2536 C ATOM 96 C ARG A 180 20.322 -6.934 -34.321 1.00 59.70 C ANISOU 96 C ARG A 180 8664 7781 6241 129 -2496 2245 C ATOM 97 O ARG A 180 20.814 -7.253 -33.238 1.00 55.56 O ANISOU 97 O ARG A 180 8007 7250 5854 104 -2350 2039 O ATOM 98 CB ARG A 180 20.388 -4.494 -34.788 1.00 52.44 C ANISOU 98 CB ARG A 180 7840 6662 5422 176 -2171 2587 C ATOM 99 CG ARG A 180 19.657 -3.179 -35.003 1.00 56.04 C ANISOU 99 CG ARG A 180 8313 6971 6009 255 -2138 2876 C ATOM 100 CD ARG A 180 20.562 -2.170 -35.692 1.00 60.39 C ANISOU 100 CD ARG A 180 9087 7466 6393 212 -1881 2943 C ATOM 101 NE ARG A 180 21.793 -1.939 -34.940 1.00 63.52 N ANISOU 101 NE ARG A 180 9447 7852 6837 113 -1549 2728 N ATOM 102 CZ ARG A 180 22.932 -1.523 -35.483 1.00 69.41 C ANISOU 102 CZ ARG A 180 10370 8632 7372 19 -1315 2669 C ATOM 103 NH1 ARG A 180 23.003 -1.302 -36.789 1.00 78.32 N ANISOU 103 NH1 ARG A 180 11736 9797 8227 17 -1376 2815 N ATOM 104 NH2 ARG A 180 24.003 -1.336 -34.724 1.00 66.04 N ANISOU 104 NH2 ARG A 180 9877 8215 7000 -73 -1020 2460 N ATOM 105 N SER A 181 20.475 -7.654 -35.426 1.00 66.69 N ANISOU 105 N SER A 181 9743 8782 6813 115 -2681 2226 N ATOM 106 CA SER A 181 21.479 -8.701 -35.505 1.00 72.74 C ANISOU 106 CA SER A 181 10617 9679 7344 72 -2663 1954 C ATOM 107 C SER A 181 22.789 -8.019 -35.866 1.00 70.42 C ANISOU 107 C SER A 181 10452 9426 6878 41 -2353 1881 C ATOM 108 O SER A 181 22.785 -6.866 -36.299 1.00 73.67 O ANISOU 108 O SER A 181 10919 9763 7310 42 -2216 2071 O ATOM 109 CB SER A 181 21.107 -9.732 -36.570 1.00 80.98 C ANISOU 109 CB SER A 181 11805 10795 8168 55 -2938 1919 C ATOM 110 OG SER A 181 20.049 -10.562 -36.127 1.00 83.39 O ANISOU 110 OG SER A 181 11969 11038 8676 20 -3137 1876 O ATOM 111 N ARG A 182 23.903 -8.717 -35.676 1.00 65.48 N ANISOU 111 N ARG A 182 9879 8925 6077 13 -2239 1606 N ATOM 112 CA ARG A 182 25.213 -8.173 -36.025 1.00 66.35 C ANISOU 112 CA ARG A 182 10097 9120 5994 -30 -1946 1509 C ATOM 113 C ARG A 182 25.660 -7.073 -35.051 1.00 54.10 C ANISOU 113 C ARG A 182 8392 7465 4700 -72 -1603 1491 C ATOM 114 O ARG A 182 26.596 -6.319 -35.326 1.00 49.17 O ANISOU 114 O ARG A 182 7840 6876 3966 -133 -1337 1470 O ATOM 115 CB ARG A 182 25.207 -7.658 -37.468 1.00 83.26 C ANISOU 115 CB ARG A 182 12456 11294 7883 -32 -1997 1714 C ATOM 116 CG ARG A 182 26.578 -7.349 -38.044 1.00 99.79 C ANISOU 116 CG ARG A 182 14694 13528 9695 -88 -1743 1601 C ATOM 117 CD ARG A 182 26.456 -6.716 -39.422 1.00114.76 C ANISOU 117 CD ARG A 182 16802 15427 11374 -89 -1784 1840 C ATOM 118 NE ARG A 182 27.713 -6.117 -39.858 1.00125.06 N ANISOU 118 NE ARG A 182 18216 16836 12464 -169 -1484 1775 N ATOM 119 CZ ARG A 182 28.171 -4.949 -39.420 1.00132.28 C ANISOU 119 CZ ARG A 182 19079 17656 13523 -256 -1166 1821 C ATOM 120 NH1 ARG A 182 27.476 -4.256 -38.527 1.00134.07 N ANISOU 120 NH1 ARG A 182 19155 17678 14110 -252 -1113 1931 N ATOM 121 NH2 ARG A 182 29.325 -4.475 -39.869 1.00135.18 N ANISOU 121 NH2 ARG A 182 19550 18143 13671 -351 -902 1754 N ATOM 122 N LEU A 183 24.986 -6.994 -33.908 1.00 46.65 N ANISOU 122 N LEU A 183 7235 6395 4093 -46 -1612 1498 N ATOM 123 CA LEU A 183 25.381 -6.084 -32.840 1.00 43.06 C ANISOU 123 CA LEU A 183 6620 5839 3900 -73 -1307 1451 C ATOM 124 C LEU A 183 26.689 -6.596 -32.245 1.00 35.62 C ANISOU 124 C LEU A 183 5643 5039 2853 -105 -1094 1115 C ATOM 125 O LEU A 183 26.876 -7.801 -32.117 1.00 35.75 O ANISOU 125 O LEU A 183 5673 5174 2738 -69 -1232 917 O ATOM 126 CB LEU A 183 24.299 -6.058 -31.762 1.00 44.92 C ANISOU 126 CB LEU A 183 6633 5933 4501 -15 -1405 1523 C ATOM 127 CG LEU A 183 23.898 -4.702 -31.192 1.00 50.35 C ANISOU 127 CG LEU A 183 7210 6437 5485 -2 -1232 1703 C ATOM 128 CD1 LEU A 183 25.126 -3.917 -30.785 1.00 55.18 C ANISOU 128 CD1 LEU A 183 7822 7041 6101 -75 -859 1566 C ATOM 129 CD2 LEU A 183 23.076 -3.924 -32.209 1.00 48.55 C ANISOU 129 CD2 LEU A 183 7111 6123 5214 28 -1359 2025 C ATOM 130 N SER A 184 27.597 -5.695 -31.887 1.00 36.30 N ANISOU 130 N SER A 184 5692 5118 2981 -170 -762 1044 N ATOM 131 CA SER A 184 28.866 -6.115 -31.285 1.00 30.41 C ANISOU 131 CA SER A 184 4890 4531 2134 -195 -544 714 C ATOM 132 C SER A 184 28.890 -5.865 -29.781 1.00 30.88 C ANISOU 132 C SER A 184 4712 4495 2526 -174 -376 587 C ATOM 133 O SER A 184 28.220 -4.961 -29.279 1.00 32.94 O ANISOU 133 O SER A 184 4870 4564 3082 -174 -322 765 O ATOM 134 CB SER A 184 30.049 -5.405 -31.949 1.00 34.89 C ANISOU 134 CB SER A 184 5575 5215 2468 -300 -275 671 C ATOM 135 OG SER A 184 30.283 -4.136 -31.361 1.00 36.48 O ANISOU 135 OG SER A 184 5685 5283 2893 -379 9 731 O ATOM 136 N LEU A 185 29.666 -6.669 -29.064 1.00 25.86 N ANISOU 136 N LEU A 185 3998 3998 1831 -141 -297 274 N ATOM 137 CA LEU A 185 29.807 -6.485 -27.630 1.00 22.20 C ANISOU 137 CA LEU A 185 3313 3465 1657 -111 -125 122 C ATOM 138 C LEU A 185 30.352 -5.095 -27.325 1.00 22.09 C ANISOU 138 C LEU A 185 3234 3376 1783 -202 200 164 C ATOM 139 O LEU A 185 29.857 -4.404 -26.436 1.00 21.29 O ANISOU 139 O LEU A 185 2982 3097 2010 -186 282 244 O ATOM 140 CB LEU A 185 30.720 -7.554 -27.032 1.00 20.82 C ANISOU 140 CB LEU A 185 3098 3480 1334 -50 -73 -241 C ATOM 141 CG LEU A 185 30.997 -7.385 -25.536 1.00 22.12 C ANISOU 141 CG LEU A 185 3036 3597 1773 -7 126 -429 C ATOM 142 CD1 LEU A 185 29.710 -7.501 -24.712 1.00 19.09 C ANISOU 142 CD1 LEU A 185 2513 3008 1732 64 -42 -287 C ATOM 143 CD2 LEU A 185 32.029 -8.404 -25.059 1.00 26.31 C ANISOU 143 CD2 LEU A 185 3554 4342 2101 67 194 -802 C ATOM 144 N SER A 186 31.367 -4.681 -28.071 1.00 23.55 N ANISOU 144 N SER A 186 3539 3696 1712 -304 382 110 N ATOM 145 CA SER A 186 32.008 -3.391 -27.813 1.00 24.82 C ANISOU 145 CA SER A 186 3661 3798 1973 -423 707 126 C ATOM 146 C SER A 186 31.066 -2.198 -28.009 1.00 28.02 C ANISOU 146 C SER A 186 4109 3935 2603 -455 695 471 C ATOM 147 O SER A 186 31.121 -1.231 -27.251 1.00 26.39 O ANISOU 147 O SER A 186 3804 3583 2643 -495 899 497 O ATOM 148 CB SER A 186 33.273 -3.236 -28.655 1.00 27.30 C ANISOU 148 CB SER A 186 4102 4334 1938 -545 897 6 C ATOM 149 OG SER A 186 34.305 -4.042 -28.119 1.00 27.17 O ANISOU 149 OG SER A 186 3988 4559 1774 -510 1002 -354 O ATOM 150 N GLU A 187 30.206 -2.268 -29.020 1.00 27.86 N ANISOU 150 N GLU A 187 4243 3853 2490 -425 452 728 N ATOM 151 CA GLU A 187 29.153 -1.265 -29.190 1.00 32.32 C ANISOU 151 CA GLU A 187 4849 4170 3260 -408 390 1058 C ATOM 152 C GLU A 187 28.341 -1.109 -27.910 1.00 26.84 C ANISOU 152 C GLU A 187 3938 3309 2953 -309 357 1080 C ATOM 153 O GLU A 187 28.140 -0.005 -27.419 1.00 27.20 O ANISOU 153 O GLU A 187 3941 3170 3222 -323 509 1198 O ATOM 154 CB GLU A 187 28.199 -1.686 -30.299 1.00 32.99 C ANISOU 154 CB GLU A 187 5083 4247 3202 -344 68 1289 C ATOM 155 CG GLU A 187 28.538 -1.171 -31.665 1.00 42.41 C ANISOU 155 CG GLU A 187 6526 5476 4110 -426 103 1445 C ATOM 156 CD GLU A 187 27.469 -1.538 -32.677 1.00 54.20 C ANISOU 156 CD GLU A 187 8150 6946 5497 -340 -229 1682 C ATOM 157 OE1 GLU A 187 27.264 -2.754 -32.902 1.00 49.83 O ANISOU 157 OE1 GLU A 187 7589 6530 4816 -281 -466 1582 O ATOM 158 OE2 GLU A 187 26.831 -0.616 -33.238 1.00 54.78 O ANISOU 158 OE2 GLU A 187 8341 6864 5610 -327 -258 1964 O ATOM 159 N VAL A 188 27.861 -2.231 -27.382 1.00 25.01 N ANISOU 159 N VAL A 188 3579 3138 2787 -208 154 968 N ATOM 160 CA VAL A 188 27.065 -2.221 -26.160 1.00 24.04 C ANISOU 160 CA VAL A 188 3238 2883 3014 -109 107 980 C ATOM 161 C VAL A 188 27.868 -1.685 -24.964 1.00 26.88 C ANISOU 161 C VAL A 188 3441 3211 3562 -134 417 777 C ATOM 162 O VAL A 188 27.373 -0.857 -24.197 1.00 27.26 O ANISOU 162 O VAL A 188 3374 3080 3902 -92 496 883 O ATOM 163 CB VAL A 188 26.472 -3.619 -25.855 1.00 26.55 C ANISOU 163 CB VAL A 188 3470 3286 3334 -20 -164 883 C ATOM 164 CG1 VAL A 188 25.794 -3.632 -24.497 1.00 26.14 C ANISOU 164 CG1 VAL A 188 3177 3120 3634 72 -175 863 C ATOM 165 CG2 VAL A 188 25.488 -4.024 -26.941 1.00 25.40 C ANISOU 165 CG2 VAL A 188 3454 3142 3055 4 -485 1112 C ATOM 166 N LEU A 189 29.109 -2.138 -24.818 1.00 21.55 N ANISOU 166 N LEU A 189 2761 2719 2709 -192 590 483 N ATOM 167 CA LEU A 189 29.955 -1.684 -23.713 1.00 21.52 C ANISOU 167 CA LEU A 189 2603 2717 2856 -218 885 261 C ATOM 168 C LEU A 189 30.255 -0.188 -23.804 1.00 23.98 C ANISOU 168 C LEU A 189 2971 2884 3257 -331 1133 395 C ATOM 169 O LEU A 189 30.209 0.526 -22.807 1.00 24.30 O ANISOU 169 O LEU A 189 2877 2785 3570 -313 1289 377 O ATOM 170 CB LEU A 189 31.264 -2.482 -23.670 1.00 20.21 C ANISOU 170 CB LEU A 189 2432 2815 2432 -252 1013 -86 C ATOM 171 CG LEU A 189 31.111 -3.961 -23.300 1.00 18.05 C ANISOU 171 CG LEU A 189 2101 2668 2090 -126 811 -276 C ATOM 172 CD1 LEU A 189 32.433 -4.697 -23.436 1.00 16.33 C ANISOU 172 CD1 LEU A 189 1918 2725 1560 -142 929 -605 C ATOM 173 CD2 LEU A 189 30.558 -4.097 -21.890 1.00 16.50 C ANISOU 173 CD2 LEU A 189 1686 2350 2234 -13 806 -340 C ATOM 174 N ASP A 190 30.565 0.273 -25.010 1.00 25.23 N ANISOU 174 N ASP A 190 3343 3069 3174 -446 1165 530 N ATOM 175 CA ASP A 190 30.887 1.677 -25.246 1.00 29.82 C ANISOU 175 CA ASP A 190 4032 3508 3793 -576 1398 669 C ATOM 176 C ASP A 190 29.679 2.599 -25.020 1.00 30.25 C ANISOU 176 C ASP A 190 4098 3270 4127 -495 1312 976 C ATOM 177 O ASP A 190 29.832 3.765 -24.658 1.00 34.74 O ANISOU 177 O ASP A 190 4691 3666 4844 -557 1516 1047 O ATOM 178 CB ASP A 190 31.421 1.860 -26.677 1.00 28.30 C ANISOU 178 CB ASP A 190 4086 3419 3250 -710 1426 761 C ATOM 179 CG ASP A 190 32.834 1.314 -26.857 1.00 31.98 C ANISOU 179 CG ASP A 190 4541 4176 3433 -819 1602 453 C ATOM 180 OD1 ASP A 190 33.317 1.282 -28.009 1.00 33.09 O ANISOU 180 OD1 ASP A 190 4863 4447 3261 -914 1612 497 O ATOM 181 OD2 ASP A 190 33.466 0.919 -25.857 1.00 32.62 O ANISOU 181 OD2 ASP A 190 4432 4370 3593 -798 1729 165 O ATOM 182 N SER A 191 28.481 2.065 -25.226 1.00 26.54 N ANISOU 182 N SER A 191 3612 2752 3719 -353 1006 1149 N ATOM 183 CA SER A 191 27.268 2.880 -25.277 1.00 31.64 C ANISOU 183 CA SER A 191 4298 3164 4562 -258 883 1466 C ATOM 184 C SER A 191 26.795 3.424 -23.931 1.00 31.72 C ANISOU 184 C SER A 191 4110 3005 4939 -159 956 1464 C ATOM 185 O SER A 191 26.053 4.403 -23.882 1.00 33.93 O ANISOU 185 O SER A 191 4441 3076 5377 -95 943 1703 O ATOM 186 CB SER A 191 26.132 2.070 -25.875 1.00 27.35 C ANISOU 186 CB SER A 191 3766 2661 3964 -139 525 1629 C ATOM 187 OG SER A 191 25.666 1.133 -24.913 1.00 24.99 O ANISOU 187 OG SER A 191 3235 2420 3841 -32 389 1493 O ATOM 188 N GLY A 192 27.200 2.777 -22.846 1.00 30.59 N ANISOU 188 N GLY A 192 3749 2954 4920 -127 1025 1197 N ATOM 189 CA GLY A 192 26.697 3.120 -21.529 1.00 30.21 C ANISOU 189 CA GLY A 192 3492 2769 5217 -9 1067 1181 C ATOM 190 C GLY A 192 25.302 2.561 -21.283 1.00 32.97 C ANISOU 190 C GLY A 192 3717 3086 5724 161 764 1337 C ATOM 191 O GLY A 192 24.685 2.835 -20.255 1.00 33.83 O ANISOU 191 O GLY A 192 3650 3086 6119 282 759 1368 O ATOM 192 N ASP A 193 24.803 1.773 -22.230 1.00 30.75 N ANISOU 192 N ASP A 193 3524 2910 5249 169 510 1434 N ATOM 193 CA ASP A 193 23.452 1.226 -22.139 1.00 29.84 C ANISOU 193 CA ASP A 193 3300 2788 5251 303 207 1594 C ATOM 194 C ASP A 193 23.402 -0.221 -21.665 1.00 28.04 C ANISOU 194 C ASP A 193 2925 2720 5008 330 62 1390 C ATOM 195 O ASP A 193 22.357 -0.857 -21.750 1.00 28.28 O ANISOU 195 O ASP A 193 2887 2780 5079 401 -207 1504 O ATOM 196 CB ASP A 193 22.748 1.331 -23.491 1.00 29.94 C ANISOU 196 CB ASP A 193 3503 2797 5074 304 -12 1861 C ATOM 197 CG ASP A 193 22.418 2.763 -23.862 1.00 38.25 C ANISOU 197 CG ASP A 193 4696 3657 6183 331 71 2118 C ATOM 198 OD1 ASP A 193 21.910 3.491 -22.989 1.00 43.10 O ANISOU 198 OD1 ASP A 193 5190 4124 7063 434 129 2196 O ATOM 199 OD2 ASP A 193 22.663 3.155 -25.021 1.00 38.61 O ANISOU 199 OD2 ASP A 193 4980 3693 5996 259 78 2242 O ATOM 200 N LEU A 194 24.519 -0.749 -21.178 1.00 20.49 N ANISOU 200 N LEU A 194 2532 2250 3003 -205 601 713 N ATOM 201 CA LEU A 194 24.551 -2.168 -20.796 1.00 26.45 C ANISOU 201 CA LEU A 194 3280 3022 3747 -211 506 649 C ATOM 202 C LEU A 194 23.410 -2.583 -19.850 1.00 25.55 C ANISOU 202 C LEU A 194 3152 2869 3689 -192 481 701 C ATOM 203 O LEU A 194 22.828 -3.651 -20.010 1.00 23.54 O ANISOU 203 O LEU A 194 2877 2640 3428 -189 394 706 O ATOM 204 CB LEU A 194 25.912 -2.563 -20.207 1.00 17.99 C ANISOU 204 CB LEU A 194 2231 1948 2657 -231 508 524 C ATOM 205 CG LEU A 194 26.013 -4.008 -19.690 1.00 22.72 C ANISOU 205 CG LEU A 194 2824 2559 3250 -235 420 455 C ATOM 206 CD1 LEU A 194 27.397 -4.601 -19.963 1.00 20.18 C ANISOU 206 CD1 LEU A 194 2516 2276 2877 -255 395 344 C ATOM 207 CD2 LEU A 194 25.664 -4.084 -18.202 1.00 26.00 C ANISOU 207 CD2 LEU A 194 3243 2915 3722 -225 439 450 C ATOM 208 N MET A 195 23.087 -1.743 -18.872 1.00 24.84 N ANISOU 208 N MET A 195 3073 2715 3652 -179 559 739 N ATOM 209 CA MET A 195 22.062 -2.103 -17.894 1.00 26.12 C ANISOU 209 CA MET A 195 3223 2834 3867 -158 543 787 C ATOM 210 C MET A 195 20.692 -2.339 -18.536 1.00 28.05 C ANISOU 210 C MET A 195 3432 3101 4124 -140 496 899 C ATOM 211 O MET A 195 19.910 -3.141 -18.043 1.00 23.21 O ANISOU 211 O MET A 195 2801 2480 3540 -128 439 922 O ATOM 212 CB MET A 195 21.976 -1.067 -16.772 1.00 24.64 C ANISOU 212 CB MET A 195 3061 2570 3730 -147 645 811 C ATOM 213 CG MET A 195 23.208 -1.048 -15.872 1.00 19.53 C ANISOU 213 CG MET A 195 2447 1898 3077 -168 676 697 C ATOM 214 SD MET A 195 23.386 -2.576 -14.918 1.00 24.30 S ANISOU 214 SD MET A 195 3043 2505 3685 -169 587 611 S ATOM 215 CE MET A 195 21.890 -2.551 -13.947 1.00 23.24 C ANISOU 215 CE MET A 195 2898 2311 3621 -133 599 711 C ATOM 216 N LYS A 196 20.408 -1.656 -19.641 1.00 22.64 N ANISOU 216 N LYS A 196 2736 2448 3419 -137 518 970 N ATOM 217 CA LYS A 196 19.182 -1.932 -20.392 1.00 26.86 C ANISOU 217 CA LYS A 196 3232 3018 3956 -125 464 1074 C ATOM 218 C LYS A 196 19.194 -3.313 -21.046 1.00 27.07 C ANISOU 218 C LYS A 196 3242 3105 3939 -143 342 1027 C ATOM 219 O LYS A 196 18.194 -4.021 -21.020 1.00 30.90 O ANISOU 219 O LYS A 196 3698 3599 4441 -137 275 1080 O ATOM 220 CB LYS A 196 18.938 -0.852 -21.447 1.00 29.39 C ANISOU 220 CB LYS A 196 3543 3362 4260 -117 518 1161 C ATOM 221 CG LYS A 196 18.630 0.525 -20.867 1.00 38.35 C ANISOU 221 CG LYS A 196 4692 4435 5445 -94 639 1234 C ATOM 222 CD LYS A 196 18.552 1.572 -21.974 1.00 49.02 C ANISOU 222 CD LYS A 196 6036 5815 6775 -87 696 1309 C ATOM 223 CE LYS A 196 18.632 2.993 -21.427 1.00 51.61 C ANISOU 223 CE LYS A 196 6390 6077 7143 -71 830 1351 C ATOM 224 NZ LYS A 196 17.363 3.408 -20.768 1.00 50.22 N ANISOU 224 NZ LYS A 196 6200 5852 7030 -38 872 1469 N ATOM 225 N PHE A 197 20.322 -3.693 -21.641 1.00 21.66 N ANISOU 225 N PHE A 197 2575 2459 3195 -166 316 929 N ATOM 226 CA PHE A 197 20.451 -5.027 -22.238 1.00 21.20 C ANISOU 226 CA PHE A 197 2510 2454 3091 -184 207 873 C ATOM 227 C PHE A 197 20.386 -6.152 -21.201 1.00 20.11 C ANISOU 227 C PHE A 197 2372 2290 2980 -185 152 815 C ATOM 228 O PHE A 197 19.724 -7.171 -21.408 1.00 22.52 O ANISOU 228 O PHE A 197 2659 2618 3281 -190 65 828 O ATOM 229 CB PHE A 197 21.773 -5.144 -23.001 1.00 21.66 C ANISOU 229 CB PHE A 197 2594 2553 3083 -204 204 778 C ATOM 230 CG PHE A 197 21.783 -4.413 -24.307 1.00 26.31 C ANISOU 230 CG PHE A 197 3179 3188 3631 -206 226 830 C ATOM 231 CD1 PHE A 197 21.528 -5.082 -25.492 1.00 32.51 C ANISOU 231 CD1 PHE A 197 3954 4036 4362 -217 146 840 C ATOM 232 CD2 PHE A 197 22.049 -3.055 -24.353 1.00 27.22 C ANISOU 232 CD2 PHE A 197 3303 3281 3761 -196 327 868 C ATOM 233 CE1 PHE A 197 21.541 -4.406 -26.702 1.00 31.27 C ANISOU 233 CE1 PHE A 197 3794 3924 4164 -216 166 889 C ATOM 234 CE2 PHE A 197 22.058 -2.376 -25.559 1.00 30.72 C ANISOU 234 CE2 PHE A 197 3740 3766 4166 -194 350 918 C ATOM 235 CZ PHE A 197 21.804 -3.055 -26.733 1.00 26.94 C ANISOU 235 CZ PHE A 197 3249 3353 3632 -203 269 930 C ATOM 236 N ALA A 198 21.089 -5.965 -20.090 1.00 19.20 N ANISOU 236 N ALA A 198 2279 2127 2890 -182 204 750 N ATOM 237 CA ALA A 198 21.265 -7.036 -19.109 1.00 18.19 C ANISOU 237 CA ALA A 198 2153 1978 2780 -182 157 679 C ATOM 238 C ALA A 198 19.970 -7.454 -18.404 1.00 16.77 C ANISOU 238 C ALA A 198 1947 1767 2658 -163 125 753 C ATOM 239 O ALA A 198 19.884 -8.567 -17.885 1.00 20.52 O ANISOU 239 O ALA A 198 2416 2239 3143 -164 62 708 O ATOM 240 CB ALA A 198 22.331 -6.645 -18.089 1.00 15.13 C ANISOU 240 CB ALA A 198 1793 1551 2405 -184 224 598 C ATOM 241 N VAL A 199 18.974 -6.566 -18.372 1.00 22.06 N ANISOU 241 N VAL A 199 2601 2413 3368 -143 172 868 N ATOM 242 CA VAL A 199 17.681 -6.900 -17.753 1.00 28.24 C ANISOU 242 CA VAL A 199 3355 3166 4208 -122 145 952 C ATOM 243 C VAL A 199 16.607 -7.272 -18.783 1.00 30.43 C ANISOU 243 C VAL A 199 3596 3490 4474 -126 73 1042 C ATOM 244 O VAL A 199 15.444 -7.482 -18.440 1.00 30.78 O ANISOU 244 O VAL A 199 3611 3519 4566 -110 49 1128 O ATOM 245 CB VAL A 199 17.144 -5.763 -16.847 1.00 21.98 C ANISOU 245 CB VAL A 199 2568 2307 3477 -93 244 1030 C ATOM 246 CG1 VAL A 199 18.118 -5.474 -15.718 1.00 20.55 C ANISOU 246 CG1 VAL A 199 2424 2077 3309 -92 307 941 C ATOM 247 CG2 VAL A 199 16.856 -4.496 -17.662 1.00 25.05 C ANISOU 247 CG2 VAL A 199 2953 2705 3858 -87 311 1120 C ATOM 248 N ASP A 200 17.010 -7.361 -20.041 1.00 26.65 N ANISOU 248 N ASP A 200 3120 3072 3933 -149 39 1022 N ATOM 249 CA ASP A 200 16.108 -7.716 -21.129 1.00 27.81 C ANISOU 249 CA ASP A 200 3236 3274 4057 -160 -33 1098 C ATOM 250 C ASP A 200 16.402 -9.150 -21.557 1.00 29.43 C ANISOU 250 C ASP A 200 3445 3520 4218 -187 -141 1015 C ATOM 251 O ASP A 200 17.564 -9.535 -21.677 1.00 25.01 O ANISOU 251 O ASP A 200 2915 2972 3614 -201 -146 903 O ATOM 252 CB ASP A 200 16.338 -6.761 -22.298 1.00 29.34 C ANISOU 252 CB ASP A 200 3433 3509 4207 -165 7 1137 C ATOM 253 CG ASP A 200 15.451 -7.068 -23.497 1.00 38.54 C ANISOU 253 CG ASP A 200 4566 4736 5341 -178 -67 1217 C ATOM 254 OD1 ASP A 200 14.248 -6.725 -23.462 1.00 36.14 O ANISOU 254 OD1 ASP A 200 4226 4428 5078 -163 -65 1339 O ATOM 255 OD2 ASP A 200 15.968 -7.633 -24.483 1.00 36.84 O ANISOU 255 OD2 ASP A 200 4363 4576 5059 -203 -126 1160 O ATOM 256 N LYS A 201 15.369 -9.954 -21.789 1.00 27.53 N ANISOU 256 N LYS A 201 3174 3299 3988 -195 -224 1069 N ATOM 257 CA LYS A 201 15.616 -11.355 -22.118 1.00 27.33 C ANISOU 257 CA LYS A 201 3157 3304 3924 -222 -324 988 C ATOM 258 C LYS A 201 16.535 -11.486 -23.328 1.00 29.71 C ANISOU 258 C LYS A 201 3486 3662 4141 -247 -346 919 C ATOM 259 O LYS A 201 17.551 -12.177 -23.279 1.00 28.78 O ANISOU 259 O LYS A 201 3400 3549 3988 -258 -364 805 O ATOM 260 CB LYS A 201 14.313 -12.122 -22.354 1.00 31.02 C ANISOU 260 CB LYS A 201 3586 3790 4410 -233 -413 1065 C ATOM 261 CG LYS A 201 14.538 -13.597 -22.671 1.00 39.60 C ANISOU 261 CG LYS A 201 4685 4902 5457 -263 -514 980 C ATOM 262 CD LYS A 201 13.223 -14.333 -22.878 1.00 47.18 C ANISOU 262 CD LYS A 201 5608 5879 6440 -278 -602 1059 C ATOM 263 CE LYS A 201 13.430 -15.663 -23.599 1.00 51.69 C ANISOU 263 CE LYS A 201 6197 6489 6954 -317 -704 983 C ATOM 264 NZ LYS A 201 14.287 -16.618 -22.837 1.00 44.74 N ANISOU 264 NZ LYS A 201 5347 5577 6076 -315 -714 860 N ATOM 265 N THR A 202 16.176 -10.811 -24.411 1.00 25.42 N ANISOU 265 N THR A 202 2932 3162 3566 -253 -341 992 N ATOM 266 CA THR A 202 16.934 -10.889 -25.651 1.00 27.70 C ANISOU 266 CA THR A 202 3245 3507 3773 -274 -362 940 C ATOM 267 C THR A 202 18.309 -10.243 -25.528 1.00 25.57 C ANISOU 267 C THR A 202 3010 3224 3481 -265 -281 859 C ATOM 268 O THR A 202 19.307 -10.789 -25.999 1.00 27.78 O ANISOU 268 O THR A 202 3322 3529 3704 -280 -304 762 O ATOM 269 CB THR A 202 16.165 -10.217 -26.811 1.00 35.81 C ANISOU 269 CB THR A 202 4248 4585 4774 -279 -370 1049 C ATOM 270 OG1 THR A 202 14.871 -10.825 -26.942 1.00 39.62 O ANISOU 270 OG1 THR A 202 4695 5085 5276 -291 -449 1129 O ATOM 271 CG2 THR A 202 16.933 -10.364 -28.118 1.00 37.12 C ANISOU 271 CG2 THR A 202 4442 4811 4851 -300 -397 995 C ATOM 272 N GLY A 203 18.358 -9.072 -24.905 1.00 23.48 N ANISOU 272 N GLY A 203 2741 2919 3262 -241 -185 901 N ATOM 273 CA GLY A 203 19.614 -8.373 -24.719 1.00 25.75 C ANISOU 273 CA GLY A 203 3059 3190 3534 -236 -104 831 C ATOM 274 C GLY A 203 20.593 -9.171 -23.873 1.00 28.17 C ANISOU 274 C GLY A 203 3391 3471 3841 -241 -114 709 C ATOM 275 O GLY A 203 21.780 -9.239 -24.181 1.00 23.91 O ANISOU 275 O GLY A 203 2878 2949 3256 -250 -99 622 O ATOM 276 N CYS A 204 20.106 -9.782 -22.800 1.00 23.94 N ANISOU 276 N CYS A 204 2843 2895 3356 -233 -138 706 N ATOM 277 CA CYS A 204 21.001 -10.510 -21.910 1.00 19.79 C ANISOU 277 CA CYS A 204 2338 2345 2835 -235 -142 597 C ATOM 278 C CYS A 204 21.486 -11.801 -22.565 1.00 24.39 C ANISOU 278 C CYS A 204 2936 2971 3360 -256 -227 515 C ATOM 279 O CYS A 204 22.603 -12.258 -22.319 1.00 22.04 O ANISOU 279 O CYS A 204 2662 2674 3037 -260 -222 414 O ATOM 280 CB CYS A 204 20.335 -10.809 -20.573 1.00 22.30 C ANISOU 280 CB CYS A 204 2640 2609 3224 -217 -142 618 C ATOM 281 SG CYS A 204 21.545 -11.189 -19.263 1.00 29.90 S ANISOU 281 SG CYS A 204 3627 3533 4201 -212 -108 497 S ATOM 282 N GLN A 205 20.636 -12.374 -23.404 1.00 22.27 N ANISOU 282 N GLN A 205 2655 2738 3070 -269 -303 562 N ATOM 283 CA GLN A 205 20.980 -13.563 -24.166 1.00 25.00 C ANISOU 283 CA GLN A 205 3019 3124 3355 -291 -384 494 C ATOM 284 C GLN A 205 22.174 -13.261 -25.055 1.00 26.55 C ANISOU 284 C GLN A 205 3247 3357 3482 -298 -356 432 C ATOM 285 O GLN A 205 23.121 -14.049 -25.130 1.00 25.06 O ANISOU 285 O GLN A 205 3087 3180 3256 -306 -377 334 O ATOM 286 CB GLN A 205 19.782 -13.979 -25.022 1.00 33.07 C ANISOU 286 CB GLN A 205 4021 4180 4363 -308 -464 571 C ATOM 287 CG GLN A 205 19.904 -15.328 -25.688 1.00 37.20 C ANISOU 287 CG GLN A 205 4566 4738 4832 -334 -556 508 C ATOM 288 CD GLN A 205 18.649 -15.688 -26.475 1.00 48.83 C ANISOU 288 CD GLN A 205 6016 6244 6293 -356 -636 590 C ATOM 289 OE1 GLN A 205 18.376 -15.119 -27.540 1.00 46.86 O ANISOU 289 OE1 GLN A 205 5763 6038 6003 -365 -641 646 O ATOM 290 NE2 GLN A 205 17.874 -16.631 -25.948 1.00 43.87 N ANISOU 290 NE2 GLN A 205 5372 5597 5701 -364 -700 600 N ATOM 291 N PHE A 206 22.133 -12.110 -25.720 1.00 26.07 N ANISOU 291 N PHE A 206 3182 3315 3409 -294 -305 492 N ATOM 292 CA PHE A 206 23.255 -11.665 -26.541 1.00 26.76 C ANISOU 292 CA PHE A 206 3296 3433 3437 -298 -267 443 C ATOM 293 C PHE A 206 24.528 -11.480 -25.702 1.00 25.55 C ANISOU 293 C PHE A 206 3162 3251 3295 -290 -204 355 C ATOM 294 O PHE A 206 25.581 -12.012 -26.041 1.00 23.26 O ANISOU 294 O PHE A 206 2899 2982 2957 -296 -214 268 O ATOM 295 CB PHE A 206 22.902 -10.371 -27.286 1.00 29.25 C ANISOU 295 CB PHE A 206 3598 3768 3747 -291 -215 533 C ATOM 296 CG PHE A 206 24.098 -9.641 -27.822 1.00 30.38 C ANISOU 296 CG PHE A 206 3765 3928 3849 -288 -150 489 C ATOM 297 CD1 PHE A 206 24.784 -10.124 -28.923 1.00 32.43 C ANISOU 297 CD1 PHE A 206 4050 4237 4033 -299 -185 437 C ATOM 298 CD2 PHE A 206 24.545 -8.474 -27.216 1.00 30.43 C ANISOU 298 CD2 PHE A 206 3769 3899 3894 -274 -53 501 C ATOM 299 CE1 PHE A 206 25.893 -9.456 -29.414 1.00 35.83 C ANISOU 299 CE1 PHE A 206 4501 4683 4429 -294 -124 400 C ATOM 300 CE2 PHE A 206 25.656 -7.802 -27.701 1.00 35.84 C ANISOU 300 CE2 PHE A 206 4474 4599 4546 -274 7 462 C ATOM 301 CZ PHE A 206 26.330 -8.297 -28.802 1.00 37.42 C ANISOU 301 CZ PHE A 206 4695 4850 4671 -282 -29 413 C ATOM 302 N LEU A 207 24.424 -10.738 -24.602 1.00 23.71 N ANISOU 302 N LEU A 207 2916 2968 3125 -276 -139 379 N ATOM 303 CA LEU A 207 25.571 -10.537 -23.717 1.00 19.48 C ANISOU 303 CA LEU A 207 2395 2404 2603 -272 -81 300 C ATOM 304 C LEU A 207 26.159 -11.852 -23.203 1.00 17.20 C ANISOU 304 C LEU A 207 2118 2114 2302 -276 -132 204 C ATOM 305 O LEU A 207 27.374 -12.037 -23.215 1.00 21.35 O ANISOU 305 O LEU A 207 2664 2652 2795 -280 -112 121 O ATOM 306 CB LEU A 207 25.209 -9.619 -22.548 1.00 19.27 C ANISOU 306 CB LEU A 207 2355 2320 2646 -258 -10 344 C ATOM 307 CG LEU A 207 24.933 -8.180 -22.982 1.00 24.41 C ANISOU 307 CG LEU A 207 3001 2966 3308 -251 64 425 C ATOM 308 CD1 LEU A 207 24.526 -7.309 -21.798 1.00 22.32 C ANISOU 308 CD1 LEU A 207 2729 2639 3112 -237 136 470 C ATOM 309 CD2 LEU A 207 26.154 -7.601 -23.705 1.00 22.60 C ANISOU 309 CD2 LEU A 207 2792 2764 3029 -260 111 376 C ATOM 310 N GLU A 208 25.295 -12.766 -22.766 1.00 20.15 N ANISOU 310 N GLU A 208 2479 2475 2703 -275 -195 218 N ATOM 311 CA GLU A 208 25.738 -14.054 -22.235 1.00 20.77 C ANISOU 311 CA GLU A 208 2567 2549 2776 -276 -243 135 C ATOM 312 C GLU A 208 26.531 -14.864 -23.258 1.00 23.78 C ANISOU 312 C GLU A 208 2977 2978 3083 -289 -285 65 C ATOM 313 O GLU A 208 27.482 -15.549 -22.904 1.00 27.36 O ANISOU 313 O GLU A 208 3445 3431 3518 -287 -287 -21 O ATOM 314 CB GLU A 208 24.551 -14.873 -21.716 1.00 28.19 C ANISOU 314 CB GLU A 208 3486 3467 3759 -273 -306 173 C ATOM 315 CG GLU A 208 24.238 -14.627 -20.249 1.00 26.58 C ANISOU 315 CG GLU A 208 3264 3208 3628 -254 -268 189 C ATOM 316 CD GLU A 208 25.306 -15.203 -19.339 1.00 36.09 C ANISOU 316 CD GLU A 208 4480 4397 4834 -249 -252 90 C ATOM 317 OE1 GLU A 208 25.247 -16.414 -19.026 1.00 36.64 O ANISOU 317 OE1 GLU A 208 4550 4466 4906 -247 -308 47 O ATOM 318 OE2 GLU A 208 26.213 -14.443 -18.941 1.00 30.86 O ANISOU 318 OE2 GLU A 208 3827 3726 4171 -246 -183 57 O ATOM 319 N LYS A 209 26.132 -14.792 -24.522 1.00 22.24 N ANISOU 319 N LYS A 209 2788 2822 2842 -300 -319 105 N ATOM 320 CA LYS A 209 26.840 -15.506 -25.579 1.00 25.67 C ANISOU 320 CA LYS A 209 3254 3299 3200 -311 -356 44 C ATOM 321 C LYS A 209 28.153 -14.790 -25.898 1.00 27.42 C ANISOU 321 C LYS A 209 3493 3537 3387 -306 -288 -1 C ATOM 322 O LYS A 209 29.198 -15.420 -26.069 1.00 25.06 O ANISOU 322 O LYS A 209 3219 3254 3048 -306 -291 -82 O ATOM 323 CB LYS A 209 25.960 -15.599 -26.827 1.00 36.87 C ANISOU 323 CB LYS A 209 4675 4756 4579 -326 -414 104 C ATOM 324 CG LYS A 209 26.638 -16.197 -28.047 1.00 45.18 C ANISOU 324 CG LYS A 209 5766 5855 5546 -338 -448 50 C ATOM 325 CD LYS A 209 26.664 -17.717 -27.977 1.00 56.42 C ANISOU 325 CD LYS A 209 7211 7277 6949 -348 -520 -16 C ATOM 326 CE LYS A 209 26.899 -18.322 -29.354 1.00 64.68 C ANISOU 326 CE LYS A 209 8297 8369 7909 -363 -569 -45 C ATOM 327 NZ LYS A 209 26.937 -19.811 -29.310 1.00 67.98 N ANISOU 327 NZ LYS A 209 8743 8782 8305 -374 -635 -111 N ATOM 328 N ALA A 210 28.096 -13.463 -25.964 1.00 21.21 N ANISOU 328 N ALA A 210 2694 2745 2620 -302 -222 55 N ATOM 329 CA ALA A 210 29.278 -12.674 -26.281 1.00 23.61 C ANISOU 329 CA ALA A 210 3011 3063 2897 -299 -153 22 C ATOM 330 C ALA A 210 30.390 -12.845 -25.241 1.00 19.96 C ANISOU 330 C ALA A 210 2553 2578 2454 -295 -114 -59 C ATOM 331 O ALA A 210 31.565 -12.941 -25.598 1.00 23.55 O ANISOU 331 O ALA A 210 3026 3056 2866 -295 -92 -120 O ATOM 332 CB ALA A 210 28.902 -11.207 -26.442 1.00 21.63 C ANISOU 332 CB ALA A 210 2743 2803 2671 -294 -88 103 C ATOM 333 N VAL A 211 30.031 -12.902 -23.959 1.00 18.37 N ANISOU 333 N VAL A 211 2333 2333 2313 -290 -105 -56 N ATOM 334 CA VAL A 211 31.058 -13.006 -22.913 1.00 19.16 C ANISOU 334 CA VAL A 211 2435 2414 2432 -287 -66 -128 C ATOM 335 C VAL A 211 31.677 -14.399 -22.767 1.00 20.94 C ANISOU 335 C VAL A 211 2673 2655 2629 -285 -115 -210 C ATOM 336 O VAL A 211 32.607 -14.589 -21.991 1.00 22.64 O ANISOU 336 O VAL A 211 2887 2862 2851 -283 -88 -272 O ATOM 337 CB VAL A 211 30.580 -12.470 -21.536 1.00 19.39 C ANISOU 337 CB VAL A 211 2444 2391 2533 -282 -28 -100 C ATOM 338 CG1 VAL A 211 30.131 -11.017 -21.666 1.00 24.98 C ANISOU 338 CG1 VAL A 211 3144 3080 3267 -282 35 -23 C ATOM 339 CG2 VAL A 211 29.457 -13.332 -20.962 1.00 23.74 C ANISOU 339 CG2 VAL A 211 2981 2919 3122 -274 -89 -74 C ATOM 340 N LYS A 212 31.183 -15.365 -23.531 1.00 21.71 N ANISOU 340 N LYS A 212 2783 2774 2692 -288 -186 -211 N ATOM 341 CA LYS A 212 31.788 -16.695 -23.553 1.00 26.19 C ANISOU 341 CA LYS A 212 3369 3356 3226 -285 -230 -287 C ATOM 342 C LYS A 212 32.877 -16.828 -24.617 1.00 30.91 C ANISOU 342 C LYS A 212 3996 3997 3753 -286 -219 -335 C ATOM 343 O LYS A 212 33.598 -17.832 -24.658 1.00 27.95 O ANISOU 343 O LYS A 212 3639 3635 3345 -281 -240 -402 O ATOM 344 CB LYS A 212 30.717 -17.766 -23.779 1.00 30.80 C ANISOU 344 CB LYS A 212 3956 3937 3810 -289 -312 -270 C ATOM 345 CG LYS A 212 29.799 -17.989 -22.578 1.00 40.76 C ANISOU 345 CG LYS A 212 5189 5155 5142 -283 -328 -241 C ATOM 346 CD LYS A 212 28.831 -19.142 -22.832 1.00 51.21 C ANISOU 346 CD LYS A 212 6516 6477 6464 -290 -412 -229 C ATOM 347 CE LYS A 212 28.009 -19.474 -21.591 1.00 58.01 C ANISOU 347 CE LYS A 212 7349 7295 7397 -280 -428 -206 C ATOM 348 NZ LYS A 212 27.074 -18.379 -21.202 1.00 55.27 N ANISOU 348 NZ LYS A 212 6973 6922 7103 -277 -399 -116 N ATOM 349 N GLY A 213 32.987 -15.831 -25.490 1.00 25.01 N ANISOU 349 N GLY A 213 3252 3270 2980 -290 -186 -296 N ATOM 350 CA GLY A 213 33.969 -15.879 -26.565 1.00 24.13 C ANISOU 350 CA GLY A 213 3169 3200 2801 -289 -173 -333 C ATOM 351 C GLY A 213 35.297 -15.251 -26.182 1.00 24.39 C ANISOU 351 C GLY A 213 3197 3235 2835 -284 -100 -373 C ATOM 352 O GLY A 213 35.584 -15.058 -25.000 1.00 22.62 O ANISOU 352 O GLY A 213 2952 2984 2658 -284 -69 -392 O ATOM 353 N SER A 214 36.119 -14.939 -27.178 1.00 19.70 N ANISOU 353 N SER A 214 2622 2676 2188 -282 -74 -387 N ATOM 354 CA SER A 214 37.374 -14.241 -26.935 1.00 24.39 C ANISOU 354 CA SER A 214 3208 3276 2782 -280 -4 -417 C ATOM 355 C SER A 214 37.054 -12.824 -26.497 1.00 25.56 C ANISOU 355 C SER A 214 3332 3400 2979 -289 54 -362 C ATOM 356 O SER A 214 36.219 -12.157 -27.096 1.00 31.84 O ANISOU 356 O SER A 214 4126 4195 3777 -291 54 -296 O ATOM 357 CB SER A 214 38.220 -14.204 -28.207 1.00 30.97 C ANISOU 357 CB SER A 214 4068 4152 3547 -273 10 -434 C ATOM 358 OG SER A 214 38.440 -15.517 -28.690 1.00 28.36 O ANISOU 358 OG SER A 214 3767 3841 3167 -264 -41 -481 O ATOM 359 N LEU A 215 37.700 -12.374 -25.433 1.00 21.92 N ANISOU 359 N LEU A 215 2854 2918 2558 -295 103 -388 N ATOM 360 CA LEU A 215 37.527 -11.005 -24.981 1.00 19.82 C ANISOU 360 CA LEU A 215 2570 2625 2336 -305 166 -343 C ATOM 361 C LEU A 215 38.893 -10.346 -24.902 1.00 22.81 C ANISOU 361 C LEU A 215 2945 3015 2705 -314 232 -380 C ATOM 362 O LEU A 215 39.835 -10.934 -24.383 1.00 20.02 O ANISOU 362 O LEU A 215 2590 2673 2345 -315 232 -443 O ATOM 363 CB LEU A 215 36.867 -10.980 -23.602 1.00 15.25 C ANISOU 363 CB LEU A 215 1973 1999 1821 -310 166 -334 C ATOM 364 CG LEU A 215 35.499 -11.666 -23.466 1.00 14.43 C ANISOU 364 CG LEU A 215 1866 1878 1738 -302 102 -296 C ATOM 365 CD1 LEU A 215 35.082 -11.671 -22.007 1.00 16.02 C ANISOU 365 CD1 LEU A 215 2050 2034 2001 -303 110 -297 C ATOM 366 CD2 LEU A 215 34.461 -10.930 -24.288 1.00 21.85 C ANISOU 366 CD2 LEU A 215 2806 2818 2679 -301 102 -212 C ATOM 367 N THR A 216 38.993 -9.130 -25.426 1.00 16.02 N ANISOU 367 N THR A 216 2085 2156 1848 -320 287 -339 N ATOM 368 CA THR A 216 40.195 -8.338 -25.273 1.00 18.50 C ANISOU 368 CA THR A 216 2392 2474 2161 -332 355 -365 C ATOM 369 C THR A 216 40.227 -7.814 -23.858 1.00 19.97 C ANISOU 369 C THR A 216 2562 2618 2405 -351 392 -375 C ATOM 370 O THR A 216 39.207 -7.789 -23.170 1.00 19.07 O ANISOU 370 O THR A 216 2444 2469 2332 -350 377 -344 O ATOM 371 CB THR A 216 40.196 -7.120 -26.207 1.00 23.05 C ANISOU 371 CB THR A 216 2972 3058 2729 -334 408 -312 C ATOM 372 OG1 THR A 216 39.171 -6.208 -25.796 1.00 24.58 O ANISOU 372 OG1 THR A 216 3158 3210 2972 -339 436 -249 O ATOM 373 CG2 THR A 216 39.946 -7.539 -27.639 1.00 24.60 C ANISOU 373 CG2 THR A 216 3186 3294 2869 -315 370 -291 C ATOM 374 N SER A 217 41.411 -7.399 -23.429 1.00 15.63 N ANISOU 374 N SER A 217 2005 2075 1858 -367 440 -416 N ATOM 375 CA SER A 217 41.607 -6.847 -22.100 1.00 14.60 C ANISOU 375 CA SER A 217 1863 1908 1777 -390 479 -432 C ATOM 376 C SER A 217 40.612 -5.732 -21.801 1.00 18.39 C ANISOU 376 C SER A 217 2346 2339 2302 -397 519 -368 C ATOM 377 O SER A 217 40.042 -5.663 -20.706 1.00 19.69 O ANISOU 377 O SER A 217 2507 2464 2509 -403 520 -363 O ATOM 378 CB SER A 217 43.037 -6.299 -21.986 1.00 15.16 C ANISOU 378 CB SER A 217 1925 1997 1837 -412 532 -472 C ATOM 379 OG SER A 217 43.240 -5.710 -20.719 1.00 26.28 O ANISOU 379 OG SER A 217 3326 3371 3288 -439 570 -489 O ATOM 380 N TYR A 218 40.395 -4.850 -22.769 1.00 19.09 N ANISOU 380 N TYR A 218 2441 2430 2381 -394 554 -317 N ATOM 381 CA TYR A 218 39.537 -3.699 -22.500 1.00 18.44 C ANISOU 381 CA TYR A 218 2362 2302 2343 -400 604 -253 C ATOM 382 C TYR A 218 38.078 -4.113 -22.393 1.00 15.75 C ANISOU 382 C TYR A 218 2022 1941 2023 -380 558 -200 C ATOM 383 O TYR A 218 37.334 -3.561 -21.591 1.00 16.95 O ANISOU 383 O TYR A 218 2173 2044 2222 -383 585 -164 O ATOM 384 CB TYR A 218 39.695 -2.603 -23.550 1.00 16.57 C ANISOU 384 CB TYR A 218 2130 2073 2093 -400 660 -207 C ATOM 385 CG TYR A 218 38.965 -1.336 -23.167 1.00 17.64 C ANISOU 385 CG TYR A 218 2269 2156 2276 -408 726 -144 C ATOM 386 CD1 TYR A 218 39.238 -0.691 -21.965 1.00 22.89 C ANISOU 386 CD1 TYR A 218 2938 2775 2983 -433 777 -165 C ATOM 387 CD2 TYR A 218 38.008 -0.783 -24.006 1.00 20.65 C ANISOU 387 CD2 TYR A 218 2652 2534 2659 -389 739 -64 C ATOM 388 CE1 TYR A 218 38.580 0.476 -21.611 1.00 24.57 C ANISOU 388 CE1 TYR A 218 3162 2936 3240 -439 843 -108 C ATOM 389 CE2 TYR A 218 37.340 0.375 -23.659 1.00 21.45 C ANISOU 389 CE2 TYR A 218 2759 2586 2805 -392 805 -2 C ATOM 390 CZ TYR A 218 37.633 1.004 -22.465 1.00 29.54 C ANISOU 390 CZ TYR A 218 3792 3561 3872 -417 859 -26 C ATOM 391 OH TYR A 218 36.965 2.156 -22.120 1.00 31.84 O ANISOU 391 OH TYR A 218 4093 3797 4206 -419 930 36 O ATOM 392 N GLN A 219 37.666 -5.084 -23.201 1.00 15.24 N ANISOU 392 N GLN A 219 1958 1911 1923 -360 490 -195 N ATOM 393 CA GLN A 219 36.306 -5.600 -23.077 1.00 15.68 C ANISOU 393 CA GLN A 219 2009 1950 1997 -344 437 -148 C ATOM 394 C GLN A 219 36.078 -6.128 -21.667 1.00 19.03 C ANISOU 394 C GLN A 219 2428 2340 2463 -348 419 -178 C ATOM 395 O GLN A 219 35.064 -5.827 -21.038 1.00 16.62 O ANISOU 395 O GLN A 219 2118 1993 2202 -343 426 -130 O ATOM 396 CB GLN A 219 36.026 -6.678 -24.131 1.00 15.43 C ANISOU 396 CB GLN A 219 1983 1964 1915 -329 361 -150 C ATOM 397 CG GLN A 219 35.879 -6.092 -25.536 1.00 21.75 C ANISOU 397 CG GLN A 219 2790 2796 2680 -321 375 -99 C ATOM 398 CD GLN A 219 35.801 -7.155 -26.604 1.00 22.02 C ANISOU 398 CD GLN A 219 2834 2877 2655 -310 303 -113 C ATOM 399 OE1 GLN A 219 36.372 -8.229 -26.458 1.00 20.46 O ANISOU 399 OE1 GLN A 219 2645 2697 2433 -309 260 -179 O ATOM 400 NE2 GLN A 219 35.087 -6.864 -27.680 1.00 23.89 N ANISOU 400 NE2 GLN A 219 3074 3135 2868 -301 290 -50 N ATOM 401 N LYS A 220 37.028 -6.904 -21.160 1.00 18.25 N ANISOU 401 N LYS A 220 2328 2258 2349 -354 400 -256 N ATOM 402 CA LYS A 220 36.926 -7.389 -19.784 1.00 15.63 C ANISOU 402 CA LYS A 220 1989 1896 2055 -357 386 -289 C ATOM 403 C LYS A 220 36.871 -6.236 -18.781 1.00 17.01 C ANISOU 403 C LYS A 220 2165 2021 2277 -373 457 -271 C ATOM 404 O LYS A 220 36.061 -6.255 -17.844 1.00 15.79 O ANISOU 404 O LYS A 220 2009 1825 2166 -367 454 -248 O ATOM 405 CB LYS A 220 38.103 -8.301 -19.445 1.00 14.00 C ANISOU 405 CB LYS A 220 1777 1720 1820 -361 364 -373 C ATOM 406 CG LYS A 220 38.128 -9.610 -20.250 1.00 15.79 C ANISOU 406 CG LYS A 220 2009 1990 2003 -343 293 -397 C ATOM 407 CD LYS A 220 39.370 -10.431 -19.888 1.00 21.50 C ANISOU 407 CD LYS A 220 2726 2742 2699 -345 283 -477 C ATOM 408 CE LYS A 220 39.613 -11.543 -20.898 1.00 37.14 C ANISOU 408 CE LYS A 220 4718 4766 4627 -328 230 -501 C ATOM 409 NZ LYS A 220 41.068 -11.817 -21.037 1.00 46.25 N ANISOU 409 NZ LYS A 220 5871 5958 5745 -331 249 -561 N ATOM 410 N PHE A 221 37.740 -5.248 -18.978 1.00 16.83 N ANISOU 410 N PHE A 221 2147 2000 2246 -394 521 -281 N ATOM 411 CA PHE A 221 37.825 -4.088 -18.088 1.00 20.34 C ANISOU 411 CA PHE A 221 2600 2397 2731 -415 595 -271 C ATOM 412 C PHE A 221 36.456 -3.425 -17.962 1.00 16.43 C ANISOU 412 C PHE A 221 2111 1853 2276 -401 617 -188 C ATOM 413 O PHE A 221 35.999 -3.097 -16.860 1.00 20.29 O ANISOU 413 O PHE A 221 2607 2294 2808 -405 642 -178 O ATOM 414 CB PHE A 221 38.857 -3.088 -18.621 1.00 20.48 C ANISOU 414 CB PHE A 221 2622 2428 2731 -439 659 -283 C ATOM 415 CG PHE A 221 39.154 -1.939 -17.674 1.00 20.89 C ANISOU 415 CG PHE A 221 2686 2432 2819 -468 735 -287 C ATOM 416 CD1 PHE A 221 40.095 -2.080 -16.664 1.00 21.95 C ANISOU 416 CD1 PHE A 221 2817 2566 2956 -495 744 -355 C ATOM 417 CD2 PHE A 221 38.498 -0.726 -17.803 1.00 24.32 C ANISOU 417 CD2 PHE A 221 3135 2823 3282 -470 799 -222 C ATOM 418 CE1 PHE A 221 40.380 -1.035 -15.803 1.00 25.83 C ANISOU 418 CE1 PHE A 221 3324 3015 3477 -527 811 -362 C ATOM 419 CE2 PHE A 221 38.770 0.331 -16.939 1.00 27.18 C ANISOU 419 CE2 PHE A 221 3514 3136 3676 -500 872 -228 C ATOM 420 CZ PHE A 221 39.719 0.177 -15.939 1.00 26.16 C ANISOU 420 CZ PHE A 221 3386 3008 3547 -530 877 -300 C ATOM 421 N GLN A 222 35.818 -3.222 -19.109 1.00 14.70 N ANISOU 421 N GLN A 222 1891 1651 2043 -385 609 -127 N ATOM 422 CA GLN A 222 34.502 -2.603 -19.185 1.00 15.74 C ANISOU 422 CA GLN A 222 2025 1746 2210 -368 629 -38 C ATOM 423 C GLN A 222 33.447 -3.458 -18.502 1.00 19.69 C ANISOU 423 C GLN A 222 2517 2226 2738 -349 572 -18 C ATOM 424 O GLN A 222 32.619 -2.947 -17.749 1.00 19.09 O ANISOU 424 O GLN A 222 2445 2099 2709 -342 604 31 O ATOM 425 CB GLN A 222 34.107 -2.389 -20.649 1.00 16.22 C ANISOU 425 CB GLN A 222 2081 1842 2240 -354 620 20 C ATOM 426 CG GLN A 222 34.872 -1.268 -21.356 1.00 17.54 C ANISOU 426 CG GLN A 222 2256 2018 2391 -367 692 27 C ATOM 427 CD GLN A 222 34.494 -1.168 -22.823 1.00 21.40 C ANISOU 427 CD GLN A 222 2739 2547 2845 -350 676 82 C ATOM 428 OE1 GLN A 222 34.690 -2.110 -23.587 1.00 20.96 O ANISOU 428 OE1 GLN A 222 2679 2541 2743 -342 611 57 O ATOM 429 NE2 GLN A 222 33.949 -0.025 -23.221 1.00 17.70 N ANISOU 429 NE2 GLN A 222 2272 2057 2395 -344 738 159 N ATOM 430 N LEU A 223 33.457 -4.759 -18.784 1.00 14.80 N ANISOU 430 N LEU A 223 1887 1645 2091 -339 491 -52 N ATOM 431 CA LEU A 223 32.537 -5.681 -18.112 1.00 13.87 C ANISOU 431 CA LEU A 223 1759 1510 2000 -322 432 -40 C ATOM 432 C LEU A 223 32.743 -5.634 -16.601 1.00 15.89 C ANISOU 432 C LEU A 223 2020 1723 2295 -329 459 -77 C ATOM 433 O LEU A 223 31.772 -5.612 -15.837 1.00 17.26 O ANISOU 433 O LEU A 223 2191 1853 2513 -315 459 -34 O ATOM 434 CB LEU A 223 32.739 -7.121 -18.616 1.00 14.59 C ANISOU 434 CB LEU A 223 1843 1649 2052 -315 346 -87 C ATOM 435 CG LEU A 223 32.208 -7.412 -20.017 1.00 17.73 C ANISOU 435 CG LEU A 223 2238 2086 2412 -306 301 -44 C ATOM 436 CD1 LEU A 223 32.820 -8.699 -20.589 1.00 20.33 C ANISOU 436 CD1 LEU A 223 2570 2463 2690 -306 232 -109 C ATOM 437 CD2 LEU A 223 30.677 -7.484 -19.970 1.00 14.51 C ANISOU 437 CD2 LEU A 223 1819 1655 2039 -290 271 40 C ATOM 438 N PHE A 224 34.003 -5.640 -16.162 1.00 14.51 N ANISOU 438 N PHE A 224 1850 1561 2104 -349 480 -155 N ATOM 439 CA PHE A 224 34.300 -5.596 -14.731 1.00 18.67 C ANISOU 439 CA PHE A 224 2381 2051 2661 -359 504 -195 C ATOM 440 C PHE A 224 33.710 -4.336 -14.096 1.00 18.23 C ANISOU 440 C PHE A 224 2343 1934 2650 -363 579 -141 C ATOM 441 O PHE A 224 33.142 -4.373 -12.998 1.00 19.88 O ANISOU 441 O PHE A 224 2556 2099 2898 -354 586 -130 O ATOM 442 CB PHE A 224 35.810 -5.635 -14.469 1.00 14.24 C ANISOU 442 CB PHE A 224 1820 1519 2071 -385 522 -279 C ATOM 443 CG PHE A 224 36.487 -6.901 -14.923 1.00 16.05 C ANISOU 443 CG PHE A 224 2035 1804 2258 -379 456 -337 C ATOM 444 CD1 PHE A 224 35.777 -8.080 -15.050 1.00 15.34 C ANISOU 444 CD1 PHE A 224 1936 1726 2167 -354 384 -330 C ATOM 445 CD2 PHE A 224 37.849 -6.907 -15.204 1.00 15.87 C ANISOU 445 CD2 PHE A 224 2010 1823 2198 -399 470 -397 C ATOM 446 CE1 PHE A 224 36.391 -9.244 -15.468 1.00 15.79 C ANISOU 446 CE1 PHE A 224 1984 1830 2184 -347 330 -383 C ATOM 447 CE2 PHE A 224 38.480 -8.066 -15.619 1.00 13.88 C ANISOU 447 CE2 PHE A 224 1748 1620 1907 -390 417 -446 C ATOM 448 CZ PHE A 224 37.757 -9.241 -15.749 1.00 16.72 C ANISOU 448 CZ PHE A 224 2101 1987 2264 -363 348 -441 C ATOM 449 N GLU A 225 33.859 -3.211 -14.783 1.00 20.58 N ANISOU 449 N GLU A 225 2652 2227 2942 -375 638 -106 N ATOM 450 CA GLU A 225 33.387 -1.947 -14.238 1.00 19.72 C ANISOU 450 CA GLU A 225 2564 2057 2873 -380 719 -56 C ATOM 451 C GLU A 225 31.862 -1.866 -14.245 1.00 18.24 C ANISOU 451 C GLU A 225 2372 1835 2723 -348 713 37 C ATOM 452 O GLU A 225 31.249 -1.388 -13.292 1.00 21.00 O ANISOU 452 O GLU A 225 2737 2127 3115 -341 754 69 O ATOM 453 CB GLU A 225 33.975 -0.768 -15.013 1.00 32.18 C ANISOU 453 CB GLU A 225 4153 3638 4435 -400 788 -42 C ATOM 454 CG GLU A 225 35.443 -0.516 -14.724 1.00 57.55 C ANISOU 454 CG GLU A 225 7374 6868 7626 -438 817 -125 C ATOM 455 CD GLU A 225 35.719 -0.286 -13.246 1.00 74.21 C ANISOU 455 CD GLU A 225 9500 8932 9763 -458 849 -166 C ATOM 456 OE1 GLU A 225 34.837 0.266 -12.551 1.00 77.91 O ANISOU 456 OE1 GLU A 225 9988 9343 10273 -449 888 -119 O ATOM 457 OE2 GLU A 225 36.821 -0.654 -12.779 1.00 79.37 O ANISOU 457 OE2 GLU A 225 10149 9612 10396 -484 836 -245 O ATOM 458 N GLN A 226 31.247 -2.336 -15.322 1.00 19.32 N ANISOU 458 N GLN A 226 2491 2008 2842 -329 663 83 N ATOM 459 CA GLN A 226 29.815 -2.111 -15.515 1.00 15.43 C ANISOU 459 CA GLN A 226 1991 1490 2383 -301 662 184 C ATOM 460 C GLN A 226 28.944 -3.183 -14.879 1.00 19.12 C ANISOU 460 C GLN A 226 2442 1948 2875 -279 595 196 C ATOM 461 O GLN A 226 27.778 -2.942 -14.587 1.00 17.30 O ANISOU 461 O GLN A 226 2207 1680 2684 -256 606 276 O ATOM 462 CB GLN A 226 29.500 -1.992 -17.007 1.00 18.06 C ANISOU 462 CB GLN A 226 2310 1867 2685 -293 644 238 C ATOM 463 CG GLN A 226 30.205 -0.790 -17.662 1.00 19.77 C ANISOU 463 CG GLN A 226 2541 2087 2884 -310 721 244 C ATOM 464 CD GLN A 226 29.816 -0.614 -19.111 1.00 23.37 C ANISOU 464 CD GLN A 226 2984 2586 3311 -298 707 305 C ATOM 465 OE1 GLN A 226 28.663 -0.825 -19.479 1.00 23.72 O ANISOU 465 OE1 GLN A 226 3012 2634 3368 -276 674 382 O ATOM 466 NE2 GLN A 226 30.777 -0.212 -19.944 1.00 18.65 N ANISOU 466 NE2 GLN A 226 2390 2021 2674 -313 732 274 N ATOM 467 N VAL A 227 29.494 -4.372 -14.669 1.00 15.62 N ANISOU 467 N VAL A 227 1989 1537 2409 -283 527 121 N ATOM 468 CA VAL A 227 28.676 -5.465 -14.134 1.00 16.04 C ANISOU 468 CA VAL A 227 2026 1583 2485 -261 460 131 C ATOM 469 C VAL A 227 28.953 -5.748 -12.663 1.00 21.17 C ANISOU 469 C VAL A 227 2684 2197 3164 -261 471 80 C ATOM 470 O VAL A 227 28.023 -5.985 -11.886 1.00 18.87 O ANISOU 470 O VAL A 227 2388 1868 2915 -239 461 120 O ATOM 471 CB VAL A 227 28.793 -6.754 -14.988 1.00 18.03 C ANISOU 471 CB VAL A 227 2260 1894 2696 -259 368 98 C ATOM 472 CG1 VAL A 227 28.018 -7.914 -14.348 1.00 13.71 C ANISOU 472 CG1 VAL A 227 1696 1337 2176 -240 300 102 C ATOM 473 CG2 VAL A 227 28.253 -6.497 -16.392 1.00 19.15 C ANISOU 473 CG2 VAL A 227 2394 2069 2814 -256 352 164 C ATOM 474 N ILE A 228 30.222 -5.712 -12.270 1.00 15.13 N ANISOU 474 N ILE A 228 1930 1445 2375 -284 491 -6 N ATOM 475 CA ILE A 228 30.568 -5.992 -10.883 1.00 18.12 C ANISOU 475 CA ILE A 228 2315 1796 2774 -286 499 -58 C ATOM 476 C ILE A 228 31.382 -4.884 -10.233 1.00 17.03 C ANISOU 476 C ILE A 228 2202 1629 2638 -314 581 -90 C ATOM 477 O ILE A 228 32.045 -5.116 -9.227 1.00 26.79 O ANISOU 477 O ILE A 228 3444 2859 3875 -326 586 -153 O ATOM 478 CB ILE A 228 31.360 -7.302 -10.752 1.00 17.84 C ANISOU 478 CB ILE A 228 2263 1807 2709 -289 433 -142 C ATOM 479 CG1 ILE A 228 32.656 -7.250 -11.576 1.00 19.79 C ANISOU 479 CG1 ILE A 228 2510 2107 2903 -315 436 -201 C ATOM 480 CG2 ILE A 228 30.502 -8.477 -11.177 1.00 16.72 C ANISOU 480 CG2 ILE A 228 2100 1684 2570 -263 352 -115 C ATOM 481 CD1 ILE A 228 33.550 -8.447 -11.324 1.00 24.03 C ANISOU 481 CD1 ILE A 228 3033 2686 3410 -317 384 -284 C ATOM 482 N GLY A 229 31.328 -3.686 -10.805 1.00 15.86 N ANISOU 482 N GLY A 229 2070 1464 2490 -325 645 -46 N ATOM 483 CA GLY A 229 32.203 -2.606 -10.383 1.00 19.33 C ANISOU 483 CA GLY A 229 2536 1881 2926 -358 722 -80 C ATOM 484 C GLY A 229 31.559 -1.609 -9.444 1.00 25.63 C ANISOU 484 C GLY A 229 3365 2605 3770 -355 796 -34 C ATOM 485 O GLY A 229 32.242 -0.966 -8.648 1.00 23.96 O ANISOU 485 O GLY A 229 3179 2365 3559 -383 850 -78 O ATOM 486 N ARG A 230 30.243 -1.467 -9.546 1.00 20.94 N ANISOU 486 N ARG A 230 2889 2139 2928 -256 760 -125 N ATOM 487 CA ARG A 230 29.517 -0.539 -8.690 1.00 24.77 C ANISOU 487 CA ARG A 230 3473 2519 3419 -254 869 -115 C ATOM 488 C ARG A 230 28.411 -1.270 -7.960 1.00 24.63 C ANISOU 488 C ARG A 230 3449 2491 3417 -193 863 -84 C ATOM 489 O ARG A 230 27.685 -2.057 -8.561 1.00 22.11 O ANISOU 489 O ARG A 230 3052 2222 3128 -128 817 -30 O ATOM 490 CB ARG A 230 28.933 0.607 -9.504 1.00 29.75 C ANISOU 490 CB ARG A 230 4136 3082 4085 -208 975 -52 C ATOM 491 CG ARG A 230 29.943 1.700 -9.830 1.00 40.45 C ANISOU 491 CG ARG A 230 5551 4402 5415 -285 1027 -93 C ATOM 492 CD ARG A 230 29.350 2.690 -10.807 1.00 50.97 C ANISOU 492 CD ARG A 230 6906 5678 6784 -221 1129 -24 C ATOM 493 NE ARG A 230 28.745 2.005 -11.947 1.00 58.63 N ANISOU 493 NE ARG A 230 7757 6720 7799 -132 1071 47 N ATOM 494 CZ ARG A 230 29.409 1.670 -13.047 1.00 53.20 C ANISOU 494 CZ ARG A 230 6994 6101 7119 -139 999 42 C ATOM 495 NH1 ARG A 230 30.698 1.966 -13.160 1.00 62.62 N ANISOU 495 NH1 ARG A 230 8203 7307 8282 -224 979 -24 N ATOM 496 NH2 ARG A 230 28.784 1.053 -14.038 1.00 43.43 N ANISOU 496 NH2 ARG A 230 5665 4922 5913 -66 950 108 N ATOM 497 N LYS A 231 28.285 -0.983 -6.667 1.00 21.99 N ANISOU 497 N LYS A 231 3204 2091 3060 -222 912 -118 N ATOM 498 CA LYS A 231 27.408 -1.729 -5.778 1.00 21.96 C ANISOU 498 CA LYS A 231 3202 2077 3064 -176 901 -102 C ATOM 499 C LYS A 231 25.961 -1.758 -6.240 1.00 24.63 C ANISOU 499 C LYS A 231 3502 2402 3455 -75 947 1 C ATOM 500 O LYS A 231 25.342 -2.816 -6.247 1.00 23.78 O ANISOU 500 O LYS A 231 3326 2350 3362 -36 885 28 O ATOM 501 CB LYS A 231 27.484 -1.159 -4.366 1.00 28.66 C ANISOU 501 CB LYS A 231 4175 2837 3878 -222 969 -149 C ATOM 502 CG LYS A 231 26.694 -1.940 -3.325 1.00 35.72 C ANISOU 502 CG LYS A 231 5078 3716 4777 -178 958 -143 C ATOM 503 CD LYS A 231 27.009 -1.402 -1.937 1.00 34.78 C ANISOU 503 CD LYS A 231 5090 3512 4611 -240 1014 -202 C ATOM 504 CE LYS A 231 26.290 -2.183 -0.862 1.00 39.24 C ANISOU 504 CE LYS A 231 5671 4059 5180 -196 1004 -201 C ATOM 505 NZ LYS A 231 26.624 -1.647 0.486 1.00 45.68 N ANISOU 505 NZ LYS A 231 6623 4789 5944 -259 1057 -261 N ATOM 506 N ASP A 232 25.409 -0.607 -6.604 1.00 25.05 N ANISOU 506 N ASP A 232 3601 2386 3532 -34 1061 63 N ATOM 507 CA ASP A 232 23.983 -0.571 -6.933 1.00 29.12 C ANISOU 507 CA ASP A 232 4072 2900 4091 68 1115 178 C ATOM 508 C ASP A 232 23.649 -1.347 -8.206 1.00 24.52 C ANISOU 508 C ASP A 232 3355 2429 3534 101 1027 233 C ATOM 509 O ASP A 232 22.706 -2.134 -8.221 1.00 22.94 O ANISOU 509 O ASP A 232 3084 2280 3350 144 990 291 O ATOM 510 CB ASP A 232 23.405 0.856 -6.944 1.00 36.02 C ANISOU 510 CB ASP A 232 5036 3675 4976 123 1276 247 C ATOM 511 CG ASP A 232 24.240 1.832 -7.749 1.00 53.46 C ANISOU 511 CG ASP A 232 7285 5854 7171 86 1320 223 C ATOM 512 OD1 ASP A 232 25.172 1.405 -8.469 1.00 54.50 O ANISOU 512 OD1 ASP A 232 7353 6057 7297 29 1220 168 O ATOM 513 OD2 ASP A 232 23.956 3.046 -7.656 1.00 61.25 O ANISOU 513 OD2 ASP A 232 8378 6742 8152 118 1463 262 O ATOM 514 N ASP A 233 24.439 -1.161 -9.259 1.00 19.95 N ANISOU 514 N ASP A 233 2743 1885 2952 72 991 212 N ATOM 515 CA ASP A 233 24.226 -1.924 -10.492 1.00 18.68 C ANISOU 515 CA ASP A 233 2471 1823 2805 93 904 256 C ATOM 516 C ASP A 233 24.486 -3.421 -10.304 1.00 22.03 C ANISOU 516 C ASP A 233 2847 2320 3205 57 778 209 C ATOM 517 O ASP A 233 23.747 -4.254 -10.837 1.00 16.61 O ANISOU 517 O ASP A 233 2089 1700 2523 79 721 263 O ATOM 518 CB ASP A 233 25.066 -1.361 -11.639 1.00 17.71 C ANISOU 518 CB ASP A 233 2336 1711 2683 74 901 243 C ATOM 519 CG ASP A 233 24.445 -0.110 -12.244 1.00 30.37 C ANISOU 519 CG ASP A 233 3956 3268 4313 138 1019 327 C ATOM 520 OD1 ASP A 233 23.318 0.238 -11.843 1.00 29.77 O ANISOU 520 OD1 ASP A 233 3890 3167 4255 205 1099 407 O ATOM 521 OD2 ASP A 233 25.071 0.517 -13.121 1.00 29.68 O ANISOU 521 OD2 ASP A 233 3874 3174 4229 129 1038 319 O ATOM 522 N PHE A 234 25.529 -3.762 -9.548 1.00 17.80 N ANISOU 522 N PHE A 234 2356 1775 2634 -2 738 112 N ATOM 523 CA PHE A 234 25.781 -5.164 -9.193 1.00 16.17 C ANISOU 523 CA PHE A 234 2124 1626 2395 -23 639 68 C ATOM 524 C PHE A 234 24.577 -5.821 -8.502 1.00 20.05 C ANISOU 524 C PHE A 234 2606 2116 2896 11 641 108 C ATOM 525 O PHE A 234 24.187 -6.945 -8.844 1.00 16.17 O ANISOU 525 O PHE A 234 2068 1686 2391 14 570 126 O ATOM 526 CB PHE A 234 27.006 -5.278 -8.297 1.00 18.06 C ANISOU 526 CB PHE A 234 2414 1859 2591 -80 615 -29 C ATOM 527 CG PHE A 234 27.179 -6.633 -7.680 1.00 16.72 C ANISOU 527 CG PHE A 234 2234 1735 2383 -85 539 -69 C ATOM 528 CD1 PHE A 234 27.652 -7.695 -8.432 1.00 15.63 C ANISOU 528 CD1 PHE A 234 2052 1671 2215 -84 456 -76 C ATOM 529 CD2 PHE A 234 26.846 -6.850 -6.348 1.00 20.62 C ANISOU 529 CD2 PHE A 234 2777 2192 2867 -85 558 -98 C ATOM 530 CE1 PHE A 234 27.822 -8.955 -7.858 1.00 17.40 C ANISOU 530 CE1 PHE A 234 2285 1931 2394 -80 401 -110 C ATOM 531 CE2 PHE A 234 27.001 -8.102 -5.772 1.00 20.72 C ANISOU 531 CE2 PHE A 234 2786 2244 2841 -82 496 -136 C ATOM 532 CZ PHE A 234 27.488 -9.154 -6.524 1.00 22.44 C ANISOU 532 CZ PHE A 234 2965 2536 3025 -79 421 -141 C ATOM 533 N LEU A 235 23.997 -5.131 -7.523 1.00 16.46 N ANISOU 533 N LEU A 235 2206 1589 2460 34 726 123 N ATOM 534 CA LEU A 235 22.819 -5.657 -6.824 1.00 19.12 C ANISOU 534 CA LEU A 235 2532 1921 2809 72 740 170 C ATOM 535 C LEU A 235 21.600 -5.753 -7.723 1.00 23.54 C ANISOU 535 C LEU A 235 3007 2536 3399 119 744 285 C ATOM 536 O LEU A 235 20.826 -6.718 -7.650 1.00 21.34 O ANISOU 536 O LEU A 235 2682 2310 3117 123 696 319 O ATOM 537 CB LEU A 235 22.483 -4.808 -5.596 1.00 23.52 C ANISOU 537 CB LEU A 235 3179 2380 3378 94 844 170 C ATOM 538 CG LEU A 235 23.517 -4.905 -4.471 1.00 32.78 C ANISOU 538 CG LEU A 235 4436 3510 4511 37 829 59 C ATOM 539 CD1 LEU A 235 23.151 -3.991 -3.303 1.00 42.46 C ANISOU 539 CD1 LEU A 235 5769 4624 5739 53 940 61 C ATOM 540 CD2 LEU A 235 23.651 -6.342 -4.004 1.00 29.75 C ANISOU 540 CD2 LEU A 235 4023 3182 4098 23 734 11 C ATOM 541 N LYS A 236 21.417 -4.738 -8.559 1.00 19.37 N ANISOU 541 N LYS A 236 2461 2002 2897 152 804 349 N ATOM 542 CA LYS A 236 20.306 -4.727 -9.495 1.00 20.51 C ANISOU 542 CA LYS A 236 2514 2215 3063 197 810 469 C ATOM 543 C LYS A 236 20.372 -5.886 -10.498 1.00 22.18 C ANISOU 543 C LYS A 236 2650 2527 3250 152 688 469 C ATOM 544 O LYS A 236 19.353 -6.487 -10.826 1.00 20.52 O ANISOU 544 O LYS A 236 2368 2391 3038 156 655 547 O ATOM 545 CB LYS A 236 20.258 -3.395 -10.235 1.00 19.96 C ANISOU 545 CB LYS A 236 2448 2118 3018 245 902 531 C ATOM 546 CG LYS A 236 19.147 -3.313 -11.270 1.00 33.59 C ANISOU 546 CG LYS A 236 4069 3932 4761 298 909 666 C ATOM 547 CD LYS A 236 18.830 -1.866 -11.625 1.00 51.42 C ANISOU 547 CD LYS A 236 6348 6146 7043 379 1043 747 C ATOM 548 CE LYS A 236 17.748 -1.773 -12.698 1.00 65.90 C ANISOU 548 CE LYS A 236 8063 8087 8888 437 1048 893 C ATOM 549 NZ LYS A 236 18.214 -2.282 -14.023 1.00 70.57 N ANISOU 549 NZ LYS A 236 8589 8758 9465 387 942 876 N ATOM 550 N LEU A 237 21.559 -6.205 -10.998 1.00 16.58 N ANISOU 550 N LEU A 237 1962 1824 2515 105 625 386 N ATOM 551 CA LEU A 237 21.661 -7.346 -11.919 1.00 15.83 C ANISOU 551 CA LEU A 237 1822 1808 2385 64 519 384 C ATOM 552 C LEU A 237 21.601 -8.667 -11.151 1.00 19.16 C ANISOU 552 C LEU A 237 2268 2245 2768 28 457 335 C ATOM 553 O LEU A 237 20.988 -9.642 -11.607 1.00 18.88 O ANISOU 553 O LEU A 237 2199 2271 2703 -1 396 369 O ATOM 554 CB LEU A 237 22.944 -7.273 -12.754 1.00 16.52 C ANISOU 554 CB LEU A 237 1927 1895 2454 39 482 326 C ATOM 555 CG LEU A 237 23.033 -6.081 -13.718 1.00 21.55 C ANISOU 555 CG LEU A 237 2541 2524 3125 70 536 374 C ATOM 556 CD1 LEU A 237 24.264 -6.223 -14.598 1.00 22.71 C ANISOU 556 CD1 LEU A 237 2699 2681 3250 42 486 320 C ATOM 557 CD2 LEU A 237 21.779 -5.978 -14.572 1.00 20.42 C ANISOU 557 CD2 LEU A 237 2319 2443 2996 100 542 493 C ATOM 558 N SER A 238 22.234 -8.696 -9.981 1.00 18.61 N ANISOU 558 N SER A 238 2262 2117 2690 25 475 254 N ATOM 559 CA SER A 238 22.254 -9.913 -9.172 1.00 16.41 C ANISOU 559 CA SER A 238 2017 1846 2373 2 427 202 C ATOM 560 C SER A 238 20.844 -10.375 -8.810 1.00 17.78 C ANISOU 560 C SER A 238 2156 2042 2556 10 434 271 C ATOM 561 O SER A 238 20.559 -11.576 -8.790 1.00 18.98 O ANISOU 561 O SER A 238 2313 2232 2667 -24 376 261 O ATOM 562 CB SER A 238 23.104 -9.720 -7.920 1.00 16.49 C ANISOU 562 CB SER A 238 2095 1797 2374 3 453 114 C ATOM 563 OG SER A 238 24.485 -9.671 -8.268 1.00 20.07 O ANISOU 563 OG SER A 238 2568 2260 2799 -20 423 49 O ATOM 564 N THR A 239 19.962 -9.418 -8.538 1.00 18.05 N ANISOU 564 N THR A 239 2162 2056 2639 55 512 347 N ATOM 565 CA THR A 239 18.581 -9.735 -8.176 1.00 20.86 C ANISOU 565 CA THR A 239 2472 2445 3009 70 528 432 C ATOM 566 C THR A 239 17.645 -9.821 -9.379 1.00 27.72 C ANISOU 566 C THR A 239 3243 3413 3878 58 500 544 C ATOM 567 O THR A 239 16.423 -9.859 -9.219 1.00 26.95 O ANISOU 567 O THR A 239 3083 3363 3794 75 522 642 O ATOM 568 CB THR A 239 17.995 -8.688 -7.201 1.00 21.64 C ANISOU 568 CB THR A 239 2592 2477 3156 139 639 478 C ATOM 569 OG1 THR A 239 18.120 -7.385 -7.779 1.00 23.43 O ANISOU 569 OG1 THR A 239 2811 2679 3413 182 711 525 O ATOM 570 CG2 THR A 239 18.736 -8.719 -5.874 1.00 22.83 C ANISOU 570 CG2 THR A 239 2842 2536 3298 138 662 372 C ATOM 571 N ASN A 240 18.206 -9.842 -10.581 1.00 25.66 N ANISOU 571 N ASN A 240 2964 3188 3597 30 451 537 N ATOM 572 CA ASN A 240 17.384 -9.835 -11.784 1.00 22.74 C ANISOU 572 CA ASN A 240 2504 2916 3221 14 423 645 C ATOM 573 C ASN A 240 17.298 -11.203 -12.431 1.00 20.80 C ANISOU 573 C ASN A 240 2256 2739 2909 -76 318 630 C ATOM 574 O ASN A 240 18.280 -11.948 -12.468 1.00 19.08 O ANISOU 574 O ASN A 240 2114 2487 2649 -113 269 531 O ATOM 575 CB ASN A 240 17.921 -8.839 -12.800 1.00 22.25 C ANISOU 575 CB ASN A 240 2424 2849 3180 46 449 664 C ATOM 576 CG ASN A 240 17.033 -8.727 -14.018 1.00 27.01 C ANISOU 576 CG ASN A 240 2928 3558 3776 39 426 784 C ATOM 577 OD1 ASN A 240 17.323 -9.301 -15.071 1.00 23.69 O ANISOU 577 OD1 ASN A 240 2500 3187 3315 -18 349 775 O ATOM 578 ND2 ASN A 240 15.925 -8.006 -13.874 1.00 18.25 N ANISOU 578 ND2 ASN A 240 1744 2490 2700 99 496 905 N ATOM 579 N ILE A 241 16.119 -11.519 -12.957 1.00 17.54 N ANISOU 579 N ILE A 241 1761 2426 2479 -112 290 735 N ATOM 580 CA ILE A 241 15.840 -12.839 -13.518 1.00 17.42 C ANISOU 580 CA ILE A 241 1755 2476 2387 -217 197 731 C ATOM 581 C ILE A 241 16.840 -13.199 -14.619 1.00 20.80 C ANISOU 581 C ILE A 241 2238 2895 2768 -258 139 673 C ATOM 582 O ILE A 241 17.294 -14.342 -14.709 1.00 22.95 O ANISOU 582 O ILE A 241 2595 3153 2973 -323 83 604 O ATOM 583 CB ILE A 241 14.375 -12.937 -14.033 1.00 26.09 C ANISOU 583 CB ILE A 241 2737 3705 3469 -261 175 872 C ATOM 584 CG1 ILE A 241 14.124 -14.277 -14.715 1.00 27.63 C ANISOU 584 CG1 ILE A 241 2960 3968 3571 -394 77 865 C ATOM 585 CG2 ILE A 241 14.046 -11.792 -14.983 1.00 27.18 C ANISOU 585 CG2 ILE A 241 2778 3905 3644 -207 207 979 C ATOM 586 CD1 ILE A 241 12.658 -14.515 -15.049 1.00 35.50 C ANISOU 586 CD1 ILE A 241 3842 5107 4539 -463 46 1000 C ATOM 587 N PHE A 242 17.205 -12.219 -15.437 1.00 17.88 N ANISOU 587 N PHE A 242 1833 2528 2434 -212 162 703 N ATOM 588 CA PHE A 242 18.176 -12.450 -16.501 1.00 18.37 C ANISOU 588 CA PHE A 242 1946 2576 2459 -238 116 656 C ATOM 589 C PHE A 242 19.593 -12.037 -16.103 1.00 19.31 C ANISOU 589 C PHE A 242 2136 2597 2604 -183 150 552 C ATOM 590 O PHE A 242 20.546 -12.763 -16.361 1.00 21.39 O ANISOU 590 O PHE A 242 2477 2830 2819 -209 110 478 O ATOM 591 CB PHE A 242 17.764 -11.713 -17.767 1.00 23.32 C ANISOU 591 CB PHE A 242 2490 3272 3099 -229 113 751 C ATOM 592 CG PHE A 242 16.367 -12.014 -18.193 1.00 27.68 C ANISOU 592 CG PHE A 242 2952 3945 3621 -287 78 869 C ATOM 593 CD1 PHE A 242 15.971 -13.324 -18.416 1.00 26.18 C ANISOU 593 CD1 PHE A 242 2797 3804 3346 -402 -2 863 C ATOM 594 CD2 PHE A 242 15.448 -10.999 -18.356 1.00 27.29 C ANISOU 594 CD2 PHE A 242 2784 3964 3619 -228 130 991 C ATOM 595 CE1 PHE A 242 14.673 -13.616 -18.796 1.00 26.75 C ANISOU 595 CE1 PHE A 242 2779 4003 3381 -475 -41 976 C ATOM 596 CE2 PHE A 242 14.145 -11.282 -18.739 1.00 34.64 C ANISOU 596 CE2 PHE A 242 3614 5032 4517 -283 94 1114 C ATOM 597 CZ PHE A 242 13.759 -12.590 -18.961 1.00 31.86 C ANISOU 597 CZ PHE A 242 3288 4738 4080 -415 4 1105 C ATOM 598 N GLY A 243 19.721 -10.876 -15.470 1.00 18.94 N ANISOU 598 N GLY A 243 2067 2504 2626 -109 228 553 N ATOM 599 CA GLY A 243 21.035 -10.334 -15.174 1.00 17.59 C ANISOU 599 CA GLY A 243 1953 2255 2476 -73 260 466 C ATOM 600 C GLY A 243 21.900 -11.194 -14.275 1.00 16.35 C ANISOU 600 C GLY A 243 1878 2054 2282 -90 236 362 C ATOM 601 O GLY A 243 23.122 -11.110 -14.341 1.00 18.16 O ANISOU 601 O GLY A 243 2149 2249 2501 -81 232 294 O ATOM 602 N ASN A 244 21.289 -12.007 -13.414 1.00 17.94 N ANISOU 602 N ASN A 244 2096 2259 2460 -112 223 354 N ATOM 603 CA ASN A 244 22.098 -12.784 -12.471 1.00 15.82 C ANISOU 603 CA ASN A 244 1905 1949 2155 -116 211 259 C ATOM 604 C ASN A 244 23.048 -13.730 -13.187 1.00 14.45 C ANISOU 604 C ASN A 244 1792 1786 1912 -142 156 212 C ATOM 605 O ASN A 244 24.122 -14.030 -12.675 1.00 15.52 O ANISOU 605 O ASN A 244 1981 1894 2022 -122 157 140 O ATOM 606 CB ASN A 244 21.243 -13.534 -11.445 1.00 15.32 C ANISOU 606 CB ASN A 244 1857 1885 2077 -131 211 259 C ATOM 607 CG ASN A 244 20.626 -14.802 -12.003 1.00 21.35 C ANISOU 607 CG ASN A 244 2640 2700 2773 -199 151 283 C ATOM 608 OD1 ASN A 244 21.242 -15.874 -11.985 1.00 20.78 O ANISOU 608 OD1 ASN A 244 2651 2615 2632 -223 118 223 O ATOM 609 ND2 ASN A 244 19.392 -14.691 -12.486 1.00 16.75 N ANISOU 609 ND2 ASN A 244 1986 2178 2201 -232 141 377 N ATOM 610 N TYR A 245 22.644 -14.203 -14.365 1.00 14.58 N ANISOU 610 N TYR A 245 1803 1847 1892 -184 112 261 N ATOM 611 CA TYR A 245 23.511 -15.047 -15.187 1.00 15.49 C ANISOU 611 CA TYR A 245 1990 1961 1935 -204 71 230 C ATOM 612 C TYR A 245 24.739 -14.288 -15.682 1.00 18.01 C ANISOU 612 C TYR A 245 2303 2261 2280 -158 86 204 C ATOM 613 O TYR A 245 25.858 -14.810 -15.674 1.00 15.50 O ANISOU 613 O TYR A 245 2045 1927 1916 -139 79 154 O ATOM 614 CB TYR A 245 22.737 -15.609 -16.384 1.00 15.41 C ANISOU 614 CB TYR A 245 1982 1997 1875 -271 23 293 C ATOM 615 CG TYR A 245 21.720 -16.661 -15.993 1.00 17.86 C ANISOU 615 CG TYR A 245 2324 2332 2131 -340 -3 308 C ATOM 616 CD1 TYR A 245 22.091 -17.991 -15.863 1.00 19.76 C ANISOU 616 CD1 TYR A 245 2684 2546 2277 -374 -22 258 C ATOM 617 CD2 TYR A 245 20.399 -16.320 -15.739 1.00 20.52 C ANISOU 617 CD2 TYR A 245 2574 2718 2503 -368 0 378 C ATOM 618 CE1 TYR A 245 21.173 -18.963 -15.516 1.00 21.45 C ANISOU 618 CE1 TYR A 245 2940 2778 2434 -447 -40 267 C ATOM 619 CE2 TYR A 245 19.469 -17.283 -15.381 1.00 21.69 C ANISOU 619 CE2 TYR A 245 2747 2896 2599 -441 -25 395 C ATOM 620 CZ TYR A 245 19.865 -18.603 -15.266 1.00 22.97 C ANISOU 620 CZ TYR A 245 3036 3024 2666 -486 -46 334 C ATOM 621 OH TYR A 245 18.953 -19.572 -14.912 1.00 23.93 O ANISOU 621 OH TYR A 245 3194 3170 2729 -569 -65 346 O ATOM 622 N LEU A 246 24.515 -13.061 -16.133 1.00 17.18 N ANISOU 622 N LEU A 246 2125 2161 2242 -138 114 247 N ATOM 623 CA LEU A 246 25.602 -12.207 -16.596 1.00 14.80 C ANISOU 623 CA LEU A 246 1812 1840 1970 -102 135 227 C ATOM 624 C LEU A 246 26.547 -11.894 -15.444 1.00 13.94 C ANISOU 624 C LEU A 246 1724 1699 1875 -76 168 155 C ATOM 625 O LEU A 246 27.764 -11.899 -15.615 1.00 15.30 O ANISOU 625 O LEU A 246 1917 1870 2027 -61 164 116 O ATOM 626 CB LEU A 246 25.044 -10.902 -17.163 1.00 15.44 C ANISOU 626 CB LEU A 246 1821 1926 2119 -83 174 288 C ATOM 627 CG LEU A 246 26.109 -10.006 -17.796 1.00 21.34 C ANISOU 627 CG LEU A 246 2562 2651 2893 -55 199 271 C ATOM 628 CD1 LEU A 246 26.862 -10.755 -18.899 1.00 17.76 C ANISOU 628 CD1 LEU A 246 2148 2214 2388 -65 148 265 C ATOM 629 CD2 LEU A 246 25.467 -8.746 -18.330 1.00 23.43 C ANISOU 629 CD2 LEU A 246 2767 2915 3219 -28 250 335 C ATOM 630 N VAL A 247 25.990 -11.609 -14.270 1.00 14.01 N ANISOU 630 N VAL A 247 1724 1688 1914 -72 201 144 N ATOM 631 CA VAL A 247 26.821 -11.373 -13.099 1.00 13.88 C ANISOU 631 CA VAL A 247 1732 1644 1898 -59 227 75 C ATOM 632 C VAL A 247 27.736 -12.574 -12.829 1.00 17.40 C ANISOU 632 C VAL A 247 2232 2110 2271 -57 187 23 C ATOM 633 O VAL A 247 28.935 -12.403 -12.611 1.00 13.58 O ANISOU 633 O VAL A 247 1754 1635 1769 -45 190 -18 O ATOM 634 CB VAL A 247 25.973 -11.048 -11.856 1.00 15.15 C ANISOU 634 CB VAL A 247 1892 1772 2092 -55 268 74 C ATOM 635 CG1 VAL A 247 26.826 -11.061 -10.597 1.00 14.27 C ANISOU 635 CG1 VAL A 247 1820 1639 1963 -53 282 -2 C ATOM 636 CG2 VAL A 247 25.306 -9.687 -12.023 1.00 14.39 C ANISOU 636 CG2 VAL A 247 1756 1649 2063 -38 331 128 C ATOM 637 N GLN A 248 27.178 -13.786 -12.864 1.00 14.46 N ANISOU 637 N GLN A 248 1898 1748 1846 -68 156 32 N ATOM 638 CA GLN A 248 27.971 -14.982 -12.586 1.00 14.77 C ANISOU 638 CA GLN A 248 2005 1800 1805 -53 135 -10 C ATOM 639 C GLN A 248 29.050 -15.201 -13.637 1.00 13.93 C ANISOU 639 C GLN A 248 1919 1716 1659 -34 119 -3 C ATOM 640 O GLN A 248 30.179 -15.572 -13.308 1.00 13.82 O ANISOU 640 O GLN A 248 1929 1722 1600 1 122 -35 O ATOM 641 CB GLN A 248 27.077 -16.225 -12.487 1.00 14.02 C ANISOU 641 CB GLN A 248 1970 1702 1657 -78 116 0 C ATOM 642 CG GLN A 248 26.097 -16.186 -11.318 1.00 18.42 C ANISOU 642 CG GLN A 248 2513 2240 2244 -88 134 -8 C ATOM 643 CD GLN A 248 25.134 -17.358 -11.332 1.00 20.90 C ANISOU 643 CD GLN A 248 2880 2556 2505 -128 114 8 C ATOM 644 OE1 GLN A 248 25.527 -18.497 -11.100 1.00 19.40 O ANISOU 644 OE1 GLN A 248 2776 2359 2236 -122 109 -26 O ATOM 645 NE2 GLN A 248 23.864 -17.080 -11.597 1.00 17.74 N ANISOU 645 NE2 GLN A 248 2430 2170 2141 -170 108 66 N ATOM 646 N SER A 249 28.706 -14.976 -14.901 1.00 13.99 N ANISOU 646 N SER A 249 1912 1724 1678 -52 103 45 N ATOM 647 CA SER A 249 29.694 -15.062 -15.975 1.00 17.57 C ANISOU 647 CA SER A 249 2384 2190 2101 -30 94 58 C ATOM 648 C SER A 249 30.842 -14.087 -15.776 1.00 16.13 C ANISOU 648 C SER A 249 2150 2023 1958 -3 116 35 C ATOM 649 O SER A 249 32.012 -14.438 -15.952 1.00 17.73 O ANISOU 649 O SER A 249 2370 2250 2114 32 115 26 O ATOM 650 CB SER A 249 29.046 -14.798 -17.337 1.00 16.33 C ANISOU 650 CB SER A 249 2213 2030 1960 -58 75 115 C ATOM 651 OG SER A 249 28.108 -15.804 -17.639 1.00 22.23 O ANISOU 651 OG SER A 249 3018 2777 2652 -101 47 139 O ATOM 652 N VAL A 250 30.517 -12.852 -15.425 1.00 13.74 N ANISOU 652 N VAL A 250 1785 1706 1731 -20 141 32 N ATOM 653 CA VAL A 250 31.558 -11.835 -15.272 1.00 14.63 C ANISOU 653 CA VAL A 250 1856 1828 1874 -16 165 8 C ATOM 654 C VAL A 250 32.421 -12.098 -14.033 1.00 14.50 C ANISOU 654 C VAL A 250 1847 1841 1822 -11 168 -43 C ATOM 655 O VAL A 250 33.632 -11.885 -14.046 1.00 16.47 O ANISOU 655 O VAL A 250 2076 2132 2051 -4 168 -56 O ATOM 656 CB VAL A 250 30.974 -10.402 -15.260 1.00 13.98 C ANISOU 656 CB VAL A 250 1730 1711 1872 -37 206 20 C ATOM 657 CG1 VAL A 250 32.064 -9.392 -14.907 1.00 14.49 C ANISOU 657 CG1 VAL A 250 1772 1780 1954 -54 236 -15 C ATOM 658 CG2 VAL A 250 30.367 -10.077 -16.613 1.00 13.79 C ANISOU 658 CG2 VAL A 250 1687 1677 1877 -32 204 78 C ATOM 659 N ILE A 251 31.811 -12.591 -12.968 1.00 15.54 N ANISOU 659 N ILE A 251 2004 1960 1941 -14 169 -67 N ATOM 660 CA ILE A 251 32.603 -13.009 -11.813 1.00 13.79 C ANISOU 660 CA ILE A 251 1793 1773 1672 -3 168 -111 C ATOM 661 C ILE A 251 33.617 -14.089 -12.233 1.00 16.40 C ANISOU 661 C ILE A 251 2151 2159 1922 45 148 -100 C ATOM 662 O ILE A 251 34.784 -14.058 -11.837 1.00 16.49 O ANISOU 662 O ILE A 251 2136 2231 1897 60 148 -113 O ATOM 663 CB ILE A 251 31.712 -13.529 -10.677 1.00 15.08 C ANISOU 663 CB ILE A 251 1991 1907 1830 -5 174 -136 C ATOM 664 CG1 ILE A 251 30.934 -12.368 -10.022 1.00 13.73 C ANISOU 664 CG1 ILE A 251 1799 1685 1732 -40 209 -145 C ATOM 665 CG2 ILE A 251 32.543 -14.281 -9.664 1.00 15.78 C ANISOU 665 CG2 ILE A 251 2103 2042 1852 22 168 -173 C ATOM 666 CD1 ILE A 251 29.854 -12.849 -9.018 1.00 13.62 C ANISOU 666 CD1 ILE A 251 1818 1635 1723 -37 219 -156 C ATOM 667 N GLY A 252 33.178 -15.032 -13.055 1.00 15.61 N ANISOU 667 N GLY A 252 2106 2041 1785 68 136 -69 N ATOM 668 CA GLY A 252 34.067 -16.064 -13.560 1.00 14.53 C ANISOU 668 CA GLY A 252 2018 1940 1564 123 134 -47 C ATOM 669 C GLY A 252 35.220 -15.507 -14.386 1.00 17.77 C ANISOU 669 C GLY A 252 2381 2392 1977 143 136 -20 C ATOM 670 O GLY A 252 36.371 -15.935 -14.249 1.00 14.46 O ANISOU 670 O GLY A 252 1959 2036 1500 194 144 -8 O ATOM 671 N ILE A 253 34.921 -14.551 -15.252 1.00 14.84 N ANISOU 671 N ILE A 253 1972 1993 1674 109 133 -3 N ATOM 672 CA ILE A 253 35.965 -13.925 -16.054 1.00 14.18 C ANISOU 672 CA ILE A 253 1843 1944 1602 122 137 21 C ATOM 673 C ILE A 253 36.938 -13.132 -15.174 1.00 16.96 C ANISOU 673 C ILE A 253 2121 2357 1965 100 145 -7 C ATOM 674 O ILE A 253 38.157 -13.182 -15.366 1.00 15.58 O ANISOU 674 O ILE A 253 1914 2253 1753 129 146 15 O ATOM 675 CB ILE A 253 35.352 -13.050 -17.160 1.00 15.20 C ANISOU 675 CB ILE A 253 1953 2024 1800 92 138 44 C ATOM 676 CG1 ILE A 253 34.519 -13.928 -18.098 1.00 14.95 C ANISOU 676 CG1 ILE A 253 1993 1950 1737 102 122 79 C ATOM 677 CG2 ILE A 253 36.443 -12.327 -17.956 1.00 14.42 C ANISOU 677 CG2 ILE A 253 1806 1955 1718 103 147 65 C ATOM 678 CD1 ILE A 253 33.521 -13.149 -18.968 1.00 17.17 C ANISOU 678 CD1 ILE A 253 2250 2189 2083 66 117 104 C ATOM 679 N SER A 254 36.397 -12.437 -14.180 1.00 14.13 N ANISOU 679 N SER A 254 1741 1976 1650 47 152 -50 N ATOM 680 CA SER A 254 37.211 -11.682 -13.233 1.00 15.10 C ANISOU 680 CA SER A 254 1812 2151 1772 4 158 -83 C ATOM 681 C SER A 254 38.192 -12.582 -12.480 1.00 17.52 C ANISOU 681 C SER A 254 2111 2553 1995 44 145 -83 C ATOM 682 O SER A 254 39.365 -12.241 -12.311 1.00 18.06 O ANISOU 682 O SER A 254 2120 2709 2035 30 140 -75 O ATOM 683 CB SER A 254 36.321 -10.954 -12.221 1.00 15.86 C ANISOU 683 CB SER A 254 1918 2190 1916 -53 176 -128 C ATOM 684 OG SER A 254 37.109 -10.245 -11.287 1.00 16.70 O ANISOU 684 OG SER A 254 1993 2343 2010 -110 182 -163 O ATOM 685 N LEU A 255 37.711 -13.730 -12.021 1.00 14.82 N ANISOU 685 N LEU A 255 1826 2198 1608 92 142 -86 N ATOM 686 CA LEU A 255 38.576 -14.681 -11.327 1.00 15.70 C ANISOU 686 CA LEU A 255 1938 2396 1630 150 140 -77 C ATOM 687 C LEU A 255 39.638 -15.282 -12.256 1.00 18.63 C ANISOU 687 C LEU A 255 2303 2835 1941 224 147 -13 C ATOM 688 O LEU A 255 40.707 -15.673 -11.807 1.00 24.18 O ANISOU 688 O LEU A 255 2968 3644 2576 269 150 13 O ATOM 689 CB LEU A 255 37.742 -15.790 -10.682 1.00 14.59 C ANISOU 689 CB LEU A 255 1878 2212 1453 189 147 -95 C ATOM 690 CG LEU A 255 36.905 -15.366 -9.473 1.00 20.24 C ANISOU 690 CG LEU A 255 2597 2884 2210 134 145 -152 C ATOM 691 CD1 LEU A 255 35.880 -16.445 -9.117 1.00 24.98 C ANISOU 691 CD1 LEU A 255 3282 3423 2786 167 154 -164 C ATOM 692 CD2 LEU A 255 37.789 -15.065 -8.288 1.00 17.70 C ANISOU 692 CD2 LEU A 255 2224 2648 1854 115 140 -178 C ATOM 693 N ALA A 256 39.338 -15.362 -13.548 1.00 18.76 N ANISOU 693 N ALA A 256 2357 2794 1979 243 152 20 N ATOM 694 CA ALA A 256 40.284 -15.923 -14.510 1.00 22.11 C ANISOU 694 CA ALA A 256 2791 3263 2345 320 167 86 C ATOM 695 C ALA A 256 41.321 -14.915 -15.022 1.00 23.08 C ANISOU 695 C ALA A 256 2817 3455 2499 296 163 113 C ATOM 696 O ALA A 256 42.249 -15.290 -15.733 1.00 30.08 O ANISOU 696 O ALA A 256 3696 4396 3339 364 179 176 O ATOM 697 CB ALA A 256 39.535 -16.549 -15.679 1.00 26.00 C ANISOU 697 CB ALA A 256 3384 3661 2832 348 176 112 C ATOM 698 N THR A 257 41.177 -13.645 -14.647 1.00 19.49 N ANISOU 698 N THR A 257 2296 2995 2116 200 149 68 N ATOM 699 CA THR A 257 42.019 -12.578 -15.196 1.00 19.46 C ANISOU 699 CA THR A 257 2212 3037 2146 156 148 85 C ATOM 700 C THR A 257 42.998 -12.041 -14.160 1.00 20.75 C ANISOU 700 C THR A 257 2286 3319 2280 98 136 72 C ATOM 701 O THR A 257 42.669 -11.166 -13.362 1.00 19.04 O ANISOU 701 O THR A 257 2053 3082 2098 3 131 14 O ATOM 702 CB THR A 257 41.151 -11.434 -15.754 1.00 21.97 C ANISOU 702 CB THR A 257 2537 3251 2559 84 154 52 C ATOM 703 OG1 THR A 257 40.250 -11.973 -16.726 1.00 18.87 O ANISOU 703 OG1 THR A 257 2218 2768 2183 130 157 72 O ATOM 704 CG2 THR A 257 42.000 -10.350 -16.398 1.00 20.13 C ANISOU 704 CG2 THR A 257 2238 3054 2358 40 162 67 C ATOM 705 N ASN A 258 44.216 -12.568 -14.188 1.00 20.95 N ANISOU 705 N ASN A 258 2257 3473 2232 156 137 133 N ATOM 706 CA ASN A 258 45.223 -12.231 -13.192 1.00 27.57 C ANISOU 706 CA ASN A 258 3000 4455 3021 104 119 135 C ATOM 707 C ASN A 258 46.048 -11.000 -13.511 1.00 26.86 C ANISOU 707 C ASN A 258 2821 4428 2957 6 111 141 C ATOM 708 O ASN A 258 47.279 -11.040 -13.454 1.00 28.62 O ANISOU 708 O ASN A 258 2950 4803 3121 12 102 200 O ATOM 709 CB ASN A 258 46.146 -13.423 -12.977 1.00 29.40 C ANISOU 709 CB ASN A 258 3204 4816 3149 220 127 212 C ATOM 710 CG ASN A 258 45.429 -14.587 -12.346 1.00 33.79 C ANISOU 710 CG ASN A 258 3850 5324 3663 298 139 195 C ATOM 711 OD1 ASN A 258 45.079 -14.539 -11.167 1.00 37.53 O ANISOU 711 OD1 ASN A 258 4324 5807 4130 250 123 141 O ATOM 712 ND2 ASN A 258 45.194 -15.637 -13.124 1.00 32.64 N ANISOU 712 ND2 ASN A 258 3793 5122 3486 413 172 240 N ATOM 713 N ASP A 259 45.385 -9.900 -13.837 1.00 19.06 N ANISOU 713 N ASP A 259 1861 3330 2052 -84 119 87 N ATOM 714 CA ASP A 259 46.119 -8.659 -14.030 1.00 18.53 C ANISOU 714 CA ASP A 259 1727 3310 2004 -194 120 81 C ATOM 715 C ASP A 259 46.259 -7.953 -12.695 1.00 24.11 C ANISOU 715 C ASP A 259 2412 4063 2686 -326 104 22 C ATOM 716 O ASP A 259 45.878 -8.496 -11.664 1.00 25.84 O ANISOU 716 O ASP A 259 2657 4288 2872 -316 91 -6 O ATOM 717 CB ASP A 259 45.459 -7.760 -15.079 1.00 22.06 C ANISOU 717 CB ASP A 259 2221 3620 2540 -222 149 58 C ATOM 718 CG ASP A 259 44.012 -7.417 -14.745 1.00 32.37 C ANISOU 718 CG ASP A 259 3618 4775 3907 -249 167 -8 C ATOM 719 OD1 ASP A 259 43.288 -7.004 -15.673 1.00 38.93 O ANISOU 719 OD1 ASP A 259 4492 5495 4804 -231 192 -9 O ATOM 720 OD2 ASP A 259 43.590 -7.564 -13.579 1.00 34.42 O ANISOU 720 OD2 ASP A 259 3901 5029 4147 -281 158 -51 O ATOM 721 N ASP A 260 46.800 -6.739 -12.722 1.00 24.22 N ANISOU 721 N ASP A 260 2389 4103 2709 -456 110 1 N ATOM 722 CA ASP A 260 47.034 -5.972 -11.508 1.00 27.03 C ANISOU 722 CA ASP A 260 2738 4503 3028 -606 98 -54 C ATOM 723 C ASP A 260 45.739 -5.607 -10.774 1.00 27.02 C ANISOU 723 C ASP A 260 2850 4346 3071 -644 123 -134 C ATOM 724 O ASP A 260 45.763 -5.311 -9.586 1.00 28.29 O ANISOU 724 O ASP A 260 3027 4531 3190 -738 113 -180 O ATOM 725 CB ASP A 260 47.812 -4.698 -11.832 1.00 29.54 C ANISOU 725 CB ASP A 260 3019 4861 3346 -748 110 -62 C ATOM 726 CG ASP A 260 48.429 -4.077 -10.607 1.00 43.98 C ANISOU 726 CG ASP A 260 4821 6789 5100 -914 87 -99 C ATOM 727 OD1 ASP A 260 49.347 -4.698 -10.025 1.00 49.68 O ANISOU 727 OD1 ASP A 260 5444 7694 5737 -914 40 -52 O ATOM 728 OD2 ASP A 260 47.994 -2.970 -10.228 1.00 42.33 O ANISOU 728 OD2 ASP A 260 4696 6476 4910 -1046 121 -170 O ATOM 729 N GLY A 261 44.614 -5.630 -11.482 1.00 19.52 N ANISOU 729 N GLY A 261 1974 3243 2199 -570 156 -145 N ATOM 730 CA GLY A 261 43.333 -5.276 -10.881 1.00 22.18 C ANISOU 730 CA GLY A 261 2411 3435 2581 -591 188 -203 C ATOM 731 C GLY A 261 42.639 -6.405 -10.125 1.00 23.94 C ANISOU 731 C GLY A 261 2663 3645 2787 -508 167 -210 C ATOM 732 O GLY A 261 41.626 -6.192 -9.470 1.00 22.06 O ANISOU 732 O GLY A 261 2498 3303 2578 -523 191 -253 O ATOM 733 N TYR A 262 43.190 -7.610 -10.210 1.00 23.02 N ANISOU 733 N TYR A 262 2495 3632 2620 -414 131 -163 N ATOM 734 CA TYR A 262 42.538 -8.794 -9.662 1.00 17.77 C ANISOU 734 CA TYR A 262 1868 2949 1936 -321 120 -164 C ATOM 735 C TYR A 262 42.111 -8.606 -8.211 1.00 18.11 C ANISOU 735 C TYR A 262 1950 2970 1960 -385 119 -223 C ATOM 736 O TYR A 262 40.950 -8.768 -7.878 1.00 20.43 O ANISOU 736 O TYR A 262 2316 3151 2294 -359 138 -253 O ATOM 737 CB TYR A 262 43.477 -10.002 -9.791 1.00 18.73 C ANISOU 737 CB TYR A 262 1931 3207 1980 -223 94 -101 C ATOM 738 CG TYR A 262 42.940 -11.321 -9.249 1.00 18.19 C ANISOU 738 CG TYR A 262 1911 3125 1874 -121 91 -98 C ATOM 739 CD1 TYR A 262 42.267 -12.220 -10.072 1.00 21.97 C ANISOU 739 CD1 TYR A 262 2452 3527 2368 -17 105 -71 C ATOM 740 CD2 TYR A 262 43.140 -11.678 -7.920 1.00 24.39 C ANISOU 740 CD2 TYR A 262 2688 3979 2600 -135 76 -121 C ATOM 741 CE1 TYR A 262 41.795 -13.432 -9.583 1.00 19.64 C ANISOU 741 CE1 TYR A 262 2215 3217 2031 66 110 -70 C ATOM 742 CE2 TYR A 262 42.676 -12.883 -7.418 1.00 26.07 C ANISOU 742 CE2 TYR A 262 2951 4177 2776 -39 80 -120 C ATOM 743 CZ TYR A 262 42.001 -13.756 -8.250 1.00 29.95 C ANISOU 743 CZ TYR A 262 3511 4586 3283 59 100 -96 C ATOM 744 OH TYR A 262 41.541 -14.949 -7.740 1.00 28.98 O ANISOU 744 OH TYR A 262 3452 4445 3116 144 111 -97 O ATOM 745 N THR A 263 43.056 -8.272 -7.344 1.00 23.22 N ANISOU 745 N THR A 263 2549 3731 2542 -472 97 -235 N ATOM 746 CA THR A 263 42.777 -8.250 -5.906 1.00 26.02 C ANISOU 746 CA THR A 263 2943 4082 2863 -526 91 -287 C ATOM 747 C THR A 263 41.655 -7.285 -5.553 1.00 26.54 C ANISOU 747 C THR A 263 3110 3980 2993 -594 137 -347 C ATOM 748 O THR A 263 40.756 -7.607 -4.775 1.00 31.13 O ANISOU 748 O THR A 263 3756 4483 3587 -566 150 -378 O ATOM 749 CB THR A 263 44.032 -7.866 -5.117 1.00 31.37 C ANISOU 749 CB THR A 263 3549 4918 3453 -636 57 -288 C ATOM 750 OG1 THR A 263 45.076 -8.798 -5.420 1.00 30.20 O ANISOU 750 OG1 THR A 263 3297 4938 3238 -554 22 -215 O ATOM 751 CG2 THR A 263 43.747 -7.886 -3.619 1.00 35.32 C ANISOU 751 CG2 THR A 263 4098 5412 3910 -691 49 -341 C ATOM 752 N LYS A 264 41.728 -6.094 -6.130 1.00 23.43 N ANISOU 752 N LYS A 264 2733 3534 2636 -679 169 -357 N ATOM 753 CA LYS A 264 40.756 -5.045 -5.884 1.00 25.74 C ANISOU 753 CA LYS A 264 3130 3669 2982 -739 231 -401 C ATOM 754 C LYS A 264 39.366 -5.484 -6.325 1.00 25.37 C ANISOU 754 C LYS A 264 3131 3496 3012 -625 260 -387 C ATOM 755 O LYS A 264 38.386 -5.265 -5.613 1.00 22.02 O ANISOU 755 O LYS A 264 2786 2968 2613 -626 298 -414 O ATOM 756 CB LYS A 264 41.157 -3.792 -6.656 1.00 40.46 C ANISOU 756 CB LYS A 264 5001 5504 4867 -829 269 -403 C ATOM 757 CG LYS A 264 40.811 -2.492 -5.967 1.00 55.09 C ANISOU 757 CG LYS A 264 6966 7250 6717 -954 334 -456 C ATOM 758 CD LYS A 264 41.958 -2.052 -5.078 1.00 66.15 C ANISOU 758 CD LYS A 264 8353 8759 8022 -1109 305 -488 C ATOM 759 CE LYS A 264 43.262 -1.994 -5.864 1.00 70.39 C ANISOU 759 CE LYS A 264 8777 9444 8524 -1153 262 -452 C ATOM 760 NZ LYS A 264 44.412 -1.565 -5.015 1.00 73.51 N ANISOU 760 NZ LYS A 264 9142 9971 8816 -1320 226 -474 N ATOM 761 N ARG A 265 39.275 -6.091 -7.507 1.00 19.89 N ANISOU 761 N ARG A 265 2392 2814 2350 -530 245 -339 N ATOM 762 CA ARG A 265 37.983 -6.589 -7.992 1.00 18.35 C ANISOU 762 CA ARG A 265 2234 2521 2216 -434 263 -318 C ATOM 763 C ARG A 265 37.364 -7.618 -7.040 1.00 18.66 C ANISOU 763 C ARG A 265 2301 2555 2236 -380 245 -332 C ATOM 764 O ARG A 265 36.160 -7.592 -6.780 1.00 20.94 O ANISOU 764 O ARG A 265 2644 2744 2569 -353 276 -337 O ATOM 765 CB ARG A 265 38.103 -7.199 -9.401 1.00 17.53 C ANISOU 765 CB ARG A 265 2085 2445 2132 -352 241 -264 C ATOM 766 CG ARG A 265 38.375 -6.193 -10.509 1.00 21.21 C ANISOU 766 CG ARG A 265 2536 2885 2638 -384 269 -246 C ATOM 767 CD ARG A 265 38.151 -6.802 -11.897 1.00 15.94 C ANISOU 767 CD ARG A 265 1846 2212 1998 -295 255 -193 C ATOM 768 NE ARG A 265 38.801 -8.102 -12.042 1.00 17.62 N ANISOU 768 NE ARG A 265 2025 2516 2152 -227 207 -164 N ATOM 769 CZ ARG A 265 40.058 -8.268 -12.449 1.00 16.10 C ANISOU 769 CZ ARG A 265 1775 2425 1916 -222 186 -137 C ATOM 770 NH1 ARG A 265 40.807 -7.213 -12.744 1.00 19.65 N ANISOU 770 NH1 ARG A 265 2188 2901 2376 -295 200 -140 N ATOM 771 NH2 ARG A 265 40.568 -9.492 -12.561 1.00 16.60 N ANISOU 771 NH2 ARG A 265 1823 2564 1922 -142 158 -100 N ATOM 772 N GLN A 266 38.171 -8.534 -6.524 1.00 21.82 N ANISOU 772 N GLN A 266 2662 3063 2565 -357 200 -332 N ATOM 773 CA GLN A 266 37.596 -9.599 -5.702 1.00 21.97 C ANISOU 773 CA GLN A 266 2713 3074 2562 -294 188 -343 C ATOM 774 C GLN A 266 37.233 -9.077 -4.313 1.00 20.38 C ANISOU 774 C GLN A 266 2564 2825 2353 -358 209 -396 C ATOM 775 O GLN A 266 36.268 -9.535 -3.702 1.00 22.51 O ANISOU 775 O GLN A 266 2886 3026 2641 -317 223 -409 O ATOM 776 CB GLN A 266 38.530 -10.806 -5.589 1.00 28.72 C ANISOU 776 CB GLN A 266 3520 4056 3336 -229 147 -319 C ATOM 777 CG GLN A 266 39.372 -11.099 -6.832 1.00 44.73 C ANISOU 777 CG GLN A 266 5490 6159 5346 -186 131 -263 C ATOM 778 CD GLN A 266 38.552 -11.315 -8.096 1.00 44.40 C ANISOU 778 CD GLN A 266 5479 6029 5362 -130 145 -233 C ATOM 779 OE1 GLN A 266 37.374 -11.669 -8.033 1.00 52.49 O ANISOU 779 OE1 GLN A 266 6560 6963 6420 -102 157 -242 O ATOM 780 NE2 GLN A 266 39.182 -11.106 -9.260 1.00 23.00 N ANISOU 780 NE2 GLN A 266 2729 3353 2657 -119 141 -192 N ATOM 781 N GLU A 267 38.010 -8.118 -3.822 1.00 22.37 N ANISOU 781 N GLU A 267 2812 3113 2575 -465 212 -423 N ATOM 782 CA GLU A 267 37.739 -7.519 -2.519 1.00 30.12 C ANISOU 782 CA GLU A 267 3862 4042 3539 -541 238 -474 C ATOM 783 C GLU A 267 36.447 -6.725 -2.590 1.00 27.85 C ANISOU 783 C GLU A 267 3662 3591 3329 -543 307 -480 C ATOM 784 O GLU A 267 35.628 -6.761 -1.679 1.00 29.93 O ANISOU 784 O GLU A 267 3993 3774 3603 -531 337 -502 O ATOM 785 CB GLU A 267 38.889 -6.603 -2.095 1.00 25.45 C ANISOU 785 CB GLU A 267 3257 3527 2887 -678 228 -500 C ATOM 786 CG GLU A 267 38.583 -5.725 -0.887 1.00 36.98 C ANISOU 786 CG GLU A 267 4818 4905 4326 -782 267 -554 C ATOM 787 CD GLU A 267 38.688 -6.472 0.440 1.00 45.99 C ANISOU 787 CD GLU A 267 5970 6098 5405 -774 235 -582 C ATOM 788 OE1 GLU A 267 39.181 -7.621 0.450 1.00 48.44 O ANISOU 788 OE1 GLU A 267 6200 6527 5678 -696 180 -557 O ATOM 789 OE2 GLU A 267 38.287 -5.899 1.475 1.00 47.42 O ANISOU 789 OE2 GLU A 267 6249 6196 5572 -841 270 -625 O ATOM 790 N LYS A 268 36.281 -6.003 -3.688 1.00 21.77 N ANISOU 790 N LYS A 268 2887 2776 2610 -549 339 -454 N ATOM 791 CA LYS A 268 35.072 -5.236 -3.931 1.00 21.77 C ANISOU 791 CA LYS A 268 2956 2635 2680 -531 413 -440 C ATOM 792 C LYS A 268 33.852 -6.156 -4.001 1.00 26.58 C ANISOU 792 C LYS A 268 3566 3199 3335 -423 412 -409 C ATOM 793 O LYS A 268 32.807 -5.868 -3.419 1.00 29.74 O ANISOU 793 O LYS A 268 4030 3502 3767 -405 465 -407 O ATOM 794 CB LYS A 268 35.223 -4.431 -5.221 1.00 27.05 C ANISOU 794 CB LYS A 268 3605 3286 3388 -543 442 -409 C ATOM 795 CG LYS A 268 33.949 -3.813 -5.700 1.00 36.64 C ANISOU 795 CG LYS A 268 4868 4378 4674 -494 516 -373 C ATOM 796 CD LYS A 268 34.144 -3.105 -7.028 1.00 41.37 C ANISOU 796 CD LYS A 268 5441 4969 5309 -495 542 -341 C ATOM 797 CE LYS A 268 35.164 -1.997 -6.935 1.00 36.31 C ANISOU 797 CE LYS A 268 4835 4332 4630 -610 572 -377 C ATOM 798 NZ LYS A 268 35.069 -1.125 -8.138 1.00 33.82 N ANISOU 798 NZ LYS A 268 4522 3970 4357 -601 625 -345 N ATOM 799 N LEU A 269 33.989 -7.275 -4.699 1.00 25.34 N ANISOU 799 N LEU A 269 3343 3114 3172 -353 355 -381 N ATOM 800 CA LEU A 269 32.889 -8.232 -4.798 1.00 23.34 C ANISOU 800 CA LEU A 269 3094 2828 2947 -269 348 -354 C ATOM 801 C LEU A 269 32.528 -8.771 -3.412 1.00 22.06 C ANISOU 801 C LEU A 269 2977 2648 2759 -259 349 -389 C ATOM 802 O LEU A 269 31.356 -8.867 -3.051 1.00 25.68 O ANISOU 802 O LEU A 269 3472 3030 3256 -224 382 -375 O ATOM 803 CB LEU A 269 33.279 -9.375 -5.731 1.00 21.13 C ANISOU 803 CB LEU A 269 2760 2627 2643 -211 291 -325 C ATOM 804 CG LEU A 269 32.180 -10.370 -6.084 1.00 35.72 C ANISOU 804 CG LEU A 269 4617 4446 4510 -143 281 -293 C ATOM 805 CD1 LEU A 269 31.146 -9.708 -6.974 1.00 31.24 C ANISOU 805 CD1 LEU A 269 4046 3813 4012 -137 315 -245 C ATOM 806 CD2 LEU A 269 32.789 -11.589 -6.768 1.00 40.83 C ANISOU 806 CD2 LEU A 269 5242 5168 5104 -95 233 -276 C ATOM 807 N LYS A 270 33.546 -9.104 -2.631 1.00 21.01 N ANISOU 807 N LYS A 270 2835 2591 2558 -289 314 -428 N ATOM 808 CA LYS A 270 33.334 -9.584 -1.273 1.00 20.53 C ANISOU 808 CA LYS A 270 2818 2518 2464 -282 314 -465 C ATOM 809 C LYS A 270 32.594 -8.554 -0.430 1.00 21.46 C ANISOU 809 C LYS A 270 3018 2522 2615 -327 380 -485 C ATOM 810 O LYS A 270 31.683 -8.898 0.328 1.00 24.38 O ANISOU 810 O LYS A 270 3436 2827 3003 -288 404 -489 O ATOM 811 CB LYS A 270 34.663 -9.933 -0.610 1.00 26.29 C ANISOU 811 CB LYS A 270 3516 3365 3106 -315 268 -496 C ATOM 812 CG LYS A 270 34.502 -10.522 0.782 1.00 34.41 C ANISOU 812 CG LYS A 270 4588 4392 4094 -300 264 -533 C ATOM 813 CD LYS A 270 35.542 -9.970 1.728 1.00 39.84 C ANISOU 813 CD LYS A 270 5278 5148 4712 -392 248 -572 C ATOM 814 CE LYS A 270 35.299 -8.511 2.011 1.00 46.23 C ANISOU 814 CE LYS A 270 6157 5861 5547 -497 300 -596 C ATOM 815 NZ LYS A 270 36.396 -7.888 2.820 1.00 44.21 N ANISOU 815 NZ LYS A 270 5908 5679 5210 -618 279 -634 N ATOM 816 N ASN A 271 32.993 -7.293 -0.567 1.00 22.94 N ANISOU 816 N ASN A 271 3231 2680 2804 -409 415 -494 N ATOM 817 CA ASN A 271 32.380 -6.190 0.170 1.00 23.30 C ANISOU 817 CA ASN A 271 3378 2604 2868 -455 495 -509 C ATOM 818 C ASN A 271 30.940 -5.943 -0.234 1.00 24.39 C ANISOU 818 C ASN A 271 3546 2636 3086 -382 561 -456 C ATOM 819 O ASN A 271 30.081 -5.728 0.618 1.00 23.28 O ANISOU 819 O ASN A 271 3480 2402 2962 -362 617 -454 O ATOM 820 CB ASN A 271 33.194 -4.898 -0.006 1.00 24.15 C ANISOU 820 CB ASN A 271 3521 2705 2950 -568 526 -530 C ATOM 821 CG ASN A 271 34.478 -4.910 0.798 1.00 33.73 C ANISOU 821 CG ASN A 271 4729 4015 4073 -668 476 -583 C ATOM 822 OD1 ASN A 271 34.621 -5.692 1.736 1.00 33.86 O ANISOU 822 OD1 ASN A 271 4742 4076 4047 -654 437 -608 O ATOM 823 ND2 ASN A 271 35.419 -4.041 0.439 1.00 31.68 N ANISOU 823 ND2 ASN A 271 4465 3794 3778 -775 477 -596 N ATOM 824 N PHE A 272 30.678 -5.978 -1.537 1.00 19.84 N ANISOU 824 N PHE A 272 2907 2078 2555 -340 554 -405 N ATOM 825 CA PHE A 272 29.327 -5.789 -2.041 1.00 21.45 C ANISOU 825 CA PHE A 272 3115 2208 2828 -269 608 -340 C ATOM 826 C PHE A 272 28.405 -6.847 -1.456 1.00 26.49 C ANISOU 826 C PHE A 272 3747 2840 3478 -203 591 -326 C ATOM 827 O PHE A 272 27.345 -6.537 -0.905 1.00 26.38 O ANISOU 827 O PHE A 272 3782 2743 3498 -168 656 -295 O ATOM 828 CB PHE A 272 29.292 -5.892 -3.572 1.00 21.05 C ANISOU 828 CB PHE A 272 2983 2204 2809 -238 582 -290 C ATOM 829 CG PHE A 272 29.902 -4.718 -4.278 1.00 23.66 C ANISOU 829 CG PHE A 272 3324 2519 3145 -288 621 -288 C ATOM 830 CD1 PHE A 272 30.278 -3.589 -3.574 1.00 22.53 C ANISOU 830 CD1 PHE A 272 3271 2311 2979 -360 687 -324 C ATOM 831 CD2 PHE A 272 30.063 -4.731 -5.661 1.00 23.18 C ANISOU 831 CD2 PHE A 272 3196 2502 3108 -266 596 -250 C ATOM 832 CE1 PHE A 272 30.832 -2.497 -4.225 1.00 30.14 C ANISOU 832 CE1 PHE A 272 4256 3255 3941 -413 730 -324 C ATOM 833 CE2 PHE A 272 30.611 -3.648 -6.317 1.00 24.09 C ANISOU 833 CE2 PHE A 272 3324 2600 3229 -309 637 -248 C ATOM 834 CZ PHE A 272 30.990 -2.525 -5.598 1.00 26.50 C ANISOU 834 CZ PHE A 272 3719 2840 3510 -383 706 -286 C ATOM 835 N ILE A 273 28.821 -8.101 -1.576 1.00 18.34 N ANISOU 835 N ILE A 273 2662 1893 2413 -182 511 -344 N ATOM 836 CA ILE A 273 27.996 -9.216 -1.129 1.00 21.24 C ANISOU 836 CA ILE A 273 3026 2259 2784 -125 492 -334 C ATOM 837 C ILE A 273 27.846 -9.231 0.396 1.00 22.52 C ANISOU 837 C ILE A 273 3261 2369 2925 -131 520 -377 C ATOM 838 O ILE A 273 26.743 -9.369 0.915 1.00 26.81 O ANISOU 838 O ILE A 273 3834 2850 3502 -89 560 -350 O ATOM 839 CB ILE A 273 28.542 -10.556 -1.652 1.00 19.78 C ANISOU 839 CB ILE A 273 2791 2168 2555 -101 413 -344 C ATOM 840 CG1 ILE A 273 28.360 -10.641 -3.174 1.00 21.14 C ANISOU 840 CG1 ILE A 273 2906 2372 2753 -87 392 -290 C ATOM 841 CG2 ILE A 273 27.832 -11.731 -0.985 1.00 19.43 C ANISOU 841 CG2 ILE A 273 2768 2117 2498 -55 400 -349 C ATOM 842 CD1 ILE A 273 28.932 -11.921 -3.783 1.00 21.73 C ANISOU 842 CD1 ILE A 273 2954 2526 2775 -64 327 -294 C ATOM 843 N SER A 274 28.951 -9.065 1.110 1.00 21.49 N ANISOU 843 N SER A 274 3157 2270 2738 -184 501 -438 N ATOM 844 CA SER A 274 28.909 -9.115 2.570 1.00 24.47 C ANISOU 844 CA SER A 274 3607 2604 3085 -196 521 -484 C ATOM 845 C SER A 274 27.933 -8.098 3.130 1.00 26.40 C ANISOU 845 C SER A 274 3938 2720 3374 -195 615 -461 C ATOM 846 O SER A 274 27.171 -8.392 4.053 1.00 26.76 O ANISOU 846 O SER A 274 4034 2703 3430 -156 646 -461 O ATOM 847 CB SER A 274 30.293 -8.865 3.164 1.00 24.78 C ANISOU 847 CB SER A 274 3659 2709 3049 -274 487 -544 C ATOM 848 OG SER A 274 31.112 -9.996 2.980 1.00 29.96 O ANISOU 848 OG SER A 274 4245 3486 3653 -249 411 -558 O ATOM 849 N SER A 275 27.959 -6.903 2.554 1.00 23.76 N ANISOU 849 N SER A 275 3627 2341 3062 -232 668 -437 N ATOM 850 CA SER A 275 27.149 -5.790 3.034 1.00 25.06 C ANISOU 850 CA SER A 275 3892 2375 3256 -229 777 -408 C ATOM 851 C SER A 275 25.656 -6.030 2.837 1.00 29.61 C ANISOU 851 C SER A 275 4449 2901 3900 -130 825 -326 C ATOM 852 O SER A 275 24.829 -5.389 3.489 1.00 28.64 O ANISOU 852 O SER A 275 4411 2673 3799 -99 920 -292 O ATOM 853 CB SER A 275 27.547 -4.502 2.308 1.00 28.12 C ANISOU 853 CB SER A 275 4309 2731 3646 -284 830 -394 C ATOM 854 OG SER A 275 26.979 -4.477 1.011 1.00 28.10 O ANISOU 854 OG SER A 275 4226 2751 3700 -226 836 -323 O ATOM 855 N GLN A 276 25.315 -6.932 1.924 1.00 23.16 N ANISOU 855 N GLN A 276 3525 2163 3111 -84 765 -288 N ATOM 856 CA GLN A 276 23.913 -7.218 1.618 1.00 24.62 C ANISOU 856 CA GLN A 276 3671 2330 3353 -6 797 -202 C ATOM 857 C GLN A 276 23.595 -8.709 1.745 1.00 23.89 C ANISOU 857 C GLN A 276 3524 2301 3252 24 722 -211 C ATOM 858 O GLN A 276 22.678 -9.215 1.102 1.00 19.38 O ANISOU 858 O GLN A 276 2888 1762 2714 63 711 -144 O ATOM 859 CB GLN A 276 23.589 -6.742 0.199 1.00 27.09 C ANISOU 859 CB GLN A 276 3914 2675 3705 11 807 -129 C ATOM 860 CG GLN A 276 23.663 -5.232 0.029 1.00 38.34 C ANISOU 860 CG GLN A 276 5403 4022 5141 -1 905 -104 C ATOM 861 CD GLN A 276 22.683 -4.494 0.935 1.00 49.04 C ANISOU 861 CD GLN A 276 6852 5264 6518 49 1025 -54 C ATOM 862 OE1 GLN A 276 21.566 -4.955 1.169 1.00 49.40 O ANISOU 862 OE1 GLN A 276 6867 5307 6598 118 1044 12 O ATOM 863 NE2 GLN A 276 23.101 -3.340 1.444 1.00 53.85 N ANISOU 863 NE2 GLN A 276 7582 5778 7102 12 1111 -80 N ATOM 864 N MET A 277 24.349 -9.408 2.583 1.00 27.82 N ANISOU 864 N MET A 277 3751 3173 3646 -533 873 -13 N ATOM 865 CA MET A 277 24.298 -10.872 2.599 1.00 22.96 C ANISOU 865 CA MET A 277 3084 2621 3019 -501 773 -27 C ATOM 866 C MET A 277 22.896 -11.458 2.789 1.00 22.51 C ANISOU 866 C MET A 277 3019 2527 3008 -435 791 42 C ATOM 867 O MET A 277 22.464 -12.314 2.010 1.00 21.48 O ANISOU 867 O MET A 277 2816 2450 2896 -395 731 80 O ATOM 868 CB MET A 277 25.263 -11.436 3.648 1.00 24.03 C ANISOU 868 CB MET A 277 3259 2780 3092 -546 716 -109 C ATOM 869 CG MET A 277 25.379 -12.958 3.622 1.00 23.33 C ANISOU 869 CG MET A 277 3108 2765 2994 -516 613 -128 C ATOM 870 SD MET A 277 26.100 -13.543 2.074 1.00 30.53 S ANISOU 870 SD MET A 277 3916 3783 3902 -504 532 -129 S ATOM 871 CE MET A 277 27.769 -12.948 2.280 1.00 36.30 C ANISOU 871 CE MET A 277 4667 4550 4576 -583 513 -188 C ATOM 872 N THR A 278 22.184 -11.011 3.819 1.00 22.82 N ANISOU 872 N THR A 278 3138 2472 3062 -425 873 63 N ATOM 873 CA THR A 278 20.873 -11.587 4.112 1.00 22.67 C ANISOU 873 CA THR A 278 3114 2416 3085 -359 887 137 C ATOM 874 C THR A 278 19.896 -11.368 2.966 1.00 23.28 C ANISOU 874 C THR A 278 3126 2495 3224 -316 918 251 C ATOM 875 O THR A 278 19.212 -12.296 2.534 1.00 23.34 O ANISOU 875 O THR A 278 3077 2542 3249 -274 859 307 O ATOM 876 CB THR A 278 20.266 -11.016 5.407 1.00 23.95 C ANISOU 876 CB THR A 278 3380 2465 3255 -353 987 147 C ATOM 877 OG1 THR A 278 21.100 -11.369 6.515 1.00 26.61 O ANISOU 877 OG1 THR A 278 3773 2808 3530 -402 946 49 O ATOM 878 CG2 THR A 278 18.867 -11.574 5.632 1.00 23.36 C ANISOU 878 CG2 THR A 278 3294 2353 3230 -276 1001 242 C ATOM 879 N ASP A 279 19.831 -10.137 2.474 1.00 23.11 N ANISOU 879 N ASP A 279 3112 2434 3234 -334 1011 291 N ATOM 880 CA ASP A 279 18.912 -9.814 1.393 1.00 20.68 C ANISOU 880 CA ASP A 279 2735 2130 2992 -306 1051 413 C ATOM 881 C ASP A 279 19.223 -10.621 0.131 1.00 22.21 C ANISOU 881 C ASP A 279 2828 2436 3173 -313 940 415 C ATOM 882 O ASP A 279 18.314 -11.096 -0.542 1.00 22.64 O ANISOU 882 O ASP A 279 2825 2515 3262 -285 920 513 O ATOM 883 CB ASP A 279 18.936 -8.316 1.092 1.00 35.85 C ANISOU 883 CB ASP A 279 4674 3995 4952 -330 1172 448 C ATOM 884 CG ASP A 279 18.305 -7.484 2.204 1.00 49.44 C ANISOU 884 CG ASP A 279 6498 5587 6699 -315 1309 480 C ATOM 885 OD1 ASP A 279 17.411 -7.999 2.910 1.00 49.85 O ANISOU 885 OD1 ASP A 279 6580 5591 6768 -267 1325 530 O ATOM 886 OD2 ASP A 279 18.707 -6.313 2.370 1.00 61.36 O ANISOU 886 OD2 ASP A 279 8061 7040 8212 -350 1402 456 O ATOM 887 N MET A 280 20.504 -10.772 -0.195 1.00 19.42 N ANISOU 887 N MET A 280 2459 2151 2770 -354 871 314 N ATOM 888 CA MET A 280 20.871 -11.560 -1.366 1.00 17.13 C ANISOU 888 CA MET A 280 2086 1961 2462 -361 774 308 C ATOM 889 C MET A 280 20.532 -13.054 -1.191 1.00 17.31 C ANISOU 889 C MET A 280 2094 2022 2461 -329 682 303 C ATOM 890 O MET A 280 20.034 -13.703 -2.116 1.00 19.04 O ANISOU 890 O MET A 280 2256 2291 2688 -319 633 360 O ATOM 891 CB MET A 280 22.349 -11.354 -1.716 1.00 16.66 C ANISOU 891 CB MET A 280 2015 1959 2356 -406 729 209 C ATOM 892 CG MET A 280 22.659 -9.952 -2.268 1.00 22.45 C ANISOU 892 CG MET A 280 2737 2677 3116 -437 802 227 C ATOM 893 SD MET A 280 24.392 -9.788 -2.736 1.00 23.43 S ANISOU 893 SD MET A 280 2840 2877 3184 -484 735 126 S ATOM 894 CE MET A 280 24.371 -10.524 -4.373 1.00 22.17 C ANISOU 894 CE MET A 280 2574 2818 3032 -476 658 160 C ATOM 895 N CYS A 281 20.772 -13.601 -0.005 1.00 20.48 N ANISOU 895 N CYS A 281 2548 2402 2833 -318 658 239 N ATOM 896 CA CYS A 281 20.495 -15.022 0.218 1.00 17.51 C ANISOU 896 CA CYS A 281 2154 2063 2437 -286 571 230 C ATOM 897 C CYS A 281 19.010 -15.340 0.043 1.00 21.10 C ANISOU 897 C CYS A 281 2592 2491 2933 -241 582 351 C ATOM 898 O CYS A 281 18.635 -16.396 -0.483 1.00 20.83 O ANISOU 898 O CYS A 281 2518 2507 2887 -224 506 379 O ATOM 899 CB CYS A 281 20.946 -15.465 1.615 1.00 19.21 C ANISOU 899 CB CYS A 281 2422 2257 2621 -285 551 150 C ATOM 900 SG CYS A 281 22.724 -15.581 1.832 1.00 23.62 S ANISOU 900 SG CYS A 281 2982 2872 3121 -342 501 25 S ATOM 901 N LEU A 282 18.170 -14.422 0.503 1.00 18.62 N ANISOU 901 N LEU A 282 2314 2095 2665 -222 681 428 N ATOM 902 CA LEU A 282 16.720 -14.596 0.473 1.00 20.36 C ANISOU 902 CA LEU A 282 2523 2280 2932 -176 706 564 C ATOM 903 C LEU A 282 16.112 -14.400 -0.920 1.00 24.63 C ANISOU 903 C LEU A 282 2995 2859 3505 -191 710 680 C ATOM 904 O LEU A 282 14.987 -14.823 -1.176 1.00 27.82 O ANISOU 904 O LEU A 282 3373 3262 3936 -165 698 803 O ATOM 905 CB LEU A 282 16.070 -13.616 1.456 1.00 24.09 C ANISOU 905 CB LEU A 282 3063 2643 3448 -151 829 615 C ATOM 906 CG LEU A 282 15.631 -14.056 2.856 1.00 30.18 C ANISOU 906 CG LEU A 282 3896 3355 4214 -107 834 601 C ATOM 907 CD1 LEU A 282 16.007 -15.479 3.234 1.00 21.28 C ANISOU 907 CD1 LEU A 282 2752 2294 3039 -96 706 522 C ATOM 908 CD2 LEU A 282 16.098 -13.067 3.908 1.00 31.48 C ANISOU 908 CD2 LEU A 282 4152 3437 4373 -128 932 533 C ATOM 909 N ASP A 283 16.852 -13.745 -1.809 1.00 26.23 N ANISOU 909 N ASP A 283 3164 3098 3705 -238 724 648 N ATOM 910 CA ASP A 283 16.358 -13.440 -3.148 1.00 25.43 C ANISOU 910 CA ASP A 283 2991 3037 3636 -265 733 755 C ATOM 911 C ASP A 283 16.517 -14.638 -4.069 1.00 27.89 C ANISOU 911 C ASP A 283 3257 3440 3900 -286 617 742 C ATOM 912 O ASP A 283 17.574 -15.256 -4.115 1.00 20.90 O ANISOU 912 O ASP A 283 2379 2603 2961 -299 547 619 O ATOM 913 CB ASP A 283 17.125 -12.256 -3.746 1.00 21.95 C ANISOU 913 CB ASP A 283 2527 2602 3210 -307 791 722 C ATOM 914 CG ASP A 283 16.556 -11.809 -5.082 1.00 24.51 C ANISOU 914 CG ASP A 283 2769 2966 3578 -341 813 844 C ATOM 915 OD1 ASP A 283 17.130 -12.157 -6.136 1.00 23.45 O ANISOU 915 OD1 ASP A 283 2583 2914 3413 -381 743 810 O ATOM 916 OD2 ASP A 283 15.514 -11.125 -5.077 1.00 30.82 O ANISOU 916 OD2 ASP A 283 3552 3714 4445 -328 902 981 O ATOM 917 N LYS A 284 15.475 -14.930 -4.836 1.00 22.84 N ANISOU 917 N LYS A 284 2574 2823 3282 -296 602 878 N ATOM 918 CA LYS A 284 15.465 -16.090 -5.720 1.00 23.66 C ANISOU 918 CA LYS A 284 2649 3006 3336 -324 496 881 C ATOM 919 C LYS A 284 16.655 -16.116 -6.684 1.00 20.97 C ANISOU 919 C LYS A 284 2280 2733 2954 -373 457 779 C ATOM 920 O LYS A 284 17.222 -17.171 -6.949 1.00 25.99 O ANISOU 920 O LYS A 284 2925 3419 3532 -382 374 700 O ATOM 921 CB LYS A 284 14.143 -16.145 -6.499 1.00 27.88 C ANISOU 921 CB LYS A 284 3139 3553 3901 -347 499 1066 C ATOM 922 CG LYS A 284 13.989 -17.344 -7.425 1.00 34.15 C ANISOU 922 CG LYS A 284 3916 4423 4636 -389 393 1085 C ATOM 923 CD LYS A 284 12.639 -17.296 -8.138 1.00 39.89 C ANISOU 923 CD LYS A 284 4601 5163 5392 -425 399 1289 C ATOM 924 CE LYS A 284 12.622 -18.154 -9.401 1.00 49.30 C ANISOU 924 CE LYS A 284 5772 6437 6522 -502 311 1312 C ATOM 925 NZ LYS A 284 12.514 -19.616 -9.131 1.00 56.37 N ANISOU 925 NZ LYS A 284 6717 7351 7349 -486 210 1270 N ATOM 926 N PHE A 285 17.045 -14.955 -7.193 1.00 19.63 N ANISOU 926 N PHE A 285 2077 2564 2818 -403 520 784 N ATOM 927 CA PHE A 285 18.120 -14.896 -8.184 1.00 18.59 C ANISOU 927 CA PHE A 285 1911 2499 2653 -448 485 704 C ATOM 928 C PHE A 285 19.495 -14.592 -7.597 1.00 19.47 C ANISOU 928 C PHE A 285 2054 2604 2739 -434 488 557 C ATOM 929 O PHE A 285 20.494 -15.180 -8.018 1.00 20.05 O ANISOU 929 O PHE A 285 2125 2731 2762 -448 427 464 O ATOM 930 CB PHE A 285 17.758 -13.901 -9.299 1.00 21.92 C ANISOU 930 CB PHE A 285 2261 2944 3122 -497 535 806 C ATOM 931 CG PHE A 285 16.386 -14.138 -9.864 1.00 22.08 C ANISOU 931 CG PHE A 285 2245 2975 3169 -523 536 974 C ATOM 932 CD1 PHE A 285 16.131 -15.268 -10.622 1.00 25.81 C ANISOU 932 CD1 PHE A 285 2712 3506 3588 -560 448 998 C ATOM 933 CD2 PHE A 285 15.345 -13.268 -9.590 1.00 23.24 C ANISOU 933 CD2 PHE A 285 2370 3069 3393 -511 626 1116 C ATOM 934 CE1 PHE A 285 14.853 -15.514 -11.126 1.00 28.19 C ANISOU 934 CE1 PHE A 285 2984 3820 3906 -594 441 1166 C ATOM 935 CE2 PHE A 285 14.071 -13.501 -10.090 1.00 28.72 C ANISOU 935 CE2 PHE A 285 3025 3774 4112 -538 625 1292 C ATOM 936 CZ PHE A 285 13.827 -14.629 -10.858 1.00 26.15 C ANISOU 936 CZ PHE A 285 2693 3514 3727 -584 526 1318 C ATOM 937 N ALA A 286 19.558 -13.680 -6.630 1.00 15.99 N ANISOU 937 N ALA A 286 1648 2097 2331 -411 562 543 N ATOM 938 CA ALA A 286 20.855 -13.324 -6.055 1.00 20.62 C ANISOU 938 CA ALA A 286 2268 2678 2888 -413 563 417 C ATOM 939 C ALA A 286 21.437 -14.477 -5.230 1.00 17.84 C ANISOU 939 C ALA A 286 1960 2336 2482 -390 494 321 C ATOM 940 O ALA A 286 22.644 -14.548 -5.026 1.00 17.29 O ANISOU 940 O ALA A 286 1903 2292 2375 -401 466 223 O ATOM 941 CB ALA A 286 20.754 -12.048 -5.219 1.00 18.83 C ANISOU 941 CB ALA A 286 2080 2373 2702 -406 664 427 C ATOM 942 N CYS A 287 20.590 -15.393 -4.763 1.00 16.11 N ANISOU 942 N CYS A 287 1759 2101 2260 -359 464 358 N ATOM 943 CA CYS A 287 21.120 -16.534 -4.019 1.00 15.26 C ANISOU 943 CA CYS A 287 1681 2010 2108 -338 397 271 C ATOM 944 C CYS A 287 21.981 -17.397 -4.947 1.00 16.99 C ANISOU 944 C CYS A 287 1869 2306 2281 -357 325 213 C ATOM 945 O CYS A 287 22.901 -18.080 -4.507 1.00 15.56 O ANISOU 945 O CYS A 287 1701 2148 2065 -351 283 126 O ATOM 946 CB CYS A 287 20.005 -17.359 -3.350 1.00 18.38 C ANISOU 946 CB CYS A 287 2096 2375 2512 -297 376 326 C ATOM 947 SG CYS A 287 19.101 -18.471 -4.445 1.00 19.61 S ANISOU 947 SG CYS A 287 2216 2582 2653 -300 306 411 S ATOM 948 N ARG A 288 21.699 -17.339 -6.240 1.00 15.48 N ANISOU 948 N ARG A 288 1637 2153 2092 -385 316 268 N ATOM 949 CA ARG A 288 22.522 -18.057 -7.211 1.00 15.85 C ANISOU 949 CA ARG A 288 1663 2267 2094 -406 261 215 C ATOM 950 C ARG A 288 23.910 -17.433 -7.349 1.00 16.27 C ANISOU 950 C ARG A 288 1705 2343 2135 -421 272 136 C ATOM 951 O ARG A 288 24.912 -18.141 -7.491 1.00 16.07 O ANISOU 951 O ARG A 288 1680 2355 2071 -419 231 64 O ATOM 952 CB ARG A 288 21.812 -18.106 -8.565 1.00 15.74 C ANISOU 952 CB ARG A 288 1612 2287 2081 -444 251 300 C ATOM 953 CG ARG A 288 20.421 -18.767 -8.485 1.00 15.76 C ANISOU 953 CG ARG A 288 1625 2274 2090 -438 230 397 C ATOM 954 CD ARG A 288 20.512 -20.290 -8.281 1.00 20.51 C ANISOU 954 CD ARG A 288 2260 2894 2640 -419 159 348 C ATOM 955 NE ARG A 288 19.207 -20.923 -8.482 1.00 20.55 N ANISOU 955 NE ARG A 288 2272 2896 2641 -426 128 453 N ATOM 956 CZ ARG A 288 19.022 -22.205 -8.781 1.00 23.11 C ANISOU 956 CZ ARG A 288 2620 3246 2916 -432 63 445 C ATOM 957 NH1 ARG A 288 20.061 -23.029 -8.912 1.00 21.85 N ANISOU 957 NH1 ARG A 288 2479 3113 2711 -427 31 335 N ATOM 958 NH2 ARG A 288 17.790 -22.665 -8.952 1.00 23.07 N ANISOU 958 NH2 ARG A 288 2622 3238 2906 -444 34 555 N ATOM 959 N VAL A 289 23.961 -16.107 -7.317 1.00 19.10 N ANISOU 959 N VAL A 289 2052 2677 2528 -436 331 158 N ATOM 960 CA VAL A 289 25.229 -15.384 -7.336 1.00 22.34 C ANISOU 960 CA VAL A 289 2455 3105 2927 -452 341 94 C ATOM 961 C VAL A 289 26.060 -15.724 -6.104 1.00 19.74 C ANISOU 961 C VAL A 289 2170 2759 2570 -438 325 17 C ATOM 962 O VAL A 289 27.269 -15.922 -6.196 1.00 16.08 O ANISOU 962 O VAL A 289 1701 2335 2075 -446 295 -42 O ATOM 963 CB VAL A 289 24.999 -13.859 -7.428 1.00 18.77 C ANISOU 963 CB VAL A 289 1989 2621 2521 -470 412 138 C ATOM 964 CG1 VAL A 289 26.324 -13.093 -7.292 1.00 16.70 C ANISOU 964 CG1 VAL A 289 1729 2373 2241 -488 417 73 C ATOM 965 CG2 VAL A 289 24.328 -13.514 -8.748 1.00 15.76 C ANISOU 965 CG2 VAL A 289 1546 2272 2170 -495 424 220 C ATOM 966 N ILE A 290 25.403 -15.806 -4.950 1.00 16.63 N ANISOU 966 N ILE A 290 1819 2310 2189 -419 346 26 N ATOM 967 CA ILE A 290 26.079 -16.186 -3.715 1.00 16.28 C ANISOU 967 CA ILE A 290 1814 2253 2119 -415 330 -40 C ATOM 968 C ILE A 290 26.675 -17.584 -3.823 1.00 15.17 C ANISOU 968 C ILE A 290 1657 2164 1944 -401 261 -85 C ATOM 969 O ILE A 290 27.846 -17.799 -3.520 1.00 16.00 O ANISOU 969 O ILE A 290 1760 2298 2022 -414 238 -138 O ATOM 970 CB ILE A 290 25.111 -16.200 -2.516 1.00 15.99 C ANISOU 970 CB ILE A 290 1824 2149 2103 -394 360 -17 C ATOM 971 CG1 ILE A 290 24.476 -14.822 -2.300 1.00 19.52 C ANISOU 971 CG1 ILE A 290 2299 2530 2588 -404 447 33 C ATOM 972 CG2 ILE A 290 25.834 -16.655 -1.254 1.00 15.84 C ANISOU 972 CG2 ILE A 290 1839 2126 2055 -401 337 -84 C ATOM 973 CD1 ILE A 290 25.466 -13.766 -1.949 1.00 31.79 C ANISOU 973 CD1 ILE A 290 3882 4071 4127 -444 483 -13 C ATOM 974 N GLN A 291 25.860 -18.542 -4.239 1.00 14.98 N ANISOU 974 N GLN A 291 1621 2150 1921 -377 230 -55 N ATOM 975 CA GLN A 291 26.341 -19.916 -4.341 1.00 15.89 C ANISOU 975 CA GLN A 291 1726 2307 2007 -361 174 -96 C ATOM 976 C GLN A 291 27.533 -20.038 -5.288 1.00 18.09 C ANISOU 976 C GLN A 291 1977 2639 2259 -377 160 -130 C ATOM 977 O GLN A 291 28.517 -20.717 -4.981 1.00 15.88 O ANISOU 977 O GLN A 291 1690 2385 1957 -372 137 -177 O ATOM 978 CB GLN A 291 25.202 -20.834 -4.775 1.00 14.63 C ANISOU 978 CB GLN A 291 1565 2146 1847 -340 145 -50 C ATOM 979 CG GLN A 291 24.139 -20.999 -3.683 1.00 14.47 C ANISOU 979 CG GLN A 291 1570 2079 1850 -312 148 -17 C ATOM 980 CD GLN A 291 22.936 -21.772 -4.175 1.00 17.75 C ANISOU 980 CD GLN A 291 1984 2495 2265 -296 116 49 C ATOM 981 OE1 GLN A 291 23.036 -22.963 -4.483 1.00 17.33 O ANISOU 981 OE1 GLN A 291 1928 2473 2182 -288 66 27 O ATOM 982 NE2 GLN A 291 21.792 -21.103 -4.251 1.00 15.26 N ANISOU 982 NE2 GLN A 291 1672 2144 1981 -295 148 138 N ATOM 983 N SER A 292 27.447 -19.383 -6.440 1.00 15.50 N ANISOU 983 N SER A 292 1628 2327 1935 -396 175 -100 N ATOM 984 CA SER A 292 28.531 -19.451 -7.414 1.00 19.68 C ANISOU 984 CA SER A 292 2131 2905 2440 -408 163 -127 C ATOM 985 C SER A 292 29.804 -18.873 -6.822 1.00 17.81 C ANISOU 985 C SER A 292 1892 2679 2197 -418 171 -165 C ATOM 986 O SER A 292 30.897 -19.424 -7.006 1.00 24.22 O ANISOU 986 O SER A 292 2690 3527 2985 -412 152 -195 O ATOM 987 CB SER A 292 28.174 -18.655 -8.675 1.00 24.14 C ANISOU 987 CB SER A 292 2667 3488 3017 -434 181 -83 C ATOM 988 OG SER A 292 27.162 -19.321 -9.389 1.00 49.39 O ANISOU 988 OG SER A 292 5866 6690 6209 -440 166 -41 O ATOM 989 N SER A 293 29.661 -17.747 -6.130 1.00 15.49 N ANISOU 989 N SER A 293 1612 2350 1922 -435 203 -155 N ATOM 990 CA SER A 293 30.808 -17.083 -5.520 1.00 15.49 C ANISOU 990 CA SER A 293 1620 2357 1909 -458 208 -181 C ATOM 991 C SER A 293 31.477 -17.946 -4.452 1.00 21.40 C ANISOU 991 C SER A 293 2383 3113 2636 -456 182 -214 C ATOM 992 O SER A 293 32.706 -17.998 -4.364 1.00 19.25 O ANISOU 992 O SER A 293 2096 2876 2342 -471 166 -227 O ATOM 993 CB SER A 293 30.407 -15.721 -4.947 1.00 19.55 C ANISOU 993 CB SER A 293 2163 2822 2443 -483 255 -164 C ATOM 994 OG SER A 293 29.913 -14.880 -5.976 1.00 18.96 O ANISOU 994 OG SER A 293 2061 2749 2395 -488 283 -126 O ATOM 995 N LEU A 294 30.664 -18.609 -3.633 1.00 16.05 N ANISOU 995 N LEU A 294 1726 2403 1968 -439 178 -218 N ATOM 996 CA LEU A 294 31.180 -19.456 -2.562 1.00 16.50 C ANISOU 996 CA LEU A 294 1787 2469 2012 -441 154 -244 C ATOM 997 C LEU A 294 32.066 -20.580 -3.100 1.00 16.18 C ANISOU 997 C LEU A 294 1709 2483 1958 -422 124 -257 C ATOM 998 O LEU A 294 33.057 -20.945 -2.475 1.00 16.92 O ANISOU 998 O LEU A 294 1787 2601 2039 -438 111 -265 O ATOM 999 CB LEU A 294 30.023 -20.064 -1.758 1.00 15.51 C ANISOU 999 CB LEU A 294 1682 2306 1904 -416 149 -242 C ATOM 1000 CG LEU A 294 29.299 -19.105 -0.812 1.00 15.57 C ANISOU 1000 CG LEU A 294 1737 2252 1927 -433 187 -231 C ATOM 1001 CD1 LEU A 294 27.956 -19.714 -0.367 1.00 14.88 C ANISOU 1001 CD1 LEU A 294 1662 2129 1862 -394 183 -211 C ATOM 1002 CD2 LEU A 294 30.208 -18.771 0.393 1.00 15.44 C ANISOU 1002 CD2 LEU A 294 1744 2234 1889 -482 190 -259 C ATOM 1003 N GLN A 295 31.715 -21.145 -4.249 1.00 15.14 N ANISOU 1003 N GLN A 295 1563 2366 1825 -394 117 -251 N ATOM 1004 CA GLN A 295 32.503 -22.271 -4.740 1.00 17.51 C ANISOU 1004 CA GLN A 295 1838 2705 2111 -373 102 -263 C ATOM 1005 C GLN A 295 33.606 -21.876 -5.717 1.00 21.26 C ANISOU 1005 C GLN A 295 2290 3216 2570 -380 111 -255 C ATOM 1006 O GLN A 295 34.507 -22.664 -5.983 1.00 22.16 O ANISOU 1006 O GLN A 295 2385 3360 2675 -364 110 -257 O ATOM 1007 CB GLN A 295 31.607 -23.364 -5.352 1.00 21.93 C ANISOU 1007 CB GLN A 295 2406 3258 2668 -342 90 -265 C ATOM 1008 CG GLN A 295 30.956 -23.005 -6.669 1.00 26.88 C ANISOU 1008 CG GLN A 295 3042 3885 3287 -348 97 -244 C ATOM 1009 CD GLN A 295 29.997 -24.090 -7.153 1.00 36.03 C ANISOU 1009 CD GLN A 295 4220 5036 4434 -332 80 -238 C ATOM 1010 OE1 GLN A 295 29.507 -24.047 -8.279 1.00 33.84 O ANISOU 1010 OE1 GLN A 295 3951 4764 4142 -346 81 -217 O ATOM 1011 NE2 GLN A 295 29.729 -25.064 -6.298 1.00 24.33 N ANISOU 1011 NE2 GLN A 295 2745 3544 2957 -308 61 -252 N ATOM 1012 N ASN A 296 33.539 -20.663 -6.247 1.00 17.98 N ANISOU 1012 N ASN A 296 1875 2799 2157 -401 123 -241 N ATOM 1013 CA ASN A 296 34.487 -20.250 -7.280 1.00 22.17 C ANISOU 1013 CA ASN A 296 2381 3368 2676 -403 126 -231 C ATOM 1014 C ASN A 296 35.556 -19.266 -6.799 1.00 20.93 C ANISOU 1014 C ASN A 296 2214 3227 2513 -433 124 -217 C ATOM 1015 O ASN A 296 36.678 -19.293 -7.285 1.00 21.70 O ANISOU 1015 O ASN A 296 2285 3362 2596 -428 119 -202 O ATOM 1016 CB ASN A 296 33.745 -19.694 -8.504 1.00 22.26 C ANISOU 1016 CB ASN A 296 2386 3378 2692 -407 135 -218 C ATOM 1017 CG ASN A 296 32.956 -20.767 -9.242 1.00 31.49 C ANISOU 1017 CG ASN A 296 3568 4545 3853 -390 130 -222 C ATOM 1018 OD1 ASN A 296 33.377 -21.917 -9.309 1.00 30.98 O ANISOU 1018 OD1 ASN A 296 3510 4490 3772 -368 126 -239 O ATOM 1019 ND2 ASN A 296 31.804 -20.392 -9.798 1.00 25.57 N ANISOU 1019 ND2 ASN A 296 2822 3780 3114 -406 135 -199 N ATOM 1020 N MET A 297 35.210 -18.403 -5.843 1.00 18.10 N ANISOU 1020 N MET A 297 1880 2837 2159 -465 131 -217 N ATOM 1021 CA MET A 297 36.144 -17.385 -5.376 1.00 18.62 C ANISOU 1021 CA MET A 297 1949 2914 2211 -505 129 -202 C ATOM 1022 C MET A 297 37.308 -18.047 -4.663 1.00 17.98 C ANISOU 1022 C MET A 297 1855 2866 2111 -519 109 -187 C ATOM 1023 O MET A 297 37.204 -19.199 -4.239 1.00 18.99 O ANISOU 1023 O MET A 297 1976 2995 2245 -499 104 -196 O ATOM 1024 CB MET A 297 35.465 -16.415 -4.402 1.00 17.16 C ANISOU 1024 CB MET A 297 1811 2678 2031 -543 151 -209 C ATOM 1025 CG MET A 297 34.484 -15.437 -5.018 1.00 28.43 C ANISOU 1025 CG MET A 297 3246 4073 3484 -539 182 -203 C ATOM 1026 SD MET A 297 33.785 -14.376 -3.714 1.00 37.34 S ANISOU 1026 SD MET A 297 4442 5128 4617 -581 226 -207 S ATOM 1027 CE MET A 297 35.201 -13.369 -3.291 1.00 60.49 C ANISOU 1027 CE MET A 297 7392 8081 7509 -642 215 -201 C ATOM 1028 N ASP A 298 38.420 -17.331 -4.538 1.00 18.27 N ANISOU 1028 N ASP A 298 1884 2931 2126 -554 96 -156 N ATOM 1029 CA ASP A 298 39.513 -17.825 -3.708 1.00 19.94 C ANISOU 1029 CA ASP A 298 2082 3175 2321 -584 78 -122 C ATOM 1030 C ASP A 298 38.924 -18.162 -2.340 1.00 20.57 C ANISOU 1030 C ASP A 298 2193 3221 2402 -615 81 -143 C ATOM 1031 O ASP A 298 38.086 -17.434 -1.830 1.00 19.01 O ANISOU 1031 O ASP A 298 2043 2976 2204 -640 96 -170 O ATOM 1032 CB ASP A 298 40.604 -16.773 -3.568 1.00 18.46 C ANISOU 1032 CB ASP A 298 1896 3014 2103 -636 60 -77 C ATOM 1033 CG ASP A 298 41.313 -16.502 -4.886 1.00 25.57 C ANISOU 1033 CG ASP A 298 2756 3955 3003 -600 51 -48 C ATOM 1034 OD1 ASP A 298 41.362 -17.412 -5.743 1.00 18.46 O ANISOU 1034 OD1 ASP A 298 1823 3072 2120 -542 60 -49 O ATOM 1035 OD2 ASP A 298 41.809 -15.380 -5.064 1.00 26.32 O ANISOU 1035 OD2 ASP A 298 2857 4064 3081 -632 37 -24 O ATOM 1036 N LEU A 299 39.362 -19.267 -1.759 1.00 16.52 N ANISOU 1036 N LEU A 299 1652 2731 1894 -614 71 -127 N ATOM 1037 CA LEU A 299 38.766 -19.751 -0.521 1.00 17.98 C ANISOU 1037 CA LEU A 299 1854 2891 2085 -637 70 -149 C ATOM 1038 C LEU A 299 38.798 -18.719 0.602 1.00 17.55 C ANISOU 1038 C LEU A 299 1853 2813 2003 -720 68 -147 C ATOM 1039 O LEU A 299 37.813 -18.547 1.313 1.00 17.32 O ANISOU 1039 O LEU A 299 1867 2734 1979 -730 82 -184 O ATOM 1040 CB LEU A 299 39.428 -21.055 -0.077 1.00 22.71 C ANISOU 1040 CB LEU A 299 2400 3531 2699 -631 60 -120 C ATOM 1041 CG LEU A 299 38.826 -21.698 1.174 1.00 20.86 C ANISOU 1041 CG LEU A 299 2169 3279 2477 -650 53 -142 C ATOM 1042 CD1 LEU A 299 37.319 -21.874 1.038 1.00 16.00 C ANISOU 1042 CD1 LEU A 299 1587 2612 1882 -600 61 -201 C ATOM 1043 CD2 LEU A 299 39.506 -23.036 1.443 1.00 23.09 C ANISOU 1043 CD2 LEU A 299 2383 3606 2783 -637 49 -107 C ATOM 1044 N SER A 300 39.923 -18.029 0.769 1.00 17.85 N ANISOU 1044 N SER A 300 1893 2883 2008 -781 54 -100 N ATOM 1045 CA SER A 300 40.018 -17.018 1.821 1.00 20.07 C ANISOU 1045 CA SER A 300 2237 3139 2251 -873 54 -97 C ATOM 1046 C SER A 300 38.934 -15.950 1.714 1.00 24.19 C ANISOU 1046 C SER A 300 2828 3591 2773 -868 89 -146 C ATOM 1047 O SER A 300 38.409 -15.483 2.725 1.00 23.48 O ANISOU 1047 O SER A 300 2803 3452 2667 -919 109 -169 O ATOM 1048 CB SER A 300 41.402 -16.366 1.824 1.00 32.06 C ANISOU 1048 CB SER A 300 3750 4705 3727 -941 28 -28 C ATOM 1049 OG SER A 300 42.383 -17.318 2.195 1.00 41.32 O ANISOU 1049 OG SER A 300 4862 5938 4901 -962 3 36 O ATOM 1050 N LEU A 301 38.596 -15.559 0.493 1.00 20.02 N ANISOU 1050 N LEU A 301 2284 3057 2265 -809 102 -157 N ATOM 1051 CA LEU A 301 37.519 -14.591 0.298 1.00 17.60 C ANISOU 1051 CA LEU A 301 2029 2688 1973 -798 144 -190 C ATOM 1052 C LEU A 301 36.138 -15.213 0.481 1.00 17.76 C ANISOU 1052 C LEU A 301 2057 2660 2029 -746 168 -224 C ATOM 1053 O LEU A 301 35.239 -14.584 1.060 1.00 19.41 O ANISOU 1053 O LEU A 301 2326 2805 2245 -760 209 -242 O ATOM 1054 CB LEU A 301 37.627 -13.915 -1.071 1.00 25.46 C ANISOU 1054 CB LEU A 301 2994 3700 2981 -762 148 -179 C ATOM 1055 CG LEU A 301 38.517 -12.669 -1.082 1.00 42.71 C ANISOU 1055 CG LEU A 301 5203 5896 5130 -822 142 -153 C ATOM 1056 CD1 LEU A 301 39.987 -13.045 -0.971 1.00 44.12 C ANISOU 1056 CD1 LEU A 301 5347 6144 5274 -855 92 -103 C ATOM 1057 CD2 LEU A 301 38.263 -11.844 -2.324 1.00 54.07 C ANISOU 1057 CD2 LEU A 301 6616 7336 6593 -784 158 -152 C ATOM 1058 N ALA A 302 35.960 -16.437 -0.014 1.00 16.86 N ANISOU 1058 N ALA A 302 1890 2577 1941 -686 148 -227 N ATOM 1059 CA ALA A 302 34.691 -17.139 0.185 1.00 17.42 C ANISOU 1059 CA ALA A 302 1966 2611 2042 -639 159 -250 C ATOM 1060 C ALA A 302 34.391 -17.296 1.671 1.00 19.62 C ANISOU 1060 C ALA A 302 2286 2856 2312 -678 163 -265 C ATOM 1061 O ALA A 302 33.240 -17.174 2.094 1.00 18.01 O ANISOU 1061 O ALA A 302 2119 2596 2127 -659 191 -279 O ATOM 1062 CB ALA A 302 34.688 -18.507 -0.516 1.00 15.90 C ANISOU 1062 CB ALA A 302 1715 2458 1868 -579 132 -251 C ATOM 1063 N CYS A 303 35.422 -17.549 2.472 1.00 17.37 N ANISOU 1063 N CYS A 303 1993 2607 2000 -736 138 -253 N ATOM 1064 CA CYS A 303 35.233 -17.628 3.925 1.00 20.92 C ANISOU 1064 CA CYS A 303 2482 3030 2435 -790 140 -265 C ATOM 1065 C CYS A 303 34.675 -16.329 4.523 1.00 23.57 C ANISOU 1065 C CYS A 303 2910 3293 2751 -837 188 -280 C ATOM 1066 O CYS A 303 33.876 -16.368 5.464 1.00 21.62 O ANISOU 1066 O CYS A 303 2708 2996 2509 -846 210 -300 O ATOM 1067 CB CYS A 303 36.540 -18.022 4.628 1.00 19.00 C ANISOU 1067 CB CYS A 303 2209 2848 2163 -862 105 -233 C ATOM 1068 SG CYS A 303 37.031 -19.723 4.291 1.00 23.41 S ANISOU 1068 SG CYS A 303 2663 3477 2756 -807 67 -213 S ATOM 1069 N LYS A 304 35.104 -15.186 3.985 1.00 25.26 N ANISOU 1069 N LYS A 304 3154 3500 2945 -865 209 -268 N ATOM 1070 CA LYS A 304 34.602 -13.878 4.426 1.00 24.04 C ANISOU 1070 CA LYS A 304 3091 3269 2774 -907 267 -280 C ATOM 1071 C LYS A 304 33.104 -13.731 4.178 1.00 26.15 C ANISOU 1071 C LYS A 304 3379 3467 3089 -836 320 -293 C ATOM 1072 O LYS A 304 32.380 -13.157 5.001 1.00 22.92 O ANISOU 1072 O LYS A 304 3048 2983 2678 -858 374 -304 O ATOM 1073 CB LYS A 304 35.342 -12.738 3.724 1.00 30.93 C ANISOU 1073 CB LYS A 304 3977 4153 3623 -940 275 -262 C ATOM 1074 CG LYS A 304 36.810 -12.612 4.079 1.00 35.94 C ANISOU 1074 CG LYS A 304 4610 4845 4201 -1025 229 -233 C ATOM 1075 CD LYS A 304 37.004 -12.310 5.552 1.00 48.72 C ANISOU 1075 CD LYS A 304 6312 6430 5768 -1130 240 -239 C ATOM 1076 CE LYS A 304 38.287 -11.523 5.775 1.00 57.87 C ANISOU 1076 CE LYS A 304 7504 7622 6861 -1235 214 -201 C ATOM 1077 NZ LYS A 304 39.372 -11.953 4.846 1.00 58.99 N ANISOU 1077 NZ LYS A 304 7552 7855 7007 -1209 154 -151 N ATOM 1078 N LEU A 305 32.634 -14.251 3.045 1.00 19.46 N ANISOU 1078 N LEU A 305 2466 2645 2284 -756 306 -282 N ATOM 1079 CA LEU A 305 31.201 -14.256 2.759 1.00 21.72 C ANISOU 1079 CA LEU A 305 2759 2878 2616 -691 347 -273 C ATOM 1080 C LEU A 305 30.423 -14.982 3.849 1.00 24.63 C ANISOU 1080 C LEU A 305 3152 3211 2994 -677 348 -284 C ATOM 1081 O LEU A 305 29.354 -14.542 4.282 1.00 23.17 O ANISOU 1081 O LEU A 305 3019 2954 2832 -659 404 -274 O ATOM 1082 CB LEU A 305 30.920 -14.942 1.419 1.00 20.49 C ANISOU 1082 CB LEU A 305 2525 2768 2493 -622 317 -255 C ATOM 1083 CG LEU A 305 31.517 -14.324 0.166 1.00 28.09 C ANISOU 1083 CG LEU A 305 3450 3768 3455 -623 314 -240 C ATOM 1084 CD1 LEU A 305 30.829 -14.920 -1.054 1.00 28.61 C ANISOU 1084 CD1 LEU A 305 3458 3857 3554 -561 301 -219 C ATOM 1085 CD2 LEU A 305 31.354 -12.821 0.187 1.00 27.09 C ANISOU 1085 CD2 LEU A 305 3373 3590 3331 -656 376 -229 C ATOM 1086 N VAL A 306 30.955 -16.118 4.271 1.00 24.18 N ANISOU 1086 N VAL A 306 3053 3208 2926 -681 289 -299 N ATOM 1087 CA VAL A 306 30.304 -16.922 5.301 1.00 21.57 C ANISOU 1087 CA VAL A 306 2732 2858 2607 -666 277 -311 C ATOM 1088 C VAL A 306 30.236 -16.139 6.611 1.00 23.82 C ANISOU 1088 C VAL A 306 3104 3081 2863 -735 322 -326 C ATOM 1089 O VAL A 306 29.256 -16.205 7.356 1.00 20.50 O ANISOU 1089 O VAL A 306 2725 2604 2461 -714 351 -328 O ATOM 1090 CB VAL A 306 31.081 -18.218 5.532 1.00 20.50 C ANISOU 1090 CB VAL A 306 2526 2798 2464 -670 209 -321 C ATOM 1091 CG1 VAL A 306 30.481 -18.991 6.683 1.00 19.66 C ANISOU 1091 CG1 VAL A 306 2422 2676 2370 -663 193 -334 C ATOM 1092 CG2 VAL A 306 31.116 -19.050 4.238 1.00 17.30 C ANISOU 1092 CG2 VAL A 306 2047 2443 2082 -602 175 -310 C ATOM 1093 N GLN A 307 31.292 -15.392 6.885 1.00 23.23 N ANISOU 1093 N GLN A 307 3066 3018 2743 -821 327 -332 N ATOM 1094 CA GLN A 307 31.353 -14.574 8.079 1.00 26.03 C ANISOU 1094 CA GLN A 307 3519 3313 3057 -905 372 -348 C ATOM 1095 C GLN A 307 30.226 -13.529 8.098 1.00 27.86 C ANISOU 1095 C GLN A 307 3835 3443 3310 -878 464 -344 C ATOM 1096 O GLN A 307 29.779 -13.105 9.163 1.00 30.55 O ANISOU 1096 O GLN A 307 4262 3712 3632 -916 516 -357 O ATOM 1097 CB GLN A 307 32.731 -13.910 8.162 1.00 26.15 C ANISOU 1097 CB GLN A 307 3557 3365 3013 -1006 355 -343 C ATOM 1098 CG GLN A 307 33.003 -13.171 9.455 1.00 42.93 C ANISOU 1098 CG GLN A 307 5791 5442 5080 -1119 390 -357 C ATOM 1099 CD GLN A 307 34.460 -12.757 9.596 1.00 53.77 C ANISOU 1099 CD GLN A 307 7173 6870 6388 -1229 352 -337 C ATOM 1100 OE1 GLN A 307 35.244 -12.857 8.649 1.00 45.78 O ANISOU 1100 OE1 GLN A 307 6092 5924 5380 -1211 310 -310 O ATOM 1101 NE2 GLN A 307 34.829 -12.291 10.786 1.00 61.08 N ANISOU 1101 NE2 GLN A 307 8189 7767 7250 -1349 367 -344 N ATOM 1102 N ALA A 308 29.764 -13.125 6.918 1.00 23.46 N ANISOU 1102 N ALA A 308 3248 2877 2791 -814 490 -319 N ATOM 1103 CA ALA A 308 28.715 -12.107 6.804 1.00 21.32 C ANISOU 1103 CA ALA A 308 3041 2512 2550 -785 586 -297 C ATOM 1104 C ALA A 308 27.298 -12.658 7.000 1.00 24.16 C ANISOU 1104 C ALA A 308 3393 2824 2961 -703 611 -270 C ATOM 1105 O ALA A 308 26.326 -11.900 6.982 1.00 24.00 O ANISOU 1105 O ALA A 308 3423 2723 2975 -673 698 -235 O ATOM 1106 CB ALA A 308 28.805 -11.408 5.454 1.00 22.32 C ANISOU 1106 CB ALA A 308 3127 2653 2700 -759 604 -269 C ATOM 1107 N LEU A 309 27.159 -13.969 7.154 1.00 19.36 N ANISOU 1107 N LEU A 309 2722 2268 2364 -665 538 -275 N ATOM 1108 CA LEU A 309 25.837 -14.505 7.470 1.00 19.80 C ANISOU 1108 CA LEU A 309 2778 2282 2464 -592 553 -244 C ATOM 1109 C LEU A 309 25.375 -13.954 8.817 1.00 25.61 C ANISOU 1109 C LEU A 309 3617 2928 3187 -624 623 -255 C ATOM 1110 O LEU A 309 26.184 -13.781 9.726 1.00 24.15 O ANISOU 1110 O LEU A 309 3482 2744 2951 -708 618 -301 O ATOM 1111 CB LEU A 309 25.850 -16.029 7.512 1.00 16.84 C ANISOU 1111 CB LEU A 309 2322 1980 2098 -553 458 -254 C ATOM 1112 CG LEU A 309 25.937 -16.730 6.156 1.00 19.88 C ANISOU 1112 CG LEU A 309 2616 2436 2503 -503 401 -235 C ATOM 1113 CD1 LEU A 309 26.342 -18.188 6.344 1.00 17.34 C ANISOU 1113 CD1 LEU A 309 2225 2188 2175 -488 312 -260 C ATOM 1114 CD2 LEU A 309 24.625 -16.617 5.397 1.00 16.82 C ANISOU 1114 CD2 LEU A 309 2217 2012 2163 -431 433 -168 C ATOM 1115 N PRO A 310 24.068 -13.685 8.945 1.00 26.38 N ANISOU 1115 N PRO A 310 3748 2946 3329 -561 692 -205 N ATOM 1116 CA PRO A 310 23.502 -13.186 10.203 1.00 22.82 C ANISOU 1116 CA PRO A 310 3401 2398 2870 -580 771 -208 C ATOM 1117 C PRO A 310 23.569 -14.261 11.281 1.00 28.33 C ANISOU 1117 C PRO A 310 4086 3127 3550 -589 702 -244 C ATOM 1118 O PRO A 310 23.656 -15.443 10.950 1.00 25.35 O ANISOU 1118 O PRO A 310 3612 2833 3187 -550 606 -246 O ATOM 1119 CB PRO A 310 22.033 -12.919 9.865 1.00 25.26 C ANISOU 1119 CB PRO A 310 3717 2634 3245 -487 845 -123 C ATOM 1120 CG PRO A 310 21.786 -13.497 8.516 1.00 29.90 C ANISOU 1120 CG PRO A 310 4195 3294 3871 -426 784 -75 C ATOM 1121 CD PRO A 310 23.042 -14.084 7.969 1.00 24.53 C ANISOU 1121 CD PRO A 310 3447 2720 3153 -469 684 -134 C ATOM 1122 N ARG A 311 23.504 -13.860 12.546 1.00 27.47 N ANISOU 1122 N ARG A 311 4075 2951 3411 -642 755 -272 N ATOM 1123 CA ARG A 311 23.582 -14.798 13.663 1.00 33.58 C ANISOU 1123 CA ARG A 311 4836 3754 4167 -662 694 -306 C ATOM 1124 C ARG A 311 22.332 -14.732 14.528 1.00 36.36 C ANISOU 1124 C ARG A 311 5252 4013 4548 -609 760 -275 C ATOM 1125 O ARG A 311 22.284 -15.312 15.608 1.00 39.01 O ANISOU 1125 O ARG A 311 5598 4354 4869 -631 729 -303 O ATOM 1126 CB ARG A 311 24.799 -14.484 14.534 1.00 33.77 C ANISOU 1126 CB ARG A 311 4917 3797 4117 -798 684 -369 C ATOM 1127 CG ARG A 311 26.036 -14.140 13.741 1.00 38.39 C ANISOU 1127 CG ARG A 311 5471 4447 4667 -861 651 -384 C ATOM 1128 CD ARG A 311 26.398 -15.282 12.822 1.00 37.92 C ANISOU 1128 CD ARG A 311 5270 4498 4637 -806 546 -375 C ATOM 1129 NE ARG A 311 27.558 -14.992 11.982 1.00 38.65 N ANISOU 1129 NE ARG A 311 5328 4654 4702 -853 515 -381 N ATOM 1130 CZ ARG A 311 28.817 -15.208 12.346 1.00 37.67 C ANISOU 1130 CZ ARG A 311 5185 4598 4530 -946 460 -403 C ATOM 1131 NH1 ARG A 311 29.094 -15.694 13.549 1.00 29.24 N ANISOU 1131 NH1 ARG A 311 4128 3546 3434 -1014 432 -423 N ATOM 1132 NH2 ARG A 311 29.802 -14.934 11.506 1.00 35.27 N ANISOU 1132 NH2 ARG A 311 4847 4349 4206 -976 434 -395 N ATOM 1133 N ASP A 312 21.325 -14.014 14.059 1.00 37.57 N ANISOU 1133 N ASP A 312 5446 4082 4746 -539 854 -210 N ATOM 1134 CA ASP A 312 20.107 -13.844 14.832 1.00 39.87 C ANISOU 1134 CA ASP A 312 5805 4275 5070 -481 933 -163 C ATOM 1135 C ASP A 312 18.940 -14.526 14.139 1.00 39.82 C ANISOU 1135 C ASP A 312 5714 4282 5135 -355 903 -72 C ATOM 1136 O ASP A 312 19.133 -15.468 13.373 1.00 34.12 O ANISOU 1136 O ASP A 312 4879 3659 4425 -323 795 -68 O ATOM 1137 CB ASP A 312 19.816 -12.357 15.053 1.00 41.88 C ANISOU 1137 CB ASP A 312 6195 4400 5318 -510 1092 -145 C ATOM 1138 CG ASP A 312 19.751 -11.570 13.754 1.00 46.15 C ANISOU 1138 CG ASP A 312 6712 4932 5892 -483 1144 -94 C ATOM 1139 OD1 ASP A 312 19.546 -12.186 12.687 1.00 39.90 O ANISOU 1139 OD1 ASP A 312 5804 4214 5140 -420 1071 -50 O ATOM 1140 OD2 ASP A 312 19.897 -10.330 13.804 1.00 47.70 O ANISOU 1140 OD2 ASP A 312 7006 5044 6073 -530 1260 -97 O ATOM 1141 N ALA A 313 17.733 -14.036 14.400 1.00 36.62 N ANISOU 1141 N ALA A 313 5366 3774 4773 -287 1003 8 N ATOM 1142 CA ALA A 313 16.522 -14.627 13.842 1.00 37.92 C ANISOU 1142 CA ALA A 313 5459 3944 5005 -171 980 117 C ATOM 1143 C ALA A 313 16.550 -14.726 12.317 1.00 32.18 C ANISOU 1143 C ALA A 313 4638 3283 4304 -145 938 167 C ATOM 1144 O ALA A 313 15.891 -15.585 11.734 1.00 31.09 O ANISOU 1144 O ALA A 313 4416 3196 4201 -75 865 235 O ATOM 1145 CB ALA A 313 15.299 -13.849 14.299 1.00 40.61 C ANISOU 1145 CB ALA A 313 5885 4153 5391 -110 1120 214 C ATOM 1146 N ARG A 314 17.310 -13.847 11.672 1.00 33.20 N ANISOU 1146 N ARG A 314 3843 3629 5142 -507 1426 63 N ATOM 1147 CA ARG A 314 17.424 -13.861 10.216 1.00 30.06 C ANISOU 1147 CA ARG A 314 3379 3265 4776 -433 1350 158 C ATOM 1148 C ARG A 314 18.087 -15.149 9.715 1.00 28.08 C ANISOU 1148 C ARG A 314 3146 3133 4391 -404 1150 150 C ATOM 1149 O ARG A 314 17.867 -15.564 8.580 1.00 30.08 O ANISOU 1149 O ARG A 314 3356 3419 4653 -345 1060 242 O ATOM 1150 CB ARG A 314 18.208 -12.641 9.723 1.00 29.18 C ANISOU 1150 CB ARG A 314 3237 3129 4720 -443 1447 131 C ATOM 1151 CG ARG A 314 17.536 -11.305 10.026 1.00 33.12 C ANISOU 1151 CG ARG A 314 3710 3500 5374 -463 1661 154 C ATOM 1152 CD ARG A 314 18.445 -10.141 9.677 1.00 32.11 C ANISOU 1152 CD ARG A 314 3564 3353 5285 -482 1757 105 C ATOM 1153 NE ARG A 314 19.616 -10.077 10.550 1.00 33.00 N ANISOU 1153 NE ARG A 314 3752 3510 5277 -564 1759 -48 N ATOM 1154 CZ ARG A 314 20.695 -9.339 10.304 1.00 37.27 C ANISOU 1154 CZ ARG A 314 4293 4069 5799 -591 1794 -111 C ATOM 1155 NH1 ARG A 314 20.766 -8.606 9.202 1.00 38.78 N ANISOU 1155 NH1 ARG A 314 4413 4237 6087 -535 1830 -40 N ATOM 1156 NH2 ARG A 314 21.712 -9.345 11.153 1.00 35.22 N ANISOU 1156 NH2 ARG A 314 4101 3859 5421 -676 1789 -240 N ATOM 1157 N LEU A 315 18.903 -15.772 10.554 1.00 26.33 N ANISOU 1157 N LEU A 315 2985 2973 4044 -449 1088 45 N ATOM 1158 CA LEU A 315 19.540 -17.025 10.162 1.00 23.54 C ANISOU 1158 CA LEU A 315 2649 2723 3571 -420 915 40 C ATOM 1159 C LEU A 315 18.507 -18.154 10.109 1.00 22.78 C ANISOU 1159 C LEU A 315 2557 2635 3463 -383 824 113 C ATOM 1160 O LEU A 315 18.604 -19.043 9.269 1.00 24.10 O ANISOU 1160 O LEU A 315 2718 2859 3582 -337 700 160 O ATOM 1161 CB LEU A 315 20.713 -17.374 11.079 1.00 24.67 C ANISOU 1161 CB LEU A 315 2845 2936 3592 -480 877 -74 C ATOM 1162 CG LEU A 315 21.506 -18.629 10.686 1.00 24.75 C ANISOU 1162 CG LEU A 315 2869 3048 3489 -448 713 -76 C ATOM 1163 CD1 LEU A 315 21.979 -18.519 9.238 1.00 24.86 C ANISOU 1163 CD1 LEU A 315 2843 3083 3518 -386 663 -24 C ATOM 1164 CD2 LEU A 315 22.679 -18.839 11.624 1.00 23.85 C ANISOU 1164 CD2 LEU A 315 2791 3003 3267 -512 691 -171 C ATOM 1165 N ILE A 316 17.508 -18.110 10.993 1.00 22.30 N ANISOU 1165 N ILE A 316 2511 2515 3448 -406 892 121 N ATOM 1166 CA ILE A 316 16.399 -19.062 10.916 1.00 23.26 C ANISOU 1166 CA ILE A 316 2630 2634 3573 -370 819 203 C ATOM 1167 C ILE A 316 15.652 -18.878 9.599 1.00 24.32 C ANISOU 1167 C ILE A 316 2701 2748 3792 -314 805 336 C ATOM 1168 O ILE A 316 15.377 -19.842 8.889 1.00 27.07 O ANISOU 1168 O ILE A 316 3045 3146 4095 -279 684 399 O ATOM 1169 CB ILE A 316 15.387 -18.882 12.072 1.00 29.21 C ANISOU 1169 CB ILE A 316 3403 3315 4379 -404 913 198 C ATOM 1170 CG1 ILE A 316 16.051 -19.109 13.426 1.00 31.23 C ANISOU 1170 CG1 ILE A 316 3721 3601 4543 -474 923 71 C ATOM 1171 CG2 ILE A 316 14.223 -19.848 11.912 1.00 27.22 C ANISOU 1171 CG2 ILE A 316 3145 3064 4135 -363 833 293 C ATOM 1172 CD1 ILE A 316 15.088 -18.992 14.600 1.00 36.82 C ANISOU 1172 CD1 ILE A 316 4456 4240 5292 -514 1014 57 C ATOM 1173 N ALA A 317 15.319 -17.627 9.287 1.00 24.84 N ANISOU 1173 N ALA A 317 2716 2740 3980 -312 937 383 N ATOM 1174 CA ALA A 317 14.650 -17.278 8.035 1.00 27.06 C ANISOU 1174 CA ALA A 317 2922 3005 4353 -267 939 523 C ATOM 1175 C ALA A 317 15.405 -17.815 6.820 1.00 24.70 C ANISOU 1175 C ALA A 317 2612 2794 3978 -239 808 539 C ATOM 1176 O ALA A 317 14.811 -18.323 5.873 1.00 24.81 O ANISOU 1176 O ALA A 317 2593 2839 3995 -212 728 646 O ATOM 1177 CB ALA A 317 14.497 -15.762 7.926 1.00 32.62 C ANISOU 1177 CB ALA A 317 3573 3623 5199 -272 1111 553 C ATOM 1178 N ILE A 318 16.723 -17.706 6.856 1.00 20.46 N ANISOU 1178 N ILE A 318 2105 2300 3370 -252 788 434 N ATOM 1179 CA ILE A 318 17.541 -18.224 5.768 1.00 20.89 C ANISOU 1179 CA ILE A 318 2156 2432 3349 -226 673 439 C ATOM 1180 C ILE A 318 17.431 -19.754 5.677 1.00 19.30 C ANISOU 1180 C ILE A 318 2000 2295 3038 -215 527 444 C ATOM 1181 O ILE A 318 17.181 -20.303 4.611 1.00 23.41 O ANISOU 1181 O ILE A 318 2505 2853 3538 -192 444 519 O ATOM 1182 CB ILE A 318 18.996 -17.754 5.899 1.00 19.36 C ANISOU 1182 CB ILE A 318 1982 2267 3107 -243 690 331 C ATOM 1183 CG1 ILE A 318 19.098 -16.276 5.510 1.00 21.22 C ANISOU 1183 CG1 ILE A 318 2161 2447 3455 -244 818 351 C ATOM 1184 CG2 ILE A 318 19.917 -18.572 4.998 1.00 22.18 C ANISOU 1184 CG2 ILE A 318 2355 2707 3365 -216 561 320 C ATOM 1185 CD1 ILE A 318 20.466 -15.682 5.758 1.00 19.24 C ANISOU 1185 CD1 ILE A 318 1931 2217 3163 -268 851 244 C ATOM 1186 N CYS A 319 17.574 -20.432 6.808 1.00 22.52 N ANISOU 1186 N CYS A 319 2465 2714 3378 -236 503 366 N ATOM 1187 CA CYS A 319 17.486 -21.894 6.828 1.00 21.31 C ANISOU 1187 CA CYS A 319 2355 2615 3126 -224 376 366 C ATOM 1188 C CYS A 319 16.162 -22.465 6.326 1.00 24.65 C ANISOU 1188 C CYS A 319 2762 3027 3577 -207 331 479 C ATOM 1189 O CYS A 319 16.138 -23.547 5.737 1.00 29.96 O ANISOU 1189 O CYS A 319 3458 3748 4175 -194 223 504 O ATOM 1190 CB CYS A 319 17.775 -22.423 8.226 1.00 21.63 C ANISOU 1190 CB CYS A 319 2448 2668 3104 -253 371 274 C ATOM 1191 SG CYS A 319 19.505 -22.277 8.659 1.00 30.54 S ANISOU 1191 SG CYS A 319 3602 3852 4152 -279 367 156 S ATOM 1192 N VAL A 320 15.064 -21.746 6.543 1.00 20.21 N ANISOU 1192 N VAL A 320 2159 2399 3121 -212 418 552 N ATOM 1193 CA VAL A 320 13.760 -22.279 6.168 1.00 20.59 C ANISOU 1193 CA VAL A 320 2188 2440 3196 -202 376 670 C ATOM 1194 C VAL A 320 13.247 -21.705 4.865 1.00 21.77 C ANISOU 1194 C VAL A 320 2265 2589 3418 -192 387 800 C ATOM 1195 O VAL A 320 12.135 -22.011 4.441 1.00 22.49 O ANISOU 1195 O VAL A 320 2327 2680 3538 -192 357 920 O ATOM 1196 CB VAL A 320 12.709 -22.093 7.286 1.00 26.17 C ANISOU 1196 CB VAL A 320 2894 3080 3968 -212 452 690 C ATOM 1197 CG1 VAL A 320 13.245 -22.657 8.594 1.00 25.95 C ANISOU 1197 CG1 VAL A 320 2934 3063 3862 -232 438 563 C ATOM 1198 CG2 VAL A 320 12.325 -20.610 7.433 1.00 22.10 C ANISOU 1198 CG2 VAL A 320 2321 2481 3595 -216 611 731 C ATOM 1199 N ASP A 321 14.068 -20.888 4.216 1.00 22.52 N ANISOU 1199 N ASP A 321 2328 2690 3537 -187 425 782 N ATOM 1200 CA ASP A 321 13.666 -20.265 2.961 1.00 22.17 C ANISOU 1200 CA ASP A 321 2207 2652 3565 -181 438 907 C ATOM 1201 C ASP A 321 13.838 -21.208 1.772 1.00 26.13 C ANISOU 1201 C ASP A 321 2723 3236 3970 -187 304 947 C ATOM 1202 O ASP A 321 14.837 -21.916 1.655 1.00 21.33 O ANISOU 1202 O ASP A 321 2175 2674 3256 -184 231 852 O ATOM 1203 CB ASP A 321 14.455 -18.976 2.716 1.00 21.54 C ANISOU 1203 CB ASP A 321 2084 2545 3556 -174 537 875 C ATOM 1204 CG ASP A 321 13.909 -18.182 1.554 1.00 27.53 C ANISOU 1204 CG ASP A 321 2746 3300 4413 -168 572 1019 C ATOM 1205 OD1 ASP A 321 12.787 -17.650 1.690 1.00 30.16 O ANISOU 1205 OD1 ASP A 321 3018 3580 4860 -168 651 1133 O ATOM 1206 OD2 ASP A 321 14.588 -18.098 0.505 1.00 25.91 O ANISOU 1206 OD2 ASP A 321 2521 3147 4175 -166 523 1027 O ATOM 1207 N GLN A 322 12.845 -21.197 0.894 1.00 19.44 N ANISOU 1207 N GLN A 322 1819 2404 3164 -200 281 1095 N ATOM 1208 CA GLN A 322 12.826 -21.994 -0.324 1.00 24.93 C ANISOU 1208 CA GLN A 322 2522 3176 3773 -223 167 1153 C ATOM 1209 C GLN A 322 14.059 -21.770 -1.222 1.00 22.15 C ANISOU 1209 C GLN A 322 2174 2866 3376 -220 143 1095 C ATOM 1210 O GLN A 322 14.527 -22.703 -1.881 1.00 27.18 O ANISOU 1210 O GLN A 322 2865 3561 3902 -236 47 1065 O ATOM 1211 CB GLN A 322 11.549 -21.652 -1.089 1.00 32.96 C ANISOU 1211 CB GLN A 322 3453 4203 4867 -249 173 1340 C ATOM 1212 CG GLN A 322 11.362 -22.349 -2.411 1.00 47.13 C ANISOU 1212 CG GLN A 322 5247 6082 6578 -294 63 1422 C ATOM 1213 CD GLN A 322 10.214 -21.738 -3.213 1.00 58.28 C ANISOU 1213 CD GLN A 322 6550 7512 8081 -326 83 1624 C ATOM 1214 OE1 GLN A 322 9.796 -20.599 -2.967 1.00 51.97 O ANISOU 1214 OE1 GLN A 322 5664 6658 7423 -303 193 1699 O ATOM 1215 NE2 GLN A 322 9.702 -22.495 -4.177 1.00 61.98 N ANISOU 1215 NE2 GLN A 322 7023 8058 8470 -385 -17 1717 N ATOM 1216 N ASN A 323 14.574 -20.543 -1.244 1.00 24.49 N ANISOU 1216 N ASN A 323 2417 3130 3759 -200 236 1081 N ATOM 1217 CA ASN A 323 15.799 -20.221 -1.992 1.00 22.71 C ANISOU 1217 CA ASN A 323 2192 2938 3499 -191 223 1021 C ATOM 1218 C ASN A 323 17.042 -20.289 -1.134 1.00 21.96 C ANISOU 1218 C ASN A 323 2162 2829 3353 -169 239 860 C ATOM 1219 O ASN A 323 18.025 -20.948 -1.492 1.00 18.53 O ANISOU 1219 O ASN A 323 1782 2440 2820 -164 169 786 O ATOM 1220 CB ASN A 323 15.727 -18.808 -2.578 1.00 20.93 C ANISOU 1220 CB ASN A 323 1865 2690 3399 -184 315 1101 C ATOM 1221 CG ASN A 323 14.455 -18.566 -3.345 1.00 31.34 C ANISOU 1221 CG ASN A 323 3097 4021 4790 -209 316 1283 C ATOM 1222 OD1 ASN A 323 14.040 -19.401 -4.137 1.00 29.73 O ANISOU 1222 OD1 ASN A 323 2905 3881 4511 -244 217 1352 O ATOM 1223 ND2 ASN A 323 13.817 -17.423 -3.100 1.00 38.31 N ANISOU 1223 ND2 ASN A 323 3892 4843 5820 -196 435 1370 N ATOM 1224 N ALA A 324 17.002 -19.590 -0.003 1.00 17.94 N ANISOU 1224 N ALA A 324 1647 2259 2912 -160 337 811 N ATOM 1225 CA ALA A 324 18.204 -19.386 0.801 1.00 21.12 C ANISOU 1225 CA ALA A 324 2094 2652 3277 -152 369 671 C ATOM 1226 C ALA A 324 18.751 -20.649 1.450 1.00 19.99 C ANISOU 1226 C ALA A 324 2039 2546 3012 -154 284 577 C ATOM 1227 O ALA A 324 19.932 -20.713 1.764 1.00 17.67 O ANISOU 1227 O ALA A 324 1780 2274 2662 -149 275 479 O ATOM 1228 CB ALA A 324 17.958 -18.316 1.862 1.00 16.43 C ANISOU 1228 CB ALA A 324 1477 1983 2781 -160 504 643 C ATOM 1229 N ASN A 325 17.913 -21.654 1.669 1.00 18.98 N ANISOU 1229 N ASN A 325 1941 2425 2844 -161 223 613 N ATOM 1230 CA ASN A 325 18.426 -22.871 2.293 1.00 20.87 C ANISOU 1230 CA ASN A 325 2256 2697 2975 -160 148 530 C ATOM 1231 C ASN A 325 19.574 -23.447 1.466 1.00 16.74 C ANISOU 1231 C ASN A 325 1766 2229 2367 -147 77 488 C ATOM 1232 O ASN A 325 20.491 -24.052 2.005 1.00 16.41 O ANISOU 1232 O ASN A 325 1772 2210 2254 -140 48 404 O ATOM 1233 CB ASN A 325 17.326 -23.921 2.507 1.00 17.21 C ANISOU 1233 CB ASN A 325 1821 2236 2481 -169 88 582 C ATOM 1234 CG ASN A 325 16.925 -24.622 1.220 1.00 21.20 C ANISOU 1234 CG ASN A 325 2331 2783 2943 -177 5 662 C ATOM 1235 OD1 ASN A 325 15.999 -24.198 0.521 1.00 22.01 O ANISOU 1235 OD1 ASN A 325 2380 2880 3103 -192 16 775 O ATOM 1236 ND2 ASN A 325 17.624 -25.693 0.897 1.00 13.99 N ANISOU 1236 ND2 ASN A 325 1478 1911 1927 -174 -72 611 N ATOM 1237 N HIS A 326 19.525 -23.238 0.153 1.00 14.34 N ANISOU 1237 N HIS A 326 1431 1944 2072 -148 55 555 N ATOM 1238 CA HIS A 326 20.575 -23.742 -0.738 1.00 15.92 C ANISOU 1238 CA HIS A 326 1664 2189 2197 -138 -2 520 C ATOM 1239 C HIS A 326 21.905 -23.019 -0.548 1.00 18.07 C ANISOU 1239 C HIS A 326 1927 2463 2474 -118 40 441 C ATOM 1240 O HIS A 326 22.967 -23.558 -0.851 1.00 15.00 O ANISOU 1240 O HIS A 326 1576 2107 2017 -103 0 390 O ATOM 1241 CB HIS A 326 20.126 -23.653 -2.197 1.00 14.94 C ANISOU 1241 CB HIS A 326 1508 2091 2079 -156 -33 615 C ATOM 1242 CG HIS A 326 18.926 -24.497 -2.495 1.00 16.28 C ANISOU 1242 CG HIS A 326 1694 2272 2219 -187 -89 695 C ATOM 1243 ND1 HIS A 326 19.002 -25.866 -2.645 1.00 17.45 N ANISOU 1243 ND1 HIS A 326 1919 2446 2266 -199 -164 668 N ATOM 1244 CD2 HIS A 326 17.620 -24.171 -2.643 1.00 19.49 C ANISOU 1244 CD2 HIS A 326 2050 2669 2688 -212 -76 806 C ATOM 1245 CE1 HIS A 326 17.793 -26.345 -2.884 1.00 17.94 C ANISOU 1245 CE1 HIS A 326 1981 2516 2320 -234 -200 753 C ATOM 1246 NE2 HIS A 326 16.938 -25.339 -2.887 1.00 18.63 N ANISOU 1246 NE2 HIS A 326 1988 2585 2504 -243 -151 842 N ATOM 1247 N VAL A 327 21.849 -21.789 -0.058 1.00 15.18 N ANISOU 1247 N VAL A 327 1512 2063 2195 -120 128 436 N ATOM 1248 CA VAL A 327 23.082 -21.097 0.290 1.00 14.59 C ANISOU 1248 CA VAL A 327 1434 1991 2120 -111 172 356 C ATOM 1249 C VAL A 327 23.763 -21.793 1.469 1.00 13.89 C ANISOU 1249 C VAL A 327 1401 1919 1959 -117 152 267 C ATOM 1250 O VAL A 327 24.975 -22.029 1.441 1.00 15.55 O ANISOU 1250 O VAL A 327 1632 2164 2111 -105 126 212 O ATOM 1251 CB VAL A 327 22.835 -19.608 0.610 1.00 14.72 C ANISOU 1251 CB VAL A 327 1390 1958 2244 -121 285 365 C ATOM 1252 CG1 VAL A 327 24.086 -18.981 1.263 1.00 14.77 C ANISOU 1252 CG1 VAL A 327 1407 1969 2236 -128 332 268 C ATOM 1253 CG2 VAL A 327 22.448 -18.854 -0.671 1.00 14.81 C ANISOU 1253 CG2 VAL A 327 1333 1964 2329 -111 304 458 C ATOM 1254 N ILE A 328 22.999 -22.106 2.512 1.00 13.95 N ANISOU 1254 N ILE A 328 1425 1904 1970 -136 165 259 N ATOM 1255 CA ILE A 328 23.578 -22.834 3.650 1.00 14.99 C ANISOU 1255 CA ILE A 328 1603 2060 2031 -147 140 186 C ATOM 1256 C ILE A 328 24.128 -24.200 3.222 1.00 14.64 C ANISOU 1256 C ILE A 328 1604 2063 1898 -123 45 181 C ATOM 1257 O ILE A 328 25.211 -24.599 3.650 1.00 14.60 O ANISOU 1257 O ILE A 328 1619 2093 1835 -119 24 129 O ATOM 1258 CB ILE A 328 22.591 -23.003 4.822 1.00 17.49 C ANISOU 1258 CB ILE A 328 1931 2347 2366 -173 166 182 C ATOM 1259 CG1 ILE A 328 22.082 -21.640 5.290 1.00 15.02 C ANISOU 1259 CG1 ILE A 328 1581 1977 2150 -200 281 183 C ATOM 1260 CG2 ILE A 328 23.264 -23.717 5.994 1.00 14.47 C ANISOU 1260 CG2 ILE A 328 1588 2001 1908 -193 138 110 C ATOM 1261 CD1 ILE A 328 23.186 -20.621 5.472 1.00 15.30 C ANISOU 1261 CD1 ILE A 328 1603 2018 2194 -219 345 119 C ATOM 1262 N GLN A 329 23.385 -24.913 2.375 1.00 14.70 N ANISOU 1262 N GLN A 329 1624 2068 1893 -111 -7 241 N ATOM 1263 CA GLN A 329 23.856 -26.202 1.854 1.00 15.53 C ANISOU 1263 CA GLN A 329 1779 2205 1918 -92 -82 237 C ATOM 1264 C GLN A 329 25.139 -26.052 1.036 1.00 15.87 C ANISOU 1264 C GLN A 329 1822 2272 1935 -70 -88 215 C ATOM 1265 O GLN A 329 26.023 -26.902 1.088 1.00 14.32 O ANISOU 1265 O GLN A 329 1661 2100 1679 -52 -120 184 O ATOM 1266 CB GLN A 329 22.766 -26.891 1.010 1.00 13.28 C ANISOU 1266 CB GLN A 329 1512 1913 1622 -100 -128 307 C ATOM 1267 CG GLN A 329 21.515 -27.232 1.814 1.00 15.66 C ANISOU 1267 CG GLN A 329 1818 2193 1940 -117 -132 335 C ATOM 1268 CD GLN A 329 20.622 -28.225 1.108 1.00 20.76 C ANISOU 1268 CD GLN A 329 2497 2845 2548 -129 -193 394 C ATOM 1269 OE1 GLN A 329 20.935 -29.407 1.034 1.00 20.17 O ANISOU 1269 OE1 GLN A 329 2477 2786 2401 -123 -241 370 O ATOM 1270 NE2 GLN A 329 19.493 -27.753 0.603 1.00 17.95 N ANISOU 1270 NE2 GLN A 329 2105 2475 2240 -152 -185 477 N ATOM 1271 N LYS A 330 25.252 -24.972 0.279 1.00 14.27 N ANISOU 1271 N LYS A 330 1576 2062 1783 -70 -52 236 N ATOM 1272 CA LYS A 330 26.491 -24.742 -0.470 1.00 14.52 C ANISOU 1272 CA LYS A 330 1606 2117 1795 -48 -55 215 C ATOM 1273 C LYS A 330 27.668 -24.464 0.482 1.00 15.04 C ANISOU 1273 C LYS A 330 1668 2202 1844 -43 -31 149 C ATOM 1274 O LYS A 330 28.771 -24.996 0.309 1.00 17.68 O ANISOU 1274 O LYS A 330 2025 2564 2129 -21 -56 126 O ATOM 1275 CB LYS A 330 26.305 -23.600 -1.478 1.00 13.45 C ANISOU 1275 CB LYS A 330 1417 1970 1722 -50 -22 257 C ATOM 1276 CG LYS A 330 27.535 -23.316 -2.358 1.00 18.49 C ANISOU 1276 CG LYS A 330 2051 2633 2344 -26 -26 239 C ATOM 1277 CD LYS A 330 27.844 -24.502 -3.273 1.00 20.63 C ANISOU 1277 CD LYS A 330 2376 2921 2542 -15 -86 249 C ATOM 1278 CE LYS A 330 26.858 -24.630 -4.422 1.00 22.29 C ANISOU 1278 CE LYS A 330 2583 3131 2757 -40 -110 319 C ATOM 1279 NZ LYS A 330 27.272 -25.732 -5.369 1.00 21.84 N ANISOU 1279 NZ LYS A 330 2588 3088 2621 -41 -155 317 N ATOM 1280 N VAL A 331 27.425 -23.646 1.498 1.00 13.39 N ANISOU 1280 N VAL A 331 1433 1979 1676 -70 23 124 N ATOM 1281 CA VAL A 331 28.455 -23.331 2.480 1.00 13.47 C ANISOU 1281 CA VAL A 331 1440 2015 1662 -86 47 65 C ATOM 1282 C VAL A 331 28.997 -24.625 3.066 1.00 13.38 C ANISOU 1282 C VAL A 331 1467 2042 1576 -78 -8 49 C ATOM 1283 O VAL A 331 30.197 -24.849 3.094 1.00 16.27 O ANISOU 1283 O VAL A 331 1835 2445 1901 -66 -23 33 O ATOM 1284 CB VAL A 331 27.923 -22.429 3.617 1.00 15.87 C ANISOU 1284 CB VAL A 331 1725 2294 2009 -134 118 35 C ATOM 1285 CG1 VAL A 331 28.922 -22.371 4.797 1.00 14.08 C ANISOU 1285 CG1 VAL A 331 1506 2110 1733 -171 131 -25 C ATOM 1286 CG2 VAL A 331 27.622 -21.028 3.098 1.00 13.88 C ANISOU 1286 CG2 VAL A 331 1429 2002 1843 -139 193 49 C ATOM 1287 N VAL A 332 28.090 -25.485 3.515 1.00 13.32 N ANISOU 1287 N VAL A 332 1485 2023 1554 -84 -36 63 N ATOM 1288 CA VAL A 332 28.462 -26.773 4.084 1.00 13.47 C ANISOU 1288 CA VAL A 332 1535 2073 1511 -74 -84 57 C ATOM 1289 C VAL A 332 29.289 -27.628 3.107 1.00 14.48 C ANISOU 1289 C VAL A 332 1688 2215 1600 -30 -123 76 C ATOM 1290 O VAL A 332 30.193 -28.351 3.516 1.00 13.88 O ANISOU 1290 O VAL A 332 1619 2171 1483 -16 -141 70 O ATOM 1291 CB VAL A 332 27.188 -27.533 4.544 1.00 13.34 C ANISOU 1291 CB VAL A 332 1543 2034 1493 -83 -108 75 C ATOM 1292 CG1 VAL A 332 27.515 -28.954 4.977 1.00 16.95 C ANISOU 1292 CG1 VAL A 332 2030 2517 1892 -66 -157 77 C ATOM 1293 CG2 VAL A 332 26.534 -26.755 5.681 1.00 16.59 C ANISOU 1293 CG2 VAL A 332 1933 2431 1938 -128 -61 52 C ATOM 1294 N ALA A 333 28.975 -27.538 1.823 1.00 15.70 N ANISOU 1294 N ALA A 333 1852 2344 1770 -11 -129 103 N ATOM 1295 CA ALA A 333 29.655 -28.332 0.802 1.00 14.94 C ANISOU 1295 CA ALA A 333 1788 2250 1638 23 -154 118 C ATOM 1296 C ALA A 333 31.085 -27.867 0.487 1.00 17.67 C ANISOU 1296 C ALA A 333 2114 2620 1979 46 -137 104 C ATOM 1297 O ALA A 333 31.982 -28.688 0.330 1.00 18.36 O ANISOU 1297 O ALA A 333 2223 2719 2033 75 -149 109 O ATOM 1298 CB ALA A 333 28.815 -28.369 -0.477 1.00 16.99 C ANISOU 1298 CB ALA A 333 2066 2483 1906 19 -167 153 C ATOM 1299 N VAL A 334 31.307 -26.560 0.402 1.00 14.84 N ANISOU 1299 N VAL A 334 1713 2266 1660 34 -104 92 N ATOM 1300 CA VAL A 334 32.576 -26.055 -0.148 1.00 20.09 C ANISOU 1300 CA VAL A 334 2359 2950 2323 57 -92 86 C ATOM 1301 C VAL A 334 33.456 -25.200 0.776 1.00 18.80 C ANISOU 1301 C VAL A 334 2157 2822 2165 37 -64 57 C ATOM 1302 O VAL A 334 34.502 -24.703 0.345 1.00 19.33 O ANISOU 1302 O VAL A 334 2205 2908 2232 54 -54 55 O ATOM 1303 CB VAL A 334 32.333 -25.270 -1.458 1.00 18.06 C ANISOU 1303 CB VAL A 334 2087 2672 2103 65 -80 104 C ATOM 1304 CG1 VAL A 334 31.513 -26.122 -2.438 1.00 23.91 C ANISOU 1304 CG1 VAL A 334 2870 3388 2826 68 -110 136 C ATOM 1305 CG2 VAL A 334 31.611 -23.961 -1.176 1.00 14.24 C ANISOU 1305 CG2 VAL A 334 1556 2173 1680 34 -39 100 C ATOM 1306 N ILE A 335 33.051 -25.030 2.031 1.00 15.48 N ANISOU 1306 N ILE A 335 1726 2412 1743 -6 -51 35 N ATOM 1307 CA ILE A 335 33.815 -24.214 2.984 1.00 13.63 C ANISOU 1307 CA ILE A 335 1460 2216 1501 -47 -20 4 C ATOM 1308 C ILE A 335 34.212 -25.083 4.172 1.00 15.17 C ANISOU 1308 C ILE A 335 1661 2459 1644 -70 -46 5 C ATOM 1309 O ILE A 335 33.401 -25.876 4.634 1.00 16.48 O ANISOU 1309 O ILE A 335 1848 2613 1800 -74 -66 11 O ATOM 1310 CB ILE A 335 32.963 -23.038 3.500 1.00 13.91 C ANISOU 1310 CB ILE A 335 1478 2224 1585 -97 36 -27 C ATOM 1311 CG1 ILE A 335 32.403 -22.207 2.334 1.00 14.77 C ANISOU 1311 CG1 ILE A 335 1569 2285 1758 -73 65 -11 C ATOM 1312 CG2 ILE A 335 33.762 -22.146 4.479 1.00 14.02 C ANISOU 1312 CG2 ILE A 335 1469 2276 1583 -156 78 -68 C ATOM 1313 CD1 ILE A 335 33.485 -21.438 1.555 1.00 14.49 C ANISOU 1313 CD1 ILE A 335 1508 2264 1732 -52 78 -13 C ATOM 1314 N PRO A 336 35.453 -24.938 4.677 1.00 17.88 N ANISOU 1314 N PRO A 336 1981 2860 1952 -89 -47 6 N ATOM 1315 CA PRO A 336 35.859 -25.735 5.843 1.00 14.77 C ANISOU 1315 CA PRO A 336 1579 2523 1508 -119 -72 21 C ATOM 1316 C PRO A 336 35.009 -25.454 7.079 1.00 17.22 C ANISOU 1316 C PRO A 336 1891 2840 1811 -192 -53 -16 C ATOM 1317 O PRO A 336 34.588 -24.328 7.312 1.00 14.76 O ANISOU 1317 O PRO A 336 1576 2508 1526 -238 -5 -59 O ATOM 1318 CB PRO A 336 37.311 -25.296 6.092 1.00 19.14 C ANISOU 1318 CB PRO A 336 2097 3143 2031 -141 -69 36 C ATOM 1319 CG PRO A 336 37.791 -24.816 4.737 1.00 18.86 C ANISOU 1319 CG PRO A 336 2062 3077 2028 -84 -59 43 C ATOM 1320 CD PRO A 336 36.577 -24.158 4.120 1.00 17.23 C ANISOU 1320 CD PRO A 336 1874 2800 1873 -78 -32 8 C ATOM 1321 N LEU A 337 34.793 -26.495 7.872 1.00 15.97 N ANISOU 1321 N LEU A 337 1737 2708 1621 -201 -86 4 N ATOM 1322 CA LEU A 337 33.895 -26.447 9.020 1.00 14.55 C ANISOU 1322 CA LEU A 337 1565 2532 1434 -264 -75 -27 C ATOM 1323 C LEU A 337 34.156 -25.281 9.971 1.00 15.81 C ANISOU 1323 C LEU A 337 1707 2725 1575 -360 -27 -74 C ATOM 1324 O LEU A 337 33.220 -24.670 10.489 1.00 22.30 O ANISOU 1324 O LEU A 337 2544 3510 2418 -407 18 -119 O ATOM 1325 CB LEU A 337 33.961 -27.772 9.786 1.00 15.32 C ANISOU 1325 CB LEU A 337 1657 2673 1491 -262 -123 10 C ATOM 1326 CG LEU A 337 33.294 -27.754 11.171 1.00 16.59 C ANISOU 1326 CG LEU A 337 1817 2859 1628 -340 -116 -19 C ATOM 1327 CD1 LEU A 337 31.798 -27.441 11.054 1.00 14.58 C ANISOU 1327 CD1 LEU A 337 1596 2524 1420 -336 -89 -54 C ATOM 1328 CD2 LEU A 337 33.519 -29.080 11.888 1.00 15.95 C ANISOU 1328 CD2 LEU A 337 1719 2832 1508 -336 -167 29 C ATOM 1329 N LYS A 338 35.421 -24.956 10.200 1.00 16.78 N ANISOU 1329 N LYS A 338 1802 2917 1658 -394 -29 -63 N ATOM 1330 CA LYS A 338 35.744 -23.930 11.198 1.00 16.80 C ANISOU 1330 CA LYS A 338 1794 2962 1626 -505 17 -109 C ATOM 1331 C LYS A 338 34.974 -22.639 10.921 1.00 21.84 C ANISOU 1331 C LYS A 338 2454 3524 2322 -526 95 -172 C ATOM 1332 O LYS A 338 34.508 -21.969 11.839 1.00 19.96 O ANISOU 1332 O LYS A 338 2228 3279 2075 -614 151 -225 O ATOM 1333 CB LYS A 338 37.249 -23.647 11.230 1.00 19.58 C ANISOU 1333 CB LYS A 338 2111 3397 1932 -534 4 -81 C ATOM 1334 CG LYS A 338 37.655 -22.576 12.246 1.00 22.90 C ANISOU 1334 CG LYS A 338 2526 3870 2304 -665 52 -129 C ATOM 1335 CD LYS A 338 37.048 -22.843 13.631 1.00 20.41 C ANISOU 1335 CD LYS A 338 2222 3590 1945 -761 58 -155 C ATOM 1336 CE LYS A 338 37.494 -21.794 14.658 1.00 24.52 C ANISOU 1336 CE LYS A 338 2745 4167 2404 -910 113 -208 C ATOM 1337 NZ LYS A 338 36.803 -21.990 15.966 1.00 18.97 N ANISOU 1337 NZ LYS A 338 2060 3489 1660 -1009 128 -242 N ATOM 1338 N ASN A 339 34.815 -22.317 9.644 1.00 17.88 N ANISOU 1338 N ASN A 339 1954 2961 1880 -447 104 -162 N ATOM 1339 CA ASN A 339 34.104 -21.107 9.240 1.00 16.61 C ANISOU 1339 CA ASN A 339 1801 2725 1787 -455 181 -203 C ATOM 1340 C ASN A 339 32.604 -21.125 9.501 1.00 20.42 C ANISOU 1340 C ASN A 339 2304 3136 2319 -457 215 -218 C ATOM 1341 O ASN A 339 32.003 -20.077 9.713 1.00 19.97 O ANISOU 1341 O ASN A 339 2250 3025 2310 -497 300 -256 O ATOM 1342 CB ASN A 339 34.337 -20.845 7.756 1.00 17.75 C ANISOU 1342 CB ASN A 339 1932 2833 1981 -370 173 -175 C ATOM 1343 CG ASN A 339 35.789 -20.648 7.432 1.00 20.81 C ANISOU 1343 CG ASN A 339 2297 3278 2330 -365 152 -162 C ATOM 1344 OD1 ASN A 339 36.343 -19.576 7.649 1.00 19.80 O ANISOU 1344 OD1 ASN A 339 2158 3166 2201 -418 202 -196 O ATOM 1345 ND2 ASN A 339 36.427 -21.693 6.913 1.00 23.20 N ANISOU 1345 ND2 ASN A 339 2596 3614 2605 -302 83 -109 N ATOM 1346 N TRP A 340 31.985 -22.301 9.456 1.00 16.19 N ANISOU 1346 N TRP A 340 1780 2595 1775 -411 156 -182 N ATOM 1347 CA TRP A 340 30.543 -22.367 9.672 1.00 18.22 C ANISOU 1347 CA TRP A 340 2055 2787 2080 -409 182 -185 C ATOM 1348 C TRP A 340 30.132 -23.145 10.914 1.00 21.54 C ANISOU 1348 C TRP A 340 2491 3237 2454 -456 159 -196 C ATOM 1349 O TRP A 340 28.955 -23.456 11.102 1.00 16.06 O ANISOU 1349 O TRP A 340 1814 2497 1792 -445 164 -188 O ATOM 1350 CB TRP A 340 29.802 -22.876 8.430 1.00 19.09 C ANISOU 1350 CB TRP A 340 2169 2847 2238 -321 146 -134 C ATOM 1351 CG TRP A 340 30.303 -24.155 7.862 1.00 15.55 C ANISOU 1351 CG TRP A 340 1729 2434 1745 -262 60 -92 C ATOM 1352 CD1 TRP A 340 31.275 -24.307 6.913 1.00 15.27 C ANISOU 1352 CD1 TRP A 340 1686 2420 1697 -215 31 -70 C ATOM 1353 CD2 TRP A 340 29.819 -25.470 8.156 1.00 14.45 C ANISOU 1353 CD2 TRP A 340 1611 2304 1577 -240 2 -67 C ATOM 1354 NE1 TRP A 340 31.436 -25.634 6.612 1.00 14.84 N ANISOU 1354 NE1 TRP A 340 1648 2382 1608 -168 -33 -34 N ATOM 1355 CE2 TRP A 340 30.558 -26.372 7.364 1.00 13.94 C ANISOU 1355 CE2 TRP A 340 1552 2261 1483 -183 -52 -32 C ATOM 1356 CE3 TRP A 340 28.838 -25.972 9.018 1.00 17.68 C ANISOU 1356 CE3 TRP A 340 2036 2701 1982 -264 -4 -71 C ATOM 1357 CZ2 TRP A 340 30.349 -27.746 7.406 1.00 15.11 C ANISOU 1357 CZ2 TRP A 340 1722 2418 1602 -150 -105 -2 C ATOM 1358 CZ3 TRP A 340 28.627 -27.338 9.060 1.00 14.60 C ANISOU 1358 CZ3 TRP A 340 1664 2325 1560 -229 -68 -40 C ATOM 1359 CH2 TRP A 340 29.382 -28.213 8.255 1.00 19.43 C ANISOU 1359 CH2 TRP A 340 2281 2955 2145 -173 -115 -7 C ATOM 1360 N GLU A 341 31.098 -23.439 11.778 1.00 20.87 N ANISOU 1360 N GLU A 341 2398 3236 2295 -511 134 -207 N ATOM 1361 CA GLU A 341 30.785 -24.124 13.021 1.00 22.65 C ANISOU 1361 CA GLU A 341 2631 3501 2472 -566 112 -215 C ATOM 1362 C GLU A 341 29.717 -23.357 13.801 1.00 21.02 C ANISOU 1362 C GLU A 341 2449 3239 2299 -632 193 -266 C ATOM 1363 O GLU A 341 28.906 -23.950 14.510 1.00 22.68 O ANISOU 1363 O GLU A 341 2673 3442 2503 -647 181 -267 O ATOM 1364 CB GLU A 341 32.046 -24.332 13.884 1.00 19.87 C ANISOU 1364 CB GLU A 341 2256 3258 2035 -638 83 -212 C ATOM 1365 CG GLU A 341 31.842 -25.411 14.943 1.00 30.92 C ANISOU 1365 CG GLU A 341 3651 4714 3384 -670 33 -192 C ATOM 1366 CD GLU A 341 33.064 -25.656 15.806 1.00 39.45 C ANISOU 1366 CD GLU A 341 4696 5913 4380 -748 0 -170 C ATOM 1367 OE1 GLU A 341 33.061 -26.644 16.576 1.00 40.36 O ANISOU 1367 OE1 GLU A 341 4793 6087 4454 -766 -50 -136 O ATOM 1368 OE2 GLU A 341 34.024 -24.869 15.714 1.00 31.42 O ANISOU 1368 OE2 GLU A 341 3665 4935 3338 -793 24 -180 O ATOM 1369 N PHE A 342 29.712 -22.038 13.667 1.00 18.54 N ANISOU 1369 N PHE A 342 2138 2881 2025 -671 284 -308 N ATOM 1370 CA PHE A 342 28.700 -21.226 14.341 1.00 21.65 C ANISOU 1370 CA PHE A 342 2556 3206 2465 -731 383 -355 C ATOM 1371 C PHE A 342 27.278 -21.587 13.920 1.00 25.91 C ANISOU 1371 C PHE A 342 3102 3661 3079 -660 384 -319 C ATOM 1372 O PHE A 342 26.342 -21.412 14.681 1.00 21.67 O ANISOU 1372 O PHE A 342 2586 3081 2568 -701 440 -341 O ATOM 1373 CB PHE A 342 28.953 -19.727 14.152 1.00 20.94 C ANISOU 1373 CB PHE A 342 2468 3071 2419 -776 494 -401 C ATOM 1374 CG PHE A 342 28.566 -19.194 12.794 1.00 27.56 C ANISOU 1374 CG PHE A 342 3286 3834 3353 -685 520 -364 C ATOM 1375 CD1 PHE A 342 27.285 -18.710 12.560 1.00 23.66 C ANISOU 1375 CD1 PHE A 342 2793 3240 2957 -659 594 -350 C ATOM 1376 CD2 PHE A 342 29.500 -19.123 11.772 1.00 25.48 C ANISOU 1376 CD2 PHE A 342 2997 3601 3083 -632 475 -339 C ATOM 1377 CE1 PHE A 342 26.935 -18.196 11.328 1.00 22.38 C ANISOU 1377 CE1 PHE A 342 2601 3018 2882 -585 617 -304 C ATOM 1378 CE2 PHE A 342 29.159 -18.612 10.527 1.00 27.13 C ANISOU 1378 CE2 PHE A 342 3183 3748 3376 -557 498 -302 C ATOM 1379 CZ PHE A 342 27.878 -18.148 10.301 1.00 22.91 C ANISOU 1379 CZ PHE A 342 2644 3123 2936 -536 566 -282 C ATOM 1380 N ILE A 343 27.114 -22.077 12.701 1.00 20.97 N ANISOU 1380 N ILE A 343 2463 3018 2489 -561 326 -260 N ATOM 1381 CA ILE A 343 25.789 -22.490 12.235 1.00 20.96 C ANISOU 1381 CA ILE A 343 2466 2950 2549 -500 315 -212 C ATOM 1382 C ILE A 343 25.347 -23.760 12.960 1.00 19.36 C ANISOU 1382 C ILE A 343 2280 2779 2296 -499 243 -199 C ATOM 1383 O ILE A 343 24.192 -23.907 13.357 1.00 24.05 O ANISOU 1383 O ILE A 343 2886 3326 2925 -501 263 -189 O ATOM 1384 CB ILE A 343 25.779 -22.705 10.706 1.00 20.68 C ANISOU 1384 CB ILE A 343 2413 2896 2549 -410 268 -152 C ATOM 1385 CG1 ILE A 343 26.112 -21.389 9.998 1.00 20.04 C ANISOU 1385 CG1 ILE A 343 2307 2780 2527 -411 344 -160 C ATOM 1386 CG2 ILE A 343 24.418 -23.208 10.241 1.00 22.40 C ANISOU 1386 CG2 ILE A 343 2633 3060 2816 -362 247 -94 C ATOM 1387 CD1 ILE A 343 26.144 -21.490 8.479 1.00 23.15 C ANISOU 1387 CD1 ILE A 343 2680 3162 2954 -333 302 -102 C ATOM 1388 N VAL A 344 26.281 -24.678 13.139 1.00 20.51 N ANISOU 1388 N VAL A 344 2422 3006 2365 -494 163 -194 N ATOM 1389 CA VAL A 344 26.008 -25.908 13.871 1.00 21.65 C ANISOU 1389 CA VAL A 344 2576 3189 2461 -494 96 -179 C ATOM 1390 C VAL A 344 25.552 -25.610 15.299 1.00 23.87 C ANISOU 1390 C VAL A 344 2870 3476 2725 -584 145 -226 C ATOM 1391 O VAL A 344 24.580 -26.187 15.788 1.00 23.63 O ANISOU 1391 O VAL A 344 2853 3422 2703 -579 130 -216 O ATOM 1392 CB VAL A 344 27.257 -26.777 13.933 1.00 25.95 C ANISOU 1392 CB VAL A 344 3104 3823 2933 -486 22 -161 C ATOM 1393 CG1 VAL A 344 26.972 -28.056 14.706 1.00 27.99 C ANISOU 1393 CG1 VAL A 344 3364 4122 3149 -484 -42 -139 C ATOM 1394 CG2 VAL A 344 27.760 -27.066 12.515 1.00 22.30 C ANISOU 1394 CG2 VAL A 344 2636 3350 2487 -401 -16 -120 C ATOM 1395 N ASP A 345 26.262 -24.710 15.968 1.00 25.34 N ANISOU 1395 N ASP A 345 3054 3692 2882 -673 206 -279 N ATOM 1396 CA ASP A 345 25.905 -24.330 17.330 1.00 29.83 C ANISOU 1396 CA ASP A 345 3642 4266 3425 -777 265 -333 C ATOM 1397 C ASP A 345 24.588 -23.556 17.347 1.00 29.58 C ANISOU 1397 C ASP A 345 3634 4124 3483 -777 362 -349 C ATOM 1398 O ASP A 345 23.764 -23.752 18.233 1.00 24.76 O ANISOU 1398 O ASP A 345 3042 3492 2873 -815 386 -365 O ATOM 1399 CB ASP A 345 27.032 -23.529 17.983 1.00 34.23 C ANISOU 1399 CB ASP A 345 4196 4887 3921 -886 311 -386 C ATOM 1400 CG ASP A 345 28.297 -24.358 18.181 1.00 44.38 C ANISOU 1400 CG ASP A 345 5450 6294 5117 -898 216 -354 C ATOM 1401 OD1 ASP A 345 28.184 -25.566 18.489 1.00 44.94 O ANISOU 1401 OD1 ASP A 345 5508 6410 5157 -869 134 -313 O ATOM 1402 OD2 ASP A 345 29.404 -23.799 18.032 1.00 50.85 O ANISOU 1402 OD2 ASP A 345 6255 7163 5903 -937 227 -364 O ATOM 1403 N PHE A 346 24.384 -22.696 16.355 1.00 22.21 N ANISOU 1403 N PHE A 346 2693 3119 2628 -732 420 -337 N ATOM 1404 CA PHE A 346 23.114 -21.991 16.221 1.00 24.42 C ANISOU 1404 CA PHE A 346 2981 3289 3008 -718 514 -327 C ATOM 1405 C PHE A 346 21.931 -22.965 16.121 1.00 26.43 C ANISOU 1405 C PHE A 346 3239 3514 3291 -654 456 -268 C ATOM 1406 O PHE A 346 20.959 -22.869 16.872 1.00 23.81 O ANISOU 1406 O PHE A 346 2925 3133 2991 -683 509 -277 O ATOM 1407 CB PHE A 346 23.140 -21.082 14.991 1.00 23.99 C ANISOU 1407 CB PHE A 346 2903 3176 3036 -665 565 -298 C ATOM 1408 CG PHE A 346 21.887 -20.262 14.813 1.00 24.57 C ANISOU 1408 CG PHE A 346 2972 3137 3226 -650 674 -271 C ATOM 1409 CD1 PHE A 346 21.790 -18.996 15.362 1.00 23.92 C ANISOU 1409 CD1 PHE A 346 2902 2992 3195 -721 822 -324 C ATOM 1410 CD2 PHE A 346 20.805 -20.761 14.100 1.00 23.94 C ANISOU 1410 CD2 PHE A 346 2875 3014 3208 -570 636 -187 C ATOM 1411 CE1 PHE A 346 20.640 -18.239 15.202 1.00 26.08 C ANISOU 1411 CE1 PHE A 346 3166 3155 3589 -703 936 -287 C ATOM 1412 CE2 PHE A 346 19.653 -20.008 13.939 1.00 24.13 C ANISOU 1412 CE2 PHE A 346 2885 2939 3347 -557 738 -143 C ATOM 1413 CZ PHE A 346 19.577 -18.742 14.486 1.00 26.96 C ANISOU 1413 CZ PHE A 346 3249 3228 3765 -618 892 -191 C ATOM 1414 N VAL A 347 22.018 -23.892 15.174 1.00 21.41 N ANISOU 1414 N VAL A 347 2588 2906 2642 -569 350 -209 N ATOM 1415 CA VAL A 347 20.961 -24.869 14.940 1.00 17.95 C ANISOU 1415 CA VAL A 347 2153 2445 2221 -509 286 -149 C ATOM 1416 C VAL A 347 20.722 -25.768 16.148 1.00 20.46 C ANISOU 1416 C VAL A 347 2490 2804 2480 -546 243 -171 C ATOM 1417 O VAL A 347 19.597 -26.183 16.399 1.00 21.13 O ANISOU 1417 O VAL A 347 2585 2849 2595 -527 237 -140 O ATOM 1418 CB VAL A 347 21.292 -25.753 13.708 1.00 24.71 C ANISOU 1418 CB VAL A 347 2999 3332 3056 -428 184 -93 C ATOM 1419 CG1 VAL A 347 20.431 -26.993 13.685 1.00 30.82 C ANISOU 1419 CG1 VAL A 347 3786 4106 3816 -385 104 -45 C ATOM 1420 CG2 VAL A 347 21.123 -24.950 12.426 1.00 20.61 C ANISOU 1420 CG2 VAL A 347 2458 2763 2608 -386 221 -52 C ATOM 1421 N ALA A 348 21.775 -26.062 16.904 1.00 20.84 N ANISOU 1421 N ALA A 348 2538 2935 2444 -600 213 -216 N ATOM 1422 CA ALA A 348 21.643 -26.986 18.028 1.00 23.54 C ANISOU 1422 CA ALA A 348 2888 3330 2726 -636 163 -227 C ATOM 1423 C ALA A 348 20.971 -26.346 19.238 1.00 28.52 C ANISOU 1423 C ALA A 348 3541 3926 3369 -722 252 -278 C ATOM 1424 O ALA A 348 20.642 -27.033 20.197 1.00 26.46 O ANISOU 1424 O ALA A 348 3288 3698 3068 -754 220 -286 O ATOM 1425 CB ALA A 348 22.992 -27.561 18.425 1.00 22.89 C ANISOU 1425 CB ALA A 348 2787 3357 2552 -669 99 -240 C ATOM 1426 N THR A 349 20.785 -25.034 19.212 1.00 27.94 N ANISOU 1426 N THR A 349 3479 3786 3353 -763 371 -312 N ATOM 1427 CA THR A 349 20.041 -24.382 20.284 1.00 30.03 C ANISOU 1427 CA THR A 349 3773 3997 3642 -842 477 -360 C ATOM 1428 C THR A 349 18.621 -24.937 20.269 1.00 33.44 C ANISOU 1428 C THR A 349 4209 4363 4133 -781 463 -306 C ATOM 1429 O THR A 349 17.980 -24.963 19.220 1.00 33.57 O ANISOU 1429 O THR A 349 4211 4323 4222 -694 450 -239 O ATOM 1430 CB THR A 349 20.005 -22.870 20.086 1.00 36.75 C ANISOU 1430 CB THR A 349 4633 4766 4563 -882 623 -396 C ATOM 1431 OG1 THR A 349 21.322 -22.341 20.283 1.00 34.95 O ANISOU 1431 OG1 THR A 349 4406 4604 4268 -957 640 -454 O ATOM 1432 CG2 THR A 349 19.050 -22.228 21.070 1.00 43.66 C ANISOU 1432 CG2 THR A 349 5543 5560 5484 -951 750 -435 C ATOM 1433 N PRO A 350 18.132 -25.397 21.432 1.00 35.76 N ANISOU 1433 N PRO A 350 4379 5177 4031 -955 1011 -217 N ATOM 1434 CA PRO A 350 16.845 -26.093 21.534 1.00 33.99 C ANISOU 1434 CA PRO A 350 4106 4916 3893 -915 1020 -143 C ATOM 1435 C PRO A 350 15.722 -25.447 20.724 1.00 33.08 C ANISOU 1435 C PRO A 350 3936 4663 3970 -826 1101 -123 C ATOM 1436 O PRO A 350 15.057 -26.143 19.956 1.00 34.67 O ANISOU 1436 O PRO A 350 4082 4820 4270 -746 1013 -23 O ATOM 1437 CB PRO A 350 16.538 -26.019 23.029 1.00 39.48 C ANISOU 1437 CB PRO A 350 4840 5673 4486 -1033 1138 -197 C ATOM 1438 CG PRO A 350 17.874 -26.020 23.669 1.00 34.10 C ANISOU 1438 CG PRO A 350 4220 5109 3625 -1138 1092 -244 C ATOM 1439 CD PRO A 350 18.788 -25.262 22.745 1.00 32.67 C ANISOU 1439 CD PRO A 350 4053 4893 3468 -1095 1062 -283 C ATOM 1440 N GLU A 351 15.515 -24.145 20.893 1.00 35.09 N ANISOU 1440 N GLU A 351 4201 4850 4281 -847 1267 -210 N ATOM 1441 CA GLU A 351 14.413 -23.461 20.225 1.00 39.30 C ANISOU 1441 CA GLU A 351 4669 5248 5015 -771 1361 -180 C ATOM 1442 C GLU A 351 14.644 -23.392 18.718 1.00 33.73 C ANISOU 1442 C GLU A 351 3920 4488 4408 -677 1242 -117 C ATOM 1443 O GLU A 351 13.707 -23.515 17.934 1.00 31.27 O ANISOU 1443 O GLU A 351 3538 4095 4247 -606 1220 -23 O ATOM 1444 CB GLU A 351 14.211 -22.058 20.800 1.00 51.62 C ANISOU 1444 CB GLU A 351 6251 6742 6622 -820 1580 -292 C ATOM 1445 CG GLU A 351 12.886 -21.415 20.412 1.00 71.00 C ANISOU 1445 CG GLU A 351 8625 9053 9300 -755 1710 -248 C ATOM 1446 CD GLU A 351 12.470 -20.301 21.363 1.00 87.36 C ANISOU 1446 CD GLU A 351 10722 11060 11410 -820 1960 -359 C ATOM 1447 OE1 GLU A 351 13.116 -19.227 21.359 1.00 92.44 O ANISOU 1447 OE1 GLU A 351 11403 11677 12045 -852 2050 -461 O ATOM 1448 OE2 GLU A 351 11.488 -20.498 22.112 1.00 89.73 O ANISOU 1448 OE2 GLU A 351 11007 11333 11753 -840 2073 -345 O ATOM 1449 N HIS A 352 15.895 -23.208 18.315 1.00 24.01 N ANISOU 1449 N HIS A 352 2730 3306 3088 -685 1163 -161 N ATOM 1450 CA HIS A 352 16.221 -23.173 16.891 1.00 26.49 C ANISOU 1450 CA HIS A 352 3010 3579 3474 -607 1048 -109 C ATOM 1451 C HIS A 352 16.057 -24.546 16.245 1.00 25.49 C ANISOU 1451 C HIS A 352 2863 3479 3344 -559 876 1 C ATOM 1452 O HIS A 352 15.484 -24.666 15.165 1.00 26.13 O ANISOU 1452 O HIS A 352 2893 3493 3540 -496 816 82 O ATOM 1453 CB HIS A 352 17.633 -22.633 16.663 1.00 28.12 C ANISOU 1453 CB HIS A 352 3268 3832 3585 -629 1013 -185 C ATOM 1454 CG HIS A 352 17.826 -21.231 17.155 1.00 27.35 C ANISOU 1454 CG HIS A 352 3194 3699 3499 -676 1177 -294 C ATOM 1455 ND1 HIS A 352 19.065 -20.709 17.453 1.00 30.37 N ANISOU 1455 ND1 HIS A 352 3638 4142 3761 -732 1179 -380 N ATOM 1456 CD2 HIS A 352 16.931 -20.247 17.410 1.00 31.56 C ANISOU 1456 CD2 HIS A 352 3697 4137 4159 -678 1349 -328 C ATOM 1457 CE1 HIS A 352 18.928 -19.460 17.860 1.00 36.84 C ANISOU 1457 CE1 HIS A 352 4471 4905 4622 -770 1344 -471 C ATOM 1458 NE2 HIS A 352 17.642 -19.157 17.849 1.00 38.35 N ANISOU 1458 NE2 HIS A 352 4606 4998 4968 -736 1455 -444 N ATOM 1459 N LEU A 353 16.553 -25.578 16.914 1.00 27.10 N ANISOU 1459 N LEU A 353 3104 3779 3415 -598 799 9 N ATOM 1460 CA LEU A 353 16.450 -26.933 16.396 1.00 24.96 C ANISOU 1460 CA LEU A 353 2818 3531 3136 -558 646 105 C ATOM 1461 C LEU A 353 14.991 -27.278 16.141 1.00 25.26 C ANISOU 1461 C LEU A 353 2798 3498 3303 -519 657 195 C ATOM 1462 O LEU A 353 14.643 -27.856 15.106 1.00 24.45 O ANISOU 1462 O LEU A 353 2667 3357 3267 -466 552 279 O ATOM 1463 CB LEU A 353 17.052 -27.935 17.385 1.00 25.05 C ANISOU 1463 CB LEU A 353 2863 3651 3004 -615 588 106 C ATOM 1464 CG LEU A 353 17.223 -29.339 16.816 1.00 26.87 C ANISOU 1464 CG LEU A 353 3083 3904 3222 -576 428 195 C ATOM 1465 CD1 LEU A 353 18.279 -29.325 15.717 1.00 29.59 C ANISOU 1465 CD1 LEU A 353 3446 4240 3556 -536 339 188 C ATOM 1466 CD2 LEU A 353 17.597 -30.326 17.902 1.00 29.50 C ANISOU 1466 CD2 LEU A 353 3430 4337 3442 -634 384 216 C ATOM 1467 N ARG A 354 14.137 -26.919 17.094 1.00 26.61 N ANISOU 1467 N ARG A 354 2952 3652 3506 -551 788 179 N ATOM 1468 CA ARG A 354 12.707 -27.189 16.982 1.00 30.02 C ANISOU 1468 CA ARG A 354 3322 4015 4069 -517 813 272 C ATOM 1469 C ARG A 354 12.117 -26.551 15.726 1.00 30.45 C ANISOU 1469 C ARG A 354 3318 3963 4288 -456 810 333 C ATOM 1470 O ARG A 354 11.478 -27.226 14.914 1.00 31.93 O ANISOU 1470 O ARG A 354 3467 4117 4547 -417 708 444 O ATOM 1471 CB ARG A 354 11.964 -26.687 18.226 1.00 31.71 C ANISOU 1471 CB ARG A 354 3530 4218 4300 -564 987 230 C ATOM 1472 CG ARG A 354 10.489 -27.062 18.256 1.00 38.33 C ANISOU 1472 CG ARG A 354 4300 4992 5270 -531 1017 335 C ATOM 1473 CD ARG A 354 9.759 -26.377 19.408 1.00 48.44 C ANISOU 1473 CD ARG A 354 5574 6243 6588 -574 1220 283 C ATOM 1474 NE ARG A 354 9.990 -24.934 19.416 1.00 61.76 N ANISOU 1474 NE ARG A 354 7268 7865 8333 -587 1378 187 N ATOM 1475 CZ ARG A 354 9.332 -24.062 18.657 1.00 71.90 C ANISOU 1475 CZ ARG A 354 8484 9029 9806 -533 1451 229 C ATOM 1476 NH1 ARG A 354 8.391 -24.481 17.818 1.00 72.73 N ANISOU 1476 NH1 ARG A 354 8510 9071 10055 -471 1375 373 N ATOM 1477 NH2 ARG A 354 9.616 -22.767 18.736 1.00 73.40 N ANISOU 1477 NH2 ARG A 354 8682 9160 10045 -549 1598 135 N ATOM 1478 N GLN A 355 12.342 -25.253 15.564 1.00 26.14 N ANISOU 1478 N GLN A 355 2766 3366 3800 -457 920 267 N ATOM 1479 CA GLN A 355 11.811 -24.515 14.424 1.00 24.62 C ANISOU 1479 CA GLN A 355 2508 3075 3773 -409 927 330 C ATOM 1480 C GLN A 355 12.364 -25.044 13.109 1.00 24.92 C ANISOU 1480 C GLN A 355 2553 3127 3788 -378 751 384 C ATOM 1481 O GLN A 355 11.625 -25.319 12.174 1.00 26.97 O ANISOU 1481 O GLN A 355 2761 3335 4150 -350 677 496 O ATOM 1482 CB GLN A 355 12.189 -23.031 14.521 1.00 31.48 C ANISOU 1482 CB GLN A 355 3374 3895 4692 -420 1071 235 C ATOM 1483 CG GLN A 355 11.422 -22.230 15.554 1.00 39.37 C ANISOU 1483 CG GLN A 355 4350 4835 5772 -446 1280 190 C ATOM 1484 CD GLN A 355 11.772 -20.752 15.495 1.00 46.74 C ANISOU 1484 CD GLN A 355 5278 5705 6776 -454 1420 102 C ATOM 1485 OE1 GLN A 355 11.560 -20.090 14.475 1.00 44.37 O ANISOU 1485 OE1 GLN A 355 4912 5327 6619 -411 1411 158 O ATOM 1486 NE2 GLN A 355 12.318 -20.231 16.587 1.00 47.97 N ANISOU 1486 NE2 GLN A 355 5502 5894 6830 -517 1548 -34 N ATOM 1487 N ILE A 356 13.679 -25.165 13.032 1.00 20.35 N ANISOU 1487 N ILE A 356 2040 2618 3074 -391 688 305 N ATOM 1488 CA ILE A 356 14.324 -25.512 11.771 1.00 20.39 C ANISOU 1488 CA ILE A 356 2060 2631 3057 -365 546 336 C ATOM 1489 C ILE A 356 14.009 -26.943 11.322 1.00 25.54 C ANISOU 1489 C ILE A 356 2720 3304 3681 -354 403 427 C ATOM 1490 O ILE A 356 13.686 -27.171 10.159 1.00 28.47 O ANISOU 1490 O ILE A 356 3070 3635 4112 -336 314 504 O ATOM 1491 CB ILE A 356 15.851 -25.277 11.850 1.00 20.17 C ANISOU 1491 CB ILE A 356 2098 2669 2898 -380 525 233 C ATOM 1492 CG1 ILE A 356 16.127 -23.792 12.110 1.00 26.72 C ANISOU 1492 CG1 ILE A 356 2918 3466 3767 -393 659 148 C ATOM 1493 CG2 ILE A 356 16.548 -25.718 10.564 1.00 21.33 C ANISOU 1493 CG2 ILE A 356 2264 2823 3019 -354 387 261 C ATOM 1494 CD1 ILE A 356 17.572 -23.480 12.469 1.00 20.97 C ANISOU 1494 CD1 ILE A 356 2255 2808 2903 -422 658 44 C ATOM 1495 N CYS A 357 14.098 -27.903 12.241 1.00 21.77 N ANISOU 1495 N CYS A 357 2272 2888 3110 -373 382 419 N ATOM 1496 CA CYS A 357 13.858 -29.310 11.892 1.00 24.35 C ANISOU 1496 CA CYS A 357 2609 3233 3409 -364 251 499 C ATOM 1497 C CYS A 357 12.421 -29.587 11.499 1.00 23.73 C ANISOU 1497 C CYS A 357 2473 3091 3453 -351 234 616 C ATOM 1498 O CYS A 357 12.148 -30.494 10.715 1.00 33.22 O ANISOU 1498 O CYS A 357 3681 4281 4662 -344 116 693 O ATOM 1499 CB CYS A 357 14.261 -30.236 13.040 1.00 27.04 C ANISOU 1499 CB CYS A 357 2983 3657 3636 -390 237 473 C ATOM 1500 SG CYS A 357 16.047 -30.337 13.254 1.00 25.48 S ANISOU 1500 SG CYS A 357 2849 3541 3293 -409 199 381 S ATOM 1501 N SER A 358 11.507 -28.797 12.049 1.00 25.24 N ANISOU 1501 N SER A 358 2610 3236 3744 -352 357 632 N ATOM 1502 CA SER A 358 10.087 -28.941 11.766 1.00 29.21 C ANISOU 1502 CA SER A 358 3044 3673 4383 -341 356 757 C ATOM 1503 C SER A 358 9.671 -28.179 10.517 1.00 26.61 C ANISOU 1503 C SER A 358 2662 3265 4182 -330 338 828 C ATOM 1504 O SER A 358 8.491 -27.908 10.320 1.00 29.36 O ANISOU 1504 O SER A 358 2935 3546 4675 -325 371 936 O ATOM 1505 CB SER A 358 9.265 -28.466 12.965 1.00 29.94 C ANISOU 1505 CB SER A 358 3094 3743 4537 -348 510 750 C ATOM 1506 OG SER A 358 9.598 -29.233 14.109 1.00 40.21 O ANISOU 1506 OG SER A 358 4441 5125 5712 -373 514 698 O ATOM 1507 N ASP A 359 10.644 -27.834 9.680 1.00 28.02 N ANISOU 1507 N ASP A 359 2877 3457 4314 -329 286 777 N ATOM 1508 CA ASP A 359 10.367 -27.123 8.435 1.00 23.58 C ANISOU 1508 CA ASP A 359 2268 2833 3859 -329 256 845 C ATOM 1509 C ASP A 359 10.806 -27.955 7.236 1.00 22.39 C ANISOU 1509 C ASP A 359 2166 2705 3637 -344 92 882 C ATOM 1510 O ASP A 359 11.822 -28.634 7.283 1.00 21.45 O ANISOU 1510 O ASP A 359 2124 2644 3383 -344 35 804 O ATOM 1511 CB ASP A 359 11.098 -25.781 8.403 1.00 22.25 C ANISOU 1511 CB ASP A 359 2093 2650 3712 -321 352 753 C ATOM 1512 CG ASP A 359 10.833 -25.012 7.126 1.00 25.12 C ANISOU 1512 CG ASP A 359 2398 2955 4192 -325 318 831 C ATOM 1513 OD1 ASP A 359 11.673 -25.071 6.201 1.00 23.51 O ANISOU 1513 OD1 ASP A 359 2236 2779 3918 -333 226 805 O ATOM 1514 OD2 ASP A 359 9.764 -24.377 7.033 1.00 25.17 O ANISOU 1514 OD2 ASP A 359 2311 2888 4366 -323 383 928 O ATOM 1515 N LYS A 360 10.034 -27.876 6.163 1.00 22.17 N ANISOU 1515 N LYS A 360 2091 2628 3707 -366 25 1004 N ATOM 1516 CA LYS A 360 10.307 -28.596 4.924 1.00 24.60 C ANISOU 1516 CA LYS A 360 2447 2948 3953 -400 -122 1046 C ATOM 1517 C LYS A 360 11.747 -28.396 4.433 1.00 24.88 C ANISOU 1517 C LYS A 360 2553 3022 3877 -395 -146 929 C ATOM 1518 O LYS A 360 12.459 -29.352 4.112 1.00 23.64 O ANISOU 1518 O LYS A 360 2476 2902 3603 -404 -229 887 O ATOM 1519 CB LYS A 360 9.329 -28.102 3.858 1.00 32.70 C ANISOU 1519 CB LYS A 360 3396 3915 5113 -438 -166 1192 C ATOM 1520 CG LYS A 360 9.284 -28.937 2.606 1.00 46.27 C ANISOU 1520 CG LYS A 360 5163 5642 6774 -498 -320 1262 C ATOM 1521 CD LYS A 360 8.095 -28.552 1.747 1.00 56.06 C ANISOU 1521 CD LYS A 360 6316 6831 8154 -552 -368 1439 C ATOM 1522 CE LYS A 360 8.139 -27.081 1.375 1.00 63.52 C ANISOU 1522 CE LYS A 360 7177 7740 9217 -547 -298 1458 C ATOM 1523 NZ LYS A 360 6.964 -26.678 0.550 1.00 67.78 N ANISOU 1523 NZ LYS A 360 7615 8229 9911 -606 -348 1653 N ATOM 1524 N TYR A 361 12.180 -27.144 4.380 1.00 17.10 N ANISOU 1524 N TYR A 361 1535 2024 2937 -380 -67 878 N ATOM 1525 CA TYR A 361 13.519 -26.844 3.890 1.00 16.74 C ANISOU 1525 CA TYR A 361 1548 2013 2798 -375 -87 776 C ATOM 1526 C TYR A 361 14.541 -26.918 5.006 1.00 21.94 C ANISOU 1526 C TYR A 361 2259 2726 3353 -344 -22 646 C ATOM 1527 O TYR A 361 15.659 -27.378 4.795 1.00 22.54 O ANISOU 1527 O TYR A 361 2404 2845 3316 -339 -71 575 O ATOM 1528 CB TYR A 361 13.546 -25.475 3.215 1.00 16.49 C ANISOU 1528 CB TYR A 361 1457 1946 2864 -379 -47 792 C ATOM 1529 CG TYR A 361 12.559 -25.387 2.078 1.00 24.36 C ANISOU 1529 CG TYR A 361 2394 2897 3965 -425 -123 939 C ATOM 1530 CD1 TYR A 361 12.744 -26.126 0.914 1.00 23.97 C ANISOU 1530 CD1 TYR A 361 2398 2866 3843 -474 -254 980 C ATOM 1531 CD2 TYR A 361 11.425 -24.590 2.179 1.00 27.93 C ANISOU 1531 CD2 TYR A 361 2735 3287 4591 -428 -59 1046 C ATOM 1532 CE1 TYR A 361 11.832 -26.061 -0.119 1.00 27.92 C ANISOU 1532 CE1 TYR A 361 2847 3334 4426 -536 -332 1125 C ATOM 1533 CE2 TYR A 361 10.513 -24.516 1.153 1.00 28.46 C ANISOU 1533 CE2 TYR A 361 2738 3317 4759 -481 -137 1203 C ATOM 1534 CZ TYR A 361 10.719 -25.252 0.007 1.00 37.22 C ANISOU 1534 CZ TYR A 361 3907 4457 5780 -541 -279 1243 C ATOM 1535 OH TYR A 361 9.804 -25.174 -1.018 1.00 42.42 O ANISOU 1535 OH TYR A 361 4503 5086 6528 -612 -365 1408 O ATOM 1536 N GLY A 362 14.151 -26.473 6.194 1.00 16.32 N ANISOU 1536 N GLY A 362 1512 2009 2681 -330 90 620 N ATOM 1537 CA GLY A 362 15.037 -26.511 7.340 1.00 18.00 C ANISOU 1537 CA GLY A 362 1772 2279 2789 -320 153 507 C ATOM 1538 C GLY A 362 15.521 -27.920 7.651 1.00 19.53 C ANISOU 1538 C GLY A 362 2028 2529 2862 -323 69 496 C ATOM 1539 O GLY A 362 16.667 -28.104 8.062 1.00 18.82 O ANISOU 1539 O GLY A 362 1989 2495 2667 -321 66 415 O ATOM 1540 N CYS A 363 14.658 -28.916 7.475 1.00 19.16 N ANISOU 1540 N CYS A 363 1974 2468 2840 -330 1 584 N ATOM 1541 CA CYS A 363 15.051 -30.288 7.792 1.00 14.61 C ANISOU 1541 CA CYS A 363 1449 1936 2166 -332 -74 581 C ATOM 1542 C CYS A 363 16.086 -30.791 6.790 1.00 19.24 C ANISOU 1542 C CYS A 363 2095 2533 2681 -330 -162 552 C ATOM 1543 O CYS A 363 17.015 -31.500 7.159 1.00 19.99 O ANISOU 1543 O CYS A 363 2235 2673 2688 -324 -187 504 O ATOM 1544 CB CYS A 363 13.848 -31.236 7.871 1.00 24.06 C ANISOU 1544 CB CYS A 363 2622 3111 3408 -341 -123 683 C ATOM 1545 SG CYS A 363 13.042 -31.541 6.282 1.00 50.75 S ANISOU 1545 SG CYS A 363 5995 6429 6858 -366 -231 795 S ATOM 1546 N ARG A 364 15.940 -30.401 5.531 1.00 17.45 N ANISOU 1546 N ARG A 364 1868 2266 2498 -342 -204 584 N ATOM 1547 CA ARG A 364 16.955 -30.707 4.514 1.00 15.13 C ANISOU 1547 CA ARG A 364 1634 1977 2138 -345 -269 546 C ATOM 1548 C ARG A 364 18.309 -30.080 4.860 1.00 17.26 C ANISOU 1548 C ARG A 364 1925 2286 2345 -322 -219 443 C ATOM 1549 O ARG A 364 19.369 -30.695 4.659 1.00 18.84 O ANISOU 1549 O ARG A 364 2178 2510 2468 -312 -254 399 O ATOM 1550 CB ARG A 364 16.484 -30.240 3.135 1.00 16.54 C ANISOU 1550 CB ARG A 364 1801 2111 2372 -377 -317 603 C ATOM 1551 CG ARG A 364 17.430 -30.562 1.977 1.00 22.41 C ANISOU 1551 CG ARG A 364 2614 2856 3045 -393 -380 565 C ATOM 1552 CD ARG A 364 17.678 -32.064 1.820 1.00 27.31 C ANISOU 1552 CD ARG A 364 3305 3477 3596 -403 -444 564 C ATOM 1553 NE ARG A 364 18.933 -32.473 2.442 1.00 25.20 N ANISOU 1553 NE ARG A 364 3074 3246 3257 -364 -416 479 N ATOM 1554 CZ ARG A 364 19.487 -33.675 2.308 1.00 33.47 C ANISOU 1554 CZ ARG A 364 4179 4289 4251 -362 -453 462 C ATOM 1555 NH1 ARG A 364 18.891 -34.611 1.572 1.00 32.53 N ANISOU 1555 NH1 ARG A 364 4099 4131 4131 -401 -516 510 N ATOM 1556 NH2 ARG A 364 20.644 -33.939 2.909 1.00 25.60 N ANISOU 1556 NH2 ARG A 364 3198 3323 3207 -326 -423 402 N ATOM 1557 N VAL A 365 18.288 -28.854 5.371 1.00 15.68 N ANISOU 1557 N VAL A 365 1683 2090 2184 -314 -133 410 N ATOM 1558 CA VAL A 365 19.536 -28.199 5.788 1.00 14.30 C ANISOU 1558 CA VAL A 365 1529 1956 1947 -300 -84 316 C ATOM 1559 C VAL A 365 20.215 -28.968 6.920 1.00 16.20 C ANISOU 1559 C VAL A 365 1800 2257 2100 -299 -77 279 C ATOM 1560 O VAL A 365 21.433 -29.189 6.899 1.00 14.11 O ANISOU 1560 O VAL A 365 1572 2028 1762 -291 -98 234 O ATOM 1561 CB VAL A 365 19.295 -26.746 6.253 1.00 17.57 C ANISOU 1561 CB VAL A 365 1895 2357 2423 -301 20 284 C ATOM 1562 CG1 VAL A 365 20.545 -26.176 6.911 1.00 14.45 C ANISOU 1562 CG1 VAL A 365 1528 2012 1949 -299 71 188 C ATOM 1563 CG2 VAL A 365 18.877 -25.877 5.078 1.00 20.33 C ANISOU 1563 CG2 VAL A 365 2206 2653 2866 -302 11 323 C ATOM 1564 N VAL A 366 19.430 -29.371 7.915 1.00 15.71 N ANISOU 1564 N VAL A 366 1716 2206 2048 -311 -49 308 N ATOM 1565 CA VAL A 366 19.989 -30.115 9.039 1.00 13.63 C ANISOU 1565 CA VAL A 366 1470 2006 1701 -323 -48 288 C ATOM 1566 C VAL A 366 20.542 -31.464 8.591 1.00 14.89 C ANISOU 1566 C VAL A 366 1665 2173 1820 -311 -142 317 C ATOM 1567 O VAL A 366 21.604 -31.883 9.050 1.00 16.02 O ANISOU 1567 O VAL A 366 1827 2363 1896 -313 -155 292 O ATOM 1568 CB VAL A 366 18.980 -30.311 10.176 1.00 18.35 C ANISOU 1568 CB VAL A 366 2037 2618 2318 -344 1 317 C ATOM 1569 CG1 VAL A 366 19.591 -31.196 11.270 1.00 17.95 C ANISOU 1569 CG1 VAL A 366 2002 2641 2176 -367 -17 311 C ATOM 1570 CG2 VAL A 366 18.584 -28.971 10.763 1.00 18.91 C ANISOU 1570 CG2 VAL A 366 2080 2678 2427 -360 119 272 C ATOM 1571 N GLN A 367 19.848 -32.143 7.682 1.00 14.66 N ANISOU 1571 N GLN A 367 1642 2093 1835 -305 -205 374 N ATOM 1572 CA GLN A 367 20.376 -33.423 7.197 1.00 18.98 C ANISOU 1572 CA GLN A 367 2229 2632 2349 -297 -280 392 C ATOM 1573 C GLN A 367 21.704 -33.245 6.471 1.00 19.61 C ANISOU 1573 C GLN A 367 2348 2713 2391 -281 -290 339 C ATOM 1574 O GLN A 367 22.639 -34.017 6.654 1.00 18.42 O ANISOU 1574 O GLN A 367 2217 2580 2202 -270 -310 330 O ATOM 1575 CB GLN A 367 19.381 -34.165 6.293 1.00 18.49 C ANISOU 1575 CB GLN A 367 2180 2512 2333 -307 -344 457 C ATOM 1576 CG GLN A 367 19.829 -35.617 6.051 1.00 20.56 C ANISOU 1576 CG GLN A 367 2484 2763 2567 -304 -405 473 C ATOM 1577 CD GLN A 367 18.925 -36.397 5.125 1.00 31.58 C ANISOU 1577 CD GLN A 367 3907 4100 3992 -328 -469 530 C ATOM 1578 OE1 GLN A 367 19.379 -37.302 4.422 1.00 41.04 O ANISOU 1578 OE1 GLN A 367 5157 5265 5171 -333 -508 522 O ATOM 1579 NE2 GLN A 367 17.645 -36.057 5.115 1.00 26.66 N ANISOU 1579 NE2 GLN A 367 3248 3460 3420 -348 -476 590 N ATOM 1580 N THR A 368 21.787 -32.216 5.639 1.00 12.69 N ANISOU 1580 N THR A 368 1475 1813 1535 -280 -274 311 N ATOM 1581 CA THR A 368 23.033 -31.918 4.938 1.00 13.54 C ANISOU 1581 CA THR A 368 1615 1922 1607 -264 -277 260 C ATOM 1582 C THR A 368 24.195 -31.634 5.901 1.00 16.03 C ANISOU 1582 C THR A 368 1924 2298 1870 -254 -238 217 C ATOM 1583 O THR A 368 25.325 -32.074 5.676 1.00 15.24 O ANISOU 1583 O THR A 368 1848 2205 1737 -239 -255 201 O ATOM 1584 CB THR A 368 22.827 -30.742 3.960 1.00 14.82 C ANISOU 1584 CB THR A 368 1770 2056 1804 -270 -266 245 C ATOM 1585 OG1 THR A 368 21.918 -31.162 2.930 1.00 17.49 O ANISOU 1585 OG1 THR A 368 2122 2344 2179 -295 -319 298 O ATOM 1586 CG2 THR A 368 24.163 -30.316 3.318 1.00 14.38 C ANISOU 1586 CG2 THR A 368 1745 2010 1710 -253 -263 190 C ATOM 1587 N ILE A 369 23.913 -30.904 6.975 1.00 13.39 N ANISOU 1587 N ILE A 369 1555 2002 1529 -271 -184 202 N ATOM 1588 CA ILE A 369 24.928 -30.618 7.989 1.00 12.62 C ANISOU 1588 CA ILE A 369 1455 1972 1370 -283 -151 169 C ATOM 1589 C ILE A 369 25.397 -31.915 8.638 1.00 14.60 C ANISOU 1589 C ILE A 369 1706 2256 1587 -289 -191 210 C ATOM 1590 O ILE A 369 26.593 -32.161 8.761 1.00 14.18 O ANISOU 1590 O ILE A 369 1659 2232 1497 -285 -205 208 O ATOM 1591 CB ILE A 369 24.394 -29.655 9.071 1.00 14.43 C ANISOU 1591 CB ILE A 369 1657 2233 1591 -317 -75 141 C ATOM 1592 CG1 ILE A 369 24.294 -28.231 8.508 1.00 14.68 C ANISOU 1592 CG1 ILE A 369 1681 2233 1662 -311 -23 94 C ATOM 1593 CG2 ILE A 369 25.310 -29.674 10.332 1.00 13.21 C ANISOU 1593 CG2 ILE A 369 1505 2160 1353 -357 -54 123 C ATOM 1594 CD1 ILE A 369 23.567 -27.243 9.430 1.00 14.56 C ANISOU 1594 CD1 ILE A 369 1641 2224 1667 -342 72 64 C ATOM 1595 N ILE A 370 24.450 -32.753 9.039 1.00 15.84 N ANISOU 1595 N ILE A 370 1849 2406 1765 -297 -211 258 N ATOM 1596 CA ILE A 370 24.789 -34.047 9.635 1.00 16.63 C ANISOU 1596 CA ILE A 370 1940 2532 1847 -303 -252 309 C ATOM 1597 C ILE A 370 25.662 -34.898 8.706 1.00 17.34 C ANISOU 1597 C ILE A 370 2055 2579 1954 -269 -296 321 C ATOM 1598 O ILE A 370 26.659 -35.493 9.146 1.00 14.28 O ANISOU 1598 O ILE A 370 1654 2221 1550 -269 -310 346 O ATOM 1599 CB ILE A 370 23.530 -34.829 10.014 1.00 17.03 C ANISOU 1599 CB ILE A 370 1973 2570 1929 -312 -273 361 C ATOM 1600 CG1 ILE A 370 22.822 -34.158 11.188 1.00 15.75 C ANISOU 1600 CG1 ILE A 370 1782 2458 1746 -351 -217 353 C ATOM 1601 CG2 ILE A 370 23.874 -36.268 10.379 1.00 17.36 C ANISOU 1601 CG2 ILE A 370 2003 2622 1971 -311 -325 420 C ATOM 1602 CD1 ILE A 370 21.392 -34.663 11.379 1.00 16.98 C ANISOU 1602 CD1 ILE A 370 1917 2588 1947 -354 -226 403 C ATOM 1603 N GLU A 371 25.296 -34.940 7.428 1.00 14.40 N ANISOU 1603 N GLU A 371 1717 2136 1617 -248 -313 308 N ATOM 1604 CA GLU A 371 26.076 -35.675 6.429 1.00 15.98 C ANISOU 1604 CA GLU A 371 1954 2285 1832 -222 -336 305 C ATOM 1605 C GLU A 371 27.522 -35.184 6.322 1.00 21.91 C ANISOU 1605 C GLU A 371 2709 3058 2560 -205 -313 273 C ATOM 1606 O GLU A 371 28.466 -35.981 6.293 1.00 20.35 O ANISOU 1606 O GLU A 371 2510 2848 2374 -187 -319 295 O ATOM 1607 CB GLU A 371 25.381 -35.615 5.070 1.00 15.37 C ANISOU 1607 CB GLU A 371 1922 2139 1780 -224 -355 290 C ATOM 1608 CG GLU A 371 24.067 -36.371 5.081 1.00 17.63 C ANISOU 1608 CG GLU A 371 2209 2396 2095 -243 -391 339 C ATOM 1609 CD GLU A 371 23.299 -36.227 3.784 1.00 28.63 C ANISOU 1609 CD GLU A 371 3642 3730 3506 -265 -417 339 C ATOM 1610 OE1 GLU A 371 22.371 -37.027 3.554 1.00 33.98 O ANISOU 1610 OE1 GLU A 371 4334 4373 4204 -287 -457 383 O ATOM 1611 OE2 GLU A 371 23.617 -35.309 3.003 1.00 35.22 O ANISOU 1611 OE2 GLU A 371 4493 4558 4332 -268 -404 302 O ATOM 1612 N LYS A 372 27.697 -33.871 6.285 1.00 15.68 N ANISOU 1612 N LYS A 372 1916 2297 1746 -210 -283 228 N ATOM 1613 CA LYS A 372 29.034 -33.302 6.222 1.00 17.52 C ANISOU 1613 CA LYS A 372 2148 2555 1952 -197 -264 202 C ATOM 1614 C LYS A 372 29.815 -33.550 7.519 1.00 18.64 C ANISOU 1614 C LYS A 372 2251 2767 2062 -218 -262 240 C ATOM 1615 O LYS A 372 31.040 -33.653 7.491 1.00 21.73 O ANISOU 1615 O LYS A 372 2636 3171 2449 -206 -262 254 O ATOM 1616 CB LYS A 372 28.965 -31.804 5.908 1.00 15.31 C ANISOU 1616 CB LYS A 372 1872 2288 1657 -202 -234 147 C ATOM 1617 CG LYS A 372 30.321 -31.120 5.837 1.00 23.09 C ANISOU 1617 CG LYS A 372 2858 3302 2613 -192 -217 121 C ATOM 1618 CD LYS A 372 31.206 -31.753 4.761 1.00 29.45 C ANISOU 1618 CD LYS A 372 3692 4058 3439 -155 -232 124 C ATOM 1619 CE LYS A 372 30.559 -31.638 3.374 1.00 32.27 C ANISOU 1619 CE LYS A 372 4089 4350 3821 -147 -240 94 C ATOM 1620 NZ LYS A 372 31.463 -32.132 2.283 1.00 32.77 N ANISOU 1620 NZ LYS A 372 4191 4364 3894 -121 -238 82 N ATOM 1621 N LEU A 373 29.115 -33.650 8.652 1.00 13.11 N ANISOU 1621 N LEU A 373 1524 2116 1342 -256 -261 264 N ATOM 1622 CA LEU A 373 29.781 -33.919 9.936 1.00 13.76 C ANISOU 1622 CA LEU A 373 1568 2276 1383 -296 -267 310 C ATOM 1623 C LEU A 373 30.026 -35.401 10.222 1.00 15.79 C ANISOU 1623 C LEU A 373 1797 2525 1678 -290 -307 391 C ATOM 1624 O LEU A 373 30.497 -35.764 11.304 1.00 18.76 O ANISOU 1624 O LEU A 373 2130 2968 2028 -332 -323 450 O ATOM 1625 CB LEU A 373 29.017 -33.294 11.110 1.00 13.71 C ANISOU 1625 CB LEU A 373 1548 2335 1327 -355 -238 296 C ATOM 1626 CG LEU A 373 28.875 -31.770 11.105 1.00 17.74 C ANISOU 1626 CG LEU A 373 2077 2858 1805 -373 -182 220 C ATOM 1627 CD1 LEU A 373 27.997 -31.302 12.270 1.00 19.49 C ANISOU 1627 CD1 LEU A 373 2289 3128 1988 -433 -135 203 C ATOM 1628 CD2 LEU A 373 30.244 -31.095 11.137 1.00 21.20 C ANISOU 1628 CD2 LEU A 373 2520 3335 2200 -385 -176 203 C ATOM 1629 N THR A 374 29.734 -36.253 9.251 1.00 14.28 N ANISOU 1629 N THR A 374 1628 2252 1548 -245 -323 397 N ATOM 1630 CA THR A 374 29.905 -37.690 9.427 1.00 16.04 C ANISOU 1630 CA THR A 374 1824 2449 1823 -235 -352 469 C ATOM 1631 C THR A 374 31.286 -38.160 8.976 1.00 22.02 C ANISOU 1631 C THR A 374 2570 3172 2624 -202 -345 498 C ATOM 1632 O THR A 374 31.759 -37.779 7.901 1.00 18.81 O ANISOU 1632 O THR A 374 2205 2712 2230 -168 -320 447 O ATOM 1633 CB THR A 374 28.826 -38.464 8.649 1.00 18.15 C ANISOU 1633 CB THR A 374 2125 2635 2135 -213 -367 461 C ATOM 1634 OG1 THR A 374 27.536 -38.119 9.169 1.00 19.16 O ANISOU 1634 OG1 THR A 374 2249 2794 2236 -241 -374 456 O ATOM 1635 CG2 THR A 374 29.028 -39.969 8.780 1.00 17.88 C ANISOU 1635 CG2 THR A 374 2067 2563 2166 -200 -390 531 C ATOM 1636 N ALA A 375 31.934 -38.982 9.798 1.00 20.04 N ANISOU 1636 N ALA A 375 2259 2951 2404 -217 -364 587 N ATOM 1637 CA ALA A 375 33.248 -39.517 9.440 1.00 21.15 C ANISOU 1637 CA ALA A 375 2373 3052 2611 -185 -350 635 C ATOM 1638 C ALA A 375 33.094 -40.678 8.465 1.00 22.45 C ANISOU 1638 C ALA A 375 2564 3099 2866 -135 -333 634 C ATOM 1639 O ALA A 375 33.295 -41.842 8.822 1.00 23.52 O ANISOU 1639 O ALA A 375 2652 3207 3078 -130 -342 713 O ATOM 1640 CB ALA A 375 34.013 -39.956 10.697 1.00 24.74 C ANISOU 1640 CB ALA A 375 2740 3583 3078 -228 -380 751 C ATOM 1641 N ASP A 376 32.716 -40.366 7.233 1.00 21.06 N ANISOU 1641 N ASP A 376 2466 2853 2683 -108 -307 545 N ATOM 1642 CA ASP A 376 32.522 -41.412 6.238 1.00 19.78 C ANISOU 1642 CA ASP A 376 2348 2577 2589 -78 -284 528 C ATOM 1643 C ASP A 376 33.592 -41.368 5.151 1.00 24.13 C ANISOU 1643 C ASP A 376 2935 3054 3180 -39 -226 491 C ATOM 1644 O ASP A 376 34.568 -40.623 5.256 1.00 22.06 O ANISOU 1644 O ASP A 376 2648 2830 2903 -28 -211 497 O ATOM 1645 CB ASP A 376 31.119 -41.343 5.634 1.00 26.92 C ANISOU 1645 CB ASP A 376 3320 3453 3457 -95 -303 468 C ATOM 1646 CG ASP A 376 30.824 -40.009 4.979 1.00 30.77 C ANISOU 1646 CG ASP A 376 3856 3962 3873 -104 -298 389 C ATOM 1647 OD1 ASP A 376 29.633 -39.736 4.749 1.00 37.34 O ANISOU 1647 OD1 ASP A 376 4719 4794 4673 -128 -323 362 O ATOM 1648 OD2 ASP A 376 31.765 -39.234 4.695 1.00 25.51 O ANISOU 1648 OD2 ASP A 376 3191 3311 3190 -88 -272 362 O ATOM 1649 N SER A 377 33.399 -42.161 4.104 1.00 18.56 N ANISOU 1649 N SER A 377 2291 2240 2520 -23 -190 452 N ATOM 1650 CA SER A 377 34.419 -42.327 3.086 1.00 25.25 C ANISOU 1650 CA SER A 377 3175 3003 3416 11 -119 418 C ATOM 1651 C SER A 377 34.680 -41.011 2.366 1.00 28.38 C ANISOU 1651 C SER A 377 3618 3430 3737 11 -110 343 C ATOM 1652 O SER A 377 35.743 -40.820 1.795 1.00 27.53 O ANISOU 1652 O SER A 377 3518 3287 3656 40 -58 329 O ATOM 1653 CB SER A 377 34.033 -43.433 2.094 1.00 29.34 C ANISOU 1653 CB SER A 377 3766 3397 3984 11 -75 377 C ATOM 1654 OG SER A 377 32.864 -43.083 1.374 1.00 37.38 O ANISOU 1654 OG SER A 377 4869 4412 4923 -30 -106 304 O ATOM 1655 N MET A 378 33.718 -40.093 2.416 1.00 20.24 N ANISOU 1655 N MET A 378 2609 2461 2619 -22 -159 303 N ATOM 1656 CA MET A 378 33.889 -38.794 1.773 1.00 23.89 C ANISOU 1656 CA MET A 378 3105 2954 3017 -25 -155 239 C ATOM 1657 C MET A 378 34.725 -37.784 2.578 1.00 22.33 C ANISOU 1657 C MET A 378 2846 2845 2793 -15 -163 267 C ATOM 1658 O MET A 378 35.126 -36.749 2.046 1.00 27.75 O ANISOU 1658 O MET A 378 3553 3551 3441 -10 -153 221 O ATOM 1659 CB MET A 378 32.528 -38.203 1.405 1.00 27.93 C ANISOU 1659 CB MET A 378 3661 3485 3467 -65 -196 194 C ATOM 1660 CG MET A 378 31.855 -38.950 0.255 1.00 40.36 C ANISOU 1660 CG MET A 378 5317 4971 5047 -90 -188 155 C ATOM 1661 SD MET A 378 30.265 -38.236 -0.210 1.00100.58 S ANISOU 1661 SD MET A 378 12981 12623 12613 -147 -246 130 S ATOM 1662 CE MET A 378 30.716 -36.516 -0.445 1.00103.42 C ANISOU 1662 CE MET A 378 13322 13046 12927 -140 -243 93 C ATOM 1663 N ASN A 379 34.989 -38.078 3.849 1.00 16.96 N ANISOU 1663 N ASN A 379 2092 2222 2131 -21 -185 345 N ATOM 1664 CA ASN A 379 35.823 -37.191 4.672 1.00 16.16 C ANISOU 1664 CA ASN A 379 1937 2208 1997 -30 -196 379 C ATOM 1665 C ASN A 379 37.234 -37.708 4.977 1.00 17.94 C ANISOU 1665 C ASN A 379 2103 2423 2291 -6 -174 461 C ATOM 1666 O ASN A 379 37.900 -37.173 5.856 1.00 19.38 O ANISOU 1666 O ASN A 379 2231 2686 2448 -28 -196 516 O ATOM 1667 CB ASN A 379 35.123 -36.850 5.999 1.00 20.41 C ANISOU 1667 CB ASN A 379 2433 2842 2480 -79 -241 410 C ATOM 1668 CG ASN A 379 34.117 -35.715 5.861 1.00 29.28 C ANISOU 1668 CG ASN A 379 3594 3999 3532 -103 -250 333 C ATOM 1669 OD1 ASN A 379 33.059 -35.731 6.494 1.00 28.47 O ANISOU 1669 OD1 ASN A 379 3484 3927 3405 -134 -270 335 O ATOM 1670 ND2 ASN A 379 34.446 -34.717 5.040 1.00 16.18 N ANISOU 1670 ND2 ASN A 379 1969 2331 1849 -88 -231 271 N ATOM 1671 N VAL A 380 37.710 -38.725 4.266 1.00 18.42 N ANISOU 1671 N VAL A 380 2174 2384 2442 34 -127 476 N ATOM 1672 CA VAL A 380 39.026 -39.285 4.608 1.00 16.49 C ANISOU 1672 CA VAL A 380 1857 2120 2288 59 -99 575 C ATOM 1673 C VAL A 380 40.173 -38.322 4.316 1.00 15.48 C ANISOU 1673 C VAL A 380 1719 2017 2144 77 -80 574 C ATOM 1674 O VAL A 380 41.291 -38.517 4.794 1.00 19.73 O ANISOU 1674 O VAL A 380 2184 2567 2745 86 -73 674 O ATOM 1675 CB VAL A 380 39.304 -40.627 3.903 1.00 21.47 C ANISOU 1675 CB VAL A 380 2498 2621 3040 101 -33 591 C ATOM 1676 CG1 VAL A 380 38.262 -41.665 4.323 1.00 24.63 C ANISOU 1676 CG1 VAL A 380 2894 2998 3467 81 -58 611 C ATOM 1677 CG2 VAL A 380 39.333 -40.439 2.388 1.00 23.16 C ANISOU 1677 CG2 VAL A 380 2810 2745 3245 128 31 480 C ATOM 1678 N ASP A 381 39.896 -37.284 3.539 1.00 16.11 N ANISOU 1678 N ASP A 381 1867 2107 2146 78 -77 473 N ATOM 1679 CA ASP A 381 40.922 -36.292 3.214 1.00 17.96 C ANISOU 1679 CA ASP A 381 2096 2368 2359 95 -63 465 C ATOM 1680 C ASP A 381 41.138 -35.244 4.315 1.00 19.82 C ANISOU 1680 C ASP A 381 2286 2727 2518 49 -120 502 C ATOM 1681 O ASP A 381 42.066 -34.437 4.231 1.00 18.04 O ANISOU 1681 O ASP A 381 2044 2533 2276 56 -117 514 O ATOM 1682 CB ASP A 381 40.576 -35.586 1.910 1.00 14.09 C ANISOU 1682 CB ASP A 381 1693 1841 1821 109 -38 348 C ATOM 1683 CG ASP A 381 39.281 -34.797 2.011 1.00 24.79 C ANISOU 1683 CG ASP A 381 3085 3250 3083 68 -86 277 C ATOM 1684 OD1 ASP A 381 38.234 -35.409 2.292 1.00 19.69 O ANISOU 1684 OD1 ASP A 381 2451 2595 2437 47 -105 275 O ATOM 1685 OD2 ASP A 381 39.314 -33.567 1.822 1.00 22.20 O ANISOU 1685 OD2 ASP A 381 2770 2971 2694 59 -100 232 O ATOM 1686 N LEU A 382 40.291 -35.240 5.340 1.00 22.69 N ANISOU 1686 N LEU A 382 2630 3158 2832 -2 -167 517 N ATOM 1687 CA LEU A 382 40.489 -34.314 6.461 1.00 16.34 C ANISOU 1687 CA LEU A 382 1791 2469 1948 -62 -210 548 C ATOM 1688 C LEU A 382 41.763 -34.653 7.222 1.00 19.14 C ANISOU 1688 C LEU A 382 2063 2861 2346 -80 -226 680 C ATOM 1689 O LEU A 382 42.086 -35.824 7.403 1.00 22.32 O ANISOU 1689 O LEU A 382 2416 3222 2844 -64 -219 771 O ATOM 1690 CB LEU A 382 39.305 -34.376 7.439 1.00 18.15 C ANISOU 1690 CB LEU A 382 2019 2758 2121 -119 -245 540 C ATOM 1691 CG LEU A 382 37.954 -33.866 6.931 1.00 17.10 C ANISOU 1691 CG LEU A 382 1950 2605 1941 -117 -238 429 C ATOM 1692 CD1 LEU A 382 36.906 -33.951 8.036 1.00 21.07 C ANISOU 1692 CD1 LEU A 382 2440 3168 2397 -175 -264 438 C ATOM 1693 CD2 LEU A 382 38.070 -32.436 6.437 1.00 25.19 C ANISOU 1693 CD2 LEU A 382 3011 3651 2909 -117 -225 349 C ATOM 1694 N THR A 383 42.486 -33.629 7.675 1.00 16.91 N ANISOU 1694 N THR A 383 1765 2658 2003 -118 -249 700 N ATOM 1695 CA THR A 383 43.554 -33.833 8.654 1.00 19.46 C ANISOU 1695 CA THR A 383 2004 3044 2344 -166 -284 843 C ATOM 1696 C THR A 383 42.942 -34.348 9.953 1.00 21.22 C ANISOU 1696 C THR A 383 2189 3342 2532 -247 -330 906 C ATOM 1697 O THR A 383 41.750 -34.164 10.199 1.00 18.41 O ANISOU 1697 O THR A 383 1878 3006 2110 -272 -334 823 O ATOM 1698 CB THR A 383 44.293 -32.523 8.997 1.00 24.57 C ANISOU 1698 CB THR A 383 2653 3776 2905 -215 -308 843 C ATOM 1699 OG1 THR A 383 43.359 -31.557 9.498 1.00 21.49 O ANISOU 1699 OG1 THR A 383 2316 3455 2394 -275 -322 745 O ATOM 1700 CG2 THR A 383 45.020 -31.958 7.783 1.00 20.56 C ANISOU 1700 CG2 THR A 383 2173 3208 2431 -141 -269 796 C ATOM 1701 N SER A 384 43.758 -34.968 10.802 1.00 24.06 N ANISOU 1701 N SER A 384 2460 3744 2936 -293 -366 1060 N ATOM 1702 CA SER A 384 43.257 -35.455 12.082 1.00 26.04 C ANISOU 1702 CA SER A 384 2668 4077 3147 -382 -416 1134 C ATOM 1703 C SER A 384 42.781 -34.301 12.963 1.00 24.61 C ANISOU 1703 C SER A 384 2532 4013 2805 -485 -445 1071 C ATOM 1704 O SER A 384 41.825 -34.448 13.725 1.00 23.83 O ANISOU 1704 O SER A 384 2445 3965 2645 -543 -461 1049 O ATOM 1705 CB SER A 384 44.301 -36.320 12.808 1.00 30.32 C ANISOU 1705 CB SER A 384 3096 4648 3777 -423 -455 1333 C ATOM 1706 OG SER A 384 45.417 -35.546 13.192 1.00 42.53 O ANISOU 1706 OG SER A 384 4611 6268 5282 -481 -487 1408 O ATOM 1707 N ALA A 385 43.416 -33.139 12.841 1.00 25.22 N ANISOU 1707 N ALA A 385 2637 4128 2816 -506 -443 1036 N ATOM 1708 CA ALA A 385 42.919 -31.970 13.560 1.00 26.18 C ANISOU 1708 CA ALA A 385 2815 4343 2791 -599 -450 953 C ATOM 1709 C ALA A 385 41.516 -31.570 13.082 1.00 24.98 C ANISOU 1709 C ALA A 385 2740 4145 2607 -557 -403 792 C ATOM 1710 O ALA A 385 40.652 -31.237 13.893 1.00 20.31 O ANISOU 1710 O ALA A 385 2176 3611 1929 -630 -399 744 O ATOM 1711 CB ALA A 385 43.881 -30.806 13.444 1.00 26.53 C ANISOU 1711 CB ALA A 385 2875 4425 2779 -626 -454 943 C ATOM 1712 N ALA A 386 41.288 -31.608 11.772 1.00 17.29 N ANISOU 1712 N ALA A 386 1799 3066 1704 -446 -364 716 N ATOM 1713 CA ALA A 386 39.964 -31.308 11.237 1.00 16.70 C ANISOU 1713 CA ALA A 386 1787 2944 1615 -408 -327 587 C ATOM 1714 C ALA A 386 38.946 -32.378 11.648 1.00 18.09 C ANISOU 1714 C ALA A 386 1949 3106 1818 -413 -336 609 C ATOM 1715 O ALA A 386 37.771 -32.070 11.879 1.00 16.11 O ANISOU 1715 O ALA A 386 1734 2863 1524 -433 -319 535 O ATOM 1716 CB ALA A 386 40.011 -31.154 9.708 1.00 18.01 C ANISOU 1716 CB ALA A 386 1989 3008 1845 -304 -293 516 C ATOM 1717 N GLN A 387 39.391 -33.631 11.740 1.00 16.86 N ANISOU 1717 N GLN A 387 1737 2926 1745 -394 -359 717 N ATOM 1718 CA GLN A 387 38.489 -34.716 12.154 1.00 16.35 C ANISOU 1718 CA GLN A 387 1652 2848 1712 -400 -374 750 C ATOM 1719 C GLN A 387 38.037 -34.489 13.586 1.00 21.57 C ANISOU 1719 C GLN A 387 2297 3622 2276 -511 -402 777 C ATOM 1720 O GLN A 387 36.902 -34.792 13.950 1.00 19.04 O ANISOU 1720 O GLN A 387 1990 3307 1937 -528 -399 747 O ATOM 1721 CB GLN A 387 39.159 -36.090 12.037 1.00 21.61 C ANISOU 1721 CB GLN A 387 2249 3464 2497 -363 -388 871 C ATOM 1722 CG GLN A 387 39.363 -36.587 10.609 1.00 23.28 C ANISOU 1722 CG GLN A 387 2487 3545 2813 -256 -344 833 C ATOM 1723 CD GLN A 387 38.097 -37.126 9.961 1.00 22.78 C ANISOU 1723 CD GLN A 387 2476 3406 2772 -213 -325 752 C ATOM 1724 OE1 GLN A 387 37.000 -36.993 10.499 1.00 25.82 O ANISOU 1724 OE1 GLN A 387 2880 3832 3099 -251 -342 716 O ATOM 1725 NE2 GLN A 387 38.248 -37.734 8.787 1.00 20.88 N ANISOU 1725 NE2 GLN A 387 2262 3052 2618 -138 -285 726 N ATOM 1726 N ASN A 388 38.933 -33.962 14.406 1.00 25.06 N ANISOU 1726 N ASN A 388 2712 4157 2654 -596 -427 838 N ATOM 1727 CA ASN A 388 38.592 -33.727 15.796 1.00 26.66 C ANISOU 1727 CA ASN A 388 2907 4474 2748 -723 -450 864 C ATOM 1728 C ASN A 388 37.600 -32.583 15.931 1.00 26.15 C ANISOU 1728 C ASN A 388 2921 4427 2588 -752 -400 720 C ATOM 1729 O ASN A 388 36.671 -32.642 16.745 1.00 22.72 O ANISOU 1729 O ASN A 388 2498 4038 2096 -815 -390 698 O ATOM 1730 CB ASN A 388 39.841 -33.443 16.624 1.00 32.80 C ANISOU 1730 CB ASN A 388 3641 5351 3472 -825 -495 974 C ATOM 1731 CG ASN A 388 39.714 -33.960 18.033 1.00 44.84 C ANISOU 1731 CG ASN A 388 5119 6985 4933 -956 -544 1075 C ATOM 1732 OD1 ASN A 388 39.682 -35.171 18.261 1.00 53.11 O ANISOU 1732 OD1 ASN A 388 6097 8023 6060 -946 -581 1184 O ATOM 1733 ND2 ASN A 388 39.618 -33.048 18.991 1.00 49.93 N ANISOU 1733 ND2 ASN A 388 5805 7734 5433 -1086 -540 1038 N ATOM 1734 N LEU A 389 37.798 -31.539 15.131 1.00 20.06 N ANISOU 1734 N LEU A 389 2198 3616 1808 -707 -361 626 N ATOM 1735 CA LEU A 389 36.840 -30.441 15.083 1.00 18.84 C ANISOU 1735 CA LEU A 389 2109 3454 1596 -717 -302 491 C ATOM 1736 C LEU A 389 35.473 -30.962 14.664 1.00 21.06 C ANISOU 1736 C LEU A 389 2404 3666 1932 -654 -278 442 C ATOM 1737 O LEU A 389 34.459 -30.620 15.275 1.00 20.18 O ANISOU 1737 O LEU A 389 2316 3578 1774 -701 -242 388 O ATOM 1738 CB LEU A 389 37.304 -29.350 14.113 1.00 23.36 C ANISOU 1738 CB LEU A 389 2718 3981 2178 -662 -271 412 C ATOM 1739 CG LEU A 389 36.553 -28.012 14.155 1.00 22.90 C ANISOU 1739 CG LEU A 389 2716 3920 2065 -686 -205 285 C ATOM 1740 CD1 LEU A 389 36.859 -27.259 15.434 1.00 23.84 C ANISOU 1740 CD1 LEU A 389 2854 4140 2064 -821 -190 277 C ATOM 1741 CD2 LEU A 389 36.912 -27.155 12.947 1.00 27.46 C ANISOU 1741 CD2 LEU A 389 3316 4434 2684 -608 -184 220 C ATOM 1742 N ARG A 390 35.451 -31.785 13.619 1.00 16.93 N ANISOU 1742 N ARG A 390 1867 3055 1509 -555 -294 463 N ATOM 1743 CA ARG A 390 34.204 -32.380 13.125 1.00 14.74 C ANISOU 1743 CA ARG A 390 1603 2709 1287 -500 -283 430 C ATOM 1744 C ARG A 390 33.516 -33.248 14.190 1.00 20.76 C ANISOU 1744 C ARG A 390 2335 3519 2034 -555 -305 489 C ATOM 1745 O ARG A 390 32.302 -33.180 14.372 1.00 24.51 O ANISOU 1745 O ARG A 390 2829 3983 2501 -560 -281 444 O ATOM 1746 CB ARG A 390 34.474 -33.259 11.898 1.00 14.25 C ANISOU 1746 CB ARG A 390 1537 2550 1326 -404 -299 453 C ATOM 1747 CG ARG A 390 33.205 -33.900 11.313 1.00 13.98 C ANISOU 1747 CG ARG A 390 1523 2443 1344 -358 -295 424 C ATOM 1748 CD ARG A 390 33.534 -35.135 10.459 1.00 17.97 C ANISOU 1748 CD ARG A 390 2019 2866 1941 -293 -314 470 C ATOM 1749 NE ARG A 390 34.447 -36.022 11.179 1.00 20.37 N ANISOU 1749 NE ARG A 390 2262 3205 2274 -315 -343 580 N ATOM 1750 CZ ARG A 390 34.106 -36.744 12.240 1.00 27.23 C ANISOU 1750 CZ ARG A 390 3085 4126 3136 -364 -374 652 C ATOM 1751 NH1 ARG A 390 32.858 -36.712 12.688 1.00 24.30 N ANISOU 1751 NH1 ARG A 390 2730 3775 2730 -391 -374 620 N ATOM 1752 NH2 ARG A 390 35.011 -37.507 12.851 1.00 27.44 N ANISOU 1752 NH2 ARG A 390 3044 4184 3198 -389 -405 767 N ATOM 1753 N GLU A 391 34.292 -34.092 14.861 1.00 21.85 N ANISOU 1753 N GLU A 391 2418 3707 2177 -595 -353 601 N ATOM 1754 CA GLU A 391 33.719 -35.027 15.832 1.00 20.87 C ANISOU 1754 CA GLU A 391 2253 3630 2046 -647 -384 673 C ATOM 1755 C GLU A 391 33.032 -34.278 16.962 1.00 25.52 C ANISOU 1755 C GLU A 391 2867 4306 2523 -749 -355 627 C ATOM 1756 O GLU A 391 31.967 -34.682 17.436 1.00 25.74 O ANISOU 1756 O GLU A 391 2893 4342 2545 -767 -348 623 O ATOM 1757 CB GLU A 391 34.787 -35.970 16.402 1.00 27.28 C ANISOU 1757 CB GLU A 391 2989 4488 2889 -685 -443 817 C ATOM 1758 CG GLU A 391 34.171 -37.089 17.250 1.00 31.32 C ANISOU 1758 CG GLU A 391 3449 5036 3416 -726 -482 902 C ATOM 1759 CD GLU A 391 32.924 -37.678 16.591 1.00 42.34 C ANISOU 1759 CD GLU A 391 4870 6342 4876 -645 -466 850 C ATOM 1760 OE1 GLU A 391 33.065 -38.179 15.458 1.00 39.33 O ANISOU 1760 OE1 GLU A 391 4496 5856 4591 -549 -460 840 O ATOM 1761 OE2 GLU A 391 31.811 -37.635 17.189 1.00 39.59 O ANISOU 1761 OE2 GLU A 391 4536 6026 4481 -683 -455 820 O ATOM 1762 N ARG A 392 33.649 -33.179 17.385 1.00 28.50 N ANISOU 1762 N ARG A 392 3270 4745 2813 -819 -332 591 N ATOM 1763 CA ARG A 392 33.099 -32.342 18.447 1.00 33.30 C ANISOU 1763 CA ARG A 392 3914 5430 3307 -927 -285 532 C ATOM 1764 C ARG A 392 31.817 -31.642 18.017 1.00 22.70 C ANISOU 1764 C ARG A 392 2622 4020 1981 -880 -207 410 C ATOM 1765 O ARG A 392 30.850 -31.577 18.776 1.00 23.02 O ANISOU 1765 O ARG A 392 2676 4090 1982 -933 -167 382 O ATOM 1766 CB ARG A 392 34.124 -31.293 18.885 1.00 45.57 C ANISOU 1766 CB ARG A 392 5494 7054 4767 -1015 -274 515 C ATOM 1767 CG ARG A 392 35.326 -31.843 19.614 1.00 64.15 C ANISOU 1767 CG ARG A 392 7793 9499 7082 -1102 -350 651 C ATOM 1768 CD ARG A 392 35.085 -31.871 21.110 1.00 82.88 C ANISOU 1768 CD ARG A 392 10166 11993 9333 -1263 -355 685 C ATOM 1769 NE ARG A 392 36.201 -32.483 21.821 1.00 93.99 N ANISOU 1769 NE ARG A 392 11509 13493 10711 -1358 -442 841 N ATOM 1770 CZ ARG A 392 36.441 -33.788 21.834 1.00100.93 C ANISOU 1770 CZ ARG A 392 12302 14368 11678 -1328 -512 978 C ATOM 1771 NH1 ARG A 392 35.642 -34.611 21.166 1.00101.93 N ANISOU 1771 NH1 ARG A 392 12411 14403 11916 -1207 -506 965 N ATOM 1772 NH2 ARG A 392 37.477 -34.271 22.506 1.00103.72 N ANISOU 1772 NH2 ARG A 392 12586 14807 12015 -1422 -590 1133 N ATOM 1773 N ALA A 393 31.815 -31.084 16.814 1.00 17.69 N ANISOU 1773 N ALA A 393 2013 3299 1410 -785 -182 345 N ATOM 1774 CA ALA A 393 30.610 -30.438 16.301 1.00 20.38 C ANISOU 1774 CA ALA A 393 2387 3569 1789 -737 -115 251 C ATOM 1775 C ALA A 393 29.467 -31.449 16.173 1.00 19.05 C ANISOU 1775 C ALA A 393 2197 3357 1684 -693 -133 285 C ATOM 1776 O ALA A 393 28.315 -31.148 16.481 1.00 23.18 O ANISOU 1776 O ALA A 393 2732 3866 2211 -705 -79 242 O ATOM 1777 CB ALA A 393 30.890 -29.781 14.942 1.00 17.95 C ANISOU 1777 CB ALA A 393 2098 3178 1542 -648 -104 197 C ATOM 1778 N LEU A 394 29.791 -32.646 15.695 1.00 15.74 N ANISOU 1778 N LEU A 394 1746 2910 1325 -640 -202 363 N ATOM 1779 CA LEU A 394 28.793 -33.695 15.523 1.00 21.40 C ANISOU 1779 CA LEU A 394 2443 3583 2104 -600 -228 402 C ATOM 1780 C LEU A 394 28.218 -34.086 16.873 1.00 21.77 C ANISOU 1780 C LEU A 394 2467 3709 2095 -683 -226 440 C ATOM 1781 O LEU A 394 27.007 -34.203 17.038 1.00 20.87 O ANISOU 1781 O LEU A 394 2356 3574 2000 -677 -200 425 O ATOM 1782 CB LEU A 394 29.414 -34.925 14.856 1.00 20.78 C ANISOU 1782 CB LEU A 394 2336 3461 2097 -541 -294 478 C ATOM 1783 CG LEU A 394 28.492 -36.138 14.723 1.00 19.40 C ANISOU 1783 CG LEU A 394 2141 3242 1986 -507 -328 527 C ATOM 1784 CD1 LEU A 394 27.281 -35.837 13.831 1.00 17.24 C ANISOU 1784 CD1 LEU A 394 1905 2887 1758 -454 -302 466 C ATOM 1785 CD2 LEU A 394 29.257 -37.370 14.206 1.00 18.44 C ANISOU 1785 CD2 LEU A 394 1991 3077 1939 -461 -380 603 C ATOM 1786 N GLN A 395 29.108 -34.297 17.838 1.00 18.06 N ANISOU 1786 N GLN A 395 1972 3333 1557 -767 -256 500 N ATOM 1787 CA GLN A 395 28.705 -34.685 19.184 1.00 23.89 C ANISOU 1787 CA GLN A 395 2688 4164 2227 -866 -261 546 C ATOM 1788 C GLN A 395 27.778 -33.636 19.787 1.00 27.99 C ANISOU 1788 C GLN A 395 3252 4702 2680 -922 -168 450 C ATOM 1789 O GLN A 395 26.795 -33.971 20.448 1.00 29.63 O ANISOU 1789 O GLN A 395 3452 4932 2876 -954 -148 458 O ATOM 1790 CB GLN A 395 29.949 -34.887 20.068 1.00 24.80 C ANISOU 1790 CB GLN A 395 2769 4383 2269 -965 -311 630 C ATOM 1791 CG GLN A 395 29.699 -34.731 21.561 1.00 43.24 C ANISOU 1791 CG GLN A 395 5106 6839 4486 -1110 -296 646 C ATOM 1792 CD GLN A 395 29.108 -35.975 22.182 1.00 56.66 C ANISOU 1792 CD GLN A 395 6749 8571 6207 -1131 -347 740 C ATOM 1793 OE1 GLN A 395 28.690 -36.893 21.476 1.00 59.24 O ANISOU 1793 OE1 GLN A 395 7045 8821 6644 -1030 -383 778 O ATOM 1794 NE2 GLN A 395 29.073 -36.016 23.511 1.00 63.90 N ANISOU 1794 NE2 GLN A 395 7655 9607 7016 -1271 -351 779 N ATOM 1795 N ARG A 396 28.078 -32.365 19.546 1.00 25.12 N ANISOU 1795 N ARG A 396 2935 4327 2284 -932 -105 359 N ATOM 1796 CA ARG A 396 27.244 -31.295 20.074 1.00 29.35 C ANISOU 1796 CA ARG A 396 3513 4864 2773 -983 3 262 C ATOM 1797 C ARG A 396 25.869 -31.271 19.416 1.00 28.62 C ANISOU 1797 C ARG A 396 3420 4674 2781 -895 48 226 C ATOM 1798 O ARG A 396 24.863 -31.063 20.084 1.00 29.42 O ANISOU 1798 O ARG A 396 3528 4780 2869 -934 118 197 O ATOM 1799 CB ARG A 396 27.932 -29.936 19.944 1.00 26.96 C ANISOU 1799 CB ARG A 396 3257 4563 2423 -1014 63 175 C ATOM 1800 CG ARG A 396 29.233 -29.839 20.759 1.00 37.60 C ANISOU 1800 CG ARG A 396 4611 6021 3656 -1127 24 214 C ATOM 1801 CD ARG A 396 29.711 -28.405 20.913 1.00 36.97 C ANISOU 1801 CD ARG A 396 4588 5953 3507 -1188 100 117 C ATOM 1802 NE ARG A 396 29.789 -27.709 19.636 1.00 39.21 N ANISOU 1802 NE ARG A 396 4880 6137 3880 -1075 121 59 N ATOM 1803 CZ ARG A 396 30.877 -27.659 18.873 1.00 39.09 C ANISOU 1803 CZ ARG A 396 4855 6111 3888 -1026 60 88 C ATOM 1804 NH1 ARG A 396 31.994 -28.272 19.254 1.00 38.95 N ANISOU 1804 NH1 ARG A 396 4811 6168 3819 -1077 -23 182 N ATOM 1805 NH2 ARG A 396 30.845 -26.997 17.724 1.00 28.17 N ANISOU 1805 NH2 ARG A 396 3481 4640 2582 -931 84 32 N ATOM 1806 N LEU A 397 25.823 -31.487 18.109 1.00 21.22 N ANISOU 1806 N LEU A 397 2474 3647 1944 -783 10 235 N ATOM 1807 CA LEU A 397 24.546 -31.486 17.400 1.00 18.68 C ANISOU 1807 CA LEU A 397 2145 3233 1718 -709 37 220 C ATOM 1808 C LEU A 397 23.713 -32.702 17.779 1.00 21.92 C ANISOU 1808 C LEU A 397 2522 3650 2155 -704 -7 296 C ATOM 1809 O LEU A 397 22.509 -32.596 17.976 1.00 25.86 O ANISOU 1809 O LEU A 397 3015 4119 2691 -700 43 287 O ATOM 1810 CB LEU A 397 24.765 -31.437 15.887 1.00 17.36 C ANISOU 1810 CB LEU A 397 1983 2978 1636 -611 -1 216 C ATOM 1811 CG LEU A 397 23.515 -31.430 15.004 1.00 20.81 C ANISOU 1811 CG LEU A 397 2412 3322 2175 -544 11 217 C ATOM 1812 CD1 LEU A 397 22.604 -30.273 15.384 1.00 25.93 C ANISOU 1812 CD1 LEU A 397 3062 3947 2842 -567 121 157 C ATOM 1813 CD2 LEU A 397 23.902 -31.358 13.515 1.00 18.44 C ANISOU 1813 CD2 LEU A 397 2122 2949 1934 -471 -33 212 C ATOM 1814 N MET A 398 24.360 -33.859 17.886 1.00 22.96 N ANISOU 1814 N MET A 398 2627 3818 2277 -705 -98 376 N ATOM 1815 CA MET A 398 23.660 -35.090 18.225 1.00 21.45 C ANISOU 1815 CA MET A 398 2399 3634 2115 -700 -150 455 C ATOM 1816 C MET A 398 23.083 -35.028 19.642 1.00 23.69 C ANISOU 1816 C MET A 398 2675 4001 2325 -794 -104 460 C ATOM 1817 O MET A 398 22.017 -35.572 19.913 1.00 21.79 O ANISOU 1817 O MET A 398 2413 3749 2117 -787 -104 493 O ATOM 1818 CB MET A 398 24.587 -36.292 18.087 1.00 23.83 C ANISOU 1818 CB MET A 398 2668 3954 2434 -686 -247 543 C ATOM 1819 CG MET A 398 24.968 -36.632 16.648 1.00 22.44 C ANISOU 1819 CG MET A 398 2503 3682 2343 -590 -287 544 C ATOM 1820 SD MET A 398 23.544 -37.152 15.663 1.00 26.05 S ANISOU 1820 SD MET A 398 2969 4034 2897 -513 -300 548 S ATOM 1821 CE MET A 398 23.227 -35.692 14.676 1.00 19.36 C ANISOU 1821 CE MET A 398 2166 3121 2070 -477 -233 452 C ATOM 1822 N THR A 399 23.790 -34.365 20.544 1.00 22.05 N ANISOU 1822 N THR A 399 2486 3879 2013 -891 -66 428 N ATOM 1823 CA THR A 399 23.293 -34.234 21.906 1.00 27.79 C ANISOU 1823 CA THR A 399 3216 4690 2652 -1000 -12 421 C ATOM 1824 C THR A 399 21.955 -33.502 21.885 1.00 29.58 C ANISOU 1824 C THR A 399 3464 4854 2921 -978 98 350 C ATOM 1825 O THR A 399 21.000 -33.899 22.554 1.00 32.04 O ANISOU 1825 O THR A 399 3759 5183 3232 -1005 123 374 O ATOM 1826 CB THR A 399 24.293 -33.494 22.800 1.00 28.50 C ANISOU 1826 CB THR A 399 3338 4879 2613 -1124 19 387 C ATOM 1827 OG1 THR A 399 25.489 -34.274 22.908 1.00 28.74 O ANISOU 1827 OG1 THR A 399 3332 4973 2617 -1151 -89 481 O ATOM 1828 CG2 THR A 399 23.705 -33.277 24.193 1.00 32.71 C ANISOU 1828 CG2 THR A 399 3888 5496 3042 -1252 91 364 C ATOM 1829 N SER A 400 21.891 -32.446 21.084 1.00 25.07 N ANISOU 1829 N SER A 400 2923 4204 2399 -925 163 271 N ATOM 1830 CA SER A 400 20.683 -31.647 20.950 1.00 26.29 C ANISOU 1830 CA SER A 400 3086 4282 2620 -898 274 212 C ATOM 1831 C SER A 400 19.544 -32.430 20.277 1.00 27.06 C ANISOU 1831 C SER A 400 3143 4304 2835 -808 232 280 C ATOM 1832 O SER A 400 18.388 -32.398 20.728 1.00 26.40 O ANISOU 1832 O SER A 400 3044 4200 2787 -815 298 286 O ATOM 1833 CB SER A 400 21.012 -30.380 20.160 1.00 36.50 C ANISOU 1833 CB SER A 400 4408 5509 3951 -861 338 129 C ATOM 1834 OG SER A 400 19.945 -29.461 20.209 1.00 42.81 O ANISOU 1834 OG SER A 400 5210 6239 4816 -852 466 73 O ATOM 1835 N VAL A 401 19.867 -33.124 19.191 1.00 17.76 N ANISOU 1835 N VAL A 401 1949 3081 1717 -728 127 332 N ATOM 1836 CA VAL A 401 18.885 -33.982 18.520 1.00 17.71 C ANISOU 1836 CA VAL A 401 1912 3008 1808 -657 70 403 C ATOM 1837 C VAL A 401 18.370 -35.041 19.483 1.00 20.83 C ANISOU 1837 C VAL A 401 2277 3463 2176 -696 36 473 C ATOM 1838 O VAL A 401 17.161 -35.252 19.601 1.00 24.48 O ANISOU 1838 O VAL A 401 2716 3892 2695 -679 60 506 O ATOM 1839 CB VAL A 401 19.469 -34.668 17.268 1.00 20.00 C ANISOU 1839 CB VAL A 401 2203 3249 2146 -585 -36 441 C ATOM 1840 CG1 VAL A 401 18.508 -35.753 16.749 1.00 20.53 C ANISOU 1840 CG1 VAL A 401 2245 3264 2293 -536 -105 521 C ATOM 1841 CG2 VAL A 401 19.755 -33.635 16.189 1.00 16.11 C ANISOU 1841 CG2 VAL A 401 1735 2690 1695 -542 -4 381 C ATOM 1842 N THR A 402 19.285 -35.689 20.196 1.00 24.80 N ANISOU 1842 N THR A 402 2772 4056 2594 -753 -21 505 N ATOM 1843 CA THR A 402 18.888 -36.738 21.135 1.00 26.93 C ANISOU 1843 CA THR A 402 3004 4392 2834 -798 -65 582 C ATOM 1844 C THR A 402 18.003 -36.194 22.262 1.00 25.92 C ANISOU 1844 C THR A 402 2882 4307 2661 -870 41 549 C ATOM 1845 O THR A 402 17.083 -36.864 22.713 1.00 27.15 O ANISOU 1845 O THR A 402 3007 4472 2839 -874 31 605 O ATOM 1846 CB THR A 402 20.102 -37.478 21.735 1.00 32.04 C ANISOU 1846 CB THR A 402 3632 5135 3407 -858 -146 638 C ATOM 1847 OG1 THR A 402 20.872 -38.069 20.681 1.00 32.43 O ANISOU 1847 OG1 THR A 402 3673 5132 3518 -785 -230 672 O ATOM 1848 CG2 THR A 402 19.634 -38.578 22.669 1.00 33.98 C ANISOU 1848 CG2 THR A 402 3830 5448 3634 -905 -196 727 C ATOM 1849 N ASN A 403 18.270 -34.969 22.701 1.00 28.11 N ANISOU 1849 N ASN A 403 3201 4604 2875 -930 150 455 N ATOM 1850 CA ASN A 403 17.461 -34.349 23.747 1.00 28.31 C ANISOU 1850 CA ASN A 403 3241 4657 2858 -1004 276 406 C ATOM 1851 C ASN A 403 16.008 -34.104 23.327 1.00 34.31 C ANISOU 1851 C ASN A 403 3982 5316 3741 -932 348 409 C ATOM 1852 O ASN A 403 15.124 -33.958 24.168 1.00 40.11 O ANISOU 1852 O ASN A 403 4712 6064 4466 -977 439 400 O ATOM 1853 CB ASN A 403 18.098 -33.038 24.210 1.00 24.49 C ANISOU 1853 CB ASN A 403 2815 4202 2288 -1085 388 295 C ATOM 1854 CG ASN A 403 19.279 -33.261 25.130 1.00 35.85 C ANISOU 1854 CG ASN A 403 4272 5772 3576 -1206 340 304 C ATOM 1855 OD1 ASN A 403 19.528 -34.377 25.585 1.00 42.19 O ANISOU 1855 OD1 ASN A 403 5038 6651 4341 -1239 237 398 O ATOM 1856 ND2 ASN A 403 20.012 -32.197 25.409 1.00 36.49 N ANISOU 1856 ND2 ASN A 403 4408 5881 3577 -1279 413 216 N ATOM 1857 N ARG A 404 15.762 -34.062 22.025 1.00 23.71 N ANISOU 1857 N ARG A 404 2625 3871 2514 -826 307 428 N ATOM 1858 CA ARG A 404 14.420 -33.804 21.531 1.00 30.72 C ANISOU 1858 CA ARG A 404 3484 4659 3528 -761 363 451 C ATOM 1859 C ARG A 404 13.954 -34.882 20.570 1.00 24.93 C ANISOU 1859 C ARG A 404 2714 3873 2884 -679 235 552 C ATOM 1860 O ARG A 404 13.098 -34.626 19.732 1.00 25.09 O ANISOU 1860 O ARG A 404 2714 3800 3019 -616 247 582 O ATOM 1861 CB ARG A 404 14.369 -32.442 20.828 1.00 35.35 C ANISOU 1861 CB ARG A 404 4088 5160 4186 -727 461 377 C ATOM 1862 CG ARG A 404 14.611 -31.262 21.757 1.00 53.84 C ANISOU 1862 CG ARG A 404 6468 7529 6459 -809 616 268 C ATOM 1863 CD ARG A 404 14.570 -29.933 21.012 1.00 64.99 C ANISOU 1863 CD ARG A 404 7888 8847 7958 -769 711 201 C ATOM 1864 NE ARG A 404 13.207 -29.439 20.824 1.00 70.89 N ANISOU 1864 NE ARG A 404 8592 9494 8851 -725 815 224 N ATOM 1865 CZ ARG A 404 12.554 -28.694 21.711 1.00 70.01 C ANISOU 1865 CZ ARG A 404 8485 9362 8756 -774 985 169 C ATOM 1866 NH1 ARG A 404 13.138 -28.359 22.854 1.00 71.38 N ANISOU 1866 NH1 ARG A 404 8716 9616 8791 -878 1067 78 N ATOM 1867 NH2 ARG A 404 11.318 -28.287 21.457 1.00 67.33 N ANISOU 1867 NH2 ARG A 404 8092 8918 8571 -725 1078 209 N ATOM 1868 N CYS A 405 14.496 -36.089 20.680 1.00 27.42 N ANISOU 1868 N CYS A 405 3362 3499 3559 -754 13 176 N ATOM 1869 CA CYS A 405 14.223 -37.063 19.632 1.00 25.04 C ANISOU 1869 CA CYS A 405 3009 3238 3266 -679 -27 221 C ATOM 1870 C CYS A 405 12.766 -37.507 19.563 1.00 22.97 C ANISOU 1870 C CYS A 405 2748 2959 3018 -663 26 211 C ATOM 1871 O CYS A 405 12.266 -37.774 18.479 1.00 26.74 O ANISOU 1871 O CYS A 405 3169 3452 3539 -602 24 252 O ATOM 1872 CB CYS A 405 15.198 -38.245 19.641 1.00 36.02 C ANISOU 1872 CB CYS A 405 4417 4675 4593 -674 -127 252 C ATOM 1873 SG CYS A 405 15.286 -39.144 21.160 1.00 52.64 S ANISOU 1873 SG CYS A 405 6621 6780 6602 -766 -166 219 S ATOM 1874 N GLN A 406 12.074 -37.567 20.699 1.00 21.43 N ANISOU 1874 N GLN A 406 2622 2731 2789 -725 75 159 N ATOM 1875 CA GLN A 406 10.649 -37.900 20.664 1.00 26.95 C ANISOU 1875 CA GLN A 406 3320 3406 3513 -709 132 154 C ATOM 1876 C GLN A 406 9.853 -36.910 19.802 1.00 22.38 C ANISOU 1876 C GLN A 406 2663 2786 3056 -667 208 178 C ATOM 1877 O GLN A 406 9.028 -37.300 18.980 1.00 24.39 O ANISOU 1877 O GLN A 406 2872 3042 3352 -619 211 224 O ATOM 1878 CB GLN A 406 10.051 -37.937 22.071 1.00 36.02 C ANISOU 1878 CB GLN A 406 4555 4518 4614 -789 188 88 C ATOM 1879 CG GLN A 406 8.541 -38.110 22.057 1.00 51.23 C ANISOU 1879 CG GLN A 406 6475 6407 6585 -772 263 84 C ATOM 1880 CD GLN A 406 8.020 -38.815 23.292 1.00 67.52 C ANISOU 1880 CD GLN A 406 8626 8463 8565 -838 276 34 C ATOM 1881 OE1 GLN A 406 7.891 -38.213 24.360 1.00 73.14 O ANISOU 1881 OE1 GLN A 406 9400 9129 9261 -919 348 -32 O ATOM 1882 NE2 GLN A 406 7.710 -40.100 23.150 1.00 70.51 N ANISOU 1882 NE2 GLN A 406 9014 8887 8888 -808 207 63 N ATOM 1883 N GLU A 407 10.097 -35.626 20.017 1.00 22.82 N ANISOU 1883 N GLU A 407 2701 2799 3170 -695 266 151 N ATOM 1884 CA GLU A 407 9.430 -34.586 19.254 1.00 24.94 C ANISOU 1884 CA GLU A 407 2884 3022 3568 -666 334 176 C ATOM 1885 C GLU A 407 9.823 -34.675 17.776 1.00 21.16 C ANISOU 1885 C GLU A 407 2320 2590 3128 -600 266 251 C ATOM 1886 O GLU A 407 8.982 -34.561 16.889 1.00 23.54 O ANISOU 1886 O GLU A 407 2556 2875 3513 -569 287 302 O ATOM 1887 CB GLU A 407 9.805 -33.212 19.822 1.00 33.02 C ANISOU 1887 CB GLU A 407 3909 3998 4641 -712 400 129 C ATOM 1888 CG GLU A 407 9.229 -32.039 19.050 1.00 46.97 C ANISOU 1888 CG GLU A 407 5573 5715 6557 -687 465 156 C ATOM 1889 CD GLU A 407 9.544 -30.695 19.695 1.00 61.37 C ANISOU 1889 CD GLU A 407 7402 7485 8431 -734 537 103 C ATOM 1890 OE1 GLU A 407 10.162 -30.674 20.783 1.00 58.71 O ANISOU 1890 OE1 GLU A 407 7159 7147 8002 -794 541 44 O ATOM 1891 OE2 GLU A 407 9.167 -29.658 19.111 1.00 68.09 O ANISOU 1891 OE2 GLU A 407 8163 8294 9415 -719 587 124 O ATOM 1892 N LEU A 408 11.107 -34.885 17.511 1.00 19.38 N ANISOU 1892 N LEU A 408 2098 2420 2845 -587 186 262 N ATOM 1893 CA LEU A 408 11.587 -34.946 16.130 1.00 17.93 C ANISOU 1893 CA LEU A 408 1841 2281 2691 -534 128 325 C ATOM 1894 C LEU A 408 11.095 -36.190 15.397 1.00 19.60 C ANISOU 1894 C LEU A 408 2053 2527 2869 -497 87 370 C ATOM 1895 O LEU A 408 10.653 -36.113 14.249 1.00 18.11 O ANISOU 1895 O LEU A 408 1802 2344 2736 -470 82 426 O ATOM 1896 CB LEU A 408 13.115 -34.882 16.100 1.00 16.32 C ANISOU 1896 CB LEU A 408 1644 2119 2438 -530 60 325 C ATOM 1897 CG LEU A 408 13.691 -33.577 16.656 1.00 20.94 C ANISOU 1897 CG LEU A 408 2225 2674 3056 -563 89 294 C ATOM 1898 CD1 LEU A 408 15.212 -33.641 16.758 1.00 20.52 C ANISOU 1898 CD1 LEU A 408 2191 2659 2948 -564 14 304 C ATOM 1899 CD2 LEU A 408 13.265 -32.407 15.796 1.00 25.62 C ANISOU 1899 CD2 LEU A 408 2724 3243 3768 -544 130 321 C ATOM 1900 N ALA A 409 11.179 -37.337 16.058 1.00 19.05 N ANISOU 1900 N ALA A 409 2054 2480 2706 -505 53 349 N ATOM 1901 CA ALA A 409 10.761 -38.601 15.452 1.00 24.73 C ANISOU 1901 CA ALA A 409 2781 3233 3382 -471 10 387 C ATOM 1902 C ALA A 409 9.300 -38.602 15.011 1.00 22.83 C ANISOU 1902 C ALA A 409 2516 2959 3200 -462 56 424 C ATOM 1903 O ALA A 409 8.956 -39.202 13.997 1.00 19.89 O ANISOU 1903 O ALA A 409 2121 2609 2828 -433 26 481 O ATOM 1904 CB ALA A 409 11.014 -39.753 16.409 1.00 26.27 C ANISOU 1904 CB ALA A 409 3052 3452 3478 -489 -32 354 C ATOM 1905 N THR A 410 8.441 -37.936 15.781 1.00 17.75 N ANISOU 1905 N THR A 410 1879 2255 2608 -492 133 395 N ATOM 1906 CA THR A 410 7.016 -37.925 15.493 1.00 17.64 C ANISOU 1906 CA THR A 410 1841 2196 2665 -487 182 436 C ATOM 1907 C THR A 410 6.598 -36.812 14.523 1.00 17.98 C ANISOU 1907 C THR A 410 1789 2200 2841 -484 218 492 C ATOM 1908 O THR A 410 5.446 -36.759 14.096 1.00 20.76 O ANISOU 1908 O THR A 410 2106 2510 3273 -484 250 548 O ATOM 1909 CB THR A 410 6.170 -37.797 16.790 1.00 17.15 C ANISOU 1909 CB THR A 410 1829 2078 2610 -524 259 381 C ATOM 1910 OG1 THR A 410 6.607 -36.654 17.530 1.00 24.10 O ANISOU 1910 OG1 THR A 410 2711 2920 3528 -563 320 320 O ATOM 1911 CG2 THR A 410 6.333 -39.031 17.668 1.00 16.31 C ANISOU 1911 CG2 THR A 410 1810 2011 2376 -534 213 342 C ATOM 1912 N ASN A 411 7.534 -35.944 14.164 1.00 21.78 N ANISOU 1912 N ASN A 411 2226 2695 3353 -486 207 484 N ATOM 1913 CA ASN A 411 7.227 -34.790 13.314 1.00 22.33 C ANISOU 1913 CA ASN A 411 2198 2730 3555 -492 235 533 C ATOM 1914 C ASN A 411 7.209 -35.091 11.817 1.00 20.06 C ANISOU 1914 C ASN A 411 1858 2481 3285 -477 173 620 C ATOM 1915 O ASN A 411 8.024 -35.859 11.318 1.00 17.13 O ANISOU 1915 O ASN A 411 1514 2175 2820 -457 106 626 O ATOM 1916 CB ASN A 411 8.231 -33.673 13.582 1.00 17.66 C ANISOU 1916 CB ASN A 411 1582 2139 2990 -504 246 488 C ATOM 1917 CG ASN A 411 7.929 -32.430 12.795 1.00 25.21 C ANISOU 1917 CG ASN A 411 2430 3058 4090 -514 273 535 C ATOM 1918 OD1 ASN A 411 7.002 -31.676 13.115 1.00 25.54 O ANISOU 1918 OD1 ASN A 411 2431 3024 4248 -537 352 537 O ATOM 1919 ND2 ASN A 411 8.706 -32.202 11.756 1.00 17.16 N ANISOU 1919 ND2 ASN A 411 1358 2089 3072 -501 209 575 N ATOM 1920 N GLU A 412 6.306 -34.425 11.103 1.00 18.25 N ANISOU 1920 N GLU A 412 1548 2203 3181 -496 200 691 N ATOM 1921 CA GLU A 412 6.102 -34.637 9.677 1.00 17.60 C ANISOU 1921 CA GLU A 412 1417 2146 3123 -505 145 785 C ATOM 1922 C GLU A 412 7.363 -34.484 8.824 1.00 18.43 C ANISOU 1922 C GLU A 412 1499 2320 3182 -499 82 786 C ATOM 1923 O GLU A 412 7.476 -35.117 7.775 1.00 18.78 O ANISOU 1923 O GLU A 412 1546 2407 3182 -504 28 840 O ATOM 1924 CB GLU A 412 5.017 -33.685 9.155 1.00 19.45 C ANISOU 1924 CB GLU A 412 1554 2308 3528 -542 183 864 C ATOM 1925 CG GLU A 412 5.376 -32.223 9.296 1.00 20.56 C ANISOU 1925 CG GLU A 412 1614 2416 3784 -558 222 840 C ATOM 1926 CD GLU A 412 4.239 -31.295 8.880 1.00 31.71 C ANISOU 1926 CD GLU A 412 2918 3743 5386 -599 265 921 C ATOM 1927 OE1 GLU A 412 3.400 -31.721 8.066 1.00 26.90 O ANISOU 1927 OE1 GLU A 412 2285 3118 4816 -624 236 1021 O ATOM 1928 OE2 GLU A 412 4.197 -30.144 9.361 1.00 30.19 O ANISOU 1928 OE2 GLU A 412 2667 3496 5309 -610 328 889 O ATOM 1929 N TYR A 413 8.301 -33.644 9.258 1.00 15.87 N ANISOU 1929 N TYR A 413 1156 2004 2870 -491 91 729 N ATOM 1930 CA TYR A 413 9.542 -33.449 8.511 1.00 19.24 C ANISOU 1930 CA TYR A 413 1558 2493 3258 -482 35 730 C ATOM 1931 C TYR A 413 10.785 -33.980 9.220 1.00 23.48 C ANISOU 1931 C TYR A 413 2166 3074 3680 -449 10 658 C ATOM 1932 O TYR A 413 11.671 -34.548 8.587 1.00 19.20 O ANISOU 1932 O TYR A 413 1638 2587 3069 -432 -41 666 O ATOM 1933 CB TYR A 413 9.766 -31.965 8.178 1.00 23.70 C ANISOU 1933 CB TYR A 413 2025 3038 3940 -502 45 744 C ATOM 1934 CG TYR A 413 8.661 -31.378 7.335 1.00 23.36 C ANISOU 1934 CG TYR A 413 1894 2953 4030 -544 56 831 C ATOM 1935 CD1 TYR A 413 8.400 -31.876 6.068 1.00 25.69 C ANISOU 1935 CD1 TYR A 413 2169 3277 4314 -572 3 913 C ATOM 1936 CD2 TYR A 413 7.887 -30.325 7.803 1.00 25.89 C ANISOU 1936 CD2 TYR A 413 2149 3196 4491 -566 119 835 C ATOM 1937 CE1 TYR A 413 7.387 -31.349 5.290 1.00 27.39 C ANISOU 1937 CE1 TYR A 413 2302 3450 4657 -626 2 1007 C ATOM 1938 CE2 TYR A 413 6.856 -29.791 7.031 1.00 27.45 C ANISOU 1938 CE2 TYR A 413 2253 3344 4832 -612 125 928 C ATOM 1939 CZ TYR A 413 6.620 -30.308 5.775 1.00 29.80 C ANISOU 1939 CZ TYR A 413 2540 3673 5108 -635 57 1017 C ATOM 1940 OH TYR A 413 5.614 -29.793 4.996 1.00 31.16 O ANISOU 1940 OH TYR A 413 2663 3785 5390 -646 33 1112 O ATOM 1941 N ALA A 414 10.859 -33.779 10.526 1.00 15.93 N ANISOU 1941 N ALA A 414 1255 2089 2709 -449 49 593 N ATOM 1942 CA ALA A 414 12.076 -34.108 11.258 1.00 15.96 C ANISOU 1942 CA ALA A 414 1319 2126 2621 -435 19 537 C ATOM 1943 C ALA A 414 12.269 -35.620 11.355 1.00 15.61 C ANISOU 1943 C ALA A 414 1346 2118 2468 -416 -20 532 C ATOM 1944 O ALA A 414 13.368 -36.087 11.655 1.00 16.85 O ANISOU 1944 O ALA A 414 1539 2308 2557 -403 -61 508 O ATOM 1945 CB ALA A 414 12.050 -33.482 12.636 1.00 17.38 C ANISOU 1945 CB ALA A 414 1536 2260 2809 -459 70 474 C ATOM 1946 N ASN A 415 11.218 -36.388 11.077 1.00 15.00 N ANISOU 1946 N ASN A 415 1285 2033 2383 -415 -12 562 N ATOM 1947 CA ASN A 415 11.354 -37.844 11.142 1.00 16.36 C ANISOU 1947 CA ASN A 415 1521 2239 2455 -397 -52 559 C ATOM 1948 C ASN A 415 12.392 -38.352 10.143 1.00 16.33 C ANISOU 1948 C ASN A 415 1506 2289 2412 -375 -103 581 C ATOM 1949 O ASN A 415 12.989 -39.389 10.349 1.00 15.31 O ANISOU 1949 O ASN A 415 1422 2186 2208 -357 -137 564 O ATOM 1950 CB ASN A 415 10.004 -38.559 10.955 1.00 17.18 C ANISOU 1950 CB ASN A 415 1645 2325 2558 -400 -38 596 C ATOM 1951 CG ASN A 415 9.541 -38.585 9.507 1.00 22.77 C ANISOU 1951 CG ASN A 415 2308 3043 3303 -405 -54 674 C ATOM 1952 OD1 ASN A 415 9.952 -39.443 8.726 1.00 17.60 O ANISOU 1952 OD1 ASN A 415 1672 2430 2586 -393 -95 696 O ATOM 1953 ND2 ASN A 415 8.660 -37.652 9.147 1.00 18.22 N ANISOU 1953 ND2 ASN A 415 1670 2421 2831 -431 -19 719 N ATOM 1954 N TYR A 416 12.600 -37.611 9.058 1.00 16.32 N ANISOU 1954 N TYR A 416 1440 2297 2465 -380 -107 620 N ATOM 1955 CA TYR A 416 13.614 -37.983 8.074 1.00 14.97 C ANISOU 1955 CA TYR A 416 1256 2172 2261 -365 -145 637 C ATOM 1956 C TYR A 416 15.017 -37.851 8.643 1.00 15.66 C ANISOU 1956 C TYR A 416 1352 2275 2325 -345 -166 597 C ATOM 1957 O TYR A 416 15.921 -38.608 8.294 1.00 15.32 O ANISOU 1957 O TYR A 416 1324 2260 2237 -324 -193 595 O ATOM 1958 CB TYR A 416 13.480 -37.122 6.823 1.00 15.26 C ANISOU 1958 CB TYR A 416 1219 2214 2363 -388 -146 689 C ATOM 1959 CG TYR A 416 12.260 -37.481 6.012 1.00 16.47 C ANISOU 1959 CG TYR A 416 1370 2357 2530 -419 -141 749 C ATOM 1960 CD1 TYR A 416 12.288 -38.549 5.137 1.00 17.56 C ANISOU 1960 CD1 TYR A 416 1546 2525 2601 -424 -162 776 C ATOM 1961 CD2 TYR A 416 11.085 -36.754 6.131 1.00 17.54 C ANISOU 1961 CD2 TYR A 416 1467 2446 2751 -448 -114 784 C ATOM 1962 CE1 TYR A 416 11.177 -38.893 4.391 1.00 21.00 C ANISOU 1962 CE1 TYR A 416 1988 2948 3042 -462 -164 841 C ATOM 1963 CE2 TYR A 416 9.959 -37.094 5.400 1.00 24.49 C ANISOU 1963 CE2 TYR A 416 2343 3309 3651 -483 -116 856 C ATOM 1964 CZ TYR A 416 10.016 -38.164 4.528 1.00 26.72 C ANISOU 1964 CZ TYR A 416 2671 3626 3853 -492 -146 886 C ATOM 1965 OH TYR A 416 8.912 -38.503 3.793 1.00 24.73 O ANISOU 1965 OH TYR A 416 2425 3356 3615 -536 -155 966 O ATOM 1966 N ILE A 417 15.199 -36.882 9.527 1.00 15.50 N ANISOU 1966 N ILE A 417 1319 2229 2339 -354 -152 568 N ATOM 1967 CA ILE A 417 16.494 -36.703 10.152 1.00 15.86 C ANISOU 1967 CA ILE A 417 1378 2283 2364 -345 -178 541 C ATOM 1968 C ILE A 417 16.780 -37.879 11.077 1.00 19.49 C ANISOU 1968 C ILE A 417 1909 2744 2752 -344 -200 515 C ATOM 1969 O ILE A 417 17.874 -38.441 11.069 1.00 15.37 O ANISOU 1969 O ILE A 417 1396 2240 2203 -328 -237 518 O ATOM 1970 CB ILE A 417 16.554 -35.394 10.948 1.00 16.57 C ANISOU 1970 CB ILE A 417 1452 2343 2502 -367 -156 518 C ATOM 1971 CG1 ILE A 417 16.421 -34.204 9.991 1.00 22.60 C ANISOU 1971 CG1 ILE A 417 2131 3108 3348 -368 -146 549 C ATOM 1972 CG2 ILE A 417 17.871 -35.324 11.731 1.00 17.01 C ANISOU 1972 CG2 ILE A 417 1537 2402 2523 -368 -192 499 C ATOM 1973 CD1 ILE A 417 16.081 -32.902 10.684 1.00 31.01 C ANISOU 1973 CD1 ILE A 417 3171 4132 4478 -392 -108 527 C ATOM 1974 N ILE A 418 15.784 -38.254 11.868 1.00 18.09 N ANISOU 1974 N ILE A 418 1777 2545 2553 -363 -177 492 N ATOM 1975 CA ILE A 418 15.966 -39.344 12.809 1.00 17.53 C ANISOU 1975 CA ILE A 418 1770 2477 2414 -373 -204 468 C ATOM 1976 C ILE A 418 16.202 -40.649 12.045 1.00 19.80 C ANISOU 1976 C ILE A 418 2062 2795 2664 -342 -236 491 C ATOM 1977 O ILE A 418 17.028 -41.475 12.431 1.00 17.90 O ANISOU 1977 O ILE A 418 1845 2566 2392 -338 -276 487 O ATOM 1978 CB ILE A 418 14.749 -39.472 13.737 1.00 18.37 C ANISOU 1978 CB ILE A 418 1922 2555 2503 -402 -170 439 C ATOM 1979 CG1 ILE A 418 14.547 -38.166 14.520 1.00 15.32 C ANISOU 1979 CG1 ILE A 418 1535 2128 2158 -438 -124 408 C ATOM 1980 CG2 ILE A 418 14.917 -40.667 14.670 1.00 15.19 C ANISOU 1980 CG2 ILE A 418 1583 2162 2028 -418 -209 418 C ATOM 1981 CD1 ILE A 418 15.800 -37.711 15.313 1.00 16.80 C ANISOU 1981 CD1 ILE A 418 1744 2313 2326 -467 -153 388 C ATOM 1982 N GLN A 419 15.471 -40.839 10.955 1.00 16.17 N ANISOU 1982 N GLN A 419 1583 2347 2216 -326 -219 521 N ATOM 1983 CA GLN A 419 15.707 -42.005 10.118 1.00 14.26 C ANISOU 1983 CA GLN A 419 1349 2131 1938 -302 -239 541 C ATOM 1984 C GLN A 419 17.108 -42.023 9.546 1.00 14.35 C ANISOU 1984 C GLN A 419 1331 2159 1963 -283 -257 548 C ATOM 1985 O GLN A 419 17.748 -43.072 9.504 1.00 15.72 O ANISOU 1985 O GLN A 419 1521 2342 2111 -268 -278 546 O ATOM 1986 CB GLN A 419 14.718 -42.056 8.966 1.00 14.09 C ANISOU 1986 CB GLN A 419 1314 2115 1923 -305 -217 580 C ATOM 1987 CG GLN A 419 13.362 -42.595 9.345 1.00 15.79 C ANISOU 1987 CG GLN A 419 1569 2317 2115 -314 -208 588 C ATOM 1988 CD GLN A 419 12.457 -42.640 8.139 1.00 17.48 C ANISOU 1988 CD GLN A 419 1771 2532 2341 -326 -196 644 C ATOM 1989 OE1 GLN A 419 12.580 -43.519 7.289 1.00 19.97 O ANISOU 1989 OE1 GLN A 419 2106 2869 2613 -321 -209 665 O ATOM 1990 NE2 GLN A 419 11.562 -41.677 8.043 1.00 15.40 N ANISOU 1990 NE2 GLN A 419 1473 2238 2139 -350 -170 672 N ATOM 1991 N HIS A 420 17.576 -40.870 9.077 1.00 14.74 N ANISOU 1991 N HIS A 420 1331 2209 2060 -285 -247 559 N ATOM 1992 CA HIS A 420 18.921 -40.798 8.527 1.00 17.18 C ANISOU 1992 CA HIS A 420 1608 2531 2388 -265 -262 569 C ATOM 1993 C HIS A 420 19.953 -41.233 9.569 1.00 20.62 C ANISOU 1993 C HIS A 420 2064 2954 2817 -261 -296 556 C ATOM 1994 O HIS A 420 20.869 -41.992 9.267 1.00 18.26 O ANISOU 1994 O HIS A 420 1759 2657 2521 -242 -309 566 O ATOM 1995 CB HIS A 420 19.258 -39.390 8.042 1.00 20.81 C ANISOU 1995 CB HIS A 420 2011 2995 2901 -270 -255 584 C ATOM 1996 CG HIS A 420 20.643 -39.279 7.482 1.00 21.71 C ANISOU 1996 CG HIS A 420 2091 3123 3037 -248 -270 597 C ATOM 1997 ND1 HIS A 420 21.723 -38.866 8.235 1.00 23.72 N ANISOU 1997 ND1 HIS A 420 2337 3365 3312 -240 -299 597 N ATOM 1998 CD2 HIS A 420 21.133 -39.592 6.261 1.00 21.28 C ANISOU 1998 CD2 HIS A 420 2013 3088 2985 -236 -259 614 C ATOM 1999 CE1 HIS A 420 22.815 -38.900 7.490 1.00 20.86 C ANISOU 1999 CE1 HIS A 420 1940 3012 2973 -217 -305 618 C ATOM 2000 NE2 HIS A 420 22.483 -39.332 6.286 1.00 31.06 N ANISOU 2000 NE2 HIS A 420 3223 4325 4255 -215 -276 623 N ATOM 2001 N ILE A 421 19.810 -40.751 10.798 1.00 15.84 N ANISOU 2001 N ILE A 421 1483 2329 2207 -288 -308 538 N ATOM 2002 CA ILE A 421 20.794 -41.091 11.822 1.00 15.57 C ANISOU 2002 CA ILE A 421 1469 2279 2167 -303 -351 537 C ATOM 2003 C ILE A 421 20.724 -42.581 12.143 1.00 17.18 C ANISOU 2003 C ILE A 421 1707 2485 2337 -303 -374 534 C ATOM 2004 O ILE A 421 21.741 -43.264 12.177 1.00 21.74 O ANISOU 2004 O ILE A 421 2272 3055 2932 -295 -405 553 O ATOM 2005 CB ILE A 421 20.606 -40.266 13.103 1.00 16.39 C ANISOU 2005 CB ILE A 421 1606 2360 2261 -350 -357 516 C ATOM 2006 CG1 ILE A 421 20.857 -38.779 12.825 1.00 19.16 C ANISOU 2006 CG1 ILE A 421 1919 2707 2655 -349 -339 522 C ATOM 2007 CG2 ILE A 421 21.536 -40.783 14.216 1.00 20.20 C ANISOU 2007 CG2 ILE A 421 2121 2825 2728 -387 -412 526 C ATOM 2008 CD1 ILE A 421 20.271 -37.845 13.907 1.00 15.96 C ANISOU 2008 CD1 ILE A 421 1548 2275 2243 -397 -317 489 C ATOM 2009 N VAL A 422 19.512 -43.081 12.358 1.00 17.95 N ANISOU 2009 N VAL A 422 1839 2587 2392 -312 -360 513 N ATOM 2010 CA VAL A 422 19.314 -44.484 12.706 1.00 16.44 C ANISOU 2010 CA VAL A 422 1679 2401 2165 -313 -387 509 C ATOM 2011 C VAL A 422 19.847 -45.401 11.595 1.00 19.92 C ANISOU 2011 C VAL A 422 2094 2853 2621 -273 -382 528 C ATOM 2012 O VAL A 422 20.419 -46.446 11.864 1.00 20.25 O ANISOU 2012 O VAL A 422 2138 2889 2667 -271 -413 535 O ATOM 2013 CB VAL A 422 17.831 -44.766 13.015 1.00 19.90 C ANISOU 2013 CB VAL A 422 2158 2845 2558 -324 -370 489 C ATOM 2014 CG1 VAL A 422 17.563 -46.255 13.161 1.00 17.00 C ANISOU 2014 CG1 VAL A 422 1818 2491 2152 -317 -400 489 C ATOM 2015 CG2 VAL A 422 17.429 -44.034 14.292 1.00 20.35 C ANISOU 2015 CG2 VAL A 422 2248 2882 2601 -373 -368 462 C ATOM 2016 N SER A 423 19.701 -44.972 10.348 1.00 14.66 N ANISOU 2016 N SER A 423 1403 2199 1969 -249 -341 539 N ATOM 2017 CA SER A 423 20.039 -45.807 9.198 1.00 16.77 C ANISOU 2017 CA SER A 423 1658 2475 2239 -222 -320 550 C ATOM 2018 C SER A 423 21.519 -45.839 8.841 1.00 18.96 C ANISOU 2018 C SER A 423 1894 2738 2572 -204 -321 564 C ATOM 2019 O SER A 423 21.978 -46.726 8.119 1.00 24.14 O ANISOU 2019 O SER A 423 2542 3389 3239 -185 -300 567 O ATOM 2020 CB SER A 423 19.239 -45.331 7.982 1.00 20.03 C ANISOU 2020 CB SER A 423 2066 2905 2638 -222 -279 560 C ATOM 2021 OG SER A 423 17.858 -45.558 8.219 1.00 27.29 O ANISOU 2021 OG SER A 423 3024 3830 3515 -236 -278 559 O ATOM 2022 N ASN A 424 22.269 -44.864 9.328 1.00 17.57 N ANISOU 2022 N ASN A 424 1691 2551 2433 -211 -340 575 N ATOM 2023 CA ASN A 424 23.650 -44.736 8.902 1.00 17.90 C ANISOU 2023 CA ASN A 424 1688 2577 2535 -192 -338 598 C ATOM 2024 C ASN A 424 24.620 -45.423 9.871 1.00 18.61 C ANISOU 2024 C ASN A 424 1771 2634 2666 -201 -385 619 C ATOM 2025 O ASN A 424 24.777 -44.998 11.012 1.00 21.41 O ANISOU 2025 O ASN A 424 2139 2976 3020 -234 -431 629 O ATOM 2026 CB ASN A 424 24.010 -43.263 8.707 1.00 20.25 C ANISOU 2026 CB ASN A 424 1954 2882 2859 -192 -337 610 C ATOM 2027 CG ASN A 424 25.354 -43.077 8.023 1.00 31.20 C ANISOU 2027 CG ASN A 424 3292 4257 4308 -167 -328 638 C ATOM 2028 OD1 ASN A 424 26.139 -44.016 7.900 1.00 36.51 O ANISOU 2028 OD1 ASN A 424 3951 4905 5016 -152 -324 651 O ATOM 2029 ND2 ASN A 424 25.619 -41.869 7.569 1.00 34.51 N ANISOU 2029 ND2 ASN A 424 3678 4691 4745 -162 -324 649 N ATOM 2030 N ASP A 425 25.242 -46.503 9.408 1.00 17.88 N ANISOU 2030 N ASP A 425 1659 2521 2612 -180 -370 629 N ATOM 2031 CA ASP A 425 26.260 -47.215 10.180 1.00 21.89 C ANISOU 2031 CA ASP A 425 2143 2988 3184 -191 -414 662 C ATOM 2032 C ASP A 425 27.360 -46.281 10.697 1.00 22.27 C ANISOU 2032 C ASP A 425 2161 3012 3290 -205 -451 707 C ATOM 2033 O ASP A 425 27.877 -46.465 11.796 1.00 18.88 O ANISOU 2033 O ASP A 425 1731 2553 2888 -243 -513 742 O ATOM 2034 CB ASP A 425 26.872 -48.343 9.337 1.00 19.57 C ANISOU 2034 CB ASP A 425 1819 2670 2948 -160 -371 667 C ATOM 2035 CG ASP A 425 25.935 -49.542 9.194 1.00 23.78 C ANISOU 2035 CG ASP A 425 2387 3217 3433 -158 -357 634 C ATOM 2036 OD1 ASP A 425 24.963 -49.653 9.975 1.00 21.34 O ANISOU 2036 OD1 ASP A 425 2119 2931 3057 -182 -397 618 O ATOM 2037 OD2 ASP A 425 26.174 -50.382 8.309 1.00 25.22 O ANISOU 2037 OD2 ASP A 425 2557 3384 3641 -133 -304 624 O ATOM 2038 N ASP A 426 27.715 -45.273 9.913 1.00 16.43 N ANISOU 2038 N ASP A 426 1397 2283 2564 -180 -420 712 N ATOM 2039 CA ASP A 426 28.735 -44.323 10.357 1.00 16.71 C ANISOU 2039 CA ASP A 426 1404 2296 2648 -189 -459 759 C ATOM 2040 C ASP A 426 28.269 -43.422 11.510 1.00 18.10 C ANISOU 2040 C ASP A 426 1621 2482 2773 -237 -508 756 C ATOM 2041 O ASP A 426 29.050 -42.647 12.055 1.00 20.73 O ANISOU 2041 O ASP A 426 1946 2796 3135 -258 -549 798 O ATOM 2042 CB ASP A 426 29.263 -43.493 9.176 1.00 19.84 C ANISOU 2042 CB ASP A 426 1759 2705 3074 -149 -415 766 C ATOM 2043 CG ASP A 426 30.116 -44.324 8.219 1.00 26.06 C ANISOU 2043 CG ASP A 426 2504 3465 3932 -112 -366 780 C ATOM 2044 OD1 ASP A 426 29.965 -44.187 6.991 1.00 24.85 O ANISOU 2044 OD1 ASP A 426 2340 3335 3767 -88 -304 753 O ATOM 2045 OD2 ASP A 426 30.924 -45.143 8.699 1.00 19.39 O ANISOU 2045 OD2 ASP A 426 1637 2571 3161 -116 -387 818 O ATOM 2046 N LEU A 427 26.996 -43.526 11.877 1.00 16.24 N ANISOU 2046 N LEU A 427 1434 2273 2464 -258 -500 709 N ATOM 2047 CA LEU A 427 26.487 -42.816 13.038 1.00 17.10 C ANISOU 2047 CA LEU A 427 1590 2383 2525 -312 -533 696 C ATOM 2048 C LEU A 427 26.001 -43.808 14.102 1.00 19.44 C ANISOU 2048 C LEU A 427 1931 2671 2784 -361 -570 685 C ATOM 2049 O LEU A 427 25.102 -43.494 14.878 1.00 18.46 O ANISOU 2049 O LEU A 427 1857 2556 2600 -402 -573 651 O ATOM 2050 CB LEU A 427 25.332 -41.893 12.616 1.00 15.89 C ANISOU 2050 CB LEU A 427 1451 2262 2324 -302 -485 651 C ATOM 2051 CG LEU A 427 25.743 -40.762 11.669 1.00 17.10 C ANISOU 2051 CG LEU A 427 1556 2429 2511 -267 -461 663 C ATOM 2052 CD1 LEU A 427 24.533 -39.954 11.154 1.00 18.19 C ANISOU 2052 CD1 LEU A 427 1695 2594 2620 -262 -416 626 C ATOM 2053 CD2 LEU A 427 26.714 -39.848 12.382 1.00 16.03 C ANISOU 2053 CD2 LEU A 427 1417 2272 2403 -292 -505 700 C ATOM 2054 N ALA A 428 26.596 -44.997 14.129 1.00 20.39 N ANISOU 2054 N ALA A 428 2028 2770 2948 -358 -596 714 N ATOM 2055 CA ALA A 428 26.103 -46.100 14.965 1.00 20.51 C ANISOU 2055 CA ALA A 428 2076 2784 2935 -399 -634 704 C ATOM 2056 C ALA A 428 25.919 -45.748 16.446 1.00 17.76 C ANISOU 2056 C ALA A 428 1781 2426 2540 -488 -692 707 C ATOM 2057 O ALA A 428 24.904 -46.107 17.049 1.00 21.11 O ANISOU 2057 O ALA A 428 2253 2870 2898 -520 -696 667 O ATOM 2058 CB ALA A 428 27.004 -47.323 14.818 1.00 24.24 C ANISOU 2058 CB ALA A 428 2499 3224 3486 -390 -660 748 C ATOM 2059 N VAL A 429 26.887 -45.055 17.036 1.00 17.23 N ANISOU 2059 N VAL A 429 1712 2329 2505 -533 -735 756 N ATOM 2060 CA VAL A 429 26.761 -44.678 18.441 1.00 21.98 C ANISOU 2060 CA VAL A 429 2376 2919 3055 -634 -787 760 C ATOM 2061 C VAL A 429 25.544 -43.772 18.695 1.00 23.80 C ANISOU 2061 C VAL A 429 2666 3176 3201 -646 -734 688 C ATOM 2062 O VAL A 429 24.863 -43.896 19.717 1.00 23.49 O ANISOU 2062 O VAL A 429 2689 3139 3098 -718 -750 658 O ATOM 2063 CB VAL A 429 28.058 -44.037 18.987 1.00 29.34 C ANISOU 2063 CB VAL A 429 3302 3810 4035 -687 -845 835 C ATOM 2064 CG1 VAL A 429 28.202 -42.595 18.498 1.00 29.33 C ANISOU 2064 CG1 VAL A 429 3300 3816 4030 -651 -803 826 C ATOM 2065 CG2 VAL A 429 28.065 -44.088 20.493 1.00 36.98 C ANISOU 2065 CG2 VAL A 429 4338 4759 4955 -815 -916 854 C ATOM 2066 N TYR A 430 25.244 -42.892 17.746 1.00 18.68 N ANISOU 2066 N TYR A 430 1995 2545 2560 -579 -670 662 N ATOM 2067 CA TYR A 430 24.073 -42.013 17.860 1.00 19.02 C ANISOU 2067 CA TYR A 430 2076 2603 2547 -584 -611 601 C ATOM 2068 C TYR A 430 22.763 -42.747 17.563 1.00 22.79 C ANISOU 2068 C TYR A 430 2567 3107 2987 -555 -572 553 C ATOM 2069 O TYR A 430 21.727 -42.479 18.175 1.00 21.50 O ANISOU 2069 O TYR A 430 2452 2945 2773 -590 -543 507 O ATOM 2070 CB TYR A 430 24.276 -40.757 17.000 1.00 20.26 C ANISOU 2070 CB TYR A 430 2194 2766 2738 -533 -569 602 C ATOM 2071 CG TYR A 430 25.555 -40.067 17.427 1.00 24.58 C ANISOU 2071 CG TYR A 430 2737 3286 3317 -567 -617 655 C ATOM 2072 CD1 TYR A 430 25.634 -39.438 18.664 1.00 26.01 C ANISOU 2072 CD1 TYR A 430 2983 3443 3458 -656 -642 653 C ATOM 2073 CD2 TYR A 430 26.701 -40.113 16.640 1.00 22.52 C ANISOU 2073 CD2 TYR A 430 2414 3020 3123 -517 -639 712 C ATOM 2074 CE1 TYR A 430 26.801 -38.829 19.091 1.00 23.18 C ANISOU 2074 CE1 TYR A 430 2627 3057 3122 -696 -694 712 C ATOM 2075 CE2 TYR A 430 27.890 -39.502 17.060 1.00 22.86 C ANISOU 2075 CE2 TYR A 430 2452 3034 3198 -549 -691 773 C ATOM 2076 CZ TYR A 430 27.929 -38.869 18.292 1.00 28.45 C ANISOU 2076 CZ TYR A 430 3227 3719 3862 -639 -723 777 C ATOM 2077 OH TYR A 430 29.093 -38.280 18.738 1.00 30.55 O ANISOU 2077 OH TYR A 430 3498 3955 4155 -679 -781 848 O ATOM 2078 N ARG A 431 22.812 -43.691 16.639 1.00 19.90 N ANISOU 2078 N ARG A 431 2160 2757 2646 -495 -568 565 N ATOM 2079 CA ARG A 431 21.684 -44.589 16.447 1.00 18.48 C ANISOU 2079 CA ARG A 431 1997 2598 2425 -475 -548 533 C ATOM 2080 C ARG A 431 21.283 -45.274 17.760 1.00 21.39 C ANISOU 2080 C ARG A 431 2421 2964 2744 -547 -594 518 C ATOM 2081 O ARG A 431 20.103 -45.375 18.090 1.00 20.18 O ANISOU 2081 O ARG A 431 2306 2822 2538 -558 -569 479 O ATOM 2082 CB ARG A 431 22.041 -45.657 15.434 1.00 20.13 C ANISOU 2082 CB ARG A 431 2163 2818 2668 -417 -549 554 C ATOM 2083 CG ARG A 431 21.153 -46.877 15.531 1.00 19.06 C ANISOU 2083 CG ARG A 431 2051 2699 2490 -412 -557 535 C ATOM 2084 CD ARG A 431 21.264 -47.668 14.262 1.00 32.58 C ANISOU 2084 CD ARG A 431 3729 4423 4229 -348 -530 545 C ATOM 2085 NE ARG A 431 22.551 -48.329 14.173 1.00 28.48 N ANISOU 2085 NE ARG A 431 3167 3880 3776 -343 -561 581 N ATOM 2086 CZ ARG A 431 23.241 -48.493 13.049 1.00 25.24 C ANISOU 2086 CZ ARG A 431 2712 3461 3418 -295 -524 597 C ATOM 2087 NH1 ARG A 431 22.793 -48.025 11.886 1.00 20.84 N ANISOU 2087 NH1 ARG A 431 2151 2922 2844 -255 -463 580 N ATOM 2088 NH2 ARG A 431 24.392 -49.132 13.096 1.00 21.44 N ANISOU 2088 NH2 ARG A 431 2188 2947 3010 -294 -549 632 N ATOM 2089 N GLU A 432 22.265 -45.765 18.504 1.00 20.17 N ANISOU 2089 N GLU A 432 2264 2790 2608 -600 -664 556 N ATOM 2090 CA GLU A 432 21.950 -46.471 19.741 1.00 19.38 C ANISOU 2090 CA GLU A 432 2213 2690 2461 -681 -719 549 C ATOM 2091 C GLU A 432 21.377 -45.552 20.812 1.00 21.05 C ANISOU 2091 C GLU A 432 2496 2892 2610 -762 -702 511 C ATOM 2092 O GLU A 432 20.472 -45.948 21.548 1.00 22.60 O ANISOU 2092 O GLU A 432 2741 3099 2746 -807 -704 474 O ATOM 2093 CB GLU A 432 23.178 -47.215 20.253 1.00 29.30 C ANISOU 2093 CB GLU A 432 3442 3923 3768 -732 -806 612 C ATOM 2094 CG GLU A 432 23.722 -48.172 19.213 1.00 34.70 C ANISOU 2094 CG GLU A 432 4053 4606 4524 -654 -808 644 C ATOM 2095 CD GLU A 432 24.818 -49.062 19.741 1.00 33.58 C ANISOU 2095 CD GLU A 432 3873 4432 4452 -704 -892 710 C ATOM 2096 OE1 GLU A 432 25.165 -48.947 20.936 1.00 36.89 O ANISOU 2096 OE1 GLU A 432 4325 4833 4857 -809 -961 740 O ATOM 2097 OE2 GLU A 432 25.326 -49.882 18.953 1.00 33.90 O ANISOU 2097 OE2 GLU A 432 3852 4463 4566 -646 -887 736 O ATOM 2098 N CYS A 433 21.898 -44.326 20.889 1.00 22.62 N ANISOU 2098 N CYS A 433 2701 3070 2824 -780 -682 518 N ATOM 2099 CA CYS A 433 21.368 -43.321 21.804 1.00 21.22 C ANISOU 2099 CA CYS A 433 2593 2876 2594 -853 -647 475 C ATOM 2100 C CYS A 433 19.880 -43.073 21.546 1.00 27.59 C ANISOU 2100 C CYS A 433 3416 3695 3370 -815 -563 410 C ATOM 2101 O CYS A 433 19.070 -43.026 22.476 1.00 21.24 O ANISOU 2101 O CYS A 433 2676 2884 2510 -881 -542 365 O ATOM 2102 CB CYS A 433 22.128 -41.999 21.660 1.00 23.95 C ANISOU 2102 CB CYS A 433 2930 3199 2971 -856 -630 493 C ATOM 2103 SG CYS A 433 23.830 -42.024 22.257 1.00 47.79 S ANISOU 2103 SG CYS A 433 5949 6189 6022 -929 -730 579 S ATOM 2104 N ILE A 434 19.529 -42.905 20.277 1.00 23.22 N ANISOU 2104 N ILE A 434 2807 3157 2858 -715 -515 411 N ATOM 2105 CA ILE A 434 18.165 -42.546 19.909 1.00 21.66 C ANISOU 2105 CA ILE A 434 2614 2963 2653 -679 -437 368 C ATOM 2106 C ILE A 434 17.200 -43.677 20.235 1.00 22.81 C ANISOU 2106 C ILE A 434 2789 3125 2752 -685 -447 349 C ATOM 2107 O ILE A 434 16.125 -43.457 20.797 1.00 22.20 O ANISOU 2107 O ILE A 434 2754 3037 2644 -714 -400 307 O ATOM 2108 CB ILE A 434 18.073 -42.213 18.418 1.00 22.21 C ANISOU 2108 CB ILE A 434 2615 3046 2779 -586 -399 388 C ATOM 2109 CG1 ILE A 434 18.734 -40.863 18.145 1.00 27.79 C ANISOU 2109 CG1 ILE A 434 3293 3735 3530 -583 -377 397 C ATOM 2110 CG2 ILE A 434 16.621 -42.228 17.956 1.00 24.81 C ANISOU 2110 CG2 ILE A 434 2943 3378 3106 -552 -338 366 C ATOM 2111 CD1 ILE A 434 18.864 -40.529 16.672 1.00 29.23 C ANISOU 2111 CD1 ILE A 434 3403 3935 3768 -504 -354 424 C ATOM 2112 N ILE A 435 17.589 -44.892 19.875 1.00 17.05 N ANISOU 2112 N ILE A 435 2034 2420 2022 -655 -506 380 N ATOM 2113 CA ILE A 435 16.765 -46.050 20.174 1.00 23.35 C ANISOU 2113 CA ILE A 435 2857 3240 2776 -658 -529 368 C ATOM 2114 C ILE A 435 16.519 -46.148 21.684 1.00 27.98 C ANISOU 2114 C ILE A 435 3511 3817 3302 -762 -556 338 C ATOM 2115 O ILE A 435 15.383 -46.317 22.129 1.00 32.14 O ANISOU 2115 O ILE A 435 4078 4347 3787 -778 -526 302 O ATOM 2116 CB ILE A 435 17.425 -47.341 19.666 1.00 20.95 C ANISOU 2116 CB ILE A 435 2513 2958 2490 -622 -595 408 C ATOM 2117 CG1 ILE A 435 17.411 -47.373 18.132 1.00 24.48 C ANISOU 2117 CG1 ILE A 435 2907 3415 2978 -527 -555 427 C ATOM 2118 CG2 ILE A 435 16.705 -48.558 20.221 1.00 30.72 C ANISOU 2118 CG2 ILE A 435 3777 4218 3676 -641 -637 397 C ATOM 2119 CD1 ILE A 435 18.316 -48.438 17.531 1.00 22.42 C ANISOU 2119 CD1 ILE A 435 2603 3164 2754 -492 -599 463 C ATOM 2120 N GLU A 436 17.587 -46.026 22.468 1.00 30.84 N ANISOU 2120 N GLU A 436 3889 4165 3662 -840 -612 357 N ATOM 2121 CA GLU A 436 17.469 -46.099 23.929 1.00 30.54 C ANISOU 2121 CA GLU A 436 3925 4117 3561 -962 -644 333 C ATOM 2122 C GLU A 436 16.687 -44.920 24.525 1.00 35.69 C ANISOU 2122 C GLU A 436 4639 4742 4181 -1010 -556 274 C ATOM 2123 O GLU A 436 15.911 -45.096 25.465 1.00 43.98 O ANISOU 2123 O GLU A 436 5752 5789 5171 -1081 -542 231 O ATOM 2124 CB GLU A 436 18.855 -46.244 24.579 1.00 38.52 C ANISOU 2124 CB GLU A 436 4937 5114 4584 -1047 -734 384 C ATOM 2125 CG GLU A 436 19.526 -47.580 24.249 1.00 50.66 C ANISOU 2125 CG GLU A 436 6416 6670 6162 -1021 -823 440 C ATOM 2126 CD GLU A 436 20.907 -47.741 24.870 1.00 67.56 C ANISOU 2126 CD GLU A 436 8546 8786 8336 -1108 -915 507 C ATOM 2127 OE1 GLU A 436 21.756 -46.840 24.695 1.00 74.36 O ANISOU 2127 OE1 GLU A 436 9399 9620 9235 -1112 -906 537 O ATOM 2128 OE2 GLU A 436 21.148 -48.782 25.522 1.00 66.37 O ANISOU 2128 OE2 GLU A 436 8393 8643 8182 -1176 -1004 538 O ATOM 2129 N LYS A 437 16.861 -43.736 23.946 1.00 34.11 N ANISOU 2129 N LYS A 437 4416 4518 4026 -970 -492 270 N ATOM 2130 CA LYS A 437 16.296 -42.502 24.491 1.00 36.92 C ANISOU 2130 CA LYS A 437 4822 4837 4370 -1017 -403 216 C ATOM 2131 C LYS A 437 14.803 -42.330 24.249 1.00 33.50 C ANISOU 2131 C LYS A 437 4391 4394 3944 -973 -310 171 C ATOM 2132 O LYS A 437 14.075 -41.890 25.135 1.00 30.63 O ANISOU 2132 O LYS A 437 4090 4001 3548 -1042 -247 117 O ATOM 2133 CB LYS A 437 17.027 -41.285 23.924 1.00 40.67 C ANISOU 2133 CB LYS A 437 5261 5290 4900 -987 -373 233 C ATOM 2134 CG LYS A 437 16.313 -39.954 24.151 1.00 42.15 C ANISOU 2134 CG LYS A 437 5475 5436 5104 -1006 -265 179 C ATOM 2135 CD LYS A 437 16.611 -39.387 25.533 1.00 47.72 C ANISOU 2135 CD LYS A 437 6275 6106 5749 -1141 -256 144 C ATOM 2136 CE LYS A 437 16.003 -38.012 25.699 1.00 51.74 C ANISOU 2136 CE LYS A 437 6805 6567 6288 -1157 -139 89 C ATOM 2137 NZ LYS A 437 16.098 -37.547 27.103 1.00 57.28 N ANISOU 2137 NZ LYS A 437 7615 7230 6918 -1301 -114 42 N ATOM 2138 N CYS A 438 14.330 -42.647 23.051 1.00 26.58 N ANISOU 2138 N CYS A 438 3447 3537 3114 -865 -296 196 N ATOM 2139 CA CYS A 438 12.929 -42.362 22.775 1.00 35.28 C ANISOU 2139 CA CYS A 438 4545 4620 4239 -826 -209 170 C ATOM 2140 C CYS A 438 12.121 -43.501 22.171 1.00 27.29 C ANISOU 2140 C CYS A 438 3510 3639 3218 -761 -233 194 C ATOM 2141 O CYS A 438 10.894 -43.454 22.210 1.00 27.67 O ANISOU 2141 O CYS A 438 3569 3669 3275 -748 -173 177 O ATOM 2142 CB CYS A 438 12.774 -41.088 21.934 1.00 37.02 C ANISOU 2142 CB CYS A 438 4713 4811 4544 -776 -133 174 C ATOM 2143 SG CYS A 438 13.057 -41.299 20.170 1.00 39.13 S ANISOU 2143 SG CYS A 438 4884 5110 4872 -663 -161 240 S ATOM 2144 N LEU A 439 12.783 -44.520 21.630 1.00 19.01 N ANISOU 2144 N LEU A 439 2432 2633 2158 -722 -316 236 N ATOM 2145 CA LEU A 439 12.042 -45.625 20.996 1.00 18.42 C ANISOU 2145 CA LEU A 439 2341 2588 2072 -660 -340 262 C ATOM 2146 C LEU A 439 11.728 -46.774 21.963 1.00 18.44 C ANISOU 2146 C LEU A 439 2391 2614 2002 -708 -399 247 C ATOM 2147 O LEU A 439 10.587 -47.242 22.041 1.00 20.77 O ANISOU 2147 O LEU A 439 2704 2913 2275 -691 -381 241 O ATOM 2148 CB LEU A 439 12.795 -46.153 19.771 1.00 20.47 C ANISOU 2148 CB LEU A 439 2541 2876 2360 -589 -384 311 C ATOM 2149 CG LEU A 439 13.170 -45.107 18.717 1.00 23.95 C ANISOU 2149 CG LEU A 439 2930 3301 2868 -544 -338 331 C ATOM 2150 CD1 LEU A 439 13.879 -45.764 17.552 1.00 25.28 C ANISOU 2150 CD1 LEU A 439 3051 3498 3055 -484 -376 373 C ATOM 2151 CD2 LEU A 439 11.925 -44.377 18.242 1.00 25.32 C ANISOU 2151 CD2 LEU A 439 3091 3449 3079 -518 -258 330 C ATOM 2152 N MET A 440 12.736 -47.235 22.690 1.00 20.50 N ANISOU 2152 N MET A 440 2667 2889 2232 -771 -475 249 N ATOM 2153 CA MET A 440 12.536 -48.343 23.624 1.00 20.71 C ANISOU 2153 CA MET A 440 2731 2942 2195 -828 -546 240 C ATOM 2154 C MET A 440 11.430 -48.006 24.607 1.00 21.40 C ANISOU 2154 C MET A 440 2885 3011 2236 -890 -490 188 C ATOM 2155 O MET A 440 11.379 -46.890 25.127 1.00 21.53 O ANISOU 2155 O MET A 440 2936 2988 2258 -944 -420 150 O ATOM 2156 CB MET A 440 13.817 -48.649 24.398 1.00 26.97 C ANISOU 2156 CB MET A 440 3533 3741 2975 -914 -633 256 C ATOM 2157 CG MET A 440 14.984 -49.092 23.542 1.00 38.92 C ANISOU 2157 CG MET A 440 4978 5264 4545 -861 -689 311 C ATOM 2158 SD MET A 440 14.551 -50.388 22.368 1.00 49.50 S ANISOU 2158 SD MET A 440 6265 6641 5902 -749 -713 341 S ATOM 2159 CE MET A 440 13.948 -51.660 23.447 1.00 15.25 C ANISOU 2159 CE MET A 440 1963 2336 1495 -811 -794 331 C ATOM 2160 N ARG A 441 10.562 -48.981 24.858 1.00 19.97 N ANISOU 2160 N ARG A 441 2720 2856 2011 -883 -519 185 N ATOM 2161 CA ARG A 441 9.414 -48.836 25.758 1.00 21.82 C ANISOU 2161 CA ARG A 441 3014 3074 2202 -935 -467 138 C ATOM 2162 C ARG A 441 8.280 -48.022 25.132 1.00 27.53 C ANISOU 2162 C ARG A 441 3726 3756 2978 -867 -351 131 C ATOM 2163 O ARG A 441 7.215 -47.867 25.725 1.00 18.54 O ANISOU 2163 O ARG A 441 2627 2594 1823 -894 -291 98 O ATOM 2164 CB ARG A 441 9.832 -48.253 27.113 1.00 27.17 C ANISOU 2164 CB ARG A 441 3761 3728 2833 -1072 -457 88 C ATOM 2165 CG ARG A 441 10.645 -49.219 27.963 1.00 32.09 C ANISOU 2165 CG ARG A 441 4405 4390 3397 -1165 -581 101 C ATOM 2166 CD ARG A 441 11.293 -48.511 29.152 1.00 41.69 C ANISOU 2166 CD ARG A 441 5690 5578 4572 -1313 -578 68 C ATOM 2167 NE ARG A 441 11.960 -47.277 28.746 1.00 48.59 N ANISOU 2167 NE ARG A 441 6553 6411 5499 -1300 -516 68 N ATOM 2168 CZ ARG A 441 13.228 -47.204 28.352 1.00 48.96 C ANISOU 2168 CZ ARG A 441 6558 6461 5583 -1292 -578 118 C ATOM 2169 NH1 ARG A 441 13.976 -48.300 28.312 1.00 49.41 N ANISOU 2169 NH1 ARG A 441 6579 6554 5642 -1299 -697 172 N ATOM 2170 NH2 ARG A 441 13.745 -46.035 27.996 1.00 48.07 N ANISOU 2170 NH2 ARG A 441 6437 6312 5514 -1278 -520 117 N ATOM 2171 N ASN A 442 8.501 -47.515 23.925 1.00 20.99 N ANISOU 2171 N ASN A 442 3525 2341 2112 -508 -395 370 N ATOM 2172 CA ASN A 442 7.465 -46.758 23.247 1.00 19.23 C ANISOU 2172 CA ASN A 442 3246 2111 1951 -477 -301 334 C ATOM 2173 C ASN A 442 7.132 -47.350 21.893 1.00 18.69 C ANISOU 2173 C ASN A 442 3036 2081 1986 -431 -294 346 C ATOM 2174 O ASN A 442 6.485 -46.692 21.085 1.00 17.82 O ANISOU 2174 O ASN A 442 2861 1967 1944 -411 -250 328 O ATOM 2175 CB ASN A 442 7.898 -45.301 23.061 1.00 21.21 C ANISOU 2175 CB ASN A 442 3503 2354 2201 -491 -331 312 C ATOM 2176 CG ASN A 442 8.118 -44.593 24.378 1.00 28.17 C ANISOU 2176 CG ASN A 442 4533 3191 2979 -538 -331 291 C ATOM 2177 OD1 ASN A 442 9.225 -44.169 24.689 1.00 31.72 O ANISOU 2177 OD1 ASN A 442 5027 3643 3384 -568 -429 309 O ATOM 2178 ND2 ASN A 442 7.064 -44.483 25.168 1.00 25.07 N ANISOU 2178 ND2 ASN A 442 4222 2753 2549 -547 -220 254 N ATOM 2179 N LEU A 443 7.558 -48.588 21.650 1.00 17.58 N ANISOU 2179 N LEU A 443 2851 1969 1861 -418 -341 378 N ATOM 2180 CA LEU A 443 7.447 -49.149 20.305 1.00 18.33 C ANISOU 2180 CA LEU A 443 2815 2102 2047 -380 -347 388 C ATOM 2181 C LEU A 443 5.993 -49.312 19.851 1.00 18.05 C ANISOU 2181 C LEU A 443 2742 2046 2070 -349 -249 378 C ATOM 2182 O LEU A 443 5.668 -49.022 18.699 1.00 18.37 O ANISOU 2182 O LEU A 443 2695 2100 2183 -330 -240 374 O ATOM 2183 CB LEU A 443 8.211 -50.475 20.186 1.00 16.77 C ANISOU 2183 CB LEU A 443 2576 1932 1861 -372 -417 418 C ATOM 2184 CG LEU A 443 9.720 -50.399 20.422 1.00 18.45 C ANISOU 2184 CG LEU A 443 2796 2160 2053 -400 -526 433 C ATOM 2185 CD1 LEU A 443 10.385 -51.755 20.247 1.00 18.00 C ANISOU 2185 CD1 LEU A 443 2681 2121 2037 -388 -591 457 C ATOM 2186 CD2 LEU A 443 10.366 -49.369 19.495 1.00 17.77 C ANISOU 2186 CD2 LEU A 443 2646 2105 2001 -402 -556 422 C ATOM 2187 N LEU A 444 5.117 -49.765 20.745 1.00 17.02 N ANISOU 2187 N LEU A 444 2678 1878 1910 -349 -178 376 N ATOM 2188 CA LEU A 444 3.720 -49.978 20.362 1.00 17.67 C ANISOU 2188 CA LEU A 444 2720 1932 2063 -318 -85 371 C ATOM 2189 C LEU A 444 3.058 -48.662 19.972 1.00 18.43 C ANISOU 2189 C LEU A 444 2796 1994 2212 -318 -32 340 C ATOM 2190 O LEU A 444 2.348 -48.569 18.966 1.00 16.75 O ANISOU 2190 O LEU A 444 2499 1771 2094 -295 -11 345 O ATOM 2191 CB LEU A 444 2.934 -50.663 21.485 1.00 21.11 C ANISOU 2191 CB LEU A 444 3234 2333 2455 -324 -12 374 C ATOM 2192 CG LEU A 444 1.432 -50.890 21.234 1.00 18.02 C ANISOU 2192 CG LEU A 444 2802 1900 2144 -294 92 372 C ATOM 2193 CD1 LEU A 444 1.174 -51.618 19.903 1.00 16.82 C ANISOU 2193 CD1 LEU A 444 2531 1770 2091 -253 59 402 C ATOM 2194 CD2 LEU A 444 0.781 -51.640 22.412 1.00 18.64 C ANISOU 2194 CD2 LEU A 444 2963 1952 2168 -308 163 379 C ATOM 2195 N SER A 445 3.296 -47.641 20.785 1.00 17.38 N ANISOU 2195 N SER A 445 2745 1838 2021 -348 -19 310 N ATOM 2196 CA SER A 445 2.751 -46.328 20.539 1.00 17.89 C ANISOU 2196 CA SER A 445 2795 1863 2139 -352 23 277 C ATOM 2197 C SER A 445 3.303 -45.728 19.249 1.00 19.66 C ANISOU 2197 C SER A 445 2926 2121 2422 -351 -57 289 C ATOM 2198 O SER A 445 2.553 -45.209 18.424 1.00 18.26 O ANISOU 2198 O SER A 445 2680 1917 2340 -342 -35 285 O ATOM 2199 CB SER A 445 3.102 -45.399 21.713 1.00 18.91 C ANISOU 2199 CB SER A 445 3040 1965 2181 -388 38 240 C ATOM 2200 OG SER A 445 2.544 -44.121 21.496 1.00 32.15 O ANISOU 2200 OG SER A 445 4698 3597 3921 -390 78 203 O ATOM 2201 N LEU A 446 4.619 -45.786 19.077 1.00 20.09 N ANISOU 2201 N LEU A 446 2979 2229 2424 -366 -153 306 N ATOM 2202 CA LEU A 446 5.242 -45.122 17.930 1.00 17.24 C ANISOU 2202 CA LEU A 446 2541 1904 2104 -376 -225 315 C ATOM 2203 C LEU A 446 4.914 -45.834 16.626 1.00 15.95 C ANISOU 2203 C LEU A 446 2276 1767 2016 -357 -232 338 C ATOM 2204 O LEU A 446 4.881 -45.216 15.566 1.00 15.85 O ANISOU 2204 O LEU A 446 2199 1765 2058 -371 -262 343 O ATOM 2205 CB LEU A 446 6.756 -45.015 18.119 1.00 16.71 C ANISOU 2205 CB LEU A 446 2495 1883 1971 -399 -319 327 C ATOM 2206 CG LEU A 446 7.178 -44.053 19.237 1.00 19.36 C ANISOU 2206 CG LEU A 446 2932 2189 2236 -427 -333 308 C ATOM 2207 CD1 LEU A 446 8.662 -44.180 19.500 1.00 21.62 C ANISOU 2207 CD1 LEU A 446 3239 2510 2465 -448 -433 331 C ATOM 2208 CD2 LEU A 446 6.810 -42.612 18.900 1.00 17.75 C ANISOU 2208 CD2 LEU A 446 2713 1957 2075 -439 -326 284 C ATOM 2209 N SER A 447 4.664 -47.138 16.711 1.00 16.24 N ANISOU 2209 N SER A 447 2305 1813 2052 -332 -211 354 N ATOM 2210 CA SER A 447 4.330 -47.929 15.530 1.00 15.03 C ANISOU 2210 CA SER A 447 2067 1681 1963 -314 -218 374 C ATOM 2211 C SER A 447 2.957 -47.558 14.985 1.00 20.46 C ANISOU 2211 C SER A 447 2719 2313 2740 -306 -163 376 C ATOM 2212 O SER A 447 2.631 -47.866 13.834 1.00 14.56 O ANISOU 2212 O SER A 447 1905 1574 2054 -304 -181 395 O ATOM 2213 CB SER A 447 4.335 -49.424 15.869 1.00 15.18 C ANISOU 2213 CB SER A 447 2090 1714 1965 -286 -211 391 C ATOM 2214 OG SER A 447 5.642 -49.889 16.132 1.00 16.84 O ANISOU 2214 OG SER A 447 2309 1969 2120 -295 -278 395 O ATOM 2215 N GLN A 448 2.144 -46.924 15.824 1.00 15.38 N ANISOU 2215 N GLN A 448 2123 1609 2112 -305 -97 356 N ATOM 2216 CA GLN A 448 0.811 -46.485 15.412 1.00 16.34 C ANISOU 2216 CA GLN A 448 2205 1661 2342 -298 -43 356 C ATOM 2217 C GLN A 448 0.777 -45.030 14.940 1.00 17.16 C ANISOU 2217 C GLN A 448 2285 1738 2497 -330 -72 342 C ATOM 2218 O GLN A 448 -0.297 -44.490 14.663 1.00 16.20 O ANISOU 2218 O GLN A 448 2129 1545 2481 -330 -37 339 O ATOM 2219 CB GLN A 448 -0.186 -46.678 16.558 1.00 16.03 C ANISOU 2219 CB GLN A 448 2218 1559 2313 -279 61 337 C ATOM 2220 CG GLN A 448 -0.397 -48.143 16.914 1.00 15.90 C ANISOU 2220 CG GLN A 448 2214 1559 2268 -251 88 361 C ATOM 2221 CD GLN A 448 -1.222 -48.312 18.167 1.00 24.32 C ANISOU 2221 CD GLN A 448 3347 2575 3320 -244 193 341 C ATOM 2222 OE1 GLN A 448 -2.437 -48.133 18.149 1.00 22.98 O ANISOU 2222 OE1 GLN A 448 3149 2336 3246 -230 271 337 O ATOM 2223 NE2 GLN A 448 -0.566 -48.652 19.267 1.00 21.40 N ANISOU 2223 NE2 GLN A 448 3067 2233 2833 -258 196 331 N ATOM 2224 N GLU A 449 1.944 -44.401 14.854 1.00 16.57 N ANISOU 2224 N GLU A 449 2225 1714 2358 -356 -141 335 N ATOM 2225 CA GLU A 449 2.039 -43.014 14.386 1.00 17.05 C ANISOU 2225 CA GLU A 449 2261 1756 2460 -391 -185 326 C ATOM 2226 C GLU A 449 2.384 -42.928 12.904 1.00 20.37 C ANISOU 2226 C GLU A 449 2608 2216 2915 -421 -265 359 C ATOM 2227 O GLU A 449 3.210 -43.687 12.408 1.00 15.95 O ANISOU 2227 O GLU A 449 2032 1726 2302 -423 -303 376 O ATOM 2228 CB GLU A 449 3.087 -42.249 15.198 1.00 17.27 C ANISOU 2228 CB GLU A 449 2354 1810 2400 -408 -218 303 C ATOM 2229 CG GLU A 449 2.805 -42.263 16.674 1.00 26.23 C ANISOU 2229 CG GLU A 449 3580 2905 3483 -392 -143 268 C ATOM 2230 CD GLU A 449 2.876 -40.895 17.296 1.00 40.56 C ANISOU 2230 CD GLU A 449 5440 4678 5292 -413 -143 231 C ATOM 2231 OE1 GLU A 449 2.904 -39.905 16.536 1.00 40.98 O ANISOU 2231 OE1 GLU A 449 5441 4722 5409 -435 -196 234 O ATOM 2232 OE2 GLU A 449 2.894 -40.815 18.545 1.00 43.67 O ANISOU 2232 OE2 GLU A 449 5929 5048 5617 -412 -91 199 O ATOM 2233 N LYS A 450 1.763 -41.985 12.203 1.00 16.74 N ANISOU 2233 N LYS A 450 2105 1709 2548 -451 -290 367 N ATOM 2234 CA LYS A 450 1.987 -41.849 10.776 1.00 15.78 C ANISOU 2234 CA LYS A 450 1923 1617 2454 -495 -367 401 C ATOM 2235 C LYS A 450 3.471 -41.680 10.464 1.00 16.65 C ANISOU 2235 C LYS A 450 2037 1820 2469 -524 -433 403 C ATOM 2236 O LYS A 450 4.009 -42.383 9.618 1.00 15.16 O ANISOU 2236 O LYS A 450 1821 1692 2248 -538 -461 421 O ATOM 2237 CB LYS A 450 1.201 -40.673 10.216 1.00 17.11 C ANISOU 2237 CB LYS A 450 2053 1713 2735 -535 -402 411 C ATOM 2238 CG LYS A 450 1.278 -40.540 8.698 1.00 18.60 C ANISOU 2238 CG LYS A 450 2189 1921 2955 -596 -485 453 C ATOM 2239 CD LYS A 450 0.479 -39.324 8.237 1.00 22.20 C ANISOU 2239 CD LYS A 450 2608 2292 3535 -642 -535 468 C ATOM 2240 CE LYS A 450 0.709 -39.027 6.755 1.00 28.42 C ANISOU 2240 CE LYS A 450 3360 3105 4334 -722 -635 514 C ATOM 2241 NZ LYS A 450 0.307 -40.171 5.882 1.00 34.99 N ANISOU 2241 NZ LYS A 450 4180 3944 5170 -728 -631 546 N ATOM 2242 N PHE A 451 4.124 -40.752 11.155 1.00 14.86 N ANISOU 2242 N PHE A 451 1844 1600 2202 -533 -456 384 N ATOM 2243 CA PHE A 451 5.512 -40.420 10.852 1.00 16.06 C ANISOU 2243 CA PHE A 451 1992 1828 2281 -564 -525 391 C ATOM 2244 C PHE A 451 6.510 -41.291 11.630 1.00 19.93 C ANISOU 2244 C PHE A 451 2521 2370 2681 -532 -512 381 C ATOM 2245 O PHE A 451 7.487 -41.776 11.064 1.00 16.19 O ANISOU 2245 O PHE A 451 2019 1965 2168 -545 -547 393 O ATOM 2246 CB PHE A 451 5.760 -38.924 11.084 1.00 15.06 C ANISOU 2246 CB PHE A 451 1877 1679 2167 -596 -577 384 C ATOM 2247 CG PHE A 451 4.771 -38.040 10.372 1.00 18.15 C ANISOU 2247 CG PHE A 451 2225 2007 2665 -632 -602 396 C ATOM 2248 CD1 PHE A 451 4.739 -37.994 8.982 1.00 17.96 C ANISOU 2248 CD1 PHE A 451 2145 2007 2673 -686 -659 433 C ATOM 2249 CD2 PHE A 451 3.858 -37.277 11.086 1.00 18.98 C ANISOU 2249 CD2 PHE A 451 2346 2022 2843 -617 -569 369 C ATOM 2250 CE1 PHE A 451 3.818 -37.193 8.318 1.00 19.91 C ANISOU 2250 CE1 PHE A 451 2353 2184 3026 -729 -699 452 C ATOM 2251 CE2 PHE A 451 2.929 -36.473 10.422 1.00 18.13 C ANISOU 2251 CE2 PHE A 451 2188 1843 2857 -652 -601 382 C ATOM 2252 CZ PHE A 451 2.916 -36.433 9.042 1.00 22.40 C ANISOU 2252 CZ PHE A 451 2675 2405 3433 -709 -674 428 C ATOM 2253 N ALA A 452 6.267 -41.520 12.915 1.00 16.58 N ANISOU 2253 N ALA A 452 2162 1911 2228 -495 -462 359 N ATOM 2254 CA ALA A 452 7.245 -42.278 13.696 1.00 15.13 C ANISOU 2254 CA ALA A 452 2020 1765 1963 -476 -469 357 C ATOM 2255 C ALA A 452 7.299 -43.758 13.335 1.00 14.85 C ANISOU 2255 C ALA A 452 1954 1764 1925 -450 -448 368 C ATOM 2256 O ALA A 452 8.294 -44.427 13.608 1.00 15.17 O ANISOU 2256 O ALA A 452 2000 1845 1920 -443 -477 372 O ATOM 2257 CB ALA A 452 7.012 -42.103 15.200 1.00 17.64 C ANISOU 2257 CB ALA A 452 2431 2034 2237 -457 -429 333 C ATOM 2258 N SER A 453 6.234 -44.286 12.736 1.00 16.55 N ANISOU 2258 N SER A 453 2134 1955 2198 -436 -405 374 N ATOM 2259 CA SER A 453 6.242 -45.697 12.345 1.00 15.36 C ANISOU 2259 CA SER A 453 1953 1833 2049 -411 -390 384 C ATOM 2260 C SER A 453 7.402 -45.986 11.387 1.00 15.65 C ANISOU 2260 C SER A 453 1937 1944 2068 -434 -443 390 C ATOM 2261 O SER A 453 7.982 -47.067 11.419 1.00 17.10 O ANISOU 2261 O SER A 453 2105 2160 2234 -414 -445 388 O ATOM 2262 CB SER A 453 4.899 -46.142 11.734 1.00 15.75 C ANISOU 2262 CB SER A 453 1972 1840 2171 -397 -346 396 C ATOM 2263 OG SER A 453 4.528 -45.322 10.636 1.00 18.71 O ANISOU 2263 OG SER A 453 2305 2205 2600 -438 -375 409 O ATOM 2264 N HIS A 454 7.741 -45.018 10.541 1.00 14.19 N ANISOU 2264 N HIS A 454 1720 1780 1891 -480 -483 395 N ATOM 2265 CA HIS A 454 8.904 -45.158 9.659 1.00 14.29 C ANISOU 2265 CA HIS A 454 1683 1863 1883 -511 -524 396 C ATOM 2266 C HIS A 454 10.216 -45.203 10.436 1.00 18.41 C ANISOU 2266 C HIS A 454 2219 2415 2361 -503 -557 390 C ATOM 2267 O HIS A 454 11.153 -45.903 10.052 1.00 15.00 O ANISOU 2267 O HIS A 454 1745 2031 1925 -503 -569 384 O ATOM 2268 CB HIS A 454 8.958 -44.003 8.664 1.00 14.12 C ANISOU 2268 CB HIS A 454 1634 1857 1875 -572 -563 408 C ATOM 2269 CG HIS A 454 7.771 -43.952 7.764 1.00 18.42 C ANISOU 2269 CG HIS A 454 2162 2367 2470 -594 -551 423 C ATOM 2270 ND1 HIS A 454 7.631 -44.786 6.680 1.00 15.70 N ANISOU 2270 ND1 HIS A 454 1784 2049 2133 -610 -540 427 N ATOM 2271 CD2 HIS A 454 6.647 -43.199 7.812 1.00 14.91 C ANISOU 2271 CD2 HIS A 454 1729 1854 2081 -604 -551 435 C ATOM 2272 CE1 HIS A 454 6.472 -44.550 6.092 1.00 15.18 C ANISOU 2272 CE1 HIS A 454 1716 1931 2120 -632 -542 448 C ATOM 2273 NE2 HIS A 454 5.857 -43.590 6.760 1.00 14.76 N ANISOU 2273 NE2 HIS A 454 1685 1819 2106 -627 -549 454 N ATOM 2274 N VAL A 455 10.291 -44.430 11.513 1.00 14.59 N ANISOU 2274 N VAL A 455 1794 1898 1853 -499 -573 390 N ATOM 2275 CA VAL A 455 11.474 -44.458 12.366 1.00 14.89 C ANISOU 2275 CA VAL A 455 1858 1947 1851 -496 -617 392 C ATOM 2276 C VAL A 455 11.604 -45.806 13.062 1.00 17.32 C ANISOU 2276 C VAL A 455 2183 2248 2151 -457 -600 389 C ATOM 2277 O VAL A 455 12.708 -46.350 13.177 1.00 15.14 O ANISOU 2277 O VAL A 455 1882 1997 1875 -457 -639 393 O ATOM 2278 CB VAL A 455 11.446 -43.337 13.418 1.00 17.95 C ANISOU 2278 CB VAL A 455 2322 2293 2207 -504 -640 392 C ATOM 2279 CG1 VAL A 455 12.662 -43.442 14.348 1.00 15.54 C ANISOU 2279 CG1 VAL A 455 2055 1990 1861 -506 -697 401 C ATOM 2280 CG2 VAL A 455 11.418 -41.989 12.723 1.00 17.80 C ANISOU 2280 CG2 VAL A 455 2278 2281 2206 -544 -672 397 C ATOM 2281 N VAL A 456 10.480 -46.342 13.533 1.00 15.30 N ANISOU 2281 N VAL A 456 1964 1951 1897 -428 -546 385 N ATOM 2282 CA VAL A 456 10.491 -47.656 14.172 1.00 16.84 C ANISOU 2282 CA VAL A 456 2176 2138 2087 -397 -534 387 C ATOM 2283 C VAL A 456 11.014 -48.736 13.216 1.00 14.80 C ANISOU 2283 C VAL A 456 1832 1924 1868 -386 -543 384 C ATOM 2284 O VAL A 456 11.816 -49.589 13.601 1.00 15.00 O ANISOU 2284 O VAL A 456 1845 1957 1899 -375 -576 386 O ATOM 2285 CB VAL A 456 9.090 -48.042 14.712 1.00 17.93 C ANISOU 2285 CB VAL A 456 2359 2226 2226 -370 -466 386 C ATOM 2286 CG1 VAL A 456 9.080 -49.496 15.171 1.00 15.01 C ANISOU 2286 CG1 VAL A 456 1993 1854 1855 -342 -461 394 C ATOM 2287 CG2 VAL A 456 8.700 -47.129 15.870 1.00 17.22 C ANISOU 2287 CG2 VAL A 456 2363 2088 2091 -381 -448 378 C ATOM 2288 N GLU A 457 10.573 -48.691 11.961 1.00 14.49 N ANISOU 2288 N GLU A 457 1736 1908 1861 -395 -516 378 N ATOM 2289 CA GLU A 457 11.073 -49.626 10.957 1.00 14.40 C ANISOU 2289 CA GLU A 457 1649 1940 1881 -391 -515 366 C ATOM 2290 C GLU A 457 12.591 -49.529 10.798 1.00 14.69 C ANISOU 2290 C GLU A 457 1641 2017 1922 -412 -561 357 C ATOM 2291 O GLU A 457 13.277 -50.551 10.802 1.00 16.49 O ANISOU 2291 O GLU A 457 1827 2258 2181 -394 -572 346 O ATOM 2292 CB GLU A 457 10.407 -49.387 9.601 1.00 14.41 C ANISOU 2292 CB GLU A 457 1613 1959 1902 -415 -487 362 C ATOM 2293 CG GLU A 457 8.923 -49.746 9.565 1.00 15.27 C ANISOU 2293 CG GLU A 457 1745 2022 2034 -392 -446 374 C ATOM 2294 CD GLU A 457 8.357 -49.608 8.158 1.00 25.78 C ANISOU 2294 CD GLU A 457 3043 3364 3389 -425 -435 377 C ATOM 2295 OE1 GLU A 457 8.858 -50.304 7.243 1.00 25.95 O ANISOU 2295 OE1 GLU A 457 3019 3427 3414 -436 -433 361 O ATOM 2296 OE2 GLU A 457 7.423 -48.806 7.972 1.00 20.26 O ANISOU 2296 OE2 GLU A 457 2364 2626 2710 -444 -431 394 O ATOM 2297 N LYS A 458 13.117 -48.312 10.650 1.00 14.97 N ANISOU 2297 N LYS A 458 1680 2068 1938 -450 -590 364 N ATOM 2298 CA LYS A 458 14.571 -48.146 10.540 1.00 16.33 C ANISOU 2298 CA LYS A 458 1807 2273 2123 -471 -634 361 C ATOM 2299 C LYS A 458 15.309 -48.731 11.739 1.00 17.06 C ANISOU 2299 C LYS A 458 1922 2334 2225 -447 -680 371 C ATOM 2300 O LYS A 458 16.382 -49.328 11.593 1.00 16.55 O ANISOU 2300 O LYS A 458 1796 2285 2208 -446 -706 363 O ATOM 2301 CB LYS A 458 14.960 -46.671 10.371 1.00 19.18 C ANISOU 2301 CB LYS A 458 2178 2648 2459 -515 -668 375 C ATOM 2302 CG LYS A 458 14.415 -46.024 9.106 1.00 20.18 C ANISOU 2302 CG LYS A 458 2279 2807 2582 -555 -642 372 C ATOM 2303 CD LYS A 458 14.732 -46.845 7.865 1.00 26.33 C ANISOU 2303 CD LYS A 458 2984 3635 3384 -570 -605 348 C ATOM 2304 CE LYS A 458 14.239 -46.118 6.620 1.00 40.56 C ANISOU 2304 CE LYS A 458 4775 5466 5170 -628 -592 352 C ATOM 2305 NZ LYS A 458 14.822 -46.685 5.382 1.00 47.98 N ANISOU 2305 NZ LYS A 458 5653 6462 6116 -662 -557 326 N ATOM 2306 N ALA A 459 14.750 -48.538 12.927 1.00 15.50 N ANISOU 2306 N ALA A 459 1813 2088 1988 -434 -692 388 N ATOM 2307 CA ALA A 459 15.393 -49.046 14.136 1.00 16.54 C ANISOU 2307 CA ALA A 459 1985 2181 2117 -426 -748 405 C ATOM 2308 C ALA A 459 15.463 -50.582 14.120 1.00 16.16 C ANISOU 2308 C ALA A 459 1893 2129 2119 -395 -744 397 C ATOM 2309 O ALA A 459 16.512 -51.166 14.416 1.00 17.60 O ANISOU 2309 O ALA A 459 2039 2301 2348 -396 -800 403 O ATOM 2310 CB ALA A 459 14.680 -48.544 15.376 1.00 17.22 C ANISOU 2310 CB ALA A 459 2189 2217 2137 -428 -749 419 C ATOM 2311 N PHE A 460 14.358 -51.238 13.774 1.00 15.62 N ANISOU 2311 N PHE A 460 1822 2062 2050 -369 -684 386 N ATOM 2312 CA PHE A 460 14.388 -52.690 13.603 1.00 18.18 C ANISOU 2312 CA PHE A 460 2095 2385 2427 -339 -681 376 C ATOM 2313 C PHE A 460 15.443 -53.113 12.573 1.00 22.64 C ANISOU 2313 C PHE A 460 2550 2989 3063 -343 -688 348 C ATOM 2314 O PHE A 460 16.195 -54.047 12.807 1.00 17.36 O ANISOU 2314 O PHE A 460 1833 2306 2456 -330 -727 344 O ATOM 2315 CB PHE A 460 13.019 -53.241 13.194 1.00 19.65 C ANISOU 2315 CB PHE A 460 2288 2569 2608 -312 -615 370 C ATOM 2316 CG PHE A 460 12.113 -53.523 14.355 1.00 20.23 C ANISOU 2316 CG PHE A 460 2448 2596 2642 -297 -607 393 C ATOM 2317 CD1 PHE A 460 11.024 -52.707 14.623 1.00 17.80 C ANISOU 2317 CD1 PHE A 460 2207 2269 2289 -302 -558 400 C ATOM 2318 CD2 PHE A 460 12.363 -54.597 15.194 1.00 16.99 C ANISOU 2318 CD2 PHE A 460 2051 2158 2246 -285 -649 408 C ATOM 2319 CE1 PHE A 460 10.194 -52.966 15.704 1.00 19.89 C ANISOU 2319 CE1 PHE A 460 2551 2490 2517 -293 -536 416 C ATOM 2320 CE2 PHE A 460 11.530 -54.866 16.269 1.00 18.06 C ANISOU 2320 CE2 PHE A 460 2273 2254 2336 -282 -638 431 C ATOM 2321 CZ PHE A 460 10.453 -54.051 16.527 1.00 17.46 C ANISOU 2321 CZ PHE A 460 2264 2162 2208 -286 -574 433 C ATOM 2322 N LEU A 461 15.490 -52.417 11.439 1.00 17.37 N ANISOU 2322 N LEU A 461 1842 2367 2390 -365 -649 329 N ATOM 2323 CA LEU A 461 16.393 -52.783 10.348 1.00 18.49 C ANISOU 2323 CA LEU A 461 1883 2551 2590 -375 -632 294 C ATOM 2324 C LEU A 461 17.871 -52.617 10.681 1.00 18.26 C ANISOU 2324 C LEU A 461 1807 2517 2612 -391 -689 297 C ATOM 2325 O LEU A 461 18.711 -53.293 10.095 1.00 19.82 O ANISOU 2325 O LEU A 461 1914 2730 2886 -389 -680 265 O ATOM 2326 CB LEU A 461 16.066 -51.968 9.092 1.00 20.01 C ANISOU 2326 CB LEU A 461 2061 2793 2749 -411 -581 279 C ATOM 2327 CG LEU A 461 14.791 -52.382 8.348 1.00 19.48 C ANISOU 2327 CG LEU A 461 2008 2730 2662 -402 -526 269 C ATOM 2328 CD1 LEU A 461 14.325 -51.285 7.384 1.00 19.82 C ANISOU 2328 CD1 LEU A 461 2065 2803 2662 -451 -501 274 C ATOM 2329 CD2 LEU A 461 15.034 -53.703 7.600 1.00 20.95 C ANISOU 2329 CD2 LEU A 461 2124 2934 2903 -382 -493 229 C ATOM 2330 N HIS A 462 18.188 -51.715 11.605 1.00 18.18 N ANISOU 2330 N HIS A 462 1857 2481 2568 -409 -747 333 N ATOM 2331 CA HIS A 462 19.577 -51.313 11.811 1.00 19.79 C ANISOU 2331 CA HIS A 462 2019 2679 2821 -432 -806 344 C ATOM 2332 C HIS A 462 20.112 -51.463 13.238 1.00 23.81 C ANISOU 2332 C HIS A 462 2581 3122 3345 -430 -901 385 C ATOM 2333 O HIS A 462 21.302 -51.284 13.470 1.00 23.64 O ANISOU 2333 O HIS A 462 2518 3080 3384 -448 -963 400 O ATOM 2334 CB HIS A 462 19.793 -49.871 11.332 1.00 20.00 C ANISOU 2334 CB HIS A 462 2055 2741 2803 -472 -802 354 C ATOM 2335 CG HIS A 462 19.550 -49.685 9.865 1.00 19.93 C ANISOU 2335 CG HIS A 462 1989 2797 2786 -493 -726 320 C ATOM 2336 ND1 HIS A 462 20.493 -49.999 8.908 1.00 22.52 N ANISOU 2336 ND1 HIS A 462 2215 3163 3177 -510 -695 287 N ATOM 2337 CD2 HIS A 462 18.473 -49.217 9.192 1.00 16.28 C ANISOU 2337 CD2 HIS A 462 1561 2361 2263 -506 -676 315 C ATOM 2338 CE1 HIS A 462 20.005 -49.735 7.709 1.00 20.35 C ANISOU 2338 CE1 HIS A 462 1925 2941 2864 -539 -629 263 C ATOM 2339 NE2 HIS A 462 18.780 -49.262 7.853 1.00 21.42 N ANISOU 2339 NE2 HIS A 462 2142 3068 2929 -538 -624 283 N ATOM 2340 N ALA A 463 19.247 -51.760 14.195 1.00 17.69 N ANISOU 2340 N ALA A 463 1899 2307 2514 -416 -914 405 N ATOM 2341 CA ALA A 463 19.705 -51.894 15.574 1.00 19.10 C ANISOU 2341 CA ALA A 463 2147 2421 2690 -429 -1008 446 C ATOM 2342 C ALA A 463 20.742 -53.005 15.659 1.00 23.49 C ANISOU 2342 C ALA A 463 2616 2944 3365 -422 -1069 447 C ATOM 2343 O ALA A 463 20.644 -54.006 14.948 1.00 22.38 O ANISOU 2343 O ALA A 463 2390 2822 3290 -394 -1026 412 O ATOM 2344 CB ALA A 463 18.541 -52.212 16.499 1.00 18.60 C ANISOU 2344 CB ALA A 463 2195 2326 2548 -419 -995 461 C ATOM 2345 N PRO A 464 21.741 -52.833 16.532 1.00 23.02 N ANISOU 2345 N PRO A 464 2576 2828 3342 -450 -1175 488 N ATOM 2346 CA PRO A 464 22.672 -53.924 16.838 1.00 27.06 C ANISOU 2346 CA PRO A 464 3015 3286 3982 -449 -1254 498 C ATOM 2347 C PRO A 464 21.902 -55.064 17.500 1.00 30.00 C ANISOU 2347 C PRO A 464 3435 3625 4338 -434 -1270 507 C ATOM 2348 O PRO A 464 20.871 -54.813 18.130 1.00 25.04 O ANISOU 2348 O PRO A 464 2927 2997 3592 -439 -1247 523 O ATOM 2349 CB PRO A 464 23.630 -53.288 17.847 1.00 26.96 C ANISOU 2349 CB PRO A 464 3058 3208 3979 -492 -1377 555 C ATOM 2350 CG PRO A 464 22.832 -52.187 18.465 1.00 25.95 C ANISOU 2350 CG PRO A 464 3077 3088 3696 -512 -1362 576 C ATOM 2351 CD PRO A 464 22.062 -51.619 17.293 1.00 23.04 C ANISOU 2351 CD PRO A 464 2672 2805 3279 -486 -1235 528 C ATOM 2352 N LEU A 465 22.394 -56.289 17.361 1.00 27.83 N ANISOU 2352 N LEU A 465 3066 3321 4189 -418 -1306 496 N ATOM 2353 CA LEU A 465 21.671 -57.477 17.834 1.00 32.13 C ANISOU 2353 CA LEU A 465 3636 3839 4733 -402 -1321 503 C ATOM 2354 C LEU A 465 21.107 -57.387 19.255 1.00 26.83 C ANISOU 2354 C LEU A 465 3122 3119 3953 -438 -1387 560 C ATOM 2355 O LEU A 465 19.977 -57.797 19.503 1.00 29.14 O ANISOU 2355 O LEU A 465 3479 3424 4169 -425 -1340 560 O ATOM 2356 CB LEU A 465 22.538 -58.733 17.696 1.00 39.34 C ANISOU 2356 CB LEU A 465 4425 4706 5819 -391 -1389 493 C ATOM 2357 CG LEU A 465 22.242 -59.620 16.489 1.00 52.80 C ANISOU 2357 CG LEU A 465 6009 6456 7596 -340 -1297 426 C ATOM 2358 CD1 LEU A 465 20.941 -60.390 16.707 1.00 53.25 C ANISOU 2358 CD1 LEU A 465 6127 6523 7583 -316 -1265 429 C ATOM 2359 CD2 LEU A 465 22.182 -58.795 15.209 1.00 59.48 C ANISOU 2359 CD2 LEU A 465 6806 7383 8409 -326 -1175 373 C ATOM 2360 N GLU A 466 21.886 -56.864 20.190 1.00 30.22 N ANISOU 2360 N GLU A 466 3617 3489 4376 -488 -1494 610 N ATOM 2361 CA GLU A 466 21.442 -56.801 21.580 1.00 32.98 C ANISOU 2361 CA GLU A 466 4128 3786 4615 -536 -1560 663 C ATOM 2362 C GLU A 466 20.221 -55.891 21.749 1.00 32.94 C ANISOU 2362 C GLU A 466 4246 3827 4443 -534 -1456 650 C ATOM 2363 O GLU A 466 19.298 -56.199 22.507 1.00 28.27 O ANISOU 2363 O GLU A 466 3762 3223 3759 -548 -1439 665 O ATOM 2364 CB GLU A 466 22.583 -56.331 22.483 1.00 49.34 C ANISOU 2364 CB GLU A 466 6253 5782 6713 -596 -1702 720 C ATOM 2365 CG GLU A 466 22.178 -56.133 23.932 1.00 70.44 C ANISOU 2365 CG GLU A 466 9114 8399 9251 -660 -1770 774 C ATOM 2366 CD GLU A 466 23.270 -55.477 24.762 1.00 88.93 C ANISOU 2366 CD GLU A 466 11525 10664 11602 -724 -1908 831 C ATOM 2367 OE1 GLU A 466 22.966 -55.016 25.884 1.00 93.02 O ANISOU 2367 OE1 GLU A 466 12216 11143 11986 -783 -1951 868 O ATOM 2368 OE2 GLU A 466 24.430 -55.420 24.293 1.00 93.76 O ANISOU 2368 OE2 GLU A 466 12019 11251 12356 -719 -1973 838 O ATOM 2369 N LEU A 467 20.212 -54.767 21.046 1.00 25.68 N ANISOU 2369 N LEU A 467 3307 2957 3492 -519 -1385 621 N ATOM 2370 CA LEU A 467 19.060 -53.878 21.104 1.00 22.36 C ANISOU 2370 CA LEU A 467 2982 2573 2940 -514 -1286 603 C ATOM 2371 C LEU A 467 17.901 -54.449 20.289 1.00 21.35 C ANISOU 2371 C LEU A 467 2804 2497 2810 -463 -1170 563 C ATOM 2372 O LEU A 467 16.742 -54.311 20.672 1.00 24.45 O ANISOU 2372 O LEU A 467 3283 2894 3112 -461 -1103 560 O ATOM 2373 CB LEU A 467 19.414 -52.467 20.618 1.00 20.71 C ANISOU 2373 CB LEU A 467 2768 2395 2707 -519 -1263 590 C ATOM 2374 CG LEU A 467 20.174 -51.594 21.607 1.00 37.79 C ANISOU 2374 CG LEU A 467 5030 4504 4826 -571 -1362 632 C ATOM 2375 CD1 LEU A 467 20.539 -50.257 20.962 1.00 36.97 C ANISOU 2375 CD1 LEU A 467 4896 4435 4714 -570 -1340 619 C ATOM 2376 CD2 LEU A 467 19.338 -51.390 22.860 1.00 34.08 C ANISOU 2376 CD2 LEU A 467 4733 3995 4222 -606 -1358 649 C ATOM 2377 N LEU A 468 18.217 -55.077 19.163 1.00 21.89 N ANISOU 2377 N LEU A 468 2733 2601 2982 -426 -1145 533 N ATOM 2378 CA LEU A 468 17.193 -55.722 18.351 1.00 21.02 C ANISOU 2378 CA LEU A 468 2575 2533 2880 -382 -1051 499 C ATOM 2379 C LEU A 468 16.438 -56.756 19.183 1.00 21.47 C ANISOU 2379 C LEU A 468 2692 2555 2911 -380 -1066 523 C ATOM 2380 O LEU A 468 15.218 -56.836 19.114 1.00 20.03 O ANISOU 2380 O LEU A 468 2549 2389 2672 -360 -986 514 O ATOM 2381 CB LEU A 468 17.793 -56.365 17.096 1.00 21.18 C ANISOU 2381 CB LEU A 468 2444 2587 3017 -351 -1032 460 C ATOM 2382 CG LEU A 468 16.792 -57.158 16.248 1.00 20.32 C ANISOU 2382 CG LEU A 468 2288 2513 2920 -308 -949 428 C ATOM 2383 CD1 LEU A 468 15.687 -56.253 15.762 1.00 17.25 C ANISOU 2383 CD1 LEU A 468 1948 2162 2444 -302 -854 416 C ATOM 2384 CD2 LEU A 468 17.463 -57.861 15.068 1.00 22.79 C ANISOU 2384 CD2 LEU A 468 2461 2853 3346 -284 -931 383 C ATOM 2385 N ALA A 469 17.165 -57.536 19.982 1.00 18.71 N ANISOU 2385 N ALA A 469 2348 2151 2609 -405 -1175 557 N ATOM 2386 CA ALA A 469 16.534 -58.554 20.817 1.00 19.44 C ANISOU 2386 CA ALA A 469 2499 2209 2679 -414 -1205 587 C ATOM 2387 C ALA A 469 15.583 -57.911 21.813 1.00 19.70 C ANISOU 2387 C ALA A 469 2691 2230 2566 -447 -1164 608 C ATOM 2388 O ALA A 469 14.481 -58.423 22.049 1.00 19.09 O ANISOU 2388 O ALA A 469 2655 2157 2443 -435 -1108 611 O ATOM 2389 CB ALA A 469 17.585 -59.406 21.539 1.00 24.31 C ANISOU 2389 CB ALA A 469 3098 2759 3378 -450 -1350 627 C ATOM 2390 N GLU A 470 16.005 -56.784 22.389 1.00 20.44 N ANISOU 2390 N GLU A 470 2871 2306 2592 -488 -1189 620 N ATOM 2391 CA GLU A 470 15.164 -56.049 23.333 1.00 21.86 C ANISOU 2391 CA GLU A 470 3204 2470 2631 -523 -1140 629 C ATOM 2392 C GLU A 470 13.921 -55.522 22.637 1.00 22.91 C ANISOU 2392 C GLU A 470 3326 2651 2728 -478 -996 587 C ATOM 2393 O GLU A 470 12.828 -55.573 23.203 1.00 25.51 O ANISOU 2393 O GLU A 470 3740 2971 2983 -485 -927 588 O ATOM 2394 CB GLU A 470 15.923 -54.881 23.980 1.00 24.26 C ANISOU 2394 CB GLU A 470 3597 2744 2877 -573 -1197 644 C ATOM 2395 CG GLU A 470 16.954 -55.311 25.019 1.00 32.19 C ANISOU 2395 CG GLU A 470 4661 3679 3889 -637 -1349 699 C ATOM 2396 CD GLU A 470 17.668 -54.123 25.645 1.00 45.94 C ANISOU 2396 CD GLU A 470 6499 5386 5570 -687 -1409 717 C ATOM 2397 OE1 GLU A 470 18.877 -54.245 25.947 1.00 52.79 O ANISOU 2397 OE1 GLU A 470 7351 6205 6502 -723 -1543 757 O ATOM 2398 OE2 GLU A 470 17.020 -53.066 25.822 1.00 40.14 O ANISOU 2398 OE2 GLU A 470 5850 4668 4734 -691 -1326 692 O ATOM 2399 N MET A 471 14.088 -55.007 21.419 1.00 18.51 N ANISOU 2399 N MET A 471 2665 2139 2228 -440 -953 554 N ATOM 2400 CA MET A 471 12.942 -54.525 20.642 1.00 18.34 C ANISOU 2400 CA MET A 471 2623 2155 2192 -403 -833 520 C ATOM 2401 C MET A 471 11.963 -55.646 20.345 1.00 18.56 C ANISOU 2401 C MET A 471 2613 2190 2249 -366 -781 519 C ATOM 2402 O MET A 471 10.759 -55.492 20.543 1.00 18.13 O ANISOU 2402 O MET A 471 2609 2129 2149 -357 -697 514 O ATOM 2403 CB MET A 471 13.387 -53.878 19.327 1.00 17.11 C ANISOU 2403 CB MET A 471 2362 2046 2094 -380 -813 491 C ATOM 2404 CG MET A 471 14.220 -52.607 19.509 1.00 18.80 C ANISOU 2404 CG MET A 471 2607 2256 2279 -413 -854 493 C ATOM 2405 SD MET A 471 14.861 -51.967 17.941 1.00 22.79 S ANISOU 2405 SD MET A 471 2984 2821 2855 -398 -839 465 S ATOM 2406 CE MET A 471 13.334 -51.474 17.143 1.00 17.63 C ANISOU 2406 CE MET A 471 2328 2193 2176 -374 -722 438 C ATOM 2407 N MET A 472 12.473 -56.767 19.841 1.00 18.71 N ANISOU 2407 N MET A 472 2537 2218 2354 -344 -831 522 N ATOM 2408 CA MET A 472 11.618 -57.916 19.551 1.00 17.96 C ANISOU 2408 CA MET A 472 2403 2127 2295 -308 -797 524 C ATOM 2409 C MET A 472 10.878 -58.334 20.818 1.00 18.46 C ANISOU 2409 C MET A 472 2577 2151 2285 -334 -795 558 C ATOM 2410 O MET A 472 9.665 -58.539 20.812 1.00 22.12 O ANISOU 2410 O MET A 472 3063 2616 2727 -314 -716 558 O ATOM 2411 CB MET A 472 12.446 -59.085 19.012 1.00 18.92 C ANISOU 2411 CB MET A 472 2414 2252 2523 -287 -868 520 C ATOM 2412 CG MET A 472 13.020 -58.840 17.632 1.00 16.71 C ANISOU 2412 CG MET A 472 2019 2015 2315 -261 -844 478 C ATOM 2413 SD MET A 472 11.742 -59.054 16.369 1.00 23.59 S ANISOU 2413 SD MET A 472 2839 2924 3199 -213 -737 450 S ATOM 2414 CE MET A 472 12.651 -58.674 14.873 1.00 22.13 C ANISOU 2414 CE MET A 472 2542 2789 3078 -207 -720 401 C ATOM 2415 N ASP A 473 11.624 -58.441 21.906 1.00 20.67 N ANISOU 2415 N ASP A 473 2930 2394 2530 -386 -886 589 N ATOM 2416 CA ASP A 473 11.067 -58.846 23.191 1.00 23.37 C ANISOU 2416 CA ASP A 473 3393 2698 2790 -429 -895 624 C ATOM 2417 C ASP A 473 9.949 -57.906 23.636 1.00 21.90 C ANISOU 2417 C ASP A 473 3309 2510 2502 -440 -778 609 C ATOM 2418 O ASP A 473 8.953 -58.344 24.217 1.00 23.11 O ANISOU 2418 O ASP A 473 3523 2649 2608 -449 -722 622 O ATOM 2419 CB ASP A 473 12.173 -58.878 24.250 1.00 24.21 C ANISOU 2419 CB ASP A 473 3575 2758 2867 -498 -1023 662 C ATOM 2420 CG ASP A 473 13.052 -60.125 24.154 1.00 40.97 C ANISOU 2420 CG ASP A 473 5610 4858 5097 -498 -1147 689 C ATOM 2421 OD1 ASP A 473 12.801 -60.983 23.277 1.00 41.54 O ANISOU 2421 OD1 ASP A 473 5566 4955 5260 -443 -1129 673 O ATOM 2422 OD2 ASP A 473 14.005 -60.243 24.958 1.00 42.86 O ANISOU 2422 OD2 ASP A 473 5897 5049 5337 -557 -1270 727 O ATOM 2423 N GLU A 474 10.111 -56.615 23.355 1.00 21.51 N ANISOU 2423 N GLU A 474 3273 2472 2428 -440 -739 579 N ATOM 2424 CA GLU A 474 9.102 -55.628 23.719 1.00 18.77 C ANISOU 2424 CA GLU A 474 3010 2116 2005 -448 -627 555 C ATOM 2425 C GLU A 474 7.786 -55.877 22.986 1.00 19.37 C ANISOU 2425 C GLU A 474 3025 2207 2126 -395 -517 538 C ATOM 2426 O GLU A 474 6.715 -55.805 23.579 1.00 18.59 O ANISOU 2426 O GLU A 474 2996 2087 1982 -404 -430 535 O ATOM 2427 CB GLU A 474 9.594 -54.196 23.436 1.00 20.41 C ANISOU 2427 CB GLU A 474 3227 2331 2197 -455 -622 527 C ATOM 2428 CG GLU A 474 8.576 -53.120 23.827 1.00 23.06 C ANISOU 2428 CG GLU A 474 3644 2649 2469 -464 -509 496 C ATOM 2429 CD GLU A 474 9.134 -51.694 23.765 1.00 25.77 C ANISOU 2429 CD GLU A 474 4014 2991 2788 -481 -522 473 C ATOM 2430 OE1 GLU A 474 10.361 -51.502 23.921 1.00 22.56 O ANISOU 2430 OE1 GLU A 474 3615 2584 2374 -508 -626 490 O ATOM 2431 OE2 GLU A 474 8.331 -50.761 23.573 1.00 21.36 O ANISOU 2431 OE2 GLU A 474 3464 2425 2225 -469 -432 438 O ATOM 2432 N ILE A 475 7.865 -56.155 21.690 1.00 18.21 N ANISOU 2432 N ILE A 475 2751 2095 2074 -345 -520 527 N ATOM 2433 CA ILE A 475 6.655 -56.438 20.918 1.00 18.19 C ANISOU 2433 CA ILE A 475 2688 2099 2124 -298 -434 519 C ATOM 2434 C ILE A 475 5.995 -57.748 21.361 1.00 17.92 C ANISOU 2434 C ILE A 475 2662 2049 2097 -289 -430 550 C ATOM 2435 O ILE A 475 4.785 -57.794 21.605 1.00 20.54 O ANISOU 2435 O ILE A 475 3024 2361 2421 -279 -342 554 O ATOM 2436 CB ILE A 475 6.952 -56.468 19.413 1.00 17.08 C ANISOU 2436 CB ILE A 475 2422 1996 2071 -258 -447 502 C ATOM 2437 CG1 ILE A 475 7.564 -55.131 18.992 1.00 18.24 C ANISOU 2437 CG1 ILE A 475 2564 2159 2207 -275 -451 476 C ATOM 2438 CG2 ILE A 475 5.664 -56.761 18.612 1.00 20.16 C ANISOU 2438 CG2 ILE A 475 2761 2383 2517 -217 -370 500 C ATOM 2439 CD1 ILE A 475 6.720 -53.914 19.392 1.00 16.96 C ANISOU 2439 CD1 ILE A 475 2472 1970 2001 -289 -371 460 C ATOM 2440 N PHE A 476 6.792 -58.803 21.500 1.00 17.08 N ANISOU 2440 N PHE A 476 2526 1947 2015 -294 -528 574 N ATOM 2441 CA PHE A 476 6.242 -60.118 21.814 1.00 19.92 C ANISOU 2441 CA PHE A 476 2880 2295 2395 -284 -543 607 C ATOM 2442 C PHE A 476 5.754 -60.227 23.268 1.00 21.38 C ANISOU 2442 C PHE A 476 3196 2446 2483 -339 -523 635 C ATOM 2443 O PHE A 476 4.823 -60.977 23.563 1.00 23.66 O ANISOU 2443 O PHE A 476 3497 2722 2770 -332 -484 659 O ATOM 2444 CB PHE A 476 7.275 -61.223 21.523 1.00 18.85 C ANISOU 2444 CB PHE A 476 2665 2166 2329 -277 -662 622 C ATOM 2445 CG PHE A 476 7.594 -61.392 20.055 1.00 17.61 C ANISOU 2445 CG PHE A 476 2378 2043 2270 -223 -666 591 C ATOM 2446 CD1 PHE A 476 6.586 -61.619 19.135 1.00 17.89 C ANISOU 2446 CD1 PHE A 476 2356 2090 2350 -175 -594 581 C ATOM 2447 CD2 PHE A 476 8.900 -61.351 19.606 1.00 18.54 C ANISOU 2447 CD2 PHE A 476 2433 2176 2438 -226 -740 572 C ATOM 2448 CE1 PHE A 476 6.878 -61.781 17.781 1.00 16.95 C ANISOU 2448 CE1 PHE A 476 2132 2001 2307 -137 -597 551 C ATOM 2449 CE2 PHE A 476 9.196 -61.507 18.255 1.00 17.06 C ANISOU 2449 CE2 PHE A 476 2132 2021 2331 -186 -730 537 C ATOM 2450 CZ PHE A 476 8.187 -61.723 17.347 1.00 19.57 C ANISOU 2450 CZ PHE A 476 2406 2352 2676 -144 -659 526 C ATOM 2451 N ASP A 477 6.379 -59.476 24.167 1.00 18.70 N ANISOU 2451 N ASP A 477 2959 2090 2057 -397 -549 633 N ATOM 2452 CA ASP A 477 6.181 -59.708 25.595 1.00 25.24 C ANISOU 2452 CA ASP A 477 3925 2885 2782 -467 -556 662 C ATOM 2453 C ASP A 477 6.203 -58.444 26.455 1.00 27.25 C ANISOU 2453 C ASP A 477 4311 3119 2925 -521 -505 639 C ATOM 2454 O ASP A 477 6.138 -58.521 27.682 1.00 33.04 O ANISOU 2454 O ASP A 477 5178 3823 3554 -592 -510 658 O ATOM 2455 CB ASP A 477 7.238 -60.690 26.106 1.00 27.96 C ANISOU 2455 CB ASP A 477 4276 3214 3134 -509 -710 707 C ATOM 2456 CG ASP A 477 6.841 -61.340 27.411 1.00 51.38 C ANISOU 2456 CG ASP A 477 7364 6148 6008 -580 -727 751 C ATOM 2457 OD1 ASP A 477 5.746 -61.017 27.924 1.00 51.12 O ANISOU 2457 OD1 ASP A 477 7412 6109 5902 -595 -605 741 O ATOM 2458 OD2 ASP A 477 7.619 -62.173 27.923 1.00 60.96 O ANISOU 2458 OD2 ASP A 477 8594 7339 7230 -625 -862 795 O ATOM 2459 N GLY A 478 6.284 -57.282 25.822 1.00 26.60 N ANISOU 2459 N GLY A 478 4196 3048 2860 -493 -457 597 N ATOM 2460 CA GLY A 478 6.441 -56.042 26.565 1.00 27.09 C ANISOU 2460 CA GLY A 478 4375 3089 2828 -541 -424 570 C ATOM 2461 C GLY A 478 5.158 -55.431 27.102 1.00 33.74 C ANISOU 2461 C GLY A 478 5296 3908 3614 -551 -272 538 C ATOM 2462 O GLY A 478 5.206 -54.533 27.938 1.00 31.37 O ANISOU 2462 O GLY A 478 5116 3583 3220 -601 -237 514 O ATOM 2463 N TYR A 479 4.011 -55.912 26.633 1.00 25.31 N ANISOU 2463 N TYR A 479 4163 2844 2609 -504 -181 536 N ATOM 2464 CA TYR A 479 2.735 -55.270 26.941 1.00 27.98 C ANISOU 2464 CA TYR A 479 4545 3155 2933 -501 -25 499 C ATOM 2465 C TYR A 479 1.687 -56.250 27.461 1.00 26.48 C ANISOU 2465 C TYR A 479 4379 2950 2733 -509 47 524 C ATOM 2466 O TYR A 479 1.649 -57.415 27.053 1.00 24.76 O ANISOU 2466 O TYR A 479 4088 2750 2570 -482 -10 567 O ATOM 2467 CB TYR A 479 2.188 -54.546 25.704 1.00 22.64 C ANISOU 2467 CB TYR A 479 3749 2484 2370 -434 35 467 C ATOM 2468 CG TYR A 479 3.115 -53.483 25.162 1.00 20.25 C ANISOU 2468 CG TYR A 479 3421 2197 2077 -430 -24 443 C ATOM 2469 CD1 TYR A 479 3.044 -52.169 25.618 1.00 25.04 C ANISOU 2469 CD1 TYR A 479 4100 2776 2636 -456 31 399 C ATOM 2470 CD2 TYR A 479 4.065 -53.794 24.194 1.00 19.05 C ANISOU 2470 CD2 TYR A 479 3170 2084 1984 -403 -134 462 C ATOM 2471 CE1 TYR A 479 3.901 -51.193 25.127 1.00 25.47 C ANISOU 2471 CE1 TYR A 479 4131 2846 2703 -455 -31 382 C ATOM 2472 CE2 TYR A 479 4.925 -52.823 23.690 1.00 18.69 C ANISOU 2472 CE2 TYR A 479 3099 2056 1948 -404 -186 443 C ATOM 2473 CZ TYR A 479 4.838 -51.531 24.162 1.00 21.68 C ANISOU 2473 CZ TYR A 479 3550 2408 2278 -430 -140 407 C ATOM 2474 OH TYR A 479 5.685 -50.575 23.660 1.00 23.01 O ANISOU 2474 OH TYR A 479 3691 2593 2458 -432 -199 394 O ATOM 2475 N ILE A 480 0.835 -55.764 28.356 1.00 26.42 N ANISOU 2475 N ILE A 480 4473 2908 2658 -546 175 495 N ATOM 2476 CA ILE A 480 -0.252 -56.571 28.910 1.00 27.59 C ANISOU 2476 CA ILE A 480 4650 3040 2795 -559 266 514 C ATOM 2477 C ILE A 480 -1.413 -56.606 27.925 1.00 24.29 C ANISOU 2477 C ILE A 480 4100 2609 2519 -480 359 506 C ATOM 2478 O ILE A 480 -1.881 -55.553 27.485 1.00 23.95 O ANISOU 2478 O ILE A 480 4021 2544 2536 -451 441 459 O ATOM 2479 CB ILE A 480 -0.798 -55.957 30.224 1.00 37.06 C ANISOU 2479 CB ILE A 480 6007 4201 3873 -633 393 475 C ATOM 2480 CG1 ILE A 480 0.341 -55.513 31.145 1.00 41.59 C ANISOU 2480 CG1 ILE A 480 6726 4774 4304 -716 308 471 C ATOM 2481 CG2 ILE A 480 -1.751 -56.926 30.914 1.00 37.30 C ANISOU 2481 CG2 ILE A 480 6080 4220 3873 -663 472 505 C ATOM 2482 CD1 ILE A 480 1.307 -56.598 31.486 1.00 45.05 C ANISOU 2482 CD1 ILE A 480 7196 5232 4691 -760 144 539 C ATOM 2483 N PRO A 481 -1.879 -57.810 27.570 1.00 23.70 N ANISOU 2483 N PRO A 481 3954 2545 2508 -449 336 556 N ATOM 2484 CA PRO A 481 -3.024 -57.926 26.658 1.00 22.81 C ANISOU 2484 CA PRO A 481 3721 2411 2534 -379 414 559 C ATOM 2485 C PRO A 481 -4.272 -57.241 27.220 1.00 28.74 C ANISOU 2485 C PRO A 481 4514 3110 3297 -390 593 520 C ATOM 2486 O PRO A 481 -4.391 -57.068 28.433 1.00 22.49 O ANISOU 2486 O PRO A 481 3849 2303 2391 -457 665 500 O ATOM 2487 CB PRO A 481 -3.250 -59.442 26.558 1.00 23.13 C ANISOU 2487 CB PRO A 481 3717 2467 2604 -363 355 623 C ATOM 2488 CG PRO A 481 -1.943 -60.063 26.977 1.00 31.25 C ANISOU 2488 CG PRO A 481 4796 3532 3546 -406 206 652 C ATOM 2489 CD PRO A 481 -1.385 -59.126 28.014 1.00 28.37 C ANISOU 2489 CD PRO A 481 4571 3158 3049 -480 229 615 C ATOM 2490 N HIS A 482 -5.188 -56.847 26.343 1.00 23.77 N ANISOU 2490 N HIS A 482 3778 2446 2809 -331 663 507 N ATOM 2491 CA HIS A 482 -6.434 -56.221 26.784 1.00 27.30 C ANISOU 2491 CA HIS A 482 4239 2830 3304 -334 835 469 C ATOM 2492 C HIS A 482 -7.171 -57.101 27.797 1.00 25.15 C ANISOU 2492 C HIS A 482 4033 2545 2979 -372 921 494 C ATOM 2493 O HIS A 482 -7.357 -58.291 27.573 1.00 25.24 O ANISOU 2493 O HIS A 482 3998 2573 3018 -353 865 557 O ATOM 2494 CB HIS A 482 -7.351 -55.913 25.595 1.00 29.52 C ANISOU 2494 CB HIS A 482 4378 3066 3774 -264 871 472 C ATOM 2495 CG HIS A 482 -8.589 -55.163 25.976 1.00 32.41 C ANISOU 2495 CG HIS A 482 4740 3354 4220 -265 1044 428 C ATOM 2496 ND1 HIS A 482 -8.682 -53.790 25.891 1.00 39.84 N ANISOU 2496 ND1 HIS A 482 5678 4254 5204 -267 1103 362 N ATOM 2497 CD2 HIS A 482 -9.776 -55.592 26.467 1.00 32.45 C ANISOU 2497 CD2 HIS A 482 4739 3311 4281 -265 1172 437 C ATOM 2498 CE1 HIS A 482 -9.878 -53.406 26.301 1.00 42.74 C ANISOU 2498 CE1 HIS A 482 6034 4547 5658 -266 1263 329 C ATOM 2499 NE2 HIS A 482 -10.562 -54.479 26.655 1.00 43.26 N ANISOU 2499 NE2 HIS A 482 6097 4608 5733 -266 1312 373 N ATOM 2500 N PRO A 483 -7.600 -56.505 28.919 1.00 25.81 N ANISOU 2500 N PRO A 483 4226 2596 2983 -429 1060 444 N ATOM 2501 CA PRO A 483 -8.198 -57.257 30.029 1.00 24.63 C ANISOU 2501 CA PRO A 483 4166 2439 2751 -486 1150 462 C ATOM 2502 C PRO A 483 -9.475 -58.007 29.652 1.00 32.86 C ANISOU 2502 C PRO A 483 5106 3447 3932 -439 1226 504 C ATOM 2503 O PRO A 483 -9.826 -58.964 30.332 1.00 31.28 O ANISOU 2503 O PRO A 483 4954 3257 3675 -476 1251 546 O ATOM 2504 CB PRO A 483 -8.522 -56.161 31.055 1.00 28.18 C ANISOU 2504 CB PRO A 483 4735 2850 3123 -545 1312 379 C ATOM 2505 CG PRO A 483 -8.556 -54.884 30.252 1.00 32.25 C ANISOU 2505 CG PRO A 483 5170 3331 3752 -492 1333 321 C ATOM 2506 CD PRO A 483 -7.460 -55.077 29.247 1.00 30.94 C ANISOU 2506 CD PRO A 483 4934 3217 3603 -452 1137 363 C ATOM 2507 N ASP A 484 -10.163 -57.580 28.599 1.00 35.01 N ANISOU 2507 N ASP A 484 5241 3675 4386 -363 1256 498 N ATOM 2508 CA ASP A 484 -11.419 -58.226 28.225 1.00 35.87 C ANISOU 2508 CA ASP A 484 5249 3737 4643 -319 1326 541 C ATOM 2509 C ASP A 484 -11.254 -59.141 27.019 1.00 25.08 C ANISOU 2509 C ASP A 484 3763 2393 3372 -253 1172 616 C ATOM 2510 O ASP A 484 -11.721 -60.275 27.032 1.00 34.74 O ANISOU 2510 O ASP A 484 4955 3620 4623 -241 1153 680 O ATOM 2511 CB ASP A 484 -12.499 -57.185 27.930 1.00 40.30 C ANISOU 2511 CB ASP A 484 5736 4210 5365 -286 1473 489 C ATOM 2512 CG ASP A 484 -12.767 -56.268 29.110 1.00 47.76 C ANISOU 2512 CG ASP A 484 6792 5122 6230 -348 1645 403 C ATOM 2513 OD1 ASP A 484 -12.757 -56.750 30.268 1.00 45.19 O ANISOU 2513 OD1 ASP A 484 6590 4822 5760 -417 1711 401 O ATOM 2514 OD2 ASP A 484 -12.992 -55.063 28.871 1.00 46.92 O ANISOU 2514 OD2 ASP A 484 6654 4964 6208 -332 1713 337 O ATOM 2515 N THR A 485 -10.593 -58.650 25.979 1.00 25.23 N ANISOU 2515 N THR A 485 3719 2428 3440 -214 1065 606 N ATOM 2516 CA THR A 485 -10.504 -59.407 24.724 1.00 27.23 C ANISOU 2516 CA THR A 485 3858 2695 3793 -153 934 666 C ATOM 2517 C THR A 485 -9.264 -60.298 24.609 1.00 26.92 C ANISOU 2517 C THR A 485 3844 2737 3649 -161 771 700 C ATOM 2518 O THR A 485 -9.244 -61.243 23.824 1.00 24.68 O ANISOU 2518 O THR A 485 3483 2467 3428 -120 673 753 O ATOM 2519 CB THR A 485 -10.514 -58.471 23.515 1.00 26.06 C ANISOU 2519 CB THR A 485 3619 2517 3766 -110 902 643 C ATOM 2520 OG1 THR A 485 -9.329 -57.675 23.540 1.00 25.37 O ANISOU 2520 OG1 THR A 485 3585 2476 3578 -136 842 596 O ATOM 2521 CG2 THR A 485 -11.730 -57.543 23.552 1.00 35.32 C ANISOU 2521 CG2 THR A 485 4750 3596 5073 -100 1050 610 C ATOM 2522 N GLY A 486 -8.222 -59.988 25.371 1.00 25.70 N ANISOU 2522 N GLY A 486 3793 2626 3344 -216 738 669 N ATOM 2523 CA GLY A 486 -6.977 -60.725 25.257 1.00 21.47 C ANISOU 2523 CA GLY A 486 3273 2155 2730 -227 579 696 C ATOM 2524 C GLY A 486 -6.149 -60.318 24.039 1.00 21.20 C ANISOU 2524 C GLY A 486 3161 2146 2747 -186 473 681 C ATOM 2525 O GLY A 486 -5.150 -60.957 23.712 1.00 22.07 O ANISOU 2525 O GLY A 486 3255 2304 2827 -182 343 702 O ATOM 2526 N LYS A 487 -6.553 -59.252 23.358 1.00 21.67 N ANISOU 2526 N LYS A 487 3170 2173 2891 -159 529 646 N ATOM 2527 CA LYS A 487 -5.746 -58.728 22.254 1.00 21.48 C ANISOU 2527 CA LYS A 487 3086 2176 2901 -135 437 628 C ATOM 2528 C LYS A 487 -4.404 -58.240 22.769 1.00 24.55 C ANISOU 2528 C LYS A 487 3552 2611 3164 -178 375 596 C ATOM 2529 O LYS A 487 -4.350 -57.530 23.768 1.00 23.63 O ANISOU 2529 O LYS A 487 3533 2482 2964 -224 442 561 O ATOM 2530 CB LYS A 487 -6.445 -57.546 21.588 1.00 33.00 C ANISOU 2530 CB LYS A 487 4491 3581 4464 -114 508 597 C ATOM 2531 CG LYS A 487 -7.344 -57.896 20.438 1.00 45.31 C ANISOU 2531 CG LYS A 487 5940 5100 6175 -64 498 634 C ATOM 2532 CD LYS A 487 -7.628 -56.637 19.645 1.00 48.01 C ANISOU 2532 CD LYS A 487 6232 5399 6609 -58 519 604 C ATOM 2533 CE LYS A 487 -8.779 -56.828 18.685 1.00 41.33 C ANISOU 2533 CE LYS A 487 5290 4485 5928 -20 529 644 C ATOM 2534 NZ LYS A 487 -9.102 -55.527 18.051 1.00 35.25 N ANISOU 2534 NZ LYS A 487 4479 3662 5253 -26 548 616 N ATOM 2535 N ASP A 488 -3.322 -58.601 22.085 1.00 19.75 N ANISOU 2535 N ASP A 488 2786 2037 2683 -41 386 207 N ATOM 2536 CA ASP A 488 -1.996 -58.151 22.496 1.00 20.30 C ANISOU 2536 CA ASP A 488 2914 2136 2662 -52 351 196 C ATOM 2537 C ASP A 488 -1.378 -57.136 21.515 1.00 21.48 C ANISOU 2537 C ASP A 488 3034 2319 2807 -57 295 190 C ATOM 2538 O ASP A 488 -2.012 -56.735 20.531 1.00 18.26 O ANISOU 2538 O ASP A 488 2566 1909 2463 -51 285 194 O ATOM 2539 CB ASP A 488 -1.055 -59.346 22.783 1.00 19.54 C ANISOU 2539 CB ASP A 488 2843 2068 2513 -53 310 204 C ATOM 2540 CG ASP A 488 -0.828 -60.237 21.566 1.00 25.69 C ANISOU 2540 CG ASP A 488 3561 2875 3325 -39 254 205 C ATOM 2541 OD1 ASP A 488 -1.085 -59.785 20.431 1.00 20.17 O ANISOU 2541 OD1 ASP A 488 2808 2190 2665 -38 229 199 O ATOM 2542 OD2 ASP A 488 -0.393 -61.402 21.746 1.00 23.45 O ANISOU 2542 OD2 ASP A 488 3290 2596 3025 -30 236 212 O ATOM 2543 N ALA A 489 -0.149 -56.715 21.796 1.00 20.34 N ANISOU 2543 N ALA A 489 2932 2207 2587 -73 255 186 N ATOM 2544 CA ALA A 489 0.538 -55.735 20.954 1.00 21.58 C ANISOU 2544 CA ALA A 489 3067 2399 2732 -85 202 186 C ATOM 2545 C ALA A 489 0.620 -56.202 19.502 1.00 20.61 C ANISOU 2545 C ALA A 489 2867 2317 2647 -74 151 190 C ATOM 2546 O ALA A 489 0.406 -55.428 18.572 1.00 17.93 O ANISOU 2546 O ALA A 489 2489 1986 2339 -80 129 193 O ATOM 2547 CB ALA A 489 1.921 -55.467 21.489 1.00 16.83 C ANISOU 2547 CB ALA A 489 2514 1834 2045 -109 159 190 C ATOM 2548 N LEU A 490 0.943 -57.474 19.311 1.00 19.29 N ANISOU 2548 N LEU A 490 2686 2171 2473 -60 133 192 N ATOM 2549 CA LEU A 490 1.053 -58.025 17.963 1.00 22.53 C ANISOU 2549 CA LEU A 490 3040 2615 2907 -52 92 189 C ATOM 2550 C LEU A 490 -0.295 -57.991 17.236 1.00 21.46 C ANISOU 2550 C LEU A 490 2860 2448 2846 -54 105 190 C ATOM 2551 O LEU A 490 -0.357 -57.646 16.058 1.00 26.22 O ANISOU 2551 O LEU A 490 3420 3075 3466 -63 67 192 O ATOM 2552 CB LEU A 490 1.597 -59.448 18.038 1.00 19.77 C ANISOU 2552 CB LEU A 490 2695 2277 2538 -32 81 186 C ATOM 2553 CG LEU A 490 2.213 -60.095 16.812 1.00 25.65 C ANISOU 2553 CG LEU A 490 3404 3064 3277 -19 41 176 C ATOM 2554 CD1 LEU A 490 3.239 -59.175 16.155 1.00 24.66 C ANISOU 2554 CD1 LEU A 490 3258 2998 3113 -29 3 181 C ATOM 2555 CD2 LEU A 490 2.855 -61.405 17.240 1.00 24.34 C ANISOU 2555 CD2 LEU A 490 3257 2896 3093 9 41 177 C ATOM 2556 N ASP A 491 -1.374 -58.340 17.935 1.00 20.15 N ANISOU 2556 N ASP A 491 2700 2231 2725 -49 157 195 N ATOM 2557 CA ASP A 491 -2.714 -58.255 17.353 1.00 16.17 C ANISOU 2557 CA ASP A 491 2144 1696 2303 -54 169 208 C ATOM 2558 C ASP A 491 -2.991 -56.823 16.891 1.00 27.08 C ANISOU 2558 C ASP A 491 3499 3075 3713 -61 162 218 C ATOM 2559 O ASP A 491 -3.474 -56.590 15.779 1.00 29.61 O ANISOU 2559 O ASP A 491 3766 3405 4078 -72 124 233 O ATOM 2560 CB ASP A 491 -3.797 -58.652 18.361 1.00 17.77 C ANISOU 2560 CB ASP A 491 2355 1845 2552 -47 239 219 C ATOM 2561 CG ASP A 491 -3.837 -60.148 18.648 1.00 32.07 C ANISOU 2561 CG ASP A 491 4181 3647 4357 -46 241 218 C ATOM 2562 OD1 ASP A 491 -3.993 -60.502 19.841 1.00 28.14 O ANISOU 2562 OD1 ASP A 491 3724 3122 3845 -41 294 222 O ATOM 2563 OD2 ASP A 491 -3.738 -60.963 17.700 1.00 28.46 O ANISOU 2563 OD2 ASP A 491 3700 3206 3908 -52 193 213 O ATOM 2564 N ILE A 492 -2.702 -55.867 17.764 1.00 16.31 N ANISOU 2564 N ILE A 492 2180 1695 2323 -57 196 213 N ATOM 2565 CA ILE A 492 -2.953 -54.453 17.470 1.00 15.65 C ANISOU 2565 CA ILE A 492 2083 1596 2269 -61 196 223 C ATOM 2566 C ILE A 492 -2.158 -54.013 16.241 1.00 20.43 C ANISOU 2566 C ILE A 492 2661 2254 2848 -80 118 228 C ATOM 2567 O ILE A 492 -2.698 -53.419 15.322 1.00 19.57 O ANISOU 2567 O ILE A 492 2503 2142 2789 -88 91 249 O ATOM 2568 CB ILE A 492 -2.536 -53.546 18.643 1.00 15.22 C ANISOU 2568 CB ILE A 492 2103 1512 2169 -61 240 208 C ATOM 2569 CG1 ILE A 492 -3.435 -53.770 19.864 1.00 24.77 C ANISOU 2569 CG1 ILE A 492 3344 2664 3403 -43 332 203 C ATOM 2570 CG2 ILE A 492 -2.593 -52.084 18.229 1.00 18.06 C ANISOU 2570 CG2 ILE A 492 2457 1854 2553 -67 228 216 C ATOM 2571 CD1 ILE A 492 -4.900 -53.761 19.534 1.00 28.86 C ANISOU 2571 CD1 ILE A 492 3794 3142 4030 -24 374 225 C ATOM 2572 N MET A 493 -0.867 -54.312 16.230 1.00 16.75 N ANISOU 2572 N MET A 493 2224 1838 2303 -89 83 215 N ATOM 2573 CA MET A 493 0.009 -53.805 15.182 1.00 17.54 C ANISOU 2573 CA MET A 493 2303 1994 2368 -109 20 222 C ATOM 2574 C MET A 493 -0.291 -54.438 13.827 1.00 16.42 C ANISOU 2574 C MET A 493 2107 1882 2249 -115 -21 228 C ATOM 2575 O MET A 493 -0.274 -53.750 12.815 1.00 16.30 O ANISOU 2575 O MET A 493 2062 1891 2242 -136 -63 243 O ATOM 2576 CB MET A 493 1.469 -54.006 15.571 1.00 14.79 C ANISOU 2576 CB MET A 493 1989 1694 1938 -115 -2 214 C ATOM 2577 CG MET A 493 1.931 -53.073 16.698 1.00 20.42 C ANISOU 2577 CG MET A 493 2761 2385 2613 -129 15 213 C ATOM 2578 SD MET A 493 3.485 -53.631 17.410 1.00 24.26 S ANISOU 2578 SD MET A 493 3283 2922 3012 -137 -11 215 S ATOM 2579 CE MET A 493 4.636 -53.285 16.067 1.00 17.32 C ANISOU 2579 CE MET A 493 2351 2127 2104 -155 -78 232 C ATOM 2580 N MET A 494 -0.579 -55.742 13.814 1.00 14.87 N ANISOU 2580 N MET A 494 1906 1682 2060 -103 -12 215 N ATOM 2581 CA MET A 494 -0.825 -56.454 12.558 1.00 18.43 C ANISOU 2581 CA MET A 494 2324 2158 2522 -115 -51 213 C ATOM 2582 C MET A 494 -1.985 -55.881 11.770 1.00 20.83 C ANISOU 2582 C MET A 494 2581 2440 2893 -136 -74 241 C ATOM 2583 O MET A 494 -2.005 -55.943 10.543 1.00 21.32 O ANISOU 2583 O MET A 494 2620 2534 2946 -162 -124 247 O ATOM 2584 CB MET A 494 -1.122 -57.938 12.809 1.00 16.45 C ANISOU 2584 CB MET A 494 2085 1887 2278 -100 -33 196 C ATOM 2585 CG MET A 494 0.094 -58.750 13.130 1.00 21.98 C ANISOU 2585 CG MET A 494 2820 2617 2916 -79 -30 174 C ATOM 2586 SD MET A 494 -0.306 -60.506 13.096 1.00 23.09 S ANISOU 2586 SD MET A 494 2975 2726 3072 -65 -20 155 S ATOM 2587 CE MET A 494 -1.774 -60.617 14.108 1.00 19.97 C ANISOU 2587 CE MET A 494 2576 2262 2751 -70 24 175 C ATOM 2588 N PHE A 495 -2.972 -55.354 12.479 1.00 15.26 N ANISOU 2588 N PHE A 495 1862 1681 2255 -127 -35 260 N ATOM 2589 CA PHE A 495 -4.166 -54.855 11.815 1.00 17.21 C ANISOU 2589 CA PHE A 495 2053 1903 2585 -142 -54 297 C ATOM 2590 C PHE A 495 -4.261 -53.331 11.829 1.00 21.47 C ANISOU 2590 C PHE A 495 2580 2424 3152 -141 -54 322 C ATOM 2591 O PHE A 495 -5.264 -52.764 11.398 1.00 19.64 O ANISOU 2591 O PHE A 495 2296 2164 3002 -146 -66 361 O ATOM 2592 CB PHE A 495 -5.409 -55.488 12.430 1.00 21.90 C ANISOU 2592 CB PHE A 495 2621 2445 3256 -130 -9 310 C ATOM 2593 CG PHE A 495 -5.518 -56.960 12.159 1.00 16.38 C ANISOU 2593 CG PHE A 495 1927 1755 2542 -143 -26 295 C ATOM 2594 CD1 PHE A 495 -5.978 -57.412 10.931 1.00 22.26 C ANISOU 2594 CD1 PHE A 495 2639 2516 3304 -180 -90 310 C ATOM 2595 CD2 PHE A 495 -5.139 -57.892 13.119 1.00 16.46 C ANISOU 2595 CD2 PHE A 495 1982 1753 2517 -123 18 267 C ATOM 2596 CE1 PHE A 495 -6.078 -58.774 10.669 1.00 16.37 C ANISOU 2596 CE1 PHE A 495 1910 1768 2541 -195 -106 291 C ATOM 2597 CE2 PHE A 495 -5.238 -59.252 12.867 1.00 20.87 C ANISOU 2597 CE2 PHE A 495 2552 2311 3068 -133 2 254 C ATOM 2598 CZ PHE A 495 -5.702 -59.694 11.639 1.00 21.54 C ANISOU 2598 CZ PHE A 495 2609 2405 3169 -169 -58 262 C ATOM 2599 N HIS A 496 -3.211 -52.671 12.304 1.00 14.14 N ANISOU 2599 N HIS A 496 1699 1511 2163 -136 -45 304 N ATOM 2600 CA HIS A 496 -3.220 -51.205 12.375 1.00 13.53 C ANISOU 2600 CA HIS A 496 1624 1408 2108 -137 -45 323 C ATOM 2601 C HIS A 496 -2.772 -50.585 11.064 1.00 14.02 C ANISOU 2601 C HIS A 496 1661 1517 2150 -172 -121 348 C ATOM 2602 O HIS A 496 -1.912 -51.140 10.379 1.00 15.03 O ANISOU 2602 O HIS A 496 1795 1709 2208 -193 -161 335 O ATOM 2603 CB HIS A 496 -2.298 -50.723 13.488 1.00 13.22 C ANISOU 2603 CB HIS A 496 1655 1361 2008 -129 -9 296 C ATOM 2604 CG HIS A 496 -2.434 -49.263 13.784 1.00 17.87 C ANISOU 2604 CG HIS A 496 2263 1902 2625 -128 5 309 C ATOM 2605 ND1 HIS A 496 -1.667 -48.302 13.160 1.00 15.28 N ANISOU 2605 ND1 HIS A 496 1942 1599 2263 -157 -49 324 N ATOM 2606 CD2 HIS A 496 -3.260 -48.597 14.627 1.00 15.93 C ANISOU 2606 CD2 HIS A 496 2035 1580 2440 -101 72 310 C ATOM 2607 CE1 HIS A 496 -2.007 -47.109 13.613 1.00 17.38 C ANISOU 2607 CE1 HIS A 496 2234 1802 2569 -150 -22 332 C ATOM 2608 NE2 HIS A 496 -2.964 -47.261 14.510 1.00 16.38 N ANISOU 2608 NE2 HIS A 496 2115 1610 2498 -112 55 321 N ATOM 2609 N GLN A 497 -3.317 -49.412 10.737 1.00 14.47 N ANISOU 2609 N GLN A 497 1692 1539 2266 -177 -136 385 N ATOM 2610 CA GLN A 497 -3.048 -48.770 9.453 1.00 18.51 C ANISOU 2610 CA GLN A 497 2178 2090 2766 -215 -212 419 C ATOM 2611 C GLN A 497 -1.570 -48.426 9.234 1.00 18.48 C ANISOU 2611 C GLN A 497 2214 2146 2662 -241 -241 403 C ATOM 2612 O GLN A 497 -1.111 -48.376 8.094 1.00 14.66 O ANISOU 2612 O GLN A 497 1714 1720 2138 -277 -300 421 O ATOM 2613 CB GLN A 497 -3.907 -47.510 9.275 1.00 17.84 C ANISOU 2613 CB GLN A 497 2059 1945 2773 -210 -220 468 C ATOM 2614 CG GLN A 497 -3.589 -46.408 10.259 1.00 22.73 C ANISOU 2614 CG GLN A 497 2729 2510 3397 -189 -173 456 C ATOM 2615 CD GLN A 497 -4.436 -45.166 10.034 1.00 33.90 C ANISOU 2615 CD GLN A 497 4113 3857 4911 -178 -178 505 C ATOM 2616 OE1 GLN A 497 -4.775 -44.827 8.897 1.00 25.13 O ANISOU 2616 OE1 GLN A 497 2950 2762 3835 -204 -247 556 O ATOM 2617 NE2 GLN A 497 -4.776 -44.479 11.117 1.00 34.00 N ANISOU 2617 NE2 GLN A 497 4161 3789 4968 -138 -105 490 N ATOM 2618 N PHE A 498 -0.832 -48.174 10.315 1.00 14.57 N ANISOU 2618 N PHE A 498 1772 1638 2126 -228 -201 375 N ATOM 2619 CA PHE A 498 0.607 -47.949 10.206 1.00 12.98 C ANISOU 2619 CA PHE A 498 1599 1497 1834 -255 -230 366 C ATOM 2620 C PHE A 498 1.406 -49.091 10.842 1.00 15.56 C ANISOU 2620 C PHE A 498 1952 1862 2098 -239 -203 328 C ATOM 2621 O PHE A 498 2.464 -49.483 10.340 1.00 14.06 O ANISOU 2621 O PHE A 498 1757 1743 1841 -254 -230 324 O ATOM 2622 CB PHE A 498 1.010 -46.593 10.818 1.00 14.81 C ANISOU 2622 CB PHE A 498 1875 1691 2063 -268 -227 376 C ATOM 2623 CG PHE A 498 0.180 -45.432 10.325 1.00 17.63 C ANISOU 2623 CG PHE A 498 2211 1993 2495 -274 -246 415 C ATOM 2624 CD1 PHE A 498 -0.010 -45.225 8.967 1.00 17.96 C ANISOU 2624 CD1 PHE A 498 2203 2072 2551 -303 -308 456 C ATOM 2625 CD2 PHE A 498 -0.398 -44.543 11.220 1.00 14.60 C ANISOU 2625 CD2 PHE A 498 1862 1518 2166 -251 -201 413 C ATOM 2626 CE1 PHE A 498 -0.783 -44.159 8.505 1.00 22.10 C ANISOU 2626 CE1 PHE A 498 2703 2543 3151 -308 -333 502 C ATOM 2627 CE2 PHE A 498 -1.160 -43.470 10.770 1.00 14.44 C ANISOU 2627 CE2 PHE A 498 1819 1440 2226 -249 -216 453 C ATOM 2628 CZ PHE A 498 -1.361 -43.285 9.405 1.00 16.93 C ANISOU 2628 CZ PHE A 498 2076 1793 2563 -277 -286 502 C ATOM 2629 N GLY A 499 0.898 -49.616 11.952 1.00 12.89 N ANISOU 2629 N GLY A 499 1639 1476 1784 -207 -147 305 N ATOM 2630 CA GLY A 499 1.557 -50.708 12.646 1.00 12.82 C ANISOU 2630 CA GLY A 499 1656 1492 1723 -190 -124 276 C ATOM 2631 C GLY A 499 1.844 -51.920 11.769 1.00 17.34 C ANISOU 2631 C GLY A 499 2197 2121 2271 -186 -146 267 C ATOM 2632 O GLY A 499 2.842 -52.616 11.972 1.00 16.16 O ANISOU 2632 O GLY A 499 2059 2015 2066 -178 -146 252 O ATOM 2633 N ASN A 500 0.982 -52.177 10.791 1.00 13.22 N ANISOU 2633 N ASN A 500 1637 1596 1791 -192 -165 277 N ATOM 2634 CA ASN A 500 1.124 -53.380 9.972 1.00 12.63 C ANISOU 2634 CA ASN A 500 1548 1561 1691 -191 -181 260 C ATOM 2635 C ASN A 500 2.456 -53.425 9.222 1.00 14.88 C ANISOU 2635 C ASN A 500 1831 1923 1899 -205 -209 256 C ATOM 2636 O ASN A 500 3.003 -54.503 8.973 1.00 12.83 O ANISOU 2636 O ASN A 500 1577 1697 1603 -189 -200 231 O ATOM 2637 CB ASN A 500 -0.049 -53.528 8.997 1.00 12.77 C ANISOU 2637 CB ASN A 500 1531 1562 1761 -210 -209 277 C ATOM 2638 CG ASN A 500 0.082 -52.633 7.784 1.00 15.02 C ANISOU 2638 CG ASN A 500 1791 1883 2031 -250 -265 307 C ATOM 2639 OD1 ASN A 500 0.713 -53.004 6.800 1.00 16.08 O ANISOU 2639 OD1 ASN A 500 1928 2077 2106 -271 -294 298 O ATOM 2640 ND2 ASN A 500 -0.524 -51.444 7.846 1.00 14.60 N ANISOU 2640 ND2 ASN A 500 1720 1794 2033 -260 -277 343 N ATOM 2641 N TYR A 501 2.979 -52.257 8.867 1.00 14.67 N ANISOU 2641 N TYR A 501 1797 1924 1851 -234 -238 282 N ATOM 2642 CA TYR A 501 4.252 -52.193 8.150 1.00 13.23 C ANISOU 2642 CA TYR A 501 1606 1822 1599 -250 -259 286 C ATOM 2643 C TYR A 501 5.429 -52.518 9.069 1.00 13.19 C ANISOU 2643 C TYR A 501 1615 1843 1554 -229 -237 276 C ATOM 2644 O TYR A 501 6.458 -53.030 8.626 1.00 13.70 O ANISOU 2644 O TYR A 501 1664 1970 1569 -222 -236 272 O ATOM 2645 CB TYR A 501 4.447 -50.806 7.548 1.00 12.52 C ANISOU 2645 CB TYR A 501 1503 1751 1503 -294 -300 324 C ATOM 2646 CG TYR A 501 3.452 -50.454 6.455 1.00 12.72 C ANISOU 2646 CG TYR A 501 1508 1765 1561 -323 -337 347 C ATOM 2647 CD1 TYR A 501 3.645 -50.890 5.150 1.00 16.44 C ANISOU 2647 CD1 TYR A 501 1966 2293 1986 -347 -362 347 C ATOM 2648 CD2 TYR A 501 2.332 -49.666 6.729 1.00 12.82 C ANISOU 2648 CD2 TYR A 501 1514 1708 1649 -326 -345 371 C ATOM 2649 CE1 TYR A 501 2.735 -50.575 4.134 1.00 14.80 C ANISOU 2649 CE1 TYR A 501 1743 2077 1802 -383 -407 374 C ATOM 2650 CE2 TYR A 501 1.428 -49.327 5.713 1.00 16.35 C ANISOU 2650 CE2 TYR A 501 1935 2146 2133 -354 -389 404 C ATOM 2651 CZ TYR A 501 1.648 -49.788 4.424 1.00 13.28 C ANISOU 2651 CZ TYR A 501 1536 1819 1692 -387 -425 407 C ATOM 2652 OH TYR A 501 0.766 -49.461 3.428 1.00 16.00 O ANISOU 2652 OH TYR A 501 1858 2156 2066 -424 -478 445 O ATOM 2653 N VAL A 502 5.284 -52.200 10.348 1.00 12.23 N ANISOU 2653 N VAL A 502 1522 1672 1452 -219 -218 276 N ATOM 2654 CA VAL A 502 6.331 -52.513 11.302 1.00 12.69 C ANISOU 2654 CA VAL A 502 1598 1752 1473 -206 -206 274 C ATOM 2655 C VAL A 502 6.413 -54.026 11.473 1.00 13.04 C ANISOU 2655 C VAL A 502 1641 1799 1515 -163 -178 249 C ATOM 2656 O VAL A 502 7.496 -54.603 11.472 1.00 18.10 O ANISOU 2656 O VAL A 502 2267 2490 2120 -147 -178 252 O ATOM 2657 CB VAL A 502 6.077 -51.843 12.649 1.00 13.21 C ANISOU 2657 CB VAL A 502 1710 1758 1549 -214 -193 277 C ATOM 2658 CG1 VAL A 502 7.068 -52.382 13.703 1.00 14.15 C ANISOU 2658 CG1 VAL A 502 1852 1897 1628 -204 -187 279 C ATOM 2659 CG2 VAL A 502 6.210 -50.316 12.506 1.00 12.78 C ANISOU 2659 CG2 VAL A 502 1666 1698 1493 -257 -223 302 C ATOM 2660 N VAL A 503 5.260 -54.670 11.603 1.00 14.91 N ANISOU 2660 N VAL A 503 1889 1981 1796 -144 -154 228 N ATOM 2661 CA VAL A 503 5.237 -56.134 11.709 1.00 12.42 C ANISOU 2661 CA VAL A 503 1579 1658 1483 -107 -130 204 C ATOM 2662 C VAL A 503 5.805 -56.811 10.457 1.00 15.01 C ANISOU 2662 C VAL A 503 1882 2039 1781 -98 -139 191 C ATOM 2663 O VAL A 503 6.521 -57.804 10.563 1.00 14.56 O ANISOU 2663 O VAL A 503 1827 2000 1706 -63 -121 178 O ATOM 2664 CB VAL A 503 3.836 -56.667 12.022 1.00 12.06 C ANISOU 2664 CB VAL A 503 1547 1542 1492 -98 -107 190 C ATOM 2665 CG1 VAL A 503 3.863 -58.213 12.175 1.00 14.82 C ANISOU 2665 CG1 VAL A 503 1910 1878 1844 -64 -85 167 C ATOM 2666 CG2 VAL A 503 3.311 -56.023 13.294 1.00 14.38 C ANISOU 2666 CG2 VAL A 503 1870 1784 1811 -102 -82 200 C ATOM 2667 N GLN A 504 5.501 -56.269 9.278 1.00 14.30 N ANISOU 2667 N GLN A 504 1775 1973 1686 -129 -163 195 N ATOM 2668 CA GLN A 504 6.061 -56.805 8.035 1.00 13.41 C ANISOU 2668 CA GLN A 504 1650 1914 1531 -128 -166 179 C ATOM 2669 C GLN A 504 7.588 -56.684 8.041 1.00 16.87 C ANISOU 2669 C GLN A 504 2066 2422 1923 -114 -158 193 C ATOM 2670 O GLN A 504 8.294 -57.587 7.606 1.00 14.02 O ANISOU 2670 O GLN A 504 1699 2093 1535 -81 -133 173 O ATOM 2671 CB GLN A 504 5.482 -56.072 6.805 1.00 13.45 C ANISOU 2671 CB GLN A 504 1645 1936 1529 -176 -201 190 C ATOM 2672 CG GLN A 504 3.981 -56.273 6.592 1.00 25.71 C ANISOU 2672 CG GLN A 504 3207 3428 3133 -193 -217 186 C ATOM 2673 CD GLN A 504 3.451 -55.536 5.357 1.00 27.61 C ANISOU 2673 CD GLN A 504 3434 3689 3367 -245 -264 208 C ATOM 2674 OE1 GLN A 504 3.757 -55.905 4.230 1.00 28.61 O ANISOU 2674 OE1 GLN A 504 3569 3859 3441 -264 -275 194 O ATOM 2675 NE2 GLN A 504 2.653 -54.496 5.576 1.00 13.54 N ANISOU 2675 NE2 GLN A 504 1634 1873 1637 -268 -289 244 N ATOM 2676 N CYS A 505 8.078 -55.541 8.502 1.00 17.21 N ANISOU 2676 N CYS A 505 2094 2486 1957 -140 -180 228 N ATOM 2677 CA CYS A 505 9.510 -55.310 8.665 1.00 16.48 C ANISOU 2677 CA CYS A 505 1972 2459 1829 -137 -181 254 C ATOM 2678 C CYS A 505 10.149 -56.362 9.587 1.00 15.39 C ANISOU 2678 C CYS A 505 1834 2316 1697 -86 -155 249 C ATOM 2679 O CYS A 505 11.176 -56.960 9.247 1.00 18.15 O ANISOU 2679 O CYS A 505 2151 2717 2026 -55 -136 253 O ATOM 2680 CB CYS A 505 9.733 -53.906 9.232 1.00 19.79 C ANISOU 2680 CB CYS A 505 2392 2881 2245 -183 -216 293 C ATOM 2681 SG CYS A 505 11.453 -53.440 9.433 1.00 21.91 S ANISOU 2681 SG CYS A 505 2617 3233 2473 -198 -233 339 S ATOM 2682 N MET A 506 9.544 -56.593 10.748 1.00 15.15 N ANISOU 2682 N MET A 506 1839 2222 1697 -76 -151 244 N ATOM 2683 CA MET A 506 10.041 -57.614 11.680 1.00 13.99 C ANISOU 2683 CA MET A 506 1699 2061 1557 -32 -134 245 C ATOM 2684 C MET A 506 10.143 -58.972 10.997 1.00 14.32 C ANISOU 2684 C MET A 506 1733 2103 1605 19 -100 214 C ATOM 2685 O MET A 506 11.131 -59.697 11.135 1.00 14.77 O ANISOU 2685 O MET A 506 1765 2188 1658 62 -84 224 O ATOM 2686 CB MET A 506 9.105 -57.735 12.889 1.00 13.39 C ANISOU 2686 CB MET A 506 1671 1908 1508 -34 -127 238 C ATOM 2687 CG MET A 506 9.063 -56.500 13.801 1.00 12.65 C ANISOU 2687 CG MET A 506 1603 1801 1404 -78 -150 263 C ATOM 2688 SD MET A 506 7.729 -56.573 15.025 1.00 19.04 S ANISOU 2688 SD MET A 506 2475 2517 2243 -80 -123 246 S ATOM 2689 CE MET A 506 8.189 -58.077 15.914 1.00 16.68 C ANISOU 2689 CE MET A 506 2190 2206 1943 -36 -107 250 C ATOM 2690 N LEU A 507 9.101 -59.333 10.265 1.00 13.17 N ANISOU 2690 N LEU A 507 1611 1922 1473 15 -89 177 N ATOM 2691 CA LEU A 507 9.067 -60.648 9.632 1.00 14.34 C ANISOU 2691 CA LEU A 507 1771 2054 1623 57 -58 140 C ATOM 2692 C LEU A 507 10.138 -60.775 8.548 1.00 14.27 C ANISOU 2692 C LEU A 507 1730 2116 1576 76 -39 135 C ATOM 2693 O LEU A 507 10.807 -61.804 8.434 1.00 17.83 O ANISOU 2693 O LEU A 507 2177 2571 2029 130 -3 120 O ATOM 2694 CB LEU A 507 7.676 -60.917 9.049 1.00 15.01 C ANISOU 2694 CB LEU A 507 1891 2086 1727 33 -63 106 C ATOM 2695 CG LEU A 507 7.500 -62.200 8.225 1.00 16.94 C ANISOU 2695 CG LEU A 507 2164 2307 1965 60 -38 60 C ATOM 2696 CD1 LEU A 507 7.751 -63.427 9.087 1.00 15.57 C ANISOU 2696 CD1 LEU A 507 2010 2087 1820 115 -10 52 C ATOM 2697 CD2 LEU A 507 6.093 -62.232 7.623 1.00 16.48 C ANISOU 2697 CD2 LEU A 507 2135 2204 1922 16 -60 40 C ATOM 2698 N THR A 508 10.280 -59.731 7.743 1.00 18.37 N ANISOU 2698 N THR A 508 2228 2689 2064 31 -57 148 N ATOM 2699 CA THR A 508 11.254 -59.722 6.655 1.00 19.30 C ANISOU 2699 CA THR A 508 2315 2881 2138 40 -33 147 C ATOM 2700 C THR A 508 12.671 -59.849 7.192 1.00 19.96 C ANISOU 2700 C THR A 508 2345 3017 2224 80 -15 183 C ATOM 2701 O THR A 508 13.515 -60.534 6.609 1.00 19.69 O ANISOU 2701 O THR A 508 2286 3019 2175 127 31 173 O ATOM 2702 CB THR A 508 11.122 -58.430 5.803 1.00 25.45 C ANISOU 2702 CB THR A 508 3080 3708 2881 -26 -65 168 C ATOM 2703 OG1 THR A 508 9.839 -58.422 5.160 1.00 24.29 O ANISOU 2703 OG1 THR A 508 2976 3518 2736 -62 -85 140 O ATOM 2704 CG2 THR A 508 12.218 -58.367 4.741 1.00 25.73 C ANISOU 2704 CG2 THR A 508 3080 3829 2866 -22 -34 173 C ATOM 2705 N ILE A 509 12.931 -59.176 8.306 1.00 19.05 N ANISOU 2705 N ILE A 509 2211 2901 2124 61 -51 228 N ATOM 2706 CA ILE A 509 14.227 -59.260 8.958 1.00 17.04 C ANISOU 2706 CA ILE A 509 1903 2694 1878 89 -50 275 C ATOM 2707 C ILE A 509 14.529 -60.707 9.352 1.00 17.87 C ANISOU 2707 C ILE A 509 2010 2766 2016 166 -12 260 C ATOM 2708 O ILE A 509 15.618 -61.226 9.095 1.00 19.09 O ANISOU 2708 O ILE A 509 2112 2966 2176 216 21 278 O ATOM 2709 CB ILE A 509 14.259 -58.380 10.212 1.00 14.57 C ANISOU 2709 CB ILE A 509 1594 2369 1572 45 -103 320 C ATOM 2710 CG1 ILE A 509 14.382 -56.906 9.810 1.00 21.21 C ANISOU 2710 CG1 ILE A 509 2420 3255 2384 -26 -140 348 C ATOM 2711 CG2 ILE A 509 15.410 -58.805 11.133 1.00 16.16 C ANISOU 2711 CG2 ILE A 509 1752 2597 1789 77 -112 369 C ATOM 2712 CD1 ILE A 509 14.030 -55.941 10.921 1.00 20.21 C ANISOU 2712 CD1 ILE A 509 2328 3091 2259 -78 -189 372 C ATOM 2713 N CYS A 510 13.562 -61.349 9.992 1.00 16.18 N ANISOU 2713 N CYS A 510 1852 2469 1827 177 -15 232 N ATOM 2714 CA CYS A 510 13.744 -62.714 10.471 1.00 17.80 C ANISOU 2714 CA CYS A 510 2068 2629 2067 246 14 222 C ATOM 2715 C CYS A 510 13.906 -63.688 9.319 1.00 18.65 C ANISOU 2715 C CYS A 510 2181 2734 2171 298 72 174 C ATOM 2716 O CYS A 510 14.730 -64.597 9.388 1.00 23.01 O ANISOU 2716 O CYS A 510 2708 3288 2748 367 108 180 O ATOM 2717 CB CYS A 510 12.570 -63.137 11.353 1.00 17.53 C ANISOU 2717 CB CYS A 510 2097 2506 2058 235 -1 204 C ATOM 2718 SG CYS A 510 12.538 -62.268 12.916 1.00 18.71 S ANISOU 2718 SG CYS A 510 2254 2648 2207 189 -52 257 S ATOM 2719 N CYS A 511 13.129 -63.497 8.256 1.00 17.57 N ANISOU 2719 N CYS A 511 2082 2591 2003 265 81 126 N ATOM 2720 CA CYS A 511 13.269 -64.348 7.075 1.00 20.90 C ANISOU 2720 CA CYS A 511 2525 3011 2404 303 137 73 C ATOM 2721 C CYS A 511 14.621 -64.147 6.387 1.00 24.17 C ANISOU 2721 C CYS A 511 2876 3513 2796 334 179 94 C ATOM 2722 O CYS A 511 15.263 -65.120 5.988 1.00 24.35 O ANISOU 2722 O CYS A 511 2893 3531 2826 405 241 71 O ATOM 2723 CB CYS A 511 12.105 -64.144 6.098 1.00 20.88 C ANISOU 2723 CB CYS A 511 2583 2985 2367 247 124 25 C ATOM 2724 SG CYS A 511 10.515 -64.746 6.748 1.00 25.19 S ANISOU 2724 SG CYS A 511 3198 3421 2952 224 92 -3 S ATOM 2725 N ASP A 512 15.060 -62.895 6.254 1.00 19.45 N ANISOU 2725 N ASP A 512 2228 2992 2172 284 150 138 N ATOM 2726 CA ASP A 512 16.385 -62.620 5.695 1.00 23.21 C ANISOU 2726 CA ASP A 512 2629 3559 2629 306 189 171 C ATOM 2727 C ASP A 512 17.475 -63.306 6.515 1.00 23.18 C ANISOU 2727 C ASP A 512 2563 3564 2680 382 211 215 C ATOM 2728 O ASP A 512 18.419 -63.879 5.969 1.00 26.59 O ANISOU 2728 O ASP A 512 2951 4034 3119 446 277 215 O ATOM 2729 CB ASP A 512 16.674 -61.113 5.649 1.00 22.21 C ANISOU 2729 CB ASP A 512 2457 3507 2475 230 140 225 C ATOM 2730 CG ASP A 512 15.917 -60.403 4.539 1.00 31.93 C ANISOU 2730 CG ASP A 512 3730 4752 3650 164 129 195 C ATOM 2731 OD1 ASP A 512 15.249 -61.085 3.736 1.00 31.12 O ANISOU 2731 OD1 ASP A 512 3689 4611 3523 174 160 133 O ATOM 2732 OD2 ASP A 512 15.987 -59.160 4.480 1.00 33.57 O ANISOU 2732 OD2 ASP A 512 3913 5006 3838 97 84 237 O ATOM 2733 N ALA A 513 17.358 -63.228 7.833 1.00 23.08 N ANISOU 2733 N ALA A 513 2545 3517 2705 373 156 255 N ATOM 2734 CA ALA A 513 18.371 -63.820 8.702 1.00 25.10 C ANISOU 2734 CA ALA A 513 2741 3783 3015 435 159 310 C ATOM 2735 C ALA A 513 18.434 -65.342 8.562 1.00 27.83 C ANISOU 2735 C ALA A 513 3110 4066 3400 529 222 271 C ATOM 2736 O ALA A 513 19.511 -65.920 8.449 1.00 23.78 O ANISOU 2736 O ALA A 513 2530 3582 2922 603 269 299 O ATOM 2737 CB ALA A 513 18.135 -63.416 10.160 1.00 21.32 C ANISOU 2737 CB ALA A 513 2270 3276 2555 394 82 359 C ATOM 2738 N VAL A 514 17.276 -65.988 8.556 1.00 24.77 N ANISOU 2738 N VAL A 514 2813 3588 3010 528 224 208 N ATOM 2739 CA VAL A 514 17.215 -67.449 8.535 1.00 28.85 C ANISOU 2739 CA VAL A 514 3368 4027 3566 609 274 169 C ATOM 2740 C VAL A 514 17.597 -68.018 7.165 1.00 32.58 C ANISOU 2740 C VAL A 514 3850 4512 4016 661 363 111 C ATOM 2741 O VAL A 514 18.079 -69.141 7.057 1.00 34.88 O ANISOU 2741 O VAL A 514 4144 4763 4347 749 422 94 O ATOM 2742 CB VAL A 514 15.816 -67.946 8.974 1.00 31.27 C ANISOU 2742 CB VAL A 514 3770 4233 3877 580 244 124 C ATOM 2743 CG1 VAL A 514 15.621 -69.407 8.629 1.00 46.00 C ANISOU 2743 CG1 VAL A 514 5694 6014 5771 651 299 69 C ATOM 2744 CG2 VAL A 514 15.639 -67.738 10.460 1.00 27.34 C ANISOU 2744 CG2 VAL A 514 3266 3712 3411 556 180 183 C ATOM 2745 N SER A 515 17.398 -67.227 6.119 1.00 29.82 N ANISOU 2745 N SER A 515 3511 4218 3601 606 373 83 N ATOM 2746 CA SER A 515 17.745 -67.653 4.770 1.00 38.85 C ANISOU 2746 CA SER A 515 4674 5380 4705 643 459 26 C ATOM 2747 C SER A 515 19.139 -67.175 4.356 1.00 43.77 C ANISOU 2747 C SER A 515 5193 6111 5327 675 508 76 C ATOM 2748 O SER A 515 19.534 -67.325 3.202 1.00 44.63 O ANISOU 2748 O SER A 515 5309 6255 5392 698 587 36 O ATOM 2749 CB SER A 515 16.712 -67.133 3.775 1.00 38.18 C ANISOU 2749 CB SER A 515 4668 5296 4544 559 442 -32 C ATOM 2750 OG SER A 515 16.861 -65.736 3.605 1.00 37.64 O ANISOU 2750 OG SER A 515 4549 5315 4439 485 399 15 O ATOM 2751 N GLY A 516 19.871 -66.583 5.292 1.00 41.12 N ANISOU 2751 N GLY A 516 4763 5828 5033 670 462 165 N ATOM 2752 CA GLY A 516 21.249 -66.196 5.043 1.00 40.46 C ANISOU 2752 CA GLY A 516 4564 5845 4963 702 502 228 C ATOM 2753 C GLY A 516 21.453 -64.954 4.194 1.00 40.94 C ANISOU 2753 C GLY A 516 4595 6005 4956 625 498 243 C ATOM 2754 O GLY A 516 22.559 -64.690 3.733 1.00 45.43 O ANISOU 2754 O GLY A 516 5073 6662 5528 650 549 286 O ATOM 2755 N ARG A 517 20.390 -64.185 3.992 1.00 33.14 N ANISOU 2755 N ARG A 517 3677 5003 3913 532 438 214 N ATOM 2756 CA ARG A 517 20.491 -62.919 3.282 1.00 35.75 C ANISOU 2756 CA ARG A 517 3984 5417 4182 449 419 237 C ATOM 2757 C ARG A 517 20.968 -61.815 4.224 1.00 41.34 C ANISOU 2757 C ARG A 517 4615 6178 4915 393 336 329 C ATOM 2758 O ARG A 517 21.348 -60.728 3.788 1.00 44.55 O ANISOU 2758 O ARG A 517 4979 6664 5284 329 317 370 O ATOM 2759 CB ARG A 517 19.142 -62.547 2.666 1.00 36.42 C ANISOU 2759 CB ARG A 517 4173 5460 4205 374 384 175 C ATOM 2760 CG ARG A 517 18.662 -63.529 1.605 1.00 43.72 C ANISOU 2760 CG ARG A 517 5184 6339 5088 408 456 85 C ATOM 2761 CD ARG A 517 17.455 -62.986 0.846 1.00 48.44 C ANISOU 2761 CD ARG A 517 5868 6918 5619 318 412 42 C ATOM 2762 NE ARG A 517 16.255 -62.962 1.675 1.00 49.15 N ANISOU 2762 NE ARG A 517 6009 6925 5743 283 332 34 N ATOM 2763 CZ ARG A 517 15.318 -63.903 1.653 1.00 53.87 C ANISOU 2763 CZ ARG A 517 6690 7430 6346 297 334 -28 C ATOM 2764 NH1 ARG A 517 15.440 -64.939 0.835 1.00 54.07 N ANISOU 2764 NH1 ARG A 517 6769 7430 6343 344 407 -93 N ATOM 2765 NH2 ARG A 517 14.256 -63.806 2.444 1.00 52.54 N ANISOU 2765 NH2 ARG A 517 6554 7195 6213 262 265 -25 N ATOM 2766 N ARG A 518 20.940 -62.110 5.519 1.00 33.07 N ANISOU 2766 N ARG A 518 3558 5083 3925 412 285 362 N ATOM 2767 CA ARG A 518 21.352 -61.171 6.553 1.00 28.01 C ANISOU 2767 CA ARG A 518 2863 4477 3304 356 201 445 C ATOM 2768 C ARG A 518 22.311 -61.856 7.519 1.00 30.71 C ANISOU 2768 C ARG A 518 3130 4822 3715 422 198 507 C ATOM 2769 O ARG A 518 22.021 -62.939 8.022 1.00 33.16 O ANISOU 2769 O ARG A 518 3476 5059 4067 486 214 481 O ATOM 2770 CB ARG A 518 20.132 -60.656 7.319 1.00 31.70 C ANISOU 2770 CB ARG A 518 3414 4873 3759 288 121 425 C ATOM 2771 CG ARG A 518 20.486 -59.944 8.609 1.00 40.25 C ANISOU 2771 CG ARG A 518 4467 5966 4862 241 38 499 C ATOM 2772 CD ARG A 518 19.246 -59.496 9.363 1.00 42.25 C ANISOU 2772 CD ARG A 518 4810 6141 5103 184 -21 471 C ATOM 2773 NE ARG A 518 19.633 -58.801 10.583 1.00 43.22 N ANISOU 2773 NE ARG A 518 4916 6272 5232 134 -96 537 N ATOM 2774 CZ ARG A 518 19.362 -57.529 10.847 1.00 35.50 C ANISOU 2774 CZ ARG A 518 3962 5301 4223 48 -153 556 C ATOM 2775 NH1 ARG A 518 18.662 -56.789 9.986 1.00 29.45 N ANISOU 2775 NH1 ARG A 518 3231 4533 3424 4 -149 520 N ATOM 2776 NH2 ARG A 518 19.786 -57.005 11.987 1.00 31.47 N ANISOU 2776 NH2 ARG A 518 3448 4795 3716 3 -219 612 N ATOM 2777 N GLN A 519 23.441 -61.205 7.778 1.00 31.02 N ANISOU 2777 N GLN A 519 3066 4949 3772 400 172 596 N ATOM 2778 CA GLN A 519 24.500 -61.745 8.625 1.00 35.39 C ANISOU 2778 CA GLN A 519 3527 5523 4396 455 160 675 C ATOM 2779 C GLN A 519 24.038 -61.851 10.079 1.00 34.06 C ANISOU 2779 C GLN A 519 3406 5286 4249 430 72 699 C ATOM 2780 O GLN A 519 23.611 -60.864 10.675 1.00 33.70 O ANISOU 2780 O GLN A 519 3400 5236 4167 337 -9 715 O ATOM 2781 CB GLN A 519 25.744 -60.858 8.517 1.00 39.18 C ANISOU 2781 CB GLN A 519 3885 6119 4883 416 139 772 C ATOM 2782 CG GLN A 519 26.857 -61.228 9.467 1.00 43.31 C ANISOU 2782 CG GLN A 519 4302 6674 5481 453 104 874 C ATOM 2783 CD GLN A 519 27.358 -62.636 9.236 1.00 46.74 C ANISOU 2783 CD GLN A 519 4688 7086 5985 587 196 865 C ATOM 2784 OE1 GLN A 519 27.012 -63.558 9.975 1.00 47.70 O ANISOU 2784 OE1 GLN A 519 4852 7125 6146 640 183 852 O ATOM 2785 NE2 GLN A 519 28.165 -62.813 8.197 1.00 42.67 N ANISOU 2785 NE2 GLN A 519 4088 6640 5484 644 293 873 N ATOM 2786 N THR A 520 24.122 -63.050 10.648 1.00 28.67 N ANISOU 2786 N THR A 520 2724 4545 3623 513 90 700 N ATOM 2787 CA THR A 520 23.624 -63.275 12.006 1.00 29.25 C ANISOU 2787 CA THR A 520 2854 4550 3711 491 14 719 C ATOM 2788 C THR A 520 24.710 -63.217 13.080 1.00 34.26 C ANISOU 2788 C THR A 520 3399 5226 4390 485 -55 833 C ATOM 2789 O THR A 520 24.405 -63.195 14.270 1.00 32.87 O ANISOU 2789 O THR A 520 3270 5007 4212 446 -130 862 O ATOM 2790 CB THR A 520 22.892 -64.628 12.120 1.00 27.12 C ANISOU 2790 CB THR A 520 2657 4175 3471 570 60 655 C ATOM 2791 OG1 THR A 520 23.708 -65.659 11.559 1.00 26.28 O ANISOU 2791 OG1 THR A 520 2483 4078 3423 679 140 661 O ATOM 2792 CG2 THR A 520 21.571 -64.584 11.373 1.00 31.10 C ANISOU 2792 CG2 THR A 520 3269 4624 3924 545 94 549 C ATOM 2793 N LYS A 521 25.973 -63.212 12.660 1.00 36.38 N ANISOU 2793 N LYS A 521 3541 5581 4701 523 -28 902 N ATOM 2794 CA LYS A 521 27.090 -63.126 13.597 1.00 36.53 C ANISOU 2794 CA LYS A 521 3458 5651 4769 513 -101 1024 C ATOM 2795 C LYS A 521 27.361 -61.681 13.984 1.00 38.19 C ANISOU 2795 C LYS A 521 3654 5928 4930 385 -195 1082 C ATOM 2796 O LYS A 521 27.519 -60.818 13.131 1.00 40.89 O ANISOU 2796 O LYS A 521 3969 6333 5235 340 -174 1073 O ATOM 2797 CB LYS A 521 28.362 -63.732 13.003 1.00 40.87 C ANISOU 2797 CB LYS A 521 3863 6268 5397 609 -31 1085 C ATOM 2798 CG LYS A 521 28.335 -65.237 12.811 1.00 47.86 C ANISOU 2798 CG LYS A 521 4752 7084 6351 745 55 1049 C ATOM 2799 CD LYS A 521 29.732 -65.748 12.470 1.00 57.00 C ANISOU 2799 CD LYS A 521 5748 8309 7600 839 112 1134 C ATOM 2800 CE LYS A 521 29.690 -67.137 11.859 1.00 64.75 C ANISOU 2800 CE LYS A 521 6741 9222 8641 983 233 1072 C ATOM 2801 NZ LYS A 521 29.034 -68.126 12.762 1.00 68.71 N ANISOU 2801 NZ LYS A 521 7328 9606 9171 1021 198 1052 N ATOM 2802 N GLU A 522 27.425 -61.430 15.282 1.00 44.46 N ANISOU 2802 N GLU A 522 4472 6704 5717 322 -300 1143 N ATOM 2803 CA GLU A 522 27.689 -60.098 15.799 1.00 45.65 C ANISOU 2803 CA GLU A 522 4624 6903 5817 194 -399 1198 C ATOM 2804 C GLU A 522 27.955 -60.257 17.279 1.00 41.81 C ANISOU 2804 C GLU A 522 4154 6394 5339 154 -504 1275 C ATOM 2805 O GLU A 522 27.406 -61.160 17.918 1.00 35.83 O ANISOU 2805 O GLU A 522 3460 5558 4594 201 -501 1249 O ATOM 2806 CB GLU A 522 26.480 -59.183 15.569 1.00 49.14 C ANISOU 2806 CB GLU A 522 5195 7299 6176 117 -403 1106 C ATOM 2807 CG GLU A 522 26.657 -57.751 16.064 1.00 53.36 C ANISOU 2807 CG GLU A 522 5752 7868 6654 -16 -499 1150 C ATOM 2808 CD GLU A 522 25.471 -56.852 15.719 1.00 61.42 C ANISOU 2808 CD GLU A 522 6891 8839 7607 -77 -490 1060 C ATOM 2809 OE1 GLU A 522 24.914 -56.984 14.606 1.00 67.41 O ANISOU 2809 OE1 GLU A 522 7661 9590 8362 -34 -409 988 O ATOM 2810 OE2 GLU A 522 25.102 -56.006 16.558 1.00 57.92 O ANISOU 2810 OE2 GLU A 522 6530 8363 7115 -170 -565 1064 O ATOM 2811 N GLY A 523 28.805 -59.395 17.822 1.00 38.93 N ANISOU 2811 N GLY A 523 3734 6096 4961 62 -601 1372 N ATOM 2812 CA GLY A 523 29.129 -59.428 19.238 1.00 42.71 C ANISOU 2812 CA GLY A 523 4233 6562 5434 3 -715 1453 C ATOM 2813 C GLY A 523 29.818 -60.705 19.687 1.00 52.71 C ANISOU 2813 C GLY A 523 5412 7827 6789 98 -717 1529 C ATOM 2814 O GLY A 523 29.672 -61.129 20.838 1.00 49.22 O ANISOU 2814 O GLY A 523 5025 7336 6339 79 -787 1564 O ATOM 2815 N GLY A 524 30.574 -61.317 18.778 1.00 54.68 N ANISOU 2815 N GLY A 524 5526 8127 7121 201 -637 1557 N ATOM 2816 CA GLY A 524 31.314 -62.528 19.083 1.00 49.82 C ANISOU 2816 CA GLY A 524 4810 7512 6607 305 -628 1635 C ATOM 2817 C GLY A 524 30.438 -63.761 19.189 1.00 50.82 C ANISOU 2817 C GLY A 524 5025 7529 6754 405 -562 1554 C ATOM 2818 O GLY A 524 30.827 -64.753 19.805 1.00 49.78 O ANISOU 2818 O GLY A 524 4853 7368 6692 471 -582 1618 O ATOM 2819 N TYR A 525 29.254 -63.707 18.585 1.00 41.50 N ANISOU 2819 N TYR A 525 3964 6288 5518 412 -488 1420 N ATOM 2820 CA TYR A 525 28.330 -64.835 18.631 1.00 44.82 C ANISOU 2820 CA TYR A 525 4475 6601 5952 494 -426 1338 C ATOM 2821 C TYR A 525 27.438 -64.874 17.387 1.00 40.63 C ANISOU 2821 C TYR A 525 4009 6038 5392 533 -313 1205 C ATOM 2822 O TYR A 525 27.142 -63.834 16.795 1.00 40.06 O ANISOU 2822 O TYR A 525 3960 6003 5257 464 -306 1162 O ATOM 2823 CB TYR A 525 27.477 -64.775 19.908 1.00 53.92 C ANISOU 2823 CB TYR A 525 5761 7680 7045 419 -509 1328 C ATOM 2824 CG TYR A 525 26.718 -66.052 20.209 1.00 56.90 C ANISOU 2824 CG TYR A 525 6215 7953 7453 498 -467 1279 C ATOM 2825 CD1 TYR A 525 27.355 -67.139 20.798 1.00 60.99 C ANISOU 2825 CD1 TYR A 525 6674 8448 8051 572 -489 1361 C ATOM 2826 CD2 TYR A 525 25.365 -66.171 19.906 1.00 59.49 C ANISOU 2826 CD2 TYR A 525 6670 8201 7731 496 -410 1158 C ATOM 2827 CE1 TYR A 525 26.669 -68.310 21.073 1.00 62.54 C ANISOU 2827 CE1 TYR A 525 6943 8542 8276 641 -453 1320 C ATOM 2828 CE2 TYR A 525 24.669 -67.338 20.178 1.00 60.54 C ANISOU 2828 CE2 TYR A 525 6872 8238 7893 561 -376 1118 C ATOM 2829 CZ TYR A 525 25.327 -68.404 20.761 1.00 62.74 C ANISOU 2829 CZ TYR A 525 7098 8492 8248 632 -397 1197 C ATOM 2830 OH TYR A 525 24.643 -69.566 21.036 1.00 59.78 O ANISOU 2830 OH TYR A 525 6794 8016 7902 692 -365 1161 O ATOM 2831 N ASP A 526 27.038 -66.080 16.985 1.00 32.55 N ANISOU 2831 N ASP A 526 3012 4942 4412 641 -228 1145 N ATOM 2832 CA ASP A 526 26.080 -66.269 15.896 1.00 31.89 C ANISOU 2832 CA ASP A 526 3009 4813 4297 673 -131 1017 C ATOM 2833 C ASP A 526 24.665 -66.302 16.471 1.00 31.89 C ANISOU 2833 C ASP A 526 3158 4719 4239 622 -158 942 C ATOM 2834 O ASP A 526 24.275 -67.266 17.123 1.00 32.81 O ANISOU 2834 O ASP A 526 3325 4755 4385 663 -163 939 O ATOM 2835 CB ASP A 526 26.372 -67.574 15.151 1.00 37.14 C ANISOU 2835 CB ASP A 526 3637 5440 5036 812 -24 987 C ATOM 2836 CG ASP A 526 25.516 -67.742 13.907 1.00 39.63 C ANISOU 2836 CG ASP A 526 4029 5718 5310 837 75 859 C ATOM 2837 OD1 ASP A 526 25.864 -68.580 13.048 1.00 41.20 O ANISOU 2837 OD1 ASP A 526 4197 5903 5553 940 174 825 O ATOM 2838 OD2 ASP A 526 24.496 -67.033 13.781 1.00 36.56 O ANISOU 2838 OD2 ASP A 526 3735 5313 4845 754 53 793 O ATOM 2839 N HIS A 527 23.898 -65.249 16.215 1.00 24.90 N ANISOU 2839 N HIS A 527 2341 3844 3278 533 -172 887 N ATOM 2840 CA HIS A 527 22.585 -65.086 16.823 1.00 21.82 C ANISOU 2840 CA HIS A 527 2081 3376 2835 475 -200 828 C ATOM 2841 C HIS A 527 21.459 -65.749 16.050 1.00 27.07 C ANISOU 2841 C HIS A 527 2826 3965 3495 519 -122 720 C ATOM 2842 O HIS A 527 20.296 -65.432 16.281 1.00 24.98 O ANISOU 2842 O HIS A 527 2656 3647 3186 465 -133 664 O ATOM 2843 CB HIS A 527 22.259 -63.598 16.963 1.00 30.03 C ANISOU 2843 CB HIS A 527 3155 4452 3802 360 -253 824 C ATOM 2844 CG HIS A 527 23.092 -62.892 17.982 1.00 40.57 C ANISOU 2844 CG HIS A 527 4453 5839 5123 289 -349 922 C ATOM 2845 ND1 HIS A 527 24.412 -62.559 17.764 1.00 43.21 N ANISOU 2845 ND1 HIS A 527 4666 6266 5487 288 -374 1007 N ATOM 2846 CD2 HIS A 527 22.790 -62.444 19.224 1.00 47.99 C ANISOU 2846 CD2 HIS A 527 5463 6751 6019 210 -428 950 C ATOM 2847 CE1 HIS A 527 24.889 -61.943 18.830 1.00 41.14 C ANISOU 2847 CE1 HIS A 527 4401 6030 5200 206 -474 1086 C ATOM 2848 NE2 HIS A 527 23.926 -61.861 19.731 1.00 54.27 N ANISOU 2848 NE2 HIS A 527 6186 7619 6814 157 -507 1050 N ATOM 2849 N ALA A 528 21.786 -66.653 15.133 1.00 26.10 N ANISOU 2849 N ALA A 528 2666 3834 3418 613 -42 690 N ATOM 2850 CA ALA A 528 20.748 -67.269 14.300 1.00 26.24 C ANISOU 2850 CA ALA A 528 2765 3781 3423 645 27 586 C ATOM 2851 C ALA A 528 19.617 -67.860 15.143 1.00 25.74 C ANISOU 2851 C ALA A 528 2804 3617 3358 630 3 555 C ATOM 2852 O ALA A 528 18.454 -67.785 14.772 1.00 20.52 O ANISOU 2852 O ALA A 528 2225 2908 2664 598 21 480 O ATOM 2853 CB ALA A 528 21.347 -68.334 13.387 1.00 22.61 C ANISOU 2853 CB ALA A 528 2264 3313 3016 756 116 562 C ATOM 2854 N ILE A 529 19.971 -68.435 16.283 1.00 22.94 N ANISOU 2854 N ILE A 529 2441 3233 3041 650 -41 621 N ATOM 2855 CA ILE A 529 18.987 -69.011 17.185 1.00 23.67 C ANISOU 2855 CA ILE A 529 2627 3236 3132 632 -65 605 C ATOM 2856 C ILE A 529 17.923 -68.000 17.619 1.00 23.37 C ANISOU 2856 C ILE A 529 2663 3190 3026 530 -102 575 C ATOM 2857 O ILE A 529 16.752 -68.350 17.769 1.00 26.41 O ANISOU 2857 O ILE A 529 3132 3502 3401 514 -87 522 O ATOM 2858 CB ILE A 529 19.673 -69.642 18.422 1.00 32.00 C ANISOU 2858 CB ILE A 529 3654 4274 4229 657 -119 699 C ATOM 2859 CG1 ILE A 529 18.670 -70.441 19.249 1.00 31.99 C ANISOU 2859 CG1 ILE A 529 3751 4174 4231 650 -130 681 C ATOM 2860 CG2 ILE A 529 20.337 -68.579 19.284 1.00 30.84 C ANISOU 2860 CG2 ILE A 529 3468 4203 4048 580 -203 782 C ATOM 2861 CD1 ILE A 529 19.312 -71.144 20.427 1.00 39.56 C ANISOU 2861 CD1 ILE A 529 4691 5111 5230 673 -185 776 C ATOM 2862 N SER A 530 18.317 -66.742 17.799 1.00 20.19 N ANISOU 2862 N SER A 530 2230 2860 2582 461 -146 609 N ATOM 2863 CA SER A 530 17.354 -65.713 18.180 1.00 19.92 C ANISOU 2863 CA SER A 530 2266 2814 2487 371 -173 580 C ATOM 2864 C SER A 530 16.378 -65.427 17.045 1.00 21.63 C ANISOU 2864 C SER A 530 2518 3014 2688 363 -122 493 C ATOM 2865 O SER A 530 15.169 -65.332 17.258 1.00 21.27 O ANISOU 2865 O SER A 530 2547 2912 2625 328 -115 448 O ATOM 2866 CB SER A 530 18.070 -64.430 18.603 1.00 22.04 C ANISOU 2866 CB SER A 530 2500 3158 2716 299 -235 637 C ATOM 2867 OG SER A 530 18.764 -64.633 19.815 1.00 25.75 O ANISOU 2867 OG SER A 530 2960 3635 3190 285 -297 718 O ATOM 2868 N PHE A 531 16.900 -65.282 15.834 1.00 18.38 N ANISOU 2868 N PHE A 531 2049 2653 2279 391 -86 474 N ATOM 2869 CA PHE A 531 16.036 -65.016 14.689 1.00 21.08 C ANISOU 2869 CA PHE A 531 2424 2985 2600 377 -45 399 C ATOM 2870 C PHE A 531 15.074 -66.178 14.433 1.00 20.42 C ANISOU 2870 C PHE A 531 2404 2814 2541 418 -4 338 C ATOM 2871 O PHE A 531 13.920 -65.969 14.048 1.00 20.28 O ANISOU 2871 O PHE A 531 2442 2760 2506 381 5 284 O ATOM 2872 CB PHE A 531 16.865 -64.732 13.438 1.00 18.79 C ANISOU 2872 CB PHE A 531 2066 2770 2303 401 -10 394 C ATOM 2873 CG PHE A 531 17.591 -63.419 13.480 1.00 22.11 C ANISOU 2873 CG PHE A 531 2431 3276 2694 342 -52 446 C ATOM 2874 CD1 PHE A 531 16.941 -62.240 13.143 1.00 22.29 C ANISOU 2874 CD1 PHE A 531 2483 3312 2672 267 -72 424 C ATOM 2875 CD2 PHE A 531 18.926 -63.362 13.857 1.00 24.84 C ANISOU 2875 CD2 PHE A 531 2692 3685 3060 360 -74 523 C ATOM 2876 CE1 PHE A 531 17.609 -61.024 13.186 1.00 21.74 C ANISOU 2876 CE1 PHE A 531 2370 3314 2576 208 -114 472 C ATOM 2877 CE2 PHE A 531 19.603 -62.154 13.892 1.00 22.97 C ANISOU 2877 CE2 PHE A 531 2405 3526 2796 296 -118 575 C ATOM 2878 CZ PHE A 531 18.944 -60.985 13.560 1.00 26.42 C ANISOU 2878 CZ PHE A 531 2883 3971 3185 219 -138 547 C ATOM 2879 N GLN A 532 15.556 -67.399 14.630 1.00 19.87 N ANISOU 2879 N GLN A 532 2325 2710 2516 492 19 350 N ATOM 2880 CA GLN A 532 14.711 -68.579 14.466 1.00 18.80 C ANISOU 2880 CA GLN A 532 2254 2483 2407 528 53 297 C ATOM 2881 C GLN A 532 13.566 -68.554 15.474 1.00 19.16 C ANISOU 2881 C GLN A 532 2369 2466 2446 475 21 296 C ATOM 2882 O GLN A 532 12.436 -68.939 15.177 1.00 18.19 O ANISOU 2882 O GLN A 532 2305 2281 2324 460 38 244 O ATOM 2883 CB GLN A 532 15.539 -69.853 14.638 1.00 22.81 C ANISOU 2883 CB GLN A 532 2738 2959 2971 619 79 321 C ATOM 2884 CG GLN A 532 16.460 -70.130 13.462 1.00 36.74 C ANISOU 2884 CG GLN A 532 4448 4765 4748 686 138 302 C ATOM 2885 CD GLN A 532 17.448 -71.244 13.738 1.00 50.56 C ANISOU 2885 CD GLN A 532 6156 6490 6565 784 164 342 C ATOM 2886 OE1 GLN A 532 18.331 -71.523 12.922 1.00 57.59 O ANISOU 2886 OE1 GLN A 532 6992 7414 7476 851 221 337 O ATOM 2887 NE2 GLN A 532 17.314 -71.879 14.896 1.00 53.27 N ANISOU 2887 NE2 GLN A 532 6522 6775 6944 794 125 386 N ATOM 2888 N ASP A 533 13.879 -68.088 16.671 1.00 19.85 N ANISOU 2888 N ASP A 533 2448 2571 2524 443 -26 358 N ATOM 2889 CA ASP A 533 12.907 -68.006 17.749 1.00 16.65 C ANISOU 2889 CA ASP A 533 2107 2113 2105 393 -50 364 C ATOM 2890 C ASP A 533 11.834 -66.984 17.376 1.00 20.82 C ANISOU 2890 C ASP A 533 2666 2643 2600 328 -45 319 C ATOM 2891 O ASP A 533 10.634 -67.284 17.406 1.00 21.28 O ANISOU 2891 O ASP A 533 2776 2641 2668 310 -27 283 O ATOM 2892 CB ASP A 533 13.647 -67.591 19.027 1.00 24.84 C ANISOU 2892 CB ASP A 533 3131 3181 3125 367 -103 441 C ATOM 2893 CG ASP A 533 12.836 -67.800 20.282 1.00 39.26 C ANISOU 2893 CG ASP A 533 5030 4948 4937 328 -119 456 C ATOM 2894 OD1 ASP A 533 11.602 -67.691 20.234 1.00 41.45 O ANISOU 2894 OD1 ASP A 533 5361 5181 5208 297 -94 409 O ATOM 2895 OD2 ASP A 533 13.448 -68.063 21.334 1.00 55.76 O ANISOU 2895 OD2 ASP A 533 7122 7040 7023 326 -159 520 O ATOM 2896 N TRP A 534 12.258 -65.780 16.998 1.00 15.20 N ANISOU 2896 N TRP A 534 1919 2001 1857 293 -62 327 N ATOM 2897 CA TRP A 534 11.300 -64.735 16.638 1.00 15.02 C ANISOU 2897 CA TRP A 534 1919 1978 1809 234 -61 293 C ATOM 2898 C TRP A 534 10.475 -65.124 15.424 1.00 14.24 C ANISOU 2898 C TRP A 534 1832 1853 1725 246 -27 233 C ATOM 2899 O TRP A 534 9.289 -64.812 15.338 1.00 16.76 O ANISOU 2899 O TRP A 534 2186 2136 2048 209 -22 205 O ATOM 2900 CB TRP A 534 12.013 -63.404 16.372 1.00 15.92 C ANISOU 2900 CB TRP A 534 1991 2168 1888 195 -89 317 C ATOM 2901 CG TRP A 534 12.853 -62.948 17.522 1.00 14.86 C ANISOU 2901 CG TRP A 534 1850 2063 1733 170 -133 379 C ATOM 2902 CD1 TRP A 534 12.563 -63.062 18.853 1.00 15.55 C ANISOU 2902 CD1 TRP A 534 1990 2110 1809 147 -152 403 C ATOM 2903 CD2 TRP A 534 14.113 -62.281 17.438 1.00 16.05 C ANISOU 2903 CD2 TRP A 534 1941 2292 1866 157 -167 427 C ATOM 2904 NE1 TRP A 534 13.583 -62.525 19.606 1.00 17.31 N ANISOU 2904 NE1 TRP A 534 2195 2379 2003 117 -202 463 N ATOM 2905 CE2 TRP A 534 14.549 -62.044 18.762 1.00 17.43 C ANISOU 2905 CE2 TRP A 534 2137 2468 2019 122 -215 481 C ATOM 2906 CE3 TRP A 534 14.929 -61.886 16.374 1.00 18.05 C ANISOU 2906 CE3 TRP A 534 2125 2616 2118 167 -163 434 C ATOM 2907 CZ2 TRP A 534 15.758 -61.424 19.048 1.00 18.12 C ANISOU 2907 CZ2 TRP A 534 2176 2623 2087 94 -266 544 C ATOM 2908 CZ3 TRP A 534 16.136 -61.264 16.660 1.00 19.02 C ANISOU 2908 CZ3 TRP A 534 2192 2809 2226 143 -206 498 C ATOM 2909 CH2 TRP A 534 16.536 -61.038 17.986 1.00 19.75 C ANISOU 2909 CH2 TRP A 534 2304 2899 2301 105 -261 554 C ATOM 2910 N LEU A 535 11.118 -65.781 14.467 1.00 15.02 N ANISOU 2910 N LEU A 535 1903 1972 1834 295 -3 215 N ATOM 2911 CA LEU A 535 10.421 -66.212 13.267 1.00 15.29 C ANISOU 2911 CA LEU A 535 1959 1980 1870 301 25 155 C ATOM 2912 C LEU A 535 9.305 -67.183 13.640 1.00 15.94 C ANISOU 2912 C LEU A 535 2100 1973 1984 302 35 130 C ATOM 2913 O LEU A 535 8.178 -67.065 13.156 1.00 19.41 O ANISOU 2913 O LEU A 535 2569 2382 2425 264 35 97 O ATOM 2914 CB LEU A 535 11.387 -66.884 12.294 1.00 15.25 C ANISOU 2914 CB LEU A 535 1926 2004 1866 360 61 137 C ATOM 2915 CG LEU A 535 10.753 -67.434 11.018 1.00 20.43 C ANISOU 2915 CG LEU A 535 2621 2630 2512 363 91 71 C ATOM 2916 CD1 LEU A 535 9.861 -66.394 10.362 1.00 20.37 C ANISOU 2916 CD1 LEU A 535 2623 2644 2473 291 68 52 C ATOM 2917 CD2 LEU A 535 11.846 -67.903 10.064 1.00 25.58 C ANISOU 2917 CD2 LEU A 535 3245 3321 3152 422 137 53 C ATOM 2918 N LYS A 536 9.631 -68.137 14.506 1.00 15.57 N ANISOU 2918 N LYS A 536 2067 1885 1964 342 38 154 N ATOM 2919 CA LYS A 536 8.656 -69.135 14.964 1.00 18.26 C ANISOU 2919 CA LYS A 536 2463 2139 2337 342 46 139 C ATOM 2920 C LYS A 536 7.439 -68.496 15.632 1.00 20.13 C ANISOU 2920 C LYS A 536 2726 2351 2572 279 33 146 C ATOM 2921 O LYS A 536 6.311 -68.964 15.471 1.00 15.53 O ANISOU 2921 O LYS A 536 2178 1712 2012 257 42 120 O ATOM 2922 CB LYS A 536 9.332 -70.133 15.915 1.00 23.81 C ANISOU 2922 CB LYS A 536 3172 2806 3067 393 45 179 C ATOM 2923 CG LYS A 536 8.438 -71.267 16.378 1.00 35.43 C ANISOU 2923 CG LYS A 536 4703 4186 4574 395 53 169 C ATOM 2924 CD LYS A 536 9.255 -72.494 16.816 1.00 52.47 C ANISOU 2924 CD LYS A 536 6867 6303 6768 464 59 196 C ATOM 2925 CE LYS A 536 9.387 -72.600 18.338 1.00 54.86 C ANISOU 2925 CE LYS A 536 7179 6590 7074 453 30 264 C ATOM 2926 NZ LYS A 536 10.460 -71.740 18.931 1.00 51.88 N ANISOU 2926 NZ LYS A 536 6750 6291 6670 451 0 320 N ATOM 2927 N LYS A 537 7.657 -67.416 16.377 1.00 17.24 N ANISOU 2927 N LYS A 537 2344 2026 2181 247 15 181 N ATOM 2928 CA LYS A 537 6.539 -66.714 17.012 1.00 14.90 C ANISOU 2928 CA LYS A 537 2072 1706 1883 193 15 184 C ATOM 2929 C LYS A 537 5.664 -66.026 15.967 1.00 18.74 C ANISOU 2929 C LYS A 537 2546 2200 2374 159 18 150 C ATOM 2930 O LYS A 537 4.443 -66.097 16.015 1.00 16.64 O ANISOU 2930 O LYS A 537 2298 1889 2136 131 29 138 O ATOM 2931 CB LYS A 537 7.052 -65.698 18.040 1.00 17.94 C ANISOU 2931 CB LYS A 537 2456 2128 2234 167 -3 224 C ATOM 2932 CG LYS A 537 7.776 -66.347 19.223 1.00 18.82 C ANISOU 2932 CG LYS A 537 2586 2228 2337 187 -16 269 C ATOM 2933 CD LYS A 537 8.762 -65.395 19.880 1.00 28.66 C ANISOU 2933 CD LYS A 537 3819 3531 3540 164 -50 311 C ATOM 2934 CE LYS A 537 8.227 -64.796 21.152 1.00 31.00 C ANISOU 2934 CE LYS A 537 4171 3805 3804 114 -50 329 C ATOM 2935 NZ LYS A 537 8.256 -65.778 22.266 1.00 27.38 N ANISOU 2935 NZ LYS A 537 3752 3305 3344 123 -52 363 N ATOM 2936 N LEU A 538 6.291 -65.361 15.012 1.00 16.79 N ANISOU 2936 N LEU A 538 2264 2012 2104 159 6 140 N ATOM 2937 CA LEU A 538 5.530 -64.741 13.935 1.00 17.62 C ANISOU 2937 CA LEU A 538 2358 2127 2210 125 1 113 C ATOM 2938 C LEU A 538 4.762 -65.771 13.097 1.00 18.58 C ANISOU 2938 C LEU A 538 2503 2203 2356 127 8 76 C ATOM 2939 O LEU A 538 3.595 -65.566 12.755 1.00 21.29 O ANISOU 2939 O LEU A 538 2850 2518 2721 88 1 67 O ATOM 2940 CB LEU A 538 6.457 -63.904 13.049 1.00 13.30 C ANISOU 2940 CB LEU A 538 1772 1655 1626 122 -13 114 C ATOM 2941 CG LEU A 538 7.084 -62.707 13.779 1.00 15.47 C ANISOU 2941 CG LEU A 538 2027 1973 1877 101 -31 152 C ATOM 2942 CD1 LEU A 538 8.241 -62.099 12.981 1.00 14.40 C ANISOU 2942 CD1 LEU A 538 1849 1916 1707 103 -44 162 C ATOM 2943 CD2 LEU A 538 6.041 -61.651 14.106 1.00 15.70 C ANISOU 2943 CD2 LEU A 538 2069 1979 1918 54 -37 157 C ATOM 2944 N HIS A 539 5.419 -66.870 12.759 1.00 17.66 N ANISOU 2944 N HIS A 539 2401 2075 2236 171 21 57 N ATOM 2945 CA HIS A 539 4.798 -67.901 11.932 1.00 19.47 C ANISOU 2945 CA HIS A 539 2666 2254 2479 171 27 15 C ATOM 2946 C HIS A 539 3.596 -68.505 12.654 1.00 24.54 C ANISOU 2946 C HIS A 539 3338 2821 3165 147 26 23 C ATOM 2947 O HIS A 539 2.547 -68.766 12.059 1.00 18.58 O ANISOU 2947 O HIS A 539 2600 2031 2429 108 13 4 O ATOM 2948 CB HIS A 539 5.814 -69.001 11.627 1.00 26.14 C ANISOU 2948 CB HIS A 539 3527 3088 3316 234 51 -6 C ATOM 2949 CG HIS A 539 5.239 -70.169 10.889 1.00 34.48 C ANISOU 2949 CG HIS A 539 4639 4079 4384 235 59 -53 C ATOM 2950 ND1 HIS A 539 4.640 -71.232 11.529 1.00 41.65 N ANISOU 2950 ND1 HIS A 539 5589 4905 5332 240 61 -52 N ATOM 2951 CD2 HIS A 539 5.183 -70.444 9.564 1.00 38.54 C ANISOU 2951 CD2 HIS A 539 5181 4594 4869 225 64 -103 C ATOM 2952 CE1 HIS A 539 4.233 -72.112 10.629 1.00 41.41 C ANISOU 2952 CE1 HIS A 539 5610 4824 5299 232 64 -100 C ATOM 2953 NE2 HIS A 539 4.551 -71.657 9.430 1.00 38.89 N ANISOU 2953 NE2 HIS A 539 5287 4554 4935 223 66 -134 N ATOM 2954 N SER A 540 3.758 -68.731 13.948 1.00 19.92 N ANISOU 2954 N SER A 540 2759 2214 2595 165 36 57 N ATOM 2955 CA SER A 540 2.676 -69.272 14.749 1.00 22.87 C ANISOU 2955 CA SER A 540 3158 2522 3007 141 43 71 C ATOM 2956 C SER A 540 1.471 -68.325 14.829 1.00 18.29 C ANISOU 2956 C SER A 540 2558 1944 2448 86 39 84 C ATOM 2957 O SER A 540 0.325 -68.767 14.764 1.00 19.55 O ANISOU 2957 O SER A 540 2727 2056 2647 54 39 83 O ATOM 2958 CB SER A 540 3.179 -69.625 16.148 1.00 24.99 C ANISOU 2958 CB SER A 540 3443 2775 3278 167 54 110 C ATOM 2959 OG SER A 540 2.088 -69.943 16.990 1.00 35.70 O ANISOU 2959 OG SER A 540 4821 4077 4664 136 67 130 O ATOM 2960 N ARG A 541 1.725 -67.030 14.986 1.00 13.53 N ANISOU 2960 N ARG A 541 1924 1393 1824 75 37 99 N ATOM 2961 CA ARG A 541 0.638 -66.047 15.012 1.00 14.40 C ANISOU 2961 CA ARG A 541 2009 1501 1959 33 39 112 C ATOM 2962 C ARG A 541 -0.040 -65.964 13.653 1.00 15.31 C ANISOU 2962 C ARG A 541 2105 1620 2091 2 11 92 C ATOM 2963 O ARG A 541 -1.265 -65.963 13.548 1.00 16.60 O ANISOU 2963 O ARG A 541 2255 1750 2301 -33 8 103 O ATOM 2964 CB ARG A 541 1.151 -64.654 15.415 1.00 14.20 C ANISOU 2964 CB ARG A 541 1966 1524 1907 30 41 129 C ATOM 2965 CG ARG A 541 0.031 -63.607 15.500 1.00 14.77 C ANISOU 2965 CG ARG A 541 2014 1584 2013 -5 51 143 C ATOM 2966 CD ARG A 541 -1.022 -63.983 16.564 1.00 20.13 C ANISOU 2966 CD ARG A 541 2708 2207 2735 -13 92 161 C ATOM 2967 NE ARG A 541 -0.412 -64.019 17.888 1.00 21.61 N ANISOU 2967 NE ARG A 541 2935 2390 2887 2 118 175 N ATOM 2968 CZ ARG A 541 -0.458 -63.025 18.771 1.00 25.06 C ANISOU 2968 CZ ARG A 541 3386 2829 3307 -6 146 188 C ATOM 2969 NH1 ARG A 541 -1.128 -61.913 18.499 1.00 19.98 N ANISOU 2969 NH1 ARG A 541 2716 2185 2691 -22 157 189 N ATOM 2970 NH2 ARG A 541 0.165 -63.147 19.937 1.00 21.18 N ANISOU 2970 NH2 ARG A 541 2940 2335 2771 0 161 200 N ATOM 2971 N VAL A 542 0.759 -65.912 12.598 1.00 15.20 N ANISOU 2971 N VAL A 542 2090 1648 2038 12 -9 67 N ATOM 2972 CA VAL A 542 0.186 -65.749 11.270 1.00 19.35 C ANISOU 2972 CA VAL A 542 2605 2183 2564 -26 -42 50 C ATOM 2973 C VAL A 542 -0.681 -66.958 10.898 1.00 19.01 C ANISOU 2973 C VAL A 542 2593 2080 2550 -48 -53 33 C ATOM 2974 O VAL A 542 -1.753 -66.809 10.306 1.00 20.51 O ANISOU 2974 O VAL A 542 2767 2255 2770 -98 -83 42 O ATOM 2975 CB VAL A 542 1.277 -65.507 10.237 1.00 19.36 C ANISOU 2975 CB VAL A 542 2607 2243 2507 -13 -53 26 C ATOM 2976 CG1 VAL A 542 0.740 -65.724 8.835 1.00 20.21 C ANISOU 2976 CG1 VAL A 542 2727 2351 2600 -54 -86 1 C ATOM 2977 CG2 VAL A 542 1.853 -64.088 10.419 1.00 18.34 C ANISOU 2977 CG2 VAL A 542 2438 2173 2355 -14 -56 52 C ATOM 2978 N THR A 543 -0.212 -68.144 11.276 1.00 14.99 N ANISOU 2978 N THR A 543 2126 1533 2036 -14 -34 15 N ATOM 2979 CA THR A 543 -0.930 -69.393 11.073 1.00 20.79 C ANISOU 2979 CA THR A 543 2901 2200 2798 -33 -43 -1 C ATOM 2980 C THR A 543 -2.278 -69.354 11.774 1.00 18.97 C ANISOU 2980 C THR A 543 2648 1929 2631 -75 -44 38 C ATOM 2981 O THR A 543 -3.316 -69.604 11.161 1.00 21.88 O ANISOU 2981 O THR A 543 3013 2270 3029 -128 -76 41 O ATOM 2982 CB THR A 543 -0.124 -70.594 11.633 1.00 29.43 C ANISOU 2982 CB THR A 543 4042 3254 3885 21 -16 -17 C ATOM 2983 OG1 THR A 543 1.062 -70.782 10.855 1.00 27.47 O ANISOU 2983 OG1 THR A 543 3812 3037 3589 63 -7 -55 O ATOM 2984 CG2 THR A 543 -0.946 -71.878 11.604 1.00 29.24 C ANISOU 2984 CG2 THR A 543 4066 3147 3897 -4 -26 -28 C ATOM 2985 N LYS A 544 -2.256 -69.030 13.061 1.00 18.43 N ANISOU 2985 N LYS A 544 2563 1858 2580 -54 -9 70 N ATOM 2986 CA LYS A 544 -3.470 -68.980 13.869 1.00 20.06 C ANISOU 2986 CA LYS A 544 2747 2028 2846 -85 8 109 C ATOM 2987 C LYS A 544 -4.466 -67.958 13.349 1.00 19.90 C ANISOU 2987 C LYS A 544 2670 2029 2864 -128 -10 132 C ATOM 2988 O LYS A 544 -5.662 -68.181 13.402 1.00 18.08 O ANISOU 2988 O LYS A 544 2413 1764 2692 -168 -15 159 O ATOM 2989 CB LYS A 544 -3.136 -68.621 15.315 1.00 19.40 C ANISOU 2989 CB LYS A 544 2665 1948 2756 -55 55 136 C ATOM 2990 CG LYS A 544 -2.502 -69.751 16.129 1.00 22.19 C ANISOU 2990 CG LYS A 544 3069 2267 3094 -23 71 136 C ATOM 2991 CD LYS A 544 -2.207 -69.204 17.509 1.00 25.04 C ANISOU 2991 CD LYS A 544 3435 2640 3438 -6 110 166 C ATOM 2992 CE LYS A 544 -1.379 -70.133 18.339 1.00 32.85 C ANISOU 2992 CE LYS A 544 4470 3607 4403 27 117 176 C ATOM 2993 NZ LYS A 544 -1.004 -69.445 19.604 1.00 28.62 N ANISOU 2993 NZ LYS A 544 3945 3094 3835 33 144 205 N ATOM 2994 N GLU A 545 -3.971 -66.824 12.871 1.00 17.00 N ANISOU 2994 N GLU A 545 2277 1715 2467 -120 -21 127 N ATOM 2995 CA GLU A 545 -4.853 -65.742 12.459 1.00 15.85 C ANISOU 2995 CA GLU A 545 2073 1586 2362 -153 -37 157 C ATOM 2996 C GLU A 545 -4.962 -65.615 10.938 1.00 15.37 C ANISOU 2996 C GLU A 545 2005 1551 2286 -191 -100 144 C ATOM 2997 O GLU A 545 -5.342 -64.562 10.416 1.00 15.12 O ANISOU 2997 O GLU A 545 1927 1546 2271 -213 -124 167 O ATOM 2998 CB GLU A 545 -4.386 -64.427 13.090 1.00 15.41 C ANISOU 2998 CB GLU A 545 1997 1564 2293 -126 -7 170 C ATOM 2999 CG GLU A 545 -4.944 -64.215 14.501 1.00 19.84 C ANISOU 2999 CG GLU A 545 2553 2094 2893 -113 54 197 C ATOM 3000 CD GLU A 545 -6.461 -63.978 14.487 1.00 27.30 C ANISOU 3000 CD GLU A 545 3441 3007 3925 -144 64 236 C ATOM 3001 OE1 GLU A 545 -7.230 -64.951 14.308 1.00 27.84 O ANISOU 3001 OE1 GLU A 545 3502 3042 4034 -173 50 248 O ATOM 3002 OE2 GLU A 545 -6.890 -62.816 14.645 1.00 31.68 O ANISOU 3002 OE2 GLU A 545 3956 3568 4514 -141 84 259 O ATOM 3003 N ARG A 546 -4.641 -66.689 10.228 1.00 15.81 N ANISOU 3003 N ARG A 546 2683 1643 1682 -194 17 -239 N ATOM 3004 CA ARG A 546 -4.557 -66.615 8.768 1.00 16.38 C ANISOU 3004 CA ARG A 546 2731 1840 1654 -218 -31 -244 C ATOM 3005 C ARG A 546 -5.840 -66.129 8.092 1.00 20.31 C ANISOU 3005 C ARG A 546 3129 2425 2165 -309 -90 -176 C ATOM 3006 O ARG A 546 -5.784 -65.416 7.100 1.00 17.09 O ANISOU 3006 O ARG A 546 2646 2135 1711 -312 -121 -125 O ATOM 3007 CB ARG A 546 -4.093 -67.948 8.166 1.00 20.39 C ANISOU 3007 CB ARG A 546 3362 2330 2054 -226 -45 -364 C ATOM 3008 CG ARG A 546 -5.054 -69.101 8.380 1.00 26.88 C ANISOU 3008 CG ARG A 546 4251 3077 2884 -312 -72 -427 C ATOM 3009 CD ARG A 546 -4.523 -70.382 7.740 1.00 33.64 C ANISOU 3009 CD ARG A 546 5233 3916 3635 -313 -87 -549 C ATOM 3010 NE ARG A 546 -5.477 -71.483 7.858 1.00 41.29 N ANISOU 3010 NE ARG A 546 6265 4815 4609 -403 -122 -608 N ATOM 3011 CZ ARG A 546 -6.251 -71.914 6.864 1.00 54.02 C ANISOU 3011 CZ ARG A 546 7877 6488 6159 -489 -187 -634 C ATOM 3012 NH1 ARG A 546 -6.180 -71.344 5.668 1.00 51.10 N ANISOU 3012 NH1 ARG A 546 7449 6255 5713 -497 -223 -607 N ATOM 3013 NH2 ARG A 546 -7.091 -72.924 7.064 1.00 61.07 N ANISOU 3013 NH2 ARG A 546 8830 7309 7066 -571 -219 -685 N ATOM 3014 N HIS A 547 -6.994 -66.497 8.635 1.00 18.17 N ANISOU 3014 N HIS A 547 2852 2097 1957 -382 -104 -170 N ATOM 3015 CA HIS A 547 -8.259 -66.103 8.027 1.00 17.74 C ANISOU 3015 CA HIS A 547 2702 2119 1918 -471 -161 -105 C ATOM 3016 C HIS A 547 -8.520 -64.598 8.090 1.00 17.13 C ANISOU 3016 C HIS A 547 2486 2108 1915 -450 -157 19 C ATOM 3017 O HIS A 547 -8.875 -63.984 7.090 1.00 17.48 O ANISOU 3017 O HIS A 547 2447 2268 1927 -483 -203 77 O ATOM 3018 CB HIS A 547 -9.412 -66.890 8.655 1.00 23.10 C ANISOU 3018 CB HIS A 547 3408 2717 2651 -554 -174 -125 C ATOM 3019 CG HIS A 547 -9.408 -68.339 8.280 1.00 27.60 C ANISOU 3019 CG HIS A 547 4099 3245 3142 -600 -201 -238 C ATOM 3020 ND1 HIS A 547 -9.639 -68.771 6.992 1.00 31.16 N ANISOU 3020 ND1 HIS A 547 4564 3781 3493 -659 -263 -275 N ATOM 3021 CD2 HIS A 547 -9.192 -69.456 9.017 1.00 29.99 C ANISOU 3021 CD2 HIS A 547 4517 3428 3452 -597 -176 -323 C ATOM 3022 CE1 HIS A 547 -9.574 -70.090 6.953 1.00 34.14 C ANISOU 3022 CE1 HIS A 547 5061 4090 3821 -689 -276 -381 C ATOM 3023 NE2 HIS A 547 -9.303 -70.530 8.168 1.00 33.60 N ANISOU 3023 NE2 HIS A 547 5054 3895 3816 -652 -224 -410 N ATOM 3024 N ARG A 548 -8.340 -63.996 9.257 1.00 16.11 N ANISOU 3024 N ARG A 548 2331 1907 1884 -394 -104 61 N ATOM 3025 CA ARG A 548 -8.489 -62.549 9.353 1.00 16.18 C ANISOU 3025 CA ARG A 548 2214 1969 1966 -364 -98 174 C ATOM 3026 C ARG A 548 -7.403 -61.824 8.557 1.00 18.70 C ANISOU 3026 C ARG A 548 2504 2377 2226 -300 -100 200 C ATOM 3027 O ARG A 548 -7.676 -60.840 7.885 1.00 15.56 O ANISOU 3027 O ARG A 548 1999 2075 1836 -311 -131 286 O ATOM 3028 CB ARG A 548 -8.499 -62.086 10.809 1.00 14.86 C ANISOU 3028 CB ARG A 548 2033 1699 1913 -316 -40 205 C ATOM 3029 CG ARG A 548 -9.919 -61.992 11.400 1.00 21.87 C ANISOU 3029 CG ARG A 548 2860 2557 2891 -383 -48 253 C ATOM 3030 CD ARG A 548 -9.896 -61.557 12.873 1.00 25.73 C ANISOU 3030 CD ARG A 548 3342 2946 3488 -330 14 277 C ATOM 3031 NE ARG A 548 -9.648 -62.711 13.730 1.00 22.33 N ANISOU 3031 NE ARG A 548 3030 2405 3050 -326 49 190 N ATOM 3032 CZ ARG A 548 -10.598 -63.496 14.229 1.00 27.47 C ANISOU 3032 CZ ARG A 548 3707 3000 3730 -393 46 167 C ATOM 3033 NH1 ARG A 548 -11.890 -63.246 13.985 1.00 17.41 N ANISOU 3033 NH1 ARG A 548 2347 1770 2498 -468 11 226 N ATOM 3034 NH2 ARG A 548 -10.250 -64.533 14.983 1.00 19.39 N ANISOU 3034 NH2 ARG A 548 2794 1875 2697 -384 77 89 N ATOM 3035 N LEU A 549 -6.172 -62.316 8.637 1.00 15.22 N ANISOU 3035 N LEU A 549 2155 1902 1726 -233 -67 129 N ATOM 3036 CA LEU A 549 -5.060 -61.682 7.936 1.00 14.83 C ANISOU 3036 CA LEU A 549 2082 1934 1619 -168 -64 153 C ATOM 3037 C LEU A 549 -5.271 -61.684 6.421 1.00 15.74 C ANISOU 3037 C LEU A 549 2162 2185 1634 -217 -124 162 C ATOM 3038 O LEU A 549 -4.910 -60.732 5.737 1.00 17.34 O ANISOU 3038 O LEU A 549 2282 2486 1819 -192 -139 234 O ATOM 3039 CB LEU A 549 -3.744 -62.381 8.293 1.00 15.48 C ANISOU 3039 CB LEU A 549 2279 1952 1651 -91 -18 67 C ATOM 3040 CG LEU A 549 -3.226 -62.129 9.713 1.00 19.36 C ANISOU 3040 CG LEU A 549 2794 2329 2233 -23 43 72 C ATOM 3041 CD1 LEU A 549 -2.114 -63.126 10.086 1.00 16.66 C ANISOU 3041 CD1 LEU A 549 2580 1911 1838 35 83 -27 C ATOM 3042 CD2 LEU A 549 -2.753 -60.692 9.849 1.00 15.77 C ANISOU 3042 CD2 LEU A 549 2240 1915 1835 36 56 172 C ATOM 3043 N SER A 550 -5.873 -62.747 5.898 1.00 16.57 N ANISOU 3043 N SER A 550 2326 2295 1673 -290 -160 92 N ATOM 3044 CA SER A 550 -6.056 -62.879 4.450 1.00 17.52 C ANISOU 3044 CA SER A 550 2427 2543 1686 -341 -219 87 C ATOM 3045 C SER A 550 -7.042 -61.846 3.889 1.00 20.87 C ANISOU 3045 C SER A 550 2712 3066 2150 -398 -267 202 C ATOM 3046 O SER A 550 -7.149 -61.665 2.672 1.00 19.02 O ANISOU 3046 O SER A 550 2436 2955 1834 -433 -316 224 O ATOM 3047 CB SER A 550 -6.444 -64.319 4.078 1.00 20.85 C ANISOU 3047 CB SER A 550 2956 2936 2029 -405 -247 -24 C ATOM 3048 OG SER A 550 -7.722 -64.672 4.583 1.00 29.57 O ANISOU 3048 OG SER A 550 4049 3983 3203 -487 -269 -17 O ATOM 3049 N ARG A 551 -7.730 -61.136 4.783 1.00 17.93 N ANISOU 3049 N ARG A 551 2265 2643 1904 -403 -252 277 N ATOM 3050 CA ARG A 551 -8.635 -60.059 4.370 1.00 23.05 C ANISOU 3050 CA ARG A 551 2775 3376 2609 -446 -292 395 C ATOM 3051 C ARG A 551 -7.871 -58.802 3.946 1.00 20.64 C ANISOU 3051 C ARG A 551 2383 3152 2307 -382 -288 482 C ATOM 3052 O ARG A 551 -8.419 -57.933 3.283 1.00 18.00 O ANISOU 3052 O ARG A 551 1936 2913 1989 -415 -329 577 O ATOM 3053 CB ARG A 551 -9.593 -59.690 5.517 1.00 21.67 C ANISOU 3053 CB ARG A 551 2548 3114 2570 -464 -272 446 C ATOM 3054 CG ARG A 551 -10.563 -60.785 5.918 1.00 18.37 C ANISOU 3054 CG ARG A 551 2190 2627 2164 -541 -283 385 C ATOM 3055 CD ARG A 551 -11.394 -60.366 7.148 1.00 21.79 C ANISOU 3055 CD ARG A 551 2571 2974 2734 -545 -252 438 C ATOM 3056 NE ARG A 551 -11.970 -59.033 6.999 1.00 22.28 N ANISOU 3056 NE ARG A 551 2489 3102 2874 -547 -269 562 N ATOM 3057 CZ ARG A 551 -12.348 -58.272 8.022 1.00 24.59 C ANISOU 3057 CZ ARG A 551 2720 3335 3288 -516 -231 623 C ATOM 3058 NH1 ARG A 551 -12.212 -58.721 9.269 1.00 16.89 N ANISOU 3058 NH1 ARG A 551 1813 2239 2365 -483 -176 574 N ATOM 3059 NH2 ARG A 551 -12.859 -57.063 7.803 1.00 18.86 N ANISOU 3059 NH2 ARG A 551 1863 2670 2631 -516 -250 734 N ATOM 3060 N PHE A 552 -6.607 -58.704 4.340 1.00 17.12 N ANISOU 3060 N PHE A 552 1988 2669 1850 -292 -239 454 N ATOM 3061 CA PHE A 552 -5.828 -57.485 4.133 1.00 17.38 C ANISOU 3061 CA PHE A 552 1940 2761 1903 -226 -229 540 C ATOM 3062 C PHE A 552 -4.610 -57.728 3.257 1.00 16.45 C ANISOU 3062 C PHE A 552 1869 2718 1663 -180 -228 500 C ATOM 3063 O PHE A 552 -3.982 -58.787 3.343 1.00 16.31 O ANISOU 3063 O PHE A 552 1968 2655 1574 -158 -203 394 O ATOM 3064 CB PHE A 552 -5.405 -56.928 5.497 1.00 22.25 C ANISOU 3064 CB PHE A 552 2556 3265 2634 -153 -170 562 C ATOM 3065 CG PHE A 552 -6.572 -56.595 6.384 1.00 16.73 C ANISOU 3065 CG PHE A 552 1804 2497 2057 -189 -166 607 C ATOM 3066 CD1 PHE A 552 -7.185 -55.353 6.299 1.00 26.31 C ANISOU 3066 CD1 PHE A 552 2886 3756 3355 -198 -188 723 C ATOM 3067 CD2 PHE A 552 -7.083 -57.532 7.272 1.00 14.66 C ANISOU 3067 CD2 PHE A 552 1619 2127 1824 -215 -142 534 C ATOM 3068 CE1 PHE A 552 -8.281 -55.048 7.095 1.00 28.19 C ANISOU 3068 CE1 PHE A 552 3073 3935 3704 -229 -182 763 C ATOM 3069 CE2 PHE A 552 -8.183 -57.242 8.063 1.00 17.57 C ANISOU 3069 CE2 PHE A 552 1935 2439 2300 -249 -136 577 C ATOM 3070 CZ PHE A 552 -8.782 -55.990 7.976 1.00 17.49 C ANISOU 3070 CZ PHE A 552 1794 2478 2373 -254 -155 690 C ATOM 3071 N SER A 553 -4.266 -56.742 2.429 1.00 16.39 N ANISOU 3071 N SER A 553 1769 2826 1634 -164 -253 588 N ATOM 3072 CA SER A 553 -3.037 -56.800 1.643 1.00 16.56 C ANISOU 3072 CA SER A 553 1819 2926 1547 -111 -246 567 C ATOM 3073 C SER A 553 -1.817 -57.115 2.514 1.00 16.44 C ANISOU 3073 C SER A 553 1892 2815 1541 -20 -181 507 C ATOM 3074 O SER A 553 -0.965 -57.917 2.134 1.00 16.47 O ANISOU 3074 O SER A 553 1983 2832 1442 12 -164 423 O ATOM 3075 CB SER A 553 -2.794 -55.480 0.903 1.00 18.78 C ANISOU 3075 CB SER A 553 1974 3326 1836 -95 -273 692 C ATOM 3076 OG SER A 553 -3.837 -55.199 -0.026 1.00 20.27 O ANISOU 3076 OG SER A 553 2080 3618 2003 -178 -337 751 O ATOM 3077 N SER A 554 -1.717 -56.462 3.665 1.00 15.46 N ANISOU 3077 N SER A 554 1741 2596 1537 24 -145 550 N ATOM 3078 CA SER A 554 -0.562 -56.666 4.537 1.00 14.78 C ANISOU 3078 CA SER A 554 1730 2420 1466 110 -86 503 C ATOM 3079 C SER A 554 -0.503 -58.113 5.024 1.00 15.99 C ANISOU 3079 C SER A 554 2019 2477 1577 104 -58 373 C ATOM 3080 O SER A 554 0.568 -58.707 5.137 1.00 14.07 O ANISOU 3080 O SER A 554 1862 2206 1278 163 -23 304 O ATOM 3081 CB SER A 554 -0.635 -55.714 5.734 1.00 13.25 C ANISOU 3081 CB SER A 554 1483 2137 1414 147 -57 571 C ATOM 3082 OG SER A 554 -1.824 -55.938 6.472 1.00 14.89 O ANISOU 3082 OG SER A 554 1690 2266 1702 94 -58 562 O ATOM 3083 N GLY A 555 -1.665 -58.677 5.330 1.00 16.52 N ANISOU 3083 N GLY A 555 2106 2494 1677 33 -75 342 N ATOM 3084 CA GLY A 555 -1.732 -60.053 5.790 1.00 16.15 C ANISOU 3084 CA GLY A 555 2185 2354 1598 18 -55 224 C ATOM 3085 C GLY A 555 -1.378 -61.044 4.699 1.00 18.44 C ANISOU 3085 C GLY A 555 2549 2709 1747 0 -77 138 C ATOM 3086 O GLY A 555 -0.626 -61.991 4.929 1.00 16.14 O ANISOU 3086 O GLY A 555 2368 2359 1405 39 -45 42 O ATOM 3087 N LYS A 556 -1.928 -60.844 3.506 1.00 16.28 N ANISOU 3087 N LYS A 556 2218 2559 1410 -59 -132 171 N ATOM 3088 CA LYS A 556 -1.542 -61.683 2.370 1.00 18.72 C ANISOU 3088 CA LYS A 556 2591 2946 1575 -71 -155 92 C ATOM 3089 C LYS A 556 -0.040 -61.617 2.137 1.00 19.95 C ANISOU 3089 C LYS A 556 2782 3133 1666 23 -116 72 C ATOM 3090 O LYS A 556 0.583 -62.621 1.810 1.00 22.23 O ANISOU 3090 O LYS A 556 3172 3414 1861 46 -102 -30 O ATOM 3091 CB LYS A 556 -2.273 -61.271 1.092 1.00 18.78 C ANISOU 3091 CB LYS A 556 2514 3097 1523 -143 -220 148 C ATOM 3092 CG LYS A 556 -3.783 -61.529 1.125 1.00 26.98 C ANISOU 3092 CG LYS A 556 3528 4119 2605 -247 -267 157 C ATOM 3093 CD LYS A 556 -4.425 -61.013 -0.159 1.00 35.27 C ANISOU 3093 CD LYS A 556 4485 5319 3596 -313 -333 224 C ATOM 3094 CE LYS A 556 -5.847 -60.543 0.075 1.00 53.82 C ANISOU 3094 CE LYS A 556 6745 7663 6041 -394 -372 301 C ATOM 3095 NZ LYS A 556 -6.317 -59.660 -1.029 1.00 61.00 N ANISOU 3095 NZ LYS A 556 7536 8722 6921 -438 -429 402 N ATOM 3096 N LYS A 557 0.542 -60.431 2.299 1.00 16.96 N ANISOU 3096 N LYS A 557 2316 2789 1339 79 -99 169 N ATOM 3097 CA LYS A 557 1.979 -60.273 2.092 1.00 17.97 C ANISOU 3097 CA LYS A 557 2465 2952 1411 169 -63 164 C ATOM 3098 C LYS A 557 2.799 -61.110 3.081 1.00 17.23 C ANISOU 3098 C LYS A 557 2486 2728 1331 234 -4 73 C ATOM 3099 O LYS A 557 3.787 -61.745 2.700 1.00 24.54 O ANISOU 3099 O LYS A 557 3485 3674 2166 286 19 4 O ATOM 3100 CB LYS A 557 2.385 -58.795 2.159 1.00 22.26 C ANISOU 3100 CB LYS A 557 2888 3548 2022 211 -60 294 C ATOM 3101 CG LYS A 557 1.912 -57.977 0.955 1.00 35.25 C ANISOU 3101 CG LYS A 557 4421 5346 3627 163 -116 386 C ATOM 3102 CD LYS A 557 2.011 -56.472 1.216 1.00 44.40 C ANISOU 3102 CD LYS A 557 5455 6530 4886 189 -120 523 C ATOM 3103 CE LYS A 557 3.456 -55.999 1.243 1.00 49.96 C ANISOU 3103 CE LYS A 557 6154 7257 5573 281 -84 552 C ATOM 3104 NZ LYS A 557 3.564 -54.534 1.517 1.00 50.29 N ANISOU 3104 NZ LYS A 557 6077 7315 5717 305 -92 684 N ATOM 3105 N MET A 558 2.395 -61.114 4.346 1.00 15.52 N ANISOU 3105 N MET A 558 2286 2383 1227 232 19 74 N ATOM 3106 CA MET A 558 3.116 -61.881 5.364 1.00 17.00 C ANISOU 3106 CA MET A 558 2580 2444 1436 290 73 -5 C ATOM 3107 C MET A 558 2.978 -63.375 5.132 1.00 21.95 C ANISOU 3107 C MET A 558 3329 3028 1983 262 71 -133 C ATOM 3108 O MET A 558 3.931 -64.135 5.289 1.00 18.79 O ANISOU 3108 O MET A 558 3021 2584 1535 320 107 -211 O ATOM 3109 CB MET A 558 2.600 -61.537 6.762 1.00 14.97 C ANISOU 3109 CB MET A 558 2308 2064 1314 286 96 28 C ATOM 3110 CG MET A 558 2.922 -60.127 7.200 1.00 13.06 C ANISOU 3110 CG MET A 558 1966 1837 1160 330 107 140 C ATOM 3111 SD MET A 558 2.775 -59.971 9.005 1.00 22.34 S ANISOU 3111 SD MET A 558 3166 2850 2474 357 153 146 S ATOM 3112 CE MET A 558 1.019 -60.211 9.202 1.00 18.63 C ANISOU 3112 CE MET A 558 2671 2350 2060 254 120 148 C ATOM 3113 N ILE A 559 1.775 -63.797 4.767 1.00 17.81 N ANISOU 3113 N ILE A 559 2803 2514 1448 171 26 -153 N ATOM 3114 CA ILE A 559 1.531 -65.191 4.447 1.00 21.35 C ANISOU 3114 CA ILE A 559 3363 2928 1822 132 14 -272 C ATOM 3115 C ILE A 559 2.423 -65.633 3.289 1.00 27.69 C ANISOU 3115 C ILE A 559 4209 3825 2486 169 10 -330 C ATOM 3116 O ILE A 559 3.015 -66.715 3.320 1.00 24.53 O ANISOU 3116 O ILE A 559 3922 3371 2028 201 33 -437 O ATOM 3117 CB ILE A 559 0.050 -65.405 4.083 1.00 22.23 C ANISOU 3117 CB ILE A 559 3446 3058 1941 21 -44 -267 C ATOM 3118 CG1 ILE A 559 -0.808 -65.316 5.348 1.00 19.18 C ANISOU 3118 CG1 ILE A 559 3047 2556 1685 -12 -32 -238 C ATOM 3119 CG2 ILE A 559 -0.138 -66.736 3.370 1.00 24.61 C ANISOU 3119 CG2 ILE A 559 3851 3360 2138 -23 -71 -385 C ATOM 3120 CD1 ILE A 559 -2.280 -65.015 5.095 1.00 19.39 C ANISOU 3120 CD1 ILE A 559 2996 2619 1752 -112 -85 -183 C ATOM 3121 N GLU A 560 2.518 -64.782 2.272 1.00 25.71 N ANISOU 3121 N GLU A 560 3867 3718 2183 165 -17 -258 N ATOM 3122 CA GLU A 560 3.339 -65.073 1.100 1.00 30.04 C ANISOU 3122 CA GLU A 560 4442 4376 2594 200 -21 -301 C ATOM 3123 C GLU A 560 4.828 -65.084 1.455 1.00 25.08 C ANISOU 3123 C GLU A 560 3855 3724 1952 311 40 -320 C ATOM 3124 O GLU A 560 5.598 -65.887 0.925 1.00 28.09 O ANISOU 3124 O GLU A 560 4316 4125 2230 353 58 -407 O ATOM 3125 CB GLU A 560 3.072 -64.041 0.009 1.00 34.52 C ANISOU 3125 CB GLU A 560 4889 5105 3120 169 -64 -202 C ATOM 3126 CG GLU A 560 4.013 -64.130 -1.176 1.00 53.68 C ANISOU 3126 CG GLU A 560 7325 7662 5409 214 -62 -226 C ATOM 3127 CD GLU A 560 3.630 -63.174 -2.288 1.00 70.88 C ANISOU 3127 CD GLU A 560 9385 10003 7542 172 -111 -128 C ATOM 3128 OE1 GLU A 560 2.469 -62.709 -2.303 1.00 76.06 O ANISOU 3128 OE1 GLU A 560 9970 10672 8256 92 -156 -65 O ATOM 3129 OE2 GLU A 560 4.491 -62.891 -3.148 1.00 77.28 O ANISOU 3129 OE2 GLU A 560 10172 10932 8260 219 -104 -110 O ATOM 3130 N THR A 561 5.225 -64.184 2.346 1.00 23.74 N ANISOU 3130 N THR A 561 3626 3509 1883 359 71 -237 N ATOM 3131 CA THR A 561 6.607 -64.120 2.810 1.00 25.84 C ANISOU 3131 CA THR A 561 3923 3743 2151 462 127 -243 C ATOM 3132 C THR A 561 6.999 -65.441 3.475 1.00 27.09 C ANISOU 3132 C THR A 561 4219 3774 2299 492 164 -365 C ATOM 3133 O THR A 561 8.038 -66.012 3.158 1.00 27.48 O ANISOU 3133 O THR A 561 4334 3838 2271 558 194 -428 O ATOM 3134 CB THR A 561 6.837 -62.922 3.763 1.00 26.13 C ANISOU 3134 CB THR A 561 3876 3740 2310 497 148 -133 C ATOM 3135 OG1 THR A 561 6.719 -61.695 3.029 1.00 27.09 O ANISOU 3135 OG1 THR A 561 3872 3989 2431 484 116 -19 O ATOM 3136 CG2 THR A 561 8.224 -62.982 4.400 1.00 25.04 C ANISOU 3136 CG2 THR A 561 3782 3549 2183 598 205 -147 C ATOM 3137 N LEU A 562 6.158 -65.939 4.378 1.00 21.68 N ANISOU 3137 N LEU A 562 3579 2967 1692 444 161 -398 N ATOM 3138 CA LEU A 562 6.416 -67.231 5.016 1.00 19.74 C ANISOU 3138 CA LEU A 562 3464 2596 1442 463 190 -512 C ATOM 3139 C LEU A 562 6.374 -68.390 4.020 1.00 31.63 C ANISOU 3139 C LEU A 562 5057 4135 2826 440 169 -624 C ATOM 3140 O LEU A 562 7.170 -69.329 4.113 1.00 31.06 O ANISOU 3140 O LEU A 562 5086 4009 2707 495 201 -716 O ATOM 3141 CB LEU A 562 5.430 -67.469 6.159 1.00 17.90 C ANISOU 3141 CB LEU A 562 3250 2234 1319 408 187 -513 C ATOM 3142 CG LEU A 562 5.668 -66.564 7.370 1.00 19.97 C ANISOU 3142 CG LEU A 562 3458 2430 1700 449 221 -430 C ATOM 3143 CD1 LEU A 562 4.407 -66.446 8.226 1.00 20.93 C ANISOU 3143 CD1 LEU A 562 3555 2472 1925 377 206 -400 C ATOM 3144 CD2 LEU A 562 6.831 -67.120 8.173 1.00 20.80 C ANISOU 3144 CD2 LEU A 562 3648 2440 1814 535 277 -482 C ATOM 3145 N ALA A 563 5.449 -68.319 3.066 1.00 35.59 N ANISOU 3145 N ALA A 563 5520 4728 3276 360 114 -617 N ATOM 3146 CA ALA A 563 5.364 -69.328 2.012 1.00 35.70 C ANISOU 3146 CA ALA A 563 5610 4789 3167 333 87 -720 C ATOM 3147 C ALA A 563 6.635 -69.367 1.162 1.00 39.46 C ANISOU 3147 C ALA A 563 6102 5360 3530 417 114 -749 C ATOM 3148 O ALA A 563 7.112 -70.441 0.807 1.00 43.18 O ANISOU 3148 O ALA A 563 6679 5809 3920 445 127 -861 O ATOM 3149 CB ALA A 563 4.140 -69.090 1.131 1.00 37.87 C ANISOU 3149 CB ALA A 563 5826 5156 3409 229 19 -692 C ATOM 3150 N ASN A 564 7.178 -68.195 0.838 1.00 33.58 N ANISOU 3150 N ASN A 564 5254 4722 2784 458 123 -645 N ATOM 3151 CA ASN A 564 8.403 -68.100 0.045 1.00 38.08 C ANISOU 3151 CA ASN A 564 5824 5395 3252 539 151 -654 C ATOM 3152 C ASN A 564 9.625 -68.655 0.778 1.00 44.84 C ANISOU 3152 C ASN A 564 6760 6157 4119 640 216 -709 C ATOM 3153 O ASN A 564 10.522 -69.228 0.159 1.00 41.68 O ANISOU 3153 O ASN A 564 6416 5802 3619 701 241 -777 O ATOM 3154 CB ASN A 564 8.680 -66.651 -0.366 1.00 37.75 C ANISOU 3154 CB ASN A 564 5643 5480 3219 557 144 -516 C ATOM 3155 CG ASN A 564 7.765 -66.170 -1.475 1.00 50.46 C ANISOU 3155 CG ASN A 564 7174 7223 4773 474 82 -469 C ATOM 3156 OD1 ASN A 564 7.776 -64.987 -1.836 1.00 48.14 O ANISOU 3156 OD1 ASN A 564 6764 7032 4496 471 66 -351 O ATOM 3157 ND2 ASN A 564 6.963 -67.082 -2.024 1.00 52.33 N ANISOU 3157 ND2 ASN A 564 7477 7460 4945 404 44 -558 N ATOM 3158 N LEU A 565 9.663 -68.471 2.093 1.00 38.67 N ANISOU 3158 N LEU A 565 5982 5250 3461 658 243 -678 N ATOM 3159 CA LEU A 565 10.766 -68.983 2.895 1.00 43.96 C ANISOU 3159 CA LEU A 565 6726 5823 4154 748 301 -723 C ATOM 3160 C LEU A 565 10.791 -70.508 2.831 1.00 52.87 C ANISOU 3160 C LEU A 565 7976 6861 5253 745 299 -846 C ATOM 3161 O LEU A 565 11.838 -71.120 2.608 1.00 43.50 O ANISOU 3161 O LEU A 565 6832 5662 4035 816 323 -881 O ATOM 3162 CB LEU A 565 10.635 -68.520 4.345 1.00 37.95 C ANISOU 3162 CB LEU A 565 5940 4938 3540 752 320 -660 C ATOM 3163 CG LEU A 565 11.836 -68.826 5.237 1.00 39.37 C ANISOU 3163 CG LEU A 565 6144 5012 3802 834 353 -635 C ATOM 3164 CD1 LEU A 565 13.105 -68.274 4.620 1.00 44.03 C ANISOU 3164 CD1 LEU A 565 6684 5704 4339 917 374 -588 C ATOM 3165 CD2 LEU A 565 11.629 -68.253 6.621 1.00 35.53 C ANISOU 3165 CD2 LEU A 565 5624 4422 3455 826 361 -557 C ATOM 3166 N ARG A 566 9.619 -71.106 3.016 1.00 64.38 N ANISOU 3166 N ARG A 566 9485 8254 6721 660 268 -905 N ATOM 3167 CA ARG A 566 9.459 -72.555 2.983 1.00 74.61 C ANISOU 3167 CA ARG A 566 10894 9455 7999 641 257 -1016 C ATOM 3168 C ARG A 566 9.996 -73.154 1.684 1.00 74.23 C ANISOU 3168 C ARG A 566 10891 9502 7811 670 252 -1095 C ATOM 3169 O ARG A 566 10.565 -74.244 1.683 1.00 74.29 O ANISOU 3169 O ARG A 566 10983 9438 7806 710 266 -1169 O ATOM 3170 CB ARG A 566 7.983 -72.911 3.146 1.00 83.30 C ANISOU 3170 CB ARG A 566 12027 10508 9115 531 213 -1060 C ATOM 3171 CG ARG A 566 7.718 -74.212 3.875 1.00 92.01 C ANISOU 3171 CG ARG A 566 13230 11450 10280 507 211 -1129 C ATOM 3172 CD ARG A 566 6.227 -74.511 3.885 1.00102.16 C ANISOU 3172 CD ARG A 566 14540 12705 11570 392 161 -1171 C ATOM 3173 NE ARG A 566 5.427 -73.288 3.942 1.00108.81 N ANISOU 3173 NE ARG A 566 15259 13618 12466 338 136 -1057 N ATOM 3174 CZ ARG A 566 5.034 -72.699 5.068 1.00112.24 C ANISOU 3174 CZ ARG A 566 15643 13981 13023 325 150 -978 C ATOM 3175 NH1 ARG A 566 5.364 -73.219 6.242 1.00114.09 N ANISOU 3175 NH1 ARG A 566 15943 14076 13329 361 189 -1007 N ATOM 3176 NH2 ARG A 566 4.310 -71.588 5.019 1.00110.97 N ANISOU 3176 NH2 ARG A 566 15365 13889 12911 278 124 -871 N ATOM 3177 N SER A 567 9.814 -72.434 0.580 1.00 74.93 N ANISOU 3177 N SER A 567 10921 9758 7792 651 231 -1075 N ATOM 3178 CA SER A 567 10.313 -72.877 -0.719 1.00 75.64 C ANISOU 3178 CA SER A 567 11041 9959 7739 678 227 -1142 C ATOM 3179 C SER A 567 11.821 -72.686 -0.838 1.00 79.27 C ANISOU 3179 C SER A 567 11477 10456 8188 795 277 -1109 C ATOM 3180 O SER A 567 12.468 -72.084 0.021 1.00 77.44 O ANISOU 3180 O SER A 567 11194 10176 8053 849 310 -1024 O ATOM 3181 CB SER A 567 9.609 -72.126 -1.849 1.00 76.23 C ANISOU 3181 CB SER A 567 11032 10200 7733 610 176 -1092 C ATOM 3182 OG SER A 567 8.205 -72.293 -1.771 1.00 79.95 O ANISOU 3182 OG SER A 567 11501 10632 8245 497 118 -1095 O TER 3183 SER A 567 ATOM 3184 O5' U B 1 -3.144 -50.397 -1.027 1.00 37.73 O ANISOU 3184 O5' U B 1 5751 4312 4272 -676 -750 852 O ATOM 3185 C5' U B 1 -4.141 -49.558 -0.475 1.00 27.96 C ANISOU 3185 C5' U B 1 4479 2973 3172 -668 -847 875 C ATOM 3186 C4' U B 1 -3.854 -49.214 0.980 1.00 19.52 C ANISOU 3186 C4' U B 1 3286 1930 2201 -593 -815 808 C ATOM 3187 O4' U B 1 -3.813 -50.402 1.758 1.00 19.60 O ANISOU 3187 O4' U B 1 3252 1999 2196 -483 -753 738 O ATOM 3188 C3' U B 1 -2.565 -48.498 1.323 1.00 19.39 C ANISOU 3188 C3' U B 1 3204 1991 2172 -620 -744 779 C ATOM 3189 O3' U B 1 -2.619 -47.069 1.053 1.00 19.92 O ANISOU 3189 O3' U B 1 3265 2000 2306 -705 -805 830 O ATOM 3190 C2' U B 1 -2.473 -48.789 2.802 1.00 21.03 C ANISOU 3190 C2' U B 1 3298 2238 2456 -519 -698 702 C ATOM 3191 O2' U B 1 -3.296 -47.934 3.554 1.00 18.75 O ANISOU 3191 O2' U B 1 2952 1860 2311 -511 -773 708 O ATOM 3192 C1' U B 1 -2.990 -50.209 2.876 1.00 19.59 C ANISOU 3192 C1' U B 1 3140 2071 2233 -436 -682 674 C ATOM 3193 N1 U B 1 -1.883 -51.217 2.933 1.00 18.31 N ANISOU 3193 N1 U B 1 2958 2035 1962 -400 -559 624 N ATOM 3194 C2 U B 1 -1.341 -51.496 4.173 1.00 17.69 C ANISOU 3194 C2 U B 1 2769 2030 1924 -323 -488 553 C ATOM 3195 O2 U B 1 -1.744 -51.008 5.202 1.00 18.67 O ANISOU 3195 O2 U B 1 2812 2121 2160 -284 -520 526 O ATOM 3196 N3 U B 1 -0.303 -52.380 4.174 1.00 17.64 N ANISOU 3196 N3 U B 1 2743 2136 1822 -300 -373 517 N ATOM 3197 C4 U B 1 0.234 -52.999 3.064 1.00 18.47 C ANISOU 3197 C4 U B 1 2932 2283 1801 -347 -322 541 C ATOM 3198 O4 U B 1 1.155 -53.776 3.247 1.00 20.39 O ANISOU 3198 O4 U B 1 3143 2625 1981 -322 -215 504 O ATOM 3199 C5 U B 1 -0.371 -52.667 1.799 1.00 19.60 C ANISOU 3199 C5 U B 1 3194 2348 1907 -428 -402 611 C ATOM 3200 C6 U B 1 -1.394 -51.796 1.782 1.00 18.83 C ANISOU 3200 C6 U B 1 3112 2141 1899 -450 -517 651 C ATOM 3201 P G B 2 -1.346 -46.220 0.756 1.00 23.46 P ANISOU 3201 P G B 2 3694 2513 2705 -770 -752 833 P ATOM 3202 OP1 G B 2 -1.864 -44.948 0.107 1.00 21.47 O ANISOU 3202 OP1 G B 2 3467 2173 2519 -866 -846 907 O ATOM 3203 OP2 G B 2 -0.361 -47.056 -0.047 1.00 20.88 O ANISOU 3203 OP2 G B 2 3434 2275 2224 -787 -671 823 O ATOM 3204 O5' G B 2 -0.698 -45.837 2.104 1.00 21.39 O ANISOU 3204 O5' G B 2 3310 2307 2510 -712 -689 767 O ATOM 3205 C5' G B 2 -1.462 -45.091 3.094 1.00 23.57 C ANISOU 3205 C5' G B 2 3502 2514 2938 -690 -742 759 C ATOM 3206 C4' G B 2 -0.537 -44.559 4.167 1.00 19.29 C ANISOU 3206 C4' G B 2 2850 2045 2435 -663 -666 703 C ATOM 3207 O4' G B 2 0.127 -45.694 4.792 1.00 20.85 O ANISOU 3207 O4' G B 2 3014 2342 2567 -583 -570 636 O ATOM 3208 C3' G B 2 0.620 -43.720 3.631 1.00 19.87 C ANISOU 3208 C3' G B 2 2928 2175 2447 -731 -622 720 C ATOM 3209 O3' G B 2 0.203 -42.387 3.446 1.00 20.22 O ANISOU 3209 O3' G B 2 2953 2146 2585 -799 -691 768 O ATOM 3210 C2' G B 2 1.568 -43.798 4.830 1.00 19.36 C ANISOU 3210 C2' G B 2 2760 2205 2389 -672 -521 649 C ATOM 3211 O2' G B 2 1.136 -42.932 5.853 1.00 22.36 O ANISOU 3211 O2' G B 2 3041 2547 2909 -664 -545 633 O ATOM 3212 C1' G B 2 1.412 -45.264 5.255 1.00 20.97 C ANISOU 3212 C1' G B 2 2966 2450 2553 -588 -480 603 C ATOM 3213 N9 G B 2 2.444 -46.119 4.686 1.00 19.65 N ANISOU 3213 N9 G B 2 2849 2374 2244 -584 -394 591 N ATOM 3214 C8 G B 2 2.601 -46.474 3.386 1.00 23.62 C ANISOU 3214 C8 G B 2 3463 2873 2640 -635 -403 633 C ATOM 3215 N7 G B 2 3.647 -47.236 3.178 1.00 21.62 N ANISOU 3215 N7 G B 2 3228 2708 2277 -624 -306 609 N ATOM 3216 C5 G B 2 4.230 -47.380 4.445 1.00 21.03 C ANISOU 3216 C5 G B 2 3045 2705 2240 -560 -228 550 C ATOM 3217 C6 G B 2 5.394 -48.094 4.863 1.00 21.41 C ANISOU 3217 C6 G B 2 3055 2860 2217 -526 -108 508 C ATOM 3218 O6 G B 2 6.162 -48.759 4.172 1.00 19.62 O ANISOU 3218 O6 G B 2 2889 2684 1881 -545 -43 513 O ATOM 3219 N1 G B 2 5.629 -47.941 6.237 1.00 18.00 N ANISOU 3219 N1 G B 2 2502 2474 1862 -471 -63 459 N ATOM 3220 C2 G B 2 4.837 -47.198 7.076 1.00 17.72 C ANISOU 3220 C2 G B 2 2394 2385 1954 -454 -126 449 C ATOM 3221 N2 G B 2 5.151 -47.183 8.383 1.00 17.12 N ANISOU 3221 N2 G B 2 2201 2364 1940 -406 -71 399 N ATOM 3222 N3 G B 2 3.734 -46.556 6.699 1.00 17.98 N ANISOU 3222 N3 G B 2 2462 2312 2057 -485 -237 486 N ATOM 3223 C4 G B 2 3.494 -46.674 5.371 1.00 20.55 C ANISOU 3223 C4 G B 2 2904 2594 2311 -537 -283 538 C ATOM 3224 P U B 3 0.887 -41.457 2.328 1.00 24.73 P ANISOU 3224 P U B 3 3572 2728 3096 -893 -700 820 P ATOM 3225 OP1 U B 3 0.142 -40.183 2.321 1.00 28.70 O ANISOU 3225 OP1 U B 3 4035 3140 3728 -952 -781 869 O ATOM 3226 OP2 U B 3 1.096 -42.227 1.083 1.00 23.43 O ANISOU 3226 OP2 U B 3 3525 2579 2797 -925 -702 850 O ATOM 3227 O5' U B 3 2.338 -41.239 2.984 1.00 21.06 O ANISOU 3227 O5' U B 3 3039 2377 2585 -863 -587 763 O ATOM 3228 C5' U B 3 3.345 -40.497 2.315 1.00 22.54 C ANISOU 3228 C5' U B 3 3249 2609 2708 -918 -558 782 C ATOM 3229 C4' U B 3 3.811 -39.373 3.228 1.00 22.85 C ANISOU 3229 C4' U B 3 3177 2674 2832 -915 -523 757 C ATOM 3230 O4' U B 3 4.288 -39.917 4.482 1.00 21.48 O ANISOU 3230 O4' U B 3 2923 2570 2666 -837 -436 688 O ATOM 3231 C3' U B 3 4.976 -38.555 2.718 1.00 24.43 C ANISOU 3231 C3' U B 3 3383 2930 2968 -956 -481 766 C ATOM 3232 O3' U B 3 4.490 -37.548 1.827 1.00 30.10 O ANISOU 3232 O3' U B 3 4127 3579 3729 -1036 -566 831 O ATOM 3233 C2' U B 3 5.488 -37.944 4.009 1.00 26.78 C ANISOU 3233 C2' U B 3 3559 3279 3337 -917 -412 718 C ATOM 3234 O2' U B 3 4.692 -36.855 4.445 1.00 29.82 O ANISOU 3234 O2' U B 3 3865 3596 3869 -948 -468 738 O ATOM 3235 C1' U B 3 5.312 -39.089 4.994 1.00 21.27 C ANISOU 3235 C1' U B 3 2827 2611 2644 -840 -367 664 C ATOM 3236 N1 U B 3 6.538 -39.913 5.187 1.00 21.88 N ANISOU 3236 N1 U B 3 2916 2794 2602 -796 -259 621 N ATOM 3237 C2 U B 3 7.425 -39.497 6.138 1.00 21.62 C ANISOU 3237 C2 U B 3 2795 2836 2583 -769 -173 581 C ATOM 3238 O2 U B 3 7.227 -38.469 6.765 1.00 20.13 O ANISOU 3238 O2 U B 3 2521 2630 2496 -783 -184 578 O ATOM 3239 N3 U B 3 8.528 -40.312 6.305 1.00 19.54 N ANISOU 3239 N3 U B 3 2545 2665 2214 -732 -74 548 N ATOM 3240 C4 U B 3 8.797 -41.478 5.589 1.00 23.09 C ANISOU 3240 C4 U B 3 3086 3135 2552 -722 -52 551 C ATOM 3241 O4 U B 3 9.822 -42.117 5.813 1.00 19.43 O ANISOU 3241 O4 U B 3 2623 2753 2008 -694 44 524 O ATOM 3242 C5 U B 3 7.808 -41.856 4.608 1.00 21.09 C ANISOU 3242 C5 U B 3 2921 2803 2290 -752 -143 591 C ATOM 3243 C6 U B 3 6.737 -41.063 4.445 1.00 21.31 C ANISOU 3243 C6 U B 3 2939 2741 2417 -787 -243 625 C ATOM 3244 P G B 4 5.296 -37.189 0.487 1.00 40.53 P ANISOU 3244 P G B 4 5534 4926 4940 -1100 -571 869 P ATOM 3245 OP1 G B 4 4.322 -36.566 -0.438 1.00 35.81 O ANISOU 3245 OP1 G B 4 4971 4236 4399 -1181 -682 943 O ATOM 3246 OP2 G B 4 6.074 -38.365 0.038 1.00 38.44 O ANISOU 3246 OP2 G B 4 5355 4722 4527 -1076 -510 844 O ATOM 3247 O5' G B 4 6.349 -36.108 1.008 1.00 35.98 O ANISOU 3247 O5' G B 4 4876 4414 4381 -1093 -506 841 O ATOM 3248 C5' G B 4 5.906 -34.954 1.697 1.00 41.21 C ANISOU 3248 C5' G B 4 5430 5043 5183 -1106 -528 848 C ATOM 3249 C4' G B 4 7.080 -34.076 2.091 1.00 40.51 C ANISOU 3249 C4' G B 4 5278 5033 5083 -1094 -451 818 C ATOM 3250 O4' G B 4 7.937 -34.834 2.976 1.00 38.11 O ANISOU 3250 O4' G B 4 4952 4812 4715 -1021 -347 754 O ATOM 3251 C3' G B 4 8.019 -33.612 0.976 1.00 42.40 C ANISOU 3251 C3' G B 4 5584 5306 5220 -1133 -447 842 C ATOM 3252 O3' G B 4 7.559 -32.412 0.378 1.00 46.71 O ANISOU 3252 O3' G B 4 6103 5799 5844 -1201 -521 895 O ATOM 3253 C2' G B 4 9.230 -33.251 1.799 1.00 36.21 C ANISOU 3253 C2' G B 4 4737 4613 4409 -1083 -341 789 C ATOM 3254 O2' G B 4 8.974 -32.036 2.458 1.00 37.42 O ANISOU 3254 O2' G B 4 4774 4756 4689 -1095 -344 791 O ATOM 3255 C1' G B 4 9.262 -34.376 2.824 1.00 39.13 C ANISOU 3255 C1' G B 4 5085 5018 4764 -1015 -276 737 C ATOM 3256 N9 G B 4 10.127 -35.460 2.391 1.00 36.68 N ANISOU 3256 N9 G B 4 4868 4762 4308 -990 -220 719 N ATOM 3257 C8 G B 4 9.819 -36.551 1.621 1.00 35.84 C ANISOU 3257 C8 G B 4 4862 4630 4124 -1001 -249 734 C ATOM 3258 N7 G B 4 10.848 -37.325 1.399 1.00 38.88 N ANISOU 3258 N7 G B 4 5308 5076 4387 -979 -173 711 N ATOM 3259 C5 G B 4 11.900 -36.698 2.056 1.00 32.43 C ANISOU 3259 C5 G B 4 4430 4327 3564 -950 -93 680 C ATOM 3260 C6 G B 4 13.258 -37.062 2.193 1.00 36.00 C ANISOU 3260 C6 G B 4 4907 4858 3914 -919 10 650 C ATOM 3261 O6 G B 4 13.859 -38.039 1.737 1.00 45.71 O ANISOU 3261 O6 G B 4 6218 6113 5037 -914 55 644 O ATOM 3262 N1 G B 4 13.962 -36.132 2.951 1.00 32.46 N ANISOU 3262 N1 G B 4 4375 4459 3499 -895 66 629 N ATOM 3263 C2 G B 4 13.419 -35.004 3.515 1.00 34.60 C ANISOU 3263 C2 G B 4 4547 4709 3890 -903 33 633 C ATOM 3264 N2 G B 4 14.254 -34.222 4.209 1.00 33.68 N ANISOU 3264 N2 G B 4 4358 4652 3785 -879 104 609 N ATOM 3265 N3 G B 4 12.151 -34.656 3.405 1.00 36.60 N ANISOU 3265 N3 G B 4 4773 4888 4247 -935 -61 660 N ATOM 3266 C4 G B 4 11.462 -35.551 2.668 1.00 35.01 C ANISOU 3266 C4 G B 4 4657 4636 4011 -955 -120 684 C ATOM 3267 P U B 5 8.202 -31.844 -0.982 1.00 45.36 P ANISOU 3267 P U B 5 6004 5640 5589 -1259 -552 934 P ATOM 3268 OP1 U B 5 7.612 -30.500 -1.153 1.00 56.09 O ANISOU 3268 OP1 U B 5 7286 6951 7075 -1317 -614 980 O ATOM 3269 OP2 U B 5 8.037 -32.865 -2.042 1.00 41.60 O ANISOU 3269 OP2 U B 5 5658 5141 5007 -1289 -592 959 O ATOM 3270 O5' U B 5 9.767 -31.685 -0.705 1.00 40.59 O ANISOU 3270 O5' U B 5 5396 5136 4890 -1210 -447 882 O ATOM 3271 C5' U B 5 10.268 -30.527 -0.032 1.00 38.42 C ANISOU 3271 C5' U B 5 5015 4901 4682 -1192 -401 862 C ATOM 3272 C4' U B 5 11.784 -30.495 0.063 1.00 33.44 C ANISOU 3272 C4' U B 5 4406 4362 3940 -1146 -306 820 C ATOM 3273 O4' U B 5 12.264 -31.681 0.735 1.00 42.42 O ANISOU 3273 O4' U B 5 5570 5545 5003 -1087 -226 773 O ATOM 3274 C3' U B 5 12.523 -30.485 -1.267 1.00 41.78 C ANISOU 3274 C3' U B 5 5573 5427 4875 -1180 -327 841 C ATOM 3275 O3' U B 5 12.604 -29.154 -1.757 1.00 45.68 O ANISOU 3275 O3' U B 5 6022 5914 5420 -1218 -367 870 O ATOM 3276 C2' U B 5 13.889 -31.050 -0.876 1.00 44.87 C ANISOU 3276 C2' U B 5 6001 5899 5150 -1117 -217 789 C ATOM 3277 O2' U B 5 14.772 -30.090 -0.340 1.00 51.73 O ANISOU 3277 O2' U B 5 6800 6826 6031 -1082 -152 764 O ATOM 3278 C1' U B 5 13.545 -32.030 0.240 1.00 35.78 C ANISOU 3278 C1' U B 5 4812 4760 4022 -1068 -166 755 C ATOM 3279 N1 U B 5 13.499 -33.427 -0.219 1.00 38.65 N ANISOU 3279 N1 U B 5 5279 5113 4292 -1068 -164 754 N ATOM 3280 C2 U B 5 14.672 -34.137 -0.376 1.00 42.46 C ANISOU 3280 C2 U B 5 5834 5651 4649 -1040 -83 727 C ATOM 3281 O2 U B 5 15.780 -33.681 -0.159 1.00 48.76 O ANISOU 3281 O2 U B 5 6621 6503 5402 -1012 -14 705 O ATOM 3282 N3 U B 5 14.508 -35.425 -0.808 1.00 46.11 N ANISOU 3282 N3 U B 5 6382 6099 5038 -1048 -81 728 N ATOM 3283 C4 U B 5 13.326 -36.070 -1.086 1.00 44.48 C ANISOU 3283 C4 U B 5 6198 5834 4866 -1073 -151 752 C ATOM 3284 O4 U B 5 13.348 -37.238 -1.462 1.00 55.94 O ANISOU 3284 O4 U B 5 7727 7286 6242 -1075 -133 749 O ATOM 3285 C5 U B 5 12.150 -35.264 -0.899 1.00 41.60 C ANISOU 3285 C5 U B 5 5763 5413 4632 -1098 -237 781 C ATOM 3286 C6 U B 5 12.275 -33.997 -0.482 1.00 41.47 C ANISOU 3286 C6 U B 5 5658 5404 4694 -1097 -239 781 C ATOM 3287 P C B 6 12.186 -28.740 -3.257 1.00 45.37 P ANISOU 3287 P C B 6 6050 5820 5369 -1303 -475 933 P ATOM 3288 OP1 C B 6 12.348 -27.276 -3.316 1.00 47.55 O ANISOU 3288 OP1 C B 6 6235 6108 5724 -1320 -489 949 O ATOM 3289 OP2 C B 6 10.921 -29.369 -3.686 1.00 34.93 O ANISOU 3289 OP2 C B 6 4767 4420 4084 -1356 -560 978 O ATOM 3290 O5' C B 6 13.360 -29.324 -4.149 1.00 32.17 O ANISOU 3290 O5' C B 6 4508 4187 3529 -1299 -444 917 O ATOM 3291 C5' C B 6 14.617 -28.692 -4.018 1.00 35.03 C ANISOU 3291 C5' C B 6 4857 4614 3840 -1256 -376 883 C ATOM 3292 C4' C B 6 15.691 -29.574 -4.591 1.00 33.21 C ANISOU 3292 C4' C B 6 4754 4414 3452 -1241 -329 859 C ATOM 3293 O4' C B 6 15.827 -30.736 -3.743 1.00 37.34 O ANISOU 3293 O4' C B 6 5290 4960 3938 -1190 -253 823 O ATOM 3294 C3' C B 6 15.351 -30.140 -5.956 1.00 33.56 C ANISOU 3294 C3' C B 6 4917 4407 3427 -1317 -407 899 C ATOM 3295 O3' C B 6 15.596 -29.149 -6.959 1.00 29.39 O ANISOU 3295 O3' C B 6 4402 3869 2893 -1366 -468 929 O ATOM 3296 C2' C B 6 16.333 -31.307 -5.986 1.00 49.98 C ANISOU 3296 C2' C B 6 7098 6521 5372 -1284 -324 861 C ATOM 3297 O2' C B 6 17.654 -30.900 -6.275 1.00 63.58 O ANISOU 3297 O2' C B 6 8861 8284 7011 -1259 -274 837 O ATOM 3298 C1' C B 6 16.254 -31.819 -4.545 1.00 44.98 C ANISOU 3298 C1' C B 6 6388 5921 4782 -1211 -243 822 C ATOM 3299 N1 C B 6 15.287 -32.935 -4.407 1.00 46.71 N ANISOU 3299 N1 C B 6 6628 6104 5016 -1224 -265 832 N ATOM 3300 C2 C B 6 15.757 -34.246 -4.522 1.00 53.83 C ANISOU 3300 C2 C B 6 7617 7023 5815 -1211 -206 810 C ATOM 3301 O2 C B 6 16.963 -34.434 -4.719 1.00 58.93 O ANISOU 3301 O2 C B 6 8321 7707 6363 -1192 -138 787 O ATOM 3302 N3 C B 6 14.878 -35.271 -4.407 1.00 52.68 N ANISOU 3302 N3 C B 6 7487 6849 5681 -1218 -224 817 N ATOM 3303 C4 C B 6 13.587 -35.020 -4.197 1.00 50.70 C ANISOU 3303 C4 C B 6 7178 6548 5538 -1236 -300 845 C ATOM 3304 N4 C B 6 12.758 -36.067 -4.096 1.00 55.24 N ANISOU 3304 N4 C B 6 7776 7096 6119 -1236 -316 850 N ATOM 3305 C5 C B 6 13.089 -33.688 -4.083 1.00 41.97 C ANISOU 3305 C5 C B 6 5987 5418 4541 -1255 -361 870 C ATOM 3306 C6 C B 6 13.965 -32.683 -4.195 1.00 40.77 C ANISOU 3306 C6 C B 6 5812 5301 4378 -1249 -340 862 C ATOM 3307 P A B 7 14.837 -29.169 -8.367 1.00 36.84 P ANISOU 3307 P A B 7 5416 4751 3829 -1471 -584 991 P ATOM 3308 OP1 A B 7 13.676 -30.087 -8.264 1.00 42.59 O ANISOU 3308 OP1 A B 7 6162 5430 4591 -1501 -621 1017 O ATOM 3309 OP2 A B 7 15.844 -29.375 -9.423 1.00 45.20 O ANISOU 3309 OP2 A B 7 6592 5824 4758 -1496 -579 983 O ATOM 3310 O5' A B 7 14.277 -27.685 -8.511 1.00 34.60 O ANISOU 3310 O5' A B 7 5023 4452 3673 -1506 -655 1032 O ATOM 3311 C5' A B 7 13.151 -27.259 -7.778 1.00 34.55 C ANISOU 3311 C5' A B 7 4903 4412 3813 -1512 -685 1056 C ATOM 3312 C4' A B 7 13.306 -25.807 -7.373 1.00 31.80 C ANISOU 3312 C4' A B 7 4426 4090 3568 -1495 -679 1057 C ATOM 3313 O4' A B 7 14.142 -25.738 -6.196 1.00 28.96 O ANISOU 3313 O4' A B 7 4013 3794 3197 -1400 -569 993 O ATOM 3314 C3' A B 7 13.998 -24.905 -8.387 1.00 31.21 C ANISOU 3314 C3' A B 7 4367 4036 3454 -1525 -713 1072 C ATOM 3315 O3' A B 7 13.047 -24.382 -9.291 1.00 34.45 O ANISOU 3315 O3' A B 7 4759 4392 3940 -1621 -823 1143 O ATOM 3316 C2' A B 7 14.449 -23.783 -7.475 1.00 29.16 C ANISOU 3316 C2' A B 7 3978 3828 3275 -1463 -652 1041 C ATOM 3317 O2' A B 7 13.363 -22.949 -7.156 1.00 32.64 O ANISOU 3317 O2' A B 7 4292 4232 3879 -1503 -699 1084 O ATOM 3318 C1' A B 7 14.896 -24.542 -6.229 1.00 28.67 C ANISOU 3318 C1' A B 7 3913 3802 3177 -1377 -546 981 C ATOM 3319 N9 A B 7 16.322 -24.852 -6.210 1.00 27.22 N ANISOU 3319 N9 A B 7 3804 3680 2859 -1313 -464 928 N ATOM 3320 C8 A B 7 16.939 -26.028 -6.553 1.00 28.86 C ANISOU 3320 C8 A B 7 4144 3892 2931 -1301 -433 906 C ATOM 3321 N7 A B 7 18.251 -25.992 -6.430 1.00 26.39 N ANISOU 3321 N7 A B 7 3871 3633 2524 -1241 -355 863 N ATOM 3322 C5 A B 7 18.503 -24.714 -5.978 1.00 26.31 C ANISOU 3322 C5 A B 7 3749 3660 2589 -1207 -335 854 C ATOM 3323 C6 A B 7 19.695 -24.053 -5.651 1.00 25.86 C ANISOU 3323 C6 A B 7 3671 3664 2490 -1138 -261 815 C ATOM 3324 N6 A B 7 20.894 -24.633 -5.744 1.00 21.94 N ANISOU 3324 N6 A B 7 3276 3197 1861 -1092 -194 780 N ATOM 3325 N1 A B 7 19.619 -22.774 -5.233 1.00 22.86 N ANISOU 3325 N1 A B 7 3163 3314 2210 -1120 -254 816 N ATOM 3326 C2 A B 7 18.416 -22.199 -5.145 1.00 23.34 C ANISOU 3326 C2 A B 7 3119 3338 2410 -1172 -318 855 C ATOM 3327 N3 A B 7 17.216 -22.717 -5.426 1.00 25.28 N ANISOU 3327 N3 A B 7 3376 3519 2712 -1241 -394 897 N ATOM 3328 C4 A B 7 17.333 -23.989 -5.843 1.00 26.09 C ANISOU 3328 C4 A B 7 3610 3599 2705 -1253 -400 893 C ATOM 3329 P U B 8 13.353 -24.210 -10.852 1.00 42.22 P ANISOU 3329 P U B 8 5833 5366 4844 -1698 -900 1180 P ATOM 3330 OP1 U B 8 12.200 -23.487 -11.442 1.00 43.44 O ANISOU 3330 OP1 U B 8 5918 5466 5119 -1794 -1004 1259 O ATOM 3331 OP2 U B 8 13.800 -25.492 -11.414 1.00 38.47 O ANISOU 3331 OP2 U B 8 5512 4887 4220 -1707 -886 1161 O ATOM 3332 O5' U B 8 14.611 -23.225 -10.880 1.00 29.57 O ANISOU 3332 O5' U B 8 4195 3830 3209 -1642 -854 1139 O ATOM 3333 C5' U B 8 15.154 -22.915 -12.157 1.00 25.98 C ANISOU 3333 C5' U B 8 3810 3379 2680 -1691 -909 1155 C ATOM 3334 C4' U B 8 15.180 -21.415 -12.335 1.00 28.94 C ANISOU 3334 C4' U B 8 4063 3776 3155 -1699 -942 1177 C ATOM 3335 O4' U B 8 16.154 -20.844 -11.438 1.00 27.66 O ANISOU 3335 O4' U B 8 3840 3680 2989 -1593 -846 1115 O ATOM 3336 C3' U B 8 15.631 -20.943 -13.701 1.00 27.26 C ANISOU 3336 C3' U B 8 3904 3568 2886 -1757 -1014 1200 C ATOM 3337 O3' U B 8 14.534 -20.977 -14.600 1.00 34.65 O ANISOU 3337 O3' U B 8 4845 4447 3874 -1877 -1122 1278 O ATOM 3338 C2' U B 8 16.049 -19.511 -13.401 1.00 29.27 C ANISOU 3338 C2' U B 8 4025 3871 3225 -1710 -995 1188 C ATOM 3339 O2' U B 8 14.959 -18.620 -13.378 1.00 36.23 O ANISOU 3339 O2' U B 8 4769 4728 4270 -1772 -1054 1250 O ATOM 3340 C1' U B 8 16.620 -19.628 -11.988 1.00 24.69 C ANISOU 3340 C1' U B 8 3403 3335 2641 -1595 -874 1121 C ATOM 3341 N1 U B 8 18.116 -19.624 -11.965 1.00 24.44 N ANISOU 3341 N1 U B 8 3441 3361 2485 -1508 -802 1055 N ATOM 3342 C2 U B 8 18.742 -18.403 -12.098 1.00 24.39 C ANISOU 3342 C2 U B 8 3357 3401 2508 -1469 -795 1041 C ATOM 3343 O2 U B 8 18.108 -17.367 -12.223 1.00 27.44 O ANISOU 3343 O2 U B 8 3617 3787 3022 -1508 -843 1082 O ATOM 3344 N3 U B 8 20.126 -18.449 -12.077 1.00 23.88 N ANISOU 3344 N3 U B 8 3368 3382 2324 -1386 -728 981 N ATOM 3345 C4 U B 8 20.920 -19.581 -11.933 1.00 23.41 C ANISOU 3345 C4 U B 8 3448 3322 2126 -1344 -667 938 C ATOM 3346 O4 U B 8 22.147 -19.476 -11.927 1.00 22.43 O ANISOU 3346 O4 U B 8 3380 3234 1907 -1272 -609 890 O ATOM 3347 C5 U B 8 20.178 -20.819 -11.818 1.00 25.63 C ANISOU 3347 C5 U B 8 3794 3556 2389 -1394 -676 957 C ATOM 3348 C6 U B 8 18.834 -20.795 -11.838 1.00 25.69 C ANISOU 3348 C6 U B 8 3734 3522 2507 -1469 -743 1011 C ATOM 3349 P U B 9 14.746 -21.412 -16.127 1.00 50.48 P ANISOU 3349 P U B 9 6982 6430 5768 -1969 -1199 1306 P ATOM 3350 OP1 U B 9 13.420 -21.687 -16.708 1.00 48.81 O ANISOU 3350 OP1 U B 9 6771 6156 5620 -2085 -1291 1388 O ATOM 3351 OP2 U B 9 15.796 -22.453 -16.170 1.00 44.26 O ANISOU 3351 OP2 U B 9 6338 5659 4818 -1919 -1132 1242 O ATOM 3352 O5' U B 9 15.295 -20.075 -16.817 1.00 53.77 O ANISOU 3352 O5' U B 9 7332 6884 6217 -1979 -1242 1314 O ATOM 3353 C5' U B 9 14.419 -18.966 -17.035 1.00 55.23 C ANISOU 3353 C5' U B 9 7376 7056 6553 -2043 -1314 1381 C ATOM 3354 C4' U B 9 15.049 -17.915 -17.937 1.00 59.16 C ANISOU 3354 C4' U B 9 7839 7590 7049 -2062 -1362 1387 C ATOM 3355 O4' U B 9 16.402 -17.636 -17.493 1.00 57.94 O ANISOU 3355 O4' U B 9 7700 7497 6819 -1941 -1277 1303 O ATOM 3356 C3' U B 9 15.204 -18.313 -19.398 1.00 62.33 C ANISOU 3356 C3' U B 9 8362 7971 7351 -2160 -1446 1415 C ATOM 3357 O3' U B 9 13.999 -18.047 -20.113 1.00 59.76 O ANISOU 3357 O3' U B 9 7984 7602 7121 -2291 -1549 1510 O ATOM 3358 C2' U B 9 16.366 -17.433 -19.863 1.00 63.81 C ANISOU 3358 C2' U B 9 8537 8213 7495 -2111 -1443 1373 C ATOM 3359 O2' U B 9 15.977 -16.138 -20.281 1.00 66.58 O ANISOU 3359 O2' U B 9 8745 8581 7971 -2156 -1509 1423 O ATOM 3360 C1' U B 9 17.225 -17.326 -18.604 1.00 60.24 C ANISOU 3360 C1' U B 9 8057 7807 7024 -1962 -1322 1292 C ATOM 3361 N1 U B 9 18.387 -18.252 -18.642 1.00 57.45 N ANISOU 3361 N1 U B 9 7864 7463 6501 -1900 -1259 1221 N ATOM 3362 C2 U B 9 19.599 -17.762 -19.069 1.00 55.88 C ANISOU 3362 C2 U B 9 7704 7303 6225 -1844 -1245 1172 C ATOM 3363 O2 U B 9 19.754 -16.603 -19.405 1.00 56.63 O ANISOU 3363 O2 U B 9 7704 7430 6384 -1839 -1283 1182 O ATOM 3364 N3 U B 9 20.624 -18.677 -19.084 1.00 53.19 N ANISOU 3364 N3 U B 9 7516 6960 5734 -1795 -1184 1113 N ATOM 3365 C4 U B 9 20.547 -20.008 -18.722 1.00 60.77 C ANISOU 3365 C4 U B 9 8582 7889 6618 -1798 -1134 1098 C ATOM 3366 O4 U B 9 21.548 -20.714 -18.783 1.00 63.84 O ANISOU 3366 O4 U B 9 9098 8278 6880 -1756 -1077 1047 O ATOM 3367 C5 U B 9 19.245 -20.447 -18.287 1.00 60.53 C ANISOU 3367 C5 U B 9 8498 7827 6674 -1852 -1153 1148 C ATOM 3368 C6 U B 9 18.234 -19.572 -18.268 1.00 59.85 C ANISOU 3368 C6 U B 9 8272 7735 6731 -1900 -1215 1207 C TER 3369 U B 9 HETATM 3370 O HOH A 1 25.514 -39.040 7.494 1.00 16.21 O HETATM 3371 O HOH A 2 4.260 -48.060 23.591 1.00 17.90 O HETATM 3372 O HOH A 3 44.832 -33.641 4.493 1.00 21.99 O HETATM 3373 O HOH A 4 4.262 -39.375 14.053 1.00 22.56 O HETATM 3374 O HOH A 5 41.696 -20.853 -3.001 1.00 20.55 O HETATM 3375 O HOH A 6 38.335 -14.369 -5.158 1.00 19.28 O HETATM 3376 O HOH A 7 -0.720 -62.835 24.064 1.00 20.63 O HETATM 3377 O HOH A 8 21.361 -27.375 -2.758 1.00 32.52 O HETATM 3378 O HOH A 9 35.152 -15.391 -22.344 1.00 20.59 O HETATM 3379 O HOH A 10 7.847 -50.683 4.941 1.00 21.36 O HETATM 3380 O HOH A 11 32.661 -28.433 4.488 1.00 26.24 O HETATM 3381 O HOH A 12 -1.016 -57.425 8.567 1.00 17.65 O HETATM 3382 O HOH A 13 27.304 0.043 -21.511 1.00 20.57 O HETATM 3383 O HOH A 14 2.203 -59.142 21.474 1.00 21.83 O HETATM 3384 O HOH A 15 36.091 -39.817 7.558 1.00 22.57 O HETATM 3385 O HOH A 16 30.931 -17.263 -11.293 1.00 23.21 O HETATM 3386 O HOH A 17 -3.702 -45.089 6.393 1.00 30.66 O HETATM 3387 O HOH A 18 32.492 -16.993 -17.065 1.00 25.14 O HETATM 3388 O HOH A 19 -3.291 -54.006 4.162 1.00 18.44 O HETATM 3389 O HOH A 20 30.742 -40.046 12.077 1.00 19.53 O HETATM 3390 O HOH A 21 25.441 -29.511 0.170 1.00 26.52 O HETATM 3391 O HOH A 22 -4.088 -51.150 7.051 1.00 27.58 O HETATM 3392 O HOH A 23 34.646 -6.129 -8.697 1.00 26.69 O HETATM 3393 O HOH A 24 -3.083 -53.674 6.964 1.00 22.29 O HETATM 3394 O HOH A 25 -7.386 -58.354 15.970 1.00 27.69 O HETATM 3395 O HOH A 26 -5.169 -52.799 0.101 1.00 23.65 O HETATM 3396 O HOH A 27 -11.043 -56.227 16.204 1.00 24.17 O HETATM 3397 O HOH A 28 24.085 0.835 -18.485 1.00 28.44 O HETATM 3398 O HOH A 29 3.640 -57.429 24.276 1.00 25.79 O HETATM 3399 O HOH A 30 42.850 -17.384 -11.740 1.00 31.73 O HETATM 3400 O HOH A 31 33.708 -30.182 2.450 1.00 32.18 O HETATM 3401 O HOH A 32 1.655 -56.917 8.948 1.00 21.57 O HETATM 3402 O HOH A 33 22.825 -51.479 9.361 1.00 30.32 O HETATM 3403 O HOH A 34 -12.594 -58.531 4.397 1.00 25.11 O HETATM 3404 O HOH A 35 35.294 -19.723 -11.775 1.00 25.97 O HETATM 3405 O HOH A 36 24.732 -20.752 -8.575 1.00 30.35 O HETATM 3406 O HOH A 37 35.493 -25.176 -4.897 1.00 25.80 O HETATM 3407 O HOH A 38 37.663 -28.843 7.879 1.00 32.76 O HETATM 3408 O HOH A 39 26.745 -0.483 -15.074 1.00 21.82 O HETATM 3409 O HOH A 40 7.003 -52.969 5.861 1.00 23.69 O HETATM 3410 O HOH A 41 34.431 -29.516 6.426 1.00 36.29 O HETATM 3411 O HOH A 42 18.892 -54.987 13.259 1.00 25.80 O HETATM 3412 O HOH A 43 41.245 -5.344 -15.979 1.00 33.73 O HETATM 3413 O HOH A 44 6.286 -59.528 5.297 1.00 38.38 O HETATM 3414 O HOH A 45 27.480 -11.334 10.493 1.00 42.36 O HETATM 3415 O HOH A 46 -5.768 -60.703 15.800 1.00 22.21 O HETATM 3416 O HOH A 47 18.062 -29.642 -1.387 1.00 23.71 O HETATM 3417 O HOH A 48 -1.362 -55.052 24.686 1.00 34.15 O HETATM 3418 O HOH A 49 -2.194 -47.314 6.000 1.00 23.46 O HETATM 3419 O HOH A 50 30.356 -57.293 16.647 1.00 37.21 O HETATM 3420 O HOH A 51 37.030 -18.502 -13.528 1.00 21.65 O HETATM 3421 O HOH A 52 6.181 -29.359 11.242 1.00 23.54 O HETATM 3422 O HOH A 53 15.388 -2.985 -20.469 1.00 38.68 O HETATM 3423 O HOH A 54 -5.791 -48.558 12.032 1.00 23.87 O HETATM 3424 O HOH A 55 11.387 -52.510 26.090 1.00 23.06 O HETATM 3425 O HOH A 56 27.597 -30.989 1.476 1.00 36.48 O HETATM 3426 O HOH A 57 -4.578 -62.680 27.876 1.00 24.62 O HETATM 3427 O HOH A 58 27.960 -42.460 5.893 1.00 30.46 O HETATM 3428 O HOH A 59 42.199 -3.053 -20.147 1.00 24.39 O HETATM 3429 O HOH A 60 20.561 -31.771 -0.429 1.00 38.62 O HETATM 3430 O HOH A 61 41.264 -6.710 -18.281 1.00 43.71 O HETATM 3431 O HOH A 62 37.771 -26.432 9.315 1.00 25.34 O HETATM 3432 O HOH A 63 35.421 -2.395 -26.224 1.00 30.53 O HETATM 3433 O HOH A 64 33.252 0.965 -18.923 1.00 29.21 O HETATM 3434 O HOH A 65 4.027 -33.217 12.574 1.00 31.78 O HETATM 3435 O HOH A 67 -7.724 -67.878 11.131 1.00 25.25 O HETATM 3436 O HOH A 68 13.733 -9.988 -11.918 1.00 29.65 O HETATM 3437 O HOH A 69 1.256 -49.280 0.888 1.00 25.56 O HETATM 3438 O HOH A 70 23.371 -25.780 -2.985 1.00 28.58 O HETATM 3439 O HOH A 71 34.042 -22.461 15.708 1.00 41.32 O HETATM 3440 O HOH A 72 37.405 -14.328 -21.320 1.00 27.27 O HETATM 3441 O HOH A 73 17.308 -48.435 5.494 1.00 29.92 O HETATM 3442 O HOH A 75 7.615 -26.335 6.239 1.00 25.77 O HETATM 3443 O HOH A 76 33.037 -6.308 -29.865 1.00 29.21 O HETATM 3444 O HOH A 77 32.447 -20.887 13.165 1.00 33.84 O HETATM 3445 O HOH A 78 9.070 -54.903 5.186 1.00 40.03 O HETATM 3446 O HOH A 79 43.918 -17.078 -6.875 1.00 33.85 O HETATM 3447 O HOH A 80 40.248 -4.340 -13.354 1.00 29.59 O HETATM 3448 O HOH A 81 14.543 -10.318 -7.376 1.00 24.66 O HETATM 3449 O HOH A 82 36.499 -30.226 10.210 1.00 28.37 O HETATM 3450 O HOH A 83 46.094 -8.082 -8.095 1.00 26.47 O HETATM 3451 O HOH A 84 39.104 -14.222 -23.712 1.00 32.07 O HETATM 3452 O HOH A 85 29.247 -32.299 -0.161 1.00 35.45 O HETATM 3453 O HOH A 86 37.690 -2.932 -14.388 1.00 35.09 O HETATM 3454 O HOH A 87 44.220 -37.342 6.502 1.00 27.89 O HETATM 3455 O HOH A 88 25.189 -47.071 6.372 1.00 30.44 O HETATM 3456 O HOH A 89 38.352 -31.167 2.969 1.00 29.04 O HETATM 3457 O HOH A 90 37.005 -25.804 1.293 1.00 31.97 O HETATM 3458 O HOH A 91 12.084 -65.076 22.341 1.00 35.62 O HETATM 3459 O HOH A 92 15.703 -10.445 -0.694 1.00 29.65 O HETATM 3460 O HOH A 93 29.922 1.159 -5.386 1.00 27.94 O HETATM 3461 O HOH A 95 15.815 -27.807 -0.527 1.00 26.11 O HETATM 3462 O HOH A 96 10.268 -19.971 1.484 1.00 30.67 O HETATM 3463 O HOH A 98 28.142 -50.611 6.545 1.00 40.79 O HETATM 3464 O HOH A 100 -5.271 -52.623 15.287 1.00 32.84 O HETATM 3465 O HOH A 101 26.198 -17.870 -16.159 1.00 35.58 O HETATM 3466 O HOH A 102 29.448 -44.561 15.937 1.00 31.14 O HETATM 3467 O HOH A 103 28.672 -2.355 -11.685 1.00 34.83 O HETATM 3468 O HOH A 104 31.932 -40.323 14.637 1.00 35.33 O HETATM 3469 O HOH A 105 3.425 -61.934 -5.453 1.00 37.69 O HETATM 3470 O HOH A 106 26.788 0.333 -17.663 1.00 29.82 O HETATM 3471 O HOH A 107 26.787 -32.792 3.392 1.00 27.02 O HETATM 3472 O HOH A 108 17.595 -25.302 -10.023 1.00 26.90 O HETATM 3473 O HOH A 109 9.618 -22.644 5.092 1.00 29.10 O HETATM 3474 O HOH A 110 -3.377 -68.500 20.735 1.00 40.13 O HETATM 3475 O HOH A 111 23.151 -9.140 5.892 1.00 35.79 O HETATM 3476 O HOH A 112 35.668 -17.823 -21.078 1.00 47.57 O HETATM 3477 O HOH A 113 20.368 -1.672 -6.880 1.00 33.42 O HETATM 3478 O HOH A 114 44.360 -5.038 -7.291 1.00 30.00 O HETATM 3479 O HOH A 115 -5.988 -54.287 2.583 1.00 30.63 O HETATM 3480 O HOH A 117 43.483 -10.016 -20.032 1.00 50.45 O HETATM 3481 O HOH A 118 10.519 -17.264 7.668 1.00 42.57 O HETATM 3482 O HOH A 119 40.066 -30.780 20.519 1.00 37.26 O HETATM 3483 O HOH A 120 3.673 -33.142 5.768 1.00 32.60 O HETATM 3484 O HOH A 122 8.373 -20.280 5.924 1.00 46.15 O HETATM 3485 O HOH A 123 12.897 -44.478 25.360 1.00 33.14 O HETATM 3486 O HOH A 124 41.720 -13.972 -22.769 1.00 42.57 O HETATM 3487 O HOH A 125 28.785 -1.158 2.719 1.00 41.72 O HETATM 3488 O HOH A 126 22.746 -69.436 16.991 1.00 28.52 O HETATM 3489 O HOH A 127 15.847 -70.712 2.715 1.00 42.81 O HETATM 3490 O HOH A 128 -4.186 -62.542 21.266 1.00 32.72 O HETATM 3491 O HOH A 129 32.784 -17.177 9.970 1.00 47.13 O HETATM 3492 O HOH A 130 37.369 -38.501 14.614 1.00 46.00 O HETATM 3493 O HOH A 131 25.437 -27.604 -2.563 1.00 39.17 O HETATM 3494 O HOH A 132 16.630 -47.502 27.041 1.00 46.39 O HETATM 3495 O HOH A 134 12.315 -55.251 26.023 1.00 33.91 O HETATM 3496 O HOH A 135 32.144 -34.859 3.057 1.00 33.97 O HETATM 3497 O HOH A 136 0.229 -43.986 19.210 1.00 33.09 O HETATM 3498 O HOH A 137 22.688 -39.727 2.659 1.00 48.99 O HETATM 3499 O HOH A 138 24.586 -29.185 22.037 1.00 38.81 O HETATM 3500 O HOH A 139 30.516 3.397 -21.568 1.00 50.07 O HETATM 3501 O HOH A 140 9.160 -40.314 1.829 1.00 37.29 O HETATM 3502 O HOH A 141 9.605 -62.319 24.408 1.00 45.31 O HETATM 3503 O HOH A 143 38.549 -3.048 -3.568 1.00 40.70 O HETATM 3504 O HOH A 144 7.813 -21.257 1.117 1.00 51.08 O HETATM 3505 O HOH A 145 -0.274 -47.497 22.577 1.00 45.93 O HETATM 3506 O HOH A 146 26.699 2.189 -6.216 1.00 39.95 O HETATM 3507 O HOH A 147 -10.961 -57.815 2.087 1.00 28.73 O HETATM 3508 O HOH A 148 5.883 -71.554 14.433 1.00 40.64 O HETATM 3509 O HOH A 149 8.123 -29.675 16.455 1.00 41.12 O HETATM 3510 O HOH A 150 9.314 -71.213 10.649 1.00 50.57 O HETATM 3511 O HOH A 151 13.925 -7.755 -16.146 1.00 30.59 O HETATM 3512 O HOH A 152 30.938 -8.870 -30.473 1.00 30.27 O HETATM 3513 O HOH A 153 11.293 -15.997 -3.715 1.00 33.28 O HETATM 3514 O HOH A 154 35.179 -4.865 -10.921 1.00 29.66 O HETATM 3515 O HOH A 155 6.352 -49.826 27.735 1.00 33.76 O HETATM 3516 O HOH A 156 16.595 -64.978 22.084 1.00 49.91 O HETATM 3517 O HOH A 157 38.590 -15.313 -19.204 1.00 33.73 O HETATM 3518 O HOH A 158 40.566 -33.278 21.790 1.00 50.14 O HETATM 3519 O HOH A 159 26.738 -29.994 -3.501 1.00 56.55 O HETATM 3520 O HOH A 160 36.733 -17.151 -18.343 1.00 32.28 O HETATM 3521 O HOH A 161 34.947 -18.022 -16.390 1.00 45.59 O HETATM 3522 O HOH A 162 -2.440 -40.982 6.558 1.00 44.41 O HETATM 3523 O HOH A 163 15.882 -40.029 5.814 1.00 30.61 O HETATM 3524 O HOH A 576 12.612 -15.251 0.314 1.00 27.88 O HETATM 3525 O HOH A 577 17.779 -29.605 21.988 1.00 39.28 O HETATM 3526 O HOH A 578 -3.571 -62.559 25.032 1.00 28.70 O HETATM 3527 O HOH A 579 17.701 -56.822 7.519 1.00 44.80 O HETATM 3528 O HOH A 580 43.012 -17.847 -16.076 1.00 33.61 O HETATM 3529 O HOH A 581 29.939 1.046 -2.330 1.00 50.23 O HETATM 3530 O HOH A 582 41.851 -12.658 -25.673 1.00 32.67 O HETATM 3531 O HOH A 583 25.055 -10.302 -32.603 1.00 46.16 O HETATM 3532 O HOH A 584 -6.388 -60.774 28.747 1.00 26.22 O HETATM 3533 O HOH A 585 12.929 -13.586 -4.366 1.00 32.59 O HETATM 3534 O HOH A 586 6.339 -58.016 0.991 1.00 42.55 O HETATM 3535 O HOH A 587 9.721 -46.720 5.655 1.00 37.40 O HETATM 3536 O HOH A 588 24.123 -24.705 20.849 1.00 35.47 O HETATM 3537 O HOH A 589 14.959 -20.989 -5.803 1.00 30.78 O HETATM 3538 O HOH A 590 2.458 -69.059 4.498 1.00 39.62 O HETATM 3539 O HOH A 591 7.073 -52.429 26.914 1.00 40.13 O HETATM 3540 O HOH A 592 -4.960 -63.508 18.119 1.00 42.16 O HETATM 3541 O HOH A 593 0.439 -57.377 24.554 1.00 28.20 O HETATM 3542 O HOH A 594 32.385 -29.623 -2.165 1.00 40.19 O HETATM 3543 O HOH A 595 22.934 -22.777 -8.240 1.00 32.73 O HETATM 3544 O HOH A 596 30.438 -36.726 4.461 1.00 32.43 O HETATM 3545 O HOH A 597 46.320 -13.180 -6.622 1.00 50.36 O HETATM 3546 O HOH A 598 8.411 -34.895 23.354 1.00 48.54 O HETATM 3547 O HOH A 599 35.450 -17.169 8.537 1.00 50.19 O HETATM 3548 O HOH A 600 26.590 -22.550 -7.661 1.00 33.02 O HETATM 3549 O HOH A 601 44.750 -11.430 -4.503 1.00 43.75 O HETATM 3550 O HOH A 602 40.883 -38.139 7.961 1.00 34.13 O HETATM 3551 O HOH A 603 15.775 -69.794 21.251 1.00 40.17 O HETATM 3552 O HOH A 604 36.420 -2.663 -10.314 1.00 45.09 O HETATM 3553 O HOH A 605 47.373 -10.143 -9.655 1.00 46.13 O HETATM 3554 O HOH A 606 -9.659 -55.015 22.755 1.00 46.59 O HETATM 3555 O HOH A 607 23.065 -16.831 -24.552 1.00 34.22 O HETATM 3556 O HOH A 608 2.452 -52.728 -0.442 1.00 47.63 O HETATM 3557 O HOH A 609 30.766 -15.887 -28.529 1.00 40.30 O HETATM 3558 O HOH A 610 40.484 -3.908 -27.077 1.00 40.51 O HETATM 3559 O HOH A 611 19.722 -22.269 -15.245 1.00 32.18 O HETATM 3560 O HOH A 612 0.921 -52.763 29.007 1.00 33.44 O HETATM 3561 O HOH A 613 12.284 -73.010 14.848 1.00 44.63 O HETATM 3562 O HOH A 614 39.645 -34.263 24.608 1.00 56.61 O HETATM 3563 O HOH A 615 12.761 -37.296 23.516 1.00 49.21 O HETATM 3564 O HOH A 616 15.586 -70.830 18.099 1.00 28.78 O HETATM 3565 O HOH A 617 38.172 -17.182 -23.799 1.00 56.67 O HETATM 3566 O HOH A 618 23.600 -52.552 12.793 1.00 36.00 O HETATM 3567 O HOH A 619 21.484 4.072 -20.277 1.00 56.66 O HETATM 3568 O HOH A 620 1.541 -48.149 24.436 1.00 34.88 O HETATM 3569 O HOH A 621 -8.214 -71.500 11.840 1.00 58.40 O HETATM 3570 O HOH A 622 16.648 -6.312 -10.240 1.00 39.49 O HETATM 3571 O HOH A 623 24.551 -20.183 18.978 1.00 47.60 O HETATM 3572 O HOH A 624 13.502 -51.410 27.755 1.00 38.16 O HETATM 3573 O HOH A 625 -6.092 -46.245 13.720 1.00 43.20 O HETATM 3574 O HOH A 626 20.977 -7.749 3.749 1.00 32.31 O HETATM 3575 O HOH A 627 24.521 -49.896 16.026 1.00 32.03 O HETATM 3576 O HOH A 628 31.671 -60.923 16.126 1.00 42.93 O HETATM 3577 O HOH A 629 36.144 -27.606 3.020 1.00 38.41 O HETATM 3578 O HOH A 630 6.271 -33.920 17.114 1.00 43.54 O HETATM 3579 O HOH A 631 -6.599 -55.636 16.064 1.00 34.04 O HETATM 3580 O HOH A 632 22.998 2.501 -16.498 1.00 48.42 O HETATM 3581 O HOH A 633 4.366 -45.171 24.785 1.00 41.34 O HETATM 3582 O HOH A 634 6.001 -57.249 3.538 1.00 39.66 O HETATM 3583 O HOH A 635 -6.229 -68.765 4.310 1.00 49.82 O HETATM 3584 O HOH A 636 -3.736 -42.722 4.775 1.00 51.96 O HETATM 3585 O HOH A 637 25.712 -53.196 8.709 1.00 49.57 O HETATM 3586 O HOH A 638 -13.897 -61.246 28.516 1.00 42.72 O HETATM 3587 O HOH A 639 38.362 -20.004 -15.853 1.00 55.33 O HETATM 3588 O HOH A 640 -3.642 -65.475 1.486 1.00 44.81 O HETATM 3589 O HOH A 641 38.935 -8.742 -30.685 1.00 54.15 O HETATM 3590 O HOH A 642 23.079 -48.757 6.190 1.00 48.94 O HETATM 3591 O HOH A 643 -4.781 -72.004 10.326 1.00 47.03 O HETATM 3592 O HOH A 644 26.098 4.222 -29.345 1.00 53.81 O HETATM 3593 O HOH A 645 28.090 -69.128 17.974 1.00 41.14 O HETATM 3594 O HOH A 646 9.757 -50.882 3.015 1.00 41.96 O HETATM 3595 O HOH A 647 29.303 -42.135 14.960 1.00 40.33 O HETATM 3596 O HOH A 648 35.197 3.314 -24.409 1.00 53.09 O HETATM 3597 O HOH A 649 19.144 1.301 -17.118 1.00 48.51 O HETATM 3598 O HOH A 650 19.468 -41.128 4.522 1.00 51.45 O HETATM 3599 O HOH A 651 19.763 -12.385 -28.316 1.00 40.03 O HETATM 3600 O HOH A 652 40.619 -13.144 -4.226 1.00 44.62 O HETATM 3601 O HOH A 653 33.277 -11.857 -27.833 1.00 50.13 O HETATM 3602 O HOH A 654 38.128 -37.327 17.420 1.00 38.30 O HETATM 3603 O HOH A 655 -10.921 -64.511 5.234 1.00 44.85 O HETATM 3604 O HOH A 656 33.836 -31.223 8.582 1.00 39.03 O HETATM 3605 O HOH A 657 3.002 -43.951 7.777 1.00 27.23 O HETATM 3606 O HOH A 658 3.044 -59.815 28.730 1.00 26.98 O HETATM 3607 O HOH A 659 48.651 -1.382 -8.094 1.00 51.75 O HETATM 3608 O HOH A 660 19.654 6.510 -20.090 1.00 51.18 O HETATM 3609 O HOH A 661 25.477 -45.280 22.335 1.00 51.80 O HETATM 3610 O HOH A 662 12.752 -55.874 6.737 1.00 46.14 O HETATM 3611 O HOH A 663 11.768 -13.546 2.339 1.00 45.32 O HETATM 3612 O HOH A 664 0.700 -36.931 13.855 1.00 56.62 O HETATM 3613 O HOH A 665 -0.489 -63.193 -2.060 1.00 48.75 O HETATM 3614 O HOH A 666 45.353 -2.007 -10.210 1.00 53.03 O HETATM 3615 O HOH A 667 1.060 -60.316 -1.940 1.00 47.79 O HETATM 3616 O HOH A 668 28.829 -28.460 24.617 1.00 47.94 O HETATM 3617 O HOH A 669 11.015 -62.569 22.000 1.00 39.33 O HETATM 3618 O HOH A 670 15.080 -73.488 14.434 1.00 48.94 O HETATM 3619 O HOH A 671 46.399 -12.887 -9.515 1.00 35.14 O HETATM 3620 O HOH A 672 10.372 -61.918 27.664 1.00 52.27 O HETATM 3621 O HOH A 673 -0.316 -40.390 13.383 1.00 21.77 O HETATM 3622 O HOH A 674 34.276 -28.865 17.285 1.00 30.18 O HETATM 3623 O HOH A 675 12.588 -9.028 -21.351 1.00 33.39 O HETATM 3624 O HOH A 676 35.710 -25.352 17.951 1.00 31.76 O HETATM 3625 O HOH A 677 44.318 -16.553 -9.575 1.00 31.30 O HETATM 3626 O HOH A 678 31.486 -44.491 4.675 1.00 34.86 O HETATM 3627 O HOH A 679 26.345 -19.657 16.769 1.00 39.18 O HETATM 3628 O HOH A 680 -0.795 -64.670 0.344 1.00 30.46 O HETATM 3629 O HOH A 681 14.239 -25.281 -2.751 1.00 36.31 O HETATM 3630 O HOH A 682 16.525 -22.421 23.083 1.00 42.11 O HETATM 3631 O HOH A 683 37.929 -3.566 -27.220 1.00 45.73 O HETATM 3632 O HOH A 684 11.539 -53.661 5.430 1.00 47.39 O HETATM 3633 O HOH A 685 -2.269 -43.706 17.740 1.00 51.89 O HETATM 3634 O HOH A 686 16.808 -19.742 -8.083 1.00 37.59 O HETATM 3635 O HOH A 687 11.641 -17.786 10.021 1.00 54.68 O HETATM 3636 O HOH A 688 39.601 -15.660 5.106 1.00 37.17 O HETATM 3637 O HOH A 689 27.190 -38.961 5.316 1.00 44.70 O HETATM 3638 O HOH A 690 9.426 -52.998 28.051 1.00 40.79 O HETATM 3639 O HOH A 691 -10.281 -63.509 2.714 1.00 37.71 O HETATM 3640 O HOH A 692 31.289 -32.078 -2.106 1.00 56.66 O HETATM 3641 O HOH A 693 10.725 -64.821 2.340 1.00 41.54 O HETATM 3642 O HOH A 694 11.240 -34.632 22.655 1.00 33.92 O HETATM 3643 O HOH A 695 -0.706 -52.022 26.824 1.00 54.65 O HETATM 3644 O HOH A 696 -6.965 -60.664 31.416 1.00 38.18 O HETATM 3645 O HOH A 697 3.185 -34.969 14.456 1.00 42.97 O HETATM 3646 O HOH A 698 0.333 -69.489 6.826 1.00 46.83 O HETATM 3647 O HOH A 699 12.212 -17.377 5.145 1.00 35.90 O HETATM 3648 O HOH A 700 35.348 -28.903 0.720 1.00 35.13 O HETATM 3649 O HOH A 701 28.213 -19.898 -11.888 1.00 35.84 O HETATM 3650 O HOH A 702 40.834 -13.456 -18.936 1.00 34.33 O HETATM 3651 O HOH A 703 -6.864 -67.162 15.499 1.00 38.98 O HETATM 3652 O HOH A 704 5.119 -28.084 13.641 1.00 51.57 O HETATM 3653 O HOH A 705 22.515 -25.341 23.064 1.00 45.65 O HETATM 3654 O HOH A 706 19.523 -58.128 24.796 1.00 46.51 O HETATM 3655 O HOH A 707 18.183 -14.172 -21.426 1.00 40.91 O HETATM 3656 O HOH A 708 32.435 -10.406 5.486 1.00 42.14 O HETATM 3657 O HOH A 709 41.328 -10.481 -3.227 1.00 42.36 O HETATM 3658 O HOH A 710 29.667 -2.551 0.140 1.00 44.40 O HETATM 3659 O HOH A 711 40.974 -40.810 7.314 1.00 40.79 O HETATM 3660 O HOH A 712 33.589 2.456 -21.406 1.00 39.91 O HETATM 3661 O HOH A 713 26.396 -26.487 20.955 1.00 43.86 O HETATM 3662 O HOH A 714 26.465 -29.871 23.993 1.00 49.38 O HETATM 3663 O HOH A 715 3.310 -58.815 31.448 1.00 47.81 O HETATM 3664 O HOH A 716 18.648 -23.722 -12.842 1.00 35.99 O HETATM 3665 O HOH A 717 21.955 -19.551 19.133 1.00 44.08 O HETATM 3666 O HOH A 718 35.430 -2.386 -1.786 1.00 54.98 O HETATM 3667 O HOH A 719 31.271 -63.699 15.380 1.00 50.19 O HETATM 3668 O HOH A 720 22.502 -9.046 -32.147 1.00 46.82 O HETATM 3669 O HOH A 721 37.190 -29.200 4.970 1.00 51.90 O HETATM 3670 O HOH A 722 12.110 -1.364 -23.787 1.00 54.13 O HETATM 3671 O HOH A 723 35.947 0.125 -27.302 1.00 48.81 O HETATM 3672 O HOH A 724 14.491 -12.272 7.369 1.00 41.29 O HETATM 3673 O HOH A 725 24.038 -38.241 21.906 1.00 44.42 O HETATM 3674 O HOH A 726 38.535 -2.905 -8.338 1.00 43.06 O HETATM 3675 O HOH A 727 8.708 -16.634 12.083 1.00 51.07 O HETATM 3676 O HOH A 728 40.819 -3.652 -9.675 1.00 50.56 O HETATM 3677 O HOH A 729 13.109 -16.117 11.834 1.00 42.98 O HETATM 3678 O HOH A 730 10.100 -56.682 27.206 1.00 37.74 O HETATM 3679 O HOH A 731 5.495 -31.845 15.507 1.00 42.67 O HETATM 3680 O HOH A 732 23.700 -11.210 13.599 1.00 53.02 O HETATM 3681 O HOH A 733 20.747 -36.683 1.186 1.00 51.97 O HETATM 3682 O HOH A 734 8.968 -25.001 11.755 1.00 53.33 O HETATM 3683 O HOH A 735 13.093 -6.060 -19.187 1.00 49.52 O HETATM 3684 O HOH A 736 13.744 -18.464 18.443 1.00 53.61 O HETATM 3685 O HOH A 737 24.899 -56.070 19.710 1.00 41.92 O HETATM 3686 O HOH A 738 18.538 -71.456 8.468 1.00 48.48 O HETATM 3687 O HOH A 739 28.861 -18.804 -14.787 1.00 52.38 O HETATM 3688 O HOH A 740 29.505 -43.217 2.399 1.00 55.60 O HETATM 3689 O HOH A 741 9.625 -69.100 19.270 1.00 44.44 O HETATM 3690 O HOH A 742 7.622 -60.497 30.306 1.00 51.46 O HETATM 3691 O HOH A 743 13.747 -60.428 1.298 1.00 51.40 O HETATM 3692 O HOH A 744 -12.365 -53.604 15.809 1.00 46.97 O HETATM 3693 O HOH A 745 20.992 -0.776 -4.142 1.00 43.25 O HETATM 3694 O HOH A 746 39.250 -9.337 2.858 1.00 45.72 O HETATM 3695 O HOH A 747 17.712 -66.391 -0.558 1.00 54.45 O HETATM 3696 O HOH A 748 29.626 -16.037 -9.086 1.00 38.35 O HETATM 3697 O HOH A 749 24.616 -65.469 8.610 1.00 44.70 O HETATM 3698 O HOH A 750 14.322 -7.733 -29.435 1.00 46.11 O HETATM 3699 O HOH A 751 18.369 -7.916 6.722 1.00 50.77 O HETATM 3700 O HOH A 752 20.453 -74.186 7.708 1.00 57.33 O HETATM 3701 O HOH A 753 25.769 2.466 -3.604 1.00 55.62 O HETATM 3702 O HOH A 754 7.258 -24.464 13.902 1.00 49.49 O HETATM 3703 O HOH A 755 -2.359 -49.012 21.757 1.00 52.97 O HETATM 3704 O HOH A 756 14.537 -16.099 17.401 1.00 49.73 O HETATM 3705 O HOH A 757 44.157 -19.159 -13.313 1.00 46.63 O HETATM 3706 O HOH A 758 11.918 -48.722 6.088 1.00 48.24 O HETATM 3707 O HOH A 759 25.849 -52.048 14.576 1.00 43.81 O HETATM 3708 O HOH A 760 25.436 -18.379 -23.821 1.00 45.16 O HETATM 3709 O HOH A 761 -3.651 -65.853 17.573 1.00 40.73 O HETATM 3710 O HOH A 762 24.774 -61.951 4.327 1.00 57.22 O HETATM 3711 O HOH A 763 28.419 2.582 -28.614 1.00 48.49 O HETATM 3712 O HOH A 764 27.510 -53.720 17.232 1.00 50.64 O HETATM 3713 O HOH A 765 13.924 -73.132 4.790 1.00 49.92 O HETATM 3714 O HOH A 766 11.478 -9.197 -16.105 1.00 51.27 O HETATM 3715 O HOH A 767 40.598 -3.195 -1.734 1.00 48.60 O HETATM 3716 O HOH A 768 0.580 -70.152 2.603 1.00 51.62 O HETATM 3717 O HOH A 769 32.608 1.016 -6.554 1.00 50.04 O HETATM 3718 O HOH A 770 28.559 -24.594 22.633 1.00 53.95 O HETATM 3719 O HOH A 771 29.818 -7.442 -35.473 1.00 43.94 O HETATM 3720 O HOH A 772 33.272 -20.845 -23.215 1.00 53.83 O HETATM 3721 O HOH A 773 43.119 -38.282 9.776 1.00 43.29 O HETATM 3722 O HOH A 774 11.741 -76.685 4.531 1.00 56.26 O HETATM 3723 O HOH A 775 32.294 -17.857 13.838 1.00 42.58 O HETATM 3724 O HOH A 776 31.903 -2.702 2.942 1.00 56.47 O HETATM 3725 O HOH A 777 10.411 -20.297 11.469 1.00 50.11 O HETATM 3726 O HOH A 778 28.115 -32.175 23.917 1.00 56.59 O HETATM 3727 O HOH A 779 19.619 -42.504 25.389 1.00 47.78 O HETATM 3728 O HOH A 780 10.635 -14.003 8.143 1.00 54.62 O HETATM 3729 O HOH A 781 5.712 -72.890 0.578 1.00 50.33 O HETATM 3730 O HOH A 782 23.159 -71.668 14.887 1.00 52.08 O HETATM 3731 O HOH A 783 28.367 -60.663 6.203 1.00 54.24 O HETATM 3732 O HOH A 784 11.117 -42.787 27.021 1.00 48.97 O HETATM 3733 O HOH A 785 0.987 -67.153 -0.328 1.00 45.85 O HETATM 3734 O HOH A 786 46.567 -4.895 -5.373 1.00 55.38 O HETATM 3735 O HOH A 787 12.414 -12.393 -6.899 1.00 53.32 O HETATM 3736 O HOH A 788 -2.540 -69.671 4.505 1.00 49.52 O HETATM 3737 O HOH A 789 17.888 -38.788 2.247 1.00 51.89 O HETATM 3738 O HOH A 790 26.268 -60.093 25.899 1.00 57.99 O HETATM 3739 O HOH A 791 36.497 -5.379 4.792 1.00 53.45 O HETATM 3740 O HOH A 792 32.421 -46.749 3.379 1.00 48.79 O HETATM 3741 O HOH A 793 5.641 -46.107 27.707 1.00 57.16 O HETATM 3742 O HOH A 794 33.123 4.925 -25.201 1.00 50.49 O HETATM 3743 O HOH A 795 21.455 -42.795 6.547 1.00 43.04 O HETATM 3744 O HOH A 796 32.401 -19.454 -13.470 1.00 56.05 O HETATM 3745 O HOH A 797 -7.323 -56.981 0.207 1.00 55.41 O HETATM 3746 O HOH A 798 -4.769 -49.074 19.616 1.00 54.57 O HETATM 3747 O HOH A 799 -9.295 -53.230 13.870 1.00 56.47 O HETATM 3748 O HOH A 800 17.266 -16.241 16.885 1.00 49.88 O HETATM 3749 O HOH A 801 23.890 -58.529 6.646 1.00 49.73 O HETATM 3750 O HOH A 802 24.905 -24.960 -7.368 1.00 53.37 O HETATM 3751 O HOH A 803 25.254 -64.718 5.793 1.00 56.05 O HETATM 3752 O HOH A 804 10.018 -15.812 -10.373 1.00 54.61 O HETATM 3753 O HOH A 805 16.858 -12.071 16.532 1.00 54.41 O HETATM 3754 O HOH A 806 -1.002 -36.709 10.603 1.00 51.19 O HETATM 3755 O HOH A 807 41.190 -1.952 -11.864 1.00 53.45 O HETATM 3756 O HOH A 808 20.724 -2.085 -0.827 1.00 57.70 O HETATM 3757 O HOH A 809 42.040 -16.833 -21.580 1.00 44.16 O HETATM 3758 O HOH A 810 -4.226 -45.857 16.928 1.00 47.37 O HETATM 3759 O HOH A 811 19.914 -5.554 -1.572 1.00 54.82 O HETATM 3760 O HOH A 812 10.820 4.098 -37.114 1.00 55.87 O HETATM 3761 O HOH A 813 33.250 -6.735 4.532 1.00 56.31 O HETATM 3762 O HOH A 814 23.301 -68.505 2.504 1.00 54.82 O HETATM 3763 O HOH A 815 14.344 -12.799 10.134 1.00 45.48 O HETATM 3764 O HOH A 816 31.802 -32.417 22.094 1.00 58.05 O HETATM 3765 O HOH A 817 -3.925 -54.496 23.737 1.00 50.14 O HETATM 3766 O HOH A 818 30.926 -9.489 7.629 1.00 51.20 O HETATM 3767 O HOH A 819 36.847 -9.709 -28.928 1.00 53.90 O HETATM 3768 O HOH A 820 29.843 -22.231 -10.992 1.00 48.10 O HETATM 3769 O HOH A 821 4.339 -42.228 24.215 1.00 53.28 O HETATM 3770 O HOH A 822 10.309 -11.317 -20.787 1.00 46.84 O HETATM 3771 O HOH A 823 30.675 2.328 -30.650 1.00 52.59 O HETATM 3772 O HOH A 824 13.338 -5.170 -15.055 1.00 50.70 O HETATM 3773 O HOH A 825 5.616 -60.909 0.601 1.00 51.87 O HETATM 3774 O HOH A 826 14.977 -0.384 -22.583 1.00 50.77 O HETATM 3775 O HOH A 827 -3.758 -41.154 2.302 1.00 57.13 O HETATM 3776 O HOH A 828 11.384 -59.285 26.875 1.00 54.07 O HETATM 3777 O HOH A 829 14.423 -7.208 -11.382 1.00 52.62 O HETATM 3778 O HOH A 830 6.340 -26.133 8.769 1.00 49.62 O HETATM 3779 O HOH A 831 24.122 -70.636 12.313 1.00 51.61 O HETATM 3780 O HOH A 832 15.915 -29.399 24.135 1.00 53.95 O HETATM 3781 O HOH A 833 19.513 5.162 -28.911 1.00 50.91 O HETATM 3782 O HOH A 834 9.544 -16.865 -5.856 1.00 57.27 O HETATM 3783 O HOH A 835 13.100 -71.892 17.558 1.00 55.08 O HETATM 3784 O HOH A 836 26.725 -52.169 19.626 1.00 44.40 O HETATM 3785 O HOH A 837 19.377 -53.518 7.366 1.00 42.62 O HETATM 3786 O HOH A 838 -7.099 -53.413 22.736 1.00 48.41 O HETATM 3787 O HOH A 839 19.711 -29.432 -3.784 1.00 52.32 O HETATM 3788 O HOH A 840 31.962 -16.792 -19.825 1.00 46.43 O HETATM 3789 O HOH A 841 28.472 -16.144 -20.165 1.00 59.75 O HETATM 3790 O HOH A 842 19.613 -29.477 24.110 1.00 57.80 O HETATM 3791 O HOH A 843 15.064 -9.258 1.851 1.00 47.87 O HETATM 3792 O HOH A 844 3.839 -27.847 8.222 1.00 52.06 O HETATM 3793 O HOH A 845 41.292 -9.273 -0.522 1.00 50.86 O HETATM 3794 O HOH A 846 39.980 -38.834 15.282 1.00 57.30 O HETATM 3795 O HOH A 847 -6.640 -50.532 13.893 1.00 50.42 O HETATM 3796 O HOH A 848 23.681 -16.557 17.569 1.00 45.15 O HETATM 3797 O HOH A 849 6.794 -41.469 25.584 1.00 51.39 O HETATM 3798 O HOH A 850 13.660 -7.855 -6.366 1.00 50.92 O HETATM 3799 O HOH A 851 22.244 -56.076 9.085 1.00 61.46 O HETATM 3800 O HOH A 852 27.972 -46.535 6.224 1.00 51.69 O HETATM 3801 O HOH A 853 20.503 -70.489 5.305 1.00 50.76 O HETATM 3802 O HOH A 854 -9.625 -73.297 10.053 1.00 53.82 O HETATM 3803 O HOH A 855 14.928 -75.001 10.995 1.00 56.49 O HETATM 3804 O HOH A 856 0.677 -72.225 15.359 1.00 47.65 O HETATM 3805 O HOH A 857 -8.442 -45.088 12.055 1.00 55.53 O HETATM 3806 O HOH A 858 22.355 -44.383 25.565 1.00 53.64 O HETATM 3807 O HOH A 859 31.351 -65.381 22.397 1.00 48.69 O HETATM 3808 O HOH A 860 -7.656 -77.102 5.904 1.00 56.50 O HETATM 3809 O HOH A 861 -3.651 -53.494 28.650 1.00 52.96 O HETATM 3810 O HOH A 862 -0.437 -35.604 7.079 1.00 56.97 O HETATM 3811 O HOH A 863 -10.891 -51.778 29.405 1.00 56.03 O HETATM 3812 O HOH A 864 32.188 -20.455 15.838 1.00 57.15 O HETATM 3813 O HOH A 865 33.170 -19.234 -20.633 1.00 54.27 O HETATM 3814 O HOH A 866 27.716 -26.112 -9.156 1.00 48.47 O HETATM 3815 O HOH A 867 30.842 -23.062 24.518 1.00 51.56 O HETATM 3816 O HOH A 868 42.423 -6.222 -0.836 1.00 53.31 O HETATM 3817 O HOH A 869 24.380 -58.180 29.278 1.00 54.47 O HETATM 3818 O HOH A 870 10.689 5.979 -28.256 1.00 54.45 O HETATM 3819 O HOH A 871 27.684 -16.388 16.091 1.00 50.50 O HETATM 3820 O HOH A 872 21.114 0.747 -9.726 1.00 49.18 O HETATM 3821 O HOH A 873 24.779 -9.402 10.749 1.00 53.91 O HETATM 3822 O HOH B 66 6.146 -34.999 5.339 1.00 24.83 O HETATM 3823 O HOH B 74 3.053 -43.959 0.842 1.00 30.67 O HETATM 3824 O HOH B 94 -5.623 -45.669 2.532 1.00 38.71 O HETATM 3825 O HOH B 97 15.697 -26.880 -11.293 1.00 44.87 O HETATM 3826 O HOH B 99 2.122 -46.221 -0.561 1.00 34.62 O HETATM 3827 O HOH B 116 11.139 -27.054 -11.331 1.00 39.41 O HETATM 3828 O HOH B 121 3.841 -48.569 0.639 1.00 28.49 O HETATM 3829 O HOH B 133 23.978 -21.292 -11.281 1.00 40.16 O HETATM 3830 O HOH B 142 15.947 -16.785 -15.104 1.00 32.37 O HETATM 3831 O HOH B 176 5.230 -51.097 1.698 1.00 54.26 O HETATM 3832 O HOH B 179 5.042 -43.831 3.021 1.00 31.58 O HETATM 3833 O HOH B 182 7.458 -45.351 2.596 1.00 45.41 O HETATM 3834 O HOH B 189 16.094 -33.957 5.991 1.00 49.75 O HETATM 3835 O HOH B 198 20.075 -14.064 -19.338 1.00 39.10 O HETATM 3836 O HOH B 221 9.443 -27.023 -6.718 1.00 50.93 O HETATM 3837 O HOH B 227 10.100 -39.157 -0.463 1.00 51.99 O HETATM 3838 O HOH B 228 2.170 -36.013 3.613 1.00 42.13 O HETATM 3839 O HOH B 232 12.260 -19.018 -12.893 1.00 47.07 O HETATM 3840 O HOH B 233 11.258 -31.940 3.883 1.00 36.35 O HETATM 3841 O HOH B 236 -3.618 -49.981 -3.755 1.00 36.03 O HETATM 3842 O HOH B 238 11.161 -44.310 4.880 1.00 43.67 O HETATM 3843 O HOH B 279 23.116 -17.950 -19.907 1.00 41.72 O HETATM 3844 O HOH B 298 -5.326 -48.904 6.100 1.00 33.70 O HETATM 3845 O HOH B 317 11.137 -25.213 -3.749 1.00 40.87 O HETATM 3846 O HOH B 322 0.132 -37.887 3.745 1.00 37.22 O HETATM 3847 O HOH B 341 10.102 -32.535 -4.145 1.00 49.13 O HETATM 3848 O HOH B 342 12.201 -40.073 0.984 1.00 53.25 O HETATM 3849 O HOH B 347 18.231 -29.408 -8.675 1.00 55.93 O HETATM 3850 O HOH B 396 21.350 -16.758 -22.050 1.00 42.04 O HETATM 3851 O HOH B 406 6.300 -47.528 -0.466 1.00 52.02 O HETATM 3852 O HOH B 410 9.187 -35.596 -2.043 1.00 41.40 O HETATM 3853 O HOH B 413 3.750 -41.713 6.199 1.00 46.39 O HETATM 3854 O HOH B 421 10.983 -30.686 -7.230 1.00 52.94 O HETATM 3855 O HOH B 422 0.109 -51.183 -0.977 1.00 40.44 O HETATM 3856 O HOH B 426 24.771 -20.770 -14.243 1.00 56.13 O HETATM 3857 O HOH B 436 12.355 -20.825 -19.563 1.00 56.61 O HETATM 3858 O HOH B 443 11.051 -29.451 -13.147 1.00 45.10 O HETATM 3859 O HOH B 504 17.681 -32.382 -1.540 1.00 44.62 O HETATM 3860 O HOH B 520 -0.662 -50.125 -3.436 1.00 56.36 O HETATM 3861 O HOH B 522 21.219 -27.481 -6.551 1.00 52.51 O HETATM 3862 O HOH B 527 6.761 -42.100 1.208 1.00 48.89 O HETATM 3863 O HOH B 543 9.546 -23.565 -10.961 1.00 47.95 O HETATM 3864 O HOH B 555 12.405 -16.106 -18.509 1.00 52.81 O MASTER 430 0 0 29 2 0 0 6 3862 2 0 33 END
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Entry Information
PDB ID
3k64
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
Fem-3 mRNA-binding factor 2
Ligand Name
9-mer
EC.Number
E.C.-.-.-.-
Resolution
2(Å)
Affinity (Kd/Ki/IC50)
Kd=52.9nM
Release Year
2009
Protein/NA Sequence
Check fasta file
Primary Reference
(2009) Proc.Natl.Acad.Sci.USA Vol. 106: pp. 20186-20191
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q09312
Entrez Gene ID
No matched NCBI Entrez Gene ID found!
ASD
Information of known allosteric effects of PDB entries
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