Browse entries in the PDBbind-CN Database
HEADER RNA/RNA BINDING PROTEIN 08-OCT-09 3K5Z TITLE CRYSTAL STRUCTURE OF FBF-2/GLD-1 FBEA G4A MUTANT 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*AP*CP*CP*AP*UP*A)-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 3 22-DEC-09 3K5Z 1 JRNL REVDAT 2 10-NOV-09 3K5Z 1 AUTHOR REVDAT 1 03-NOV-09 3K5Z 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. 2.40 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) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.02 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 21281 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.160 REMARK 3 FREE R VALUE : 0.231 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1097 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) : 33.88 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 : 0.006 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): 14.1453 19.8799 -28.6650 REMARK 3 T TENSOR REMARK 3 T11: 0.6243 T22: 0.5259 REMARK 3 T33: 0.5678 T12: 0.0193 REMARK 3 T13: -0.3742 T23: 0.1413 REMARK 3 L TENSOR REMARK 3 L11: 3.4835 L22: -0.3452 REMARK 3 L33: 3.2794 L12: 0.3756 REMARK 3 L13: -2.3248 L23: 0.6220 REMARK 3 S TENSOR REMARK 3 S11: 0.7523 S12: 1.1816 S13: -0.2443 REMARK 3 S21: -1.2252 S22: -0.0403 S23: 1.0988 REMARK 3 S31: -0.1195 S32: -0.8022 S33: 0.6870 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN A AND RESID 194:229 REMARK 3 ORIGIN FOR THE GROUP (A): 21.3809 20.7845 -20.2711 REMARK 3 T TENSOR REMARK 3 T11: 0.2909 T22: 0.2713 REMARK 3 T33: 0.3955 T12: 0.0323 REMARK 3 T13: -0.0419 T23: 0.0873 REMARK 3 L TENSOR REMARK 3 L11: 0.9448 L22: 0.4268 REMARK 3 L33: 0.7692 L12: -0.2139 REMARK 3 L13: 0.0814 L23: -0.8931 REMARK 3 S TENSOR REMARK 3 S11: 0.1183 S12: -0.0566 S13: -0.0104 REMARK 3 S21: -0.4704 S22: 0.2423 S23: 0.5223 REMARK 3 S31: -0.0241 S32: -0.3473 S33: -0.0001 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN A AND RESID 230:276 REMARK 3 ORIGIN FOR THE GROUP (A): 23.1716 21.9170 -8.3540 REMARK 3 T TENSOR REMARK 3 T11: 0.2459 T22: 0.2361 REMARK 3 T33: 0.2697 T12: 0.0360 REMARK 3 T13: 0.0565 T23: 0.0680 REMARK 3 L TENSOR REMARK 3 L11: -0.4071 L22: 0.2845 REMARK 3 L33: 2.2830 L12: -0.9154 REMARK 3 L13: 1.0577 L23: -1.6679 REMARK 3 S TENSOR REMARK 3 S11: 0.0252 S12: -0.2478 S13: -0.0934 REMARK 3 S21: 0.0829 S22: 0.2954 S23: 0.3824 REMARK 3 S31: -0.3078 S32: -0.1395 S33: 0.0032 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN A AND RESID 277:313 REMARK 3 ORIGIN FOR THE GROUP (A): 27.1709 15.2512 0.8798 REMARK 3 T TENSOR REMARK 3 T11: 0.3038 T22: 0.1886 REMARK 3 T33: 0.2227 T12: 0.0329 REMARK 3 T13: 0.0611 T23: 0.0714 REMARK 3 L TENSOR REMARK 3 L11: -0.0904 L22: 0.9122 REMARK 3 L33: 0.3679 L12: -0.6301 REMARK 3 L13: 1.7081 L23: -0.3923 REMARK 3 S TENSOR REMARK 3 S11: -0.0672 S12: 0.1063 S13: 0.0841 REMARK 3 S21: 0.1039 S22: 0.5798 S23: 0.3631 REMARK 3 S31: -0.3202 S32: -0.1456 S33: 0.0483 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN A AND RESID 314:349 REMARK 3 ORIGIN FOR THE GROUP (A): 31.6791 9.4937 7.9492 REMARK 3 T TENSOR REMARK 3 T11: 0.1936 T22: 0.0857 REMARK 3 T33: 0.1248 T12: 0.0120 REMARK 3 T13: 0.0029 T23: 0.0295 REMARK 3 L TENSOR REMARK 3 L11: 0.1504 L22: 0.6992 REMARK 3 L33: 1.2616 L12: -0.5108 REMARK 3 L13: 0.6739 L23: 0.1351 REMARK 3 S TENSOR REMARK 3 S11: 0.0315 S12: 0.0340 S13: 0.0875 REMARK 3 S21: 0.1947 S22: 0.3131 S23: 0.2742 REMARK 3 S31: -0.1276 S32: 0.1574 S33: 0.0507 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN A AND RESID 350:404 REMARK 3 ORIGIN FOR THE GROUP (A): 40.3210 5.6993 12.8858 REMARK 3 T TENSOR REMARK 3 T11: 0.3136 T22: 0.1413 REMARK 3 T33: 0.1887 T12: -0.0226 REMARK 3 T13: -0.0241 T23: -0.0210 REMARK 3 L TENSOR REMARK 3 L11: 0.5868 L22: 1.4416 REMARK 3 L33: 0.2882 L12: -0.4149 REMARK 3 L13: 0.5666 L23: -1.4441 REMARK 3 S TENSOR REMARK 3 S11: 0.1340 S12: 0.1046 S13: -0.1039 REMARK 3 S21: 0.4407 S22: 0.1426 S23: 0.0274 REMARK 3 S31: -0.0303 S32: 0.0461 S33: 0.0039 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN A AND RESID 405:441 REMARK 3 ORIGIN FOR THE GROUP (A): 44.4317 -6.3156 16.1574 REMARK 3 T TENSOR REMARK 3 T11: 0.3173 T22: 0.1533 REMARK 3 T33: 0.2615 T12: 0.0213 REMARK 3 T13: -0.0676 T23: -0.0177 REMARK 3 L TENSOR REMARK 3 L11: 0.2062 L22: 1.1686 REMARK 3 L33: -0.7435 L12: -1.7785 REMARK 3 L13: 1.1655 L23: -0.0491 REMARK 3 S TENSOR REMARK 3 S11: -0.1635 S12: -0.0635 S13: 0.2358 REMARK 3 S21: 0.2447 S22: 0.3254 S23: 0.2025 REMARK 3 S31: -0.0230 S32: 0.0431 S33: 0.0028 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN A AND RESID 442:487 REMARK 3 ORIGIN FOR THE GROUP (A): 49.1835 -19.5177 19.6426 REMARK 3 T TENSOR REMARK 3 T11: 0.2788 T22: 0.1955 REMARK 3 T33: 0.1750 T12: 0.0293 REMARK 3 T13: -0.0896 T23: -0.0125 REMARK 3 L TENSOR REMARK 3 L11: 1.2991 L22: 2.2451 REMARK 3 L33: -0.8813 L12: -0.9376 REMARK 3 L13: 0.2940 L23: 0.8471 REMARK 3 S TENSOR REMARK 3 S11: -0.0408 S12: -0.3153 S13: -0.0083 REMARK 3 S21: 0.3332 S22: 0.1711 S23: 0.0912 REMARK 3 S31: 0.0265 S32: -0.0153 S33: -0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN A AND RESID 488:545 REMARK 3 ORIGIN FOR THE GROUP (A): 58.3575 -22.0173 13.6518 REMARK 3 T TENSOR REMARK 3 T11: 0.2373 T22: 0.1960 REMARK 3 T33: 0.1782 T12: -0.0182 REMARK 3 T13: 0.0078 T23: -0.0001 REMARK 3 L TENSOR REMARK 3 L11: 1.7405 L22: 1.0245 REMARK 3 L33: 0.2624 L12: -1.0289 REMARK 3 L13: 1.1400 L23: 0.1694 REMARK 3 S TENSOR REMARK 3 S11: -0.0761 S12: -0.1346 S13: 0.0477 REMARK 3 S21: -0.3295 S22: -0.0648 S23: -0.0524 REMARK 3 S31: -0.0058 S32: 0.1809 S33: -0.0034 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN A AND RESID 546:567 REMARK 3 ORIGIN FOR THE GROUP (A): 55.8974 -32.3174 5.5032 REMARK 3 T TENSOR REMARK 3 T11: 0.3737 T22: 0.3009 REMARK 3 T33: 0.1479 T12: 0.0151 REMARK 3 T13: 0.0919 T23: 0.0074 REMARK 3 L TENSOR REMARK 3 L11: 0.5340 L22: 0.0741 REMARK 3 L33: -0.0817 L12: 0.2765 REMARK 3 L13: 0.3921 L23: 0.3531 REMARK 3 S TENSOR REMARK 3 S11: -0.1617 S12: 0.5630 S13: -0.5487 REMARK 3 S21: -0.9131 S22: 0.1020 S23: -0.2256 REMARK 3 S31: 0.2613 S32: 0.3924 S33: -0.0003 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): 34.0757 -7.8867 -2.8656 REMARK 3 T TENSOR REMARK 3 T11: 0.5145 T22: 0.2682 REMARK 3 T33: 0.3451 T12: 0.0154 REMARK 3 T13: -0.2014 T23: 0.0180 REMARK 3 L TENSOR REMARK 3 L11: -0.4699 L22: 0.2497 REMARK 3 L33: -0.4187 L12: -0.5833 REMARK 3 L13: -0.2175 L23: 0.1468 REMARK 3 S TENSOR REMARK 3 S11: 0.1219 S12: 0.1719 S13: -0.1298 REMARK 3 S21: -0.3705 S22: -0.0812 S23: 0.0061 REMARK 3 S31: 0.1502 S32: 0.1806 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 3K5Z 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 RCSB055588. 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 : 21281 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 28.015 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 8.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.12800 REMARK 200
FOR THE DATA SET : 18.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4 REMARK 200 DATA REDUNDANCY IN SHELL : 8.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.89500 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 (%): 55.71 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78 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 33.90100 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 67.80200 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 50.85150 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 84.75250 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 16.95050 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: 2610 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19510 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 ASP A 174 REMARK 465 SER A 175 REMARK 465 ASN A 176 REMARK 465 GLY A 177 REMARK 465 GLU A 178 REMARK 465 MET A 179 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: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 G B 2 P G B 2 O5' -0.071 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 G B 2 N1 - C6 - O6 ANGL. DEV. = 4.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 258 42.15 -83.23 REMARK 500 ASP A 312 -153.07 -137.32 REMARK 500 ARG A 441 -4.43 75.21 REMARK 500 ASP A 477 23.41 -160.35 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 88 DISTANCE = 5.13 ANGSTROMS REMARK 525 HOH A 616 DISTANCE = 6.23 ANGSTROMS REMARK 525 HOH A 619 DISTANCE = 6.24 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: 3K61 RELATED DB: PDB REMARK 900 RELATED ID: 3K62 RELATED DB: PDB REMARK 900 RELATED ID: 3K64 RELATED DB: PDB DBREF 3K5Z A 164 575 UNP Q09312 FBF2_CAEEL 164 575 DBREF 3K5Z B 1 9 PDB 3K5Z 3K5Z 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 A C C A U A FORMUL 3 HOH *193(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 LYS A 212 1 13 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 SER A 275 1 15 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 ASP A 321 1 10 HELIX 13 13 ALA A 324 ILE A 335 1 12 HELIX 14 14 PRO A 336 ASN A 339 5 4 HELIX 15 15 TRP A 340 THR A 349 1 10 HELIX 16 16 THR A 349 SER A 358 1 10 HELIX 17 17 TYR A 361 LEU A 373 1 13 HELIX 18 18 ASP A 376 VAL A 380 5 5 HELIX 19 19 THR A 383 ARG A 404 1 22 HELIX 20 20 ARG A 404 ASN A 411 1 8 HELIX 21 21 ALA A 414 ASN A 424 1 11 HELIX 22 22 LEU A 427 CYS A 438 1 12 HELIX 23 23 ASN A 442 SER A 447 1 6 HELIX 24 24 PHE A 451 ALA A 463 1 13 HELIX 25 25 PRO A 464 GLY A 478 1 15 HELIX 26 26 ASP A 488 PHE A 495 1 8 HELIX 27 27 PHE A 498 SER A 515 1 18 HELIX 28 28 HIS A 527 GLU A 545 1 19 HELIX 29 29 GLU A 545 SER A 550 1 6 HELIX 30 30 PHE A 552 SER A 567 1 16 CRYST1 97.048 97.048 101.703 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 0.010304 0.005949 0.000000 0.00000 SCALE2 0.000000 0.011898 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009833 0.00000 ATOM 1 N LEU A 168 9.122 12.061 -23.826 1.00 64.30 N ANISOU 1 N LEU A 168 6652 6901 10880 -1664 -5448 643 N ATOM 2 CA LEU A 168 9.723 13.132 -24.620 1.00 69.43 C ANISOU 2 CA LEU A 168 7546 7718 11118 -1377 -5307 733 C ATOM 3 C LEU A 168 8.669 13.993 -25.304 1.00 75.27 C ANISOU 3 C LEU A 168 8143 8739 11717 -1212 -5508 888 C ATOM 4 O LEU A 168 7.693 13.467 -25.839 1.00 81.48 O ANISOU 4 O LEU A 168 8764 9669 12525 -1290 -5889 767 O ATOM 5 CB LEU A 168 10.658 12.563 -25.690 1.00 73.12 C ANISOU 5 CB LEU A 168 8371 8175 11235 -1301 -5395 455 C ATOM 6 CG LEU A 168 12.053 12.066 -25.299 1.00 66.49 C ANISOU 6 CG LEU A 168 7780 7125 10358 -1327 -5115 337 C ATOM 7 CD1 LEU A 168 12.845 11.690 -26.547 1.00 67.71 C ANISOU 7 CD1 LEU A 168 8281 7330 10116 -1214 -5234 69 C ATOM 8 CD2 LEU A 168 12.811 13.095 -24.474 1.00 56.39 C ANISOU 8 CD2 LEU A 168 6531 5844 9050 -1229 -4652 577 C ATOM 9 N PRO A 169 8.872 15.324 -25.301 1.00 68.43 N ANISOU 9 N PRO A 169 7338 7965 10696 -979 -5232 1154 N ATOM 10 CA PRO A 169 7.957 16.274 -25.949 1.00 67.03 C ANISOU 10 CA PRO A 169 7049 8053 10365 -753 -5360 1365 C ATOM 11 C PRO A 169 7.793 15.959 -27.427 1.00 67.29 C ANISOU 11 C PRO A 169 7219 8334 10012 -626 -5723 1191 C ATOM 12 O PRO A 169 8.753 15.563 -28.084 1.00 66.71 O ANISOU 12 O PRO A 169 7453 8222 9672 -601 -5717 983 O ATOM 13 CB PRO A 169 8.671 17.624 -25.773 1.00 65.02 C ANISOU 13 CB PRO A 169 6977 7762 9964 -526 -4899 1620 C ATOM 14 CG PRO A 169 10.099 17.258 -25.437 1.00 63.07 C ANISOU 14 CG PRO A 169 7005 7312 9648 -619 -4613 1453 C ATOM 15 CD PRO A 169 9.962 16.027 -24.610 1.00 60.39 C ANISOU 15 CD PRO A 169 6481 6810 9657 -922 -4743 1281 C ATOM 16 N THR A 170 6.585 16.137 -27.945 1.00 70.13 N ANISOU 16 N THR A 170 7335 8985 10328 -548 -6033 1272 N ATOM 17 CA THR A 170 6.312 15.732 -29.310 1.00 79.24 C ANISOU 17 CA THR A 170 8544 10445 11118 -470 -6409 1079 C ATOM 18 C THR A 170 7.122 16.547 -30.320 1.00 79.06 C ANISOU 18 C THR A 170 8857 10553 10627 -153 -6271 1174 C ATOM 19 O THR A 170 7.627 15.990 -31.298 1.00 82.22 O ANISOU 19 O THR A 170 9462 11061 10719 -153 -6450 913 O ATOM 20 CB THR A 170 4.801 15.763 -29.631 1.00 87.42 C ANISOU 20 CB THR A 170 9197 11844 12174 -452 -6770 1148 C ATOM 21 OG1 THR A 170 4.545 14.961 -30.787 1.00 93.36 O ANISOU 21 OG1 THR A 170 9949 12886 12638 -514 -7164 837 O ATOM 22 CG2 THR A 170 4.316 17.188 -29.880 1.00 89.33 C ANISOU 22 CG2 THR A 170 9368 12321 12252 -78 -6647 1567 C ATOM 23 N TRP A 171 7.268 17.849 -30.072 1.00 73.34 N ANISOU 23 N TRP A 171 8198 9806 9862 103 -5932 1533 N ATOM 24 CA TRP A 171 8.034 18.726 -30.964 1.00 73.77 C ANISOU 24 CA TRP A 171 8585 9956 9489 408 -5744 1660 C ATOM 25 C TRP A 171 9.450 18.210 -31.208 1.00 75.22 C ANISOU 25 C TRP A 171 9140 9955 9485 315 -5608 1382 C ATOM 26 O TRP A 171 10.112 18.605 -32.171 1.00 76.65 O ANISOU 26 O TRP A 171 9607 10259 9255 513 -5561 1375 O ATOM 27 CB TRP A 171 8.097 20.162 -30.423 1.00 70.02 C ANISOU 27 CB TRP A 171 8150 9371 9085 639 -5292 2065 C ATOM 28 CG TRP A 171 8.872 20.310 -29.140 1.00 68.62 C ANISOU 28 CG TRP A 171 8039 8820 9215 457 -4851 2068 C ATOM 29 CD1 TRP A 171 8.353 20.468 -27.886 1.00 69.86 C ANISOU 29 CD1 TRP A 171 7916 8818 9807 310 -4689 2197 C ATOM 30 CD2 TRP A 171 10.301 20.313 -28.984 1.00 68.57 C ANISOU 30 CD2 TRP A 171 8371 8605 9078 398 -4515 1926 C ATOM 31 NE1 TRP A 171 9.366 20.563 -26.962 1.00 69.83 N ANISOU 31 NE1 TRP A 171 8044 8542 9946 158 -4273 2145 N ATOM 32 CE2 TRP A 171 10.570 20.467 -27.608 1.00 66.17 C ANISOU 32 CE2 TRP A 171 7955 8050 9135 211 -4159 1978 C ATOM 33 CE3 TRP A 171 11.376 20.198 -29.872 1.00 66.97 C ANISOU 33 CE3 TRP A 171 8537 8436 8473 478 -4482 1751 C ATOM 34 CZ2 TRP A 171 11.869 20.508 -27.100 1.00 58.86 C ANISOU 34 CZ2 TRP A 171 7260 6940 8162 109 -3771 1862 C ATOM 35 CZ3 TRP A 171 12.658 20.238 -29.369 1.00 62.88 C ANISOU 35 CZ3 TRP A 171 8262 7710 7920 380 -4103 1635 C ATOM 36 CH2 TRP A 171 12.896 20.393 -27.994 1.00 58.87 C ANISOU 36 CH2 TRP A 171 7623 6985 7761 200 -3749 1691 C ATOM 37 N SER A 172 9.908 17.324 -30.331 1.00 70.76 N ANISOU 37 N SER A 172 8562 9109 9215 26 -5541 1164 N ATOM 38 CA SER A 172 11.268 16.830 -30.386 1.00 71.15 C ANISOU 38 CA SER A 172 8935 8972 9125 -55 -5373 920 C ATOM 39 C SER A 172 11.342 15.409 -30.910 1.00 85.34 C ANISOU 39 C SER A 172 10757 10775 10894 -254 -5731 521 C ATOM 40 O SER A 172 12.437 14.918 -31.184 1.00 85.33 O ANISOU 40 O SER A 172 11034 10663 10725 -290 -5649 289 O ATOM 41 CB SER A 172 11.879 16.847 -28.992 1.00 63.84 C ANISOU 41 CB SER A 172 7990 7737 8529 -214 -4984 971 C ATOM 42 OG SER A 172 11.529 15.672 -28.281 1.00 53.56 O ANISOU 42 OG SER A 172 6479 6281 7589 -496 -5160 793 O ATOM 43 N LEU A 173 10.196 14.737 -31.018 1.00 98.34 N ANISOU 43 N LEU A 173 12109 12544 12712 -397 -6102 424 N ATOM 44 CA LEU A 173 10.186 13.348 -31.484 1.00106.04 C ANISOU 44 CA LEU A 173 13092 13497 13699 -626 -6414 14 C ATOM 45 C LEU A 173 10.707 13.268 -32.910 1.00109.21 C ANISOU 45 C LEU A 173 13745 14139 13611 -493 -6581 -193 C ATOM 46 O LEU A 173 9.991 13.220 -33.915 1.00106.53 O ANISOU 46 O LEU A 173 13290 14159 13027 -441 -6909 -272 O ATOM 47 CB LEU A 173 8.819 12.692 -31.316 1.00109.44 C ANISOU 47 CB LEU A 173 13147 14035 14399 -835 -6751 -69 C ATOM 48 CG LEU A 173 8.672 12.098 -29.913 1.00106.27 C ANISOU 48 CG LEU A 173 12581 13281 14517 -1093 -6612 -57 C ATOM 49 CD1 LEU A 173 7.675 10.950 -29.915 1.00111.75 C ANISOU 49 CD1 LEU A 173 13016 13994 15450 -1393 -6952 -321 C ATOM 50 CD2 LEU A 173 10.027 11.628 -29.399 1.00 97.86 C ANISOU 50 CD2 LEU A 173 11800 11864 13520 -1152 -6315 -171 C ATOM 51 N ARG A 180 14.475 13.402 -32.972 1.00 85.39 N ANISOU 51 N ARG A 180 11662 10674 10108 -326 -5829 -428 N ATOM 52 CA ARG A 180 15.163 13.729 -34.206 1.00 96.19 C ANISOU 52 CA ARG A 180 13316 12259 10971 -148 -5869 -537 C ATOM 53 C ARG A 180 16.657 13.663 -33.993 1.00 97.20 C ANISOU 53 C ARG A 180 13769 12204 10961 -130 -5547 -659 C ATOM 54 O ARG A 180 17.116 13.413 -32.887 1.00 92.60 O ANISOU 54 O ARG A 180 13165 11358 10659 -236 -5291 -634 O ATOM 55 CB ARG A 180 14.776 15.150 -34.643 1.00 98.30 C ANISOU 55 CB ARG A 180 13584 12780 10987 126 -5781 -175 C ATOM 56 CG ARG A 180 13.316 15.311 -35.067 1.00103.00 C ANISOU 56 CG ARG A 180 13859 13662 11613 174 -6120 -37 C ATOM 57 CD ARG A 180 12.710 16.641 -34.600 1.00102.90 C ANISOU 57 CD ARG A 180 13717 13700 11680 383 -5900 429 C ATOM 58 NE ARG A 180 13.586 17.787 -34.838 1.00103.46 N ANISOU 58 NE ARG A 180 14093 13761 11458 625 -5529 641 N ATOM 59 CZ ARG A 180 13.339 19.020 -34.401 1.00103.17 C ANISOU 59 CZ ARG A 180 14030 13688 11483 812 -5217 1032 C ATOM 60 NH1 ARG A 180 12.237 19.268 -33.705 1.00104.69 N ANISOU 60 NH1 ARG A 180 13893 13869 12015 800 -5254 1259 N ATOM 61 NH2 ARG A 180 14.193 20.007 -34.657 1.00 98.64 N ANISOU 61 NH2 ARG A 180 13762 13080 10636 1002 -4849 1186 N ATOM 62 N SER A 181 17.410 13.869 -35.069 1.00107.41 N ANISOU 62 N SER A 181 15343 13672 11797 6 -5567 -796 N ATOM 63 CA SER A 181 18.841 14.111 -34.976 1.00110.86 C ANISOU 63 CA SER A 181 16099 14015 12007 71 -5227 -867 C ATOM 64 C SER A 181 19.014 15.588 -35.263 1.00112.89 C ANISOU 64 C SER A 181 16490 14434 11969 300 -4973 -559 C ATOM 65 O SER A 181 18.034 16.276 -35.553 1.00115.10 O ANISOU 65 O SER A 181 16615 14877 12240 419 -5086 -303 O ATOM 66 CB SER A 181 19.607 13.290 -36.010 1.00115.07 C ANISOU 66 CB SER A 181 16869 14628 12224 51 -5414 -1261 C ATOM 67 OG SER A 181 19.178 11.941 -36.013 1.00118.43 O ANISOU 67 OG SER A 181 17156 14932 12909 -153 -5705 -1554 O ATOM 68 N ARG A 182 20.246 16.078 -35.193 1.00110.29 N ANISOU 68 N ARG A 182 16446 14067 11394 368 -4616 -580 N ATOM 69 CA ARG A 182 20.501 17.489 -35.459 1.00110.89 C ANISOU 69 CA ARG A 182 16688 14255 11190 567 -4312 -306 C ATOM 70 C ARG A 182 19.594 18.366 -34.587 1.00102.20 C ANISOU 70 C ARG A 182 15348 13071 10414 604 -4122 80 C ATOM 71 O ARG A 182 18.881 19.246 -35.081 1.00101.41 O ANISOU 71 O ARG A 182 15209 13113 10207 789 -4152 354 O ATOM 72 CB ARG A 182 20.286 17.802 -36.945 1.00118.75 C ANISOU 72 CB ARG A 182 17817 15553 11750 750 -4575 -310 C ATOM 73 CG ARG A 182 20.703 19.206 -37.359 1.00122.51 C ANISOU 73 CG ARG A 182 18532 16129 11887 972 -4237 -43 C ATOM 74 CD ARG A 182 19.785 19.752 -38.438 1.00129.53 C ANISOU 74 CD ARG A 182 19361 17310 12544 1194 -4501 177 C ATOM 75 NE ARG A 182 19.778 21.212 -38.465 1.00132.74 N ANISOU 75 NE ARG A 182 19899 17721 12816 1420 -4122 572 N ATOM 76 CZ ARG A 182 18.816 21.946 -39.019 1.00137.53 C ANISOU 76 CZ ARG A 182 20396 18519 13339 1658 -4227 912 C ATOM 77 NH1 ARG A 182 17.774 21.356 -39.591 1.00140.92 N ANISOU 77 NH1 ARG A 182 20556 19208 13780 1684 -4718 889 N ATOM 78 NH2 ARG A 182 18.892 23.270 -38.997 1.00136.84 N ANISOU 78 NH2 ARG A 182 20462 18378 13154 1870 -3821 1274 N ATOM 79 N LEU A 183 19.613 18.103 -33.286 1.00 92.21 N ANISOU 79 N LEU A 183 13907 11585 9541 436 -3926 105 N ATOM 80 CA LEU A 183 18.838 18.893 -32.343 1.00 81.88 C ANISOU 80 CA LEU A 183 12361 10185 8565 438 -3712 435 C ATOM 81 C LEU A 183 19.786 19.783 -31.555 1.00 70.87 C ANISOU 81 C LEU A 183 11106 8688 7132 424 -3132 530 C ATOM 82 O LEU A 183 20.889 19.361 -31.210 1.00 72.90 O ANISOU 82 O LEU A 183 11500 8899 7299 317 -2941 312 O ATOM 83 CB LEU A 183 18.079 17.978 -31.389 1.00 76.99 C ANISOU 83 CB LEU A 183 11398 9423 8432 230 -3903 400 C ATOM 84 CG LEU A 183 16.873 18.618 -30.709 1.00 73.62 C ANISOU 84 CG LEU A 183 10657 8968 8347 243 -3871 722 C ATOM 85 CD1 LEU A 183 15.637 18.469 -31.574 1.00 72.81 C ANISOU 85 CD1 LEU A 183 10390 9058 8217 341 -4331 785 C ATOM 86 CD2 LEU A 183 16.648 17.980 -29.365 1.00 74.40 C ANISOU 86 CD2 LEU A 183 10480 8877 8911 5 -3810 704 C ATOM 87 N SER A 184 19.363 21.010 -31.268 1.00 59.60 N ANISOU 87 N SER A 184 9637 7240 5770 531 -2834 846 N ATOM 88 CA SER A 184 20.237 21.960 -30.579 1.00 54.91 C ANISOU 88 CA SER A 184 9179 6563 5119 497 -2237 915 C ATOM 89 C SER A 184 19.961 22.050 -29.082 1.00 46.44 C ANISOU 89 C SER A 184 7804 5350 4491 308 -1970 1014 C ATOM 90 O SER A 184 18.853 21.779 -28.612 1.00 46.11 O ANISOU 90 O SER A 184 7447 5256 4818 264 -2197 1149 O ATOM 91 CB SER A 184 20.138 23.353 -31.201 1.00 57.77 C ANISOU 91 CB SER A 184 9742 6961 5249 723 -1960 1179 C ATOM 92 OG SER A 184 19.075 24.099 -30.629 1.00 65.93 O ANISOU 92 OG SER A 184 10533 7904 6613 781 -1840 1505 O ATOM 93 N LEU A 185 20.985 22.436 -28.336 1.00 41.11 N ANISOU 93 N LEU A 185 7212 4649 3759 186 -1480 934 N ATOM 94 CA LEU A 185 20.852 22.565 -26.898 1.00 37.18 C ANISOU 94 CA LEU A 185 6419 4072 3635 -10 -1179 1006 C ATOM 95 C LEU A 185 19.947 23.748 -26.555 1.00 41.60 C ANISOU 95 C LEU A 185 6840 4545 4420 58 -937 1325 C ATOM 96 O LEU A 185 19.150 23.680 -25.613 1.00 42.87 O ANISOU 96 O LEU A 185 6659 4637 4991 -56 -948 1452 O ATOM 97 CB LEU A 185 22.223 22.732 -26.262 1.00 30.26 C ANISOU 97 CB LEU A 185 5656 3267 2575 -157 -695 819 C ATOM 98 CG LEU A 185 22.248 23.007 -24.766 1.00 29.54 C ANISOU 98 CG LEU A 185 5260 3165 2800 -375 -298 877 C ATOM 99 CD1 LEU A 185 21.697 21.806 -24.008 1.00 27.70 C ANISOU 99 CD1 LEU A 185 4687 2897 2940 -506 -641 857 C ATOM 100 CD2 LEU A 185 23.678 23.352 -24.306 1.00 25.94 C ANISOU 100 CD2 LEU A 185 4939 2862 2055 -504 229 678 C ATOM 101 N SER A 186 20.066 24.830 -27.322 1.00 41.10 N ANISOU 101 N SER A 186 7043 4480 4093 250 -708 1462 N ATOM 102 CA SER A 186 19.247 26.011 -27.068 1.00 46.92 C ANISOU 102 CA SER A 186 7686 5108 5033 354 -432 1782 C ATOM 103 C SER A 186 17.751 25.745 -27.277 1.00 49.63 C ANISOU 103 C SER A 186 7757 5450 5651 485 -908 2004 C ATOM 104 O SER A 186 16.924 26.278 -26.549 1.00 52.31 O ANISOU 104 O SER A 186 7841 5699 6336 470 -761 2219 O ATOM 105 CB SER A 186 19.731 27.212 -27.877 1.00 45.39 C ANISOU 105 CB SER A 186 7864 4888 4493 552 -53 1899 C ATOM 106 OG SER A 186 20.840 27.822 -27.239 1.00 40.13 O ANISOU 106 OG SER A 186 7337 4188 3722 372 563 1756 O ATOM 107 N GLU A 187 17.410 24.901 -28.246 1.00 47.42 N ANISOU 107 N GLU A 187 7511 5294 5212 593 -1466 1927 N ATOM 108 CA GLU A 187 16.029 24.453 -28.394 1.00 53.52 C ANISOU 108 CA GLU A 187 7984 6125 6227 662 -1952 2066 C ATOM 109 C GLU A 187 15.517 23.823 -27.107 1.00 49.68 C ANISOU 109 C GLU A 187 7115 5551 6211 404 -2012 2027 C ATOM 110 O GLU A 187 14.503 24.245 -26.547 1.00 41.93 O ANISOU 110 O GLU A 187 5853 4528 5551 419 -1994 2253 O ATOM 111 CB GLU A 187 15.914 23.424 -29.509 1.00 56.29 C ANISOU 111 CB GLU A 187 8406 6648 6332 724 -2524 1880 C ATOM 112 CG GLU A 187 15.631 24.005 -30.869 1.00 64.70 C ANISOU 112 CG GLU A 187 9666 7888 7030 1036 -2674 2041 C ATOM 113 CD GLU A 187 15.566 22.933 -31.937 1.00 73.59 C ANISOU 113 CD GLU A 187 10834 9223 7905 1050 -3227 1803 C ATOM 114 OE1 GLU A 187 16.492 22.092 -31.980 1.00 68.18 O ANISOU 114 OE1 GLU A 187 10295 8508 7101 885 -3283 1474 O ATOM 115 OE2 GLU A 187 14.593 22.929 -32.727 1.00 84.62 O ANISOU 115 OE2 GLU A 187 12102 10833 9215 1224 -3594 1935 O ATOM 116 N VAL A 188 16.218 22.791 -26.656 1.00 38.99 N ANISOU 116 N VAL A 188 5746 4177 4890 181 -2087 1748 N ATOM 117 CA VAL A 188 15.832 22.098 -25.438 1.00 37.03 C ANISOU 117 CA VAL A 188 5149 3854 5066 -68 -2139 1709 C ATOM 118 C VAL A 188 15.750 23.087 -24.265 1.00 43.87 C ANISOU 118 C VAL A 188 5835 4638 6196 -161 -1629 1891 C ATOM 119 O VAL A 188 14.807 23.045 -23.479 1.00 51.71 O ANISOU 119 O VAL A 188 6484 5590 7573 -257 -1700 2023 O ATOM 120 CB VAL A 188 16.810 20.934 -25.119 1.00 40.16 C ANISOU 120 CB VAL A 188 5605 4239 5415 -257 -2195 1407 C ATOM 121 CG1 VAL A 188 16.441 20.244 -23.821 1.00 33.01 C ANISOU 121 CG1 VAL A 188 4339 3260 4944 -501 -2213 1404 C ATOM 122 CG2 VAL A 188 16.844 19.933 -26.265 1.00 40.14 C ANISOU 122 CG2 VAL A 188 5768 4295 5187 -185 -2684 1201 C ATOM 123 N LEU A 189 16.718 23.989 -24.155 1.00 36.63 N ANISOU 123 N LEU A 189 5142 3704 5069 -148 -1103 1880 N ATOM 124 CA LEU A 189 16.738 24.911 -23.023 1.00 41.85 C ANISOU 124 CA LEU A 189 5633 4299 5968 -278 -568 1997 C ATOM 125 C LEU A 189 15.593 25.922 -23.072 1.00 46.33 C ANISOU 125 C LEU A 189 6076 4784 6743 -112 -493 2312 C ATOM 126 O LEU A 189 15.009 26.260 -22.036 1.00 41.19 O ANISOU 126 O LEU A 189 5114 4077 6461 -243 -302 2427 O ATOM 127 CB LEU A 189 18.083 25.637 -22.933 1.00 39.56 C ANISOU 127 CB LEU A 189 5620 4032 5378 -331 10 1869 C ATOM 128 CG LEU A 189 19.255 24.770 -22.491 1.00 36.39 C ANISOU 128 CG LEU A 189 5248 3751 4828 -531 69 1575 C ATOM 129 CD1 LEU A 189 20.547 25.550 -22.598 1.00 32.35 C ANISOU 129 CD1 LEU A 189 5032 3310 3951 -561 616 1435 C ATOM 130 CD2 LEU A 189 19.035 24.272 -21.064 1.00 33.53 C ANISOU 130 CD2 LEU A 189 4470 3422 4848 -792 138 1560 C ATOM 131 N ASP A 190 15.288 26.400 -24.278 1.00 45.27 N ANISOU 131 N ASP A 190 6179 4662 6361 186 -637 2458 N ATOM 132 CA ASP A 190 14.247 27.406 -24.487 1.00 48.29 C ANISOU 132 CA ASP A 190 6483 4983 6882 417 -556 2793 C ATOM 133 C ASP A 190 12.829 26.833 -24.325 1.00 51.47 C ANISOU 133 C ASP A 190 6504 5452 7601 439 -1061 2921 C ATOM 134 O ASP A 190 11.896 27.572 -24.013 1.00 49.00 O ANISOU 134 O ASP A 190 5994 5089 7535 548 -949 3182 O ATOM 135 CB ASP A 190 14.384 28.031 -25.888 1.00 48.17 C ANISOU 135 CB ASP A 190 6833 5007 6461 757 -574 2931 C ATOM 136 CG ASP A 190 15.611 28.934 -26.023 1.00 56.63 C ANISOU 136 CG ASP A 190 8283 5980 7253 762 29 2874 C ATOM 137 OD1 ASP A 190 15.933 29.335 -27.164 1.00 61.03 O ANISOU 137 OD1 ASP A 190 9176 6577 7437 1005 29 2944 O ATOM 138 OD2 ASP A 190 16.258 29.247 -25.003 1.00 59.32 O ANISOU 138 OD2 ASP A 190 8578 6232 7729 512 512 2750 O ATOM 139 N SER A 191 12.680 25.521 -24.530 1.00 50.80 N ANISOU 139 N SER A 191 6317 5476 7509 327 -1590 2724 N ATOM 140 CA SER A 191 11.360 24.892 -24.668 1.00 53.31 C ANISOU 140 CA SER A 191 6322 5901 8031 358 -2127 2802 C ATOM 141 C SER A 191 10.639 24.660 -23.339 1.00 58.70 C ANISOU 141 C SER A 191 6583 6520 9201 117 -2109 2841 C ATOM 142 O SER A 191 9.419 24.460 -23.307 1.00 58.06 O ANISOU 142 O SER A 191 6209 6522 9330 153 -2446 2961 O ATOM 143 CB SER A 191 11.472 23.563 -25.422 1.00 46.50 C ANISOU 143 CB SER A 191 5523 5164 6982 301 -2668 2544 C ATOM 144 OG SER A 191 12.220 22.622 -24.676 1.00 45.57 O ANISOU 144 OG SER A 191 5376 4958 6979 7 -2640 2280 O ATOM 145 N GLY A 192 11.399 24.684 -22.249 1.00 54.43 N ANISOU 145 N GLY A 192 5996 5870 8816 -132 -1716 2731 N ATOM 146 CA GLY A 192 10.852 24.470 -20.922 1.00 48.47 C ANISOU 146 CA GLY A 192 4839 5075 8501 -385 -1654 2756 C ATOM 147 C GLY A 192 10.759 22.994 -20.594 1.00 52.96 C ANISOU 147 C GLY A 192 5236 5679 9208 -616 -2074 2551 C ATOM 148 O GLY A 192 10.293 22.627 -19.524 1.00 51.66 O ANISOU 148 O GLY A 192 4732 5495 9402 -841 -2085 2561 O ATOM 149 N ASP A 193 11.213 22.147 -21.516 1.00 53.96 N ANISOU 149 N ASP A 193 5601 5848 9056 -564 -2398 2364 N ATOM 150 CA ASP A 193 10.987 20.708 -21.420 1.00 42.44 C ANISOU 150 CA ASP A 193 4010 4390 7725 -748 -2833 2173 C ATOM 151 C ASP A 193 12.221 19.939 -20.977 1.00 46.94 C ANISOU 151 C ASP A 193 4711 4899 8225 -920 -2679 1951 C ATOM 152 O ASP A 193 12.281 18.721 -21.130 1.00 53.27 O ANISOU 152 O ASP A 193 5516 5669 9056 -1024 -3003 1769 O ATOM 153 CB ASP A 193 10.527 20.169 -22.772 1.00 43.11 C ANISOU 153 CB ASP A 193 4231 4578 7570 -588 -3333 2088 C ATOM 154 CG ASP A 193 9.142 20.676 -23.166 1.00 60.44 C ANISOU 154 CG ASP A 193 6212 6903 9849 -430 -3581 2301 C ATOM 155 OD1 ASP A 193 8.973 21.137 -24.317 1.00 65.48 O ANISOU 155 OD1 ASP A 193 7027 7679 10175 -163 -3711 2375 O ATOM 156 OD2 ASP A 193 8.221 20.624 -22.323 1.00 68.17 O ANISOU 156 OD2 ASP A 193 6834 7875 11194 -564 -3641 2403 O ATOM 157 N LEU A 194 13.204 20.653 -20.444 1.00 44.85 N ANISOU 157 N LEU A 194 4508 5428 7106 340 -1121 1916 N ATOM 158 CA LEU A 194 14.483 20.057 -20.047 1.00 43.86 C ANISOU 158 CA LEU A 194 4482 5282 6900 305 -1037 1739 C ATOM 159 C LEU A 194 14.282 18.803 -19.190 1.00 41.23 C ANISOU 159 C LEU A 194 4007 5013 6644 245 -1096 1793 C ATOM 160 O LEU A 194 14.787 17.740 -19.511 1.00 42.62 O ANISOU 160 O LEU A 194 4273 5138 6782 149 -1194 1732 O ATOM 161 CB LEU A 194 15.330 21.100 -19.302 1.00 35.63 C ANISOU 161 CB LEU A 194 3464 4265 5810 410 -788 1611 C ATOM 162 CG LEU A 194 16.719 20.778 -18.719 1.00 48.32 C ANISOU 162 CG LEU A 194 5157 5870 7332 397 -651 1431 C ATOM 163 CD1 LEU A 194 16.633 19.888 -17.467 1.00 47.85 C ANISOU 163 CD1 LEU A 194 4924 5910 7345 380 -621 1465 C ATOM 164 CD2 LEU A 194 17.643 20.171 -19.755 1.00 49.28 C ANISOU 164 CD2 LEU A 194 5497 5889 7339 313 -733 1314 C ATOM 165 N MET A 195 13.529 18.951 -18.108 1.00 36.24 N ANISOU 165 N MET A 195 3151 4495 6122 307 -1035 1915 N ATOM 166 CA MET A 195 13.288 17.880 -17.149 1.00 39.52 C ANISOU 166 CA MET A 195 3399 4993 6624 267 -1069 1986 C ATOM 167 C MET A 195 12.828 16.582 -17.799 1.00 45.40 C ANISOU 167 C MET A 195 4150 5688 7412 133 -1315 2071 C ATOM 168 O MET A 195 13.094 15.500 -17.277 1.00 52.68 O ANISOU 168 O MET A 195 5019 6631 8367 70 -1351 2062 O ATOM 169 CB MET A 195 12.272 18.330 -16.095 1.00 37.20 C ANISOU 169 CB MET A 195 2853 4833 6448 363 -997 2149 C ATOM 170 CG MET A 195 12.794 19.454 -15.207 1.00 37.31 C ANISOU 170 CG MET A 195 2850 4904 6423 495 -744 2050 C ATOM 171 SD MET A 195 14.178 18.865 -14.225 1.00 53.48 S ANISOU 171 SD MET A 195 4928 6988 8405 475 -594 1867 S ATOM 172 CE MET A 195 13.288 17.599 -13.284 1.00 40.54 C ANISOU 172 CE MET A 195 3020 5473 6909 435 -697 2054 C ATOM 173 N LYS A 196 12.151 16.684 -18.938 1.00 39.57 N ANISOU 173 N LYS A 196 3481 4882 6674 87 -1485 2152 N ATOM 174 CA LYS A 196 11.727 15.486 -19.660 1.00 46.38 C ANISOU 174 CA LYS A 196 4375 5680 7565 -48 -1735 2222 C ATOM 175 C LYS A 196 12.887 14.790 -20.371 1.00 49.75 C ANISOU 175 C LYS A 196 5043 5990 7869 -128 -1775 2033 C ATOM 176 O LYS A 196 12.930 13.569 -20.439 1.00 55.36 O ANISOU 176 O LYS A 196 5767 6663 8606 -229 -1912 2038 O ATOM 177 CB LYS A 196 10.601 15.809 -20.642 1.00 52.73 C ANISOU 177 CB LYS A 196 5171 6458 8405 -77 -1912 2377 C ATOM 178 CG LYS A 196 9.329 16.296 -19.967 1.00 57.95 C ANISOU 178 CG LYS A 196 5577 7239 9202 -9 -1902 2601 C ATOM 179 CD LYS A 196 8.158 16.314 -20.944 1.00 70.37 C ANISOU 179 CD LYS A 196 7126 8789 10823 -68 -2119 2783 C ATOM 180 CE LYS A 196 6.968 17.110 -20.401 1.00 77.29 C ANISOU 180 CE LYS A 196 7773 9783 11812 29 -2071 3001 C ATOM 181 NZ LYS A 196 7.231 18.587 -20.349 1.00 81.99 N ANISOU 181 NZ LYS A 196 8410 10390 12352 172 -1858 2935 N ATOM 182 N PHE A 197 13.831 15.570 -20.887 1.00 47.96 N ANISOU 182 N PHE A 197 5006 5706 7511 -78 -1652 1871 N ATOM 183 CA PHE A 197 15.027 15.027 -21.522 1.00 41.11 C ANISOU 183 CA PHE A 197 4369 4738 6514 -131 -1658 1689 C ATOM 184 C PHE A 197 15.973 14.403 -20.507 1.00 45.69 C ANISOU 184 C PHE A 197 4920 5354 7086 -130 -1524 1588 C ATOM 185 O PHE A 197 16.547 13.336 -20.735 1.00 39.62 O ANISOU 185 O PHE A 197 4251 4523 6279 -207 -1597 1516 O ATOM 186 CB PHE A 197 15.770 16.133 -22.262 1.00 38.08 C ANISOU 186 CB PHE A 197 4170 4300 5999 -65 -1546 1564 C ATOM 187 CG PHE A 197 15.181 16.464 -23.601 1.00 46.43 C ANISOU 187 CG PHE A 197 5335 5290 7018 -93 -1706 1619 C ATOM 188 CD1 PHE A 197 15.610 15.803 -24.743 1.00 52.44 C ANISOU 188 CD1 PHE A 197 6304 5945 7675 -170 -1849 1538 C ATOM 189 CD2 PHE A 197 14.193 17.429 -23.721 1.00 44.81 C ANISOU 189 CD2 PHE A 197 5021 5128 6877 -38 -1712 1754 C ATOM 190 CE1 PHE A 197 15.063 16.105 -25.983 1.00 53.92 C ANISOU 190 CE1 PHE A 197 6589 6078 7820 -197 -1999 1589 C ATOM 191 CE2 PHE A 197 13.642 17.732 -24.951 1.00 45.53 C ANISOU 191 CE2 PHE A 197 5201 5166 6934 -66 -1859 1813 C ATOM 192 CZ PHE A 197 14.076 17.071 -26.084 1.00 51.13 C ANISOU 192 CZ PHE A 197 6117 5776 7535 -149 -2005 1730 C ATOM 193 N ALA A 198 16.144 15.091 -19.388 1.00 42.08 N ANISOU 193 N ALA A 198 4330 4998 6662 -39 -1324 1581 N ATOM 194 CA ALA A 198 17.127 14.691 -18.401 1.00 33.15 C ANISOU 194 CA ALA A 198 3172 3914 5508 -27 -1169 1478 C ATOM 195 C ALA A 198 16.817 13.340 -17.734 1.00 40.18 C ANISOU 195 C ALA A 198 3921 4845 6501 -102 -1263 1559 C ATOM 196 O ALA A 198 17.720 12.684 -17.228 1.00 39.65 O ANISOU 196 O ALA A 198 3878 4785 6401 -126 -1185 1466 O ATOM 197 CB ALA A 198 17.283 15.775 -17.359 1.00 30.76 C ANISOU 197 CB ALA A 198 2757 3714 5218 86 -945 1460 C ATOM 198 N VAL A 199 15.557 12.916 -17.723 1.00 46.29 N ANISOU 198 N VAL A 199 4541 5647 7399 -142 -1430 1739 N ATOM 199 CA VAL A 199 15.228 11.636 -17.081 1.00 45.60 C ANISOU 199 CA VAL A 199 4306 5597 7421 -215 -1527 1830 C ATOM 200 C VAL A 199 14.998 10.513 -18.084 1.00 47.93 C ANISOU 200 C VAL A 199 4719 5770 7722 -343 -1774 1851 C ATOM 201 O VAL A 199 14.681 9.392 -17.710 1.00 50.88 O ANISOU 201 O VAL A 199 4990 6152 8192 -419 -1886 1932 O ATOM 202 CB VAL A 199 14.016 11.750 -16.136 1.00 43.39 C ANISOU 202 CB VAL A 199 3738 5453 7296 -175 -1539 2036 C ATOM 203 CG1 VAL A 199 14.305 12.765 -15.053 1.00 40.96 C ANISOU 203 CG1 VAL A 199 3322 5266 6976 -45 -1289 2001 C ATOM 204 CG2 VAL A 199 12.731 12.098 -16.926 1.00 40.05 C ANISOU 204 CG2 VAL A 199 3277 5006 6932 -192 -1716 2200 C ATOM 205 N ASP A 200 15.151 10.835 -19.360 1.00 52.63 N ANISOU 205 N ASP A 200 5531 6253 8214 -365 -1859 1779 N ATOM 206 CA ASP A 200 15.051 9.864 -20.439 1.00 49.21 C ANISOU 206 CA ASP A 200 5254 5690 7753 -480 -2087 1767 C ATOM 207 C ASP A 200 16.471 9.450 -20.820 1.00 49.86 C ANISOU 207 C ASP A 200 5568 5683 7694 -491 -2010 1561 C ATOM 208 O ASP A 200 17.376 10.281 -20.841 1.00 51.43 O ANISOU 208 O ASP A 200 5871 5890 7781 -412 -1826 1433 O ATOM 209 CB ASP A 200 14.366 10.520 -21.635 1.00 53.11 C ANISOU 209 CB ASP A 200 5846 6126 8206 -489 -2220 1815 C ATOM 210 CG ASP A 200 14.117 9.552 -22.786 1.00 62.60 C ANISOU 210 CG ASP A 200 7208 7199 9380 -611 -2478 1814 C ATOM 211 OD1 ASP A 200 13.169 8.732 -22.702 1.00 60.46 O ANISOU 211 OD1 ASP A 200 6815 6926 9230 -700 -2672 1963 O ATOM 212 OD2 ASP A 200 14.855 9.643 -23.791 1.00 63.86 O ANISOU 212 OD2 ASP A 200 7614 7259 9392 -616 -2490 1670 O ATOM 213 N LYS A 201 16.674 8.177 -21.124 1.00 46.10 N ANISOU 213 N LYS A 201 5175 5118 7222 -586 -2150 1533 N ATOM 214 CA LYS A 201 18.008 7.704 -21.477 1.00 51.14 C ANISOU 214 CA LYS A 201 6032 5673 7728 -591 -2077 1349 C ATOM 215 C LYS A 201 18.577 8.443 -22.693 1.00 52.54 C ANISOU 215 C LYS A 201 6460 5767 7734 -554 -2061 1225 C ATOM 216 O LYS A 201 19.655 9.028 -22.629 1.00 56.47 O ANISOU 216 O LYS A 201 7059 6276 8120 -481 -1871 1097 O ATOM 217 CB LYS A 201 17.987 6.203 -21.747 1.00 54.54 C ANISOU 217 CB LYS A 201 6524 6003 8195 -701 -2258 1350 C ATOM 218 CG LYS A 201 19.363 5.581 -21.873 1.00 61.63 C ANISOU 218 CG LYS A 201 7610 6830 8977 -697 -2162 1179 C ATOM 219 CD LYS A 201 19.253 4.082 -22.128 1.00 74.16 C ANISOU 219 CD LYS A 201 9256 8309 10614 -804 -2350 1188 C ATOM 220 CE LYS A 201 20.572 3.358 -21.864 1.00 80.37 C ANISOU 220 CE LYS A 201 10156 9054 11325 -792 -2220 1052 C ATOM 221 NZ LYS A 201 21.744 4.072 -22.454 1.00 82.00 N ANISOU 221 NZ LYS A 201 10581 9235 11340 -710 -2060 890 N ATOM 222 N THR A 202 17.845 8.410 -23.799 1.00 44.69 N ANISOU 222 N THR A 202 5561 4695 6722 -606 -2266 1272 N ATOM 223 CA THR A 202 18.312 9.015 -25.038 1.00 46.73 C ANISOU 223 CA THR A 202 6057 4876 6820 -576 -2277 1167 C ATOM 224 C THR A 202 18.467 10.520 -24.900 1.00 48.53 C ANISOU 224 C THR A 202 6249 5183 7009 -468 -2094 1158 C ATOM 225 O THR A 202 19.442 11.096 -25.388 1.00 47.17 O ANISOU 225 O THR A 202 6245 4980 6696 -408 -1974 1029 O ATOM 226 CB THR A 202 17.345 8.732 -26.200 1.00 54.12 C ANISOU 226 CB THR A 202 7075 5731 7756 -657 -2544 1241 C ATOM 227 OG1 THR A 202 17.147 7.317 -26.327 1.00 56.18 O ANISOU 227 OG1 THR A 202 7374 5909 8062 -766 -2731 1252 O ATOM 228 CG2 THR A 202 17.904 9.288 -27.502 1.00 54.50 C ANISOU 228 CG2 THR A 202 7377 5705 7625 -623 -2552 1127 C ATOM 229 N GLY A 203 17.489 11.148 -24.248 1.00 44.92 N ANISOU 229 N GLY A 203 5570 4821 6677 -441 -2076 1301 N ATOM 230 CA GLY A 203 17.531 12.568 -23.966 1.00 37.13 C ANISOU 230 CA GLY A 203 4523 3908 5676 -335 -1899 1304 C ATOM 231 C GLY A 203 18.754 12.951 -23.141 1.00 46.92 C ANISOU 231 C GLY A 203 5775 5194 6858 -260 -1646 1176 C ATOM 232 O GLY A 203 19.494 13.880 -23.495 1.00 44.77 O ANISOU 232 O GLY A 203 5623 4910 6479 -192 -1514 1079 O ATOM 233 N CYS A 204 18.984 12.241 -22.040 1.00 48.77 N ANISOU 233 N CYS A 204 5882 5486 7164 -276 -1580 1181 N ATOM 234 CA CYS A 204 20.093 12.598 -21.168 1.00 51.77 C ANISOU 234 CA CYS A 204 6252 5923 7494 -212 -1342 1073 C ATOM 235 C CYS A 204 21.419 12.373 -21.873 1.00 49.10 C ANISOU 235 C CYS A 204 6159 5499 6997 -215 -1290 910 C ATOM 236 O CYS A 204 22.375 13.096 -21.646 1.00 46.91 O ANISOU 236 O CYS A 204 5941 5246 6635 -151 -1104 813 O ATOM 237 CB CYS A 204 20.044 11.842 -19.838 1.00 54.30 C ANISOU 237 CB CYS A 204 6374 6333 7924 -231 -1285 1122 C ATOM 238 SG CYS A 204 20.854 12.758 -18.490 1.00 68.99 S ANISOU 238 SG CYS A 204 8124 8319 9768 -131 -987 1055 S ATOM 239 N GLN A 205 21.459 11.379 -22.747 1.00 48.76 N ANISOU 239 N GLN A 205 6261 5355 6911 -289 -1459 886 N ATOM 240 CA GLN A 205 22.664 11.079 -23.493 1.00 49.78 C ANISOU 240 CA GLN A 205 6631 5399 6883 -285 -1423 742 C ATOM 241 C GLN A 205 22.982 12.265 -24.377 1.00 54.65 C ANISOU 241 C GLN A 205 7390 5992 7384 -219 -1369 689 C ATOM 242 O GLN A 205 24.143 12.597 -24.609 1.00 53.74 O ANISOU 242 O GLN A 205 7417 5860 7144 -172 -1234 576 O ATOM 243 CB GLN A 205 22.447 9.832 -24.338 1.00 56.88 C ANISOU 243 CB GLN A 205 7661 6187 7763 -372 -1639 737 C ATOM 244 CG GLN A 205 23.707 9.222 -24.919 1.00 67.22 C ANISOU 244 CG GLN A 205 9203 7414 8924 -368 -1599 595 C ATOM 245 CD GLN A 205 23.418 7.935 -25.707 1.00 77.49 C ANISOU 245 CD GLN A 205 10635 8595 10213 -454 -1822 587 C ATOM 246 OE1 GLN A 205 22.722 7.042 -25.223 1.00 79.28 O ANISOU 246 OE1 GLN A 205 10738 8818 10569 -528 -1941 668 O ATOM 247 NE2 GLN A 205 23.953 7.844 -26.922 1.00 76.79 N ANISOU 247 NE2 GLN A 205 10799 8409 9968 -441 -1880 491 N ATOM 248 N PHE A 206 21.931 12.914 -24.863 1.00 53.01 N ANISOU 248 N PHE A 206 7133 5785 7223 -216 -1474 782 N ATOM 249 CA PHE A 206 22.084 14.078 -25.721 1.00 47.38 C ANISOU 249 CA PHE A 206 6534 5052 6418 -154 -1435 753 C ATOM 250 C PHE A 206 22.615 15.292 -24.936 1.00 50.74 C ANISOU 250 C PHE A 206 6882 5555 6844 -64 -1200 722 C ATOM 251 O PHE A 206 23.572 15.963 -25.357 1.00 46.95 O ANISOU 251 O PHE A 206 6540 5053 6247 -10 -1084 628 O ATOM 252 CB PHE A 206 20.748 14.395 -26.392 1.00 44.38 C ANISOU 252 CB PHE A 206 6101 4660 6101 -180 -1614 879 C ATOM 253 CG PHE A 206 20.665 15.786 -26.944 1.00 50.69 C ANISOU 253 CG PHE A 206 6935 5469 6855 -105 -1547 889 C ATOM 254 CD1 PHE A 206 21.381 16.140 -28.075 1.00 48.61 C ANISOU 254 CD1 PHE A 206 6886 5142 6441 -78 -1547 801 C ATOM 255 CD2 PHE A 206 19.869 16.745 -26.330 1.00 53.44 C ANISOU 255 CD2 PHE A 206 7099 5893 7313 -55 -1481 993 C ATOM 256 CE1 PHE A 206 21.306 17.429 -28.586 1.00 49.01 C ANISOU 256 CE1 PHE A 206 6960 5202 6459 -10 -1486 818 C ATOM 257 CE2 PHE A 206 19.794 18.035 -26.830 1.00 52.50 C ANISOU 257 CE2 PHE A 206 7011 5777 7161 15 -1416 1005 C ATOM 258 CZ PHE A 206 20.515 18.376 -27.960 1.00 51.74 C ANISOU 258 CZ PHE A 206 7123 5615 6922 35 -1420 919 C ATOM 259 N LEU A 207 21.991 15.564 -23.791 1.00 42.06 N ANISOU 259 N LEU A 207 5561 4545 5876 -46 -1133 803 N ATOM 260 CA LEU A 207 22.395 16.682 -22.952 1.00 36.08 C ANISOU 260 CA LEU A 207 4722 3860 5128 37 -919 774 C ATOM 261 C LEU A 207 23.850 16.538 -22.528 1.00 33.34 C ANISOU 261 C LEU A 207 4463 3519 4685 52 -751 641 C ATOM 262 O LEU A 207 24.626 17.503 -22.558 1.00 32.40 O ANISOU 262 O LEU A 207 4416 3404 4492 112 -604 569 O ATOM 263 CB LEU A 207 21.493 16.775 -21.724 1.00 40.42 C ANISOU 263 CB LEU A 207 5019 4510 5828 53 -883 882 C ATOM 264 CG LEU A 207 20.034 17.062 -22.068 1.00 40.85 C ANISOU 264 CG LEU A 207 4966 4573 5983 50 -1029 1034 C ATOM 265 CD1 LEU A 207 19.167 17.092 -20.825 1.00 45.32 C ANISOU 265 CD1 LEU A 207 5278 5247 6693 75 -988 1150 C ATOM 266 CD2 LEU A 207 19.946 18.368 -22.811 1.00 34.64 C ANISOU 266 CD2 LEU A 207 4259 3756 5147 116 -990 1030 C ATOM 267 N GLU A 208 24.223 15.318 -22.165 1.00 28.71 N ANISOU 267 N GLU A 208 3875 2933 4102 -5 -780 616 N ATOM 268 CA GLU A 208 25.558 15.050 -21.661 1.00 39.41 C ANISOU 268 CA GLU A 208 5290 4307 5378 3 -622 510 C ATOM 269 C GLU A 208 26.627 15.351 -22.709 1.00 39.19 C ANISOU 269 C GLU A 208 5499 4204 5189 28 -586 408 C ATOM 270 O GLU A 208 27.708 15.835 -22.375 1.00 46.98 O ANISOU 270 O GLU A 208 6533 5217 6101 66 -415 332 O ATOM 271 CB GLU A 208 25.662 13.613 -21.117 1.00 49.24 C ANISOU 271 CB GLU A 208 6479 5561 6669 -64 -672 519 C ATOM 272 CG GLU A 208 25.151 13.465 -19.678 1.00 55.84 C ANISOU 272 CG GLU A 208 7064 6512 7642 -66 -605 593 C ATOM 273 CD GLU A 208 26.018 14.231 -18.669 1.00 69.65 C ANISOU 273 CD GLU A 208 8752 8351 9360 -9 -370 529 C ATOM 274 OE1 GLU A 208 27.174 13.814 -18.396 1.00 69.48 O ANISOU 274 OE1 GLU A 208 8798 8339 9263 -19 -262 448 O ATOM 275 OE2 GLU A 208 25.536 15.255 -18.142 1.00 75.93 O ANISOU 275 OE2 GLU A 208 9435 9209 10206 47 -294 564 O ATOM 276 N LYS A 209 26.315 15.085 -23.970 1.00 41.20 N ANISOU 276 N LYS A 209 5900 4370 5387 7 -749 414 N ATOM 277 CA LYS A 209 27.208 15.439 -25.070 1.00 47.19 C ANISOU 277 CA LYS A 209 6879 5062 5988 41 -727 333 C ATOM 278 C LYS A 209 27.220 16.958 -25.286 1.00 43.26 C ANISOU 278 C LYS A 209 6382 4583 5471 111 -633 338 C ATOM 279 O LYS A 209 28.276 17.570 -25.430 1.00 42.02 O ANISOU 279 O LYS A 209 6324 4426 5218 158 -498 269 O ATOM 280 CB LYS A 209 26.769 14.738 -26.355 1.00 54.79 C ANISOU 280 CB LYS A 209 7991 5930 6895 1 -938 341 C ATOM 281 CG LYS A 209 27.814 14.730 -27.466 1.00 68.95 C ANISOU 281 CG LYS A 209 10029 7659 8511 35 -924 251 C ATOM 282 CD LYS A 209 28.891 13.673 -27.217 1.00 78.35 C ANISOU 282 CD LYS A 209 11308 8831 9629 21 -861 173 C ATOM 283 CE LYS A 209 29.801 13.510 -28.431 1.00 85.18 C ANISOU 283 CE LYS A 209 12424 9626 10314 59 -875 96 C ATOM 284 NZ LYS A 209 31.138 12.955 -28.067 1.00 86.43 N ANISOU 284 NZ LYS A 209 12659 9793 10386 80 -731 24 N ATOM 285 N ALA A 210 26.031 17.550 -25.284 1.00 39.23 N ANISOU 285 N ALA A 210 5755 4089 5062 118 -706 430 N ATOM 286 CA ALA A 210 25.848 18.956 -25.606 1.00 33.48 C ANISOU 286 CA ALA A 210 5026 3365 4330 183 -645 451 C ATOM 287 C ALA A 210 26.517 19.836 -24.567 1.00 34.57 C ANISOU 287 C ALA A 210 5087 3564 4485 236 -429 408 C ATOM 288 O ALA A 210 27.071 20.893 -24.875 1.00 41.02 O ANISOU 288 O ALA A 210 5975 4367 5245 290 -329 372 O ATOM 289 CB ALA A 210 24.362 19.266 -25.665 1.00 32.69 C ANISOU 289 CB ALA A 210 4791 3279 4350 177 -765 575 C ATOM 290 N VAL A 211 26.446 19.378 -23.326 1.00 32.86 N ANISOU 290 N VAL A 211 4721 3415 4348 217 -362 414 N ATOM 291 CA VAL A 211 26.936 20.117 -22.174 1.00 27.56 C ANISOU 291 CA VAL A 211 3953 2814 3705 258 -169 378 C ATOM 292 C VAL A 211 28.477 20.186 -22.097 1.00 34.85 C ANISOU 292 C VAL A 211 4999 3735 4508 265 -25 270 C ATOM 293 O VAL A 211 29.031 21.088 -21.463 1.00 38.38 O ANISOU 293 O VAL A 211 5417 4217 4948 304 132 230 O ATOM 294 CB VAL A 211 26.290 19.540 -20.882 1.00 44.42 C ANISOU 294 CB VAL A 211 5878 5035 5963 237 -156 432 C ATOM 295 CG1 VAL A 211 27.163 19.727 -19.686 1.00 45.37 C ANISOU 295 CG1 VAL A 211 5934 5232 6074 253 33 365 C ATOM 296 CG2 VAL A 211 24.919 20.161 -20.655 1.00 44.34 C ANISOU 296 CG2 VAL A 211 5717 5054 6074 271 -208 540 C ATOM 297 N LYS A 212 29.158 19.254 -22.759 1.00 35.96 N ANISOU 297 N LYS A 212 5279 3830 4553 230 -80 229 N ATOM 298 CA LYS A 212 30.627 19.235 -22.829 1.00 38.72 C ANISOU 298 CA LYS A 212 5756 4177 4779 238 44 144 C ATOM 299 C LYS A 212 31.189 20.189 -23.875 1.00 43.73 C ANISOU 299 C LYS A 212 6549 4757 5311 287 69 118 C ATOM 300 O LYS A 212 32.397 20.421 -23.914 1.00 45.02 O ANISOU 300 O LYS A 212 6805 4924 5377 304 186 62 O ATOM 301 CB LYS A 212 31.133 17.835 -23.191 1.00 44.78 C ANISOU 301 CB LYS A 212 6622 4915 5479 193 -23 116 C ATOM 302 CG LYS A 212 31.239 16.865 -22.037 1.00 57.34 C ANISOU 302 CG LYS A 212 8084 6569 7132 148 22 118 C ATOM 303 CD LYS A 212 32.004 15.608 -22.471 1.00 65.38 C ANISOU 303 CD LYS A 212 9232 7546 8064 116 -14 78 C ATOM 304 CE LYS A 212 32.107 14.603 -21.333 1.00 69.12 C ANISOU 304 CE LYS A 212 9572 8084 8609 69 30 89 C ATOM 305 NZ LYS A 212 33.218 13.630 -21.536 1.00 72.13 N ANISOU 305 NZ LYS A 212 10075 8441 8890 55 71 40 N ATOM 306 N GLY A 213 30.330 20.710 -24.749 1.00 36.87 N ANISOU 306 N GLY A 213 5706 3839 4461 308 -45 167 N ATOM 307 CA GLY A 213 30.799 21.566 -25.821 1.00 32.43 C ANISOU 307 CA GLY A 213 5288 3227 3805 355 -35 154 C ATOM 308 C GLY A 213 31.010 22.994 -25.359 1.00 36.88 C ANISOU 308 C GLY A 213 5797 3811 4404 404 105 151 C ATOM 309 O GLY A 213 31.007 23.284 -24.162 1.00 37.06 O ANISOU 309 O GLY A 213 5691 3889 4502 403 214 139 O ATOM 310 N SER A 214 31.195 23.895 -26.312 1.00 31.41 N ANISOU 310 N SER A 214 5205 3073 3657 449 100 161 N ATOM 311 CA SER A 214 31.312 25.299 -25.994 1.00 39.61 C ANISOU 311 CA SER A 214 6201 4114 4737 496 216 164 C ATOM 312 C SER A 214 29.930 25.784 -25.614 1.00 44.00 C ANISOU 312 C SER A 214 6609 4677 5431 511 168 231 C ATOM 313 O SER A 214 28.944 25.485 -26.278 1.00 53.59 O ANISOU 313 O SER A 214 7814 5872 6677 503 23 295 O ATOM 314 CB SER A 214 31.837 26.087 -27.194 1.00 41.68 C ANISOU 314 CB SER A 214 6604 4323 4910 540 212 172 C ATOM 315 OG SER A 214 32.986 25.457 -27.739 1.00 46.27 O ANISOU 315 OG SER A 214 7329 4898 5352 533 227 129 O ATOM 316 N LEU A 215 29.854 26.521 -24.527 1.00 42.29 N ANISOU 316 N LEU A 215 6279 4495 5296 533 291 218 N ATOM 317 CA LEU A 215 28.575 27.027 -24.068 1.00 35.66 C ANISOU 317 CA LEU A 215 5293 3669 4586 562 267 286 C ATOM 318 C LEU A 215 28.672 28.531 -23.968 1.00 33.02 C ANISOU 318 C LEU A 215 4955 3305 4284 625 376 281 C ATOM 319 O LEU A 215 29.670 29.069 -23.463 1.00 27.75 O ANISOU 319 O LEU A 215 4324 2639 3581 633 511 211 O ATOM 320 CB LEU A 215 28.238 26.442 -22.691 1.00 31.69 C ANISOU 320 CB LEU A 215 4636 3242 4161 540 314 279 C ATOM 321 CG LEU A 215 28.064 24.933 -22.596 1.00 31.39 C ANISOU 321 CG LEU A 215 4572 3236 4117 475 212 291 C ATOM 322 CD1 LEU A 215 27.577 24.536 -21.209 1.00 26.85 C ANISOU 322 CD1 LEU A 215 3817 2746 3639 465 261 307 C ATOM 323 CD2 LEU A 215 27.103 24.437 -23.656 1.00 31.23 C ANISOU 323 CD2 LEU A 215 4580 3177 4112 456 21 371 C ATOM 324 N THR A 216 27.641 29.219 -24.445 1.00 34.04 N ANISOU 324 N THR A 216 5042 3405 4486 668 316 362 N ATOM 325 CA THR A 216 27.602 30.658 -24.288 1.00 28.34 C ANISOU 325 CA THR A 216 4305 2648 3815 734 418 365 C ATOM 326 C THR A 216 27.116 30.952 -22.894 1.00 26.01 C ANISOU 326 C THR A 216 3862 2401 3619 761 516 355 C ATOM 327 O THR A 216 26.586 30.075 -22.200 1.00 30.40 O ANISOU 327 O THR A 216 4312 3021 4217 735 481 374 O ATOM 328 CB THR A 216 26.621 31.331 -25.262 1.00 36.13 C ANISOU 328 CB THR A 216 5286 3590 4851 777 329 466 C ATOM 329 OG1 THR A 216 25.289 30.908 -24.955 1.00 40.60 O ANISOU 329 OG1 THR A 216 5715 4196 5513 779 243 553 O ATOM 330 CG2 THR A 216 26.956 30.988 -26.714 1.00 29.41 C ANISOU 330 CG2 THR A 216 4575 2702 3897 754 214 485 C ATOM 331 N SER A 217 27.262 32.212 -22.514 1.00 25.01 N ANISOU 331 N SER A 217 3730 2241 3533 818 634 331 N ATOM 332 CA SER A 217 26.884 32.681 -21.204 1.00 25.08 C ANISOU 332 CA SER A 217 3618 2287 3624 860 743 309 C ATOM 333 C SER A 217 25.434 32.372 -20.859 1.00 32.81 C ANISOU 333 C SER A 217 4445 3315 4707 891 676 409 C ATOM 334 O SER A 217 25.133 31.926 -19.746 1.00 31.13 O ANISOU 334 O SER A 217 4115 3177 4536 893 718 400 O ATOM 335 CB SER A 217 27.137 34.178 -21.121 1.00 25.67 C ANISOU 335 CB SER A 217 3732 2292 3728 923 856 279 C ATOM 336 OG SER A 217 26.680 34.665 -19.885 1.00 32.53 O ANISOU 336 OG SER A 217 4493 3193 4675 974 958 257 O ATOM 337 N TYR A 218 24.537 32.611 -21.812 1.00 33.85 N ANISOU 337 N TYR A 218 4572 3411 4879 916 571 513 N ATOM 338 CA TYR A 218 23.120 32.405 -21.572 1.00 30.93 C ANISOU 338 CA TYR A 218 4054 3086 4611 948 501 631 C ATOM 339 C TYR A 218 22.763 30.925 -21.488 1.00 32.13 C ANISOU 339 C TYR A 218 4145 3306 4758 876 378 671 C ATOM 340 O TYR A 218 21.894 30.543 -20.706 1.00 29.81 O ANISOU 340 O TYR A 218 3700 3081 4544 891 365 736 O ATOM 341 CB TYR A 218 22.271 33.093 -22.638 1.00 29.37 C ANISOU 341 CB TYR A 218 3865 2837 4459 991 422 744 C ATOM 342 CG TYR A 218 20.815 33.096 -22.288 1.00 32.00 C ANISOU 342 CG TYR A 218 4034 3218 4905 1038 376 877 C ATOM 343 CD1 TYR A 218 20.387 33.627 -21.082 1.00 38.25 C ANISOU 343 CD1 TYR A 218 4708 4048 5776 1114 499 878 C ATOM 344 CD2 TYR A 218 19.859 32.559 -23.149 1.00 34.37 C ANISOU 344 CD2 TYR A 218 4296 3532 5232 1008 209 1008 C ATOM 345 CE1 TYR A 218 19.040 33.635 -20.727 1.00 36.10 C ANISOU 345 CE1 TYR A 218 4277 3830 5608 1169 465 1015 C ATOM 346 CE2 TYR A 218 18.498 32.571 -22.812 1.00 31.58 C ANISOU 346 CE2 TYR A 218 3780 3230 4987 1051 166 1151 C ATOM 347 CZ TYR A 218 18.101 33.111 -21.591 1.00 41.92 C ANISOU 347 CZ TYR A 218 4969 4582 6376 1136 300 1157 C ATOM 348 OH TYR A 218 16.767 33.139 -21.218 1.00 43.94 O ANISOU 348 OH TYR A 218 5058 4898 6738 1191 268 1310 O ATOM 349 N GLN A 219 23.418 30.093 -22.300 1.00 29.47 N ANISOU 349 N GLN A 219 3924 2947 4327 800 286 636 N ATOM 350 CA GLN A 219 23.240 28.646 -22.168 1.00 27.76 C ANISOU 350 CA GLN A 219 3666 2782 4100 725 177 655 C ATOM 351 C GLN A 219 23.584 28.158 -20.763 1.00 25.97 C ANISOU 351 C GLN A 219 3343 2632 3894 715 280 596 C ATOM 352 O GLN A 219 22.861 27.359 -20.200 1.00 33.69 O ANISOU 352 O GLN A 219 4191 3674 4935 694 221 660 O ATOM 353 CB GLN A 219 24.031 27.873 -23.226 1.00 26.38 C ANISOU 353 CB GLN A 219 3652 2562 3808 656 82 608 C ATOM 354 CG GLN A 219 23.531 28.135 -24.626 1.00 29.92 C ANISOU 354 CG GLN A 219 4179 2953 4235 659 -48 681 C ATOM 355 CD GLN A 219 24.309 27.410 -25.692 1.00 30.01 C ANISOU 355 CD GLN A 219 4360 2923 4119 603 -138 632 C ATOM 356 OE1 GLN A 219 25.536 27.330 -25.642 1.00 29.66 O ANISOU 356 OE1 GLN A 219 4421 2866 3983 594 -53 531 O ATOM 357 NE2 GLN A 219 23.597 26.893 -26.686 1.00 33.71 N ANISOU 357 NE2 GLN A 219 4858 3372 4577 570 -313 707 N ATOM 358 N LYS A 220 24.687 28.628 -20.196 1.00 32.62 N ANISOU 358 N LYS A 220 4242 3471 4681 725 429 482 N ATOM 359 CA LYS A 220 25.031 28.239 -18.830 1.00 32.50 C ANISOU 359 CA LYS A 220 4132 3538 4680 717 534 427 C ATOM 360 C LYS A 220 23.968 28.759 -17.875 1.00 37.10 C ANISOU 360 C LYS A 220 4544 4177 5374 791 586 491 C ATOM 361 O LYS A 220 23.559 28.066 -16.939 1.00 31.66 O ANISOU 361 O LYS A 220 3717 3577 4734 784 591 520 O ATOM 362 CB LYS A 220 26.380 28.813 -18.416 1.00 29.05 C ANISOU 362 CB LYS A 220 3787 3086 4163 716 685 300 C ATOM 363 CG LYS A 220 27.555 28.310 -19.211 1.00 31.74 C ANISOU 363 CG LYS A 220 4287 3386 4386 653 660 239 C ATOM 364 CD LYS A 220 28.857 28.981 -18.743 1.00 31.58 C ANISOU 364 CD LYS A 220 4345 3358 4297 652 813 132 C ATOM 365 CE LYS A 220 30.063 28.438 -19.537 1.00 38.64 C ANISOU 365 CE LYS A 220 5392 4220 5068 595 794 87 C ATOM 366 NZ LYS A 220 31.377 28.695 -18.868 1.00 39.99 N ANISOU 366 NZ LYS A 220 5609 4415 5171 572 935 -4 N ATOM 367 N PHE A 221 23.528 29.992 -18.126 1.00 28.27 N ANISOU 367 N PHE A 221 3437 3007 4296 868 629 518 N ATOM 368 CA PHE A 221 22.565 30.649 -17.266 1.00 26.60 C ANISOU 368 CA PHE A 221 3083 2840 4184 958 697 576 C ATOM 369 C PHE A 221 21.313 29.775 -17.119 1.00 27.98 C ANISOU 369 C PHE A 221 3100 3088 4443 952 578 716 C ATOM 370 O PHE A 221 20.797 29.565 -16.017 1.00 29.52 O ANISOU 370 O PHE A 221 3144 3374 4697 990 629 749 O ATOM 371 CB PHE A 221 22.213 32.019 -17.847 1.00 27.43 C ANISOU 371 CB PHE A 221 3240 2861 4322 1037 733 604 C ATOM 372 CG PHE A 221 21.441 32.885 -16.915 1.00 28.20 C ANISOU 372 CG PHE A 221 3222 2988 4506 1144 839 637 C ATOM 373 CD1 PHE A 221 22.092 33.637 -15.954 1.00 28.31 C ANISOU 373 CD1 PHE A 221 3256 3000 4501 1189 1002 521 C ATOM 374 CD2 PHE A 221 20.059 32.942 -16.982 1.00 40.22 C ANISOU 374 CD2 PHE A 221 4616 4542 6125 1203 776 787 C ATOM 375 CE1 PHE A 221 21.374 34.439 -15.073 1.00 34.71 C ANISOU 375 CE1 PHE A 221 3969 3834 5383 1299 1104 544 C ATOM 376 CE2 PHE A 221 19.328 33.745 -16.103 1.00 38.49 C ANISOU 376 CE2 PHE A 221 4289 4354 5982 1318 883 824 C ATOM 377 CZ PHE A 221 19.987 34.491 -15.149 1.00 32.02 C ANISOU 377 CZ PHE A 221 3501 3528 5138 1370 1049 697 C ATOM 378 N GLN A 222 20.842 29.264 -18.248 1.00 28.51 N ANISOU 378 N GLN A 222 3203 3119 4512 904 415 801 N ATOM 379 CA GLN A 222 19.655 28.432 -18.304 1.00 29.79 C ANISOU 379 CA GLN A 222 3231 3337 4753 883 274 947 C ATOM 380 C GLN A 222 19.873 27.061 -17.671 1.00 32.79 C ANISOU 380 C GLN A 222 3541 3790 5127 808 230 934 C ATOM 381 O GLN A 222 18.978 26.522 -17.038 1.00 36.02 O ANISOU 381 O GLN A 222 3784 4281 5622 816 186 1039 O ATOM 382 CB GLN A 222 19.251 28.226 -19.756 1.00 29.06 C ANISOU 382 CB GLN A 222 3221 3177 4644 836 104 1023 C ATOM 383 CG GLN A 222 18.686 29.442 -20.440 1.00 34.06 C ANISOU 383 CG GLN A 222 3877 3753 5310 909 114 1089 C ATOM 384 CD GLN A 222 18.453 29.173 -21.908 1.00 38.66 C ANISOU 384 CD GLN A 222 4557 4276 5855 852 -55 1149 C ATOM 385 OE1 GLN A 222 19.391 28.857 -22.640 1.00 35.42 O ANISOU 385 OE1 GLN A 222 4304 3813 5342 793 -89 1057 O ATOM 386 NE2 GLN A 222 17.197 29.275 -22.346 1.00 39.44 N ANISOU 386 NE2 GLN A 222 4562 4390 6032 869 -163 1310 N ATOM 387 N LEU A 223 21.051 26.484 -17.887 1.00 32.86 N ANISOU 387 N LEU A 223 3676 3770 5038 735 237 817 N ATOM 388 CA LEU A 223 21.399 25.221 -17.269 1.00 29.78 C ANISOU 388 CA LEU A 223 3232 3444 4640 666 213 795 C ATOM 389 C LEU A 223 21.414 25.396 -15.768 1.00 32.79 C ANISOU 389 C LEU A 223 3468 3927 5064 718 361 772 C ATOM 390 O LEU A 223 20.811 24.605 -15.041 1.00 39.01 O ANISOU 390 O LEU A 223 4097 4803 5921 707 324 850 O ATOM 391 CB LEU A 223 22.765 24.738 -17.749 1.00 32.57 C ANISOU 391 CB LEU A 223 3756 3745 4872 596 226 669 C ATOM 392 CG LEU A 223 22.812 24.049 -19.117 1.00 33.16 C ANISOU 392 CG LEU A 223 3965 3741 4892 527 57 687 C ATOM 393 CD1 LEU A 223 24.243 23.905 -19.622 1.00 31.22 C ANISOU 393 CD1 LEU A 223 3906 3441 4515 489 106 560 C ATOM 394 CD2 LEU A 223 22.134 22.695 -19.057 1.00 26.50 C ANISOU 394 CD2 LEU A 223 3030 2932 4105 458 -94 772 C ATOM 395 N PHE A 224 22.094 26.445 -15.307 1.00 32.07 N ANISOU 395 N PHE A 224 3430 3823 4931 775 524 670 N ATOM 396 CA PHE A 224 22.150 26.757 -13.883 1.00 37.12 C ANISOU 396 CA PHE A 224 3949 4557 5597 832 674 635 C ATOM 397 C PHE A 224 20.757 26.832 -13.259 1.00 37.96 C ANISOU 397 C PHE A 224 3861 4743 5819 908 654 773 C ATOM 398 O PHE A 224 20.516 26.248 -12.212 1.00 42.73 O ANISOU 398 O PHE A 224 4315 5458 6463 916 688 804 O ATOM 399 CB PHE A 224 22.913 28.059 -13.618 1.00 24.95 C ANISOU 399 CB PHE A 224 2506 2970 4002 889 834 515 C ATOM 400 CG PHE A 224 24.368 28.011 -14.039 1.00 24.63 C ANISOU 400 CG PHE A 224 2638 2871 3848 819 874 387 C ATOM 401 CD1 PHE A 224 25.033 26.803 -14.154 1.00 26.03 C ANISOU 401 CD1 PHE A 224 2844 3074 3972 726 820 362 C ATOM 402 CD2 PHE A 224 25.074 29.182 -14.304 1.00 25.02 C ANISOU 402 CD2 PHE A 224 2819 2841 3847 849 967 299 C ATOM 403 CE1 PHE A 224 26.380 26.757 -14.544 1.00 25.37 C ANISOU 403 CE1 PHE A 224 2915 2943 3780 670 863 257 C ATOM 404 CE2 PHE A 224 26.405 29.144 -14.689 1.00 25.10 C ANISOU 404 CE2 PHE A 224 2977 2806 3754 787 1003 199 C ATOM 405 CZ PHE A 224 27.052 27.926 -14.811 1.00 26.28 C ANISOU 405 CZ PHE A 224 3152 2988 3845 701 953 181 C ATOM 406 N GLU A 225 19.849 27.544 -13.915 1.00 33.67 N ANISOU 406 N GLU A 225 3315 4150 5330 965 602 866 N ATOM 407 CA GLU A 225 18.521 27.772 -13.378 1.00 38.85 C ANISOU 407 CA GLU A 225 3790 4877 6092 1051 595 1009 C ATOM 408 C GLU A 225 17.675 26.509 -13.368 1.00 37.69 C ANISOU 408 C GLU A 225 3500 4804 6017 995 442 1154 C ATOM 409 O GLU A 225 16.923 26.266 -12.428 1.00 36.06 O ANISOU 409 O GLU A 225 3109 4707 5885 1047 465 1249 O ATOM 410 CB GLU A 225 17.794 28.844 -14.198 1.00 53.85 C ANISOU 410 CB GLU A 225 5731 6700 8030 1122 573 1083 C ATOM 411 CG GLU A 225 18.378 30.232 -14.075 1.00 74.76 C ANISOU 411 CG GLU A 225 8488 9279 10638 1199 730 968 C ATOM 412 CD GLU A 225 18.209 30.831 -12.684 1.00 91.40 C ANISOU 412 CD GLU A 225 10489 11464 12774 1306 896 937 C ATOM 413 OE1 GLU A 225 18.810 31.900 -12.420 1.00 96.69 O ANISOU 413 OE1 GLU A 225 11254 12079 13406 1361 1032 821 O ATOM 414 OE2 GLU A 225 17.476 30.241 -11.857 1.00 96.33 O ANISOU 414 OE2 GLU A 225 10939 12205 13459 1337 887 1031 O ATOM 415 N GLN A 226 17.799 25.714 -14.423 1.00 36.79 N ANISOU 415 N GLN A 226 3473 4626 5878 892 283 1173 N ATOM 416 CA GLN A 226 16.892 24.599 -14.654 1.00 33.48 C ANISOU 416 CA GLN A 226 2939 4247 5534 830 105 1323 C ATOM 417 C GLN A 226 17.353 23.324 -13.985 1.00 33.78 C ANISOU 417 C GLN A 226 2914 4352 5569 753 85 1295 C ATOM 418 O GLN A 226 16.534 22.505 -13.595 1.00 37.17 O ANISOU 418 O GLN A 226 3180 4857 6086 732 -8 1428 O ATOM 419 CB GLN A 226 16.701 24.359 -16.160 1.00 34.23 C ANISOU 419 CB GLN A 226 3162 4237 5605 755 -72 1363 C ATOM 420 CG GLN A 226 15.983 25.534 -16.853 1.00 36.64 C ANISOU 420 CG GLN A 226 3491 4493 5938 830 -76 1439 C ATOM 421 CD GLN A 226 15.705 25.294 -18.327 1.00 41.42 C ANISOU 421 CD GLN A 226 4207 5010 6519 757 -257 1493 C ATOM 422 OE1 GLN A 226 15.216 24.232 -18.717 1.00 45.95 O ANISOU 422 OE1 GLN A 226 4743 5592 7122 671 -431 1580 O ATOM 423 NE2 GLN A 226 15.991 26.295 -19.151 1.00 41.29 N ANISOU 423 NE2 GLN A 226 4325 4910 6451 793 -221 1446 N ATOM 424 N VAL A 227 18.664 23.162 -13.853 1.00 34.72 N ANISOU 424 N VAL A 227 3156 4445 5590 711 171 1133 N ATOM 425 CA VAL A 227 19.227 21.920 -13.351 1.00 36.69 C ANISOU 425 CA VAL A 227 3369 4745 5828 630 151 1100 C ATOM 426 C VAL A 227 19.621 22.046 -11.870 1.00 37.09 C ANISOU 426 C VAL A 227 3298 4914 5881 683 326 1048 C ATOM 427 O VAL A 227 19.373 21.144 -11.079 1.00 40.02 O ANISOU 427 O VAL A 227 3515 5384 6308 660 308 1111 O ATOM 428 CB VAL A 227 20.421 21.421 -14.229 1.00 37.05 C ANISOU 428 CB VAL A 227 3624 4691 5761 539 113 974 C ATOM 429 CG1 VAL A 227 21.077 20.188 -13.612 1.00 24.80 C ANISOU 429 CG1 VAL A 227 2031 3194 4197 466 118 936 C ATOM 430 CG2 VAL A 227 19.954 21.118 -15.647 1.00 28.91 C ANISOU 430 CG2 VAL A 227 2700 3558 4727 483 -77 1034 C ATOM 431 N ILE A 228 20.201 23.176 -11.487 1.00 28.93 N ANISOU 431 N ILE A 228 2329 3874 4790 754 491 939 N ATOM 432 CA ILE A 228 20.560 23.367 -10.095 1.00 29.45 C ANISOU 432 CA ILE A 228 2289 4053 4848 805 655 884 C ATOM 433 C ILE A 228 20.045 24.664 -9.487 1.00 34.06 C ANISOU 433 C ILE A 228 2818 4667 5456 935 781 887 C ATOM 434 O ILE A 228 20.658 25.188 -8.561 1.00 35.53 O ANISOU 434 O ILE A 228 3000 4904 5595 979 939 785 O ATOM 435 CB ILE A 228 22.093 23.349 -9.909 1.00 35.61 C ANISOU 435 CB ILE A 228 3204 4813 5513 752 765 712 C ATOM 436 CG1 ILE A 228 22.730 24.540 -10.627 1.00 32.09 C ANISOU 436 CG1 ILE A 228 2953 4250 4990 776 827 605 C ATOM 437 CG2 ILE A 228 22.685 22.028 -10.380 1.00 32.06 C ANISOU 437 CG2 ILE A 228 2805 4341 5033 635 665 703 C ATOM 438 CD1 ILE A 228 24.200 24.661 -10.366 1.00 31.28 C ANISOU 438 CD1 ILE A 228 2971 4138 4778 733 945 452 C ATOM 439 N GLY A 229 18.923 25.173 -9.988 1.00 37.47 N ANISOU 439 N GLY A 229 3210 5069 5960 996 712 1007 N ATOM 440 CA GLY A 229 18.401 26.450 -9.528 1.00 40.27 C ANISOU 440 CA GLY A 229 3529 5435 6339 1129 829 1016 C ATOM 441 C GLY A 229 17.203 26.362 -8.590 1.00 44.67 C ANISOU 441 C GLY A 229 3857 6122 6993 1224 846 1165 C ATOM 442 O GLY A 229 17.027 27.225 -7.726 1.00 40.61 O ANISOU 442 O GLY A 229 3291 5659 6479 1340 990 1138 O ATOM 443 N ARG A 230 16.378 25.329 -8.769 1.00 43.05 N ANISOU 443 N ARG A 230 5256 5335 5765 931 923 1407 N ATOM 444 CA ARG A 230 15.204 25.091 -7.925 1.00 46.69 C ANISOU 444 CA ARG A 230 5575 5929 6237 1084 996 1659 C ATOM 445 C ARG A 230 15.338 23.786 -7.146 1.00 50.52 C ANISOU 445 C ARG A 230 5900 6491 6806 1044 937 1755 C ATOM 446 O ARG A 230 15.554 22.717 -7.728 1.00 50.30 O ANISOU 446 O ARG A 230 5778 6426 6908 888 797 1764 O ATOM 447 CB ARG A 230 13.932 25.055 -8.761 1.00 54.30 C ANISOU 447 CB ARG A 230 6412 6918 7300 1092 977 1860 C ATOM 448 CG ARG A 230 13.678 26.340 -9.546 1.00 67.87 C ANISOU 448 CG ARG A 230 8281 8571 8937 1143 1045 1775 C ATOM 449 CD ARG A 230 12.628 26.135 -10.631 1.00 77.35 C ANISOU 449 CD ARG A 230 9353 9766 10269 1092 995 1937 C ATOM 450 NE ARG A 230 12.943 25.022 -11.532 1.00 80.66 N ANISOU 450 NE ARG A 230 9682 10096 10868 887 818 1920 N ATOM 451 CZ ARG A 230 13.391 25.160 -12.780 1.00 84.68 C ANISOU 451 CZ ARG A 230 10272 10465 11438 765 737 1765 C ATOM 452 NH1 ARG A 230 13.587 26.371 -13.295 1.00 83.59 N ANISOU 452 NH1 ARG A 230 10290 10264 11208 804 816 1608 N ATOM 453 NH2 ARG A 230 13.639 24.080 -13.519 1.00 85.83 N ANISOU 453 NH2 ARG A 230 10354 10530 11726 613 567 1772 N ATOM 454 N LYS A 231 15.198 23.888 -5.828 1.00 48.11 N ANISOU 454 N LYS A 231 5580 6285 6413 1201 1039 1828 N ATOM 455 CA LYS A 231 15.395 22.762 -4.925 1.00 50.41 C ANISOU 455 CA LYS A 231 5734 6656 6763 1183 1003 1900 C ATOM 456 C LYS A 231 14.750 21.460 -5.387 1.00 46.25 C ANISOU 456 C LYS A 231 4989 6170 6416 1062 862 2095 C ATOM 457 O LYS A 231 15.346 20.395 -5.256 1.00 43.62 O ANISOU 457 O LYS A 231 4602 5822 6148 941 759 2049 O ATOM 458 CB LYS A 231 14.878 23.112 -3.537 1.00 51.72 C ANISOU 458 CB LYS A 231 5875 6949 6827 1417 1143 2035 C ATOM 459 CG LYS A 231 15.012 21.995 -2.510 1.00 52.57 C ANISOU 459 CG LYS A 231 5829 7150 6996 1419 1121 2119 C ATOM 460 CD LYS A 231 14.782 22.581 -1.141 1.00 55.95 C ANISOU 460 CD LYS A 231 6299 7672 7288 1674 1274 2186 C ATOM 461 CE LYS A 231 15.219 21.661 -0.038 1.00 63.70 C ANISOU 461 CE LYS A 231 7181 8718 8303 1681 1272 2192 C ATOM 462 NZ LYS A 231 15.110 22.375 1.271 1.00 69.47 N ANISOU 462 NZ LYS A 231 8002 9513 8882 1951 1425 2224 N ATOM 463 N ASP A 232 13.541 21.547 -5.931 1.00 40.21 N ANISOU 463 N ASP A 232 4109 5451 5718 1090 848 2318 N ATOM 464 CA ASP A 232 12.763 20.346 -6.227 1.00 44.83 C ANISOU 464 CA ASP A 232 4483 6087 6464 982 700 2563 C ATOM 465 C ASP A 232 13.242 19.610 -7.474 1.00 36.02 C ANISOU 465 C ASP A 232 3409 4818 5460 759 508 2459 C ATOM 466 O ASP A 232 13.453 18.400 -7.448 1.00 47.48 O ANISOU 466 O ASP A 232 4790 6254 6994 638 357 2503 O ATOM 467 CB ASP A 232 11.259 20.662 -6.307 1.00 57.72 C ANISOU 467 CB ASP A 232 5962 7848 8122 1089 745 2883 C ATOM 468 CG ASP A 232 10.971 22.012 -6.976 1.00 65.22 C ANISOU 468 CG ASP A 232 7048 8752 8981 1182 859 2810 C ATOM 469 OD1 ASP A 232 9.980 22.668 -6.579 1.00 63.97 O ANISOU 469 OD1 ASP A 232 6828 8732 8745 1371 985 3014 O ATOM 470 OD2 ASP A 232 11.731 22.418 -7.891 1.00 64.21 O ANISOU 470 OD2 ASP A 232 7089 8461 8847 1077 824 2558 O ATOM 471 N ASP A 233 13.423 20.336 -8.563 1.00 36.74 N ANISOU 471 N ASP A 233 3628 4790 5539 719 508 2321 N ATOM 472 CA ASP A 233 13.956 19.737 -9.783 1.00 38.16 C ANISOU 472 CA ASP A 233 3877 4817 5805 544 334 2206 C ATOM 473 C ASP A 233 15.370 19.216 -9.579 1.00 40.15 C ANISOU 473 C ASP A 233 4236 5013 6005 475 285 1971 C ATOM 474 O ASP A 233 15.769 18.206 -10.158 1.00 38.89 O ANISOU 474 O ASP A 233 4093 4776 5908 354 114 1945 O ATOM 475 CB ASP A 233 13.936 20.760 -10.904 1.00 38.28 C ANISOU 475 CB ASP A 233 4010 4729 5804 541 371 2088 C ATOM 476 CG ASP A 233 12.547 20.944 -11.484 1.00 50.17 C ANISOU 476 CG ASP A 233 5404 6261 7395 556 358 2332 C ATOM 477 OD1 ASP A 233 11.616 20.247 -11.013 1.00 46.49 O ANISOU 477 OD1 ASP A 233 4760 5903 7001 558 308 2612 O ATOM 478 OD2 ASP A 233 12.393 21.767 -12.421 1.00 55.75 O ANISOU 478 OD2 ASP A 233 6195 6889 8099 558 393 2254 O ATOM 479 N PHE A 234 16.130 19.926 -8.758 1.00 38.02 N ANISOU 479 N PHE A 234 4057 4784 5606 562 431 1807 N ATOM 480 CA PHE A 234 17.480 19.517 -8.448 1.00 34.89 C ANISOU 480 CA PHE A 234 3751 4363 5143 506 407 1602 C ATOM 481 C PHE A 234 17.458 18.179 -7.730 1.00 34.80 C ANISOU 481 C PHE A 234 3622 4416 5184 468 320 1708 C ATOM 482 O PHE A 234 18.268 17.296 -8.014 1.00 28.59 O ANISOU 482 O PHE A 234 2881 3584 4399 373 202 1611 O ATOM 483 CB PHE A 234 18.151 20.549 -7.558 1.00 36.05 C ANISOU 483 CB PHE A 234 4009 4547 5141 605 574 1452 C ATOM 484 CG PHE A 234 19.396 20.048 -6.902 1.00 36.82 C ANISOU 484 CG PHE A 234 4159 4663 5169 562 569 1298 C ATOM 485 CD1 PHE A 234 20.558 19.893 -7.630 1.00 34.40 C ANISOU 485 CD1 PHE A 234 3957 4292 4823 455 495 1116 C ATOM 486 CD2 PHE A 234 19.402 19.726 -5.558 1.00 34.21 C ANISOU 486 CD2 PHE A 234 3765 4427 4807 639 643 1347 C ATOM 487 CE1 PHE A 234 21.704 19.430 -7.027 1.00 35.38 C ANISOU 487 CE1 PHE A 234 4122 4454 4869 420 497 991 C ATOM 488 CE2 PHE A 234 20.539 19.261 -4.954 1.00 27.40 C ANISOU 488 CE2 PHE A 234 2947 3584 3879 597 644 1205 C ATOM 489 CZ PHE A 234 21.695 19.114 -5.688 1.00 37.11 C ANISOU 489 CZ PHE A 234 4281 4757 5062 484 573 1030 C ATOM 490 N LEU A 235 16.533 18.046 -6.788 1.00 36.25 N ANISOU 490 N LEU A 235 3658 4716 5397 558 379 1915 N ATOM 491 CA LEU A 235 16.321 16.779 -6.082 1.00 42.96 C ANISOU 491 CA LEU A 235 4371 5641 6312 521 288 2057 C ATOM 492 C LEU A 235 15.832 15.668 -7.014 1.00 38.63 C ANISOU 492 C LEU A 235 3768 5024 5887 374 56 2200 C ATOM 493 O LEU A 235 16.277 14.536 -6.918 1.00 39.79 O ANISOU 493 O LEU A 235 3917 5150 6052 286 -81 2184 O ATOM 494 CB LEU A 235 15.330 16.967 -4.928 1.00 40.93 C ANISOU 494 CB LEU A 235 3950 5542 6060 667 403 2285 C ATOM 495 CG LEU A 235 15.921 16.931 -3.519 1.00 53.25 C ANISOU 495 CG LEU A 235 5506 7190 7538 770 525 2206 C ATOM 496 CD1 LEU A 235 17.384 17.377 -3.491 1.00 50.30 C ANISOU 496 CD1 LEU A 235 5333 6730 7049 745 585 1884 C ATOM 497 CD2 LEU A 235 15.077 17.761 -2.561 1.00 58.97 C ANISOU 497 CD2 LEU A 235 6156 8045 8207 987 699 2367 C ATOM 498 N LYS A 236 14.920 16.005 -7.919 1.00 39.52 N ANISOU 498 N LYS A 236 3849 5093 6075 351 6 2340 N ATOM 499 CA LYS A 236 14.349 15.024 -8.829 1.00 39.37 C ANISOU 499 CA LYS A 236 3795 4991 6174 211 -230 2503 C ATOM 500 C LYS A 236 15.397 14.458 -9.793 1.00 40.34 C ANISOU 500 C LYS A 236 4103 4951 6274 108 -382 2292 C ATOM 501 O LYS A 236 15.373 13.275 -10.130 1.00 47.56 O ANISOU 501 O LYS A 236 5037 5797 7235 4 -600 2370 O ATOM 502 CB LYS A 236 13.192 15.642 -9.606 1.00 48.04 C ANISOU 502 CB LYS A 236 4831 6077 7347 215 -231 2687 C ATOM 503 CG LYS A 236 12.483 14.668 -10.532 1.00 61.53 C ANISOU 503 CG LYS A 236 6505 7690 9183 62 -490 2892 C ATOM 504 CD LYS A 236 11.262 15.322 -11.162 1.00 77.49 C ANISOU 504 CD LYS A 236 8436 9730 11278 72 -468 3104 C ATOM 505 CE LYS A 236 10.593 14.417 -12.197 1.00 89.22 C ANISOU 505 CE LYS A 236 9917 11091 12892 -96 -745 3304 C ATOM 506 NZ LYS A 236 11.379 14.310 -13.462 1.00 93.29 N ANISOU 506 NZ LYS A 236 10656 11382 13410 -165 -867 3070 N ATOM 507 N LEU A 237 16.324 15.299 -10.230 1.00 27.49 N ANISOU 507 N LEU A 237 2621 3265 4559 148 -278 2036 N ATOM 508 CA LEU A 237 17.353 14.848 -11.155 1.00 30.60 C ANISOU 508 CA LEU A 237 3183 3533 4910 85 -404 1850 C ATOM 509 C LEU A 237 18.471 14.117 -10.421 1.00 32.46 C ANISOU 509 C LEU A 237 3471 3817 5046 85 -411 1713 C ATOM 510 O LEU A 237 18.999 13.113 -10.898 1.00 33.39 O ANISOU 510 O LEU A 237 3685 3863 5138 31 -584 1674 O ATOM 511 CB LEU A 237 17.926 16.032 -11.926 1.00 35.28 C ANISOU 511 CB LEU A 237 3893 4067 5446 123 -296 1654 C ATOM 512 CG LEU A 237 16.977 16.738 -12.893 1.00 34.88 C ANISOU 512 CG LEU A 237 3826 3943 5483 120 -300 1746 C ATOM 513 CD1 LEU A 237 17.752 17.789 -13.645 1.00 34.01 C ANISOU 513 CD1 LEU A 237 3847 3772 5304 148 -213 1524 C ATOM 514 CD2 LEU A 237 16.344 15.752 -13.862 1.00 35.61 C ANISOU 514 CD2 LEU A 237 3926 3915 5690 27 -539 1901 C ATOM 515 N SER A 238 18.821 14.629 -9.251 1.00 34.03 N ANISOU 515 N SER A 238 3620 4135 5176 157 -226 1644 N ATOM 516 CA SER A 238 19.874 14.034 -8.445 1.00 35.83 C ANISOU 516 CA SER A 238 3883 4423 5306 161 -204 1513 C ATOM 517 C SER A 238 19.579 12.579 -8.114 1.00 36.90 C ANISOU 517 C SER A 238 3963 4569 5487 101 -375 1648 C ATOM 518 O SER A 238 20.479 11.744 -8.128 1.00 35.74 O ANISOU 518 O SER A 238 3910 4408 5260 73 -461 1538 O ATOM 519 CB SER A 238 20.068 14.839 -7.162 1.00 32.80 C ANISOU 519 CB SER A 238 3447 4155 4860 253 16 1459 C ATOM 520 OG SER A 238 20.737 16.055 -7.450 1.00 36.46 O ANISOU 520 OG SER A 238 4023 4595 5237 288 140 1286 O ATOM 521 N THR A 239 18.313 12.292 -7.822 1.00 36.96 N ANISOU 521 N THR A 239 3820 4612 5613 84 -430 1899 N ATOM 522 CA THR A 239 17.860 10.952 -7.438 1.00 39.23 C ANISOU 522 CA THR A 239 4033 4917 5955 11 -610 2073 C ATOM 523 C THR A 239 17.452 10.122 -8.650 1.00 40.31 C ANISOU 523 C THR A 239 4261 4906 6151 -100 -886 2184 C ATOM 524 O THR A 239 16.863 9.051 -8.521 1.00 45.34 O ANISOU 524 O THR A 239 4851 5530 6846 -185 -1084 2376 O ATOM 525 CB THR A 239 16.638 11.004 -6.470 1.00 38.20 C ANISOU 525 CB THR A 239 3672 4923 5920 44 -551 2341 C ATOM 526 OG1 THR A 239 15.589 11.821 -7.028 1.00 40.22 O ANISOU 526 OG1 THR A 239 3853 5174 6255 65 -517 2504 O ATOM 527 CG2 THR A 239 17.049 11.551 -5.112 1.00 36.16 C ANISOU 527 CG2 THR A 239 3342 4804 5593 170 -313 2249 C ATOM 528 N ASN A 240 17.761 10.621 -9.833 1.00 39.95 N ANISOU 528 N ASN A 240 4354 4739 6088 -100 -912 2071 N ATOM 529 CA ASN A 240 17.357 9.936 -11.040 1.00 37.77 C ANISOU 529 CA ASN A 240 4186 4299 5864 -186 -1173 2173 C ATOM 530 C ASN A 240 18.527 9.236 -11.685 1.00 37.51 C ANISOU 530 C ASN A 240 4384 4163 5704 -178 -1304 1983 C ATOM 531 O ASN A 240 19.631 9.785 -11.755 1.00 36.89 O ANISOU 531 O ASN A 240 4390 4115 5513 -100 -1161 1750 O ATOM 532 CB ASN A 240 16.746 10.917 -12.034 1.00 36.00 C ANISOU 532 CB ASN A 240 3960 4000 5718 -180 -1134 2209 C ATOM 533 CG ASN A 240 16.228 10.223 -13.258 1.00 40.36 C ANISOU 533 CG ASN A 240 4625 4371 6340 -269 -1410 2336 C ATOM 534 OD1 ASN A 240 16.867 10.241 -14.317 1.00 42.59 O ANISOU 534 OD1 ASN A 240 5094 4518 6570 -246 -1486 2187 O ATOM 535 ND2 ASN A 240 15.079 9.553 -13.114 1.00 37.87 N ANISOU 535 ND2 ASN A 240 4202 4052 6134 -370 -1580 2628 N ATOM 536 N ILE A 241 18.271 8.030 -12.175 1.00 43.12 N ANISOU 536 N ILE A 241 5206 4755 6422 -252 -1589 2101 N ATOM 537 CA ILE A 241 19.313 7.170 -12.725 1.00 39.35 C ANISOU 537 CA ILE A 241 4973 4183 5794 -218 -1745 1954 C ATOM 538 C ILE A 241 20.132 7.845 -13.816 1.00 36.91 C ANISOU 538 C ILE A 241 4816 3801 5406 -128 -1689 1761 C ATOM 539 O ILE A 241 21.342 7.634 -13.909 1.00 43.24 O ANISOU 539 O ILE A 241 5756 4631 6043 -43 -1661 1576 O ATOM 540 CB ILE A 241 18.725 5.848 -13.257 1.00 43.09 C ANISOU 540 CB ILE A 241 5586 4500 6288 -310 -2101 2141 C ATOM 541 CG1 ILE A 241 19.807 5.028 -13.968 1.00 50.41 C ANISOU 541 CG1 ILE A 241 6813 5314 7026 -233 -2269 1987 C ATOM 542 CG2 ILE A 241 17.548 6.103 -14.170 1.00 37.24 C ANISOU 542 CG2 ILE A 241 4821 3626 5702 -391 -2239 2344 C ATOM 543 CD1 ILE A 241 19.392 3.594 -14.241 1.00 52.35 C ANISOU 543 CD1 ILE A 241 7241 5410 7241 -311 -2633 2151 C ATOM 544 N PHE A 242 19.470 8.646 -14.640 1.00 35.40 N ANISOU 544 N PHE A 242 4593 3530 5326 -142 -1672 1817 N ATOM 545 CA PHE A 242 20.141 9.384 -15.708 1.00 38.38 C ANISOU 545 CA PHE A 242 5091 3842 5650 -59 -1614 1650 C ATOM 546 C PHE A 242 20.432 10.810 -15.289 1.00 40.13 C ANISOU 546 C PHE A 242 5176 4194 5877 -16 -1312 1521 C ATOM 547 O PHE A 242 21.494 11.355 -15.587 1.00 39.69 O ANISOU 547 O PHE A 242 5195 4177 5710 59 -1204 1332 O ATOM 548 CB PHE A 242 19.279 9.408 -16.958 1.00 35.47 C ANISOU 548 CB PHE A 242 4793 3286 5396 -97 -1788 1774 C ATOM 549 CG PHE A 242 18.864 8.053 -17.414 1.00 44.12 C ANISOU 549 CG PHE A 242 6049 4221 6492 -153 -2121 1929 C ATOM 550 CD1 PHE A 242 19.815 7.052 -17.585 1.00 45.60 C ANISOU 550 CD1 PHE A 242 6460 4360 6504 -82 -2274 1836 C ATOM 551 CD2 PHE A 242 17.531 7.766 -17.656 1.00 46.03 C ANISOU 551 CD2 PHE A 242 6232 4365 6893 -277 -2291 2183 C ATOM 552 CE1 PHE A 242 19.444 5.789 -18.004 1.00 44.93 C ANISOU 552 CE1 PHE A 242 6536 4135 6400 -168 -2572 1911 C ATOM 553 CE2 PHE A 242 17.147 6.501 -18.072 1.00 49.89 C ANISOU 553 CE2 PHE A 242 6862 4719 7376 -383 -2604 2279 C ATOM 554 CZ PHE A 242 18.103 5.509 -18.246 1.00 49.31 C ANISOU 554 CZ PHE A 242 7022 4590 7124 -332 -2747 2128 C ATOM 555 N GLY A 243 19.473 11.400 -14.585 1.00 38.62 N ANISOU 555 N GLY A 243 4794 4078 5802 -59 -1189 1643 N ATOM 556 CA GLY A 243 19.549 12.786 -14.172 1.00 33.76 C ANISOU 556 CA GLY A 243 4075 3565 5187 -14 -925 1550 C ATOM 557 C GLY A 243 20.779 13.161 -13.373 1.00 34.01 C ANISOU 557 C GLY A 243 4122 3723 5076 44 -750 1352 C ATOM 558 O GLY A 243 21.284 14.281 -13.502 1.00 35.00 O ANISOU 558 O GLY A 243 4263 3883 5154 84 -591 1216 O ATOM 559 N ASN A 244 21.267 12.233 -12.553 1.00 32.24 N ANISOU 559 N ASN A 244 3901 3567 4780 40 -788 1342 N ATOM 560 CA ASN A 244 22.333 12.561 -11.626 1.00 25.98 C ANISOU 560 CA ASN A 244 3101 2906 3862 83 -615 1181 C ATOM 561 C ASN A 244 23.606 12.944 -12.358 1.00 30.63 C ANISOU 561 C ASN A 244 3825 3494 4317 126 -588 994 C ATOM 562 O ASN A 244 24.375 13.767 -11.868 1.00 41.23 O ANISOU 562 O ASN A 244 5157 4933 5578 148 -419 869 O ATOM 563 CB ASN A 244 22.585 11.432 -10.617 1.00 24.70 C ANISOU 563 CB ASN A 244 2914 2819 3652 71 -663 1207 C ATOM 564 CG ASN A 244 23.259 10.225 -11.239 1.00 29.85 C ANISOU 564 CG ASN A 244 3730 3410 4201 75 -864 1169 C ATOM 565 OD1 ASN A 244 24.485 10.121 -11.251 1.00 28.67 O ANISOU 565 OD1 ASN A 244 3678 3321 3896 126 -821 1014 O ATOM 566 ND2 ASN A 244 22.460 9.308 -11.770 1.00 29.77 N ANISOU 566 ND2 ASN A 244 3767 3282 4264 27 -1094 1325 N ATOM 567 N TYR A 245 23.817 12.362 -13.538 1.00 30.35 N ANISOU 567 N TYR A 245 3924 3353 4255 143 -765 993 N ATOM 568 CA TYR A 245 24.985 12.702 -14.353 1.00 28.77 C ANISOU 568 CA TYR A 245 3842 3166 3922 205 -751 848 C ATOM 569 C TYR A 245 24.925 14.133 -14.879 1.00 31.12 C ANISOU 569 C TYR A 245 4106 3453 4266 204 -623 789 C ATOM 570 O TYR A 245 25.955 14.811 -14.946 1.00 35.18 O ANISOU 570 O TYR A 245 4647 4052 4669 229 -521 666 O ATOM 571 CB TYR A 245 25.145 11.748 -15.529 1.00 27.65 C ANISOU 571 CB TYR A 245 3869 2904 3733 258 -979 876 C ATOM 572 CG TYR A 245 25.533 10.345 -15.156 1.00 30.33 C ANISOU 572 CG TYR A 245 4305 3259 3961 285 -1120 899 C ATOM 573 CD1 TYR A 245 26.860 9.994 -14.970 1.00 35.92 C ANISOU 573 CD1 TYR A 245 5095 4088 4464 366 -1083 785 C ATOM 574 CD2 TYR A 245 24.573 9.366 -15.012 1.00 32.81 C ANISOU 574 CD2 TYR A 245 4635 3470 4361 228 -1300 1047 C ATOM 575 CE1 TYR A 245 27.214 8.701 -14.635 1.00 39.62 C ANISOU 575 CE1 TYR A 245 5672 4572 4810 403 -1211 800 C ATOM 576 CE2 TYR A 245 24.912 8.083 -14.675 1.00 37.70 C ANISOU 576 CE2 TYR A 245 5364 4093 4867 248 -1446 1066 C ATOM 577 CZ TYR A 245 26.225 7.745 -14.492 1.00 39.97 C ANISOU 577 CZ TYR A 245 5747 4496 4944 343 -1398 933 C ATOM 578 OH TYR A 245 26.540 6.448 -14.163 1.00 44.62 O ANISOU 578 OH TYR A 245 6464 5087 5403 374 -1545 948 O ATOM 579 N LEU A 246 23.725 14.580 -15.261 1.00 28.45 N ANISOU 579 N LEU A 246 3712 3015 4083 170 -638 888 N ATOM 580 CA LEU A 246 23.532 15.953 -15.725 1.00 30.04 C ANISOU 580 CA LEU A 246 3887 3198 4328 169 -516 835 C ATOM 581 C LEU A 246 23.759 16.944 -14.591 1.00 32.09 C ANISOU 581 C LEU A 246 4073 3579 4542 160 -308 772 C ATOM 582 O LEU A 246 24.370 17.990 -14.785 1.00 36.91 O ANISOU 582 O LEU A 246 4717 4222 5087 165 -208 662 O ATOM 583 CB LEU A 246 22.135 16.141 -16.307 1.00 27.30 C ANISOU 583 CB LEU A 246 3493 2732 4148 141 -572 971 C ATOM 584 CG LEU A 246 21.945 17.478 -17.015 1.00 36.97 C ANISOU 584 CG LEU A 246 4720 3917 5409 150 -471 906 C ATOM 585 CD1 LEU A 246 22.955 17.655 -18.154 1.00 29.33 C ANISOU 585 CD1 LEU A 246 3869 2909 4365 191 -525 777 C ATOM 586 CD2 LEU A 246 20.513 17.599 -17.534 1.00 43.67 C ANISOU 586 CD2 LEU A 246 5513 4663 6418 124 -520 1057 C ATOM 587 N VAL A 247 23.269 16.606 -13.400 1.00 20.21 N ANISOU 587 N VAL A 247 2478 2137 3064 151 -256 850 N ATOM 588 CA VAL A 247 23.538 17.428 -12.232 1.00 21.45 C ANISOU 588 CA VAL A 247 2593 2399 3159 165 -74 793 C ATOM 589 C VAL A 247 25.037 17.582 -11.941 1.00 25.14 C ANISOU 589 C VAL A 247 3131 2954 3466 161 -20 639 C ATOM 590 O VAL A 247 25.523 18.679 -11.635 1.00 25.19 O ANISOU 590 O VAL A 247 3169 3001 3401 156 99 552 O ATOM 591 CB VAL A 247 22.833 16.861 -11.004 1.00 28.34 C ANISOU 591 CB VAL A 247 3355 3331 4081 176 -41 913 C ATOM 592 CG1 VAL A 247 23.179 17.685 -9.769 1.00 24.27 C ANISOU 592 CG1 VAL A 247 2825 2911 3486 215 141 847 C ATOM 593 CG2 VAL A 247 21.316 16.834 -11.245 1.00 26.50 C ANISOU 593 CG2 VAL A 247 3028 3044 3997 177 -85 1104 C ATOM 594 N GLN A 248 25.781 16.487 -12.048 1.00 20.31 N ANISOU 594 N GLN A 248 2558 2376 2784 164 -118 615 N ATOM 595 CA GLN A 248 27.212 16.541 -11.775 1.00 18.64 C ANISOU 595 CA GLN A 248 2399 2276 2409 164 -68 497 C ATOM 596 C GLN A 248 27.967 17.404 -12.800 1.00 24.12 C ANISOU 596 C GLN A 248 3162 2971 3032 161 -67 419 C ATOM 597 O GLN A 248 28.875 18.143 -12.444 1.00 34.35 O ANISOU 597 O GLN A 248 4475 4356 4219 133 22 344 O ATOM 598 CB GLN A 248 27.786 15.124 -11.698 1.00 18.19 C ANISOU 598 CB GLN A 248 2377 2264 2272 190 -174 502 C ATOM 599 CG GLN A 248 27.121 14.277 -10.618 1.00 26.23 C ANISOU 599 CG GLN A 248 3319 3294 3353 180 -180 578 C ATOM 600 CD GLN A 248 27.648 12.852 -10.604 1.00 26.31 C ANISOU 600 CD GLN A 248 3390 3335 3272 206 -304 579 C ATOM 601 OE1 GLN A 248 28.837 12.631 -10.462 1.00 27.15 O ANISOU 601 OE1 GLN A 248 3551 3546 3219 232 -273 490 O ATOM 602 NE2 GLN A 248 26.760 11.888 -10.762 1.00 21.66 N ANISOU 602 NE2 GLN A 248 2802 2657 2771 198 -454 693 N ATOM 603 N SER A 249 27.572 17.313 -14.066 1.00 23.99 N ANISOU 603 N SER A 249 3185 2852 3080 186 -175 449 N ATOM 604 CA SER A 249 28.173 18.092 -15.135 1.00 22.59 C ANISOU 604 CA SER A 249 3059 2670 2853 195 -184 390 C ATOM 605 C SER A 249 27.896 19.551 -14.957 1.00 22.78 C ANISOU 605 C SER A 249 3066 2680 2910 145 -65 351 C ATOM 606 O SER A 249 28.776 20.376 -15.174 1.00 26.70 O ANISOU 606 O SER A 249 3595 3241 3310 117 -24 285 O ATOM 607 CB SER A 249 27.591 17.680 -16.484 1.00 25.61 C ANISOU 607 CB SER A 249 3489 2918 3324 244 -325 438 C ATOM 608 OG SER A 249 28.095 16.421 -16.867 1.00 35.61 O ANISOU 608 OG SER A 249 4828 4193 4510 314 -460 461 O ATOM 609 N VAL A 250 26.659 19.878 -14.589 1.00 21.40 N ANISOU 609 N VAL A 250 2847 2424 2859 138 -19 407 N ATOM 610 CA VAL A 250 26.271 21.286 -14.467 1.00 23.53 C ANISOU 610 CA VAL A 250 3131 2667 3143 116 88 375 C ATOM 611 C VAL A 250 26.905 21.914 -13.245 1.00 24.82 C ANISOU 611 C VAL A 250 3318 2922 3191 88 200 321 C ATOM 612 O VAL A 250 27.275 23.079 -13.267 1.00 33.04 O ANISOU 612 O VAL A 250 4425 3965 4162 54 253 259 O ATOM 613 CB VAL A 250 24.737 21.482 -14.444 1.00 24.21 C ANISOU 613 CB VAL A 250 3167 2662 3371 143 113 472 C ATOM 614 CG1 VAL A 250 24.369 22.945 -14.139 1.00 22.12 C ANISOU 614 CG1 VAL A 250 2944 2382 3077 149 237 436 C ATOM 615 CG2 VAL A 250 24.139 21.056 -15.775 1.00 20.49 C ANISOU 615 CG2 VAL A 250 2692 2080 3014 153 -6 523 C ATOM 616 N ILE A 251 27.036 21.143 -12.174 1.00 27.68 N ANISOU 616 N ILE A 251 3639 3351 3529 99 225 347 N ATOM 617 CA ILE A 251 27.811 21.589 -11.020 1.00 24.46 C ANISOU 617 CA ILE A 251 3265 3029 3001 73 316 292 C ATOM 618 C ILE A 251 29.260 21.860 -11.450 1.00 27.38 C ANISOU 618 C ILE A 251 3690 3481 3233 11 284 218 C ATOM 619 O ILE A 251 29.839 22.876 -11.104 1.00 26.06 O ANISOU 619 O ILE A 251 3591 3340 2972 -43 331 172 O ATOM 620 CB ILE A 251 27.759 20.541 -9.897 1.00 28.60 C ANISOU 620 CB ILE A 251 3723 3613 3530 101 339 331 C ATOM 621 CG1 ILE A 251 26.369 20.546 -9.256 1.00 30.55 C ANISOU 621 CG1 ILE A 251 3906 3811 3891 164 391 429 C ATOM 622 CG2 ILE A 251 28.857 20.772 -8.866 1.00 23.08 C ANISOU 622 CG2 ILE A 251 3065 3012 2694 65 409 262 C ATOM 623 CD1 ILE A 251 26.136 19.392 -8.267 1.00 31.68 C ANISOU 623 CD1 ILE A 251 3958 4010 4067 193 393 492 C ATOM 624 N GLY A 252 29.839 20.967 -12.244 1.00 26.51 N ANISOU 624 N GLY A 252 3559 3416 3098 25 193 224 N ATOM 625 CA GLY A 252 31.172 21.210 -12.764 1.00 23.93 C ANISOU 625 CA GLY A 252 3265 3196 2633 -12 161 188 C ATOM 626 C GLY A 252 31.290 22.520 -13.526 1.00 29.15 C ANISOU 626 C GLY A 252 3973 3820 3283 -62 158 161 C ATOM 627 O GLY A 252 32.261 23.270 -13.364 1.00 33.97 O ANISOU 627 O GLY A 252 4619 4516 3771 -138 171 141 O ATOM 628 N ILE A 253 30.302 22.795 -14.370 1.00 25.63 N ANISOU 628 N ILE A 253 3529 3246 2961 -27 131 169 N ATOM 629 CA ILE A 253 30.299 24.001 -15.187 1.00 21.87 C ANISOU 629 CA ILE A 253 3100 2722 2488 -66 124 137 C ATOM 630 C ILE A 253 30.085 25.244 -14.318 1.00 26.77 C ANISOU 630 C ILE A 253 3796 3309 3067 -127 206 103 C ATOM 631 O ILE A 253 30.735 26.271 -14.520 1.00 29.90 O ANISOU 631 O ILE A 253 4258 3729 3373 -204 194 72 O ATOM 632 CB ILE A 253 29.230 23.895 -16.288 1.00 24.78 C ANISOU 632 CB ILE A 253 3453 2957 3007 -6 79 154 C ATOM 633 CG1 ILE A 253 29.608 22.756 -17.249 1.00 29.40 C ANISOU 633 CG1 ILE A 253 4012 3561 3599 65 -30 185 C ATOM 634 CG2 ILE A 253 29.095 25.202 -17.036 1.00 20.63 C ANISOU 634 CG2 ILE A 253 2977 2370 2491 -44 89 109 C ATOM 635 CD1 ILE A 253 28.423 22.220 -18.093 1.00 24.72 C ANISOU 635 CD1 ILE A 253 3410 2815 3166 130 -98 228 C ATOM 636 N SER A 254 29.198 25.136 -13.332 1.00 23.04 N ANISOU 636 N SER A 254 3323 2785 2646 -85 279 123 N ATOM 637 CA SER A 254 28.992 26.226 -12.395 1.00 24.23 C ANISOU 637 CA SER A 254 3576 2900 2730 -104 353 99 C ATOM 638 C SER A 254 30.265 26.606 -11.665 1.00 26.88 C ANISOU 638 C SER A 254 3980 3326 2908 -195 348 70 C ATOM 639 O SER A 254 30.560 27.789 -11.502 1.00 33.75 O ANISOU 639 O SER A 254 4977 4165 3684 -258 343 40 O ATOM 640 CB SER A 254 27.926 25.893 -11.362 1.00 25.98 C ANISOU 640 CB SER A 254 3771 3084 3014 -13 434 149 C ATOM 641 OG SER A 254 27.829 26.964 -10.441 1.00 38.56 O ANISOU 641 OG SER A 254 5497 4645 4511 -2 499 127 O ATOM 642 N LEU A 255 31.016 25.608 -11.211 1.00 26.11 N ANISOU 642 N LEU A 255 3811 3338 2771 -205 341 86 N ATOM 643 CA LEU A 255 32.274 25.870 -10.521 1.00 19.56 C ANISOU 643 CA LEU A 255 3030 2612 1789 -300 335 77 C ATOM 644 C LEU A 255 33.313 26.462 -11.456 1.00 31.63 C ANISOU 644 C LEU A 255 4576 4216 3226 -400 251 84 C ATOM 645 O LEU A 255 34.167 27.226 -11.020 1.00 38.51 O ANISOU 645 O LEU A 255 5529 5135 3970 -510 226 92 O ATOM 646 CB LEU A 255 32.811 24.601 -9.873 1.00 24.27 C ANISOU 646 CB LEU A 255 3538 3322 2363 -276 356 94 C ATOM 647 CG LEU A 255 31.959 24.093 -8.710 1.00 29.79 C ANISOU 647 CG LEU A 255 4217 3970 3131 -195 438 97 C ATOM 648 CD1 LEU A 255 32.475 22.736 -8.224 1.00 37.03 C ANISOU 648 CD1 LEU A 255 5041 4999 4030 -173 446 108 C ATOM 649 CD2 LEU A 255 31.918 25.121 -7.590 1.00 28.88 C ANISOU 649 CD2 LEU A 255 4231 3799 2944 -215 495 77 C ATOM 650 N ALA A 256 33.232 26.126 -12.746 1.00 27.91 N ANISOU 650 N ALA A 256 4034 3755 2817 -361 198 96 N ATOM 651 CA ALA A 256 34.203 26.636 -13.715 1.00 32.72 C ANISOU 651 CA ALA A 256 4636 4455 3342 -434 118 123 C ATOM 652 C ALA A 256 33.878 28.040 -14.174 1.00 37.03 C ANISOU 652 C ALA A 256 5280 4898 3891 -500 91 93 C ATOM 653 O ALA A 256 34.698 28.674 -14.821 1.00 42.35 O ANISOU 653 O ALA A 256 5961 5647 4484 -587 18 123 O ATOM 654 CB ALA A 256 34.354 25.681 -14.943 1.00 18.56 C ANISOU 654 CB ALA A 256 2740 2721 1590 -337 64 154 C ATOM 655 N THR A 257 32.695 28.534 -13.818 1.00 36.40 N ANISOU 655 N THR A 257 5280 4660 3892 -455 147 45 N ATOM 656 CA THR A 257 32.200 29.791 -14.366 1.00 30.72 C ANISOU 656 CA THR A 257 4666 3828 3179 -487 126 7 C ATOM 657 C THR A 257 32.205 30.923 -13.355 1.00 35.14 C ANISOU 657 C THR A 257 5411 4318 3623 -554 134 -15 C ATOM 658 O THR A 257 31.236 31.125 -12.621 1.00 33.17 O ANISOU 658 O THR A 257 5242 3963 3397 -468 208 -37 O ATOM 659 CB THR A 257 30.786 29.613 -14.926 1.00 30.88 C ANISOU 659 CB THR A 257 4655 3719 3358 -368 177 -18 C ATOM 660 OG1 THR A 257 30.768 28.459 -15.782 1.00 28.43 O ANISOU 660 OG1 THR A 257 4203 3450 3148 -301 148 10 O ATOM 661 CG2 THR A 257 30.354 30.862 -15.720 1.00 22.94 C ANISOU 661 CG2 THR A 257 3746 2613 2356 -395 155 -64 C ATOM 662 N ASN A 258 33.299 31.673 -13.336 1.00 41.95 N ANISOU 662 N ASN A 258 6350 5242 4346 -700 45 8 N ATOM 663 CA ASN A 258 33.513 32.690 -12.301 1.00 51.40 C ANISOU 663 CA ASN A 258 7757 6370 5402 -781 16 2 C ATOM 664 C ASN A 258 32.839 34.035 -12.562 1.00 44.53 C ANISOU 664 C ASN A 258 7085 5344 4491 -786 -15 -49 C ATOM 665 O ASN A 258 33.440 35.079 -12.330 1.00 45.89 O ANISOU 665 O ASN A 258 7434 5484 4517 -916 -118 -38 O ATOM 666 CB ASN A 258 35.012 32.908 -12.078 1.00 61.32 C ANISOU 666 CB ASN A 258 9025 7762 6513 -958 -90 75 C ATOM 667 CG ASN A 258 35.718 31.649 -11.633 1.00 74.63 C ANISOU 667 CG ASN A 258 10548 9608 8199 -945 -49 125 C ATOM 668 OD1 ASN A 258 35.394 31.083 -10.584 1.00 86.69 O ANISOU 668 OD1 ASN A 258 12087 11109 9743 -871 33 104 O ATOM 669 ND2 ASN A 258 36.689 31.198 -12.426 1.00 71.49 N ANISOU 669 ND2 ASN A 258 10000 9388 7774 -1001 -104 199 N ATOM 670 N ASP A 259 31.598 34.009 -13.039 1.00 39.06 N ANISOU 670 N ASP A 259 6371 4556 3915 -649 64 -96 N ATOM 671 CA ASP A 259 30.826 35.234 -13.232 1.00 35.00 C ANISOU 671 CA ASP A 259 6052 3895 3350 -619 57 -148 C ATOM 672 C ASP A 259 30.332 35.762 -11.895 1.00 40.30 C ANISOU 672 C ASP A 259 6943 4465 3903 -538 98 -156 C ATOM 673 O ASP A 259 30.687 35.236 -10.828 1.00 43.58 O ANISOU 673 O ASP A 259 7356 4920 4281 -527 123 -124 O ATOM 674 CB ASP A 259 29.641 35.008 -14.178 1.00 36.13 C ANISOU 674 CB ASP A 259 6093 3984 3652 -492 135 -180 C ATOM 675 CG ASP A 259 28.563 34.057 -13.589 1.00 65.59 C ANISOU 675 CG ASP A 259 9721 7703 7496 -321 265 -151 C ATOM 676 OD1 ASP A 259 27.406 34.098 -14.060 1.00 66.28 O ANISOU 676 OD1 ASP A 259 9780 7726 7678 -209 333 -156 O ATOM 677 OD2 ASP A 259 28.864 33.264 -12.670 1.00 61.89 O ANISOU 677 OD2 ASP A 259 9194 7299 7023 -303 294 -112 O ATOM 678 N ASP A 260 29.494 36.789 -11.961 1.00 40.46 N ANISOU 678 N ASP A 260 7160 4354 3857 -462 109 -198 N ATOM 679 CA ASP A 260 28.988 37.457 -10.773 1.00 54.04 C ANISOU 679 CA ASP A 260 9140 5967 5427 -350 137 -201 C ATOM 680 C ASP A 260 28.015 36.605 -9.942 1.00 53.12 C ANISOU 680 C ASP A 260 8925 5867 5390 -141 290 -161 C ATOM 681 O ASP A 260 27.929 36.773 -8.727 1.00 56.49 O ANISOU 681 O ASP A 260 9509 6252 5704 -52 315 -139 O ATOM 682 CB ASP A 260 28.315 38.768 -11.170 1.00 63.13 C ANISOU 682 CB ASP A 260 10537 6984 6465 -299 109 -252 C ATOM 683 CG ASP A 260 28.539 39.862 -10.158 1.00 72.25 C ANISOU 683 CG ASP A 260 12062 8017 7373 -293 22 -259 C ATOM 684 OD1 ASP A 260 29.696 40.327 -10.021 1.00 73.69 O ANISOU 684 OD1 ASP A 260 12366 8192 7442 -492 -137 -249 O ATOM 685 OD2 ASP A 260 27.550 40.262 -9.512 1.00 81.83 O ANISOU 685 OD2 ASP A 260 13454 9145 8494 -81 103 -259 O ATOM 686 N GLY A 261 27.283 35.705 -10.591 1.00 46.89 N ANISOU 686 N GLY A 261 7887 5137 4792 -64 382 -138 N ATOM 687 CA GLY A 261 26.334 34.860 -9.884 1.00 49.46 C ANISOU 687 CA GLY A 261 8094 5496 5205 116 510 -73 C ATOM 688 C GLY A 261 26.922 33.581 -9.299 1.00 43.82 C ANISOU 688 C GLY A 261 7189 4887 4573 79 525 -34 C ATOM 689 O GLY A 261 26.183 32.718 -8.808 1.00 43.69 O ANISOU 689 O GLY A 261 7034 4914 4654 205 617 31 O ATOM 690 N TYR A 262 28.247 33.463 -9.361 1.00 39.22 N ANISOU 690 N TYR A 262 6599 4357 3946 -95 431 -62 N ATOM 691 CA TYR A 262 28.968 32.275 -8.896 1.00 37.42 C ANISOU 691 CA TYR A 262 6202 4242 3773 -144 438 -34 C ATOM 692 C TYR A 262 28.589 31.963 -7.452 1.00 39.33 C ANISOU 692 C TYR A 262 6487 4476 3979 -16 522 0 C ATOM 693 O TYR A 262 28.152 30.874 -7.127 1.00 38.43 O ANISOU 693 O TYR A 262 6197 4426 3980 67 594 44 O ATOM 694 CB TYR A 262 30.481 32.511 -9.010 1.00 24.48 C ANISOU 694 CB TYR A 262 4604 2667 2031 -341 323 -49 C ATOM 695 CG TYR A 262 31.383 31.406 -8.472 1.00 38.47 C ANISOU 695 CG TYR A 262 6232 4569 3816 -396 329 -20 C ATOM 696 CD1 TYR A 262 31.989 30.490 -9.337 1.00 41.54 C ANISOU 696 CD1 TYR A 262 6419 5084 4280 -458 299 -2 C ATOM 697 CD2 TYR A 262 31.657 31.295 -7.112 1.00 40.61 C ANISOU 697 CD2 TYR A 262 6585 4838 4007 -374 362 -10 C ATOM 698 CE1 TYR A 262 32.826 29.487 -8.865 1.00 31.93 C ANISOU 698 CE1 TYR A 262 5086 3996 3048 -493 307 25 C ATOM 699 CE2 TYR A 262 32.489 30.297 -6.631 1.00 46.77 C ANISOU 699 CE2 TYR A 262 7236 5743 4793 -425 374 10 C ATOM 700 CZ TYR A 262 33.068 29.392 -7.513 1.00 45.36 C ANISOU 700 CZ TYR A 262 6858 5697 4679 -485 348 27 C ATOM 701 OH TYR A 262 33.887 28.395 -7.036 1.00 40.84 O ANISOU 701 OH TYR A 262 6172 5258 4089 -518 365 48 O ATOM 702 N THR A 263 28.753 32.953 -6.594 1.00 42.94 N ANISOU 702 N THR A 263 7199 4848 4268 5 500 -15 N ATOM 703 CA THR A 263 28.552 32.784 -5.171 1.00 43.20 C ANISOU 703 CA THR A 263 7311 4864 4240 132 567 14 C ATOM 704 C THR A 263 27.158 32.288 -4.829 1.00 44.47 C ANISOU 704 C THR A 263 7364 5035 4496 358 698 81 C ATOM 705 O THR A 263 27.011 31.299 -4.118 1.00 47.65 O ANISOU 705 O THR A 263 7615 5511 4977 427 767 126 O ATOM 706 CB THR A 263 28.803 34.102 -4.444 1.00 50.90 C ANISOU 706 CB THR A 263 8634 5708 4997 146 501 -8 C ATOM 707 OG1 THR A 263 30.169 34.490 -4.631 1.00 56.39 O ANISOU 707 OG1 THR A 263 9415 6409 5601 -89 362 -37 O ATOM 708 CG2 THR A 263 28.522 33.951 -2.951 1.00 54.73 C ANISOU 708 CG2 THR A 263 9219 6163 5412 316 574 26 C ATOM 709 N LYS A 264 26.142 32.989 -5.319 1.00 52.51 N ANISOU 709 N LYS A 264 8460 5993 5500 473 729 99 N ATOM 710 CA LYS A 264 24.760 32.612 -5.056 1.00 58.82 C ANISOU 710 CA LYS A 264 9150 6824 6375 690 850 198 C ATOM 711 C LYS A 264 24.525 31.176 -5.486 1.00 56.40 C ANISOU 711 C LYS A 264 8516 6627 6285 650 878 253 C ATOM 712 O LYS A 264 23.864 30.420 -4.785 1.00 60.76 O ANISOU 712 O LYS A 264 8934 7244 6907 778 957 349 O ATOM 713 CB LYS A 264 23.777 33.544 -5.773 1.00 68.46 C ANISOU 713 CB LYS A 264 10476 7982 7552 791 874 212 C ATOM 714 CG LYS A 264 23.653 34.935 -5.157 1.00 79.09 C ANISOU 714 CG LYS A 264 12182 9215 8655 913 862 186 C ATOM 715 CD LYS A 264 22.667 35.806 -5.933 1.00 86.87 C ANISOU 715 CD LYS A 264 13265 10153 9589 1019 893 197 C ATOM 716 CE LYS A 264 22.535 37.203 -5.325 1.00 92.65 C ANISOU 716 CE LYS A 264 14397 10763 10044 1161 868 171 C ATOM 717 NZ LYS A 264 23.766 38.021 -5.500 1.00 94.64 N ANISOU 717 NZ LYS A 264 14890 10902 10166 950 705 51 N ATOM 718 N ARG A 265 25.082 30.795 -6.631 1.00 43.73 N ANISOU 718 N ARG A 265 6794 5044 4778 478 802 202 N ATOM 719 CA ARG A 265 24.881 29.444 -7.124 1.00 33.62 C ANISOU 719 CA ARG A 265 5247 3844 3682 443 801 253 C ATOM 720 C ARG A 265 25.467 28.394 -6.183 1.00 34.64 C ANISOU 720 C ARG A 265 5274 4054 3833 426 813 267 C ATOM 721 O ARG A 265 24.819 27.395 -5.845 1.00 33.51 O ANISOU 721 O ARG A 265 4961 3970 3801 501 855 356 O ATOM 722 CB ARG A 265 25.489 29.274 -8.513 1.00 36.12 C ANISOU 722 CB ARG A 265 5495 4161 4067 287 707 192 C ATOM 723 CG ARG A 265 24.682 29.901 -9.632 1.00 36.35 C ANISOU 723 CG ARG A 265 5542 4125 4146 310 703 195 C ATOM 724 CD ARG A 265 25.128 29.402 -10.993 1.00 28.54 C ANISOU 724 CD ARG A 265 4436 3144 3262 193 617 160 C ATOM 725 NE ARG A 265 26.577 29.323 -11.130 1.00 33.73 N ANISOU 725 NE ARG A 265 5117 3852 3848 54 538 90 N ATOM 726 CZ ARG A 265 27.346 30.307 -11.592 1.00 35.17 C ANISOU 726 CZ ARG A 265 5427 4011 3927 -46 477 21 C ATOM 727 NH1 ARG A 265 26.812 31.456 -11.968 1.00 25.02 N ANISOU 727 NH1 ARG A 265 4275 2635 2595 -23 485 -9 N ATOM 728 NH2 ARG A 265 28.658 30.135 -11.691 1.00 33.90 N ANISOU 728 NH2 ARG A 265 5255 3928 3699 -170 404 -4 N ATOM 729 N GLN A 266 26.705 28.602 -5.775 1.00 34.49 N ANISOU 729 N GLN A 266 5354 4043 3705 318 769 189 N ATOM 730 CA GLN A 266 27.378 27.582 -4.988 1.00 43.86 C ANISOU 730 CA GLN A 266 6441 5315 4909 286 781 189 C ATOM 731 C GLN A 266 26.768 27.541 -3.594 1.00 45.90 C ANISOU 731 C GLN A 266 6732 5569 5138 450 876 244 C ATOM 732 O GLN A 266 26.697 26.487 -2.971 1.00 43.19 O ANISOU 732 O GLN A 266 6241 5299 4868 487 915 284 O ATOM 733 CB GLN A 266 28.884 27.838 -4.935 1.00 45.08 C ANISOU 733 CB GLN A 266 6685 5497 4946 122 710 111 C ATOM 734 CG GLN A 266 29.703 26.612 -4.550 1.00 52.22 C ANISOU 734 CG GLN A 266 7446 6517 5879 61 710 106 C ATOM 735 CD GLN A 266 31.188 26.919 -4.356 1.00 57.35 C ANISOU 735 CD GLN A 266 8182 7217 6391 -93 650 58 C ATOM 736 OE1 GLN A 266 31.596 28.086 -4.294 1.00 66.02 O ANISOU 736 OE1 GLN A 266 9466 8249 7369 -160 600 38 O ATOM 737 NE2 GLN A 266 32.001 25.871 -4.252 1.00 43.31 N ANISOU 737 NE2 GLN A 266 6277 5561 4619 -152 645 55 N ATOM 738 N GLU A 267 26.313 28.697 -3.119 1.00 51.98 N ANISOU 738 N GLU A 267 7706 6254 5791 562 908 252 N ATOM 739 CA GLU A 267 25.737 28.801 -1.784 1.00 55.16 C ANISOU 739 CA GLU A 267 8174 6648 6135 757 999 313 C ATOM 740 C GLU A 267 24.397 28.093 -1.765 1.00 54.58 C ANISOU 740 C GLU A 267 7897 6644 6196 914 1078 449 C ATOM 741 O GLU A 267 24.066 27.364 -0.827 1.00 56.57 O ANISOU 741 O GLU A 267 8036 6964 6493 1022 1143 523 O ATOM 742 CB GLU A 267 25.553 30.271 -1.400 1.00 58.66 C ANISOU 742 CB GLU A 267 8927 6972 6388 863 996 295 C ATOM 743 CG GLU A 267 24.457 30.526 -0.375 1.00 65.49 C ANISOU 743 CG GLU A 267 9859 7832 7192 1147 1103 401 C ATOM 744 CD GLU A 267 24.884 30.196 1.049 1.00 74.64 C ANISOU 744 CD GLU A 267 11065 8999 8296 1230 1143 404 C ATOM 745 OE1 GLU A 267 26.093 29.943 1.272 1.00 82.56 O ANISOU 745 OE1 GLU A 267 12091 9994 9282 1054 1083 312 O ATOM 746 OE2 GLU A 267 24.010 30.195 1.943 1.00 69.63 O ANISOU 746 OE2 GLU A 267 10439 8388 7628 1480 1238 508 O ATOM 747 N LYS A 268 23.633 28.322 -2.823 1.00 42.67 N ANISOU 747 N LYS A 268 6338 5124 4751 918 1066 491 N ATOM 748 CA LYS A 268 22.326 27.728 -2.977 1.00 38.21 C ANISOU 748 CA LYS A 268 5578 4628 4313 1039 1120 647 C ATOM 749 C LYS A 268 22.462 26.215 -3.065 1.00 45.56 C ANISOU 749 C LYS A 268 6256 5645 5411 944 1083 688 C ATOM 750 O LYS A 268 21.717 25.467 -2.437 1.00 52.12 O ANISOU 750 O LYS A 268 6929 6557 6319 1049 1130 824 O ATOM 751 CB LYS A 268 21.680 28.284 -4.231 1.00 34.00 C ANISOU 751 CB LYS A 268 5053 4052 3814 1019 1096 663 C ATOM 752 CG LYS A 268 20.491 27.528 -4.701 1.00 41.23 C ANISOU 752 CG LYS A 268 5739 5037 4888 1070 1112 826 C ATOM 753 CD LYS A 268 20.071 28.051 -6.062 1.00 47.35 C ANISOU 753 CD LYS A 268 6531 5755 5704 1012 1075 811 C ATOM 754 CE LYS A 268 19.466 29.430 -5.968 1.00 44.30 C ANISOU 754 CE LYS A 268 6345 5324 5163 1167 1148 820 C ATOM 755 NZ LYS A 268 18.803 29.775 -7.265 1.00 45.81 N ANISOU 755 NZ LYS A 268 6503 5481 5423 1131 1131 838 N ATOM 756 N LEU A 269 23.444 25.766 -3.825 1.00 44.55 N ANISOU 756 N LEU A 269 6100 5506 5321 752 993 580 N ATOM 757 CA LEU A 269 23.668 24.344 -4.002 1.00 41.97 C ANISOU 757 CA LEU A 269 5580 5248 5121 665 938 605 C ATOM 758 C LEU A 269 23.996 23.695 -2.649 1.00 42.21 C ANISOU 758 C LEU A 269 5564 5345 5130 717 991 616 C ATOM 759 O LEU A 269 23.564 22.581 -2.355 1.00 37.41 O ANISOU 759 O LEU A 269 4782 4806 4627 737 984 707 O ATOM 760 CB LEU A 269 24.795 24.144 -5.011 1.00 36.98 C ANISOU 760 CB LEU A 269 4972 4599 4481 487 839 483 C ATOM 761 CG LEU A 269 25.123 22.734 -5.478 1.00 45.15 C ANISOU 761 CG LEU A 269 5856 5686 5612 402 756 494 C ATOM 762 CD1 LEU A 269 23.926 22.080 -6.119 1.00 42.82 C ANISOU 762 CD1 LEU A 269 5424 5380 5467 434 710 628 C ATOM 763 CD2 LEU A 269 26.273 22.822 -6.462 1.00 50.19 C ANISOU 763 CD2 LEU A 269 6556 6318 6196 271 674 382 C ATOM 764 N LYS A 270 24.744 24.415 -1.823 1.00 39.96 N ANISOU 764 N LYS A 270 5446 5031 4705 736 1034 527 N ATOM 765 CA LYS A 270 25.097 23.935 -0.499 1.00 39.15 C ANISOU 765 CA LYS A 270 5325 4979 4573 795 1093 523 C ATOM 766 C LYS A 270 23.863 23.819 0.381 1.00 43.36 C ANISOU 766 C LYS A 270 5776 5553 5146 1007 1183 677 C ATOM 767 O LYS A 270 23.706 22.832 1.109 1.00 42.43 O ANISOU 767 O LYS A 270 5506 5516 5101 1048 1210 737 O ATOM 768 CB LYS A 270 26.132 24.852 0.151 1.00 34.58 C ANISOU 768 CB LYS A 270 4972 4338 3827 767 1103 407 C ATOM 769 CG LYS A 270 26.458 24.491 1.581 1.00 38.38 C ANISOU 769 CG LYS A 270 5461 4850 4270 848 1172 400 C ATOM 770 CD LYS A 270 25.553 25.235 2.570 1.00 43.08 C ANISOU 770 CD LYS A 270 6169 5403 4795 1090 1261 486 C ATOM 771 CE LYS A 270 25.987 26.692 2.748 1.00 39.89 C ANISOU 771 CE LYS A 270 6082 4871 4204 1111 1237 414 C ATOM 772 NZ LYS A 270 24.967 27.532 3.464 1.00 42.71 N ANISOU 772 NZ LYS A 270 6587 5177 4462 1383 1310 509 N ATOM 773 N ASN A 271 23.002 24.832 0.313 1.00 42.09 N ANISOU 773 N ASN A 271 5717 5350 4925 1151 1228 748 N ATOM 774 CA ASN A 271 21.723 24.812 1.020 1.00 45.15 C ANISOU 774 CA ASN A 271 6019 5804 5331 1381 1317 932 C ATOM 775 C ASN A 271 20.820 23.654 0.621 1.00 40.85 C ANISOU 775 C ASN A 271 5190 5362 4968 1362 1289 1098 C ATOM 776 O ASN A 271 20.199 23.044 1.488 1.00 38.74 O ANISOU 776 O ASN A 271 4776 5194 4750 1489 1340 1241 O ATOM 777 CB ASN A 271 20.952 26.125 0.825 1.00 45.14 C ANISOU 777 CB ASN A 271 6190 5750 5211 1542 1364 986 C ATOM 778 CG ASN A 271 21.549 27.280 1.612 1.00 50.30 C ANISOU 778 CG ASN A 271 7152 6302 5657 1640 1394 882 C ATOM 779 OD1 ASN A 271 22.344 27.077 2.531 1.00 54.45 O ANISOU 779 OD1 ASN A 271 7740 6812 6136 1630 1402 808 O ATOM 780 ND2 ASN A 271 21.172 28.502 1.247 1.00 47.29 N ANISOU 780 ND2 ASN A 271 6984 5843 5141 1730 1400 877 N ATOM 781 N PHE A 272 20.731 23.374 -0.683 1.00 37.04 N ANISOU 781 N PHE A 272 4639 4856 4580 1208 1196 1090 N ATOM 782 CA PHE A 272 19.831 22.339 -1.193 1.00 40.56 C ANISOU 782 CA PHE A 272 4848 5373 5191 1172 1136 1261 C ATOM 783 C PHE A 272 20.231 20.988 -0.621 1.00 48.29 C ANISOU 783 C PHE A 272 5679 6417 6252 1100 1091 1270 C ATOM 784 O PHE A 272 19.417 20.266 -0.053 1.00 51.15 O ANISOU 784 O PHE A 272 5863 6877 6697 1176 1099 1452 O ATOM 785 CB PHE A 272 19.885 22.244 -2.722 1.00 36.06 C ANISOU 785 CB PHE A 272 4273 4733 4697 1006 1024 1217 C ATOM 786 CG PHE A 272 19.191 23.373 -3.440 1.00 40.77 C ANISOU 786 CG PHE A 272 4958 5279 5252 1071 1058 1251 C ATOM 787 CD1 PHE A 272 18.406 24.285 -2.745 1.00 43.40 C ANISOU 787 CD1 PHE A 272 5356 5649 5484 1283 1177 1352 C ATOM 788 CD2 PHE A 272 19.300 23.496 -4.826 1.00 33.25 C ANISOU 788 CD2 PHE A 272 4031 4248 4353 937 971 1187 C ATOM 789 CE1 PHE A 272 17.759 25.318 -3.411 1.00 44.37 C ANISOU 789 CE1 PHE A 272 5574 5733 5551 1353 1211 1381 C ATOM 790 CE2 PHE A 272 18.675 24.523 -5.500 1.00 38.64 C ANISOU 790 CE2 PHE A 272 4795 4885 5000 993 1006 1208 C ATOM 791 CZ PHE A 272 17.890 25.440 -4.794 1.00 43.23 C ANISOU 791 CZ PHE A 272 5446 5507 5473 1198 1127 1304 C ATOM 792 N ILE A 273 21.501 20.654 -0.793 1.00 54.30 N ANISOU 792 N ILE A 273 6515 7136 6982 954 1039 1082 N ATOM 793 CA ILE A 273 22.015 19.370 -0.360 1.00 51.92 C ANISOU 793 CA ILE A 273 6101 6890 6735 876 990 1062 C ATOM 794 C ILE A 273 21.951 19.248 1.169 1.00 50.81 C ANISOU 794 C ILE A 273 5922 6822 6562 1017 1098 1101 C ATOM 795 O ILE A 273 21.553 18.210 1.702 1.00 43.11 O ANISOU 795 O ILE A 273 4777 5929 5674 1034 1079 1210 O ATOM 796 CB ILE A 273 23.451 19.159 -0.875 1.00 42.36 C ANISOU 796 CB ILE A 273 4995 5637 5461 715 929 858 C ATOM 797 CG1 ILE A 273 23.483 19.252 -2.405 1.00 35.40 C ANISOU 797 CG1 ILE A 273 4148 4690 4613 603 821 832 C ATOM 798 CG2 ILE A 273 23.988 17.814 -0.433 1.00 45.51 C ANISOU 798 CG2 ILE A 273 5298 6102 5892 650 882 833 C ATOM 799 CD1 ILE A 273 24.861 19.028 -2.994 1.00 30.01 C ANISOU 799 CD1 ILE A 273 3553 3993 3854 470 757 665 C ATOM 800 N SER A 274 22.337 20.311 1.867 1.00 44.56 N ANISOU 800 N SER A 274 5298 5991 5640 1120 1200 1018 N ATOM 801 CA SER A 274 22.290 20.299 3.321 1.00 48.85 C ANISOU 801 CA SER A 274 5835 6585 6141 1280 1305 1049 C ATOM 802 C SER A 274 20.927 19.850 3.821 1.00 53.30 C ANISOU 802 C SER A 274 6198 7258 6796 1443 1342 1295 C ATOM 803 O SER A 274 20.823 18.935 4.642 1.00 58.76 O ANISOU 803 O SER A 274 6739 8036 7551 1479 1357 1361 O ATOM 804 CB SER A 274 22.616 21.680 3.890 1.00 46.27 C ANISOU 804 CB SER A 274 5757 6176 5648 1404 1389 967 C ATOM 805 OG SER A 274 24.012 21.903 3.911 1.00 49.14 O ANISOU 805 OG SER A 274 6277 6470 5922 1260 1362 765 O ATOM 806 N SER A 275 19.881 20.485 3.305 1.00 41.95 N ANISOU 806 N SER A 275 4749 5829 5360 1539 1353 1443 N ATOM 807 CA SER A 275 18.533 20.293 3.832 1.00 42.94 C ANISOU 807 CA SER A 275 4694 6083 5538 1730 1405 1715 C ATOM 808 C SER A 275 17.989 18.902 3.546 1.00 42.08 C ANISOU 808 C SER A 275 4317 6069 5602 1610 1297 1876 C ATOM 809 O SER A 275 16.915 18.536 4.020 1.00 44.94 O ANISOU 809 O SER A 275 4486 6563 6025 1736 1317 2132 O ATOM 810 CB SER A 275 17.585 21.350 3.253 1.00 39.00 C ANISOU 810 CB SER A 275 4260 5579 4979 1856 1444 1836 C ATOM 811 OG SER A 275 17.518 21.216 1.845 1.00 37.99 O ANISOU 811 OG SER A 275 4109 5393 4932 1660 1333 1812 O ATOM 812 N GLN A 276 18.723 18.130 2.762 1.00 42.47 N ANISOU 812 N GLN A 276 4364 6054 5718 1374 1171 1744 N ATOM 813 CA GLN A 276 18.263 16.804 2.380 1.00 47.95 C ANISOU 813 CA GLN A 276 4856 6805 6559 1243 1031 1886 C ATOM 814 C GLN A 276 19.403 15.800 2.501 1.00 41.46 C ANISOU 814 C GLN A 276 4055 5952 5745 1088 958 1705 C ATOM 815 O GLN A 276 19.366 14.725 1.907 1.00 41.33 O ANISOU 815 O GLN A 276 3958 5930 5814 937 805 1747 O ATOM 816 CB GLN A 276 17.741 16.838 0.939 1.00 51.02 C ANISOU 816 CB GLN A 276 5237 7133 7015 1120 909 1956 C ATOM 817 CG GLN A 276 16.531 17.727 0.742 1.00 56.95 C ANISOU 817 CG GLN A 276 5947 7933 7760 1265 976 2159 C ATOM 818 CD GLN A 276 15.243 17.114 1.293 1.00 61.07 C ANISOU 818 CD GLN A 276 6213 8618 8371 1358 961 2496 C ATOM 819 OE1 GLN A 276 15.193 15.924 1.618 1.00 64.94 O ANISOU 819 OE1 GLN A 276 6553 9166 8956 1269 861 2585 O ATOM 820 NE2 GLN A 276 14.188 17.928 1.387 1.00 55.02 N ANISOU 820 NE2 GLN A 276 5400 7939 7565 1540 1055 2699 N ATOM 821 N MET A 277 20.418 16.165 3.276 1.00 38.77 N ANISOU 821 N MET A 277 5219 4329 5183 1049 1000 2037 N ATOM 822 CA MET A 277 21.640 15.381 3.358 1.00 40.13 C ANISOU 822 CA MET A 277 5434 4525 5288 952 917 1794 C ATOM 823 C MET A 277 21.397 13.871 3.438 1.00 41.04 C ANISOU 823 C MET A 277 5419 4704 5472 908 799 1860 C ATOM 824 O MET A 277 21.832 13.114 2.569 1.00 45.87 O ANISOU 824 O MET A 277 5992 5347 6090 749 643 1777 O ATOM 825 CB MET A 277 22.508 15.850 4.524 1.00 40.79 C ANISOU 825 CB MET A 277 5662 4568 5268 1077 1018 1605 C ATOM 826 CG MET A 277 23.934 15.249 4.516 1.00 44.94 C ANISOU 826 CG MET A 277 6258 5098 5718 960 933 1313 C ATOM 827 SD MET A 277 24.946 15.724 3.074 1.00 48.27 S ANISOU 827 SD MET A 277 6736 5523 6083 735 839 1125 S ATOM 828 CE MET A 277 24.813 17.509 3.152 1.00125.32 C ANISOU 828 CE MET A 277 16619 15196 15800 824 958 1163 C ATOM 829 N THR A 278 20.682 13.443 4.466 1.00 42.91 N ANISOU 829 N THR A 278 5585 4964 5753 1056 862 2019 N ATOM 830 CA THR A 278 20.537 12.019 4.747 1.00 43.43 C ANISOU 830 CA THR A 278 5539 5091 5874 1025 741 2072 C ATOM 831 C THR A 278 19.837 11.288 3.624 1.00 42.45 C ANISOU 831 C THR A 278 5274 4991 5864 897 570 2249 C ATOM 832 O THR A 278 20.253 10.202 3.210 1.00 47.40 O ANISOU 832 O THR A 278 5857 5654 6499 780 385 2171 O ATOM 833 CB THR A 278 19.748 11.791 6.035 1.00 44.56 C ANISOU 833 CB THR A 278 5619 5261 6051 1213 851 2257 C ATOM 834 OG1 THR A 278 20.305 12.599 7.076 1.00 49.93 O ANISOU 834 OG1 THR A 278 6448 5897 6625 1364 1014 2111 O ATOM 835 CG2 THR A 278 19.817 10.335 6.442 1.00 47.74 C ANISOU 835 CG2 THR A 278 5929 5722 6488 1169 712 2267 C ATOM 836 N ASP A 279 18.770 11.895 3.131 1.00 39.64 N ANISOU 836 N ASP A 279 4856 4607 5598 929 620 2486 N ATOM 837 CA ASP A 279 17.994 11.306 2.060 1.00 46.88 C ANISOU 837 CA ASP A 279 5651 5517 6645 826 460 2682 C ATOM 838 C ASP A 279 18.864 11.120 0.831 1.00 45.65 C ANISOU 838 C ASP A 279 5558 5347 6441 645 306 2482 C ATOM 839 O ASP A 279 18.815 10.074 0.190 1.00 44.20 O ANISOU 839 O ASP A 279 5300 5181 6313 551 102 2520 O ATOM 840 CB ASP A 279 16.786 12.185 1.745 1.00 65.74 C ANISOU 840 CB ASP A 279 7992 7855 9132 892 559 2935 C ATOM 841 CG ASP A 279 15.980 12.530 2.990 1.00 84.03 C ANISOU 841 CG ASP A 279 10258 10202 11469 1096 738 3118 C ATOM 842 OD1 ASP A 279 16.430 13.409 3.763 1.00 89.92 O ANISOU 842 OD1 ASP A 279 11121 10944 12100 1211 900 2984 O ATOM 843 OD2 ASP A 279 14.904 11.920 3.197 1.00 86.96 O ANISOU 843 OD2 ASP A 279 10472 10600 11970 1150 709 3402 O ATOM 844 N MET A 280 19.673 12.133 0.519 1.00 42.94 N ANISOU 844 N MET A 280 5350 4976 5990 605 394 2275 N ATOM 845 CA MET A 280 20.564 12.080 -0.638 1.00 38.52 C ANISOU 845 CA MET A 280 4853 4417 5366 440 274 2080 C ATOM 846 C MET A 280 21.687 11.056 -0.481 1.00 34.79 C ANISOU 846 C MET A 280 4399 4012 4807 374 147 1844 C ATOM 847 O MET A 280 21.987 10.318 -1.421 1.00 33.94 O ANISOU 847 O MET A 280 4265 3933 4699 260 -36 1790 O ATOM 848 CB MET A 280 21.125 13.467 -0.953 1.00 35.48 C ANISOU 848 CB MET A 280 4599 3992 4889 413 399 1940 C ATOM 849 CG MET A 280 20.054 14.419 -1.503 1.00 31.66 C ANISOU 849 CG MET A 280 4101 3437 4490 431 463 2150 C ATOM 850 SD MET A 280 20.744 15.969 -2.084 1.00 42.35 S ANISOU 850 SD MET A 280 5607 4745 5737 360 550 1984 S ATOM 851 CE MET A 280 21.316 15.517 -3.716 1.00 37.35 C ANISOU 851 CE MET A 280 4977 4127 5087 148 376 1883 C ATOM 852 N CYS A 281 22.285 10.993 0.706 1.00 33.82 N ANISOU 852 N CYS A 281 4328 3909 4613 454 235 1704 N ATOM 853 CA CYS A 281 23.346 10.010 0.964 1.00 36.14 C ANISOU 853 CA CYS A 281 4645 4257 4828 395 113 1467 C ATOM 854 C CYS A 281 22.826 8.597 0.755 1.00 37.66 C ANISOU 854 C CYS A 281 4711 4496 5103 360 -103 1593 C ATOM 855 O CYS A 281 23.460 7.789 0.080 1.00 42.72 O ANISOU 855 O CYS A 281 5347 5183 5702 254 -295 1451 O ATOM 856 CB CYS A 281 23.909 10.144 2.383 1.00 27.49 C ANISOU 856 CB CYS A 281 3628 3148 3667 503 241 1326 C ATOM 857 SG CYS A 281 24.802 11.684 2.702 1.00 42.60 S ANISOU 857 SG CYS A 281 5719 4995 5473 545 440 1130 S ATOM 858 N LEU A 282 21.657 8.307 1.324 1.00 34.51 N ANISOU 858 N LEU A 282 4205 4089 4820 455 -85 1869 N ATOM 859 CA LEU A 282 21.079 6.971 1.226 1.00 34.98 C ANISOU 859 CA LEU A 282 4133 4184 4972 429 -306 2027 C ATOM 860 C LEU A 282 20.596 6.589 -0.177 1.00 36.88 C ANISOU 860 C LEU A 282 4311 4406 5295 335 -505 2159 C ATOM 861 O LEU A 282 20.425 5.412 -0.476 1.00 47.64 O ANISOU 861 O LEU A 282 5596 5796 6709 290 -751 2223 O ATOM 862 CB LEU A 282 19.956 6.813 2.241 1.00 39.77 C ANISOU 862 CB LEU A 282 4633 4794 5684 559 -222 2308 C ATOM 863 CG LEU A 282 20.399 6.921 3.703 1.00 40.68 C ANISOU 863 CG LEU A 282 4808 4929 5721 667 -65 2188 C ATOM 864 CD1 LEU A 282 19.188 6.999 4.624 1.00 37.44 C ANISOU 864 CD1 LEU A 282 4291 4529 5406 816 61 2496 C ATOM 865 CD2 LEU A 282 21.322 5.775 4.116 1.00 31.24 C ANISOU 865 CD2 LEU A 282 3635 3778 4456 602 -236 1963 C ATOM 866 N ASP A 283 20.380 7.573 -1.038 1.00 34.93 N ANISOU 866 N ASP A 283 4107 4103 5060 306 -418 2200 N ATOM 867 CA ASP A 283 19.965 7.288 -2.412 1.00 37.68 C ANISOU 867 CA ASP A 283 4422 4413 5483 222 -601 2311 C ATOM 868 C ASP A 283 21.129 6.860 -3.310 1.00 34.68 C ANISOU 868 C ASP A 283 4118 4079 4981 110 -762 2040 C ATOM 869 O ASP A 283 22.177 7.499 -3.353 1.00 42.64 O ANISOU 869 O ASP A 283 5231 5117 5851 70 -650 1784 O ATOM 870 CB ASP A 283 19.246 8.497 -3.030 1.00 39.77 C ANISOU 870 CB ASP A 283 4710 4590 5813 228 -456 2458 C ATOM 871 CG ASP A 283 18.736 8.213 -4.432 1.00 46.66 C ANISOU 871 CG ASP A 283 5558 5394 6778 150 -645 2588 C ATOM 872 OD1 ASP A 283 19.426 8.581 -5.415 1.00 47.88 O ANISOU 872 OD1 ASP A 283 5805 5543 6846 60 -675 2418 O ATOM 873 OD2 ASP A 283 17.646 7.605 -4.549 1.00 49.02 O ANISOU 873 OD2 ASP A 283 5691 5691 7245 144 -738 2773 O ATOM 874 N LYS A 284 20.919 5.778 -4.040 1.00 39.87 N ANISOU 874 N LYS A 284 4717 4741 5690 68 -1036 2111 N ATOM 875 CA LYS A 284 21.923 5.199 -4.934 1.00 37.18 C ANISOU 875 CA LYS A 284 4436 4458 5234 -16 -1229 1878 C ATOM 876 C LYS A 284 22.566 6.221 -5.867 1.00 39.91 C ANISOU 876 C LYS A 284 4886 4797 5480 -84 -1112 1722 C ATOM 877 O LYS A 284 23.758 6.145 -6.146 1.00 47.11 O ANISOU 877 O LYS A 284 5868 5790 6241 -141 -1138 1446 O ATOM 878 CB LYS A 284 21.280 4.077 -5.761 1.00 40.98 C ANISOU 878 CB LYS A 284 4833 4913 5827 -56 -1518 2014 C ATOM 879 CG LYS A 284 22.247 3.154 -6.515 1.00 44.24 C ANISOU 879 CG LYS A 284 5295 5388 6126 -131 -1747 1766 C ATOM 880 CD LYS A 284 21.457 2.226 -7.454 1.00 53.11 C ANISOU 880 CD LYS A 284 6360 6421 7399 -217 -1946 1871 C ATOM 881 CE LYS A 284 22.308 1.111 -8.085 1.00 61.11 C ANISOU 881 CE LYS A 284 7450 7445 8323 -278 -2156 1638 C ATOM 882 NZ LYS A 284 23.577 1.572 -8.737 1.00 63.35 N ANISOU 882 NZ LYS A 284 7851 7818 8402 -267 -2137 1388 N ATOM 883 N PHE A 285 21.777 7.171 -6.358 1.00 33.96 N ANISOU 883 N PHE A 285 4140 3950 4813 -83 -990 1901 N ATOM 884 CA PHE A 285 22.275 8.114 -7.349 1.00 30.98 C ANISOU 884 CA PHE A 285 3857 3559 4355 -160 -908 1785 C ATOM 885 C PHE A 285 22.668 9.454 -6.760 1.00 30.61 C ANISOU 885 C PHE A 285 3882 3510 4238 -157 -629 1683 C ATOM 886 O PHE A 285 23.696 9.999 -7.139 1.00 32.90 O ANISOU 886 O PHE A 285 4255 3851 4394 -227 -566 1464 O ATOM 887 CB PHE A 285 21.266 8.314 -8.485 1.00 35.76 C ANISOU 887 CB PHE A 285 4450 4048 5088 -180 -992 2015 C ATOM 888 CG PHE A 285 20.711 7.040 -9.001 1.00 40.92 C ANISOU 888 CG PHE A 285 5037 4671 5840 -161 -1284 2164 C ATOM 889 CD1 PHE A 285 21.525 6.150 -9.686 1.00 38.32 C ANISOU 889 CD1 PHE A 285 4738 4417 5406 -194 -1506 1994 C ATOM 890 CD2 PHE A 285 19.384 6.705 -8.775 1.00 45.72 C ANISOU 890 CD2 PHE A 285 5503 5213 6654 -142 -1314 2394 C ATOM 891 CE1 PHE A 285 21.021 4.940 -10.153 1.00 39.24 C ANISOU 891 CE1 PHE A 285 4770 4508 5631 -224 -1748 2042 C ATOM 892 CE2 PHE A 285 18.869 5.494 -9.237 1.00 45.94 C ANISOU 892 CE2 PHE A 285 5424 5233 6799 -193 -1550 2439 C ATOM 893 CZ PHE A 285 19.688 4.609 -9.928 1.00 36.85 C ANISOU 893 CZ PHE A 285 4331 4120 5549 -240 -1765 2261 C ATOM 894 N ALA A 286 21.858 9.989 -5.848 1.00 33.84 N ANISOU 894 N ALA A 286 4258 3864 4735 -70 -473 1848 N ATOM 895 CA ALA A 286 22.155 11.300 -5.261 1.00 33.45 C ANISOU 895 CA ALA A 286 4288 3800 4623 -45 -231 1768 C ATOM 896 C ALA A 286 23.465 11.294 -4.447 1.00 32.67 C ANISOU 896 C ALA A 286 4255 3780 4377 -42 -161 1486 C ATOM 897 O ALA A 286 24.128 12.325 -4.302 1.00 35.55 O ANISOU 897 O ALA A 286 4712 4141 4653 -59 -18 1347 O ATOM 898 CB ALA A 286 20.994 11.785 -4.419 1.00 33.96 C ANISOU 898 CB ALA A 286 4302 3800 4802 74 -96 2004 C ATOM 899 N CYS A 287 23.840 10.126 -3.934 1.00 23.29 N ANISOU 899 N CYS A 287 3024 2654 3169 -24 -281 1403 N ATOM 900 CA CYS A 287 25.069 10.004 -3.172 1.00 28.24 C ANISOU 900 CA CYS A 287 3717 3340 3672 -25 -236 1129 C ATOM 901 C CYS A 287 26.272 10.277 -4.085 1.00 24.20 C ANISOU 901 C CYS A 287 3279 2886 3030 -142 -268 888 C ATOM 902 O CYS A 287 27.326 10.681 -3.633 1.00 29.30 O ANISOU 902 O CYS A 287 4001 3556 3574 -157 -178 669 O ATOM 903 CB CYS A 287 25.141 8.626 -2.485 1.00 35.56 C ANISOU 903 CB CYS A 287 4581 4317 4613 9 -387 1095 C ATOM 904 SG CYS A 287 25.796 7.238 -3.492 1.00 33.39 S ANISOU 904 SG CYS A 287 4275 4134 4278 -92 -695 949 S ATOM 905 N ARG A 288 26.088 10.082 -5.386 1.00 26.19 N ANISOU 905 N ARG A 288 3508 3152 3289 -220 -395 943 N ATOM 906 CA ARG A 288 27.120 10.409 -6.359 1.00 24.43 C ANISOU 906 CA ARG A 288 3345 2994 2941 -326 -414 750 C ATOM 907 C ARG A 288 27.249 11.930 -6.535 1.00 27.30 C ANISOU 907 C ARG A 288 3784 3311 3278 -362 -221 753 C ATOM 908 O ARG A 288 28.335 12.442 -6.777 1.00 24.87 O ANISOU 908 O ARG A 288 3537 3057 2854 -433 -167 560 O ATOM 909 CB ARG A 288 26.811 9.741 -7.705 1.00 28.38 C ANISOU 909 CB ARG A 288 3809 3517 3457 -379 -615 824 C ATOM 910 CG ARG A 288 26.736 8.211 -7.662 1.00 31.28 C ANISOU 910 CG ARG A 288 4110 3933 3841 -345 -857 817 C ATOM 911 CD ARG A 288 28.099 7.527 -7.455 1.00 32.39 C ANISOU 911 CD ARG A 288 4275 4200 3831 -375 -938 512 C ATOM 912 NE ARG A 288 28.018 6.078 -7.677 1.00 33.40 N ANISOU 912 NE ARG A 288 4349 4378 3961 -351 -1219 504 N ATOM 913 CZ ARG A 288 29.058 5.304 -7.974 1.00 27.50 C ANISOU 913 CZ ARG A 288 3618 3749 3080 -379 -1373 263 C ATOM 914 NH1 ARG A 288 30.269 5.826 -8.083 1.00 29.58 N ANISOU 914 NH1 ARG A 288 3940 4094 3204 -436 -1258 16 N ATOM 915 NH2 ARG A 288 28.891 4.006 -8.168 1.00 29.51 N ANISOU 915 NH2 ARG A 288 3829 4041 3342 -348 -1655 271 N ATOM 916 N VAL A 289 26.125 12.635 -6.413 1.00 28.13 N ANISOU 916 N VAL A 289 3880 3315 3493 -313 -132 978 N ATOM 917 CA VAL A 289 26.084 14.090 -6.471 1.00 30.06 C ANISOU 917 CA VAL A 289 4197 3501 3722 -333 28 1002 C ATOM 918 C VAL A 289 26.771 14.703 -5.254 1.00 26.74 C ANISOU 918 C VAL A 289 3844 3076 3240 -269 172 868 C ATOM 919 O VAL A 289 27.552 15.653 -5.368 1.00 27.37 O ANISOU 919 O VAL A 289 4005 3159 3238 -323 250 745 O ATOM 920 CB VAL A 289 24.634 14.605 -6.573 1.00 32.59 C ANISOU 920 CB VAL A 289 4488 3713 4180 -280 69 1276 C ATOM 921 CG1 VAL A 289 24.596 16.101 -6.411 1.00 31.52 C ANISOU 921 CG1 VAL A 289 4436 3518 4022 -279 220 1286 C ATOM 922 CG2 VAL A 289 24.016 14.202 -7.910 1.00 24.92 C ANISOU 922 CG2 VAL A 289 3479 2713 3275 -354 -75 1403 C ATOM 923 N ILE A 290 26.506 14.124 -4.093 1.00 27.86 N ANISOU 923 N ILE A 290 3957 3205 3424 -152 193 892 N ATOM 924 CA ILE A 290 27.190 14.507 -2.861 1.00 25.83 C ANISOU 924 CA ILE A 290 3774 2929 3111 -72 308 752 C ATOM 925 C ILE A 290 28.703 14.326 -2.969 1.00 29.57 C ANISOU 925 C ILE A 290 4302 3468 3464 -159 274 469 C ATOM 926 O ILE A 290 29.471 15.243 -2.659 1.00 33.84 O ANISOU 926 O ILE A 290 4935 3979 3942 -165 367 349 O ATOM 927 CB ILE A 290 26.644 13.706 -1.678 1.00 24.33 C ANISOU 927 CB ILE A 290 3535 2725 2985 61 314 826 C ATOM 928 CG1 ILE A 290 25.174 14.062 -1.465 1.00 25.83 C ANISOU 928 CG1 ILE A 290 3669 2855 3291 162 378 1116 C ATOM 929 CG2 ILE A 290 27.433 13.990 -0.403 1.00 19.71 C ANISOU 929 CG2 ILE A 290 3044 2107 2339 150 417 659 C ATOM 930 CD1 ILE A 290 24.549 13.252 -0.361 1.00 38.26 C ANISOU 930 CD1 ILE A 290 5176 4431 4931 291 384 1225 C ATOM 931 N GLN A 291 29.128 13.156 -3.435 1.00 25.48 N ANISOU 931 N GLN A 291 3729 3038 2915 -223 127 367 N ATOM 932 CA GLN A 291 30.553 12.861 -3.556 1.00 29.94 C ANISOU 932 CA GLN A 291 4333 3679 3364 -302 84 93 C ATOM 933 C GLN A 291 31.249 13.830 -4.500 1.00 30.54 C ANISOU 933 C GLN A 291 4454 3787 3362 -414 128 23 C ATOM 934 O GLN A 291 32.304 14.381 -4.191 1.00 23.41 O ANISOU 934 O GLN A 291 3621 2888 2388 -444 194 -147 O ATOM 935 CB GLN A 291 30.766 11.419 -4.021 1.00 17.96 C ANISOU 935 CB GLN A 291 2743 2260 1821 -342 -110 12 C ATOM 936 CG GLN A 291 30.464 10.415 -2.921 1.00 18.34 C ANISOU 936 CG GLN A 291 2760 2288 1920 -251 -169 11 C ATOM 937 CD GLN A 291 30.470 8.978 -3.418 1.00 29.97 C ANISOU 937 CD GLN A 291 4157 3848 3381 -284 -401 -28 C ATOM 938 OE1 GLN A 291 31.525 8.426 -3.738 1.00 30.57 O ANISOU 938 OE1 GLN A 291 4248 4014 3354 -347 -503 -260 O ATOM 939 NE2 GLN A 291 29.286 8.361 -3.469 1.00 19.18 N ANISOU 939 NE2 GLN A 291 2709 2457 2122 -236 -500 202 N ATOM 940 N SER A 292 30.634 14.050 -5.647 1.00 26.87 N ANISOU 940 N SER A 292 3954 3338 2919 -478 86 165 N ATOM 941 CA SER A 292 31.191 14.956 -6.629 1.00 29.76 C ANISOU 941 CA SER A 292 4356 3739 3211 -594 120 124 C ATOM 942 C SER A 292 31.230 16.402 -6.054 1.00 29.93 C ANISOU 942 C SER A 292 4464 3668 3243 -572 269 159 C ATOM 943 O SER A 292 32.225 17.132 -6.195 1.00 29.42 O ANISOU 943 O SER A 292 4452 3628 3098 -646 312 34 O ATOM 944 CB SER A 292 30.386 14.794 -7.937 1.00 33.34 C ANISOU 944 CB SER A 292 4763 4206 3700 -652 30 282 C ATOM 945 OG SER A 292 30.324 15.987 -8.682 1.00 49.29 O ANISOU 945 OG SER A 292 6828 6197 5702 -736 97 347 O ATOM 946 N SER A 293 30.175 16.800 -5.351 1.00 26.66 N ANISOU 946 N SER A 293 4061 3147 2922 -462 335 330 N ATOM 947 CA SER A 293 30.171 18.121 -4.706 1.00 24.41 C ANISOU 947 CA SER A 293 3866 2769 2640 -410 450 361 C ATOM 948 C SER A 293 31.265 18.277 -3.646 1.00 26.13 C ANISOU 948 C SER A 293 4160 2965 2802 -358 500 172 C ATOM 949 O SER A 293 31.874 19.334 -3.527 1.00 39.16 O ANISOU 949 O SER A 293 5893 4575 4411 -381 546 119 O ATOM 950 CB SER A 293 28.801 18.422 -4.082 1.00 26.77 C ANISOU 950 CB SER A 293 4159 2972 3043 -273 508 576 C ATOM 951 OG SER A 293 27.758 18.295 -5.039 1.00 30.14 O ANISOU 951 OG SER A 293 4519 3394 3539 -319 456 757 O ATOM 952 N LEU A 294 31.500 17.230 -2.863 1.00 27.61 N ANISOU 952 N LEU A 294 4326 3167 2997 -287 478 76 N ATOM 953 CA LEU A 294 32.485 17.292 -1.792 1.00 26.43 C ANISOU 953 CA LEU A 294 4259 2971 2811 -228 519 -106 C ATOM 954 C LEU A 294 33.901 17.534 -2.307 1.00 30.92 C ANISOU 954 C LEU A 294 4860 3599 3290 -359 493 -307 C ATOM 955 O LEU A 294 34.676 18.268 -1.681 1.00 31.30 O ANISOU 955 O LEU A 294 5003 3572 3317 -333 541 -404 O ATOM 956 CB LEU A 294 32.464 16.002 -0.969 1.00 19.32 C ANISOU 956 CB LEU A 294 3325 2081 1934 -150 478 -182 C ATOM 957 CG LEU A 294 31.296 15.839 -0.004 1.00 28.89 C ANISOU 957 CG LEU A 294 4526 3219 3231 14 532 -9 C ATOM 958 CD1 LEU A 294 31.179 14.361 0.489 1.00 21.27 C ANISOU 958 CD1 LEU A 294 3493 2297 2290 46 448 -57 C ATOM 959 CD2 LEU A 294 31.488 16.817 1.163 1.00 21.62 C ANISOU 959 CD2 LEU A 294 3733 2171 2309 153 647 -29 C ATOM 960 N GLN A 295 34.253 16.912 -3.433 1.00 24.78 N ANISOU 960 N GLN A 295 4002 2953 2460 -490 409 -364 N ATOM 961 CA GLN A 295 35.628 17.009 -3.886 1.00 32.32 C ANISOU 961 CA GLN A 295 4969 3987 3323 -605 386 -558 C ATOM 962 C GLN A 295 35.843 18.194 -4.841 1.00 30.96 C ANISOU 962 C GLN A 295 4812 3841 3111 -721 415 -488 C ATOM 963 O GLN A 295 36.955 18.690 -4.978 1.00 33.57 O ANISOU 963 O GLN A 295 5172 4202 3382 -800 426 -608 O ATOM 964 CB GLN A 295 36.139 15.667 -4.457 1.00 25.54 C ANISOU 964 CB GLN A 295 4029 3273 2404 -668 274 -703 C ATOM 965 CG GLN A 295 35.761 15.380 -5.873 1.00 25.77 C ANISOU 965 CG GLN A 295 3976 3418 2396 -759 199 -617 C ATOM 966 CD GLN A 295 36.163 13.965 -6.316 1.00 39.78 C ANISOU 966 CD GLN A 295 5680 5325 4109 -781 59 -756 C ATOM 967 OE1 GLN A 295 35.836 13.535 -7.417 1.00 37.86 O ANISOU 967 OE1 GLN A 295 5378 5171 3834 -827 -30 -694 O ATOM 968 NE2 GLN A 295 36.872 13.248 -5.456 1.00 42.18 N ANISOU 968 NE2 GLN A 295 6000 5631 4394 -741 27 -947 N ATOM 969 N ASN A 296 34.772 18.674 -5.457 1.00 26.84 N ANISOU 969 N ASN A 296 4271 3297 2629 -732 421 -288 N ATOM 970 CA ASN A 296 34.908 19.749 -6.436 1.00 32.31 C ANISOU 970 CA ASN A 296 4978 4016 3283 -855 430 -218 C ATOM 971 C ASN A 296 34.578 21.149 -5.917 1.00 34.26 C ANISOU 971 C ASN A 296 5318 4130 3568 -811 488 -111 C ATOM 972 O ASN A 296 35.195 22.122 -6.351 1.00 32.72 O ANISOU 972 O ASN A 296 5160 3945 3326 -912 486 -121 O ATOM 973 CB ASN A 296 34.110 19.435 -7.712 1.00 37.67 C ANISOU 973 CB ASN A 296 5587 4761 3966 -929 375 -92 C ATOM 974 CG ASN A 296 34.633 18.195 -8.429 1.00 41.60 C ANISOU 974 CG ASN A 296 6005 5405 4396 -982 289 -211 C ATOM 975 OD1 ASN A 296 35.838 18.030 -8.587 1.00 39.32 O ANISOU 975 OD1 ASN A 296 5707 5217 4016 -1047 279 -383 O ATOM 976 ND2 ASN A 296 33.727 17.314 -8.853 1.00 43.05 N ANISOU 976 ND2 ASN A 296 6134 5598 4625 -945 213 -116 N ATOM 977 N MET A 297 33.619 21.261 -4.995 1.00 31.02 N ANISOU 977 N MET A 297 4944 3604 3237 -658 528 -3 N ATOM 978 CA MET A 297 33.242 22.573 -4.477 1.00 27.23 C ANISOU 978 CA MET A 297 4561 3001 2784 -589 564 98 C ATOM 979 C MET A 297 34.411 23.221 -3.756 1.00 33.20 C ANISOU 979 C MET A 297 5412 3701 3502 -572 570 -33 C ATOM 980 O MET A 297 35.352 22.535 -3.355 1.00 37.24 O ANISOU 980 O MET A 297 5919 4243 3989 -573 569 -201 O ATOM 981 CB MET A 297 32.086 22.453 -3.493 1.00 29.91 C ANISOU 981 CB MET A 297 4919 3243 3204 -397 613 220 C ATOM 982 CG MET A 297 30.732 22.225 -4.123 1.00 34.57 C ANISOU 982 CG MET A 297 5435 3842 3857 -398 605 407 C ATOM 983 SD MET A 297 29.456 22.084 -2.852 1.00 54.09 S ANISOU 983 SD MET A 297 7915 6218 6419 -160 675 557 S ATOM 984 CE MET A 297 29.356 23.772 -2.283 1.00 77.01 C ANISOU 984 CE MET A 297 10956 9003 9301 -67 704 610 C ATOM 985 N ASP A 298 34.346 24.538 -3.567 1.00 32.93 N ANISOU 985 N ASP A 298 5470 3573 3468 -551 561 42 N ATOM 986 CA ASP A 298 35.317 25.210 -2.716 1.00 33.59 C ANISOU 986 CA ASP A 298 5664 3563 3538 -496 547 -54 C ATOM 987 C ASP A 298 35.322 24.536 -1.350 1.00 34.09 C ANISOU 987 C ASP A 298 5776 3537 3638 -303 595 -133 C ATOM 988 O ASP A 298 34.268 24.223 -0.793 1.00 33.36 O ANISOU 988 O ASP A 298 5680 3405 3592 -158 641 -38 O ATOM 989 CB ASP A 298 34.970 26.684 -2.554 1.00 36.38 C ANISOU 989 CB ASP A 298 6122 3806 3895 -453 504 67 C ATOM 990 CG ASP A 298 35.082 27.463 -3.854 1.00 42.05 C ANISOU 990 CG ASP A 298 6808 4599 4572 -658 440 135 C ATOM 991 OD1 ASP A 298 35.889 27.082 -4.737 1.00 40.37 O ANISOU 991 OD1 ASP A 298 6516 4512 4313 -834 429 57 O ATOM 992 OD2 ASP A 298 34.358 28.469 -3.981 1.00 40.38 O ANISOU 992 OD2 ASP A 298 6652 4321 4370 -639 398 266 O ATOM 993 N LEU A 299 36.506 24.325 -0.800 1.00 34.50 N ANISOU 993 N LEU A 299 5876 3556 3677 -302 584 -302 N ATOM 994 CA LEU A 299 36.623 23.599 0.455 1.00 36.33 C ANISOU 994 CA LEU A 299 6162 3700 3943 -137 623 -403 C ATOM 995 C LEU A 299 35.717 24.156 1.547 1.00 33.92 C ANISOU 995 C LEU A 299 5961 3248 3678 93 660 -286 C ATOM 996 O LEU A 299 35.137 23.405 2.304 1.00 39.87 O ANISOU 996 O LEU A 299 6707 3979 4462 230 713 -279 O ATOM 997 CB LEU A 299 38.073 23.562 0.920 1.00 41.10 C ANISOU 997 CB LEU A 299 6834 4246 4536 -165 592 -598 C ATOM 998 CG LEU A 299 38.356 22.620 2.087 1.00 42.68 C ANISOU 998 CG LEU A 299 7084 4365 4768 -32 622 -745 C ATOM 999 CD1 LEU A 299 37.845 21.222 1.770 1.00 36.88 C ANISOU 999 CD1 LEU A 299 6220 3766 4028 -69 640 -773 C ATOM 1000 CD2 LEU A 299 39.856 22.619 2.393 1.00 40.12 C ANISOU 1000 CD2 LEU A 299 6824 3979 4440 -87 581 -945 C ATOM 1001 N SER A 300 35.569 25.470 1.609 1.00 33.07 N ANISOU 1001 N SER A 300 5948 3053 3565 138 622 -187 N ATOM 1002 CA SER A 300 34.772 26.082 2.667 1.00 37.12 C ANISOU 1002 CA SER A 300 6574 3430 4101 380 645 -84 C ATOM 1003 C SER A 300 33.277 25.800 2.559 1.00 37.25 C ANISOU 1003 C SER A 300 6509 3504 4140 459 708 86 C ATOM 1004 O SER A 300 32.572 25.774 3.573 1.00 34.83 O ANISOU 1004 O SER A 300 6257 3124 3854 679 763 150 O ATOM 1005 CB SER A 300 35.006 27.584 2.701 1.00 43.81 C ANISOU 1005 CB SER A 300 7547 4171 4927 408 553 -23 C ATOM 1006 OG SER A 300 36.384 27.858 2.895 1.00 52.47 O ANISOU 1006 OG SER A 300 8721 5195 6019 350 485 -161 O ATOM 1007 N LEU A 301 32.796 25.627 1.329 1.00 29.75 N ANISOU 1007 N LEU A 301 5434 2680 3189 286 698 165 N ATOM 1008 CA LEU A 301 31.419 25.226 1.095 1.00 29.41 C ANISOU 1008 CA LEU A 301 5296 2692 3186 332 748 327 C ATOM 1009 C LEU A 301 31.281 23.714 1.290 1.00 28.48 C ANISOU 1009 C LEU A 301 5073 2649 3101 338 795 280 C ATOM 1010 O LEU A 301 30.322 23.258 1.891 1.00 29.02 O ANISOU 1010 O LEU A 301 5105 2708 3212 483 852 386 O ATOM 1011 CB LEU A 301 30.956 25.625 -0.318 1.00 36.67 C ANISOU 1011 CB LEU A 301 6139 3691 4104 146 702 429 C ATOM 1012 CG LEU A 301 30.433 27.041 -0.606 1.00 48.84 C ANISOU 1012 CG LEU A 301 7755 5171 5632 154 652 550 C ATOM 1013 CD1 LEU A 301 29.033 27.248 -0.047 1.00 55.34 C ANISOU 1013 CD1 LEU A 301 8581 5946 6498 346 702 716 C ATOM 1014 CD2 LEU A 301 31.376 28.115 -0.080 1.00 50.76 C ANISOU 1014 CD2 LEU A 301 8144 5314 5828 195 583 472 C ATOM 1015 N ALA A 302 32.239 22.943 0.779 1.00 21.55 N ANISOU 1015 N ALA A 302 4142 1850 2199 183 759 126 N ATOM 1016 CA ALA A 302 32.264 21.499 1.026 1.00 22.44 C ANISOU 1016 CA ALA A 302 4169 2025 2330 188 769 52 C ATOM 1017 C ALA A 302 32.235 21.187 2.523 1.00 31.21 C ANISOU 1017 C ALA A 302 5358 3036 3464 395 824 8 C ATOM 1018 O ALA A 302 31.570 20.237 2.944 1.00 38.71 O ANISOU 1018 O ALA A 302 6239 4016 4452 469 849 60 O ATOM 1019 CB ALA A 302 33.463 20.862 0.379 1.00 21.05 C ANISOU 1019 CB ALA A 302 3953 1938 2108 14 709 -138 C ATOM 1020 N CYS A 303 32.917 21.992 3.336 1.00 31.54 N ANISOU 1020 N CYS A 303 5547 2951 3484 494 833 -74 N ATOM 1021 CA CYS A 303 32.891 21.780 4.797 1.00 32.54 C ANISOU 1021 CA CYS A 303 5773 2962 3629 712 885 -116 C ATOM 1022 C CYS A 303 31.499 21.954 5.419 1.00 33.47 C ANISOU 1022 C CYS A 303 5882 3059 3777 912 960 90 C ATOM 1023 O CYS A 303 31.164 21.281 6.391 1.00 40.35 O ANISOU 1023 O CYS A 303 6760 3903 4669 1060 1014 95 O ATOM 1024 CB CYS A 303 33.927 22.647 5.534 1.00 25.20 C ANISOU 1024 CB CYS A 303 5023 1874 2678 792 861 -242 C ATOM 1025 SG CYS A 303 35.676 22.289 5.102 1.00 39.98 S ANISOU 1025 SG CYS A 303 6908 3754 4528 588 785 -502 S ATOM 1026 N LYS A 304 30.684 22.840 4.861 1.00 33.28 N ANISOU 1026 N LYS A 304 5839 3052 3754 916 961 261 N ATOM 1027 CA LYS A 304 29.321 23.013 5.360 1.00 38.40 C ANISOU 1027 CA LYS A 304 6462 3698 4431 1101 1032 466 C ATOM 1028 C LYS A 304 28.469 21.776 5.068 1.00 43.57 C ANISOU 1028 C LYS A 304 6943 4468 5142 1055 1061 569 C ATOM 1029 O LYS A 304 27.564 21.455 5.832 1.00 48.93 O ANISOU 1029 O LYS A 304 7590 5150 5853 1226 1132 699 O ATOM 1030 CB LYS A 304 28.645 24.241 4.743 1.00 39.93 C ANISOU 1030 CB LYS A 304 6674 3883 4616 1099 1009 613 C ATOM 1031 CG LYS A 304 29.491 25.503 4.696 1.00 51.00 C ANISOU 1031 CG LYS A 304 8226 5189 5964 1085 933 530 C ATOM 1032 CD LYS A 304 29.343 26.351 5.945 1.00 61.74 C ANISOU 1032 CD LYS A 304 9750 6416 7294 1363 947 557 C ATOM 1033 CE LYS A 304 29.810 27.785 5.677 1.00 68.26 C ANISOU 1033 CE LYS A 304 10707 7154 8074 1347 834 545 C ATOM 1034 NZ LYS A 304 29.724 28.663 6.885 1.00 73.42 N ANISOU 1034 NZ LYS A 304 11541 7664 8690 1637 814 566 N ATOM 1035 N LEU A 305 28.748 21.101 3.952 1.00 36.18 N ANISOU 1035 N LEU A 305 5898 3629 4220 832 995 523 N ATOM 1036 CA LEU A 305 28.014 19.890 3.579 1.00 38.43 C ANISOU 1036 CA LEU A 305 6025 4014 4564 777 980 620 C ATOM 1037 C LEU A 305 28.209 18.811 4.619 1.00 34.29 C ANISOU 1037 C LEU A 305 5492 3488 4050 871 999 544 C ATOM 1038 O LEU A 305 27.275 18.112 4.984 1.00 37.79 O ANISOU 1038 O LEU A 305 5841 3970 4547 952 1025 691 O ATOM 1039 CB LEU A 305 28.476 19.345 2.222 1.00 38.39 C ANISOU 1039 CB LEU A 305 5931 4104 4553 536 882 549 C ATOM 1040 CG LEU A 305 27.902 20.035 0.996 1.00 44.73 C ANISOU 1040 CG LEU A 305 6692 4933 5372 422 852 680 C ATOM 1041 CD1 LEU A 305 28.138 19.179 -0.242 1.00 42.15 C ANISOU 1041 CD1 LEU A 305 6261 4705 5048 225 754 641 C ATOM 1042 CD2 LEU A 305 26.421 20.270 1.223 1.00 46.70 C ANISOU 1042 CD2 LEU A 305 6889 5160 5695 551 907 927 C ATOM 1043 N VAL A 306 29.445 18.665 5.069 1.00 28.51 N ANISOU 1043 N VAL A 306 4857 2707 3270 850 977 314 N ATOM 1044 CA VAL A 306 29.780 17.709 6.120 1.00 29.01 C ANISOU 1044 CA VAL A 306 4942 2743 3336 934 985 204 C ATOM 1045 C VAL A 306 29.072 18.037 7.453 1.00 35.17 C ANISOU 1045 C VAL A 306 5794 3441 4130 1193 1093 320 C ATOM 1046 O VAL A 306 28.623 17.134 8.157 1.00 37.14 O ANISOU 1046 O VAL A 306 5990 3714 4408 1275 1115 365 O ATOM 1047 CB VAL A 306 31.306 17.688 6.339 1.00 21.18 C ANISOU 1047 CB VAL A 306 4066 1686 2296 865 940 -76 C ATOM 1048 CG1 VAL A 306 31.671 16.659 7.391 1.00 27.76 C ANISOU 1048 CG1 VAL A 306 4932 2480 3137 936 935 -210 C ATOM 1049 CG2 VAL A 306 32.021 17.427 5.015 1.00 19.63 C ANISOU 1049 CG2 VAL A 306 3796 1590 2071 624 844 -184 C ATOM 1050 N GLN A 307 28.983 19.326 7.796 1.00 38.30 N ANISOU 1050 N GLN A 307 6310 3745 4498 1328 1149 368 N ATOM 1051 CA GLN A 307 28.258 19.754 8.997 1.00 44.67 C ANISOU 1051 CA GLN A 307 7191 4483 5300 1600 1250 491 C ATOM 1052 C GLN A 307 26.812 19.254 8.959 1.00 42.81 C ANISOU 1052 C GLN A 307 6792 4354 5118 1662 1305 745 C ATOM 1053 O GLN A 307 26.227 18.944 9.987 1.00 45.87 O ANISOU 1053 O GLN A 307 7179 4736 5513 1852 1385 837 O ATOM 1054 CB GLN A 307 28.256 21.283 9.140 1.00 48.84 C ANISOU 1054 CB GLN A 307 7861 4913 5785 1727 1266 530 C ATOM 1055 CG GLN A 307 29.620 21.930 9.388 1.00 62.58 C ANISOU 1055 CG GLN A 307 9780 6516 7481 1714 1206 314 C ATOM 1056 CD GLN A 307 29.520 23.455 9.593 1.00 72.02 C ANISOU 1056 CD GLN A 307 11121 7609 8634 1862 1191 378 C ATOM 1057 OE1 GLN A 307 28.419 24.009 9.692 1.00 70.15 O ANISOU 1057 OE1 GLN A 307 10862 7401 8391 2002 1237 568 O ATOM 1058 NE2 GLN A 307 30.672 24.131 9.655 1.00 72.81 N ANISOU 1058 NE2 GLN A 307 11370 7588 8708 1832 1112 221 N ATOM 1059 N ALA A 308 26.245 19.170 7.761 1.00 36.98 N ANISOU 1059 N ALA A 308 5918 3711 4423 1500 1259 864 N ATOM 1060 CA ALA A 308 24.853 18.765 7.590 1.00 32.11 C ANISOU 1060 CA ALA A 308 5141 3182 3876 1543 1295 1123 C ATOM 1061 C ALA A 308 24.625 17.264 7.811 1.00 35.09 C ANISOU 1061 C ALA A 308 5388 3638 4308 1497 1260 1154 C ATOM 1062 O ALA A 308 23.487 16.799 7.817 1.00 44.92 O ANISOU 1062 O ALA A 308 6493 4953 5623 1543 1283 1382 O ATOM 1063 CB ALA A 308 24.354 19.182 6.215 1.00 26.57 C ANISOU 1063 CB ALA A 308 4355 2526 3213 1383 1240 1232 C ATOM 1064 N LEU A 309 25.700 16.508 7.990 1.00 34.73 N ANISOU 1064 N LEU A 309 5384 3579 4233 1404 1192 929 N ATOM 1065 CA LEU A 309 25.580 15.079 8.302 1.00 41.94 C ANISOU 1065 CA LEU A 309 6192 4556 5186 1365 1132 932 C ATOM 1066 C LEU A 309 24.863 14.865 9.639 1.00 42.20 C ANISOU 1066 C LEU A 309 6223 4579 5232 1590 1239 1067 C ATOM 1067 O LEU A 309 25.087 15.608 10.594 1.00 41.87 O ANISOU 1067 O LEU A 309 6326 4447 5137 1776 1342 1016 O ATOM 1068 CB LEU A 309 26.967 14.398 8.311 1.00 37.39 C ANISOU 1068 CB LEU A 309 5687 3957 4564 1233 1032 630 C ATOM 1069 CG LEU A 309 27.588 14.050 6.948 1.00 33.43 C ANISOU 1069 CG LEU A 309 5127 3520 4054 991 895 514 C ATOM 1070 CD1 LEU A 309 29.015 13.540 7.070 1.00 33.74 C ANISOU 1070 CD1 LEU A 309 5252 3533 4036 890 814 202 C ATOM 1071 CD2 LEU A 309 26.729 13.035 6.189 1.00 30.15 C ANISOU 1071 CD2 LEU A 309 4527 3217 3710 892 786 686 C ATOM 1072 N PRO A 310 23.989 13.848 9.707 1.00 45.01 N ANISOU 1072 N PRO A 310 6416 5028 5660 1582 1205 1251 N ATOM 1073 CA PRO A 310 23.259 13.484 10.929 1.00 42.83 C ANISOU 1073 CA PRO A 310 6106 4770 5399 1778 1300 1404 C ATOM 1074 C PRO A 310 24.175 12.948 12.022 1.00 43.05 C ANISOU 1074 C PRO A 310 6256 4731 5372 1833 1299 1182 C ATOM 1075 O PRO A 310 25.215 12.370 11.732 1.00 46.47 O ANISOU 1075 O PRO A 310 6735 5139 5784 1673 1179 940 O ATOM 1076 CB PRO A 310 22.313 12.375 10.449 1.00 45.34 C ANISOU 1076 CB PRO A 310 6203 5205 5817 1681 1204 1629 C ATOM 1077 CG PRO A 310 22.969 11.839 9.224 1.00 47.05 C ANISOU 1077 CG PRO A 310 6385 5443 6048 1431 1025 1484 C ATOM 1078 CD PRO A 310 23.524 13.058 8.558 1.00 49.29 C ANISOU 1078 CD PRO A 310 6787 5663 6278 1394 1069 1362 C ATOM 1079 N ARG A 311 23.777 13.132 13.273 1.00 50.23 N ANISOU 1079 N ARG A 311 7221 5608 6255 2065 1429 1264 N ATOM 1080 CA ARG A 311 24.601 12.741 14.412 1.00 53.06 C ANISOU 1080 CA ARG A 311 7724 5875 6562 2146 1442 1057 C ATOM 1081 C ARG A 311 23.921 11.661 15.253 1.00 51.48 C ANISOU 1081 C ARG A 311 7415 5751 6396 2213 1450 1205 C ATOM 1082 O ARG A 311 24.169 11.558 16.443 1.00 51.12 O ANISOU 1082 O ARG A 311 7483 5633 6306 2370 1521 1132 O ATOM 1083 CB ARG A 311 24.870 13.962 15.299 1.00 53.21 C ANISOU 1083 CB ARG A 311 7951 5761 6506 2392 1582 997 C ATOM 1084 CG ARG A 311 25.146 15.244 14.529 1.00 53.54 C ANISOU 1084 CG ARG A 311 8074 5748 6520 2374 1589 957 C ATOM 1085 CD ARG A 311 26.354 15.056 13.634 1.00 51.36 C ANISOU 1085 CD ARG A 311 7839 5433 6242 2122 1452 700 C ATOM 1086 NE ARG A 311 26.641 16.217 12.797 1.00 51.20 N ANISOU 1086 NE ARG A 311 7879 5375 6199 2070 1442 671 N ATOM 1087 CZ ARG A 311 27.377 17.252 13.184 1.00 49.04 C ANISOU 1087 CZ ARG A 311 7801 4960 5870 2173 1467 535 C ATOM 1088 NH1 ARG A 311 27.884 17.281 14.406 1.00 45.44 N ANISOU 1088 NH1 ARG A 311 7502 4422 5343 2297 1499 432 N ATOM 1089 NH2 ARG A 311 27.596 18.264 12.351 1.00 49.81 N ANISOU 1089 NH2 ARG A 311 7936 5039 5952 2103 1436 527 N ATOM 1090 N ASP A 312 23.055 10.865 14.641 1.00 49.94 N ANISOU 1090 N ASP A 312 7001 5691 6281 2099 1369 1421 N ATOM 1091 CA ASP A 312 22.272 9.900 15.398 1.00 53.11 C ANISOU 1091 CA ASP A 312 7273 6180 6725 2162 1371 1616 C ATOM 1092 C ASP A 312 22.206 8.557 14.682 1.00 52.89 C ANISOU 1092 C ASP A 312 7078 6244 6773 1925 1150 1642 C ATOM 1093 O ASP A 312 23.104 8.217 13.929 1.00 54.16 O ANISOU 1093 O ASP A 312 7279 6377 6923 1732 997 1412 O ATOM 1094 CB ASP A 312 20.865 10.443 15.694 1.00 53.91 C ANISOU 1094 CB ASP A 312 7257 6367 6860 2360 1530 1974 C ATOM 1095 CG ASP A 312 20.103 10.839 14.435 1.00 61.70 C ANISOU 1095 CG ASP A 312 8101 7420 7922 2264 1498 2170 C ATOM 1096 OD1 ASP A 312 20.611 10.596 13.322 1.00 62.83 O ANISOU 1096 OD1 ASP A 312 8225 7553 8093 2042 1346 2047 O ATOM 1097 OD2 ASP A 312 18.989 11.401 14.558 1.00 65.79 O ANISOU 1097 OD2 ASP A 312 8530 7998 8469 2417 1624 2446 O ATOM 1098 N ALA A 313 21.145 7.796 14.925 1.00 51.19 N ANISOU 1098 N ALA A 313 6677 6141 6632 1947 1124 1929 N ATOM 1099 CA ALA A 313 20.966 6.499 14.278 1.00 48.54 C ANISOU 1099 CA ALA A 313 6176 5889 6377 1739 885 1994 C ATOM 1100 C ALA A 313 21.153 6.555 12.761 1.00 53.98 C ANISOU 1100 C ALA A 313 6817 6587 7106 1546 738 1950 C ATOM 1101 O ALA A 313 21.607 5.589 12.153 1.00 51.64 O ANISOU 1101 O ALA A 313 6477 6316 6828 1359 509 1837 O ATOM 1102 CB ALA A 313 19.598 5.924 14.613 1.00 41.91 C ANISOU 1102 CB ALA A 313 5122 5169 5633 1807 892 2383 C ATOM 1103 N ARG A 314 20.796 7.682 12.154 1.00 53.12 N ANISOU 1103 N ARG A 314 7037 5744 7403 532 594 1510 N ATOM 1104 CA ARG A 314 20.907 7.837 10.709 1.00 46.92 C ANISOU 1104 CA ARG A 314 6189 4978 6661 457 494 1479 C ATOM 1105 C ARG A 314 22.354 7.816 10.224 1.00 45.98 C ANISOU 1105 C ARG A 314 6146 4882 6440 414 398 1332 C ATOM 1106 O ARG A 314 22.629 7.383 9.111 1.00 49.33 O ANISOU 1106 O ARG A 314 6526 5335 6882 351 281 1299 O ATOM 1107 CB ARG A 314 20.217 9.116 10.252 1.00 45.47 C ANISOU 1107 CB ARG A 314 5971 4773 6532 472 566 1527 C ATOM 1108 CG ARG A 314 18.711 9.086 10.432 1.00 49.20 C ANISOU 1108 CG ARG A 314 6342 5230 7121 510 637 1681 C ATOM 1109 CD ARG A 314 18.095 10.462 10.256 1.00 42.94 C ANISOU 1109 CD ARG A 314 5550 4410 6357 554 724 1720 C ATOM 1110 NE ARG A 314 18.564 11.404 11.267 1.00 48.92 N ANISOU 1110 NE ARG A 314 6430 5140 7017 628 826 1676 N ATOM 1111 CZ ARG A 314 18.459 12.726 11.153 1.00 50.37 C ANISOU 1111 CZ ARG A 314 6665 5291 7180 665 880 1664 C ATOM 1112 NH1 ARG A 314 17.905 13.248 10.070 1.00 43.54 N ANISOU 1112 NH1 ARG A 314 5742 4418 6384 634 847 1692 N ATOM 1113 NH2 ARG A 314 18.917 13.525 12.111 1.00 50.54 N ANISOU 1113 NH2 ARG A 314 6808 5283 7111 735 959 1622 N ATOM 1114 N LEU A 315 23.277 8.289 11.047 1.00 38.11 N ANISOU 1114 N LEU A 315 5262 3881 5337 450 446 1238 N ATOM 1115 CA LEU A 315 24.687 8.208 10.691 1.00 38.96 C ANISOU 1115 CA LEU A 315 5420 4040 5340 408 360 1077 C ATOM 1116 C LEU A 315 25.148 6.755 10.595 1.00 36.66 C ANISOU 1116 C LEU A 315 5124 3785 5019 391 238 1037 C ATOM 1117 O LEU A 315 25.879 6.379 9.664 1.00 33.18 O ANISOU 1117 O LEU A 315 4667 3394 4545 339 121 957 O ATOM 1118 CB LEU A 315 25.552 8.987 11.683 1.00 37.51 C ANISOU 1118 CB LEU A 315 5341 3862 5050 450 435 965 C ATOM 1119 CG LEU A 315 27.024 9.091 11.296 1.00 33.66 C ANISOU 1119 CG LEU A 315 4894 3437 4456 400 357 795 C ATOM 1120 CD1 LEU A 315 27.186 9.812 9.973 1.00 28.57 C ANISOU 1120 CD1 LEU A 315 4207 2813 3836 320 317 784 C ATOM 1121 CD2 LEU A 315 27.827 9.781 12.389 1.00 28.95 C ANISOU 1121 CD2 LEU A 315 4400 2838 3762 447 425 688 C ATOM 1122 N ILE A 316 24.722 5.937 11.555 1.00 36.52 N ANISOU 1122 N ILE A 316 5126 3744 5007 438 262 1093 N ATOM 1123 CA ILE A 316 24.977 4.497 11.481 1.00 37.44 C ANISOU 1123 CA ILE A 316 5245 3877 5102 425 138 1075 C ATOM 1124 C ILE A 316 24.394 3.926 10.181 1.00 37.53 C ANISOU 1124 C ILE A 316 5158 3891 5209 363 26 1151 C ATOM 1125 O ILE A 316 25.053 3.179 9.463 1.00 41.93 O ANISOU 1125 O ILE A 316 5720 4484 5728 334 -116 1081 O ATOM 1126 CB ILE A 316 24.350 3.731 12.661 1.00 40.05 C ANISOU 1126 CB ILE A 316 5607 4167 5444 475 190 1160 C ATOM 1127 CG1 ILE A 316 25.084 4.025 13.963 1.00 44.96 C ANISOU 1127 CG1 ILE A 316 6341 4791 5951 547 271 1060 C ATOM 1128 CG2 ILE A 316 24.391 2.243 12.400 1.00 45.53 C ANISOU 1128 CG2 ILE A 316 6297 4865 6137 448 47 1169 C ATOM 1129 CD1 ILE A 316 24.457 3.353 15.182 1.00 45.74 C ANISOU 1129 CD1 ILE A 316 6480 4847 6051 603 339 1148 C ATOM 1130 N ALA A 317 23.150 4.278 9.885 1.00 35.31 N ANISOU 1130 N ALA A 317 4777 3591 5048 347 87 1272 N ATOM 1131 CA ALA A 317 22.502 3.807 8.667 1.00 39.16 C ANISOU 1131 CA ALA A 317 5154 4091 5633 289 -13 1328 C ATOM 1132 C ALA A 317 23.300 4.221 7.430 1.00 40.81 C ANISOU 1132 C ALA A 317 5365 4334 5808 249 -101 1237 C ATOM 1133 O ALA A 317 23.362 3.488 6.431 1.00 38.34 O ANISOU 1133 O ALA A 317 5006 4044 5516 209 -237 1223 O ATOM 1134 CB ALA A 317 21.095 4.342 8.581 1.00 33.09 C ANISOU 1134 CB ALA A 317 4283 3295 4995 291 79 1466 C ATOM 1135 N ILE A 318 23.913 5.396 7.499 1.00 33.07 N ANISOU 1135 N ILE A 318 4443 3353 4770 260 -26 1178 N ATOM 1136 CA ILE A 318 24.722 5.862 6.383 1.00 35.17 C ANISOU 1136 CA ILE A 318 4720 3650 4995 219 -96 1100 C ATOM 1137 C ILE A 318 25.965 4.995 6.243 1.00 32.99 C ANISOU 1137 C ILE A 318 4488 3441 4606 213 -218 970 C ATOM 1138 O ILE A 318 26.266 4.523 5.159 1.00 34.15 O ANISOU 1138 O ILE A 318 4603 3625 4749 183 -340 942 O ATOM 1139 CB ILE A 318 25.076 7.352 6.504 1.00 33.36 C ANISOU 1139 CB ILE A 318 4535 3414 4726 214 15 1056 C ATOM 1140 CG1 ILE A 318 23.888 8.186 6.014 1.00 32.15 C ANISOU 1140 CG1 ILE A 318 4318 3214 4683 210 81 1166 C ATOM 1141 CG2 ILE A 318 26.318 7.683 5.689 1.00 32.18 C ANISOU 1141 CG2 ILE A 318 4406 3337 4483 162 -51 921 C ATOM 1142 CD1 ILE A 318 23.933 9.620 6.489 1.00 28.30 C ANISOU 1142 CD1 ILE A 318 3896 2689 4168 228 206 1159 C ATOM 1143 N CYS A 319 26.652 4.765 7.356 1.00 33.57 N ANISOU 1143 N CYS A 319 4633 3537 4586 249 -186 885 N ATOM 1144 CA CYS A 319 27.854 3.939 7.377 1.00 35.74 C ANISOU 1144 CA CYS A 319 4952 3887 4741 256 -297 742 C ATOM 1145 C CYS A 319 27.662 2.519 6.863 1.00 37.32 C ANISOU 1145 C CYS A 319 5131 4091 4959 259 -454 771 C ATOM 1146 O CYS A 319 28.605 1.944 6.302 1.00 30.06 O ANISOU 1146 O CYS A 319 4224 3246 3951 258 -579 658 O ATOM 1147 CB CYS A 319 28.438 3.873 8.788 1.00 27.04 C ANISOU 1147 CB CYS A 319 3938 2790 3548 308 -234 660 C ATOM 1148 SG CYS A 319 29.140 5.429 9.359 1.00 49.19 S ANISOU 1148 SG CYS A 319 6792 5610 6288 308 -97 567 S ATOM 1149 N VAL A 320 26.468 1.946 7.062 1.00 32.56 N ANISOU 1149 N VAL A 320 4496 3409 4464 266 -453 921 N ATOM 1150 CA VAL A 320 26.259 0.538 6.705 1.00 29.06 C ANISOU 1150 CA VAL A 320 4035 2973 4034 253 -601 929 C ATOM 1151 C VAL A 320 25.523 0.336 5.389 1.00 31.20 C ANISOU 1151 C VAL A 320 4202 3244 4409 195 -681 989 C ATOM 1152 O VAL A 320 25.258 -0.797 5.002 1.00 31.76 O ANISOU 1152 O VAL A 320 4253 3309 4504 173 -807 998 O ATOM 1153 CB VAL A 320 25.521 -0.273 7.803 1.00 34.39 C ANISOU 1153 CB VAL A 320 4728 3596 4742 267 -570 1007 C ATOM 1154 CG1 VAL A 320 26.152 -0.050 9.165 1.00 31.22 C ANISOU 1154 CG1 VAL A 320 4436 3183 4242 332 -480 952 C ATOM 1155 CG2 VAL A 320 24.025 0.061 7.820 1.00 30.36 C ANISOU 1155 CG2 VAL A 320 4115 3037 4385 235 -472 1167 C ATOM 1156 N ASP A 321 25.172 1.422 4.704 1.00 33.96 N ANISOU 1156 N ASP A 321 4494 3589 4821 171 -612 1028 N ATOM 1157 CA ASP A 321 24.542 1.281 3.386 1.00 28.54 C ANISOU 1157 CA ASP A 321 3717 2901 4227 124 -693 1073 C ATOM 1158 C ASP A 321 25.644 1.106 2.357 1.00 21.28 C ANISOU 1158 C ASP A 321 2826 2046 3215 120 -815 955 C ATOM 1159 O ASP A 321 26.719 1.690 2.489 1.00 29.23 O ANISOU 1159 O ASP A 321 3891 3101 4113 146 -789 868 O ATOM 1160 CB ASP A 321 23.654 2.483 3.031 1.00 32.17 C ANISOU 1160 CB ASP A 321 4108 3328 4789 108 -579 1160 C ATOM 1161 CG ASP A 321 23.035 2.357 1.634 1.00 47.10 C ANISOU 1161 CG ASP A 321 5913 5213 6770 67 -670 1198 C ATOM 1162 OD1 ASP A 321 22.008 1.646 1.499 1.00 48.70 O ANISOU 1162 OD1 ASP A 321 6042 5380 7080 46 -718 1286 O ATOM 1163 OD2 ASP A 321 23.578 2.958 0.670 1.00 43.53 O ANISOU 1163 OD2 ASP A 321 5469 4787 6281 55 -696 1142 O ATOM 1164 N GLN A 322 25.383 0.315 1.327 1.00 26.17 N ANISOU 1164 N GLN A 322 3403 2667 3875 89 -945 953 N ATOM 1165 CA GLN A 322 26.438 -0.045 0.402 1.00 29.94 C ANISOU 1165 CA GLN A 322 3913 3208 4255 93 -1061 831 C ATOM 1166 C GLN A 322 26.752 1.091 -0.571 1.00 32.73 C ANISOU 1166 C GLN A 322 4242 3596 4599 80 -1023 817 C ATOM 1167 O GLN A 322 27.837 1.133 -1.141 1.00 32.52 O ANISOU 1167 O GLN A 322 4244 3646 4465 92 -1075 710 O ATOM 1168 CB GLN A 322 26.102 -1.332 -0.331 1.00 29.44 C ANISOU 1168 CB GLN A 322 3840 3115 4231 67 -1209 822 C ATOM 1169 CG GLN A 322 25.978 -1.186 -1.815 1.00 49.05 C ANISOU 1169 CG GLN A 322 6285 5596 6755 39 -1270 814 C ATOM 1170 CD GLN A 322 26.079 -2.520 -2.540 1.00 60.23 C ANISOU 1170 CD GLN A 322 7737 6981 8165 32 -1424 758 C ATOM 1171 OE1 GLN A 322 27.147 -3.150 -2.583 1.00 52.08 O ANISOU 1171 OE1 GLN A 322 6783 5989 7016 70 -1485 632 O ATOM 1172 NE2 GLN A 322 24.963 -2.953 -3.126 1.00 63.80 N ANISOU 1172 NE2 GLN A 322 8136 7359 8747 -11 -1487 850 N ATOM 1173 N ASN A 323 25.807 2.013 -0.745 1.00 29.85 N ANISOU 1173 N ASN A 323 3823 3177 4341 58 -929 922 N ATOM 1174 CA ASN A 323 26.059 3.229 -1.532 1.00 30.14 C ANISOU 1174 CA ASN A 323 3855 3230 4368 45 -876 919 C ATOM 1175 C ASN A 323 26.482 4.409 -0.685 1.00 30.01 C ANISOU 1175 C ASN A 323 3893 3208 4302 58 -736 919 C ATOM 1176 O ASN A 323 27.458 5.091 -1.005 1.00 36.12 O ANISOU 1176 O ASN A 323 4703 4041 4981 45 -719 844 O ATOM 1177 CB ASN A 323 24.834 3.623 -2.361 1.00 31.89 C ANISOU 1177 CB ASN A 323 4001 3391 4726 15 -863 1014 C ATOM 1178 CG ASN A 323 24.447 2.551 -3.351 1.00 44.11 C ANISOU 1178 CG ASN A 323 5507 4927 6325 -6 -1006 1012 C ATOM 1179 OD1 ASN A 323 25.226 2.190 -4.251 1.00 44.82 O ANISOU 1179 OD1 ASN A 323 5627 5060 6343 -7 -1099 928 O ATOM 1180 ND2 ASN A 323 23.246 2.019 -3.187 1.00 46.21 N ANISOU 1180 ND2 ASN A 323 5709 5133 6715 -23 -1022 1103 N ATOM 1181 N ALA A 324 25.731 4.656 0.384 1.00 25.60 N ANISOU 1181 N ALA A 324 3331 2590 3804 67 -626 986 N ATOM 1182 CA ALA A 324 25.943 5.837 1.225 1.00 22.98 C ANISOU 1182 CA ALA A 324 3058 2231 3443 72 -476 989 C ATOM 1183 C ALA A 324 27.281 5.822 1.944 1.00 30.95 C ANISOU 1183 C ALA A 324 4128 3323 4308 74 -462 843 C ATOM 1184 O ALA A 324 27.826 6.883 2.217 1.00 38.13 O ANISOU 1184 O ALA A 324 5072 4253 5161 48 -366 782 O ATOM 1185 CB ALA A 324 24.799 5.988 2.234 1.00 27.14 C ANISOU 1185 CB ALA A 324 3553 2698 4059 93 -365 1078 C ATOM 1186 N ASN A 325 27.820 4.640 2.255 1.00 30.42 N ANISOU 1186 N ASN A 325 4077 3302 4177 104 -561 781 N ATOM 1187 CA ASN A 325 29.093 4.582 2.993 1.00 29.72 C ANISOU 1187 CA ASN A 325 4045 3298 3950 114 -552 630 C ATOM 1188 C ASN A 325 30.218 5.296 2.220 1.00 27.42 C ANISOU 1188 C ASN A 325 3750 3106 3563 67 -560 512 C ATOM 1189 O ASN A 325 31.150 5.852 2.798 1.00 27.40 O ANISOU 1189 O ASN A 325 3784 3159 3468 52 -500 403 O ATOM 1190 CB ASN A 325 29.475 3.136 3.356 1.00 27.49 C ANISOU 1190 CB ASN A 325 3788 3049 3608 161 -678 578 C ATOM 1191 CG ASN A 325 30.173 2.402 2.211 1.00 32.51 C ANISOU 1191 CG ASN A 325 4401 3772 4178 164 -841 502 C ATOM 1192 OD1 ASN A 325 29.541 1.703 1.405 1.00 28.91 O ANISOU 1192 OD1 ASN A 325 3912 3283 3789 173 -950 581 O ATOM 1193 ND2 ASN A 325 31.476 2.568 2.130 1.00 25.29 N ANISOU 1193 ND2 ASN A 325 3504 2975 3131 159 -860 348 N ATOM 1194 N HIS A 326 30.101 5.306 0.901 1.00 25.56 N ANISOU 1194 N HIS A 326 3468 2890 3354 41 -632 540 N ATOM 1195 CA HIS A 326 31.055 6.022 0.066 1.00 20.87 C ANISOU 1195 CA HIS A 326 2864 2388 2676 -12 -632 450 C ATOM 1196 C HIS A 326 31.035 7.550 0.246 1.00 24.74 C ANISOU 1196 C HIS A 326 3377 2844 3179 -70 -487 462 C ATOM 1197 O HIS A 326 31.980 8.232 -0.139 1.00 28.18 O ANISOU 1197 O HIS A 326 3817 3360 3530 -126 -465 374 O ATOM 1198 CB HIS A 326 30.856 5.632 -1.397 1.00 19.46 C ANISOU 1198 CB HIS A 326 2639 2231 2523 -14 -746 487 C ATOM 1199 CG HIS A 326 31.166 4.195 -1.664 1.00 27.79 C ANISOU 1199 CG HIS A 326 3685 3342 3533 45 -908 443 C ATOM 1200 ND1 HIS A 326 32.455 3.736 -1.842 1.00 29.32 N ANISOU 1200 ND1 HIS A 326 3881 3676 3582 59 -985 297 N ATOM 1201 CD2 HIS A 326 30.362 3.107 -1.749 1.00 24.02 C ANISOU 1201 CD2 HIS A 326 3199 2798 3128 95 -1013 524 C ATOM 1202 CE1 HIS A 326 32.429 2.430 -2.035 1.00 33.54 C ANISOU 1202 CE1 HIS A 326 4425 4200 4118 109 -1093 270 C ATOM 1203 NE2 HIS A 326 31.173 2.025 -1.988 1.00 30.93 N ANISOU 1203 NE2 HIS A 326 4091 3743 3920 116 -1107 396 N ATOM 1204 N VAL A 327 29.970 8.093 0.824 1.00 22.12 N ANISOU 1204 N VAL A 327 3061 2396 2947 -58 -390 571 N ATOM 1205 CA VAL A 327 29.970 9.521 1.146 1.00 21.76 C ANISOU 1205 CA VAL A 327 3057 2312 2901 -100 -261 575 C ATOM 1206 C VAL A 327 30.945 9.783 2.294 1.00 28.12 C ANISOU 1206 C VAL A 327 3914 3163 3607 -101 -204 461 C ATOM 1207 O VAL A 327 31.780 10.697 2.204 1.00 30.35 O ANISOU 1207 O VAL A 327 4223 3491 3819 -161 -162 382 O ATOM 1208 CB VAL A 327 28.561 10.061 1.527 1.00 24.33 C ANISOU 1208 CB VAL A 327 3388 2507 3350 -70 -174 717 C ATOM 1209 CG1 VAL A 327 28.672 11.519 1.958 1.00 31.01 C ANISOU 1209 CG1 VAL A 327 4295 3314 4173 -101 -53 704 C ATOM 1210 CG2 VAL A 327 27.562 9.919 0.364 1.00 14.65 C ANISOU 1210 CG2 VAL A 327 2109 1229 2230 -70 -229 828 C ATOM 1211 N ILE A 328 30.844 8.980 3.366 1.00 19.77 N ANISOU 1211 N ILE A 328 2875 2091 2544 -35 -208 451 N ATOM 1212 CA ILE A 328 31.753 9.123 4.494 1.00 18.20 C ANISOU 1212 CA ILE A 328 2731 1931 2251 -20 -165 336 C ATOM 1213 C ILE A 328 33.193 8.949 4.033 1.00 23.00 C ANISOU 1213 C ILE A 328 3326 2675 2737 -62 -237 183 C ATOM 1214 O ILE A 328 34.084 9.705 4.423 1.00 27.33 O ANISOU 1214 O ILE A 328 3907 3267 3211 -100 -188 86 O ATOM 1215 CB ILE A 328 31.437 8.135 5.636 1.00 27.21 C ANISOU 1215 CB ILE A 328 3901 3038 3398 63 -173 348 C ATOM 1216 CG1 ILE A 328 30.003 8.314 6.128 1.00 29.63 C ANISOU 1216 CG1 ILE A 328 4210 3226 3824 104 -91 505 C ATOM 1217 CG2 ILE A 328 32.396 8.334 6.790 1.00 20.89 C ANISOU 1217 CG2 ILE A 328 3168 2272 2498 87 -131 222 C ATOM 1218 CD1 ILE A 328 29.606 9.750 6.271 1.00 33.62 C ANISOU 1218 CD1 ILE A 328 4742 3669 4364 84 29 552 C ATOM 1219 N GLN A 329 33.415 7.981 3.158 1.00 26.16 N ANISOU 1219 N GLN A 329 3677 3148 3117 -55 -358 162 N ATOM 1220 CA GLN A 329 34.759 7.755 2.652 1.00 24.23 C ANISOU 1220 CA GLN A 329 3407 3051 2750 -85 -432 18 C ATOM 1221 C GLN A 329 35.278 8.915 1.808 1.00 18.82 C ANISOU 1221 C GLN A 329 2701 2415 2036 -181 -385 -5 C ATOM 1222 O GLN A 329 36.473 9.161 1.770 1.00 23.88 O ANISOU 1222 O GLN A 329 3331 3171 2572 -224 -393 -131 O ATOM 1223 CB GLN A 329 34.828 6.451 1.853 1.00 21.98 C ANISOU 1223 CB GLN A 329 3079 2830 2442 -41 -581 6 C ATOM 1224 CG GLN A 329 34.552 5.196 2.688 1.00 23.24 C ANISOU 1224 CG GLN A 329 3271 2957 2602 46 -649 4 C ATOM 1225 CD GLN A 329 34.933 3.917 1.941 1.00 31.44 C ANISOU 1225 CD GLN A 329 4284 4081 3582 92 -817 -47 C ATOM 1226 OE1 GLN A 329 34.082 3.115 1.608 1.00 32.14 O ANISOU 1226 OE1 GLN A 329 4365 4103 3742 128 -895 49 O ATOM 1227 NE2 GLN A 329 36.213 3.745 1.662 1.00 35.00 N ANISOU 1227 NE2 GLN A 329 4719 4680 3901 92 -877 -198 N ATOM 1228 N LYS A 330 34.387 9.609 1.109 1.00 13.18 N ANISOU 1228 N LYS A 330 1979 1616 1411 -217 -342 116 N ATOM 1229 CA LYS A 330 34.813 10.746 0.324 1.00 22.21 C ANISOU 1229 CA LYS A 330 3119 2790 2528 -313 -296 104 C ATOM 1230 C LYS A 330 35.178 11.881 1.268 1.00 27.48 C ANISOU 1230 C LYS A 330 3848 3422 3170 -357 -187 65 C ATOM 1231 O LYS A 330 36.194 12.549 1.092 1.00 23.85 O ANISOU 1231 O LYS A 330 3389 3043 2629 -437 -167 -23 O ATOM 1232 CB LYS A 330 33.720 11.215 -0.622 1.00 23.89 C ANISOU 1232 CB LYS A 330 3326 2909 2842 -331 -282 241 C ATOM 1233 CG LYS A 330 34.110 12.458 -1.376 1.00 23.01 C ANISOU 1233 CG LYS A 330 3230 2812 2699 -432 -229 236 C ATOM 1234 CD LYS A 330 35.245 12.139 -2.282 1.00 27.22 C ANISOU 1234 CD LYS A 330 3712 3503 3128 -479 -299 141 C ATOM 1235 CE LYS A 330 34.824 11.063 -3.255 1.00 31.14 C ANISOU 1235 CE LYS A 330 4156 4024 3653 -418 -412 183 C ATOM 1236 NZ LYS A 330 35.862 10.906 -4.301 1.00 34.59 N ANISOU 1236 NZ LYS A 330 4544 4615 3984 -460 -473 103 N ATOM 1237 N VAL A 331 34.346 12.071 2.284 1.00 20.78 N ANISOU 1237 N VAL A 331 3051 2455 2391 -301 -120 132 N ATOM 1238 CA VAL A 331 34.598 13.092 3.281 1.00 19.69 C ANISOU 1238 CA VAL A 331 2985 2267 2231 -320 -25 99 C ATOM 1239 C VAL A 331 35.999 12.923 3.864 1.00 19.57 C ANISOU 1239 C VAL A 331 2972 2363 2099 -338 -47 -62 C ATOM 1240 O VAL A 331 36.791 13.853 3.893 1.00 26.21 O ANISOU 1240 O VAL A 331 3837 3239 2885 -418 -11 -129 O ATOM 1241 CB VAL A 331 33.520 13.022 4.382 1.00 20.31 C ANISOU 1241 CB VAL A 331 3110 2220 2386 -227 38 187 C ATOM 1242 CG1 VAL A 331 33.919 13.816 5.594 1.00 21.43 C ANISOU 1242 CG1 VAL A 331 3332 2324 2487 -216 116 130 C ATOM 1243 CG2 VAL A 331 32.199 13.507 3.833 1.00 18.59 C ANISOU 1243 CG2 VAL A 331 2890 1895 2278 -220 76 337 C ATOM 1244 N VAL A 332 36.307 11.710 4.286 1.00 20.16 N ANISOU 1244 N VAL A 332 3024 2497 2137 -266 -115 -125 N ATOM 1245 CA VAL A 332 37.600 11.370 4.873 1.00 23.03 C ANISOU 1245 CA VAL A 332 3389 2972 2389 -262 -151 -287 C ATOM 1246 C VAL A 332 38.764 11.654 3.927 1.00 24.45 C ANISOU 1246 C VAL A 332 3508 3301 2482 -358 -192 -385 C ATOM 1247 O VAL A 332 39.831 12.107 4.358 1.00 22.55 O ANISOU 1247 O VAL A 332 3273 3133 2162 -403 -177 -504 O ATOM 1248 CB VAL A 332 37.613 9.874 5.255 1.00 24.36 C ANISOU 1248 CB VAL A 332 3545 3178 2532 -161 -241 -328 C ATOM 1249 CG1 VAL A 332 38.996 9.411 5.625 1.00 27.44 C ANISOU 1249 CG1 VAL A 332 3926 3705 2797 -151 -301 -507 C ATOM 1250 CG2 VAL A 332 36.650 9.643 6.378 1.00 23.23 C ANISOU 1250 CG2 VAL A 332 3467 2903 2457 -75 -188 -247 C ATOM 1251 N ALA A 333 38.547 11.381 2.641 1.00 13.87 N ANISOU 1251 N ALA A 333 2107 2007 1156 -387 -244 -333 N ATOM 1252 CA ALA A 333 39.556 11.610 1.612 1.00 13.26 C ANISOU 1252 CA ALA A 333 1964 2078 996 -475 -279 -408 C ATOM 1253 C ALA A 333 39.767 13.079 1.304 1.00 21.78 C ANISOU 1253 C ALA A 333 3066 3132 2077 -599 -192 -384 C ATOM 1254 O ALA A 333 40.900 13.499 1.097 1.00 23.83 O ANISOU 1254 O ALA A 333 3292 3512 2251 -683 -190 -484 O ATOM 1255 CB ALA A 333 39.193 10.877 0.323 1.00 12.46 C ANISOU 1255 CB ALA A 333 1803 2023 908 -455 -362 -351 C ATOM 1256 N VAL A 334 38.694 13.868 1.239 1.00 31.44 N ANISOU 1256 N VAL A 334 4346 4203 3397 -614 -124 -253 N ATOM 1257 CA VAL A 334 38.859 15.234 0.738 1.00 29.53 C ANISOU 1257 CA VAL A 334 4136 3934 3152 -736 -60 -222 C ATOM 1258 C VAL A 334 38.613 16.372 1.699 1.00 25.41 C ANISOU 1258 C VAL A 334 3711 3286 2659 -759 27 -200 C ATOM 1259 O VAL A 334 38.817 17.515 1.331 1.00 22.21 O ANISOU 1259 O VAL A 334 3344 2854 2242 -865 71 -182 O ATOM 1260 CB VAL A 334 38.074 15.502 -0.560 1.00 30.52 C ANISOU 1260 CB VAL A 334 4250 4013 3332 -768 -64 -104 C ATOM 1261 CG1 VAL A 334 38.468 14.493 -1.624 1.00 32.25 C ANISOU 1261 CG1 VAL A 334 4379 4370 3506 -752 -156 -135 C ATOM 1262 CG2 VAL A 334 36.572 15.499 -0.305 1.00 27.65 C ANISOU 1262 CG2 VAL A 334 3935 3481 3090 -685 -37 31 C ATOM 1263 N ILE A 335 38.199 16.084 2.926 1.00 28.02 N ANISOU 1263 N ILE A 335 4089 3537 3022 -660 49 -201 N ATOM 1264 CA ILE A 335 37.928 17.157 3.876 1.00 17.56 C ANISOU 1264 CA ILE A 335 2864 2088 1720 -663 126 -179 C ATOM 1265 C ILE A 335 38.897 17.098 5.065 1.00 24.94 C ANISOU 1265 C ILE A 335 3824 3065 2585 -643 127 -311 C ATOM 1266 O ILE A 335 39.159 16.025 5.604 1.00 31.16 O ANISOU 1266 O ILE A 335 4581 3911 3348 -559 85 -378 O ATOM 1267 CB ILE A 335 36.477 17.097 4.362 1.00 24.97 C ANISOU 1267 CB ILE A 335 3851 2877 2758 -555 168 -51 C ATOM 1268 CG1 ILE A 335 35.520 17.118 3.164 1.00 30.96 C ANISOU 1268 CG1 ILE A 335 4579 3594 3589 -569 158 71 C ATOM 1269 CG2 ILE A 335 36.170 18.234 5.323 1.00 31.35 C ANISOU 1269 CG2 ILE A 335 4770 3560 3581 -541 244 -28 C ATOM 1270 CD1 ILE A 335 35.459 18.429 2.411 1.00 22.14 C ANISOU 1270 CD1 ILE A 335 3512 2427 2473 -674 193 117 C ATOM 1271 N PRO A 336 39.429 18.258 5.483 1.00 25.32 N ANISOU 1271 N PRO A 336 3940 3079 2603 -718 167 -351 N ATOM 1272 CA PRO A 336 40.324 18.297 6.647 1.00 18.98 C ANISOU 1272 CA PRO A 336 3170 2301 1740 -696 164 -477 C ATOM 1273 C PRO A 336 39.647 17.756 7.914 1.00 26.67 C ANISOU 1273 C PRO A 336 4204 3181 2749 -540 186 -461 C ATOM 1274 O PRO A 336 38.439 17.897 8.109 1.00 27.04 O ANISOU 1274 O PRO A 336 4298 3104 2871 -468 232 -338 O ATOM 1275 CB PRO A 336 40.655 19.786 6.787 1.00 24.67 C ANISOU 1275 CB PRO A 336 3972 2954 2448 -801 205 -479 C ATOM 1276 CG PRO A 336 40.432 20.371 5.382 1.00 29.13 C ANISOU 1276 CG PRO A 336 4510 3530 3028 -922 210 -395 C ATOM 1277 CD PRO A 336 39.258 19.587 4.858 1.00 28.89 C ANISOU 1277 CD PRO A 336 4445 3464 3070 -831 206 -284 C ATOM 1278 N LEU A 337 40.445 17.130 8.768 1.00 27.81 N ANISOU 1278 N LEU A 337 4345 3388 2833 -485 154 -587 N ATOM 1279 CA LEU A 337 39.935 16.315 9.861 1.00 23.86 C ANISOU 1279 CA LEU A 337 3888 2829 2350 -335 161 -585 C ATOM 1280 C LEU A 337 39.053 17.110 10.832 1.00 22.41 C ANISOU 1280 C LEU A 337 3819 2479 2217 -261 241 -501 C ATOM 1281 O LEU A 337 38.018 16.625 11.290 1.00 30.35 O ANISOU 1281 O LEU A 337 4849 3407 3277 -152 273 -409 O ATOM 1282 CB LEU A 337 41.101 15.623 10.582 1.00 24.35 C ANISOU 1282 CB LEU A 337 3938 2990 2323 -297 105 -755 C ATOM 1283 CG LEU A 337 40.787 15.033 11.965 1.00 27.87 C ANISOU 1283 CG LEU A 337 4464 3360 2767 -146 120 -777 C ATOM 1284 CD1 LEU A 337 39.645 14.002 11.883 1.00 23.40 C ANISOU 1284 CD1 LEU A 337 3882 2751 2260 -52 121 -662 C ATOM 1285 CD2 LEU A 337 42.034 14.407 12.553 1.00 21.69 C ANISOU 1285 CD2 LEU A 337 3671 2681 1888 -116 54 -959 C ATOM 1286 N LYS A 338 39.435 18.346 11.103 1.00 26.60 N ANISOU 1286 N LYS A 338 4420 2957 2729 -322 269 -526 N ATOM 1287 CA LYS A 338 38.690 19.189 12.032 1.00 32.01 C ANISOU 1287 CA LYS A 338 5226 3489 3448 -244 335 -458 C ATOM 1288 C LYS A 338 37.187 19.138 11.749 1.00 31.62 C ANISOU 1288 C LYS A 338 5180 3350 3486 -179 386 -291 C ATOM 1289 O LYS A 338 36.369 19.055 12.654 1.00 34.08 O ANISOU 1289 O LYS A 338 5551 3571 3827 -52 436 -231 O ATOM 1290 CB LYS A 338 39.226 20.630 11.986 1.00 27.52 C ANISOU 1290 CB LYS A 338 4729 2873 2853 -348 341 -486 C ATOM 1291 CG LYS A 338 38.672 21.560 13.059 1.00 31.19 C ANISOU 1291 CG LYS A 338 5336 3185 3332 -258 391 -445 C ATOM 1292 CD LYS A 338 38.593 20.849 14.404 1.00 34.07 C ANISOU 1292 CD LYS A 338 5746 3521 3679 -97 406 -492 C ATOM 1293 CE LYS A 338 37.842 21.661 15.448 1.00 31.74 C ANISOU 1293 CE LYS A 338 5588 3075 3398 23 463 -430 C ATOM 1294 NZ LYS A 338 37.781 20.884 16.737 1.00 33.38 N ANISOU 1294 NZ LYS A 338 5837 3262 3583 184 482 -474 N ATOM 1295 N ASN A 339 36.828 19.150 10.479 1.00 33.06 N ANISOU 1295 N ASN A 339 5293 3564 3706 -261 372 -218 N ATOM 1296 CA ASN A 339 35.426 19.132 10.096 1.00 31.98 C ANISOU 1296 CA ASN A 339 5149 3348 3656 -208 411 -65 C ATOM 1297 C ASN A 339 34.678 17.824 10.314 1.00 32.76 C ANISOU 1297 C ASN A 339 5188 3459 3802 -103 409 -9 C ATOM 1298 O ASN A 339 33.454 17.815 10.406 1.00 35.71 O ANISOU 1298 O ASN A 339 5568 3754 4248 -31 455 116 O ATOM 1299 CB ASN A 339 35.303 19.555 8.647 1.00 28.68 C ANISOU 1299 CB ASN A 339 4682 2954 3262 -327 390 -10 C ATOM 1300 CG ASN A 339 35.692 20.978 8.459 1.00 33.22 C ANISOU 1300 CG ASN A 339 5338 3479 3806 -423 405 -23 C ATOM 1301 OD1 ASN A 339 34.927 21.886 8.780 1.00 42.15 O ANISOU 1301 OD1 ASN A 339 6560 4488 4966 -383 451 52 O ATOM 1302 ND2 ASN A 339 36.894 21.194 7.966 1.00 31.53 N ANISOU 1302 ND2 ASN A 339 5095 3358 3527 -551 364 -121 N ATOM 1303 N TRP A 340 35.400 16.717 10.390 1.00 30.32 N ANISOU 1303 N TRP A 340 4821 3250 3448 -95 350 -100 N ATOM 1304 CA TRP A 340 34.721 15.446 10.552 1.00 28.08 C ANISOU 1304 CA TRP A 340 4490 2974 3205 -7 334 -45 C ATOM 1305 C TRP A 340 35.202 14.689 11.786 1.00 30.25 C ANISOU 1305 C TRP A 340 4806 3263 3424 87 326 -135 C ATOM 1306 O TRP A 340 35.044 13.479 11.888 1.00 30.27 O ANISOU 1306 O TRP A 340 4771 3300 3429 140 285 -133 O ATOM 1307 CB TRP A 340 34.797 14.609 9.260 1.00 21.13 C ANISOU 1307 CB TRP A 340 3503 2185 2339 -69 255 -34 C ATOM 1308 CG TRP A 340 36.172 14.355 8.707 1.00 20.80 C ANISOU 1308 CG TRP A 340 3414 2280 2209 -150 179 -174 C ATOM 1309 CD1 TRP A 340 36.841 15.102 7.777 1.00 28.25 C ANISOU 1309 CD1 TRP A 340 4330 3283 3120 -271 164 -212 C ATOM 1310 CD2 TRP A 340 37.030 13.245 9.020 1.00 21.06 C ANISOU 1310 CD2 TRP A 340 3418 2414 2169 -114 105 -295 C ATOM 1311 NE1 TRP A 340 38.076 14.536 7.507 1.00 22.73 N ANISOU 1311 NE1 TRP A 340 3576 2728 2334 -312 92 -348 N ATOM 1312 CE2 TRP A 340 38.209 13.394 8.256 1.00 16.65 C ANISOU 1312 CE2 TRP A 340 2806 1985 1536 -212 51 -405 C ATOM 1313 CE3 TRP A 340 36.909 12.137 9.867 1.00 23.67 C ANISOU 1313 CE3 TRP A 340 3768 2741 2486 -8 78 -320 C ATOM 1314 CZ2 TRP A 340 39.266 12.477 8.320 1.00 24.05 C ANISOU 1314 CZ2 TRP A 340 3702 3053 2384 -196 -32 -546 C ATOM 1315 CZ3 TRP A 340 37.961 11.236 9.940 1.00 25.03 C ANISOU 1315 CZ3 TRP A 340 3914 3028 2567 7 -9 -461 C ATOM 1316 CH2 TRP A 340 39.126 11.412 9.169 1.00 26.42 C ANISOU 1316 CH2 TRP A 340 4031 3340 2669 -83 -65 -576 C ATOM 1317 N GLU A 341 35.778 15.418 12.734 1.00 35.26 N ANISOU 1317 N GLU A 341 5528 3863 4007 110 359 -214 N ATOM 1318 CA GLU A 341 36.152 14.815 14.001 1.00 44.73 C ANISOU 1318 CA GLU A 341 6787 5055 5154 215 360 -296 C ATOM 1319 C GLU A 341 34.935 14.224 14.684 1.00 39.12 C ANISOU 1319 C GLU A 341 6099 4265 4499 334 415 -175 C ATOM 1320 O GLU A 341 35.035 13.246 15.402 1.00 36.30 O ANISOU 1320 O GLU A 341 5760 3920 4111 414 397 -213 O ATOM 1321 CB GLU A 341 36.818 15.823 14.931 1.00 47.87 C ANISOU 1321 CB GLU A 341 7286 5405 5497 231 390 -385 C ATOM 1322 CG GLU A 341 38.295 15.558 15.121 1.00 55.71 C ANISOU 1322 CG GLU A 341 8273 6497 6399 193 317 -568 C ATOM 1323 CD GLU A 341 38.855 16.269 16.337 1.00 66.92 C ANISOU 1323 CD GLU A 341 9805 7853 7768 251 340 -658 C ATOM 1324 OE1 GLU A 341 38.430 17.425 16.583 1.00 72.11 O ANISOU 1324 OE1 GLU A 341 10536 8411 8453 251 395 -596 O ATOM 1325 OE2 GLU A 341 39.716 15.672 17.038 1.00 63.23 O ANISOU 1325 OE2 GLU A 341 9360 7432 7232 301 295 -794 O ATOM 1326 N PHE A 342 33.777 14.819 14.460 1.00 32.21 N ANISOU 1326 N PHE A 342 5223 3311 3703 347 482 -30 N ATOM 1327 CA PHE A 342 32.585 14.316 15.116 1.00 31.28 C ANISOU 1327 CA PHE A 342 5115 3129 3641 456 544 92 C ATOM 1328 C PHE A 342 32.261 12.877 14.692 1.00 34.97 C ANISOU 1328 C PHE A 342 5500 3648 4140 457 487 132 C ATOM 1329 O PHE A 342 31.642 12.122 15.438 1.00 37.63 O ANISOU 1329 O PHE A 342 5851 3952 4494 545 517 191 O ATOM 1330 CB PHE A 342 31.398 15.265 14.912 1.00 23.92 C ANISOU 1330 CB PHE A 342 4189 2113 2785 473 623 236 C ATOM 1331 CG PHE A 342 30.847 15.275 13.525 1.00 31.98 C ANISOU 1331 CG PHE A 342 5115 3155 3880 385 592 321 C ATOM 1332 CD1 PHE A 342 29.772 14.460 13.187 1.00 36.24 C ANISOU 1332 CD1 PHE A 342 5577 3690 4504 412 596 446 C ATOM 1333 CD2 PHE A 342 31.365 16.135 12.562 1.00 36.73 C ANISOU 1333 CD2 PHE A 342 5710 3776 4470 275 560 283 C ATOM 1334 CE1 PHE A 342 29.241 14.472 11.907 1.00 27.77 C ANISOU 1334 CE1 PHE A 342 4422 2628 3502 340 562 522 C ATOM 1335 CE2 PHE A 342 30.832 16.159 11.273 1.00 31.17 C ANISOU 1335 CE2 PHE A 342 4929 3084 3830 202 532 363 C ATOM 1336 CZ PHE A 342 29.776 15.323 10.949 1.00 31.90 C ANISOU 1336 CZ PHE A 342 4945 3169 4007 240 530 478 C ATOM 1337 N ILE A 343 32.714 12.491 13.506 1.00 37.18 N ANISOU 1337 N ILE A 343 5699 4008 4421 361 401 98 N ATOM 1338 CA ILE A 343 32.424 11.164 12.982 1.00 35.99 C ANISOU 1338 CA ILE A 343 5475 3902 4299 358 328 135 C ATOM 1339 C ILE A 343 33.279 10.136 13.695 1.00 36.36 C ANISOU 1339 C ILE A 343 5559 3999 4258 408 266 12 C ATOM 1340 O ILE A 343 32.807 9.066 14.101 1.00 35.85 O ANISOU 1340 O ILE A 343 5497 3918 4206 467 246 57 O ATOM 1341 CB ILE A 343 32.678 11.128 11.482 1.00 31.07 C ANISOU 1341 CB ILE A 343 4763 3347 3693 253 250 130 C ATOM 1342 CG1 ILE A 343 31.712 12.093 10.786 1.00 28.26 C ANISOU 1342 CG1 ILE A 343 4382 2929 3428 215 308 259 C ATOM 1343 CG2 ILE A 343 32.537 9.718 10.942 1.00 26.96 C ANISOU 1343 CG2 ILE A 343 4180 2877 3187 258 151 147 C ATOM 1344 CD1 ILE A 343 31.880 12.133 9.287 1.00 28.72 C ANISOU 1344 CD1 ILE A 343 4364 3044 3506 117 239 266 C ATOM 1345 N VAL A 344 34.544 10.486 13.863 1.00 30.49 N ANISOU 1345 N VAL A 344 4848 3314 3422 382 233 -145 N ATOM 1346 CA VAL A 344 35.464 9.662 14.614 1.00 32.62 C ANISOU 1346 CA VAL A 344 5165 3632 3597 438 175 -285 C ATOM 1347 C VAL A 344 34.904 9.364 16.004 1.00 44.46 C ANISOU 1347 C VAL A 344 6757 5041 5096 559 242 -245 C ATOM 1348 O VAL A 344 34.855 8.210 16.443 1.00 44.31 O ANISOU 1348 O VAL A 344 6760 5026 5049 619 198 -257 O ATOM 1349 CB VAL A 344 36.806 10.365 14.782 1.00 27.86 C ANISOU 1349 CB VAL A 344 4590 3089 2907 400 155 -452 C ATOM 1350 CG1 VAL A 344 37.704 9.578 15.737 1.00 24.70 C ANISOU 1350 CG1 VAL A 344 4252 2725 2407 479 102 -603 C ATOM 1351 CG2 VAL A 344 37.484 10.567 13.418 1.00 17.97 C ANISOU 1351 CG2 VAL A 344 3241 1946 1639 278 87 -502 C ATOM 1352 N ASP A 345 34.479 10.406 16.704 1.00 49.34 N ANISOU 1352 N ASP A 345 7435 5575 5736 599 347 -195 N ATOM 1353 CA ASP A 345 34.016 10.229 18.072 1.00 49.66 C ANISOU 1353 CA ASP A 345 7570 5535 5762 723 420 -163 C ATOM 1354 C ASP A 345 32.680 9.502 18.134 1.00 47.33 C ANISOU 1354 C ASP A 345 7242 5193 5547 764 461 8 C ATOM 1355 O ASP A 345 32.398 8.765 19.077 1.00 53.24 O ANISOU 1355 O ASP A 345 8049 5907 6273 852 483 28 O ATOM 1356 CB ASP A 345 34.006 11.568 18.811 1.00 57.90 C ANISOU 1356 CB ASP A 345 8695 6506 6796 767 510 -168 C ATOM 1357 CG ASP A 345 35.405 11.968 19.278 1.00 66.98 C ANISOU 1357 CG ASP A 345 9912 7687 7849 765 464 -357 C ATOM 1358 OD1 ASP A 345 36.042 11.137 19.962 1.00 76.15 O ANISOU 1358 OD1 ASP A 345 11122 8873 8940 827 418 -464 O ATOM 1359 OD2 ASP A 345 35.879 13.081 18.957 1.00 59.53 O ANISOU 1359 OD2 ASP A 345 8973 6744 6900 700 468 -401 O ATOM 1360 N PHE A 346 31.871 9.690 17.106 1.00 38.80 N ANISOU 1360 N PHE A 346 6069 4114 4560 695 467 130 N ATOM 1361 CA PHE A 346 30.618 8.975 17.007 1.00 35.89 C ANISOU 1361 CA PHE A 346 5647 3711 4276 715 492 293 C ATOM 1362 C PHE A 346 30.875 7.478 16.849 1.00 35.50 C ANISOU 1362 C PHE A 346 5581 3706 4202 708 385 261 C ATOM 1363 O PHE A 346 30.304 6.657 17.558 1.00 40.03 O ANISOU 1363 O PHE A 346 6184 4242 4784 768 405 329 O ATOM 1364 CB PHE A 346 29.827 9.505 15.819 1.00 32.88 C ANISOU 1364 CB PHE A 346 5168 3328 3997 638 500 408 C ATOM 1365 CG PHE A 346 28.548 8.761 15.561 1.00 39.22 C ANISOU 1365 CG PHE A 346 5898 4104 4900 644 511 573 C ATOM 1366 CD1 PHE A 346 27.337 9.263 16.002 1.00 35.23 C ANISOU 1366 CD1 PHE A 346 5381 3537 4467 698 624 718 C ATOM 1367 CD2 PHE A 346 28.554 7.570 14.859 1.00 35.01 C ANISOU 1367 CD2 PHE A 346 5305 3610 4388 597 401 584 C ATOM 1368 CE1 PHE A 346 26.168 8.594 15.752 1.00 38.96 C ANISOU 1368 CE1 PHE A 346 5774 3992 5037 695 633 870 C ATOM 1369 CE2 PHE A 346 27.379 6.906 14.605 1.00 41.22 C ANISOU 1369 CE2 PHE A 346 6023 4366 5272 593 402 739 C ATOM 1370 CZ PHE A 346 26.183 7.419 15.053 1.00 38.93 C ANISOU 1370 CZ PHE A 346 5712 4019 5061 637 521 883 C ATOM 1371 N VAL A 347 31.740 7.145 15.902 1.00 31.89 N ANISOU 1371 N VAL A 347 5079 3329 3708 635 270 159 N ATOM 1372 CA VAL A 347 32.110 5.767 15.596 1.00 30.15 C ANISOU 1372 CA VAL A 347 4846 3159 3450 629 144 111 C ATOM 1373 C VAL A 347 32.855 5.100 16.749 1.00 29.86 C ANISOU 1373 C VAL A 347 4917 3123 3304 712 118 -11 C ATOM 1374 O VAL A 347 32.809 3.896 16.915 1.00 32.60 O ANISOU 1374 O VAL A 347 5289 3472 3625 740 42 -12 O ATOM 1375 CB VAL A 347 32.991 5.736 14.312 1.00 29.40 C ANISOU 1375 CB VAL A 347 4682 3165 3322 543 31 12 C ATOM 1376 CG1 VAL A 347 33.739 4.453 14.206 1.00 31.68 C ANISOU 1376 CG1 VAL A 347 4987 3520 3528 562 -107 -96 C ATOM 1377 CG2 VAL A 347 32.134 5.971 13.065 1.00 28.06 C ANISOU 1377 CG2 VAL A 347 4410 2989 3262 469 24 145 C ATOM 1378 N ALA A 348 33.552 5.895 17.546 1.00 38.89 N ANISOU 1378 N ALA A 348 6135 4260 4383 755 174 -116 N ATOM 1379 CA ALA A 348 34.296 5.359 18.674 1.00 37.06 C ANISOU 1379 CA ALA A 348 6014 4023 4046 844 152 -243 C ATOM 1380 C ALA A 348 33.387 5.112 19.875 1.00 40.75 C ANISOU 1380 C ALA A 348 6561 4392 4532 940 249 -134 C ATOM 1381 O ALA A 348 33.771 4.410 20.792 1.00 38.86 O ANISOU 1381 O ALA A 348 6419 4133 4212 1019 226 -207 O ATOM 1382 CB ALA A 348 35.441 6.287 19.060 1.00 33.27 C ANISOU 1382 CB ALA A 348 5581 3572 3488 853 163 -405 C ATOM 1383 N THR A 349 32.190 5.690 19.880 1.00 41.36 N ANISOU 1383 N THR A 349 6598 4409 4708 938 360 38 N ATOM 1384 CA THR A 349 31.223 5.355 20.919 1.00 41.51 C ANISOU 1384 CA THR A 349 6671 4350 4749 1023 455 162 C ATOM 1385 C THR A 349 30.952 3.853 20.853 1.00 49.77 C ANISOU 1385 C THR A 349 7718 5399 5792 1015 370 203 C ATOM 1386 O THR A 349 30.530 3.326 19.817 1.00 49.35 O ANISOU 1386 O THR A 349 7570 5374 5807 934 299 277 O ATOM 1387 CB THR A 349 29.913 6.115 20.744 1.00 45.29 C ANISOU 1387 CB THR A 349 7081 4786 5342 1015 574 348 C ATOM 1388 OG1 THR A 349 30.120 7.500 21.051 1.00 42.67 O ANISOU 1388 OG1 THR A 349 6785 4432 4997 1047 655 311 O ATOM 1389 CG2 THR A 349 28.855 5.550 21.673 1.00 42.13 C ANISOU 1389 CG2 THR A 349 6712 4328 4969 1089 662 490 C ATOM 1390 N PRO A 350 31.219 3.154 21.964 1.00 53.45 N ANISOU 1390 N PRO A 350 8569 5339 6399 263 599 1125 N ATOM 1391 CA PRO A 350 31.221 1.691 22.057 1.00 47.47 C ANISOU 1391 CA PRO A 350 7707 4585 5746 246 440 1148 C ATOM 1392 C PRO A 350 30.051 1.019 21.345 1.00 45.57 C ANISOU 1392 C PRO A 350 7274 4360 5679 240 436 1337 C ATOM 1393 O PRO A 350 30.269 0.082 20.578 1.00 41.78 O ANISOU 1393 O PRO A 350 6649 3914 5312 174 257 1280 O ATOM 1394 CB PRO A 350 31.137 1.450 23.562 1.00 44.55 C ANISOU 1394 CB PRO A 350 7502 4144 5282 335 497 1222 C ATOM 1395 CG PRO A 350 31.840 2.619 24.146 1.00 45.88 C ANISOU 1395 CG PRO A 350 7886 4276 5269 358 576 1103 C ATOM 1396 CD PRO A 350 31.523 3.788 23.260 1.00 48.69 C ANISOU 1396 CD PRO A 350 8209 4664 5626 340 694 1108 C ATOM 1397 N GLU A 351 28.834 1.487 21.599 1.00 47.05 N ANISOU 1397 N GLU A 351 7467 4517 5892 312 624 1568 N ATOM 1398 CA GLU A 351 27.657 0.892 20.986 1.00 49.70 C ANISOU 1398 CA GLU A 351 7623 4852 6408 305 619 1786 C ATOM 1399 C GLU A 351 27.679 1.037 19.469 1.00 44.57 C ANISOU 1399 C GLU A 351 6824 4260 5852 204 536 1714 C ATOM 1400 O GLU A 351 27.340 0.102 18.740 1.00 45.03 O ANISOU 1400 O GLU A 351 6730 4325 6056 153 385 1765 O ATOM 1401 CB GLU A 351 26.384 1.519 21.545 1.00 62.26 C ANISOU 1401 CB GLU A 351 9253 6397 8006 406 862 2063 C ATOM 1402 CG GLU A 351 25.108 1.018 20.860 1.00 73.49 C ANISOU 1402 CG GLU A 351 10480 7809 9634 391 860 2324 C ATOM 1403 CD GLU A 351 24.920 -0.499 20.975 1.00 76.58 C ANISOU 1403 CD GLU A 351 10751 8181 10167 377 662 2406 C ATOM 1404 OE1 GLU A 351 25.538 -1.117 21.873 1.00 80.61 O ANISOU 1404 OE1 GLU A 351 11340 8679 10610 412 587 2323 O ATOM 1405 OE2 GLU A 351 24.151 -1.074 20.167 1.00 70.54 O ANISOU 1405 OE2 GLU A 351 9788 7434 9581 329 570 2524 O ATOM 1406 N HIS A 352 28.088 2.211 19.005 1.00 37.38 N ANISOU 1406 N HIS A 352 5963 3385 4853 178 626 1597 N ATOM 1407 CA HIS A 352 28.186 2.493 17.574 1.00 37.20 C ANISOU 1407 CA HIS A 352 5811 3426 4897 88 564 1518 C ATOM 1408 C HIS A 352 29.277 1.654 16.925 1.00 38.68 C ANISOU 1408 C HIS A 352 5938 3660 5099 20 329 1297 C ATOM 1409 O HIS A 352 29.066 1.074 15.862 1.00 45.09 O ANISOU 1409 O HIS A 352 6614 4498 6021 -36 206 1297 O ATOM 1410 CB HIS A 352 28.456 3.985 17.326 1.00 41.15 C ANISOU 1410 CB HIS A 352 6381 3959 5295 82 716 1442 C ATOM 1411 CG HIS A 352 27.431 4.896 17.930 1.00 48.85 C ANISOU 1411 CG HIS A 352 7429 4887 6246 158 961 1649 C ATOM 1412 ND1 HIS A 352 27.708 6.201 18.281 1.00 56.51 N ANISOU 1412 ND1 HIS A 352 8535 5851 7084 191 1113 1590 N ATOM 1413 CD2 HIS A 352 26.132 4.686 18.256 1.00 48.40 C ANISOU 1413 CD2 HIS A 352 7329 4779 6280 214 1079 1924 C ATOM 1414 CE1 HIS A 352 26.620 6.760 18.783 1.00 55.56 C ANISOU 1414 CE1 HIS A 352 8462 5682 6968 269 1326 1811 C ATOM 1415 NE2 HIS A 352 25.652 5.861 18.784 1.00 56.20 N ANISOU 1415 NE2 HIS A 352 8431 5736 7185 287 1316 2024 N ATOM 1416 N LEU A 353 30.434 1.583 17.574 1.00 34.90 N ANISOU 1416 N LEU A 353 5570 3183 4508 29 266 1117 N ATOM 1417 CA LEU A 353 31.549 0.805 17.059 1.00 32.36 C ANISOU 1417 CA LEU A 353 5200 2901 4194 -24 59 914 C ATOM 1418 C LEU A 353 31.086 -0.623 16.842 1.00 41.10 C ANISOU 1418 C LEU A 353 6197 3985 5434 -35 -99 989 C ATOM 1419 O LEU A 353 31.357 -1.234 15.805 1.00 38.47 O ANISOU 1419 O LEU A 353 5762 3687 5169 -83 -251 902 O ATOM 1420 CB LEU A 353 32.731 0.824 18.040 1.00 29.95 C ANISOU 1420 CB LEU A 353 5035 2577 3767 -10 17 762 C ATOM 1421 CG LEU A 353 34.031 0.234 17.487 1.00 33.99 C ANISOU 1421 CG LEU A 353 5502 3134 4277 -62 -171 549 C ATOM 1422 CD1 LEU A 353 34.597 1.126 16.383 1.00 37.86 C ANISOU 1422 CD1 LEU A 353 5943 3699 4741 -101 -155 432 C ATOM 1423 CD2 LEU A 353 35.071 -0.005 18.569 1.00 29.93 C ANISOU 1423 CD2 LEU A 353 5112 2583 3676 -54 -235 442 C ATOM 1424 N ARG A 354 30.370 -1.145 17.830 1.00 43.50 N ANISOU 1424 N ARG A 354 6527 4226 5774 18 -65 1159 N ATOM 1425 CA ARG A 354 29.856 -2.504 17.764 1.00 42.15 C ANISOU 1425 CA ARG A 354 6251 4022 5743 12 -220 1261 C ATOM 1426 C ARG A 354 28.972 -2.740 16.526 1.00 42.61 C ANISOU 1426 C ARG A 354 6163 4083 5943 -32 -280 1372 C ATOM 1427 O ARG A 354 29.110 -3.756 15.853 1.00 45.19 O ANISOU 1427 O ARG A 354 6404 4407 6358 -71 -482 1320 O ATOM 1428 CB ARG A 354 29.086 -2.839 19.041 1.00 39.23 C ANISOU 1428 CB ARG A 354 5924 3588 5395 88 -137 1470 C ATOM 1429 CG ARG A 354 28.829 -4.320 19.225 1.00 49.95 C ANISOU 1429 CG ARG A 354 7184 4909 6884 85 -325 1548 C ATOM 1430 CD ARG A 354 27.929 -4.583 20.425 1.00 59.68 C ANISOU 1430 CD ARG A 354 8436 6086 8153 170 -224 1798 C ATOM 1431 NE ARG A 354 26.527 -4.638 20.032 1.00 68.13 N ANISOU 1431 NE ARG A 354 9388 7123 9375 186 -173 2080 N ATOM 1432 CZ ARG A 354 25.808 -3.570 19.716 1.00 77.30 C ANISOU 1432 CZ ARG A 354 10558 8287 10527 203 18 2204 C ATOM 1433 NH1 ARG A 354 26.372 -2.375 19.754 1.00 82.93 N ANISOU 1433 NH1 ARG A 354 11395 9035 11080 209 168 2059 N ATOM 1434 NH2 ARG A 354 24.536 -3.692 19.359 1.00 79.44 N ANISOU 1434 NH2 ARG A 354 10709 8520 10956 210 52 2481 N ATOM 1435 N GLN A 355 28.073 -1.806 16.224 1.00 37.75 N ANISOU 1435 N GLN A 355 5528 3467 5348 -26 -112 1525 N ATOM 1436 CA GLN A 355 27.160 -1.991 15.096 1.00 40.21 C ANISOU 1436 CA GLN A 355 5707 3770 5802 -76 -168 1657 C ATOM 1437 C GLN A 355 27.881 -1.786 13.775 1.00 42.31 C ANISOU 1437 C GLN A 355 5934 4103 6039 -143 -266 1447 C ATOM 1438 O GLN A 355 27.715 -2.551 12.836 1.00 49.98 O ANISOU 1438 O GLN A 355 6820 5066 7105 -187 -442 1438 O ATOM 1439 CB GLN A 355 25.984 -1.018 15.167 1.00 44.09 C ANISOU 1439 CB GLN A 355 6181 4240 6332 -54 52 1897 C ATOM 1440 CG GLN A 355 25.022 -1.215 16.338 1.00 47.41 C ANISOU 1440 CG GLN A 355 6619 4591 6805 29 170 2168 C ATOM 1441 CD GLN A 355 23.900 -0.180 16.321 1.00 53.97 C ANISOU 1441 CD GLN A 355 7413 5424 7671 59 404 2381 C ATOM 1442 OE1 GLN A 355 23.201 -0.030 15.315 1.00 57.06 O ANISOU 1442 OE1 GLN A 355 7663 5844 8174 1 384 2453 O ATOM 1443 NE2 GLN A 355 23.730 0.544 17.428 1.00 54.39 N ANISOU 1443 NE2 GLN A 355 7567 5479 7619 157 622 2434 N ATOM 1444 N ILE A 356 28.694 -0.745 13.705 1.00 33.15 N ANISOU 1444 N ILE A 356 4844 3006 4746 -144 -158 1284 N ATOM 1445 CA ILE A 356 29.406 -0.434 12.475 1.00 29.57 C ANISOU 1445 CA ILE A 356 4349 2627 4259 -194 -226 1099 C ATOM 1446 C ILE A 356 30.427 -1.509 12.083 1.00 37.70 C ANISOU 1446 C ILE A 356 5369 3676 5279 -204 -446 901 C ATOM 1447 O ILE A 356 30.527 -1.894 10.913 1.00 38.18 O ANISOU 1447 O ILE A 356 5363 3764 5380 -236 -572 831 O ATOM 1448 CB ILE A 356 30.077 0.925 12.596 1.00 25.53 C ANISOU 1448 CB ILE A 356 3908 2176 3618 -188 -66 987 C ATOM 1449 CG1 ILE A 356 28.993 1.991 12.797 1.00 27.23 C ANISOU 1449 CG1 ILE A 356 4125 2370 3851 -178 150 1185 C ATOM 1450 CG2 ILE A 356 30.906 1.234 11.364 1.00 27.39 C ANISOU 1450 CG2 ILE A 356 4091 2499 3819 -228 -135 802 C ATOM 1451 CD1 ILE A 356 29.530 3.344 13.245 1.00 27.86 C ANISOU 1451 CD1 ILE A 356 4304 2482 3801 -156 318 1106 C ATOM 1452 N CYS A 357 31.180 -2.005 13.054 1.00 38.76 N ANISOU 1452 N CYS A 357 5575 3793 5359 -173 -494 815 N ATOM 1453 CA CYS A 357 32.218 -2.980 12.744 1.00 40.55 C ANISOU 1453 CA CYS A 357 5794 4037 5575 -179 -687 629 C ATOM 1454 C CYS A 357 31.675 -4.376 12.541 1.00 48.22 C ANISOU 1454 C CYS A 357 6702 4948 6671 -184 -876 702 C ATOM 1455 O CYS A 357 32.384 -5.249 12.070 1.00 53.46 O ANISOU 1455 O CYS A 357 7352 5620 7341 -186 -1048 559 O ATOM 1456 CB CYS A 357 33.294 -3.003 13.825 1.00 37.95 C ANISOU 1456 CB CYS A 357 5560 3707 5150 -156 -681 508 C ATOM 1457 SG CYS A 357 34.250 -1.490 13.856 1.00 42.42 S ANISOU 1457 SG CYS A 357 6203 4340 5576 -158 -532 378 S ATOM 1458 N SER A 358 30.423 -4.603 12.903 1.00 48.13 N ANISOU 1458 N SER A 358 6653 4871 6765 -180 -849 934 N ATOM 1459 CA SER A 358 29.859 -5.912 12.674 1.00 44.26 C ANISOU 1459 CA SER A 358 6094 4314 6410 -190 -1050 1024 C ATOM 1460 C SER A 358 29.180 -5.924 11.312 1.00 35.64 C ANISOU 1460 C SER A 358 4930 3213 5398 -233 -1128 1079 C ATOM 1461 O SER A 358 28.527 -6.895 10.952 1.00 39.48 O ANISOU 1461 O SER A 358 5360 3629 6011 -250 -1304 1184 O ATOM 1462 CB SER A 358 28.894 -6.300 13.798 1.00 47.06 C ANISOU 1462 CB SER A 358 6430 4595 6856 -161 -1010 1268 C ATOM 1463 OG SER A 358 27.684 -5.578 13.685 1.00 54.74 O ANISOU 1463 OG SER A 358 7362 5544 7893 -163 -865 1501 O ATOM 1464 N ASP A 359 29.349 -4.847 10.553 1.00 37.43 N ANISOU 1464 N ASP A 359 5162 3508 5553 -252 -1009 1011 N ATOM 1465 CA ASP A 359 28.743 -4.725 9.217 1.00 32.47 C ANISOU 1465 CA ASP A 359 4474 2878 4985 -297 -1069 1056 C ATOM 1466 C ASP A 359 29.743 -4.741 8.046 1.00 26.04 C ANISOU 1466 C ASP A 359 3676 2135 4084 -299 -1162 814 C ATOM 1467 O ASP A 359 30.847 -4.225 8.129 1.00 25.90 O ANISOU 1467 O ASP A 359 3699 2197 3944 -274 -1088 632 O ATOM 1468 CB ASP A 359 27.896 -3.459 9.122 1.00 31.13 C ANISOU 1468 CB ASP A 359 4274 2725 4828 -321 -854 1219 C ATOM 1469 CG ASP A 359 27.168 -3.345 7.788 1.00 40.09 C ANISOU 1469 CG ASP A 359 5342 3849 6042 -379 -919 1294 C ATOM 1470 OD1 ASP A 359 26.087 -3.961 7.631 1.00 43.92 O ANISOU 1470 OD1 ASP A 359 5772 4242 6674 -409 -1023 1503 O ATOM 1471 OD2 ASP A 359 27.673 -2.630 6.898 1.00 36.83 O ANISOU 1471 OD2 ASP A 359 4929 3517 5549 -396 -873 1156 O ATOM 1472 N LYS A 360 29.311 -5.330 6.951 1.00 31.32 N ANISOU 1472 N LYS A 360 4313 2766 4819 -325 -1327 830 N ATOM 1473 CA LYS A 360 30.098 -5.457 5.738 1.00 40.78 C ANISOU 1473 CA LYS A 360 5534 4021 5940 -313 -1427 627 C ATOM 1474 C LYS A 360 30.694 -4.118 5.302 1.00 37.78 C ANISOU 1474 C LYS A 360 5150 3759 5445 -311 -1238 523 C ATOM 1475 O LYS A 360 31.884 -4.012 5.012 1.00 38.76 O ANISOU 1475 O LYS A 360 5303 3962 5461 -269 -1238 321 O ATOM 1476 CB LYS A 360 29.177 -5.995 4.639 1.00 44.30 C ANISOU 1476 CB LYS A 360 5956 4393 6482 -352 -1597 725 C ATOM 1477 CG LYS A 360 29.876 -6.552 3.433 1.00 50.03 C ANISOU 1477 CG LYS A 360 6730 5140 7137 -321 -1763 528 C ATOM 1478 CD LYS A 360 28.859 -7.000 2.384 1.00 58.19 C ANISOU 1478 CD LYS A 360 7761 6085 8266 -367 -1936 645 C ATOM 1479 CE LYS A 360 28.408 -8.432 2.606 1.00 66.26 C ANISOU 1479 CE LYS A 360 8804 6969 9401 -367 -2194 718 C ATOM 1480 NZ LYS A 360 29.539 -9.401 2.513 1.00 65.28 N ANISOU 1480 NZ LYS A 360 8757 6853 9193 -292 -2343 486 N ATOM 1481 N TYR A 361 29.858 -3.091 5.255 1.00 34.96 N ANISOU 1481 N TYR A 361 4748 3414 5123 -354 -1076 676 N ATOM 1482 CA TYR A 361 30.288 -1.811 4.710 1.00 29.17 C ANISOU 1482 CA TYR A 361 3994 2787 4301 -362 -914 598 C ATOM 1483 C TYR A 361 30.802 -0.892 5.794 1.00 29.00 C ANISOU 1483 C TYR A 361 4000 2810 4206 -341 -722 576 C ATOM 1484 O TYR A 361 31.729 -0.126 5.556 1.00 28.81 O ANISOU 1484 O TYR A 361 3981 2879 4085 -324 -642 435 O ATOM 1485 CB TYR A 361 29.184 -1.174 3.856 1.00 28.67 C ANISOU 1485 CB TYR A 361 3865 2717 4311 -425 -859 756 C ATOM 1486 CG TYR A 361 28.702 -2.113 2.765 1.00 30.61 C ANISOU 1486 CG TYR A 361 4106 2902 4624 -448 -1077 775 C ATOM 1487 CD1 TYR A 361 29.506 -2.407 1.665 1.00 28.45 C ANISOU 1487 CD1 TYR A 361 3862 2685 4264 -416 -1191 580 C ATOM 1488 CD2 TYR A 361 27.459 -2.728 2.850 1.00 35.90 C ANISOU 1488 CD2 TYR A 361 4750 3451 5441 -495 -1177 996 C ATOM 1489 CE1 TYR A 361 29.076 -3.280 0.678 1.00 34.17 C ANISOU 1489 CE1 TYR A 361 4611 3340 5033 -428 -1403 589 C ATOM 1490 CE2 TYR A 361 27.016 -3.595 1.869 1.00 35.36 C ANISOU 1490 CE2 TYR A 361 4692 3308 5435 -521 -1403 1018 C ATOM 1491 CZ TYR A 361 27.829 -3.877 0.791 1.00 45.48 C ANISOU 1491 CZ TYR A 361 6025 4640 6615 -486 -1519 805 C ATOM 1492 OH TYR A 361 27.384 -4.753 -0.177 1.00 54.63 O ANISOU 1492 OH TYR A 361 7223 5711 7823 -504 -1756 821 O ATOM 1493 N GLY A 362 30.237 -1.000 6.996 1.00 27.57 N ANISOU 1493 N GLY A 362 3845 2559 4071 -337 -659 717 N ATOM 1494 CA GLY A 362 30.679 -0.177 8.103 1.00 30.74 C ANISOU 1494 CA GLY A 362 4304 2984 4393 -311 -491 700 C ATOM 1495 C GLY A 362 32.161 -0.392 8.376 1.00 31.51 C ANISOU 1495 C GLY A 362 4457 3130 4386 -273 -551 477 C ATOM 1496 O GLY A 362 32.887 0.538 8.697 1.00 30.29 O ANISOU 1496 O GLY A 362 4337 3029 4142 -263 -438 395 O ATOM 1497 N CYS A 363 32.615 -1.625 8.219 1.00 25.19 N ANISOU 1497 N CYS A 363 3662 2304 3603 -255 -738 388 N ATOM 1498 CA CYS A 363 34.026 -1.947 8.420 1.00 33.30 C ANISOU 1498 CA CYS A 363 4731 3372 4548 -220 -806 191 C ATOM 1499 C CYS A 363 34.958 -1.263 7.428 1.00 27.27 C ANISOU 1499 C CYS A 363 3940 2713 3708 -209 -778 43 C ATOM 1500 O CYS A 363 36.084 -0.927 7.767 1.00 35.47 O ANISOU 1500 O CYS A 363 5007 3796 4673 -187 -752 -74 O ATOM 1501 CB CYS A 363 34.239 -3.465 8.362 1.00 32.24 C ANISOU 1501 CB CYS A 363 4603 3186 4462 -200 -1015 136 C ATOM 1502 SG CYS A 363 33.604 -4.264 9.820 1.00 49.75 S ANISOU 1502 SG CYS A 363 6851 5297 6752 -200 -1048 278 S ATOM 1503 N ARG A 364 34.495 -1.081 6.199 1.00 21.50 N ANISOU 1503 N ARG A 364 3150 2018 2999 -222 -793 59 N ATOM 1504 CA ARG A 364 35.291 -0.401 5.189 1.00 27.05 C ANISOU 1504 CA ARG A 364 3815 2830 3633 -204 -757 -61 C ATOM 1505 C ARG A 364 35.450 1.053 5.568 1.00 27.01 C ANISOU 1505 C ARG A 364 3798 2879 3586 -225 -571 -33 C ATOM 1506 O ARG A 364 36.509 1.657 5.375 1.00 28.78 O ANISOU 1506 O ARG A 364 4009 3183 3744 -201 -534 -141 O ATOM 1507 CB ARG A 364 34.627 -0.531 3.832 1.00 32.48 C ANISOU 1507 CB ARG A 364 4453 3534 4354 -217 -814 -33 C ATOM 1508 CG ARG A 364 34.869 -1.883 3.222 1.00 50.20 C ANISOU 1508 CG ARG A 364 6727 5743 6605 -175 -1017 -120 C ATOM 1509 CD ARG A 364 36.096 -1.832 2.311 1.00 61.38 C ANISOU 1509 CD ARG A 364 8136 7258 7926 -105 -1041 -295 C ATOM 1510 NE ARG A 364 37.371 -2.038 2.993 1.00 57.46 N ANISOU 1510 NE ARG A 364 7667 6788 7378 -56 -1045 -411 N ATOM 1511 CZ ARG A 364 38.550 -1.893 2.397 1.00 59.74 C ANISOU 1511 CZ ARG A 364 7940 7167 7594 11 -1040 -538 C ATOM 1512 NH1 ARG A 364 38.602 -1.536 1.122 1.00 59.75 N ANISOU 1512 NH1 ARG A 364 7902 7245 7554 45 -1025 -573 N ATOM 1513 NH2 ARG A 364 39.677 -2.107 3.064 1.00 65.53 N ANISOU 1513 NH2 ARG A 364 8691 7909 8297 47 -1050 -618 N ATOM 1514 N VAL A 365 34.383 1.595 6.136 1.00 21.25 N ANISOU 1514 N VAL A 365 3074 2099 2900 -264 -458 124 N ATOM 1515 CA VAL A 365 34.404 2.941 6.648 1.00 23.74 C ANISOU 1515 CA VAL A 365 3401 2443 3177 -280 -283 165 C ATOM 1516 C VAL A 365 35.409 3.055 7.779 1.00 23.46 C ANISOU 1516 C VAL A 365 3451 2391 3070 -252 -274 82 C ATOM 1517 O VAL A 365 36.183 3.995 7.804 1.00 22.22 O ANISOU 1517 O VAL A 365 3297 2290 2856 -250 -209 15 O ATOM 1518 CB VAL A 365 33.017 3.388 7.153 1.00 28.88 C ANISOU 1518 CB VAL A 365 4057 3028 3889 -312 -157 366 C ATOM 1519 CG1 VAL A 365 33.111 4.769 7.768 1.00 27.38 C ANISOU 1519 CG1 VAL A 365 3903 2856 3643 -315 23 393 C ATOM 1520 CG2 VAL A 365 32.006 3.387 6.011 1.00 32.37 C ANISOU 1520 CG2 VAL A 365 4407 3479 4413 -355 -165 468 C ATOM 1521 N VAL A 366 35.404 2.106 8.715 1.00 26.79 N ANISOU 1521 N VAL A 366 3941 2733 3504 -236 -350 93 N ATOM 1522 CA VAL A 366 36.287 2.214 9.864 1.00 23.86 C ANISOU 1522 CA VAL A 366 3664 2333 3067 -218 -345 29 C ATOM 1523 C VAL A 366 37.716 2.076 9.378 1.00 26.69 C ANISOU 1523 C VAL A 366 3998 2759 3384 -200 -438 -137 C ATOM 1524 O VAL A 366 38.621 2.739 9.869 1.00 27.75 O ANISOU 1524 O VAL A 366 4176 2907 3461 -198 -408 -195 O ATOM 1525 CB VAL A 366 36.010 1.152 10.938 1.00 29.64 C ANISOU 1525 CB VAL A 366 4465 2973 3825 -204 -415 76 C ATOM 1526 CG1 VAL A 366 37.172 1.097 11.910 1.00 30.66 C ANISOU 1526 CG1 VAL A 366 4683 3082 3886 -192 -453 -24 C ATOM 1527 CG2 VAL A 366 34.734 1.491 11.691 1.00 28.50 C ANISOU 1527 CG2 VAL A 366 4360 2761 3708 -204 -289 261 C ATOM 1528 N GLN A 367 37.901 1.227 8.377 1.00 25.01 N ANISOU 1528 N GLN A 367 3719 2582 3201 -181 -553 -201 N ATOM 1529 CA GLN A 367 39.215 0.986 7.807 1.00 26.68 C ANISOU 1529 CA GLN A 367 3900 2860 3379 -146 -635 -342 C ATOM 1530 C GLN A 367 39.787 2.256 7.171 1.00 27.79 C ANISOU 1530 C GLN A 367 3983 3097 3480 -144 -541 -372 C ATOM 1531 O GLN A 367 40.953 2.607 7.357 1.00 34.94 O ANISOU 1531 O GLN A 367 4889 4036 4351 -128 -552 -440 O ATOM 1532 CB GLN A 367 39.092 -0.096 6.744 1.00 34.45 C ANISOU 1532 CB GLN A 367 4837 3860 4393 -113 -759 -391 C ATOM 1533 CG GLN A 367 40.376 -0.392 6.043 1.00 46.94 C ANISOU 1533 CG GLN A 367 6387 5513 5937 -55 -829 -524 C ATOM 1534 CD GLN A 367 41.359 -1.031 6.980 1.00 54.23 C ANISOU 1534 CD GLN A 367 7361 6392 6852 -41 -903 -586 C ATOM 1535 OE1 GLN A 367 40.953 -1.641 7.961 1.00 58.13 O ANISOU 1535 OE1 GLN A 367 7914 6799 7375 -67 -944 -546 O ATOM 1536 NE2 GLN A 367 42.658 -0.892 6.696 1.00 53.86 N ANISOU 1536 NE2 GLN A 367 7286 6407 6773 1 -918 -671 N ATOM 1537 N THR A 368 38.955 2.932 6.398 1.00 25.28 N ANISOU 1537 N THR A 368 3605 2822 3179 -165 -457 -307 N ATOM 1538 CA THR A 368 39.382 4.135 5.704 1.00 31.10 C ANISOU 1538 CA THR A 368 4269 3657 3892 -166 -370 -322 C ATOM 1539 C THR A 368 39.747 5.267 6.659 1.00 27.58 C ANISOU 1539 C THR A 368 3871 3192 3414 -191 -279 -296 C ATOM 1540 O THR A 368 40.706 5.995 6.427 1.00 24.09 O ANISOU 1540 O THR A 368 3388 2815 2950 -180 -268 -342 O ATOM 1541 CB THR A 368 38.325 4.608 4.712 1.00 32.06 C ANISOU 1541 CB THR A 368 4315 3821 4046 -193 -300 -247 C ATOM 1542 OG1 THR A 368 38.141 3.593 3.719 1.00 40.21 O ANISOU 1542 OG1 THR A 368 5316 4868 5095 -164 -408 -286 O ATOM 1543 CG2 THR A 368 38.786 5.877 4.025 1.00 28.06 C ANISOU 1543 CG2 THR A 368 3720 3422 3520 -196 -210 -259 C ATOM 1544 N ILE A 369 38.984 5.396 7.732 1.00 23.54 N ANISOU 1544 N ILE A 369 3453 2588 2902 -219 -219 -214 N ATOM 1545 CA ILE A 369 39.256 6.384 8.763 1.00 24.64 C ANISOU 1545 CA ILE A 369 3680 2684 2997 -235 -144 -191 C ATOM 1546 C ILE A 369 40.581 6.109 9.432 1.00 27.12 C ANISOU 1546 C ILE A 369 4055 2974 3277 -220 -244 -280 C ATOM 1547 O ILE A 369 41.375 7.017 9.629 1.00 33.57 O ANISOU 1547 O ILE A 369 4884 3805 4065 -228 -232 -303 O ATOM 1548 CB ILE A 369 38.185 6.339 9.851 1.00 28.70 C ANISOU 1548 CB ILE A 369 4305 3093 3507 -244 -67 -84 C ATOM 1549 CG1 ILE A 369 36.855 6.858 9.299 1.00 26.87 C ANISOU 1549 CG1 ILE A 369 4014 2876 3320 -265 57 38 C ATOM 1550 CG2 ILE A 369 38.628 7.153 11.069 1.00 22.67 C ANISOU 1550 CG2 ILE A 369 3677 2262 2673 -244 -19 -83 C ATOM 1551 CD1 ILE A 369 35.742 6.837 10.322 1.00 30.49 C ANISOU 1551 CD1 ILE A 369 4569 3234 3782 -259 153 173 C ATOM 1552 N ILE A 370 40.822 4.847 9.776 1.00 29.09 N ANISOU 1552 N ILE A 370 4337 3179 3536 -203 -352 -321 N ATOM 1553 CA ILE A 370 42.078 4.463 10.409 1.00 29.42 C ANISOU 1553 CA ILE A 370 4429 3192 3557 -195 -455 -396 C ATOM 1554 C ILE A 370 43.264 4.821 9.525 1.00 30.41 C ANISOU 1554 C ILE A 370 4452 3412 3690 -175 -497 -461 C ATOM 1555 O ILE A 370 44.280 5.341 10.015 1.00 26.67 O ANISOU 1555 O ILE A 370 4009 2923 3201 -185 -531 -479 O ATOM 1556 CB ILE A 370 42.112 2.965 10.764 1.00 29.52 C ANISOU 1556 CB ILE A 370 4468 3153 3594 -180 -567 -429 C ATOM 1557 CG1 ILE A 370 41.239 2.710 11.988 1.00 22.21 C ANISOU 1557 CG1 ILE A 370 3659 2123 2657 -197 -534 -353 C ATOM 1558 CG2 ILE A 370 43.561 2.475 11.040 1.00 23.00 C ANISOU 1558 CG2 ILE A 370 3649 2323 2766 -170 -684 -514 C ATOM 1559 CD1 ILE A 370 40.901 1.239 12.171 1.00 21.10 C ANISOU 1559 CD1 ILE A 370 3515 1939 2562 -184 -634 -355 C ATOM 1560 N GLU A 371 43.123 4.569 8.226 1.00 26.83 N ANISOU 1560 N GLU A 371 3881 3051 3262 -142 -498 -484 N ATOM 1561 CA GLU A 371 44.203 4.855 7.283 1.00 28.50 C ANISOU 1561 CA GLU A 371 3985 3364 3479 -102 -525 -531 C ATOM 1562 C GLU A 371 44.494 6.332 7.245 1.00 29.67 C ANISOU 1562 C GLU A 371 4097 3553 3622 -127 -448 -489 C ATOM 1563 O GLU A 371 45.646 6.739 7.296 1.00 31.69 O ANISOU 1563 O GLU A 371 4321 3833 3886 -116 -491 -499 O ATOM 1564 CB GLU A 371 43.857 4.364 5.882 1.00 23.53 C ANISOU 1564 CB GLU A 371 3257 2823 2861 -54 -528 -558 C ATOM 1565 CG GLU A 371 43.914 2.862 5.740 1.00 30.83 C ANISOU 1565 CG GLU A 371 4207 3714 3792 -12 -637 -619 C ATOM 1566 CD GLU A 371 43.424 2.394 4.381 1.00 39.70 C ANISOU 1566 CD GLU A 371 5268 4903 4914 36 -651 -644 C ATOM 1567 OE1 GLU A 371 43.535 1.187 4.104 1.00 42.87 O ANISOU 1567 OE1 GLU A 371 5693 5280 5316 83 -752 -701 O ATOM 1568 OE2 GLU A 371 42.912 3.227 3.598 1.00 50.66 O ANISOU 1568 OE2 GLU A 371 6590 6360 6299 26 -568 -605 O ATOM 1569 N LYS A 372 43.435 7.128 7.145 1.00 26.57 N ANISOU 1569 N LYS A 372 3705 3165 3226 -161 -340 -428 N ATOM 1570 CA LYS A 372 43.558 8.574 7.128 1.00 25.56 C ANISOU 1570 CA LYS A 372 3548 3068 3096 -188 -264 -383 C ATOM 1571 C LYS A 372 44.240 9.101 8.397 1.00 25.34 C ANISOU 1571 C LYS A 372 3641 2945 3043 -216 -303 -376 C ATOM 1572 O LYS A 372 45.024 10.032 8.328 1.00 30.77 O ANISOU 1572 O LYS A 372 4289 3660 3741 -224 -317 -363 O ATOM 1573 CB LYS A 372 42.178 9.220 6.971 1.00 27.38 C ANISOU 1573 CB LYS A 372 3778 3296 3329 -223 -136 -311 C ATOM 1574 CG LYS A 372 42.208 10.756 6.876 1.00 33.83 C ANISOU 1574 CG LYS A 372 4557 4148 4149 -251 -51 -264 C ATOM 1575 CD LYS A 372 43.210 11.267 5.840 1.00 31.69 C ANISOU 1575 CD LYS A 372 4130 4003 3910 -227 -84 -287 C ATOM 1576 CE LYS A 372 42.972 10.662 4.443 1.00 41.87 C ANISOU 1576 CE LYS A 372 5285 5404 5219 -188 -79 -309 C ATOM 1577 NZ LYS A 372 43.753 11.356 3.342 1.00 36.31 N ANISOU 1577 NZ LYS A 372 4416 4838 4542 -155 -74 -307 N ATOM 1578 N LEU A 373 43.942 8.493 9.545 1.00 22.53 N ANISOU 1578 N LEU A 373 3432 2474 2655 -231 -329 -377 N ATOM 1579 CA LEU A 373 44.476 8.944 10.836 1.00 24.57 C ANISOU 1579 CA LEU A 373 3839 2622 2874 -258 -370 -370 C ATOM 1580 C LEU A 373 45.854 8.381 11.126 1.00 23.53 C ANISOU 1580 C LEU A 373 3709 2470 2759 -254 -512 -417 C ATOM 1581 O LEU A 373 46.380 8.575 12.209 1.00 31.09 O ANISOU 1581 O LEU A 373 4798 3326 3688 -283 -575 -413 O ATOM 1582 CB LEU A 373 43.538 8.570 11.986 1.00 18.21 C ANISOU 1582 CB LEU A 373 3199 1701 2019 -267 -326 -339 C ATOM 1583 CG LEU A 373 42.135 9.178 11.940 1.00 25.26 C ANISOU 1583 CG LEU A 373 4114 2588 2897 -268 -173 -263 C ATOM 1584 CD1 LEU A 373 41.345 8.735 13.149 1.00 23.42 C ANISOU 1584 CD1 LEU A 373 4043 2239 2615 -258 -133 -216 C ATOM 1585 CD2 LEU A 373 42.184 10.703 11.875 1.00 24.84 C ANISOU 1585 CD2 LEU A 373 4069 2545 2825 -285 -100 -230 C ATOM 1586 N THR A 374 46.444 7.694 10.153 1.00 25.75 N ANISOU 1586 N THR A 374 3853 2844 3087 -216 -563 -454 N ATOM 1587 CA THR A 374 47.765 7.106 10.335 1.00 28.86 C ANISOU 1587 CA THR A 374 4230 3225 3511 -205 -687 -483 C ATOM 1588 C THR A 374 48.834 8.073 9.873 1.00 35.24 C ANISOU 1588 C THR A 374 4940 4089 4360 -201 -717 -445 C ATOM 1589 O THR A 374 48.714 8.682 8.813 1.00 36.26 O ANISOU 1589 O THR A 374 4938 4329 4510 -172 -653 -425 O ATOM 1590 CB THR A 374 47.911 5.746 9.596 1.00 24.77 C ANISOU 1590 CB THR A 374 3629 2764 3020 -149 -729 -538 C ATOM 1591 OG1 THR A 374 46.913 4.853 10.088 1.00 29.32 O ANISOU 1591 OG1 THR A 374 4292 3277 3573 -159 -721 -558 O ATOM 1592 CG2 THR A 374 49.300 5.119 9.848 1.00 22.90 C ANISOU 1592 CG2 THR A 374 3375 2506 2820 -135 -848 -555 C ATOM 1593 N ALA A 375 49.880 8.210 10.681 1.00 29.94 N ANISOU 1593 N ALA A 375 4331 3338 3707 -232 -824 -423 N ATOM 1594 CA ALA A 375 50.964 9.119 10.365 1.00 24.48 C ANISOU 1594 CA ALA A 375 3548 2681 3073 -235 -879 -361 C ATOM 1595 C ALA A 375 51.951 8.398 9.441 1.00 29.94 C ANISOU 1595 C ALA A 375 4077 3470 3830 -167 -922 -357 C ATOM 1596 O ALA A 375 53.071 8.035 9.838 1.00 26.51 O ANISOU 1596 O ALA A 375 3640 2988 3445 -173 -1030 -327 O ATOM 1597 CB ALA A 375 51.639 9.574 11.651 1.00 25.47 C ANISOU 1597 CB ALA A 375 3822 2661 3196 -303 -992 -324 C ATOM 1598 N ASP A 376 51.511 8.167 8.208 1.00 24.96 N ANISOU 1598 N ASP A 376 3318 2970 3197 -99 -835 -383 N ATOM 1599 CA ASP A 376 52.351 7.523 7.212 1.00 27.14 C ANISOU 1599 CA ASP A 376 3449 3347 3516 -9 -853 -380 C ATOM 1600 C ASP A 376 52.834 8.510 6.145 1.00 30.59 C ANISOU 1600 C ASP A 376 3711 3913 3999 40 -809 -306 C ATOM 1601 O ASP A 376 52.635 9.719 6.257 1.00 35.71 O ANISOU 1601 O ASP A 376 4347 4562 4659 -9 -786 -254 O ATOM 1602 CB ASP A 376 51.570 6.390 6.546 1.00 39.41 C ANISOU 1602 CB ASP A 376 5000 4948 5024 49 -804 -467 C ATOM 1603 CG ASP A 376 50.179 6.825 6.055 1.00 41.53 C ANISOU 1603 CG ASP A 376 5273 5260 5246 34 -697 -489 C ATOM 1604 OD1 ASP A 376 49.948 8.022 5.778 1.00 39.37 O ANISOU 1604 OD1 ASP A 376 4945 5032 4981 10 -636 -438 O ATOM 1605 OD2 ASP A 376 49.301 5.949 5.934 1.00 52.44 O ANISOU 1605 OD2 ASP A 376 6707 6625 6593 44 -681 -548 O ATOM 1606 N SER A 377 53.437 7.965 5.096 1.00 35.29 N ANISOU 1606 N SER A 377 4174 4617 4616 144 -794 -301 N ATOM 1607 CA SER A 377 53.988 8.733 3.999 1.00 39.99 C ANISOU 1607 CA SER A 377 4587 5350 5256 215 -749 -221 C ATOM 1608 C SER A 377 52.994 9.709 3.400 1.00 40.45 C ANISOU 1608 C SER A 377 4597 5484 5287 192 -650 -222 C ATOM 1609 O SER A 377 53.375 10.784 2.942 1.00 44.94 O ANISOU 1609 O SER A 377 5039 6128 5907 199 -631 -134 O ATOM 1610 CB SER A 377 54.476 7.789 2.908 1.00 44.01 C ANISOU 1610 CB SER A 377 5000 5965 5757 352 -719 -240 C ATOM 1611 OG SER A 377 55.795 7.378 3.189 1.00 58.21 O ANISOU 1611 OG SER A 377 6757 7735 7624 392 -797 -170 O ATOM 1612 N MET A 378 51.723 9.335 3.396 1.00 28.15 N ANISOU 1612 N MET A 378 3131 3905 3659 164 -590 -308 N ATOM 1613 CA MET A 378 50.698 10.184 2.788 1.00 34.14 C ANISOU 1613 CA MET A 378 3842 4733 4397 138 -488 -303 C ATOM 1614 C MET A 378 50.241 11.344 3.672 1.00 32.19 C ANISOU 1614 C MET A 378 3664 4406 4161 32 -478 -262 C ATOM 1615 O MET A 378 49.456 12.162 3.229 1.00 33.65 O ANISOU 1615 O MET A 378 3802 4643 4342 5 -393 -243 O ATOM 1616 CB MET A 378 49.489 9.353 2.328 1.00 34.96 C ANISOU 1616 CB MET A 378 4003 4845 4436 151 -432 -386 C ATOM 1617 CG MET A 378 49.814 8.404 1.158 1.00 42.57 C ANISOU 1617 CG MET A 378 4894 5906 5375 270 -430 -430 C ATOM 1618 SD MET A 378 48.526 7.167 0.866 1.00164.07 S ANISOU 1618 SD MET A 378 20392 21251 20694 276 -426 -528 S ATOM 1619 CE MET A 378 48.681 6.114 2.313 1.00 87.48 C ANISOU 1619 CE MET A 378 10854 11388 10996 230 -527 -573 C ATOM 1620 N ASN A 379 50.724 11.426 4.912 1.00 25.42 N ANISOU 1620 N ASN A 379 2927 3417 3315 -25 -566 -246 N ATOM 1621 CA ASN A 379 50.354 12.559 5.768 1.00 23.35 C ANISOU 1621 CA ASN A 379 2755 3067 3050 -112 -564 -209 C ATOM 1622 C ASN A 379 51.493 13.519 6.087 1.00 26.51 C ANISOU 1622 C ASN A 379 3108 3442 3521 -134 -662 -117 C ATOM 1623 O ASN A 379 51.344 14.384 6.938 1.00 30.80 O ANISOU 1623 O ASN A 379 3760 3884 4057 -203 -693 -91 O ATOM 1624 CB ASN A 379 49.682 12.082 7.062 1.00 27.98 C ANISOU 1624 CB ASN A 379 3562 3499 3572 -170 -579 -260 C ATOM 1625 CG ASN A 379 48.222 11.711 6.849 1.00 33.15 C ANISOU 1625 CG ASN A 379 4261 4163 4170 -174 -463 -306 C ATOM 1626 OD1 ASN A 379 47.702 10.761 7.450 1.00 36.12 O ANISOU 1626 OD1 ASN A 379 4756 4463 4506 -181 -470 -352 O ATOM 1627 ND2 ASN A 379 47.556 12.452 5.972 1.00 23.73 N ANISOU 1627 ND2 ASN A 379 2963 3066 2988 -172 -362 -280 N ATOM 1628 N VAL A 380 52.626 13.372 5.402 1.00 29.00 N ANISOU 1628 N VAL A 380 3267 3844 3908 -70 -714 -58 N ATOM 1629 CA VAL A 380 53.797 14.208 5.688 1.00 29.24 C ANISOU 1629 CA VAL A 380 3236 3845 4031 -91 -829 58 C ATOM 1630 C VAL A 380 53.546 15.682 5.382 1.00 27.72 C ANISOU 1630 C VAL A 380 2962 3695 3877 -125 -801 125 C ATOM 1631 O VAL A 380 54.312 16.540 5.805 1.00 31.47 O ANISOU 1631 O VAL A 380 3420 4111 4424 -165 -912 221 O ATOM 1632 CB VAL A 380 55.059 13.767 4.882 1.00 26.22 C ANISOU 1632 CB VAL A 380 2668 3563 3732 3 -871 139 C ATOM 1633 CG1 VAL A 380 55.644 12.484 5.436 1.00 24.32 C ANISOU 1633 CG1 VAL A 380 2513 3243 3483 21 -941 105 C ATOM 1634 CG2 VAL A 380 54.735 13.639 3.382 1.00 30.16 C ANISOU 1634 CG2 VAL A 380 2989 4252 4219 105 -742 128 C ATOM 1635 N ASP A 381 52.490 15.961 4.621 1.00 22.48 N ANISOU 1635 N ASP A 381 2239 3129 3172 -113 -664 83 N ATOM 1636 CA ASP A 381 52.162 17.328 4.246 1.00 30.67 C ANISOU 1636 CA ASP A 381 3183 4220 4249 -145 -623 143 C ATOM 1637 C ASP A 381 51.439 18.086 5.359 1.00 35.80 C ANISOU 1637 C ASP A 381 4028 4722 4853 -238 -630 120 C ATOM 1638 O ASP A 381 51.149 19.271 5.208 1.00 37.35 O ANISOU 1638 O ASP A 381 4175 4936 5080 -273 -606 167 O ATOM 1639 CB ASP A 381 51.316 17.362 2.959 1.00 21.34 C ANISOU 1639 CB ASP A 381 1858 3203 3049 -101 -472 117 C ATOM 1640 CG ASP A 381 49.978 16.707 3.133 1.00 30.20 C ANISOU 1640 CG ASP A 381 3116 4286 4074 -125 -369 12 C ATOM 1641 OD1 ASP A 381 49.941 15.473 3.331 1.00 37.34 O ANISOU 1641 OD1 ASP A 381 4106 5152 4929 -94 -383 -56 O ATOM 1642 OD2 ASP A 381 48.957 17.418 3.062 1.00 31.42 O ANISOU 1642 OD2 ASP A 381 3283 4445 4212 -173 -277 10 O ATOM 1643 N LEU A 382 51.154 17.419 6.475 1.00 28.39 N ANISOU 1643 N LEU A 382 3313 3637 3839 -271 -661 53 N ATOM 1644 CA LEU A 382 50.387 18.068 7.534 1.00 22.48 C ANISOU 1644 CA LEU A 382 2771 2747 3025 -337 -646 30 C ATOM 1645 C LEU A 382 51.277 19.001 8.326 1.00 22.96 C ANISOU 1645 C LEU A 382 2906 2689 3129 -385 -803 100 C ATOM 1646 O LEU A 382 52.433 18.693 8.576 1.00 26.23 O ANISOU 1646 O LEU A 382 3304 3064 3600 -383 -946 146 O ATOM 1647 CB LEU A 382 49.729 17.038 8.484 1.00 20.44 C ANISOU 1647 CB LEU A 382 2729 2372 2665 -347 -620 -56 C ATOM 1648 CG LEU A 382 48.729 16.038 7.878 1.00 27.86 C ANISOU 1648 CG LEU A 382 3632 3393 3562 -310 -488 -120 C ATOM 1649 CD1 LEU A 382 48.141 15.139 8.954 1.00 26.40 C ANISOU 1649 CD1 LEU A 382 3659 3079 3293 -324 -482 -179 C ATOM 1650 CD2 LEU A 382 47.622 16.730 7.143 1.00 17.57 C ANISOU 1650 CD2 LEU A 382 2247 2174 2255 -316 -340 -107 C ATOM 1651 N THR A 383 50.726 20.137 8.732 1.00 27.38 N ANISOU 1651 N THR A 383 3556 3182 3667 -427 -782 115 N ATOM 1652 CA THR A 383 51.315 20.934 9.795 1.00 26.75 C ANISOU 1652 CA THR A 383 3643 2933 3588 -478 -939 156 C ATOM 1653 C THR A 383 51.330 20.113 11.084 1.00 37.60 C ANISOU 1653 C THR A 383 5281 4139 4866 -496 -1000 94 C ATOM 1654 O THR A 383 50.595 19.116 11.221 1.00 38.26 O ANISOU 1654 O THR A 383 5431 4232 4872 -472 -892 17 O ATOM 1655 CB THR A 383 50.491 22.204 10.072 1.00 37.28 C ANISOU 1655 CB THR A 383 5070 4211 4884 -509 -878 160 C ATOM 1656 OG1 THR A 383 49.136 21.839 10.380 1.00 41.29 O ANISOU 1656 OG1 THR A 383 5715 4695 5277 -496 -702 82 O ATOM 1657 CG2 THR A 383 50.518 23.157 8.858 1.00 33.17 C ANISOU 1657 CG2 THR A 383 4284 3849 4470 -503 -834 232 C ATOM 1658 N SER A 384 52.170 20.547 12.021 1.00 30.81 N ANISOU 1658 N SER A 384 4570 3121 4017 -540 -1186 136 N ATOM 1659 CA SER A 384 52.270 19.951 13.343 1.00 30.91 C ANISOU 1659 CA SER A 384 4854 2956 3936 -566 -1269 88 C ATOM 1660 C SER A 384 50.952 20.022 14.095 1.00 30.89 C ANISOU 1660 C SER A 384 5084 2869 3785 -554 -1129 9 C ATOM 1661 O SER A 384 50.548 19.048 14.729 1.00 31.53 O ANISOU 1661 O SER A 384 5302 2896 3781 -541 -1085 -53 O ATOM 1662 CB SER A 384 53.344 20.673 14.150 1.00 34.89 C ANISOU 1662 CB SER A 384 5482 3294 4480 -623 -1505 162 C ATOM 1663 OG SER A 384 54.591 20.496 13.524 1.00 42.64 O ANISOU 1663 OG SER A 384 6245 4345 5611 -628 -1634 260 O ATOM 1664 N ALA A 385 50.301 21.182 14.050 1.00 30.08 N ANISOU 1664 N ALA A 385 5024 2751 3656 -556 -1061 22 N ATOM 1665 CA ALA A 385 48.984 21.319 14.657 1.00 33.60 C ANISOU 1665 CA ALA A 385 5668 3129 3968 -530 -898 -31 C ATOM 1666 C ALA A 385 48.058 20.243 14.120 1.00 33.83 C ANISOU 1666 C ALA A 385 5596 3281 3977 -490 -713 -74 C ATOM 1667 O ALA A 385 47.329 19.601 14.882 1.00 34.56 O ANISOU 1667 O ALA A 385 5865 3299 3967 -466 -633 -116 O ATOM 1668 CB ALA A 385 48.400 22.685 14.371 1.00 32.79 C ANISOU 1668 CB ALA A 385 5554 3034 3868 -530 -825 0 C ATOM 1669 N ALA A 386 48.093 20.045 12.804 1.00 26.07 N ANISOU 1669 N ALA A 386 4331 2482 3093 -480 -653 -57 N ATOM 1670 CA ALA A 386 47.200 19.073 12.178 1.00 23.26 C ANISOU 1670 CA ALA A 386 3874 2239 2726 -446 -495 -92 C ATOM 1671 C ALA A 386 47.586 17.652 12.569 1.00 24.43 C ANISOU 1671 C ALA A 386 4069 2359 2853 -434 -559 -137 C ATOM 1672 O ALA A 386 46.716 16.789 12.695 1.00 22.15 O ANISOU 1672 O ALA A 386 3825 2075 2514 -410 -456 -171 O ATOM 1673 CB ALA A 386 47.172 19.240 10.645 1.00 18.97 C ANISOU 1673 CB ALA A 386 3034 1891 2282 -435 -427 -64 C ATOM 1674 N GLN A 387 48.885 17.400 12.757 1.00 26.52 N ANISOU 1674 N GLN A 387 4315 2592 3169 -452 -733 -125 N ATOM 1675 CA GLN A 387 49.334 16.051 13.148 1.00 28.13 C ANISOU 1675 CA GLN A 387 4558 2766 3363 -444 -801 -165 C ATOM 1676 C GLN A 387 48.836 15.759 14.563 1.00 27.10 C ANISOU 1676 C GLN A 387 4711 2469 3118 -455 -803 -200 C ATOM 1677 O GLN A 387 48.365 14.670 14.869 1.00 31.81 O ANISOU 1677 O GLN A 387 5357 3056 3672 -436 -757 -241 O ATOM 1678 CB GLN A 387 50.860 15.923 13.110 1.00 26.94 C ANISOU 1678 CB GLN A 387 4331 2604 3303 -465 -986 -123 C ATOM 1679 CG GLN A 387 51.493 15.796 11.729 1.00 27.70 C ANISOU 1679 CG GLN A 387 4139 2873 3511 -429 -983 -83 C ATOM 1680 CD GLN A 387 51.325 14.411 11.079 1.00 29.60 C ANISOU 1680 CD GLN A 387 4273 3217 3756 -377 -918 -137 C ATOM 1681 OE1 GLN A 387 50.707 13.518 11.641 1.00 33.21 O ANISOU 1681 OE1 GLN A 387 4854 3620 4144 -375 -880 -201 O ATOM 1682 NE2 GLN A 387 51.899 14.238 9.888 1.00 28.88 N ANISOU 1682 NE2 GLN A 387 3954 3273 3746 -328 -910 -105 N ATOM 1683 N ASN A 388 48.927 16.759 15.419 1.00 29.25 N ANISOU 1683 N ASN A 388 5172 2607 3335 -480 -860 -179 N ATOM 1684 CA ASN A 388 48.446 16.627 16.778 1.00 31.29 C ANISOU 1684 CA ASN A 388 5720 2702 3465 -476 -854 -206 C ATOM 1685 C ASN A 388 46.967 16.273 16.814 1.00 32.22 C ANISOU 1685 C ASN A 388 5881 2851 3509 -426 -645 -223 C ATOM 1686 O ASN A 388 46.549 15.363 17.541 1.00 37.77 O ANISOU 1686 O ASN A 388 6708 3497 4147 -405 -616 -247 O ATOM 1687 CB ASN A 388 48.689 17.917 17.547 1.00 46.02 C ANISOU 1687 CB ASN A 388 7788 4421 5275 -498 -938 -181 C ATOM 1688 CG ASN A 388 48.242 17.814 18.986 1.00 67.32 C ANISOU 1688 CG ASN A 388 10815 6942 7822 -479 -934 -209 C ATOM 1689 OD1 ASN A 388 48.645 16.896 19.706 1.00 76.06 O ANISOU 1689 OD1 ASN A 388 12022 7978 8898 -491 -1019 -233 O ATOM 1690 ND2 ASN A 388 47.391 18.745 19.413 1.00 70.41 N ANISOU 1690 ND2 ASN A 388 11375 7261 8115 -442 -829 -202 N ATOM 1691 N LEU A 389 46.181 16.989 16.016 1.00 27.37 N ANISOU 1691 N LEU A 389 5153 2327 2917 -409 -504 -197 N ATOM 1692 CA LEU A 389 44.768 16.703 15.885 1.00 30.56 C ANISOU 1692 CA LEU A 389 5559 2771 3281 -367 -305 -184 C ATOM 1693 C LEU A 389 44.568 15.265 15.421 1.00 31.89 C ANISOU 1693 C LEU A 389 5597 3027 3493 -355 -285 -207 C ATOM 1694 O LEU A 389 43.742 14.540 15.970 1.00 37.34 O ANISOU 1694 O LEU A 389 6383 3675 4130 -325 -205 -201 O ATOM 1695 CB LEU A 389 44.141 17.663 14.890 1.00 36.33 C ANISOU 1695 CB LEU A 389 6136 3606 4063 -367 -180 -144 C ATOM 1696 CG LEU A 389 42.623 17.794 14.912 1.00 38.29 C ANISOU 1696 CG LEU A 389 6424 3858 4268 -330 32 -99 C ATOM 1697 CD1 LEU A 389 42.186 18.293 16.255 1.00 35.67 C ANISOU 1697 CD1 LEU A 389 6387 3359 3807 -293 76 -83 C ATOM 1698 CD2 LEU A 389 42.189 18.769 13.824 1.00 35.63 C ANISOU 1698 CD2 LEU A 389 5904 3632 4002 -347 131 -57 C ATOM 1699 N ARG A 390 45.341 14.852 14.419 1.00 32.97 N ANISOU 1699 N ARG A 390 5520 3281 3727 -371 -362 -227 N ATOM 1700 CA ARG A 390 45.277 13.485 13.896 1.00 33.10 C ANISOU 1700 CA ARG A 390 5415 3377 3786 -355 -366 -258 C ATOM 1701 C ARG A 390 45.555 12.463 14.995 1.00 30.39 C ANISOU 1701 C ARG A 390 5227 2924 3393 -355 -450 -289 C ATOM 1702 O ARG A 390 44.824 11.480 15.152 1.00 31.62 O ANISOU 1702 O ARG A 390 5399 3080 3535 -332 -396 -295 O ATOM 1703 CB ARG A 390 46.273 13.301 12.729 1.00 25.64 C ANISOU 1703 CB ARG A 390 4244 2560 2939 -357 -448 -272 C ATOM 1704 CG ARG A 390 46.124 11.995 11.988 1.00 26.32 C ANISOU 1704 CG ARG A 390 4201 2736 3062 -327 -440 -308 C ATOM 1705 CD ARG A 390 47.458 11.539 11.374 1.00 33.98 C ANISOU 1705 CD ARG A 390 5033 3775 4103 -315 -563 -327 C ATOM 1706 NE ARG A 390 48.570 11.914 12.242 1.00 34.37 N ANISOU 1706 NE ARG A 390 5179 3724 4156 -349 -697 -310 N ATOM 1707 CZ ARG A 390 48.961 11.227 13.309 1.00 36.32 C ANISOU 1707 CZ ARG A 390 5573 3855 4372 -370 -790 -331 C ATOM 1708 NH1 ARG A 390 48.347 10.093 13.651 1.00 29.95 N ANISOU 1708 NH1 ARG A 390 4823 3024 3531 -354 -760 -372 N ATOM 1709 NH2 ARG A 390 49.975 11.674 14.029 1.00 37.49 N ANISOU 1709 NH2 ARG A 390 5806 3907 4531 -410 -923 -303 N ATOM 1710 N GLU A 391 46.616 12.701 15.760 1.00 32.59 N ANISOU 1710 N GLU A 391 5619 3107 3656 -385 -594 -299 N ATOM 1711 CA GLU A 391 47.015 11.786 16.829 1.00 29.70 C ANISOU 1711 CA GLU A 391 5400 2634 3250 -396 -691 -326 C ATOM 1712 C GLU A 391 45.930 11.613 17.887 1.00 33.75 C ANISOU 1712 C GLU A 391 6120 3048 3655 -366 -592 -314 C ATOM 1713 O GLU A 391 45.632 10.500 18.318 1.00 37.85 O ANISOU 1713 O GLU A 391 6672 3549 4162 -352 -592 -327 O ATOM 1714 CB GLU A 391 48.318 12.253 17.480 1.00 28.31 C ANISOU 1714 CB GLU A 391 5322 2356 3078 -444 -869 -320 C ATOM 1715 CG GLU A 391 48.972 11.177 18.311 1.00 36.66 C ANISOU 1715 CG GLU A 391 6467 3332 4129 -468 -992 -346 C ATOM 1716 CD GLU A 391 49.010 9.827 17.590 1.00 50.39 C ANISOU 1716 CD GLU A 391 8022 5181 5943 -448 -983 -377 C ATOM 1717 OE1 GLU A 391 49.535 9.781 16.450 1.00 56.61 O ANISOU 1717 OE1 GLU A 391 8599 6089 6822 -439 -997 -374 O ATOM 1718 OE2 GLU A 391 48.533 8.814 18.164 1.00 48.01 O ANISOU 1718 OE2 GLU A 391 7789 4845 5607 -437 -965 -401 O ATOM 1719 N ARG A 392 45.331 12.714 18.312 1.00 37.19 N ANISOU 1719 N ARG A 392 6695 3419 4014 -349 -505 -281 N ATOM 1720 CA ARG A 392 44.277 12.608 19.305 1.00 44.39 C ANISOU 1720 CA ARG A 392 7808 4240 4820 -300 -390 -252 C ATOM 1721 C ARG A 392 43.124 11.749 18.797 1.00 35.35 C ANISOU 1721 C ARG A 392 6537 3183 3712 -263 -251 -218 C ATOM 1722 O ARG A 392 42.629 10.874 19.508 1.00 37.02 O ANISOU 1722 O ARG A 392 6835 3346 3886 -233 -226 -200 O ATOM 1723 CB ARG A 392 43.781 13.987 19.740 1.00 53.15 C ANISOU 1723 CB ARG A 392 9084 5271 5841 -273 -301 -217 C ATOM 1724 CG ARG A 392 44.552 14.561 20.922 1.00 67.66 C ANISOU 1724 CG ARG A 392 11186 6942 7580 -286 -433 -239 C ATOM 1725 CD ARG A 392 44.245 16.048 21.089 1.00 79.94 C ANISOU 1725 CD ARG A 392 12875 8430 9067 -264 -374 -214 C ATOM 1726 NE ARG A 392 42.879 16.365 20.671 1.00 83.36 N ANISOU 1726 NE ARG A 392 13256 8928 9490 -206 -145 -159 N ATOM 1727 CZ ARG A 392 42.456 17.589 20.371 1.00 79.89 C ANISOU 1727 CZ ARG A 392 12830 8487 9036 -190 -56 -128 C ATOM 1728 NH1 ARG A 392 43.298 18.610 20.447 1.00 68.09 N ANISOU 1728 NH1 ARG A 392 11404 6929 7536 -227 -188 -152 N ATOM 1729 NH2 ARG A 392 41.197 17.793 19.989 1.00 83.58 N ANISOU 1729 NH2 ARG A 392 13238 9012 9507 -142 157 -64 N ATOM 1730 N ALA A 393 42.686 12.013 17.574 1.00 22.89 N ANISOU 1730 N ALA A 393 4758 1728 2211 -266 -169 -199 N ATOM 1731 CA ALA A 393 41.599 11.237 17.002 1.00 29.75 C ANISOU 1731 CA ALA A 393 5503 2671 3128 -240 -59 -155 C ATOM 1732 C ALA A 393 42.012 9.774 16.875 1.00 32.09 C ANISOU 1732 C ALA A 393 5716 2999 3479 -250 -170 -200 C ATOM 1733 O ALA A 393 41.222 8.883 17.140 1.00 35.34 O ANISOU 1733 O ALA A 393 6135 3396 3896 -224 -126 -161 O ATOM 1734 CB ALA A 393 41.162 11.806 15.650 1.00 23.00 C ANISOU 1734 CB ALA A 393 4449 1941 2349 -252 26 -131 C ATOM 1735 N LEU A 394 43.260 9.535 16.493 1.00 28.51 N ANISOU 1735 N LEU A 394 5181 2581 3071 -284 -314 -270 N ATOM 1736 CA LEU A 394 43.741 8.167 16.390 1.00 31.46 C ANISOU 1736 CA LEU A 394 5482 2977 3494 -289 -422 -316 C ATOM 1737 C LEU A 394 43.619 7.462 17.740 1.00 34.13 C ANISOU 1737 C LEU A 394 5996 3199 3773 -282 -458 -308 C ATOM 1738 O LEU A 394 43.116 6.348 17.809 1.00 31.39 O ANISOU 1738 O LEU A 394 5613 2859 3454 -265 -460 -299 O ATOM 1739 CB LEU A 394 45.182 8.119 15.893 1.00 21.46 C ANISOU 1739 CB LEU A 394 4118 1753 2282 -318 -563 -374 C ATOM 1740 CG LEU A 394 45.778 6.718 15.777 1.00 29.17 C ANISOU 1740 CG LEU A 394 5023 2750 3312 -318 -674 -423 C ATOM 1741 CD1 LEU A 394 45.001 5.903 14.757 1.00 23.92 C ANISOU 1741 CD1 LEU A 394 4209 2180 2698 -284 -621 -428 C ATOM 1742 CD2 LEU A 394 47.247 6.797 15.372 1.00 26.00 C ANISOU 1742 CD2 LEU A 394 4534 2379 2965 -338 -798 -454 C ATOM 1743 N GLN A 395 44.071 8.109 18.809 1.00 32.70 N ANISOU 1743 N GLN A 395 6009 2907 3510 -293 -494 -309 N ATOM 1744 CA GLN A 395 44.022 7.484 20.134 1.00 35.96 C ANISOU 1744 CA GLN A 395 6603 3207 3855 -285 -532 -302 C ATOM 1745 C GLN A 395 42.599 7.184 20.586 1.00 41.96 C ANISOU 1745 C GLN A 395 7426 3945 4573 -224 -384 -224 C ATOM 1746 O GLN A 395 42.330 6.128 21.148 1.00 45.05 O ANISOU 1746 O GLN A 395 7839 4308 4969 -210 -407 -207 O ATOM 1747 CB GLN A 395 44.678 8.366 21.177 1.00 32.92 C ANISOU 1747 CB GLN A 395 6441 2694 3373 -303 -596 -311 C ATOM 1748 CG GLN A 395 46.122 8.652 20.912 1.00 45.54 C ANISOU 1748 CG GLN A 395 7992 4289 5023 -366 -763 -358 C ATOM 1749 CD GLN A 395 46.732 9.505 22.002 1.00 59.02 C ANISOU 1749 CD GLN A 395 9943 5847 6637 -391 -851 -357 C ATOM 1750 OE1 GLN A 395 46.678 9.155 23.179 1.00 71.64 O ANISOU 1750 OE1 GLN A 395 11738 7332 8149 -384 -883 -356 O ATOM 1751 NE2 GLN A 395 47.313 10.628 21.619 1.00 60.29 N ANISOU 1751 NE2 GLN A 395 10093 6001 6813 -418 -900 -352 N ATOM 1752 N ARG A 396 41.697 8.128 20.353 1.00 31.45 N ANISOU 1752 N ARG A 396 6116 2625 3210 -188 -230 -162 N ATOM 1753 CA ARG A 396 40.305 7.960 20.720 1.00 32.67 C ANISOU 1753 CA ARG A 396 6317 2759 3337 -124 -71 -57 C ATOM 1754 C ARG A 396 39.759 6.702 20.062 1.00 42.12 C ANISOU 1754 C ARG A 396 7326 4034 4643 -125 -83 -27 C ATOM 1755 O ARG A 396 39.199 5.829 20.730 1.00 51.10 O ANISOU 1755 O ARG A 396 8504 5131 5779 -91 -70 32 O ATOM 1756 CB ARG A 396 39.503 9.167 20.255 1.00 39.63 C ANISOU 1756 CB ARG A 396 7194 3663 4200 -97 91 7 C ATOM 1757 CG ARG A 396 38.583 9.756 21.309 1.00 52.28 C ANISOU 1757 CG ARG A 396 9009 5166 5689 -18 247 103 C ATOM 1758 CD ARG A 396 38.772 11.301 21.416 1.00 70.68 C ANISOU 1758 CD ARG A 396 11469 7448 7937 -10 302 88 C ATOM 1759 NE ARG A 396 38.394 12.012 20.191 1.00 66.93 N ANISOU 1759 NE ARG A 396 10813 7074 7544 -36 382 110 N ATOM 1760 CZ ARG A 396 39.222 12.748 19.453 1.00 64.95 C ANISOU 1760 CZ ARG A 396 10475 6873 7330 -95 301 37 C ATOM 1761 NH1 ARG A 396 40.489 12.899 19.812 1.00 71.68 N ANISOU 1761 NH1 ARG A 396 11405 7677 8153 -134 132 -53 N ATOM 1762 NH2 ARG A 396 38.781 13.341 18.354 1.00 56.36 N ANISOU 1762 NH2 ARG A 396 9216 5881 6318 -114 386 68 N ATOM 1763 N LEU A 397 39.928 6.616 18.746 1.00 36.35 N ANISOU 1763 N LEU A 397 6394 3410 4007 -160 -114 -65 N ATOM 1764 CA LEU A 397 39.447 5.477 17.986 1.00 28.23 C ANISOU 1764 CA LEU A 397 5196 2449 3081 -162 -146 -46 C ATOM 1765 C LEU A 397 40.096 4.162 18.428 1.00 29.26 C ANISOU 1765 C LEU A 397 5323 2555 3239 -175 -297 -103 C ATOM 1766 O LEU A 397 39.419 3.149 18.576 1.00 32.56 O ANISOU 1766 O LEU A 397 5701 2963 3705 -156 -308 -47 O ATOM 1767 CB LEU A 397 39.651 5.708 16.489 1.00 21.38 C ANISOU 1767 CB LEU A 397 4140 1695 2288 -190 -162 -90 C ATOM 1768 CG LEU A 397 39.001 4.619 15.630 1.00 30.47 C ANISOU 1768 CG LEU A 397 5138 2902 3535 -188 -193 -63 C ATOM 1769 CD1 LEU A 397 37.543 4.396 16.087 1.00 31.94 C ANISOU 1769 CD1 LEU A 397 5357 3040 3739 -155 -80 87 C ATOM 1770 CD2 LEU A 397 39.071 4.922 14.108 1.00 23.49 C ANISOU 1770 CD2 LEU A 397 4086 2130 2710 -206 -193 -98 C ATOM 1771 N MET A 398 41.406 4.182 18.649 1.00 39.81 N ANISOU 1771 N MET A 398 6695 3877 4555 -211 -419 -202 N ATOM 1772 CA MET A 398 42.139 2.975 19.013 1.00 38.42 C ANISOU 1772 CA MET A 398 6504 3680 4414 -231 -566 -260 C ATOM 1773 C MET A 398 41.794 2.519 20.414 1.00 35.09 C ANISOU 1773 C MET A 398 6239 3158 3935 -212 -562 -209 C ATOM 1774 O MET A 398 41.845 1.334 20.723 1.00 35.78 O ANISOU 1774 O MET A 398 6292 3233 4069 -216 -647 -214 O ATOM 1775 CB MET A 398 43.645 3.195 18.911 1.00 32.84 C ANISOU 1775 CB MET A 398 5792 2976 3708 -276 -691 -353 C ATOM 1776 CG MET A 398 44.187 3.285 17.492 1.00 32.17 C ANISOU 1776 CG MET A 398 5525 3002 3696 -283 -723 -406 C ATOM 1777 SD MET A 398 43.965 1.782 16.470 1.00 35.90 S ANISOU 1777 SD MET A 398 5817 3555 4269 -262 -789 -440 S ATOM 1778 CE MET A 398 42.629 2.296 15.415 1.00 27.32 C ANISOU 1778 CE MET A 398 4638 2541 3200 -233 -651 -377 C ATOM 1779 N THR A 399 41.441 3.455 21.278 1.00 31.81 N ANISOU 1779 N THR A 399 6001 2669 3416 -184 -463 -157 N ATOM 1780 CA THR A 399 41.087 3.050 22.622 1.00 34.04 C ANISOU 1780 CA THR A 399 6445 2858 3630 -150 -447 -102 C ATOM 1781 C THR A 399 39.825 2.186 22.536 1.00 38.79 C ANISOU 1781 C THR A 399 6956 3487 4298 -102 -374 8 C ATOM 1782 O THR A 399 39.767 1.102 23.102 1.00 42.34 O ANISOU 1782 O THR A 399 7397 3912 4779 -98 -443 29 O ATOM 1783 CB THR A 399 40.916 4.259 23.562 1.00 40.77 C ANISOU 1783 CB THR A 399 7534 3618 4340 -112 -348 -66 C ATOM 1784 OG1 THR A 399 42.116 5.037 23.549 1.00 50.85 O ANISOU 1784 OG1 THR A 399 8879 4864 5577 -166 -447 -159 O ATOM 1785 CG2 THR A 399 40.677 3.807 24.976 1.00 32.65 C ANISOU 1785 CG2 THR A 399 6688 2492 3226 -68 -340 -16 C ATOM 1786 N SER A 400 38.833 2.648 21.786 1.00 31.37 N ANISOU 1786 N SER A 400 5932 2596 3392 -73 -247 88 N ATOM 1787 CA SER A 400 37.605 1.883 21.611 1.00 34.95 C ANISOU 1787 CA SER A 400 6284 3067 3928 -34 -189 217 C ATOM 1788 C SER A 400 37.843 0.541 20.912 1.00 37.77 C ANISOU 1788 C SER A 400 6465 3476 4411 -74 -345 171 C ATOM 1789 O SER A 400 37.174 -0.456 21.204 1.00 35.06 O ANISOU 1789 O SER A 400 6072 3116 4135 -51 -372 261 O ATOM 1790 CB SER A 400 36.590 2.699 20.806 1.00 36.26 C ANISOU 1790 CB SER A 400 6381 3274 4121 -12 -37 312 C ATOM 1791 OG SER A 400 36.098 3.781 21.570 1.00 44.32 O ANISOU 1791 OG SER A 400 7571 4236 5034 45 127 390 O ATOM 1792 N VAL A 401 38.789 0.526 19.980 1.00 33.94 N ANISOU 1792 N VAL A 401 5886 3051 3960 -125 -447 40 N ATOM 1793 CA VAL A 401 39.024 -0.653 19.174 1.00 30.75 C ANISOU 1793 CA VAL A 401 5325 2695 3662 -149 -587 -13 C ATOM 1794 C VAL A 401 39.747 -1.715 19.992 1.00 33.84 C ANISOU 1794 C VAL A 401 5751 3043 4066 -166 -724 -66 C ATOM 1795 O VAL A 401 39.410 -2.899 19.941 1.00 31.28 O ANISOU 1795 O VAL A 401 5342 2715 3826 -162 -811 -38 O ATOM 1796 CB VAL A 401 39.792 -0.302 17.883 1.00 31.52 C ANISOU 1796 CB VAL A 401 5318 2875 3782 -179 -634 -126 C ATOM 1797 CG1 VAL A 401 40.498 -1.504 17.330 1.00 22.91 C ANISOU 1797 CG1 VAL A 401 4123 1815 2766 -195 -797 -219 C ATOM 1798 CG2 VAL A 401 38.838 0.294 16.858 1.00 28.63 C ANISOU 1798 CG2 VAL A 401 4865 2563 3448 -167 -529 -58 C ATOM 1799 N THR A 402 40.732 -1.288 20.764 1.00 31.24 N ANISOU 1799 N THR A 402 5544 2671 3656 -189 -753 -134 N ATOM 1800 CA THR A 402 41.433 -2.223 21.623 1.00 38.77 C ANISOU 1800 CA THR A 402 6538 3576 4619 -214 -878 -176 C ATOM 1801 C THR A 402 40.567 -2.679 22.808 1.00 46.33 C ANISOU 1801 C THR A 402 7581 4467 5554 -174 -831 -58 C ATOM 1802 O THR A 402 40.718 -3.804 23.285 1.00 48.88 O ANISOU 1802 O THR A 402 7871 4770 5932 -185 -936 -58 O ATOM 1803 CB THR A 402 42.764 -1.653 22.103 1.00 38.89 C ANISOU 1803 CB THR A 402 6658 3552 4565 -259 -940 -268 C ATOM 1804 OG1 THR A 402 42.523 -0.429 22.800 1.00 45.88 O ANISOU 1804 OG1 THR A 402 7718 4382 5334 -239 -827 -224 O ATOM 1805 CG2 THR A 402 43.668 -1.380 20.919 1.00 32.95 C ANISOU 1805 CG2 THR A 402 5790 2872 3857 -289 -996 -362 C ATOM 1806 N ASN A 403 39.652 -1.832 23.278 1.00 40.87 N ANISOU 1806 N ASN A 403 6996 3746 4788 -119 -671 50 N ATOM 1807 CA ASN A 403 38.677 -2.292 24.277 1.00 41.98 C ANISOU 1807 CA ASN A 403 7196 3837 4919 -59 -604 192 C ATOM 1808 C ASN A 403 37.717 -3.414 23.802 1.00 36.58 C ANISOU 1808 C ASN A 403 6336 3186 4377 -40 -639 297 C ATOM 1809 O ASN A 403 37.224 -4.182 24.616 1.00 44.10 O ANISOU 1809 O ASN A 403 7295 4104 5358 -6 -653 397 O ATOM 1810 CB ASN A 403 37.885 -1.121 24.866 1.00 40.37 C ANISOU 1810 CB ASN A 403 7149 3589 4599 13 -408 299 C ATOM 1811 CG ASN A 403 38.736 -0.240 25.753 1.00 43.99 C ANISOU 1811 CG ASN A 403 7829 3977 4907 8 -400 221 C ATOM 1812 OD1 ASN A 403 39.785 -0.664 26.230 1.00 43.17 O ANISOU 1812 OD1 ASN A 403 7774 3842 4787 -46 -539 123 O ATOM 1813 ND2 ASN A 403 38.306 1.003 25.951 1.00 45.88 N ANISOU 1813 ND2 ASN A 403 8208 4186 5040 59 -247 266 N ATOM 1814 N ARG A 404 37.454 -3.505 22.501 1.00 34.30 N ANISOU 1814 N ARG A 404 5896 2960 4179 -61 -664 281 N ATOM 1815 CA ARG A 404 36.588 -4.561 21.962 1.00 30.87 C ANISOU 1815 CA ARG A 404 5303 2542 3885 -52 -730 377 C ATOM 1816 C ARG A 404 37.360 -5.499 21.065 1.00 29.79 C ANISOU 1816 C ARG A 404 5041 2445 3835 -105 -918 241 C ATOM 1817 O ARG A 404 36.779 -6.183 20.218 1.00 36.36 O ANISOU 1817 O ARG A 404 5742 3295 4776 -106 -990 282 O ATOM 1818 CB ARG A 404 35.426 -3.983 21.148 1.00 31.84 C ANISOU 1818 CB ARG A 404 5356 2689 4051 -26 -611 503 C ATOM 1819 CG ARG A 404 34.421 -3.201 21.953 1.00 46.72 C ANISOU 1819 CG ARG A 404 7341 4533 5878 44 -413 680 C ATOM 1820 CD ARG A 404 33.302 -2.655 21.063 1.00 57.37 C ANISOU 1820 CD ARG A 404 8603 5906 7290 58 -301 812 C ATOM 1821 NE ARG A 404 32.131 -3.526 21.055 1.00 68.64 N ANISOU 1821 NE ARG A 404 9917 7309 8854 86 -324 1014 N ATOM 1822 CZ ARG A 404 31.236 -3.579 22.041 1.00 72.65 C ANISOU 1822 CZ ARG A 404 10468 7768 9366 161 -211 1217 C ATOM 1823 NH1 ARG A 404 31.383 -2.818 23.120 1.00 67.37 N ANISOU 1823 NH1 ARG A 404 9977 7068 8554 222 -64 1229 N ATOM 1824 NH2 ARG A 404 30.199 -4.399 21.952 1.00 76.71 N ANISOU 1824 NH2 ARG A 404 10856 8260 10028 182 -250 1418 N ATOM 1825 N CYS A 405 38.666 -5.531 21.253 1.00 30.15 N ANISOU 1825 N CYS A 405 4668 2671 4118 814 -169 241 N ATOM 1826 CA CYS A 405 39.542 -6.303 20.389 1.00 34.35 C ANISOU 1826 CA CYS A 405 5181 3241 4629 694 -245 180 C ATOM 1827 C CYS A 405 39.109 -7.769 20.247 1.00 33.60 C ANISOU 1827 C CYS A 405 5064 3145 4558 685 -203 277 C ATOM 1828 O CYS A 405 39.161 -8.331 19.153 1.00 29.95 O ANISOU 1828 O CYS A 405 4544 2686 4149 559 -272 302 O ATOM 1829 CB CYS A 405 41.000 -6.230 20.882 1.00 29.57 C ANISOU 1829 CB CYS A 405 4652 2684 3899 754 -307 8 C ATOM 1830 SG CYS A 405 42.136 -6.818 19.612 1.00 58.13 S ANISOU 1830 SG CYS A 405 8234 6356 7497 583 -420 -69 S ATOM 1831 N GLN A 406 38.704 -8.383 21.353 1.00 40.84 N ANISOU 1831 N GLN A 406 6023 4056 5437 835 -100 335 N ATOM 1832 CA GLN A 406 38.273 -9.781 21.348 1.00 44.17 C ANISOU 1832 CA GLN A 406 6411 4473 5899 842 -64 438 C ATOM 1833 C GLN A 406 37.093 -9.962 20.386 1.00 40.71 C ANISOU 1833 C GLN A 406 5862 3955 5652 738 -70 595 C ATOM 1834 O GLN A 406 37.161 -10.777 19.475 1.00 32.21 O ANISOU 1834 O GLN A 406 4729 2875 4633 643 -157 618 O ATOM 1835 CB GLN A 406 37.892 -10.230 22.763 1.00 56.12 C ANISOU 1835 CB GLN A 406 7983 5983 7359 1042 73 499 C ATOM 1836 CG GLN A 406 37.557 -11.717 22.894 1.00 75.44 C ANISOU 1836 CG GLN A 406 10389 8429 9846 1064 110 603 C ATOM 1837 CD GLN A 406 38.774 -12.591 23.189 1.00 89.84 C ANISOU 1837 CD GLN A 406 12287 10336 11513 1081 51 459 C ATOM 1838 OE1 GLN A 406 39.804 -12.113 23.673 1.00 93.21 O ANISOU 1838 OE1 GLN A 406 12819 10803 11792 1134 25 286 O ATOM 1839 NE2 GLN A 406 38.651 -13.885 22.908 1.00 94.05 N ANISOU 1839 NE2 GLN A 406 12763 10883 12087 1040 17 525 N ATOM 1840 N GLU A 407 36.036 -9.173 20.572 1.00 30.54 N ANISOU 1840 N GLU A 407 4547 2594 4462 766 7 692 N ATOM 1841 CA GLU A 407 34.881 -9.207 19.676 1.00 34.18 C ANISOU 1841 CA GLU A 407 4914 2950 5124 672 -2 823 C ATOM 1842 C GLU A 407 35.220 -8.880 18.201 1.00 33.28 C ANISOU 1842 C GLU A 407 4764 2823 5056 504 -141 753 C ATOM 1843 O GLU A 407 34.757 -9.559 17.280 1.00 32.50 O ANISOU 1843 O GLU A 407 4601 2658 5091 439 -206 822 O ATOM 1844 CB GLU A 407 33.766 -8.282 20.193 1.00 39.05 C ANISOU 1844 CB GLU A 407 5524 3496 5817 729 102 916 C ATOM 1845 CG GLU A 407 32.624 -8.097 19.189 1.00 55.52 C ANISOU 1845 CG GLU A 407 7527 5452 8115 616 78 1015 C ATOM 1846 CD GLU A 407 31.663 -6.973 19.558 1.00 69.95 C ANISOU 1846 CD GLU A 407 9359 7224 9996 640 153 1068 C ATOM 1847 OE1 GLU A 407 31.242 -6.225 18.641 1.00 73.44 O ANISOU 1847 OE1 GLU A 407 9775 7600 10528 514 90 1041 O ATOM 1848 OE2 GLU A 407 31.329 -6.839 20.759 1.00 72.02 O ANISOU 1848 OE2 GLU A 407 9654 7509 10202 793 272 1132 O ATOM 1849 N LEU A 408 36.029 -7.852 17.975 1.00 28.12 N ANISOU 1849 N LEU A 408 4151 2228 4305 453 -194 621 N ATOM 1850 CA LEU A 408 36.346 -7.446 16.610 1.00 33.13 C ANISOU 1850 CA LEU A 408 4754 2854 4980 313 -305 567 C ATOM 1851 C LEU A 408 37.206 -8.474 15.874 1.00 36.40 C ANISOU 1851 C LEU A 408 5161 3325 5346 272 -407 525 C ATOM 1852 O LEU A 408 36.982 -8.754 14.697 1.00 31.19 O ANISOU 1852 O LEU A 408 4457 2621 4773 201 -491 556 O ATOM 1853 CB LEU A 408 37.018 -6.074 16.594 1.00 27.40 C ANISOU 1853 CB LEU A 408 4057 2175 4180 276 -333 453 C ATOM 1854 CG LEU A 408 36.198 -4.968 17.244 1.00 30.68 C ANISOU 1854 CG LEU A 408 4479 2546 4632 317 -268 482 C ATOM 1855 CD1 LEU A 408 36.968 -3.661 17.256 1.00 34.76 C ANISOU 1855 CD1 LEU A 408 5011 3112 5083 290 -328 364 C ATOM 1856 CD2 LEU A 408 34.888 -4.805 16.508 1.00 32.64 C ANISOU 1856 CD2 LEU A 408 4675 2680 5048 241 -254 584 C ATOM 1857 N ALA A 409 38.181 -9.036 16.579 1.00 34.42 N ANISOU 1857 N ALA A 409 4960 3169 4951 331 -407 449 N ATOM 1858 CA ALA A 409 39.088 -10.024 16.000 1.00 31.63 C ANISOU 1858 CA ALA A 409 4608 2888 4522 296 -511 395 C ATOM 1859 C ALA A 409 38.400 -11.319 15.580 1.00 33.42 C ANISOU 1859 C ALA A 409 4777 3071 4850 306 -559 507 C ATOM 1860 O ALA A 409 38.864 -11.990 14.665 1.00 29.30 O ANISOU 1860 O ALA A 409 4235 2587 4312 263 -684 488 O ATOM 1861 CB ALA A 409 40.218 -10.331 16.975 1.00 31.93 C ANISOU 1861 CB ALA A 409 4723 3021 4387 361 -496 276 C ATOM 1862 N THR A 410 37.311 -11.675 16.259 1.00 32.14 N ANISOU 1862 N THR A 410 4584 2829 4800 376 -469 632 N ATOM 1863 CA THR A 410 36.607 -12.926 15.985 1.00 28.60 C ANISOU 1863 CA THR A 410 4061 2319 4485 401 -520 754 C ATOM 1864 C THR A 410 35.442 -12.741 15.018 1.00 34.55 C ANISOU 1864 C THR A 410 4740 2921 5464 363 -562 863 C ATOM 1865 O THR A 410 34.824 -13.714 14.577 1.00 37.45 O ANISOU 1865 O THR A 410 5035 3207 5987 386 -642 964 O ATOM 1866 CB THR A 410 36.048 -13.563 17.280 1.00 31.13 C ANISOU 1866 CB THR A 410 4374 2622 4834 514 -395 853 C ATOM 1867 OG1 THR A 410 35.289 -12.588 18.003 1.00 37.29 O ANISOU 1867 OG1 THR A 410 5170 3340 5660 564 -244 909 O ATOM 1868 CG2 THR A 410 37.165 -14.065 18.158 1.00 24.17 C ANISOU 1868 CG2 THR A 410 3570 1870 3742 568 -379 741 C ATOM 1869 N ASN A 411 35.145 -11.490 14.695 1.00 27.10 N ANISOU 1869 N ASN A 411 3816 1931 4551 310 -522 836 N ATOM 1870 CA ASN A 411 34.021 -11.179 13.846 1.00 25.65 C ANISOU 1870 CA ASN A 411 3581 1589 4576 274 -550 916 C ATOM 1871 C ASN A 411 34.334 -11.400 12.374 1.00 29.04 C ANISOU 1871 C ASN A 411 3999 1997 5038 226 -717 873 C ATOM 1872 O ASN A 411 35.468 -11.247 11.953 1.00 30.89 O ANISOU 1872 O ASN A 411 4275 2353 5110 191 -780 765 O ATOM 1873 CB ASN A 411 33.578 -9.741 14.053 1.00 21.93 C ANISOU 1873 CB ASN A 411 3140 1081 4113 234 -454 892 C ATOM 1874 CG ASN A 411 32.478 -9.359 13.107 1.00 33.08 C ANISOU 1874 CG ASN A 411 4515 2322 5731 184 -491 946 C ATOM 1875 OD1 ASN A 411 31.333 -9.798 13.257 1.00 35.92 O ANISOU 1875 OD1 ASN A 411 4822 2539 6287 224 -458 1071 O ATOM 1876 ND2 ASN A 411 32.820 -8.578 12.092 1.00 22.92 N ANISOU 1876 ND2 ASN A 411 3256 1037 4416 105 -563 855 N ATOM 1877 N GLU A 412 33.312 -11.749 11.601 1.00 35.88 N ANISOU 1877 N GLU A 412 4812 2696 6125 240 -789 960 N ATOM 1878 CA GLU A 412 33.475 -12.073 10.187 1.00 35.04 C ANISOU 1878 CA GLU A 412 4700 2544 6069 239 -964 931 C ATOM 1879 C GLU A 412 33.991 -10.915 9.332 1.00 31.83 C ANISOU 1879 C GLU A 412 4352 2174 5569 169 -976 824 C ATOM 1880 O GLU A 412 34.645 -11.144 8.322 1.00 28.99 O ANISOU 1880 O GLU A 412 4011 1859 5146 183 -1102 775 O ATOM 1881 CB GLU A 412 32.156 -12.568 9.613 1.00 34.08 C ANISOU 1881 CB GLU A 412 4503 2220 6225 282 -1037 1029 C ATOM 1882 CG GLU A 412 31.014 -11.611 9.839 1.00 38.67 C ANISOU 1882 CG GLU A 412 5058 2696 6940 231 -913 1052 C ATOM 1883 CD GLU A 412 29.695 -12.179 9.364 1.00 45.33 C ANISOU 1883 CD GLU A 412 5758 3436 8031 244 -976 1103 C ATOM 1884 OE1 GLU A 412 29.728 -13.049 8.460 1.00 47.83 O ANISOU 1884 OE1 GLU A 412 6012 3753 8408 275 -1150 1079 O ATOM 1885 OE2 GLU A 412 28.636 -11.758 9.891 1.00 37.76 O ANISOU 1885 OE2 GLU A 412 4748 2392 7208 227 -859 1163 O ATOM 1886 N TYR A 413 33.682 -9.680 9.719 1.00 20.22 N ANISOU 1886 N TYR A 413 2907 685 4091 105 -853 797 N ATOM 1887 CA TYR A 413 34.141 -8.520 8.962 1.00 25.61 C ANISOU 1887 CA TYR A 413 3632 1399 4700 34 -861 704 C ATOM 1888 C TYR A 413 35.249 -7.748 9.677 1.00 28.49 C ANISOU 1888 C TYR A 413 4027 1936 4862 -11 -784 618 C ATOM 1889 O TYR A 413 36.215 -7.319 9.054 1.00 28.50 O ANISOU 1889 O TYR A 413 4048 2027 4754 -44 -827 544 O ATOM 1890 CB TYR A 413 32.980 -7.580 8.644 1.00 31.43 C ANISOU 1890 CB TYR A 413 4372 1974 5597 -13 -818 719 C ATOM 1891 CG TYR A 413 31.834 -8.267 7.948 1.00 38.49 C ANISOU 1891 CG TYR A 413 5222 2693 6711 36 -899 784 C ATOM 1892 CD1 TYR A 413 32.031 -8.922 6.739 1.00 37.77 C ANISOU 1892 CD1 TYR A 413 5105 2615 6633 85 -1053 753 C ATOM 1893 CD2 TYR A 413 30.553 -8.266 8.498 1.00 35.73 C ANISOU 1893 CD2 TYR A 413 4798 2265 6514 33 -828 844 C ATOM 1894 CE1 TYR A 413 30.985 -9.552 6.090 1.00 38.07 C ANISOU 1894 CE1 TYR A 413 5045 2581 6841 124 -1148 766 C ATOM 1895 CE2 TYR A 413 29.497 -8.899 7.858 1.00 36.53 C ANISOU 1895 CE2 TYR A 413 4791 2290 6799 65 -910 868 C ATOM 1896 CZ TYR A 413 29.720 -9.539 6.649 1.00 40.28 C ANISOU 1896 CZ TYR A 413 5241 2772 7292 108 -1078 822 C ATOM 1897 OH TYR A 413 28.690 -10.192 5.997 1.00 37.77 O ANISOU 1897 OH TYR A 413 4813 2367 7170 143 -1185 834 O ATOM 1898 N ALA A 414 35.133 -7.596 10.987 1.00 31.42 N ANISOU 1898 N ALA A 414 4402 2346 5192 7 -676 632 N ATOM 1899 CA ALA A 414 36.069 -6.740 11.707 1.00 30.62 C ANISOU 1899 CA ALA A 414 4332 2371 4931 -13 -620 543 C ATOM 1900 C ALA A 414 37.476 -7.339 11.873 1.00 30.48 C ANISOU 1900 C ALA A 414 4337 2498 4746 10 -665 471 C ATOM 1901 O ALA A 414 38.427 -6.615 12.151 1.00 26.61 O ANISOU 1901 O ALA A 414 3869 2095 4146 -10 -654 383 O ATOM 1902 CB ALA A 414 35.486 -6.317 13.039 1.00 26.58 C ANISOU 1902 CB ALA A 414 3830 1846 4422 32 -504 573 C ATOM 1903 N ASN A 415 37.626 -8.645 11.676 1.00 28.11 N ANISOU 1903 N ASN A 415 4027 2216 4438 53 -730 504 N ATOM 1904 CA ASN A 415 38.966 -9.226 11.736 1.00 22.80 C ANISOU 1904 CA ASN A 415 3381 1681 3601 64 -787 424 C ATOM 1905 C ASN A 415 39.944 -8.558 10.755 1.00 23.09 C ANISOU 1905 C ASN A 415 3424 1782 3567 8 -846 352 C ATOM 1906 O ASN A 415 41.132 -8.414 11.037 1.00 31.96 O ANISOU 1906 O ASN A 415 4573 3010 4560 -1 -851 266 O ATOM 1907 CB ASN A 415 38.922 -10.745 11.540 1.00 28.56 C ANISOU 1907 CB ASN A 415 4091 2423 4336 114 -878 471 C ATOM 1908 CG ASN A 415 38.608 -11.156 10.098 1.00 29.81 C ANISOU 1908 CG ASN A 415 4218 2523 4585 118 -1012 517 C ATOM 1909 OD1 ASN A 415 39.507 -11.309 9.271 1.00 27.02 O ANISOU 1909 OD1 ASN A 415 3880 2254 4134 113 -1107 466 O ATOM 1910 ND2 ASN A 415 37.332 -11.388 9.813 1.00 22.69 N ANISOU 1910 ND2 ASN A 415 3276 1468 3876 146 -1027 616 N ATOM 1911 N TYR A 416 39.430 -8.111 9.621 1.00 21.87 N ANISOU 1911 N TYR A 416 3249 1552 3510 -22 -886 389 N ATOM 1912 CA TYR A 416 40.250 -7.433 8.624 1.00 26.10 C ANISOU 1912 CA TYR A 416 3784 2138 3994 -61 -927 345 C ATOM 1913 C TYR A 416 40.878 -6.162 9.156 1.00 28.40 C ANISOU 1913 C TYR A 416 4074 2475 4242 -114 -855 278 C ATOM 1914 O TYR A 416 41.984 -5.780 8.766 1.00 32.07 O ANISOU 1914 O TYR A 416 4533 3020 4634 -135 -877 230 O ATOM 1915 CB TYR A 416 39.404 -7.130 7.391 1.00 21.90 C ANISOU 1915 CB TYR A 416 3241 1491 3588 -64 -970 396 C ATOM 1916 CG TYR A 416 39.135 -8.375 6.576 1.00 27.75 C ANISOU 1916 CG TYR A 416 3983 2197 4363 17 -1092 446 C ATOM 1917 CD1 TYR A 416 40.080 -8.861 5.682 1.00 31.50 C ANISOU 1917 CD1 TYR A 416 4470 2767 4733 63 -1191 431 C ATOM 1918 CD2 TYR A 416 37.949 -9.079 6.720 1.00 27.82 C ANISOU 1918 CD2 TYR A 416 3976 2077 4518 61 -1121 516 C ATOM 1919 CE1 TYR A 416 39.830 -10.010 4.924 1.00 28.86 C ANISOU 1919 CE1 TYR A 416 4136 2401 4426 163 -1336 475 C ATOM 1920 CE2 TYR A 416 37.693 -10.214 5.979 1.00 33.32 C ANISOU 1920 CE2 TYR A 416 4663 2726 5271 153 -1264 562 C ATOM 1921 CZ TYR A 416 38.629 -10.680 5.082 1.00 33.23 C ANISOU 1921 CZ TYR A 416 4670 2815 5142 208 -1381 537 C ATOM 1922 OH TYR A 416 38.355 -11.819 4.345 1.00 40.67 O ANISOU 1922 OH TYR A 416 5602 3710 6140 323 -1553 582 O ATOM 1923 N ILE A 417 40.152 -5.517 10.057 1.00 28.14 N ANISOU 1923 N ILE A 417 4042 2384 4266 -123 -778 282 N ATOM 1924 CA ILE A 417 40.576 -4.271 10.648 1.00 28.53 C ANISOU 1924 CA ILE A 417 4084 2458 4296 -153 -735 222 C ATOM 1925 C ILE A 417 41.691 -4.547 11.645 1.00 24.60 C ANISOU 1925 C ILE A 417 3615 2051 3681 -105 -731 144 C ATOM 1926 O ILE A 417 42.713 -3.871 11.649 1.00 21.84 O ANISOU 1926 O ILE A 417 3253 1749 3297 -123 -752 78 O ATOM 1927 CB ILE A 417 39.379 -3.563 11.334 1.00 27.80 C ANISOU 1927 CB ILE A 417 3991 2281 4290 -155 -672 252 C ATOM 1928 CG1 ILE A 417 38.391 -3.088 10.264 1.00 23.08 C ANISOU 1928 CG1 ILE A 417 3373 1582 3816 -218 -685 299 C ATOM 1929 CG2 ILE A 417 39.853 -2.406 12.218 1.00 21.10 C ANISOU 1929 CG2 ILE A 417 3140 1468 3407 -148 -654 183 C ATOM 1930 CD1 ILE A 417 37.228 -2.356 10.797 1.00 27.84 C ANISOU 1930 CD1 ILE A 417 3975 2100 4503 -235 -633 323 C ATOM 1931 N ILE A 418 41.494 -5.567 12.470 1.00 20.48 N ANISOU 1931 N ILE A 418 3130 1540 3112 -38 -707 153 N ATOM 1932 CA ILE A 418 42.501 -5.936 13.454 1.00 20.30 C ANISOU 1932 CA ILE A 418 3153 1587 2971 21 -703 65 C ATOM 1933 C ILE A 418 43.761 -6.400 12.730 1.00 25.66 C ANISOU 1933 C ILE A 418 3832 2349 3569 -11 -779 10 C ATOM 1934 O ILE A 418 44.878 -6.127 13.168 1.00 25.45 O ANISOU 1934 O ILE A 418 3827 2365 3477 2 -794 -86 O ATOM 1935 CB ILE A 418 41.980 -7.053 14.393 1.00 25.10 C ANISOU 1935 CB ILE A 418 3801 2190 3544 103 -658 96 C ATOM 1936 CG1 ILE A 418 40.686 -6.608 15.114 1.00 25.49 C ANISOU 1936 CG1 ILE A 418 3847 2157 3680 150 -569 173 C ATOM 1937 CG2 ILE A 418 43.054 -7.477 15.373 1.00 23.85 C ANISOU 1937 CG2 ILE A 418 3709 2097 3255 171 -659 -15 C ATOM 1938 CD1 ILE A 418 40.742 -5.216 15.773 1.00 23.41 C ANISOU 1938 CD1 ILE A 418 3595 1877 3421 177 -539 121 C ATOM 1939 N GLN A 419 43.582 -7.104 11.617 1.00 26.71 N ANISOU 1939 N GLN A 419 3942 2495 3711 -39 -836 71 N ATOM 1940 CA GLN A 419 44.728 -7.532 10.821 1.00 24.62 C ANISOU 1940 CA GLN A 419 3676 2318 3361 -57 -912 34 C ATOM 1941 C GLN A 419 45.449 -6.342 10.251 1.00 25.11 C ANISOU 1941 C GLN A 419 3700 2388 3452 -104 -908 13 C ATOM 1942 O GLN A 419 46.670 -6.323 10.220 1.00 22.56 O ANISOU 1942 O GLN A 419 3380 2129 3063 -109 -935 -50 O ATOM 1943 CB GLN A 419 44.320 -8.425 9.667 1.00 21.35 C ANISOU 1943 CB GLN A 419 3246 1910 2956 -47 -993 112 C ATOM 1944 CG GLN A 419 43.974 -9.858 10.040 1.00 19.32 C ANISOU 1944 CG GLN A 419 3010 1671 2659 3 -1044 130 C ATOM 1945 CD GLN A 419 43.611 -10.628 8.790 1.00 26.99 C ANISOU 1945 CD GLN A 419 3959 2637 3661 34 -1161 204 C ATOM 1946 OE1 GLN A 419 44.455 -10.837 7.919 1.00 27.25 O ANISOU 1946 OE1 GLN A 419 3994 2750 3608 44 -1241 188 O ATOM 1947 NE2 GLN A 419 42.347 -11.013 8.670 1.00 21.62 N ANISOU 1947 NE2 GLN A 419 3255 1850 3111 67 -1177 290 N ATOM 1948 N HIS A 420 44.702 -5.346 9.786 1.00 22.56 N ANISOU 1948 N HIS A 420 3337 1994 3240 -140 -877 66 N ATOM 1949 CA HIS A 420 45.364 -4.181 9.233 1.00 20.64 C ANISOU 1949 CA HIS A 420 3043 1756 3041 -185 -875 57 C ATOM 1950 C HIS A 420 46.223 -3.485 10.289 1.00 27.57 C ANISOU 1950 C HIS A 420 3916 2642 3916 -175 -863 -33 C ATOM 1951 O HIS A 420 47.389 -3.177 10.053 1.00 31.93 O ANISOU 1951 O HIS A 420 4440 3233 4461 -185 -888 -68 O ATOM 1952 CB HIS A 420 44.381 -3.190 8.627 1.00 27.88 C ANISOU 1952 CB HIS A 420 3922 2594 4076 -229 -850 115 C ATOM 1953 CG HIS A 420 45.052 -1.956 8.114 1.00 39.20 C ANISOU 1953 CG HIS A 420 5292 4034 5568 -275 -849 112 C ATOM 1954 ND1 HIS A 420 45.126 -0.788 8.843 1.00 41.46 N ANISOU 1954 ND1 HIS A 420 5540 4289 5922 -299 -838 71 N ATOM 1955 CD2 HIS A 420 45.738 -1.729 6.969 1.00 39.56 C ANISOU 1955 CD2 HIS A 420 5297 4116 5617 -287 -863 153 C ATOM 1956 CE1 HIS A 420 45.802 0.114 8.156 1.00 38.93 C ANISOU 1956 CE1 HIS A 420 5149 3980 5665 -337 -850 88 C ATOM 1957 NE2 HIS A 420 46.177 -0.429 7.013 1.00 40.73 N ANISOU 1957 NE2 HIS A 420 5374 4248 5852 -331 -852 143 N ATOM 1958 N ILE A 421 45.647 -3.246 11.458 1.00 24.48 N ANISOU 1958 N ILE A 421 3556 2206 3541 -138 -831 -67 N ATOM 1959 CA ILE A 421 46.388 -2.628 12.543 1.00 22.17 C ANISOU 1959 CA ILE A 421 3274 1901 3249 -90 -841 -162 C ATOM 1960 C ILE A 421 47.650 -3.420 12.913 1.00 26.64 C ANISOU 1960 C ILE A 421 3886 2518 3720 -52 -872 -252 C ATOM 1961 O ILE A 421 48.735 -2.860 13.048 1.00 23.58 O ANISOU 1961 O ILE A 421 3473 2122 3364 -45 -910 -318 O ATOM 1962 CB ILE A 421 45.508 -2.461 13.783 1.00 21.84 C ANISOU 1962 CB ILE A 421 3279 1810 3209 -15 -802 -179 C ATOM 1963 CG1 ILE A 421 44.338 -1.530 13.446 1.00 24.47 C ANISOU 1963 CG1 ILE A 421 3566 2091 3641 -61 -781 -105 C ATOM 1964 CG2 ILE A 421 46.359 -1.931 14.929 1.00 21.61 C ANISOU 1964 CG2 ILE A 421 3278 1759 3172 76 -835 -292 C ATOM 1965 CD1 ILE A 421 43.144 -1.614 14.402 1.00 23.19 C ANISOU 1965 CD1 ILE A 421 3448 1886 3476 7 -726 -75 C ATOM 1966 N VAL A 422 47.500 -4.729 13.075 1.00 30.27 N ANISOU 1966 N VAL A 422 4407 3021 4074 -27 -866 -255 N ATOM 1967 CA VAL A 422 48.621 -5.597 13.443 1.00 24.29 C ANISOU 1967 CA VAL A 422 3706 2316 3208 1 -903 -353 C ATOM 1968 C VAL A 422 49.736 -5.619 12.390 1.00 27.33 C ANISOU 1968 C VAL A 422 4047 2759 3580 -56 -953 -353 C ATOM 1969 O VAL A 422 50.910 -5.712 12.714 1.00 32.18 O ANISOU 1969 O VAL A 422 4684 3385 4159 -42 -986 -450 O ATOM 1970 CB VAL A 422 48.126 -7.034 13.761 1.00 28.16 C ANISOU 1970 CB VAL A 422 4259 2848 3592 32 -898 -345 C ATOM 1971 CG1 VAL A 422 49.290 -8.018 13.862 1.00 27.36 C ANISOU 1971 CG1 VAL A 422 4212 2820 3364 36 -955 -444 C ATOM 1972 CG2 VAL A 422 47.358 -7.027 15.059 1.00 27.75 C ANISOU 1972 CG2 VAL A 422 4260 2741 3542 118 -834 -362 C ATOM 1973 N SER A 423 49.370 -5.481 11.129 1.00 29.56 N ANISOU 1973 N SER A 423 4268 3064 3898 -107 -957 -244 N ATOM 1974 CA SER A 423 50.351 -5.575 10.060 1.00 36.63 C ANISOU 1974 CA SER A 423 5125 4025 4768 -136 -995 -218 C ATOM 1975 C SER A 423 50.990 -4.232 9.670 1.00 37.78 C ANISOU 1975 C SER A 423 5183 4131 5039 -165 -979 -197 C ATOM 1976 O SER A 423 51.930 -4.187 8.876 1.00 42.04 O ANISOU 1976 O SER A 423 5681 4718 5575 -178 -995 -168 O ATOM 1977 CB SER A 423 49.696 -6.232 8.839 1.00 33.02 C ANISOU 1977 CB SER A 423 4659 3615 4273 -138 -1020 -109 C ATOM 1978 OG SER A 423 48.750 -5.357 8.269 1.00 33.80 O ANISOU 1978 OG SER A 423 4710 3648 4487 -160 -982 -23 O ATOM 1979 N ASN A 424 50.482 -3.140 10.224 1.00 37.56 N ANISOU 1979 N ASN A 424 5122 4021 5128 -168 -954 -202 N ATOM 1980 CA ASN A 424 50.952 -1.819 9.831 1.00 31.35 C ANISOU 1980 CA ASN A 424 4236 3192 4485 -198 -955 -169 C ATOM 1981 C ASN A 424 52.043 -1.288 10.760 1.00 30.27 C ANISOU 1981 C ASN A 424 4083 2999 4420 -161 -996 -273 C ATOM 1982 O ASN A 424 51.786 -1.043 11.932 1.00 33.02 O ANISOU 1982 O ASN A 424 4474 3285 4785 -106 -1015 -358 O ATOM 1983 CB ASN A 424 49.782 -0.842 9.788 1.00 35.94 C ANISOU 1983 CB ASN A 424 4778 3715 5165 -225 -932 -115 C ATOM 1984 CG ASN A 424 50.094 0.404 8.995 1.00 36.48 C ANISOU 1984 CG ASN A 424 4731 3758 5373 -272 -934 -48 C ATOM 1985 OD1 ASN A 424 51.246 0.805 8.864 1.00 40.57 O ANISOU 1985 OD1 ASN A 424 5183 4273 5960 -269 -956 -54 O ATOM 1986 ND2 ASN A 424 49.064 1.027 8.467 1.00 46.27 N ANISOU 1986 ND2 ASN A 424 5943 4971 6667 -314 -912 17 N ATOM 1987 N ASP A 425 53.253 -1.110 10.227 1.00 26.33 N ANISOU 1987 N ASP A 425 3522 2511 3971 -175 -1014 -263 N ATOM 1988 CA ASP A 425 54.371 -0.648 11.020 1.00 23.68 C ANISOU 1988 CA ASP A 425 3165 2097 3734 -133 -1067 -364 C ATOM 1989 C ASP A 425 54.069 0.712 11.602 1.00 27.30 C ANISOU 1989 C ASP A 425 3552 2451 4368 -108 -1107 -374 C ATOM 1990 O ASP A 425 54.440 0.990 12.745 1.00 26.62 O ANISOU 1990 O ASP A 425 3499 2277 4337 -28 -1170 -493 O ATOM 1991 CB ASP A 425 55.658 -0.599 10.198 1.00 33.81 C ANISOU 1991 CB ASP A 425 4370 3400 5075 -156 -1071 -319 C ATOM 1992 CG ASP A 425 56.228 -1.988 9.913 1.00 39.37 C ANISOU 1992 CG ASP A 425 5160 4202 5596 -157 -1068 -353 C ATOM 1993 OD1 ASP A 425 55.855 -2.959 10.611 1.00 39.05 O ANISOU 1993 OD1 ASP A 425 5239 4190 5406 -134 -1081 -446 O ATOM 1994 OD2 ASP A 425 57.056 -2.107 8.988 1.00 41.58 O ANISOU 1994 OD2 ASP A 425 5384 4535 5880 -176 -1055 -280 O ATOM 1995 N ASP A 426 53.368 1.543 10.836 1.00 23.59 N ANISOU 1995 N ASP A 426 2995 1990 3980 -165 -1082 -260 N ATOM 1996 CA ASP A 426 53.033 2.888 11.304 1.00 30.91 C ANISOU 1996 CA ASP A 426 3842 2830 5071 -150 -1140 -264 C ATOM 1997 C ASP A 426 52.016 2.891 12.460 1.00 32.90 C ANISOU 1997 C ASP A 426 4187 3052 5261 -86 -1161 -342 C ATOM 1998 O ASP A 426 51.734 3.943 13.034 1.00 32.62 O ANISOU 1998 O ASP A 426 4104 2950 5340 -47 -1232 -365 O ATOM 1999 CB ASP A 426 52.558 3.771 10.143 1.00 28.28 C ANISOU 1999 CB ASP A 426 3395 2517 4833 -235 -1110 -128 C ATOM 2000 CG ASP A 426 53.674 4.063 9.137 1.00 34.87 C ANISOU 2000 CG ASP A 426 4113 3362 5774 -266 -1093 -38 C ATOM 2001 OD1 ASP A 426 53.384 4.115 7.924 1.00 39.79 O ANISOU 2001 OD1 ASP A 426 4696 4044 6380 -319 -1025 82 O ATOM 2002 OD2 ASP A 426 54.842 4.228 9.554 1.00 34.34 O ANISOU 2002 OD2 ASP A 426 3998 3236 5814 -223 -1147 -85 O ATOM 2003 N LEU A 427 51.490 1.712 12.800 1.00 23.87 N ANISOU 2003 N LEU A 427 3168 1959 3941 -65 -1106 -374 N ATOM 2004 CA LEU A 427 50.588 1.545 13.941 1.00 25.46 C ANISOU 2004 CA LEU A 427 3466 2137 4072 17 -1104 -434 C ATOM 2005 C LEU A 427 51.242 0.638 15.003 1.00 27.09 C ANISOU 2005 C LEU A 427 3788 2327 4180 122 -1117 -563 C ATOM 2006 O LEU A 427 50.554 0.044 15.846 1.00 28.15 O ANISOU 2006 O LEU A 427 4024 2466 4205 196 -1083 -600 O ATOM 2007 CB LEU A 427 49.227 0.963 13.489 1.00 23.22 C ANISOU 2007 CB LEU A 427 3224 1911 3690 -38 -1020 -346 C ATOM 2008 CG LEU A 427 48.354 1.912 12.636 1.00 27.60 C ANISOU 2008 CG LEU A 427 3694 2459 4335 -125 -1010 -247 C ATOM 2009 CD1 LEU A 427 47.160 1.238 11.976 1.00 21.68 C ANISOU 2009 CD1 LEU A 427 2983 1740 3513 -180 -937 -164 C ATOM 2010 CD2 LEU A 427 47.850 3.087 13.430 1.00 23.50 C ANISOU 2010 CD2 LEU A 427 3145 1880 3904 -80 -1068 -277 C ATOM 2011 N ALA A 428 52.567 0.520 14.953 1.00 23.69 N ANISOU 2011 N ALA A 428 3342 1870 3791 133 -1163 -629 N ATOM 2012 CA ALA A 428 53.271 -0.472 15.778 1.00 26.55 C ANISOU 2012 CA ALA A 428 3824 2219 4044 212 -1174 -763 C ATOM 2013 C ALA A 428 52.794 -0.505 17.243 1.00 29.83 C ANISOU 2013 C ALA A 428 4352 2571 4409 366 -1191 -867 C ATOM 2014 O ALA A 428 52.486 -1.569 17.777 1.00 33.13 O ANISOU 2014 O ALA A 428 4887 3029 4673 410 -1138 -911 O ATOM 2015 CB ALA A 428 54.772 -0.258 15.709 1.00 36.48 C ANISOU 2015 CB ALA A 428 5042 3412 5408 222 -1244 -840 C ATOM 2016 N VAL A 429 52.704 0.659 17.877 1.00 28.64 N ANISOU 2016 N VAL A 429 4165 2327 4389 462 -1268 -898 N ATOM 2017 CA VAL A 429 52.309 0.736 19.283 1.00 33.08 C ANISOU 2017 CA VAL A 429 4838 2824 4905 649 -1296 -994 C ATOM 2018 C VAL A 429 50.928 0.125 19.535 1.00 35.25 C ANISOU 2018 C VAL A 429 5183 3178 5032 658 -1186 -917 C ATOM 2019 O VAL A 429 50.689 -0.508 20.567 1.00 42.08 O ANISOU 2019 O VAL A 429 6174 4030 5783 795 -1152 -985 O ATOM 2020 CB VAL A 429 52.356 2.194 19.789 1.00 42.53 C ANISOU 2020 CB VAL A 429 5965 3916 6277 757 -1426 -1021 C ATOM 2021 CG1 VAL A 429 51.348 3.032 19.042 1.00 40.76 C ANISOU 2021 CG1 VAL A 429 5625 3748 6113 646 -1410 -875 C ATOM 2022 CG2 VAL A 429 52.107 2.258 21.282 1.00 42.20 C ANISOU 2022 CG2 VAL A 429 6054 3800 6181 997 -1475 -1133 C ATOM 2023 N TYR A 430 50.024 0.296 18.582 1.00 34.24 N ANISOU 2023 N TYR A 430 4973 3120 4916 519 -1127 -773 N ATOM 2024 CA TYR A 430 48.696 -0.307 18.679 1.00 37.78 C ANISOU 2024 CA TYR A 430 5468 3626 5260 511 -1024 -684 C ATOM 2025 C TYR A 430 48.717 -1.807 18.427 1.00 34.96 C ANISOU 2025 C TYR A 430 5176 3338 4769 462 -946 -672 C ATOM 2026 O TYR A 430 47.959 -2.557 19.037 1.00 36.84 O ANISOU 2026 O TYR A 430 5490 3596 4913 529 -873 -650 O ATOM 2027 CB TYR A 430 47.717 0.416 17.757 1.00 35.50 C ANISOU 2027 CB TYR A 430 5078 3363 5049 387 -1003 -552 C ATOM 2028 CG TYR A 430 47.570 1.825 18.226 1.00 35.83 C ANISOU 2028 CG TYR A 430 5069 3344 5200 456 -1093 -572 C ATOM 2029 CD1 TYR A 430 46.901 2.108 19.422 1.00 36.53 C ANISOU 2029 CD1 TYR A 430 5228 3402 5249 620 -1102 -600 C ATOM 2030 CD2 TYR A 430 48.167 2.870 17.540 1.00 34.35 C ANISOU 2030 CD2 TYR A 430 4762 3131 5160 380 -1182 -565 C ATOM 2031 CE1 TYR A 430 46.787 3.419 19.896 1.00 36.93 C ANISOU 2031 CE1 TYR A 430 5234 3403 5395 705 -1216 -627 C ATOM 2032 CE2 TYR A 430 48.058 4.177 18.006 1.00 38.06 C ANISOU 2032 CE2 TYR A 430 5175 3545 5742 450 -1295 -589 C ATOM 2033 CZ TYR A 430 47.366 4.443 19.186 1.00 38.62 C ANISOU 2033 CZ TYR A 430 5321 3591 5762 615 -1322 -625 C ATOM 2034 OH TYR A 430 47.270 5.737 19.651 1.00 51.15 O ANISOU 2034 OH TYR A 430 6852 5129 7454 701 -1462 -653 O ATOM 2035 N ARG A 431 49.622 -2.241 17.561 1.00 27.71 N ANISOU 2035 N ARG A 431 4224 2458 3847 359 -969 -685 N ATOM 2036 CA ARG A 431 49.797 -3.664 17.298 1.00 30.86 C ANISOU 2036 CA ARG A 431 4680 2931 4114 318 -931 -689 C ATOM 2037 C ARG A 431 50.274 -4.418 18.533 1.00 33.66 C ANISOU 2037 C ARG A 431 5164 3262 4362 448 -931 -826 C ATOM 2038 O ARG A 431 49.774 -5.494 18.837 1.00 35.51 O ANISOU 2038 O ARG A 431 5464 3542 4485 469 -876 -809 O ATOM 2039 CB ARG A 431 50.793 -3.860 16.167 1.00 28.81 C ANISOU 2039 CB ARG A 431 4361 2718 3866 206 -973 -684 C ATOM 2040 CG ARG A 431 51.738 -5.011 16.387 1.00 27.68 C ANISOU 2040 CG ARG A 431 4300 2616 3601 216 -996 -789 C ATOM 2041 CD ARG A 431 52.400 -5.331 15.100 1.00 31.93 C ANISOU 2041 CD ARG A 431 4775 3230 4128 105 -1023 -738 C ATOM 2042 NE ARG A 431 53.611 -4.560 14.908 1.00 32.07 N ANISOU 2042 NE ARG A 431 4739 3196 4248 96 -1074 -792 N ATOM 2043 CZ ARG A 431 54.032 -4.095 13.737 1.00 28.27 C ANISOU 2043 CZ ARG A 431 4153 2745 3843 16 -1082 -699 C ATOM 2044 NH1 ARG A 431 53.316 -4.278 12.634 1.00 27.61 N ANISOU 2044 NH1 ARG A 431 4020 2739 3733 -51 -1048 -560 N ATOM 2045 NH2 ARG A 431 55.169 -3.429 13.678 1.00 28.10 N ANISOU 2045 NH2 ARG A 431 4077 2663 3937 19 -1124 -744 N ATOM 2046 N GLU A 432 51.256 -3.851 19.226 1.00 33.75 N ANISOU 2046 N GLU A 432 5211 3190 4422 542 -1000 -962 N ATOM 2047 CA GLU A 432 51.741 -4.389 20.493 1.00 33.14 C ANISOU 2047 CA GLU A 432 5275 3060 4257 698 -1009 -1117 C ATOM 2048 C GLU A 432 50.640 -4.446 21.547 1.00 33.12 C ANISOU 2048 C GLU A 432 5347 3040 4196 849 -940 -1088 C ATOM 2049 O GLU A 432 50.498 -5.437 22.241 1.00 37.25 O ANISOU 2049 O GLU A 432 5977 3583 4593 928 -885 -1131 O ATOM 2050 CB GLU A 432 52.917 -3.551 20.986 1.00 36.92 C ANISOU 2050 CB GLU A 432 5765 3416 4846 791 -1118 -1264 C ATOM 2051 CG GLU A 432 54.049 -3.510 19.948 1.00 49.13 C ANISOU 2051 CG GLU A 432 7228 4975 6465 648 -1173 -1276 C ATOM 2052 CD GLU A 432 55.367 -2.969 20.495 1.00 57.03 C ANISOU 2052 CD GLU A 432 8252 5834 7583 744 -1284 -1440 C ATOM 2053 OE1 GLU A 432 56.377 -3.008 19.752 1.00 53.53 O ANISOU 2053 OE1 GLU A 432 7748 5389 7203 642 -1323 -1455 O ATOM 2054 OE2 GLU A 432 55.393 -2.507 21.659 1.00 60.91 O ANISOU 2054 OE2 GLU A 432 8824 6208 8113 934 -1337 -1551 O ATOM 2055 N CYS A 433 49.845 -3.388 21.650 1.00 25.72 N ANISOU 2055 N CYS A 433 4352 2071 3348 890 -940 -1006 N ATOM 2056 CA CYS A 433 48.717 -3.379 22.581 1.00 29.19 C ANISOU 2056 CA CYS A 433 4853 2503 3736 1037 -866 -951 C ATOM 2057 C CYS A 433 47.728 -4.544 22.340 1.00 41.12 C ANISOU 2057 C CYS A 433 6371 4098 5155 971 -743 -826 C ATOM 2058 O CYS A 433 47.357 -5.269 23.273 1.00 41.10 O ANISOU 2058 O CYS A 433 6466 4096 5055 1106 -669 -835 O ATOM 2059 CB CYS A 433 48.000 -2.023 22.505 1.00 24.20 C ANISOU 2059 CB CYS A 433 4138 1841 3217 1055 -902 -872 C ATOM 2060 SG CYS A 433 46.538 -1.832 23.550 1.00 67.55 S ANISOU 2060 SG CYS A 433 9685 7328 8651 1235 -814 -781 S ATOM 2061 N ILE A 434 47.295 -4.708 21.091 1.00 37.36 N ANISOU 2061 N ILE A 434 5789 3681 4725 779 -728 -705 N ATOM 2062 CA ILE A 434 46.399 -5.799 20.718 1.00 32.66 C ANISOU 2062 CA ILE A 434 5181 3145 4084 713 -645 -583 C ATOM 2063 C ILE A 434 47.002 -7.166 21.037 1.00 33.26 C ANISOU 2063 C ILE A 434 5337 3263 4036 733 -638 -659 C ATOM 2064 O ILE A 434 46.349 -8.054 21.582 1.00 34.65 O ANISOU 2064 O ILE A 434 5555 3457 4154 798 -562 -605 O ATOM 2065 CB ILE A 434 46.094 -5.744 19.218 1.00 31.28 C ANISOU 2065 CB ILE A 434 4892 3009 3985 522 -668 -475 C ATOM 2066 CG1 ILE A 434 45.128 -4.591 18.937 1.00 35.07 C ANISOU 2066 CG1 ILE A 434 5300 3449 4578 496 -652 -378 C ATOM 2067 CG2 ILE A 434 45.504 -7.062 18.752 1.00 24.11 C ANISOU 2067 CG2 ILE A 434 3973 2152 3037 463 -632 -383 C ATOM 2068 CD1 ILE A 434 45.096 -4.147 17.497 1.00 35.85 C ANISOU 2068 CD1 ILE A 434 5297 3562 4762 332 -694 -314 C ATOM 2069 N ILE A 435 48.267 -7.328 20.696 1.00 28.86 N ANISOU 2069 N ILE A 435 4797 2722 3447 677 -720 -781 N ATOM 2070 CA ILE A 435 48.939 -8.575 20.953 1.00 33.78 C ANISOU 2070 CA ILE A 435 5499 3390 3944 681 -734 -876 C ATOM 2071 C ILE A 435 48.926 -8.907 22.444 1.00 42.41 C ANISOU 2071 C ILE A 435 6727 4436 4951 877 -680 -970 C ATOM 2072 O ILE A 435 48.451 -9.978 22.839 1.00 41.26 O ANISOU 2072 O ILE A 435 6623 4330 4724 912 -619 -933 O ATOM 2073 CB ILE A 435 50.364 -8.511 20.450 1.00 32.72 C ANISOU 2073 CB ILE A 435 5370 3265 3799 605 -832 -1006 C ATOM 2074 CG1 ILE A 435 50.362 -8.554 18.925 1.00 28.81 C ANISOU 2074 CG1 ILE A 435 4756 2843 3347 429 -872 -897 C ATOM 2075 CG2 ILE A 435 51.178 -9.650 21.036 1.00 43.39 C ANISOU 2075 CG2 ILE A 435 6837 4640 5008 643 -856 -1155 C ATOM 2076 CD1 ILE A 435 51.750 -8.543 18.295 1.00 30.96 C ANISOU 2076 CD1 ILE A 435 5017 3137 3608 352 -958 -994 C ATOM 2077 N GLU A 436 49.423 -7.971 23.255 1.00 50.32 N ANISOU 2077 N GLU A 436 7791 5345 5983 1019 -709 -1085 N ATOM 2078 CA GLU A 436 49.532 -8.125 24.716 1.00 52.66 C ANISOU 2078 CA GLU A 436 8236 5575 6199 1251 -673 -1198 C ATOM 2079 C GLU A 436 48.208 -8.368 25.437 1.00 51.43 C ANISOU 2079 C GLU A 436 8101 5429 6009 1382 -545 -1060 C ATOM 2080 O GLU A 436 48.119 -9.234 26.301 1.00 59.18 O ANISOU 2080 O GLU A 436 9187 6414 6884 1508 -476 -1096 O ATOM 2081 CB GLU A 436 50.178 -6.887 25.347 1.00 56.70 C ANISOU 2081 CB GLU A 436 8793 5968 6785 1402 -757 -1327 C ATOM 2082 CG GLU A 436 51.638 -6.640 24.983 1.00 68.38 C ANISOU 2082 CG GLU A 436 10276 7392 8314 1337 -883 -1492 C ATOM 2083 CD GLU A 436 52.171 -5.311 25.545 1.00 81.22 C ANISOU 2083 CD GLU A 436 11915 8879 10067 1493 -990 -1595 C ATOM 2084 OE1 GLU A 436 51.360 -4.493 26.044 1.00 88.65 O ANISOU 2084 OE1 GLU A 436 12844 9789 11052 1627 -979 -1523 O ATOM 2085 OE2 GLU A 436 53.400 -5.081 25.479 1.00 80.04 O ANISOU 2085 OE2 GLU A 436 11737 8705 9971 1467 -1109 -1683 O ATOM 2086 N LYS A 437 47.188 -7.590 25.104 1.00 44.12 N ANISOU 2086 N LYS A 437 7079 4505 5180 1357 -509 -903 N ATOM 2087 CA LYS A 437 45.986 -7.562 25.927 1.00 47.38 C ANISOU 2087 CA LYS A 437 7518 4907 5579 1517 -391 -778 C ATOM 2088 C LYS A 437 44.829 -8.304 25.290 1.00 53.39 C ANISOU 2088 C LYS A 437 8180 5728 6378 1391 -299 -575 C ATOM 2089 O LYS A 437 43.790 -8.532 25.914 1.00 53.03 O ANISOU 2089 O LYS A 437 8142 5676 6331 1508 -182 -446 O ATOM 2090 CB LYS A 437 45.582 -6.119 26.228 1.00 50.60 C ANISOU 2090 CB LYS A 437 7903 5259 6064 1622 -422 -754 C ATOM 2091 CG LYS A 437 46.729 -5.234 26.699 1.00 49.04 C ANISOU 2091 CG LYS A 437 7772 4980 5881 1740 -555 -947 C ATOM 2092 CD LYS A 437 46.330 -3.763 26.645 1.00 56.74 C ANISOU 2092 CD LYS A 437 8678 5917 6964 1780 -627 -905 C ATOM 2093 CE LYS A 437 47.551 -2.849 26.583 1.00 62.37 C ANISOU 2093 CE LYS A 437 9385 6549 7762 1801 -798 -1068 C ATOM 2094 NZ LYS A 437 47.156 -1.414 26.456 1.00 62.36 N ANISOU 2094 NZ LYS A 437 9296 6519 7878 1824 -891 -1022 N ATOM 2095 N CYS A 438 45.000 -8.697 24.040 1.00 49.63 N ANISOU 2095 N CYS A 438 7608 5301 5947 1168 -356 -540 N ATOM 2096 CA CYS A 438 43.949 -9.445 23.394 1.00 39.49 C ANISOU 2096 CA CYS A 438 6231 4051 4723 1063 -299 -360 C ATOM 2097 C CYS A 438 44.410 -10.840 22.974 1.00 34.40 C ANISOU 2097 C CYS A 438 5584 3470 4014 972 -338 -385 C ATOM 2098 O CYS A 438 43.720 -11.829 23.245 1.00 36.56 O ANISOU 2098 O CYS A 438 5844 3758 4287 1006 -273 -281 O ATOM 2099 CB CYS A 438 43.414 -8.679 22.186 1.00 44.83 C ANISOU 2099 CB CYS A 438 6785 4719 5530 902 -340 -261 C ATOM 2100 SG CYS A 438 42.115 -9.576 21.330 1.00 62.63 S ANISOU 2100 SG CYS A 438 8928 6977 7892 792 -299 -53 S ATOM 2101 N LEU A 439 45.563 -10.921 22.311 1.00 27.17 N ANISOU 2101 N LEU A 439 4676 2594 3053 860 -452 -513 N ATOM 2102 CA LEU A 439 45.984 -12.187 21.723 1.00 31.73 C ANISOU 2102 CA LEU A 439 5238 3248 3569 756 -519 -531 C ATOM 2103 C LEU A 439 46.717 -13.091 22.714 1.00 36.05 C ANISOU 2103 C LEU A 439 5910 3817 3971 852 -514 -673 C ATOM 2104 O LEU A 439 46.519 -14.305 22.718 1.00 44.38 O ANISOU 2104 O LEU A 439 6958 4926 4981 832 -520 -635 O ATOM 2105 CB LEU A 439 46.836 -11.948 20.471 1.00 29.04 C ANISOU 2105 CB LEU A 439 4844 2951 3237 596 -641 -584 C ATOM 2106 CG LEU A 439 46.154 -11.089 19.398 1.00 33.25 C ANISOU 2106 CG LEU A 439 5263 3462 3907 501 -650 -453 C ATOM 2107 CD1 LEU A 439 47.012 -11.007 18.163 1.00 27.02 C ANISOU 2107 CD1 LEU A 439 4427 2726 3112 370 -758 -491 C ATOM 2108 CD2 LEU A 439 44.772 -11.636 19.048 1.00 34.62 C ANISOU 2108 CD2 LEU A 439 5359 3621 4173 485 -608 -268 C ATOM 2109 N MET A 440 47.555 -12.495 23.555 1.00 39.70 N ANISOU 2109 N MET A 440 6485 4227 4370 966 -514 -842 N ATOM 2110 CA MET A 440 48.437 -13.264 24.424 1.00 35.33 C ANISOU 2110 CA MET A 440 6070 3678 3676 1053 -527 -1020 C ATOM 2111 C MET A 440 47.600 -14.076 25.411 1.00 31.71 C ANISOU 2111 C MET A 440 5658 3219 3170 1197 -408 -940 C ATOM 2112 O MET A 440 46.606 -13.589 25.958 1.00 33.00 O ANISOU 2112 O MET A 440 5806 3335 3396 1324 -296 -810 O ATOM 2113 CB MET A 440 49.423 -12.334 25.150 1.00 41.98 C ANISOU 2113 CB MET A 440 7026 4427 4497 1177 -561 -1217 C ATOM 2114 CG MET A 440 50.746 -12.986 25.581 1.00 43.79 C ANISOU 2114 CG MET A 440 7344 4675 4618 1185 -644 -1386 C ATOM 2115 SD MET A 440 51.763 -13.695 24.238 1.00 46.10 S ANISOU 2115 SD MET A 440 7519 5087 4909 935 -780 -1370 S ATOM 2116 CE MET A 440 52.277 -12.198 23.410 1.00 47.76 C ANISOU 2116 CE MET A 440 7669 5232 5246 864 -842 -1411 C ATOM 2117 N ARG A 441 47.999 -15.323 25.610 1.00 22.87 N ANISOU 2117 N ARG A 441 4589 2156 1942 1177 -434 -1010 N ATOM 2118 CA ARG A 441 47.263 -16.266 26.456 1.00 32.60 C ANISOU 2118 CA ARG A 441 5850 3401 3137 1298 -327 -923 C ATOM 2119 C ARG A 441 45.996 -16.804 25.799 1.00 38.72 C ANISOU 2119 C ARG A 441 6460 4213 4038 1214 -293 -666 C ATOM 2120 O ARG A 441 45.339 -17.665 26.359 1.00 39.79 O ANISOU 2120 O ARG A 441 6585 4358 4177 1294 -213 -562 O ATOM 2121 CB ARG A 441 46.940 -15.659 27.828 1.00 33.77 C ANISOU 2121 CB ARG A 441 6115 3459 3258 1563 -188 -939 C ATOM 2122 CG ARG A 441 48.185 -15.360 28.653 1.00 42.23 C ANISOU 2122 CG ARG A 441 7371 4467 4206 1693 -233 -1211 C ATOM 2123 CD ARG A 441 47.876 -14.618 29.940 1.00 49.13 C ANISOU 2123 CD ARG A 441 8347 5260 5060 1972 -137 -1196 C ATOM 2124 NE ARG A 441 47.272 -13.321 29.662 1.00 58.11 N ANISOU 2124 NE ARG A 441 9420 6339 6322 2008 -114 -1114 N ATOM 2125 CZ ARG A 441 47.964 -12.248 29.299 1.00 60.82 C ANISOU 2125 CZ ARG A 441 9761 6629 6718 1970 -226 -1227 C ATOM 2126 NH1 ARG A 441 49.290 -12.334 29.177 1.00 51.27 N ANISOU 2126 NH1 ARG A 441 8568 5452 5460 1869 -381 -1352 N ATOM 2127 NH2 ARG A 441 47.332 -11.095 29.058 1.00 60.78 N ANISOU 2127 NH2 ARG A 441 9672 6596 6824 1984 -221 -1113 N ATOM 2128 N ASN A 442 45.653 -16.311 24.611 1.00 36.63 N ANISOU 2128 N ASN A 442 5393 4614 3912 478 -526 -164 N ATOM 2129 CA ASN A 442 44.477 -16.833 23.923 1.00 31.60 C ANISOU 2129 CA ASN A 442 4707 3900 3399 413 -447 -75 C ATOM 2130 C ASN A 442 44.806 -17.479 22.596 1.00 30.28 C ANISOU 2130 C ASN A 442 4492 3672 3341 360 -518 -47 C ATOM 2131 O ASN A 442 43.913 -17.702 21.780 1.00 28.89 O ANISOU 2131 O ASN A 442 4259 3419 3297 314 -489 -8 O ATOM 2132 CB ASN A 442 43.460 -15.719 23.700 1.00 30.38 C ANISOU 2132 CB ASN A 442 4484 3716 3343 369 -394 -126 C ATOM 2133 CG ASN A 442 42.920 -15.178 24.995 1.00 39.11 C ANISOU 2133 CG ASN A 442 5627 4877 4355 416 -303 -148 C ATOM 2134 OD1 ASN A 442 43.153 -14.021 25.345 1.00 40.89 O ANISOU 2134 OD1 ASN A 442 5828 5156 4553 433 -336 -251 O ATOM 2135 ND2 ASN A 442 42.232 -16.029 25.743 1.00 39.88 N ANISOU 2135 ND2 ASN A 442 5783 4963 4406 446 -185 -52 N ATOM 2136 N LEU A 443 46.085 -17.767 22.383 1.00 26.84 N ANISOU 2136 N LEU A 443 4077 3261 2859 374 -618 -79 N ATOM 2137 CA LEU A 443 46.560 -18.141 21.060 1.00 26.73 C ANISOU 2137 CA LEU A 443 4016 3199 2940 325 -691 -79 C ATOM 2138 C LEU A 443 46.011 -19.485 20.602 1.00 31.50 C ANISOU 2138 C LEU A 443 4600 3754 3613 308 -676 24 C ATOM 2139 O LEU A 443 45.594 -19.625 19.458 1.00 39.02 O ANISOU 2139 O LEU A 443 5495 4646 4683 272 -696 35 O ATOM 2140 CB LEU A 443 48.079 -18.151 21.015 1.00 26.94 C ANISOU 2140 CB LEU A 443 4064 3251 2919 341 -789 -148 C ATOM 2141 CG LEU A 443 48.805 -16.822 21.219 1.00 28.23 C ANISOU 2141 CG LEU A 443 4217 3436 3073 363 -824 -267 C ATOM 2142 CD1 LEU A 443 50.275 -16.983 20.918 1.00 26.35 C ANISOU 2142 CD1 LEU A 443 3982 3183 2849 370 -917 -337 C ATOM 2143 CD2 LEU A 443 48.226 -15.757 20.321 1.00 27.75 C ANISOU 2143 CD2 LEU A 443 4089 3340 3116 316 -796 -294 C ATOM 2144 N LEU A 444 46.002 -20.475 21.485 1.00 26.16 N ANISOU 2144 N LEU A 444 3969 3100 2872 345 -645 98 N ATOM 2145 CA LEU A 444 45.507 -21.797 21.100 1.00 29.78 C ANISOU 2145 CA LEU A 444 4386 3507 3424 335 -632 197 C ATOM 2146 C LEU A 444 44.048 -21.689 20.696 1.00 33.02 C ANISOU 2146 C LEU A 444 4732 3837 3977 319 -547 233 C ATOM 2147 O LEU A 444 43.616 -22.248 19.698 1.00 37.20 O ANISOU 2147 O LEU A 444 5188 4296 4651 302 -579 253 O ATOM 2148 CB LEU A 444 45.641 -22.790 22.250 1.00 26.56 C ANISOU 2148 CB LEU A 444 4040 3128 2923 383 -592 283 C ATOM 2149 CG LEU A 444 45.036 -24.181 22.016 1.00 29.91 C ANISOU 2149 CG LEU A 444 4404 3492 3469 382 -561 398 C ATOM 2150 CD1 LEU A 444 45.615 -24.873 20.763 1.00 22.96 C ANISOU 2150 CD1 LEU A 444 3440 2585 2698 343 -686 379 C ATOM 2151 CD2 LEU A 444 45.235 -25.056 23.252 1.00 22.56 C ANISOU 2151 CD2 LEU A 444 3552 2592 2427 434 -512 492 C ATOM 2152 N SER A 445 43.306 -20.938 21.489 1.00 28.62 N ANISOU 2152 N SER A 445 4202 3285 3388 332 -446 225 N ATOM 2153 CA SER A 445 41.886 -20.783 21.315 1.00 29.32 C ANISOU 2153 CA SER A 445 4234 3282 3623 317 -353 245 C ATOM 2154 C SER A 445 41.558 -19.993 20.045 1.00 26.46 C ANISOU 2154 C SER A 445 3811 2860 3383 273 -423 166 C ATOM 2155 O SER A 445 40.687 -20.387 19.269 1.00 23.10 O ANISOU 2155 O SER A 445 3318 2329 3130 266 -426 179 O ATOM 2156 CB SER A 445 41.309 -20.094 22.558 1.00 31.10 C ANISOU 2156 CB SER A 445 4511 3539 3766 338 -228 241 C ATOM 2157 OG SER A 445 40.103 -19.446 22.255 1.00 43.47 O ANISOU 2157 OG SER A 445 6017 5019 5479 304 -166 206 O ATOM 2158 N LEU A 446 42.244 -18.872 19.849 1.00 22.77 N ANISOU 2158 N LEU A 446 3366 2450 2835 254 -482 80 N ATOM 2159 CA LEU A 446 42.033 -18.033 18.665 1.00 19.05 C ANISOU 2159 CA LEU A 446 2855 1926 2457 218 -546 12 C ATOM 2160 C LEU A 446 42.498 -18.713 17.366 1.00 23.78 C ANISOU 2160 C LEU A 446 3434 2489 3113 218 -644 23 C ATOM 2161 O LEU A 446 41.906 -18.525 16.304 1.00 23.90 O ANISOU 2161 O LEU A 446 3418 2422 3240 210 -687 -1 O ATOM 2162 CB LEU A 446 42.729 -16.690 18.841 1.00 20.38 C ANISOU 2162 CB LEU A 446 3043 2162 2539 205 -573 -72 C ATOM 2163 CG LEU A 446 42.154 -15.811 19.952 1.00 23.61 C ANISOU 2163 CG LEU A 446 3454 2604 2912 207 -493 -108 C ATOM 2164 CD1 LEU A 446 42.973 -14.559 20.124 1.00 25.62 C ANISOU 2164 CD1 LEU A 446 3705 2928 3102 207 -538 -198 C ATOM 2165 CD2 LEU A 446 40.726 -15.464 19.613 1.00 24.31 C ANISOU 2165 CD2 LEU A 446 3491 2593 3153 172 -446 -119 C ATOM 2166 N SER A 447 43.561 -19.506 17.459 1.00 19.47 N ANISOU 2166 N SER A 447 2910 2001 2488 231 -688 50 N ATOM 2167 CA SER A 447 44.068 -20.234 16.306 1.00 17.86 C ANISOU 2167 CA SER A 447 2683 1773 2331 232 -778 56 C ATOM 2168 C SER A 447 43.040 -21.226 15.784 1.00 24.25 C ANISOU 2168 C SER A 447 3429 2493 3294 255 -784 105 C ATOM 2169 O SER A 447 43.171 -21.704 14.675 1.00 27.34 O ANISOU 2169 O SER A 447 3790 2848 3749 268 -865 95 O ATOM 2170 CB SER A 447 45.355 -20.981 16.677 1.00 22.79 C ANISOU 2170 CB SER A 447 3332 2468 2860 235 -821 70 C ATOM 2171 OG SER A 447 46.383 -20.058 17.013 1.00 21.92 O ANISOU 2171 OG SER A 447 3268 2415 2645 225 -834 3 O ATOM 2172 N GLN A 448 42.023 -21.536 16.586 1.00 27.01 N ANISOU 2172 N GLN A 448 3753 2798 3713 269 -694 152 N ATOM 2173 CA GLN A 448 40.987 -22.465 16.162 1.00 28.59 C ANISOU 2173 CA GLN A 448 3871 2886 4105 301 -691 190 C ATOM 2174 C GLN A 448 39.724 -21.760 15.662 1.00 23.70 C ANISOU 2174 C GLN A 448 3220 2149 3636 303 -677 136 C ATOM 2175 O GLN A 448 38.749 -22.406 15.309 1.00 29.73 O ANISOU 2175 O GLN A 448 3909 2792 4597 339 -678 144 O ATOM 2176 CB GLN A 448 40.641 -23.445 17.286 1.00 29.36 C ANISOU 2176 CB GLN A 448 3946 2978 4232 322 -590 285 C ATOM 2177 CG GLN A 448 41.807 -24.336 17.694 1.00 33.16 C ANISOU 2177 CG GLN A 448 4451 3553 4595 325 -628 339 C ATOM 2178 CD GLN A 448 41.485 -25.212 18.889 1.00 34.38 C ANISOU 2178 CD GLN A 448 4605 3704 4753 352 -517 445 C ATOM 2179 OE1 GLN A 448 40.732 -26.195 18.790 1.00 37.79 O ANISOU 2179 OE1 GLN A 448 4947 4046 5366 382 -483 509 O ATOM 2180 NE2 GLN A 448 42.069 -24.872 20.025 1.00 27.37 N ANISOU 2180 NE2 GLN A 448 3820 2909 3672 353 -463 464 N ATOM 2181 N GLU A 449 39.744 -20.437 15.641 1.00 26.44 N ANISOU 2181 N GLU A 449 3616 2519 3912 268 -673 72 N ATOM 2182 CA GLU A 449 38.612 -19.651 15.134 1.00 26.71 C ANISOU 2182 CA GLU A 449 3627 2437 4085 262 -679 6 C ATOM 2183 C GLU A 449 38.753 -19.415 13.653 1.00 25.15 C ANISOU 2183 C GLU A 449 3442 2192 3922 284 -812 -48 C ATOM 2184 O GLU A 449 39.845 -19.131 13.170 1.00 29.56 O ANISOU 2184 O GLU A 449 4051 2836 4342 275 -866 -55 O ATOM 2185 CB GLU A 449 38.605 -18.290 15.789 1.00 30.36 C ANISOU 2185 CB GLU A 449 4128 2950 4457 213 -623 -40 C ATOM 2186 CG GLU A 449 38.477 -18.347 17.279 1.00 40.34 C ANISOU 2186 CG GLU A 449 5401 4271 5654 204 -492 2 C ATOM 2187 CD GLU A 449 37.051 -18.407 17.678 1.00 49.90 C ANISOU 2187 CD GLU A 449 6559 5357 7043 201 -397 -2 C ATOM 2188 OE1 GLU A 449 36.400 -19.432 17.397 1.00 63.75 O ANISOU 2188 OE1 GLU A 449 8257 7001 8963 236 -386 36 O ATOM 2189 OE2 GLU A 449 36.572 -17.417 18.247 1.00 54.14 O ANISOU 2189 OE2 GLU A 449 7100 5896 7576 166 -337 -52 O ATOM 2190 N LYS A 450 37.646 -19.498 12.936 1.00 32.04 N ANISOU 2190 N LYS A 450 4273 2918 4983 319 -861 -93 N ATOM 2191 CA LYS A 450 37.663 -19.276 11.504 1.00 28.41 C ANISOU 2191 CA LYS A 450 3844 2401 4549 361 -995 -149 C ATOM 2192 C LYS A 450 38.237 -17.909 11.181 1.00 30.05 C ANISOU 2192 C LYS A 450 4133 2669 4614 318 -1012 -186 C ATOM 2193 O LYS A 450 39.088 -17.769 10.308 1.00 25.92 O ANISOU 2193 O LYS A 450 3669 2195 3985 336 -1077 -187 O ATOM 2194 CB LYS A 450 36.257 -19.396 10.946 1.00 26.24 C ANISOU 2194 CB LYS A 450 3518 1937 4515 413 -1051 -214 C ATOM 2195 CG LYS A 450 36.173 -19.328 9.427 1.00 31.87 C ANISOU 2195 CG LYS A 450 4275 2574 5260 488 -1209 -277 C ATOM 2196 CD LYS A 450 34.710 -19.361 8.982 1.00 38.28 C ANISOU 2196 CD LYS A 450 5036 3174 6333 547 -1278 -364 C ATOM 2197 CE LYS A 450 34.556 -19.098 7.493 1.00 40.92 C ANISOU 2197 CE LYS A 450 5444 3425 6680 636 -1449 -441 C ATOM 2198 NZ LYS A 450 35.480 -19.944 6.681 1.00 41.69 N ANISOU 2198 NZ LYS A 450 5566 3606 6667 708 -1528 -408 N ATOM 2199 N PHE A 451 37.783 -16.895 11.900 1.00 35.52 N ANISOU 2199 N PHE A 451 4823 3358 5314 261 -945 -215 N ATOM 2200 CA PHE A 451 38.178 -15.537 11.566 1.00 29.71 C ANISOU 2200 CA PHE A 451 4140 2658 4488 223 -966 -255 C ATOM 2201 C PHE A 451 39.453 -15.076 12.296 1.00 30.99 C ANISOU 2201 C PHE A 451 4325 2978 4473 181 -903 -226 C ATOM 2202 O PHE A 451 40.353 -14.489 11.683 1.00 28.27 O ANISOU 2202 O PHE A 451 4026 2680 4034 178 -934 -232 O ATOM 2203 CB PHE A 451 37.002 -14.585 11.769 1.00 28.26 C ANISOU 2203 CB PHE A 451 3929 2373 4435 187 -958 -324 C ATOM 2204 CG PHE A 451 35.741 -15.028 11.056 1.00 32.37 C ANISOU 2204 CG PHE A 451 4425 2710 5163 237 -1034 -375 C ATOM 2205 CD1 PHE A 451 35.690 -15.078 9.660 1.00 28.73 C ANISOU 2205 CD1 PHE A 451 4021 2171 4725 305 -1168 -407 C ATOM 2206 CD2 PHE A 451 34.612 -15.404 11.779 1.00 33.71 C ANISOU 2206 CD2 PHE A 451 4517 2774 5516 228 -971 -397 C ATOM 2207 CE1 PHE A 451 34.523 -15.491 8.995 1.00 34.88 C ANISOU 2207 CE1 PHE A 451 4776 2764 5712 372 -1262 -474 C ATOM 2208 CE2 PHE A 451 33.440 -15.817 11.124 1.00 35.10 C ANISOU 2208 CE2 PHE A 451 4656 2754 5927 284 -1048 -463 C ATOM 2209 CZ PHE A 451 33.401 -15.860 9.729 1.00 35.09 C ANISOU 2209 CZ PHE A 451 4709 2673 5953 360 -1207 -508 C ATOM 2210 N ALA A 452 39.555 -15.368 13.587 1.00 23.07 N ANISOU 2210 N ALA A 452 3291 2043 3429 161 -813 -198 N ATOM 2211 CA ALA A 452 40.678 -14.854 14.359 1.00 17.29 C ANISOU 2211 CA ALA A 452 2578 1443 2549 138 -772 -195 C ATOM 2212 C ALA A 452 41.986 -15.547 13.988 1.00 20.82 C ANISOU 2212 C ALA A 452 3059 1959 2893 160 -808 -160 C ATOM 2213 O ALA A 452 43.056 -15.023 14.240 1.00 26.19 O ANISOU 2213 O ALA A 452 3757 2717 3479 150 -802 -178 O ATOM 2214 CB ALA A 452 40.397 -14.960 15.854 1.00 21.27 C ANISOU 2214 CB ALA A 452 3061 1999 3022 128 -675 -181 C ATOM 2215 N SER A 453 41.914 -16.720 13.372 1.00 25.76 N ANISOU 2215 N SER A 453 3682 2546 3560 194 -851 -121 N ATOM 2216 CA SER A 453 43.157 -17.415 13.030 1.00 24.14 C ANISOU 2216 CA SER A 453 3499 2405 3270 207 -888 -97 C ATOM 2217 C SER A 453 43.992 -16.566 12.066 1.00 26.80 C ANISOU 2217 C SER A 453 3880 2750 3554 201 -921 -132 C ATOM 2218 O SER A 453 45.224 -16.573 12.122 1.00 32.28 O ANISOU 2218 O SER A 453 4591 3505 4170 191 -918 -138 O ATOM 2219 CB SER A 453 42.883 -18.809 12.474 1.00 16.54 C ANISOU 2219 CB SER A 453 2507 1399 2379 247 -939 -58 C ATOM 2220 OG SER A 453 42.000 -18.743 11.366 1.00 19.00 O ANISOU 2220 OG SER A 453 2816 1607 2798 284 -1001 -84 O ATOM 2221 N HIS A 454 43.316 -15.823 11.192 1.00 23.54 N ANISOU 2221 N HIS A 454 3488 2262 3196 209 -950 -158 N ATOM 2222 CA HIS A 454 43.987 -14.855 10.327 1.00 22.72 C ANISOU 2222 CA HIS A 454 3432 2154 3045 205 -958 -179 C ATOM 2223 C HIS A 454 44.686 -13.768 11.143 1.00 23.92 C ANISOU 2223 C HIS A 454 3563 2366 3157 165 -898 -208 C ATOM 2224 O HIS A 454 45.783 -13.337 10.812 1.00 25.10 O ANISOU 2224 O HIS A 454 3732 2541 3266 162 -880 -217 O ATOM 2225 CB HIS A 454 42.982 -14.253 9.339 1.00 23.97 C ANISOU 2225 CB HIS A 454 3626 2211 3272 229 -1008 -200 C ATOM 2226 CG HIS A 454 42.399 -15.272 8.414 1.00 30.02 C ANISOU 2226 CG HIS A 454 4415 2907 4087 294 -1089 -191 C ATOM 2227 ND1 HIS A 454 43.064 -15.725 7.296 1.00 29.80 N ANISOU 2227 ND1 HIS A 454 4445 2879 3997 344 -1133 -177 N ATOM 2228 CD2 HIS A 454 41.241 -15.972 8.471 1.00 32.71 C ANISOU 2228 CD2 HIS A 454 4714 3168 4547 327 -1134 -203 C ATOM 2229 CE1 HIS A 454 42.335 -16.648 6.696 1.00 29.34 C ANISOU 2229 CE1 HIS A 454 4382 2756 4011 411 -1218 -186 C ATOM 2230 NE2 HIS A 454 41.226 -16.820 7.391 1.00 34.47 N ANISOU 2230 NE2 HIS A 454 4965 3348 4784 403 -1221 -203 N ATOM 2231 N VAL A 455 44.049 -13.339 12.228 1.00 21.87 N ANISOU 2231 N VAL A 455 3259 2126 2926 140 -865 -229 N ATOM 2232 CA VAL A 455 44.612 -12.288 13.056 1.00 25.66 C ANISOU 2232 CA VAL A 455 3704 2663 3382 117 -824 -273 C ATOM 2233 C VAL A 455 45.875 -12.805 13.717 1.00 26.03 C ANISOU 2233 C VAL A 455 3752 2786 3353 132 -811 -275 C ATOM 2234 O VAL A 455 46.866 -12.088 13.805 1.00 29.34 O ANISOU 2234 O VAL A 455 4156 3228 3765 133 -801 -316 O ATOM 2235 CB VAL A 455 43.599 -11.809 14.118 1.00 23.32 C ANISOU 2235 CB VAL A 455 3361 2376 3125 96 -793 -302 C ATOM 2236 CG1 VAL A 455 44.253 -10.887 15.086 1.00 20.91 C ANISOU 2236 CG1 VAL A 455 3012 2145 2788 92 -765 -356 C ATOM 2237 CG2 VAL A 455 42.415 -11.145 13.448 1.00 18.29 C ANISOU 2237 CG2 VAL A 455 2714 1645 2590 74 -818 -322 C ATOM 2238 N VAL A 456 45.828 -14.063 14.157 1.00 22.09 N ANISOU 2238 N VAL A 456 3266 2312 2817 146 -818 -236 N ATOM 2239 CA VAL A 456 46.938 -14.711 14.856 1.00 21.83 C ANISOU 2239 CA VAL A 456 3242 2340 2713 162 -823 -240 C ATOM 2240 C VAL A 456 48.164 -14.932 13.950 1.00 19.80 C ANISOU 2240 C VAL A 456 3003 2069 2452 161 -852 -252 C ATOM 2241 O VAL A 456 49.319 -14.755 14.374 1.00 19.22 O ANISOU 2241 O VAL A 456 2924 2020 2359 168 -856 -300 O ATOM 2242 CB VAL A 456 46.500 -16.059 15.456 1.00 25.87 C ANISOU 2242 CB VAL A 456 3762 2869 3199 176 -823 -182 C ATOM 2243 CG1 VAL A 456 47.710 -16.853 15.914 1.00 20.62 C ANISOU 2243 CG1 VAL A 456 3115 2251 2468 190 -854 -185 C ATOM 2244 CG2 VAL A 456 45.497 -15.853 16.610 1.00 22.71 C ANISOU 2244 CG2 VAL A 456 3352 2487 2791 182 -765 -172 C ATOM 2245 N GLU A 457 47.915 -15.284 12.698 1.00 19.44 N ANISOU 2245 N GLU A 457 2980 1974 2434 161 -873 -219 N ATOM 2246 CA GLU A 457 48.990 -15.364 11.704 1.00 22.85 C ANISOU 2246 CA GLU A 457 3436 2384 2863 162 -880 -229 C ATOM 2247 C GLU A 457 49.684 -14.008 11.550 1.00 27.43 C ANISOU 2247 C GLU A 457 4008 2943 3471 154 -833 -276 C ATOM 2248 O GLU A 457 50.922 -13.920 11.604 1.00 25.75 O ANISOU 2248 O GLU A 457 3784 2727 3271 153 -817 -317 O ATOM 2249 CB GLU A 457 48.435 -15.784 10.354 1.00 23.62 C ANISOU 2249 CB GLU A 457 3571 2431 2972 181 -910 -191 C ATOM 2250 CG GLU A 457 48.025 -17.252 10.271 1.00 33.94 C ANISOU 2250 CG GLU A 457 4864 3745 4285 200 -968 -155 C ATOM 2251 CD GLU A 457 47.558 -17.629 8.866 1.00 39.45 C ANISOU 2251 CD GLU A 457 5598 4390 5002 242 -1016 -138 C ATOM 2252 OE1 GLU A 457 48.411 -17.615 7.954 1.00 40.36 O ANISOU 2252 OE1 GLU A 457 5753 4499 5082 252 -1013 -146 O ATOM 2253 OE2 GLU A 457 46.353 -17.920 8.673 1.00 29.56 O ANISOU 2253 OE2 GLU A 457 4334 3092 3804 274 -1057 -124 O ATOM 2254 N LYS A 458 48.873 -12.960 11.368 1.00 18.55 N ANISOU 2254 N LYS A 458 2878 1792 2380 151 -814 -276 N ATOM 2255 CA LYS A 458 49.380 -11.599 11.227 1.00 24.87 C ANISOU 2255 CA LYS A 458 3651 2566 3233 146 -768 -313 C ATOM 2256 C LYS A 458 50.229 -11.204 12.404 1.00 26.59 C ANISOU 2256 C LYS A 458 3805 2823 3475 152 -758 -383 C ATOM 2257 O LYS A 458 51.270 -10.577 12.231 1.00 28.94 O ANISOU 2257 O LYS A 458 4072 3088 3836 160 -724 -425 O ATOM 2258 CB LYS A 458 48.249 -10.575 11.090 1.00 29.63 C ANISOU 2258 CB LYS A 458 4239 3140 3877 135 -768 -310 C ATOM 2259 CG LYS A 458 47.704 -10.448 9.686 1.00 30.01 C ANISOU 2259 CG LYS A 458 4360 3118 3925 146 -778 -263 C ATOM 2260 CD LYS A 458 48.766 -10.757 8.659 1.00 37.69 C ANISOU 2260 CD LYS A 458 5391 4063 4867 168 -745 -237 C ATOM 2261 CE LYS A 458 48.408 -10.181 7.292 1.00 42.86 C ANISOU 2261 CE LYS A 458 6128 4643 5513 195 -735 -195 C ATOM 2262 NZ LYS A 458 46.968 -10.342 6.968 1.00 40.03 N ANISOU 2262 NZ LYS A 458 5809 4251 5151 211 -814 -182 N ATOM 2263 N ALA A 459 49.772 -11.548 13.603 1.00 18.71 N ANISOU 2263 N ALA A 459 2787 1885 2437 158 -785 -399 N ATOM 2264 CA ALA A 459 50.524 -11.199 14.806 1.00 20.88 C ANISOU 2264 CA ALA A 459 3015 2200 2718 186 -795 -477 C ATOM 2265 C ALA A 459 51.886 -11.904 14.830 1.00 19.44 C ANISOU 2265 C ALA A 459 2847 2004 2536 202 -816 -511 C ATOM 2266 O ALA A 459 52.876 -11.317 15.199 1.00 25.86 O ANISOU 2266 O ALA A 459 3614 2794 3417 230 -819 -594 O ATOM 2267 CB ALA A 459 49.725 -11.526 16.056 1.00 17.14 C ANISOU 2267 CB ALA A 459 2545 1794 2172 201 -811 -476 C ATOM 2268 N PHE A 460 51.930 -13.168 14.433 1.00 22.80 N ANISOU 2268 N PHE A 460 3324 2432 2907 187 -838 -458 N ATOM 2269 CA PHE A 460 53.200 -13.864 14.369 1.00 24.94 C ANISOU 2269 CA PHE A 460 3602 2680 3193 190 -865 -498 C ATOM 2270 C PHE A 460 54.148 -13.208 13.356 1.00 29.15 C ANISOU 2270 C PHE A 460 4116 3132 3828 181 -814 -532 C ATOM 2271 O PHE A 460 55.350 -13.128 13.599 1.00 25.88 O ANISOU 2271 O PHE A 460 3672 2673 3488 194 -821 -613 O ATOM 2272 CB PHE A 460 52.999 -15.332 13.993 1.00 21.23 C ANISOU 2272 CB PHE A 460 3175 2228 2665 170 -902 -432 C ATOM 2273 CG PHE A 460 52.821 -16.240 15.161 1.00 22.09 C ANISOU 2273 CG PHE A 460 3298 2393 2703 187 -953 -422 C ATOM 2274 CD1 PHE A 460 51.581 -16.807 15.438 1.00 31.45 C ANISOU 2274 CD1 PHE A 460 4498 3617 3835 187 -949 -341 C ATOM 2275 CD2 PHE A 460 53.887 -16.554 15.977 1.00 23.50 C ANISOU 2275 CD2 PHE A 460 3479 2572 2877 208 -1005 -493 C ATOM 2276 CE1 PHE A 460 51.410 -17.662 16.530 1.00 26.59 C ANISOU 2276 CE1 PHE A 460 3903 3046 3152 208 -975 -315 C ATOM 2277 CE2 PHE A 460 53.724 -17.411 17.062 1.00 30.53 C ANISOU 2277 CE2 PHE A 460 4402 3512 3685 233 -1052 -473 C ATOM 2278 CZ PHE A 460 52.484 -17.965 17.331 1.00 27.44 C ANISOU 2278 CZ PHE A 460 4030 3165 3230 233 -1027 -375 C ATOM 2279 N LEU A 461 53.595 -12.780 12.218 1.00 29.44 N ANISOU 2279 N LEU A 461 4175 3139 3872 164 -763 -470 N ATOM 2280 CA LEU A 461 54.368 -12.211 11.120 1.00 26.10 C ANISOU 2280 CA LEU A 461 3755 2635 3526 160 -689 -475 C ATOM 2281 C LEU A 461 54.927 -10.853 11.444 1.00 29.00 C ANISOU 2281 C LEU A 461 4048 2953 4018 180 -639 -540 C ATOM 2282 O LEU A 461 55.970 -10.487 10.914 1.00 30.34 O ANISOU 2282 O LEU A 461 4195 3040 4293 184 -573 -574 O ATOM 2283 CB LEU A 461 53.531 -12.099 9.839 1.00 26.29 C ANISOU 2283 CB LEU A 461 3846 2641 3503 156 -656 -386 C ATOM 2284 CG LEU A 461 53.271 -13.414 9.099 1.00 33.88 C ANISOU 2284 CG LEU A 461 4872 3620 4381 154 -697 -334 C ATOM 2285 CD1 LEU A 461 52.097 -13.302 8.108 1.00 31.87 C ANISOU 2285 CD1 LEU A 461 4684 3353 4072 174 -705 -263 C ATOM 2286 CD2 LEU A 461 54.552 -13.899 8.417 1.00 19.34 C ANISOU 2286 CD2 LEU A 461 3045 1733 2569 146 -657 -358 C ATOM 2287 N HIS A 462 54.241 -10.108 12.307 1.00 25.99 N ANISOU 2287 N HIS A 462 3617 2615 3642 194 -666 -563 N ATOM 2288 CA HIS A 462 54.608 -8.721 12.568 1.00 24.50 C ANISOU 2288 CA HIS A 462 3336 2383 3590 218 -628 -626 C ATOM 2289 C HIS A 462 54.994 -8.391 14.014 1.00 31.88 C ANISOU 2289 C HIS A 462 4190 3350 4574 265 -691 -739 C ATOM 2290 O HIS A 462 55.412 -7.282 14.286 1.00 31.83 O ANISOU 2290 O HIS A 462 4084 3301 4709 298 -675 -811 O ATOM 2291 CB HIS A 462 53.507 -7.773 12.089 1.00 19.41 C ANISOU 2291 CB HIS A 462 2685 1741 2948 200 -600 -568 C ATOM 2292 CG HIS A 462 53.212 -7.889 10.622 1.00 31.74 C ANISOU 2292 CG HIS A 462 4335 3254 4471 179 -545 -471 C ATOM 2293 ND1 HIS A 462 53.993 -7.296 9.650 1.00 32.51 N ANISOU 2293 ND1 HIS A 462 4436 3260 4657 188 -449 -451 N ATOM 2294 CD2 HIS A 462 52.218 -8.532 9.963 1.00 27.40 C ANISOU 2294 CD2 HIS A 462 3879 2726 3805 164 -573 -392 C ATOM 2295 CE1 HIS A 462 53.502 -7.581 8.457 1.00 21.13 C ANISOU 2295 CE1 HIS A 462 3104 1798 3129 182 -422 -360 C ATOM 2296 NE2 HIS A 462 52.418 -8.317 8.621 1.00 29.76 N ANISOU 2296 NE2 HIS A 462 4248 2955 4103 172 -507 -331 N ATOM 2297 N ALA A 463 54.852 -9.330 14.941 1.00 29.56 N ANISOU 2297 N ALA A 463 3936 3126 4170 279 -766 -756 N ATOM 2298 CA ALA A 463 55.275 -9.078 16.315 1.00 29.25 C ANISOU 2298 CA ALA A 463 3846 3116 4153 344 -836 -868 C ATOM 2299 C ALA A 463 56.757 -8.680 16.369 1.00 32.77 C ANISOU 2299 C ALA A 463 4219 3459 4775 391 -842 -987 C ATOM 2300 O ALA A 463 57.591 -9.288 15.689 1.00 31.58 O ANISOU 2300 O ALA A 463 4095 3234 4669 366 -817 -986 O ATOM 2301 CB ALA A 463 55.039 -10.328 17.192 1.00 22.60 C ANISOU 2301 CB ALA A 463 3086 2349 3150 358 -907 -852 C ATOM 2302 N PRO A 464 57.087 -7.659 17.182 1.00 26.19 N ANISOU 2302 N PRO A 464 3282 2609 4058 462 -878 -1103 N ATOM 2303 CA PRO A 464 58.479 -7.366 17.577 1.00 31.66 C ANISOU 2303 CA PRO A 464 3895 3195 4937 535 -918 -1253 C ATOM 2304 C PRO A 464 59.030 -8.589 18.286 1.00 35.86 C ANISOU 2304 C PRO A 464 4513 3740 5371 563 -1015 -1303 C ATOM 2305 O PRO A 464 58.268 -9.276 18.970 1.00 37.36 O ANISOU 2305 O PRO A 464 4792 4044 5361 566 -1068 -1252 O ATOM 2306 CB PRO A 464 58.337 -6.214 18.595 1.00 25.04 C ANISOU 2306 CB PRO A 464 2944 2385 4186 624 -976 -1364 C ATOM 2307 CG PRO A 464 56.933 -6.292 19.065 1.00 26.25 C ANISOU 2307 CG PRO A 464 3155 2683 4137 600 -989 -1281 C ATOM 2308 CD PRO A 464 56.143 -6.736 17.822 1.00 22.93 C ANISOU 2308 CD PRO A 464 2811 2273 3626 486 -894 -1114 C ATOM 2309 N LEU A 465 60.319 -8.857 18.129 1.00 32.87 N ANISOU 2309 N LEU A 465 4109 3238 5142 584 -1035 -1401 N ATOM 2310 CA LEU A 465 60.904 -10.119 18.580 1.00 45.86 C ANISOU 2310 CA LEU A 465 5840 4875 6709 590 -1129 -1441 C ATOM 2311 C LEU A 465 60.615 -10.508 20.038 1.00 44.05 C ANISOU 2311 C LEU A 465 5676 4740 6323 676 -1262 -1493 C ATOM 2312 O LEU A 465 60.431 -11.685 20.344 1.00 46.41 O ANISOU 2312 O LEU A 465 6082 5096 6455 655 -1314 -1438 O ATOM 2313 CB LEU A 465 62.411 -10.170 18.272 1.00 51.34 C ANISOU 2313 CB LEU A 465 6476 5393 7640 607 -1140 -1575 C ATOM 2314 CG LEU A 465 62.762 -9.977 16.786 1.00 56.30 C ANISOU 2314 CG LEU A 465 7068 5924 8400 522 -986 -1509 C ATOM 2315 CD1 LEU A 465 64.122 -10.571 16.439 1.00 55.52 C ANISOU 2315 CD1 LEU A 465 6953 5668 8472 506 -994 -1613 C ATOM 2316 CD2 LEU A 465 61.692 -10.564 15.867 1.00 55.41 C ANISOU 2316 CD2 LEU A 465 7051 5922 8081 424 -907 -1316 C ATOM 2317 N GLU A 466 60.554 -9.540 20.935 1.00 40.15 N ANISOU 2317 N GLU A 466 5116 4262 5877 778 -1315 -1595 N ATOM 2318 CA GLU A 466 60.316 -9.874 22.334 1.00 49.34 C ANISOU 2318 CA GLU A 466 6357 5514 6876 879 -1435 -1649 C ATOM 2319 C GLU A 466 58.940 -10.512 22.488 1.00 48.71 C ANISOU 2319 C GLU A 466 6386 5588 6532 820 -1387 -1477 C ATOM 2320 O GLU A 466 58.776 -11.491 23.220 1.00 51.39 O ANISOU 2320 O GLU A 466 6844 5988 6693 848 -1448 -1446 O ATOM 2321 CB GLU A 466 60.441 -8.641 23.226 1.00 62.54 C ANISOU 2321 CB GLU A 466 7929 7184 8650 1010 -1501 -1797 C ATOM 2322 CG GLU A 466 60.438 -8.953 24.716 1.00 84.14 C ANISOU 2322 CG GLU A 466 10756 9989 11224 1148 -1642 -1886 C ATOM 2323 CD GLU A 466 60.709 -7.720 25.587 1.00100.45 C ANISOU 2323 CD GLU A 466 12708 12041 13417 1303 -1730 -2066 C ATOM 2324 OE1 GLU A 466 60.697 -7.849 26.835 1.00102.08 O ANISOU 2324 OE1 GLU A 466 12994 12308 13485 1440 -1850 -2152 O ATOM 2325 OE2 GLU A 466 60.931 -6.622 25.025 1.00105.62 O ANISOU 2325 OE2 GLU A 466 13195 12623 14313 1295 -1681 -2120 O ATOM 2326 N LEU A 467 57.952 -9.963 21.786 1.00 39.55 N ANISOU 2326 N LEU A 467 5185 4478 5364 743 -1275 -1367 N ATOM 2327 CA LEU A 467 56.599 -10.510 21.831 1.00 32.92 C ANISOU 2327 CA LEU A 467 4429 3755 4323 684 -1220 -1214 C ATOM 2328 C LEU A 467 56.500 -11.813 21.036 1.00 30.34 C ANISOU 2328 C LEU A 467 4183 3421 3923 591 -1187 -1091 C ATOM 2329 O LEU A 467 55.828 -12.761 21.434 1.00 38.51 O ANISOU 2329 O LEU A 467 5308 4527 4795 579 -1190 -999 O ATOM 2330 CB LEU A 467 55.609 -9.492 21.287 1.00 36.21 C ANISOU 2330 CB LEU A 467 4770 4203 4784 632 -1130 -1156 C ATOM 2331 CG LEU A 467 55.456 -8.274 22.183 1.00 44.06 C ANISOU 2331 CG LEU A 467 5677 5233 5830 720 -1167 -1267 C ATOM 2332 CD1 LEU A 467 54.521 -7.270 21.539 1.00 44.58 C ANISOU 2332 CD1 LEU A 467 5658 5316 5967 653 -1086 -1213 C ATOM 2333 CD2 LEU A 467 54.945 -8.714 23.542 1.00 41.70 C ANISOU 2333 CD2 LEU A 467 5470 5040 5335 798 -1218 -1277 C ATOM 2334 N LEU A 468 57.186 -11.857 19.906 1.00 21.99 N ANISOU 2334 N LEU A 468 3085 2271 2998 532 -1152 -1091 N ATOM 2335 CA LEU A 468 57.245 -13.070 19.131 1.00 23.82 C ANISOU 2335 CA LEU A 468 3378 2492 3182 455 -1138 -1001 C ATOM 2336 C LEU A 468 57.701 -14.235 20.018 1.00 26.01 C ANISOU 2336 C LEU A 468 3734 2787 3363 491 -1240 -1027 C ATOM 2337 O LEU A 468 57.228 -15.357 19.881 1.00 32.79 O ANISOU 2337 O LEU A 468 4655 3691 4113 446 -1240 -923 O ATOM 2338 CB LEU A 468 58.177 -12.896 17.927 1.00 20.74 C ANISOU 2338 CB LEU A 468 2936 1988 2959 407 -1091 -1031 C ATOM 2339 CG LEU A 468 58.286 -14.141 17.057 1.00 24.93 C ANISOU 2339 CG LEU A 468 3518 2509 3446 331 -1082 -951 C ATOM 2340 CD1 LEU A 468 56.913 -14.564 16.593 1.00 22.34 C ANISOU 2340 CD1 LEU A 468 3234 2268 2985 284 -1036 -801 C ATOM 2341 CD2 LEU A 468 59.208 -13.889 15.889 1.00 32.64 C ANISOU 2341 CD2 LEU A 468 4449 3372 4579 291 -1016 -985 C ATOM 2342 N ALA A 469 58.608 -13.959 20.938 1.00 22.12 N ANISOU 2342 N ALA A 469 3235 2251 2919 582 -1333 -1170 N ATOM 2343 CA ALA A 469 59.178 -15.009 21.772 1.00 24.91 C ANISOU 2343 CA ALA A 469 3673 2600 3192 627 -1448 -1212 C ATOM 2344 C ALA A 469 58.162 -15.498 22.786 1.00 29.46 C ANISOU 2344 C ALA A 469 4349 3299 3547 670 -1456 -1120 C ATOM 2345 O ALA A 469 58.042 -16.699 23.009 1.00 31.58 O ANISOU 2345 O ALA A 469 4697 3596 3707 650 -1487 -1044 O ATOM 2346 CB ALA A 469 60.421 -14.514 22.459 1.00 24.72 C ANISOU 2346 CB ALA A 469 3619 2477 3297 730 -1561 -1409 C ATOM 2347 N GLU A 470 57.413 -14.574 23.381 1.00 33.99 N ANISOU 2347 N GLU A 470 4910 3940 4064 727 -1418 -1124 N ATOM 2348 CA GLU A 470 56.288 -14.949 24.237 1.00 29.36 C ANISOU 2348 CA GLU A 470 4413 3465 3276 758 -1383 -1021 C ATOM 2349 C GLU A 470 55.242 -15.753 23.466 1.00 27.02 C ANISOU 2349 C GLU A 470 4131 3207 2929 648 -1282 -843 C ATOM 2350 O GLU A 470 54.730 -16.750 23.969 1.00 40.92 O ANISOU 2350 O GLU A 470 5975 5015 4558 653 -1272 -744 O ATOM 2351 CB GLU A 470 55.624 -13.719 24.849 1.00 38.96 C ANISOU 2351 CB GLU A 470 5591 4742 4470 822 -1347 -1064 C ATOM 2352 CG GLU A 470 56.525 -12.839 25.683 1.00 50.00 C ANISOU 2352 CG GLU A 470 6959 6110 5930 954 -1455 -1251 C ATOM 2353 CD GLU A 470 55.758 -11.662 26.303 1.00 62.55 C ANISOU 2353 CD GLU A 470 8498 7774 7493 1015 -1421 -1291 C ATOM 2354 OE1 GLU A 470 56.363 -10.585 26.519 1.00 65.83 O ANISOU 2354 OE1 GLU A 470 8814 8151 8047 1093 -1484 -1444 O ATOM 2355 OE2 GLU A 470 54.543 -11.814 26.563 1.00 62.76 O ANISOU 2355 OE2 GLU A 470 8573 7892 7382 985 -1330 -1175 O ATOM 2356 N MET A 471 54.920 -15.329 22.248 1.00 24.24 N ANISOU 2356 N MET A 471 3697 2825 2688 559 -1210 -803 N ATOM 2357 CA MET A 471 53.971 -16.086 21.399 1.00 23.08 C ANISOU 2357 CA MET A 471 3555 2695 2521 469 -1136 -655 C ATOM 2358 C MET A 471 54.432 -17.500 21.130 1.00 25.86 C ANISOU 2358 C MET A 471 3945 3025 2855 435 -1185 -605 C ATOM 2359 O MET A 471 53.668 -18.452 21.305 1.00 31.87 O ANISOU 2359 O MET A 471 4744 3824 3540 419 -1159 -493 O ATOM 2360 CB MET A 471 53.722 -15.381 20.067 1.00 21.58 C ANISOU 2360 CB MET A 471 3287 2461 2450 398 -1074 -639 C ATOM 2361 CG MET A 471 53.043 -14.020 20.223 1.00 26.22 C ANISOU 2361 CG MET A 471 3824 3070 3068 413 -1022 -668 C ATOM 2362 SD MET A 471 52.780 -13.137 18.685 1.00 31.82 S ANISOU 2362 SD MET A 471 4460 3719 3911 341 -957 -645 S ATOM 2363 CE MET A 471 51.550 -14.145 17.874 1.00 21.33 C ANISOU 2363 CE MET A 471 3173 2400 2531 276 -915 -501 C ATOM 2364 N MET A 472 55.687 -17.639 20.715 1.00 27.11 N ANISOU 2364 N MET A 472 4080 3114 3107 423 -1253 -695 N ATOM 2365 CA MET A 472 56.248 -18.958 20.410 1.00 26.39 C ANISOU 2365 CA MET A 472 4008 2996 3024 382 -1314 -668 C ATOM 2366 C MET A 472 56.242 -19.789 21.681 1.00 28.88 C ANISOU 2366 C MET A 472 4412 3353 3210 443 -1380 -647 C ATOM 2367 O MET A 472 55.905 -20.973 21.665 1.00 28.43 O ANISOU 2367 O MET A 472 4378 3317 3106 412 -1389 -548 O ATOM 2368 CB MET A 472 57.666 -18.821 19.863 1.00 22.16 C ANISOU 2368 CB MET A 472 3429 2362 2629 363 -1374 -795 C ATOM 2369 CG MET A 472 57.717 -18.210 18.469 1.00 20.14 C ANISOU 2369 CG MET A 472 3101 2058 2492 299 -1291 -791 C ATOM 2370 SD MET A 472 57.319 -19.412 17.190 1.00 35.41 S ANISOU 2370 SD MET A 472 5024 4004 4428 208 -1267 -674 S ATOM 2371 CE MET A 472 57.403 -18.421 15.699 1.00 34.43 C ANISOU 2371 CE MET A 472 4851 3822 4410 169 -1164 -680 C ATOM 2372 N ASP A 473 56.585 -19.147 22.791 1.00 22.69 N ANISOU 2372 N ASP A 473 3677 2577 2369 541 -1427 -740 N ATOM 2373 CA ASP A 473 56.714 -19.865 24.050 1.00 29.63 C ANISOU 2373 CA ASP A 473 4665 3486 3105 622 -1499 -733 C ATOM 2374 C ASP A 473 55.347 -20.356 24.510 1.00 35.42 C ANISOU 2374 C ASP A 473 5453 4306 3699 626 -1398 -568 C ATOM 2375 O ASP A 473 55.241 -21.451 25.082 1.00 31.16 O ANISOU 2375 O ASP A 473 4989 3785 3065 645 -1421 -487 O ATOM 2376 CB ASP A 473 57.387 -19.003 25.118 1.00 40.58 C ANISOU 2376 CB ASP A 473 6098 4860 4461 750 -1583 -886 C ATOM 2377 CG ASP A 473 57.653 -19.768 26.402 1.00 66.36 C ANISOU 2377 CG ASP A 473 9503 8146 7566 852 -1677 -890 C ATOM 2378 OD1 ASP A 473 58.330 -20.818 26.338 1.00 80.57 O ANISOU 2378 OD1 ASP A 473 11335 9896 9383 825 -1768 -892 O ATOM 2379 OD2 ASP A 473 57.188 -19.328 27.481 1.00 69.94 O ANISOU 2379 OD2 ASP A 473 10040 8664 7871 963 -1663 -894 O ATOM 2380 N GLU A 474 54.303 -19.576 24.208 1.00 25.31 N ANISOU 2380 N GLU A 474 4125 3063 2427 604 -1282 -518 N ATOM 2381 CA GLU A 474 52.945 -19.940 24.596 1.00 22.97 C ANISOU 2381 CA GLU A 474 3865 2825 2038 604 -1169 -375 C ATOM 2382 C GLU A 474 52.466 -21.188 23.834 1.00 26.53 C ANISOU 2382 C GLU A 474 4281 3256 2545 523 -1137 -244 C ATOM 2383 O GLU A 474 51.762 -22.042 24.377 1.00 26.56 O ANISOU 2383 O GLU A 474 4330 3282 2479 540 -1082 -125 O ATOM 2384 CB GLU A 474 51.970 -18.767 24.354 1.00 23.55 C ANISOU 2384 CB GLU A 474 3880 2922 2146 588 -1067 -376 C ATOM 2385 CG GLU A 474 50.496 -19.162 24.568 1.00 21.99 C ANISOU 2385 CG GLU A 474 3697 2753 1905 571 -937 -236 C ATOM 2386 CD GLU A 474 49.537 -17.982 24.591 1.00 29.47 C ANISOU 2386 CD GLU A 474 4600 3720 2876 564 -849 -256 C ATOM 2387 OE1 GLU A 474 49.991 -16.841 24.829 1.00 23.71 O ANISOU 2387 OE1 GLU A 474 3849 3009 2151 601 -888 -374 O ATOM 2388 OE2 GLU A 474 48.322 -18.204 24.370 1.00 26.23 O ANISOU 2388 OE2 GLU A 474 4166 3298 2503 523 -745 -161 O ATOM 2389 N ILE A 475 52.817 -21.265 22.556 1.00 30.24 N ANISOU 2389 N ILE A 475 4662 3679 3148 442 -1165 -265 N ATOM 2390 CA ILE A 475 52.497 -22.434 21.756 1.00 31.32 C ANISOU 2390 CA ILE A 475 4749 3795 3355 378 -1164 -168 C ATOM 2391 C ILE A 475 53.314 -23.655 22.225 1.00 35.12 C ANISOU 2391 C ILE A 475 5270 4268 3806 387 -1262 -158 C ATOM 2392 O ILE A 475 52.760 -24.719 22.506 1.00 27.70 O ANISOU 2392 O ILE A 475 4338 3340 2848 388 -1240 -43 O ATOM 2393 CB ILE A 475 52.738 -22.152 20.272 1.00 24.88 C ANISOU 2393 CB ILE A 475 3846 2937 2672 306 -1175 -207 C ATOM 2394 CG1 ILE A 475 51.917 -20.929 19.844 1.00 27.64 C ANISOU 2394 CG1 ILE A 475 4166 3288 3049 300 -1089 -214 C ATOM 2395 CG2 ILE A 475 52.403 -23.399 19.420 1.00 24.53 C ANISOU 2395 CG2 ILE A 475 3740 2874 2705 254 -1191 -120 C ATOM 2396 CD1 ILE A 475 50.419 -21.033 20.208 1.00 28.66 C ANISOU 2396 CD1 ILE A 475 4299 3438 3154 312 -992 -110 C ATOM 2397 N PHE A 476 54.625 -23.488 22.362 1.00 26.03 N ANISOU 2397 N PHE A 476 4141 3085 2666 399 -1372 -284 N ATOM 2398 CA PHE A 476 55.468 -24.632 22.708 1.00 33.71 C ANISOU 2398 CA PHE A 476 5144 4033 3631 398 -1486 -293 C ATOM 2399 C PHE A 476 55.307 -25.107 24.146 1.00 33.34 C ANISOU 2399 C PHE A 476 5220 4021 3428 487 -1501 -239 C ATOM 2400 O PHE A 476 55.595 -26.260 24.449 1.00 29.45 O ANISOU 2400 O PHE A 476 4753 3516 2920 482 -1568 -189 O ATOM 2401 CB PHE A 476 56.942 -24.325 22.432 1.00 31.57 C ANISOU 2401 CB PHE A 476 4857 3691 3447 385 -1605 -462 C ATOM 2402 CG PHE A 476 57.250 -24.127 20.975 1.00 29.39 C ANISOU 2402 CG PHE A 476 4472 3372 3322 294 -1587 -501 C ATOM 2403 CD1 PHE A 476 56.906 -25.094 20.053 1.00 28.16 C ANISOU 2403 CD1 PHE A 476 4244 3222 3233 220 -1580 -416 C ATOM 2404 CD2 PHE A 476 57.876 -22.974 20.529 1.00 27.10 C ANISOU 2404 CD2 PHE A 476 4150 3031 3114 295 -1574 -622 C ATOM 2405 CE1 PHE A 476 57.184 -24.929 18.709 1.00 29.20 C ANISOU 2405 CE1 PHE A 476 4295 3320 3482 152 -1562 -452 C ATOM 2406 CE2 PHE A 476 58.153 -22.797 19.187 1.00 35.12 C ANISOU 2406 CE2 PHE A 476 5085 4005 4254 221 -1538 -645 C ATOM 2407 CZ PHE A 476 57.807 -23.779 18.273 1.00 32.21 C ANISOU 2407 CZ PHE A 476 4665 3651 3922 152 -1533 -560 C ATOM 2408 N ASP A 477 54.853 -24.227 25.032 1.00 29.34 N ANISOU 2408 N ASP A 477 4791 3555 2801 573 -1439 -250 N ATOM 2409 CA ASP A 477 54.900 -24.546 26.453 1.00 33.86 C ANISOU 2409 CA ASP A 477 5509 4157 3198 683 -1464 -225 C ATOM 2410 C ASP A 477 53.962 -23.725 27.339 1.00 40.20 C ANISOU 2410 C ASP A 477 6388 5025 3862 769 -1344 -187 C ATOM 2411 O ASP A 477 54.198 -23.598 28.536 1.00 38.09 O ANISOU 2411 O ASP A 477 6254 4784 3434 887 -1379 -218 O ATOM 2412 CB ASP A 477 56.330 -24.382 26.961 1.00 34.07 C ANISOU 2412 CB ASP A 477 5601 4134 3211 746 -1638 -394 C ATOM 2413 CG ASP A 477 56.536 -24.996 28.331 1.00 48.24 C ANISOU 2413 CG ASP A 477 7563 5944 4823 863 -1703 -367 C ATOM 2414 OD1 ASP A 477 55.867 -26.008 28.656 1.00 48.94 O ANISOU 2414 OD1 ASP A 477 7697 6061 4836 858 -1637 -201 O ATOM 2415 OD2 ASP A 477 57.369 -24.457 29.089 1.00 54.68 O ANISOU 2415 OD2 ASP A 477 8466 6734 5575 971 -1821 -515 O ATOM 2416 N GLY A 478 52.897 -23.178 26.767 1.00 40.01 N ANISOU 2416 N GLY A 478 6282 5022 3898 717 -1210 -129 N ATOM 2417 CA GLY A 478 51.982 -22.362 27.542 1.00 40.66 C ANISOU 2417 CA GLY A 478 6417 5160 3873 784 -1093 -106 C ATOM 2418 C GLY A 478 50.755 -23.103 28.052 1.00 45.59 C ANISOU 2418 C GLY A 478 7087 5806 4429 795 -940 72 C ATOM 2419 O GLY A 478 49.978 -22.542 28.809 1.00 50.69 O ANISOU 2419 O GLY A 478 7791 6494 4976 855 -829 98 O ATOM 2420 N TYR A 479 50.581 -24.356 27.635 1.00 44.14 N ANISOU 2420 N TYR A 479 6868 5587 4318 740 -930 189 N ATOM 2421 CA TYR A 479 49.348 -25.110 27.900 1.00 42.43 C ANISOU 2421 CA TYR A 479 6651 5360 4109 738 -770 364 C ATOM 2422 C TYR A 479 49.659 -26.506 28.425 1.00 41.77 C ANISOU 2422 C TYR A 479 6633 5262 3976 768 -799 475 C ATOM 2423 O TYR A 479 50.626 -27.130 28.002 1.00 41.15 O ANISOU 2423 O TYR A 479 6524 5160 3950 732 -947 432 O ATOM 2424 CB TYR A 479 48.487 -25.236 26.625 1.00 35.38 C ANISOU 2424 CB TYR A 479 5593 4417 3433 634 -706 411 C ATOM 2425 CG TYR A 479 48.021 -23.913 26.066 1.00 38.02 C ANISOU 2425 CG TYR A 479 5865 4755 3827 600 -668 322 C ATOM 2426 CD1 TYR A 479 46.886 -23.290 26.568 1.00 39.99 C ANISOU 2426 CD1 TYR A 479 6130 5011 4053 624 -518 356 C ATOM 2427 CD2 TYR A 479 48.727 -23.272 25.048 1.00 33.93 C ANISOU 2427 CD2 TYR A 479 5272 4226 3396 544 -776 202 C ATOM 2428 CE1 TYR A 479 46.459 -22.070 26.071 1.00 37.42 C ANISOU 2428 CE1 TYR A 479 5741 4685 3792 588 -497 270 C ATOM 2429 CE2 TYR A 479 48.303 -22.051 24.538 1.00 31.98 C ANISOU 2429 CE2 TYR A 479 4968 3976 3206 515 -742 129 C ATOM 2430 CZ TYR A 479 47.171 -21.454 25.057 1.00 32.97 C ANISOU 2430 CZ TYR A 479 5105 4112 3309 535 -612 161 C ATOM 2431 OH TYR A 479 46.737 -20.243 24.564 1.00 33.50 O ANISOU 2431 OH TYR A 479 5111 4173 3444 501 -590 86 O ATOM 2432 N ILE A 480 48.836 -27.005 29.338 1.00 45.57 N ANISOU 2432 N ILE A 480 7198 5749 4367 831 -652 618 N ATOM 2433 CA ILE A 480 49.038 -28.354 29.846 1.00 47.87 C ANISOU 2433 CA ILE A 480 7548 6018 4621 862 -662 746 C ATOM 2434 C ILE A 480 48.416 -29.371 28.883 1.00 46.55 C ANISOU 2434 C ILE A 480 7207 5786 4694 769 -617 857 C ATOM 2435 O ILE A 480 47.256 -29.236 28.494 1.00 51.81 O ANISOU 2435 O ILE A 480 7778 6415 5490 738 -469 920 O ATOM 2436 CB ILE A 480 48.483 -28.507 31.290 1.00 66.42 C ANISOU 2436 CB ILE A 480 10081 8395 6761 986 -512 865 C ATOM 2437 CG1 ILE A 480 48.719 -29.923 31.814 1.00 67.60 C ANISOU 2437 CG1 ILE A 480 10298 8515 6874 1021 -522 1011 C ATOM 2438 CG2 ILE A 480 47.007 -28.153 31.344 1.00 72.18 C ANISOU 2438 CG2 ILE A 480 10763 9106 7556 978 -274 959 C ATOM 2439 CD1 ILE A 480 48.295 -30.125 33.261 1.00 73.59 C ANISOU 2439 CD1 ILE A 480 11266 9297 7398 1158 -375 1138 C ATOM 2440 N PRO A 481 49.206 -30.374 28.471 1.00 41.69 N ANISOU 2440 N PRO A 481 6538 5147 4157 727 -760 863 N ATOM 2441 CA PRO A 481 48.773 -31.428 27.544 1.00 38.30 C ANISOU 2441 CA PRO A 481 5927 4658 3967 650 -756 949 C ATOM 2442 C PRO A 481 47.541 -32.176 28.067 1.00 43.99 C ANISOU 2442 C PRO A 481 6631 5331 4751 690 -555 1143 C ATOM 2443 O PRO A 481 47.311 -32.200 29.269 1.00 41.60 O ANISOU 2443 O PRO A 481 6487 5045 4273 779 -443 1232 O ATOM 2444 CB PRO A 481 49.975 -32.396 27.504 1.00 36.07 C ANISOU 2444 CB PRO A 481 5645 4372 3688 627 -947 926 C ATOM 2445 CG PRO A 481 51.131 -31.613 27.973 1.00 43.69 C ANISOU 2445 CG PRO A 481 6750 5376 4472 664 -1081 772 C ATOM 2446 CD PRO A 481 50.602 -30.555 28.916 1.00 47.42 C ANISOU 2446 CD PRO A 481 7370 5892 4755 759 -951 770 C ATOM 2447 N HIS A 482 46.774 -32.797 27.177 1.00 46.31 N ANISOU 2447 N HIS A 482 6736 5557 5303 636 -509 1205 N ATOM 2448 CA HIS A 482 45.619 -33.571 27.605 1.00 51.02 C ANISOU 2448 CA HIS A 482 7286 6080 6020 675 -316 1383 C ATOM 2449 C HIS A 482 46.003 -34.644 28.609 1.00 50.91 C ANISOU 2449 C HIS A 482 7370 6065 5908 733 -303 1523 C ATOM 2450 O HIS A 482 46.897 -35.447 28.357 1.00 51.10 O ANISOU 2450 O HIS A 482 7353 6098 5966 701 -474 1510 O ATOM 2451 CB HIS A 482 44.900 -34.231 26.430 1.00 49.61 C ANISOU 2451 CB HIS A 482 6865 5812 6173 621 -316 1407 C ATOM 2452 CG HIS A 482 43.678 -34.978 26.848 1.00 59.04 C ANISOU 2452 CG HIS A 482 7989 6905 7541 667 -108 1578 C ATOM 2453 ND1 HIS A 482 42.446 -34.373 26.980 1.00 62.08 N ANISOU 2453 ND1 HIS A 482 8360 7221 8006 691 90 1602 N ATOM 2454 CD2 HIS A 482 43.508 -36.267 27.226 1.00 61.93 C ANISOU 2454 CD2 HIS A 482 8293 7212 8025 697 -56 1734 C ATOM 2455 CE1 HIS A 482 41.564 -35.265 27.393 1.00 68.00 C ANISOU 2455 CE1 HIS A 482 9040 7866 8931 734 264 1763 C ATOM 2456 NE2 HIS A 482 42.184 -36.422 27.553 1.00 67.22 N ANISOU 2456 NE2 HIS A 482 8910 7773 8858 742 183 1852 N ATOM 2457 N PRO A 483 45.311 -34.666 29.751 1.00 53.96 N ANISOU 2457 N PRO A 483 7891 6437 6177 819 -96 1659 N ATOM 2458 CA PRO A 483 45.633 -35.558 30.875 1.00 57.12 C ANISOU 2458 CA PRO A 483 8435 6838 6430 898 -58 1806 C ATOM 2459 C PRO A 483 45.664 -37.051 30.498 1.00 55.40 C ANISOU 2459 C PRO A 483 8055 6550 6446 864 -104 1926 C ATOM 2460 O PRO A 483 46.425 -37.824 31.082 1.00 49.71 O ANISOU 2460 O PRO A 483 7425 5844 5619 894 -196 1988 O ATOM 2461 CB PRO A 483 44.499 -35.269 31.873 1.00 56.09 C ANISOU 2461 CB PRO A 483 8423 6678 6213 986 235 1941 C ATOM 2462 CG PRO A 483 43.403 -34.634 31.030 1.00 55.39 C ANISOU 2462 CG PRO A 483 8161 6528 6356 928 348 1889 C ATOM 2463 CD PRO A 483 44.170 -33.791 30.066 1.00 52.35 C ANISOU 2463 CD PRO A 483 7719 6209 5961 851 123 1676 C ATOM 2464 N ASP A 484 44.854 -37.450 29.525 1.00 56.14 N ANISOU 2464 N ASP A 484 7905 6561 6866 809 -56 1949 N ATOM 2465 CA ASP A 484 44.768 -38.860 29.153 1.00 57.05 C ANISOU 2465 CA ASP A 484 7832 6602 7243 787 -92 2060 C ATOM 2466 C ASP A 484 45.670 -39.234 27.979 1.00 49.67 C ANISOU 2466 C ASP A 484 6729 5695 6446 694 -367 1921 C ATOM 2467 O ASP A 484 46.457 -40.171 28.085 1.00 44.32 O ANISOU 2467 O ASP A 484 6029 5029 5783 676 -507 1954 O ATOM 2468 CB ASP A 484 43.316 -39.240 28.860 1.00 59.49 C ANISOU 2468 CB ASP A 484 7955 6780 7867 805 123 2171 C ATOM 2469 CG ASP A 484 42.384 -38.877 30.007 1.00 63.09 C ANISOU 2469 CG ASP A 484 8571 7194 8208 892 421 2307 C ATOM 2470 OD1 ASP A 484 42.611 -39.377 31.137 1.00 55.10 O ANISOU 2470 OD1 ASP A 484 7727 6194 7014 963 511 2455 O ATOM 2471 OD2 ASP A 484 41.440 -38.080 29.777 1.00 67.10 O ANISOU 2471 OD2 ASP A 484 9041 7653 8799 890 562 2261 O ATOM 2472 N THR A 485 45.563 -38.499 26.873 1.00 42.17 N ANISOU 2472 N THR A 485 5670 4757 5595 636 -442 1766 N ATOM 2473 CA THR A 485 46.296 -38.838 25.647 1.00 49.21 C ANISOU 2473 CA THR A 485 6394 5669 6636 554 -675 1636 C ATOM 2474 C THR A 485 47.691 -38.215 25.541 1.00 51.29 C ANISOU 2474 C THR A 485 6783 6028 6677 507 -873 1472 C ATOM 2475 O THR A 485 48.573 -38.761 24.874 1.00 40.62 O ANISOU 2475 O THR A 485 5333 4694 5406 443 -1070 1391 O ATOM 2476 CB THR A 485 45.525 -38.406 24.405 1.00 44.54 C ANISOU 2476 CB THR A 485 5625 5032 6267 526 -668 1547 C ATOM 2477 OG1 THR A 485 45.403 -36.976 24.400 1.00 40.17 O ANISOU 2477 OG1 THR A 485 5204 4519 5538 526 -616 1444 O ATOM 2478 CG2 THR A 485 44.142 -39.052 24.401 1.00 41.94 C ANISOU 2478 CG2 THR A 485 5139 4577 6220 577 -491 1681 C ATOM 2479 N GLY A 486 47.880 -37.064 26.178 1.00 49.74 N ANISOU 2479 N GLY A 486 6790 5884 6225 540 -821 1413 N ATOM 2480 CA GLY A 486 49.153 -36.376 26.122 1.00 44.98 C ANISOU 2480 CA GLY A 486 6299 5349 5441 510 -994 1247 C ATOM 2481 C GLY A 486 49.290 -35.423 24.951 1.00 40.54 C ANISOU 2481 C GLY A 486 5658 4806 4940 449 -1060 1083 C ATOM 2482 O GLY A 486 50.381 -34.898 24.708 1.00 42.00 O ANISOU 2482 O GLY A 486 5896 5028 5032 414 -1204 937 O ATOM 2483 N LYS A 487 48.193 -35.190 24.230 1.00 38.62 N ANISOU 2483 N LYS A 487 5289 4522 4862 442 -954 1105 N ATOM 2484 CA LYS A 487 48.182 -34.194 23.154 1.00 38.52 C ANISOU 2484 CA LYS A 487 5226 4522 4890 398 -995 965 C ATOM 2485 C LYS A 487 48.395 -32.788 23.696 1.00 35.47 C ANISOU 2485 C LYS A 487 5009 4185 4284 422 -948 882 C ATOM 2486 O LYS A 487 47.760 -32.385 24.675 1.00 35.02 O ANISOU 2486 O LYS A 487 5062 4132 4113 483 -801 953 O ATOM 2487 CB LYS A 487 46.865 -34.237 22.375 1.00 48.36 C ANISOU 2487 CB LYS A 487 6321 5697 6357 404 -896 1005 C ATOM 2488 CG LYS A 487 46.675 -35.503 21.548 1.00 60.22 C ANISOU 2488 CG LYS A 487 7615 7146 8121 387 -975 1043 C ATOM 2489 CD LYS A 487 45.237 -35.643 21.078 1.00 68.54 C ANISOU 2489 CD LYS A 487 8530 8102 9412 426 -860 1097 C ATOM 2490 CE LYS A 487 45.027 -35.038 19.709 1.00 70.65 C ANISOU 2490 CE LYS A 487 8711 8352 9780 406 -940 966 C ATOM 2491 NZ LYS A 487 45.557 -35.932 18.639 1.00 74.34 N ANISOU 2491 NZ LYS A 487 9017 8823 10405 382 -1117 911 N ATOM 2492 N ASP A 488 49.277 -32.034 23.048 1.00 31.06 N ANISOU 2492 N ASP A 488 3163 4393 4247 -5 109 870 N ATOM 2493 CA ASP A 488 49.532 -30.652 23.449 1.00 26.64 C ANISOU 2493 CA ASP A 488 2615 3975 3533 20 123 747 C ATOM 2494 C ASP A 488 48.956 -29.618 22.454 1.00 30.25 C ANISOU 2494 C ASP A 488 3183 4317 3994 -4 49 583 C ATOM 2495 O ASP A 488 48.277 -29.972 21.483 1.00 28.08 O ANISOU 2495 O ASP A 488 2976 3860 3834 -34 -9 562 O ATOM 2496 CB ASP A 488 51.034 -30.433 23.726 1.00 24.81 C ANISOU 2496 CB ASP A 488 2413 3820 3193 47 165 717 C ATOM 2497 CG ASP A 488 51.923 -30.806 22.536 1.00 38.20 C ANISOU 2497 CG ASP A 488 4242 5340 4931 21 144 668 C ATOM 2498 OD1 ASP A 488 51.478 -30.651 21.373 1.00 36.07 O ANISOU 2498 OD1 ASP A 488 4077 4907 4723 -7 85 592 O ATOM 2499 OD2 ASP A 488 53.083 -31.235 22.769 1.00 38.71 O ANISOU 2499 OD2 ASP A 488 4307 5440 4962 37 184 701 O ATOM 2500 N ALA A 489 49.209 -28.342 22.720 1.00 28.58 N ANISOU 2500 N ALA A 489 2985 4208 3665 14 38 465 N ATOM 2501 CA ALA A 489 48.717 -27.276 21.866 1.00 31.55 C ANISOU 2501 CA ALA A 489 3462 4487 4040 -10 -40 313 C ATOM 2502 C ALA A 489 49.181 -27.482 20.426 1.00 32.29 C ANISOU 2502 C ALA A 489 3715 4369 4186 -44 -73 263 C ATOM 2503 O ALA A 489 48.414 -27.341 19.491 1.00 31.98 O ANISOU 2503 O ALA A 489 3760 4179 4211 -66 -138 198 O ATOM 2504 CB ALA A 489 49.173 -25.933 22.386 1.00 26.77 C ANISOU 2504 CB ALA A 489 2842 4016 3315 18 -59 202 C ATOM 2505 N LEU A 490 50.434 -27.849 20.252 1.00 31.93 N ANISOU 2505 N LEU A 490 3707 4316 4108 -38 -28 292 N ATOM 2506 CA LEU A 490 50.975 -28.028 18.907 1.00 31.18 C ANISOU 2506 CA LEU A 490 3756 4052 4038 -53 -49 246 C ATOM 2507 C LEU A 490 50.327 -29.206 18.158 1.00 30.09 C ANISOU 2507 C LEU A 490 3654 3751 4028 -52 -88 294 C ATOM 2508 O LEU A 490 50.067 -29.108 16.964 1.00 27.00 O ANISOU 2508 O LEU A 490 3384 3204 3670 -51 -145 219 O ATOM 2509 CB LEU A 490 52.482 -28.203 19.007 1.00 32.78 C ANISOU 2509 CB LEU A 490 3968 4309 4180 -41 13 271 C ATOM 2510 CG LEU A 490 53.351 -27.974 17.784 1.00 38.25 C ANISOU 2510 CG LEU A 490 4793 4894 4845 -47 12 211 C ATOM 2511 CD1 LEU A 490 53.109 -26.604 17.180 1.00 26.28 C ANISOU 2511 CD1 LEU A 490 3359 3340 3287 -71 -35 102 C ATOM 2512 CD2 LEU A 490 54.805 -28.133 18.200 1.00 39.69 C ANISOU 2512 CD2 LEU A 490 4944 5165 4972 -34 83 244 C ATOM 2513 N ASP A 491 50.056 -30.311 18.860 1.00 21.67 N ANISOU 2513 N ASP A 491 2478 2717 3040 -44 -66 420 N ATOM 2514 CA ASP A 491 49.342 -31.419 18.259 1.00 31.85 C ANISOU 2514 CA ASP A 491 3775 3843 4483 -40 -124 470 C ATOM 2515 C ASP A 491 47.975 -30.937 17.810 1.00 38.77 C ANISOU 2515 C ASP A 491 4679 4624 5429 -52 -197 399 C ATOM 2516 O ASP A 491 47.547 -31.203 16.693 1.00 47.48 O ANISOU 2516 O ASP A 491 5881 5543 6617 -39 -275 337 O ATOM 2517 CB ASP A 491 49.143 -32.584 19.231 1.00 38.68 C ANISOU 2517 CB ASP A 491 4492 4766 5440 -39 -95 638 C ATOM 2518 CG ASP A 491 50.407 -33.398 19.453 1.00 58.61 C ANISOU 2518 CG ASP A 491 7003 7324 7942 -23 -54 709 C ATOM 2519 OD1 ASP A 491 51.184 -33.622 18.481 1.00 56.94 O ANISOU 2519 OD1 ASP A 491 6902 7010 7724 -5 -80 642 O ATOM 2520 OD2 ASP A 491 50.603 -33.829 20.618 1.00 61.81 O ANISOU 2520 OD2 ASP A 491 7284 7867 8333 -22 5 832 O ATOM 2521 N ILE A 492 47.275 -30.247 18.697 1.00 26.77 N ANISOU 2521 N ILE A 492 3067 3234 3871 -67 -177 401 N ATOM 2522 CA ILE A 492 45.931 -29.832 18.376 1.00 26.92 C ANISOU 2522 CA ILE A 492 3094 3172 3963 -79 -247 334 C ATOM 2523 C ILE A 492 45.942 -28.938 17.143 1.00 26.31 C ANISOU 2523 C ILE A 492 3191 2962 3846 -81 -317 169 C ATOM 2524 O ILE A 492 45.143 -29.128 16.249 1.00 26.03 O ANISOU 2524 O ILE A 492 3228 2749 3912 -75 -399 111 O ATOM 2525 CB ILE A 492 45.268 -29.086 19.537 1.00 30.00 C ANISOU 2525 CB ILE A 492 3358 3752 4290 -83 -216 341 C ATOM 2526 CG1 ILE A 492 44.856 -30.086 20.625 1.00 35.06 C ANISOU 2526 CG1 ILE A 492 3821 4498 5002 -78 -156 523 C ATOM 2527 CG2 ILE A 492 44.041 -28.335 19.029 1.00 20.08 C ANISOU 2527 CG2 ILE A 492 2145 2407 3079 -97 -300 218 C ATOM 2528 CD1 ILE A 492 44.242 -29.409 21.824 1.00 40.63 C ANISOU 2528 CD1 ILE A 492 4390 5425 5624 -61 -115 539 C ATOM 2529 N MET A 493 46.871 -27.986 17.099 1.00 22.95 N ANISOU 2529 N MET A 493 2826 2616 3278 -84 -288 101 N ATOM 2530 CA MET A 493 46.916 -26.970 16.055 1.00 24.17 C ANISOU 2530 CA MET A 493 3132 2673 3380 -92 -347 -37 C ATOM 2531 C MET A 493 47.334 -27.480 14.681 1.00 30.15 C ANISOU 2531 C MET A 493 4037 3254 4165 -66 -378 -65 C ATOM 2532 O MET A 493 46.798 -27.036 13.668 1.00 34.56 O ANISOU 2532 O MET A 493 4717 3676 4738 -58 -454 -165 O ATOM 2533 CB MET A 493 47.834 -25.818 16.474 1.00 28.51 C ANISOU 2533 CB MET A 493 3681 3358 3792 -105 -312 -82 C ATOM 2534 CG MET A 493 47.186 -24.839 17.447 1.00 26.85 C ANISOU 2534 CG MET A 493 3375 3286 3542 -113 -338 -133 C ATOM 2535 SD MET A 493 48.419 -23.813 18.250 1.00 39.72 S ANISOU 2535 SD MET A 493 4954 5094 5045 -106 -301 -156 S ATOM 2536 CE MET A 493 48.751 -22.607 16.981 1.00 30.31 C ANISOU 2536 CE MET A 493 3927 3766 3823 -140 -375 -277 C ATOM 2537 N MET A 494 48.298 -28.393 14.648 1.00 30.37 N ANISOU 2537 N MET A 494 4053 3294 4191 -44 -325 15 N ATOM 2538 CA MET A 494 48.790 -28.956 13.394 1.00 29.67 C ANISOU 2538 CA MET A 494 4092 3067 4115 1 -353 -13 C ATOM 2539 C MET A 494 47.706 -29.659 12.606 1.00 32.90 C ANISOU 2539 C MET A 494 4549 3287 4663 40 -456 -48 C ATOM 2540 O MET A 494 47.728 -29.668 11.377 1.00 29.94 O ANISOU 2540 O MET A 494 4313 2781 4282 90 -514 -128 O ATOM 2541 CB MET A 494 49.871 -29.987 13.671 1.00 30.36 C ANISOU 2541 CB MET A 494 4127 3206 4201 24 -293 80 C ATOM 2542 CG MET A 494 51.252 -29.433 13.731 1.00 27.01 C ANISOU 2542 CG MET A 494 3727 2894 3642 15 -211 79 C ATOM 2543 SD MET A 494 52.428 -30.739 14.080 1.00 39.42 S ANISOU 2543 SD MET A 494 5234 4515 5228 45 -154 176 S ATOM 2544 CE MET A 494 53.937 -29.746 14.032 1.00 33.55 C ANISOU 2544 CE MET A 494 4529 3891 4328 29 -62 148 C ATOM 2545 N PHE A 495 46.774 -30.282 13.314 1.00 25.28 N ANISOU 2545 N PHE A 495 3464 2311 3831 26 -481 16 N ATOM 2546 CA PHE A 495 45.749 -31.049 12.637 1.00 29.39 C ANISOU 2546 CA PHE A 495 4007 2638 4521 65 -589 -8 C ATOM 2547 C PHE A 495 44.394 -30.353 12.689 1.00 28.86 C ANISOU 2547 C PHE A 495 3934 2518 4512 38 -649 -80 C ATOM 2548 O PHE A 495 43.382 -30.924 12.297 1.00 27.77 O ANISOU 2548 O PHE A 495 3790 2222 4539 63 -741 -98 O ATOM 2549 CB PHE A 495 45.659 -32.457 13.226 1.00 30.43 C ANISOU 2549 CB PHE A 495 4003 2750 4807 73 -594 128 C ATOM 2550 CG PHE A 495 46.932 -33.251 13.104 1.00 30.91 C ANISOU 2550 CG PHE A 495 4072 2840 4831 106 -559 183 C ATOM 2551 CD1 PHE A 495 47.209 -33.979 11.947 1.00 28.09 C ANISOU 2551 CD1 PHE A 495 3815 2328 4530 187 -646 125 C ATOM 2552 CD2 PHE A 495 47.857 -33.268 14.144 1.00 31.55 C ANISOU 2552 CD2 PHE A 495 4061 3106 4819 69 -449 281 C ATOM 2553 CE1 PHE A 495 48.375 -34.714 11.838 1.00 34.29 C ANISOU 2553 CE1 PHE A 495 4602 3147 5279 224 -622 164 C ATOM 2554 CE2 PHE A 495 49.030 -34.003 14.044 1.00 33.28 C ANISOU 2554 CE2 PHE A 495 4287 3349 5010 100 -423 322 C ATOM 2555 CZ PHE A 495 49.295 -34.729 12.894 1.00 33.31 C ANISOU 2555 CZ PHE A 495 4385 3203 5069 174 -508 263 C ATOM 2556 N HIS A 496 44.367 -29.108 13.152 1.00 19.70 N ANISOU 2556 N HIS A 496 2773 1483 3228 -7 -610 -130 N ATOM 2557 CA HIS A 496 43.093 -28.400 13.204 1.00 19.69 C ANISOU 2557 CA HIS A 496 2767 1441 3276 -30 -675 -214 C ATOM 2558 C HIS A 496 42.789 -27.740 11.854 1.00 24.48 C ANISOU 2558 C HIS A 496 3563 1879 3860 0 -771 -369 C ATOM 2559 O HIS A 496 43.709 -27.300 11.147 1.00 26.09 O ANISOU 2559 O HIS A 496 3890 2080 3941 18 -754 -409 O ATOM 2560 CB HIS A 496 43.109 -27.380 14.321 1.00 18.31 C ANISOU 2560 CB HIS A 496 2496 1472 2988 -77 -616 -213 C ATOM 2561 CG HIS A 496 41.771 -26.769 14.591 1.00 27.78 C ANISOU 2561 CG HIS A 496 3651 2661 4243 -97 -680 -289 C ATOM 2562 ND1 HIS A 496 41.347 -25.608 13.983 1.00 25.17 N ANISOU 2562 ND1 HIS A 496 3434 2268 3861 -106 -759 -444 N ATOM 2563 CD2 HIS A 496 40.761 -27.162 15.402 1.00 22.83 C ANISOU 2563 CD2 HIS A 496 2872 2081 3720 -108 -676 -228 C ATOM 2564 CE1 HIS A 496 40.135 -25.308 14.415 1.00 28.88 C ANISOU 2564 CE1 HIS A 496 3827 2746 4399 -120 -808 -491 C ATOM 2565 NE2 HIS A 496 39.757 -26.238 15.275 1.00 25.91 N ANISOU 2565 NE2 HIS A 496 3286 2442 4117 -120 -752 -358 N ATOM 2566 N GLN A 497 41.510 -27.687 11.495 1.00 26.14 N ANISOU 2566 N GLN A 497 3792 1949 4189 9 -870 -448 N ATOM 2567 CA GLN A 497 41.091 -27.166 10.187 1.00 24.39 C ANISOU 2567 CA GLN A 497 3755 1548 3963 51 -977 -598 C ATOM 2568 C GLN A 497 41.533 -25.724 9.954 1.00 25.68 C ANISOU 2568 C GLN A 497 4022 1783 3952 18 -968 -685 C ATOM 2569 O GLN A 497 41.820 -25.341 8.820 1.00 30.33 O ANISOU 2569 O GLN A 497 4780 2269 4474 57 -1013 -762 O ATOM 2570 CB GLN A 497 39.584 -27.250 10.025 1.00 22.44 C ANISOU 2570 CB GLN A 497 3492 1152 3881 59 -1087 -677 C ATOM 2571 CG GLN A 497 38.848 -26.398 11.037 1.00 32.81 C ANISOU 2571 CG GLN A 497 4692 2594 5180 -10 -1072 -697 C ATOM 2572 CD GLN A 497 37.334 -26.578 10.969 1.00 42.10 C ANISOU 2572 CD GLN A 497 5825 3633 6539 -4 -1171 -763 C ATOM 2573 OE1 GLN A 497 36.758 -26.752 9.892 1.00 37.56 O ANISOU 2573 OE1 GLN A 497 5374 2839 6059 48 -1285 -869 O ATOM 2574 NE2 GLN A 497 36.684 -26.514 12.124 1.00 42.79 N ANISOU 2574 NE2 GLN A 497 5732 3854 6671 -51 -1129 -705 N ATOM 2575 N PHE A 498 41.585 -24.928 11.016 1.00 19.04 N ANISOU 2575 N PHE A 498 3076 1118 3041 -46 -918 -668 N ATOM 2576 CA PHE A 498 42.117 -23.569 10.919 1.00 21.44 C ANISOU 2576 CA PHE A 498 3452 1496 3200 -81 -919 -735 C ATOM 2577 C PHE A 498 43.530 -23.420 11.532 1.00 25.58 C ANISOU 2577 C PHE A 498 3917 2197 3605 -103 -806 -638 C ATOM 2578 O PHE A 498 44.385 -22.703 10.989 1.00 18.13 O ANISOU 2578 O PHE A 498 3070 1260 2559 -111 -794 -658 O ATOM 2579 CB PHE A 498 41.160 -22.545 11.546 1.00 20.05 C ANISOU 2579 CB PHE A 498 3216 1373 3029 -123 -984 -829 C ATOM 2580 CG PHE A 498 39.752 -22.641 11.049 1.00 26.57 C ANISOU 2580 CG PHE A 498 4083 2032 3979 -106 -1096 -932 C ATOM 2581 CD1 PHE A 498 39.480 -22.679 9.689 1.00 29.49 C ANISOU 2581 CD1 PHE A 498 4615 2220 4369 -52 -1178 -995 C ATOM 2582 CD2 PHE A 498 38.694 -22.694 11.938 1.00 27.95 C ANISOU 2582 CD2 PHE A 498 4113 2266 4240 -124 -1115 -942 C ATOM 2583 CE1 PHE A 498 38.191 -22.777 9.226 1.00 25.56 C ANISOU 2583 CE1 PHE A 498 4106 1638 3969 -1 -1278 -1037 C ATOM 2584 CE2 PHE A 498 37.390 -22.780 11.479 1.00 30.24 C ANISOU 2584 CE2 PHE A 498 4435 2395 4662 -110 -1220 -1041 C ATOM 2585 CZ PHE A 498 37.138 -22.824 10.115 1.00 26.17 C ANISOU 2585 CZ PHE A 498 4051 1735 4158 -34 -1300 -1070 C ATOM 2586 N GLY A 499 43.775 -24.092 12.655 1.00 32.61 N ANISOU 2586 N GLY A 499 4647 3226 4516 -110 -724 -529 N ATOM 2587 CA GLY A 499 45.027 -23.924 13.387 1.00 24.69 C ANISOU 2587 CA GLY A 499 3574 2396 3412 -125 -626 -450 C ATOM 2588 C GLY A 499 46.241 -24.374 12.588 1.00 18.07 C ANISOU 2588 C GLY A 499 2830 1513 2522 -101 -572 -402 C ATOM 2589 O GLY A 499 47.345 -23.912 12.812 1.00 25.78 O ANISOU 2589 O GLY A 499 3798 2591 3407 -117 -511 -373 O ATOM 2590 N ASN A 500 46.039 -25.284 11.645 1.00 17.12 N ANISOU 2590 N ASN A 500 2795 1243 2468 -54 -602 -401 N ATOM 2591 CA ASN A 500 47.162 -25.785 10.870 1.00 21.91 C ANISOU 2591 CA ASN A 500 3483 1821 3019 -14 -555 -363 C ATOM 2592 C ASN A 500 47.850 -24.653 10.085 1.00 25.05 C ANISOU 2592 C ASN A 500 4007 2218 3294 -25 -550 -415 C ATOM 2593 O ASN A 500 49.059 -24.685 9.858 1.00 23.49 O ANISOU 2593 O ASN A 500 3828 2080 3015 -17 -475 -363 O ATOM 2594 CB ASN A 500 46.711 -26.930 9.957 1.00 18.83 C ANISOU 2594 CB ASN A 500 3163 1265 2729 60 -617 -376 C ATOM 2595 CG ASN A 500 46.007 -26.435 8.694 1.00 24.88 C ANISOU 2595 CG ASN A 500 4094 1865 3494 101 -719 -497 C ATOM 2596 OD1 ASN A 500 46.656 -26.095 7.706 1.00 20.75 O ANISOU 2596 OD1 ASN A 500 3703 1312 2871 140 -712 -528 O ATOM 2597 ND2 ASN A 500 44.674 -26.411 8.720 1.00 26.89 N ANISOU 2597 ND2 ASN A 500 4340 2014 3862 99 -812 -562 N ATOM 2598 N TYR A 501 47.078 -23.645 9.690 1.00 24.63 N ANISOU 2598 N TYR A 501 4029 2096 3235 -47 -632 -511 N ATOM 2599 CA TYR A 501 47.639 -22.500 8.972 1.00 25.19 C ANISOU 2599 CA TYR A 501 4210 2157 3204 -67 -639 -546 C ATOM 2600 C TYR A 501 48.544 -21.639 9.853 1.00 30.81 C ANISOU 2600 C TYR A 501 4825 3025 3855 -129 -580 -503 C ATOM 2601 O TYR A 501 49.470 -20.986 9.362 1.00 21.62 O ANISOU 2601 O TYR A 501 3717 1880 2617 -145 -546 -477 O ATOM 2602 CB TYR A 501 46.524 -21.640 8.396 1.00 20.75 C ANISOU 2602 CB TYR A 501 3747 1474 2663 -77 -759 -663 C ATOM 2603 CG TYR A 501 45.761 -22.322 7.303 1.00 20.17 C ANISOU 2603 CG TYR A 501 3799 1225 2639 -1 -831 -723 C ATOM 2604 CD1 TYR A 501 46.281 -22.398 6.012 1.00 26.55 C ANISOU 2604 CD1 TYR A 501 4761 1956 3371 64 -827 -726 C ATOM 2605 CD2 TYR A 501 44.510 -22.899 7.552 1.00 21.75 C ANISOU 2605 CD2 TYR A 501 3959 1338 2968 17 -906 -777 C ATOM 2606 CE1 TYR A 501 45.586 -23.043 4.986 1.00 24.13 C ANISOU 2606 CE1 TYR A 501 4574 1487 3108 159 -909 -796 C ATOM 2607 CE2 TYR A 501 43.804 -23.545 6.528 1.00 28.27 C ANISOU 2607 CE2 TYR A 501 4896 1983 3861 100 -990 -843 C ATOM 2608 CZ TYR A 501 44.353 -23.607 5.257 1.00 28.10 C ANISOU 2608 CZ TYR A 501 5034 1887 3756 176 -996 -860 C ATOM 2609 OH TYR A 501 43.663 -24.232 4.262 1.00 38.12 O ANISOU 2609 OH TYR A 501 6384 3029 5071 281 -1092 -909 O ATOM 2610 N VAL A 502 48.267 -21.637 11.157 1.00 29.35 N ANISOU 2610 N VAL A 502 4490 2955 3707 -156 -572 -491 N ATOM 2611 CA VAL A 502 49.056 -20.867 12.100 1.00 20.84 C ANISOU 2611 CA VAL A 502 3308 2026 2585 -194 -536 -467 C ATOM 2612 C VAL A 502 50.421 -21.528 12.303 1.00 25.49 C ANISOU 2612 C VAL A 502 3853 2699 3136 -180 -419 -362 C ATOM 2613 O VAL A 502 51.456 -20.869 12.305 1.00 23.54 O ANISOU 2613 O VAL A 502 3599 2505 2842 -202 -383 -338 O ATOM 2614 CB VAL A 502 48.325 -20.697 13.442 1.00 17.55 C ANISOU 2614 CB VAL A 502 2742 1724 2202 -203 -566 -494 C ATOM 2615 CG1 VAL A 502 49.225 -19.960 14.440 1.00 16.30 C ANISOU 2615 CG1 VAL A 502 2473 1724 1998 -217 -539 -478 C ATOM 2616 CG2 VAL A 502 47.027 -19.927 13.230 1.00 16.67 C ANISOU 2616 CG2 VAL A 502 2672 1537 2127 -218 -688 -612 C ATOM 2617 N VAL A 503 50.415 -22.839 12.476 1.00 24.69 N ANISOU 2617 N VAL A 503 3713 2599 3067 -143 -368 -302 N ATOM 2618 CA VAL A 503 51.659 -23.584 12.563 1.00 28.50 C ANISOU 2618 CA VAL A 503 4166 3145 3519 -123 -269 -214 C ATOM 2619 C VAL A 503 52.485 -23.463 11.282 1.00 33.65 C ANISOU 2619 C VAL A 503 4947 3728 4111 -105 -240 -208 C ATOM 2620 O VAL A 503 53.699 -23.262 11.346 1.00 29.51 O ANISOU 2620 O VAL A 503 4399 3277 3537 -115 -167 -160 O ATOM 2621 CB VAL A 503 51.405 -25.044 12.893 1.00 23.24 C ANISOU 2621 CB VAL A 503 3442 2472 2917 -85 -245 -154 C ATOM 2622 CG1 VAL A 503 52.735 -25.783 13.077 1.00 22.90 C ANISOU 2622 CG1 VAL A 503 3360 2501 2841 -65 -153 -74 C ATOM 2623 CG2 VAL A 503 50.570 -25.127 14.155 1.00 20.05 C ANISOU 2623 CG2 VAL A 503 2902 2152 2563 -101 -261 -139 C ATOM 2624 N GLN A 504 51.837 -23.571 10.127 1.00 26.85 N ANISOU 2624 N GLN A 504 4217 2731 3253 -71 -298 -257 N ATOM 2625 CA GLN A 504 52.538 -23.329 8.867 1.00 27.05 C ANISOU 2625 CA GLN A 504 4371 2707 3200 -42 -272 -251 C ATOM 2626 C GLN A 504 53.181 -21.942 8.864 1.00 29.81 C ANISOU 2626 C GLN A 504 4723 3107 3498 -105 -255 -240 C ATOM 2627 O GLN A 504 54.291 -21.746 8.408 1.00 26.81 O ANISOU 2627 O GLN A 504 4363 2767 3056 -103 -181 -182 O ATOM 2628 CB GLN A 504 51.571 -23.431 7.685 1.00 20.17 C ANISOU 2628 CB GLN A 504 3647 1682 2335 12 -359 -324 C ATOM 2629 CG GLN A 504 51.091 -24.841 7.416 1.00 35.45 C ANISOU 2629 CG GLN A 504 5592 3540 4336 92 -390 -335 C ATOM 2630 CD GLN A 504 50.359 -24.939 6.100 1.00 40.84 C ANISOU 2630 CD GLN A 504 6433 4070 5014 171 -478 -415 C ATOM 2631 OE1 GLN A 504 50.981 -24.998 5.040 1.00 56.42 O ANISOU 2631 OE1 GLN A 504 8513 6029 6896 240 -453 -411 O ATOM 2632 NE2 GLN A 504 49.035 -24.937 6.155 1.00 21.50 N ANISOU 2632 NE2 GLN A 504 3999 1511 2660 171 -581 -490 N ATOM 2633 N CYS A 505 52.457 -20.966 9.367 1.00 26.53 N ANISOU 2633 N CYS A 505 4279 2685 3116 -158 -334 -297 N ATOM 2634 CA CYS A 505 52.998 -19.626 9.461 1.00 27.55 C ANISOU 2634 CA CYS A 505 4392 2848 3226 -218 -348 -291 C ATOM 2635 C CYS A 505 54.235 -19.532 10.410 1.00 31.17 C ANISOU 2635 C CYS A 505 4715 3442 3688 -242 -267 -224 C ATOM 2636 O CYS A 505 55.260 -18.943 10.053 1.00 29.46 O ANISOU 2636 O CYS A 505 4503 3245 3447 -267 -221 -169 O ATOM 2637 CB CYS A 505 51.871 -18.690 9.882 1.00 21.66 C ANISOU 2637 CB CYS A 505 3634 2068 2528 -257 -473 -388 C ATOM 2638 SG CYS A 505 52.345 -17.031 10.225 1.00 29.77 S ANISOU 2638 SG CYS A 505 4612 3129 3573 -328 -538 -402 S ATOM 2639 N MET A 506 54.137 -20.114 11.605 1.00 26.89 N ANISOU 2639 N MET A 506 4049 2991 3178 -231 -250 -224 N ATOM 2640 CA MET A 506 55.276 -20.217 12.531 1.00 28.53 C ANISOU 2640 CA MET A 506 4132 3322 3386 -235 -176 -169 C ATOM 2641 C MET A 506 56.502 -20.854 11.880 1.00 27.96 C ANISOU 2641 C MET A 506 4093 3258 3273 -214 -66 -89 C ATOM 2642 O MET A 506 57.634 -20.397 12.055 1.00 26.45 O ANISOU 2642 O MET A 506 3848 3122 3080 -235 -16 -46 O ATOM 2643 CB MET A 506 54.896 -21.074 13.754 1.00 24.38 C ANISOU 2643 CB MET A 506 3492 2887 2884 -205 -162 -165 C ATOM 2644 CG MET A 506 53.810 -20.479 14.641 1.00 22.14 C ANISOU 2644 CG MET A 506 3138 2645 2630 -212 -253 -238 C ATOM 2645 SD MET A 506 53.202 -21.644 15.892 1.00 34.12 S ANISOU 2645 SD MET A 506 4531 4268 4166 -170 -221 -202 S ATOM 2646 CE MET A 506 54.675 -21.805 16.909 1.00 28.59 C ANISOU 2646 CE MET A 506 3713 3713 3437 -148 -137 -141 C ATOM 2647 N LEU A 507 56.276 -21.944 11.154 1.00 26.44 N ANISOU 2647 N LEU A 507 3978 3010 3056 -165 -37 -75 N ATOM 2648 CA LEU A 507 57.368 -22.674 10.538 1.00 28.03 C ANISOU 2648 CA LEU A 507 4207 3232 3212 -128 57 -14 C ATOM 2649 C LEU A 507 58.043 -21.800 9.495 1.00 31.42 C ANISOU 2649 C LEU A 507 4715 3636 3589 -145 88 17 C ATOM 2650 O LEU A 507 59.271 -21.799 9.360 1.00 27.71 O ANISOU 2650 O LEU A 507 4210 3227 3091 -146 177 80 O ATOM 2651 CB LEU A 507 56.855 -23.950 9.876 1.00 23.56 C ANISOU 2651 CB LEU A 507 3715 2598 2639 -56 47 -26 C ATOM 2652 CG LEU A 507 57.920 -24.785 9.163 1.00 30.08 C ANISOU 2652 CG LEU A 507 4572 3447 3409 3 128 18 C ATOM 2653 CD1 LEU A 507 59.012 -25.184 10.142 1.00 28.24 C ANISOU 2653 CD1 LEU A 507 4213 3327 3191 -12 204 67 C ATOM 2654 CD2 LEU A 507 57.293 -26.027 8.528 1.00 28.96 C ANISOU 2654 CD2 LEU A 507 4497 3224 3281 89 80 -14 C ATOM 2655 N THR A 508 57.229 -21.052 8.762 1.00 26.20 N ANISOU 2655 N THR A 508 4154 2886 2916 -159 15 -20 N ATOM 2656 CA THR A 508 57.727 -20.278 7.627 1.00 28.76 C ANISOU 2656 CA THR A 508 4568 3177 3183 -168 41 25 C ATOM 2657 C THR A 508 58.510 -19.074 8.107 1.00 27.95 C ANISOU 2657 C THR A 508 4377 3120 3124 -247 50 72 C ATOM 2658 O THR A 508 59.442 -18.628 7.455 1.00 27.49 O ANISOU 2658 O THR A 508 4332 3078 3035 -261 117 154 O ATOM 2659 CB THR A 508 56.580 -19.836 6.682 1.00 34.66 C ANISOU 2659 CB THR A 508 5459 3804 3906 -154 -53 -31 C ATOM 2660 OG1 THR A 508 56.174 -20.957 5.891 1.00 42.41 O ANISOU 2660 OG1 THR A 508 6538 4737 4840 -58 -49 -60 O ATOM 2661 CG2 THR A 508 57.040 -18.716 5.747 1.00 33.83 C ANISOU 2661 CG2 THR A 508 5426 3673 3756 -186 -41 30 C ATOM 2662 N ILE A 509 58.117 -18.549 9.258 1.00 30.04 N ANISOU 2662 N ILE A 509 4542 3405 3465 -291 -25 20 N ATOM 2663 CA ILE A 509 58.832 -17.447 9.866 1.00 28.22 C ANISOU 2663 CA ILE A 509 4208 3212 3303 -352 -45 45 C ATOM 2664 C ILE A 509 60.228 -17.928 10.247 1.00 25.83 C ANISOU 2664 C ILE A 509 3809 2999 3004 -341 71 117 C ATOM 2665 O ILE A 509 61.226 -17.281 9.957 1.00 30.05 O ANISOU 2665 O ILE A 509 4309 3543 3566 -376 114 190 O ATOM 2666 CB ILE A 509 58.082 -16.944 11.114 1.00 30.43 C ANISOU 2666 CB ILE A 509 4393 3517 3654 -370 -159 -48 C ATOM 2667 CG1 ILE A 509 56.823 -16.192 10.680 1.00 30.18 C ANISOU 2667 CG1 ILE A 509 4447 3389 3631 -393 -286 -123 C ATOM 2668 CG2 ILE A 509 58.988 -16.081 11.982 1.00 28.31 C ANISOU 2668 CG2 ILE A 509 3985 3305 3465 -402 -181 -35 C ATOM 2669 CD1 ILE A 509 55.859 -15.893 11.818 1.00 29.30 C ANISOU 2669 CD1 ILE A 509 4254 3313 3566 -390 -398 -231 C ATOM 2670 N CYS A 510 60.295 -19.086 10.883 1.00 21.78 N ANISOU 2670 N CYS A 510 3252 2549 2475 -293 119 100 N ATOM 2671 CA CYS A 510 61.587 -19.600 11.331 1.00 33.83 C ANISOU 2671 CA CYS A 510 4687 4159 4009 -279 218 152 C ATOM 2672 C CYS A 510 62.497 -19.925 10.176 1.00 39.77 C ANISOU 2672 C CYS A 510 5501 4911 4699 -261 326 232 C ATOM 2673 O CYS A 510 63.692 -19.638 10.235 1.00 39.94 O ANISOU 2673 O CYS A 510 5450 4978 4748 -280 395 293 O ATOM 2674 CB CYS A 510 61.426 -20.824 12.232 1.00 32.05 C ANISOU 2674 CB CYS A 510 4407 3995 3777 -230 238 123 C ATOM 2675 SG CYS A 510 60.612 -20.430 13.765 1.00 30.52 S ANISOU 2675 SG CYS A 510 4105 3851 3642 -236 138 50 S ATOM 2676 N CYS A 511 61.938 -20.525 9.127 1.00 39.40 N ANISOU 2676 N CYS A 511 5582 4819 4571 -213 336 229 N ATOM 2677 CA CYS A 511 62.746 -20.880 7.970 1.00 39.02 C ANISOU 2677 CA CYS A 511 5597 4790 4440 -172 435 297 C ATOM 2678 C CYS A 511 63.262 -19.643 7.237 1.00 38.31 C ANISOU 2678 C CYS A 511 5524 4684 4349 -224 461 380 C ATOM 2679 O CYS A 511 64.414 -19.614 6.822 1.00 41.81 O ANISOU 2679 O CYS A 511 5930 5185 4769 -221 566 465 O ATOM 2680 CB CYS A 511 61.995 -21.828 7.033 1.00 35.09 C ANISOU 2680 CB CYS A 511 5231 4247 3856 -85 420 258 C ATOM 2681 SG CYS A 511 61.781 -23.495 7.730 1.00 42.09 S ANISOU 2681 SG CYS A 511 6076 5158 4760 -16 411 199 S ATOM 2682 N ASP A 512 62.421 -18.623 7.087 1.00 34.53 N ANISOU 2682 N ASP A 512 5092 4126 3902 -273 363 361 N ATOM 2683 CA ASP A 512 62.890 -17.336 6.559 1.00 38.44 C ANISOU 2683 CA ASP A 512 5580 4593 4430 -339 365 451 C ATOM 2684 C ASP A 512 64.023 -16.745 7.401 1.00 41.64 C ANISOU 2684 C ASP A 512 5824 5046 4952 -400 394 503 C ATOM 2685 O ASP A 512 64.968 -16.185 6.864 1.00 45.63 O ANISOU 2685 O ASP A 512 6294 5567 5476 -433 465 618 O ATOM 2686 CB ASP A 512 61.759 -16.313 6.501 1.00 39.01 C ANISOU 2686 CB ASP A 512 5711 4565 4547 -389 224 400 C ATOM 2687 CG ASP A 512 60.740 -16.633 5.431 1.00 48.64 C ANISOU 2687 CG ASP A 512 7103 5717 5661 -333 192 364 C ATOM 2688 OD1 ASP A 512 61.017 -17.531 4.602 1.00 47.49 O ANISOU 2688 OD1 ASP A 512 7032 5606 5405 -250 282 393 O ATOM 2689 OD2 ASP A 512 59.661 -15.990 5.431 1.00 50.86 O ANISOU 2689 OD2 ASP A 512 7441 5910 5973 -362 67 295 O ATOM 2690 N ALA A 513 63.919 -16.862 8.720 1.00 44.41 N ANISOU 2690 N ALA A 513 6071 5421 5384 -409 335 423 N ATOM 2691 CA ALA A 513 64.892 -16.244 9.619 1.00 40.35 C ANISOU 2691 CA ALA A 513 5400 4937 4994 -452 331 446 C ATOM 2692 C ALA A 513 66.260 -16.907 9.494 1.00 35.16 C ANISOU 2692 C ALA A 513 4681 4357 4321 -428 476 521 C ATOM 2693 O ALA A 513 67.285 -16.246 9.333 1.00 41.85 O ANISOU 2693 O ALA A 513 5447 5207 5246 -471 522 611 O ATOM 2694 CB ALA A 513 64.397 -16.312 11.052 1.00 31.72 C ANISOU 2694 CB ALA A 513 4220 3868 3964 -439 233 332 C ATOM 2695 N VAL A 514 66.259 -18.228 9.562 1.00 34.57 N ANISOU 2695 N VAL A 514 4640 4339 4157 -360 541 483 N ATOM 2696 CA VAL A 514 67.479 -19.011 9.518 1.00 37.16 C ANISOU 2696 CA VAL A 514 4912 4745 4463 -325 666 527 C ATOM 2697 C VAL A 514 68.146 -18.981 8.133 1.00 45.88 C ANISOU 2697 C VAL A 514 6074 5873 5487 -313 781 637 C ATOM 2698 O VAL A 514 69.326 -19.292 7.996 1.00 47.93 O ANISOU 2698 O VAL A 514 6266 6199 5746 -299 889 694 O ATOM 2699 CB VAL A 514 67.200 -20.462 9.956 1.00 37.59 C ANISOU 2699 CB VAL A 514 4989 4844 4450 -252 680 451 C ATOM 2700 CG1 VAL A 514 68.416 -21.332 9.734 1.00 48.67 C ANISOU 2700 CG1 VAL A 514 6352 6324 5815 -208 800 486 C ATOM 2701 CG2 VAL A 514 66.784 -20.499 11.416 1.00 33.98 C ANISOU 2701 CG2 VAL A 514 4447 4394 4068 -259 594 369 C ATOM 2702 N SER A 515 67.402 -18.579 7.111 1.00 46.23 N ANISOU 2702 N SER A 515 6239 5868 5459 -312 758 668 N ATOM 2703 CA SER A 515 67.922 -18.659 5.758 1.00 49.27 C ANISOU 2703 CA SER A 515 6692 6295 5734 -274 869 771 C ATOM 2704 C SER A 515 68.228 -17.291 5.160 1.00 54.81 C ANISOU 2704 C SER A 515 7376 6959 6489 -352 878 900 C ATOM 2705 O SER A 515 68.524 -17.182 3.965 1.00 53.30 O ANISOU 2705 O SER A 515 7250 6805 6197 -322 966 1005 O ATOM 2706 CB SER A 515 66.933 -19.403 4.863 1.00 52.79 C ANISOU 2706 CB SER A 515 7303 6724 6032 -185 848 716 C ATOM 2707 OG SER A 515 65.831 -18.574 4.551 1.00 56.24 O ANISOU 2707 OG SER A 515 7829 7063 6477 -221 743 702 O ATOM 2708 N GLY A 516 68.141 -16.248 5.979 1.00 51.72 N ANISOU 2708 N GLY A 516 6894 6499 6258 -442 779 895 N ATOM 2709 CA GLY A 516 68.426 -14.907 5.507 1.00 53.37 C ANISOU 2709 CA GLY A 516 7069 6653 6556 -525 761 1021 C ATOM 2710 C GLY A 516 67.258 -14.103 4.950 1.00 56.12 C ANISOU 2710 C GLY A 516 7534 6904 6885 -556 646 1017 C ATOM 2711 O GLY A 516 67.376 -12.886 4.774 1.00 57.41 O ANISOU 2711 O GLY A 516 7656 6999 7159 -638 589 1107 O ATOM 2712 N ARG A 517 66.132 -14.759 4.674 1.00 50.05 N ANISOU 2712 N ARG A 517 6907 6116 5993 -491 601 911 N ATOM 2713 CA ARG A 517 64.978 -14.065 4.103 1.00 46.64 C ANISOU 2713 CA ARG A 517 6599 5586 5537 -511 488 890 C ATOM 2714 C ARG A 517 64.310 -13.074 5.065 1.00 53.38 C ANISOU 2714 C ARG A 517 7390 6345 6547 -592 310 808 C ATOM 2715 O ARG A 517 63.571 -12.195 4.628 1.00 56.36 O ANISOU 2715 O ARG A 517 7839 6632 6944 -633 204 812 O ATOM 2716 CB ARG A 517 63.959 -15.061 3.551 1.00 46.25 C ANISOU 2716 CB ARG A 517 6711 5531 5332 -412 478 790 C ATOM 2717 CG ARG A 517 64.480 -15.857 2.355 1.00 53.26 C ANISOU 2717 CG ARG A 517 7684 6502 6050 -312 622 865 C ATOM 2718 CD ARG A 517 63.374 -16.604 1.621 1.00 55.24 C ANISOU 2718 CD ARG A 517 8107 6716 6166 -207 576 768 C ATOM 2719 NE ARG A 517 62.835 -17.700 2.419 1.00 57.79 N ANISOU 2719 NE ARG A 517 8418 7035 6504 -159 529 623 N ATOM 2720 CZ ARG A 517 63.450 -18.865 2.595 1.00 60.29 C ANISOU 2720 CZ ARG A 517 8692 7438 6778 -88 611 603 C ATOM 2721 NH1 ARG A 517 64.629 -19.084 2.026 1.00 65.78 N ANISOU 2721 NH1 ARG A 517 9353 8237 7402 -51 748 705 N ATOM 2722 NH2 ARG A 517 62.891 -19.810 3.343 1.00 55.23 N ANISOU 2722 NH2 ARG A 517 8036 6781 6169 -54 555 487 N ATOM 2723 N ARG A 518 64.585 -13.202 6.363 1.00 54.96 N ANISOU 2723 N ARG A 518 7456 6572 6853 -605 270 730 N ATOM 2724 CA ARG A 518 64.049 -12.272 7.368 1.00 51.76 C ANISOU 2724 CA ARG A 518 6971 6101 6594 -659 96 639 C ATOM 2725 C ARG A 518 65.117 -11.788 8.359 1.00 43.36 C ANISOU 2725 C ARG A 518 5718 5061 5696 -696 81 661 C ATOM 2726 O ARG A 518 65.955 -12.559 8.822 1.00 42.65 O ANISOU 2726 O ARG A 518 5554 5053 5599 -660 185 667 O ATOM 2727 CB ARG A 518 62.865 -12.897 8.125 1.00 53.31 C ANISOU 2727 CB ARG A 518 7207 6303 6745 -610 10 470 C ATOM 2728 CG ARG A 518 62.721 -12.382 9.552 1.00 56.90 C ANISOU 2728 CG ARG A 518 7524 6765 7331 -626 -120 365 C ATOM 2729 CD ARG A 518 61.829 -13.281 10.395 1.00 54.71 C ANISOU 2729 CD ARG A 518 7257 6540 6992 -563 -148 231 C ATOM 2730 NE ARG A 518 60.416 -13.016 10.153 1.00 55.71 N ANISOU 2730 NE ARG A 518 7483 6599 7083 -565 -263 142 N ATOM 2731 CZ ARG A 518 59.620 -12.311 10.958 1.00 45.96 C ANISOU 2731 CZ ARG A 518 6198 5347 5919 -574 -421 30 C ATOM 2732 NH1 ARG A 518 60.085 -11.786 12.104 1.00 33.42 N ANISOU 2732 NH1 ARG A 518 4456 3807 4436 -573 -492 -14 N ATOM 2733 NH2 ARG A 518 58.345 -12.137 10.610 1.00 38.17 N ANISOU 2733 NH2 ARG A 518 5311 4296 4894 -575 -514 -50 N ATOM 2734 N GLN A 519 65.064 -10.499 8.670 1.00 49.82 N ANISOU 2734 N GLN A 519 6459 5797 6672 -763 -64 665 N ATOM 2735 CA GLN A 519 66.006 -9.852 9.573 1.00 57.43 C ANISOU 2735 CA GLN A 519 7240 6755 7827 -792 -119 675 C ATOM 2736 C GLN A 519 65.877 -10.391 10.987 1.00 59.22 C ANISOU 2736 C GLN A 519 7381 7048 8070 -727 -170 519 C ATOM 2737 O GLN A 519 64.824 -10.254 11.618 1.00 60.73 O ANISOU 2737 O GLN A 519 7591 7232 8250 -701 -302 382 O ATOM 2738 CB GLN A 519 65.753 -8.339 9.572 1.00 65.09 C ANISOU 2738 CB GLN A 519 8157 7605 8970 -867 -306 691 C ATOM 2739 CG GLN A 519 66.622 -7.538 10.524 1.00 71.11 C ANISOU 2739 CG GLN A 519 8720 8335 9963 -889 -410 683 C ATOM 2740 CD GLN A 519 68.095 -7.586 10.158 1.00 77.91 C ANISOU 2740 CD GLN A 519 9485 9213 10906 -921 -263 851 C ATOM 2741 OE1 GLN A 519 68.618 -6.672 9.518 1.00 79.79 O ANISOU 2741 OE1 GLN A 519 9672 9369 11275 -999 -281 1003 O ATOM 2742 NE2 GLN A 519 68.770 -8.657 10.559 1.00 80.04 N ANISOU 2742 NE2 GLN A 519 9723 9586 11104 -862 -119 832 N ATOM 2743 N THR A 520 66.948 -11.000 11.485 1.00 53.73 N ANISOU 2743 N THR A 520 6591 6424 7400 -696 -65 542 N ATOM 2744 CA THR A 520 66.968 -11.517 12.855 1.00 50.58 C ANISOU 2744 CA THR A 520 6105 6097 7018 -627 -106 409 C ATOM 2745 C THR A 520 67.488 -10.485 13.848 1.00 54.42 C ANISOU 2745 C THR A 520 6422 6545 7711 -630 -256 359 C ATOM 2746 O THR A 520 67.337 -10.648 15.057 1.00 48.15 O ANISOU 2746 O THR A 520 5551 5805 6937 -561 -335 231 O ATOM 2747 CB THR A 520 67.833 -12.783 12.982 1.00 42.23 C ANISOU 2747 CB THR A 520 5033 5134 5879 -578 68 438 C ATOM 2748 OG1 THR A 520 69.162 -12.501 12.523 1.00 42.56 O ANISOU 2748 OG1 THR A 520 4996 5161 6014 -617 159 565 O ATOM 2749 CG2 THR A 520 67.236 -13.953 12.161 1.00 41.33 C ANISOU 2749 CG2 THR A 520 5077 5063 5563 -547 187 454 C ATOM 2750 N LYS A 521 68.119 -9.433 13.336 1.00 67.94 N ANISOU 2750 N LYS A 521 8069 8164 9581 -703 -299 464 N ATOM 2751 CA LYS A 521 68.629 -8.365 14.191 1.00 74.55 C ANISOU 2751 CA LYS A 521 8738 8939 10651 -705 -469 419 C ATOM 2752 C LYS A 521 67.549 -7.327 14.439 1.00 83.28 C ANISOU 2752 C LYS A 521 9848 9971 11822 -716 -695 318 C ATOM 2753 O LYS A 521 67.331 -6.448 13.611 1.00 90.89 O ANISOU 2753 O LYS A 521 10844 10833 12858 -797 -762 404 O ATOM 2754 CB LYS A 521 69.844 -7.675 13.561 1.00 72.82 C ANISOU 2754 CB LYS A 521 8422 8638 10610 -783 -426 589 C ATOM 2755 CG LYS A 521 71.152 -8.427 13.670 1.00 75.22 C ANISOU 2755 CG LYS A 521 8651 9003 10928 -762 -254 656 C ATOM 2756 CD LYS A 521 72.334 -7.479 13.485 1.00 80.30 C ANISOU 2756 CD LYS A 521 9135 9550 11826 -827 -282 785 C ATOM 2757 CE LYS A 521 72.149 -6.587 12.254 1.00 82.83 C ANISOU 2757 CE LYS A 521 9498 9776 12196 -935 -290 959 C ATOM 2758 NZ LYS A 521 73.137 -5.460 12.193 1.00 78.39 N ANISOU 2758 NZ LYS A 521 8759 9094 11931 -1006 -369 1085 N ATOM 2759 N GLU A 522 66.867 -7.428 15.572 1.00 84.81 N ANISOU 2759 N GLU A 522 10009 10227 11988 -629 -817 140 N ATOM 2760 CA GLU A 522 65.917 -6.393 15.953 1.00 83.95 C ANISOU 2760 CA GLU A 522 9878 10062 11957 -622 -1054 19 C ATOM 2761 C GLU A 522 66.590 -5.371 16.864 1.00 85.38 C ANISOU 2761 C GLU A 522 9868 10189 12382 -587 -1250 -49 C ATOM 2762 O GLU A 522 66.767 -5.608 18.067 1.00 78.40 O ANISOU 2762 O GLU A 522 8888 9389 11511 -478 -1307 -179 O ATOM 2763 CB GLU A 522 64.676 -6.989 16.618 1.00 82.78 C ANISOU 2763 CB GLU A 522 9797 10020 11638 -541 -1088 -138 C ATOM 2764 CG GLU A 522 63.674 -5.944 17.089 1.00 84.39 C ANISOU 2764 CG GLU A 522 9967 10187 11911 -518 -1340 -285 C ATOM 2765 CD GLU A 522 62.250 -6.474 17.145 1.00 84.10 C ANISOU 2765 CD GLU A 522 10045 10220 11687 -484 -1339 -384 C ATOM 2766 OE1 GLU A 522 61.768 -7.004 16.119 1.00 81.08 O ANISOU 2766 OE1 GLU A 522 9816 9810 11182 -543 -1216 -303 O ATOM 2767 OE2 GLU A 522 61.609 -6.346 18.211 1.00 86.16 O ANISOU 2767 OE2 GLU A 522 10239 10567 11929 -391 -1467 -544 O ATOM 2768 N GLY A 523 66.972 -4.243 16.264 1.00 93.04 N ANISOU 2768 N GLY A 523 10784 11016 13552 -675 -1358 45 N ATOM 2769 CA GLY A 523 67.618 -3.152 16.970 1.00 95.72 C ANISOU 2769 CA GLY A 523 10936 11267 14168 -652 -1572 -5 C ATOM 2770 C GLY A 523 69.092 -3.390 17.222 1.00 97.55 C ANISOU 2770 C GLY A 523 11041 11492 14534 -643 -1473 79 C ATOM 2771 O GLY A 523 69.615 -3.012 18.270 1.00 99.92 O ANISOU 2771 O GLY A 523 11186 11783 14997 -557 -1618 -33 O ATOM 2772 N GLY A 524 69.762 -4.021 16.263 1.00 95.81 N ANISOU 2772 N GLY A 524 10883 11279 14243 -721 -1231 267 N ATOM 2773 CA GLY A 524 71.186 -4.284 16.377 1.00 97.36 C ANISOU 2773 CA GLY A 524 10962 11469 14561 -722 -1116 359 C ATOM 2774 C GLY A 524 71.501 -5.506 17.214 1.00 95.94 C ANISOU 2774 C GLY A 524 10786 11431 14235 -615 -989 259 C ATOM 2775 O GLY A 524 72.670 -5.854 17.414 1.00 90.76 O ANISOU 2775 O GLY A 524 10039 10782 13664 -601 -892 308 O ATOM 2776 N TYR A 525 70.447 -6.156 17.705 1.00 97.52 N ANISOU 2776 N TYR A 525 11088 11741 14223 -540 -994 122 N ATOM 2777 CA TYR A 525 70.579 -7.383 18.488 1.00 91.78 C ANISOU 2777 CA TYR A 525 10381 11156 13336 -440 -875 37 C ATOM 2778 C TYR A 525 70.108 -8.583 17.687 1.00 74.39 C ANISOU 2778 C TYR A 525 8352 9037 10876 -472 -655 112 C ATOM 2779 O TYR A 525 68.996 -8.589 17.165 1.00 74.31 O ANISOU 2779 O TYR A 525 8465 9028 10740 -502 -668 106 O ATOM 2780 CB TYR A 525 69.804 -7.264 19.794 1.00 97.90 C ANISOU 2780 CB TYR A 525 11113 12006 14077 -313 -1051 -170 C ATOM 2781 CG TYR A 525 70.345 -6.155 20.654 1.00108.91 C ANISOU 2781 CG TYR A 525 12327 13326 15727 -250 -1283 -268 C ATOM 2782 CD1 TYR A 525 71.508 -6.335 21.394 1.00114.34 C ANISOU 2782 CD1 TYR A 525 12888 14019 16536 -178 -1276 -298 C ATOM 2783 CD2 TYR A 525 69.717 -4.919 20.703 1.00110.98 C ANISOU 2783 CD2 TYR A 525 12542 13500 16126 -259 -1524 -336 C ATOM 2784 CE1 TYR A 525 72.022 -5.321 22.178 1.00118.36 C ANISOU 2784 CE1 TYR A 525 13226 14447 17299 -106 -1507 -398 C ATOM 2785 CE2 TYR A 525 70.224 -3.898 21.482 1.00116.51 C ANISOU 2785 CE2 TYR A 525 13067 14121 17080 -190 -1761 -436 C ATOM 2786 CZ TYR A 525 71.377 -4.104 22.220 1.00120.12 C ANISOU 2786 CZ TYR A 525 13399 14583 17659 -110 -1753 -467 C ATOM 2787 OH TYR A 525 71.891 -3.093 23.003 1.00121.67 O ANISOU 2787 OH TYR A 525 13416 14689 18124 -25 -2007 -578 O ATOM 2788 N ASP A 526 70.968 -9.590 17.584 1.00 57.59 N ANISOU 2788 N ASP A 526 6231 6970 8682 -461 -467 175 N ATOM 2789 CA ASP A 526 70.690 -10.737 16.733 1.00 55.59 C ANISOU 2789 CA ASP A 526 6129 6784 8210 -486 -266 252 C ATOM 2790 C ASP A 526 70.020 -11.870 17.506 1.00 53.34 C ANISOU 2790 C ASP A 526 5904 6619 7743 -396 -230 140 C ATOM 2791 O ASP A 526 70.655 -12.558 18.308 1.00 58.27 O ANISOU 2791 O ASP A 526 6469 7312 8358 -326 -183 92 O ATOM 2792 CB ASP A 526 71.961 -11.227 16.036 1.00 57.60 C ANISOU 2792 CB ASP A 526 6362 7041 8483 -525 -81 390 C ATOM 2793 CG ASP A 526 71.657 -12.064 14.812 1.00 64.97 C ANISOU 2793 CG ASP A 526 7451 8016 9219 -561 95 492 C ATOM 2794 OD1 ASP A 526 70.537 -12.605 14.747 1.00 66.63 O ANISOU 2794 OD1 ASP A 526 7783 8267 9267 -534 89 431 O ATOM 2795 OD2 ASP A 526 72.518 -12.176 13.913 1.00 68.40 O ANISOU 2795 OD2 ASP A 526 7881 8445 9661 -607 233 629 O ATOM 2796 N HIS A 527 68.729 -12.052 17.244 1.00 43.64 N ANISOU 2796 N HIS A 527 4793 5411 6379 -399 -256 104 N ATOM 2797 CA HIS A 527 67.943 -13.085 17.884 1.00 40.54 C ANISOU 2797 CA HIS A 527 4456 5122 5824 -325 -226 20 C ATOM 2798 C HIS A 527 68.006 -14.386 17.116 1.00 41.06 C ANISOU 2798 C HIS A 527 4636 5228 5736 -338 -39 100 C ATOM 2799 O HIS A 527 67.158 -15.252 17.310 1.00 51.92 O ANISOU 2799 O HIS A 527 6084 6663 6979 -300 -12 60 O ATOM 2800 CB HIS A 527 66.488 -12.658 17.955 1.00 45.02 C ANISOU 2800 CB HIS A 527 5085 5685 6336 -322 -349 -58 C ATOM 2801 CG HIS A 527 66.236 -11.528 18.896 1.00 53.80 C ANISOU 2801 CG HIS A 527 6083 6787 7570 -278 -555 -175 C ATOM 2802 ND1 HIS A 527 66.721 -10.259 18.676 1.00 53.97 N ANISOU 2802 ND1 HIS A 527 6027 6702 7778 -324 -678 -158 N ATOM 2803 CD2 HIS A 527 65.531 -11.470 20.049 1.00 59.94 C ANISOU 2803 CD2 HIS A 527 6806 7654 8314 -184 -669 -310 C ATOM 2804 CE1 HIS A 527 66.334 -9.467 19.658 1.00 60.14 C ANISOU 2804 CE1 HIS A 527 6711 7498 8641 -255 -875 -295 C ATOM 2805 NE2 HIS A 527 65.611 -10.178 20.506 1.00 63.72 N ANISOU 2805 NE2 HIS A 527 7177 8080 8952 -164 -868 -391 N ATOM 2806 N ALA A 528 68.995 -14.522 16.244 1.00 31.64 N ANISOU 2806 N ALA A 528 3451 4003 4567 -385 81 212 N ATOM 2807 CA ALA A 528 69.111 -15.704 15.389 1.00 36.16 C ANISOU 2807 CA ALA A 528 4130 4614 4996 -386 245 282 C ATOM 2808 C ALA A 528 68.969 -17.040 16.127 1.00 36.89 C ANISOU 2808 C ALA A 528 4235 4797 4984 -312 298 220 C ATOM 2809 O ALA A 528 68.326 -17.968 15.638 1.00 43.13 O ANISOU 2809 O ALA A 528 5133 5609 5645 -298 357 229 O ATOM 2810 CB ALA A 528 70.410 -15.676 14.645 1.00 36.43 C ANISOU 2810 CB ALA A 528 4127 4633 5081 -422 365 394 C ATOM 2811 N ILE A 529 69.573 -17.154 17.297 1.00 34.02 N ANISOU 2811 N ILE A 529 3760 4482 4683 -259 268 159 N ATOM 2812 CA ILE A 529 69.550 -18.431 17.974 1.00 38.97 C ANISOU 2812 CA ILE A 529 4395 5193 5217 -193 323 121 C ATOM 2813 C ILE A 529 68.189 -18.737 18.607 1.00 35.58 C ANISOU 2813 C ILE A 529 4005 4810 4705 -153 250 57 C ATOM 2814 O ILE A 529 67.886 -19.896 18.874 1.00 38.55 O ANISOU 2814 O ILE A 529 4417 5242 4989 -115 303 56 O ATOM 2815 CB ILE A 529 70.691 -18.578 18.980 1.00 50.15 C ANISOU 2815 CB ILE A 529 5691 6650 6713 -140 327 82 C ATOM 2816 CG1 ILE A 529 70.382 -17.839 20.274 1.00 49.69 C ANISOU 2816 CG1 ILE A 529 5536 6620 6725 -79 181 -19 C ATOM 2817 CG2 ILE A 529 72.004 -18.101 18.360 1.00 59.68 C ANISOU 2817 CG2 ILE A 529 6841 7803 8034 -186 387 148 C ATOM 2818 CD1 ILE A 529 71.244 -18.328 21.404 1.00 52.37 C ANISOU 2818 CD1 ILE A 529 5784 7022 7094 5 184 -75 C ATOM 2819 N SER A 530 67.371 -17.709 18.818 1.00 23.36 N ANISOU 2819 N SER A 530 2444 3237 3196 -163 126 7 N ATOM 2820 CA SER A 530 65.977 -17.934 19.180 1.00 31.17 C ANISOU 2820 CA SER A 530 3477 4264 4101 -137 67 -43 C ATOM 2821 C SER A 530 65.213 -18.611 18.041 1.00 31.52 C ANISOU 2821 C SER A 530 3662 4263 4052 -179 134 12 C ATOM 2822 O SER A 530 64.481 -19.575 18.260 1.00 32.77 O ANISOU 2822 O SER A 530 3859 4462 4129 -148 159 7 O ATOM 2823 CB SER A 530 65.300 -16.628 19.562 1.00 34.53 C ANISOU 2823 CB SER A 530 3857 4669 4592 -136 -90 -120 C ATOM 2824 OG SER A 530 65.959 -16.072 20.679 1.00 48.10 O ANISOU 2824 OG SER A 530 5443 6435 6398 -72 -171 -188 O ATOM 2825 N PHE A 531 65.396 -18.110 16.825 1.00 28.60 N ANISOU 2825 N PHE A 531 3362 3807 3699 -242 158 67 N ATOM 2826 CA PHE A 531 64.753 -18.703 15.663 1.00 28.94 C ANISOU 2826 CA PHE A 531 3542 3803 3652 -264 214 111 C ATOM 2827 C PHE A 531 65.237 -20.124 15.402 1.00 34.89 C ANISOU 2827 C PHE A 531 4330 4593 4334 -228 332 152 C ATOM 2828 O PHE A 531 64.468 -20.968 14.936 1.00 37.71 O ANISOU 2828 O PHE A 531 4776 4935 4618 -210 349 154 O ATOM 2829 CB PHE A 531 64.975 -17.840 14.434 1.00 27.94 C ANISOU 2829 CB PHE A 531 3477 3591 3549 -325 220 172 C ATOM 2830 CG PHE A 531 64.229 -16.554 14.474 1.00 33.13 C ANISOU 2830 CG PHE A 531 4131 4188 4268 -364 85 129 C ATOM 2831 CD1 PHE A 531 62.868 -16.524 14.224 1.00 28.18 C ANISOU 2831 CD1 PHE A 531 3593 3525 3588 -365 14 78 C ATOM 2832 CD2 PHE A 531 64.883 -15.367 14.763 1.00 35.98 C ANISOU 2832 CD2 PHE A 531 4395 4520 4757 -398 14 134 C ATOM 2833 CE1 PHE A 531 62.173 -15.340 14.262 1.00 27.81 C ANISOU 2833 CE1 PHE A 531 3544 3423 3600 -399 -123 26 C ATOM 2834 CE2 PHE A 531 64.187 -14.171 14.798 1.00 36.69 C ANISOU 2834 CE2 PHE A 531 4478 4547 4916 -431 -134 87 C ATOM 2835 CZ PHE A 531 62.830 -14.160 14.544 1.00 33.67 C ANISOU 2835 CZ PHE A 531 4191 4137 4465 -432 -201 29 C ATOM 2836 N GLN A 532 66.500 -20.389 15.722 1.00 32.94 N ANISOU 2836 N GLN A 532 4008 4388 4120 -214 400 177 N ATOM 2837 CA GLN A 532 67.067 -21.712 15.517 1.00 30.74 C ANISOU 2837 CA GLN A 532 3752 4147 3783 -178 499 205 C ATOM 2838 C GLN A 532 66.460 -22.662 16.513 1.00 30.77 C ANISOU 2838 C GLN A 532 3732 4203 3756 -129 471 166 C ATOM 2839 O GLN A 532 66.126 -23.792 16.179 1.00 32.61 O ANISOU 2839 O GLN A 532 4024 4434 3932 -103 504 182 O ATOM 2840 CB GLN A 532 68.584 -21.688 15.652 1.00 40.36 C ANISOU 2840 CB GLN A 532 4887 5395 5054 -176 571 232 C ATOM 2841 CG GLN A 532 69.262 -21.007 14.487 1.00 58.51 C ANISOU 2841 CG GLN A 532 7209 7652 7372 -222 630 304 C ATOM 2842 CD GLN A 532 70.756 -20.864 14.684 1.00 72.87 C ANISOU 2842 CD GLN A 532 8924 9496 9269 -226 697 332 C ATOM 2843 OE1 GLN A 532 71.445 -20.223 13.880 1.00 72.99 O ANISOU 2843 OE1 GLN A 532 8924 9486 9322 -267 751 406 O ATOM 2844 NE2 GLN A 532 71.270 -21.459 15.761 1.00 76.35 N ANISOU 2844 NE2 GLN A 532 9286 9985 9737 -182 694 279 N ATOM 2845 N ASP A 533 66.284 -22.176 17.733 1.00 29.62 N ANISOU 2845 N ASP A 533 3495 4106 3652 -109 403 118 N ATOM 2846 CA ASP A 533 65.652 -22.956 18.770 1.00 31.91 C ANISOU 2846 CA ASP A 533 3750 4464 3908 -59 378 97 C ATOM 2847 C ASP A 533 64.210 -23.310 18.373 1.00 34.25 C ANISOU 2847 C ASP A 533 4128 4729 4159 -69 343 102 C ATOM 2848 O ASP A 533 63.809 -24.470 18.470 1.00 39.88 O ANISOU 2848 O ASP A 533 4861 5453 4840 -45 368 131 O ATOM 2849 CB ASP A 533 65.706 -22.184 20.092 1.00 42.11 C ANISOU 2849 CB ASP A 533 4929 5829 5242 -20 303 38 C ATOM 2850 CG ASP A 533 65.198 -22.994 21.272 1.00 51.58 C ANISOU 2850 CG ASP A 533 6078 7128 6394 45 292 33 C ATOM 2851 OD1 ASP A 533 65.221 -24.240 21.209 1.00 57.81 O ANISOU 2851 OD1 ASP A 533 6895 7926 7145 56 353 84 O ATOM 2852 OD2 ASP A 533 64.780 -22.377 22.269 1.00 51.78 O ANISOU 2852 OD2 ASP A 533 6029 7226 6421 92 217 -20 O ATOM 2853 N TRP A 534 63.438 -22.337 17.890 1.00 29.83 N ANISOU 2853 N TRP A 534 3611 4115 3609 -105 279 74 N ATOM 2854 CA TRP A 534 62.041 -22.622 17.523 1.00 30.29 C ANISOU 2854 CA TRP A 534 3742 4132 3636 -111 238 66 C ATOM 2855 C TRP A 534 61.959 -23.576 16.335 1.00 25.37 C ANISOU 2855 C TRP A 534 3227 3433 2978 -114 291 108 C ATOM 2856 O TRP A 534 61.077 -24.435 16.252 1.00 24.56 O ANISOU 2856 O TRP A 534 3160 3306 2864 -95 276 116 O ATOM 2857 CB TRP A 534 61.276 -21.331 17.208 1.00 23.44 C ANISOU 2857 CB TRP A 534 2903 3214 2789 -148 147 15 C ATOM 2858 CG TRP A 534 61.286 -20.392 18.350 1.00 27.73 C ANISOU 2858 CG TRP A 534 3335 3831 3370 -128 68 -45 C ATOM 2859 CD1 TRP A 534 61.193 -20.709 19.686 1.00 25.58 C ANISOU 2859 CD1 TRP A 534 2960 3675 3085 -67 54 -67 C ATOM 2860 CD2 TRP A 534 61.367 -18.976 18.281 1.00 32.08 C ANISOU 2860 CD2 TRP A 534 3862 4348 3978 -156 -21 -94 C ATOM 2861 NE1 TRP A 534 61.230 -19.567 20.445 1.00 29.09 N ANISOU 2861 NE1 TRP A 534 3318 4167 3567 -42 -42 -141 N ATOM 2862 CE2 TRP A 534 61.341 -18.488 19.606 1.00 34.38 C ANISOU 2862 CE2 TRP A 534 4032 4738 4293 -100 -98 -162 C ATOM 2863 CE3 TRP A 534 61.470 -18.066 17.230 1.00 30.51 C ANISOU 2863 CE3 TRP A 534 3730 4046 3818 -218 -52 -84 C ATOM 2864 CZ2 TRP A 534 61.414 -17.137 19.897 1.00 36.02 C ANISOU 2864 CZ2 TRP A 534 4178 4933 4573 -101 -218 -233 C ATOM 2865 CZ3 TRP A 534 61.553 -16.723 17.527 1.00 32.09 C ANISOU 2865 CZ3 TRP A 534 3867 4227 4097 -233 -166 -137 C ATOM 2866 CH2 TRP A 534 61.517 -16.271 18.846 1.00 33.66 C ANISOU 2866 CH2 TRP A 534 3942 4516 4331 -174 -255 -218 C ATOM 2867 N LEU A 535 62.889 -23.414 15.412 1.00 22.59 N ANISOU 2867 N LEU A 535 2921 3046 2616 -129 348 135 N ATOM 2868 CA LEU A 535 62.913 -24.237 14.222 1.00 24.13 C ANISOU 2868 CA LEU A 535 3218 3184 2765 -109 392 163 C ATOM 2869 C LEU A 535 63.217 -25.672 14.606 1.00 27.42 C ANISOU 2869 C LEU A 535 3605 3636 3176 -62 428 181 C ATOM 2870 O LEU A 535 62.604 -26.617 14.098 1.00 31.57 O ANISOU 2870 O LEU A 535 4193 4113 3690 -30 409 183 O ATOM 2871 CB LEU A 535 63.967 -23.722 13.257 1.00 21.96 C ANISOU 2871 CB LEU A 535 2976 2897 2469 -125 458 197 C ATOM 2872 CG LEU A 535 64.189 -24.562 12.011 1.00 33.78 C ANISOU 2872 CG LEU A 535 4571 4365 3899 -81 511 220 C ATOM 2873 CD1 LEU A 535 62.870 -24.728 11.263 1.00 41.11 C ANISOU 2873 CD1 LEU A 535 5613 5208 4799 -61 443 191 C ATOM 2874 CD2 LEU A 535 65.215 -23.874 11.157 1.00 32.76 C ANISOU 2874 CD2 LEU A 535 4456 4248 3744 -98 586 270 C ATOM 2875 N LYS A 536 64.145 -25.822 15.534 1.00 22.28 N ANISOU 2875 N LYS A 536 2857 3063 2547 -54 464 190 N ATOM 2876 CA LYS A 536 64.572 -27.132 15.983 1.00 29.85 C ANISOU 2876 CA LYS A 536 3779 4056 3505 -14 493 210 C ATOM 2877 C LYS A 536 63.414 -27.856 16.678 1.00 29.84 C ANISOU 2877 C LYS A 536 3758 4055 3523 2 436 222 C ATOM 2878 O LYS A 536 63.243 -29.066 16.533 1.00 31.45 O ANISOU 2878 O LYS A 536 3978 4234 3740 32 429 247 O ATOM 2879 CB LYS A 536 65.785 -26.976 16.898 1.00 36.08 C ANISOU 2879 CB LYS A 536 4468 4924 4317 -7 534 208 C ATOM 2880 CG LYS A 536 66.210 -28.215 17.640 1.00 53.10 C ANISOU 2880 CG LYS A 536 6572 7125 6478 33 549 225 C ATOM 2881 CD LYS A 536 67.433 -27.899 18.525 1.00 64.46 C ANISOU 2881 CD LYS A 536 7918 8633 7942 45 582 208 C ATOM 2882 CE LYS A 536 67.909 -29.123 19.290 1.00 61.23 C ANISOU 2882 CE LYS A 536 7462 8267 7537 86 592 223 C ATOM 2883 NZ LYS A 536 67.723 -30.343 18.459 1.00 57.46 N ANISOU 2883 NZ LYS A 536 7050 7736 7045 100 592 246 N ATOM 2884 N LYS A 537 62.587 -27.110 17.397 1.00 23.79 N ANISOU 2884 N LYS A 537 2952 3318 2769 -15 389 207 N ATOM 2885 CA LYS A 537 61.434 -27.715 18.049 1.00 26.14 C ANISOU 2885 CA LYS A 537 3218 3628 3086 -2 345 231 C ATOM 2886 C LYS A 537 60.411 -28.183 17.023 1.00 25.88 C ANISOU 2886 C LYS A 537 3278 3483 3071 -6 304 232 C ATOM 2887 O LYS A 537 59.907 -29.296 17.104 1.00 28.19 O ANISOU 2887 O LYS A 537 3563 3745 3403 15 283 273 O ATOM 2888 CB LYS A 537 60.798 -26.730 19.032 1.00 24.16 C ANISOU 2888 CB LYS A 537 2897 3453 2831 -6 303 203 C ATOM 2889 CG LYS A 537 61.745 -26.332 20.141 1.00 29.45 C ANISOU 2889 CG LYS A 537 3468 4234 3490 21 324 191 C ATOM 2890 CD LYS A 537 61.250 -25.089 20.872 1.00 34.86 C ANISOU 2890 CD LYS A 537 4093 4984 4168 31 262 132 C ATOM 2891 CE LYS A 537 60.464 -25.450 22.087 1.00 33.32 C ANISOU 2891 CE LYS A 537 3811 4901 3949 78 243 155 C ATOM 2892 NZ LYS A 537 61.393 -25.838 23.169 1.00 35.54 N ANISOU 2892 NZ LYS A 537 4006 5289 4211 136 277 175 N ATOM 2893 N LEU A 538 60.128 -27.325 16.051 1.00 23.84 N ANISOU 2893 N LEU A 538 3107 3156 2794 -28 283 187 N ATOM 2894 CA LEU A 538 59.185 -27.634 14.998 1.00 29.50 C ANISOU 2894 CA LEU A 538 3925 3758 3524 -19 234 169 C ATOM 2895 C LEU A 538 59.667 -28.816 14.163 1.00 31.23 C ANISOU 2895 C LEU A 538 4199 3923 3745 29 250 186 C ATOM 2896 O LEU A 538 58.896 -29.734 13.852 1.00 30.53 O ANISOU 2896 O LEU A 538 4137 3757 3708 60 195 191 O ATOM 2897 CB LEU A 538 58.961 -26.390 14.114 1.00 33.09 C ANISOU 2897 CB LEU A 538 4468 4159 3945 -48 212 120 C ATOM 2898 CG LEU A 538 58.144 -25.288 14.801 1.00 31.47 C ANISOU 2898 CG LEU A 538 4221 3980 3755 -86 155 81 C ATOM 2899 CD1 LEU A 538 58.261 -23.882 14.170 1.00 29.31 C ANISOU 2899 CD1 LEU A 538 4005 3671 3460 -125 129 41 C ATOM 2900 CD2 LEU A 538 56.726 -25.720 14.850 1.00 26.25 C ANISOU 2900 CD2 LEU A 538 3574 3263 3136 -78 89 66 C ATOM 2901 N HIS A 539 60.944 -28.791 13.801 1.00 25.80 N ANISOU 2901 N HIS A 539 3519 3273 3011 40 315 189 N ATOM 2902 CA HIS A 539 61.523 -29.877 13.021 1.00 31.30 C ANISOU 2902 CA HIS A 539 4258 3938 3695 99 327 191 C ATOM 2903 C HIS A 539 61.478 -31.201 13.784 1.00 34.76 C ANISOU 2903 C HIS A 539 4624 4385 4200 124 299 226 C ATOM 2904 O HIS A 539 61.323 -32.278 13.196 1.00 30.40 O ANISOU 2904 O HIS A 539 4106 3765 3681 179 249 219 O ATOM 2905 CB HIS A 539 62.967 -29.550 12.641 1.00 30.87 C ANISOU 2905 CB HIS A 539 4203 3948 3579 104 413 192 C ATOM 2906 CG HIS A 539 63.661 -30.650 11.898 1.00 40.13 C ANISOU 2906 CG HIS A 539 5407 5113 4728 176 425 182 C ATOM 2907 ND1 HIS A 539 64.317 -31.682 12.538 1.00 51.23 N ANISOU 2907 ND1 HIS A 539 6741 6557 6167 199 430 195 N ATOM 2908 CD2 HIS A 539 63.819 -30.866 10.569 1.00 33.91 C ANISOU 2908 CD2 HIS A 539 4714 4292 3880 240 425 153 C ATOM 2909 CE1 HIS A 539 64.845 -32.491 11.633 1.00 46.61 C ANISOU 2909 CE1 HIS A 539 6200 5959 5550 272 425 166 C ATOM 2910 NE2 HIS A 539 64.555 -32.019 10.432 1.00 41.26 N ANISOU 2910 NE2 HIS A 539 5622 5244 4810 305 425 140 N ATOM 2911 N SER A 540 61.626 -31.125 15.100 1.00 38.13 N ANISOU 2911 N SER A 540 4946 4893 4648 92 321 264 N ATOM 2912 CA SER A 540 61.567 -32.335 15.908 1.00 39.58 C ANISOU 2912 CA SER A 540 5054 5091 4895 110 296 318 C ATOM 2913 C SER A 540 60.145 -32.916 15.905 1.00 34.60 C ANISOU 2913 C SER A 540 4423 4376 4346 113 215 349 C ATOM 2914 O SER A 540 59.957 -34.135 15.798 1.00 34.07 O ANISOU 2914 O SER A 540 4342 4247 4357 145 160 382 O ATOM 2915 CB SER A 540 62.049 -32.051 17.332 1.00 38.16 C ANISOU 2915 CB SER A 540 4766 5031 4702 89 341 354 C ATOM 2916 OG SER A 540 61.922 -33.198 18.150 1.00 43.66 O ANISOU 2916 OG SER A 540 5389 5744 5455 105 318 423 O ATOM 2917 N ARG A 541 59.151 -32.039 16.014 1.00 27.21 N ANISOU 2917 N ARG A 541 3498 3433 3409 81 197 335 N ATOM 2918 CA ARG A 541 57.754 -32.473 16.033 1.00 22.54 C ANISOU 2918 CA ARG A 541 2897 2763 2906 79 124 361 C ATOM 2919 C ARG A 541 57.372 -33.072 14.694 1.00 21.94 C ANISOU 2919 C ARG A 541 2921 2539 2877 124 51 316 C ATOM 2920 O ARG A 541 56.753 -34.125 14.628 1.00 22.03 O ANISOU 2920 O ARG A 541 2908 2463 2998 150 -22 351 O ATOM 2921 CB ARG A 541 56.810 -31.304 16.344 1.00 18.22 C ANISOU 2921 CB ARG A 541 2345 2242 2337 40 115 333 C ATOM 2922 CG ARG A 541 55.315 -31.728 16.489 1.00 18.41 C ANISOU 2922 CG ARG A 541 2339 2195 2462 35 46 365 C ATOM 2923 CD ARG A 541 55.167 -32.874 17.521 1.00 24.61 C ANISOU 2923 CD ARG A 541 3000 3024 3327 39 49 483 C ATOM 2924 NE ARG A 541 55.483 -32.392 18.864 1.00 26.94 N ANISOU 2924 NE ARG A 541 3192 3492 3553 25 116 529 N ATOM 2925 CZ ARG A 541 54.587 -31.905 19.719 1.00 27.01 C ANISOU 2925 CZ ARG A 541 3122 3585 3557 11 119 557 C ATOM 2926 NH1 ARG A 541 53.302 -31.861 19.389 1.00 24.71 N ANISOU 2926 NH1 ARG A 541 2837 3213 3337 -2 64 551 N ATOM 2927 NH2 ARG A 541 54.974 -31.473 20.911 1.00 28.13 N ANISOU 2927 NH2 ARG A 541 3173 3894 3620 23 173 585 N ATOM 2928 N VAL A 542 57.727 -32.374 13.628 1.00 27.06 N ANISOU 2928 N VAL A 542 3678 3157 3446 141 64 241 N ATOM 2929 CA VAL A 542 57.360 -32.788 12.289 1.00 23.43 C ANISOU 2929 CA VAL A 542 3326 2570 3005 205 -7 182 C ATOM 2930 C VAL A 542 57.967 -34.157 11.942 1.00 33.16 C ANISOU 2930 C VAL A 542 4550 3766 4284 276 -46 188 C ATOM 2931 O VAL A 542 57.269 -35.028 11.431 1.00 36.14 O ANISOU 2931 O VAL A 542 4947 4022 4760 331 -150 172 O ATOM 2932 CB VAL A 542 57.752 -31.712 11.277 1.00 25.78 C ANISOU 2932 CB VAL A 542 3737 2872 3187 214 32 118 C ATOM 2933 CG1 VAL A 542 57.632 -32.230 9.831 1.00 25.59 C ANISOU 2933 CG1 VAL A 542 3830 2744 3150 311 -31 54 C ATOM 2934 CG2 VAL A 542 56.878 -30.476 11.503 1.00 19.33 C ANISOU 2934 CG2 VAL A 542 2935 2050 2358 152 24 98 C ATOM 2935 N THR A 543 59.253 -34.330 12.249 1.00 27.63 N ANISOU 2935 N THR A 543 3812 3164 3524 277 26 206 N ATOM 2936 CA THR A 543 59.969 -35.594 12.114 1.00 25.98 C ANISOU 2936 CA THR A 543 3575 2941 3353 338 -10 208 C ATOM 2937 C THR A 543 59.285 -36.743 12.857 1.00 29.03 C ANISOU 2937 C THR A 543 3871 3264 3894 334 -98 277 C ATOM 2938 O THR A 543 58.985 -37.767 12.259 1.00 33.10 O ANISOU 2938 O THR A 543 4401 3670 4504 402 -209 255 O ATOM 2939 CB THR A 543 61.401 -35.468 12.662 1.00 34.16 C ANISOU 2939 CB THR A 543 4560 4106 4312 318 90 224 C ATOM 2940 OG1 THR A 543 62.148 -34.589 11.818 1.00 34.96 O ANISOU 2940 OG1 THR A 543 4736 4256 4290 333 165 172 O ATOM 2941 CG2 THR A 543 62.110 -36.844 12.739 1.00 25.71 C ANISOU 2941 CG2 THR A 543 3445 3027 3297 373 40 228 C ATOM 2942 N LYS A 544 59.040 -36.574 14.154 1.00 29.69 N ANISOU 2942 N LYS A 544 3855 3418 4006 261 -55 364 N ATOM 2943 CA LYS A 544 58.324 -37.590 14.932 1.00 27.22 C ANISOU 2943 CA LYS A 544 3443 3057 3841 248 -125 460 C ATOM 2944 C LYS A 544 56.918 -37.914 14.402 1.00 28.04 C ANISOU 2944 C LYS A 544 3566 3013 4076 264 -235 459 C ATOM 2945 O LYS A 544 56.458 -39.032 14.547 1.00 31.24 O ANISOU 2945 O LYS A 544 3908 3325 4636 282 -331 519 O ATOM 2946 CB LYS A 544 58.166 -37.147 16.379 1.00 25.76 C ANISOU 2946 CB LYS A 544 3155 2998 3636 179 -47 555 C ATOM 2947 CG LYS A 544 59.426 -37.084 17.208 1.00 31.75 C ANISOU 2947 CG LYS A 544 3863 3890 4310 168 37 577 C ATOM 2948 CD LYS A 544 59.073 -36.411 18.547 1.00 29.85 C ANISOU 2948 CD LYS A 544 3533 3778 4030 122 105 648 C ATOM 2949 CE LYS A 544 60.247 -36.362 19.478 1.00 35.53 C ANISOU 2949 CE LYS A 544 4197 4626 4676 124 176 668 C ATOM 2950 NZ LYS A 544 59.899 -35.623 20.738 1.00 40.34 N ANISOU 2950 NZ LYS A 544 4724 5372 5230 105 232 718 N ATOM 2951 N GLU A 545 56.224 -36.930 13.830 1.00 25.48 N ANISOU 2951 N GLU A 545 3320 2658 3705 257 -228 394 N ATOM 2952 CA GLU A 545 54.834 -37.116 13.416 1.00 21.60 C ANISOU 2952 CA GLU A 545 2841 2024 3340 268 -329 386 C ATOM 2953 C GLU A 545 54.677 -37.168 11.899 1.00 22.26 C ANISOU 2953 C GLU A 545 3059 1978 3421 357 -416 263 C ATOM 2954 O GLU A 545 53.563 -37.017 11.386 1.00 27.33 O ANISOU 2954 O GLU A 545 3744 2502 4140 374 -494 222 O ATOM 2955 CB GLU A 545 53.929 -36.003 13.987 1.00 28.42 C ANISOU 2955 CB GLU A 545 3685 2941 4173 199 -278 400 C ATOM 2956 CG GLU A 545 53.458 -36.237 15.428 1.00 37.69 C ANISOU 2956 CG GLU A 545 4708 4202 5410 138 -241 533 C ATOM 2957 CD GLU A 545 52.554 -37.477 15.562 1.00 52.04 C ANISOU 2957 CD GLU A 545 6441 5893 7439 147 -344 623 C ATOM 2958 OE1 GLU A 545 53.077 -38.576 15.886 1.00 52.57 O ANISOU 2958 OE1 GLU A 545 6441 5948 7584 162 -373 702 O ATOM 2959 OE2 GLU A 545 51.321 -37.358 15.329 1.00 53.45 O ANISOU 2959 OE2 GLU A 545 6615 5975 7720 140 -405 615 O ATOM 2960 N ARG A 546 55.778 -37.398 11.185 1.00 24.40 N ANISOU 2960 N ARG A 546 3254 2732 3286 693 818 167 N ATOM 2961 CA ARG A 546 55.769 -37.334 9.727 1.00 29.06 C ANISOU 2961 CA ARG A 546 4054 3355 3633 643 879 21 C ATOM 2962 C ARG A 546 54.700 -38.227 9.077 1.00 28.84 C ANISOU 2962 C ARG A 546 4191 3189 3577 627 765 -118 C ATOM 2963 O ARG A 546 54.102 -37.864 8.072 1.00 31.16 O ANISOU 2963 O ARG A 546 4673 3505 3660 543 709 -184 O ATOM 2964 CB ARG A 546 57.162 -37.657 9.158 1.00 30.92 C ANISOU 2964 CB ARG A 546 4268 3646 3832 712 1124 -84 C ATOM 2965 CG ARG A 546 57.548 -39.115 9.254 1.00 40.15 C ANISOU 2965 CG ARG A 546 5386 4684 5184 826 1207 -216 C ATOM 2966 CD ARG A 546 59.042 -39.328 9.006 1.00 49.72 C ANISOU 2966 CD ARG A 546 6521 5961 6408 903 1448 -290 C ATOM 2967 NE ARG A 546 59.402 -40.743 8.914 1.00 59.53 N ANISOU 2967 NE ARG A 546 7735 7077 7808 1007 1526 -445 N ATOM 2968 CZ ARG A 546 59.389 -41.439 7.776 1.00 71.95 C ANISOU 2968 CZ ARG A 546 9452 8610 9276 1012 1586 -641 C ATOM 2969 NH1 ARG A 546 59.029 -40.857 6.634 1.00 73.15 N ANISOU 2969 NH1 ARG A 546 9791 8840 9161 916 1579 -704 N ATOM 2970 NH2 ARG A 546 59.732 -42.721 7.773 1.00 76.53 N ANISOU 2970 NH2 ARG A 546 9986 9072 10020 1110 1649 -777 N ATOM 2971 N HIS A 547 54.450 -39.391 9.652 1.00 27.37 N ANISOU 2971 N HIS A 547 3935 2858 3606 707 726 -160 N ATOM 2972 CA HIS A 547 53.473 -40.297 9.061 1.00 34.73 C ANISOU 2972 CA HIS A 547 5016 3655 4526 702 624 -296 C ATOM 2973 C HIS A 547 52.040 -39.783 9.124 1.00 36.07 C ANISOU 2973 C HIS A 547 5284 3794 4625 602 395 -234 C ATOM 2974 O HIS A 547 51.329 -39.837 8.125 1.00 43.23 O ANISOU 2974 O HIS A 547 6386 4672 5368 545 334 -339 O ATOM 2975 CB HIS A 547 53.586 -41.693 9.659 1.00 34.55 C ANISOU 2975 CB HIS A 547 4889 3481 4756 813 637 -357 C ATOM 2976 CG HIS A 547 54.869 -42.378 9.309 1.00 52.05 C ANISOU 2976 CG HIS A 547 7051 5702 7022 909 853 -472 C ATOM 2977 ND1 HIS A 547 55.203 -42.712 8.012 1.00 54.57 N ANISOU 2977 ND1 HIS A 547 7516 6036 7180 911 969 -653 N ATOM 2978 CD2 HIS A 547 55.905 -42.786 10.082 1.00 58.32 C ANISOU 2978 CD2 HIS A 547 7659 6491 8010 1005 973 -438 C ATOM 2979 CE1 HIS A 547 56.381 -43.309 8.005 1.00 57.15 C ANISOU 2979 CE1 HIS A 547 7746 6365 7602 1003 1149 -731 C ATOM 2980 NE2 HIS A 547 56.830 -43.365 9.247 1.00 60.44 N ANISOU 2980 NE2 HIS A 547 7963 6765 8235 1063 1155 -603 N ATOM 2981 N ARG A 548 51.615 -39.281 10.276 1.00 29.91 N ANISOU 2981 N ARG A 548 4374 3025 3968 579 269 -69 N ATOM 2982 CA ARG A 548 50.281 -38.702 10.359 1.00 29.82 C ANISOU 2982 CA ARG A 548 4448 2996 3888 479 50 -10 C ATOM 2983 C ARG A 548 50.178 -37.424 9.528 1.00 32.20 C ANISOU 2983 C ARG A 548 4881 3428 3927 370 35 14 C ATOM 2984 O ARG A 548 49.169 -37.208 8.835 1.00 26.99 O ANISOU 2984 O ARG A 548 4395 2736 3123 288 -97 -40 O ATOM 2985 CB ARG A 548 49.845 -38.479 11.813 1.00 26.98 C ANISOU 2985 CB ARG A 548 3905 2621 3724 476 -85 154 C ATOM 2986 CG ARG A 548 49.062 -39.684 12.382 1.00 38.97 C ANISOU 2986 CG ARG A 548 5395 3972 5439 522 -199 112 C ATOM 2987 CD ARG A 548 48.669 -39.525 13.865 1.00 32.63 C ANISOU 2987 CD ARG A 548 4400 3159 4838 517 -327 273 C ATOM 2988 NE ARG A 548 49.772 -39.906 14.741 1.00 38.71 N ANISOU 2988 NE ARG A 548 4965 3945 5799 612 -193 340 N ATOM 2989 CZ ARG A 548 50.031 -41.148 15.160 1.00 35.86 C ANISOU 2989 CZ ARG A 548 4527 3464 5634 705 -151 290 C ATOM 2990 NH1 ARG A 548 49.251 -42.173 14.805 1.00 34.43 N ANISOU 2990 NH1 ARG A 548 4452 3138 5491 719 -234 173 N ATOM 2991 NH2 ARG A 548 51.087 -41.366 15.939 1.00 27.61 N ANISOU 2991 NH2 ARG A 548 3296 2444 4752 784 -28 358 N ATOM 2992 N LEU A 549 51.232 -36.601 9.563 1.00 29.93 N ANISOU 2992 N LEU A 549 4513 3282 3577 369 171 89 N ATOM 2993 CA LEU A 549 51.211 -35.310 8.865 1.00 29.16 C ANISOU 2993 CA LEU A 549 4521 3318 3241 262 155 133 C ATOM 2994 C LEU A 549 51.212 -35.481 7.349 1.00 31.25 C ANISOU 2994 C LEU A 549 5011 3589 3276 224 223 -29 C ATOM 2995 O LEU A 549 50.777 -34.598 6.623 1.00 28.58 O ANISOU 2995 O LEU A 549 4813 3318 2729 118 153 -20 O ATOM 2996 CB LEU A 549 52.398 -34.421 9.265 1.00 27.02 C ANISOU 2996 CB LEU A 549 4105 3199 2961 275 294 251 C ATOM 2997 CG LEU A 549 52.465 -33.884 10.693 1.00 27.69 C ANISOU 2997 CG LEU A 549 3969 3323 3227 291 228 434 C ATOM 2998 CD1 LEU A 549 53.863 -33.371 10.995 1.00 25.41 C ANISOU 2998 CD1 LEU A 549 3537 3162 2956 340 418 510 C ATOM 2999 CD2 LEU A 549 51.413 -32.806 10.926 1.00 24.64 C ANISOU 2999 CD2 LEU A 549 3614 2979 2770 176 15 543 C ATOM 3000 N SER A 550 51.718 -36.607 6.863 1.00 31.06 N ANISOU 3000 N SER A 550 5017 3496 3290 307 359 -179 N ATOM 3001 CA SER A 550 51.816 -36.793 5.422 1.00 29.68 C ANISOU 3001 CA SER A 550 5042 3338 2898 273 441 -340 C ATOM 3002 C SER A 550 50.443 -37.131 4.805 1.00 34.43 C ANISOU 3002 C SER A 550 5832 3830 3419 215 266 -428 C ATOM 3003 O SER A 550 50.279 -37.110 3.591 1.00 37.22 O ANISOU 3003 O SER A 550 6373 4202 3568 162 291 -546 O ATOM 3004 CB SER A 550 52.899 -37.823 5.073 1.00 28.40 C ANISOU 3004 CB SER A 550 4839 3154 2798 380 654 -479 C ATOM 3005 OG SER A 550 52.509 -39.138 5.435 1.00 40.49 O ANISOU 3005 OG SER A 550 6336 4523 4526 467 615 -563 O ATOM 3006 N ARG A 551 49.460 -37.404 5.660 1.00 36.12 N ANISOU 3006 N ARG A 551 5995 3938 3792 220 88 -368 N ATOM 3007 CA ARG A 551 48.068 -37.582 5.245 1.00 38.46 C ANISOU 3007 CA ARG A 551 6454 4132 4026 157 -103 -427 C ATOM 3008 C ARG A 551 47.364 -36.269 4.860 1.00 36.19 C ANISOU 3008 C ARG A 551 6283 3927 3540 20 -244 -350 C ATOM 3009 O ARG A 551 46.313 -36.298 4.231 1.00 34.24 O ANISOU 3009 O ARG A 551 6208 3614 3187 -44 -381 -419 O ATOM 3010 CB ARG A 551 47.264 -38.244 6.378 1.00 35.36 C ANISOU 3010 CB ARG A 551 5952 3607 3874 202 -252 -378 C ATOM 3011 CG ARG A 551 47.717 -39.648 6.720 1.00 39.18 C ANISOU 3011 CG ARG A 551 6345 3980 4562 329 -154 -464 C ATOM 3012 CD ARG A 551 47.073 -40.140 8.000 1.00 31.51 C ANISOU 3012 CD ARG A 551 5233 2904 3834 365 -294 -378 C ATOM 3013 NE ARG A 551 45.632 -39.973 7.975 1.00 36.96 N ANISOU 3013 NE ARG A 551 6036 3523 4485 286 -514 -376 N ATOM 3014 CZ ARG A 551 44.857 -40.006 9.054 1.00 39.00 C ANISOU 3014 CZ ARG A 551 6193 3723 4903 274 -676 -278 C ATOM 3015 NH1 ARG A 551 45.394 -40.217 10.259 1.00 30.19 N ANISOU 3015 NH1 ARG A 551 4859 2612 3999 335 -642 -170 N ATOM 3016 NH2 ARG A 551 43.546 -39.823 8.919 1.00 36.89 N ANISOU 3016 NH2 ARG A 551 6043 3395 4581 197 -873 -292 N ATOM 3017 N PHE A 552 47.922 -35.131 5.267 1.00 35.58 N ANISOU 3017 N PHE A 552 6108 3986 3423 -22 -219 -207 N ATOM 3018 CA PHE A 552 47.292 -33.827 5.034 1.00 29.59 C ANISOU 3018 CA PHE A 552 5433 3307 2501 -151 -365 -118 C ATOM 3019 C PHE A 552 48.107 -32.927 4.131 1.00 34.07 C ANISOU 3019 C PHE A 552 6079 4025 2840 -213 -242 -112 C ATOM 3020 O PHE A 552 49.332 -33.011 4.117 1.00 33.04 O ANISOU 3020 O PHE A 552 5860 3973 2719 -154 -43 -113 O ATOM 3021 CB PHE A 552 46.999 -33.137 6.360 1.00 20.12 C ANISOU 3021 CB PHE A 552 4053 2135 1456 -167 -493 60 C ATOM 3022 CG PHE A 552 46.215 -34.007 7.297 1.00 30.43 C ANISOU 3022 CG PHE A 552 5273 3301 2986 -113 -614 60 C ATOM 3023 CD1 PHE A 552 44.835 -33.943 7.324 1.00 29.76 C ANISOU 3023 CD1 PHE A 552 5283 3132 2894 -181 -834 48 C ATOM 3024 CD2 PHE A 552 46.859 -34.938 8.104 1.00 27.46 C ANISOU 3024 CD2 PHE A 552 4730 2875 2828 5 -505 64 C ATOM 3025 CE1 PHE A 552 44.107 -34.772 8.161 1.00 35.89 C ANISOU 3025 CE1 PHE A 552 5984 3781 3870 -136 -944 44 C ATOM 3026 CE2 PHE A 552 46.145 -35.764 8.953 1.00 30.43 C ANISOU 3026 CE2 PHE A 552 5030 3125 3409 49 -618 67 C ATOM 3027 CZ PHE A 552 44.761 -35.687 8.977 1.00 33.52 C ANISOU 3027 CZ PHE A 552 5515 3436 3785 -22 -837 56 C ATOM 3028 N SER A 553 47.411 -32.084 3.367 1.00 31.45 N ANISOU 3028 N SER A 553 5916 3730 2304 -335 -365 -109 N ATOM 3029 CA SER A 553 48.066 -31.065 2.566 1.00 33.78 C ANISOU 3029 CA SER A 553 6286 4176 2374 -416 -282 -79 C ATOM 3030 C SER A 553 48.939 -30.180 3.452 1.00 34.41 C ANISOU 3030 C SER A 553 6166 4381 2527 -404 -220 88 C ATOM 3031 O SER A 553 50.077 -29.882 3.098 1.00 30.70 O ANISOU 3031 O SER A 553 5668 4027 1970 -392 -38 94 O ATOM 3032 CB SER A 553 47.045 -30.211 1.816 1.00 35.07 C ANISOU 3032 CB SER A 553 6641 4348 2337 -556 -467 -73 C ATOM 3033 OG SER A 553 46.313 -30.974 0.877 1.00 35.51 O ANISOU 3033 OG SER A 553 6893 4298 2299 -571 -509 -233 O ATOM 3034 N SER A 554 48.412 -29.769 4.604 1.00 18.25 N ANISOU 3034 N SER A 554 3978 2315 641 -407 -369 220 N ATOM 3035 CA SER A 554 49.206 -28.953 5.530 1.00 25.30 C ANISOU 3035 CA SER A 554 4666 3325 1623 -389 -316 381 C ATOM 3036 C SER A 554 50.499 -29.639 5.959 1.00 24.97 C ANISOU 3036 C SER A 554 4469 3306 1711 -262 -85 368 C ATOM 3037 O SER A 554 51.565 -29.023 5.964 1.00 23.52 O ANISOU 3037 O SER A 554 4209 3251 1479 -255 57 433 O ATOM 3038 CB SER A 554 48.407 -28.569 6.772 1.00 19.64 C ANISOU 3038 CB SER A 554 3806 2574 1083 -401 -510 510 C ATOM 3039 OG SER A 554 47.681 -29.679 7.275 1.00 33.13 O ANISOU 3039 OG SER A 554 5493 4131 2963 -340 -586 445 O ATOM 3040 N GLY A 555 50.392 -30.916 6.316 1.00 23.09 N ANISOU 3040 N GLY A 555 4188 2941 1642 -164 -53 283 N ATOM 3041 CA GLY A 555 51.529 -31.683 6.761 1.00 19.39 C ANISOU 3041 CA GLY A 555 3574 2472 1321 -40 147 259 C ATOM 3042 C GLY A 555 52.566 -31.838 5.670 1.00 29.54 C ANISOU 3042 C GLY A 555 4951 3830 2443 -27 361 147 C ATOM 3043 O GLY A 555 53.768 -31.663 5.919 1.00 33.00 O ANISOU 3043 O GLY A 555 5267 4360 2913 28 537 186 O ATOM 3044 N LYS A 556 52.103 -32.148 4.459 1.00 24.13 N ANISOU 3044 N LYS A 556 4480 3109 1578 -78 347 6 N ATOM 3045 CA LYS A 556 53.009 -32.239 3.314 1.00 36.59 C ANISOU 3045 CA LYS A 556 6161 4767 2972 -84 540 -110 C ATOM 3046 C LYS A 556 53.708 -30.917 3.031 1.00 34.77 C ANISOU 3046 C LYS A 556 5927 4713 2570 -162 604 -8 C ATOM 3047 O LYS A 556 54.869 -30.918 2.630 1.00 34.86 O ANISOU 3047 O LYS A 556 5913 4817 2514 -132 806 -50 O ATOM 3048 CB LYS A 556 52.314 -32.777 2.053 1.00 31.36 C ANISOU 3048 CB LYS A 556 5733 4039 2142 -134 502 -279 C ATOM 3049 CG LYS A 556 52.111 -34.296 2.094 1.00 39.37 C ANISOU 3049 CG LYS A 556 6746 4900 3312 -29 533 -425 C ATOM 3050 CD LYS A 556 51.350 -34.830 0.874 1.00 48.56 C ANISOU 3050 CD LYS A 556 8139 5995 4317 -76 484 -592 C ATOM 3051 CE LYS A 556 49.909 -34.329 0.853 1.00 60.96 C ANISOU 3051 CE LYS A 556 9827 7504 5829 -172 235 -541 C ATOM 3052 NZ LYS A 556 49.063 -34.954 -0.213 1.00 70.91 N ANISOU 3052 NZ LYS A 556 11302 8674 6967 -206 172 -702 N ATOM 3053 N LYS A 557 53.009 -29.799 3.234 1.00 33.50 N ANISOU 3053 N LYS A 557 5790 4598 2342 -263 429 123 N ATOM 3054 CA LYS A 557 53.615 -28.488 3.013 1.00 35.97 C ANISOU 3054 CA LYS A 557 6092 5074 2499 -342 469 233 C ATOM 3055 C LYS A 557 54.721 -28.255 4.034 1.00 27.20 C ANISOU 3055 C LYS A 557 4747 4039 1547 -256 602 345 C ATOM 3056 O LYS A 557 55.765 -27.737 3.707 1.00 28.99 O ANISOU 3056 O LYS A 557 4950 4394 1672 -263 759 366 O ATOM 3057 CB LYS A 557 52.595 -27.363 3.142 1.00 38.63 C ANISOU 3057 CB LYS A 557 6481 5432 2764 -461 236 354 C ATOM 3058 CG LYS A 557 51.640 -27.185 1.979 1.00 51.56 C ANISOU 3058 CG LYS A 557 8367 7039 4185 -578 107 269 C ATOM 3059 CD LYS A 557 50.790 -25.932 2.223 1.00 57.83 C ANISOU 3059 CD LYS A 557 9156 7846 4973 -694 -117 397 C ATOM 3060 CE LYS A 557 49.430 -26.005 1.561 1.00 63.20 C ANISOU 3060 CE LYS A 557 10014 8402 5596 -784 -311 319 C ATOM 3061 NZ LYS A 557 48.657 -24.746 1.793 1.00 66.24 N ANISOU 3061 NZ LYS A 557 10313 8730 6127 -903 -499 409 N ATOM 3062 N MET A 558 54.482 -28.649 5.276 1.00 23.35 N ANISOU 3062 N MET A 558 4087 3473 1311 -177 538 417 N ATOM 3063 CA MET A 558 55.465 -28.425 6.329 1.00 33.83 C ANISOU 3063 CA MET A 558 5185 4867 2804 -94 650 531 C ATOM 3064 C MET A 558 56.714 -29.264 6.116 1.00 35.10 C ANISOU 3064 C MET A 558 5293 5036 3006 11 900 427 C ATOM 3065 O MET A 558 57.828 -28.765 6.184 1.00 29.19 O ANISOU 3065 O MET A 558 4456 4405 2230 33 1057 475 O ATOM 3066 CB MET A 558 54.855 -28.722 7.690 1.00 26.84 C ANISOU 3066 CB MET A 558 4132 3889 2176 -40 516 624 C ATOM 3067 CG MET A 558 53.870 -27.669 8.088 1.00 26.20 C ANISOU 3067 CG MET A 558 4049 3836 2071 -140 290 754 C ATOM 3068 SD MET A 558 53.688 -27.675 9.868 1.00 34.62 S ANISOU 3068 SD MET A 558 4845 4870 3438 -71 198 906 S ATOM 3069 CE MET A 558 52.891 -29.257 10.095 1.00 16.77 C ANISOU 3069 CE MET A 558 2618 2413 1342 -2 135 782 C ATOM 3070 N ILE A 559 56.504 -30.544 5.853 1.00 38.51 N ANISOU 3070 N ILE A 559 5780 5342 3510 75 931 277 N ATOM 3071 CA ILE A 559 57.589 -31.451 5.547 1.00 38.43 C ANISOU 3071 CA ILE A 559 5737 5326 3540 172 1154 150 C ATOM 3072 C ILE A 559 58.409 -30.887 4.401 1.00 45.93 C ANISOU 3072 C ILE A 559 6798 6414 4239 112 1308 88 C ATOM 3073 O ILE A 559 59.644 -30.857 4.449 1.00 47.80 O ANISOU 3073 O ILE A 559 6940 6734 4489 168 1504 80 O ATOM 3074 CB ILE A 559 57.032 -32.795 5.131 1.00 35.69 C ANISOU 3074 CB ILE A 559 5485 4826 3249 218 1132 -20 C ATOM 3075 CG1 ILE A 559 56.464 -33.514 6.357 1.00 27.63 C ANISOU 3075 CG1 ILE A 559 4325 3668 2506 297 1019 35 C ATOM 3076 CG2 ILE A 559 58.097 -33.618 4.392 1.00 36.53 C ANISOU 3076 CG2 ILE A 559 5615 4945 3319 287 1360 -189 C ATOM 3077 CD1 ILE A 559 55.637 -34.761 6.012 1.00 27.49 C ANISOU 3077 CD1 ILE A 559 4411 3487 2548 329 945 -113 C ATOM 3078 N GLU A 560 57.711 -30.421 3.375 1.00 45.17 N ANISOU 3078 N GLU A 560 6904 6345 3913 -6 1216 47 N ATOM 3079 CA GLU A 560 58.375 -29.889 2.194 1.00 45.10 C ANISOU 3079 CA GLU A 560 7022 6469 3644 -80 1345 -16 C ATOM 3080 C GLU A 560 59.141 -28.601 2.518 1.00 38.57 C ANISOU 3080 C GLU A 560 6099 5802 2755 -121 1399 143 C ATOM 3081 O GLU A 560 60.252 -28.396 2.032 1.00 39.61 O ANISOU 3081 O GLU A 560 6223 6048 2781 -117 1590 104 O ATOM 3082 CB GLU A 560 57.365 -29.679 1.064 1.00 41.46 C ANISOU 3082 CB GLU A 560 6802 5992 2958 -203 1213 -87 C ATOM 3083 CG GLU A 560 57.892 -28.890 -0.126 1.00 56.61 C ANISOU 3083 CG GLU A 560 8861 8063 4585 -311 1306 -117 C ATOM 3084 CD GLU A 560 56.814 -28.620 -1.174 1.00 79.21 C ANISOU 3084 CD GLU A 560 11960 10906 7232 -440 1153 -171 C ATOM 3085 OE1 GLU A 560 55.647 -29.034 -0.962 1.00 83.40 O ANISOU 3085 OE1 GLU A 560 12544 11303 7843 -441 975 -186 O ATOM 3086 OE2 GLU A 560 57.134 -27.994 -2.213 1.00 90.16 O ANISOU 3086 OE2 GLU A 560 13479 12411 8367 -542 1210 -198 O ATOM 3087 N THR A 561 58.554 -27.746 3.349 1.00 34.72 N ANISOU 3087 N THR A 561 5532 5325 2337 -158 1232 316 N ATOM 3088 CA THR A 561 59.232 -26.518 3.770 1.00 40.88 C ANISOU 3088 CA THR A 561 6201 6250 3083 -189 1268 476 C ATOM 3089 C THR A 561 60.582 -26.821 4.427 1.00 41.79 C ANISOU 3089 C THR A 561 6123 6410 3346 -68 1484 489 C ATOM 3090 O THR A 561 61.571 -26.168 4.142 1.00 47.74 O ANISOU 3090 O THR A 561 6844 7286 4010 -83 1612 516 O ATOM 3091 CB THR A 561 58.371 -25.711 4.752 1.00 38.64 C ANISOU 3091 CB THR A 561 5820 5945 2916 -226 1044 649 C ATOM 3092 OG1 THR A 561 57.249 -25.160 4.057 1.00 39.37 O ANISOU 3092 OG1 THR A 561 6079 6009 2869 -354 839 640 O ATOM 3093 CG2 THR A 561 59.183 -24.573 5.392 1.00 35.65 C ANISOU 3093 CG2 THR A 561 5225 5637 2685 -210 1023 765 C ATOM 3094 N LEU A 562 60.613 -27.833 5.287 1.00 38.63 N ANISOU 3094 N LEU A 562 5591 5892 3192 52 1504 461 N ATOM 3095 CA LEU A 562 61.832 -28.209 6.000 1.00 35.97 C ANISOU 3095 CA LEU A 562 5065 5579 3024 175 1694 472 C ATOM 3096 C LEU A 562 62.860 -28.827 5.074 1.00 44.05 C ANISOU 3096 C LEU A 562 6152 6639 3946 211 1922 302 C ATOM 3097 O LEU A 562 64.060 -28.630 5.245 1.00 47.37 O ANISOU 3097 O LEU A 562 6464 7149 4385 263 2104 316 O ATOM 3098 CB LEU A 562 61.497 -29.185 7.116 1.00 27.53 C ANISOU 3098 CB LEU A 562 3854 4364 2244 284 1636 482 C ATOM 3099 CG LEU A 562 60.884 -28.531 8.353 1.00 29.26 C ANISOU 3099 CG LEU A 562 3928 4575 2614 277 1464 673 C ATOM 3100 CD1 LEU A 562 60.312 -29.590 9.278 1.00 27.36 C ANISOU 3100 CD1 LEU A 562 3590 4177 2627 361 1378 662 C ATOM 3101 CD2 LEU A 562 61.942 -27.702 9.078 1.00 26.43 C ANISOU 3101 CD2 LEU A 562 3381 4300 2361 326 1516 794 C ATOM 3102 N ALA A 563 62.379 -29.583 4.096 1.00 45.04 N ANISOU 3102 N ALA A 563 6451 6697 3967 183 1911 135 N ATOM 3103 CA ALA A 563 63.252 -30.203 3.117 1.00 44.55 C ANISOU 3103 CA ALA A 563 6463 6671 3794 206 2115 -47 C ATOM 3104 C ALA A 563 63.901 -29.128 2.253 1.00 48.59 C ANISOU 3104 C ALA A 563 7059 7363 4042 106 2212 -26 C ATOM 3105 O ALA A 563 65.097 -29.185 1.989 1.00 50.32 O ANISOU 3105 O ALA A 563 7227 7669 4223 144 2420 -88 O ATOM 3106 CB ALA A 563 62.470 -31.191 2.255 1.00 47.56 C ANISOU 3106 CB ALA A 563 7014 6941 4116 190 2059 -224 C ATOM 3107 N ASN A 564 63.111 -28.145 1.824 1.00 51.26 N ANISOU 3107 N ASN A 564 7522 7754 4199 -25 2057 61 N ATOM 3108 CA ASN A 564 63.629 -27.038 1.019 1.00 64.53 C ANISOU 3108 CA ASN A 564 9288 9606 5623 -136 2122 100 C ATOM 3109 C ASN A 564 64.617 -26.153 1.780 1.00 70.48 C ANISOU 3109 C ASN A 564 9847 10435 6496 -102 2167 245 C ATOM 3110 O ASN A 564 65.313 -25.323 1.192 1.00 67.49 O ANISOU 3110 O ASN A 564 9488 10159 5995 -169 2210 263 O ATOM 3111 CB ASN A 564 62.485 -26.181 0.472 1.00 65.59 C ANISOU 3111 CB ASN A 564 9590 9757 5573 -284 1910 171 C ATOM 3112 CG ASN A 564 61.777 -26.837 -0.698 1.00 74.96 C ANISOU 3112 CG ASN A 564 10996 10883 6604 -345 1867 1 C ATOM 3113 OD1 ASN A 564 62.130 -27.950 -1.111 1.00 74.97 O ANISOU 3113 OD1 ASN A 564 11020 10829 6634 -277 1996 -173 O ATOM 3114 ND2 ASN A 564 60.767 -26.151 -1.242 1.00 75.28 N ANISOU 3114 ND2 ASN A 564 11195 10929 6479 -475 1682 49 N ATOM 3115 N LEU A 565 64.664 -26.331 3.093 1.00 70.83 N ANISOU 3115 N LEU A 565 9695 10402 6817 4 2118 343 N ATOM 3116 CA LEU A 565 65.547 -25.541 3.932 1.00 69.08 C ANISOU 3116 CA LEU A 565 9271 10205 6770 56 2100 473 C ATOM 3117 C LEU A 565 66.977 -26.091 3.856 1.00 73.91 C ANISOU 3117 C LEU A 565 9805 10850 7430 149 2340 380 C ATOM 3118 O LEU A 565 67.927 -25.362 3.547 1.00 65.44 O ANISOU 3118 O LEU A 565 8703 9866 6296 127 2404 401 O ATOM 3119 CB LEU A 565 65.019 -25.538 5.366 1.00 58.11 C ANISOU 3119 CB LEU A 565 7708 8716 5656 133 1936 605 C ATOM 3120 CG LEU A 565 65.369 -24.345 6.253 1.00 52.05 C ANISOU 3120 CG LEU A 565 6764 7971 5042 155 1792 766 C ATOM 3121 CD1 LEU A 565 66.287 -24.746 7.390 1.00 50.26 C ANISOU 3121 CD1 LEU A 565 6339 7688 5068 305 1855 810 C ATOM 3122 CD2 LEU A 565 65.978 -23.236 5.421 1.00 48.43 C ANISOU 3122 CD2 LEU A 565 6360 7635 4407 68 1811 778 C ATOM 3123 N ARG A 566 67.111 -27.388 4.109 1.00 85.40 N ANISOU 3123 N ARG A 566 11225 12229 8996 251 2468 267 N ATOM 3124 CA ARG A 566 68.410 -28.049 4.095 1.00 98.83 C ANISOU 3124 CA ARG A 566 12840 13936 10775 348 2685 160 C ATOM 3125 C ARG A 566 68.940 -28.239 2.676 1.00 98.18 C ANISOU 3125 C ARG A 566 12915 13957 10434 285 2865 -17 C ATOM 3126 O ARG A 566 70.042 -28.745 2.474 1.00102.09 O ANISOU 3126 O ARG A 566 13357 14472 10959 349 3053 -129 O ATOM 3127 CB ARG A 566 68.316 -29.394 4.807 1.00110.91 C ANISOU 3127 CB ARG A 566 14276 15341 12526 477 2745 84 C ATOM 3128 CG ARG A 566 69.650 -30.003 5.184 1.00123.13 C ANISOU 3128 CG ARG A 566 15683 16858 14243 594 2913 19 C ATOM 3129 CD ARG A 566 69.431 -31.235 6.043 1.00134.22 C ANISOU 3129 CD ARG A 566 16976 18118 15903 717 2920 -25 C ATOM 3130 NE ARG A 566 68.426 -32.131 5.469 1.00142.49 N ANISOU 3130 NE ARG A 566 18148 19112 16880 709 2913 -170 N ATOM 3131 CZ ARG A 566 67.125 -32.084 5.750 1.00143.80 C ANISOU 3131 CZ ARG A 566 18369 19193 17076 663 2692 -92 C ATOM 3132 NH1 ARG A 566 66.659 -31.177 6.598 1.00142.70 N ANISOU 3132 NH1 ARG A 566 18151 19083 16987 631 2557 110 N ATOM 3133 NH2 ARG A 566 66.288 -32.940 5.178 1.00143.96 N ANISOU 3133 NH2 ARG A 566 18521 19102 17077 648 2606 -222 N ATOM 3134 N SER A 567 68.141 -27.843 1.694 1.00 90.52 N ANISOU 3134 N SER A 567 12139 13045 9208 157 2798 -45 N ATOM 3135 CA SER A 567 68.615 -27.769 0.323 1.00 84.64 C ANISOU 3135 CA SER A 567 11551 12415 8192 72 2934 -186 C ATOM 3136 C SER A 567 68.988 -26.326 0.010 1.00 79.31 C ANISOU 3136 C SER A 567 10887 11849 7397 -38 2863 -56 C ATOM 3137 O SER A 567 69.432 -25.571 0.886 1.00 68.36 O ANISOU 3137 O SER A 567 9342 10458 6175 -1 2790 98 O ATOM 3138 CB SER A 567 67.547 -28.262 -0.657 1.00 85.96 C ANISOU 3138 CB SER A 567 11942 12569 8152 -6 2888 -313 C ATOM 3139 OG SER A 567 67.169 -29.598 -0.376 1.00 86.47 O ANISOU 3139 OG SER A 567 11978 12466 8410 97 2868 -435 O TER 3140 SER A 567 ATOM 3141 O5' U B 1 41.710 -29.335 -0.119 1.00 46.63 O ANISOU 3141 O5' U B 1 7447 5001 5270 786 -1806 -386 O ATOM 3142 C5' U B 1 41.631 -27.970 0.296 1.00 31.78 C ANISOU 3142 C5' U B 1 5523 3096 3455 750 -1798 -356 C ATOM 3143 C4' U B 1 41.134 -27.875 1.714 1.00 31.18 C ANISOU 3143 C4' U B 1 5373 2984 3489 739 -1780 -383 C ATOM 3144 O4' U B 1 42.052 -28.588 2.591 1.00 30.70 O ANISOU 3144 O4' U B 1 5285 2974 3403 759 -1702 -419 O ATOM 3145 C3' U B 1 41.093 -26.466 2.256 1.00 36.16 C ANISOU 3145 C3' U B 1 5953 3595 4189 701 -1770 -347 C ATOM 3146 O3' U B 1 39.807 -25.875 1.922 1.00 31.23 O ANISOU 3146 O3' U B 1 5334 2901 3632 680 -1848 -329 O ATOM 3147 C2' U B 1 41.266 -26.698 3.760 1.00 33.39 C ANISOU 3147 C2' U B 1 5538 3241 3909 710 -1716 -380 C ATOM 3148 O2' U B 1 40.057 -27.030 4.372 1.00 37.96 O ANISOU 3148 O2' U B 1 6093 3744 4584 716 -1758 -403 O ATOM 3149 C1' U B 1 42.220 -27.885 3.814 1.00 30.21 C ANISOU 3149 C1' U B 1 5157 2901 3422 745 -1659 -420 C ATOM 3150 N1 U B 1 43.643 -27.363 3.878 1.00 38.58 N ANISOU 3150 N1 U B 1 6208 4029 4423 738 -1588 -404 N ATOM 3151 C2 U B 1 44.092 -26.938 5.109 1.00 29.68 C ANISOU 3151 C2 U B 1 5018 2905 3355 740 -1534 -418 C ATOM 3152 O2 U B 1 43.413 -26.925 6.138 1.00 33.92 O ANISOU 3152 O2 U B 1 5509 3391 3986 748 -1539 -437 O ATOM 3153 N3 U B 1 45.388 -26.475 5.146 1.00 31.67 N ANISOU 3153 N3 U B 1 5260 3214 3559 737 -1471 -408 N ATOM 3154 C4 U B 1 46.240 -26.402 4.080 1.00 38.20 C ANISOU 3154 C4 U B 1 6136 4089 4289 732 -1455 -383 C ATOM 3155 O4 U B 1 47.359 -25.967 4.276 1.00 36.96 O ANISOU 3155 O4 U B 1 5962 3973 4110 731 -1394 -380 O ATOM 3156 C5 U B 1 45.718 -26.843 2.830 1.00 30.65 C ANISOU 3156 C5 U B 1 5249 3126 3273 732 -1512 -364 C ATOM 3157 C6 U B 1 44.471 -27.291 2.781 1.00 30.66 C ANISOU 3157 C6 U B 1 5258 3076 3317 736 -1577 -376 C ATOM 3158 P G B 2 39.738 -24.378 1.459 1.00 33.27 P ANISOU 3158 P G B 2 5591 3153 3898 641 -1864 -275 P ATOM 3159 OP1 G B 2 38.382 -24.196 0.753 1.00 31.80 O ANISOU 3159 OP1 G B 2 5439 2898 3747 632 -1956 -271 O ATOM 3160 OP2 G B 2 40.968 -23.989 0.692 1.00 36.87 O ANISOU 3160 OP2 G B 2 6078 3675 4255 646 -1816 -247 O ATOM 3161 O5' G B 2 39.712 -23.632 2.785 1.00 32.50 O ANISOU 3161 O5' G B 2 5415 3041 3894 614 -1832 -264 O ATOM 3162 C5' G B 2 38.672 -23.869 3.777 1.00 30.41 C ANISOU 3162 C5' G B 2 5110 2706 3738 611 -1861 -283 C ATOM 3163 C4' G B 2 38.711 -22.796 4.863 1.00 31.56 C ANISOU 3163 C4' G B 2 5188 2840 3964 582 -1835 -252 C ATOM 3164 O4' G B 2 39.980 -22.825 5.576 1.00 33.21 O ANISOU 3164 O4' G B 2 5360 3107 4149 600 -1752 -261 O ATOM 3165 C3' G B 2 38.591 -21.383 4.343 1.00 33.01 C ANISOU 3165 C3' G B 2 5369 3030 4144 536 -1856 -195 C ATOM 3166 O3' G B 2 37.208 -21.095 4.129 1.00 35.99 O ANISOU 3166 O3' G B 2 5759 3335 4582 509 -1934 -184 O ATOM 3167 C2' G B 2 39.174 -20.587 5.490 1.00 31.74 C ANISOU 3167 C2' G B 2 5135 2887 4036 522 -1802 -172 C ATOM 3168 O2' G B 2 38.243 -20.340 6.530 1.00 36.32 O ANISOU 3168 O2' G B 2 5673 3400 4729 508 -1830 -161 O ATOM 3169 C1' G B 2 40.311 -21.501 5.975 1.00 30.43 C ANISOU 3169 C1' G B 2 4961 2770 3831 568 -1731 -215 C ATOM 3170 N9 G B 2 41.615 -21.088 5.446 1.00 33.30 N ANISOU 3170 N9 G B 2 5330 3209 4112 569 -1674 -202 N ATOM 3171 C8 G B 2 42.108 -21.331 4.182 1.00 31.33 C ANISOU 3171 C8 G B 2 5143 2999 3761 577 -1672 -200 C ATOM 3172 N7 G B 2 43.300 -20.819 3.993 1.00 31.41 N ANISOU 3172 N7 G B 2 5144 3065 3724 579 -1610 -186 N ATOM 3173 C5 G B 2 43.571 -20.223 5.228 1.00 31.88 C ANISOU 3173 C5 G B 2 5128 3125 3861 572 -1574 -182 C ATOM 3174 C6 G B 2 44.721 -19.508 5.631 1.00 32.36 C ANISOU 3174 C6 G B 2 5142 3230 3923 574 -1505 -171 C ATOM 3175 O6 G B 2 45.714 -19.298 4.922 1.00 30.11 O ANISOU 3175 O6 G B 2 4879 2992 3571 580 -1461 -164 O ATOM 3176 N1 G B 2 44.599 -19.064 6.965 1.00 29.81 N ANISOU 3176 N1 G B 2 4745 2885 3695 574 -1493 -171 N ATOM 3177 C2 G B 2 43.500 -19.282 7.795 1.00 28.64 C ANISOU 3177 C2 G B 2 4577 2676 3630 572 -1539 -174 C ATOM 3178 N2 G B 2 43.483 -18.803 9.060 1.00 28.02 N ANISOU 3178 N2 G B 2 4431 2574 3640 580 -1524 -168 N ATOM 3179 N3 G B 2 42.427 -19.960 7.410 1.00 29.81 N ANISOU 3179 N3 G B 2 4768 2778 3779 569 -1599 -185 N ATOM 3180 C4 G B 2 42.540 -20.375 6.129 1.00 30.92 C ANISOU 3180 C4 G B 2 4975 2944 3829 568 -1613 -189 C ATOM 3181 P U B 3 36.722 -20.022 3.060 1.00 40.52 P ANISOU 3181 P U B 3 6368 3904 5124 472 -1982 -144 P ATOM 3182 OP1 U B 3 35.256 -19.922 3.194 1.00 47.76 O ANISOU 3182 OP1 U B 3 7288 4735 6124 448 -2059 -144 O ATOM 3183 OP2 U B 3 37.329 -20.338 1.756 1.00 31.20 O ANISOU 3183 OP2 U B 3 5254 2769 3833 499 -1976 -153 O ATOM 3184 O5' U B 3 37.370 -18.672 3.585 1.00 38.90 O ANISOU 3184 O5' U B 3 6107 3741 4932 436 -1931 -93 O ATOM 3185 C5' U B 3 37.218 -17.435 2.878 1.00 33.55 C ANISOU 3185 C5' U B 3 5442 3080 4228 398 -1945 -49 C ATOM 3186 C4' U B 3 36.412 -16.478 3.729 1.00 33.97 C ANISOU 3186 C4' U B 3 5442 3094 4372 348 -1971 -9 C ATOM 3187 O4' U B 3 37.073 -16.387 5.012 1.00 31.77 O ANISOU 3187 O4' U B 3 5092 2833 4147 354 -1915 0 O ATOM 3188 C3' U B 3 36.292 -15.053 3.225 1.00 36.48 C ANISOU 3188 C3' U B 3 5758 3437 4667 302 -1973 41 C ATOM 3189 O3' U B 3 35.136 -14.931 2.393 1.00 41.04 O ANISOU 3189 O3' U B 3 6391 3965 5237 284 -2048 37 O ATOM 3190 C2' U B 3 36.072 -14.300 4.518 1.00 35.25 C ANISOU 3190 C2' U B 3 5524 3267 4602 265 -1964 82 C ATOM 3191 O2' U B 3 34.758 -14.470 4.979 1.00 35.53 O ANISOU 3191 O2' U B 3 5562 3221 4718 241 -2034 85 O ATOM 3192 C1' U B 3 36.964 -15.051 5.491 1.00 39.58 C ANISOU 3192 C1' U B 3 6029 3832 5176 307 -1909 56 C ATOM 3193 N1 U B 3 38.346 -14.482 5.685 1.00 36.36 N ANISOU 3193 N1 U B 3 5579 3502 4735 318 -1827 71 N ATOM 3194 C2 U B 3 38.506 -13.561 6.690 1.00 36.45 C ANISOU 3194 C2 U B 3 5517 3521 4811 295 -1804 113 C ATOM 3195 O2 U B 3 37.566 -13.198 7.381 1.00 38.59 O ANISOU 3195 O2 U B 3 5763 3740 5158 264 -1848 143 O ATOM 3196 N3 U B 3 39.779 -13.069 6.850 1.00 28.17 N ANISOU 3196 N3 U B 3 4426 2538 3738 310 -1730 120 N ATOM 3197 C4 U B 3 40.896 -13.415 6.103 1.00 38.40 C ANISOU 3197 C4 U B 3 5750 3888 4952 344 -1675 90 C ATOM 3198 O4 U B 3 41.986 -12.902 6.369 1.00 31.46 O ANISOU 3198 O4 U B 3 4825 3058 4069 356 -1609 97 O ATOM 3199 C5 U B 3 40.652 -14.392 5.065 1.00 29.34 C ANISOU 3199 C5 U B 3 4684 2727 3735 365 -1704 54 C ATOM 3200 C6 U B 3 39.410 -14.878 4.903 1.00 29.34 C ANISOU 3200 C6 U B 3 4723 2667 3759 353 -1778 45 C ATOM 3201 P A B 4 35.186 -14.019 1.083 1.00 45.49 P ANISOU 3201 P A B 4 7007 4562 5715 273 -2050 55 P ATOM 3202 OP1 A B 4 34.085 -14.475 0.209 1.00 46.81 O ANISOU 3202 OP1 A B 4 7247 4668 5870 283 -2132 23 O ATOM 3203 OP2 A B 4 36.566 -14.025 0.540 1.00 44.75 O ANISOU 3203 OP2 A B 4 6925 4539 5538 311 -1974 53 O ATOM 3204 O5' A B 4 34.921 -12.550 1.662 1.00 40.06 O ANISOU 3204 O5' A B 4 6263 3890 5067 210 -2039 114 O ATOM 3205 C5' A B 4 33.736 -12.245 2.392 1.00 39.81 C ANISOU 3205 C5' A B 4 6206 3798 5122 161 -2098 136 C ATOM 3206 C4' A B 4 33.676 -10.787 2.861 1.00 39.87 C ANISOU 3206 C4' A B 4 6161 3838 5150 101 -2078 200 C ATOM 3207 O4' A B 4 34.859 -10.484 3.672 1.00 43.94 O ANISOU 3207 O4' A B 4 6604 4412 5679 111 -2000 224 O ATOM 3208 C3' A B 4 33.672 -9.702 1.771 1.00 37.03 C ANISOU 3208 C3' A B 4 5838 3522 4709 80 -2067 219 C ATOM 3209 O3' A B 4 32.355 -9.525 1.258 1.00 39.58 O ANISOU 3209 O3' A B 4 6213 3788 5036 49 -2147 212 O ATOM 3210 C2' A B 4 34.073 -8.505 2.638 1.00 41.87 C ANISOU 3210 C2' A B 4 6369 4185 5355 34 -2019 282 C ATOM 3211 O2' A B 4 33.003 -8.080 3.465 1.00 41.31 O ANISOU 3211 O2' A B 4 6268 4066 5363 -23 -2074 320 O ATOM 3212 C1' A B 4 35.157 -9.101 3.543 1.00 44.04 C ANISOU 3212 C1' A B 4 6585 4483 5666 73 -1962 274 C ATOM 3213 N9 A B 4 36.476 -8.939 2.984 1.00 38.08 N ANISOU 3213 N9 A B 4 5829 3799 4842 110 -1882 264 N ATOM 3214 C8 A B 4 37.114 -9.746 2.087 1.00 35.04 C ANISOU 3214 C8 A B 4 5501 3425 4387 166 -1860 218 C ATOM 3215 N7 A B 4 38.307 -9.350 1.752 1.00 35.58 N ANISOU 3215 N7 A B 4 5556 3555 4408 190 -1781 223 N ATOM 3216 C5 A B 4 38.495 -8.191 2.500 1.00 37.35 C ANISOU 3216 C5 A B 4 5701 3814 4675 150 -1746 272 C ATOM 3217 C6 A B 4 39.572 -7.302 2.620 1.00 45.46 C ANISOU 3217 C6 A B 4 6673 4905 5695 154 -1663 296 C ATOM 3218 N6 A B 4 40.710 -7.452 1.937 1.00 47.35 N ANISOU 3218 N6 A B 4 6933 5181 5877 201 -1594 274 N ATOM 3219 N1 A B 4 39.433 -6.253 3.452 1.00 37.60 N ANISOU 3219 N1 A B 4 5601 3932 4755 109 -1653 346 N ATOM 3220 C2 A B 4 38.290 -6.104 4.141 1.00 31.54 C ANISOU 3220 C2 A B 4 4816 3122 4045 61 -1722 375 C ATOM 3221 N3 A B 4 37.198 -6.878 4.107 1.00 35.85 N ANISOU 3221 N3 A B 4 5413 3600 4608 52 -1803 356 N ATOM 3222 C4 A B 4 37.368 -7.911 3.259 1.00 34.49 C ANISOU 3222 C4 A B 4 5312 3410 4382 99 -1810 301 C ATOM 3223 P C B 5 32.056 -8.883 -0.190 1.00 42.69 P ANISOU 3223 P C B 5 6685 4198 5336 52 -2159 199 P ATOM 3224 OP1 C B 5 30.578 -8.839 -0.316 1.00 45.70 O ANISOU 3224 OP1 C B 5 7105 4505 5755 15 -2251 189 O ATOM 3225 OP2 C B 5 32.862 -9.559 -1.224 1.00 46.79 O ANISOU 3225 OP2 C B 5 7264 4740 5775 125 -2129 156 O ATOM 3226 O5' C B 5 32.609 -7.395 -0.084 1.00 46.60 O ANISOU 3226 O5' C B 5 7134 4773 5800 11 -2091 256 O ATOM 3227 C5' C B 5 31.996 -6.445 0.774 1.00 42.57 C ANISOU 3227 C5' C B 5 6567 4263 5345 -62 -2107 312 C ATOM 3228 C4' C B 5 32.803 -5.161 0.757 1.00 39.72 C ANISOU 3228 C4' C B 5 6159 3990 4941 -84 -2025 359 C ATOM 3229 O4' C B 5 34.131 -5.408 1.297 1.00 33.75 O ANISOU 3229 O4' C B 5 5343 3280 4199 -46 -1950 364 O ATOM 3230 C3' C B 5 33.020 -4.628 -0.654 1.00 43.57 C ANISOU 3230 C3' C B 5 6716 4515 5322 -56 -1993 337 C ATOM 3231 O3' C B 5 31.928 -3.779 -1.039 1.00 38.63 O ANISOU 3231 O3' C B 5 6125 3878 4674 -109 -2037 351 O ATOM 3232 C2' C B 5 34.333 -3.862 -0.502 1.00 50.84 C ANISOU 3232 C2' C B 5 7576 5521 6220 -45 -1886 368 C ATOM 3233 O2' C B 5 34.123 -2.553 -0.016 1.00 54.12 O ANISOU 3233 O2' C B 5 7933 5981 6648 -109 -1864 427 O ATOM 3234 C1' C B 5 35.092 -4.697 0.539 1.00 44.26 C ANISOU 3234 C1' C B 5 6679 4683 5457 -22 -1867 367 C ATOM 3235 N1 C B 5 36.056 -5.659 -0.057 1.00 47.70 N ANISOU 3235 N1 C B 5 7153 5122 5850 54 -1829 319 N ATOM 3236 C2 C B 5 37.356 -5.220 -0.378 1.00 53.77 C ANISOU 3236 C2 C B 5 7900 5953 6578 89 -1733 324 C ATOM 3237 O2 C B 5 37.661 -4.050 -0.155 1.00 58.93 O ANISOU 3237 O2 C B 5 8499 6658 7234 59 -1680 365 O ATOM 3238 N3 C B 5 38.230 -6.100 -0.929 1.00 54.26 N ANISOU 3238 N3 C B 5 8001 6015 6600 155 -1699 285 N ATOM 3239 C4 C B 5 37.859 -7.358 -1.167 1.00 66.95 C ANISOU 3239 C4 C B 5 9665 7571 8203 186 -1758 244 C ATOM 3240 N4 C B 5 38.741 -8.199 -1.712 1.00 70.69 N ANISOU 3240 N4 C B 5 10179 8049 8632 248 -1724 211 N ATOM 3241 C5 C B 5 36.536 -7.822 -0.846 1.00 64.22 C ANISOU 3241 C5 C B 5 9337 7162 7901 154 -1854 234 C ATOM 3242 C6 C B 5 35.688 -6.940 -0.307 1.00 56.39 C ANISOU 3242 C6 C B 5 8309 6165 6953 89 -1886 272 C ATOM 3243 P C B 6 31.345 -3.805 -2.526 1.00 38.81 P ANISOU 3243 P C B 6 6261 3875 4610 -74 -2070 299 P ATOM 3244 OP1 C B 6 30.144 -2.932 -2.524 1.00 49.52 O ANISOU 3244 OP1 C B 6 7632 5215 5966 -144 -2121 320 O ATOM 3245 OP2 C B 6 31.221 -5.228 -2.970 1.00 36.09 O ANISOU 3245 OP2 C B 6 5977 3465 4272 -10 -2121 238 O ATOM 3246 O5' C B 6 32.444 -3.142 -3.453 1.00 31.47 O ANISOU 3246 O5' C B 6 5353 3018 3588 -25 -1969 296 O ATOM 3247 C5' C B 6 32.819 -1.761 -3.294 1.00 32.50 C ANISOU 3247 C5' C B 6 5432 3224 3694 -64 -1896 345 C ATOM 3248 C4' C B 6 34.086 -1.447 -4.079 1.00 36.61 C ANISOU 3248 C4' C B 6 5966 3799 4146 2 -1790 335 C ATOM 3249 O4' C B 6 35.238 -2.055 -3.435 1.00 46.67 O ANISOU 3249 O4' C B 6 7178 5091 5465 32 -1742 342 O ATOM 3250 C3' C B 6 34.126 -2.011 -5.494 1.00 45.56 C ANISOU 3250 C3' C B 6 7216 4896 5199 86 -1796 275 C ATOM 3251 O3' C B 6 33.403 -1.168 -6.372 1.00 45.94 O ANISOU 3251 O3' C B 6 7331 4946 5179 82 -1802 263 O ATOM 3252 C2' C B 6 35.628 -1.993 -5.765 1.00 57.36 C ANISOU 3252 C2' C B 6 8691 6435 6668 148 -1688 279 C ATOM 3253 O2' C B 6 36.122 -0.698 -6.053 1.00 62.15 O ANISOU 3253 O2' C B 6 9275 7105 7234 143 -1594 305 O ATOM 3254 C1' C B 6 36.170 -2.473 -4.416 1.00 54.32 C ANISOU 3254 C1' C B 6 8203 6063 6372 116 -1684 307 C ATOM 3255 N1 C B 6 36.318 -3.949 -4.363 1.00 62.12 N ANISOU 3255 N1 C B 6 9221 7000 7382 159 -1731 270 N ATOM 3256 C2 C B 6 37.458 -4.557 -4.913 1.00 74.74 C ANISOU 3256 C2 C B 6 10849 8606 8944 233 -1673 248 C ATOM 3257 O2 C B 6 38.330 -3.848 -5.420 1.00 82.79 O ANISOU 3257 O2 C B 6 11868 9667 9921 264 -1581 259 O ATOM 3258 N3 C B 6 37.566 -5.908 -4.865 1.00 73.12 N ANISOU 3258 N3 C B 6 10671 8360 8751 269 -1716 216 N ATOM 3259 C4 C B 6 36.606 -6.642 -4.307 1.00 70.54 C ANISOU 3259 C4 C B 6 10341 7985 8476 239 -1808 202 C ATOM 3260 N4 C B 6 36.753 -7.973 -4.279 1.00 69.58 N ANISOU 3260 N4 C B 6 10245 7829 8364 278 -1842 168 N ATOM 3261 C5 C B 6 35.437 -6.034 -3.742 1.00 62.59 C ANISOU 3261 C5 C B 6 9305 6960 7515 167 -1867 223 C ATOM 3262 C6 C B 6 35.340 -4.703 -3.792 1.00 58.82 C ANISOU 3262 C6 C B 6 8803 6526 7019 128 -1828 258 C ATOM 3263 P A B 7 32.825 -1.738 -7.747 1.00 42.16 P ANISOU 3263 P A B 7 6987 4403 4630 156 -1855 196 P ATOM 3264 OP1 A B 7 32.995 -3.208 -7.731 1.00 53.63 O ANISOU 3264 OP1 A B 7 8462 5800 6115 204 -1907 164 O ATOM 3265 OP2 A B 7 33.384 -0.918 -8.842 1.00 51.21 O ANISOU 3265 OP2 A B 7 8189 5584 5683 215 -1766 185 O ATOM 3266 O5' A B 7 31.262 -1.429 -7.681 1.00 46.83 O ANISOU 3266 O5' A B 7 7608 4954 5232 92 -1953 185 O ATOM 3267 C5' A B 7 30.391 -2.271 -6.952 1.00 43.13 C ANISOU 3267 C5' A B 7 7121 4422 4844 50 -2056 178 C ATOM 3268 C4' A B 7 29.271 -1.450 -6.329 1.00 46.03 C ANISOU 3268 C4' A B 7 7458 4788 5243 -48 -2105 210 C ATOM 3269 O4' A B 7 29.833 -0.714 -5.197 1.00 48.55 O ANISOU 3269 O4' A B 7 7664 5176 5606 -114 -2044 283 O ATOM 3270 C3' A B 7 28.688 -0.345 -7.225 1.00 39.31 C ANISOU 3270 C3' A B 7 6673 3958 4305 -56 -2093 195 C ATOM 3271 O3' A B 7 27.659 -0.842 -8.064 1.00 40.02 O ANISOU 3271 O3' A B 7 6866 3969 4372 -22 -2182 128 O ATOM 3272 C2' A B 7 28.079 0.559 -6.142 1.00 41.09 C ANISOU 3272 C2' A B 7 6819 4216 4577 -172 -2106 260 C ATOM 3273 O2' A B 7 26.866 0.029 -5.637 1.00 43.28 O ANISOU 3273 O2' A B 7 7105 4414 4925 -222 -2218 252 O ATOM 3274 C1' A B 7 29.131 0.497 -5.033 1.00 43.03 C ANISOU 3274 C1' A B 7 6951 4511 4887 -191 -2046 319 C ATOM 3275 N9 A B 7 30.054 1.618 -5.130 1.00 43.59 N ANISOU 3275 N9 A B 7 6978 4678 4906 -192 -1932 357 N ATOM 3276 C8 A B 7 31.364 1.613 -5.460 1.00 41.79 C ANISOU 3276 C8 A B 7 6734 4495 4650 -126 -1835 353 C ATOM 3277 N7 A B 7 31.934 2.771 -5.451 1.00 39.97 N ANISOU 3277 N7 A B 7 6458 4346 4384 -143 -1743 390 N ATOM 3278 C5 A B 7 30.911 3.647 -5.079 1.00 40.48 C ANISOU 3278 C5 A B 7 6507 4428 4446 -232 -1781 425 C ATOM 3279 C6 A B 7 30.858 5.037 -4.883 1.00 39.59 C ANISOU 3279 C6 A B 7 6348 4396 4299 -292 -1724 474 C ATOM 3280 N6 A B 7 31.906 5.829 -5.038 1.00 35.02 N ANISOU 3280 N6 A B 7 5723 3894 3688 -266 -1606 494 N ATOM 3281 N1 A B 7 29.693 5.565 -4.520 1.00 38.51 N ANISOU 3281 N1 A B 7 6213 4254 4165 -379 -1789 501 N ATOM 3282 C2 A B 7 28.613 4.768 -4.358 1.00 35.59 C ANISOU 3282 C2 A B 7 5889 3796 3836 -403 -1907 479 C ATOM 3283 N3 A B 7 28.558 3.430 -4.526 1.00 36.71 N ANISOU 3283 N3 A B 7 6074 3854 4019 -347 -1968 428 N ATOM 3284 C4 A B 7 29.746 2.934 -4.886 1.00 39.61 C ANISOU 3284 C4 A B 7 6438 4237 4375 -263 -1900 404 C ATOM 3285 P U B 8 27.659 -0.536 -9.637 1.00 52.62 P ANISOU 3285 P U B 8 8582 5559 5853 68 -2157 67 P ATOM 3286 OP1 U B 8 26.386 -1.068 -10.182 1.00 54.36 O ANISOU 3286 OP1 U B 8 8889 5687 6079 83 -2272 2 O ATOM 3287 OP2 U B 8 28.944 -0.973 -10.215 1.00 51.73 O ANISOU 3287 OP2 U B 8 8487 5466 5702 163 -2080 57 O ATOM 3288 O5' U B 8 27.629 1.057 -9.700 1.00 51.91 O ANISOU 3288 O5' U B 8 8475 5550 5697 15 -2082 102 O ATOM 3289 C5' U B 8 27.730 1.696 -10.950 1.00 44.78 C ANISOU 3289 C5' U B 8 7664 4663 4686 85 -2028 60 C ATOM 3290 C4' U B 8 26.385 2.285 -11.323 1.00 46.47 C ANISOU 3290 C4' U B 8 7943 4850 4862 45 -2094 26 C ATOM 3291 O4' U B 8 26.083 3.394 -10.441 1.00 47.31 O ANISOU 3291 O4' U B 8 7969 5026 4980 -72 -2069 92 O ATOM 3292 C3' U B 8 26.324 2.884 -12.724 1.00 48.80 C ANISOU 3292 C3' U B 8 8354 5148 5040 131 -2050 -34 C ATOM 3293 O3' U B 8 26.064 1.855 -13.672 1.00 62.30 O ANISOU 3293 O3' U B 8 10169 6766 6737 236 -2117 -110 O ATOM 3294 C2' U B 8 25.171 3.884 -12.568 1.00 46.72 C ANISOU 3294 C2' U B 8 8102 4903 4747 41 -2084 -32 C ATOM 3295 O2' U B 8 23.882 3.302 -12.606 1.00 50.72 O ANISOU 3295 O2' U B 8 8661 5319 5292 19 -2216 -80 O ATOM 3296 C1' U B 8 25.441 4.427 -11.169 1.00 44.57 C ANISOU 3296 C1' U B 8 7691 4703 4539 -79 -2051 64 C ATOM 3297 N1 U B 8 26.258 5.686 -11.165 1.00 47.39 N ANISOU 3297 N1 U B 8 8001 5172 4834 -94 -1917 111 N ATOM 3298 C2 U B 8 25.570 6.894 -11.212 1.00 46.02 C ANISOU 3298 C2 U B 8 7837 5051 4597 -162 -1899 123 C ATOM 3299 O2 U B 8 24.358 6.959 -11.243 1.00 49.95 O ANISOU 3299 O2 U B 8 8382 5507 5090 -212 -1989 98 O ATOM 3300 N3 U B 8 26.366 8.007 -11.210 1.00 42.17 N ANISOU 3300 N3 U B 8 7300 4666 4055 -169 -1771 164 N ATOM 3301 C4 U B 8 27.735 8.057 -11.182 1.00 42.72 C ANISOU 3301 C4 U B 8 7316 4784 4133 -115 -1661 191 C ATOM 3302 O4 U B 8 28.303 9.131 -11.190 1.00 37.77 O ANISOU 3302 O4 U B 8 6646 4246 3460 -125 -1550 224 O ATOM 3303 C5 U B 8 28.383 6.755 -11.143 1.00 44.65 C ANISOU 3303 C5 U B 8 7557 4965 4443 -47 -1691 175 C ATOM 3304 C6 U B 8 27.635 5.656 -11.133 1.00 48.26 C ANISOU 3304 C6 U B 8 8060 5329 4947 -40 -1814 138 C ATOM 3305 P A B 9 26.404 2.082 -15.219 1.00 76.18 P ANISOU 3305 P A B 9 12055 8507 8381 374 -2062 -175 P ATOM 3306 OP1 A B 9 26.093 0.828 -15.947 1.00 69.50 O ANISOU 3306 OP1 A B 9 11299 7559 7548 471 -2154 -242 O ATOM 3307 OP2 A B 9 27.764 2.667 -15.307 1.00 76.34 O ANISOU 3307 OP2 A B 9 12038 8605 8363 409 -1918 -131 O ATOM 3308 O5' A B 9 25.353 3.198 -15.648 1.00115.46 O ANISOU 3308 O5' A B 9 17091 13495 13284 340 -2072 -209 O ATOM 3309 C5' A B 9 23.950 2.919 -15.595 1.00113.87 C ANISOU 3309 C5' A B 9 16931 13223 13113 296 -2200 -255 C ATOM 3310 C4' A B 9 23.255 3.486 -16.811 1.00113.99 C ANISOU 3310 C4' A B 9 17077 13208 13025 367 -2208 -337 C ATOM 3311 O4' A B 9 23.266 4.931 -16.739 1.00110.45 O ANISOU 3311 O4' A B 9 16611 12854 12501 309 -2115 -307 O ATOM 3312 C3' A B 9 23.933 3.146 -18.130 1.00117.40 C ANISOU 3312 C3' A B 9 17619 13604 13384 534 -2160 -394 C ATOM 3313 O3' A B 9 23.458 1.901 -18.636 1.00120.04 O ANISOU 3313 O3' A B 9 18025 13828 13757 613 -2275 -458 O ATOM 3314 C2' A B 9 23.514 4.300 -19.030 1.00114.00 C ANISOU 3314 C2' A B 9 17283 13196 12836 573 -2107 -445 C ATOM 3315 O2' A B 9 22.284 4.047 -19.663 1.00113.65 O ANISOU 3315 O2' A B 9 17342 13065 12775 608 -2218 -533 O ATOM 3316 C1' A B 9 23.383 5.471 -18.049 1.00110.62 C ANISOU 3316 C1' A B 9 16752 12872 12406 425 -2051 -374 C ATOM 3317 N9 A B 9 24.515 6.395 -18.081 1.00106.25 N ANISOU 3317 N9 A B 9 16155 12417 11797 439 -1893 -323 N ATOM 3318 C8 A B 9 25.835 6.110 -17.842 1.00103.07 C ANISOU 3318 C8 A B 9 15687 12047 11426 473 -1808 -271 C ATOM 3319 N7 A B 9 26.624 7.153 -17.946 1.00 99.18 N ANISOU 3319 N7 A B 9 15166 11641 10876 481 -1667 -238 N ATOM 3320 C5 A B 9 25.763 8.193 -18.274 1.00 99.87 C ANISOU 3320 C5 A B 9 15304 11760 10883 448 -1657 -270 C ATOM 3321 C6 A B 9 25.976 9.562 -18.523 1.00 99.19 C ANISOU 3321 C6 A B 9 15217 11763 10708 440 -1531 -260 C ATOM 3322 N6 A B 9 27.181 10.143 -18.475 1.00 93.56 N ANISOU 3322 N6 A B 9 14445 11121 9981 467 -1386 -214 N ATOM 3323 N1 A B 9 24.896 10.317 -18.825 1.00102.58 N ANISOU 3323 N1 A B 9 15708 12205 11063 403 -1558 -303 N ATOM 3324 C2 A B 9 23.691 9.742 -18.873 1.00102.48 C ANISOU 3324 C2 A B 9 15752 12113 11070 377 -1703 -353 C ATOM 3325 N3 A B 9 23.370 8.466 -18.658 1.00103.84 N ANISOU 3325 N3 A B 9 15928 12193 11332 384 -1829 -368 N ATOM 3326 C4 A B 9 24.461 7.739 -18.362 1.00102.97 C ANISOU 3326 C4 A B 9 15756 12079 11288 421 -1797 -323 C TER 3327 A B 9 HETATM 3328 O HOH A 1 44.710 -29.883 8.122 1.00 31.00 O HETATM 3329 O HOH A 2 46.745 2.703 8.359 1.00 26.41 O HETATM 3330 O HOH A 3 38.988 26.523 -2.939 1.00 44.87 O HETATM 3331 O HOH A 4 40.981 14.341 5.351 1.00 26.64 O HETATM 3332 O HOH A 5 54.356 -32.227 25.041 1.00 29.96 O HETATM 3333 O HOH A 6 16.614 13.297 -28.170 1.00 40.42 O HETATM 3334 O HOH A 7 25.706 32.817 -15.910 1.00 43.27 O HETATM 3335 O HOH A 9 48.092 -18.542 5.577 1.00 31.64 O HETATM 3336 O HOH A 10 57.493 -11.262 13.888 1.00 30.38 O HETATM 3337 O HOH A 11 43.874 -20.334 24.368 1.00 28.59 O HETATM 3338 O HOH A 12 56.394 -5.994 10.102 1.00 40.41 O HETATM 3339 O HOH A 13 42.841 9.435 0.654 1.00 41.77 O HETATM 3340 O HOH A 14 34.816 5.230 -2.060 1.00 37.56 O HETATM 3341 O HOH A 15 31.198 22.766 -21.488 1.00 31.36 O HETATM 3342 O HOH A 16 50.964 2.785 6.665 1.00 40.29 O HETATM 3343 O HOH A 17 45.570 -15.143 6.253 1.00 51.44 O HETATM 3344 O HOH A 19 52.860 11.591 8.690 1.00 32.43 O HETATM 3345 O HOH A 20 21.765 31.258 -13.270 1.00 49.66 O HETATM 3346 O HOH A 21 49.693 -20.440 6.697 1.00 36.37 O HETATM 3347 O HOH A 23 51.150 -8.777 5.995 1.00 39.15 O HETATM 3348 O HOH A 24 52.491 -27.645 22.511 1.00 33.28 O HETATM 3349 O HOH A 26 52.381 -34.749 22.309 1.00 52.08 O HETATM 3350 O HOH A 27 44.274 -29.725 29.257 1.00 52.04 O HETATM 3351 O HOH A 29 58.498 -13.282 7.827 1.00 49.67 O HETATM 3352 O HOH A 30 46.788 -28.519 25.327 1.00 45.32 O HETATM 3353 O HOH A 31 47.246 8.308 5.527 1.00 37.13 O HETATM 3354 O HOH A 32 49.601 -29.684 9.491 1.00 30.82 O HETATM 3355 O HOH A 33 32.627 -11.456 17.741 1.00 32.02 O HETATM 3356 O HOH A 35 16.507 23.674 -10.713 1.00 43.67 O HETATM 3357 O HOH A 36 34.041 31.643 -17.836 1.00 49.09 O HETATM 3358 O HOH A 37 32.393 32.900 -3.926 1.00 47.79 O HETATM 3359 O HOH A 38 51.798 -25.774 25.161 1.00 29.58 O HETATM 3360 O HOH A 40 40.174 -12.187 2.011 1.00 45.76 O HETATM 3361 O HOH A 41 52.599 -19.462 5.877 1.00 42.90 O HETATM 3362 O HOH A 42 36.899 8.602 -1.881 1.00 49.97 O HETATM 3363 O HOH A 44 29.293 28.062 -8.150 1.00 36.53 O HETATM 3364 O HOH A 45 33.583 21.981 -20.351 1.00 49.03 O HETATM 3365 O HOH A 46 30.745 18.164 -10.438 1.00 41.00 O HETATM 3366 O HOH A 47 33.854 -6.065 4.949 1.00 36.75 O HETATM 3367 O HOH A 49 11.851 21.228 -17.765 1.00 41.52 O HETATM 3368 O HOH A 52 38.377 7.140 1.071 1.00 43.10 O HETATM 3369 O HOH A 53 37.844 17.794 20.508 1.00 48.24 O HETATM 3370 O HOH A 54 43.677 -23.792 1.556 1.00 42.87 O HETATM 3371 O HOH A 55 21.576 -0.841 3.613 1.00 47.71 O HETATM 3372 O HOH A 57 40.028 -3.807 6.618 1.00 46.78 O HETATM 3373 O HOH A 58 15.774 6.764 -10.953 1.00 43.67 O HETATM 3374 O HOH A 61 50.130 6.310 13.341 1.00 33.06 O HETATM 3375 O HOH A 62 19.520 15.436 6.719 1.00 47.77 O HETATM 3376 O HOH A 64 39.634 17.783 -3.965 1.00 25.54 O HETATM 3377 O HOH A 65 31.046 31.416 -19.911 1.00 48.52 O HETATM 3378 O HOH A 69 59.235 -22.691 24.617 1.00 47.56 O HETATM 3379 O HOH A 71 38.430 -7.496 24.248 1.00 43.07 O HETATM 3380 O HOH A 72 55.061 -24.322 5.891 1.00 46.14 O HETATM 3381 O HOH A 74 37.408 27.278 0.116 1.00 36.31 O HETATM 3382 O HOH A 76 39.311 -29.673 12.932 1.00 38.37 O HETATM 3383 O HOH A 77 31.253 19.582 -16.432 1.00 45.25 O HETATM 3384 O HOH A 78 48.818 -13.853 6.689 1.00 49.78 O HETATM 3385 O HOH A 79 62.577 -21.998 23.576 1.00 39.25 O HETATM 3386 O HOH A 81 57.787 -37.299 21.635 1.00 41.66 O HETATM 3387 O HOH A 84 24.366 -3.827 5.462 1.00 47.30 O HETATM 3388 O HOH A 85 36.585 -16.076 14.541 1.00 27.88 O HETATM 3389 O HOH A 86 53.882 -1.646 7.075 1.00 44.74 O HETATM 3390 O HOH A 88 62.745 -38.649 17.034 1.00 54.72 O HETATM 3391 O HOH A 90 41.380 19.004 2.192 1.00 38.12 O HETATM 3392 O HOH A 91 16.911 8.068 -0.328 1.00 46.78 O HETATM 3393 O HOH A 93 42.816 15.180 7.438 1.00 49.92 O HETATM 3394 O HOH A 95 57.062 3.902 7.856 1.00 43.77 O HETATM 3395 O HOH A 97 41.597 -19.054 25.885 1.00 43.42 O HETATM 3396 O HOH A 98 26.772 -6.582 6.818 1.00 34.41 O HETATM 3397 O HOH A 102 50.498 -27.043 9.916 1.00 38.83 O HETATM 3398 O HOH A 103 54.818 19.608 7.423 1.00 50.76 O HETATM 3399 O HOH A 104 41.780 8.467 24.351 1.00 47.87 O HETATM 3400 O HOH A 105 43.950 17.861 8.582 1.00 44.98 O HETATM 3401 O HOH A 106 35.262 20.640 -10.793 1.00 41.15 O HETATM 3402 O HOH A 107 34.451 25.087 -24.396 1.00 48.99 O HETATM 3403 O HOH A 110 36.899 28.293 -10.904 1.00 47.56 O HETATM 3404 O HOH A 111 53.222 3.215 16.486 1.00 45.58 O HETATM 3405 O HOH A 112 49.878 -2.512 6.224 1.00 46.39 O HETATM 3406 O HOH A 113 65.021 -2.173 17.954 1.00 49.43 O HETATM 3407 O HOH A 115 30.028 13.323 17.330 1.00 42.11 O HETATM 3408 O HOH A 117 9.943 9.338 -25.890 1.00 53.33 O HETATM 3409 O HOH A 119 23.007 17.724 11.400 1.00 51.41 O HETATM 3410 O HOH A 120 18.902 8.073 17.149 1.00 44.87 O HETATM 3411 O HOH A 121 37.238 -25.770 7.116 1.00 49.78 O HETATM 3412 O HOH A 125 40.215 1.706 2.809 1.00 49.07 O HETATM 3413 O HOH A 127 45.986 -42.528 29.892 1.00 51.24 O HETATM 3414 O HOH A 130 13.930 23.343 -20.935 1.00 41.06 O HETATM 3415 O HOH A 131 45.678 -30.089 5.214 1.00 27.23 O HETATM 3416 O HOH A 132 51.806 22.044 5.359 1.00 25.95 O HETATM 3417 O HOH A 133 28.703 -9.549 11.875 1.00 36.53 O HETATM 3418 O HOH A 134 29.922 -0.283 -1.556 1.00 36.31 O HETATM 3419 O HOH A 135 54.423 5.286 5.596 1.00 35.34 O HETATM 3420 O HOH A 136 58.432 -43.485 12.545 1.00 52.22 O HETATM 3421 O HOH A 137 55.969 -3.434 16.480 1.00 44.47 O HETATM 3422 O HOH A 139 42.224 19.358 10.302 1.00 37.32 O HETATM 3423 O HOH A 140 35.370 31.971 -15.593 1.00 38.99 O HETATM 3424 O HOH A 141 40.979 15.763 -5.003 1.00 44.71 O HETATM 3425 O HOH A 143 50.780 -9.823 28.075 1.00 52.06 O HETATM 3426 O HOH A 144 34.933 22.656 -12.732 1.00 32.02 O HETATM 3427 O HOH A 145 21.239 14.577 13.862 1.00 43.59 O HETATM 3428 O HOH A 146 34.197 8.959 21.810 1.00 46.42 O HETATM 3429 O HOH A 147 53.425 -27.618 29.861 1.00 38.56 O HETATM 3430 O HOH A 148 22.842 26.876 -7.985 1.00 52.73 O HETATM 3431 O HOH A 149 30.972 2.351 -8.919 1.00 34.05 O HETATM 3432 O HOH A 152 32.399 -15.184 15.010 1.00 40.95 O HETATM 3433 O HOH A 153 43.052 -30.822 16.227 1.00 32.52 O HETATM 3434 O HOH A 154 31.086 -13.285 13.119 1.00 42.57 O HETATM 3435 O HOH A 155 34.306 7.714 -2.502 1.00 41.90 O HETATM 3436 O HOH A 157 31.453 8.527 -7.372 1.00 46.85 O HETATM 3437 O HOH A 158 47.955 3.836 6.294 1.00 45.01 O HETATM 3438 O HOH A 159 50.139 -28.057 25.637 1.00 49.72 O HETATM 3439 O HOH A 160 43.986 21.227 11.980 1.00 35.32 O HETATM 3440 O HOH A 162 37.621 6.422 23.149 1.00 46.73 O HETATM 3441 O HOH A 163 42.849 14.314 3.345 1.00 36.15 O HETATM 3442 O HOH A 576 10.415 11.521 -19.607 1.00 51.13 O HETATM 3443 O HOH A 577 51.579 -16.422 26.974 1.00 38.43 O HETATM 3444 O HOH A 578 46.490 10.721 3.955 1.00 40.03 O HETATM 3445 O HOH A 579 65.438 -31.443 15.667 1.00 45.64 O HETATM 3446 O HOH A 580 55.280 12.792 9.357 1.00 38.76 O HETATM 3447 O HOH A 581 28.070 3.253 23.834 1.00 45.00 O HETATM 3448 O HOH A 582 46.070 -35.279 1.035 1.00 49.42 O HETATM 3449 O HOH A 583 63.504 -8.742 23.616 1.00 47.79 O HETATM 3450 O HOH A 584 21.030 1.096 10.583 1.00 45.39 O HETATM 3451 O HOH A 585 31.454 25.349 -20.377 1.00 37.31 O HETATM 3452 O HOH A 586 34.973 0.695 -0.207 1.00 42.94 O HETATM 3453 O HOH A 587 54.450 -16.764 26.798 1.00 42.14 O HETATM 3454 O HOH A 588 37.221 -0.752 -1.080 1.00 43.03 O HETATM 3455 O HOH A 589 33.178 4.078 -8.895 1.00 54.23 O HETATM 3456 O HOH A 590 22.416 25.373 -28.788 1.00 47.72 O HETATM 3457 O HOH A 591 49.631 -35.855 29.629 1.00 44.03 O HETATM 3458 O HOH A 592 41.702 -5.405 26.129 1.00 52.18 O HETATM 3459 O HOH A 593 38.108 -21.926 19.919 1.00 45.33 O HETATM 3460 O HOH A 594 32.995 29.450 -21.623 1.00 39.12 O HETATM 3461 O HOH A 595 34.891 -20.792 14.054 1.00 39.31 O HETATM 3462 O HOH A 596 69.883 -22.157 4.105 1.00 53.06 O HETATM 3463 O HOH A 597 43.374 -6.313 6.359 1.00 37.22 O HETATM 3464 O HOH A 598 60.830 -34.649 8.030 1.00 52.51 O HETATM 3465 O HOH A 599 49.428 11.020 -0.562 1.00 45.56 O HETATM 3466 O HOH A 600 19.972 29.475 -25.272 1.00 44.80 O HETATM 3467 O HOH A 601 60.222 -18.729 23.461 1.00 48.91 O HETATM 3468 O HOH A 602 33.152 18.417 -12.360 1.00 54.54 O HETATM 3469 O HOH A 603 29.643 -8.081 16.705 1.00 40.29 O HETATM 3470 O HOH A 604 36.559 29.051 -6.820 1.00 42.61 O HETATM 3471 O HOH A 605 7.351 24.305 -25.413 1.00 50.57 O HETATM 3472 O HOH A 606 44.611 16.447 11.000 1.00 43.98 O HETATM 3473 O HOH A 607 73.133 -14.493 11.876 1.00 52.50 O HETATM 3474 O HOH A 608 33.029 24.898 -17.925 1.00 46.58 O HETATM 3475 O HOH A 609 19.250 2.960 1.310 1.00 46.02 O HETATM 3476 O HOH A 610 28.896 13.668 -15.523 1.00 49.12 O HETATM 3477 O HOH A 611 42.205 12.915 -1.288 1.00 44.58 O HETATM 3478 O HOH A 612 41.881 6.998 4.293 1.00 36.31 O HETATM 3479 O HOH A 613 30.108 35.915 -7.323 1.00 45.98 O HETATM 3480 O HOH A 614 26.594 35.967 -6.448 1.00 47.04 O HETATM 3481 O HOH A 615 34.633 33.588 -8.973 1.00 50.16 O HETATM 3482 O HOH A 616 56.774 -39.349 0.902 1.00 53.10 O HETATM 3483 O HOH A 617 13.800 7.841 -15.535 1.00 52.14 O HETATM 3484 O HOH A 618 12.496 27.873 -20.540 1.00 50.59 O HETATM 3485 O HOH A 619 42.929 -24.554 26.993 1.00 50.77 O HETATM 3486 O HOH A 620 53.696 16.303 8.924 1.00 40.15 O HETATM 3487 O HOH A 621 50.749 -18.628 28.716 1.00 52.03 O HETATM 3488 O HOH A 622 23.114 -2.179 1.479 1.00 47.87 O HETATM 3489 O HOH A 623 35.835 -7.694 23.053 1.00 48.59 O HETATM 3490 O HOH A 624 40.959 8.309 2.046 1.00 46.79 O HETATM 3491 O HOH A 625 41.135 -24.284 23.043 1.00 46.60 O HETATM 3492 O HOH A 626 53.096 -23.498 3.463 1.00 49.18 O HETATM 3493 O HOH A 627 60.375 -9.216 9.873 1.00 53.59 O HETATM 3494 O HOH A 628 21.907 3.712 17.687 1.00 52.19 O HETATM 3495 O HOH A 629 42.913 16.684 1.797 1.00 46.34 O HETATM 3496 O HOH A 630 55.058 3.169 14.562 1.00 51.38 O HETATM 3497 O HOH A 631 40.646 -34.596 32.883 1.00 53.00 O HETATM 3498 O HOH A 632 18.168 4.475 -3.690 1.00 54.17 O HETATM 3499 O HOH A 633 27.239 43.426 -10.884 1.00 44.09 O HETATM 3500 O HOH A 634 63.492 -1.125 15.755 1.00 54.37 O HETATM 3501 O HOH A 635 22.264 32.113 -2.503 1.00 50.73 O HETATM 3502 O HOH A 636 28.362 42.909 -8.315 1.00 49.91 O HETATM 3503 O HOH A 637 45.285 7.474 3.322 1.00 53.25 O HETATM 3504 O HOH A 638 34.944 -22.789 7.079 1.00 51.26 O HETATM 3505 O HOH A 639 32.042 -6.339 15.729 1.00 54.50 O HETATM 3506 O HOH A 640 39.970 -25.568 6.679 1.00 33.87 O HETATM 3507 O HOH B 28 41.677 -4.566 0.323 1.00 49.96 O HETATM 3508 O HOH B 34 41.845 -4.463 4.380 1.00 44.50 O HETATM 3509 O HOH B 50 43.454 -30.928 1.251 1.00 38.05 O HETATM 3510 O HOH B 56 33.605 -12.558 6.027 1.00 34.34 O HETATM 3511 O HOH B 118 32.426 -0.532 0.121 1.00 34.41 O HETATM 3512 O HOH B 142 43.912 -31.757 3.760 1.00 42.21 O HETATM 3513 O HOH B 156 39.988 -19.304 1.618 1.00 34.00 O HETATM 3514 O HOH B 161 41.291 -21.145 0.174 1.00 42.53 O HETATM 3515 O HOH B 170 31.306 0.074 -10.512 1.00 49.67 O HETATM 3516 O HOH B 172 34.826 4.904 -5.173 1.00 52.15 O HETATM 3517 O HOH B 186 32.745 -16.587 4.474 1.00 44.54 O HETATM 3518 O HOH B 204 43.176 -16.447 3.127 1.00 45.29 O HETATM 3519 O HOH B 213 40.799 -17.664 3.806 1.00 38.56 O HETATM 3520 O HOH B 266 47.327 -21.007 2.461 1.00 49.95 O MASTER 473 0 0 30 0 0 0 6 3518 2 0 33 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
1si2
RCSB PDB
PDBbind
9-mer
1si3
RCSB PDB
PDBbind
9-mer
3gib
RCSB PDB
PDBbind
9-mer
3h15
RCSB PDB
PDBbind
9-mer
3k5q
RCSB PDB
PDBbind
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3k5y
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PDBbind
9-mer
3k61
RCSB PDB
PDBbind
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PDBbind
9-mer
3k64
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PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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Entry Information
PDB ID
3k5z
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
2.4(Å)
Affinity (Kd/Ki/IC50)
Kd=39.4nM
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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