Browse entries in the PDBbind-CN Database
HEADER SIGNALING PROTEIN 15-APR-09 2WFX TITLE CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN HUMAN HEDGEHOG- TITLE 2 INTERACTING PROTEIN HIP AND SONIC HEDGEHOG IN THE PRESENCE TITLE 3 OF CALCIUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: SONIC HEDGEHOG PROTEIN N-PRODUCT; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL SIGNALLING DOMAIN OF SHH, RESIDUES COMPND 5 40-191; COMPND 6 SYNONYM: SONIC HEDGEHOG SHH, SONIC HEDGEHOG PROTEIN, COMPND 7 HHG-1, SHH; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: HEDGEHOG-INTERACTING PROTEIN; COMPND 11 CHAIN: B; COMPND 12 FRAGMENT: C-TERMINAL DOMAIN OF HIP, RESIDUES 214-670; COMPND 13 SYNONYM: HHIP, HIP, HEDGEHOG-INTERACTING PROTEIN HIP; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HUMAN EMBRYONIC KIDNEY (HEK) SOURCE 9 293T CELLS; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHLSEC; SOURCE 11 OTHER_DETAILS: IMAGE CLONE; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: HUMAN EMBRYONIC KIDNEY (HEK) SOURCE 20 293T CELLS; SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PHLSEC; SOURCE 22 OTHER_DETAILS: IMAGE CLONE KEYWDS SIGNALING PROTEIN, AUTOCATALYTIC CLEAVAGE, PROTEASE, KEYWDS 2 MEMBRANE, SECRETED, PALMITATE, HYDROLASE, SIGNAL KEYWDS 3 TRANSDUCTION, DEVELOPMENTAL PROTEIN, LIPOPROTEIN, KEYWDS 4 DEVELOPMENT, GLYCOPROTEIN, CELL MEMBRANE, DISULFIDE BOND, KEYWDS 5 EGF-LIKE DOMAIN, HEDGEHOG SIGNALING EXPDTA X-RAY DIFFRACTION AUTHOR B.BISHOP,A.R.ARICESCU,K.HARLOS,C.A.O'CALLAGHAN,E.Y.JONES, AUTHOR 2 C.SIEBOLD REVDAT 2 21-JUL-09 2WFX 1 JRNL REVDAT 1 30-JUN-09 2WFX 0 JRNL AUTH B.BISHOP,A.R.ARICESCU,K.HARLOS,C.A.O'CALLAGHAN, JRNL AUTH 2 E.Y.JONES,C.SIEBOLD JRNL TITL STRUCTURAL INSIGHTS INTO HEDGEHOG LIGAND JRNL TITL 2 SEQUESTRATION BY THE HUMAN HEDGEHOG-INTERACTING JRNL TITL 3 PROTEIN HIP JRNL REF NAT.STRUCT.MOL.BIOL. V. 16 698 2009 JRNL REFN ISSN 1545-9993 JRNL PMID 19561611 JRNL DOI 10.1038/NSMB.1607 REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.200 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.774 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.33 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.04 REMARK 3 NUMBER OF REFLECTIONS : 13372 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.2448 REMARK 3 R VALUE (WORKING SET) : 0.2400 REMARK 3 FREE R VALUE : 0.3003 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.9 REMARK 3 FREE R VALUE TEST SET COUNT : 1056 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 19.7739 - 6.3381 1.00 1634 151 0.2674 0.3053 REMARK 3 2 6.3381 - 5.0585 1.00 1576 145 0.1969 0.2406 REMARK 3 3 5.0585 - 4.4272 1.00 1547 128 0.1607 0.2254 REMARK 3 4 4.4272 - 4.0262 1.00 1575 109 0.1814 0.2167 REMARK 3 5 4.0262 - 3.7397 0.98 1509 118 0.2418 0.3412 REMARK 3 6 3.7397 - 3.5205 0.95 1448 135 0.3012 0.3834 REMARK 3 7 3.5205 - 3.3451 1.00 1508 138 0.2856 0.3727 REMARK 3 8 3.3451 - 3.2001 1.00 1519 132 0.3272 0.3853 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.248 REMARK 3 B_SOL : 7.909 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.48 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.48 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 60.28 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 12.8101 REMARK 3 B22 (A**2) : 12.8101 REMARK 3 B33 (A**2) : -25.6202 REMARK 3 B12 (A**2) : 0.0000 REMARK 3 B13 (A**2) : -0.0000 REMARK 3 B23 (A**2) : 0.0000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 4592 REMARK 3 ANGLE : 0.524 6166 REMARK 3 CHIRALITY : 0.032 667 REMARK 3 PLANARITY : 0.002 810 REMARK 3 DIHEDRAL : 13.433 1680 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND RESID 40:50) REMARK 3 ORIGIN FOR THE GROUP (A): -15.5353 22.8480 0.3450 REMARK 3 T TENSOR REMARK 3 T11: 0.5297 T22: 1.0370 REMARK 3 T33: 0.6838 T12: -0.1245 REMARK 3 T13: -0.1163 T23: -0.2138 REMARK 3 L TENSOR REMARK 3 L11: -2.4294 L22: 4.9135 REMARK 3 L33: 2.1742 L12: -3.1334 REMARK 3 L13: 4.7320 L23: 1.6174 REMARK 3 S TENSOR REMARK 3 S11: -0.0499 S12: -0.8210 S13: -1.2316 REMARK 3 S21: 0.4665 S22: 1.4941 S23: -0.7643 REMARK 3 S31: -0.0026 S32: -0.2846 S33: -1.1499 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND RESID 51:77) REMARK 3 ORIGIN FOR THE GROUP (A): -11.8330 34.0435 -19.9891 REMARK 3 T TENSOR REMARK 3 T11: 0.8607 T22: 1.0365 REMARK 3 T33: 0.4562 T12: 0.0941 REMARK 3 T13: -0.0032 T23: -0.0106 REMARK 3 L TENSOR REMARK 3 L11: 3.1371 L22: 7.5743 REMARK 3 L33: -4.9182 L12: -1.8838 REMARK 3 L13: -0.4953 L23: 1.6011 REMARK 3 S TENSOR REMARK 3 S11: 0.5495 S12: 1.0968 S13: 0.1377 REMARK 3 S21: -1.5653 S22: -0.4481 S23: -0.2300 REMARK 3 S31: 0.0118 S32: -0.2764 S33: -0.0682 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN A AND RESID 78:129) REMARK 3 ORIGIN FOR THE GROUP (A): -26.3295 36.9906 -9.4577 REMARK 3 T TENSOR REMARK 3 T11: 0.5165 T22: 0.9748 REMARK 3 T33: 0.5970 T12: 0.0075 REMARK 3 T13: -0.0886 T23: 0.0304 REMARK 3 L TENSOR REMARK 3 L11: 1.3094 L22: 1.4462 REMARK 3 L33: 2.6502 L12: -0.4983 REMARK 3 L13: -0.7001 L23: 0.5389 REMARK 3 S TENSOR REMARK 3 S11: 0.2247 S12: 1.1195 S13: -0.1708 REMARK 3 S21: -0.3408 S22: -0.1539 S23: 0.4019 REMARK 3 S31: -0.1673 S32: -1.1965 S33: -0.1407 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN A AND RESID 130:188) REMARK 3 ORIGIN FOR THE GROUP (A): -16.9924 32.7139 -5.8563 REMARK 3 T TENSOR REMARK 3 T11: 0.2992 T22: 0.7566 REMARK 3 T33: 0.4464 T12: 0.0356 REMARK 3 T13: -0.0703 T23: -0.1785 REMARK 3 L TENSOR REMARK 3 L11: 1.1435 L22: 0.0843 REMARK 3 L33: 1.3815 L12: 0.2477 REMARK 3 L13: 1.2833 L23: -0.5812 REMARK 3 S TENSOR REMARK 3 S11: -0.2039 S12: 0.2014 S13: 0.1094 REMARK 3 S21: 0.0043 S22: 0.3389 S23: 0.0046 REMARK 3 S31: 0.1828 S32: -0.7050 S33: -0.1783 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN B AND RESID 215:276) REMARK 3 ORIGIN FOR THE GROUP (A): 20.1565 45.0919 17.4177 REMARK 3 T TENSOR REMARK 3 T11: 0.3652 T22: 0.7194 REMARK 3 T33: 0.5277 T12: -0.0163 REMARK 3 T13: -0.0330 T23: -0.0506 REMARK 3 L TENSOR REMARK 3 L11: 1.5604 L22: 0.1235 REMARK 3 L33: 0.4431 L12: -0.7924 REMARK 3 L13: -0.1874 L23: 0.4841 REMARK 3 S TENSOR REMARK 3 S11: -0.0197 S12: 0.4995 S13: 0.3204 REMARK 3 S21: -0.0475 S22: -0.0054 S23: -0.1371 REMARK 3 S31: -0.0953 S32: 0.4436 S33: -0.0138 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN B AND RESID 277:442) REMARK 3 ORIGIN FOR THE GROUP (A): 3.0018 34.6198 12.6870 REMARK 3 T TENSOR REMARK 3 T11: 0.2723 T22: 0.7624 REMARK 3 T33: 0.3937 T12: 0.0659 REMARK 3 T13: -0.0213 T23: -0.0981 REMARK 3 L TENSOR REMARK 3 L11: -0.0457 L22: 1.3461 REMARK 3 L33: 1.1187 L12: -0.3737 REMARK 3 L13: 0.4248 L23: -0.3078 REMARK 3 S TENSOR REMARK 3 S11: -0.0491 S12: 0.2367 S13: -0.1060 REMARK 3 S21: 0.0121 S22: -0.0761 S23: 0.0342 REMARK 3 S31: 0.0209 S32: -0.0927 S33: 0.0906 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN B AND RESID 443:530) REMARK 3 ORIGIN FOR THE GROUP (A): -2.1887 44.9735 30.0318 REMARK 3 T TENSOR REMARK 3 T11: 0.1597 T22: 0.7029 REMARK 3 T33: 0.4017 T12: 0.1170 REMARK 3 T13: 0.0120 T23: -0.1089 REMARK 3 L TENSOR REMARK 3 L11: 0.7905 L22: 1.2980 REMARK 3 L33: 1.0919 L12: 0.7218 REMARK 3 L13: 0.3897 L23: 0.0143 REMARK 3 S TENSOR REMARK 3 S11: -0.0249 S12: -0.5464 S13: 0.2577 REMARK 3 S21: 0.1862 S22: -0.0851 S23: 0.3193 REMARK 3 S31: 0.0958 S32: -0.3845 S33: 0.0153 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN B AND RESID 531:637) REMARK 3 ORIGIN FOR THE GROUP (A): 17.2663 35.2201 22.3916 REMARK 3 T TENSOR REMARK 3 T11: 0.2732 T22: 0.7627 REMARK 3 T33: 0.3600 T12: 0.1215 REMARK 3 T13: 0.0217 T23: -0.0559 REMARK 3 L TENSOR REMARK 3 L11: 1.2024 L22: 1.2333 REMARK 3 L33: -0.0351 L12: -0.1183 REMARK 3 L13: -0.1388 L23: -0.0028 REMARK 3 S TENSOR REMARK 3 S11: 0.2409 S12: -0.2881 S13: 0.1975 REMARK 3 S21: -0.1675 S22: -0.1381 S23: -0.5438 REMARK 3 S31: 0.0483 S32: 0.0114 S33: -0.1052 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN B AND RESID 638:666) REMARK 3 ORIGIN FOR THE GROUP (A): 15.4861 -1.5974 -6.2923 REMARK 3 T TENSOR REMARK 3 T11: 1.6644 T22: 1.5525 REMARK 3 T33: 1.2350 T12: 0.5014 REMARK 3 T13: -0.2514 T23: -0.1946 REMARK 3 L TENSOR REMARK 3 L11: 8.3785 L22: 3.5831 REMARK 3 L33: 1.8269 L12: -0.2190 REMARK 3 L13: 2.6373 L23: -0.9309 REMARK 3 S TENSOR REMARK 3 S11: 0.3035 S12: 0.1657 S13: 1.0410 REMARK 3 S21: -1.0186 S22: -0.9270 S23: -0.1415 REMARK 3 S31: 0.6768 S32: -0.1210 S33: 0.5289 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 2WFX COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-09. REMARK 100 THE PDBE ID CODE IS EBI-39471. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13529 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.20 REMARK 200 RESOLUTION RANGE LOW (A) : 20.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 6.5 REMARK 200 R MERGE (I) : 0.19 REMARK 200 R SYM (I) : NULL REMARK 200
FOR THE DATA SET : 10.60 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.30 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.7 REMARK 200 R MERGE FOR SHELL (I) : 0.73 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200
FOR SHELL : 2.50 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 ENTRIES 1VHH AND 2WFT REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):3.14 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 4.6 REMARK 280 0.5 M POTASSIUM THIOCYANATE 5 MM CACL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 114.28600 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 57.14300 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 57.14300 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 114.28600 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 GENERATING THE BIOMOLECULE 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: 2360 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.88 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 HIS B 279 REMARK 465 GLY B 279 REMARK 465 GLN B 308 REMARK 465 GLU B 309 REMARK 465 ARG B 310 REMARK 465 TRP B 311 REMARK 465 ALA B 312 REMARK 465 ILE B 313 REMARK 465 GLY B 314 REMARK 465 PRO B 315 REMARK 465 GLY B 458 REMARK 465 LYS B 459 REMARK 465 GLY B 539 REMARK 465 THR B 540 REMARK 465 SER B 541 REMARK 465 GLY B 542 REMARK 465 SER B 543 REMARK 465 CYS B 544 REMARK 465 ARG B 545 REMARK 465 GLY B 546 REMARK 465 TYR B 547 REMARK 465 PHE B 548 REMARK 465 SER B 549 REMARK 465 SER B 569 REMARK 465 LYS B 570 REMARK 465 SER B 571 REMARK 465 MET B 572 REMARK 465 THR B 573 REMARK 465 LYS B 659 REMARK 465 LYS B 660 REMARK 465 GLN B 669 REMARK 465 VAL B 670 REMARK 465 ASP B 671 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 189 CG CD OE1 OE2 REMARK 470 SER A 191 OG REMARK 470 LYS B 277 CG CD CE NZ REMARK 470 ARG B 460 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 651 CG CD NE CZ NH1 NH2 REMARK 470 TYR B 661 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU B 667 CA C O CB CG CD OE1 OE2 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 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 LYS A 55 54.04 -104.95 REMARK 500 ALA A 59 -129.10 -103.31 REMARK 500 ASN A 92 -5.10 69.41 REMARK 500 ASP A 132 -172.96 152.33 REMARK 500 HIS A 134 -13.83 171.90 REMARK 500 GLU A 137 152.21 -41.22 REMARK 500 ARG A 154 -3.72 63.23 REMARK 500 ASP A 155 104.80 -57.88 REMARK 500 TRP A 173 108.18 -169.59 REMARK 500 GLU A 177 -72.29 -45.50 REMARK 500 GLN B 240 27.84 49.95 REMARK 500 ILE B 268 30.52 -141.35 REMARK 500 SER B 274 -114.31 -74.56 REMARK 500 LEU B 285 -64.24 -92.92 REMARK 500 ARG B 350 41.97 -108.44 REMARK 500 ASP B 400 38.05 -94.11 REMARK 500 THR B 418 49.72 -109.06 REMARK 500 ASN B 419 -16.73 -157.46 REMARK 500 HIS B 430 -82.35 -132.63 REMARK 500 ASP B 431 73.95 -117.23 REMARK 500 SER B 462 -140.52 -115.75 REMARK 500 ALA B 463 110.62 -174.03 REMARK 500 SER B 487 -72.66 -46.71 REMARK 500 GLN B 523 -153.22 -103.98 REMARK 500 THR B 527 -26.71 67.05 REMARK 500 ASN B 576 9.64 -159.08 REMARK 500 MET B 590 80.71 -151.94 REMARK 500 ALA B 596 108.56 -166.11 REMARK 500 LEU B 611 48.69 -142.65 REMARK 500 ARG B 644 -97.91 -93.07 REMARK 500 VAL B 650 -89.51 -128.51 REMARK 500 PRO B 652 105.49 -41.82 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B1668 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TYR B 474 O REMARK 620 2 GLU B 475 OE1 66.4 REMARK 620 3 ARG B 410 O 126.7 150.3 REMARK 620 4 ASN B 412 O 70.9 124.2 84.8 REMARK 620 5 ASP B 473 OD1 84.7 90.8 66.8 119.3 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B1669 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ILE B 446 O REMARK 620 2 PRO B 441 O 114.7 REMARK 620 3 ASP B 443 O 75.8 83.3 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1193 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 96 OD1 REMARK 620 2 ASP A 96 OD2 50.2 REMARK 620 3 THR A 126 O 101.1 74.3 REMARK 620 4 GLU A 90 OE2 150.1 144.6 108.2 REMARK 620 5 GLU A 91 OE1 78.5 118.4 158.7 72.2 REMARK 620 6 GLU A 91 OE2 68.2 78.8 151.0 88.0 48.6 REMARK 620 7 GLU A 90 OE1 140.8 94.7 81.3 52.4 112.7 90.8 REMARK 620 8 GLU A 127 OE1 98.6 133.4 81.3 80.6 77.7 125.9 120.2 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1194 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 91 OE1 REMARK 620 2 GLU A 127 OE2 96.5 REMARK 620 3 ASP A 130 OD1 153.3 89.1 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1192 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 141 NE2 REMARK 620 2 ASP A 148 OD1 97.5 REMARK 620 3 HIS A 183 ND1 96.0 94.2 REMARK 620 4 ASP B 383 OD1 87.1 128.0 137.1 REMARK 620 5 ASP B 383 OD2 147.5 91.7 114.4 63.2 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1192 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1193 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1194 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1667 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1668 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1669 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B1670 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2WFT RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN HIP REMARK 900 ECTODOMAIN REMARK 900 RELATED ID: 2WG4 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN REMARK 900 HUMAN HEDGEHOG-INTERACTING PROTEIN HIP AND REMARK 900 SONIC HEDGEHOG WITHOUT CALCIUM REMARK 900 RELATED ID: 1VHH RELATED DB: PDB REMARK 900 MOL_ID: 1; MOLECULE: SONIC HEDGEHOG; CHAIN: REMARK 900 NULL; DOMAIN: AMINO-TERMINAL DOMAIN (RESIDUES REMARK 900 34 - 195); SYNONYM: HHG-1, VHH-1; REMARK 900 ENGINEERED: YES REMARK 900 RELATED ID: 2WG3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN REMARK 900 HUMAN HEDGEHOG-INTERACTING PROTEIN HIP AND REMARK 900 DESERT HEDGEHOG WITHOUT CALCIUM REMARK 900 RELATED ID: 2WGR RELATED DB: PDB REMARK 900 COMBINING CRYSTALLOGRAPHY AND MOLECULAR DYNAMICS REMARK 900 : THE CASE OF SCHISTOSOMA MANSONI REMARK 900 PHOSPHOLIPID GLUTATHIONE PEROXIDASE REMARK 900 RELATED ID: 2WGQ RELATED DB: PDB REMARK 900 ZINC SUBSTITUTED E COLI COPPER AMINE OXIDASE REMARK 900 , A MODEL FOR THE PRECURSOR FOR 2,4,5- REMARK 900 TRIHYDROXYPHENYLALANINEQUINONE FORMATION DBREF 2WFX A 40 191 UNP Q62226 SHH_MOUSE 40 191 DBREF 2WFX B 214 670 UNP Q96QV1 HHIP_HUMAN 214 670 SEQRES 1 A 152 LEU THR PRO LEU ALA TYR LYS GLN PHE ILE PRO ASN VAL SEQRES 2 A 152 ALA GLU LYS THR LEU GLY ALA SER GLY ARG TYR GLU GLY SEQRES 3 A 152 LYS ILE THR ARG ASN SER GLU ARG PHE LYS GLU LEU THR SEQRES 4 A 152 PRO ASN TYR ASN PRO ASP ILE ILE PHE LYS ASP GLU GLU SEQRES 5 A 152 ASN THR GLY ALA ASP ARG LEU MET THR GLN ARG CYS LYS SEQRES 6 A 152 ASP LYS LEU ASN ALA LEU ALA ILE SER VAL MET ASN GLN SEQRES 7 A 152 TRP PRO GLY VAL LYS LEU ARG VAL THR GLU GLY TRP ASP SEQRES 8 A 152 GLU ASP GLY HIS HIS SER GLU GLU SER LEU HIS TYR GLU SEQRES 9 A 152 GLY ARG ALA VAL ASP ILE THR THR SER ASP ARG ASP ARG SEQRES 10 A 152 SER LYS TYR GLY MET LEU ALA ARG LEU ALA VAL GLU ALA SEQRES 11 A 152 GLY PHE ASP TRP VAL TYR TYR GLU SER LYS ALA HIS ILE SEQRES 12 A 152 HIS CYS SER VAL LYS ALA GLU ASN SER SEQRES 1 B 457 HIS ASN CYS PHE CYS ILE GLN GLU VAL VAL SER GLY LEU SEQRES 2 B 457 ARG GLN PRO VAL GLY ALA LEU HIS SER GLY ASP GLY SER SEQRES 3 B 457 GLN ARG LEU PHE ILE LEU GLU LYS GLU GLY TYR VAL LYS SEQRES 4 B 457 ILE LEU THR PRO GLU GLY GLU ILE PHE LYS GLU PRO TYR SEQRES 5 B 457 LEU ASP ILE HIS LYS LEU VAL GLN SER GLY ILE LYS GLY SEQRES 6 B 457 GLY ASP GLU ARG GLY LEU LEU SER LEU ALA PHE HIS PRO SEQRES 7 B 457 ASN TYR LYS LYS ASN GLY LYS LEU TYR VAL SER TYR THR SEQRES 8 B 457 THR ASN GLN GLU ARG TRP ALA ILE GLY PRO HIS ASP HIS SEQRES 9 B 457 ILE LEU ARG VAL VAL GLU TYR THR VAL SER ARG LYS ASN SEQRES 10 B 457 PRO HIS GLN VAL ASP LEU ARG THR ALA ARG VAL PHE LEU SEQRES 11 B 457 GLU VAL ALA GLU LEU HIS ARG LYS HIS LEU GLY GLY GLN SEQRES 12 B 457 LEU LEU PHE GLY PRO ASP GLY PHE LEU TYR ILE ILE LEU SEQRES 13 B 457 GLY ASP GLY MET ILE THR LEU ASP ASP MET GLU GLU MET SEQRES 14 B 457 ASP GLY LEU SER ASP PHE THR GLY SER VAL LEU ARG LEU SEQRES 15 B 457 ASP VAL ASP THR ASP MET CYS ASN VAL PRO TYR SER ILE SEQRES 16 B 457 PRO ARG SER ASN PRO HIS PHE ASN SER THR ASN GLN PRO SEQRES 17 B 457 PRO GLU VAL PHE ALA HIS GLY LEU HIS ASP PRO GLY ARG SEQRES 18 B 457 CYS ALA VAL ASP ARG HIS PRO THR ASP ILE ASN ILE ASN SEQRES 19 B 457 LEU THR ILE LEU CYS SER ASP SER ASN GLY LYS ASN ARG SEQRES 20 B 457 SER SER ALA ARG ILE LEU GLN ILE ILE LYS GLY LYS ASP SEQRES 21 B 457 TYR GLU SER GLU PRO SER LEU LEU GLU PHE LYS PRO PHE SEQRES 22 B 457 SER ASN GLY PRO LEU VAL GLY GLY PHE VAL TYR ARG GLY SEQRES 23 B 457 CYS GLN SER GLU ARG LEU TYR GLY SER TYR VAL PHE GLY SEQRES 24 B 457 ASP ARG ASN GLY ASN PHE LEU THR LEU GLN GLN SER PRO SEQRES 25 B 457 VAL THR LYS GLN TRP GLN GLU LYS PRO LEU CYS LEU GLY SEQRES 26 B 457 THR SER GLY SER CYS ARG GLY TYR PHE SER GLY HIS ILE SEQRES 27 B 457 LEU GLY PHE GLY GLU ASP GLU LEU GLY GLU VAL TYR ILE SEQRES 28 B 457 LEU SER SER SER LYS SER MET THR GLN THR HIS ASN GLY SEQRES 29 B 457 LYS LEU TYR LYS ILE VAL ASP PRO LYS ARG PRO LEU MET SEQRES 30 B 457 PRO GLU GLU CYS ARG ALA THR VAL GLN PRO ALA GLN THR SEQRES 31 B 457 LEU THR SER GLU CYS SER ARG LEU CYS ARG ASN GLY TYR SEQRES 32 B 457 CYS THR PRO THR GLY LYS CYS CYS CYS SER PRO GLY TRP SEQRES 33 B 457 GLU GLY ASP PHE CYS ARG THR ALA LYS CYS GLU PRO ALA SEQRES 34 B 457 CYS ARG HIS GLY GLY VAL CYS VAL ARG PRO ASN LYS CYS SEQRES 35 B 457 LEU CYS LYS LYS GLY TYR LEU GLY PRO GLN CYS GLU GLN SEQRES 36 B 457 VAL ASP HET ZN A1192 1 HET CA A1193 1 HET CA A1194 1 HET NA B1667 1 HET NA B1668 1 HET NA B1669 1 HET CA B1670 1 HETNAM NA SODIUM ION HETNAM CA CALCIUM ION HETNAM ZN ZINC ION FORMUL 3 NA 3(NA 1+) FORMUL 4 CA 3(CA 2+) FORMUL 5 ZN ZN 2+ HELIX 1 1 SER A 71 LEU A 77 5 7 HELIX 2 2 THR A 100 TRP A 118 1 19 HELIX 3 3 ASP A 155 SER A 157 5 3 HELIX 4 4 LYS A 158 GLY A 170 1 13 HELIX 5 5 ASN B 292 GLY B 297 1 6 HELIX 6 6 THR B 375 MET B 382 1 8 HELIX 7 7 PRO B 591 ARG B 595 5 5 HELIX 8 8 SER B 606 CYS B 612 1 7 SHEET 1 AA 6 PHE A 48 ILE A 49 0 SHEET 2 AA 6 TRP A 173 SER A 178 -1 O VAL A 174 N ILE A 49 SHEET 3 AA 6 HIS A 181 SER A 185 -1 O HIS A 181 N SER A 178 SHEET 4 AA 6 ALA A 146 THR A 151 -1 O VAL A 147 N CYS A 184 SHEET 5 AA 6 LEU A 123 GLU A 127 -1 O ARG A 124 N THR A 150 SHEET 6 AA 6 ILE A 85 PHE A 87 1 O ILE A 86 N VAL A 125 SHEET 1 BA 4 CYS B 218 LEU B 226 0 SHEET 2 BA 4 GLY B 577 VAL B 583 -1 O GLY B 577 N LEU B 226 SHEET 3 BA 4 VAL B 562 SER B 566 -1 O VAL B 562 N ILE B 582 SHEET 4 BA 4 ILE B 551 GLU B 556 -1 N LEU B 552 O LEU B 565 SHEET 1 BB 4 PRO B 229 LEU B 233 0 SHEET 2 BB 4 PHE B 243 GLU B 246 -1 O PHE B 243 N LEU B 233 SHEET 3 BB 4 TYR B 250 LYS B 252 -1 O TYR B 250 N GLU B 246 SHEET 4 BB 4 LEU B 266 ASP B 267 -1 O LEU B 266 N VAL B 251 SHEET 1 BC 4 LEU B 284 PHE B 289 0 SHEET 2 BC 4 LYS B 298 THR B 305 -1 O TYR B 300 N ALA B 288 SHEET 3 BC 4 HIS B 317 VAL B 326 -1 O ILE B 318 N THR B 305 SHEET 4 BC 4 VAL B 334 GLU B 347 -1 N ASP B 335 O THR B 325 SHEET 1 BD 4 GLN B 356 PHE B 359 0 SHEET 2 BD 4 LEU B 365 ILE B 368 -1 O TYR B 366 N LEU B 358 SHEET 3 BD 4 SER B 391 LEU B 395 -1 O LEU B 393 N ILE B 367 SHEET 4 BD 4 VAL B 424 HIS B 427 -1 N PHE B 425 O VAL B 392 SHEET 1 BE 4 ALA B 436 ASP B 438 0 SHEET 2 BE 4 ILE B 446 CYS B 452 -1 O THR B 449 N ASP B 438 SHEET 3 BE 4 ARG B 464 ILE B 469 -1 O ARG B 464 N CYS B 452 SHEET 4 BE 4 LEU B 481 GLU B 482 -1 O LEU B 481 N ILE B 465 SHEET 1 BF 4 GLY B 493 VAL B 496 0 SHEET 2 BF 4 TYR B 509 GLY B 512 -1 O VAL B 510 N PHE B 495 SHEET 3 BF 4 PHE B 518 GLN B 522 -1 O LEU B 519 N PHE B 511 SHEET 4 BF 4 GLN B 531 LEU B 535 -1 O GLN B 531 N GLN B 522 SHEET 1 BG 2 GLY B 615 CYS B 617 0 SHEET 2 BG 2 CYS B 623 CYS B 625 -1 O CYS B 624 N TYR B 616 SHEET 1 BH 2 TRP B 629 GLU B 630 0 SHEET 2 BH 2 THR B 636 ALA B 637 -1 O THR B 636 N GLU B 630 SSBOND 1 CYS B 216 CYS B 536 1555 1555 2.03 SSBOND 2 CYS B 402 CYS B 624 1555 1555 2.03 SSBOND 3 CYS B 435 CYS B 452 1555 1555 2.03 SSBOND 4 CYS B 500 CYS B 594 1555 1555 2.03 SSBOND 5 CYS B 608 CYS B 617 1555 1555 2.03 SSBOND 6 CYS B 612 CYS B 623 1555 1555 2.03 SSBOND 7 CYS B 625 CYS B 634 1555 1555 2.03 SSBOND 8 CYS B 639 CYS B 649 1555 1555 2.03 SSBOND 9 CYS B 643 CYS B 655 1555 1555 2.03 SSBOND 10 CYS B 657 CYS B 666 1555 1555 2.03 LINK ZN ZN A1192 NE2 HIS A 141 1555 1555 2.01 LINK ZN ZN A1192 OD2 ASP B 383 1555 1555 2.07 LINK ZN ZN A1192 OD1 ASP B 383 1555 1555 2.12 LINK ZN ZN A1192 ND1 HIS A 183 1555 1555 2.00 LINK ZN ZN A1192 OD1 ASP A 148 1555 1555 2.03 LINK CA CA A1193 OD1 ASP A 96 1555 1555 2.75 LINK CA CA A1193 OD2 ASP A 96 1555 1555 2.36 LINK CA CA A1193 O THR A 126 1555 1555 2.39 LINK CA CA A1193 OE2 GLU A 90 1555 1555 2.30 LINK CA CA A1193 OE1 GLU A 91 1555 1555 2.37 LINK CA CA A1193 OE1 GLU A 127 1555 1555 2.40 LINK CA CA A1193 OE1 GLU A 90 1555 1555 2.63 LINK CA CA A1193 OE2 GLU A 91 1555 1555 2.86 LINK CA CA A1194 OE1 GLU A 91 1555 1555 2.39 LINK CA CA A1194 OE2 GLU A 127 1555 1555 2.29 LINK CA CA A1194 OD1 ASP A 130 1555 1555 2.40 LINK NA NA B1668 OE1 GLU B 475 1555 1555 2.50 LINK NA NA B1668 O TYR B 474 1555 1555 2.57 LINK NA NA B1668 O ASN B 412 1555 1555 2.51 LINK NA NA B1668 O ARG B 410 1555 1555 2.53 LINK NA NA B1668 OD1 ASP B 473 1555 1555 2.51 LINK NA NA B1669 O ASP B 443 1555 1555 2.49 LINK NA NA B1669 O PRO B 441 1555 1555 2.55 LINK NA NA B1669 O ILE B 446 1555 1555 2.47 LINK CA CA B1670 O GLY B 354 1555 1555 3.09 CISPEP 1 ILE A 49 PRO A 50 0 0.12 CISPEP 2 GLY B 354 GLY B 355 0 -6.68 CISPEP 3 GLU B 640 PRO B 641 0 0.49 CISPEP 4 GLY B 646 GLY B 647 0 -0.76 SITE 1 AC1 4 HIS A 141 ASP A 148 HIS A 183 ASP B 383 SITE 1 AC2 5 GLU A 90 GLU A 91 ASP A 96 THR A 126 SITE 2 AC2 5 GLU A 127 SITE 1 AC3 3 GLU A 91 GLU A 127 ASP A 130 SITE 1 AC4 2 CYS B 623 GLY B 631 SITE 1 AC5 5 ARG B 410 ASN B 412 ASP B 473 TYR B 474 SITE 2 AC5 5 GLU B 475 SITE 1 AC6 3 PRO B 441 ASP B 443 ILE B 446 SITE 1 AC7 1 GLY B 354 CRYST1 89.150 89.150 171.429 90.00 90.00 120.00 P 32 2 1 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 0.011217 0.006476 0.000000 0.00000 SCALE2 0.000000 0.012952 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005833 0.00000 ATOM 1 N LEU A 40 -27.073 17.102 2.016 1.00 77.78 N ANISOU 1 N LEU A 40 6245 13739 9569 -1720 -1614 5374 N ATOM 2 CA LEU A 40 -26.046 17.955 1.425 1.00 74.68 C ANISOU 2 CA LEU A 40 6132 13210 9031 -1654 -1514 4451 C ATOM 3 C LEU A 40 -25.120 18.545 2.488 1.00 80.66 C ANISOU 3 C LEU A 40 7079 14258 9310 -1340 -1384 4124 C ATOM 4 O LEU A 40 -25.525 19.425 3.248 1.00 81.96 O ANISOU 4 O LEU A 40 7315 14876 8950 -1060 -1042 4304 O ATOM 5 CB LEU A 40 -26.689 19.082 0.610 1.00 74.67 C ANISOU 5 CB LEU A 40 6251 13272 8849 -1662 -1151 4192 C ATOM 6 CG LEU A 40 -27.304 18.731 -0.748 1.00 76.91 C ANISOU 6 CG LEU A 40 6507 13070 9646 -1920 -1302 4179 C ATOM 7 CD1 LEU A 40 -28.096 19.905 -1.309 1.00 70.19 C ANISOU 7 CD1 LEU A 40 5831 12326 8510 -1877 -936 3963 C ATOM 8 CD2 LEU A 40 -26.230 18.292 -1.732 1.00 78.40 C ANISOU 8 CD2 LEU A 40 6854 12713 10221 -2062 -1606 3550 C ATOM 9 N THR A 41 -23.879 18.065 2.537 1.00 75.59 N ANISOU 9 N THR A 41 6531 13335 8856 -1348 -1700 3627 N ATOM 10 CA THR A 41 -22.903 18.568 3.504 1.00 77.23 C ANISOU 10 CA THR A 41 6937 13690 8716 -1026 -1658 3242 C ATOM 11 C THR A 41 -22.089 19.729 2.936 1.00 73.89 C ANISOU 11 C THR A 41 6706 13233 8136 -970 -1443 2412 C ATOM 12 O THR A 41 -21.308 19.548 2.002 1.00 68.46 O ANISOU 12 O THR A 41 6027 12191 7794 -1186 -1585 1812 O ATOM 13 CB THR A 41 -21.938 17.463 3.990 1.00 79.49 C ANISOU 13 CB THR A 41 7248 13675 9280 -1027 -2150 3073 C ATOM 14 OG1 THR A 41 -21.204 16.937 2.877 1.00 75.27 O ANISOU 14 OG1 THR A 41 6664 12724 9213 -1301 -2459 2511 O ATOM 15 CG2 THR A 41 -22.704 16.337 4.670 1.00 84.54 C ANISOU 15 CG2 THR A 41 7767 14351 10004 -1089 -2389 3908 C ATOM 16 N PRO A 42 -22.265 20.927 3.513 1.00 83.31 N ANISOU 16 N PRO A 42 8065 14806 8784 -666 -1118 2391 N ATOM 17 CA PRO A 42 -21.610 22.162 3.074 1.00 75.24 C ANISOU 17 CA PRO A 42 7258 13807 7524 -606 -920 1685 C ATOM 18 C PRO A 42 -20.104 21.993 2.910 1.00 72.30 C ANISOU 18 C PRO A 42 6931 13079 7460 -647 -1137 928 C ATOM 19 O PRO A 42 -19.498 21.183 3.608 1.00 74.88 O ANISOU 19 O PRO A 42 7211 13250 7989 -530 -1443 935 O ATOM 20 CB PRO A 42 -21.905 23.134 4.229 1.00 72.47 C ANISOU 20 CB PRO A 42 7084 13926 6526 -131 -744 1941 C ATOM 21 CG PRO A 42 -22.323 22.251 5.377 1.00 79.51 C ANISOU 21 CG PRO A 42 7876 14938 7397 88 -873 2645 C ATOM 22 CD PRO A 42 -23.091 21.170 4.704 1.00 84.66 C ANISOU 22 CD PRO A 42 8251 15427 8489 -320 -953 3076 C ATOM 23 N LEU A 43 -19.513 22.751 1.992 1.00 74.29 N ANISOU 23 N LEU A 43 7290 13194 7745 -815 -981 259 N ATOM 24 CA LEU A 43 -18.069 22.716 1.792 1.00 76.79 C ANISOU 24 CA LEU A 43 7606 13209 8360 -863 -1124 -502 C ATOM 25 C LEU A 43 -17.345 23.245 3.025 1.00 76.52 C ANISOU 25 C LEU A 43 7698 13292 8084 -437 -1220 -663 C ATOM 26 O LEU A 43 -17.864 24.100 3.743 1.00 71.93 O ANISOU 26 O LEU A 43 7291 13052 6990 -114 -1082 -355 O ATOM 27 CB LEU A 43 -17.661 23.529 0.559 1.00 75.81 C ANISOU 27 CB LEU A 43 7592 12942 8271 -1143 -862 -1138 C ATOM 28 CG LEU A 43 -18.076 23.022 -0.825 1.00 76.80 C ANISOU 28 CG LEU A 43 7677 12782 8720 -1523 -803 -1180 C ATOM 29 CD1 LEU A 43 -17.402 23.848 -1.909 1.00 73.78 C ANISOU 29 CD1 LEU A 43 7471 12209 8354 -1753 -533 -1910 C ATOM 30 CD2 LEU A 43 -17.739 21.551 -0.995 1.00 83.21 C ANISOU 30 CD2 LEU A 43 8250 13291 10074 -1631 -1192 -1108 C ATOM 31 N ALA A 44 -16.144 22.730 3.262 1.00 68.22 N ANISOU 31 N ALA A 44 6579 11934 7409 -397 -1502 -1168 N ATOM 32 CA ALA A 44 -15.336 23.156 4.397 1.00 67.98 C ANISOU 32 CA ALA A 44 6695 11871 7264 41 -1670 -1411 C ATOM 33 C ALA A 44 -14.541 24.412 4.059 1.00 66.41 C ANISOU 33 C ALA A 44 6594 11659 6982 56 -1497 -2048 C ATOM 34 O ALA A 44 -14.388 24.765 2.890 1.00 63.56 O ANISOU 34 O ALA A 44 6169 11244 6736 -332 -1262 -2421 O ATOM 35 CB ALA A 44 -14.402 22.036 4.832 1.00 70.45 C ANISOU 35 CB ALA A 44 6921 11809 8038 94 -2107 -1734 C ATOM 36 N TYR A 45 -14.042 25.084 5.090 1.00 68.01 N ANISOU 36 N TYR A 45 6984 11873 6982 525 -1637 -2156 N ATOM 37 CA TYR A 45 -13.227 26.280 4.913 1.00 69.20 C ANISOU 37 CA TYR A 45 7235 11982 7077 580 -1564 -2729 C ATOM 38 C TYR A 45 -12.046 26.003 3.983 1.00 70.82 C ANISOU 38 C TYR A 45 7193 11833 7881 172 -1554 -3535 C ATOM 39 O TYR A 45 -11.370 24.979 4.106 1.00 67.44 O ANISOU 39 O TYR A 45 6584 11102 7937 142 -1818 -3819 O ATOM 40 CB TYR A 45 -12.733 26.786 6.273 1.00 71.55 C ANISOU 40 CB TYR A 45 7769 12208 7210 1228 -1865 -2731 C ATOM 41 CG TYR A 45 -11.956 28.085 6.220 1.00 64.01 C ANISOU 41 CG TYR A 45 6939 11207 6173 1349 -1875 -3227 C ATOM 42 CD1 TYR A 45 -12.598 29.293 5.987 1.00 65.73 C ANISOU 42 CD1 TYR A 45 7377 11801 5796 1379 -1687 -3014 C ATOM 43 CD2 TYR A 45 -10.583 28.103 6.417 1.00 68.87 C ANISOU 43 CD2 TYR A 45 7463 11394 7312 1438 -2122 -3922 C ATOM 44 CE1 TYR A 45 -11.890 30.482 5.942 1.00 64.66 C ANISOU 44 CE1 TYR A 45 7386 11617 5564 1472 -1765 -3441 C ATOM 45 CE2 TYR A 45 -9.868 29.287 6.374 1.00 67.86 C ANISOU 45 CE2 TYR A 45 7427 11200 7158 1530 -2162 -4342 C ATOM 46 CZ TYR A 45 -10.527 30.472 6.135 1.00 64.49 C ANISOU 46 CZ TYR A 45 7238 11154 6110 1538 -1993 -4078 C ATOM 47 OH TYR A 45 -9.822 31.654 6.090 1.00 64.11 O ANISOU 47 OH TYR A 45 7311 11036 6013 1611 -2096 -4469 O ATOM 48 N LYS A 46 -11.813 26.917 3.046 1.00 70.13 N ANISOU 48 N LYS A 46 7124 11795 7728 -139 -1256 -3914 N ATOM 49 CA LYS A 46 -10.704 26.797 2.103 1.00 66.95 C ANISOU 49 CA LYS A 46 6489 11102 7847 -532 -1154 -4673 C ATOM 50 C LYS A 46 -10.729 25.486 1.322 1.00 65.84 C ANISOU 50 C LYS A 46 6099 10789 8128 -867 -1176 -4727 C ATOM 51 O LYS A 46 -9.686 25.002 0.885 1.00 64.57 O ANISOU 51 O LYS A 46 5696 10363 8476 -1043 -1251 -5339 O ATOM 52 CB LYS A 46 -9.363 26.950 2.823 1.00 65.61 C ANISOU 52 CB LYS A 46 6220 10646 8062 -263 -1442 -5252 C ATOM 53 CG LYS A 46 -9.051 28.370 3.265 1.00 68.21 C ANISOU 53 CG LYS A 46 6766 11050 8099 -17 -1437 -5380 C ATOM 54 CD LYS A 46 -8.674 29.257 2.092 1.00 65.38 C ANISOU 54 CD LYS A 46 6382 10720 7740 -500 -1057 -5829 C ATOM 55 CE LYS A 46 -8.137 30.597 2.560 1.00 66.03 C ANISOU 55 CE LYS A 46 6650 10807 7632 -271 -1168 -6039 C ATOM 56 NZ LYS A 46 -7.599 31.414 1.440 1.00 65.28 N ANISOU 56 NZ LYS A 46 6523 10681 7598 -788 -814 -6544 N ATOM 57 N GLN A 47 -11.918 24.915 1.150 1.00 65.34 N ANISOU 57 N GLN A 47 6090 10878 7859 -932 -1147 -4088 N ATOM 58 CA GLN A 47 -12.071 23.706 0.345 1.00 66.02 C ANISOU 58 CA GLN A 47 5987 10790 8308 -1223 -1233 -4054 C ATOM 59 C GLN A 47 -12.632 24.039 -1.032 1.00 62.09 C ANISOU 59 C GLN A 47 5574 10291 7728 -1606 -854 -4059 C ATOM 60 O GLN A 47 -13.401 24.988 -1.184 1.00 60.10 O ANISOU 60 O GLN A 47 5565 10245 7026 -1623 -576 -3817 O ATOM 61 CB GLN A 47 -12.976 22.685 1.040 1.00 69.22 C ANISOU 61 CB GLN A 47 6384 11269 8646 -1052 -1532 -3334 C ATOM 62 CG GLN A 47 -13.087 21.364 0.292 1.00 68.66 C ANISOU 62 CG GLN A 47 6134 10989 8966 -1309 -1765 -3273 C ATOM 63 CD GLN A 47 -14.247 20.508 0.762 1.00 70.55 C ANISOU 63 CD GLN A 47 6386 11330 9088 -1239 -1986 -2438 C ATOM 64 OE1 GLN A 47 -15.078 20.945 1.557 1.00 66.66 O ANISOU 64 OE1 GLN A 47 6023 11108 8198 -1024 -1868 -1876 O ATOM 65 NE2 GLN A 47 -14.312 19.280 0.266 1.00 66.67 N ANISOU 65 NE2 GLN A 47 5759 10635 8939 -1411 -2327 -2338 N ATOM 66 N PHE A 48 -12.248 23.253 -2.031 1.00 63.08 N ANISOU 66 N PHE A 48 5544 10157 8265 -1874 -885 -4359 N ATOM 67 CA PHE A 48 -12.724 23.468 -3.390 1.00 60.79 C ANISOU 67 CA PHE A 48 5401 9750 7948 -2185 -561 -4402 C ATOM 68 C PHE A 48 -13.054 22.157 -4.093 1.00 63.56 C ANISOU 68 C PHE A 48 5638 9861 8649 -2287 -821 -4193 C ATOM 69 O PHE A 48 -12.429 21.128 -3.839 1.00 64.47 O ANISOU 69 O PHE A 48 5516 9863 9117 -2217 -1220 -4331 O ATOM 70 CB PHE A 48 -11.696 24.259 -4.198 1.00 62.77 C ANISOU 70 CB PHE A 48 5680 9870 8300 -2418 -206 -5161 C ATOM 71 CG PHE A 48 -10.299 23.727 -4.086 1.00 63.60 C ANISOU 71 CG PHE A 48 5452 9824 8888 -2411 -389 -5778 C ATOM 72 CD1 PHE A 48 -9.447 24.189 -3.099 1.00 65.85 C ANISOU 72 CD1 PHE A 48 5613 10182 9224 -2220 -501 -6092 C ATOM 73 CD2 PHE A 48 -9.836 22.767 -4.968 1.00 66.21 C ANISOU 73 CD2 PHE A 48 5609 9920 9629 -2554 -492 -6065 C ATOM 74 CE1 PHE A 48 -8.161 23.704 -2.993 1.00 67.24 C ANISOU 74 CE1 PHE A 48 5473 10188 9885 -2203 -694 -6723 C ATOM 75 CE2 PHE A 48 -8.549 22.276 -4.867 1.00 68.76 C ANISOU 75 CE2 PHE A 48 5609 10137 10381 -2532 -684 -6688 C ATOM 76 CZ PHE A 48 -7.711 22.745 -3.879 1.00 67.90 C ANISOU 76 CZ PHE A 48 5355 10092 10353 -2373 -776 -7038 C ATOM 77 N ILE A 49 -14.048 22.210 -4.975 1.00 72.67 N ANISOU 77 N ILE A 49 7001 10909 9699 -2424 -654 -3877 N ATOM 78 CA ILE A 49 -14.482 21.049 -5.743 1.00 77.66 C ANISOU 78 CA ILE A 49 7588 11255 10665 -2483 -940 -3620 C ATOM 79 C ILE A 49 -14.661 21.431 -7.210 1.00 78.70 C ANISOU 79 C ILE A 49 8005 11069 10830 -2677 -610 -3886 C ATOM 80 O ILE A 49 -15.358 22.398 -7.519 1.00 74.04 O ANISOU 80 O ILE A 49 7730 10504 9898 -2751 -255 -3817 O ATOM 81 CB ILE A 49 -15.812 20.484 -5.206 1.00 80.38 C ANISOU 81 CB ILE A 49 7924 11699 10916 -2371 -1201 -2759 C ATOM 82 CG1 ILE A 49 -15.645 19.992 -3.767 1.00 84.31 C ANISOU 82 CG1 ILE A 49 8206 12455 11372 -2164 -1536 -2470 C ATOM 83 CG2 ILE A 49 -16.316 19.363 -6.101 1.00 83.20 C ANISOU 83 CG2 ILE A 49 8270 11698 11644 -2427 -1540 -2469 C ATOM 84 CD1 ILE A 49 -14.687 18.827 -3.626 1.00 88.73 C ANISOU 84 CD1 ILE A 49 8542 12843 12328 -2128 -2033 -2753 C ATOM 85 N PRO A 50 -14.032 20.674 -8.123 1.00 81.80 N ANISOU 85 N PRO A 50 8335 11141 11605 -2727 -755 -4218 N ATOM 86 CA PRO A 50 -13.189 19.509 -7.830 1.00 85.52 C ANISOU 86 CA PRO A 50 8464 11586 12446 -2626 -1249 -4375 C ATOM 87 C PRO A 50 -11.922 19.882 -7.069 1.00 86.33 C ANISOU 87 C PRO A 50 8322 11909 12572 -2611 -1179 -4960 C ATOM 88 O PRO A 50 -11.534 21.051 -7.045 1.00 82.82 O ANISOU 88 O PRO A 50 7967 11577 11923 -2713 -707 -5323 O ATOM 89 CB PRO A 50 -12.822 18.982 -9.222 1.00 88.62 C ANISOU 89 CB PRO A 50 8950 11589 13133 -2668 -1281 -4698 C ATOM 90 CG PRO A 50 -13.863 19.541 -10.138 1.00 87.67 C ANISOU 90 CG PRO A 50 9255 11203 12853 -2736 -959 -4445 C ATOM 91 CD PRO A 50 -14.190 20.884 -9.571 1.00 84.43 C ANISOU 91 CD PRO A 50 8999 11077 12002 -2844 -483 -4453 C ATOM 92 N ASN A 51 -11.289 18.887 -6.457 1.00 61.43 N ANISOU 92 N ASN A 51 6192 9032 8118 -872 -835 -1371 N ATOM 93 CA ASN A 51 -10.092 19.108 -5.657 1.00 63.77 C ANISOU 93 CA ASN A 51 6762 9142 8327 -1037 -966 -1278 C ATOM 94 C ASN A 51 -8.856 19.315 -6.527 1.00 57.04 C ANISOU 94 C ASN A 51 5839 8305 7530 -1229 -1106 -1382 C ATOM 95 O ASN A 51 -7.855 18.614 -6.376 1.00 53.93 O ANISOU 95 O ASN A 51 5310 7786 7396 -1440 -1229 -1435 O ATOM 96 CB ASN A 51 -9.876 17.935 -4.698 1.00 69.33 C ANISOU 96 CB ASN A 51 7352 9714 9276 -1107 -980 -1228 C ATOM 97 CG ASN A 51 -9.048 18.313 -3.486 1.00 78.01 C ANISOU 97 CG ASN A 51 8898 10538 10205 -1163 -1132 -1100 C ATOM 98 OD1 ASN A 51 -8.969 19.484 -3.111 1.00 84.94 O ANISOU 98 OD1 ASN A 51 10183 11316 10774 -1077 -1170 -1032 O ATOM 99 ND2 ASN A 51 -8.432 17.319 -2.858 1.00 78.32 N ANISOU 99 ND2 ASN A 51 8845 10440 10473 -1293 -1246 -1081 N ATOM 100 N VAL A 52 -8.939 20.279 -7.438 1.00 54.62 N ANISOU 100 N VAL A 52 5626 8109 7018 -1157 -1064 -1406 N ATOM 101 CA VAL A 52 -7.842 20.587 -8.350 1.00 53.79 C ANISOU 101 CA VAL A 52 5496 7972 6970 -1291 -1099 -1487 C ATOM 102 C VAL A 52 -7.758 22.090 -8.592 1.00 59.70 C ANISOU 102 C VAL A 52 6555 8683 7446 -1164 -1046 -1394 C ATOM 103 O VAL A 52 -8.567 22.855 -8.066 1.00 65.02 O ANISOU 103 O VAL A 52 7427 9384 7893 -1008 -1012 -1283 O ATOM 104 CB VAL A 52 -8.018 19.878 -9.707 1.00 47.39 C ANISOU 104 CB VAL A 52 4339 7409 6259 -1316 -1042 -1657 C ATOM 105 CG1 VAL A 52 -7.812 18.379 -9.559 1.00 46.28 C ANISOU 105 CG1 VAL A 52 3783 7291 6511 -1490 -1099 -1776 C ATOM 106 CG2 VAL A 52 -9.391 20.178 -10.288 1.00 47.70 C ANISOU 106 CG2 VAL A 52 4361 7691 6073 -1060 -979 -1675 C ATOM 107 N ALA A 53 -6.780 22.509 -9.389 1.00 50.67 N ANISOU 107 N ALA A 53 5427 7445 6378 -1233 -1005 -1439 N ATOM 108 CA ALA A 53 -6.632 23.919 -9.737 1.00 54.58 C ANISOU 108 CA ALA A 53 6148 7897 6692 -1091 -909 -1343 C ATOM 109 C ALA A 53 -7.814 24.397 -10.581 1.00 60.35 C ANISOU 109 C ALA A 53 6892 8946 7092 -905 -808 -1306 C ATOM 110 O ALA A 53 -8.392 23.625 -11.346 1.00 58.22 O ANISOU 110 O ALA A 53 6446 8893 6780 -887 -803 -1414 O ATOM 111 CB ALA A 53 -5.322 24.150 -10.470 1.00 55.08 C ANISOU 111 CB ALA A 53 6204 7725 6999 -1181 -815 -1400 C ATOM 112 N GLU A 54 -8.165 25.673 -10.439 1.00 65.55 N ANISOU 112 N GLU A 54 7736 9609 7561 -763 -757 -1173 N ATOM 113 CA GLU A 54 -9.344 26.233 -11.099 1.00 60.08 C ANISOU 113 CA GLU A 54 7074 9156 6595 -603 -711 -1129 C ATOM 114 C GLU A 54 -9.268 26.186 -12.622 1.00 61.95 C ANISOU 114 C GLU A 54 7292 9560 6687 -526 -628 -1189 C ATOM 115 O GLU A 54 -10.285 26.014 -13.295 1.00 68.00 O ANISOU 115 O GLU A 54 8027 10529 7282 -406 -684 -1250 O ATOM 116 CB GLU A 54 -9.583 27.678 -10.645 1.00 51.24 C ANISOU 116 CB GLU A 54 6110 7987 5372 -509 -668 -969 C ATOM 117 CG GLU A 54 -10.805 28.337 -11.281 1.00 54.54 C ANISOU 117 CG GLU A 54 6551 8600 5572 -382 -650 -919 C ATOM 118 CD GLU A 54 -10.936 29.809 -10.929 1.00 51.75 C ANISOU 118 CD GLU A 54 6275 8208 5179 -327 -590 -759 C ATOM 119 OE1 GLU A 54 -9.906 30.516 -10.895 1.00 52.62 O ANISOU 119 OE1 GLU A 54 6403 8200 5390 -302 -506 -686 O ATOM 120 OE2 GLU A 54 -12.075 30.264 -10.694 1.00 54.71 O ANISOU 120 OE2 GLU A 54 6653 8635 5497 -308 -621 -721 O ATOM 121 N LYS A 55 -8.067 26.344 -13.164 1.00 53.10 N ANISOU 121 N LYS A 55 6213 8303 5660 -573 -495 -1187 N ATOM 122 CA LYS A 55 -7.903 26.448 -14.610 1.00 54.44 C ANISOU 122 CA LYS A 55 6457 8591 5635 -470 -349 -1213 C ATOM 123 C LYS A 55 -7.336 25.172 -15.231 1.00 53.38 C ANISOU 123 C LYS A 55 6177 8466 5637 -606 -329 -1405 C ATOM 124 O LYS A 55 -6.331 25.207 -15.942 1.00 53.86 O ANISOU 124 O LYS A 55 6307 8373 5784 -650 -123 -1423 O ATOM 125 CB LYS A 55 -7.028 27.655 -14.953 1.00 56.44 C ANISOU 125 CB LYS A 55 6877 8650 5919 -382 -109 -1057 C ATOM 126 CG LYS A 55 -7.515 28.952 -14.321 1.00 53.56 C ANISOU 126 CG LYS A 55 6571 8285 5496 -264 -125 -879 C ATOM 127 CD LYS A 55 -6.401 29.979 -14.242 1.00 56.29 C ANISOU 127 CD LYS A 55 6947 8330 6110 -198 91 -761 C ATOM 128 CE LYS A 55 -6.720 31.064 -13.227 1.00 56.43 C ANISOU 128 CE LYS A 55 6917 8307 6217 -136 12 -640 C ATOM 129 NZ LYS A 55 -5.530 31.911 -12.939 1.00 53.78 N ANISOU 129 NZ LYS A 55 6523 7605 6306 -53 167 -588 N ATOM 130 N THR A 56 -7.996 24.050 -14.958 1.00 60.24 N ANISOU 130 N THR A 56 6817 9488 6585 -668 -514 -1553 N ATOM 131 CA THR A 56 -7.613 22.765 -15.533 1.00 62.87 C ANISOU 131 CA THR A 56 6913 9884 7092 -802 -525 -1760 C ATOM 132 C THR A 56 -8.778 22.169 -16.315 1.00 66.62 C ANISOU 132 C THR A 56 7263 10677 7374 -610 -666 -1921 C ATOM 133 O THR A 56 -9.918 22.619 -16.184 1.00 63.46 O ANISOU 133 O THR A 56 6930 10381 6800 -412 -788 -1880 O ATOM 134 CB THR A 56 -7.170 21.763 -14.449 1.00 60.23 C ANISOU 134 CB THR A 56 6299 9396 7189 -1059 -633 -1826 C ATOM 135 OG1 THR A 56 -8.280 21.449 -13.599 1.00 60.70 O ANISOU 135 OG1 THR A 56 6239 9567 7257 -976 -789 -1811 O ATOM 136 CG2 THR A 56 -6.040 22.343 -13.611 1.00 52.50 C ANISOU 136 CG2 THR A 56 5462 8038 6446 -1211 -583 -1709 C ATOM 137 N LEU A 57 -8.489 21.158 -17.126 1.00 99.42 N ANISOU 137 N LEU A 57 11213 14942 11619 -668 -666 -2132 N ATOM 138 CA LEU A 57 -9.510 20.515 -17.946 1.00107.37 C ANISOU 138 CA LEU A 57 12065 16226 12506 -444 -844 -2347 C ATOM 139 C LEU A 57 -10.667 19.994 -17.099 1.00104.82 C ANISOU 139 C LEU A 57 11445 15943 12438 -357 -1052 -2408 C ATOM 140 O LEU A 57 -11.827 20.058 -17.509 1.00104.42 O ANISOU 140 O LEU A 57 11387 16001 12287 -79 -1225 -2511 O ATOM 141 CB LEU A 57 -8.904 19.378 -18.771 1.00113.87 C ANISOU 141 CB LEU A 57 12625 17150 13491 -563 -811 -2593 C ATOM 142 CG LEU A 57 -8.140 19.785 -20.033 1.00117.38 C ANISOU 142 CG LEU A 57 13409 17592 13599 -522 -591 -2604 C ATOM 143 CD1 LEU A 57 -9.078 20.455 -21.026 1.00119.45 C ANISOU 143 CD1 LEU A 57 14021 18054 13311 -118 -700 -2615 C ATOM 144 CD2 LEU A 57 -6.965 20.695 -19.701 1.00115.30 C ANISOU 144 CD2 LEU A 57 13436 16997 13377 -703 -288 -2363 C ATOM 145 N GLY A 58 -10.342 19.481 -15.916 1.00 78.15 N ANISOU 145 N GLY A 58 7843 12423 9429 -578 -1028 -2348 N ATOM 146 CA GLY A 58 -11.348 18.961 -15.009 1.00 69.73 C ANISOU 146 CA GLY A 58 6520 11328 8648 -495 -1130 -2370 C ATOM 147 C GLY A 58 -12.113 20.056 -14.291 1.00 67.70 C ANISOU 147 C GLY A 58 6572 10941 8210 -369 -1118 -2173 C ATOM 148 O GLY A 58 -13.205 19.824 -13.773 1.00 69.38 O ANISOU 148 O GLY A 58 6649 11089 8624 -224 -1167 -2206 O ATOM 149 N ALA A 59 -11.542 21.255 -14.263 1.00 53.82 N ANISOU 149 N ALA A 59 5198 9109 6141 -421 -1025 -1979 N ATOM 150 CA ALA A 59 -12.173 22.380 -13.583 1.00 51.19 C ANISOU 150 CA ALA A 59 5127 8664 5658 -340 -1003 -1794 C ATOM 151 C ALA A 59 -12.824 23.352 -14.564 1.00 53.57 C ANISOU 151 C ALA A 59 5651 9066 5638 -132 -1054 -1779 C ATOM 152 O ALA A 59 -13.599 22.949 -15.429 1.00 55.35 O ANISOU 152 O ALA A 59 5778 9405 5849 58 -1200 -1962 O ATOM 153 CB ALA A 59 -11.167 23.103 -12.698 1.00 51.12 C ANISOU 153 CB ALA A 59 5332 8478 5614 -515 -895 -1592 C ATOM 154 N SER A 60 -12.503 24.634 -14.419 1.00 62.49 N ANISOU 154 N SER A 60 7063 10136 6546 -150 -956 -1572 N ATOM 155 CA SER A 60 -13.114 25.676 -15.236 1.00 65.71 C ANISOU 155 CA SER A 60 7683 10620 6666 28 -996 -1509 C ATOM 156 C SER A 60 -12.381 25.876 -16.558 1.00 65.79 C ANISOU 156 C SER A 60 7864 10759 6374 117 -920 -1515 C ATOM 157 O SER A 60 -12.872 26.566 -17.453 1.00 66.76 O ANISOU 157 O SER A 60 8188 10972 6208 306 -975 -1482 O ATOM 158 CB SER A 60 -13.182 26.992 -14.461 1.00 66.80 C ANISOU 158 CB SER A 60 7977 10642 6763 -24 -906 -1279 C ATOM 159 OG SER A 60 -14.019 26.866 -13.325 1.00 67.88 O ANISOU 159 OG SER A 60 8021 10639 7131 -79 -947 -1279 O ATOM 160 N GLY A 61 -11.203 25.275 -16.676 1.00 56.32 N ANISOU 160 N GLY A 61 6607 9531 5262 -23 -781 -1554 N ATOM 161 CA GLY A 61 -10.461 25.310 -17.921 1.00 61.19 C ANISOU 161 CA GLY A 61 7397 10214 5640 49 -637 -1580 C ATOM 162 C GLY A 61 -9.412 26.401 -17.985 1.00 60.19 C ANISOU 162 C GLY A 61 7496 9915 5457 21 -345 -1353 C ATOM 163 O GLY A 61 -9.378 27.298 -17.146 1.00 59.30 O ANISOU 163 O GLY A 61 7404 9678 5450 -13 -305 -1179 O ATOM 164 N ARG A 62 -8.559 26.322 -19.000 1.00 90.29 N ANISOU 164 N ARG A 62 11467 13694 9147 57 -118 -1370 N ATOM 165 CA ARG A 62 -7.457 27.262 -19.163 1.00 93.04 C ANISOU 165 CA ARG A 62 11998 13790 9562 65 234 -1176 C ATOM 166 C ARG A 62 -7.930 28.705 -19.325 1.00 88.72 C ANISOU 166 C ARG A 62 11652 13286 8772 284 303 -932 C ATOM 167 O ARG A 62 -9.080 28.965 -19.679 1.00 86.85 O ANISOU 167 O ARG A 62 11502 13283 8213 446 91 -925 O ATOM 168 CB ARG A 62 -6.577 26.850 -20.347 1.00101.18 C ANISOU 168 CB ARG A 62 13200 14742 10502 89 524 -1248 C ATOM 169 CG ARG A 62 -7.353 26.459 -21.592 1.00108.10 C ANISOU 169 CG ARG A 62 14276 15932 10864 316 412 -1370 C ATOM 170 CD ARG A 62 -6.463 25.737 -22.590 1.00118.40 C ANISOU 170 CD ARG A 62 15698 17157 12132 274 681 -1509 C ATOM 171 NE ARG A 62 -7.226 25.207 -23.718 1.00123.88 N ANISOU 171 NE ARG A 62 16567 18168 12334 510 499 -1688 N ATOM 172 CZ ARG A 62 -6.723 24.404 -24.650 1.00126.03 C ANISOU 172 CZ ARG A 62 16926 18462 12496 501 648 -1876 C ATOM 173 NH1 ARG A 62 -5.453 24.030 -24.594 1.00125.29 N ANISOU 173 NH1 ARG A 62 16744 18059 12801 225 1012 -1901 N ATOM 174 NH2 ARG A 62 -7.493 23.970 -25.640 1.00129.36 N ANISOU 174 NH2 ARG A 62 17520 19181 12452 771 416 -2066 N ATOM 175 N TYR A 63 -7.021 29.635 -19.056 1.00 67.01 N ANISOU 175 N TYR A 63 8932 10266 6261 291 591 -749 N ATOM 176 CA TYR A 63 -7.307 31.061 -19.144 1.00 66.51 C ANISOU 176 CA TYR A 63 8966 10217 6086 484 706 -501 C ATOM 177 C TYR A 63 -7.188 31.542 -20.587 1.00 70.87 C ANISOU 177 C TYR A 63 9852 10826 6248 746 985 -376 C ATOM 178 O TYR A 63 -6.172 31.315 -21.244 1.00 70.90 O ANISOU 178 O TYR A 63 9999 10617 6323 778 1335 -381 O ATOM 179 CB TYR A 63 -6.342 31.831 -18.240 1.00 66.03 C ANISOU 179 CB TYR A 63 8735 9812 6540 429 896 -387 C ATOM 180 CG TYR A 63 -6.547 33.328 -18.211 1.00 65.80 C ANISOU 180 CG TYR A 63 8687 9785 6529 617 1033 -139 C ATOM 181 CD1 TYR A 63 -7.641 33.887 -17.565 1.00 64.45 C ANISOU 181 CD1 TYR A 63 8396 9830 6263 594 763 -80 C ATOM 182 CD2 TYR A 63 -5.632 34.184 -18.808 1.00 66.52 C ANISOU 182 CD2 TYR A 63 8839 9621 6812 812 1465 35 C ATOM 183 CE1 TYR A 63 -7.825 35.257 -17.530 1.00 63.44 C ANISOU 183 CE1 TYR A 63 8176 9713 6213 731 884 138 C ATOM 184 CE2 TYR A 63 -5.806 35.553 -18.776 1.00 67.98 C ANISOU 184 CE2 TYR A 63 8925 9816 7088 993 1606 268 C ATOM 185 CZ TYR A 63 -6.904 36.085 -18.136 1.00 66.10 C ANISOU 185 CZ TYR A 63 8533 9843 6739 937 1295 316 C ATOM 186 OH TYR A 63 -7.079 37.448 -18.104 1.00 64.83 O ANISOU 186 OH TYR A 63 8206 9704 6723 1084 1431 540 O ATOM 187 N GLU A 64 -8.233 32.202 -21.076 1.00 96.36 N ANISOU 187 N GLU A 64 13229 14302 9082 934 838 -265 N ATOM 188 CA GLU A 64 -8.259 32.691 -22.451 1.00102.93 C ANISOU 188 CA GLU A 64 14446 15211 9450 1226 1053 -126 C ATOM 189 C GLU A 64 -7.526 34.021 -22.595 1.00103.77 C ANISOU 189 C GLU A 64 14590 15103 9737 1386 1505 186 C ATOM 190 O GLU A 64 -6.576 34.137 -23.369 1.00103.89 O ANISOU 190 O GLU A 64 14830 14903 9742 1532 1965 280 O ATOM 191 CB GLU A 64 -9.702 32.833 -22.941 1.00106.21 C ANISOU 191 CB GLU A 64 15015 15931 9410 1377 646 -155 C ATOM 192 CG GLU A 64 -10.424 31.510 -23.146 1.00111.36 C ANISOU 192 CG GLU A 64 15665 16757 9888 1342 241 -486 C ATOM 193 CD GLU A 64 -9.938 30.764 -24.374 1.00121.82 C ANISOU 193 CD GLU A 64 17322 18129 10835 1505 385 -612 C ATOM 194 OE1 GLU A 64 -9.722 31.411 -25.420 1.00128.68 O ANISOU 194 OE1 GLU A 64 18602 19001 11290 1773 630 -436 O ATOM 195 OE2 GLU A 64 -9.779 29.528 -24.295 1.00123.82 O ANISOU 195 OE2 GLU A 64 17422 18414 11208 1372 267 -885 O ATOM 196 N GLY A 65 -7.975 35.023 -21.847 1.00 85.19 N ANISOU 196 N GLY A 65 11988 12779 7602 1364 1404 339 N ATOM 197 CA GLY A 65 -7.369 36.341 -21.895 1.00 83.98 C ANISOU 197 CA GLY A 65 11749 12437 7722 1533 1805 627 C ATOM 198 C GLY A 65 -8.208 37.398 -21.201 1.00 76.12 C ANISOU 198 C GLY A 65 10465 11588 6869 1497 1589 766 C ATOM 199 O GLY A 65 -9.338 37.136 -20.787 1.00 67.30 O ANISOU 199 O GLY A 65 9284 10695 5593 1348 1145 648 O ATOM 200 N LYS A 66 -7.652 38.599 -21.076 1.00 79.52 N ANISOU 200 N LYS A 66 10686 11852 7676 1636 1929 1004 N ATOM 201 CA LYS A 66 -8.345 39.705 -20.425 1.00 77.45 C ANISOU 201 CA LYS A 66 10077 11717 7635 1591 1776 1142 C ATOM 202 C LYS A 66 -9.351 40.350 -21.375 1.00 76.67 C ANISOU 202 C LYS A 66 10180 11879 7074 1734 1685 1334 C ATOM 203 O LYS A 66 -8.976 40.938 -22.390 1.00 86.67 O ANISOU 203 O LYS A 66 11654 13102 8173 2018 2050 1572 O ATOM 204 CB LYS A 66 -7.336 40.742 -19.921 1.00 83.13 C ANISOU 204 CB LYS A 66 10409 12146 9030 1714 2160 1296 C ATOM 205 CG LYS A 66 -7.913 41.784 -18.972 1.00 83.32 C ANISOU 205 CG LYS A 66 9961 12281 9417 1614 1979 1369 C ATOM 206 CD LYS A 66 -6.814 42.678 -18.413 1.00 87.79 C ANISOU 206 CD LYS A 66 10091 12521 10745 1775 2320 1448 C ATOM 207 CE LYS A 66 -7.370 43.733 -17.468 1.00 81.91 C ANISOU 207 CE LYS A 66 8833 11907 10381 1681 2140 1497 C ATOM 208 NZ LYS A 66 -8.218 44.737 -18.170 1.00 86.49 N ANISOU 208 NZ LYS A 66 9322 12755 10784 1749 2195 1770 N ATOM 209 N ILE A 67 -10.630 40.230 -21.036 1.00 69.93 N ANISOU 209 N ILE A 67 9278 11244 6050 1546 1202 1227 N ATOM 210 CA ILE A 67 -11.705 40.766 -21.863 1.00 70.45 C ANISOU 210 CA ILE A 67 9529 11502 5737 1643 992 1353 C ATOM 211 C ILE A 67 -12.050 42.199 -21.471 1.00 72.15 C ANISOU 211 C ILE A 67 9332 11751 6330 1598 1049 1593 C ATOM 212 O ILE A 67 -12.961 42.436 -20.680 1.00 68.81 O ANISOU 212 O ILE A 67 8624 11388 6131 1338 717 1507 O ATOM 213 CB ILE A 67 -12.973 39.893 -21.765 1.00 70.82 C ANISOU 213 CB ILE A 67 9711 11668 5528 1474 425 1078 C ATOM 214 CG1 ILE A 67 -12.668 38.464 -22.216 1.00 72.00 C ANISOU 214 CG1 ILE A 67 10197 11815 5343 1538 357 828 C ATOM 215 CG2 ILE A 67 -14.102 40.486 -22.592 1.00 74.34 C ANISOU 215 CG2 ILE A 67 10341 12226 5678 1575 136 1175 C ATOM 216 CD1 ILE A 67 -13.866 37.544 -22.177 1.00 70.38 C ANISOU 216 CD1 ILE A 67 10075 11681 4984 1441 -177 531 C ATOM 217 N THR A 68 -11.310 43.152 -22.027 1.00 76.56 N ANISOU 217 N THR A 68 9833 12244 7013 1855 1507 1893 N ATOM 218 CA THR A 68 -11.556 44.564 -21.764 1.00 80.97 C ANISOU 218 CA THR A 68 9932 12847 7985 1846 1610 2143 C ATOM 219 C THR A 68 -12.834 45.019 -22.461 1.00 83.11 C ANISOU 219 C THR A 68 10363 13308 7907 1823 1268 2250 C ATOM 220 O THR A 68 -13.440 44.261 -23.219 1.00 79.46 O ANISOU 220 O THR A 68 10408 12913 6873 1882 967 2128 O ATOM 221 CB THR A 68 -10.381 45.434 -22.245 1.00 86.74 C ANISOU 221 CB THR A 68 10530 13408 9017 2186 2249 2445 C ATOM 222 OG1 THR A 68 -10.210 45.265 -23.657 1.00 91.19 O ANISOU 222 OG1 THR A 68 11680 13973 8995 2508 2486 2615 O ATOM 223 CG2 THR A 68 -9.096 45.030 -21.541 1.00 86.76 C ANISOU 223 CG2 THR A 68 10346 13116 9504 2217 2551 2305 C ATOM 224 N ARG A 69 -13.244 46.256 -22.201 1.00105.02 N ANISOU 224 N ARG A 69 12678 16144 11080 1739 1283 2456 N ATOM 225 CA ARG A 69 -14.456 46.797 -22.807 1.00112.95 C ANISOU 225 CA ARG A 69 13770 17271 11873 1677 932 2562 C ATOM 226 C ARG A 69 -14.300 47.004 -24.310 1.00119.09 C ANISOU 226 C ARG A 69 15086 18088 12077 2078 1113 2821 C ATOM 227 O ARG A 69 -15.183 46.645 -25.089 1.00120.24 O ANISOU 227 O ARG A 69 15701 18284 11702 2127 698 2751 O ATOM 228 CB ARG A 69 -14.861 48.111 -22.136 1.00116.71 C ANISOU 228 CB ARG A 69 13550 17796 13000 1453 940 2726 C ATOM 229 CG ARG A 69 -15.562 47.931 -20.802 1.00112.87 C ANISOU 229 CG ARG A 69 12667 17280 12937 1005 593 2447 C ATOM 230 CD ARG A 69 -16.103 49.251 -20.278 1.00110.87 C ANISOU 230 CD ARG A 69 11745 17082 13299 757 570 2597 C ATOM 231 NE ARG A 69 -16.971 49.056 -19.120 1.00103.38 N ANISOU 231 NE ARG A 69 10524 16066 12689 311 228 2324 N ATOM 232 CZ ARG A 69 -18.289 48.911 -19.192 1.00104.35 C ANISOU 232 CZ ARG A 69 10755 16106 12788 29 -222 2188 C ATOM 233 NH1 ARG A 69 -18.899 48.945 -20.370 1.00111.95 N ANISOU 233 NH1 ARG A 69 12092 17060 13383 157 -462 2282 N ATOM 234 NH2 ARG A 69 -18.999 48.735 -18.085 1.00 95.23 N ANISOU 234 NH2 ARG A 69 9356 14824 12004 -361 -430 1946 N ATOM 235 N ASN A 70 -13.174 47.585 -24.713 1.00115.57 N ANISOU 235 N ASN A 70 14587 17571 11753 2398 1739 3112 N ATOM 236 CA ASN A 70 -12.915 47.835 -26.126 1.00124.33 C ANISOU 236 CA ASN A 70 16248 18681 12311 2826 2032 3403 C ATOM 237 C ASN A 70 -12.493 46.570 -26.868 1.00125.19 C ANISOU 237 C ASN A 70 17103 18729 11734 3042 2073 3224 C ATOM 238 O ASN A 70 -12.305 46.584 -28.084 1.00131.97 O ANISOU 238 O ASN A 70 18560 19580 12003 3414 2292 3416 O ATOM 239 CB ASN A 70 -11.871 48.941 -26.302 1.00130.64 C ANISOU 239 CB ASN A 70 16698 19358 13580 3123 2770 3793 C ATOM 240 CG ASN A 70 -10.537 48.593 -25.675 1.00131.19 C ANISOU 240 CG ASN A 70 16532 19175 14140 3193 3260 3690 C ATOM 241 OD1 ASN A 70 -10.300 47.452 -25.280 1.00127.72 O ANISOU 241 OD1 ASN A 70 16305 18668 13556 3049 3089 3362 O ATOM 242 ND2 ASN A 70 -9.654 49.580 -25.582 1.00136.08 N ANISOU 242 ND2 ASN A 70 16678 19613 15415 3428 3863 3960 N ATOM 243 N SER A 71 -12.347 45.477 -26.125 1.00111.15 N ANISOU 243 N SER A 71 15286 16908 10038 2809 1871 2858 N ATOM 244 CA SER A 71 -12.024 44.184 -26.712 1.00109.08 C ANISOU 244 CA SER A 71 15624 16610 9213 2940 1846 2632 C ATOM 245 C SER A 71 -13.244 43.617 -27.431 1.00108.41 C ANISOU 245 C SER A 71 16034 16682 8476 2970 1208 2451 C ATOM 246 O SER A 71 -14.350 43.630 -26.894 1.00105.10 O ANISOU 246 O SER A 71 15373 16328 8232 2698 647 2281 O ATOM 247 CB SER A 71 -11.546 43.213 -25.630 1.00104.40 C ANISOU 247 CB SER A 71 14757 15921 8988 2659 1789 2301 C ATOM 248 OG SER A 71 -11.204 41.954 -26.182 1.00105.75 O ANISOU 248 OG SER A 71 15422 16063 8696 2752 1777 2076 O ATOM 249 N GLU A 72 -13.039 43.123 -28.647 1.00135.95 N ANISOU 249 N GLU A 72 20220 20180 11255 3320 1299 2467 N ATOM 250 CA GLU A 72 -14.138 42.609 -29.460 1.00139.68 C ANISOU 250 CA GLU A 72 21216 20764 11094 3446 668 2275 C ATOM 251 C GLU A 72 -14.913 41.492 -28.763 1.00130.34 C ANISOU 251 C GLU A 72 19858 19601 10063 3151 49 1802 C ATOM 252 O GLU A 72 -16.127 41.375 -28.928 1.00132.51 O ANISOU 252 O GLU A 72 20224 19890 10233 3116 -595 1616 O ATOM 253 CB GLU A 72 -13.628 42.129 -30.823 1.00150.73 C ANISOU 253 CB GLU A 72 23422 22164 11685 3897 913 2325 C ATOM 254 CG GLU A 72 -13.669 43.183 -31.931 1.00161.03 C ANISOU 254 CG GLU A 72 25183 23478 12523 4296 1149 2745 C ATOM 255 CD GLU A 72 -12.688 44.323 -31.713 1.00165.00 C ANISOU 255 CD GLU A 72 25326 23861 13506 4364 1950 3195 C ATOM 256 OE1 GLU A 72 -12.778 45.004 -30.669 1.00163.00 O ANISOU 256 OE1 GLU A 72 24320 23601 14012 4053 1954 3263 O ATOM 257 OE2 GLU A 72 -11.834 44.549 -32.596 1.00168.63 O ANISOU 257 OE2 GLU A 72 26252 24204 13615 4755 2594 3473 O ATOM 258 N ARG A 73 -14.209 40.680 -27.982 1.00 94.64 N ANISOU 258 N ARG A 73 15072 15031 5855 2951 250 1606 N ATOM 259 CA ARG A 73 -14.825 39.541 -27.308 1.00 90.87 C ANISOU 259 CA ARG A 73 14418 14558 5552 2703 -240 1181 C ATOM 260 C ARG A 73 -15.766 39.973 -26.181 1.00 86.81 C ANISOU 260 C ARG A 73 13356 13997 5631 2342 -596 1110 C ATOM 261 O ARG A 73 -16.403 39.138 -25.537 1.00 82.85 O ANISOU 261 O ARG A 73 12672 13446 5361 2138 -976 783 O ATOM 262 CB ARG A 73 -13.746 38.596 -26.769 1.00 90.99 C ANISOU 262 CB ARG A 73 14294 14519 5760 2581 102 1028 C ATOM 263 CG ARG A 73 -14.285 37.308 -26.169 1.00 91.74 C ANISOU 263 CG ARG A 73 14225 14625 6008 2373 -339 607 C ATOM 264 CD ARG A 73 -13.176 36.469 -25.556 1.00 93.85 C ANISOU 264 CD ARG A 73 14301 14821 6535 2211 -2 492 C ATOM 265 NE ARG A 73 -12.370 35.795 -26.568 1.00104.60 N ANISOU 265 NE ARG A 73 16092 16188 7462 2439 269 444 N ATOM 266 CZ ARG A 73 -12.665 34.605 -27.084 1.00110.32 C ANISOU 266 CZ ARG A 73 17027 17001 7887 2519 -25 123 C ATOM 267 NH1 ARG A 73 -13.751 33.958 -26.684 1.00112.08 N ANISOU 267 NH1 ARG A 73 17052 17284 8250 2420 -595 -175 N ATOM 268 NH2 ARG A 73 -11.875 34.062 -28.001 1.00112.57 N ANISOU 268 NH2 ARG A 73 17697 17281 7791 2707 274 87 N ATOM 269 N PHE A 74 -15.858 41.278 -25.952 1.00104.26 N ANISOU 269 N PHE A 74 15288 16202 8123 2270 -439 1418 N ATOM 270 CA PHE A 74 -16.682 41.805 -24.869 1.00100.54 C ANISOU 270 CA PHE A 74 14279 15669 8253 1901 -700 1371 C ATOM 271 C PHE A 74 -18.157 41.441 -25.013 1.00106.16 C ANISOU 271 C PHE A 74 15092 16281 8964 1815 -1383 1096 C ATOM 272 O PHE A 74 -18.852 41.236 -24.019 1.00109.57 O ANISOU 272 O PHE A 74 15158 16583 9892 1494 -1625 893 O ATOM 273 CB PHE A 74 -16.540 43.325 -24.768 1.00 99.54 C ANISOU 273 CB PHE A 74 13817 15571 8431 1865 -419 1753 C ATOM 274 CG PHE A 74 -17.489 43.956 -23.788 1.00 97.91 C ANISOU 274 CG PHE A 74 13079 15297 8827 1474 -703 1705 C ATOM 275 CD1 PHE A 74 -18.740 44.391 -24.195 1.00 99.79 C ANISOU 275 CD1 PHE A 74 13368 15461 9086 1397 -1182 1682 C ATOM 276 CD2 PHE A 74 -17.133 44.106 -22.457 1.00 93.99 C ANISOU 276 CD2 PHE A 74 12050 14768 8894 1183 -504 1664 C ATOM 277 CE1 PHE A 74 -19.617 44.966 -23.295 1.00 97.90 C ANISOU 277 CE1 PHE A 74 12630 15100 9469 997 -1406 1623 C ATOM 278 CE2 PHE A 74 -18.005 44.682 -21.554 1.00 91.49 C ANISOU 278 CE2 PHE A 74 11272 14372 9116 817 -723 1611 C ATOM 279 CZ PHE A 74 -19.249 45.113 -21.973 1.00 94.47 C ANISOU 279 CZ PHE A 74 11677 14660 9558 703 -1149 1593 C ATOM 280 N LYS A 75 -18.632 41.364 -26.251 1.00103.87 N ANISOU 280 N LYS A 75 15319 16001 8147 2127 -1687 1077 N ATOM 281 CA LYS A 75 -20.053 41.157 -26.511 1.00104.79 C ANISOU 281 CA LYS A 75 15542 15935 8340 2103 -2387 809 C ATOM 282 C LYS A 75 -20.534 39.749 -26.160 1.00 99.25 C ANISOU 282 C LYS A 75 14834 15103 7771 2063 -2743 342 C ATOM 283 O LYS A 75 -21.716 39.436 -26.310 1.00 99.80 O ANISOU 283 O LYS A 75 14946 14935 8037 2069 -3327 51 O ATOM 284 CB LYS A 75 -20.387 41.501 -27.963 1.00115.73 C ANISOU 284 CB LYS A 75 17529 17342 9103 2503 -2661 911 C ATOM 285 CG LYS A 75 -20.054 42.939 -28.332 1.00121.58 C ANISOU 285 CG LYS A 75 18241 18180 9774 2557 -2326 1396 C ATOM 286 CD LYS A 75 -20.583 43.910 -27.284 1.00119.81 C ANISOU 286 CD LYS A 75 17324 17857 10341 2101 -2342 1507 C ATOM 287 CE LYS A 75 -20.135 45.337 -27.563 1.00121.66 C ANISOU 287 CE LYS A 75 17392 18217 10617 2148 -1938 1997 C ATOM 288 NZ LYS A 75 -20.653 45.840 -28.865 1.00128.75 N ANISOU 288 NZ LYS A 75 18818 19093 11007 2471 -2248 2160 N ATOM 289 N GLU A 76 -19.618 38.906 -25.694 1.00108.32 N ANISOU 289 N GLU A 76 15901 16367 8890 2031 -2392 262 N ATOM 290 CA GLU A 76 -19.984 37.585 -25.195 1.00110.17 C ANISOU 290 CA GLU A 76 16010 16492 9356 1960 -2642 -144 C ATOM 291 C GLU A 76 -20.473 37.700 -23.755 1.00103.26 C ANISOU 291 C GLU A 76 14589 15434 9210 1543 -2631 -210 C ATOM 292 O GLU A 76 -20.964 36.732 -23.172 1.00 98.91 O ANISOU 292 O GLU A 76 13866 14722 8992 1451 -2823 -522 O ATOM 293 CB GLU A 76 -18.796 36.623 -25.277 1.00115.92 C ANISOU 293 CB GLU A 76 16852 17401 9792 2064 -2278 -197 C ATOM 294 CG GLU A 76 -18.409 36.223 -26.695 1.00127.31 C ANISOU 294 CG GLU A 76 18872 18983 10519 2481 -2308 -229 C ATOM 295 CD GLU A 76 -17.318 35.167 -26.727 1.00129.28 C ANISOU 295 CD GLU A 76 19171 19353 10597 2517 -1970 -339 C ATOM 296 OE1 GLU A 76 -16.746 34.869 -25.655 1.00122.62 O ANISOU 296 OE1 GLU A 76 17927 18489 10176 2224 -1687 -336 O ATOM 297 OE2 GLU A 76 -17.034 34.636 -27.823 1.00134.23 O ANISOU 297 OE2 GLU A 76 20249 20078 10674 2835 -1999 -436 O ATOM 298 N LEU A 77 -20.334 38.897 -23.194 1.00 85.14 N ANISOU 298 N LEU A 77 12018 13154 7176 1313 -2379 87 N ATOM 299 CA LEU A 77 -20.728 39.164 -21.817 1.00 75.89 C ANISOU 299 CA LEU A 77 10363 11821 6651 919 -2310 58 C ATOM 300 C LEU A 77 -22.014 39.977 -21.768 1.00 78.33 C ANISOU 300 C LEU A 77 10514 11871 7376 734 -2666 39 C ATOM 301 O LEU A 77 -22.010 41.183 -22.012 1.00 80.78 O ANISOU 301 O LEU A 77 10733 12250 7710 674 -2589 318 O ATOM 302 CB LEU A 77 -19.616 39.917 -21.086 1.00 68.72 C ANISOU 302 CB LEU A 77 9178 11087 5844 773 -1778 359 C ATOM 303 CG LEU A 77 -18.238 39.258 -21.102 1.00 68.85 C ANISOU 303 CG LEU A 77 9317 11274 5568 924 -1397 396 C ATOM 304 CD1 LEU A 77 -17.171 40.241 -20.647 1.00 71.30 C ANISOU 304 CD1 LEU A 77 9375 11679 6036 874 -920 702 C ATOM 305 CD2 LEU A 77 -18.234 38.006 -20.238 1.00 65.67 C ANISOU 305 CD2 LEU A 77 8814 10781 5355 792 -1451 109 C ATOM 306 N THR A 78 -23.116 39.310 -21.451 1.00 94.88 N ANISOU 306 N THR A 78 10662 16752 8636 1412 -1180 583 N ATOM 307 CA THR A 78 -24.405 39.978 -21.354 1.00 99.91 C ANISOU 307 CA THR A 78 11138 17661 9162 1635 -1268 719 C ATOM 308 C THR A 78 -24.795 40.196 -19.895 1.00 96.23 C ANISOU 308 C THR A 78 10632 16936 8995 1560 -1210 785 C ATOM 309 O THR A 78 -24.508 39.358 -19.040 1.00 91.17 O ANISOU 309 O THR A 78 9967 16051 8623 1273 -1197 609 O ATOM 310 CB THR A 78 -25.503 39.173 -22.069 1.00104.93 C ANISOU 310 CB THR A 78 11479 18783 9608 1608 -1508 487 C ATOM 311 OG1 THR A 78 -25.524 37.834 -21.559 1.00104.48 O ANISOU 311 OG1 THR A 78 11290 18640 9766 1249 -1582 172 O ATOM 312 CG2 THR A 78 -25.237 39.130 -23.565 1.00105.45 C ANISOU 312 CG2 THR A 78 11589 19150 9328 1744 -1572 454 C ATOM 313 N PRO A 79 -25.445 41.334 -19.607 1.00 80.68 N ANISOU 313 N PRO A 79 8669 15016 6969 1831 -1168 1043 N ATOM 314 CA PRO A 79 -25.892 41.666 -18.251 1.00 78.81 C ANISOU 314 CA PRO A 79 8399 14558 6987 1801 -1106 1127 C ATOM 315 C PRO A 79 -26.870 40.627 -17.716 1.00 80.02 C ANISOU 315 C PRO A 79 8254 14883 7266 1586 -1259 877 C ATOM 316 O PRO A 79 -27.558 39.971 -18.496 1.00 86.86 O ANISOU 316 O PRO A 79 8899 16143 7961 1560 -1434 695 O ATOM 317 CB PRO A 79 -26.605 43.009 -18.434 1.00 80.37 C ANISOU 317 CB PRO A 79 8621 14915 7002 2188 -1076 1423 C ATOM 318 CG PRO A 79 -26.035 43.578 -19.681 1.00 82.12 C ANISOU 318 CG PRO A 79 9019 15246 6936 2399 -1034 1559 C ATOM 319 CD PRO A 79 -25.757 42.406 -20.567 1.00 83.09 C ANISOU 319 CD PRO A 79 9040 15577 6954 2203 -1164 1281 C ATOM 320 N ASN A 80 -26.922 40.480 -16.397 1.00 75.40 N ANISOU 320 N ASN A 80 7669 14004 6974 1427 -1186 864 N ATOM 321 CA ASN A 80 -27.833 39.534 -15.768 1.00 77.37 C ANISOU 321 CA ASN A 80 7658 14373 7367 1208 -1296 645 C ATOM 322 C ASN A 80 -28.841 40.256 -14.881 1.00 85.96 C ANISOU 322 C ASN A 80 8631 15499 8530 1359 -1271 801 C ATOM 323 O ASN A 80 -28.468 40.900 -13.901 1.00 86.77 O ANISOU 323 O ASN A 80 8907 15251 8810 1397 -1119 969 O ATOM 324 CB ASN A 80 -27.052 38.501 -14.957 1.00 70.71 C ANISOU 324 CB ASN A 80 6903 13157 6806 853 -1238 453 C ATOM 325 CG ASN A 80 -27.906 37.323 -14.536 1.00 69.36 C ANISOU 325 CG ASN A 80 6480 13120 6753 586 -1352 186 C ATOM 326 OD1 ASN A 80 -29.130 37.429 -14.444 1.00 70.64 O ANISOU 326 OD1 ASN A 80 6396 13581 6862 653 -1439 177 O ATOM 327 ND2 ASN A 80 -27.264 36.191 -14.276 1.00 67.81 N ANISOU 327 ND2 ASN A 80 6347 12701 6718 282 -1343 -35 N ATOM 328 N TYR A 81 -30.119 40.148 -15.232 1.00112.38 N ANISOU 328 N TYR A 81 11680 19285 11736 1448 -1420 735 N ATOM 329 CA TYR A 81 -31.167 40.877 -14.526 1.00116.26 C ANISOU 329 CA TYR A 81 12032 19882 12260 1635 -1405 885 C ATOM 330 C TYR A 81 -32.131 39.962 -13.774 1.00109.52 C ANISOU 330 C TYR A 81 10887 19149 11577 1386 -1480 666 C ATOM 331 O TYR A 81 -33.327 40.239 -13.705 1.00109.82 O ANISOU 331 O TYR A 81 10665 19520 11542 1527 -1557 688 O ATOM 332 CB TYR A 81 -31.948 41.765 -15.498 1.00127.49 C ANISOU 332 CB TYR A 81 13340 21738 13360 2024 -1498 1044 C ATOM 333 CG TYR A 81 -31.127 42.867 -16.131 1.00133.15 C ANISOU 333 CG TYR A 81 14366 22319 13906 2314 -1390 1314 C ATOM 334 CD1 TYR A 81 -30.780 44.004 -15.411 1.00134.48 C ANISOU 334 CD1 TYR A 81 14776 22151 14168 2501 -1206 1592 C ATOM 335 CD2 TYR A 81 -30.705 42.776 -17.452 1.00135.58 C ANISOU 335 CD2 TYR A 81 14730 22831 13953 2396 -1462 1286 C ATOM 336 CE1 TYR A 81 -30.032 45.014 -15.986 1.00135.42 C ANISOU 336 CE1 TYR A 81 15189 22128 14137 2746 -1088 1836 C ATOM 337 CE2 TYR A 81 -29.958 43.782 -18.036 1.00135.89 C ANISOU 337 CE2 TYR A 81 15061 22739 13832 2652 -1344 1538 C ATOM 338 CZ TYR A 81 -29.625 44.898 -17.298 1.00136.02 C ANISOU 338 CZ TYR A 81 15316 22408 13956 2819 -1153 1813 C ATOM 339 OH TYR A 81 -28.881 45.902 -17.875 1.00135.87 O ANISOU 339 OH TYR A 81 15598 22242 13785 3053 -1017 2061 O ATOM 340 N ASN A 82 -31.610 38.877 -13.208 1.00 78.28 N ANISOU 340 N ASN A 82 6975 14924 7845 1020 -1451 458 N ATOM 341 CA ASN A 82 -32.436 37.959 -12.432 1.00 73.77 C ANISOU 341 CA ASN A 82 6166 14409 7454 749 -1491 251 C ATOM 342 C ASN A 82 -32.917 38.603 -11.136 1.00 70.88 C ANISOU 342 C ASN A 82 5801 13863 7267 829 -1368 419 C ATOM 343 O ASN A 82 -32.123 38.847 -10.226 1.00 70.45 O ANISOU 343 O ASN A 82 6002 13362 7403 780 -1216 526 O ATOM 344 CB ASN A 82 -31.676 36.666 -12.131 1.00 71.50 C ANISOU 344 CB ASN A 82 5979 13831 7357 358 -1469 7 C ATOM 345 CG ASN A 82 -32.558 35.603 -11.503 1.00 70.89 C ANISOU 345 CG ASN A 82 5659 13840 7438 53 -1513 -232 C ATOM 346 OD1 ASN A 82 -33.718 35.854 -11.175 1.00 74.24 O ANISOU 346 OD1 ASN A 82 5831 14522 7856 120 -1546 -211 O ATOM 347 ND2 ASN A 82 -32.011 34.406 -11.333 1.00 70.48 N ANISOU 347 ND2 ASN A 82 5684 13567 7528 -281 -1504 -460 N ATOM 348 N PRO A 83 -34.227 38.882 -11.051 1.00 81.28 N ANISOU 348 N PRO A 83 6823 15544 8517 957 -1437 434 N ATOM 349 CA PRO A 83 -34.847 39.547 -9.900 1.00 80.59 C ANISOU 349 CA PRO A 83 6699 15355 8567 1071 -1328 593 C ATOM 350 C PRO A 83 -34.550 38.842 -8.577 1.00 79.96 C ANISOU 350 C PRO A 83 6712 14873 8796 752 -1206 498 C ATOM 351 O PRO A 83 -34.594 39.474 -7.520 1.00 78.59 O ANISOU 351 O PRO A 83 6646 14456 8760 841 -1070 664 O ATOM 352 CB PRO A 83 -36.348 39.462 -10.223 1.00 78.68 C ANISOU 352 CB PRO A 83 6039 15657 8200 1151 -1466 502 C ATOM 353 CG PRO A 83 -36.452 38.376 -11.258 1.00 79.48 C ANISOU 353 CG PRO A 83 5958 16057 8184 932 -1638 218 C ATOM 354 CD PRO A 83 -35.229 38.576 -12.081 1.00 79.53 C ANISOU 354 CD PRO A 83 6263 15885 8069 1011 -1632 287 C ATOM 355 N ASP A 84 -34.251 37.549 -8.641 1.00 84.41 N ANISOU 355 N ASP A 84 7250 15364 9458 394 -1249 237 N ATOM 356 CA ASP A 84 -33.984 36.766 -7.440 1.00 79.33 C ANISOU 356 CA ASP A 84 6702 14350 9091 86 -1139 134 C ATOM 357 C ASP A 84 -32.497 36.750 -7.095 1.00 73.83 C ANISOU 357 C ASP A 84 6385 13156 8510 22 -1031 197 C ATOM 358 O ASP A 84 -32.002 35.802 -6.485 1.00 70.43 O ANISOU 358 O ASP A 84 6061 12436 8262 -266 -982 50 O ATOM 359 CB ASP A 84 -34.503 35.336 -7.609 1.00 79.88 C ANISOU 359 CB ASP A 84 6551 14583 9217 -277 -1228 -186 C ATOM 360 CG ASP A 84 -35.979 35.289 -7.955 1.00 86.52 C ANISOU 360 CG ASP A 84 6981 15942 9949 -246 -1341 -280 C ATOM 361 OD1 ASP A 84 -36.679 36.297 -7.721 1.00 89.30 O ANISOU 361 OD1 ASP A 84 7220 16472 10239 37 -1321 -89 O ATOM 362 OD2 ASP A 84 -36.441 34.244 -8.461 1.00 88.82 O ANISOU 362 OD2 ASP A 84 7061 16468 10218 -503 -1448 -551 O ATOM 363 N ILE A 85 -31.789 37.805 -7.489 1.00 65.95 N ANISOU 363 N ILE A 85 5590 12064 7402 295 -991 413 N ATOM 364 CA ILE A 85 -30.365 37.929 -7.196 1.00 63.15 C ANISOU 364 CA ILE A 85 5578 11267 7149 258 -886 483 C ATOM 365 C ILE A 85 -30.001 39.360 -6.810 1.00 63.25 C ANISOU 365 C ILE A 85 5793 11091 7148 553 -765 778 C ATOM 366 O ILE A 85 -30.440 40.317 -7.452 1.00 64.35 O ANISOU 366 O ILE A 85 5879 11472 7099 846 -790 941 O ATOM 367 CB ILE A 85 -29.497 37.494 -8.395 1.00 66.14 C ANISOU 367 CB ILE A 85 6042 11695 7393 210 -961 378 C ATOM 368 CG1 ILE A 85 -29.825 36.057 -8.804 1.00 65.46 C ANISOU 368 CG1 ILE A 85 5777 11776 7317 -90 -1077 69 C ATOM 369 CG2 ILE A 85 -28.019 37.627 -8.059 1.00 62.79 C ANISOU 369 CG2 ILE A 85 5946 10829 7081 170 -847 443 C ATOM 370 CD1 ILE A 85 -28.957 35.532 -9.924 1.00 66.10 C ANISOU 370 CD1 ILE A 85 5951 11889 7276 -152 -1145 -57 C ATOM 371 N ILE A 86 -29.200 39.497 -5.758 1.00 63.80 N ANISOU 371 N ILE A 86 6102 10726 7413 479 -633 843 N ATOM 372 CA ILE A 86 -28.755 40.805 -5.291 1.00 62.32 C ANISOU 372 CA ILE A 86 6134 10306 7239 717 -505 1100 C ATOM 373 C ILE A 86 -27.320 41.081 -5.725 1.00 60.44 C ANISOU 373 C ILE A 86 6167 9811 6985 726 -449 1152 C ATOM 374 O ILE A 86 -26.400 40.353 -5.356 1.00 58.27 O ANISOU 374 O ILE A 86 6020 9267 6851 505 -425 1028 O ATOM 375 CB ILE A 86 -28.846 40.929 -3.756 1.00 56.30 C ANISOU 375 CB ILE A 86 5458 9237 6695 652 -386 1150 C ATOM 376 CG1 ILE A 86 -30.306 40.976 -3.302 1.00 58.25 C ANISOU 376 CG1 ILE A 86 5446 9744 6941 709 -406 1155 C ATOM 377 CG2 ILE A 86 -28.110 42.170 -3.277 1.00 53.95 C ANISOU 377 CG2 ILE A 86 5437 8632 6429 846 -249 1378 C ATOM 378 CD1 ILE A 86 -30.999 39.631 -3.304 1.00 58.57 C ANISOU 378 CD1 ILE A 86 5239 9980 7036 431 -499 905 C ATOM 379 N PHE A 87 -27.134 42.132 -6.514 1.00 61.05 N ANISOU 379 N PHE A 87 6332 9978 6887 988 -425 1335 N ATOM 380 CA PHE A 87 -25.800 42.522 -6.953 1.00 63.76 C ANISOU 380 CA PHE A 87 6928 10090 7207 1007 -350 1403 C ATOM 381 C PHE A 87 -25.340 43.760 -6.200 1.00 64.82 C ANISOU 381 C PHE A 87 7301 9909 7419 1164 -188 1629 C ATOM 382 O PHE A 87 -26.010 44.792 -6.218 1.00 65.36 O ANISOU 382 O PHE A 87 7369 10074 7390 1424 -146 1821 O ATOM 383 CB PHE A 87 -25.776 42.774 -8.464 1.00 69.70 C ANISOU 383 CB PHE A 87 7645 11142 7697 1165 -419 1440 C ATOM 384 CG PHE A 87 -26.092 41.557 -9.283 1.00 71.03 C ANISOU 384 CG PHE A 87 7603 11607 7777 999 -579 1199 C ATOM 385 CD1 PHE A 87 -25.096 40.655 -9.617 1.00 70.80 C ANISOU 385 CD1 PHE A 87 7652 11451 7796 779 -597 1023 C ATOM 386 CD2 PHE A 87 -27.385 41.309 -9.712 1.00 73.17 C ANISOU 386 CD2 PHE A 87 7594 12290 7918 1064 -711 1136 C ATOM 387 CE1 PHE A 87 -25.383 39.530 -10.367 1.00 71.66 C ANISOU 387 CE1 PHE A 87 7587 11817 7824 623 -737 790 C ATOM 388 CE2 PHE A 87 -27.679 40.185 -10.463 1.00 73.48 C ANISOU 388 CE2 PHE A 87 7441 12602 7877 893 -858 895 C ATOM 389 CZ PHE A 87 -26.676 39.295 -10.791 1.00 72.73 C ANISOU 389 CZ PHE A 87 7449 12354 7830 670 -868 722 C ATOM 390 N LYS A 88 -24.198 43.650 -5.529 1.00 75.10 N ANISOU 390 N LYS A 88 8805 10835 8893 1010 -98 1598 N ATOM 391 CA LYS A 88 -23.672 44.760 -4.747 1.00 79.36 C ANISOU 391 CA LYS A 88 9578 11051 9523 1118 56 1780 C ATOM 392 C LYS A 88 -23.379 45.946 -5.655 1.00 84.61 C ANISOU 392 C LYS A 88 10384 11754 10009 1362 132 1986 C ATOM 393 O LYS A 88 -23.747 47.081 -5.350 1.00 89.38 O ANISOU 393 O LYS A 88 11088 12292 10582 1579 227 2187 O ATOM 394 CB LYS A 88 -22.411 44.341 -3.987 1.00 75.81 C ANISOU 394 CB LYS A 88 9301 10230 9274 896 117 1680 C ATOM 395 CG LYS A 88 -22.015 45.300 -2.873 1.00 76.04 C ANISOU 395 CG LYS A 88 9537 9918 9436 955 259 1818 C ATOM 396 CD LYS A 88 -20.874 44.745 -2.034 1.00 71.40 C ANISOU 396 CD LYS A 88 9078 9005 9045 730 292 1689 C ATOM 397 CE LYS A 88 -20.578 45.642 -0.840 1.00 65.16 C ANISOU 397 CE LYS A 88 8476 7897 8386 777 417 1801 C ATOM 398 NZ LYS A 88 -19.504 45.080 0.024 1.00 53.49 N ANISOU 398 NZ LYS A 88 7107 6127 7089 571 431 1668 N ATOM 399 N ASP A 89 -22.722 45.669 -6.778 1.00 77.08 N ANISOU 399 N ASP A 89 9450 10903 8933 1329 99 1936 N ATOM 400 CA ASP A 89 -22.403 46.696 -7.759 1.00 83.85 C ANISOU 400 CA ASP A 89 10449 11809 9600 1547 177 2125 C ATOM 401 C ASP A 89 -21.824 47.930 -7.081 1.00 84.35 C ANISOU 401 C ASP A 89 10777 11520 9752 1643 363 2319 C ATOM 402 O ASP A 89 -22.248 49.054 -7.350 1.00 87.89 O ANISOU 402 O ASP A 89 11322 12000 10074 1904 442 2536 O ATOM 403 CB ASP A 89 -23.649 47.075 -8.562 1.00 94.03 C ANISOU 403 CB ASP A 89 11583 13491 10653 1811 94 2231 C ATOM 404 CG ASP A 89 -23.325 47.913 -9.783 1.00101.79 C ANISOU 404 CG ASP A 89 12703 14575 11399 2030 152 2403 C ATOM 405 OD1 ASP A 89 -22.127 48.166 -10.030 1.00101.51 O ANISOU 405 OD1 ASP A 89 12873 14307 11390 1954 264 2431 O ATOM 406 OD2 ASP A 89 -24.267 48.318 -10.497 1.00107.36 O ANISOU 406 OD2 ASP A 89 13307 15600 11885 2283 88 2509 O ATOM 407 N GLU A 90 -20.856 47.716 -6.197 1.00 87.57 N ANISOU 407 N GLU A 90 11307 11590 10374 1436 432 2235 N ATOM 408 CA GLU A 90 -20.237 48.818 -5.472 1.00 90.32 C ANISOU 408 CA GLU A 90 11903 11589 10827 1485 605 2382 C ATOM 409 C GLU A 90 -19.467 49.731 -6.421 1.00 92.42 C ANISOU 409 C GLU A 90 12364 11793 10960 1594 732 2534 C ATOM 410 O GLU A 90 -19.050 50.825 -6.041 1.00 91.83 O ANISOU 410 O GLU A 90 12510 11455 10928 1670 893 2686 O ATOM 411 CB GLU A 90 -19.317 48.298 -4.361 1.00 89.40 C ANISOU 411 CB GLU A 90 11853 11157 10956 1229 630 2233 C ATOM 412 CG GLU A 90 -18.000 47.710 -4.849 1.00 92.48 C ANISOU 412 CG GLU A 90 12289 11464 11385 1034 634 2097 C ATOM 413 CD GLU A 90 -18.123 46.263 -5.292 1.00 94.02 C ANISOU 413 CD GLU A 90 12281 11878 11563 882 472 1880 C ATOM 414 OE1 GLU A 90 -19.192 45.656 -5.068 1.00 95.18 O ANISOU 414 OE1 GLU A 90 12253 12211 11701 886 360 1816 O ATOM 415 OE2 GLU A 90 -17.142 45.733 -5.858 1.00 92.10 O ANISOU 415 OE2 GLU A 90 12057 11617 11319 752 466 1767 O ATOM 416 N GLU A 91 -19.286 49.276 -7.657 1.00 97.58 N ANISOU 416 N GLU A 91 12944 12686 11448 1595 668 2487 N ATOM 417 CA GLU A 91 -18.597 50.065 -8.672 1.00104.28 C ANISOU 417 CA GLU A 91 13970 13509 12144 1700 792 2630 C ATOM 418 C GLU A 91 -19.573 50.986 -9.398 1.00107.47 C ANISOU 418 C GLU A 91 14404 14123 12307 2031 812 2858 C ATOM 419 O GLU A 91 -19.163 51.942 -10.058 1.00107.45 O ANISOU 419 O GLU A 91 14605 14046 12176 2175 955 3041 O ATOM 420 CB GLU A 91 -17.889 49.156 -9.682 1.00108.14 C ANISOU 420 CB GLU A 91 14383 14154 12553 1557 725 2474 C ATOM 421 CG GLU A 91 -16.974 48.106 -9.067 1.00105.90 C ANISOU 421 CG GLU A 91 14047 13706 12484 1254 683 2235 C ATOM 422 CD GLU A 91 -17.685 46.792 -8.806 1.00105.57 C ANISOU 422 CD GLU A 91 13764 13859 12490 1138 489 2026 C ATOM 423 OE1 GLU A 91 -16.991 45.770 -8.607 1.00105.58 O ANISOU 423 OE1 GLU A 91 13713 13792 12612 915 435 1820 O ATOM 424 OE2 GLU A 91 -18.935 46.780 -8.808 1.00105.85 O ANISOU 424 OE2 GLU A 91 13661 14117 12439 1271 397 2066 O ATOM 425 N ASN A 92 -20.863 50.687 -9.270 1.00112.11 N ANISOU 425 N ASN A 92 14787 14976 12832 2154 674 2844 N ATOM 426 CA ASN A 92 -21.915 51.451 -9.936 1.00116.33 C ANISOU 426 CA ASN A 92 15305 15767 13129 2493 660 3042 C ATOM 427 C ASN A 92 -21.907 51.250 -11.449 1.00113.71 C ANISOU 427 C ASN A 92 14925 15753 12526 2598 592 3055 C ATOM 428 O ASN A 92 -22.785 51.743 -12.157 1.00117.74 O ANISOU 428 O ASN A 92 15395 16539 12803 2888 549 3198 O ATOM 429 CB ASN A 92 -21.807 52.940 -9.596 1.00122.47 C ANISOU 429 CB ASN A 92 16365 16267 13900 2704 863 3304 C ATOM 430 CG ASN A 92 -21.914 53.205 -8.109 1.00125.16 C ANISOU 430 CG ASN A 92 16758 16314 14483 2630 927 3295 C ATOM 431 OD1 ASN A 92 -22.268 52.318 -7.331 1.00121.99 O ANISOU 431 OD1 ASN A 92 16163 15955 14232 2465 811 3118 O ATOM 432 ND2 ASN A 92 -21.606 54.432 -7.704 1.00130.26 N ANISOU 432 ND2 ASN A 92 17677 16651 15163 2751 1119 3485 N ATOM 433 N THR A 93 -20.909 50.519 -11.933 1.00 86.12 N ANISOU 433 N THR A 93 11437 12229 9058 2372 582 2901 N ATOM 434 CA THR A 93 -20.765 50.259 -13.359 1.00 84.98 C ANISOU 434 CA THR A 93 11262 12367 8661 2443 527 2892 C ATOM 435 C THR A 93 -21.655 49.102 -13.805 1.00 85.38 C ANISOU 435 C THR A 93 10999 12828 8614 2405 287 2693 C ATOM 436 O THR A 93 -21.912 48.927 -14.997 1.00 89.80 O ANISOU 436 O THR A 93 11490 13710 8920 2526 203 2691 O ATOM 437 CB THR A 93 -19.302 49.942 -13.724 1.00 80.15 C ANISOU 437 CB THR A 93 10781 11561 8112 2217 624 2800 C ATOM 438 OG1 THR A 93 -18.858 48.798 -12.984 1.00 71.64 O ANISOU 438 OG1 THR A 93 9574 10376 7270 1907 542 2540 O ATOM 439 CG2 THR A 93 -18.406 51.127 -13.402 1.00 80.94 C ANISOU 439 CG2 THR A 93 11187 11277 8291 2243 871 2991 C ATOM 440 N GLY A 94 -22.126 48.319 -12.840 1.00 96.12 N ANISOU 440 N GLY A 94 12174 14174 10172 2232 184 2521 N ATOM 441 CA GLY A 94 -22.949 47.162 -13.135 1.00 93.90 C ANISOU 441 CA GLY A 94 11594 14247 9837 2145 -29 2306 C ATOM 442 C GLY A 94 -22.131 46.041 -13.742 1.00 89.52 C ANISOU 442 C GLY A 94 10997 13732 9285 1899 -94 2077 C ATOM 443 O GLY A 94 -22.660 45.182 -14.447 1.00 91.80 O ANISOU 443 O GLY A 94 11082 14354 9444 1860 -260 1913 O ATOM 444 N ALA A 95 -20.831 46.054 -13.467 1.00 77.67 N ANISOU 444 N ALA A 95 9686 11894 7932 1735 37 2057 N ATOM 445 CA ALA A 95 -19.925 45.039 -13.991 1.00 73.55 C ANISOU 445 CA ALA A 95 9146 11372 7426 1513 -1 1846 C ATOM 446 C ALA A 95 -20.134 43.702 -13.287 1.00 73.66 C ANISOU 446 C ALA A 95 8980 11378 7630 1251 -132 1578 C ATOM 447 O ALA A 95 -19.663 42.665 -13.754 1.00 72.71 O ANISOU 447 O ALA A 95 8798 11322 7505 1076 -204 1368 O ATOM 448 CB ALA A 95 -18.480 45.495 -13.851 1.00 68.11 C ANISOU 448 CB ALA A 95 8697 10335 6846 1425 184 1906 C ATOM 449 N ASP A 96 -20.846 43.735 -12.164 1.00 79.12 N ANISOU 449 N ASP A 96 9598 11982 8483 1229 -151 1587 N ATOM 450 CA ASP A 96 -21.102 42.531 -11.381 1.00 83.60 C ANISOU 450 CA ASP A 96 10017 12510 9238 984 -250 1356 C ATOM 451 C ASP A 96 -22.186 41.665 -12.017 1.00 84.66 C ANISOU 451 C ASP A 96 9891 13041 9236 961 -434 1195 C ATOM 452 O ASP A 96 -22.419 40.533 -11.590 1.00 81.30 O ANISOU 452 O ASP A 96 9337 12619 8935 739 -522 977 O ATOM 453 CB ASP A 96 -21.498 42.897 -9.948 1.00 87.74 C ANISOU 453 CB ASP A 96 10563 12803 9971 972 -192 1429 C ATOM 454 CG ASP A 96 -20.391 43.621 -9.205 1.00 90.10 C ANISOU 454 CG ASP A 96 11109 12697 10429 950 -23 1542 C ATOM 455 OD1 ASP A 96 -19.304 43.813 -9.792 1.00 90.72 O ANISOU 455 OD1 ASP A 96 11328 12674 10467 930 52 1558 O ATOM 456 OD2 ASP A 96 -20.608 43.998 -8.033 1.00 90.45 O ANISOU 456 OD2 ASP A 96 11200 12532 10634 948 36 1607 O ATOM 457 N ARG A 97 -22.844 42.202 -13.040 1.00 93.03 N ANISOU 457 N ARG A 97 10879 14434 10033 1190 -490 1301 N ATOM 458 CA ARG A 97 -23.930 41.498 -13.712 1.00 96.62 C ANISOU 458 CA ARG A 97 11069 15311 10332 1191 -674 1152 C ATOM 459 C ARG A 97 -23.457 40.873 -15.022 1.00 92.66 C ANISOU 459 C ARG A 97 10554 15016 9637 1146 -751 1011 C ATOM 460 O ARG A 97 -24.020 39.882 -15.484 1.00 97.11 O ANISOU 460 O ARG A 97 10916 15848 10132 1025 -905 790 O ATOM 461 CB ARG A 97 -25.103 42.449 -13.970 1.00105.84 C ANISOU 461 CB ARG A 97 12130 16767 11316 1497 -711 1343 C ATOM 462 CG ARG A 97 -25.480 43.308 -12.771 1.00109.42 C ANISOU 462 CG ARG A 97 12643 17002 11929 1601 -604 1527 C ATOM 463 CD ARG A 97 -26.577 44.304 -13.116 1.00117.11 C ANISOU 463 CD ARG A 97 13531 18264 12702 1944 -632 1729 C ATOM 464 NE ARG A 97 -27.889 43.670 -13.208 1.00120.22 N ANISOU 464 NE ARG A 97 13592 19052 13034 1931 -807 1584 N ATOM 465 CZ ARG A 97 -28.737 43.560 -12.191 1.00117.54 C ANISOU 465 CZ ARG A 97 13099 18711 12851 1886 -817 1557 C ATOM 466 NH1 ARG A 97 -29.910 42.968 -12.363 1.00117.77 N ANISOU 466 NH1 ARG A 97 12807 19125 12815 1859 -972 1411 N ATOM 467 NH2 ARG A 97 -28.411 44.043 -11.000 1.00112.77 N ANISOU 467 NH2 ARG A 97 12657 17727 12464 1861 -669 1668 N ATOM 468 N LEU A 98 -22.419 41.458 -15.614 1.00 66.68 N ANISOU 468 N LEU A 98 7481 11596 6259 1236 -635 1134 N ATOM 469 CA LEU A 98 -21.866 40.959 -16.870 1.00 65.83 C ANISOU 469 CA LEU A 98 7390 11665 5958 1212 -682 1020 C ATOM 470 C LEU A 98 -21.182 39.609 -16.680 1.00 62.38 C ANISOU 470 C LEU A 98 6929 11089 5682 898 -722 734 C ATOM 471 O LEU A 98 -20.303 39.463 -15.833 1.00 61.11 O ANISOU 471 O LEU A 98 6898 10563 5756 748 -616 714 O ATOM 472 CB LEU A 98 -20.877 41.968 -17.461 1.00 66.79 C ANISOU 472 CB LEU A 98 7763 11650 5963 1375 -516 1235 C ATOM 473 CG LEU A 98 -21.403 43.376 -17.749 1.00 74.08 C ANISOU 473 CG LEU A 98 8772 12669 6705 1708 -446 1542 C ATOM 474 CD1 LEU A 98 -20.328 44.219 -18.419 1.00 73.41 C ANISOU 474 CD1 LEU A 98 8952 12435 6506 1823 -267 1724 C ATOM 475 CD2 LEU A 98 -22.656 43.320 -18.607 1.00 79.15 C ANISOU 475 CD2 LEU A 98 9210 13793 7071 1901 -623 1531 C ATOM 476 N MET A 99 -21.581 38.627 -17.482 1.00 65.13 N ANISOU 476 N MET A 99 7118 11732 5895 809 -875 510 N ATOM 477 CA MET A 99 -21.059 37.273 -17.348 1.00 63.77 C ANISOU 477 CA MET A 99 6922 11446 5861 520 -922 223 C ATOM 478 C MET A 99 -21.349 36.455 -18.605 1.00 64.83 C ANISOU 478 C MET A 99 6932 11938 5761 485 -1069 13 C ATOM 479 O MET A 99 -22.250 36.787 -19.374 1.00 70.53 O ANISOU 479 O MET A 99 7521 13035 6242 654 -1175 55 O ATOM 480 CB MET A 99 -21.693 36.596 -16.137 1.00 61.44 C ANISOU 480 CB MET A 99 6508 11023 5815 324 -969 100 C ATOM 481 CG MET A 99 -23.204 36.735 -16.105 1.00 63.52 C ANISOU 481 CG MET A 99 6534 11610 5991 405 -1091 111 C ATOM 482 SD MET A 99 -23.938 36.119 -14.585 1.00 63.91 S ANISOU 482 SD MET A 99 6461 11481 6338 189 -1102 11 S ATOM 483 CE MET A 99 -22.971 37.008 -13.370 1.00 59.54 C ANISOU 483 CE MET A 99 6168 10439 6016 240 -901 241 C ATOM 484 N THR A 100 -20.582 35.388 -18.811 1.00 80.44 N ANISOU 484 N THR A 100 8957 13805 7803 277 -1078 -218 N ATOM 485 CA THR A 100 -20.783 34.500 -19.955 1.00 82.45 C ANISOU 485 CA THR A 100 9111 14366 7851 214 -1213 -452 C ATOM 486 C THR A 100 -22.080 33.698 -19.824 1.00 90.43 C ANISOU 486 C THR A 100 9869 15625 8865 79 -1387 -656 C ATOM 487 O THR A 100 -22.601 33.521 -18.725 1.00 92.85 O ANISOU 487 O THR A 100 10101 15786 9390 -37 -1385 -667 O ATOM 488 CB THR A 100 -19.599 33.528 -20.126 1.00 75.06 C ANISOU 488 CB THR A 100 8302 13213 7002 24 -1165 -656 C ATOM 489 OG1 THR A 100 -19.592 32.581 -19.049 1.00 73.65 O ANISOU 489 OG1 THR A 100 8105 12773 7108 -226 -1172 -828 O ATOM 490 CG2 THR A 100 -18.280 34.291 -20.141 1.00 67.98 C ANISOU 490 CG2 THR A 100 7632 12059 6137 128 -980 -470 C ATOM 491 N GLN A 101 -22.595 33.215 -20.951 1.00 74.92 N ANISOU 491 N GLN A 101 7772 14042 6653 88 -1534 -823 N ATOM 492 CA GLN A 101 -23.851 32.464 -20.973 1.00 76.79 C ANISOU 492 CA GLN A 101 7746 14567 6864 -48 -1707 -1039 C ATOM 493 C GLN A 101 -23.862 31.317 -19.955 1.00 76.60 C ANISOU 493 C GLN A 101 7698 14264 7141 -378 -1698 -1260 C ATOM 494 O GLN A 101 -24.803 31.186 -19.162 1.00 70.89 O ANISOU 494 O GLN A 101 6815 13566 6552 -471 -1738 -1285 O ATOM 495 CB GLN A 101 -24.110 31.921 -22.379 1.00 79.25 C ANISOU 495 CB GLN A 101 7958 15278 6875 -37 -1858 -1242 C ATOM 496 CG GLN A 101 -25.306 30.995 -22.499 1.00 81.93 C ANISOU 496 CG GLN A 101 8022 15920 7186 -226 -2042 -1522 C ATOM 497 CD GLN A 101 -26.627 31.735 -22.515 1.00 81.37 C ANISOU 497 CD GLN A 101 7708 16220 6988 -45 -2150 -1400 C ATOM 498 OE1 GLN A 101 -26.797 32.742 -21.829 1.00 86.80 O ANISOU 498 OE1 GLN A 101 8423 16801 7755 132 -2064 -1125 O ATOM 499 NE2 GLN A 101 -27.576 31.233 -23.302 1.00 84.53 N ANISOU 499 NE2 GLN A 101 7864 17068 7187 -85 -2342 -1614 N ATOM 500 N ARG A 102 -22.813 30.497 -19.975 1.00 74.90 N ANISOU 500 N ARG A 102 7650 13783 7027 -543 -1637 -1415 N ATOM 501 CA ARG A 102 -22.707 29.367 -19.062 1.00 68.90 C ANISOU 501 CA ARG A 102 6912 12729 6537 -839 -1616 -1621 C ATOM 502 C ARG A 102 -22.786 29.816 -17.610 1.00 67.46 C ANISOU 502 C ARG A 102 6772 12237 6624 -854 -1510 -1446 C ATOM 503 O ARG A 102 -23.377 29.137 -16.772 1.00 70.26 O ANISOU 503 O ARG A 102 7045 12489 7162 -1058 -1527 -1567 O ATOM 504 CB ARG A 102 -21.409 28.602 -19.312 1.00 69.55 C ANISOU 504 CB ARG A 102 7203 12551 6673 -945 -1546 -1765 C ATOM 505 CG ARG A 102 -21.163 27.470 -18.322 1.00 67.24 C ANISOU 505 CG ARG A 102 6982 11905 6660 -1217 -1505 -1952 C ATOM 506 CD ARG A 102 -19.973 26.621 -18.738 1.00 66.63 C ANISOU 506 CD ARG A 102 7088 11631 6596 -1302 -1458 -2127 C ATOM 507 NE ARG A 102 -19.851 25.426 -17.908 1.00 65.10 N ANISOU 507 NE ARG A 102 6966 11132 6639 -1556 -1434 -2330 N ATOM 508 CZ ARG A 102 -20.573 24.322 -18.075 1.00 67.48 C ANISOU 508 CZ ARG A 102 7174 11523 6942 -1782 -1526 -2604 C ATOM 509 NH1 ARG A 102 -21.479 24.257 -19.042 1.00 70.61 N ANISOU 509 NH1 ARG A 102 7381 12332 7118 -1791 -1662 -2723 N ATOM 510 NH2 ARG A 102 -20.394 23.281 -17.274 1.00 66.27 N ANISOU 510 NH2 ARG A 102 7123 11048 7007 -2000 -1479 -2763 N ATOM 511 N CYS A 103 -22.177 30.959 -17.317 1.00 69.19 N ANISOU 511 N CYS A 103 7127 12300 6861 -645 -1393 -1163 N ATOM 512 CA CYS A 103 -22.195 31.508 -15.970 1.00 66.98 C ANISOU 512 CA CYS A 103 6904 11730 6815 -634 -1288 -983 C ATOM 513 C CYS A 103 -23.596 31.995 -15.614 1.00 73.04 C ANISOU 513 C CYS A 103 7457 12735 7559 -567 -1354 -896 C ATOM 514 O CYS A 103 -24.038 31.866 -14.472 1.00 75.39 O ANISOU 514 O CYS A 103 7718 12862 8064 -672 -1317 -882 O ATOM 515 CB CYS A 103 -21.187 32.652 -15.841 1.00 63.81 C ANISOU 515 CB CYS A 103 6702 11121 6422 -431 -1145 -716 C ATOM 516 SG CYS A 103 -21.072 33.357 -14.182 1.00 61.11 S ANISOU 516 SG CYS A 103 6458 10399 6360 -415 -1011 -506 S ATOM 517 N LYS A 104 -24.291 32.552 -16.600 1.00 75.04 N ANISOU 517 N LYS A 104 7568 13395 7550 -381 -1451 -839 N ATOM 518 CA LYS A 104 -25.660 33.018 -16.406 1.00 78.85 C ANISOU 518 CA LYS A 104 7816 14167 7977 -287 -1530 -768 C ATOM 519 C LYS A 104 -26.587 31.847 -16.095 1.00 76.45 C ANISOU 519 C LYS A 104 7297 13980 7770 -567 -1633 -1045 C ATOM 520 O LYS A 104 -27.577 31.998 -15.381 1.00 73.74 O ANISOU 520 O LYS A 104 6785 13716 7516 -588 -1647 -1011 O ATOM 521 CB LYS A 104 -26.163 33.754 -17.649 1.00 87.87 C ANISOU 521 CB LYS A 104 8851 15749 8787 -17 -1630 -673 C ATOM 522 CG LYS A 104 -25.298 34.927 -18.083 1.00 89.69 C ANISOU 522 CG LYS A 104 9303 15884 8892 261 -1518 -396 C ATOM 523 CD LYS A 104 -25.844 35.597 -19.340 1.00 96.64 C ANISOU 523 CD LYS A 104 10090 17208 9422 539 -1619 -303 C ATOM 524 CE LYS A 104 -27.039 36.495 -19.036 1.00101.42 C ANISOU 524 CE LYS A 104 10525 18046 9963 762 -1661 -120 C ATOM 525 NZ LYS A 104 -28.264 35.731 -18.666 1.00105.32 N ANISOU 525 NZ LYS A 104 10713 18777 10525 590 -1800 -329 N ATOM 526 N ASP A 105 -26.262 30.682 -16.646 1.00 70.42 N ANISOU 526 N ASP A 105 6544 13225 6986 -785 -1694 -1321 N ATOM 527 CA ASP A 105 -27.055 29.479 -16.429 1.00 74.45 C ANISOU 527 CA ASP A 105 6879 13820 7589 -1086 -1778 -1611 C ATOM 528 C ASP A 105 -26.827 28.930 -15.027 1.00 72.74 C ANISOU 528 C ASP A 105 6772 13171 7694 -1303 -1657 -1637 C ATOM 529 O ASP A 105 -27.776 28.688 -14.284 1.00 76.10 O ANISOU 529 O ASP A 105 7037 13633 8244 -1434 -1663 -1683 O ATOM 530 CB ASP A 105 -26.705 28.407 -17.466 1.00 78.34 C ANISOU 530 CB ASP A 105 7386 14422 7957 -1248 -1868 -1903 C ATOM 531 CG ASP A 105 -27.113 28.798 -18.874 1.00 78.97 C ANISOU 531 CG ASP A 105 7324 14983 7696 -1061 -2011 -1923 C ATOM 532 OD1 ASP A 105 -27.579 29.940 -19.072 1.00 79.11 O ANISOU 532 OD1 ASP A 105 7256 15232 7571 -782 -2033 -1689 O ATOM 533 OD2 ASP A 105 -26.966 27.959 -19.786 1.00 78.66 O ANISOU 533 OD2 ASP A 105 7272 15090 7526 -1183 -2101 -2173 O ATOM 534 N LYS A 106 -25.562 28.728 -14.677 1.00 67.93 N ANISOU 534 N LYS A 106 6434 12164 7211 -1334 -1545 -1609 N ATOM 535 CA LYS A 106 -25.202 28.208 -13.364 1.00 64.09 C ANISOU 535 CA LYS A 106 6089 11251 7013 -1511 -1430 -1623 C ATOM 536 C LYS A 106 -25.699 29.125 -12.251 1.00 64.48 C ANISOU 536 C LYS A 106 6104 11208 7189 -1399 -1351 -1382 C ATOM 537 O LYS A 106 -26.238 28.662 -11.245 1.00 64.88 O ANISOU 537 O LYS A 106 6111 11115 7423 -1570 -1310 -1433 O ATOM 538 CB LYS A 106 -23.686 28.016 -13.257 1.00 61.98 C ANISOU 538 CB LYS A 106 6108 10613 6827 -1501 -1332 -1606 C ATOM 539 CG LYS A 106 -23.190 26.660 -13.733 1.00 62.80 C ANISOU 539 CG LYS A 106 6293 10628 6941 -1718 -1365 -1900 C ATOM 540 CD LYS A 106 -23.691 26.344 -15.132 1.00 67.15 C ANISOU 540 CD LYS A 106 6684 11591 7239 -1728 -1506 -2077 C ATOM 541 CE LYS A 106 -23.405 24.901 -15.512 1.00 66.67 C ANISOU 541 CE LYS A 106 6688 11440 7202 -1979 -1539 -2400 C ATOM 542 NZ LYS A 106 -24.077 24.531 -16.787 1.00 68.86 N ANISOU 542 NZ LYS A 106 6784 12141 7238 -2022 -1689 -2604 N ATOM 543 N LEU A 107 -25.522 30.429 -12.442 1.00 68.70 N ANISOU 543 N LEU A 107 6669 11817 7616 -1111 -1321 -1120 N ATOM 544 CA LEU A 107 -25.912 31.406 -11.435 1.00 63.07 C ANISOU 544 CA LEU A 107 5952 11005 7007 -973 -1238 -878 C ATOM 545 C LEU A 107 -27.416 31.385 -11.189 1.00 62.75 C ANISOU 545 C LEU A 107 5628 11258 6955 -1012 -1307 -915 C ATOM 546 O LEU A 107 -27.861 31.270 -10.049 1.00 62.75 O ANISOU 546 O LEU A 107 5606 11093 7143 -1112 -1238 -891 O ATOM 547 CB LEU A 107 -25.472 32.810 -11.845 1.00 63.83 C ANISOU 547 CB LEU A 107 6141 11146 6964 -653 -1192 -602 C ATOM 548 CG LEU A 107 -25.386 33.817 -10.698 1.00 59.65 C ANISOU 548 CG LEU A 107 5720 10365 6580 -517 -1064 -349 C ATOM 549 CD1 LEU A 107 -24.205 33.481 -9.803 1.00 55.49 C ANISOU 549 CD1 LEU A 107 5440 9373 6271 -641 -949 -357 C ATOM 550 CD2 LEU A 107 -25.270 35.238 -11.224 1.00 62.89 C ANISOU 550 CD2 LEU A 107 6183 10891 6819 -196 -1030 -83 C ATOM 551 N ASN A 108 -28.193 31.504 -12.262 1.00 70.37 N ANISOU 551 N ASN A 108 6373 12671 7692 -926 -1441 -976 N ATOM 552 CA ASN A 108 -29.649 31.482 -12.161 1.00 74.14 C ANISOU 552 CA ASN A 108 6539 13493 8135 -954 -1524 -1031 C ATOM 553 C ASN A 108 -30.159 30.178 -11.558 1.00 75.69 C ANISOU 553 C ASN A 108 6635 13610 8513 -1319 -1527 -1295 C ATOM 554 O ASN A 108 -31.210 30.146 -10.917 1.00 72.91 O ANISOU 554 O ASN A 108 6082 13376 8244 -1392 -1523 -1309 O ATOM 555 CB ASN A 108 -30.290 31.709 -13.533 1.00 78.87 C ANISOU 555 CB ASN A 108 6921 14608 8437 -806 -1689 -1088 C ATOM 556 CG ASN A 108 -30.162 33.142 -14.008 1.00 70.87 C ANISOU 556 CG ASN A 108 5964 13731 7235 -413 -1679 -791 C ATOM 557 OD1 ASN A 108 -29.941 34.053 -13.211 1.00 68.97 O ANISOU 557 OD1 ASN A 108 5853 13260 7094 -251 -1556 -543 O ATOM 558 ND2 ASN A 108 -30.306 33.350 -15.312 1.00 80.61 N ANISOU 558 ND2 ASN A 108 7110 15333 8185 -255 -1803 -817 N ATOM 559 N ALA A 109 -29.406 29.103 -11.773 1.00 92.31 N ANISOU 559 N ALA A 109 8887 15507 10677 -1545 -1524 -1502 N ATOM 560 CA ALA A 109 -29.762 27.797 -11.236 1.00 96.56 C ANISOU 560 CA ALA A 109 9386 15914 11388 -1902 -1508 -1757 C ATOM 561 C ALA A 109 -29.435 27.734 -9.753 1.00 94.04 C ANISOU 561 C ALA A 109 9248 15148 11335 -1984 -1347 -1648 C ATOM 562 O ALA A 109 -30.094 27.029 -8.990 1.00 92.28 O ANISOU 562 O ALA A 109 8948 14848 11267 -2222 -1302 -1765 O ATOM 563 CB ALA A 109 -29.029 26.699 -11.988 1.00101.45 C ANISOU 563 CB ALA A 109 10131 16446 11970 -2087 -1553 -2007 C ATOM 564 N LEU A 110 -28.408 28.478 -9.355 1.00101.59 N ANISOU 564 N LEU A 110 10449 15815 12336 -1790 -1255 -1428 N ATOM 565 CA LEU A 110 -27.996 28.543 -7.960 1.00 95.61 C ANISOU 565 CA LEU A 110 9881 14639 11807 -1827 -1110 -1307 C ATOM 566 C LEU A 110 -28.932 29.441 -7.159 1.00 93.83 C ANISOU 566 C LEU A 110 9515 14511 11626 -1701 -1062 -1115 C ATOM 567 O LEU A 110 -29.208 29.180 -5.990 1.00 94.11 O ANISOU 567 O LEU A 110 9588 14325 11845 -1823 -964 -1099 O ATOM 568 CB LEU A 110 -26.560 29.058 -7.856 1.00 89.88 C ANISOU 568 CB LEU A 110 9445 13600 11105 -1665 -1038 -1155 C ATOM 569 CG LEU A 110 -25.982 29.215 -6.449 1.00 84.70 C ANISOU 569 CG LEU A 110 9004 12515 10665 -1671 -899 -1024 C ATOM 570 CD1 LEU A 110 -26.101 27.912 -5.675 1.00 84.97 C ANISOU 570 CD1 LEU A 110 9100 12310 10876 -1965 -854 -1214 C ATOM 571 CD2 LEU A 110 -24.534 29.676 -6.513 1.00 79.76 C ANISOU 571 CD2 LEU A 110 8630 11632 10043 -1526 -848 -911 C ATOM 572 N ALA A 111 -29.423 30.497 -7.800 1.00 78.33 N ANISOU 572 N ALA A 111 7398 12880 9484 -1444 -1126 -968 N ATOM 573 CA ALA A 111 -30.301 31.461 -7.145 1.00 75.37 C ANISOU 573 CA ALA A 111 6889 12622 9125 -1274 -1084 -773 C ATOM 574 C ALA A 111 -31.610 30.824 -6.690 1.00 72.84 C ANISOU 574 C ALA A 111 6301 12494 8881 -1481 -1099 -920 C ATOM 575 O ALA A 111 -32.285 31.341 -5.798 1.00 74.64 O ANISOU 575 O ALA A 111 6449 12717 9193 -1416 -1024 -792 O ATOM 576 CB ALA A 111 -30.574 32.640 -8.067 1.00 77.91 C ANISOU 576 CB ALA A 111 7104 13283 9213 -945 -1159 -602 C ATOM 577 N ILE A 112 -31.965 29.702 -7.307 1.00 69.75 N ANISOU 577 N ILE A 112 5771 12271 8459 -1736 -1188 -1197 N ATOM 578 CA ILE A 112 -33.182 28.985 -6.942 1.00 74.46 C ANISOU 578 CA ILE A 112 6105 13053 9133 -1982 -1196 -1373 C ATOM 579 C ILE A 112 -32.949 28.118 -5.706 1.00 68.07 C ANISOU 579 C ILE A 112 5471 11814 8577 -2255 -1050 -1441 C ATOM 580 O ILE A 112 -33.775 28.091 -4.792 1.00 69.82 O ANISOU 580 O ILE A 112 5575 12033 8919 -2345 -966 -1418 O ATOM 581 CB ILE A 112 -33.698 28.111 -8.105 1.00 73.46 C ANISOU 581 CB ILE A 112 5755 13285 8871 -2170 -1349 -1664 C ATOM 582 CG1 ILE A 112 -33.831 28.946 -9.380 1.00 74.55 C ANISOU 582 CG1 ILE A 112 5750 13843 8731 -1878 -1501 -1592 C ATOM 583 CG2 ILE A 112 -35.029 27.471 -7.744 1.00 75.08 C ANISOU 583 CG2 ILE A 112 5654 13721 9155 -2426 -1354 -1845 C ATOM 584 CD1 ILE A 112 -34.217 28.142 -10.600 1.00 81.79 C ANISOU 584 CD1 ILE A 112 6473 15119 9487 -2035 -1665 -1879 C ATOM 585 N SER A 113 -31.820 27.416 -5.684 1.00 65.22 N ANISOU 585 N SER A 113 5396 11096 8287 -2374 -1013 -1520 N ATOM 586 CA SER A 113 -31.443 26.606 -4.531 1.00 64.92 C ANISOU 586 CA SER A 113 5577 10617 8472 -2594 -874 -1566 C ATOM 587 C SER A 113 -31.446 27.458 -3.269 1.00 62.56 C ANISOU 587 C SER A 113 5377 10104 8290 -2437 -744 -1312 C ATOM 588 O SER A 113 -31.977 27.054 -2.236 1.00 64.73 O ANISOU 588 O SER A 113 5645 10232 8716 -2601 -636 -1328 O ATOM 589 CB SER A 113 -30.050 26.003 -4.729 1.00 62.57 C ANISOU 589 CB SER A 113 5596 9971 8205 -2638 -861 -1632 C ATOM 590 OG SER A 113 -30.030 25.075 -5.798 1.00 66.13 O ANISOU 590 OG SER A 113 5987 10574 8564 -2812 -962 -1891 O ATOM 591 N VAL A 114 -30.847 28.641 -3.368 1.00 78.54 N ANISOU 591 N VAL A 114 7500 12104 10238 -2125 -749 -1081 N ATOM 592 CA VAL A 114 -30.718 29.548 -2.234 1.00 76.93 C ANISOU 592 CA VAL A 114 7419 11681 10129 -1951 -631 -838 C ATOM 593 C VAL A 114 -32.068 29.864 -1.599 1.00 81.92 C ANISOU 593 C VAL A 114 7806 12520 10798 -1956 -584 -787 C ATOM 594 O VAL A 114 -32.282 29.603 -0.415 1.00 85.85 O ANISOU 594 O VAL A 114 8380 12784 11454 -2069 -459 -760 O ATOM 595 CB VAL A 114 -30.041 30.865 -2.649 1.00 74.60 C ANISOU 595 CB VAL A 114 7222 11406 9716 -1612 -653 -610 C ATOM 596 CG1 VAL A 114 -29.912 31.793 -1.452 1.00 74.29 C ANISOU 596 CG1 VAL A 114 7321 11127 9778 -1447 -527 -377 C ATOM 597 CG2 VAL A 114 -28.678 30.587 -3.263 1.00 71.33 C ANISOU 597 CG2 VAL A 114 7038 10797 9268 -1606 -685 -658 C ATOM 598 N MET A 115 -32.974 30.431 -2.389 1.00 79.52 N ANISOU 598 N MET A 115 7210 12665 10340 -1822 -683 -773 N ATOM 599 CA MET A 115 -34.301 30.784 -1.901 1.00 76.42 C ANISOU 599 CA MET A 115 6542 12530 9964 -1800 -650 -731 C ATOM 600 C MET A 115 -35.010 29.561 -1.326 1.00 74.83 C ANISOU 600 C MET A 115 6229 12297 9908 -2168 -588 -945 C ATOM 601 O MET A 115 -35.763 29.665 -0.357 1.00 74.75 O ANISOU 601 O MET A 115 6128 12271 10003 -2212 -479 -891 O ATOM 602 CB MET A 115 -35.137 31.402 -3.024 1.00 81.48 C ANISOU 602 CB MET A 115 6865 13701 10393 -1611 -795 -727 C ATOM 603 CG MET A 115 -34.483 32.601 -3.694 1.00 83.90 C ANISOU 603 CG MET A 115 7291 14052 10537 -1246 -847 -514 C ATOM 604 SD MET A 115 -35.553 33.408 -4.903 1.00 70.40 S ANISOU 604 SD MET A 115 5219 12967 8560 -975 -1008 -476 S ATOM 605 CE MET A 115 -36.904 33.943 -3.853 1.00123.53 C ANISOU 605 CE MET A 115 11701 19861 15374 -897 -919 -372 C ATOM 606 N ASN A 116 -34.757 28.404 -1.928 1.00 81.37 N ANISOU 606 N ASN A 116 7074 13103 10740 -2434 -648 -1189 N ATOM 607 CA ASN A 116 -35.376 27.157 -1.500 1.00 86.25 C ANISOU 607 CA ASN A 116 7610 13671 11491 -2814 -584 -1414 C ATOM 608 C ASN A 116 -34.784 26.650 -0.187 1.00 81.00 C ANISOU 608 C ASN A 116 7262 12489 11026 -2950 -409 -1366 C ATOM 609 O ASN A 116 -35.488 26.070 0.640 1.00 82.94 O ANISOU 609 O ASN A 116 7447 12663 11402 -3175 -292 -1433 O ATOM 610 CB ASN A 116 -35.231 26.097 -2.594 1.00 94.20 C ANISOU 610 CB ASN A 116 8567 14795 12429 -3046 -700 -1695 C ATOM 611 CG ASN A 116 -36.097 24.876 -2.348 1.00103.29 C ANISOU 611 CG ASN A 116 9566 15988 13691 -3449 -649 -1953 C ATOM 612 OD1 ASN A 116 -36.214 24.398 -1.220 1.00106.11 O ANISOU 612 OD1 ASN A 116 10046 16046 14225 -3625 -486 -1943 O ATOM 613 ND2 ASN A 116 -36.704 24.360 -3.410 1.00109.70 N ANISOU 613 ND2 ASN A 116 10115 17172 14394 -3602 -782 -2191 N ATOM 614 N GLN A 117 -33.488 26.880 -0.002 1.00 62.83 N ANISOU 614 N GLN A 117 5294 9836 8742 -2808 -389 -1248 N ATOM 615 CA GLN A 117 -32.786 26.437 1.197 1.00 62.91 C ANISOU 615 CA GLN A 117 5629 9356 8919 -2896 -243 -1195 C ATOM 616 C GLN A 117 -33.164 27.286 2.409 1.00 67.12 C ANISOU 616 C GLN A 117 6182 9795 9527 -2746 -118 -974 C ATOM 617 O GLN A 117 -33.577 26.760 3.442 1.00 60.14 O ANISOU 617 O GLN A 117 5348 8727 8775 -2921 18 -992 O ATOM 618 CB GLN A 117 -31.273 26.475 0.967 1.00 62.49 C ANISOU 618 CB GLN A 117 5894 9002 8849 -2771 -276 -1147 C ATOM 619 CG GLN A 117 -30.442 25.826 2.066 1.00 58.02 C ANISOU 619 CG GLN A 117 5669 7940 8437 -2871 -152 -1135 C ATOM 620 CD GLN A 117 -30.565 24.314 2.086 1.00 60.44 C ANISOU 620 CD GLN A 117 6040 8098 8827 -3211 -113 -1377 C ATOM 621 OE1 GLN A 117 -31.618 23.759 1.773 1.00 64.29 O ANISOU 621 OE1 GLN A 117 6292 8823 9314 -3430 -119 -1536 O ATOM 622 NE2 GLN A 117 -29.484 23.639 2.461 1.00 64.26 N ANISOU 622 NE2 GLN A 117 6847 8187 9383 -3256 -69 -1410 N ATOM 623 N TRP A 118 -33.024 28.601 2.276 1.00 83.37 N ANISOU 623 N TRP A 118 8213 11970 11494 -2421 -156 -764 N ATOM 624 CA TRP A 118 -33.358 29.518 3.361 1.00 85.45 C ANISOU 624 CA TRP A 118 8503 12154 11811 -2246 -42 -551 C ATOM 625 C TRP A 118 -34.394 30.547 2.918 1.00 87.06 C ANISOU 625 C TRP A 118 8390 12792 11897 -2034 -95 -452 C ATOM 626 O TRP A 118 -34.101 31.413 2.095 1.00 87.51 O ANISOU 626 O TRP A 118 8417 13017 11816 -1784 -194 -353 O ATOM 627 CB TRP A 118 -32.104 30.232 3.870 1.00 86.47 C ANISOU 627 CB TRP A 118 8963 11932 11962 -2029 -5 -365 C ATOM 628 CG TRP A 118 -30.960 29.311 4.162 1.00 88.68 C ANISOU 628 CG TRP A 118 9547 11817 12329 -2180 19 -456 C ATOM 629 CD1 TRP A 118 -30.772 28.566 5.289 1.00 88.67 C ANISOU 629 CD1 TRP A 118 9747 11477 12468 -2344 140 -484 C ATOM 630 CD2 TRP A 118 -29.837 29.045 3.312 1.00 90.70 C ANISOU 630 CD2 TRP A 118 9947 11985 12530 -2161 -76 -526 C ATOM 631 NE1 TRP A 118 -29.603 27.849 5.192 1.00 89.46 N ANISOU 631 NE1 TRP A 118 10104 11284 12602 -2416 118 -568 N ATOM 632 CE2 TRP A 118 -29.012 28.126 3.991 1.00 90.54 C ANISOU 632 CE2 TRP A 118 10204 11572 12626 -2309 -12 -599 C ATOM 633 CE3 TRP A 118 -29.452 29.493 2.046 1.00 92.10 C ANISOU 633 CE3 TRP A 118 10050 12381 12564 -2023 -204 -531 C ATOM 634 CZ2 TRP A 118 -27.824 27.646 3.440 1.00 90.88 C ANISOU 634 CZ2 TRP A 118 10433 11446 12652 -2320 -75 -683 C ATOM 635 CZ3 TRP A 118 -28.273 29.016 1.504 1.00 93.33 C ANISOU 635 CZ3 TRP A 118 10393 12363 12703 -2050 -256 -614 C ATOM 636 CH2 TRP A 118 -27.473 28.102 2.201 1.00 92.16 C ANISOU 636 CH2 TRP A 118 10504 11833 12680 -2195 -193 -692 C ATOM 637 N PRO A 119 -35.611 30.456 3.471 1.00 75.85 N ANISOU 637 N PRO A 119 6737 11555 10529 -2126 -20 -474 N ATOM 638 CA PRO A 119 -36.691 31.390 3.138 1.00 76.37 C ANISOU 638 CA PRO A 119 6478 12051 10487 -1916 -63 -386 C ATOM 639 C PRO A 119 -36.259 32.840 3.332 1.00 71.89 C ANISOU 639 C PRO A 119 6048 11417 9852 -1527 -49 -115 C ATOM 640 O PRO A 119 -35.556 33.145 4.295 1.00 66.13 O ANISOU 640 O PRO A 119 5608 10304 9212 -1463 61 17 O ATOM 641 CB PRO A 119 -37.784 31.029 4.146 1.00 78.71 C ANISOU 641 CB PRO A 119 6611 12393 10903 -2088 77 -423 C ATOM 642 CG PRO A 119 -37.516 29.612 4.501 1.00 79.14 C ANISOU 642 CG PRO A 119 6801 12178 11089 -2469 144 -618 C ATOM 643 CD PRO A 119 -36.028 29.460 4.471 1.00 76.34 C ANISOU 643 CD PRO A 119 6834 11421 10751 -2428 121 -580 C ATOM 644 N GLY A 120 -36.672 33.716 2.422 1.00 75.80 N ANISOU 644 N GLY A 120 6344 12275 10181 -1270 -158 -38 N ATOM 645 CA GLY A 120 -36.362 35.130 2.524 1.00 74.09 C ANISOU 645 CA GLY A 120 6250 12014 9888 -895 -136 218 C ATOM 646 C GLY A 120 -34.886 35.436 2.353 1.00 70.16 C ANISOU 646 C GLY A 120 6108 11167 9380 -803 -146 306 C ATOM 647 O GLY A 120 -34.440 36.556 2.603 1.00 65.98 O ANISOU 647 O GLY A 120 5749 10501 8820 -533 -99 515 O ATOM 648 N VAL A 121 -34.126 34.435 1.923 1.00 84.05 N ANISOU 648 N VAL A 121 7980 12785 11170 -1031 -201 139 N ATOM 649 CA VAL A 121 -32.692 34.597 1.716 1.00 83.53 C ANISOU 649 CA VAL A 121 8229 12409 11101 -971 -213 192 C ATOM 650 C VAL A 121 -32.322 34.328 0.261 1.00 88.86 C ANISOU 650 C VAL A 121 8837 13296 11630 -974 -360 85 C ATOM 651 O VAL A 121 -32.427 33.199 -0.217 1.00 91.12 O ANISOU 651 O VAL A 121 9032 13664 11923 -1225 -425 -135 O ATOM 652 CB VAL A 121 -31.886 33.655 2.626 1.00 78.71 C ANISOU 652 CB VAL A 121 7875 11368 10662 -1210 -129 104 C ATOM 653 CG1 VAL A 121 -30.396 33.870 2.421 1.00 74.87 C ANISOU 653 CG1 VAL A 121 7686 10589 10171 -1132 -144 156 C ATOM 654 CG2 VAL A 121 -32.269 33.874 4.081 1.00 81.07 C ANISOU 654 CG2 VAL A 121 8248 11462 11091 -1211 20 205 C ATOM 655 N LYS A 122 -31.889 35.372 -0.439 1.00 82.26 N ANISOU 655 N LYS A 122 8059 12540 10655 -697 -404 240 N ATOM 656 CA LYS A 122 -31.562 35.259 -1.856 1.00 82.89 C ANISOU 656 CA LYS A 122 8082 12845 10568 -659 -536 165 C ATOM 657 C LYS A 122 -30.057 35.183 -2.081 1.00 79.05 C ANISOU 657 C LYS A 122 7896 12038 10100 -670 -524 174 C ATOM 658 O LYS A 122 -29.270 35.374 -1.155 1.00 78.33 O ANISOU 658 O LYS A 122 8051 11571 10141 -671 -420 259 O ATOM 659 CB LYS A 122 -32.143 36.442 -2.634 1.00 85.80 C ANISOU 659 CB LYS A 122 8302 13560 10739 -333 -595 328 C ATOM 660 CG LYS A 122 -33.649 36.593 -2.512 1.00 90.92 C ANISOU 660 CG LYS A 122 8620 14580 11347 -282 -621 321 C ATOM 661 CD LYS A 122 -34.138 37.807 -3.282 1.00 94.77 C ANISOU 661 CD LYS A 122 8991 15391 11625 84 -679 501 C ATOM 662 CE LYS A 122 -35.642 37.976 -3.152 1.00 98.86 C ANISOU 662 CE LYS A 122 9158 16305 12099 160 -710 491 C ATOM 663 NZ LYS A 122 -36.132 39.166 -3.901 1.00101.55 N ANISOU 663 NZ LYS A 122 9396 16967 12223 552 -770 674 N ATOM 664 N LEU A 123 -29.665 34.900 -3.319 1.00 71.59 N ANISOU 664 N LEU A 123 6923 11262 9017 -676 -631 79 N ATOM 665 CA LEU A 123 -28.257 34.852 -3.689 1.00 64.64 C ANISOU 665 CA LEU A 123 6296 10131 8133 -672 -622 81 C ATOM 666 C LEU A 123 -27.721 36.260 -3.921 1.00 59.36 C ANISOU 666 C LEU A 123 5765 9419 7371 -369 -575 328 C ATOM 667 O LEU A 123 -28.327 37.054 -4.641 1.00 58.72 O ANISOU 667 O LEU A 123 5553 9639 7119 -152 -621 438 O ATOM 668 CB LEU A 123 -28.061 33.995 -4.942 1.00 68.94 C ANISOU 668 CB LEU A 123 6759 10878 8556 -794 -744 -122 C ATOM 669 CG LEU A 123 -26.683 34.009 -5.611 1.00 70.84 C ANISOU 669 CG LEU A 123 7217 10955 8745 -756 -746 -124 C ATOM 670 CD1 LEU A 123 -25.601 33.537 -4.654 1.00 71.94 C ANISOU 670 CD1 LEU A 123 7610 10643 9082 -889 -652 -152 C ATOM 671 CD2 LEU A 123 -26.697 33.149 -6.863 1.00 74.50 C ANISOU 671 CD2 LEU A 123 7569 11667 9070 -870 -870 -337 C ATOM 672 N ARG A 124 -26.588 36.566 -3.301 1.00 52.86 N ANISOU 672 N ARG A 124 5209 8219 6657 -354 -479 413 N ATOM 673 CA ARG A 124 -25.967 37.875 -3.444 1.00 55.57 C ANISOU 673 CA ARG A 124 5713 8465 6935 -104 -412 636 C ATOM 674 C ARG A 124 -24.617 37.760 -4.138 1.00 56.47 C ANISOU 674 C ARG A 124 6004 8440 7014 -128 -414 600 C ATOM 675 O ARG A 124 -23.793 36.922 -3.774 1.00 56.36 O ANISOU 675 O ARG A 124 6105 8187 7123 -314 -403 466 O ATOM 676 CB ARG A 124 -25.800 38.540 -2.077 1.00 58.28 C ANISOU 676 CB ARG A 124 6216 8495 7433 -47 -284 780 C ATOM 677 CG ARG A 124 -24.954 39.806 -2.095 1.00 59.20 C ANISOU 677 CG ARG A 124 6546 8429 7519 159 -195 984 C ATOM 678 CD ARG A 124 -25.006 40.519 -0.753 1.00 56.41 C ANISOU 678 CD ARG A 124 6323 7813 7299 228 -77 1119 C ATOM 679 NE ARG A 124 -24.032 41.602 -0.659 1.00 56.90 N ANISOU 679 NE ARG A 124 6618 7638 7364 368 18 1277 N ATOM 680 CZ ARG A 124 -22.835 41.482 -0.094 1.00 55.37 C ANISOU 680 CZ ARG A 124 6625 7118 7295 262 72 1240 C ATOM 681 NH1 ARG A 124 -22.463 40.322 0.429 1.00 53.86 N ANISOU 681 NH1 ARG A 124 6445 6793 7228 41 36 1064 N ATOM 682 NH2 ARG A 124 -22.009 42.519 -0.049 1.00 53.33 N ANISOU 682 NH2 ARG A 124 6559 6669 7036 378 163 1376 N ATOM 683 N VAL A 125 -24.402 38.603 -5.143 1.00 55.56 N ANISOU 683 N VAL A 125 5908 8479 6722 72 -422 722 N ATOM 684 CA VAL A 125 -23.137 38.637 -5.863 1.00 54.47 C ANISOU 684 CA VAL A 125 5932 8231 6534 71 -404 710 C ATOM 685 C VAL A 125 -22.392 39.927 -5.545 1.00 55.05 C ANISOU 685 C VAL A 125 6216 8072 6626 245 -273 932 C ATOM 686 O VAL A 125 -22.920 41.022 -5.739 1.00 57.43 O ANISOU 686 O VAL A 125 6513 8486 6821 470 -235 1124 O ATOM 687 CB VAL A 125 -23.346 38.536 -7.386 1.00 52.49 C ANISOU 687 CB VAL A 125 5562 8333 6048 146 -502 664 C ATOM 688 CG1 VAL A 125 -22.016 38.664 -8.113 1.00 53.08 C ANISOU 688 CG1 VAL A 125 5812 8289 6066 158 -459 670 C ATOM 689 CG2 VAL A 125 -24.029 37.226 -7.740 1.00 52.16 C ANISOU 689 CG2 VAL A 125 5316 8517 5988 -51 -633 417 C ATOM 690 N THR A 126 -21.168 39.791 -5.048 1.00 57.51 N ANISOU 690 N THR A 126 6715 8061 7074 141 -203 899 N ATOM 691 CA THR A 126 -20.357 40.946 -4.686 1.00 58.72 C ANISOU 691 CA THR A 126 7074 7970 7268 261 -74 1078 C ATOM 692 C THR A 126 -19.439 41.347 -5.828 1.00 61.59 C ANISOU 692 C THR A 126 7527 8374 7499 328 -41 1120 C ATOM 693 O THR A 126 -19.170 42.528 -6.034 1.00 64.80 O ANISOU 693 O THR A 126 8056 8723 7842 493 60 1310 O ATOM 694 CB THR A 126 -19.483 40.657 -3.458 1.00 55.40 C ANISOU 694 CB THR A 126 6800 7181 7067 116 -13 1018 C ATOM 695 OG1 THR A 126 -18.561 39.603 -3.765 1.00 51.57 O ANISOU 695 OG1 THR A 126 6337 6632 6627 -57 -59 828 O ATOM 696 CG2 THR A 126 -20.343 40.252 -2.273 1.00 55.78 C ANISOU 696 CG2 THR A 126 6785 7167 7243 47 -28 983 C ATOM 697 N GLU A 127 -18.955 40.354 -6.565 1.00 52.32 N ANISOU 697 N GLU A 127 6303 7291 6285 197 -114 941 N ATOM 698 CA GLU A 127 -18.021 40.604 -7.652 1.00 52.29 C ANISOU 698 CA GLU A 127 6381 7329 6158 241 -77 958 C ATOM 699 C GLU A 127 -18.298 39.669 -8.827 1.00 56.05 C ANISOU 699 C GLU A 127 6714 8105 6475 189 -200 796 C ATOM 700 O GLU A 127 -18.593 38.489 -8.637 1.00 52.38 O ANISOU 700 O GLU A 127 6145 7682 6076 23 -297 596 O ATOM 701 CB GLU A 127 -16.583 40.434 -7.158 1.00 48.21 C ANISOU 701 CB GLU A 127 6020 6497 5800 114 3 893 C ATOM 702 CG GLU A 127 -15.531 41.061 -8.054 1.00 54.84 C ANISOU 702 CG GLU A 127 6975 7319 6541 177 97 967 C ATOM 703 CD GLU A 127 -15.514 42.577 -7.976 1.00 60.24 C ANISOU 703 CD GLU A 127 7790 7914 7184 352 232 1218 C ATOM 704 OE1 GLU A 127 -16.376 43.154 -7.279 1.00 61.77 O ANISOU 704 OE1 GLU A 127 7979 8081 7410 446 243 1338 O ATOM 705 OE2 GLU A 127 -14.634 43.191 -8.615 1.00 61.43 O ANISOU 705 OE2 GLU A 127 8056 8016 7268 393 339 1295 O ATOM 706 N GLY A 128 -18.211 40.210 -10.039 1.00 68.80 N ANISOU 706 N GLY A 128 8340 9924 7876 334 -189 884 N ATOM 707 CA GLY A 128 -18.426 39.437 -11.249 1.00 67.21 C ANISOU 707 CA GLY A 128 8019 10025 7494 308 -301 738 C ATOM 708 C GLY A 128 -17.289 39.612 -12.235 1.00 67.55 C ANISOU 708 C GLY A 128 8182 10061 7425 336 -232 747 C ATOM 709 O GLY A 128 -16.167 39.165 -11.986 1.00 50.09 O ANISOU 709 O GLY A 128 6064 7628 5342 200 -178 645 O ATOM 710 N TRP A 129 -17.580 40.260 -13.360 1.00 53.11 N ANISOU 710 N TRP A 129 6348 8484 5347 523 -231 869 N ATOM 711 CA TRP A 129 -16.553 40.582 -14.345 1.00 59.27 C ANISOU 711 CA TRP A 129 7255 9269 5995 574 -139 912 C ATOM 712 C TRP A 129 -15.881 41.902 -13.998 1.00 57.13 C ANISOU 712 C TRP A 129 7181 8750 5775 682 49 1152 C ATOM 713 O TRP A 129 -16.551 42.917 -13.807 1.00 56.74 O ANISOU 713 O TRP A 129 7169 8718 5671 860 93 1361 O ATOM 714 CB TRP A 129 -17.143 40.662 -15.754 1.00 61.31 C ANISOU 714 CB TRP A 129 7439 9916 5942 731 -217 936 C ATOM 715 CG TRP A 129 -16.215 41.296 -16.752 1.00 58.09 C ANISOU 715 CG TRP A 129 7189 9515 5369 836 -90 1051 C ATOM 716 CD1 TRP A 129 -15.119 40.725 -17.328 1.00 58.09 C ANISOU 716 CD1 TRP A 129 7246 9471 5355 721 -46 917 C ATOM 717 CD2 TRP A 129 -16.304 42.624 -17.288 1.00 60.45 C ANISOU 717 CD2 TRP A 129 7616 9862 5488 1078 25 1326 C ATOM 718 NE1 TRP A 129 -14.519 41.613 -18.188 1.00 59.34 N ANISOU 718 NE1 TRP A 129 7552 9655 5341 864 94 1090 N ATOM 719 CE2 TRP A 129 -15.227 42.785 -18.182 1.00 60.65 C ANISOU 719 CE2 TRP A 129 7776 9868 5402 1082 142 1346 C ATOM 720 CE3 TRP A 129 -17.189 43.689 -17.099 1.00 60.02 C ANISOU 720 CE3 TRP A 129 7587 9861 5356 1300 49 1560 C ATOM 721 CZ2 TRP A 129 -15.013 43.969 -18.885 1.00 61.84 C ANISOU 721 CZ2 TRP A 129 8094 10038 5364 1287 290 1596 C ATOM 722 CZ3 TRP A 129 -16.973 44.863 -17.798 1.00 62.55 C ANISOU 722 CZ3 TRP A 129 8083 10195 5488 1520 188 1809 C ATOM 723 CH2 TRP A 129 -15.895 44.993 -18.680 1.00 63.85 C ANISOU 723 CH2 TRP A 129 8389 10327 5543 1505 311 1828 C ATOM 724 N ASP A 130 -14.554 41.882 -13.927 1.00 78.06 N ANISOU 724 N ASP A 130 7218 12654 9785 399 -1241 -1169 N ATOM 725 CA ASP A 130 -13.782 43.057 -13.536 1.00 91.16 C ANISOU 725 CA ASP A 130 8903 14157 11577 552 -1367 -1134 C ATOM 726 C ASP A 130 -13.039 43.677 -14.720 1.00100.11 C ANISOU 726 C ASP A 130 9965 15334 12737 432 -1456 -1048 C ATOM 727 O ASP A 130 -12.637 42.971 -15.644 1.00103.03 O ANISOU 727 O ASP A 130 10311 15806 13029 252 -1393 -1072 O ATOM 728 CB ASP A 130 -12.802 42.686 -12.420 1.00 94.95 C ANISOU 728 CB ASP A 130 9534 14426 12116 679 -1337 -1254 C ATOM 729 CG ASP A 130 -12.403 43.878 -11.575 1.00100.01 C ANISOU 729 CG ASP A 130 10222 14891 12889 891 -1465 -1222 C ATOM 730 OD1 ASP A 130 -13.288 44.685 -11.217 1.00106.33 O ANISOU 730 OD1 ASP A 130 10970 15712 13717 1015 -1536 -1162 O ATOM 731 OD2 ASP A 130 -11.206 43.999 -11.250 1.00 98.51 O ANISOU 731 OD2 ASP A 130 10122 14539 12770 939 -1499 -1260 O ATOM 732 N GLU A 131 -12.856 44.996 -14.689 1.00 95.99 N ANISOU 732 N GLU A 131 9409 14742 12322 530 -1613 -947 N ATOM 733 CA GLU A 131 -12.185 45.694 -15.784 1.00102.50 C ANISOU 733 CA GLU A 131 10151 15619 13174 410 -1725 -839 C ATOM 734 C GLU A 131 -10.814 46.244 -15.381 1.00107.62 C ANISOU 734 C GLU A 131 10883 16083 13923 496 -1824 -839 C ATOM 735 O GLU A 131 -10.488 47.383 -15.728 1.00107.23 O ANISOU 735 O GLU A 131 10784 16004 13955 506 -1996 -715 O ATOM 736 CB GLU A 131 -13.041 46.857 -16.302 1.00103.71 C ANISOU 736 CB GLU A 131 10179 15855 13372 411 -1867 -685 C ATOM 737 CG GLU A 131 -14.547 46.693 -16.132 1.00105.78 C ANISOU 737 CG GLU A 131 10380 16232 13579 440 -1808 -674 C ATOM 738 CD GLU A 131 -15.301 47.978 -16.441 1.00106.61 C ANISOU 738 CD GLU A 131 10377 16375 13755 492 -1971 -531 C ATOM 739 OE1 GLU A 131 -14.640 48.999 -16.739 1.00108.03 O ANISOU 739 OE1 GLU A 131 10539 16473 14033 506 -2141 -441 O ATOM 740 OE2 GLU A 131 -16.550 47.972 -16.386 1.00105.44 O ANISOU 740 OE2 GLU A 131 10160 16339 13565 518 -1938 -501 O ATOM 741 N ASP A 132 -10.026 45.446 -14.657 1.00145.87 N ANISOU 741 N ASP A 132 15854 20806 18765 550 -1728 -968 N ATOM 742 CA ASP A 132 -8.661 45.820 -14.266 1.00152.38 C ANISOU 742 CA ASP A 132 16763 21463 19672 618 -1804 -972 C ATOM 743 C ASP A 132 -8.240 45.137 -12.969 1.00152.27 C ANISOU 743 C ASP A 132 16906 21265 19685 759 -1712 -1114 C ATOM 744 O ASP A 132 -8.956 44.291 -12.438 1.00152.72 O ANISOU 744 O ASP A 132 17000 21339 19687 785 -1587 -1213 O ATOM 745 CB ASP A 132 -8.511 47.336 -14.103 1.00157.36 C ANISOU 745 CB ASP A 132 17377 21986 20425 724 -2021 -835 C ATOM 746 CG ASP A 132 -7.056 47.778 -14.058 1.00159.62 C ANISOU 746 CG ASP A 132 17719 22150 20778 730 -2123 -791 C ATOM 747 OD1 ASP A 132 -6.656 48.418 -13.061 1.00160.45 O ANISOU 747 OD1 ASP A 132 17931 22043 20990 903 -2224 -788 O ATOM 748 OD2 ASP A 132 -6.308 47.481 -15.015 1.00158.66 O ANISOU 748 OD2 ASP A 132 17532 22154 20597 563 -2105 -758 O ATOM 749 N GLY A 133 -7.075 45.528 -12.461 1.00113.19 N ANISOU 749 N GLY A 133 12043 16144 14819 841 -1784 -1112 N ATOM 750 CA GLY A 133 -6.562 45.006 -11.208 1.00109.57 C ANISOU 750 CA GLY A 133 11735 15495 14403 975 -1716 -1232 C ATOM 751 C GLY A 133 -7.581 45.056 -10.090 1.00108.56 C ANISOU 751 C GLY A 133 11657 15293 14296 1138 -1693 -1286 C ATOM 752 O GLY A 133 -8.217 46.088 -9.860 1.00107.73 O ANISOU 752 O GLY A 133 11521 15164 14247 1249 -1812 -1209 O ATOM 753 N HIS A 134 -7.724 43.929 -9.397 1.00122.51 N ANISOU 753 N HIS A 134 13499 17032 16017 1152 -1545 -1417 N ATOM 754 CA HIS A 134 -8.649 43.790 -8.277 1.00122.34 C ANISOU 754 CA HIS A 134 13519 16970 15994 1293 -1503 -1476 C ATOM 755 C HIS A 134 -8.650 42.312 -7.908 1.00118.53 C ANISOU 755 C HIS A 134 13098 16501 15437 1222 -1339 -1606 C ATOM 756 O HIS A 134 -9.142 41.915 -6.848 1.00117.17 O ANISOU 756 O HIS A 134 12981 16281 15257 1318 -1285 -1674 O ATOM 757 CB HIS A 134 -10.057 44.230 -8.677 1.00125.33 C ANISOU 757 CB HIS A 134 13776 17519 16324 1292 -1529 -1404 C ATOM 758 CG HIS A 134 -10.782 44.998 -7.616 1.00128.11 C ANISOU 758 CG HIS A 134 14148 17803 16726 1510 -1596 -1399 C ATOM 759 ND1 HIS A 134 -11.817 44.462 -6.884 1.00128.50 N ANISOU 759 ND1 HIS A 134 14186 17930 16707 1575 -1504 -1457 N ATOM 760 CD2 HIS A 134 -10.628 46.270 -7.173 1.00130.27 C ANISOU 760 CD2 HIS A 134 14448 17947 17104 1683 -1755 -1344 C ATOM 761 CE1 HIS A 134 -12.268 45.366 -6.031 1.00129.87 C ANISOU 761 CE1 HIS A 134 14372 18039 16934 1788 -1592 -1447 C ATOM 762 NE2 HIS A 134 -11.561 46.471 -6.186 1.00131.69 N ANISOU 762 NE2 HIS A 134 14633 18131 17273 1861 -1748 -1385 N ATOM 763 N HIS A 135 -8.094 41.505 -8.810 1.00112.71 N ANISOU 763 N HIS A 135 12346 15837 14641 1051 -1272 -1639 N ATOM 764 CA HIS A 135 -7.909 40.072 -8.602 1.00106.21 C ANISOU 764 CA HIS A 135 11592 15008 13754 969 -1140 -1766 C ATOM 765 C HIS A 135 -6.545 39.662 -9.154 1.00106.28 C ANISOU 765 C HIS A 135 11643 14968 13773 889 -1123 -1811 C ATOM 766 O HIS A 135 -5.978 40.352 -10.002 1.00105.18 O ANISOU 766 O HIS A 135 11438 14877 13647 844 -1196 -1728 O ATOM 767 CB HIS A 135 -9.011 39.279 -9.306 1.00100.49 C ANISOU 767 CB HIS A 135 10789 14487 12906 822 -1062 -1772 C ATOM 768 CG HIS A 135 -10.388 39.824 -9.079 1.00 96.66 C ANISOU 768 CG HIS A 135 10223 14109 12396 879 -1089 -1695 C ATOM 769 ND1 HIS A 135 -11.198 39.395 -8.048 1.00 95.20 N ANISOU 769 ND1 HIS A 135 10068 13920 12183 954 -1041 -1735 N ATOM 770 CD2 HIS A 135 -11.097 40.761 -9.749 1.00 94.92 C ANISOU 770 CD2 HIS A 135 9883 14013 12169 872 -1163 -1576 C ATOM 771 CE1 HIS A 135 -12.345 40.047 -8.094 1.00 94.33 C ANISOU 771 CE1 HIS A 135 9858 13938 12046 1001 -1077 -1648 C ATOM 772 NE2 HIS A 135 -12.311 40.882 -9.116 1.00 95.36 N ANISOU 772 NE2 HIS A 135 9901 14138 12194 955 -1152 -1553 N ATOM 773 N SER A 136 -6.015 38.542 -8.675 1.00125.28 N ANISOU 773 N SER A 136 14148 17285 16167 871 -1035 -1937 N ATOM 774 CA SER A 136 -4.722 38.058 -9.148 1.00123.80 C ANISOU 774 CA SER A 136 14000 17059 15981 812 -1010 -1995 C ATOM 775 C SER A 136 -4.767 37.773 -10.645 1.00114.17 C ANISOU 775 C SER A 136 12675 16047 14657 646 -990 -1980 C ATOM 776 O SER A 136 -5.591 36.986 -11.106 1.00109.98 O ANISOU 776 O SER A 136 12116 15640 14032 540 -927 -2024 O ATOM 777 CB SER A 136 -4.289 36.809 -8.375 1.00129.16 C ANISOU 777 CB SER A 136 14803 17609 16662 819 -922 -2142 C ATOM 778 OG SER A 136 -4.047 37.110 -7.011 1.00130.09 O ANISOU 778 OG SER A 136 15017 17532 16879 966 -943 -2153 O ATOM 779 N GLU A 137 -3.883 38.423 -11.397 1.00108.26 N ANISOU 779 N GLU A 137 11869 15344 13921 618 -1052 -1910 N ATOM 780 CA GLU A 137 -3.842 38.278 -12.852 1.00112.00 C ANISOU 780 CA GLU A 137 12228 16035 14293 463 -1042 -1885 C ATOM 781 C GLU A 137 -4.045 36.832 -13.295 1.00106.31 C ANISOU 781 C GLU A 137 11536 15395 13463 356 -928 -2029 C ATOM 782 O GLU A 137 -3.721 35.897 -12.560 1.00105.46 O ANISOU 782 O GLU A 137 11547 15154 13370 398 -865 -2158 O ATOM 783 CB GLU A 137 -2.532 38.834 -13.420 1.00118.33 C ANISOU 783 CB GLU A 137 12986 16861 15112 451 -1104 -1826 C ATOM 784 CG GLU A 137 -2.590 40.308 -13.819 1.00124.46 C ANISOU 784 CG GLU A 137 13659 17691 15939 454 -1247 -1638 C ATOM 785 CD GLU A 137 -2.914 41.234 -12.658 1.00128.80 C ANISOU 785 CD GLU A 137 14275 18049 16614 612 -1337 -1570 C ATOM 786 OE1 GLU A 137 -4.015 41.115 -12.079 1.00129.90 O ANISOU 786 OE1 GLU A 137 14440 18156 16759 665 -1307 -1598 O ATOM 787 OE2 GLU A 137 -2.068 42.095 -12.334 1.00129.81 O ANISOU 787 OE2 GLU A 137 14428 18066 16829 685 -1446 -1485 O ATOM 788 N GLU A 138 -4.584 36.666 -14.501 1.00 70.98 N ANISOU 788 N GLU A 138 6956 11133 8880 213 -913 -2004 N ATOM 789 CA GLU A 138 -4.972 35.358 -15.021 1.00 64.28 C ANISOU 789 CA GLU A 138 6133 10373 7917 100 -825 -2129 C ATOM 790 C GLU A 138 -6.297 34.904 -14.411 1.00 56.13 C ANISOU 790 C GLU A 138 5141 9316 6869 91 -796 -2139 C ATOM 791 O GLU A 138 -6.741 33.780 -14.638 1.00 56.48 O ANISOU 791 O GLU A 138 5229 9402 6829 1 -739 -2234 O ATOM 792 CB GLU A 138 -3.880 34.315 -14.768 1.00 70.72 C ANISOU 792 CB GLU A 138 7060 11082 8728 130 -768 -2295 C ATOM 793 CG GLU A 138 -2.650 34.469 -15.647 1.00 77.60 C ANISOU 793 CG GLU A 138 7871 12051 9562 105 -777 -2306 C ATOM 794 CD GLU A 138 -2.872 33.942 -17.052 1.00 86.03 C ANISOU 794 CD GLU A 138 8851 13354 10483 -45 -744 -2346 C ATOM 795 OE1 GLU A 138 -3.418 32.827 -17.192 1.00 89.83 O ANISOU 795 OE1 GLU A 138 9395 13847 10890 -107 -688 -2466 O ATOM 796 OE2 GLU A 138 -2.493 34.639 -18.016 1.00 88.58 O ANISOU 796 OE2 GLU A 138 9043 13853 10760 -105 -784 -2254 O ATOM 797 N SER A 139 -6.922 35.791 -13.642 1.00 56.71 N ANISOU 797 N SER A 139 5197 9329 7020 187 -844 -2036 N ATOM 798 CA SER A 139 -8.180 35.486 -12.964 1.00 58.73 C ANISOU 798 CA SER A 139 5473 9583 7259 198 -821 -2026 C ATOM 799 C SER A 139 -9.329 35.290 -13.948 1.00 59.91 C ANISOU 799 C SER A 139 5523 9946 7295 46 -807 -1966 C ATOM 800 O SER A 139 -9.366 35.916 -15.007 1.00 64.48 O ANISOU 800 O SER A 139 5988 10668 7841 -31 -843 -1880 O ATOM 801 CB SER A 139 -8.531 36.597 -11.972 1.00 64.76 C ANISOU 801 CB SER A 139 6227 10254 8123 356 -883 -1932 C ATOM 802 OG SER A 139 -9.732 36.306 -11.278 1.00 70.26 O ANISOU 802 OG SER A 139 6930 10975 8791 377 -858 -1922 O ATOM 803 N LEU A 140 -10.271 34.423 -13.588 1.00 43.04 N ANISOU 803 N LEU A 140 3425 7833 5095 -5 -764 -2001 N ATOM 804 CA LEU A 140 -11.428 34.167 -14.437 1.00 43.58 C ANISOU 804 CA LEU A 140 3408 8099 5052 -155 -752 -1936 C ATOM 805 C LEU A 140 -12.526 35.203 -14.215 1.00 46.60 C ANISOU 805 C LEU A 140 3684 8567 5455 -102 -794 -1784 C ATOM 806 O LEU A 140 -13.618 35.089 -14.771 1.00 47.48 O ANISOU 806 O LEU A 140 3717 8843 5480 -212 -786 -1707 O ATOM 807 CB LEU A 140 -11.978 32.756 -14.212 1.00 42.20 C ANISOU 807 CB LEU A 140 3320 7923 4790 -251 -704 -2023 C ATOM 808 CG LEU A 140 -11.006 31.591 -14.416 1.00 41.91 C ANISOU 808 CG LEU A 140 3402 7794 4728 -301 -674 -2191 C ATOM 809 CD1 LEU A 140 -11.771 30.293 -14.627 1.00 45.82 C ANISOU 809 CD1 LEU A 140 3956 8342 5113 -447 -658 -2244 C ATOM 810 CD2 LEU A 140 -10.084 31.864 -15.589 1.00 42.25 C ANISOU 810 CD2 LEU A 140 3393 7912 4748 -346 -675 -2218 C ATOM 811 N HIS A 141 -12.237 36.209 -13.396 1.00 77.31 N ANISOU 811 N HIS A 141 7574 12344 9457 71 -843 -1741 N ATOM 812 CA HIS A 141 -13.157 37.325 -13.217 1.00 79.56 C ANISOU 812 CA HIS A 141 7758 12699 9773 150 -901 -1607 C ATOM 813 C HIS A 141 -13.032 38.285 -14.394 1.00 79.31 C ANISOU 813 C HIS A 141 7606 12777 9750 85 -968 -1499 C ATOM 814 O HIS A 141 -13.981 38.990 -14.737 1.00 79.18 O ANISOU 814 O HIS A 141 7479 12884 9721 73 -1011 -1380 O ATOM 815 CB HIS A 141 -12.875 38.064 -11.907 1.00 78.27 C ANISOU 815 CB HIS A 141 7650 12365 9725 369 -945 -1611 C ATOM 816 CG HIS A 141 -13.365 37.348 -10.686 1.00 82.93 C ANISOU 816 CG HIS A 141 8316 12897 10298 439 -892 -1676 C ATOM 817 ND1 HIS A 141 -14.685 37.379 -10.284 1.00 83.24 N ANISOU 817 ND1 HIS A 141 8290 13059 10278 461 -882 -1611 N ATOM 818 CD2 HIS A 141 -12.713 36.594 -9.771 1.00 86.42 C ANISOU 818 CD2 HIS A 141 8884 13182 10769 488 -852 -1790 C ATOM 819 CE1 HIS A 141 -14.823 36.669 -9.180 1.00 84.74 C ANISOU 819 CE1 HIS A 141 8559 13183 10456 514 -840 -1679 C ATOM 820 NE2 HIS A 141 -13.641 36.181 -8.845 1.00 86.39 N ANISOU 820 NE2 HIS A 141 8887 13213 10723 528 -823 -1789 N ATOM 821 N TYR A 142 -11.854 38.303 -15.010 1.00 69.44 N ANISOU 821 N TYR A 142 6371 11494 8519 39 -981 -1537 N ATOM 822 CA TYR A 142 -11.594 39.174 -16.150 1.00 72.72 C ANISOU 822 CA TYR A 142 6668 12025 8939 -41 -1054 -1430 C ATOM 823 C TYR A 142 -12.341 38.704 -17.394 1.00 72.65 C ANISOU 823 C TYR A 142 6563 12237 8803 -245 -1016 -1391 C ATOM 824 O TYR A 142 -12.447 39.438 -18.376 1.00 72.36 O ANISOU 824 O TYR A 142 6403 12333 8757 -333 -1078 -1279 O ATOM 825 CB TYR A 142 -10.096 39.232 -16.456 1.00 76.20 C ANISOU 825 CB TYR A 142 7142 12396 9413 -41 -1075 -1478 C ATOM 826 CG TYR A 142 -9.253 39.828 -15.352 1.00 78.72 C ANISOU 826 CG TYR A 142 7550 12500 9861 145 -1130 -1492 C ATOM 827 CD1 TYR A 142 -9.287 41.189 -15.083 1.00 81.05 C ANISOU 827 CD1 TYR A 142 7800 12737 10258 252 -1256 -1369 C ATOM 828 CD2 TYR A 142 -8.409 39.031 -14.592 1.00 80.31 C ANISOU 828 CD2 TYR A 142 7884 12546 10083 211 -1067 -1628 C ATOM 829 CE1 TYR A 142 -8.511 41.738 -14.078 1.00 83.84 C ANISOU 829 CE1 TYR A 142 8246 12885 10726 418 -1317 -1379 C ATOM 830 CE2 TYR A 142 -7.629 39.570 -13.586 1.00 83.02 C ANISOU 830 CE2 TYR A 142 8311 12691 10543 372 -1118 -1634 C ATOM 831 CZ TYR A 142 -7.683 40.924 -13.332 1.00 84.96 C ANISOU 831 CZ TYR A 142 8515 12882 10882 474 -1242 -1510 C ATOM 832 OH TYR A 142 -6.907 41.464 -12.330 1.00 83.88 O ANISOU 832 OH TYR A 142 8472 12540 10857 632 -1303 -1514 O ATOM 833 N GLU A 143 -12.856 37.479 -17.348 1.00 67.49 N ANISOU 833 N GLU A 143 5968 11621 8054 -327 -926 -1478 N ATOM 834 CA GLU A 143 -13.513 36.888 -18.507 1.00 63.67 C ANISOU 834 CA GLU A 143 5416 11335 7442 -528 -889 -1455 C ATOM 835 C GLU A 143 -15.024 36.761 -18.325 1.00 59.42 C ANISOU 835 C GLU A 143 4833 10896 6849 -569 -874 -1372 C ATOM 836 O GLU A 143 -15.732 36.328 -19.233 1.00 64.16 O ANISOU 836 O GLU A 143 5374 11662 7342 -740 -850 -1330 O ATOM 837 CB GLU A 143 -12.909 35.518 -18.817 1.00 67.18 C ANISOU 837 CB GLU A 143 5963 11763 7800 -620 -816 -1615 C ATOM 838 CG GLU A 143 -11.411 35.543 -19.078 1.00 70.15 C ANISOU 838 CG GLU A 143 6371 12073 8208 -584 -821 -1703 C ATOM 839 CD GLU A 143 -10.922 34.286 -19.771 1.00 75.25 C ANISOU 839 CD GLU A 143 7080 12767 8744 -697 -760 -1851 C ATOM 840 OE1 GLU A 143 -11.688 33.708 -20.572 1.00 81.36 O ANISOU 840 OE1 GLU A 143 7823 13687 9404 -851 -736 -1845 O ATOM 841 OE2 GLU A 143 -9.770 33.878 -19.520 1.00 70.57 O ANISOU 841 OE2 GLU A 143 6570 12066 8177 -629 -741 -1974 O ATOM 842 N GLY A 144 -15.516 37.140 -17.153 1.00 47.99 N ANISOU 842 N GLY A 144 3408 9359 5467 -412 -889 -1344 N ATOM 843 CA GLY A 144 -16.930 37.016 -16.854 1.00 47.37 C ANISOU 843 CA GLY A 144 3281 9389 5330 -431 -872 -1263 C ATOM 844 C GLY A 144 -17.305 35.573 -16.586 1.00 51.42 C ANISOU 844 C GLY A 144 3886 9910 5740 -528 -801 -1347 C ATOM 845 O GLY A 144 -18.468 35.187 -16.704 1.00 48.69 O ANISOU 845 O GLY A 144 3495 9702 5304 -621 -783 -1273 O ATOM 846 N ARG A 145 -16.309 34.771 -16.223 1.00 70.85 N ANISOU 846 N ARG A 145 6479 12223 8218 -509 -770 -1496 N ATOM 847 CA ARG A 145 -16.526 33.364 -15.914 1.00 74.89 C ANISOU 847 CA ARG A 145 7099 12708 8648 -597 -726 -1587 C ATOM 848 C ARG A 145 -16.515 33.109 -14.411 1.00 78.84 C ANISOU 848 C ARG A 145 7687 13064 9204 -453 -718 -1637 C ATOM 849 O ARG A 145 -16.788 31.996 -13.963 1.00 79.60 O ANISOU 849 O ARG A 145 7869 13132 9242 -517 -699 -1694 O ATOM 850 CB ARG A 145 -15.462 32.497 -16.586 1.00 73.21 C ANISOU 850 CB ARG A 145 6978 12433 8404 -686 -704 -1732 C ATOM 851 CG ARG A 145 -15.631 32.346 -18.084 1.00 74.59 C ANISOU 851 CG ARG A 145 7082 12780 8479 -868 -702 -1704 C ATOM 852 CD ARG A 145 -14.836 31.159 -18.595 1.00 72.10 C ANISOU 852 CD ARG A 145 6879 12416 8100 -956 -678 -1869 C ATOM 853 NE ARG A 145 -13.397 31.375 -18.491 1.00 70.02 N ANISOU 853 NE ARG A 145 6660 12028 7916 -845 -674 -1977 N ATOM 854 CZ ARG A 145 -12.495 30.401 -18.523 1.00 71.09 C ANISOU 854 CZ ARG A 145 6914 12065 8033 -847 -655 -2146 C ATOM 855 NH1 ARG A 145 -12.884 29.140 -18.645 1.00 76.52 N ANISOU 855 NH1 ARG A 145 7697 12745 8630 -954 -650 -2232 N ATOM 856 NH2 ARG A 145 -11.204 30.684 -18.427 1.00 67.49 N ANISOU 856 NH2 ARG A 145 6481 11516 7647 -741 -651 -2225 N ATOM 857 N ALA A 146 -16.195 34.138 -13.633 1.00 79.29 N ANISOU 857 N ALA A 146 7724 13029 9372 -263 -744 -1613 N ATOM 858 CA ALA A 146 -16.108 33.987 -12.186 1.00 79.97 C ANISOU 858 CA ALA A 146 7890 12980 9515 -116 -738 -1662 C ATOM 859 C ALA A 146 -17.078 34.909 -11.453 1.00 78.67 C ANISOU 859 C ALA A 146 7632 12890 9369 21 -762 -1551 C ATOM 860 O ALA A 146 -17.394 36.000 -11.928 1.00 83.84 O ANISOU 860 O ALA A 146 8179 13624 10051 67 -803 -1453 O ATOM 861 CB ALA A 146 -14.681 34.229 -11.712 1.00 79.04 C ANISOU 861 CB ALA A 146 7867 12650 9515 10 -747 -1767 C ATOM 862 N VAL A 147 -17.549 34.456 -10.295 1.00 53.10 N ANISOU 862 N VAL A 147 4431 9633 6110 86 -744 -1567 N ATOM 863 CA VAL A 147 -18.439 35.251 -9.456 1.00 46.27 C ANISOU 863 CA VAL A 147 3482 8848 5250 241 -763 -1482 C ATOM 864 C VAL A 147 -18.156 35.035 -7.975 1.00 53.81 C ANISOU 864 C VAL A 147 4520 9677 6250 388 -753 -1555 C ATOM 865 O VAL A 147 -18.049 33.902 -7.506 1.00 54.50 O ANISOU 865 O VAL A 147 4691 9721 6296 304 -724 -1619 O ATOM 866 CB VAL A 147 -19.923 34.929 -9.717 1.00 45.14 C ANISOU 866 CB VAL A 147 3230 8949 4973 131 -748 -1363 C ATOM 867 CG1 VAL A 147 -20.397 35.592 -10.998 1.00 45.98 C ANISOU 867 CG1 VAL A 147 3218 9198 5054 46 -770 -1257 C ATOM 868 CG2 VAL A 147 -20.143 33.424 -9.758 1.00 44.54 C ANISOU 868 CG2 VAL A 147 3226 8904 4793 -62 -716 -1397 C ATOM 869 N ASP A 148 -18.038 36.136 -7.244 1.00 65.94 N ANISOU 869 N ASP A 148 6033 11150 7871 604 -788 -1546 N ATOM 870 CA ASP A 148 -17.886 36.081 -5.801 1.00 61.52 C ANISOU 870 CA ASP A 148 5533 10494 7346 760 -782 -1604 C ATOM 871 C ASP A 148 -19.250 36.303 -5.166 1.00 58.22 C ANISOU 871 C ASP A 148 5001 10282 6837 837 -778 -1517 C ATOM 872 O ASP A 148 -19.847 37.370 -5.308 1.00 53.68 O ANISOU 872 O ASP A 148 4322 9804 6270 958 -816 -1443 O ATOM 873 CB ASP A 148 -16.877 37.129 -5.338 1.00 61.43 C ANISOU 873 CB ASP A 148 5581 10282 7479 958 -832 -1655 C ATOM 874 CG ASP A 148 -15.527 36.959 -6.006 1.00 61.42 C ANISOU 874 CG ASP A 148 5674 10107 7557 882 -838 -1724 C ATOM 875 OD1 ASP A 148 -15.123 35.797 -6.221 1.00 57.39 O ANISOU 875 OD1 ASP A 148 5237 9559 7010 733 -790 -1792 O ATOM 876 OD2 ASP A 148 -14.875 37.977 -6.323 1.00 64.82 O ANISOU 876 OD2 ASP A 148 6103 10445 8082 972 -898 -1707 O ATOM 877 N ILE A 149 -19.744 35.281 -4.477 1.00 56.16 N ANISOU 877 N ILE A 149 4755 10099 6486 763 -741 -1523 N ATOM 878 CA ILE A 149 -21.110 35.298 -3.976 1.00 57.48 C ANISOU 878 CA ILE A 149 4796 10512 6533 795 -732 -1423 C ATOM 879 C ILE A 149 -21.201 35.097 -2.467 1.00 54.96 C ANISOU 879 C ILE A 149 4498 10187 6198 926 -721 -1464 C ATOM 880 O ILE A 149 -20.275 34.584 -1.836 1.00 55.08 O ANISOU 880 O ILE A 149 4638 10011 6279 928 -714 -1565 O ATOM 881 CB ILE A 149 -21.973 34.231 -4.683 1.00 56.50 C ANISOU 881 CB ILE A 149 4624 10576 6266 542 -710 -1338 C ATOM 882 CG1 ILE A 149 -21.354 32.843 -4.511 1.00 53.31 C ANISOU 882 CG1 ILE A 149 4357 10048 5851 372 -698 -1419 C ATOM 883 CG2 ILE A 149 -22.122 34.559 -6.159 1.00 52.53 C ANISOU 883 CG2 ILE A 149 4069 10132 5758 425 -719 -1277 C ATOM 884 CD1 ILE A 149 -22.130 31.743 -5.196 1.00 56.36 C ANISOU 884 CD1 ILE A 149 4723 10590 6103 117 -700 -1341 C ATOM 885 N THR A 150 -22.325 35.531 -1.903 1.00 52.59 N ANISOU 885 N THR A 150 4065 10109 5807 1039 -721 -1383 N ATOM 886 CA THR A 150 -22.659 35.302 -0.503 1.00 53.96 C ANISOU 886 CA THR A 150 4220 10358 5926 1148 -708 -1399 C ATOM 887 C THR A 150 -24.172 35.193 -0.405 1.00 52.03 C ANISOU 887 C THR A 150 3802 10455 5510 1123 -696 -1263 C ATOM 888 O THR A 150 -24.872 35.305 -1.410 1.00 50.53 O ANISOU 888 O THR A 150 3524 10414 5262 1022 -698 -1163 O ATOM 889 CB THR A 150 -22.211 36.464 0.402 1.00 47.87 C ANISOU 889 CB THR A 150 3466 9469 5253 1446 -734 -1475 C ATOM 890 OG1 THR A 150 -23.022 37.617 0.142 1.00 47.00 O ANISOU 890 OG1 THR A 150 3225 9513 5121 1611 -763 -1409 O ATOM 891 CG2 THR A 150 -20.746 36.803 0.169 1.00 46.40 C ANISOU 891 CG2 THR A 150 3435 8957 5239 1483 -759 -1583 C ATOM 892 N THR A 151 -24.681 34.978 0.803 1.00 51.98 N ANISOU 892 N THR A 151 3741 10591 5419 1209 -684 -1251 N ATOM 893 CA THR A 151 -26.121 35.003 1.016 1.00 56.56 C ANISOU 893 CA THR A 151 4136 11526 5827 1222 -674 -1117 C ATOM 894 C THR A 151 -26.583 36.449 1.165 1.00 59.74 C ANISOU 894 C THR A 151 4430 12020 6249 1509 -690 -1114 C ATOM 895 O THR A 151 -25.762 37.367 1.214 1.00 57.06 O ANISOU 895 O THR A 151 4170 11455 6057 1690 -719 -1216 O ATOM 896 CB THR A 151 -26.542 34.174 2.244 1.00 60.57 C ANISOU 896 CB THR A 151 4607 12193 6215 1190 -662 -1091 C ATOM 897 OG1 THR A 151 -25.767 34.567 3.383 1.00 67.46 O ANISOU 897 OG1 THR A 151 5555 12902 7175 1393 -663 -1218 O ATOM 898 CG2 THR A 151 -26.324 32.693 1.982 1.00 58.44 C ANISOU 898 CG2 THR A 151 4427 11871 5906 879 -672 -1063 C ATOM 899 N SER A 152 -27.895 36.651 1.219 1.00 67.79 N ANISOU 899 N SER A 152 5267 13369 7120 1551 -681 -992 N ATOM 900 CA SER A 152 -28.450 37.995 1.327 1.00 68.62 C ANISOU 900 CA SER A 152 5257 13583 7232 1830 -705 -987 C ATOM 901 C SER A 152 -28.263 38.557 2.731 1.00 73.51 C ANISOU 901 C SER A 152 5878 14190 7861 2117 -712 -1091 C ATOM 902 O SER A 152 -28.006 39.748 2.904 1.00 79.92 O ANISOU 902 O SER A 152 6703 14894 8771 2379 -758 -1169 O ATOM 903 CB SER A 152 -29.932 37.997 0.948 1.00 66.88 C ANISOU 903 CB SER A 152 4833 13738 6841 1786 -690 -821 C ATOM 904 OG SER A 152 -30.663 37.083 1.747 1.00 67.52 O ANISOU 904 OG SER A 152 4825 14084 6744 1699 -657 -742 O ATOM 905 N ASP A 153 -28.389 37.691 3.730 1.00 72.68 N ANISOU 905 N ASP A 153 5764 14197 7656 2062 -679 -1091 N ATOM 906 CA ASP A 153 -28.303 38.110 5.125 1.00 71.38 C ANISOU 906 CA ASP A 153 5585 14065 7472 2316 -680 -1181 C ATOM 907 C ASP A 153 -26.860 38.191 5.614 1.00 72.47 C ANISOU 907 C ASP A 153 5927 13826 7784 2375 -698 -1338 C ATOM 908 O ASP A 153 -26.605 38.539 6.769 1.00 79.66 O ANISOU 908 O ASP A 153 6856 14710 8700 2579 -703 -1429 O ATOM 909 CB ASP A 153 -29.112 37.163 6.016 1.00 68.88 C ANISOU 909 CB ASP A 153 5149 14065 6958 2223 -643 -1096 C ATOM 910 CG ASP A 153 -28.714 35.709 5.835 1.00 60.27 C ANISOU 910 CG ASP A 153 4153 12893 5854 1882 -633 -1053 C ATOM 911 OD1 ASP A 153 -27.596 35.446 5.339 1.00 52.29 O ANISOU 911 OD1 ASP A 153 3324 11545 5001 1771 -644 -1136 O ATOM 912 OD2 ASP A 153 -29.521 34.827 6.194 1.00 60.12 O ANISOU 912 OD2 ASP A 153 4025 13153 5664 1726 -622 -932 O ATOM 913 N ARG A 154 -25.925 37.863 4.729 1.00 68.80 N ANISOU 913 N ARG A 154 5608 13082 7453 2196 -707 -1367 N ATOM 914 CA ARG A 154 -24.501 37.889 5.055 1.00 69.16 C ANISOU 914 CA ARG A 154 5847 12766 7665 2226 -723 -1501 C ATOM 915 C ARG A 154 -24.120 36.897 6.150 1.00 69.33 C ANISOU 915 C ARG A 154 5930 12760 7653 2145 -694 -1543 C ATOM 916 O ARG A 154 -22.944 36.768 6.483 1.00 70.34 O ANISOU 916 O ARG A 154 6218 12598 7911 2145 -703 -1647 O ATOM 917 CB ARG A 154 -24.051 39.294 5.465 1.00 75.08 C ANISOU 917 CB ARG A 154 6638 13358 8530 2544 -778 -1599 C ATOM 918 CG ARG A 154 -24.119 40.338 4.365 1.00 83.13 C ANISOU 918 CG ARG A 154 7636 14317 9631 2618 -835 -1571 C ATOM 919 CD ARG A 154 -23.163 41.483 4.666 1.00 90.74 C ANISOU 919 CD ARG A 154 8722 14994 10762 2854 -914 -1681 C ATOM 920 NE ARG A 154 -23.417 42.663 3.843 1.00 97.90 N ANISOU 920 NE ARG A 154 9582 15882 11733 2979 -995 -1649 N ATOM 921 CZ ARG A 154 -22.589 43.699 3.750 1.00 97.60 C ANISOU 921 CZ ARG A 154 9649 15581 11852 3135 -1093 -1712 C ATOM 922 NH1 ARG A 154 -22.901 44.733 2.980 1.00 99.72 N ANISOU 922 NH1 ARG A 154 9865 15849 12174 3230 -1182 -1667 N ATOM 923 NH2 ARG A 154 -21.445 43.700 4.422 1.00 91.79 N ANISOU 923 NH2 ARG A 154 9074 14582 11222 3188 -1112 -1810 N ATOM 924 N ASP A 155 -25.106 36.205 6.715 1.00 69.96 N ANISOU 924 N ASP A 155 5878 13147 7555 2069 -667 -1455 N ATOM 925 CA ASP A 155 -24.827 35.225 7.763 1.00 70.79 C ANISOU 925 CA ASP A 155 6026 13254 7618 1970 -653 -1476 C ATOM 926 C ASP A 155 -23.855 34.157 7.252 1.00 64.62 C ANISOU 926 C ASP A 155 5412 12206 6936 1701 -658 -1506 C ATOM 927 O ASP A 155 -24.228 33.272 6.478 1.00 65.44 O ANISOU 927 O ASP A 155 5500 12388 6977 1449 -661 -1416 O ATOM 928 CB ASP A 155 -26.122 34.602 8.297 1.00 71.19 C ANISOU 928 CB ASP A 155 5890 13713 7446 1892 -638 -1344 C ATOM 929 CG ASP A 155 -26.935 35.576 9.147 1.00 71.75 C ANISOU 929 CG ASP A 155 5801 14050 7411 2193 -629 -1346 C ATOM 930 OD1 ASP A 155 -27.946 35.151 9.750 1.00 68.81 O ANISOU 930 OD1 ASP A 155 5262 14035 6846 2164 -615 -1244 O ATOM 931 OD2 ASP A 155 -26.561 36.768 9.214 1.00 70.18 O ANISOU 931 OD2 ASP A 155 5642 13708 7315 2463 -645 -1450 O ATOM 932 N ARG A 156 -22.603 34.257 7.694 1.00 49.67 N ANISOU 932 N ARG A 156 3680 9996 5196 1764 -666 -1633 N ATOM 933 CA ARG A 156 -21.517 33.428 7.179 1.00 45.57 C ANISOU 933 CA ARG A 156 3330 9188 4796 1560 -672 -1687 C ATOM 934 C ARG A 156 -21.680 31.946 7.493 1.00 47.26 C ANISOU 934 C ARG A 156 3558 9469 4929 1297 -680 -1637 C ATOM 935 O ARG A 156 -20.972 31.109 6.936 1.00 45.29 O ANISOU 935 O ARG A 156 3434 9021 4752 1102 -695 -1670 O ATOM 936 CB ARG A 156 -20.177 33.906 7.739 1.00 45.04 C ANISOU 936 CB ARG A 156 3420 8792 4900 1705 -680 -1825 C ATOM 937 CG ARG A 156 -19.857 35.369 7.487 1.00 46.76 C ANISOU 937 CG ARG A 156 3653 8897 5217 1959 -700 -1877 C ATOM 938 CD ARG A 156 -18.566 35.749 8.192 1.00 48.09 C ANISOU 938 CD ARG A 156 3978 8755 5540 2087 -717 -1995 C ATOM 939 NE ARG A 156 -18.048 37.043 7.758 1.00 47.20 N ANISOU 939 NE ARG A 156 3914 8475 5546 2279 -761 -2037 N ATOM 940 CZ ARG A 156 -16.849 37.513 8.087 1.00 49.71 C ANISOU 940 CZ ARG A 156 4377 8499 6013 2380 -791 -2123 C ATOM 941 NH1 ARG A 156 -16.041 36.794 8.855 1.00 46.61 N ANISOU 941 NH1 ARG A 156 4092 7946 5670 2312 -772 -2183 N ATOM 942 NH2 ARG A 156 -16.457 38.700 7.646 1.00 53.63 N ANISOU 942 NH2 ARG A 156 4910 8861 6607 2540 -852 -2139 N ATOM 943 N SER A 157 -22.601 31.619 8.392 1.00 64.75 N ANISOU 943 N SER A 157 5643 11967 6991 1293 -681 -1558 N ATOM 944 CA SER A 157 -22.790 30.231 8.799 1.00 67.08 C ANISOU 944 CA SER A 157 5944 12336 7206 1039 -713 -1494 C ATOM 945 C SER A 157 -23.263 29.347 7.644 1.00 71.83 C ANISOU 945 C SER A 157 6543 13005 7745 766 -742 -1396 C ATOM 946 O SER A 157 -23.164 28.122 7.716 1.00 77.82 O ANISOU 946 O SER A 157 7361 13729 8479 526 -791 -1363 O ATOM 947 CB SER A 157 -23.744 30.131 9.996 1.00 65.51 C ANISOU 947 CB SER A 157 5582 12471 6838 1090 -715 -1409 C ATOM 948 OG SER A 157 -24.891 30.946 9.820 1.00 66.92 O ANISOU 948 OG SER A 157 5577 12965 6885 1237 -690 -1325 O ATOM 949 N LYS A 158 -23.765 29.966 6.578 1.00 50.31 N ANISOU 949 N LYS A 158 3754 10366 4997 800 -722 -1349 N ATOM 950 CA LYS A 158 -24.251 29.208 5.428 1.00 53.62 C ANISOU 950 CA LYS A 158 4167 10855 5349 549 -749 -1254 C ATOM 951 C LYS A 158 -23.339 29.304 4.201 1.00 53.03 C ANISOU 951 C LYS A 158 4234 10498 5418 498 -743 -1344 C ATOM 952 O LYS A 158 -23.572 28.637 3.192 1.00 48.94 O ANISOU 952 O LYS A 158 3739 9995 4860 288 -767 -1291 O ATOM 953 CB LYS A 158 -25.672 29.631 5.055 1.00 57.29 C ANISOU 953 CB LYS A 158 4434 11685 5649 566 -737 -1100 C ATOM 954 CG LYS A 158 -26.711 29.298 6.104 1.00 58.24 C ANISOU 954 CG LYS A 158 4393 12146 5588 556 -751 -978 C ATOM 955 CD LYS A 158 -27.225 30.551 6.788 1.00 55.50 C ANISOU 955 CD LYS A 158 3900 11992 5194 869 -704 -986 C ATOM 956 CE LYS A 158 -28.116 31.353 5.851 1.00 52.93 C ANISOU 956 CE LYS A 158 3445 11859 4807 943 -682 -901 C ATOM 957 NZ LYS A 158 -28.884 32.395 6.582 1.00 54.85 N ANISOU 957 NZ LYS A 158 3514 12366 4959 1229 -653 -882 N ATOM 958 N TYR A 159 -22.305 30.133 4.293 1.00 61.24 N ANISOU 958 N TYR A 159 5365 11291 6614 687 -716 -1476 N ATOM 959 CA TYR A 159 -21.365 30.310 3.192 1.00 57.84 C ANISOU 959 CA TYR A 159 5054 10609 6315 656 -711 -1559 C ATOM 960 C TYR A 159 -20.819 28.978 2.685 1.00 57.68 C ANISOU 960 C TYR A 159 5165 10436 6315 401 -744 -1594 C ATOM 961 O TYR A 159 -20.415 28.863 1.528 1.00 66.79 O ANISOU 961 O TYR A 159 6381 11483 7513 309 -745 -1626 O ATOM 962 CB TYR A 159 -20.221 31.230 3.620 1.00 59.44 C ANISOU 962 CB TYR A 159 5349 10556 6680 879 -695 -1688 C ATOM 963 CG TYR A 159 -20.587 32.695 3.606 1.00 62.28 C ANISOU 963 CG TYR A 159 5611 10999 7053 1127 -684 -1671 C ATOM 964 CD1 TYR A 159 -21.914 33.100 3.686 1.00 61.84 C ANISOU 964 CD1 TYR A 159 5382 11256 6859 1187 -679 -1559 C ATOM 965 CD2 TYR A 159 -19.608 33.675 3.531 1.00 65.91 C ANISOU 965 CD2 TYR A 159 6153 11228 7663 1302 -692 -1761 C ATOM 966 CE1 TYR A 159 -22.255 34.439 3.677 1.00 62.40 C ANISOU 966 CE1 TYR A 159 5368 11395 6947 1426 -683 -1552 C ATOM 967 CE2 TYR A 159 -19.939 35.017 3.525 1.00 67.73 C ANISOU 967 CE2 TYR A 159 6306 11516 7912 1529 -707 -1746 C ATOM 968 CZ TYR A 159 -21.263 35.393 3.597 1.00 63.47 C ANISOU 968 CZ TYR A 159 5598 11277 7240 1596 -703 -1649 C ATOM 969 OH TYR A 159 -21.594 36.728 3.590 1.00 58.77 O ANISOU 969 OH TYR A 159 4931 10730 6670 1833 -731 -1643 O ATOM 970 N GLY A 160 -20.811 27.974 3.554 1.00 46.59 N ANISOU 970 N GLY A 160 3799 9027 4875 288 -780 -1590 N ATOM 971 CA GLY A 160 -20.349 26.651 3.182 1.00 47.17 C ANISOU 971 CA GLY A 160 4002 8954 4965 51 -834 -1625 C ATOM 972 C GLY A 160 -21.422 25.879 2.442 1.00 50.50 C ANISOU 972 C GLY A 160 4361 9589 5238 -177 -881 -1494 C ATOM 973 O GLY A 160 -21.144 25.228 1.434 1.00 47.04 O ANISOU 973 O GLY A 160 4014 9047 4814 -338 -912 -1524 O ATOM 974 N MET A 161 -22.651 25.947 2.948 1.00 49.84 N ANISOU 974 N MET A 161 4118 9814 5004 -188 -890 -1346 N ATOM 975 CA MET A 161 -23.781 25.292 2.299 1.00 55.35 C ANISOU 975 CA MET A 161 4738 10748 5545 -403 -939 -1192 C ATOM 976 C MET A 161 -24.033 25.916 0.932 1.00 60.40 C ANISOU 976 C MET A 161 5342 11427 6180 -395 -899 -1171 C ATOM 977 O MET A 161 -24.402 25.230 -0.023 1.00 60.94 O ANISOU 977 O MET A 161 5436 11535 6183 -602 -942 -1113 O ATOM 978 CB MET A 161 -25.034 25.399 3.167 1.00 52.59 C ANISOU 978 CB MET A 161 4202 10752 5029 -385 -947 -1029 C ATOM 979 CG MET A 161 -26.269 24.722 2.585 1.00 52.87 C ANISOU 979 CG MET A 161 4144 11059 4887 -615 -1005 -841 C ATOM 980 SD MET A 161 -26.254 22.926 2.749 1.00 67.95 S ANISOU 980 SD MET A 161 6172 12902 6742 -955 -1150 -787 S ATOM 981 CE MET A 161 -25.320 22.446 1.307 1.00153.68 C ANISOU 981 CE MET A 161 17236 23431 17723 -1076 -1172 -925 C ATOM 982 N LEU A 162 -23.825 27.226 0.844 1.00 71.07 N ANISOU 982 N LEU A 162 6636 12764 7601 -158 -827 -1218 N ATOM 983 CA LEU A 162 -23.965 27.934 -0.420 1.00 67.34 C ANISOU 983 CA LEU A 162 6127 12314 7144 -137 -795 -1201 C ATOM 984 C LEU A 162 -22.981 27.369 -1.436 1.00 65.54 C ANISOU 984 C LEU A 162 6060 11835 7009 -270 -811 -1311 C ATOM 985 O LEU A 162 -23.339 27.118 -2.587 1.00 67.07 O ANISOU 985 O LEU A 162 6246 12090 7148 -418 -823 -1261 O ATOM 986 CB LEU A 162 -23.731 29.435 -0.232 1.00 62.43 C ANISOU 986 CB LEU A 162 5442 11671 6609 148 -740 -1248 C ATOM 987 CG LEU A 162 -24.033 30.312 -1.450 1.00 57.92 C ANISOU 987 CG LEU A 162 4799 11163 6046 180 -718 -1204 C ATOM 988 CD1 LEU A 162 -25.485 30.151 -1.866 1.00 61.83 C ANISOU 988 CD1 LEU A 162 5140 11983 6371 64 -726 -1026 C ATOM 989 CD2 LEU A 162 -23.712 31.770 -1.168 1.00 48.10 C ANISOU 989 CD2 LEU A 162 3512 9863 4903 464 -693 -1255 C ATOM 990 N ALA A 163 -21.743 27.161 -1.001 1.00 46.87 N ANISOU 990 N ALA A 163 3838 9195 4776 -213 -811 -1460 N ATOM 991 CA ALA A 163 -20.715 26.608 -1.873 1.00 46.02 C ANISOU 991 CA ALA A 163 3881 8851 4754 -314 -825 -1580 C ATOM 992 C ALA A 163 -21.114 25.227 -2.392 1.00 47.50 C ANISOU 992 C ALA A 163 4131 9071 4847 -584 -897 -1543 C ATOM 993 O ALA A 163 -20.842 24.892 -3.541 1.00 48.17 O ANISOU 993 O ALA A 163 4279 9092 4933 -696 -909 -1585 O ATOM 994 CB ALA A 163 -19.380 26.546 -1.152 1.00 45.41 C ANISOU 994 CB ALA A 163 3936 8492 4824 -206 -818 -1734 C ATOM 995 N ARG A 164 -21.758 24.428 -1.548 1.00 60.08 N ANISOU 995 N ARG A 164 5706 10769 6352 -691 -957 -1460 N ATOM 996 CA ARG A 164 -22.238 23.117 -1.973 1.00 64.71 C ANISOU 996 CA ARG A 164 6352 11395 6840 -958 -1053 -1402 C ATOM 997 C ARG A 164 -23.345 23.260 -3.008 1.00 71.87 C ANISOU 997 C ARG A 164 7153 12539 7614 -1073 -1054 -1260 C ATOM 998 O ARG A 164 -23.309 22.620 -4.059 1.00 74.62 O ANISOU 998 O ARG A 164 7580 12838 7933 -1239 -1098 -1277 O ATOM 999 CB ARG A 164 -22.744 22.304 -0.781 1.00 62.55 C ANISOU 999 CB ARG A 164 6064 11207 6495 -1055 -1132 -1317 C ATOM 1000 CG ARG A 164 -23.523 21.052 -1.173 1.00 59.11 C ANISOU 1000 CG ARG A 164 5659 10871 5930 -1341 -1254 -1203 C ATOM 1001 CD ARG A 164 -22.669 20.100 -1.987 1.00 59.56 C ANISOU 1001 CD ARG A 164 5913 10660 6055 -1476 -1324 -1342 C ATOM 1002 NE ARG A 164 -21.429 19.758 -1.296 1.00 63.08 N ANISOU 1002 NE ARG A 164 6498 10821 6649 -1401 -1338 -1510 N ATOM 1003 CZ ARG A 164 -20.473 18.991 -1.811 1.00 67.25 C ANISOU 1003 CZ ARG A 164 7204 11086 7262 -1466 -1392 -1665 C ATOM 1004 NH1 ARG A 164 -20.611 18.481 -3.028 1.00 72.26 N ANISOU 1004 NH1 ARG A 164 7903 11707 7844 -1605 -1438 -1683 N ATOM 1005 NH2 ARG A 164 -19.378 18.733 -1.108 1.00 63.27 N ANISOU 1005 NH2 ARG A 164 6811 10337 6892 -1388 -1400 -1806 N ATOM 1006 N LEU A 165 -24.329 24.100 -2.702 1.00 74.19 N ANISOU 1006 N LEU A 165 7268 13095 7826 -979 -1008 -1121 N ATOM 1007 CA LEU A 165 -25.433 24.344 -3.623 1.00 77.20 C ANISOU 1007 CA LEU A 165 7529 13721 8083 -1073 -1003 -970 C ATOM 1008 C LEU A 165 -24.916 24.848 -4.966 1.00 79.84 C ANISOU 1008 C LEU A 165 7903 13947 8485 -1059 -958 -1049 C ATOM 1009 O LEU A 165 -25.554 24.650 -5.999 1.00 84.49 O ANISOU 1009 O LEU A 165 8459 14657 8985 -1212 -976 -961 O ATOM 1010 CB LEU A 165 -26.429 25.343 -3.029 1.00 73.11 C ANISOU 1010 CB LEU A 165 6807 13485 7488 -918 -950 -835 C ATOM 1011 CG LEU A 165 -27.128 24.926 -1.734 1.00 66.48 C ANISOU 1011 CG LEU A 165 5884 12832 6544 -932 -989 -728 C ATOM 1012 CD1 LEU A 165 -28.239 25.907 -1.396 1.00 63.27 C ANISOU 1012 CD1 LEU A 165 5259 12748 6034 -786 -936 -588 C ATOM 1013 CD2 LEU A 165 -27.677 23.514 -1.846 1.00 64.43 C ANISOU 1013 CD2 LEU A 165 5673 12644 6164 -1232 -1103 -618 C ATOM 1014 N ALA A 166 -23.758 25.501 -4.942 1.00 67.63 N ANISOU 1014 N ALA A 166 6422 12184 7091 -882 -904 -1206 N ATOM 1015 CA ALA A 166 -23.122 25.972 -6.164 1.00 60.98 C ANISOU 1015 CA ALA A 166 5616 11236 6317 -868 -868 -1286 C ATOM 1016 C ALA A 166 -22.566 24.796 -6.957 1.00 63.01 C ANISOU 1016 C ALA A 166 6029 11341 6569 -1064 -923 -1379 C ATOM 1017 O ALA A 166 -22.728 24.728 -8.173 1.00 70.64 O ANISOU 1017 O ALA A 166 6994 12355 7490 -1178 -925 -1364 O ATOM 1018 CB ALA A 166 -22.023 26.969 -5.843 1.00 53.63 C ANISOU 1018 CB ALA A 166 4710 10123 5543 -632 -811 -1413 C ATOM 1019 N VAL A 167 -21.912 23.869 -6.263 1.00 53.91 N ANISOU 1019 N VAL A 167 5013 10008 5462 -1101 -974 -1479 N ATOM 1020 CA VAL A 167 -21.395 22.665 -6.902 1.00 57.54 C ANISOU 1020 CA VAL A 167 5634 10312 5916 -1275 -1047 -1580 C ATOM 1021 C VAL A 167 -22.527 21.863 -7.536 1.00 65.98 C ANISOU 1021 C VAL A 167 6686 11556 6829 -1515 -1125 -1444 C ATOM 1022 O VAL A 167 -22.394 21.360 -8.653 1.00 74.46 O ANISOU 1022 O VAL A 167 7835 12590 7868 -1646 -1158 -1491 O ATOM 1023 CB VAL A 167 -20.628 21.773 -5.907 1.00 54.29 C ANISOU 1023 CB VAL A 167 5363 9686 5579 -1277 -1107 -1690 C ATOM 1024 CG1 VAL A 167 -20.439 20.377 -6.478 1.00 54.73 C ANISOU 1024 CG1 VAL A 167 5576 9622 5596 -1484 -1218 -1759 C ATOM 1025 CG2 VAL A 167 -19.286 22.396 -5.559 1.00 52.01 C ANISOU 1025 CG2 VAL A 167 5131 9180 5452 -1070 -1038 -1851 C ATOM 1026 N GLU A 168 -23.643 21.754 -6.824 1.00 69.17 N ANISOU 1026 N GLU A 168 6987 12164 7130 -1574 -1160 -1270 N ATOM 1027 CA GLU A 168 -24.802 21.037 -7.342 1.00 75.01 C ANISOU 1027 CA GLU A 168 7698 13093 7710 -1809 -1243 -1108 C ATOM 1028 C GLU A 168 -25.546 21.867 -8.388 1.00 80.13 C ANISOU 1028 C GLU A 168 8211 13947 8289 -1818 -1178 -997 C ATOM 1029 O GLU A 168 -26.334 21.334 -9.169 1.00 84.05 O ANISOU 1029 O GLU A 168 8701 14569 8664 -2020 -1236 -887 O ATOM 1030 CB GLU A 168 -25.745 20.635 -6.205 1.00 75.26 C ANISOU 1030 CB GLU A 168 7649 13302 7643 -1877 -1307 -942 C ATOM 1031 CG GLU A 168 -25.081 19.819 -5.104 1.00 76.44 C ANISOU 1031 CG GLU A 168 7919 13266 7860 -1885 -1382 -1031 C ATOM 1032 CD GLU A 168 -24.431 18.547 -5.618 1.00 76.76 C ANISOU 1032 CD GLU A 168 8169 13067 7929 -2056 -1501 -1151 C ATOM 1033 OE1 GLU A 168 -24.876 18.028 -6.663 1.00 79.95 O ANISOU 1033 OE1 GLU A 168 8616 13515 8246 -2232 -1562 -1107 O ATOM 1034 OE2 GLU A 168 -23.477 18.064 -4.973 1.00 72.84 O ANISOU 1034 OE2 GLU A 168 7798 12336 7542 -2011 -1537 -1294 O ATOM 1035 N ALA A 169 -25.286 23.172 -8.401 1.00 90.60 N ANISOU 1035 N ALA A 169 9433 15299 9693 -1605 -1068 -1023 N ATOM 1036 CA ALA A 169 -25.905 24.065 -9.375 1.00 87.66 C ANISOU 1036 CA ALA A 169 8928 15103 9276 -1597 -1010 -925 C ATOM 1037 C ALA A 169 -25.258 23.904 -10.746 1.00 88.67 C ANISOU 1037 C ALA A 169 9145 15112 9432 -1683 -1006 -1031 C ATOM 1038 O ALA A 169 -25.863 24.229 -11.766 1.00 93.44 O ANISOU 1038 O ALA A 169 9670 15864 9967 -1771 -990 -938 O ATOM 1039 CB ALA A 169 -25.813 25.509 -8.911 1.00 84.04 C ANISOU 1039 CB ALA A 169 8338 14693 8900 -1338 -918 -920 C ATOM 1040 N GLY A 170 -24.025 23.408 -10.763 1.00 78.22 N ANISOU 1040 N GLY A 170 7981 13535 8205 -1655 -1019 -1226 N ATOM 1041 CA GLY A 170 -23.346 23.125 -12.013 1.00 80.36 C ANISOU 1041 CA GLY A 170 8343 13701 8489 -1734 -1021 -1345 C ATOM 1042 C GLY A 170 -22.003 23.811 -12.173 1.00 75.21 C ANISOU 1042 C GLY A 170 7726 12873 7979 -1552 -952 -1516 C ATOM 1043 O GLY A 170 -21.212 23.433 -13.038 1.00 79.87 O ANISOU 1043 O GLY A 170 8409 13351 8586 -1598 -958 -1649 O ATOM 1044 N PHE A 171 -21.744 24.821 -11.349 1.00 56.26 N ANISOU 1044 N PHE A 171 5248 10455 5673 -1345 -893 -1509 N ATOM 1045 CA PHE A 171 -20.478 25.544 -11.420 1.00 52.37 C ANISOU 1045 CA PHE A 171 4784 9800 5317 -1172 -839 -1647 C ATOM 1046 C PHE A 171 -19.298 24.581 -11.463 1.00 48.48 C ANISOU 1046 C PHE A 171 4467 9076 4877 -1197 -869 -1839 C ATOM 1047 O PHE A 171 -19.165 23.702 -10.609 1.00 48.47 O ANISOU 1047 O PHE A 171 4568 8962 4887 -1223 -920 -1888 O ATOM 1048 CB PHE A 171 -20.332 26.517 -10.249 1.00 53.05 C ANISOU 1048 CB PHE A 171 4804 9856 5498 -951 -800 -1625 C ATOM 1049 CG PHE A 171 -21.138 27.776 -10.401 1.00 52.30 C ANISOU 1049 CG PHE A 171 4535 9950 5387 -862 -764 -1482 C ATOM 1050 CD1 PHE A 171 -20.617 28.869 -11.073 1.00 52.57 C ANISOU 1050 CD1 PHE A 171 4510 9967 5496 -762 -731 -1498 C ATOM 1051 CD2 PHE A 171 -22.415 27.868 -9.871 1.00 48.41 C ANISOU 1051 CD2 PHE A 171 3933 9659 4803 -879 -774 -1326 C ATOM 1052 CE1 PHE A 171 -21.356 30.031 -11.214 1.00 51.16 C ANISOU 1052 CE1 PHE A 171 4178 9948 5314 -678 -716 -1369 C ATOM 1053 CE2 PHE A 171 -23.157 29.026 -10.008 1.00 50.52 C ANISOU 1053 CE2 PHE A 171 4039 10097 5058 -782 -746 -1203 C ATOM 1054 CZ PHE A 171 -22.628 30.109 -10.681 1.00 47.36 C ANISOU 1054 CZ PHE A 171 3593 9658 4746 -680 -722 -1228 C ATOM 1055 N ASP A 172 -18.446 24.761 -12.467 1.00 51.20 N ANISOU 1055 N ASP A 172 4839 9361 5252 -1189 -843 -1945 N ATOM 1056 CA ASP A 172 -17.338 23.849 -12.730 1.00 55.13 C ANISOU 1056 CA ASP A 172 5494 9669 5783 -1212 -870 -2135 C ATOM 1057 C ASP A 172 -16.221 23.956 -11.701 1.00 57.93 C ANISOU 1057 C ASP A 172 5924 9813 6275 -1040 -852 -2252 C ATOM 1058 O ASP A 172 -15.249 23.200 -11.751 1.00 60.24 O ANISOU 1058 O ASP A 172 6347 9934 6607 -1037 -875 -2413 O ATOM 1059 CB ASP A 172 -16.778 24.099 -14.128 1.00 55.72 C ANISOU 1059 CB ASP A 172 5550 9786 5834 -1243 -839 -2204 C ATOM 1060 CG ASP A 172 -17.838 23.995 -15.197 1.00 56.65 C ANISOU 1060 CG ASP A 172 5597 10109 5818 -1422 -856 -2090 C ATOM 1061 OD1 ASP A 172 -18.370 22.883 -15.402 1.00 59.66 O ANISOU 1061 OD1 ASP A 172 6066 10497 6105 -1585 -926 -2095 O ATOM 1062 OD2 ASP A 172 -18.139 25.026 -15.831 1.00 53.94 O ANISOU 1062 OD2 ASP A 172 5115 9914 5466 -1405 -810 -1991 O ATOM 1063 N TRP A 173 -16.357 24.895 -10.773 1.00 64.98 N ANISOU 1063 N TRP A 173 6735 10717 7236 -894 -814 -2173 N ATOM 1064 CA TRP A 173 -15.366 25.057 -9.720 1.00 66.40 C ANISOU 1064 CA TRP A 173 6982 10702 7545 -733 -799 -2266 C ATOM 1065 C TRP A 173 -15.855 26.011 -8.641 1.00 66.45 C ANISOU 1065 C TRP A 173 6893 10760 7595 -592 -773 -2156 C ATOM 1066 O TRP A 173 -15.942 27.219 -8.861 1.00 69.07 O ANISOU 1066 O TRP A 173 7116 11170 7957 -484 -735 -2088 O ATOM 1067 CB TRP A 173 -14.041 25.556 -10.299 1.00 66.59 C ANISOU 1067 CB TRP A 173 7031 10616 7653 -630 -759 -2383 C ATOM 1068 CG TRP A 173 -12.864 25.316 -9.401 1.00 64.71 C ANISOU 1068 CG TRP A 173 6904 10148 7534 -511 -757 -2510 C ATOM 1069 CD1 TRP A 173 -12.243 24.123 -9.164 1.00 67.07 C ANISOU 1069 CD1 TRP A 173 7348 10284 7851 -561 -797 -2647 C ATOM 1070 CD2 TRP A 173 -12.162 26.295 -8.625 1.00 57.03 C ANISOU 1070 CD2 TRP A 173 5910 9076 6681 -325 -722 -2509 C ATOM 1071 NE1 TRP A 173 -11.201 24.299 -8.286 1.00 61.64 N ANISOU 1071 NE1 TRP A 173 6724 9410 7288 -420 -780 -2726 N ATOM 1072 CE2 TRP A 173 -11.130 25.621 -7.942 1.00 54.76 C ANISOU 1072 CE2 TRP A 173 5754 8573 6477 -277 -733 -2641 C ATOM 1073 CE3 TRP A 173 -12.309 27.672 -8.441 1.00 51.79 C ANISOU 1073 CE3 TRP A 173 5136 8477 6065 -194 -693 -2408 C ATOM 1074 CZ2 TRP A 173 -10.247 26.282 -7.089 1.00 47.59 C ANISOU 1074 CZ2 TRP A 173 4869 7520 5694 -110 -709 -2668 C ATOM 1075 CZ3 TRP A 173 -11.431 28.325 -7.596 1.00 45.15 C ANISOU 1075 CZ3 TRP A 173 4326 7484 5346 -24 -680 -2440 C ATOM 1076 CH2 TRP A 173 -10.413 27.630 -6.930 1.00 43.87 C ANISOU 1076 CH2 TRP A 173 4294 7114 5261 12 -684 -2565 C ATOM 1077 N VAL A 174 -16.180 25.458 -7.477 1.00 61.97 N ANISOU 1077 N VAL A 174 6367 10153 7028 -594 -804 -2140 N ATOM 1078 CA VAL A 174 -16.565 26.264 -6.326 1.00 54.53 C ANISOU 1078 CA VAL A 174 5345 9254 6122 -445 -782 -2059 C ATOM 1079 C VAL A 174 -15.467 26.224 -5.271 1.00 52.33 C ANISOU 1079 C VAL A 174 5165 8748 5970 -314 -776 -2171 C ATOM 1080 O VAL A 174 -14.945 25.159 -4.946 1.00 57.71 O ANISOU 1080 O VAL A 174 5971 9284 6674 -388 -815 -2265 O ATOM 1081 CB VAL A 174 -17.884 25.781 -5.703 1.00 50.26 C ANISOU 1081 CB VAL A 174 4741 8888 5467 -541 -819 -1928 C ATOM 1082 CG1 VAL A 174 -18.284 26.696 -4.558 1.00 49.65 C ANISOU 1082 CG1 VAL A 174 4567 8883 5415 -365 -790 -1855 C ATOM 1083 CG2 VAL A 174 -18.978 25.723 -6.758 1.00 46.02 C ANISOU 1083 CG2 VAL A 174 4114 8573 4799 -691 -830 -1808 C ATOM 1084 N TYR A 175 -15.119 27.390 -4.742 1.00 52.92 N ANISOU 1084 N TYR A 175 5190 8788 6130 -120 -738 -2158 N ATOM 1085 CA TYR A 175 -14.028 27.495 -3.784 1.00 51.69 C ANISOU 1085 CA TYR A 175 5125 8414 6099 13 -730 -2255 C ATOM 1086 C TYR A 175 -14.435 28.340 -2.586 1.00 57.68 C ANISOU 1086 C TYR A 175 5817 9214 6886 177 -718 -2188 C ATOM 1087 O TYR A 175 -14.876 29.476 -2.745 1.00 61.25 O ANISOU 1087 O TYR A 175 6162 9776 7333 290 -702 -2112 O ATOM 1088 CB TYR A 175 -12.798 28.095 -4.466 1.00 48.65 C ANISOU 1088 CB TYR A 175 4779 7895 5812 97 -705 -2338 C ATOM 1089 CG TYR A 175 -11.610 28.314 -3.558 1.00 48.84 C ANISOU 1089 CG TYR A 175 4894 7695 5969 238 -697 -2425 C ATOM 1090 CD1 TYR A 175 -11.143 27.299 -2.733 1.00 53.55 C ANISOU 1090 CD1 TYR A 175 5605 8140 6603 199 -716 -2509 C ATOM 1091 CD2 TYR A 175 -10.938 29.530 -3.543 1.00 47.37 C ANISOU 1091 CD2 TYR A 175 4683 7443 5872 400 -683 -2416 C ATOM 1092 CE1 TYR A 175 -10.050 27.494 -1.907 1.00 52.29 C ANISOU 1092 CE1 TYR A 175 5528 7774 6566 320 -708 -2581 C ATOM 1093 CE2 TYR A 175 -9.845 29.733 -2.722 1.00 48.29 C ANISOU 1093 CE2 TYR A 175 4887 7354 6108 520 -680 -2484 C ATOM 1094 CZ TYR A 175 -9.406 28.712 -1.907 1.00 48.83 C ANISOU 1094 CZ TYR A 175 5064 7279 6210 480 -686 -2567 C ATOM 1095 OH TYR A 175 -8.317 28.908 -1.091 1.00 47.68 O ANISOU 1095 OH TYR A 175 5004 6928 6183 593 -683 -2628 O ATOM 1096 N TYR A 176 -14.297 27.778 -1.388 1.00 58.90 N ANISOU 1096 N TYR A 176 6031 9283 7065 191 -734 -2220 N ATOM 1097 CA TYR A 176 -14.568 28.512 -0.156 1.00 57.15 C ANISOU 1097 CA TYR A 176 5757 9090 6868 356 -723 -2177 C ATOM 1098 C TYR A 176 -13.424 29.493 0.077 1.00 54.76 C ANISOU 1098 C TYR A 176 5505 8596 6705 545 -703 -2246 C ATOM 1099 O TYR A 176 -12.667 29.368 1.039 1.00 61.27 O ANISOU 1099 O TYR A 176 6414 9249 7615 617 -704 -2312 O ATOM 1100 CB TYR A 176 -14.683 27.546 1.022 1.00 60.92 C ANISOU 1100 CB TYR A 176 6286 9532 7330 292 -752 -2190 C ATOM 1101 CG TYR A 176 -15.515 28.053 2.183 1.00 62.68 C ANISOU 1101 CG TYR A 176 6407 9909 7500 403 -746 -2108 C ATOM 1102 CD1 TYR A 176 -15.319 29.324 2.707 1.00 63.23 C ANISOU 1102 CD1 TYR A 176 6435 9957 7631 633 -718 -2111 C ATOM 1103 CD2 TYR A 176 -16.483 27.248 2.769 1.00 61.07 C ANISOU 1103 CD2 TYR A 176 6148 9877 7178 280 -780 -2026 C ATOM 1104 CE1 TYR A 176 -16.074 29.783 3.770 1.00 60.25 C ANISOU 1104 CE1 TYR A 176 5964 9732 7195 752 -714 -2051 C ATOM 1105 CE2 TYR A 176 -17.240 27.697 3.833 1.00 56.99 C ANISOU 1105 CE2 TYR A 176 5525 9532 6598 386 -772 -1953 C ATOM 1106 CZ TYR A 176 -17.032 28.964 4.329 1.00 57.19 C ANISOU 1106 CZ TYR A 176 5510 9538 6682 630 -734 -1974 C ATOM 1107 OH TYR A 176 -17.786 29.415 5.387 1.00 57.53 O ANISOU 1107 OH TYR A 176 5445 9763 6652 754 -727 -1916 O ATOM 1108 N GLU A 177 -13.310 30.466 -0.820 1.00 53.37 N ANISOU 1108 N GLU A 177 5276 8452 6551 612 -694 -2219 N ATOM 1109 CA GLU A 177 -12.187 31.397 -0.845 1.00 52.15 C ANISOU 1109 CA GLU A 177 5169 8123 6522 761 -694 -2267 C ATOM 1110 C GLU A 177 -11.846 31.937 0.536 1.00 60.82 C ANISOU 1110 C GLU A 177 6305 9105 7699 938 -700 -2286 C ATOM 1111 O GLU A 177 -10.826 31.574 1.119 1.00 60.49 O ANISOU 1111 O GLU A 177 6375 8862 7745 958 -698 -2368 O ATOM 1112 CB GLU A 177 -12.486 32.548 -1.805 1.00 47.57 C ANISOU 1112 CB GLU A 177 4489 7651 5935 819 -706 -2191 C ATOM 1113 CG GLU A 177 -11.266 33.336 -2.223 1.00 49.77 C ANISOU 1113 CG GLU A 177 4815 7767 6327 906 -724 -2226 C ATOM 1114 CD GLU A 177 -10.895 34.398 -1.220 1.00 55.75 C ANISOU 1114 CD GLU A 177 5595 8408 7180 1118 -755 -2218 C ATOM 1115 OE1 GLU A 177 -11.786 35.179 -0.824 1.00 56.60 O ANISOU 1115 OE1 GLU A 177 5619 8629 7258 1231 -777 -2150 O ATOM 1116 OE2 GLU A 177 -9.708 34.457 -0.836 1.00 58.53 O ANISOU 1116 OE2 GLU A 177 6049 8556 7634 1175 -763 -2281 O ATOM 1117 N SER A 178 -12.699 32.811 1.055 1.00 80.46 N ANISOU 1117 N SER A 178 8697 11722 10151 1072 -710 -2214 N ATOM 1118 CA SER A 178 -12.488 33.370 2.383 1.00 84.13 C ANISOU 1118 CA SER A 178 9191 12101 10674 1252 -720 -2235 C ATOM 1119 C SER A 178 -13.713 33.166 3.264 1.00 85.58 C ANISOU 1119 C SER A 178 9282 12488 10745 1274 -712 -2181 C ATOM 1120 O SER A 178 -14.726 32.623 2.823 1.00 82.54 O ANISOU 1120 O SER A 178 8810 12311 10241 1145 -702 -2115 O ATOM 1121 CB SER A 178 -12.138 34.857 2.297 1.00 86.38 C ANISOU 1121 CB SER A 178 9462 12316 11040 1451 -760 -2215 C ATOM 1122 OG SER A 178 -13.174 35.588 1.667 1.00 88.12 O ANISOU 1122 OG SER A 178 9553 12739 11191 1488 -778 -2128 O ATOM 1123 N LYS A 179 -13.614 33.600 4.515 1.00 83.31 N ANISOU 1123 N LYS A 179 9012 12152 10490 1435 -719 -2205 N ATOM 1124 CA LYS A 179 -14.725 33.495 5.448 1.00 86.55 C ANISOU 1124 CA LYS A 179 9322 12776 10787 1480 -711 -2156 C ATOM 1125 C LYS A 179 -15.806 34.504 5.077 1.00 85.64 C ANISOU 1125 C LYS A 179 9063 12882 10593 1604 -722 -2076 C ATOM 1126 O LYS A 179 -16.921 34.461 5.598 1.00 86.22 O ANISOU 1126 O LYS A 179 9018 13197 10544 1635 -713 -2016 O ATOM 1127 CB LYS A 179 -14.232 33.741 6.873 1.00 92.03 C ANISOU 1127 CB LYS A 179 10077 13353 11539 1630 -716 -2214 C ATOM 1128 CG LYS A 179 -15.261 33.489 7.957 1.00102.85 C ANISOU 1128 CG LYS A 179 11345 14951 12783 1665 -706 -2173 C ATOM 1129 CD LYS A 179 -14.686 33.823 9.325 1.00110.97 C ANISOU 1129 CD LYS A 179 12438 15853 13874 1823 -712 -2239 C ATOM 1130 CE LYS A 179 -15.725 33.658 10.420 1.00115.95 C ANISOU 1130 CE LYS A 179 12947 16744 14364 1873 -702 -2197 C ATOM 1131 NZ LYS A 179 -15.168 33.949 11.771 1.00117.72 N ANISOU 1131 NZ LYS A 179 13234 16854 14642 2020 -707 -2266 N ATOM 1132 N ALA A 180 -15.467 35.400 4.154 1.00 80.95 N ANISOU 1132 N ALA A 180 8473 12213 10070 1668 -748 -2069 N ATOM 1133 CA ALA A 180 -16.347 36.505 3.784 1.00 75.01 C ANISOU 1133 CA ALA A 180 7599 11627 9274 1807 -776 -2001 C ATOM 1134 C ALA A 180 -17.119 36.270 2.486 1.00 70.41 C ANISOU 1134 C ALA A 180 6918 11226 8609 1647 -765 -1914 C ATOM 1135 O ALA A 180 -18.111 36.950 2.225 1.00 70.97 O ANISOU 1135 O ALA A 180 6862 11491 8611 1727 -781 -1840 O ATOM 1136 CB ALA A 180 -15.558 37.804 3.704 1.00 75.36 C ANISOU 1136 CB ALA A 180 7704 11479 9453 2000 -839 -2034 C ATOM 1137 N HIS A 181 -16.662 35.323 1.672 1.00 60.70 N ANISOU 1137 N HIS A 181 5748 9932 7383 1426 -743 -1927 N ATOM 1138 CA HIS A 181 -17.359 34.981 0.431 1.00 59.74 C ANISOU 1138 CA HIS A 181 5545 9977 7176 1252 -733 -1849 C ATOM 1139 C HIS A 181 -16.816 33.706 -0.202 1.00 53.63 C ANISOU 1139 C HIS A 181 4861 9121 6396 1014 -711 -1890 C ATOM 1140 O HIS A 181 -15.685 33.302 0.062 1.00 50.65 O ANISOU 1140 O HIS A 181 4611 8522 6110 1001 -709 -1985 O ATOM 1141 CB HIS A 181 -17.270 36.127 -0.583 1.00 63.02 C ANISOU 1141 CB HIS A 181 5913 10384 7648 1322 -770 -1810 C ATOM 1142 CG HIS A 181 -15.916 36.289 -1.197 1.00 67.39 C ANISOU 1142 CG HIS A 181 6577 10703 8326 1295 -789 -1874 C ATOM 1143 ND1 HIS A 181 -15.460 35.491 -2.225 1.00 67.04 N ANISOU 1143 ND1 HIS A 181 6574 10629 8270 1092 -767 -1893 N ATOM 1144 CD2 HIS A 181 -14.911 37.160 -0.929 1.00 67.42 C ANISOU 1144 CD2 HIS A 181 6655 10503 8458 1446 -834 -1919 C ATOM 1145 CE1 HIS A 181 -14.238 35.860 -2.561 1.00 63.54 C ANISOU 1145 CE1 HIS A 181 6213 9992 7939 1123 -789 -1947 C ATOM 1146 NE2 HIS A 181 -13.882 36.871 -1.789 1.00 63.37 N ANISOU 1146 NE2 HIS A 181 6214 9859 8005 1328 -833 -1955 N ATOM 1147 N ILE A 182 -17.631 33.075 -1.042 1.00 60.71 N ANISOU 1147 N ILE A 182 5692 10194 7182 831 -701 -1820 N ATOM 1148 CA ILE A 182 -17.186 31.921 -1.814 1.00 64.44 C ANISOU 1148 CA ILE A 182 6248 10597 7639 611 -695 -1862 C ATOM 1149 C ILE A 182 -17.003 32.297 -3.281 1.00 62.94 C ANISOU 1149 C ILE A 182 6032 10422 7459 539 -698 -1844 C ATOM 1150 O ILE A 182 -17.650 33.214 -3.783 1.00 66.02 O ANISOU 1150 O ILE A 182 6310 10951 7826 597 -707 -1757 O ATOM 1151 CB ILE A 182 -18.150 30.721 -1.692 1.00 72.76 C ANISOU 1151 CB ILE A 182 7273 11818 8556 421 -700 -1802 C ATOM 1152 CG1 ILE A 182 -19.597 31.158 -1.921 1.00 79.20 C ANISOU 1152 CG1 ILE A 182 7922 12926 9245 419 -698 -1658 C ATOM 1153 CG2 ILE A 182 -18.012 30.072 -0.323 1.00 72.92 C ANISOU 1153 CG2 ILE A 182 7349 11778 8580 440 -708 -1840 C ATOM 1154 CD1 ILE A 182 -20.280 31.682 -0.676 1.00 82.36 C ANISOU 1154 CD1 ILE A 182 8232 13457 9605 589 -694 -1610 C ATOM 1155 N HIS A 183 -16.118 31.581 -3.963 1.00 49.13 N ANISOU 1155 N HIS A 183 4384 8539 5743 414 -694 -1927 N ATOM 1156 CA HIS A 183 -15.752 31.913 -5.333 1.00 50.65 C ANISOU 1156 CA HIS A 183 4558 8740 5948 347 -696 -1925 C ATOM 1157 C HIS A 183 -16.160 30.813 -6.306 1.00 55.29 C ANISOU 1157 C HIS A 183 5155 9424 6429 116 -692 -1920 C ATOM 1158 O HIS A 183 -15.745 29.663 -6.167 1.00 56.16 O ANISOU 1158 O HIS A 183 5374 9436 6529 11 -697 -2005 O ATOM 1159 CB HIS A 183 -14.246 32.160 -5.421 1.00 47.59 C ANISOU 1159 CB HIS A 183 4271 8125 5685 419 -698 -2030 C ATOM 1160 CG HIS A 183 -13.740 32.327 -6.821 1.00 52.65 C ANISOU 1160 CG HIS A 183 4894 8783 6326 332 -699 -2039 C ATOM 1161 ND1 HIS A 183 -13.609 33.561 -7.420 1.00 57.20 N ANISOU 1161 ND1 HIS A 183 5390 9397 6947 410 -725 -1973 N ATOM 1162 CD2 HIS A 183 -13.328 31.418 -7.733 1.00 55.58 C ANISOU 1162 CD2 HIS A 183 5316 9147 6653 174 -687 -2106 C ATOM 1163 CE1 HIS A 183 -13.139 33.404 -8.645 1.00 60.23 C ANISOU 1163 CE1 HIS A 183 5764 9811 7308 294 -722 -1990 C ATOM 1164 NE2 HIS A 183 -12.960 32.113 -8.861 1.00 57.88 N ANISOU 1164 NE2 HIS A 183 5547 9491 6954 158 -694 -2078 N ATOM 1165 N CYS A 184 -16.972 31.174 -7.294 1.00 67.72 N ANISOU 1165 N CYS A 184 6620 11184 7927 38 -694 -1821 N ATOM 1166 CA CYS A 184 -17.442 30.217 -8.289 1.00 69.49 C ANISOU 1166 CA CYS A 184 6849 11513 8041 -184 -697 -1804 C ATOM 1167 C CYS A 184 -16.974 30.595 -9.689 1.00 64.97 C ANISOU 1167 C CYS A 184 6250 10960 7475 -247 -692 -1816 C ATOM 1168 O CYS A 184 -16.772 31.770 -9.991 1.00 62.44 O ANISOU 1168 O CYS A 184 5853 10655 7216 -140 -696 -1772 O ATOM 1169 CB CYS A 184 -18.967 30.123 -8.260 1.00 73.56 C ANISOU 1169 CB CYS A 184 7252 12267 8431 -264 -705 -1658 C ATOM 1170 SG CYS A 184 -19.642 29.482 -6.712 1.00 57.84 S ANISOU 1170 SG CYS A 184 5272 10314 6391 -238 -718 -1625 S ATOM 1171 N SER A 185 -16.804 29.591 -10.542 1.00 62.43 N ANISOU 1171 N SER A 185 5991 10641 7087 -422 -696 -1874 N ATOM 1172 CA SER A 185 -16.391 29.825 -11.921 1.00 60.42 C ANISOU 1172 CA SER A 185 5706 10435 6816 -501 -690 -1890 C ATOM 1173 C SER A 185 -16.821 28.681 -12.829 1.00 62.34 C ANISOU 1173 C SER A 185 5989 10763 6936 -717 -702 -1909 C ATOM 1174 O SER A 185 -16.979 27.544 -12.381 1.00 65.83 O ANISOU 1174 O SER A 185 6530 11146 7335 -798 -726 -1961 O ATOM 1175 CB SER A 185 -14.878 30.030 -12.010 1.00 55.17 C ANISOU 1175 CB SER A 185 5115 9593 6255 -407 -680 -2018 C ATOM 1176 OG SER A 185 -14.178 28.886 -11.554 1.00 54.32 O ANISOU 1176 OG SER A 185 5153 9324 6161 -431 -682 -2159 O ATOM 1177 N VAL A 186 -17.009 28.995 -14.107 1.00 60.73 N ANISOU 1177 N VAL A 186 5707 10692 6675 -816 -696 -1863 N ATOM 1178 CA VAL A 186 -17.438 28.011 -15.091 1.00 56.97 C ANISOU 1178 CA VAL A 186 5264 10308 6075 -1023 -713 -1876 C ATOM 1179 C VAL A 186 -16.434 27.937 -16.236 1.00 56.64 C ANISOU 1179 C VAL A 186 5245 10245 6029 -1064 -700 -1987 C ATOM 1180 O VAL A 186 -15.462 28.693 -16.268 1.00 49.35 O ANISOU 1180 O VAL A 186 4299 9255 5196 -941 -681 -2031 O ATOM 1181 CB VAL A 186 -18.825 28.363 -15.652 1.00 51.59 C ANISOU 1181 CB VAL A 186 4451 9855 5296 -1137 -718 -1697 C ATOM 1182 CG1 VAL A 186 -19.886 28.209 -14.575 1.00 58.15 C ANISOU 1182 CG1 VAL A 186 5257 10741 6096 -1120 -733 -1589 C ATOM 1183 CG2 VAL A 186 -18.828 29.780 -16.200 1.00 46.82 C ANISOU 1183 CG2 VAL A 186 3700 9348 4742 -1062 -700 -1603 C ATOM 1184 N LYS A 187 -16.666 27.023 -17.172 1.00 61.53 N ANISOU 1184 N LYS A 187 5911 10932 6537 -1237 -718 -2030 N ATOM 1185 CA LYS A 187 -15.808 26.906 -18.345 1.00 65.65 C ANISOU 1185 CA LYS A 187 6441 11476 7027 -1283 -706 -2136 C ATOM 1186 C LYS A 187 -16.263 27.904 -19.403 1.00 65.41 C ANISOU 1186 C LYS A 187 6246 11650 6957 -1348 -690 -2003 C ATOM 1187 O LYS A 187 -17.247 28.622 -19.209 1.00 58.75 O ANISOU 1187 O LYS A 187 5294 10914 6116 -1352 -692 -1836 O ATOM 1188 CB LYS A 187 -15.859 25.486 -18.910 1.00 71.15 C ANISOU 1188 CB LYS A 187 7265 12153 7614 -1433 -743 -2253 C ATOM 1189 CG LYS A 187 -16.028 24.403 -17.857 1.00 79.38 C ANISOU 1189 CG LYS A 187 8455 13038 8667 -1438 -792 -2313 C ATOM 1190 CD LYS A 187 -16.417 23.071 -18.483 1.00 87.07 C ANISOU 1190 CD LYS A 187 9544 14018 9519 -1617 -858 -2381 C ATOM 1191 CE LYS A 187 -15.201 22.199 -18.745 1.00 93.27 C ANISOU 1191 CE LYS A 187 10475 14648 10317 -1577 -880 -2614 C ATOM 1192 NZ LYS A 187 -14.645 21.644 -17.479 1.00 95.24 N ANISOU 1192 NZ LYS A 187 10847 14673 10665 -1474 -911 -2707 N ATOM 1193 N ALA A 188 -15.545 27.949 -20.520 1.00 62.87 N ANISOU 1193 N ALA A 188 5899 11392 6597 -1396 -678 -2074 N ATOM 1194 CA ALA A 188 -15.915 28.818 -21.632 1.00 70.72 C ANISOU 1194 CA ALA A 188 6736 12588 7546 -1484 -671 -1951 C ATOM 1195 C ALA A 188 -16.742 28.048 -22.662 1.00 78.83 C ANISOU 1195 C ALA A 188 7767 13763 8423 -1697 -684 -1929 C ATOM 1196 O ALA A 188 -16.979 26.848 -22.509 1.00 71.37 O ANISOU 1196 O ALA A 188 6954 12753 7411 -1770 -707 -2015 O ATOM 1197 CB ALA A 188 -14.674 29.411 -22.276 1.00 69.85 C ANISOU 1197 CB ALA A 188 6573 12497 7472 -1424 -657 -2017 C ATOM 1198 N GLU A 189 -17.180 28.739 -23.710 1.00 81.29 N ATOM 1199 CA GLU A 189 -17.924 28.094 -24.787 1.00 95.63 C ATOM 1200 C GLU A 189 -17.078 27.008 -25.445 1.00108.37 C ATOM 1201 O GLU A 189 -17.558 26.259 -26.298 1.00108.44 O ATOM 1202 CB GLU A 189 -18.370 29.121 -25.816 1.00 94.30 C ATOM 1203 N ASN A 190 -15.815 26.932 -25.037 1.00113.94 N ATOM 1204 CA ASN A 190 -14.880 25.946 -25.563 1.00121.05 C ATOM 1205 C ASN A 190 -14.963 24.622 -24.809 1.00130.04 C ATOM 1206 O ASN A 190 -13.948 24.085 -24.365 1.00132.16 O ATOM 1207 CB ASN A 190 -13.453 26.493 -25.502 1.00117.48 C ATOM 1208 CG ASN A 190 -13.353 27.918 -26.011 1.00114.48 C ATOM 1209 OD1 ASN A 190 -14.117 28.334 -26.882 1.00113.34 O ATOM 1210 ND2 ASN A 190 -12.408 28.676 -25.467 1.00113.25 N ATOM 1211 N SER A 191 -16.179 24.102 -24.666 1.00138.94 N ATOM 1212 CA SER A 191 -16.396 22.833 -23.980 1.00139.40 C ATOM 1213 C SER A 191 -17.814 22.317 -24.207 1.00139.36 C ATOM 1214 O SER A 191 -18.730 23.091 -24.485 1.00139.27 O ATOM 1215 CB SER A 191 -16.115 22.977 -22.491 1.00138.49 C TER 1216 ALA A 191 ATOM 1217 N ASN B 215 11.371 57.766 43.032 1.00120.61 N ANISOU 1217 N ASN B 215 13758 14935 17132 283 -1887 -1931 N ATOM 1218 CA ASN B 215 10.256 58.390 42.329 1.00120.37 C ANISOU 1218 CA ASN B 215 13813 14754 17169 157 -1913 -1842 C ATOM 1219 C ASN B 215 10.513 58.511 40.825 1.00120.37 C ANISOU 1219 C ASN B 215 13843 14701 17192 2 -1837 -1708 C ATOM 1220 O ASN B 215 9.593 58.388 40.012 1.00122.13 O ANISOU 1220 O ASN B 215 14182 14841 17380 -62 -1804 -1603 O ATOM 1221 CB ASN B 215 9.965 59.767 42.931 1.00120.17 C ANISOU 1221 CB ASN B 215 13694 14650 17317 110 -2044 -1928 C ATOM 1222 CG ASN B 215 8.857 60.499 42.206 1.00119.04 C ANISOU 1222 CG ASN B 215 13632 14349 17249 -19 -2075 -1838 C ATOM 1223 OD1 ASN B 215 7.845 59.906 41.831 1.00116.83 O ANISOU 1223 OD1 ASN B 215 13496 14028 16867 -9 -2036 -1759 O ATOM 1224 ND2 ASN B 215 9.039 61.800 42.009 1.00119.09 N ANISOU 1224 ND2 ASN B 215 13543 14264 17441 -138 -2145 -1853 N ATOM 1225 N CYS B 216 11.772 58.736 40.462 1.00 90.09 N ANISOU 1225 N CYS B 216 9896 10924 13409 -51 -1807 -1717 N ATOM 1226 CA CYS B 216 12.130 58.989 39.073 1.00 81.97 C ANISOU 1226 CA CYS B 216 8870 9858 12416 -197 -1739 -1591 C ATOM 1227 C CYS B 216 13.161 57.986 38.560 1.00 72.92 C ANISOU 1227 C CYS B 216 7714 8841 11153 -165 -1636 -1561 C ATOM 1228 O CYS B 216 14.175 57.738 39.211 1.00 73.67 O ANISOU 1228 O CYS B 216 7713 9045 11234 -89 -1637 -1659 O ATOM 1229 CB CYS B 216 12.669 60.413 38.937 1.00 84.40 C ANISOU 1229 CB CYS B 216 9042 10093 12933 -324 -1798 -1609 C ATOM 1230 SG CYS B 216 12.622 61.087 37.265 1.00 98.70 S ANISOU 1230 SG CYS B 216 10873 11806 14822 -515 -1734 -1425 S ATOM 1231 N PHE B 217 12.900 57.417 37.386 1.00 62.93 N ANISOU 1231 N PHE B 217 6541 7570 9799 -218 -1549 -1434 N ATOM 1232 CA PHE B 217 13.824 56.464 36.771 1.00 58.74 C ANISOU 1232 CA PHE B 217 6003 7160 9155 -195 -1452 -1399 C ATOM 1233 C PHE B 217 14.884 57.147 35.905 1.00 58.20 C ANISOU 1233 C PHE B 217 5823 7113 9176 -323 -1423 -1346 C ATOM 1234 O PHE B 217 14.770 58.326 35.575 1.00 60.60 O ANISOU 1234 O PHE B 217 6075 7320 9630 -442 -1461 -1305 O ATOM 1235 CB PHE B 217 13.059 55.428 35.942 1.00 53.23 C ANISOU 1235 CB PHE B 217 5446 6462 8315 -175 -1373 -1304 C ATOM 1236 CG PHE B 217 12.455 54.322 36.761 1.00 52.68 C ANISOU 1236 CG PHE B 217 5470 6420 8128 -24 -1360 -1360 C ATOM 1237 CD1 PHE B 217 13.169 53.161 37.010 1.00 55.00 C ANISOU 1237 CD1 PHE B 217 5763 6831 8302 88 -1296 -1397 C ATOM 1238 CD2 PHE B 217 11.177 54.440 37.279 1.00 49.46 C ANISOU 1238 CD2 PHE B 217 5148 5916 7729 9 -1408 -1373 C ATOM 1239 CE1 PHE B 217 12.620 52.138 37.762 1.00 51.82 C ANISOU 1239 CE1 PHE B 217 5445 6444 7801 230 -1273 -1435 C ATOM 1240 CE2 PHE B 217 10.621 53.421 38.031 1.00 48.85 C ANISOU 1240 CE2 PHE B 217 5152 5859 7550 147 -1386 -1414 C ATOM 1241 CZ PHE B 217 11.345 52.268 38.272 1.00 50.70 C ANISOU 1241 CZ PHE B 217 5385 6204 7675 259 -1314 -1440 C ATOM 1242 N CYS B 218 15.916 56.394 35.540 1.00 54.06 N ANISOU 1242 N CYS B 218 5261 6717 8563 -295 -1351 -1344 N ATOM 1243 CA CYS B 218 16.997 56.924 34.717 1.00 56.50 C ANISOU 1243 CA CYS B 218 5461 7066 8942 -408 -1312 -1293 C ATOM 1244 C CYS B 218 17.312 55.981 33.560 1.00 57.93 C ANISOU 1244 C CYS B 218 5690 7340 8980 -416 -1210 -1194 C ATOM 1245 O CYS B 218 17.252 54.761 33.713 1.00 58.85 O ANISOU 1245 O CYS B 218 5879 7536 8946 -303 -1170 -1221 O ATOM 1246 CB CYS B 218 18.254 57.151 35.565 1.00 59.60 C ANISOU 1246 CB CYS B 218 5706 7545 9396 -370 -1341 -1429 C ATOM 1247 SG CYS B 218 18.160 58.540 36.726 1.00 44.55 S ANISOU 1247 SG CYS B 218 3685 5538 7704 -392 -1463 -1556 S ATOM 1248 N ILE B 219 17.638 56.547 32.402 1.00 66.42 N ANISOU 1248 N ILE B 219 6723 8407 10108 -543 -1167 -1077 N ATOM 1249 CA ILE B 219 18.055 55.744 31.254 1.00 62.46 C ANISOU 1249 CA ILE B 219 6243 8014 9476 -553 -1075 -987 C ATOM 1250 C ILE B 219 19.501 56.042 30.872 1.00 62.78 C ANISOU 1250 C ILE B 219 6142 8151 9559 -617 -1038 -983 C ATOM 1251 O ILE B 219 19.942 57.189 30.912 1.00 59.60 O ANISOU 1251 O ILE B 219 5635 7689 9322 -717 -1063 -975 O ATOM 1252 CB ILE B 219 17.137 55.942 30.018 1.00 58.28 C ANISOU 1252 CB ILE B 219 5793 7426 8924 -628 -1038 -834 C ATOM 1253 CG1 ILE B 219 17.380 57.303 29.355 1.00 54.55 C ANISOU 1253 CG1 ILE B 219 5236 6883 8608 -775 -1039 -729 C ATOM 1254 CG2 ILE B 219 15.674 55.764 30.400 1.00 59.29 C ANISOU 1254 CG2 ILE B 219 6053 7450 9026 -576 -1080 -846 C ATOM 1255 CD1 ILE B 219 16.673 58.459 30.030 1.00 54.96 C ANISOU 1255 CD1 ILE B 219 5285 6771 8828 -823 -1123 -751 C ATOM 1256 N GLN B 220 20.236 54.997 30.510 1.00 68.07 N ANISOU 1256 N GLN B 220 6808 8968 10088 -558 -977 -994 N ATOM 1257 CA GLN B 220 21.623 55.146 30.092 1.00 73.39 C ANISOU 1257 CA GLN B 220 7352 9753 10779 -612 -935 -993 C ATOM 1258 C GLN B 220 21.814 54.596 28.685 1.00 74.86 C ANISOU 1258 C GLN B 220 7558 10037 10848 -647 -851 -866 C ATOM 1259 O GLN B 220 21.235 53.572 28.325 1.00 70.94 O ANISOU 1259 O GLN B 220 7165 9582 10206 -571 -822 -846 O ATOM 1260 CB GLN B 220 22.562 54.430 31.065 1.00 76.33 C ANISOU 1260 CB GLN B 220 7673 10242 11086 -497 -947 -1149 C ATOM 1261 CG GLN B 220 22.374 52.920 31.112 1.00 83.48 C ANISOU 1261 CG GLN B 220 8682 11242 11795 -359 -910 -1178 C ATOM 1262 CD GLN B 220 23.501 52.216 31.841 1.00 92.95 C ANISOU 1262 CD GLN B 220 9818 12581 12919 -252 -905 -1309 C ATOM 1263 OE1 GLN B 220 24.547 52.808 32.111 1.00 97.47 O ANISOU 1263 OE1 GLN B 220 10259 13204 13571 -291 -920 -1374 O ATOM 1264 NE2 GLN B 220 23.295 50.943 32.162 1.00 95.02 N ANISOU 1264 NE2 GLN B 220 10169 12902 13030 -112 -882 -1351 N ATOM 1265 N GLU B 221 22.625 55.284 27.891 1.00 84.05 N ANISOU 1265 N GLU B 221 8614 11239 12082 -759 -811 -783 N ATOM 1266 CA GLU B 221 22.893 54.855 26.525 1.00 83.52 C ANISOU 1266 CA GLU B 221 8544 11283 11905 -791 -732 -659 C ATOM 1267 C GLU B 221 23.745 53.591 26.510 1.00 75.96 C ANISOU 1267 C GLU B 221 7575 10502 10785 -696 -697 -737 C ATOM 1268 O GLU B 221 24.714 53.474 27.261 1.00 69.16 O ANISOU 1268 O GLU B 221 6635 9703 9939 -662 -713 -855 O ATOM 1269 CB GLU B 221 23.582 55.970 25.737 1.00 89.06 C ANISOU 1269 CB GLU B 221 9124 11981 12734 -934 -693 -542 C ATOM 1270 CG GLU B 221 24.019 55.567 24.343 1.00 93.96 C ANISOU 1270 CG GLU B 221 9718 12744 13237 -962 -609 -414 C ATOM 1271 CD GLU B 221 24.763 56.675 23.631 1.00102.08 C ANISOU 1271 CD GLU B 221 10618 13769 14397 -1099 -560 -292 C ATOM 1272 OE1 GLU B 221 24.561 57.853 23.992 1.00104.50 O ANISOU 1272 OE1 GLU B 221 10885 13923 14896 -1184 -588 -267 O ATOM 1273 OE2 GLU B 221 25.551 56.368 22.711 1.00106.07 O ANISOU 1273 OE2 GLU B 221 11059 14425 14819 -1119 -493 -221 O ATOM 1274 N VAL B 222 23.370 52.643 25.659 1.00 59.17 N ANISOU 1274 N VAL B 222 5522 8458 8504 -646 -652 -681 N ATOM 1275 CA VAL B 222 24.131 51.414 25.502 1.00 57.61 C ANISOU 1275 CA VAL B 222 5314 8426 8150 -556 -616 -744 C ATOM 1276 C VAL B 222 24.928 51.463 24.205 1.00 61.82 C ANISOU 1276 C VAL B 222 5760 9100 8630 -625 -551 -640 C ATOM 1277 O VAL B 222 26.073 51.010 24.149 1.00 64.48 O ANISOU 1277 O VAL B 222 6017 9577 8904 -605 -528 -692 O ATOM 1278 CB VAL B 222 23.214 50.180 25.487 1.00 53.63 C ANISOU 1278 CB VAL B 222 4941 7926 7509 -438 -608 -775 C ATOM 1279 CG1 VAL B 222 24.044 48.905 25.520 1.00 54.57 C ANISOU 1279 CG1 VAL B 222 5047 8201 7485 -335 -578 -860 C ATOM 1280 CG2 VAL B 222 22.251 50.224 26.661 1.00 52.55 C ANISOU 1280 CG2 VAL B 222 4896 7640 7429 -379 -665 -849 C ATOM 1281 N VAL B 223 24.315 52.018 23.164 1.00 71.26 N ANISOU 1281 N VAL B 223 6967 10264 9845 -701 -523 -490 N ATOM 1282 CA VAL B 223 24.975 52.148 21.871 1.00 70.89 C ANISOU 1282 CA VAL B 223 6835 10354 9747 -763 -457 -369 C ATOM 1283 C VAL B 223 24.209 53.074 20.927 1.00 66.41 C ANISOU 1283 C VAL B 223 6277 9716 9239 -849 -432 -195 C ATOM 1284 O VAL B 223 22.989 52.974 20.785 1.00 58.95 O ANISOU 1284 O VAL B 223 5438 8690 8270 -816 -448 -166 O ATOM 1285 CB VAL B 223 25.184 50.775 21.195 1.00 71.32 C ANISOU 1285 CB VAL B 223 6912 10585 9602 -665 -422 -397 C ATOM 1286 CG1 VAL B 223 23.847 50.114 20.899 1.00 70.78 C ANISOU 1286 CG1 VAL B 223 6971 10471 9452 -591 -427 -388 C ATOM 1287 CG2 VAL B 223 26.008 50.928 19.924 1.00 72.99 C ANISOU 1287 CG2 VAL B 223 7015 10961 9755 -723 -358 -281 C ATOM 1288 N SER B 224 24.941 53.983 20.292 1.00 66.60 N ANISOU 1288 N SER B 224 6188 9773 9343 -955 -388 -79 N ATOM 1289 CA SER B 224 24.365 54.894 19.315 1.00 71.68 C ANISOU 1289 CA SER B 224 6826 10368 10041 -1033 -350 107 C ATOM 1290 C SER B 224 24.786 54.465 17.915 1.00 72.07 C ANISOU 1290 C SER B 224 6822 10618 9943 -1022 -275 224 C ATOM 1291 O SER B 224 25.583 53.541 17.757 1.00 68.67 O ANISOU 1291 O SER B 224 6351 10353 9389 -967 -259 153 O ATOM 1292 CB SER B 224 24.825 56.328 19.590 1.00 78.28 C ANISOU 1292 CB SER B 224 7568 11080 11097 -1163 -345 174 C ATOM 1293 OG SER B 224 24.242 57.243 18.679 1.00 82.84 O ANISOU 1293 OG SER B 224 8144 11597 11734 -1233 -303 366 O ATOM 1294 N GLY B 225 24.244 55.133 16.902 1.00 83.43 N ANISOU 1294 N GLY B 225 8258 12050 11392 -1064 -231 401 N ATOM 1295 CA GLY B 225 24.602 54.846 15.526 1.00 83.58 C ANISOU 1295 CA GLY B 225 8214 12269 11272 -1048 -158 528 C ATOM 1296 C GLY B 225 23.803 53.713 14.919 1.00 80.88 C ANISOU 1296 C GLY B 225 7956 12041 10735 -926 -163 491 C ATOM 1297 O GLY B 225 24.101 53.256 13.816 1.00 82.94 O ANISOU 1297 O GLY B 225 8162 12496 10855 -886 -113 561 O ATOM 1298 N LEU B 226 22.786 53.255 15.641 1.00 67.18 N ANISOU 1298 N LEU B 226 6344 10186 8996 -863 -223 377 N ATOM 1299 CA LEU B 226 21.915 52.203 15.137 1.00 68.28 C ANISOU 1299 CA LEU B 226 6562 10406 8976 -749 -229 326 C ATOM 1300 C LEU B 226 21.196 52.666 13.878 1.00 73.33 C ANISOU 1300 C LEU B 226 7199 11104 9560 -746 -186 488 C ATOM 1301 O LEU B 226 21.237 53.845 13.529 1.00 77.78 O ANISOU 1301 O LEU B 226 7721 11611 10222 -831 -155 645 O ATOM 1302 CB LEU B 226 20.904 51.770 16.199 1.00 68.05 C ANISOU 1302 CB LEU B 226 6663 10212 8980 -695 -294 185 C ATOM 1303 CG LEU B 226 21.417 50.791 17.256 1.00 67.63 C ANISOU 1303 CG LEU B 226 6632 10160 8905 -635 -329 5 C ATOM 1304 CD1 LEU B 226 20.302 50.406 18.209 1.00 65.24 C ANISOU 1304 CD1 LEU B 226 6458 9698 8633 -576 -382 -107 C ATOM 1305 CD2 LEU B 226 21.996 49.558 16.588 1.00 68.05 C ANISOU 1305 CD2 LEU B 226 6644 10421 8792 -551 -297 -49 C ATOM 1306 N ARG B 227 20.534 51.731 13.206 1.00 90.15 N ANISOU 1306 N ARG B 227 9369 13347 11537 -641 -181 445 N ATOM 1307 CA ARG B 227 19.894 52.006 11.926 1.00 91.72 C ANISOU 1307 CA ARG B 227 9553 13648 11649 -608 -139 580 C ATOM 1308 C ARG B 227 18.425 51.599 11.944 1.00 89.98 C ANISOU 1308 C ARG B 227 9449 13354 11386 -530 -174 506 C ATOM 1309 O ARG B 227 18.087 50.449 11.652 1.00 88.85 O ANISOU 1309 O ARG B 227 9326 13314 11120 -427 -181 390 O ATOM 1310 CB ARG B 227 20.645 51.280 10.809 1.00 99.07 C ANISOU 1310 CB ARG B 227 10379 14849 12412 -547 -90 605 C ATOM 1311 CG ARG B 227 20.028 51.404 9.428 1.00109.86 C ANISOU 1311 CG ARG B 227 11717 16368 13659 -484 -46 728 C ATOM 1312 CD ARG B 227 20.906 50.696 8.410 1.00116.77 C ANISOU 1312 CD ARG B 227 12473 17523 14373 -423 -4 743 C ATOM 1313 NE ARG B 227 21.372 49.403 8.908 1.00118.70 N ANISOU 1313 NE ARG B 227 12721 17824 14556 -365 -39 546 N ATOM 1314 CZ ARG B 227 22.302 48.663 8.313 1.00118.54 C ANISOU 1314 CZ ARG B 227 12600 18026 14413 -318 -18 516 C ATOM 1315 NH1 ARG B 227 22.872 49.089 7.194 1.00121.70 N ANISOU 1315 NH1 ARG B 227 12885 18621 14734 -323 40 673 N ATOM 1316 NH2 ARG B 227 22.664 47.500 8.836 1.00113.31 N ANISOU 1316 NH2 ARG B 227 11952 17393 13707 -263 -53 334 N ATOM 1317 N GLN B 228 17.562 52.551 12.293 1.00 92.33 N ANISOU 1317 N GLN B 228 9818 13469 11796 -579 -197 568 N ATOM 1318 CA GLN B 228 16.124 52.310 12.393 1.00 89.53 C ANISOU 1318 CA GLN B 228 9575 13023 11418 -516 -233 499 C ATOM 1319 C GLN B 228 15.796 51.072 13.218 1.00 81.03 C ANISOU 1319 C GLN B 228 8572 11904 10311 -445 -277 289 C ATOM 1320 O GLN B 228 15.291 50.089 12.688 1.00 79.11 O ANISOU 1320 O GLN B 228 8344 11765 9949 -346 -270 204 O ATOM 1321 CB GLN B 228 15.486 52.203 11.004 1.00 96.20 C ANISOU 1321 CB GLN B 228 10398 14033 12122 -437 -192 579 C ATOM 1322 CG GLN B 228 15.172 53.551 10.359 1.00103.39 C ANISOU 1322 CG GLN B 228 11292 14913 13080 -489 -159 786 C ATOM 1323 CD GLN B 228 14.728 53.443 8.902 1.00107.61 C ANISOU 1323 CD GLN B 228 11780 15653 13453 -395 -109 878 C ATOM 1324 OE1 GLN B 228 15.197 54.196 8.045 1.00109.75 O ANISOU 1324 OE1 GLN B 228 11969 16026 13705 -418 -49 1068 O ATOM 1325 NE2 GLN B 228 13.827 52.507 8.616 1.00108.58 N ANISOU 1325 NE2 GLN B 228 11949 15843 13462 -284 -131 742 N ATOM 1326 N PRO B 229 16.083 51.120 14.527 1.00 62.44 N ANISOU 1326 N PRO B 229 6258 9396 8071 -488 -320 203 N ATOM 1327 CA PRO B 229 15.767 50.006 15.427 1.00 56.11 C ANISOU 1327 CA PRO B 229 5531 8536 7254 -418 -355 19 C ATOM 1328 C PRO B 229 14.261 49.898 15.649 1.00 47.78 C ANISOU 1328 C PRO B 229 4590 7355 6210 -375 -386 -40 C ATOM 1329 O PRO B 229 13.573 50.918 15.635 1.00 49.24 O ANISOU 1329 O PRO B 229 4812 7431 6465 -426 -404 45 O ATOM 1330 CB PRO B 229 16.461 50.403 16.741 1.00 57.77 C ANISOU 1330 CB PRO B 229 5742 8616 7591 -481 -391 -23 C ATOM 1331 CG PRO B 229 17.417 51.506 16.376 1.00 60.15 C ANISOU 1331 CG PRO B 229 5941 8953 7960 -582 -365 120 C ATOM 1332 CD PRO B 229 16.775 52.212 15.229 1.00 61.43 C ANISOU 1332 CD PRO B 229 6094 9151 8093 -599 -333 272 C ATOM 1333 N VAL B 230 13.755 48.685 15.847 1.00 43.66 N ANISOU 1333 N VAL B 230 4120 6842 5625 -283 -390 -184 N ATOM 1334 CA VAL B 230 12.325 48.488 16.066 1.00 43.72 C ANISOU 1334 CA VAL B 230 4231 6734 5645 -240 -415 -255 C ATOM 1335 C VAL B 230 12.030 47.695 17.336 1.00 42.86 C ANISOU 1335 C VAL B 230 4203 6493 5587 -200 -443 -404 C ATOM 1336 O VAL B 230 10.892 47.673 17.810 1.00 46.46 O ANISOU 1336 O VAL B 230 4751 6817 6084 -181 -469 -461 O ATOM 1337 CB VAL B 230 11.662 47.778 14.871 1.00 44.46 C ANISOU 1337 CB VAL B 230 4309 6969 5615 -154 -382 -288 C ATOM 1338 CG1 VAL B 230 12.019 48.481 13.574 1.00 45.79 C ANISOU 1338 CG1 VAL B 230 4387 7298 5712 -173 -347 -135 C ATOM 1339 CG2 VAL B 230 12.082 46.320 14.826 1.00 43.20 C ANISOU 1339 CG2 VAL B 230 4121 6910 5383 -68 -359 -423 C ATOM 1340 N GLY B 231 13.052 47.043 17.880 1.00 48.53 N ANISOU 1340 N GLY B 231 4886 7252 6299 -181 -435 -463 N ATOM 1341 CA GLY B 231 12.889 46.242 19.079 1.00 43.97 C ANISOU 1341 CA GLY B 231 4378 6567 5762 -128 -451 -591 C ATOM 1342 C GLY B 231 14.141 45.469 19.439 1.00 45.74 C ANISOU 1342 C GLY B 231 4546 6880 5951 -92 -432 -645 C ATOM 1343 O GLY B 231 14.978 45.191 18.582 1.00 49.93 O ANISOU 1343 O GLY B 231 4990 7579 6402 -86 -401 -616 O ATOM 1344 N ALA B 232 14.274 45.127 20.716 1.00 46.21 N ANISOU 1344 N ALA B 232 4656 6838 6065 -62 -451 -724 N ATOM 1345 CA ALA B 232 15.413 44.346 21.186 1.00 45.34 C ANISOU 1345 CA ALA B 232 4504 6805 5920 -12 -435 -786 C ATOM 1346 C ALA B 232 14.943 43.174 22.038 1.00 47.38 C ANISOU 1346 C ALA B 232 4841 6982 6179 92 -422 -905 C ATOM 1347 O ALA B 232 14.019 43.305 22.836 1.00 50.22 O ANISOU 1347 O ALA B 232 5285 7190 6605 104 -443 -933 O ATOM 1348 CB ALA B 232 16.375 45.224 21.971 1.00 45.68 C ANISOU 1348 CB ALA B 232 4502 6827 6029 -74 -467 -752 C ATOM 1349 N LEU B 233 15.579 42.023 21.856 1.00 44.04 N ANISOU 1349 N LEU B 233 4387 6660 5686 168 -384 -972 N ATOM 1350 CA LEU B 233 15.208 40.823 22.595 1.00 43.23 C ANISOU 1350 CA LEU B 233 4353 6485 5589 274 -357 -1076 C ATOM 1351 C LEU B 233 16.415 39.925 22.841 1.00 48.40 C ANISOU 1351 C LEU B 233 4960 7245 6186 344 -332 -1129 C ATOM 1352 O LEU B 233 17.514 40.198 22.357 1.00 50.31 O ANISOU 1352 O LEU B 233 5114 7628 6376 308 -336 -1094 O ATOM 1353 CB LEU B 233 14.115 40.043 21.857 1.00 41.80 C ANISOU 1353 CB LEU B 233 4206 6284 5393 319 -323 -1127 C ATOM 1354 CG LEU B 233 14.319 39.797 20.359 1.00 45.09 C ANISOU 1354 CG LEU B 233 4539 6869 5725 314 -302 -1116 C ATOM 1355 CD1 LEU B 233 13.651 38.503 19.929 1.00 44.40 C ANISOU 1355 CD1 LEU B 233 4465 6782 5623 405 -259 -1225 C ATOM 1356 CD2 LEU B 233 13.807 40.973 19.536 1.00 47.09 C ANISOU 1356 CD2 LEU B 233 4772 7143 5976 228 -327 -1018 C ATOM 1357 N HIS B 234 16.200 38.852 23.595 1.00 54.90 N ANISOU 1357 N HIS B 234 5841 7998 7019 446 -301 -1212 N ATOM 1358 CA HIS B 234 17.270 37.914 23.920 1.00 54.73 C ANISOU 1358 CA HIS B 234 5787 8063 6943 530 -274 -1268 C ATOM 1359 C HIS B 234 16.926 36.506 23.447 1.00 55.78 C ANISOU 1359 C HIS B 234 5934 8209 7052 622 -219 -1347 C ATOM 1360 O HIS B 234 15.783 36.223 23.081 1.00 47.71 O ANISOU 1360 O HIS B 234 4954 7104 6069 628 -200 -1371 O ATOM 1361 CB HIS B 234 17.535 37.906 25.427 1.00 53.68 C ANISOU 1361 CB HIS B 234 5705 7843 6848 589 -283 -1291 C ATOM 1362 CG HIS B 234 16.379 37.413 26.240 1.00 55.98 C ANISOU 1362 CG HIS B 234 6101 7964 7205 655 -260 -1324 C ATOM 1363 ND1 HIS B 234 16.269 36.106 26.665 1.00 58.51 N ANISOU 1363 ND1 HIS B 234 6465 8244 7523 774 -202 -1388 N ATOM 1364 CD2 HIS B 234 15.279 38.053 26.708 1.00 56.60 C ANISOU 1364 CD2 HIS B 234 6247 7900 7357 619 -284 -1300 C ATOM 1365 CE1 HIS B 234 15.153 35.961 27.357 1.00 60.84 C ANISOU 1365 CE1 HIS B 234 6848 8379 7890 808 -185 -1396 C ATOM 1366 NE2 HIS B 234 14.535 37.128 27.398 1.00 60.24 N ANISOU 1366 NE2 HIS B 234 6788 8244 7856 715 -238 -1348 N ATOM 1367 N SER B 235 17.923 35.626 23.460 1.00 64.96 N ANISOU 1367 N SER B 235 7054 9473 8155 695 -194 -1396 N ATOM 1368 CA SER B 235 17.729 34.249 23.029 1.00 67.55 C ANISOU 1368 CA SER B 235 7382 9816 8470 786 -142 -1480 C ATOM 1369 C SER B 235 17.379 33.343 24.203 1.00 65.49 C ANISOU 1369 C SER B 235 7208 9409 8268 895 -97 -1530 C ATOM 1370 O SER B 235 16.529 32.460 24.091 1.00 63.93 O ANISOU 1370 O SER B 235 7050 9118 8123 950 -50 -1587 O ATOM 1371 CB SER B 235 18.982 33.729 22.323 1.00 71.51 C ANISOU 1371 CB SER B 235 7785 10511 8874 812 -138 -1508 C ATOM 1372 OG SER B 235 20.129 33.897 23.137 1.00 71.60 O ANISOU 1372 OG SER B 235 7782 10575 8848 834 -153 -1498 O ATOM 1373 N GLY B 236 18.041 33.568 25.331 1.00 62.81 N ANISOU 1373 N GLY B 236 6892 9053 7920 930 -109 -1511 N ATOM 1374 CA GLY B 236 17.852 32.726 26.494 1.00 62.96 C ANISOU 1374 CA GLY B 236 6987 8958 7979 1049 -62 -1544 C ATOM 1375 C GLY B 236 18.706 31.479 26.382 1.00 62.49 C ANISOU 1375 C GLY B 236 6896 8982 7868 1156 -16 -1605 C ATOM 1376 O GLY B 236 18.196 30.357 26.418 1.00 64.32 O ANISOU 1376 O GLY B 236 7165 9129 8146 1239 47 -1654 O ATOM 1377 N ASP B 237 20.011 31.680 26.232 1.00 62.83 N ANISOU 1377 N ASP B 237 6865 9187 7819 1151 -46 -1605 N ATOM 1378 CA ASP B 237 20.952 30.573 26.122 1.00 63.52 C ANISOU 1378 CA ASP B 237 6916 9374 7843 1251 -13 -1665 C ATOM 1379 C ASP B 237 22.204 30.842 26.951 1.00 65.65 C ANISOU 1379 C ASP B 237 7161 9741 8040 1295 -36 -1662 C ATOM 1380 O ASP B 237 23.227 30.176 26.786 1.00 64.43 O ANISOU 1380 O ASP B 237 6959 9712 7809 1360 -26 -1707 O ATOM 1381 CB ASP B 237 21.319 30.311 24.656 1.00 63.26 C ANISOU 1381 CB ASP B 237 6790 9492 7755 1204 -24 -1697 C ATOM 1382 CG ASP B 237 21.940 31.520 23.981 1.00 60.26 C ANISOU 1382 CG ASP B 237 6328 9257 7313 1080 -86 -1643 C ATOM 1383 OD1 ASP B 237 22.093 32.564 24.649 1.00 56.75 O ANISOU 1383 OD1 ASP B 237 5897 8785 6882 1024 -122 -1587 O ATOM 1384 OD2 ASP B 237 22.275 31.424 22.780 1.00 60.37 O ANISOU 1384 OD2 ASP B 237 6257 9412 7269 1041 -97 -1656 O ATOM 1385 N GLY B 238 22.114 31.827 27.839 1.00 52.27 N ANISOU 1385 N GLY B 238 5494 7995 6370 1264 -71 -1618 N ATOM 1386 CA GLY B 238 23.202 32.144 28.747 1.00 48.93 C ANISOU 1386 CA GLY B 238 5045 7657 5889 1315 -96 -1630 C ATOM 1387 C GLY B 238 24.222 33.101 28.166 1.00 51.81 C ANISOU 1387 C GLY B 238 5305 8183 6197 1207 -155 -1620 C ATOM 1388 O GLY B 238 25.152 33.515 28.857 1.00 49.71 O ANISOU 1388 O GLY B 238 5000 7996 5891 1233 -183 -1641 O ATOM 1389 N SER B 239 24.048 33.454 26.896 1.00 68.43 N ANISOU 1389 N SER B 239 7358 10342 8301 1093 -171 -1591 N ATOM 1390 CA SER B 239 24.987 34.335 26.208 1.00 69.25 C ANISOU 1390 CA SER B 239 7356 10600 8357 985 -215 -1568 C ATOM 1391 C SER B 239 24.716 35.799 26.521 1.00 67.79 C ANISOU 1391 C SER B 239 7161 10354 8242 870 -262 -1506 C ATOM 1392 O SER B 239 25.558 36.660 26.282 1.00 71.60 O ANISOU 1392 O SER B 239 7557 10939 8708 787 -296 -1486 O ATOM 1393 CB SER B 239 24.921 34.114 24.698 1.00 70.49 C ANISOU 1393 CB SER B 239 7453 10853 8475 921 -207 -1553 C ATOM 1394 OG SER B 239 23.710 34.618 24.169 1.00 71.40 O ANISOU 1394 OG SER B 239 7603 10866 8660 842 -211 -1497 O ATOM 1395 N GLN B 240 23.526 36.071 27.045 1.00 55.30 N ANISOU 1395 N GLN B 240 5665 8602 6745 866 -263 -1478 N ATOM 1396 CA GLN B 240 23.124 37.431 27.390 1.00 54.64 C ANISOU 1396 CA GLN B 240 5580 8440 6741 764 -311 -1424 C ATOM 1397 C GLN B 240 23.369 38.397 26.233 1.00 54.45 C ANISOU 1397 C GLN B 240 5472 8496 6721 616 -336 -1357 C ATOM 1398 O GLN B 240 23.586 39.596 26.443 1.00 54.13 O ANISOU 1398 O GLN B 240 5390 8442 6736 524 -377 -1317 O ATOM 1399 CB GLN B 240 23.859 37.917 28.640 1.00 56.88 C ANISOU 1399 CB GLN B 240 5842 8736 7034 806 -343 -1462 C ATOM 1400 CG GLN B 240 23.497 37.134 29.897 1.00 56.44 C ANISOU 1400 CG GLN B 240 5872 8593 6978 959 -318 -1510 C ATOM 1401 CD GLN B 240 24.261 37.628 31.106 1.00 53.29 C ANISOU 1401 CD GLN B 240 5437 8234 6576 1016 -353 -1558 C ATOM 1402 OE1 GLN B 240 24.374 38.835 31.335 1.00 51.12 O ANISOU 1402 OE1 GLN B 240 5113 7950 6362 926 -408 -1547 O ATOM 1403 NE2 GLN B 240 24.783 36.699 31.893 1.00 51.04 N ANISOU 1403 NE2 GLN B 240 5173 7996 6224 1172 -322 -1616 N ATOM 1404 N ARG B 241 23.331 37.878 25.010 1.00 43.32 N ANISOU 1404 N ARG B 241 4033 7170 5256 599 -310 -1343 N ATOM 1405 CA ARG B 241 23.432 38.728 23.834 1.00 46.76 C ANISOU 1405 CA ARG B 241 4394 7686 5688 473 -324 -1263 C ATOM 1406 C ARG B 241 22.137 39.512 23.669 1.00 42.03 C ANISOU 1406 C ARG B 241 3852 6945 5174 399 -339 -1195 C ATOM 1407 O ARG B 241 21.062 39.029 24.019 1.00 41.67 O ANISOU 1407 O ARG B 241 3897 6771 5164 452 -326 -1221 O ATOM 1408 CB ARG B 241 23.727 37.885 22.592 1.00 43.05 C ANISOU 1408 CB ARG B 241 3870 7364 5123 497 -293 -1276 C ATOM 1409 CG ARG B 241 25.048 37.140 22.658 1.00 45.74 C ANISOU 1409 CG ARG B 241 4148 7859 5373 565 -283 -1343 C ATOM 1410 CD ARG B 241 25.258 36.253 21.441 1.00 45.31 C ANISOU 1410 CD ARG B 241 4039 7950 5228 597 -259 -1368 C ATOM 1411 NE ARG B 241 24.307 35.148 21.403 1.00 45.58 N ANISOU 1411 NE ARG B 241 4147 7895 5277 689 -228 -1427 N ATOM 1412 CZ ARG B 241 24.214 34.278 20.402 1.00 45.93 C ANISOU 1412 CZ ARG B 241 4152 8033 5265 731 -208 -1469 C ATOM 1413 NH1 ARG B 241 23.318 33.301 20.449 1.00 44.39 N ANISOU 1413 NH1 ARG B 241 4020 7737 5108 812 -177 -1534 N ATOM 1414 NH2 ARG B 241 25.016 34.386 19.351 1.00 44.78 N ANISOU 1414 NH2 ARG B 241 3897 8086 5031 695 -217 -1451 N ATOM 1415 N LEU B 242 22.245 40.728 23.149 1.00 47.77 N ANISOU 1415 N LEU B 242 4522 7693 5936 278 -363 -1107 N ATOM 1416 CA LEU B 242 21.076 41.565 22.934 1.00 50.83 C ANISOU 1416 CA LEU B 242 4958 7955 6399 205 -380 -1037 C ATOM 1417 C LEU B 242 20.853 41.777 21.440 1.00 56.64 C ANISOU 1417 C LEU B 242 5643 8789 7089 146 -361 -959 C ATOM 1418 O LEU B 242 21.583 42.529 20.791 1.00 58.55 O ANISOU 1418 O LEU B 242 5794 9134 7318 65 -362 -882 O ATOM 1419 CB LEU B 242 21.227 42.905 23.656 1.00 50.87 C ANISOU 1419 CB LEU B 242 4947 7876 6505 119 -424 -992 C ATOM 1420 CG LEU B 242 19.939 43.713 23.843 1.00 57.61 C ANISOU 1420 CG LEU B 242 5873 8563 7452 66 -452 -942 C ATOM 1421 CD1 LEU B 242 18.838 42.842 24.431 1.00 56.35 C ANISOU 1421 CD1 LEU B 242 5828 8287 7296 161 -443 -1009 C ATOM 1422 CD2 LEU B 242 20.188 44.934 24.714 1.00 60.16 C ANISOU 1422 CD2 LEU B 242 6172 8803 7884 -3 -501 -923 C ATOM 1423 N PHE B 243 19.847 41.095 20.899 1.00 49.58 N ANISOU 1423 N PHE B 243 4801 7868 6170 194 -340 -983 N ATOM 1424 CA PHE B 243 19.556 41.140 19.472 1.00 50.24 C ANISOU 1424 CA PHE B 243 4834 8063 6193 168 -321 -929 C ATOM 1425 C PHE B 243 18.727 42.366 19.101 1.00 53.18 C ANISOU 1425 C PHE B 243 5224 8358 6625 77 -339 -823 C ATOM 1426 O PHE B 243 17.638 42.575 19.635 1.00 57.08 O ANISOU 1426 O PHE B 243 5807 8692 7187 78 -356 -836 O ATOM 1427 CB PHE B 243 18.834 39.863 19.047 1.00 48.35 C ANISOU 1427 CB PHE B 243 4629 7832 5908 267 -292 -1021 C ATOM 1428 CG PHE B 243 19.651 38.617 19.236 1.00 52.26 C ANISOU 1428 CG PHE B 243 5099 8413 6344 360 -270 -1119 C ATOM 1429 CD1 PHE B 243 19.698 37.985 20.466 1.00 52.37 C ANISOU 1429 CD1 PHE B 243 5182 8316 6398 431 -265 -1195 C ATOM 1430 CD2 PHE B 243 20.374 38.080 18.184 1.00 56.71 C ANISOU 1430 CD2 PHE B 243 5566 9175 6808 385 -253 -1133 C ATOM 1431 CE1 PHE B 243 20.453 36.837 20.643 1.00 55.80 C ANISOU 1431 CE1 PHE B 243 5596 8826 6778 525 -241 -1279 C ATOM 1432 CE2 PHE B 243 21.130 36.934 18.354 1.00 57.14 C ANISOU 1432 CE2 PHE B 243 5597 9307 6809 474 -236 -1227 C ATOM 1433 CZ PHE B 243 21.168 36.312 19.585 1.00 58.84 C ANISOU 1433 CZ PHE B 243 5888 9401 7069 543 -229 -1299 C ATOM 1434 N ILE B 244 19.246 43.167 18.175 1.00 47.14 N ANISOU 1434 N ILE B 244 4371 7710 5831 2 -332 -715 N ATOM 1435 CA ILE B 244 18.586 44.402 17.768 1.00 46.80 C ANISOU 1435 CA ILE B 244 4335 7603 5843 -84 -344 -596 C ATOM 1436 C ILE B 244 17.985 44.291 16.368 1.00 54.16 C ANISOU 1436 C ILE B 244 5236 8650 6692 -64 -317 -546 C ATOM 1437 O ILE B 244 18.707 44.141 15.381 1.00 59.61 O ANISOU 1437 O ILE B 244 5829 9528 7291 -59 -289 -503 O ATOM 1438 CB ILE B 244 19.568 45.587 17.794 1.00 44.65 C ANISOU 1438 CB ILE B 244 3982 7358 5624 -190 -349 -488 C ATOM 1439 CG1 ILE B 244 20.384 45.573 19.088 1.00 44.73 C ANISOU 1439 CG1 ILE B 244 3994 7306 5698 -193 -374 -561 C ATOM 1440 CG2 ILE B 244 18.822 46.902 17.631 1.00 44.81 C ANISOU 1440 CG2 ILE B 244 4025 7265 5733 -277 -363 -370 C ATOM 1441 CD1 ILE B 244 21.347 46.735 19.217 1.00 46.32 C ANISOU 1441 CD1 ILE B 244 4106 7518 5974 -299 -380 -480 C ATOM 1442 N LEU B 245 16.660 44.365 16.286 1.00 61.25 N ANISOU 1442 N LEU B 245 6213 9445 7616 -46 -326 -558 N ATOM 1443 CA LEU B 245 15.973 44.336 15.000 1.00 54.26 C ANISOU 1443 CA LEU B 245 5299 8665 6652 -17 -304 -520 C ATOM 1444 C LEU B 245 16.038 45.694 14.317 1.00 56.80 C ANISOU 1444 C LEU B 245 5575 9022 6985 -102 -299 -348 C ATOM 1445 O LEU B 245 15.798 46.727 14.945 1.00 59.93 O ANISOU 1445 O LEU B 245 6015 9267 7487 -180 -323 -279 O ATOM 1446 CB LEU B 245 14.513 43.915 15.173 1.00 46.13 C ANISOU 1446 CB LEU B 245 4367 7514 5647 37 -315 -607 C ATOM 1447 CG LEU B 245 14.228 42.415 15.128 1.00 46.44 C ANISOU 1447 CG LEU B 245 4418 7587 5642 145 -296 -766 C ATOM 1448 CD1 LEU B 245 15.054 41.679 16.169 1.00 46.64 C ANISOU 1448 CD1 LEU B 245 4459 7567 5696 170 -296 -845 C ATOM 1449 CD2 LEU B 245 12.744 42.151 15.324 1.00 46.11 C ANISOU 1449 CD2 LEU B 245 4468 7408 5644 184 -302 -845 C ATOM 1450 N GLU B 246 16.362 45.688 13.028 1.00 62.52 N ANISOU 1450 N GLU B 246 6205 9947 7603 -81 -264 -277 N ATOM 1451 CA GLU B 246 16.431 46.922 12.256 1.00 59.53 C ANISOU 1451 CA GLU B 246 5775 9618 7226 -148 -244 -96 C ATOM 1452 C GLU B 246 15.425 46.929 11.111 1.00 59.06 C ANISOU 1452 C GLU B 246 5710 9653 7078 -84 -227 -64 C ATOM 1453 O GLU B 246 15.354 45.983 10.326 1.00 58.90 O ANISOU 1453 O GLU B 246 5640 9798 6941 11 -211 -141 O ATOM 1454 CB GLU B 246 17.849 47.152 11.736 1.00 54.01 C ANISOU 1454 CB GLU B 246 4952 9088 6481 -188 -211 -2 C ATOM 1455 CG GLU B 246 18.831 47.563 12.820 1.00 50.60 C ANISOU 1455 CG GLU B 246 4514 8554 6158 -273 -227 -2 C ATOM 1456 CD GLU B 246 20.227 47.799 12.284 1.00 55.99 C ANISOU 1456 CD GLU B 246 5068 9405 6799 -316 -190 84 C ATOM 1457 OE1 GLU B 246 20.844 48.817 12.660 1.00 59.86 O ANISOU 1457 OE1 GLU B 246 5524 9824 7395 -418 -184 178 O ATOM 1458 OE2 GLU B 246 20.706 46.970 11.484 1.00 60.34 O ANISOU 1458 OE2 GLU B 246 5547 10161 7218 -247 -167 52 O ATOM 1459 N LYS B 247 14.652 48.007 11.031 1.00 62.40 N ANISOU 1459 N LYS B 247 6179 9972 7556 -130 -233 44 N ATOM 1460 CA LYS B 247 13.596 48.158 10.033 1.00 67.95 C ANISOU 1460 CA LYS B 247 6888 10750 8181 -66 -220 78 C ATOM 1461 C LYS B 247 13.999 47.628 8.658 1.00 69.67 C ANISOU 1461 C LYS B 247 6986 11247 8237 20 -177 100 C ATOM 1462 O LYS B 247 13.281 46.826 8.064 1.00 68.52 O ANISOU 1462 O LYS B 247 6834 11198 8001 125 -178 -10 O ATOM 1463 CB LYS B 247 13.196 49.631 9.925 1.00 70.07 C ANISOU 1463 CB LYS B 247 7182 10920 8521 -143 -216 254 C ATOM 1464 CG LYS B 247 11.898 49.899 9.177 1.00 65.56 C ANISOU 1464 CG LYS B 247 6649 10371 7890 -78 -214 276 C ATOM 1465 CD LYS B 247 10.689 49.560 10.027 1.00 63.10 C ANISOU 1465 CD LYS B 247 6463 9871 7643 -59 -264 126 C ATOM 1466 CE LYS B 247 9.586 50.598 9.853 1.00 65.92 C ANISOU 1466 CE LYS B 247 6885 10130 8032 -74 -278 214 C ATOM 1467 NZ LYS B 247 9.315 50.923 8.424 1.00 68.68 N ANISOU 1467 NZ LYS B 247 7167 10678 8251 -2 -234 324 N ATOM 1468 N GLU B 248 15.149 48.077 8.161 1.00 71.73 N ANISOU 1468 N GLU B 248 7145 11641 8466 -23 -141 236 N ATOM 1469 CA GLU B 248 15.608 47.720 6.819 1.00 74.50 C ANISOU 1469 CA GLU B 248 7372 12277 8659 57 -99 284 C ATOM 1470 C GLU B 248 15.627 46.214 6.560 1.00 73.81 C ANISOU 1470 C GLU B 248 7247 12326 8471 170 -113 86 C ATOM 1471 O GLU B 248 15.393 45.768 5.438 1.00 79.07 O ANISOU 1471 O GLU B 248 7834 13206 9003 274 -95 66 O ATOM 1472 CB GLU B 248 16.990 48.318 6.539 1.00 81.89 C ANISOU 1472 CB GLU B 248 8205 13318 9593 -17 -59 441 C ATOM 1473 CG GLU B 248 16.986 49.820 6.296 1.00 89.83 C ANISOU 1473 CG GLU B 248 9202 14261 10669 -103 -23 670 C ATOM 1474 CD GLU B 248 18.331 50.332 5.813 1.00 96.99 C ANISOU 1474 CD GLU B 248 9987 15304 11562 -163 32 828 C ATOM 1475 OE1 GLU B 248 18.406 51.507 5.397 1.00100.49 O ANISOU 1475 OE1 GLU B 248 10399 15731 12050 -221 78 1034 O ATOM 1476 OE2 GLU B 248 19.313 49.559 5.848 1.00 97.38 O ANISOU 1476 OE2 GLU B 248 9967 15474 11558 -151 32 749 O ATOM 1477 N GLY B 249 15.914 45.434 7.597 1.00 68.46 N ANISOU 1477 N GLY B 249 6622 11529 7862 155 -143 -60 N ATOM 1478 CA GLY B 249 15.940 43.987 7.473 1.00 65.84 C ANISOU 1478 CA GLY B 249 6262 11293 7462 256 -153 -251 C ATOM 1479 C GLY B 249 17.198 43.354 8.035 1.00 66.65 C ANISOU 1479 C GLY B 249 6328 11422 7572 235 -157 -309 C ATOM 1480 O GLY B 249 17.617 42.284 7.592 1.00 67.23 O ANISOU 1480 O GLY B 249 6331 11654 7559 317 -155 -420 O ATOM 1481 N TYR B 250 17.800 44.016 9.017 1.00 59.56 N ANISOU 1481 N TYR B 250 5474 10376 6781 130 -165 -243 N ATOM 1482 CA TYR B 250 19.015 43.515 9.645 1.00 55.78 C ANISOU 1482 CA TYR B 250 4964 9917 6313 108 -170 -298 C ATOM 1483 C TYR B 250 18.770 43.151 11.107 1.00 57.08 C ANISOU 1483 C TYR B 250 5244 9849 6593 93 -202 -414 C ATOM 1484 O TYR B 250 17.826 43.640 11.729 1.00 59.34 O ANISOU 1484 O TYR B 250 5631 9943 6973 63 -221 -408 O ATOM 1485 CB TYR B 250 20.130 44.558 9.560 1.00 54.69 C ANISOU 1485 CB TYR B 250 4754 9831 6195 6 -148 -134 C ATOM 1486 CG TYR B 250 20.458 45.015 8.156 1.00 54.55 C ANISOU 1486 CG TYR B 250 4617 10044 6067 18 -106 10 C ATOM 1487 CD1 TYR B 250 21.469 44.405 7.426 1.00 59.66 C ANISOU 1487 CD1 TYR B 250 5144 10932 6593 63 -87 -3 C ATOM 1488 CD2 TYR B 250 19.764 46.064 7.565 1.00 54.93 C ANISOU 1488 CD2 TYR B 250 4671 10074 6127 -10 -84 164 C ATOM 1489 CE1 TYR B 250 21.778 44.823 6.142 1.00 65.64 C ANISOU 1489 CE1 TYR B 250 5786 11915 7241 82 -46 136 C ATOM 1490 CE2 TYR B 250 20.064 46.489 6.283 1.00 60.64 C ANISOU 1490 CE2 TYR B 250 5283 11017 6743 13 -37 309 C ATOM 1491 CZ TYR B 250 21.072 45.865 5.576 1.00 66.89 C ANISOU 1491 CZ TYR B 250 5952 12052 7411 59 -18 296 C ATOM 1492 OH TYR B 250 21.376 46.284 4.302 1.00 71.59 O ANISOU 1492 OH TYR B 250 6430 12879 7891 91 31 448 O ATOM 1493 N VAL B 251 19.626 42.290 11.650 1.00 61.85 N ANISOU 1493 N VAL B 251 5832 10482 7185 122 -208 -516 N ATOM 1494 CA VAL B 251 19.568 41.921 13.061 1.00 58.19 C ANISOU 1494 CA VAL B 251 5466 9824 6819 121 -232 -616 C ATOM 1495 C VAL B 251 20.973 41.917 13.655 1.00 55.57 C ANISOU 1495 C VAL B 251 5087 9536 6491 86 -234 -617 C ATOM 1496 O VAL B 251 21.743 40.983 13.441 1.00 58.45 O ANISOU 1496 O VAL B 251 5395 10038 6777 147 -227 -696 O ATOM 1497 CB VAL B 251 18.933 40.532 13.264 1.00 57.32 C ANISOU 1497 CB VAL B 251 5407 9678 6694 231 -233 -786 C ATOM 1498 CG1 VAL B 251 18.964 40.144 14.734 1.00 55.74 C ANISOU 1498 CG1 VAL B 251 5302 9290 6585 240 -248 -870 C ATOM 1499 CG2 VAL B 251 17.508 40.515 12.733 1.00 58.29 C ANISOU 1499 CG2 VAL B 251 5573 9751 6822 267 -231 -807 C ATOM 1500 N LYS B 252 21.304 42.967 14.398 1.00 57.06 N ANISOU 1500 N LYS B 252 5293 9610 6776 -8 -247 -539 N ATOM 1501 CA LYS B 252 22.632 43.101 14.987 1.00 61.86 C ANISOU 1501 CA LYS B 252 5848 10259 7399 -47 -250 -545 C ATOM 1502 C LYS B 252 22.719 42.430 16.359 1.00 63.57 C ANISOU 1502 C LYS B 252 6142 10346 7665 4 -275 -678 C ATOM 1503 O LYS B 252 21.722 42.329 17.076 1.00 63.62 O ANISOU 1503 O LYS B 252 6254 10179 7740 29 -292 -724 O ATOM 1504 CB LYS B 252 23.019 44.578 15.100 1.00 63.96 C ANISOU 1504 CB LYS B 252 6075 10473 7756 -172 -249 -407 C ATOM 1505 CG LYS B 252 23.122 45.307 13.769 1.00 70.12 C ANISOU 1505 CG LYS B 252 6765 11390 8488 -222 -213 -251 C ATOM 1506 CD LYS B 252 23.488 46.773 13.973 1.00 77.68 C ANISOU 1506 CD LYS B 252 7686 12264 9564 -349 -205 -114 C ATOM 1507 CE LYS B 252 23.712 47.488 12.647 1.00 80.28 C ANISOU 1507 CE LYS B 252 7918 12739 9846 -394 -155 60 C ATOM 1508 NZ LYS B 252 24.057 48.927 12.836 1.00 80.00 N ANISOU 1508 NZ LYS B 252 7842 12604 9948 -522 -139 201 N ATOM 1509 N ILE B 253 23.917 41.973 16.715 1.00 47.85 N ANISOU 1509 N ILE B 253 4099 8449 5635 26 -274 -737 N ATOM 1510 CA ILE B 253 24.156 41.362 18.019 1.00 49.89 C ANISOU 1510 CA ILE B 253 4419 8610 5927 87 -292 -854 C ATOM 1511 C ILE B 253 24.938 42.306 18.925 1.00 50.39 C ANISOU 1511 C ILE B 253 4455 8618 6072 14 -313 -832 C ATOM 1512 O ILE B 253 25.777 43.080 18.462 1.00 48.10 O ANISOU 1512 O ILE B 253 4067 8424 5785 -70 -304 -754 O ATOM 1513 CB ILE B 253 24.935 40.039 17.895 1.00 54.81 C ANISOU 1513 CB ILE B 253 5007 9375 6444 188 -279 -962 C ATOM 1514 CG1 ILE B 253 24.276 39.120 16.867 1.00 58.81 C ANISOU 1514 CG1 ILE B 253 5512 9960 6874 258 -259 -995 C ATOM 1515 CG2 ILE B 253 25.028 39.344 19.245 1.00 53.25 C ANISOU 1515 CG2 ILE B 253 4887 9068 6278 271 -289 -1074 C ATOM 1516 CD1 ILE B 253 24.949 37.770 16.749 1.00 61.82 C ANISOU 1516 CD1 ILE B 253 5859 10464 7163 364 -249 -1111 C ATOM 1517 N LEU B 254 24.664 42.231 20.222 1.00 61.34 N ANISOU 1517 N LEU B 254 5921 9856 7531 50 -337 -903 N ATOM 1518 CA LEU B 254 25.312 43.103 21.191 1.00 56.66 C ANISOU 1518 CA LEU B 254 5300 9204 7025 -4 -364 -908 C ATOM 1519 C LEU B 254 25.664 42.312 22.445 1.00 52.46 C ANISOU 1519 C LEU B 254 4814 8639 6480 104 -378 -1037 C ATOM 1520 O LEU B 254 24.778 41.884 23.181 1.00 54.37 O ANISOU 1520 O LEU B 254 5158 8749 6752 173 -386 -1083 O ATOM 1521 CB LEU B 254 24.383 44.268 21.541 1.00 57.45 C ANISOU 1521 CB LEU B 254 5447 9128 7254 -86 -390 -836 C ATOM 1522 CG LEU B 254 25.000 45.560 22.080 1.00 60.29 C ANISOU 1522 CG LEU B 254 5740 9439 7729 -187 -416 -801 C ATOM 1523 CD1 LEU B 254 24.032 46.719 21.916 1.00 58.40 C ANISOU 1523 CD1 LEU B 254 5531 9055 7603 -280 -432 -698 C ATOM 1524 CD2 LEU B 254 25.411 45.408 23.533 1.00 66.54 C ANISOU 1524 CD2 LEU B 254 6548 10171 8561 -125 -450 -921 C ATOM 1525 N THR B 255 26.957 42.109 22.681 1.00 63.35 N ANISOU 1525 N THR B 255 6115 10145 7812 124 -377 -1093 N ATOM 1526 CA THR B 255 27.402 41.379 23.864 1.00 68.76 C ANISOU 1526 CA THR B 255 6833 10821 8471 239 -387 -1213 C ATOM 1527 C THR B 255 26.981 42.109 25.134 1.00 73.40 C ANISOU 1527 C THR B 255 7467 11251 9172 236 -424 -1236 C ATOM 1528 O THR B 255 26.788 43.324 25.120 1.00 71.45 O ANISOU 1528 O THR B 255 7188 10933 9028 125 -448 -1173 O ATOM 1529 CB THR B 255 28.933 41.184 23.880 1.00 69.25 C ANISOU 1529 CB THR B 255 6792 11059 8462 255 -384 -1272 C ATOM 1530 OG1 THR B 255 29.581 42.461 23.922 1.00 71.70 O ANISOU 1530 OG1 THR B 255 7005 11383 8853 136 -401 -1233 O ATOM 1531 CG2 THR B 255 29.389 40.427 22.646 1.00 70.22 C ANISOU 1531 CG2 THR B 255 6863 11353 8466 267 -353 -1258 C ATOM 1532 N PRO B 256 26.838 41.367 26.240 1.00 64.62 N ANISOU 1532 N PRO B 256 6425 10086 8041 364 -428 -1327 N ATOM 1533 CA PRO B 256 26.427 41.967 27.512 1.00 62.91 C ANISOU 1533 CA PRO B 256 6248 9738 7918 384 -466 -1359 C ATOM 1534 C PRO B 256 27.269 43.192 27.857 1.00 64.81 C ANISOU 1534 C PRO B 256 6381 10007 8237 294 -504 -1370 C ATOM 1535 O PRO B 256 26.718 44.229 28.223 1.00 64.01 O ANISOU 1535 O PRO B 256 6282 9785 8252 221 -540 -1338 O ATOM 1536 CB PRO B 256 26.682 40.837 28.522 1.00 60.90 C ANISOU 1536 CB PRO B 256 6046 9504 7591 555 -452 -1461 C ATOM 1537 CG PRO B 256 27.594 39.871 27.795 1.00 61.52 C ANISOU 1537 CG PRO B 256 6079 9747 7548 601 -416 -1490 C ATOM 1538 CD PRO B 256 27.096 39.929 26.397 1.00 64.95 C ANISOU 1538 CD PRO B 256 6507 10194 7976 505 -396 -1402 C ATOM 1539 N GLU B 257 28.586 43.073 27.726 1.00 76.26 N ANISOU 1539 N GLU B 257 7732 11614 9630 298 -496 -1420 N ATOM 1540 CA GLU B 257 29.495 44.160 28.079 1.00 82.57 C ANISOU 1540 CA GLU B 257 8414 12449 10511 219 -526 -1451 C ATOM 1541 C GLU B 257 29.242 45.422 27.251 1.00 76.55 C ANISOU 1541 C GLU B 257 7595 11628 9864 44 -530 -1334 C ATOM 1542 O GLU B 257 29.542 46.532 27.695 1.00 72.99 O ANISOU 1542 O GLU B 257 7069 11127 9536 -34 -560 -1346 O ATOM 1543 CB GLU B 257 30.954 43.707 27.946 1.00 95.57 C ANISOU 1543 CB GLU B 257 9962 14288 12063 255 -510 -1527 C ATOM 1544 CG GLU B 257 31.275 42.421 28.706 1.00103.87 C ANISOU 1544 CG GLU B 257 11067 15408 12992 437 -501 -1636 C ATOM 1545 CD GLU B 257 32.751 42.054 28.665 1.00108.21 C ANISOU 1545 CD GLU B 257 11516 16151 13449 476 -493 -1725 C ATOM 1546 OE1 GLU B 257 33.593 42.910 29.011 1.00109.31 O ANISOU 1546 OE1 GLU B 257 11544 16339 13651 420 -517 -1778 O ATOM 1547 OE2 GLU B 257 33.070 40.902 28.298 1.00107.85 O ANISOU 1547 OE2 GLU B 257 11497 16207 13274 566 -463 -1749 O ATOM 1548 N GLY B 258 28.695 45.251 26.050 1.00 76.60 N ANISOU 1548 N GLY B 258 7632 11642 9832 -10 -496 -1222 N ATOM 1549 CA GLY B 258 28.334 46.382 25.212 1.00 74.29 C ANISOU 1549 CA GLY B 258 7300 11292 9636 -159 -491 -1092 C ATOM 1550 C GLY B 258 28.982 46.416 23.838 1.00 70.89 C ANISOU 1550 C GLY B 258 6783 11008 9143 -234 -445 -1002 C ATOM 1551 O GLY B 258 28.848 47.400 23.108 1.00 66.24 O ANISOU 1551 O GLY B 258 6146 10391 8633 -355 -430 -882 O ATOM 1552 N GLU B 259 29.686 45.347 23.479 1.00 68.32 N ANISOU 1552 N GLU B 259 6438 10844 8676 -156 -420 -1054 N ATOM 1553 CA GLU B 259 30.334 45.272 22.174 1.00 70.62 C ANISOU 1553 CA GLU B 259 6642 11301 8890 -211 -379 -977 C ATOM 1554 C GLU B 259 29.326 44.915 21.087 1.00 68.43 C ANISOU 1554 C GLU B 259 6425 11022 8552 -208 -354 -879 C ATOM 1555 O GLU B 259 28.389 44.153 21.325 1.00 66.32 O ANISOU 1555 O GLU B 259 6266 10680 8251 -121 -362 -919 O ATOM 1556 CB GLU B 259 31.479 44.251 22.186 1.00 75.76 C ANISOU 1556 CB GLU B 259 7243 12135 9407 -125 -368 -1081 C ATOM 1557 CG GLU B 259 32.296 44.221 20.895 1.00 80.22 C ANISOU 1557 CG GLU B 259 7699 12891 9888 -181 -330 -1011 C ATOM 1558 CD GLU B 259 33.340 43.115 20.873 1.00 82.69 C ANISOU 1558 CD GLU B 259 7972 13389 10058 -85 -325 -1120 C ATOM 1559 OE1 GLU B 259 33.226 42.168 21.680 1.00 81.67 O ANISOU 1559 OE1 GLU B 259 7919 13235 9876 41 -343 -1235 O ATOM 1560 OE2 GLU B 259 34.272 43.191 20.043 1.00 83.25 O ANISOU 1560 OE2 GLU B 259 7933 13631 10068 -134 -300 -1088 O ATOM 1561 N ILE B 260 29.520 45.472 19.896 1.00 59.61 N ANISOU 1561 N ILE B 260 5230 9993 7426 -298 -320 -754 N ATOM 1562 CA ILE B 260 28.656 45.175 18.759 1.00 56.35 C ANISOU 1562 CA ILE B 260 4852 9614 6943 -287 -296 -664 C ATOM 1563 C ILE B 260 29.414 44.346 17.719 1.00 55.73 C ANISOU 1563 C ILE B 260 4697 9767 6712 -245 -265 -667 C ATOM 1564 O ILE B 260 30.622 44.512 17.543 1.00 55.19 O ANISOU 1564 O ILE B 260 4521 9832 6617 -282 -251 -669 O ATOM 1565 CB ILE B 260 28.105 46.468 18.122 1.00 54.46 C ANISOU 1565 CB ILE B 260 4591 9301 6802 -406 -279 -501 C ATOM 1566 CG1 ILE B 260 26.920 46.156 17.207 1.00 54.86 C ANISOU 1566 CG1 ILE B 260 4705 9350 6789 -370 -265 -433 C ATOM 1567 CG2 ILE B 260 29.206 47.214 17.380 1.00 54.21 C ANISOU 1567 CG2 ILE B 260 4418 9400 6781 -504 -240 -401 C ATOM 1568 CD1 ILE B 260 26.203 47.388 16.700 1.00 55.64 C ANISOU 1568 CD1 ILE B 260 4805 9354 6981 -466 -252 -277 C ATOM 1569 N PHE B 261 28.704 43.449 17.041 1.00 65.67 N ANISOU 1569 N PHE B 261 6002 11076 7872 -165 -257 -678 N ATOM 1570 CA PHE B 261 29.330 42.525 16.097 1.00 71.08 C ANISOU 1570 CA PHE B 261 6617 11982 8407 -104 -237 -705 C ATOM 1571 C PHE B 261 29.521 43.115 14.701 1.00 71.97 C ANISOU 1571 C PHE B 261 6627 12246 8470 -170 -201 -560 C ATOM 1572 O PHE B 261 28.662 43.837 14.194 1.00 71.89 O ANISOU 1572 O PHE B 261 6639 12170 8508 -218 -187 -444 O ATOM 1573 CB PHE B 261 28.525 41.227 16.003 1.00 72.32 C ANISOU 1573 CB PHE B 261 6856 12131 8491 22 -245 -802 C ATOM 1574 CG PHE B 261 28.785 40.269 17.130 1.00 74.12 C ANISOU 1574 CG PHE B 261 7148 12302 8712 118 -265 -951 C ATOM 1575 CD1 PHE B 261 29.305 39.010 16.881 1.00 76.22 C ANISOU 1575 CD1 PHE B 261 7391 12705 8865 221 -261 -1053 C ATOM 1576 CD2 PHE B 261 28.515 40.628 18.439 1.00 73.81 C ANISOU 1576 CD2 PHE B 261 7187 12079 8779 114 -286 -989 C ATOM 1577 CE1 PHE B 261 29.546 38.126 17.917 1.00 76.18 C ANISOU 1577 CE1 PHE B 261 7447 12645 8854 319 -272 -1179 C ATOM 1578 CE2 PHE B 261 28.755 39.748 19.478 1.00 72.74 C ANISOU 1578 CE2 PHE B 261 7109 11902 8629 218 -298 -1115 C ATOM 1579 CZ PHE B 261 29.271 38.497 19.216 1.00 73.60 C ANISOU 1579 CZ PHE B 261 7200 12140 8626 321 -287 -1205 C ATOM 1580 N LYS B 262 30.655 42.789 14.087 1.00 82.10 N ANISOU 1580 N LYS B 262 7800 13743 9653 -164 -183 -566 N ATOM 1581 CA LYS B 262 30.976 43.248 12.741 1.00 86.11 C ANISOU 1581 CA LYS B 262 8195 14429 10092 -211 -143 -428 C ATOM 1582 C LYS B 262 30.062 42.621 11.693 1.00 79.20 C ANISOU 1582 C LYS B 262 7335 13641 9114 -130 -137 -410 C ATOM 1583 O LYS B 262 29.783 43.228 10.660 1.00 77.51 O ANISOU 1583 O LYS B 262 7066 13511 8874 -164 -104 -269 O ATOM 1584 CB LYS B 262 32.438 42.934 12.407 1.00 93.88 C ANISOU 1584 CB LYS B 262 9056 15631 10983 -213 -131 -459 C ATOM 1585 CG LYS B 262 33.454 43.812 13.125 1.00101.15 C ANISOU 1585 CG LYS B 262 9918 16507 12007 -315 -123 -446 C ATOM 1586 CD LYS B 262 33.848 45.020 12.282 1.00108.03 C ANISOU 1586 CD LYS B 262 10678 17442 12925 -437 -69 -260 C ATOM 1587 CE LYS B 262 32.671 45.952 12.031 1.00110.58 C ANISOU 1587 CE LYS B 262 11058 17606 13349 -492 -51 -116 C ATOM 1588 NZ LYS B 262 33.035 47.078 11.125 1.00112.46 N ANISOU 1588 NZ LYS B 262 11187 17913 13628 -598 12 83 N ATOM 1589 N GLU B 263 29.606 41.401 11.963 1.00 66.20 N ANISOU 1589 N GLU B 263 5758 11979 7415 -16 -165 -556 N ATOM 1590 CA GLU B 263 28.734 40.683 11.038 1.00 64.95 C ANISOU 1590 CA GLU B 263 5607 11902 7169 72 -164 -577 C ATOM 1591 C GLU B 263 27.320 40.550 11.591 1.00 58.37 C ANISOU 1591 C GLU B 263 4908 10850 6420 104 -180 -620 C ATOM 1592 O GLU B 263 27.129 40.074 12.709 1.00 54.97 O ANISOU 1592 O GLU B 263 4570 10262 6053 137 -202 -728 O ATOM 1593 CB GLU B 263 29.303 39.295 10.724 1.00 70.54 C ANISOU 1593 CB GLU B 263 6268 12783 7752 184 -178 -718 C ATOM 1594 CG GLU B 263 30.500 39.305 9.784 1.00 77.80 C ANISOU 1594 CG GLU B 263 7038 13973 8550 174 -163 -672 C ATOM 1595 CD GLU B 263 30.134 39.735 8.375 1.00 86.41 C ANISOU 1595 CD GLU B 263 8041 15227 9562 172 -135 -543 C ATOM 1596 OE1 GLU B 263 31.013 40.280 7.674 1.00 90.70 O ANISOU 1596 OE1 GLU B 263 8467 15949 10046 122 -107 -434 O ATOM 1597 OE2 GLU B 263 28.970 39.529 7.967 1.00 86.59 O ANISOU 1597 OE2 GLU B 263 8110 15207 9582 227 -138 -551 O ATOM 1598 N PRO B 264 26.324 40.976 10.802 1.00 52.80 N ANISOU 1598 N PRO B 264 4210 10141 5710 101 -167 -535 N ATOM 1599 CA PRO B 264 24.911 40.875 11.179 1.00 52.00 C ANISOU 1599 CA PRO B 264 4227 9851 5680 131 -180 -575 C ATOM 1600 C PRO B 264 24.522 39.440 11.504 1.00 51.11 C ANISOU 1600 C PRO B 264 4168 9711 5542 248 -197 -756 C ATOM 1601 O PRO B 264 25.069 38.507 10.919 1.00 54.13 O ANISOU 1601 O PRO B 264 4475 10271 5821 323 -197 -834 O ATOM 1602 CB PRO B 264 24.180 41.342 9.916 1.00 52.32 C ANISOU 1602 CB PRO B 264 4222 9993 5663 138 -159 -468 C ATOM 1603 CG PRO B 264 25.161 42.222 9.217 1.00 54.99 C ANISOU 1603 CG PRO B 264 4444 10490 5960 63 -128 -313 C ATOM 1604 CD PRO B 264 26.502 41.608 9.483 1.00 54.49 C ANISOU 1604 CD PRO B 264 4314 10544 5845 73 -134 -389 C ATOM 1605 N TYR B 265 23.589 39.270 12.432 1.00 51.10 N ANISOU 1605 N TYR B 265 4290 9489 5639 264 -211 -819 N ATOM 1606 CA TYR B 265 23.118 37.942 12.802 1.00 46.79 C ANISOU 1606 CA TYR B 265 3800 8885 5093 371 -216 -980 C ATOM 1607 C TYR B 265 22.083 37.452 11.799 1.00 49.25 C ANISOU 1607 C TYR B 265 4095 9255 5363 438 -208 -1023 C ATOM 1608 O TYR B 265 21.934 36.251 11.583 1.00 47.59 O ANISOU 1608 O TYR B 265 3871 9091 5120 536 -206 -1157 O ATOM 1609 CB TYR B 265 22.533 37.952 14.218 1.00 48.15 C ANISOU 1609 CB TYR B 265 4106 8800 5388 366 -226 -1026 C ATOM 1610 CG TYR B 265 21.860 36.658 14.616 1.00 46.71 C ANISOU 1610 CG TYR B 265 3991 8526 5229 473 -219 -1173 C ATOM 1611 CD1 TYR B 265 20.476 36.546 14.618 1.00 48.52 C ANISOU 1611 CD1 TYR B 265 4295 8618 5521 494 -213 -1203 C ATOM 1612 CD2 TYR B 265 22.607 35.548 14.982 1.00 44.70 C ANISOU 1612 CD2 TYR B 265 3723 8319 4941 553 -213 -1281 C ATOM 1613 CE1 TYR B 265 19.854 35.366 14.977 1.00 43.75 C ANISOU 1613 CE1 TYR B 265 3747 7920 4957 587 -197 -1336 C ATOM 1614 CE2 TYR B 265 21.994 34.363 15.342 1.00 46.47 C ANISOU 1614 CE2 TYR B 265 4006 8446 5203 651 -197 -1406 C ATOM 1615 CZ TYR B 265 20.617 34.278 15.338 1.00 44.24 C ANISOU 1615 CZ TYR B 265 3793 8021 4995 665 -186 -1432 C ATOM 1616 OH TYR B 265 19.998 33.103 15.696 1.00 44.04 O ANISOU 1616 OH TYR B 265 3820 7888 5025 757 -162 -1556 O ATOM 1617 N LEU B 266 21.371 38.392 11.188 1.00 48.52 N ANISOU 1617 N LEU B 266 3999 9161 5275 390 -203 -913 N ATOM 1618 CA LEU B 266 20.393 38.069 10.153 1.00 51.79 C ANISOU 1618 CA LEU B 266 4384 9656 5639 457 -196 -949 C ATOM 1619 C LEU B 266 20.334 39.164 9.092 1.00 48.66 C ANISOU 1619 C LEU B 266 3914 9394 5178 411 -183 -787 C ATOM 1620 O LEU B 266 19.904 40.287 9.362 1.00 52.81 O ANISOU 1620 O LEU B 266 4496 9799 5772 329 -181 -666 O ATOM 1621 CB LEU B 266 19.006 37.849 10.760 1.00 46.83 C ANISOU 1621 CB LEU B 266 3875 8806 5111 480 -201 -1026 C ATOM 1622 CG LEU B 266 17.868 37.699 9.749 1.00 46.02 C ANISOU 1622 CG LEU B 266 3747 8769 4970 541 -195 -1063 C ATOM 1623 CD1 LEU B 266 18.128 36.521 8.832 1.00 50.22 C ANISOU 1623 CD1 LEU B 266 4170 9503 5407 651 -191 -1192 C ATOM 1624 CD2 LEU B 266 16.536 37.544 10.462 1.00 45.81 C ANISOU 1624 CD2 LEU B 266 3843 8509 5054 552 -198 -1140 C ATOM 1625 N ASP B 267 20.773 38.832 7.884 1.00 59.25 N ANISOU 1625 N ASP B 267 5129 10994 6391 470 -173 -783 N ATOM 1626 CA ASP B 267 20.774 39.791 6.789 1.00 60.91 C ANISOU 1626 CA ASP B 267 5256 11363 6522 446 -152 -621 C ATOM 1627 C ASP B 267 19.778 39.393 5.704 1.00 55.86 C ANISOU 1627 C ASP B 267 4571 10851 5802 552 -149 -680 C ATOM 1628 O ASP B 267 20.005 38.439 4.959 1.00 53.82 O ANISOU 1628 O ASP B 267 4216 10788 5446 653 -155 -789 O ATOM 1629 CB ASP B 267 22.176 39.921 6.195 1.00 62.96 C ANISOU 1629 CB ASP B 267 5388 11851 6683 428 -136 -540 C ATOM 1630 CG ASP B 267 22.317 41.134 5.303 1.00 66.59 C ANISOU 1630 CG ASP B 267 5775 12434 7092 377 -101 -329 C ATOM 1631 OD1 ASP B 267 23.447 41.412 4.852 1.00 67.68 O ANISOU 1631 OD1 ASP B 267 5810 12743 7163 346 -80 -236 O ATOM 1632 OD2 ASP B 267 21.298 41.811 5.056 1.00 68.93 O ANISOU 1632 OD2 ASP B 267 6118 12655 7416 371 -91 -253 O ATOM 1633 N ILE B 268 18.672 40.126 5.620 1.00 50.18 N ANISOU 1633 N ILE B 268 3916 10026 5125 535 -144 -616 N ATOM 1634 CA ILE B 268 17.645 39.841 4.625 1.00 51.43 C ANISOU 1634 CA ILE B 268 4032 10300 5208 640 -143 -676 C ATOM 1635 C ILE B 268 17.045 41.117 4.045 1.00 55.71 C ANISOU 1635 C ILE B 268 4579 10860 5728 609 -122 -496 C ATOM 1636 O ILE B 268 15.879 41.134 3.653 1.00 57.02 O ANISOU 1636 O ILE B 268 4769 11013 5882 671 -125 -542 O ATOM 1637 CB ILE B 268 16.504 38.979 5.210 1.00 50.82 C ANISOU 1637 CB ILE B 268 4047 10044 5219 694 -163 -871 C ATOM 1638 CG1 ILE B 268 15.853 39.688 6.399 1.00 48.07 C ANISOU 1638 CG1 ILE B 268 3855 9396 5015 597 -170 -822 C ATOM 1639 CG2 ILE B 268 17.021 37.609 5.613 1.00 50.80 C ANISOU 1639 CG2 ILE B 268 4026 10044 5233 748 -176 -1052 C ATOM 1640 CD1 ILE B 268 14.691 38.926 7.003 1.00 47.23 C ANISOU 1640 CD1 ILE B 268 3841 9103 5000 643 -183 -996 C ATOM 1641 N HIS B 269 17.844 42.179 3.980 1.00 81.30 N ANISOU 1641 N HIS B 269 7793 14131 8967 518 -96 -294 N ATOM 1642 CA HIS B 269 17.353 43.467 3.496 1.00 83.89 C ANISOU 1642 CA HIS B 269 8130 14454 9290 481 -69 -100 C ATOM 1643 C HIS B 269 16.918 43.403 2.033 1.00 84.81 C ANISOU 1643 C HIS B 269 8136 14840 9246 606 -47 -73 C ATOM 1644 O HIS B 269 16.277 44.325 1.525 1.00 86.93 O ANISOU 1644 O HIS B 269 8415 15120 9494 611 -24 64 O ATOM 1645 CB HIS B 269 18.400 44.566 3.701 1.00 83.42 C ANISOU 1645 CB HIS B 269 8047 14375 9276 357 -37 108 C ATOM 1646 CG HIS B 269 19.557 44.483 2.756 1.00 83.91 C ANISOU 1646 CG HIS B 269 7956 14716 9210 384 -4 193 C ATOM 1647 ND1 HIS B 269 20.582 43.575 2.912 1.00 85.69 N ANISOU 1647 ND1 HIS B 269 8119 15042 9396 399 -18 85 N ATOM 1648 CD2 HIS B 269 19.857 45.205 1.651 1.00 85.36 C ANISOU 1648 CD2 HIS B 269 8035 15103 9294 402 46 381 C ATOM 1649 CE1 HIS B 269 21.460 43.736 1.939 1.00 87.82 C ANISOU 1649 CE1 HIS B 269 8251 15570 9546 421 17 196 C ATOM 1650 NE2 HIS B 269 21.045 44.718 1.160 1.00 87.63 N ANISOU 1650 NE2 HIS B 269 8198 15614 9484 424 60 380 N ATOM 1651 N LYS B 270 17.271 42.312 1.362 1.00111.97 N ANISOU 1651 N LYS B 270 11468 18503 12573 715 -57 -207 N ATOM 1652 CA LYS B 270 16.861 42.099 -0.020 1.00114.80 C ANISOU 1652 CA LYS B 270 11706 19141 12771 856 -45 -218 C ATOM 1653 C LYS B 270 15.462 41.494 -0.065 1.00108.68 C ANISOU 1653 C LYS B 270 10980 18302 12012 950 -73 -406 C ATOM 1654 O LYS B 270 14.665 41.813 -0.947 1.00113.51 O ANISOU 1654 O LYS B 270 11550 19043 12536 1041 -61 -379 O ATOM 1655 CB LYS B 270 17.850 41.180 -0.739 1.00121.52 C ANISOU 1655 CB LYS B 270 12406 20272 13495 938 -49 -296 C ATOM 1656 CG LYS B 270 17.856 39.749 -0.217 1.00127.90 C ANISOU 1656 CG LYS B 270 13225 21025 14347 985 -94 -559 C ATOM 1657 CD LYS B 270 18.779 38.856 -1.031 1.00131.34 C ANISOU 1657 CD LYS B 270 13499 21754 14648 1079 -104 -641 C ATOM 1658 CE LYS B 270 18.629 37.398 -0.620 1.00132.31 C ANISOU 1658 CE LYS B 270 13628 21823 14822 1144 -145 -913 C ATOM 1659 NZ LYS B 270 18.823 37.210 0.847 1.00133.51 N ANISOU 1659 NZ LYS B 270 13924 21667 15136 1035 -156 -957 N ATOM 1660 N LEU B 271 15.173 40.620 0.894 1.00 58.00 N ANISOU 1660 N LEU B 271 4646 11685 5707 933 -106 -598 N ATOM 1661 CA LEU B 271 13.885 39.938 0.956 1.00 54.06 C ANISOU 1661 CA LEU B 271 4191 11102 5248 1014 -129 -797 C ATOM 1662 C LEU B 271 12.795 40.825 1.551 1.00 51.98 C ANISOU 1662 C LEU B 271 4069 10600 5082 949 -129 -732 C ATOM 1663 O LEU B 271 11.611 40.611 1.306 1.00 53.83 O ANISOU 1663 O LEU B 271 4325 10812 5317 1023 -138 -846 O ATOM 1664 CB LEU B 271 14.004 38.646 1.768 1.00 51.76 C ANISOU 1664 CB LEU B 271 3934 10681 5051 1022 -154 -1016 C ATOM 1665 CG LEU B 271 14.743 37.481 1.109 1.00 51.78 C ANISOU 1665 CG LEU B 271 3794 10916 4964 1122 -164 -1156 C ATOM 1666 CD1 LEU B 271 15.108 36.415 2.131 1.00 52.12 C ANISOU 1666 CD1 LEU B 271 3893 10789 5122 1098 -180 -1314 C ATOM 1667 CD2 LEU B 271 13.903 36.890 -0.011 1.00 53.19 C ANISOU 1667 CD2 LEU B 271 3861 11295 5052 1276 -173 -1310 C ATOM 1668 N VAL B 272 13.197 41.822 2.331 1.00 66.81 N ANISOU 1668 N VAL B 272 6037 12303 7046 814 -120 -557 N ATOM 1669 CA VAL B 272 12.236 42.702 2.987 1.00 69.13 C ANISOU 1669 CA VAL B 272 6466 12359 7443 744 -127 -493 C ATOM 1670 C VAL B 272 12.177 44.082 2.331 1.00 72.97 C ANISOU 1670 C VAL B 272 6934 12917 7873 718 -97 -255 C ATOM 1671 O VAL B 272 13.209 44.673 2.001 1.00 72.57 O ANISOU 1671 O VAL B 272 6816 12975 7783 671 -67 -80 O ATOM 1672 CB VAL B 272 12.529 42.839 4.501 1.00 68.00 C ANISOU 1672 CB VAL B 272 6449 11923 7463 615 -146 -493 C ATOM 1673 CG1 VAL B 272 13.986 43.182 4.738 1.00 67.39 C ANISOU 1673 CG1 VAL B 272 6327 11888 7391 530 -131 -363 C ATOM 1674 CG2 VAL B 272 11.621 43.883 5.132 1.00 67.71 C ANISOU 1674 CG2 VAL B 272 6540 11659 7527 539 -157 -407 C ATOM 1675 N GLN B 273 10.961 44.581 2.134 1.00 65.41 N ANISOU 1675 N GLN B 273 6035 11901 6917 752 -101 -249 N ATOM 1676 CA GLN B 273 10.754 45.919 1.592 1.00 70.26 C ANISOU 1676 CA GLN B 273 6650 12552 7493 732 -71 -22 C ATOM 1677 C GLN B 273 10.528 46.930 2.710 1.00 68.07 C ANISOU 1677 C GLN B 273 6513 11973 7378 589 -85 85 C ATOM 1678 O GLN B 273 9.475 46.942 3.347 1.00 56.78 O ANISOU 1678 O GLN B 273 5195 10352 6028 578 -117 -11 O ATOM 1679 CB GLN B 273 9.570 45.932 0.623 1.00 76.38 C ANISOU 1679 CB GLN B 273 7397 13468 8157 870 -68 -73 C ATOM 1680 CG GLN B 273 9.944 45.658 -0.827 1.00 83.55 C ANISOU 1680 CG GLN B 273 8137 14737 8872 1010 -36 -42 C ATOM 1681 CD GLN B 273 10.653 46.833 -1.474 1.00 92.74 C ANISOU 1681 CD GLN B 273 9243 16024 9970 981 19 251 C ATOM 1682 OE1 GLN B 273 10.663 47.941 -0.934 1.00 93.25 O ANISOU 1682 OE1 GLN B 273 9397 15899 10137 865 33 428 O ATOM 1683 NE2 GLN B 273 11.250 46.597 -2.638 1.00 97.79 N ANISOU 1683 NE2 GLN B 273 9728 16984 10445 1088 51 302 N ATOM 1684 N SER B 274 11.527 47.777 2.941 1.00 87.93 N ANISOU 1684 N SER B 274 9014 14451 9945 480 -59 278 N ATOM 1685 CA SER B 274 11.456 48.792 3.984 1.00 99.41 C ANISOU 1685 CA SER B 274 10580 15631 11561 342 -73 382 C ATOM 1686 C SER B 274 10.542 49.950 3.589 1.00107.93 C ANISOU 1686 C SER B 274 11705 16662 12641 346 -60 528 C ATOM 1687 O SER B 274 9.333 49.774 3.441 1.00109.75 O ANISOU 1687 O SER B 274 11990 16869 12841 420 -83 428 O ATOM 1688 CB SER B 274 12.857 49.314 4.314 1.00103.38 C ANISOU 1688 CB SER B 274 11033 16117 12128 228 -48 527 C ATOM 1689 OG SER B 274 13.549 49.696 3.137 1.00106.61 O ANISOU 1689 OG SER B 274 11316 16771 12421 265 11 696 O ATOM 1690 N GLY B 275 11.126 51.132 3.421 1.00104.69 N ANISOU 1690 N GLY B 275 11269 16234 12273 266 -20 763 N ATOM 1691 CA GLY B 275 10.367 52.315 3.058 1.00109.81 C ANISOU 1691 CA GLY B 275 11960 16828 12935 265 -1 927 C ATOM 1692 C GLY B 275 10.124 53.226 4.246 1.00114.29 C ANISOU 1692 C GLY B 275 12645 17081 13698 126 -35 975 C ATOM 1693 O GLY B 275 9.770 52.762 5.331 1.00112.28 O ANISOU 1693 O GLY B 275 12481 16642 13539 84 -94 807 O ATOM 1694 N ILE B 276 10.312 54.527 4.040 1.00163.90 N ANISOU 1694 N ILE B 276 18921 23307 20046 61 4 1204 N ATOM 1695 CA ILE B 276 10.166 55.503 5.118 1.00164.59 C ANISOU 1695 CA ILE B 276 19102 23104 20332 -73 -29 1260 C ATOM 1696 C ILE B 276 8.930 56.389 4.963 1.00165.72 C ANISOU 1696 C ILE B 276 19330 23144 20495 -50 -41 1333 C ATOM 1697 O ILE B 276 8.513 56.705 3.847 1.00167.93 O ANISOU 1697 O ILE B 276 19570 23586 20648 48 6 1448 O ATOM 1698 CB ILE B 276 11.424 56.390 5.256 1.00162.79 C ANISOU 1698 CB ILE B 276 18802 22829 20221 -197 19 1453 C ATOM 1699 CG1 ILE B 276 12.038 56.674 3.881 1.00164.21 C ANISOU 1699 CG1 ILE B 276 18856 23264 20274 -137 111 1654 C ATOM 1700 CG2 ILE B 276 12.448 55.722 6.160 1.00157.99 C ANISOU 1700 CG2 ILE B 276 18171 22170 19686 -273 -8 1327 C ATOM 1701 CD1 ILE B 276 11.239 57.635 3.025 1.00162.81 C ANISOU 1701 CD1 ILE B 276 18690 23121 20050 -78 155 1840 C ATOM 1702 N LYS B 277 8.353 56.785 6.095 1.00102.99 N ANISOU 1702 N LYS B 277 11936 16002 11196 557 -1374 201 N ATOM 1703 CA LYS B 277 7.187 57.662 6.109 1.00 96.32 C ANISOU 1703 CA LYS B 277 11216 15144 10239 628 -1454 148 C ATOM 1704 C LYS B 277 6.835 58.073 7.534 1.00 87.06 C ANISOU 1704 C LYS B 277 10140 13876 9064 662 -1543 163 C ATOM 1705 O LYS B 277 6.480 57.236 8.362 1.00 80.29 O ANISOU 1705 O LYS B 277 9232 13002 8272 698 -1497 112 O ATOM 1706 CB LYS B 277 5.999 56.986 5.442 1.00 96.14 C ANISOU 1706 CB LYS B 277 11140 15200 10188 707 -1380 12 C ATOM 1707 N ASP B 280 4.207 54.327 7.351 1.00 76.16 N ANISOU 1707 N ASP B 280 8431 12675 7831 828 -1226 -198 N ATOM 1708 CA ASP B 280 4.660 53.161 6.598 1.00 80.18 C ANISOU 1708 CA ASP B 280 8814 13244 8405 794 -1121 -231 C ATOM 1709 C ASP B 280 5.331 52.154 7.524 1.00 75.69 C ANISOU 1709 C ASP B 280 8175 12635 7947 760 -1066 -211 C ATOM 1710 O ASP B 280 6.480 52.336 7.927 1.00 77.04 O ANISOU 1710 O ASP B 280 8351 12759 8159 702 -1088 -116 O ATOM 1711 CB ASP B 280 5.622 53.583 5.485 1.00 86.37 C ANISOU 1711 CB ASP B 280 9598 14061 9157 739 -1117 -165 C ATOM 1712 CG ASP B 280 5.913 52.461 4.507 1.00 89.51 C ANISOU 1712 CG ASP B 280 9887 14530 9594 729 -1007 -211 C ATOM 1713 OD1 ASP B 280 6.621 52.712 3.509 1.00 94.44 O ANISOU 1713 OD1 ASP B 280 10507 15190 10187 697 -985 -164 O ATOM 1714 OD2 ASP B 280 5.434 51.331 4.733 1.00 86.06 O ANISOU 1714 OD2 ASP B 280 9376 14110 9214 755 -943 -290 O ATOM 1715 N GLU B 281 4.609 51.088 7.850 1.00 63.10 N ANISOU 1715 N GLU B 281 6514 11058 6402 794 -999 -299 N ATOM 1716 CA GLU B 281 5.077 50.114 8.830 1.00 63.42 C ANISOU 1716 CA GLU B 281 6505 11053 6540 772 -952 -293 C ATOM 1717 C GLU B 281 5.768 48.918 8.183 1.00 60.72 C ANISOU 1717 C GLU B 281 6053 10756 6262 738 -858 -313 C ATOM 1718 O GLU B 281 6.119 47.952 8.860 1.00 64.95 O ANISOU 1718 O GLU B 281 6541 11262 6877 724 -810 -322 O ATOM 1719 CB GLU B 281 3.908 49.639 9.691 1.00 64.37 C ANISOU 1719 CB GLU B 281 6626 11155 6677 827 -932 -369 C ATOM 1720 CG GLU B 281 3.093 50.767 10.294 1.00 63.41 C ANISOU 1720 CG GLU B 281 6612 10996 6483 883 -1013 -358 C ATOM 1721 CD GLU B 281 1.720 50.314 10.738 1.00 62.29 C ANISOU 1721 CD GLU B 281 6447 10874 6347 948 -975 -445 C ATOM 1722 OE1 GLU B 281 0.834 51.181 10.887 1.00 61.87 O ANISOU 1722 OE1 GLU B 281 6461 10823 6224 1011 -1026 -457 O ATOM 1723 OE2 GLU B 281 1.525 49.095 10.930 1.00 62.06 O ANISOU 1723 OE2 GLU B 281 6330 10858 6391 937 -893 -499 O ATOM 1724 N ARG B 282 5.962 48.987 6.871 1.00 54.36 N ANISOU 1724 N ARG B 282 5220 10020 5415 731 -832 -320 N ATOM 1725 CA ARG B 282 6.629 47.912 6.146 1.00 54.90 C ANISOU 1725 CA ARG B 282 5199 10133 5527 712 -742 -335 C ATOM 1726 C ARG B 282 8.089 47.787 6.560 1.00 52.67 C ANISOU 1726 C ARG B 282 4883 9817 5312 658 -728 -236 C ATOM 1727 O ARG B 282 8.746 48.782 6.864 1.00 48.33 O ANISOU 1727 O ARG B 282 4380 9231 4754 622 -795 -139 O ATOM 1728 CB ARG B 282 6.546 48.142 4.638 1.00 59.48 C ANISOU 1728 CB ARG B 282 5779 10786 6033 724 -721 -355 C ATOM 1729 CG ARG B 282 5.173 47.912 4.037 1.00 60.13 C ANISOU 1729 CG ARG B 282 5870 10910 6067 778 -721 -468 C ATOM 1730 CD ARG B 282 5.191 48.247 2.562 1.00 63.98 C ANISOU 1730 CD ARG B 282 6380 11454 6473 792 -713 -479 C ATOM 1731 NE ARG B 282 5.628 49.621 2.337 1.00 63.20 N ANISOU 1731 NE ARG B 282 6358 11346 6310 772 -777 -393 N ATOM 1732 CZ ARG B 282 6.125 50.069 1.190 1.00 59.23 C ANISOU 1732 CZ ARG B 282 5882 10879 5743 764 -763 -358 C ATOM 1733 NH1 ARG B 282 6.496 51.336 1.079 1.00 55.44 N ANISOU 1733 NH1 ARG B 282 5477 10382 5205 738 -827 -276 N ATOM 1734 NH2 ARG B 282 6.257 49.247 0.157 1.00 61.55 N ANISOU 1734 NH2 ARG B 282 6140 11221 6026 784 -685 -401 N ATOM 1735 N GLY B 283 8.591 46.558 6.555 1.00 62.98 N ANISOU 1735 N GLY B 283 6109 11136 6685 654 -648 -260 N ATOM 1736 CA GLY B 283 9.962 46.288 6.941 1.00 67.02 C ANISOU 1736 CA GLY B 283 6572 11623 7272 611 -629 -174 C ATOM 1737 C GLY B 283 10.025 45.145 7.930 1.00 70.20 C ANISOU 1737 C GLY B 283 6940 11978 7756 617 -595 -214 C ATOM 1738 O GLY B 283 9.149 44.278 7.945 1.00 69.56 O ANISOU 1738 O GLY B 283 6848 11909 7674 651 -553 -314 O ATOM 1739 N LEU B 284 11.062 45.140 8.760 1.00 66.23 N ANISOU 1739 N LEU B 284 6422 11418 7325 581 -619 -135 N ATOM 1740 CA LEU B 284 11.201 44.120 9.790 1.00 61.95 C ANISOU 1740 CA LEU B 284 5862 10818 6858 587 -598 -167 C ATOM 1741 C LEU B 284 10.240 44.410 10.936 1.00 60.36 C ANISOU 1741 C LEU B 284 5746 10540 6646 603 -656 -202 C ATOM 1742 O LEU B 284 10.340 45.445 11.596 1.00 59.92 O ANISOU 1742 O LEU B 284 5765 10424 6577 588 -744 -135 O ATOM 1743 CB LEU B 284 12.638 44.062 10.300 1.00 56.74 C ANISOU 1743 CB LEU B 284 5161 10117 6280 547 -615 -68 C ATOM 1744 CG LEU B 284 12.952 42.849 11.174 1.00 51.07 C ANISOU 1744 CG LEU B 284 4417 9347 5641 557 -582 -105 C ATOM 1745 CD1 LEU B 284 12.541 41.581 10.450 1.00 47.90 C ANISOU 1745 CD1 LEU B 284 3963 9009 5227 596 -478 -206 C ATOM 1746 CD2 LEU B 284 14.425 42.813 11.540 1.00 51.82 C ANISOU 1746 CD2 LEU B 284 4459 9412 5820 521 -603 -5 C ATOM 1747 N LEU B 285 9.303 43.496 11.165 1.00 62.75 N ANISOU 1747 N LEU B 285 6044 10845 6952 636 -605 -302 N ATOM 1748 CA LEU B 285 8.269 43.704 12.173 1.00 62.26 C ANISOU 1748 CA LEU B 285 6055 10724 6876 661 -639 -340 C ATOM 1749 C LEU B 285 8.647 43.123 13.531 1.00 63.60 C ANISOU 1749 C LEU B 285 6256 10796 7113 655 -645 -328 C ATOM 1750 O LEU B 285 8.805 43.857 14.506 1.00 65.86 O ANISOU 1750 O LEU B 285 6626 10999 7401 654 -718 -270 O ATOM 1751 CB LEU B 285 6.938 43.113 11.704 1.00 60.20 C ANISOU 1751 CB LEU B 285 5770 10520 6585 695 -585 -449 C ATOM 1752 CG LEU B 285 6.441 43.580 10.336 1.00 59.49 C ANISOU 1752 CG LEU B 285 5658 10521 6425 709 -582 -476 C ATOM 1753 CD1 LEU B 285 5.038 43.055 10.077 1.00 62.82 C ANISOU 1753 CD1 LEU B 285 6060 10981 6827 740 -551 -580 C ATOM 1754 CD2 LEU B 285 6.480 45.097 10.239 1.00 54.89 C ANISOU 1754 CD2 LEU B 285 5143 9933 5781 710 -666 -406 C ATOM 1755 N SER B 286 8.791 41.804 13.590 1.00 59.49 N ANISOU 1755 N SER B 286 5682 10279 6643 654 -573 -384 N ATOM 1756 CA SER B 286 9.059 41.136 14.855 1.00 56.70 C ANISOU 1756 CA SER B 286 5366 9830 6349 653 -573 -386 C ATOM 1757 C SER B 286 10.006 39.947 14.708 1.00 56.17 C ANISOU 1757 C SER B 286 5232 9766 6344 639 -520 -398 C ATOM 1758 O SER B 286 10.326 39.519 13.601 1.00 58.68 O ANISOU 1758 O SER B 286 5474 10166 6655 638 -469 -414 O ATOM 1759 CB SER B 286 7.746 40.680 15.494 1.00 59.45 C ANISOU 1759 CB SER B 286 5753 10153 6682 681 -539 -466 C ATOM 1760 OG SER B 286 7.965 40.147 16.787 1.00 65.63 O ANISOU 1760 OG SER B 286 6593 10831 7510 683 -542 -464 O ATOM 1761 N LEU B 287 10.450 39.426 15.845 1.00 53.28 N ANISOU 1761 N LEU B 287 4906 9306 6033 636 -533 -388 N ATOM 1762 CA LEU B 287 11.318 38.258 15.895 1.00 45.54 C ANISOU 1762 CA LEU B 287 3878 8314 5112 631 -490 -404 C ATOM 1763 C LEU B 287 11.073 37.551 17.229 1.00 43.37 C ANISOU 1763 C LEU B 287 3678 7931 4871 640 -491 -440 C ATOM 1764 O LEU B 287 10.723 38.190 18.225 1.00 43.48 O ANISOU 1764 O LEU B 287 3783 7862 4875 645 -545 -414 O ATOM 1765 CB LEU B 287 12.784 38.680 15.765 1.00 39.99 C ANISOU 1765 CB LEU B 287 3132 7607 4457 609 -535 -304 C ATOM 1766 CG LEU B 287 13.828 37.643 15.336 1.00 41.33 C ANISOU 1766 CG LEU B 287 3217 7809 4679 614 -481 -306 C ATOM 1767 CD1 LEU B 287 15.085 38.333 14.825 1.00 41.05 C ANISOU 1767 CD1 LEU B 287 3110 7810 4678 591 -513 -197 C ATOM 1768 CD2 LEU B 287 14.165 36.684 16.469 1.00 45.05 C ANISOU 1768 CD2 LEU B 287 3729 8181 5208 623 -486 -334 C ATOM 1769 N ALA B 288 11.233 36.232 17.245 1.00 39.31 N ANISOU 1769 N ALA B 288 3138 7412 4386 646 -430 -502 N ATOM 1770 CA ALA B 288 11.002 35.458 18.457 1.00 41.21 C ANISOU 1770 CA ALA B 288 3455 7548 4654 652 -423 -542 C ATOM 1771 C ALA B 288 11.842 34.184 18.480 1.00 41.03 C ANISOU 1771 C ALA B 288 3404 7508 4679 657 -388 -571 C ATOM 1772 O ALA B 288 11.640 33.285 17.663 1.00 43.78 O ANISOU 1772 O ALA B 288 3699 7923 5012 664 -321 -635 O ATOM 1773 CB ALA B 288 9.524 35.122 18.591 1.00 40.75 C ANISOU 1773 CB ALA B 288 3427 7499 4556 659 -371 -621 C ATOM 1774 N PHE B 289 12.784 34.110 19.415 1.00 44.93 N ANISOU 1774 N PHE B 289 3940 7906 5225 657 -440 -526 N ATOM 1775 CA PHE B 289 13.617 32.922 19.553 1.00 43.16 C ANISOU 1775 CA PHE B 289 3699 7655 5047 669 -415 -553 C ATOM 1776 C PHE B 289 12.817 31.780 20.167 1.00 39.32 C ANISOU 1776 C PHE B 289 3284 7110 4546 676 -364 -647 C ATOM 1777 O PHE B 289 12.070 31.980 21.126 1.00 43.85 O ANISOU 1777 O PHE B 289 3950 7604 5106 671 -376 -659 O ATOM 1778 CB PHE B 289 14.855 33.216 20.408 1.00 44.68 C ANISOU 1778 CB PHE B 289 3917 7756 5305 667 -499 -475 C ATOM 1779 CG PHE B 289 15.816 34.189 19.778 1.00 44.72 C ANISOU 1779 CG PHE B 289 3835 7819 5339 652 -549 -374 C ATOM 1780 CD1 PHE B 289 15.653 35.557 19.944 1.00 44.30 C ANISOU 1780 CD1 PHE B 289 3814 7751 5269 628 -621 -302 C ATOM 1781 CD2 PHE B 289 16.885 33.735 19.021 1.00 42.72 C ANISOU 1781 CD2 PHE B 289 3472 7634 5125 663 -521 -349 C ATOM 1782 CE1 PHE B 289 16.537 36.455 19.364 1.00 43.93 C ANISOU 1782 CE1 PHE B 289 3689 7753 5249 603 -670 -203 C ATOM 1783 CE2 PHE B 289 17.771 34.628 18.439 1.00 45.81 C ANISOU 1783 CE2 PHE B 289 3776 8083 5548 643 -559 -247 C ATOM 1784 CZ PHE B 289 17.596 35.988 18.611 1.00 49.30 C ANISOU 1784 CZ PHE B 289 4250 8506 5977 607 -635 -174 C ATOM 1785 N HIS B 290 12.966 30.585 19.602 1.00 45.39 N ANISOU 1785 N HIS B 290 4015 7917 5314 688 -304 -711 N ATOM 1786 CA HIS B 290 12.325 29.400 20.156 1.00 51.90 C ANISOU 1786 CA HIS B 290 4910 8682 6129 687 -260 -797 C ATOM 1787 C HIS B 290 12.877 29.154 21.551 1.00 57.68 C ANISOU 1787 C HIS B 290 5740 9274 6901 693 -306 -781 C ATOM 1788 O HIS B 290 14.085 29.253 21.765 1.00 58.11 O ANISOU 1788 O HIS B 290 5780 9297 7002 709 -357 -728 O ATOM 1789 CB HIS B 290 12.579 28.181 19.267 1.00 56.54 C ANISOU 1789 CB HIS B 290 5451 9328 6704 704 -204 -860 C ATOM 1790 CG HIS B 290 11.825 26.954 19.686 1.00 62.10 C ANISOU 1790 CG HIS B 290 6228 9978 7391 693 -161 -950 C ATOM 1791 ND1 HIS B 290 12.291 26.092 20.658 1.00 64.22 N ANISOU 1791 ND1 HIS B 290 6579 10137 7684 702 -172 -975 N ATOM 1792 CD2 HIS B 290 10.649 26.445 19.262 1.00 62.73 C ANISOU 1792 CD2 HIS B 290 6310 10092 7432 669 -114 -1019 C ATOM 1793 CE1 HIS B 290 11.427 25.106 20.814 1.00 64.06 C ANISOU 1793 CE1 HIS B 290 6614 10088 7637 681 -127 -1053 C ATOM 1794 NE2 HIS B 290 10.421 25.293 19.982 1.00 64.04 N ANISOU 1794 NE2 HIS B 290 6560 10172 7600 658 -93 -1080 N ATOM 1795 N PRO B 291 11.991 28.845 22.509 1.00 53.00 N ANISOU 1795 N PRO B 291 5251 8596 6293 682 -290 -822 N ATOM 1796 CA PRO B 291 12.395 28.605 23.898 1.00 50.53 C ANISOU 1796 CA PRO B 291 5057 8135 6006 692 -332 -812 C ATOM 1797 C PRO B 291 13.620 27.697 23.994 1.00 49.43 C ANISOU 1797 C PRO B 291 4916 7956 5909 714 -354 -822 C ATOM 1798 O PRO B 291 14.530 27.972 24.779 1.00 51.78 O ANISOU 1798 O PRO B 291 5261 8163 6249 729 -428 -771 O ATOM 1799 CB PRO B 291 11.167 27.920 24.496 1.00 49.91 C ANISOU 1799 CB PRO B 291 5062 8006 5894 677 -268 -881 C ATOM 1800 CG PRO B 291 10.026 28.494 23.729 1.00 50.23 C ANISOU 1800 CG PRO B 291 5034 8154 5898 658 -225 -890 C ATOM 1801 CD PRO B 291 10.535 28.707 22.325 1.00 50.68 C ANISOU 1801 CD PRO B 291 4963 8340 5955 661 -228 -877 C ATOM 1802 N ASN B 292 13.646 26.635 23.194 1.00 56.56 N ANISOU 1802 N ASN B 292 5769 8924 6799 721 -296 -885 N ATOM 1803 CA ASN B 292 14.778 25.713 23.186 1.00 61.68 C ANISOU 1803 CA ASN B 292 6413 9546 7478 754 -309 -900 C ATOM 1804 C ASN B 292 15.853 26.103 22.179 1.00 59.17 C ANISOU 1804 C ASN B 292 5962 9331 7189 780 -324 -843 C ATOM 1805 O ASN B 292 16.578 25.246 21.674 1.00 59.75 O ANISOU 1805 O ASN B 292 5996 9438 7270 816 -302 -867 O ATOM 1806 CB ASN B 292 14.311 24.281 22.919 1.00 70.89 C ANISOU 1806 CB ASN B 292 7616 10714 8607 757 -244 -999 C ATOM 1807 CG ASN B 292 13.512 23.706 24.069 1.00 84.33 C ANISOU 1807 CG ASN B 292 9456 12294 10292 732 -231 -1050 C ATOM 1808 OD1 ASN B 292 12.820 24.432 24.784 1.00 85.15 O ANISOU 1808 OD1 ASN B 292 9612 12349 10391 709 -239 -1024 O ATOM 1809 ND2 ASN B 292 13.600 22.393 24.252 1.00 92.44 N ANISOU 1809 ND2 ASN B 292 10550 13269 11304 741 -208 -1121 N ATOM 1810 N TYR B 293 15.954 27.399 21.895 1.00 49.27 N ANISOU 1810 N TYR B 293 4646 8127 5948 763 -359 -763 N ATOM 1811 CA TYR B 293 16.943 27.903 20.951 1.00 49.82 C ANISOU 1811 CA TYR B 293 4587 8295 6047 779 -368 -694 C ATOM 1812 C TYR B 293 18.348 27.433 21.313 1.00 57.70 C ANISOU 1812 C TYR B 293 5562 9249 7112 814 -411 -660 C ATOM 1813 O TYR B 293 19.191 27.239 20.439 1.00 58.20 O ANISOU 1813 O TYR B 293 5517 9402 7194 846 -384 -633 O ATOM 1814 CB TYR B 293 16.905 29.431 20.882 1.00 49.20 C ANISOU 1814 CB TYR B 293 4473 8242 5978 747 -421 -603 C ATOM 1815 CG TYR B 293 18.003 30.015 20.024 1.00 57.62 C ANISOU 1815 CG TYR B 293 5409 9399 7083 754 -436 -517 C ATOM 1816 CD1 TYR B 293 19.228 30.364 20.576 1.00 64.85 C ANISOU 1816 CD1 TYR B 293 6300 10263 8079 754 -516 -434 C ATOM 1817 CD2 TYR B 293 17.820 30.209 18.661 1.00 55.31 C ANISOU 1817 CD2 TYR B 293 5022 9243 6750 759 -371 -515 C ATOM 1818 CE1 TYR B 293 20.238 30.893 19.796 1.00 65.19 C ANISOU 1818 CE1 TYR B 293 6211 10394 8165 755 -523 -346 C ATOM 1819 CE2 TYR B 293 18.824 30.739 17.873 1.00 56.12 C ANISOU 1819 CE2 TYR B 293 5006 9430 6885 766 -373 -430 C ATOM 1820 CZ TYR B 293 20.031 31.079 18.447 1.00 60.40 C ANISOU 1820 CZ TYR B 293 5512 9925 7513 761 -445 -343 C ATOM 1821 OH TYR B 293 21.039 31.606 17.675 1.00 61.60 O ANISOU 1821 OH TYR B 293 5535 10165 7706 762 -442 -249 O ATOM 1822 N LYS B 294 18.595 27.259 22.607 1.00 67.19 N ANISOU 1822 N LYS B 294 6868 10313 8349 813 -476 -660 N ATOM 1823 CA LYS B 294 19.899 26.810 23.074 1.00 66.85 C ANISOU 1823 CA LYS B 294 6812 10213 8376 848 -531 -632 C ATOM 1824 C LYS B 294 20.223 25.422 22.528 1.00 62.34 C ANISOU 1824 C LYS B 294 6218 9683 7786 900 -464 -706 C ATOM 1825 O LYS B 294 21.392 25.050 22.405 1.00 63.10 O ANISOU 1825 O LYS B 294 6248 9792 7934 944 -483 -677 O ATOM 1826 CB LYS B 294 19.948 26.807 24.603 1.00 70.90 C ANISOU 1826 CB LYS B 294 7471 10552 8916 841 -617 -633 C ATOM 1827 CG LYS B 294 21.349 26.643 25.172 1.00 75.66 C ANISOU 1827 CG LYS B 294 8057 11085 9605 870 -705 -583 C ATOM 1828 CD LYS B 294 21.361 26.798 26.685 1.00 78.03 C ANISOU 1828 CD LYS B 294 8519 11203 9927 863 -804 -578 C ATOM 1829 CE LYS B 294 22.780 26.760 27.231 1.00 77.40 C ANISOU 1829 CE LYS B 294 8415 11052 9943 888 -912 -520 C ATOM 1830 NZ LYS B 294 23.492 25.517 26.823 1.00 76.63 N ANISOU 1830 NZ LYS B 294 8259 10995 9863 944 -868 -571 N ATOM 1831 N LYS B 295 19.182 24.665 22.195 1.00 44.60 N ANISOU 1831 N LYS B 295 4026 7456 5465 897 -388 -799 N ATOM 1832 CA LYS B 295 19.355 23.307 21.688 1.00 44.55 C ANISOU 1832 CA LYS B 295 4027 7476 5423 946 -329 -878 C ATOM 1833 C LYS B 295 19.124 23.213 20.181 1.00 42.33 C ANISOU 1833 C LYS B 295 3647 7344 5091 964 -249 -891 C ATOM 1834 O LYS B 295 20.010 22.794 19.434 1.00 47.07 O ANISOU 1834 O LYS B 295 4170 8017 5699 1024 -221 -878 O ATOM 1835 CB LYS B 295 18.428 22.332 22.421 1.00 44.60 C ANISOU 1835 CB LYS B 295 4184 7381 5382 928 -311 -976 C ATOM 1836 CG LYS B 295 18.658 20.873 22.053 1.00 50.02 C ANISOU 1836 CG LYS B 295 4907 8069 6029 978 -269 -1059 C ATOM 1837 CD LYS B 295 17.706 19.954 22.802 1.00 56.64 C ANISOU 1837 CD LYS B 295 5899 8802 6821 947 -255 -1149 C ATOM 1838 CE LYS B 295 17.945 18.495 22.441 1.00 58.98 C ANISOU 1838 CE LYS B 295 6249 9091 7071 995 -225 -1232 C ATOM 1839 NZ LYS B 295 16.954 17.585 23.086 1.00 58.65 N ANISOU 1839 NZ LYS B 295 6355 8950 6981 953 -208 -1317 N ATOM 1840 N ASN B 296 17.932 23.605 19.740 1.00 49.08 N ANISOU 1840 N ASN B 296 4510 8243 5894 919 -213 -915 N ATOM 1841 CA ASN B 296 17.567 23.492 18.332 1.00 49.53 C ANISOU 1841 CA ASN B 296 4498 8427 5893 935 -145 -938 C ATOM 1842 C ASN B 296 18.024 24.681 17.491 1.00 47.00 C ANISOU 1842 C ASN B 296 4052 8215 5592 936 -143 -845 C ATOM 1843 O ASN B 296 18.127 24.580 16.270 1.00 46.00 O ANISOU 1843 O ASN B 296 3859 8195 5425 969 -87 -847 O ATOM 1844 CB ASN B 296 16.058 23.256 18.173 1.00 49.81 C ANISOU 1844 CB ASN B 296 4597 8461 5866 889 -113 -1013 C ATOM 1845 CG ASN B 296 15.217 24.415 18.688 1.00 46.06 C ANISOU 1845 CG ASN B 296 4131 7968 5403 828 -141 -976 C ATOM 1846 OD1 ASN B 296 15.650 25.566 18.688 1.00 44.68 O ANISOU 1846 OD1 ASN B 296 3896 7819 5261 820 -176 -892 O ATOM 1847 ND2 ASN B 296 13.999 24.110 19.120 1.00 42.71 N ANISOU 1847 ND2 ASN B 296 3783 7497 4948 786 -126 -1036 N ATOM 1848 N GLY B 297 18.302 25.801 18.151 1.00 49.84 N ANISOU 1848 N GLY B 297 4391 8538 6006 899 -206 -764 N ATOM 1849 CA GLY B 297 18.744 27.001 17.465 1.00 52.27 C ANISOU 1849 CA GLY B 297 4590 8935 6334 887 -215 -668 C ATOM 1850 C GLY B 297 17.711 27.531 16.490 1.00 55.59 C ANISOU 1850 C GLY B 297 4990 9444 6686 864 -172 -686 C ATOM 1851 O GLY B 297 18.055 28.009 15.409 1.00 59.64 O ANISOU 1851 O GLY B 297 5414 10063 7184 880 -138 -640 O ATOM 1852 N LYS B 298 16.442 27.446 16.873 1.00 52.84 N ANISOU 1852 N LYS B 298 4727 9054 6298 829 -171 -751 N ATOM 1853 CA LYS B 298 15.350 27.897 16.018 1.00 52.18 C ANISOU 1853 CA LYS B 298 4628 9046 6153 807 -138 -778 C ATOM 1854 C LYS B 298 14.947 29.333 16.329 1.00 51.88 C ANISOU 1854 C LYS B 298 4586 9004 6123 764 -189 -712 C ATOM 1855 O LYS B 298 14.974 29.759 17.483 1.00 53.29 O ANISOU 1855 O LYS B 298 4821 9089 6337 741 -247 -682 O ATOM 1856 CB LYS B 298 14.138 26.977 16.167 1.00 52.50 C ANISOU 1856 CB LYS B 298 4747 9051 6148 792 -108 -883 C ATOM 1857 CG LYS B 298 14.363 25.571 15.649 1.00 56.14 C ANISOU 1857 CG LYS B 298 5227 9524 6580 834 -61 -955 C ATOM 1858 CD LYS B 298 14.673 25.580 14.166 1.00 59.33 C ANISOU 1858 CD LYS B 298 5558 10044 6939 876 -16 -947 C ATOM 1859 CE LYS B 298 14.796 24.169 13.622 1.00 66.47 C ANISOU 1859 CE LYS B 298 6503 10953 7800 926 26 -1024 C ATOM 1860 NZ LYS B 298 15.008 24.160 12.147 1.00 71.89 N ANISOU 1860 NZ LYS B 298 7140 11747 8429 977 73 -1020 N ATOM 1861 N LEU B 299 14.576 30.076 15.291 1.00 45.25 N ANISOU 1861 N LEU B 299 3691 8260 5241 758 -171 -692 N ATOM 1862 CA LEU B 299 14.076 31.436 15.459 1.00 44.43 C ANISOU 1862 CA LEU B 299 3593 8160 5130 723 -219 -639 C ATOM 1863 C LEU B 299 12.990 31.736 14.433 1.00 47.83 C ANISOU 1863 C LEU B 299 4007 8675 5491 719 -185 -681 C ATOM 1864 O LEU B 299 12.914 31.090 13.389 1.00 48.90 O ANISOU 1864 O LEU B 299 4109 8880 5588 744 -131 -727 O ATOM 1865 CB LEU B 299 15.208 32.462 15.361 1.00 44.17 C ANISOU 1865 CB LEU B 299 3500 8146 5136 715 -266 -524 C ATOM 1866 CG LEU B 299 15.996 32.545 14.053 1.00 41.53 C ANISOU 1866 CG LEU B 299 3064 7923 4792 740 -219 -482 C ATOM 1867 CD1 LEU B 299 16.735 33.870 13.969 1.00 43.67 C ANISOU 1867 CD1 LEU B 299 3284 8214 5094 710 -274 -362 C ATOM 1868 CD2 LEU B 299 16.964 31.381 13.920 1.00 42.86 C ANISOU 1868 CD2 LEU B 299 3195 8098 4993 786 -174 -497 C ATOM 1869 N TYR B 300 12.146 32.714 14.742 1.00 46.63 N ANISOU 1869 N TYR B 300 3885 8512 5318 693 -223 -666 N ATOM 1870 CA TYR B 300 11.009 33.038 13.893 1.00 41.98 C ANISOU 1870 CA TYR B 300 3287 7995 4670 690 -203 -710 C ATOM 1871 C TYR B 300 10.892 34.541 13.691 1.00 47.17 C ANISOU 1871 C TYR B 300 3936 8682 5304 677 -253 -640 C ATOM 1872 O TYR B 300 10.800 35.303 14.655 1.00 50.20 O ANISOU 1872 O TYR B 300 4370 9000 5703 662 -308 -596 O ATOM 1873 CB TYR B 300 9.725 32.483 14.504 1.00 42.13 C ANISOU 1873 CB TYR B 300 3360 7970 4679 676 -189 -790 C ATOM 1874 CG TYR B 300 9.809 31.012 14.823 1.00 39.84 C ANISOU 1874 CG TYR B 300 3094 7634 4409 680 -149 -857 C ATOM 1875 CD1 TYR B 300 10.489 30.565 15.948 1.00 47.97 C ANISOU 1875 CD1 TYR B 300 4172 8569 5486 680 -164 -841 C ATOM 1876 CD2 TYR B 300 9.216 30.067 14.000 1.00 42.61 C ANISOU 1876 CD2 TYR B 300 3434 8030 4728 684 -107 -937 C ATOM 1877 CE1 TYR B 300 10.574 29.219 16.243 1.00 51.33 C ANISOU 1877 CE1 TYR B 300 4631 8948 5923 686 -131 -905 C ATOM 1878 CE2 TYR B 300 9.293 28.719 14.290 1.00 48.36 C ANISOU 1878 CE2 TYR B 300 4198 8710 5466 686 -78 -998 C ATOM 1879 CZ TYR B 300 9.975 28.301 15.412 1.00 52.00 C ANISOU 1879 CZ TYR B 300 4705 9079 5971 687 -88 -982 C ATOM 1880 OH TYR B 300 10.059 26.960 15.708 1.00 55.98 O ANISOU 1880 OH TYR B 300 5257 9531 6480 691 -63 -1044 O ATOM 1881 N VAL B 301 10.890 34.961 12.431 1.00 46.56 N ANISOU 1881 N VAL B 301 3811 8699 5183 687 -236 -630 N ATOM 1882 CA VAL B 301 10.850 36.378 12.104 1.00 45.99 C ANISOU 1882 CA VAL B 301 3736 8658 5080 675 -283 -562 C ATOM 1883 C VAL B 301 9.678 36.704 11.187 1.00 40.21 C ANISOU 1883 C VAL B 301 3005 7995 4279 684 -273 -617 C ATOM 1884 O VAL B 301 9.228 35.859 10.417 1.00 41.74 O ANISOU 1884 O VAL B 301 3180 8232 4447 701 -225 -691 O ATOM 1885 CB VAL B 301 12.172 36.829 11.449 1.00 46.97 C ANISOU 1885 CB VAL B 301 3801 8827 5218 673 -283 -473 C ATOM 1886 CG1 VAL B 301 12.538 35.898 10.304 1.00 44.61 C ANISOU 1886 CG1 VAL B 301 3449 8603 4898 708 -203 -510 C ATOM 1887 CG2 VAL B 301 12.073 38.266 10.970 1.00 44.04 C ANISOU 1887 CG2 VAL B 301 3435 8493 4805 656 -330 -406 C ATOM 1888 N SER B 302 9.177 37.931 11.293 1.00 40.57 N ANISOU 1888 N SER B 302 3081 8042 4293 676 -328 -581 N ATOM 1889 CA SER B 302 8.123 38.414 10.412 1.00 43.12 C ANISOU 1889 CA SER B 302 3404 8429 4549 689 -332 -624 C ATOM 1890 C SER B 302 8.562 39.703 9.730 1.00 40.63 C ANISOU 1890 C SER B 302 3091 8157 4192 685 -372 -548 C ATOM 1891 O SER B 302 9.304 40.502 10.303 1.00 40.67 O ANISOU 1891 O SER B 302 3116 8121 4217 664 -421 -460 O ATOM 1892 CB SER B 302 6.820 38.638 11.182 1.00 44.95 C ANISOU 1892 CB SER B 302 3679 8627 4773 692 -357 -669 C ATOM 1893 OG SER B 302 6.967 39.658 12.154 1.00 40.55 O ANISOU 1893 OG SER B 302 3177 8009 4220 688 -418 -600 O ATOM 1894 N TYR B 303 8.105 39.896 8.498 1.00 55.98 N ANISOU 1894 N TYR B 303 5021 10175 6073 702 -358 -580 N ATOM 1895 CA TYR B 303 8.497 41.053 7.704 1.00 57.76 C ANISOU 1895 CA TYR B 303 5254 10445 6248 698 -388 -513 C ATOM 1896 C TYR B 303 7.631 41.166 6.453 1.00 53.50 C ANISOU 1896 C TYR B 303 4720 9974 5633 726 -378 -576 C ATOM 1897 O TYR B 303 6.938 40.221 6.078 1.00 44.16 O ANISOU 1897 O TYR B 303 3523 8809 4444 746 -344 -666 O ATOM 1898 CB TYR B 303 9.976 40.960 7.315 1.00 57.23 C ANISOU 1898 CB TYR B 303 5141 10397 6209 685 -354 -432 C ATOM 1899 CG TYR B 303 10.324 39.717 6.525 1.00 56.75 C ANISOU 1899 CG TYR B 303 5034 10379 6151 714 -268 -481 C ATOM 1900 CD1 TYR B 303 10.613 38.520 7.168 1.00 57.17 C ANISOU 1900 CD1 TYR B 303 5065 10393 6262 720 -231 -517 C ATOM 1901 CD2 TYR B 303 10.364 39.740 5.138 1.00 59.14 C ANISOU 1901 CD2 TYR B 303 5328 10754 6387 742 -227 -493 C ATOM 1902 CE1 TYR B 303 10.929 37.383 6.452 1.00 59.74 C ANISOU 1902 CE1 TYR B 303 5364 10754 6581 755 -159 -562 C ATOM 1903 CE2 TYR B 303 10.680 38.607 4.414 1.00 61.89 C ANISOU 1903 CE2 TYR B 303 5652 11135 6727 780 -151 -537 C ATOM 1904 CZ TYR B 303 10.961 37.431 5.075 1.00 60.90 C ANISOU 1904 CZ TYR B 303 5507 10973 6660 788 -119 -571 C ATOM 1905 OH TYR B 303 11.276 36.300 4.355 1.00 56.39 O ANISOU 1905 OH TYR B 303 4926 10429 6070 833 -49 -616 O ATOM 1906 N THR B 304 7.672 42.331 5.815 1.00 52.11 N ANISOU 1906 N THR B 304 4573 9830 5398 725 -417 -529 N ATOM 1907 CA THR B 304 6.904 42.567 4.602 1.00 59.22 C ANISOU 1907 CA THR B 304 5492 10789 6219 755 -419 -583 C ATOM 1908 C THR B 304 7.765 42.343 3.363 1.00 62.03 C ANISOU 1908 C THR B 304 5830 11198 6540 767 -361 -557 C ATOM 1909 O THR B 304 8.942 42.697 3.346 1.00 64.77 O ANISOU 1909 O THR B 304 6156 11548 6905 745 -343 -463 O ATOM 1910 CB THR B 304 6.332 43.992 4.577 1.00 62.65 C ANISOU 1910 CB THR B 304 5986 11224 6594 756 -499 -556 C ATOM 1911 OG1 THR B 304 7.408 44.937 4.603 1.00 67.10 O ANISOU 1911 OG1 THR B 304 6568 11778 7150 725 -524 -443 O ATOM 1912 CG2 THR B 304 5.431 44.223 5.779 1.00 59.55 C ANISOU 1912 CG2 THR B 304 5618 10782 6226 760 -548 -581 C ATOM 1913 N THR B 305 7.172 41.759 2.327 1.00 52.85 N ANISOU 1913 N THR B 305 4677 10076 5329 804 -333 -637 N ATOM 1914 CA THR B 305 7.902 41.453 1.102 1.00 51.61 C ANISOU 1914 CA THR B 305 4518 9965 5126 831 -269 -621 C ATOM 1915 C THR B 305 6.982 41.350 -0.109 1.00 54.07 C ANISOU 1915 C THR B 305 4880 10311 5355 874 -279 -704 C ATOM 1916 O THR B 305 5.775 41.165 0.032 1.00 52.08 O ANISOU 1916 O THR B 305 4641 10046 5100 880 -328 -788 O ATOM 1917 CB THR B 305 8.678 40.133 1.230 1.00 52.34 C ANISOU 1917 CB THR B 305 4563 10052 5270 844 -191 -629 C ATOM 1918 OG1 THR B 305 9.402 39.887 0.019 1.00 56.27 O ANISOU 1918 OG1 THR B 305 5066 10598 5714 884 -121 -608 O ATOM 1919 CG2 THR B 305 7.726 38.971 1.488 1.00 50.83 C ANISOU 1919 CG2 THR B 305 4376 9837 5100 858 -193 -741 C ATOM 1920 N ASN B 306 7.561 41.463 -1.299 1.00 65.87 N ANISOU 1920 N ASN B 306 6400 11844 6783 904 -234 -677 N ATOM 1921 CA ASN B 306 6.808 41.309 -2.541 1.00 68.10 C ANISOU 1921 CA ASN B 306 6746 12150 6979 952 -243 -754 C ATOM 1922 C ASN B 306 7.617 40.595 -3.624 1.00 62.39 C ANISOU 1922 C ASN B 306 6043 11455 6208 1002 -154 -746 C ATOM 1923 O ASN B 306 8.382 39.671 -3.341 1.00 54.51 O ANISOU 1923 O ASN B 306 5001 10454 5256 1011 -86 -730 O ATOM 1924 CB ASN B 306 6.319 42.671 -3.046 1.00 70.01 C ANISOU 1924 CB ASN B 306 7048 12406 7148 951 -309 -736 C ATOM 1925 CG ASN B 306 7.388 43.748 -2.958 1.00 70.51 C ANISOU 1925 CG ASN B 306 7107 12481 7202 918 -295 -611 C ATOM 1926 OD1 ASN B 306 8.583 43.455 -2.868 1.00 66.90 O ANISOU 1926 OD1 ASN B 306 6602 12034 6781 906 -221 -535 O ATOM 1927 ND2 ASN B 306 6.961 45.004 -2.987 1.00 72.28 N ANISOU 1927 ND2 ASN B 306 7381 12701 7379 902 -369 -587 N ATOM 1928 N ASP B 316 -0.378 44.814 -3.069 1.00 82.33 N ANISOU 1928 N ASP B 316 8711 13960 8612 1028 -748 -1086 N ATOM 1929 CA ASP B 316 0.707 45.657 -2.576 1.00 92.72 C ANISOU 1929 CA ASP B 316 10045 15267 9916 1001 -721 -979 C ATOM 1930 C ASP B 316 1.908 44.821 -2.137 1.00 95.29 C ANISOU 1930 C ASP B 316 10323 15581 10302 967 -628 -925 C ATOM 1931 O ASP B 316 2.854 44.629 -2.901 1.00101.41 O ANISOU 1931 O ASP B 316 11120 16368 11042 971 -570 -887 O ATOM 1932 CB ASP B 316 0.220 46.537 -1.420 1.00 97.75 C ANISOU 1932 CB ASP B 316 10673 15889 10577 993 -776 -951 C ATOM 1933 CG ASP B 316 1.247 47.578 -0.999 1.00 97.95 C ANISOU 1933 CG ASP B 316 10741 15897 10579 965 -778 -839 C ATOM 1934 OD1 ASP B 316 0.835 48.639 -0.484 1.00 99.79 O ANISOU 1934 OD1 ASP B 316 11016 16116 10783 975 -846 -814 O ATOM 1935 OD2 ASP B 316 2.460 47.341 -1.181 1.00 94.28 O ANISOU 1935 OD2 ASP B 316 10269 15430 10123 935 -715 -772 O ATOM 1936 N HIS B 317 1.868 44.330 -0.902 1.00 68.80 N ANISOU 1936 N HIS B 317 6904 12200 7036 938 -612 -920 N ATOM 1937 CA HIS B 317 2.961 43.526 -0.369 1.00 63.12 C ANISOU 1937 CA HIS B 317 6139 11464 6381 908 -534 -873 C ATOM 1938 C HIS B 317 2.449 42.320 0.413 1.00 54.97 C ANISOU 1938 C HIS B 317 5047 10408 5431 896 -512 -935 C ATOM 1939 O HIS B 317 1.267 41.987 0.357 1.00 54.29 O ANISOU 1939 O HIS B 317 4948 10326 5354 908 -550 -1016 O ATOM 1940 CB HIS B 317 3.878 44.378 0.511 1.00 68.93 C ANISOU 1940 CB HIS B 317 6875 12176 7140 873 -537 -765 C ATOM 1941 CG HIS B 317 3.210 44.914 1.740 1.00 75.52 C ANISOU 1941 CG HIS B 317 7708 12976 8009 863 -593 -761 C ATOM 1942 ND1 HIS B 317 3.299 44.290 2.966 1.00 77.65 N ANISOU 1942 ND1 HIS B 317 7935 13206 8363 841 -571 -757 N ATOM 1943 CD2 HIS B 317 2.446 46.014 1.933 1.00 79.55 C ANISOU 1943 CD2 HIS B 317 8265 13484 8475 881 -670 -760 C ATOM 1944 CE1 HIS B 317 2.618 44.982 3.861 1.00 78.24 C ANISOU 1944 CE1 HIS B 317 8031 13254 8442 847 -625 -751 C ATOM 1945 NE2 HIS B 317 2.090 46.035 3.260 1.00 78.64 N ANISOU 1945 NE2 HIS B 317 8136 13330 8416 874 -686 -753 N ATOM 1946 N ILE B 318 3.348 41.667 1.141 1.00 67.21 N ANISOU 1946 N ILE B 318 6560 11933 7045 870 -454 -894 N ATOM 1947 CA ILE B 318 2.997 40.477 1.908 1.00 63.35 C ANISOU 1947 CA ILE B 318 6026 11414 6631 855 -428 -947 C ATOM 1948 C ILE B 318 3.657 40.466 3.284 1.00 62.99 C ANISOU 1948 C ILE B 318 5954 11323 6656 822 -408 -885 C ATOM 1949 O ILE B 318 4.862 40.683 3.404 1.00 61.16 O ANISOU 1949 O ILE B 318 5721 11084 6434 810 -380 -807 O ATOM 1950 CB ILE B 318 3.386 39.188 1.153 1.00 58.82 C ANISOU 1950 CB ILE B 318 5448 10847 6054 870 -372 -992 C ATOM 1951 CG1 ILE B 318 2.296 38.815 0.149 1.00 61.20 C ANISOU 1951 CG1 ILE B 318 5774 11169 6312 896 -410 -1085 C ATOM 1952 CG2 ILE B 318 3.610 38.040 2.122 1.00 55.24 C ANISOU 1952 CG2 ILE B 318 4956 10352 5680 845 -331 -1008 C ATOM 1953 CD1 ILE B 318 2.494 37.454 -0.481 1.00 64.50 C ANISOU 1953 CD1 ILE B 318 6205 11578 6724 912 -371 -1139 C ATOM 1954 N LEU B 319 2.860 40.220 4.321 1.00 53.41 N ANISOU 1954 N LEU B 319 4723 10077 5495 809 -424 -918 N ATOM 1955 CA LEU B 319 3.400 40.019 5.659 1.00 49.43 C ANISOU 1955 CA LEU B 319 4208 9517 5058 783 -405 -873 C ATOM 1956 C LEU B 319 3.731 38.543 5.829 1.00 48.45 C ANISOU 1956 C LEU B 319 4055 9370 4984 771 -346 -914 C ATOM 1957 O LEU B 319 2.838 37.704 5.925 1.00 46.36 O ANISOU 1957 O LEU B 319 3773 9099 4742 765 -339 -989 O ATOM 1958 CB LEU B 319 2.403 40.469 6.726 1.00 44.73 C ANISOU 1958 CB LEU B 319 3620 8891 4484 783 -441 -883 C ATOM 1959 CG LEU B 319 2.970 40.692 8.133 1.00 43.76 C ANISOU 1959 CG LEU B 319 3519 8699 4408 766 -441 -819 C ATOM 1960 CD1 LEU B 319 1.955 41.404 9.009 1.00 40.51 C ANISOU 1960 CD1 LEU B 319 3134 8265 3991 786 -479 -821 C ATOM 1961 CD2 LEU B 319 3.417 39.387 8.779 1.00 41.43 C ANISOU 1961 CD2 LEU B 319 3201 8360 4181 744 -386 -839 C ATOM 1962 N ARG B 320 5.021 38.236 5.865 1.00 48.86 N ANISOU 1962 N ARG B 320 4101 9409 5054 766 -307 -861 N ATOM 1963 CA ARG B 320 5.481 36.857 5.916 1.00 51.24 C ANISOU 1963 CA ARG B 320 4386 9692 5392 765 -252 -896 C ATOM 1964 C ARG B 320 6.047 36.516 7.288 1.00 54.43 C ANISOU 1964 C ARG B 320 4785 10028 5867 741 -240 -862 C ATOM 1965 O ARG B 320 6.653 37.359 7.948 1.00 59.27 O ANISOU 1965 O ARG B 320 5407 10615 6499 729 -266 -784 O ATOM 1966 CB ARG B 320 6.537 36.623 4.834 1.00 56.47 C ANISOU 1966 CB ARG B 320 5043 10395 6018 793 -208 -869 C ATOM 1967 CG ARG B 320 7.088 35.213 4.782 1.00 58.57 C ANISOU 1967 CG ARG B 320 5302 10645 6308 807 -152 -904 C ATOM 1968 CD ARG B 320 8.102 35.073 3.658 1.00 58.99 C ANISOU 1968 CD ARG B 320 5353 10745 6315 850 -100 -871 C ATOM 1969 NE ARG B 320 7.507 35.354 2.353 1.00 59.76 N ANISOU 1969 NE ARG B 320 5483 10891 6330 880 -111 -908 N ATOM 1970 CZ ARG B 320 8.182 35.360 1.208 1.00 53.57 C ANISOU 1970 CZ ARG B 320 4716 10153 5487 925 -66 -884 C ATOM 1971 NH1 ARG B 320 9.483 35.100 1.198 1.00 49.77 N ANISOU 1971 NH1 ARG B 320 4205 9683 5023 946 -1 -818 N ATOM 1972 NH2 ARG B 320 7.555 35.626 0.072 1.00 52.88 N ANISOU 1972 NH2 ARG B 320 4674 10096 5320 954 -84 -924 N ATOM 1973 N VAL B 321 5.836 35.277 7.716 1.00 49.70 N ANISOU 1973 N VAL B 321 4183 9393 5305 734 -209 -920 N ATOM 1974 CA VAL B 321 6.371 34.798 8.985 1.00 46.64 C ANISOU 1974 CA VAL B 321 3805 8934 4981 716 -196 -898 C ATOM 1975 C VAL B 321 7.156 33.515 8.752 1.00 46.82 C ANISOU 1975 C VAL B 321 3823 8946 5021 729 -147 -924 C ATOM 1976 O VAL B 321 6.572 32.448 8.571 1.00 52.31 O ANISOU 1976 O VAL B 321 4529 9633 5714 727 -128 -1001 O ATOM 1977 CB VAL B 321 5.254 34.518 10.007 1.00 43.31 C ANISOU 1977 CB VAL B 321 3401 8463 4592 693 -206 -944 C ATOM 1978 CG1 VAL B 321 5.851 34.051 11.326 1.00 42.51 C ANISOU 1978 CG1 VAL B 321 3327 8277 4549 678 -194 -919 C ATOM 1979 CG2 VAL B 321 4.389 35.758 10.212 1.00 42.78 C ANISOU 1979 CG2 VAL B 321 3341 8410 4502 695 -251 -923 C ATOM 1980 N VAL B 322 8.479 33.618 8.757 1.00 50.34 N ANISOU 1980 N VAL B 322 4253 9392 5484 742 -130 -856 N ATOM 1981 CA VAL B 322 9.324 32.468 8.455 1.00 55.25 C ANISOU 1981 CA VAL B 322 4867 10012 6113 770 -80 -874 C ATOM 1982 C VAL B 322 10.110 31.963 9.659 1.00 57.48 C ANISOU 1982 C VAL B 322 5156 10221 6463 761 -77 -848 C ATOM 1983 O VAL B 322 10.319 32.687 10.633 1.00 58.10 O ANISOU 1983 O VAL B 322 5241 10253 6583 736 -116 -792 O ATOM 1984 CB VAL B 322 10.314 32.781 7.320 1.00 57.21 C ANISOU 1984 CB VAL B 322 5082 10331 6326 809 -47 -820 C ATOM 1985 CG1 VAL B 322 9.568 33.019 6.023 1.00 63.11 C ANISOU 1985 CG1 VAL B 322 5842 11141 6995 829 -44 -861 C ATOM 1986 CG2 VAL B 322 11.165 33.984 7.680 1.00 55.57 C ANISOU 1986 CG2 VAL B 322 4841 10127 6148 790 -72 -710 C ATOM 1987 N GLU B 323 10.541 30.708 9.577 1.00 49.68 N ANISOU 1987 N GLU B 323 4178 9216 5481 787 -38 -892 N ATOM 1988 CA GLU B 323 11.392 30.113 10.595 1.00 45.24 C ANISOU 1988 CA GLU B 323 3626 8585 4978 789 -36 -873 C ATOM 1989 C GLU B 323 12.803 29.950 10.056 1.00 46.85 C ANISOU 1989 C GLU B 323 3782 8828 5190 835 -1 -816 C ATOM 1990 O GLU B 323 13.017 29.257 9.065 1.00 50.53 O ANISOU 1990 O GLU B 323 4246 9344 5611 882 47 -849 O ATOM 1991 CB GLU B 323 10.860 28.743 11.009 1.00 42.74 C ANISOU 1991 CB GLU B 323 3365 8211 4662 786 -19 -964 C ATOM 1992 CG GLU B 323 11.660 28.095 12.126 1.00 45.04 C ANISOU 1992 CG GLU B 323 3684 8421 5010 789 -22 -953 C ATOM 1993 CD GLU B 323 11.831 26.603 11.936 1.00 47.94 C ANISOU 1993 CD GLU B 323 4092 8765 5359 820 11 -1026 C ATOM 1994 OE1 GLU B 323 11.190 25.827 12.676 1.00 52.08 O ANISOU 1994 OE1 GLU B 323 4679 9217 5893 792 5 -1087 O ATOM 1995 OE2 GLU B 323 12.607 26.207 11.040 1.00 43.79 O ANISOU 1995 OE2 GLU B 323 3542 8291 4804 876 46 -1020 O ATOM 1996 N TYR B 324 13.765 30.592 10.709 1.00 46.39 N ANISOU 1996 N TYR B 324 3689 8747 5190 824 -27 -728 N ATOM 1997 CA TYR B 324 15.166 30.438 10.344 1.00 43.88 C ANISOU 1997 CA TYR B 324 3308 8465 4898 865 5 -663 C ATOM 1998 C TYR B 324 15.882 29.537 11.345 1.00 42.93 C ANISOU 1998 C TYR B 324 3203 8269 4839 880 -2 -672 C ATOM 1999 O TYR B 324 15.314 29.161 12.369 1.00 44.97 O ANISOU 1999 O TYR B 324 3528 8440 5118 852 -36 -720 O ATOM 2000 CB TYR B 324 15.860 31.799 10.269 1.00 46.69 C ANISOU 2000 CB TYR B 324 3600 8854 5285 839 -25 -546 C ATOM 2001 CG TYR B 324 15.673 32.520 8.953 1.00 51.94 C ANISOU 2001 CG TYR B 324 4234 9615 5885 849 6 -520 C ATOM 2002 CD1 TYR B 324 16.426 32.174 7.838 1.00 56.30 C ANISOU 2002 CD1 TYR B 324 4736 10246 6407 906 81 -498 C ATOM 2003 CD2 TYR B 324 14.752 33.550 8.827 1.00 51.74 C ANISOU 2003 CD2 TYR B 324 4237 9598 5823 810 -37 -518 C ATOM 2004 CE1 TYR B 324 16.263 32.830 6.635 1.00 57.77 C ANISOU 2004 CE1 TYR B 324 4909 10514 6528 918 112 -474 C ATOM 2005 CE2 TYR B 324 14.582 34.212 7.628 1.00 54.91 C ANISOU 2005 CE2 TYR B 324 4622 10080 6160 821 -13 -498 C ATOM 2006 CZ TYR B 324 15.339 33.848 6.534 1.00 59.79 C ANISOU 2006 CZ TYR B 324 5198 10772 6749 873 62 -476 C ATOM 2007 OH TYR B 324 15.172 34.505 5.337 1.00 65.67 O ANISOU 2007 OH TYR B 324 5939 11589 7423 887 88 -455 O ATOM 2008 N THR B 325 17.130 29.197 11.043 1.00 45.12 N ANISOU 2008 N THR B 325 3420 8579 5145 928 31 -623 N ATOM 2009 CA THR B 325 17.930 28.339 11.910 1.00 47.17 C ANISOU 2009 CA THR B 325 3689 8772 5463 952 21 -629 C ATOM 2010 C THR B 325 19.389 28.773 11.908 1.00 44.79 C ANISOU 2010 C THR B 325 3285 8502 5231 972 18 -518 C ATOM 2011 O THR B 325 20.051 28.739 10.876 1.00 48.35 O ANISOU 2011 O THR B 325 3663 9045 5663 1022 83 -479 O ATOM 2012 CB THR B 325 17.864 26.870 11.460 1.00 49.35 C ANISOU 2012 CB THR B 325 4010 9052 5688 1017 78 -721 C ATOM 2013 OG1 THR B 325 16.514 26.398 11.549 1.00 47.16 O ANISOU 2013 OG1 THR B 325 3825 8736 5359 987 71 -821 O ATOM 2014 CG2 THR B 325 18.758 26.008 12.329 1.00 48.29 C ANISOU 2014 CG2 THR B 325 3889 8850 5611 1050 65 -726 C ATOM 2015 N VAL B 326 19.888 29.185 13.067 1.00 51.57 N ANISOU 2015 N VAL B 326 4142 9281 6172 935 -57 -464 N ATOM 2016 CA VAL B 326 21.282 29.595 13.196 1.00 55.69 C ANISOU 2016 CA VAL B 326 4560 9821 6778 943 -77 -353 C ATOM 2017 C VAL B 326 22.200 28.582 12.507 1.00 53.56 C ANISOU 2017 C VAL B 326 4227 9617 6507 1031 4 -359 C ATOM 2018 O VAL B 326 21.885 27.394 12.439 1.00 54.91 O ANISOU 2018 O VAL B 326 4464 9769 6631 1083 43 -457 O ATOM 2019 CB VAL B 326 21.679 29.768 14.685 1.00 56.24 C ANISOU 2019 CB VAL B 326 4666 9767 6935 905 -180 -322 C ATOM 2020 CG1 VAL B 326 21.467 28.472 15.447 1.00 49.15 C ANISOU 2020 CG1 VAL B 326 3862 8781 6032 939 -180 -423 C ATOM 2021 CG2 VAL B 326 23.117 30.247 14.810 1.00 56.70 C ANISOU 2021 CG2 VAL B 326 4608 9843 7093 904 -216 -200 C ATOM 2022 N SER B 327 23.322 29.056 11.975 1.00 47.17 N ANISOU 2022 N SER B 327 3291 8886 5747 1051 30 -252 N ATOM 2023 CA SER B 327 24.275 28.166 11.325 1.00 51.55 C ANISOU 2023 CA SER B 327 3775 9510 6303 1147 114 -244 C ATOM 2024 C SER B 327 24.940 27.264 12.357 1.00 57.99 C ANISOU 2024 C SER B 327 4606 10242 7187 1181 71 -269 C ATOM 2025 O SER B 327 25.179 27.680 13.490 1.00 61.80 O ANISOU 2025 O SER B 327 5097 10633 7752 1125 -28 -233 O ATOM 2026 CB SER B 327 25.333 28.965 10.558 1.00 59.89 C ANISOU 2026 CB SER B 327 4679 10673 7406 1154 158 -109 C ATOM 2027 OG SER B 327 26.191 29.669 11.438 1.00 61.02 O ANISOU 2027 OG SER B 327 4743 10772 7671 1097 69 -4 O ATOM 2028 N ARG B 328 25.232 26.027 11.966 1.00 71.31 N ANISOU 2028 N ARG B 328 6310 11952 8833 1279 140 -333 N ATOM 2029 CA ARG B 328 25.863 25.075 12.874 1.00 73.12 C ANISOU 2029 CA ARG B 328 6565 12103 9115 1324 102 -366 C ATOM 2030 C ARG B 328 27.375 25.280 12.921 1.00 68.04 C ANISOU 2030 C ARG B 328 5767 11507 8578 1363 101 -250 C ATOM 2031 O ARG B 328 28.115 24.417 13.393 1.00 67.14 O ANISOU 2031 O ARG B 328 5646 11359 8505 1429 90 -268 O ATOM 2032 CB ARG B 328 25.533 23.634 12.472 1.00 79.67 C ANISOU 2032 CB ARG B 328 7492 12929 9849 1415 166 -486 C ATOM 2033 CG ARG B 328 26.128 23.204 11.141 1.00 88.93 C ANISOU 2033 CG ARG B 328 8595 14227 10965 1524 282 -466 C ATOM 2034 CD ARG B 328 26.033 21.698 10.947 1.00 96.60 C ANISOU 2034 CD ARG B 328 9674 15174 11855 1626 323 -577 C ATOM 2035 NE ARG B 328 26.849 21.244 9.824 1.00105.23 N ANISOU 2035 NE ARG B 328 10700 16379 12904 1752 431 -545 N ATOM 2036 CZ ARG B 328 28.129 20.895 9.921 1.00109.51 C ANISOU 2036 CZ ARG B 328 11143 16957 13509 1839 456 -486 C ATOM 2037 NH1 ARG B 328 28.743 20.943 11.096 1.00107.97 N ANISOU 2037 NH1 ARG B 328 10907 16689 13427 1808 371 -456 N ATOM 2038 NH2 ARG B 328 28.795 20.496 8.845 1.00111.35 N ANISOU 2038 NH2 ARG B 328 11320 17297 13691 1963 567 -457 N ATOM 2039 N LYS B 329 27.827 26.429 12.431 1.00 57.14 N ANISOU 2039 N LYS B 329 4261 10205 7244 1319 110 -130 N ATOM 2040 CA LYS B 329 29.248 26.745 12.419 1.00 61.19 C ANISOU 2040 CA LYS B 329 4605 10773 7871 1342 110 -2 C ATOM 2041 C LYS B 329 29.509 28.098 13.082 1.00 58.08 C ANISOU 2041 C LYS B 329 4150 10338 7580 1224 -1 111 C ATOM 2042 O LYS B 329 30.554 28.313 13.698 1.00 56.07 O ANISOU 2042 O LYS B 329 3796 10059 7448 1211 -69 200 O ATOM 2043 CB LYS B 329 29.779 26.737 10.982 1.00 70.82 C ANISOU 2043 CB LYS B 329 5711 12149 9049 1419 250 56 C ATOM 2044 CG LYS B 329 31.288 26.572 10.868 1.00 75.68 C ANISOU 2044 CG LYS B 329 6153 12836 9768 1487 285 163 C ATOM 2045 CD LYS B 329 31.714 26.333 9.423 1.00 77.16 C ANISOU 2045 CD LYS B 329 6256 13173 9888 1590 447 201 C ATOM 2046 CE LYS B 329 33.199 25.998 9.331 1.00 79.29 C ANISOU 2046 CE LYS B 329 6351 13518 10256 1677 496 299 C ATOM 2047 NZ LYS B 329 33.617 25.655 7.942 1.00 79.09 N ANISOU 2047 NZ LYS B 329 6259 13637 10155 1800 668 332 N ATOM 2048 N ASN B 330 28.548 29.006 12.950 1.00 51.88 N ANISOU 2048 N ASN B 330 3429 9541 6744 1140 -27 108 N ATOM 2049 CA ASN B 330 28.653 30.328 13.554 1.00 55.01 C ANISOU 2049 CA ASN B 330 3798 9888 7215 1029 -139 208 C ATOM 2050 C ASN B 330 27.403 30.672 14.355 1.00 53.52 C ANISOU 2050 C ASN B 330 3775 9584 6975 961 -224 131 C ATOM 2051 O ASN B 330 26.394 31.093 13.789 1.00 51.82 O ANISOU 2051 O ASN B 330 3619 9400 6668 935 -188 92 O ATOM 2052 CB ASN B 330 28.893 31.390 12.480 1.00 60.57 C ANISOU 2052 CB ASN B 330 4391 10710 7912 993 -84 318 C ATOM 2053 CG ASN B 330 29.214 32.751 13.069 1.00 62.65 C ANISOU 2053 CG ASN B 330 4615 10926 8264 879 -208 439 C ATOM 2054 OD1 ASN B 330 29.278 32.915 14.287 1.00 62.37 O ANISOU 2054 OD1 ASN B 330 4637 10765 8295 832 -338 443 O ATOM 2055 ND2 ASN B 330 29.420 33.737 12.202 1.00 64.49 N ANISOU 2055 ND2 ASN B 330 4761 11250 8492 835 -172 541 N ATOM 2056 N PRO B 331 27.467 30.494 15.683 1.00 63.89 N ANISOU 2056 N PRO B 331 5166 10762 8348 936 -335 109 N ATOM 2057 CA PRO B 331 26.330 30.748 16.574 1.00 62.69 C ANISOU 2057 CA PRO B 331 5178 10491 8151 883 -411 39 C ATOM 2058 C PRO B 331 25.855 32.197 16.514 1.00 61.28 C ANISOU 2058 C PRO B 331 5012 10312 7961 796 -468 110 C ATOM 2059 O PRO B 331 24.825 32.527 17.104 1.00 59.75 O ANISOU 2059 O PRO B 331 4949 10038 7717 759 -517 58 O ATOM 2060 CB PRO B 331 26.900 30.437 17.963 1.00 61.17 C ANISOU 2060 CB PRO B 331 5037 10160 8047 879 -525 43 C ATOM 2061 CG PRO B 331 28.045 29.515 17.707 1.00 61.25 C ANISOU 2061 CG PRO B 331 4937 10219 8115 957 -481 57 C ATOM 2062 CD PRO B 331 28.637 29.978 16.414 1.00 64.54 C ANISOU 2062 CD PRO B 331 5187 10793 8540 969 -392 148 C ATOM 2063 N HIS B 332 26.597 33.043 15.805 1.00 55.58 N ANISOU 2063 N HIS B 332 4158 9679 7282 767 -461 230 N ATOM 2064 CA HIS B 332 26.283 34.466 15.731 1.00 55.97 C ANISOU 2064 CA HIS B 332 4218 9726 7323 682 -526 310 C ATOM 2065 C HIS B 332 25.762 34.877 14.358 1.00 56.78 C ANISOU 2065 C HIS B 332 4282 9957 7334 686 -421 310 C ATOM 2066 O HIS B 332 25.797 36.056 14.006 1.00 56.13 O ANISOU 2066 O HIS B 332 4171 9905 7251 623 -456 399 O ATOM 2067 CB HIS B 332 27.517 35.304 16.073 1.00 56.52 C ANISOU 2067 CB HIS B 332 4180 9778 7516 624 -625 462 C ATOM 2068 CG HIS B 332 28.223 34.861 17.315 1.00 56.58 C ANISOU 2068 CG HIS B 332 4208 9665 7626 628 -732 472 C ATOM 2069 ND1 HIS B 332 27.869 35.303 18.571 1.00 55.07 N ANISOU 2069 ND1 HIS B 332 4156 9319 7451 582 -872 466 N ATOM 2070 CD2 HIS B 332 29.269 34.019 17.494 1.00 57.67 C ANISOU 2070 CD2 HIS B 332 4250 9810 7851 680 -721 488 C ATOM 2071 CE1 HIS B 332 28.663 34.751 19.471 1.00 57.01 C ANISOU 2071 CE1 HIS B 332 4397 9476 7789 601 -949 475 C ATOM 2072 NE2 HIS B 332 29.522 33.968 18.843 1.00 57.02 N ANISOU 2072 NE2 HIS B 332 4252 9575 7838 660 -861 488 N ATOM 2073 N GLN B 333 25.285 33.907 13.584 1.00 67.39 N ANISOU 2073 N GLN B 333 5637 11370 8598 759 -300 211 N ATOM 2074 CA GLN B 333 24.743 34.188 12.257 1.00 68.18 C ANISOU 2074 CA GLN B 333 5719 11584 8603 774 -202 199 C ATOM 2075 C GLN B 333 23.852 33.053 11.766 1.00 59.53 C ANISOU 2075 C GLN B 333 4700 10512 7409 846 -110 57 C ATOM 2076 O GLN B 333 24.257 31.892 11.749 1.00 54.01 O ANISOU 2076 O GLN B 333 3987 9819 6717 917 -57 7 O ATOM 2077 CB GLN B 333 25.869 34.449 11.255 1.00 75.98 C ANISOU 2077 CB GLN B 333 6550 12692 9629 793 -127 312 C ATOM 2078 CG GLN B 333 25.381 34.803 9.861 1.00 83.60 C ANISOU 2078 CG GLN B 333 7506 13767 10490 810 -27 308 C ATOM 2079 CD GLN B 333 26.512 35.170 8.921 1.00 91.89 C ANISOU 2079 CD GLN B 333 8404 14931 11578 823 51 434 C ATOM 2080 OE1 GLN B 333 27.617 35.494 9.358 1.00 93.77 O ANISOU 2080 OE1 GLN B 333 8532 15165 11931 790 7 547 O ATOM 2081 NE2 GLN B 333 26.240 35.124 7.621 1.00 93.44 N ANISOU 2081 NE2 GLN B 333 8595 15228 11678 872 167 418 N ATOM 2082 N VAL B 334 22.636 33.400 11.362 1.00 54.58 N ANISOU 2082 N VAL B 334 4156 9893 6688 827 -100 -6 N ATOM 2083 CA VAL B 334 21.661 32.405 10.934 1.00 58.19 C ANISOU 2083 CA VAL B 334 4693 10361 7054 879 -33 -138 C ATOM 2084 C VAL B 334 21.897 31.954 9.493 1.00 62.11 C ANISOU 2084 C VAL B 334 5138 10975 7485 950 85 -147 C ATOM 2085 O VAL B 334 22.229 32.760 8.623 1.00 65.97 O ANISOU 2085 O VAL B 334 5561 11545 7958 941 120 -67 O ATOM 2086 CB VAL B 334 20.215 32.929 11.095 1.00 55.27 C ANISOU 2086 CB VAL B 334 4429 9954 6617 833 -74 -204 C ATOM 2087 CG1 VAL B 334 20.030 34.224 10.330 1.00 55.91 C ANISOU 2087 CG1 VAL B 334 4481 10099 6662 793 -81 -134 C ATOM 2088 CG2 VAL B 334 19.215 31.886 10.635 1.00 50.63 C ANISOU 2088 CG2 VAL B 334 3914 9376 5946 877 -14 -334 C ATOM 2089 N ASP B 335 21.735 30.655 9.255 1.00 65.55 N ANISOU 2089 N ASP B 335 5615 11413 7878 1023 145 -242 N ATOM 2090 CA ASP B 335 21.851 30.095 7.913 1.00 66.88 C ANISOU 2090 CA ASP B 335 5768 11677 7967 1105 254 -266 C ATOM 2091 C ASP B 335 20.624 30.473 7.089 1.00 63.03 C ANISOU 2091 C ASP B 335 5353 11218 7377 1089 267 -324 C ATOM 2092 O ASP B 335 19.500 30.098 7.423 1.00 59.87 O ANISOU 2092 O ASP B 335 5049 10761 6938 1068 231 -425 O ATOM 2093 CB ASP B 335 21.998 28.572 7.981 1.00 69.61 C ANISOU 2093 CB ASP B 335 6159 12000 8290 1189 297 -355 C ATOM 2094 CG ASP B 335 22.262 27.946 6.625 1.00 75.48 C ANISOU 2094 CG ASP B 335 6896 12834 8947 1291 409 -372 C ATOM 2095 OD1 ASP B 335 22.337 26.702 6.551 1.00 74.40 O ANISOU 2095 OD1 ASP B 335 6813 12681 8774 1369 444 -448 O ATOM 2096 OD2 ASP B 335 22.396 28.696 5.634 1.00 79.94 O ANISOU 2096 OD2 ASP B 335 7414 13484 9476 1297 460 -309 O ATOM 2097 N LEU B 336 20.846 31.223 6.015 1.00 53.00 N ANISOU 2097 N LEU B 336 4035 10036 6067 1098 317 -259 N ATOM 2098 CA LEU B 336 19.748 31.721 5.195 1.00 52.28 C ANISOU 2098 CA LEU B 336 4010 9972 5881 1083 320 -305 C ATOM 2099 C LEU B 336 19.119 30.628 4.332 1.00 48.89 C ANISOU 2099 C LEU B 336 3663 9560 5352 1160 379 -416 C ATOM 2100 O LEU B 336 18.033 30.812 3.781 1.00 46.88 O ANISOU 2100 O LEU B 336 3481 9308 5022 1148 363 -480 O ATOM 2101 CB LEU B 336 20.223 32.885 4.323 1.00 52.25 C ANISOU 2101 CB LEU B 336 3942 10049 5860 1068 352 -197 C ATOM 2102 CG LEU B 336 20.431 34.216 5.048 1.00 48.08 C ANISOU 2102 CG LEU B 336 3370 9494 5404 971 266 -99 C ATOM 2103 CD1 LEU B 336 21.254 35.178 4.206 1.00 48.41 C ANISOU 2103 CD1 LEU B 336 3329 9618 5446 960 311 28 C ATOM 2104 CD2 LEU B 336 19.088 34.829 5.413 1.00 48.07 C ANISOU 2104 CD2 LEU B 336 3463 9440 5364 911 182 -162 C ATOM 2105 N ARG B 337 19.804 29.493 4.221 1.00 62.83 N ANISOU 2105 N ARG B 337 5422 11333 7116 1241 438 -438 N ATOM 2106 CA ARG B 337 19.318 28.377 3.415 1.00 65.97 C ANISOU 2106 CA ARG B 337 5912 11738 7416 1322 487 -539 C ATOM 2107 C ARG B 337 18.214 27.624 4.146 1.00 64.97 C ANISOU 2107 C ARG B 337 5884 11521 7282 1286 418 -658 C ATOM 2108 O ARG B 337 17.381 26.957 3.529 1.00 68.35 O ANISOU 2108 O ARG B 337 6405 11939 7627 1315 423 -751 O ATOM 2109 CB ARG B 337 20.462 27.416 3.083 1.00 66.28 C ANISOU 2109 CB ARG B 337 5919 11812 7451 1431 572 -519 C ATOM 2110 CG ARG B 337 21.704 28.087 2.524 1.00 70.17 C ANISOU 2110 CG ARG B 337 6291 12398 7975 1467 649 -386 C ATOM 2111 CD ARG B 337 22.651 27.066 1.911 1.00 78.21 C ANISOU 2111 CD ARG B 337 7294 13465 8957 1601 752 -380 C ATOM 2112 NE ARG B 337 22.977 25.982 2.834 1.00 82.56 N ANISOU 2112 NE ARG B 337 7862 13953 9556 1631 724 -431 N ATOM 2113 CZ ARG B 337 24.095 25.919 3.552 1.00 85.52 C ANISOU 2113 CZ ARG B 337 8129 14331 10034 1642 727 -358 C ATOM 2114 NH1 ARG B 337 24.306 24.892 4.364 1.00 85.65 N ANISOU 2114 NH1 ARG B 337 8181 14282 10082 1674 695 -418 N ATOM 2115 NH2 ARG B 337 25.003 26.881 3.456 1.00 85.05 N ANISOU 2115 NH2 ARG B 337 7928 14339 10050 1617 755 -224 N ATOM 2116 N THR B 338 18.219 27.745 5.469 1.00 70.04 N ANISOU 2116 N THR B 338 6508 12092 8012 1220 352 -650 N ATOM 2117 CA THR B 338 17.303 27.009 6.328 1.00 64.31 C ANISOU 2117 CA THR B 338 5868 11275 7292 1182 295 -749 C ATOM 2118 C THR B 338 15.966 27.720 6.473 1.00 63.05 C ANISOU 2118 C THR B 338 5747 11093 7115 1103 236 -786 C ATOM 2119 O THR B 338 15.152 27.361 7.325 1.00 64.47 O ANISOU 2119 O THR B 338 5982 11200 7315 1055 188 -849 O ATOM 2120 CB THR B 338 17.898 26.848 7.727 1.00 53.50 C ANISOU 2120 CB THR B 338 4475 9833 6021 1152 252 -723 C ATOM 2121 OG1 THR B 338 18.042 28.141 8.327 1.00 48.04 O ANISOU 2121 OG1 THR B 338 3724 9134 5395 1081 200 -636 O ATOM 2122 CG2 THR B 338 19.262 26.177 7.645 1.00 52.25 C ANISOU 2122 CG2 THR B 338 4264 9698 5890 1234 304 -682 C ATOM 2123 N ALA B 339 15.748 28.739 5.648 1.00 55.26 N ANISOU 2123 N ALA B 339 4734 10171 6092 1093 243 -743 N ATOM 2124 CA ALA B 339 14.501 29.488 5.682 1.00 49.66 C ANISOU 2124 CA ALA B 339 4056 9450 5361 1029 188 -774 C ATOM 2125 C ALA B 339 13.328 28.545 5.463 1.00 50.21 C ANISOU 2125 C ALA B 339 4211 9488 5380 1032 174 -893 C ATOM 2126 O ALA B 339 13.412 27.615 4.658 1.00 55.41 O ANISOU 2126 O ALA B 339 4912 10163 5978 1094 214 -943 O ATOM 2127 CB ALA B 339 14.510 30.579 4.628 1.00 53.85 C ANISOU 2127 CB ALA B 339 4560 10058 5842 1035 203 -718 C ATOM 2128 N ARG B 340 12.240 28.783 6.186 1.00 47.38 N ANISOU 2128 N ARG B 340 3877 9081 5043 966 116 -934 N ATOM 2129 CA ARG B 340 11.063 27.929 6.100 1.00 48.55 C ANISOU 2129 CA ARG B 340 4092 9195 5160 951 95 -1038 C ATOM 2130 C ARG B 340 9.812 28.739 6.407 1.00 54.98 C ANISOU 2130 C ARG B 340 4905 10003 5984 887 40 -1055 C ATOM 2131 O ARG B 340 9.538 29.059 7.564 1.00 57.71 O ANISOU 2131 O ARG B 340 5242 10298 6386 839 11 -1041 O ATOM 2132 CB ARG B 340 11.194 26.751 7.068 1.00 53.34 C ANISOU 2132 CB ARG B 340 4737 9724 5807 944 94 -1084 C ATOM 2133 CG ARG B 340 10.286 25.574 6.751 1.00 60.64 C ANISOU 2133 CG ARG B 340 5737 10616 6689 941 84 -1187 C ATOM 2134 CD ARG B 340 10.693 24.340 7.542 1.00 60.17 C ANISOU 2134 CD ARG B 340 5725 10481 6654 950 92 -1225 C ATOM 2135 NE ARG B 340 10.531 24.532 8.979 1.00 58.16 N ANISOU 2135 NE ARG B 340 5463 10159 6474 889 67 -1210 N ATOM 2136 CZ ARG B 340 9.472 24.126 9.673 1.00 60.58 C ANISOU 2136 CZ ARG B 340 5810 10407 6801 828 40 -1265 C ATOM 2137 NH1 ARG B 340 8.478 23.498 9.060 1.00 59.28 N ANISOU 2137 NH1 ARG B 340 5685 10243 6595 809 25 -1337 N ATOM 2138 NH2 ARG B 340 9.409 24.344 10.980 1.00 62.83 N ANISOU 2138 NH2 ARG B 340 6098 10628 7147 784 26 -1244 N ATOM 2139 N VAL B 341 9.055 29.066 5.363 1.00 71.59 N ANISOU 2139 N VAL B 341 7021 12153 8027 895 27 -1086 N ATOM 2140 CA VAL B 341 7.904 29.954 5.496 1.00 68.08 C ANISOU 2140 CA VAL B 341 6566 11716 7585 848 -25 -1097 C ATOM 2141 C VAL B 341 6.720 29.303 6.203 1.00 65.61 C ANISOU 2141 C VAL B 341 6275 11351 7304 799 -56 -1170 C ATOM 2142 O VAL B 341 6.317 28.189 5.869 1.00 62.50 O ANISOU 2142 O VAL B 341 5920 10935 6891 802 -56 -1242 O ATOM 2143 CB VAL B 341 7.432 30.477 4.128 1.00 63.98 C ANISOU 2143 CB VAL B 341 6060 11260 6991 875 -37 -1112 C ATOM 2144 CG1 VAL B 341 6.392 31.570 4.314 1.00 62.29 C ANISOU 2144 CG1 VAL B 341 5826 11059 6781 836 -92 -1109 C ATOM 2145 CG2 VAL B 341 8.614 30.991 3.316 1.00 60.60 C ANISOU 2145 CG2 VAL B 341 5616 10885 6522 927 9 -1039 C ATOM 2146 N PHE B 342 6.167 30.016 7.178 1.00 63.16 N ANISOU 2146 N PHE B 342 5942 11016 7038 755 -84 -1148 N ATOM 2147 CA PHE B 342 5.005 29.547 7.918 1.00 65.02 C ANISOU 2147 CA PHE B 342 6186 11209 7310 707 -103 -1203 C ATOM 2148 C PHE B 342 3.738 30.219 7.413 1.00 59.43 C ANISOU 2148 C PHE B 342 5456 10543 6582 691 -145 -1230 C ATOM 2149 O PHE B 342 2.800 29.553 6.976 1.00 60.77 O ANISOU 2149 O PHE B 342 5630 10714 6745 673 -164 -1299 O ATOM 2150 CB PHE B 342 5.177 29.832 9.410 1.00 69.11 C ANISOU 2150 CB PHE B 342 6704 11666 7888 679 -100 -1161 C ATOM 2151 CG PHE B 342 5.941 28.772 10.143 1.00 74.85 C ANISOU 2151 CG PHE B 342 7465 12326 8649 679 -71 -1170 C ATOM 2152 CD1 PHE B 342 5.399 28.160 11.260 1.00 76.87 C ANISOU 2152 CD1 PHE B 342 7749 12510 8947 640 -66 -1199 C ATOM 2153 CD2 PHE B 342 7.194 28.374 9.706 1.00 77.14 C ANISOU 2153 CD2 PHE B 342 7759 12625 8924 722 -45 -1147 C ATOM 2154 CE1 PHE B 342 6.097 27.177 11.937 1.00 77.66 C ANISOU 2154 CE1 PHE B 342 7893 12542 9071 642 -44 -1211 C ATOM 2155 CE2 PHE B 342 7.896 27.390 10.376 1.00 81.12 C ANISOU 2155 CE2 PHE B 342 8297 13067 9456 729 -24 -1158 C ATOM 2156 CZ PHE B 342 7.347 26.791 11.494 1.00 80.21 C ANISOU 2156 CZ PHE B 342 8222 12875 9381 688 -28 -1193 C ATOM 2157 N LEU B 343 3.722 31.545 7.479 1.00 49.90 N ANISOU 2157 N LEU B 343 4225 9367 5366 699 -165 -1175 N ATOM 2158 CA LEU B 343 2.557 32.322 7.079 1.00 52.70 C ANISOU 2158 CA LEU B 343 4559 9763 5701 693 -208 -1195 C ATOM 2159 C LEU B 343 2.892 33.341 6.002 1.00 49.08 C ANISOU 2159 C LEU B 343 4102 9365 5179 730 -229 -1160 C ATOM 2160 O LEU B 343 3.933 33.997 6.052 1.00 45.86 O ANISOU 2160 O LEU B 343 3698 8964 4760 746 -215 -1089 O ATOM 2161 CB LEU B 343 1.959 33.046 8.287 1.00 57.46 C ANISOU 2161 CB LEU B 343 5147 10341 6346 671 -221 -1165 C ATOM 2162 CG LEU B 343 0.809 32.369 9.032 1.00 65.04 C ANISOU 2162 CG LEU B 343 6089 11268 7354 633 -215 -1215 C ATOM 2163 CD1 LEU B 343 1.011 30.866 9.121 1.00 68.67 C ANISOU 2163 CD1 LEU B 343 6569 11685 7839 607 -185 -1265 C ATOM 2164 CD2 LEU B 343 0.658 32.981 10.413 1.00 68.32 C ANISOU 2164 CD2 LEU B 343 6512 11641 7806 627 -205 -1168 C ATOM 2165 N GLU B 344 1.999 33.470 5.028 1.00 47.41 N ANISOU 2165 N GLU B 344 3891 9195 4928 739 -266 -1210 N ATOM 2166 CA GLU B 344 2.104 34.531 4.040 1.00 49.79 C ANISOU 2166 CA GLU B 344 4204 9549 5163 773 -293 -1184 C ATOM 2167 C GLU B 344 0.793 35.300 3.978 1.00 48.53 C ANISOU 2167 C GLU B 344 4026 9414 4997 768 -352 -1211 C ATOM 2168 O GLU B 344 -0.199 34.815 3.434 1.00 46.98 O ANISOU 2168 O GLU B 344 3821 9229 4799 763 -386 -1281 O ATOM 2169 CB GLU B 344 2.481 33.967 2.672 1.00 54.39 C ANISOU 2169 CB GLU B 344 4825 10157 5684 810 -281 -1216 C ATOM 2170 CG GLU B 344 3.921 33.486 2.599 1.00 58.43 C ANISOU 2170 CG GLU B 344 5352 10661 6189 834 -216 -1170 C ATOM 2171 CD GLU B 344 4.296 32.963 1.229 1.00 60.97 C ANISOU 2171 CD GLU B 344 5722 11007 6436 886 -196 -1197 C ATOM 2172 OE1 GLU B 344 3.426 32.365 0.562 1.00 64.39 O ANISOU 2172 OE1 GLU B 344 6189 11435 6842 892 -233 -1275 O ATOM 2173 OE2 GLU B 344 5.464 33.145 0.823 1.00 57.65 O ANISOU 2173 OE2 GLU B 344 5309 10609 5986 922 -144 -1138 O ATOM 2174 N VAL B 345 0.799 36.499 4.552 1.00 47.53 N ANISOU 2174 N VAL B 345 3896 9294 4870 772 -371 -1154 N ATOM 2175 CA VAL B 345 -0.402 37.316 4.657 1.00 49.58 C ANISOU 2175 CA VAL B 345 4138 9577 5123 779 -424 -1173 C ATOM 2176 C VAL B 345 -0.438 38.421 3.604 1.00 59.23 C ANISOU 2176 C VAL B 345 5393 10847 6267 815 -471 -1159 C ATOM 2177 O VAL B 345 0.522 39.175 3.447 1.00 62.99 O ANISOU 2177 O VAL B 345 5902 11327 6703 826 -464 -1091 O ATOM 2178 CB VAL B 345 -0.512 37.949 6.053 1.00 46.23 C ANISOU 2178 CB VAL B 345 3708 9122 4738 770 -420 -1122 C ATOM 2179 CG1 VAL B 345 -1.597 39.014 6.075 1.00 45.34 C ANISOU 2179 CG1 VAL B 345 3587 9039 4600 797 -474 -1128 C ATOM 2180 CG2 VAL B 345 -0.776 36.877 7.098 1.00 43.83 C ANISOU 2180 CG2 VAL B 345 3376 8769 4508 736 -378 -1147 C ATOM 2181 N ALA B 346 -1.554 38.510 2.887 1.00 66.73 N ANISOU 2181 N ALA B 346 6332 11828 7195 830 -523 -1221 N ATOM 2182 CA ALA B 346 -1.741 39.538 1.872 1.00 64.24 C ANISOU 2182 CA ALA B 346 6057 11552 6800 867 -576 -1219 C ATOM 2183 C ALA B 346 -2.057 40.889 2.512 1.00 68.28 C ANISOU 2183 C ALA B 346 6576 12071 7295 885 -613 -1172 C ATOM 2184 O ALA B 346 -2.829 40.964 3.468 1.00 72.85 O ANISOU 2184 O ALA B 346 7116 12641 7923 880 -620 -1179 O ATOM 2185 CB ALA B 346 -2.850 39.133 0.919 1.00 62.42 C ANISOU 2185 CB ALA B 346 5817 11344 6556 880 -632 -1305 C ATOM 2186 N GLU B 347 -1.463 41.953 1.978 1.00 54.66 N ANISOU 2186 N GLU B 347 4910 10361 5498 907 -636 -1122 N ATOM 2187 CA GLU B 347 -1.695 43.302 2.490 1.00 54.37 C ANISOU 2187 CA GLU B 347 4904 10326 5429 928 -683 -1075 C ATOM 2188 C GLU B 347 -1.954 44.300 1.362 1.00 56.43 C ANISOU 2188 C GLU B 347 5224 10621 5596 965 -746 -1083 C ATOM 2189 O GLU B 347 -1.319 44.237 0.313 1.00 55.47 O ANISOU 2189 O GLU B 347 5142 10511 5423 968 -735 -1078 O ATOM 2190 CB GLU B 347 -0.505 43.767 3.334 1.00 55.36 C ANISOU 2190 CB GLU B 347 5057 10412 5563 905 -655 -978 C ATOM 2191 CG GLU B 347 -0.305 42.992 4.631 1.00 58.06 C ANISOU 2191 CG GLU B 347 5360 10709 5992 876 -606 -965 C ATOM 2192 CD GLU B 347 -1.385 43.279 5.660 1.00 60.72 C ANISOU 2192 CD GLU B 347 5680 11032 6357 894 -628 -982 C ATOM 2193 OE1 GLU B 347 -1.348 42.673 6.752 1.00 57.84 O ANISOU 2193 OE1 GLU B 347 5293 10626 6058 874 -587 -974 O ATOM 2194 OE2 GLU B 347 -2.270 44.115 5.380 1.00 66.05 O ANISOU 2194 OE2 GLU B 347 6370 11737 6987 933 -683 -1001 O ATOM 2195 N LEU B 348 -2.884 45.224 1.586 1.00 56.88 N ANISOU 2195 N LEU B 348 5294 10691 5626 1000 -810 -1094 N ATOM 2196 CA LEU B 348 -3.227 46.228 0.580 1.00 53.61 C ANISOU 2196 CA LEU B 348 4945 10304 5119 1041 -881 -1106 C ATOM 2197 C LEU B 348 -2.640 47.597 0.926 1.00 57.71 C ANISOU 2197 C LEU B 348 5545 10807 5576 1051 -914 -1022 C ATOM 2198 O LEU B 348 -2.320 48.385 0.037 1.00 61.80 O ANISOU 2198 O LEU B 348 6138 11335 6007 1065 -950 -1002 O ATOM 2199 CB LEU B 348 -4.746 46.338 0.420 1.00 49.18 C ANISOU 2199 CB LEU B 348 4348 9773 4563 1083 -945 -1185 C ATOM 2200 CG LEU B 348 -5.531 45.024 0.392 1.00 49.29 C ANISOU 2200 CG LEU B 348 4270 9798 4661 1064 -926 -1262 C ATOM 2201 CD1 LEU B 348 -7.011 45.285 0.152 1.00 51.89 C ANISOU 2201 CD1 LEU B 348 4557 10162 4997 1106 -1001 -1329 C ATOM 2202 CD2 LEU B 348 -4.972 44.079 -0.659 1.00 48.92 C ANISOU 2202 CD2 LEU B 348 4239 9744 4602 1042 -901 -1293 C ATOM 2203 N HIS B 349 -2.510 47.876 2.219 1.00 66.30 N ANISOU 2203 N HIS B 349 6626 11862 6702 1042 -905 -971 N ATOM 2204 CA HIS B 349 -1.921 49.128 2.681 1.00 63.72 C ANISOU 2204 CA HIS B 349 6385 11505 6320 1046 -946 -885 C ATOM 2205 C HIS B 349 -0.735 48.819 3.586 1.00 55.68 C ANISOU 2205 C HIS B 349 5359 10439 5358 993 -895 -806 C ATOM 2206 O HIS B 349 -0.519 47.665 3.951 1.00 57.07 O ANISOU 2206 O HIS B 349 5465 10607 5614 965 -828 -826 O ATOM 2207 CB HIS B 349 -2.956 49.953 3.445 1.00 65.84 C ANISOU 2207 CB HIS B 349 6680 11769 6567 1102 -1005 -895 C ATOM 2208 CG HIS B 349 -4.267 50.088 2.738 1.00 68.03 C ANISOU 2208 CG HIS B 349 6937 12096 6815 1158 -1053 -981 C ATOM 2209 ND1 HIS B 349 -5.115 49.020 2.529 1.00 67.84 N ANISOU 2209 ND1 HIS B 349 6813 12105 6858 1159 -1025 -1062 N ATOM 2210 CD2 HIS B 349 -4.887 51.167 2.202 1.00 72.13 C ANISOU 2210 CD2 HIS B 349 7525 12636 7247 1215 -1136 -997 C ATOM 2211 CE1 HIS B 349 -6.194 49.433 1.890 1.00 68.74 C ANISOU 2211 CE1 HIS B 349 6925 12259 6935 1212 -1090 -1124 C ATOM 2212 NE2 HIS B 349 -6.081 50.733 1.679 1.00 72.34 N ANISOU 2212 NE2 HIS B 349 7483 12708 7293 1251 -1156 -1088 N ATOM 2213 N ARG B 350 0.035 49.842 3.950 1.00 43.27 N ANISOU 2213 N ARG B 350 3865 8831 3747 980 -934 -716 N ATOM 2214 CA ARG B 350 1.164 49.638 4.856 1.00 45.35 C ANISOU 2214 CA ARG B 350 4124 9041 4067 930 -904 -635 C ATOM 2215 C ARG B 350 0.928 50.216 6.253 1.00 55.87 C ANISOU 2215 C ARG B 350 5507 10311 5409 949 -946 -595 C ATOM 2216 O ARG B 350 1.822 50.820 6.846 1.00 57.14 O ANISOU 2216 O ARG B 350 5727 10417 5567 919 -980 -505 O ATOM 2217 CB ARG B 350 2.466 50.184 4.261 1.00 45.01 C ANISOU 2217 CB ARG B 350 4120 8992 3991 883 -910 -546 C ATOM 2218 CG ARG B 350 2.301 51.318 3.265 1.00 48.23 C ANISOU 2218 CG ARG B 350 4609 9426 4292 902 -974 -534 C ATOM 2219 CD ARG B 350 2.384 50.796 1.842 1.00 53.81 C ANISOU 2219 CD ARG B 350 5285 10189 4969 904 -925 -579 C ATOM 2220 NE ARG B 350 2.946 51.786 0.929 1.00 59.66 N ANISOU 2220 NE ARG B 350 6104 10940 5622 890 -959 -521 N ATOM 2221 CZ ARG B 350 3.327 51.523 -0.318 1.00 64.24 C ANISOU 2221 CZ ARG B 350 6684 11560 6165 888 -913 -530 C ATOM 2222 NH1 ARG B 350 3.830 52.486 -1.077 1.00 62.81 N ANISOU 2222 NH1 ARG B 350 6581 11383 5901 873 -941 -470 N ATOM 2223 NH2 ARG B 350 3.208 50.294 -0.805 1.00 67.25 N ANISOU 2223 NH2 ARG B 350 6996 11971 6585 902 -840 -597 N ATOM 2224 N LYS B 351 -0.278 50.022 6.773 1.00 69.67 N ANISOU 2224 N LYS B 351 7234 12068 7170 1000 -945 -659 N ATOM 2225 CA LYS B 351 -0.617 50.479 8.115 1.00 69.38 C ANISOU 2225 CA LYS B 351 7251 11974 7137 1034 -972 -628 C ATOM 2226 C LYS B 351 -1.519 49.463 8.800 1.00 69.65 C ANISOU 2226 C LYS B 351 7205 12015 7244 1055 -907 -694 C ATOM 2227 O LYS B 351 -2.234 48.716 8.133 1.00 68.05 O ANISOU 2227 O LYS B 351 6916 11871 7067 1059 -871 -772 O ATOM 2228 CB LYS B 351 -1.305 51.846 8.063 1.00 68.49 C ANISOU 2228 CB LYS B 351 7235 11862 6925 1099 -1061 -618 C ATOM 2229 CG LYS B 351 -0.417 52.959 7.534 1.00 68.56 C ANISOU 2229 CG LYS B 351 7344 11850 6856 1072 -1135 -542 C ATOM 2230 CD LYS B 351 -1.166 54.276 7.434 1.00 69.59 C ANISOU 2230 CD LYS B 351 7582 11980 6879 1143 -1229 -541 C ATOM 2231 CE LYS B 351 -0.274 55.358 6.844 1.00 70.27 C ANISOU 2231 CE LYS B 351 7772 12042 6885 1105 -1305 -464 C ATOM 2232 NZ LYS B 351 -0.963 56.674 6.766 1.00 69.93 N ANISOU 2232 NZ LYS B 351 7854 11990 6727 1176 -1406 -462 N ATOM 2233 N HIS B 352 -1.481 49.436 10.130 1.00 58.37 N ANISOU 2233 N HIS B 352 5810 10521 5845 1068 -895 -659 N ATOM 2234 CA HIS B 352 -2.299 48.504 10.896 1.00 54.47 C ANISOU 2234 CA HIS B 352 5250 10027 5420 1086 -826 -710 C ATOM 2235 C HIS B 352 -1.864 47.074 10.607 1.00 55.43 C ANISOU 2235 C HIS B 352 5275 10161 5625 1021 -750 -747 C ATOM 2236 O HIS B 352 -2.687 46.160 10.590 1.00 56.82 O ANISOU 2236 O HIS B 352 5366 10370 5852 1021 -697 -814 O ATOM 2237 CB HIS B 352 -3.776 48.676 10.535 1.00 53.71 C ANISOU 2237 CB HIS B 352 5106 9999 5301 1148 -831 -779 C ATOM 2238 CG HIS B 352 -4.333 50.022 10.882 1.00 54.23 C ANISOU 2238 CG HIS B 352 5269 10056 5281 1230 -901 -750 C ATOM 2239 ND1 HIS B 352 -5.636 50.204 11.293 1.00 54.55 N ANISOU 2239 ND1 HIS B 352 5285 10128 5315 1307 -890 -787 N ATOM 2240 CD2 HIS B 352 -3.761 51.249 10.892 1.00 56.27 C ANISOU 2240 CD2 HIS B 352 5652 10274 5454 1248 -983 -685 C ATOM 2241 CE1 HIS B 352 -5.845 51.486 11.533 1.00 57.07 C ANISOU 2241 CE1 HIS B 352 5715 10427 5541 1380 -962 -750 C ATOM 2242 NE2 HIS B 352 -4.723 52.142 11.299 1.00 58.46 N ANISOU 2242 NE2 HIS B 352 5990 10556 5667 1342 -1025 -689 N ATOM 2243 N LEU B 353 -0.566 46.888 10.384 1.00 66.44 N ANISOU 2243 N LEU B 353 6683 11529 7035 966 -748 -700 N ATOM 2244 CA LEU B 353 -0.039 45.602 9.935 1.00 66.74 C ANISOU 2244 CA LEU B 353 6640 11582 7135 914 -682 -733 C ATOM 2245 C LEU B 353 0.123 44.590 11.066 1.00 70.10 C ANISOU 2245 C LEU B 353 7045 11949 7640 892 -622 -737 C ATOM 2246 O LEU B 353 -0.534 43.549 11.084 1.00 78.17 O ANISOU 2246 O LEU B 353 8000 12992 8710 884 -567 -803 O ATOM 2247 CB LEU B 353 1.304 45.797 9.224 1.00 62.34 C ANISOU 2247 CB LEU B 353 6098 11026 6563 872 -694 -677 C ATOM 2248 CG LEU B 353 1.341 46.731 8.013 1.00 56.39 C ANISOU 2248 CG LEU B 353 5373 10325 5728 883 -744 -665 C ATOM 2249 CD1 LEU B 353 2.777 46.998 7.595 1.00 54.86 C ANISOU 2249 CD1 LEU B 353 5196 10120 5529 838 -748 -585 C ATOM 2250 CD2 LEU B 353 0.543 46.152 6.856 1.00 51.22 C ANISOU 2250 CD2 LEU B 353 4659 9743 5060 898 -721 -755 C ATOM 2251 N GLY B 354 1.002 44.908 12.009 1.00 52.63 N ANISOU 2251 N GLY B 354 4899 9659 5439 881 -641 -664 N ATOM 2252 CA GLY B 354 1.426 43.965 13.027 1.00 49.15 C ANISOU 2252 CA GLY B 354 4454 9151 5068 857 -593 -659 C ATOM 2253 C GLY B 354 2.894 44.229 13.286 1.00 58.58 C ANISOU 2253 C GLY B 354 5692 10288 6277 822 -626 -577 C ATOM 2254 O GLY B 354 3.288 45.385 13.440 1.00 65.45 O ANISOU 2254 O GLY B 354 6636 11128 7102 831 -700 -507 O ATOM 2255 N GLY B 355 3.710 43.180 13.346 1.00 57.39 N ANISOU 2255 N GLY B 355 5497 10119 6189 783 -580 -581 N ATOM 2256 CA GLY B 355 3.251 41.804 13.317 1.00 55.77 C ANISOU 2256 CA GLY B 355 5227 9931 6033 773 -503 -661 C ATOM 2257 C GLY B 355 3.947 41.068 14.447 1.00 57.76 C ANISOU 2257 C GLY B 355 5507 10094 6346 754 -480 -640 C ATOM 2258 O GLY B 355 4.730 40.141 14.229 1.00 52.47 O ANISOU 2258 O GLY B 355 4796 9421 5719 726 -444 -650 O ATOM 2259 N GLN B 356 3.659 41.509 15.667 1.00 66.58 N ANISOU 2259 N GLN B 356 6704 11133 7461 778 -503 -611 N ATOM 2260 CA GLN B 356 4.326 41.022 16.868 1.00 67.46 C ANISOU 2260 CA GLN B 356 6871 11141 7621 768 -500 -582 C ATOM 2261 C GLN B 356 4.305 39.502 16.998 1.00 67.93 C ANISOU 2261 C GLN B 356 6881 11193 7737 743 -422 -647 C ATOM 2262 O GLN B 356 3.246 38.877 16.935 1.00 71.18 O ANISOU 2262 O GLN B 356 7256 11637 8153 748 -367 -715 O ATOM 2263 CB GLN B 356 3.687 41.660 18.101 1.00 71.11 C ANISOU 2263 CB GLN B 356 7438 11525 8057 812 -523 -558 C ATOM 2264 CG GLN B 356 4.380 41.338 19.410 1.00 78.66 C ANISOU 2264 CG GLN B 356 8482 12356 9050 810 -537 -521 C ATOM 2265 CD GLN B 356 3.751 42.061 20.586 1.00 86.64 C ANISOU 2265 CD GLN B 356 9616 13285 10020 867 -562 -492 C ATOM 2266 OE1 GLN B 356 2.790 42.813 20.424 1.00 90.21 O ANISOU 2266 OE1 GLN B 356 10082 13780 10416 912 -566 -498 O ATOM 2267 NE2 GLN B 356 4.292 41.836 21.778 1.00 87.36 N ANISOU 2267 NE2 GLN B 356 9806 13253 10133 874 -580 -460 N ATOM 2268 N LEU B 357 5.486 38.919 17.181 1.00 73.03 N ANISOU 2268 N LEU B 357 7526 11795 8428 717 -424 -623 N ATOM 2269 CA LEU B 357 5.623 37.487 17.427 1.00 67.85 C ANISOU 2269 CA LEU B 357 6846 11114 7822 698 -361 -679 C ATOM 2270 C LEU B 357 6.100 37.255 18.856 1.00 70.75 C ANISOU 2270 C LEU B 357 7303 11355 8222 702 -376 -649 C ATOM 2271 O LEU B 357 6.847 38.066 19.406 1.00 77.19 O ANISOU 2271 O LEU B 357 8181 12108 9039 709 -446 -574 O ATOM 2272 CB LEU B 357 6.626 36.864 16.455 1.00 63.84 C ANISOU 2272 CB LEU B 357 6267 10656 7335 677 -346 -683 C ATOM 2273 CG LEU B 357 6.389 37.042 14.956 1.00 63.47 C ANISOU 2273 CG LEU B 357 6144 10723 7250 677 -333 -706 C ATOM 2274 CD1 LEU B 357 7.543 36.440 14.175 1.00 65.44 C ANISOU 2274 CD1 LEU B 357 6340 11006 7517 669 -312 -696 C ATOM 2275 CD2 LEU B 357 5.072 36.411 14.541 1.00 60.30 C ANISOU 2275 CD2 LEU B 357 5710 10369 6832 678 -288 -795 C ATOM 2276 N LEU B 358 5.675 36.145 19.454 1.00 64.63 N ANISOU 2276 N LEU B 358 6543 10537 7475 696 -317 -706 N ATOM 2277 CA LEU B 358 6.071 35.815 20.819 1.00 64.39 C ANISOU 2277 CA LEU B 358 6613 10381 7473 703 -326 -687 C ATOM 2278 C LEU B 358 5.612 34.416 21.218 1.00 61.32 C ANISOU 2278 C LEU B 358 6227 9961 7111 686 -250 -760 C ATOM 2279 O LEU B 358 4.618 33.911 20.701 1.00 63.49 O ANISOU 2279 O LEU B 358 6442 10302 7378 673 -193 -820 O ATOM 2280 CB LEU B 358 5.520 36.856 21.800 1.00 67.00 C ANISOU 2280 CB LEU B 358 7046 10645 7767 741 -361 -641 C ATOM 2281 CG LEU B 358 4.004 37.060 21.854 1.00 67.46 C ANISOU 2281 CG LEU B 358 7096 10748 7789 766 -308 -678 C ATOM 2282 CD1 LEU B 358 3.358 36.074 22.814 1.00 68.59 C ANISOU 2282 CD1 LEU B 358 7283 10825 7953 766 -232 -722 C ATOM 2283 CD2 LEU B 358 3.677 38.483 22.267 1.00 66.28 C ANISOU 2283 CD2 LEU B 358 7025 10575 7584 816 -365 -619 C ATOM 2284 N PHE B 359 6.342 33.794 22.139 1.00 59.59 N ANISOU 2284 N PHE B 359 6080 9636 6924 684 -257 -753 N ATOM 2285 CA PHE B 359 5.968 32.479 22.649 1.00 59.26 C ANISOU 2285 CA PHE B 359 6066 9547 6904 667 -191 -817 C ATOM 2286 C PHE B 359 5.251 32.590 23.991 1.00 61.68 C ANISOU 2286 C PHE B 359 6484 9754 7198 688 -168 -810 C ATOM 2287 O PHE B 359 5.487 33.525 24.756 1.00 67.99 O ANISOU 2287 O PHE B 359 7371 10482 7979 723 -220 -749 O ATOM 2288 CB PHE B 359 7.198 31.580 22.789 1.00 58.67 C ANISOU 2288 CB PHE B 359 6008 9417 6868 657 -208 -825 C ATOM 2289 CG PHE B 359 7.768 31.123 21.478 1.00 61.35 C ANISOU 2289 CG PHE B 359 6240 9855 7216 644 -201 -847 C ATOM 2290 CD1 PHE B 359 7.188 30.075 20.784 1.00 63.79 C ANISOU 2290 CD1 PHE B 359 6499 10221 7519 622 -141 -924 C ATOM 2291 CD2 PHE B 359 8.887 31.738 20.942 1.00 59.97 C ANISOU 2291 CD2 PHE B 359 6020 9713 7054 654 -255 -789 C ATOM 2292 CE1 PHE B 359 7.711 29.652 19.577 1.00 62.84 C ANISOU 2292 CE1 PHE B 359 6298 10183 7394 622 -135 -944 C ATOM 2293 CE2 PHE B 359 9.413 31.319 19.736 1.00 58.57 C ANISOU 2293 CE2 PHE B 359 5751 9627 6878 652 -237 -805 C ATOM 2294 CZ PHE B 359 8.825 30.275 19.053 1.00 59.99 C ANISOU 2294 CZ PHE B 359 5895 9858 7041 641 -176 -885 C ATOM 2295 N GLY B 360 4.372 31.632 24.268 1.00 55.59 N ANISOU 2295 N GLY B 360 5714 8974 6433 668 -89 -868 N ATOM 2296 CA GLY B 360 3.644 31.599 25.523 1.00 54.34 C ANISOU 2296 CA GLY B 360 5658 8725 6262 688 -45 -862 C ATOM 2297 C GLY B 360 4.170 30.524 26.454 1.00 57.26 C ANISOU 2297 C GLY B 360 6127 8973 6655 676 -28 -885 C ATOM 2298 O GLY B 360 5.033 29.735 26.068 1.00 58.61 O ANISOU 2298 O GLY B 360 6276 9140 6852 652 -47 -913 O ATOM 2299 N PRO B 361 3.655 30.491 27.691 1.00 52.94 N ANISOU 2299 N PRO B 361 5699 8325 6092 700 12 -874 N ATOM 2300 CA PRO B 361 4.054 29.517 28.716 1.00 52.42 C ANISOU 2300 CA PRO B 361 5753 8126 6038 694 31 -895 C ATOM 2301 C PRO B 361 3.912 28.066 28.254 1.00 47.24 C ANISOU 2301 C PRO B 361 5043 7498 5410 634 85 -969 C ATOM 2302 O PRO B 361 4.595 27.187 28.784 1.00 41.47 O ANISOU 2302 O PRO B 361 4395 6672 4692 625 77 -993 O ATOM 2303 CB PRO B 361 3.082 29.805 29.863 1.00 53.49 C ANISOU 2303 CB PRO B 361 5995 8189 6141 729 95 -873 C ATOM 2304 CG PRO B 361 2.720 31.234 29.690 1.00 53.70 C ANISOU 2304 CG PRO B 361 6003 8268 6134 779 62 -817 C ATOM 2305 CD PRO B 361 2.683 31.468 28.209 1.00 52.91 C ANISOU 2305 CD PRO B 361 5732 8322 6049 746 38 -835 C ATOM 2306 N ASP B 362 3.037 27.819 27.285 1.00 63.23 N ANISOU 2306 N ASP B 362 6939 9646 7441 595 132 -1005 N ATOM 2307 CA ASP B 362 2.859 26.472 26.757 1.00 72.43 C ANISOU 2307 CA ASP B 362 8058 10837 8626 535 171 -1074 C ATOM 2308 C ASP B 362 3.803 26.201 25.589 1.00 73.79 C ANISOU 2308 C ASP B 362 8151 11076 8808 527 114 -1097 C ATOM 2309 O ASP B 362 3.875 25.080 25.082 1.00 76.39 O ANISOU 2309 O ASP B 362 8459 11421 9147 489 130 -1154 O ATOM 2310 CB ASP B 362 1.406 26.237 26.340 1.00 81.92 C ANISOU 2310 CB ASP B 362 9168 12124 9834 492 243 -1102 C ATOM 2311 CG ASP B 362 0.506 25.915 27.519 1.00 93.44 C ANISOU 2311 CG ASP B 362 10706 13505 11292 483 326 -1096 C ATOM 2312 OD1 ASP B 362 -0.683 25.600 27.296 1.00 99.11 O ANISOU 2312 OD1 ASP B 362 11348 14284 12026 440 391 -1114 O ATOM 2313 OD2 ASP B 362 0.990 25.973 28.670 1.00 95.02 O ANISOU 2313 OD2 ASP B 362 11047 13580 11476 519 326 -1069 O ATOM 2314 N GLY B 363 4.528 27.233 25.170 1.00 67.97 N ANISOU 2314 N GLY B 363 7380 10379 8067 565 50 -1048 N ATOM 2315 CA GLY B 363 5.498 27.101 24.098 1.00 66.64 C ANISOU 2315 CA GLY B 363 7138 10276 7906 567 4 -1056 C ATOM 2316 C GLY B 363 4.928 27.431 22.731 1.00 61.87 C ANISOU 2316 C GLY B 363 6405 9813 7289 553 11 -1071 C ATOM 2317 O GLY B 363 5.654 27.463 21.737 1.00 59.46 O ANISOU 2317 O GLY B 363 6036 9574 6982 562 -20 -1070 O ATOM 2318 N PHE B 364 3.623 27.678 22.683 1.00 50.88 N ANISOU 2318 N PHE B 364 4977 8467 5889 534 52 -1083 N ATOM 2319 CA PHE B 364 2.948 28.002 21.434 1.00 49.21 C ANISOU 2319 CA PHE B 364 4651 8382 5665 522 52 -1101 C ATOM 2320 C PHE B 364 3.353 29.380 20.918 1.00 52.47 C ANISOU 2320 C PHE B 364 5025 8855 6057 561 -2 -1044 C ATOM 2321 O PHE B 364 3.715 30.263 21.694 1.00 50.25 O ANISOU 2321 O PHE B 364 4805 8519 5770 594 -31 -985 O ATOM 2322 CB PHE B 364 1.431 27.928 21.613 1.00 46.50 C ANISOU 2322 CB PHE B 364 4273 8067 5327 493 105 -1124 C ATOM 2323 CG PHE B 364 0.938 26.583 22.070 1.00 46.71 C ANISOU 2323 CG PHE B 364 4332 8039 5376 441 158 -1175 C ATOM 2324 CD1 PHE B 364 0.054 26.478 23.132 1.00 44.05 C ANISOU 2324 CD1 PHE B 364 4038 7648 5052 428 218 -1165 C ATOM 2325 CD2 PHE B 364 1.365 25.421 21.445 1.00 46.12 C ANISOU 2325 CD2 PHE B 364 4254 7964 5305 408 149 -1229 C ATOM 2326 CE1 PHE B 364 -0.402 25.240 23.556 1.00 45.14 C ANISOU 2326 CE1 PHE B 364 4208 7732 5210 372 268 -1207 C ATOM 2327 CE2 PHE B 364 0.913 24.181 21.865 1.00 46.80 C ANISOU 2327 CE2 PHE B 364 4381 7992 5407 355 190 -1275 C ATOM 2328 CZ PHE B 364 0.029 24.091 22.922 1.00 47.91 C ANISOU 2328 CZ PHE B 364 4560 8080 5565 331 249 -1262 C ATOM 2329 N LEU B 365 3.291 29.558 19.602 1.00 65.07 N ANISOU 2329 N LEU B 365 6531 10556 7638 557 -18 -1061 N ATOM 2330 CA LEU B 365 3.674 30.821 18.978 1.00 61.12 C ANISOU 2330 CA LEU B 365 5994 10117 7113 589 -68 -1009 C ATOM 2331 C LEU B 365 2.470 31.720 18.723 1.00 54.77 C ANISOU 2331 C LEU B 365 5146 9378 6285 598 -67 -1004 C ATOM 2332 O LEU B 365 1.488 31.301 18.109 1.00 51.76 O ANISOU 2332 O LEU B 365 4703 9059 5906 575 -41 -1055 O ATOM 2333 CB LEU B 365 4.416 30.571 17.665 1.00 60.43 C ANISOU 2333 CB LEU B 365 5844 10103 7013 590 -85 -1023 C ATOM 2334 CG LEU B 365 4.743 31.820 16.844 1.00 57.91 C ANISOU 2334 CG LEU B 365 5481 9857 6664 615 -129 -972 C ATOM 2335 CD1 LEU B 365 5.703 32.716 17.609 1.00 55.66 C ANISOU 2335 CD1 LEU B 365 5248 9513 6389 635 -175 -890 C ATOM 2336 CD2 LEU B 365 5.316 31.441 15.487 1.00 58.68 C ANISOU 2336 CD2 LEU B 365 5521 10031 6743 619 -127 -992 C ATOM 2337 N TYR B 366 2.555 32.958 19.195 1.00 50.80 N ANISOU 2337 N TYR B 366 4681 8859 5762 634 -103 -942 N ATOM 2338 CA TYR B 366 1.482 33.928 19.007 1.00 53.20 C ANISOU 2338 CA TYR B 366 4956 9222 6036 657 -108 -932 C ATOM 2339 C TYR B 366 1.867 34.965 17.961 1.00 51.39 C ANISOU 2339 C TYR B 366 4687 9068 5769 676 -167 -901 C ATOM 2340 O TYR B 366 3.003 35.438 17.933 1.00 48.11 O ANISOU 2340 O TYR B 366 4304 8629 5348 684 -212 -849 O ATOM 2341 CB TYR B 366 1.140 34.621 20.328 1.00 53.47 C ANISOU 2341 CB TYR B 366 5079 9178 6058 696 -105 -885 C ATOM 2342 CG TYR B 366 0.451 33.721 21.327 1.00 56.04 C ANISOU 2342 CG TYR B 366 5440 9441 6412 682 -33 -915 C ATOM 2343 CD1 TYR B 366 -0.915 33.822 21.556 1.00 57.00 C ANISOU 2343 CD1 TYR B 366 5527 9598 6532 692 19 -930 C ATOM 2344 CD2 TYR B 366 1.166 32.769 22.037 1.00 58.24 C ANISOU 2344 CD2 TYR B 366 5784 9625 6719 660 -14 -924 C ATOM 2345 CE1 TYR B 366 -1.549 33.001 22.469 1.00 58.81 C ANISOU 2345 CE1 TYR B 366 5784 9772 6789 675 95 -949 C ATOM 2346 CE2 TYR B 366 0.542 31.942 22.951 1.00 62.18 C ANISOU 2346 CE2 TYR B 366 6326 10062 7239 644 54 -949 C ATOM 2347 CZ TYR B 366 -0.815 32.063 23.164 1.00 62.33 C ANISOU 2347 CZ TYR B 366 6307 10119 7257 649 112 -959 C ATOM 2348 OH TYR B 366 -1.437 31.240 24.074 1.00 65.79 O ANISOU 2348 OH TYR B 366 6783 10495 7717 628 189 -976 O ATOM 2349 N ILE B 367 0.915 35.316 17.104 1.00 52.45 N ANISOU 2349 N ILE B 367 4755 9294 5882 681 -168 -930 N ATOM 2350 CA ILE B 367 1.161 36.300 16.061 1.00 54.90 C ANISOU 2350 CA ILE B 367 5037 9676 6148 700 -222 -907 C ATOM 2351 C ILE B 367 0.061 37.352 16.040 1.00 59.47 C ANISOU 2351 C ILE B 367 5608 10298 6689 738 -242 -899 C ATOM 2352 O ILE B 367 -1.049 37.093 15.577 1.00 64.66 O ANISOU 2352 O ILE B 367 6201 11017 7352 734 -221 -951 O ATOM 2353 CB ILE B 367 1.254 35.640 14.677 1.00 56.48 C ANISOU 2353 CB ILE B 367 5164 9951 6344 676 -216 -958 C ATOM 2354 CG1 ILE B 367 2.192 34.432 14.728 1.00 56.40 C ANISOU 2354 CG1 ILE B 367 5162 9900 6369 648 -186 -977 C ATOM 2355 CG2 ILE B 367 1.720 36.648 13.641 1.00 58.39 C ANISOU 2355 CG2 ILE B 367 5394 10255 6537 696 -266 -924 C ATOM 2356 CD1 ILE B 367 2.283 33.673 13.431 1.00 56.38 C ANISOU 2356 CD1 ILE B 367 5107 9959 6354 635 -177 -1029 C ATOM 2357 N ILE B 368 0.376 38.538 16.548 1.00 54.99 N ANISOU 2357 N ILE B 368 5112 9697 6085 775 -289 -833 N ATOM 2358 CA ILE B 368 -0.582 39.635 16.573 1.00 52.81 C ANISOU 2358 CA ILE B 368 4847 9457 5762 825 -316 -820 C ATOM 2359 C ILE B 368 -0.562 40.405 15.255 1.00 51.06 C ANISOU 2359 C ILE B 368 4588 9320 5493 833 -369 -822 C ATOM 2360 O ILE B 368 0.410 41.093 14.935 1.00 51.28 O ANISOU 2360 O ILE B 368 4655 9339 5491 831 -422 -769 O ATOM 2361 CB ILE B 368 -0.312 40.605 17.741 1.00 50.97 C ANISOU 2361 CB ILE B 368 4731 9138 5497 871 -351 -748 C ATOM 2362 CG1 ILE B 368 -0.700 39.963 19.076 1.00 53.54 C ANISOU 2362 CG1 ILE B 368 5105 9383 5856 882 -290 -753 C ATOM 2363 CG2 ILE B 368 -1.080 41.901 17.544 1.00 48.77 C ANISOU 2363 CG2 ILE B 368 4476 8902 5152 931 -397 -729 C ATOM 2364 CD1 ILE B 368 0.252 38.882 19.545 1.00 55.67 C ANISOU 2364 CD1 ILE B 368 5396 9580 6179 834 -264 -757 C ATOM 2365 N LEU B 369 -1.641 40.277 14.490 1.00 48.37 N ANISOU 2365 N LEU B 369 4171 9060 5147 839 -359 -880 N ATOM 2366 CA LEU B 369 -1.769 40.989 13.228 1.00 45.78 C ANISOU 2366 CA LEU B 369 3817 8810 4768 852 -411 -890 C ATOM 2367 C LEU B 369 -2.916 41.992 13.294 1.00 43.63 C ANISOU 2367 C LEU B 369 3549 8576 4453 912 -441 -892 C ATOM 2368 O LEU B 369 -4.015 41.662 13.740 1.00 42.13 O ANISOU 2368 O LEU B 369 3313 8401 4292 928 -402 -925 O ATOM 2369 CB LEU B 369 -1.998 40.002 12.081 1.00 48.43 C ANISOU 2369 CB LEU B 369 4068 9206 5127 815 -391 -960 C ATOM 2370 CG LEU B 369 -0.933 38.920 11.888 1.00 48.86 C ANISOU 2370 CG LEU B 369 4117 9232 5217 769 -357 -967 C ATOM 2371 CD1 LEU B 369 -1.348 37.930 10.808 1.00 47.38 C ANISOU 2371 CD1 LEU B 369 3864 9096 5042 742 -343 -1043 C ATOM 2372 CD2 LEU B 369 0.412 39.544 11.557 1.00 49.00 C ANISOU 2372 CD2 LEU B 369 4181 9237 5202 769 -389 -903 C ATOM 2373 N GLY B 370 -2.651 43.219 12.860 1.00 44.22 N ANISOU 2373 N GLY B 370 3677 8666 4458 945 -509 -852 N ATOM 2374 CA GLY B 370 -3.678 44.242 12.795 1.00 42.06 C ANISOU 2374 CA GLY B 370 3418 8433 4132 1010 -549 -856 C ATOM 2375 C GLY B 370 -4.557 44.055 11.573 1.00 44.02 C ANISOU 2375 C GLY B 370 3577 8772 4376 1012 -562 -927 C ATOM 2376 O GLY B 370 -4.275 43.209 10.727 1.00 46.74 O ANISOU 2376 O GLY B 370 3866 9143 4749 962 -547 -968 O ATOM 2377 N ASP B 371 -5.619 44.848 11.476 1.00 58.48 N ANISOU 2377 N ASP B 371 5402 10648 6170 1075 -595 -941 N ATOM 2378 CA ASP B 371 -6.579 44.709 10.384 1.00 64.63 C ANISOU 2378 CA ASP B 371 6095 11510 6950 1082 -619 -1010 C ATOM 2379 C ASP B 371 -6.015 45.168 9.040 1.00 71.37 C ANISOU 2379 C ASP B 371 6980 12395 7743 1072 -682 -1019 C ATOM 2380 O ASP B 371 -6.604 44.905 7.990 1.00 72.41 O ANISOU 2380 O ASP B 371 7054 12583 7875 1069 -708 -1079 O ATOM 2381 CB ASP B 371 -7.873 45.464 10.701 1.00 66.20 C ANISOU 2381 CB ASP B 371 6274 11749 7128 1162 -637 -1021 C ATOM 2382 CG ASP B 371 -7.635 46.929 11.011 1.00 65.62 C ANISOU 2382 CG ASP B 371 6322 11652 6959 1233 -698 -963 C ATOM 2383 OD1 ASP B 371 -6.475 47.383 10.902 1.00 64.91 O ANISOU 2383 OD1 ASP B 371 6323 11515 6823 1209 -733 -914 O ATOM 2384 OD2 ASP B 371 -8.610 47.626 11.364 1.00 63.78 O ANISOU 2384 OD2 ASP B 371 6091 11446 6697 1313 -713 -965 O ATOM 2385 N GLY B 372 -4.879 45.857 9.080 1.00 52.65 N ANISOU 2385 N GLY B 372 4703 9982 5320 1066 -710 -954 N ATOM 2386 CA GLY B 372 -4.207 46.295 7.870 1.00 54.90 C ANISOU 2386 CA GLY B 372 5024 10291 5546 1052 -758 -948 C ATOM 2387 C GLY B 372 -5.069 47.151 6.962 1.00 60.25 C ANISOU 2387 C GLY B 372 5712 11025 6154 1105 -828 -985 C ATOM 2388 O GLY B 372 -4.946 47.092 5.737 1.00 62.33 O ANISOU 2388 O GLY B 372 5972 11324 6385 1093 -853 -1017 O ATOM 2389 N MET B 373 -5.948 47.945 7.566 1.00 59.47 N ANISOU 2389 N MET B 373 5634 10933 6028 1171 -858 -980 N ATOM 2390 CA MET B 373 -6.807 48.862 6.822 1.00 60.91 C ANISOU 2390 CA MET B 373 5836 11166 6141 1234 -933 -1013 C ATOM 2391 C MET B 373 -7.725 48.145 5.832 1.00 54.93 C ANISOU 2391 C MET B 373 4978 10473 5421 1229 -939 -1102 C ATOM 2392 O MET B 373 -8.404 48.787 5.032 1.00 55.48 O ANISOU 2392 O MET B 373 5058 10584 5436 1277 -1008 -1139 O ATOM 2393 CB MET B 373 -5.964 49.917 6.098 1.00 65.92 C ANISOU 2393 CB MET B 373 6584 11787 6676 1235 -1000 -969 C ATOM 2394 CG MET B 373 -5.074 50.751 7.013 1.00 67.88 C ANISOU 2394 CG MET B 373 6941 11966 6884 1236 -1019 -875 C ATOM 2395 SD MET B 373 -5.775 52.348 7.488 1.00 77.05 S ANISOU 2395 SD MET B 373 8218 13116 7941 1337 -1108 -847 S ATOM 2396 CE MET B 373 -7.253 51.851 8.374 1.00 46.55 C ANISOU 2396 CE MET B 373 4260 9285 4141 1406 -1057 -900 C ATOM 2397 N ILE B 374 -7.748 46.816 5.894 1.00 53.76 N ANISOU 2397 N ILE B 374 4739 10324 5362 1172 -876 -1136 N ATOM 2398 CA ILE B 374 -8.600 46.016 5.016 1.00 53.52 C ANISOU 2398 CA ILE B 374 4616 10342 5375 1158 -890 -1218 C ATOM 2399 C ILE B 374 -10.029 45.937 5.547 1.00 55.10 C ANISOU 2399 C ILE B 374 4720 10582 5632 1197 -889 -1252 C ATOM 2400 O ILE B 374 -10.277 45.340 6.594 1.00 59.56 O ANISOU 2400 O ILE B 374 5228 11131 6270 1179 -820 -1237 O ATOM 2401 CB ILE B 374 -8.057 44.583 4.858 1.00 49.36 C ANISOU 2401 CB ILE B 374 4042 9794 4918 1079 -831 -1240 C ATOM 2402 CG1 ILE B 374 -6.635 44.603 4.296 1.00 46.48 C ANISOU 2402 CG1 ILE B 374 3758 9399 4502 1048 -821 -1203 C ATOM 2403 CG2 ILE B 374 -8.973 43.763 3.967 1.00 47.41 C ANISOU 2403 CG2 ILE B 374 3713 9586 4715 1062 -861 -1322 C ATOM 2404 CD1 ILE B 374 -6.004 43.232 4.201 1.00 43.53 C ANISOU 2404 CD1 ILE B 374 3351 9001 4187 985 -760 -1220 C ATOM 2405 N THR B 375 -10.966 46.535 4.819 1.00 46.60 N ANISOU 2405 N THR B 375 3624 9557 4523 1251 -965 -1295 N ATOM 2406 CA THR B 375 -12.359 46.573 5.252 1.00 52.15 C ANISOU 2406 CA THR B 375 4225 10309 5281 1297 -968 -1323 C ATOM 2407 C THR B 375 -13.072 45.247 5.002 1.00 53.74 C ANISOU 2407 C THR B 375 4290 10535 5594 1236 -948 -1379 C ATOM 2408 O THR B 375 -12.496 44.318 4.436 1.00 49.50 O ANISOU 2408 O THR B 375 3754 9973 5080 1164 -939 -1403 O ATOM 2409 CB THR B 375 -13.138 47.704 4.554 1.00 60.20 C ANISOU 2409 CB THR B 375 5268 11376 6228 1384 -1066 -1351 C ATOM 2410 OG1 THR B 375 -13.274 47.405 3.159 1.00 64.61 O ANISOU 2410 OG1 THR B 375 5819 11955 6776 1360 -1138 -1415 O ATOM 2411 CG2 THR B 375 -12.412 49.030 4.718 1.00 62.19 C ANISOU 2411 CG2 THR B 375 5671 11598 6362 1438 -1100 -1295 C ATOM 2412 N LEU B 376 -14.326 45.165 5.438 1.00 86.33 N ANISOU 2412 N LEU B 376 8302 14710 9788 1266 -941 -1396 N ATOM 2413 CA LEU B 376 -15.139 43.975 5.207 1.00 88.40 C ANISOU 2413 CA LEU B 376 8426 14998 10164 1203 -935 -1445 C ATOM 2414 C LEU B 376 -15.505 43.881 3.734 1.00 90.82 C ANISOU 2414 C LEU B 376 8722 15329 10457 1196 -1044 -1514 C ATOM 2415 O LEU B 376 -15.502 42.797 3.149 1.00 93.75 O ANISOU 2415 O LEU B 376 9054 15684 10882 1121 -1059 -1556 O ATOM 2416 CB LEU B 376 -16.408 44.006 6.062 1.00 87.55 C ANISOU 2416 CB LEU B 376 8187 14942 10136 1241 -897 -1435 C ATOM 2417 CG LEU B 376 -17.486 42.975 5.709 1.00 83.78 C ANISOU 2417 CG LEU B 376 7548 14504 9781 1181 -915 -1483 C ATOM 2418 CD1 LEU B 376 -16.941 41.553 5.785 1.00 80.44 C ANISOU 2418 CD1 LEU B 376 7110 14029 9425 1065 -865 -1492 C ATOM 2419 CD2 LEU B 376 -18.702 43.134 6.609 1.00 82.17 C ANISOU 2419 CD2 LEU B 376 7208 14358 9653 1227 -865 -1458 C ATOM 2420 N ASP B 377 -15.822 45.027 3.142 1.00 77.79 N ANISOU 2420 N ASP B 377 7121 13709 8726 1277 -1127 -1528 N ATOM 2421 CA ASP B 377 -16.129 45.091 1.722 1.00 75.08 C ANISOU 2421 CA ASP B 377 6795 13380 8350 1284 -1240 -1594 C ATOM 2422 C ASP B 377 -14.974 44.505 0.923 1.00 67.10 C ANISOU 2422 C ASP B 377 5886 12315 7295 1223 -1241 -1605 C ATOM 2423 O ASP B 377 -15.183 43.748 -0.021 1.00 68.44 O ANISOU 2423 O ASP B 377 6039 12476 7490 1182 -1296 -1661 O ATOM 2424 CB ASP B 377 -16.391 46.535 1.289 1.00 81.37 C ANISOU 2424 CB ASP B 377 7669 14204 9043 1387 -1321 -1597 C ATOM 2425 CG ASP B 377 -17.617 47.130 1.956 1.00 87.25 C ANISOU 2425 CG ASP B 377 8314 15011 9828 1465 -1329 -1592 C ATOM 2426 OD1 ASP B 377 -17.863 46.827 3.143 1.00 90.16 O ANISOU 2426 OD1 ASP B 377 8603 15390 10265 1459 -1235 -1550 O ATOM 2427 OD2 ASP B 377 -18.333 47.907 1.291 1.00 91.11 O ANISOU 2427 OD2 ASP B 377 8806 15537 10274 1539 -1427 -1630 O ATOM 2428 N ASP B 378 -13.754 44.857 1.315 1.00 49.75 N ANISOU 2428 N ASP B 378 3795 10077 5030 1219 -1180 -1548 N ATOM 2429 CA ASP B 378 -12.558 44.354 0.653 1.00 48.34 C ANISOU 2429 CA ASP B 378 3708 9852 4807 1170 -1163 -1546 C ATOM 2430 C ASP B 378 -12.519 42.829 0.658 1.00 54.78 C ANISOU 2430 C ASP B 378 4456 10644 5713 1087 -1123 -1574 C ATOM 2431 O ASP B 378 -12.413 42.200 -0.394 1.00 59.93 O ANISOU 2431 O ASP B 378 5137 11281 6354 1062 -1168 -1623 O ATOM 2432 CB ASP B 378 -11.301 44.911 1.326 1.00 47.12 C ANISOU 2432 CB ASP B 378 3648 9661 4593 1171 -1096 -1468 C ATOM 2433 CG ASP B 378 -11.190 46.418 1.196 1.00 51.94 C ANISOU 2433 CG ASP B 378 4354 10282 5099 1244 -1148 -1437 C ATOM 2434 OD1 ASP B 378 -12.012 47.015 0.471 1.00 49.91 O ANISOU 2434 OD1 ASP B 378 4101 10060 4805 1298 -1235 -1481 O ATOM 2435 OD2 ASP B 378 -10.277 47.004 1.821 1.00 55.88 O ANISOU 2435 OD2 ASP B 378 4929 10750 5552 1247 -1109 -1367 O ATOM 2436 N MET B 379 -12.614 42.243 1.847 1.00 72.37 N ANISOU 2436 N MET B 379 6609 12864 8025 1050 -1040 -1544 N ATOM 2437 CA MET B 379 -12.543 40.794 2.001 1.00 78.98 C ANISOU 2437 CA MET B 379 7392 13672 8946 968 -997 -1565 C ATOM 2438 C MET B 379 -13.745 40.087 1.381 1.00 84.61 C ANISOU 2438 C MET B 379 8006 14409 9733 939 -1070 -1632 C ATOM 2439 O MET B 379 -13.786 38.859 1.318 1.00 87.68 O ANISOU 2439 O MET B 379 8360 14770 10186 868 -1059 -1657 O ATOM 2440 CB MET B 379 -12.435 40.422 3.481 1.00 79.79 C ANISOU 2440 CB MET B 379 7444 13757 9115 939 -893 -1515 C ATOM 2441 CG MET B 379 -11.225 41.008 4.182 1.00 81.94 C ANISOU 2441 CG MET B 379 7813 13993 9326 958 -830 -1447 C ATOM 2442 SD MET B 379 -11.334 40.831 5.971 1.00100.00 S ANISOU 2442 SD MET B 379 10056 16257 11682 949 -725 -1390 S ATOM 2443 CE MET B 379 -11.573 39.062 6.120 1.00194.39 C ANISOU 2443 CE MET B 379 21929 28185 23744 850 -681 -1428 C ATOM 2444 N GLU B 380 -14.717 40.868 0.919 1.00 67.96 N ANISOU 2444 N GLU B 380 5859 12349 7615 995 -1154 -1659 N ATOM 2445 CA GLU B 380 -15.959 40.313 0.391 1.00 69.34 C ANISOU 2445 CA GLU B 380 5925 12550 7872 970 -1237 -1717 C ATOM 2446 C GLU B 380 -16.015 40.379 -1.138 1.00 70.46 C ANISOU 2446 C GLU B 380 6141 12678 7951 989 -1358 -1779 C ATOM 2447 O GLU B 380 -16.753 39.627 -1.772 1.00 71.51 O ANISOU 2447 O GLU B 380 6219 12806 8145 949 -1438 -1832 O ATOM 2448 CB GLU B 380 -17.160 41.043 1.002 1.00 70.81 C ANISOU 2448 CB GLU B 380 5991 12803 8110 1023 -1248 -1705 C ATOM 2449 CG GLU B 380 -18.463 40.258 0.971 1.00 73.01 C ANISOU 2449 CG GLU B 380 6106 13113 8520 974 -1293 -1738 C ATOM 2450 CD GLU B 380 -19.568 40.928 1.772 1.00 72.91 C ANISOU 2450 CD GLU B 380 5962 13174 8568 1030 -1272 -1711 C ATOM 2451 OE1 GLU B 380 -19.724 42.163 1.664 1.00 72.17 O ANISOU 2451 OE1 GLU B 380 5908 13115 8399 1130 -1306 -1705 O ATOM 2452 OE2 GLU B 380 -20.285 40.216 2.507 1.00 71.81 O ANISOU 2452 OE2 GLU B 380 5681 13056 8547 978 -1220 -1694 O ATOM 2453 N GLU B 381 -15.224 41.274 -1.724 1.00 64.31 N ANISOU 2453 N GLU B 381 5497 11889 7049 1047 -1374 -1770 N ATOM 2454 CA GLU B 381 -15.224 41.468 -3.172 1.00 63.17 C ANISOU 2454 CA GLU B 381 5448 11728 6827 1078 -1483 -1825 C ATOM 2455 C GLU B 381 -13.828 41.349 -3.777 1.00 62.29 C ANISOU 2455 C GLU B 381 5489 11566 6613 1075 -1443 -1810 C ATOM 2456 O GLU B 381 -13.606 41.730 -4.925 1.00 66.62 O ANISOU 2456 O GLU B 381 6147 12097 7068 1115 -1511 -1841 O ATOM 2457 CB GLU B 381 -15.835 42.824 -3.524 1.00 64.85 C ANISOU 2457 CB GLU B 381 5679 11982 6979 1166 -1562 -1837 C ATOM 2458 CG GLU B 381 -15.047 44.013 -3.012 1.00 65.15 C ANISOU 2458 CG GLU B 381 5804 12029 6923 1220 -1504 -1774 C ATOM 2459 CD GLU B 381 -15.934 45.198 -2.694 1.00 68.82 C ANISOU 2459 CD GLU B 381 6230 12546 7373 1301 -1553 -1770 C ATOM 2460 OE1 GLU B 381 -15.395 46.284 -2.396 1.00 71.91 O ANISOU 2460 OE1 GLU B 381 6710 12938 7674 1354 -1531 -1725 O ATOM 2461 OE2 GLU B 381 -17.172 45.042 -2.734 1.00 67.89 O ANISOU 2461 OE2 GLU B 381 5993 12467 7334 1314 -1616 -1811 O ATOM 2462 N MET B 382 -12.893 40.820 -2.996 1.00 60.87 N ANISOU 2462 N MET B 382 5316 11363 6450 1031 -1330 -1761 N ATOM 2463 CA MET B 382 -11.528 40.591 -3.457 1.00 58.06 C ANISOU 2463 CA MET B 382 5082 10965 6013 1026 -1277 -1738 C ATOM 2464 C MET B 382 -11.089 39.166 -3.140 1.00 63.77 C ANISOU 2464 C MET B 382 5782 11648 6798 956 -1215 -1741 C ATOM 2465 O MET B 382 -11.292 38.680 -2.030 1.00 65.47 O ANISOU 2465 O MET B 382 5906 11867 7103 911 -1156 -1718 O ATOM 2466 CB MET B 382 -10.565 41.584 -2.802 1.00 51.57 C ANISOU 2466 CB MET B 382 4312 10151 5132 1053 -1202 -1660 C ATOM 2467 CG MET B 382 -10.314 42.842 -3.611 1.00 53.73 C ANISOU 2467 CG MET B 382 4691 10436 5289 1118 -1254 -1651 C ATOM 2468 SD MET B 382 -9.132 43.955 -2.822 1.00 77.80 S ANISOU 2468 SD MET B 382 7804 13482 8273 1134 -1177 -1551 S ATOM 2469 CE MET B 382 -10.222 44.978 -1.843 1.00 47.59 C ANISOU 2469 CE MET B 382 3910 9697 4477 1178 -1214 -1539 C ATOM 2470 N ASP B 383 -10.486 38.498 -4.116 1.00 69.51 N ANISOU 2470 N ASP B 383 6604 12336 7472 954 -1228 -1769 N ATOM 2471 CA ASP B 383 -9.985 37.146 -3.908 1.00 74.64 C ANISOU 2471 CA ASP B 383 7255 12942 8162 899 -1175 -1775 C ATOM 2472 C ASP B 383 -8.549 37.171 -3.390 1.00 69.57 C ANISOU 2472 C ASP B 383 6665 12287 7482 901 -1058 -1708 C ATOM 2473 O ASP B 383 -7.782 38.080 -3.704 1.00 68.39 O ANISOU 2473 O ASP B 383 6587 12151 7250 946 -1034 -1668 O ATOM 2474 CB ASP B 383 -10.050 36.342 -5.210 1.00 87.58 C ANISOU 2474 CB ASP B 383 8981 14537 9757 905 -1250 -1839 C ATOM 2475 CG ASP B 383 -11.445 36.312 -5.814 1.00102.62 C ANISOU 2475 CG ASP B 383 10842 16447 11701 902 -1385 -1905 C ATOM 2476 OD1 ASP B 383 -11.607 36.798 -6.955 1.00111.98 O ANISOU 2476 OD1 ASP B 383 12116 17624 12806 956 -1470 -1941 O ATOM 2477 OD2 ASP B 383 -12.380 35.815 -5.152 1.00104.64 O ANISOU 2477 OD2 ASP B 383 10975 16713 12070 846 -1409 -1919 O ATOM 2478 N GLY B 384 -8.194 36.168 -2.594 1.00 69.50 N ANISOU 2478 N GLY B 384 6619 12251 7538 849 -989 -1696 N ATOM 2479 CA GLY B 384 -6.829 36.008 -2.127 1.00 65.41 C ANISOU 2479 CA GLY B 384 6145 11715 6994 848 -886 -1638 C ATOM 2480 C GLY B 384 -6.408 36.926 -0.994 1.00 59.55 C ANISOU 2480 C GLY B 384 5366 10993 6268 851 -823 -1565 C ATOM 2481 O GLY B 384 -5.257 37.365 -0.944 1.00 53.69 O ANISOU 2481 O GLY B 384 4677 10247 5475 872 -768 -1508 O ATOM 2482 N LEU B 385 -7.331 37.212 -0.080 1.00 60.49 N ANISOU 2482 N LEU B 385 5397 11130 6457 833 -833 -1562 N ATOM 2483 CA LEU B 385 -7.015 38.032 1.086 1.00 55.39 C ANISOU 2483 CA LEU B 385 4730 10492 5825 841 -779 -1494 C ATOM 2484 C LEU B 385 -6.757 37.174 2.324 1.00 55.86 C ANISOU 2484 C LEU B 385 4745 10515 5963 791 -702 -1471 C ATOM 2485 O LEU B 385 -7.312 36.082 2.462 1.00 54.26 O ANISOU 2485 O LEU B 385 4495 10296 5826 745 -701 -1514 O ATOM 2486 CB LEU B 385 -8.120 39.057 1.354 1.00 52.53 C ANISOU 2486 CB LEU B 385 4316 10172 5472 874 -831 -1496 C ATOM 2487 CG LEU B 385 -8.168 40.262 0.408 1.00 50.84 C ANISOU 2487 CG LEU B 385 4166 9988 5164 935 -900 -1497 C ATOM 2488 CD1 LEU B 385 -9.208 41.270 0.871 1.00 46.35 C ANISOU 2488 CD1 LEU B 385 3548 9458 4604 976 -943 -1494 C ATOM 2489 CD2 LEU B 385 -6.799 40.919 0.298 1.00 50.13 C ANISOU 2489 CD2 LEU B 385 4169 9883 4995 953 -860 -1433 C ATOM 2490 N SER B 386 -5.917 37.688 3.219 1.00 76.40 N ANISOU 2490 N SER B 386 7371 13100 8557 799 -644 -1403 N ATOM 2491 CA SER B 386 -5.407 36.931 4.364 1.00 73.83 C ANISOU 2491 CA SER B 386 7031 12728 8291 759 -569 -1376 C ATOM 2492 C SER B 386 -6.466 36.202 5.189 1.00 70.75 C ANISOU 2492 C SER B 386 6562 12329 7990 718 -553 -1404 C ATOM 2493 O SER B 386 -6.402 34.982 5.351 1.00 68.70 O ANISOU 2493 O SER B 386 6292 12036 7777 669 -525 -1432 O ATOM 2494 CB SER B 386 -4.592 37.846 5.279 1.00 65.41 C ANISOU 2494 CB SER B 386 6003 11644 7206 780 -533 -1296 C ATOM 2495 OG SER B 386 -4.035 37.118 6.360 1.00 57.23 O ANISOU 2495 OG SER B 386 4966 10555 6223 746 -468 -1271 O ATOM 2496 N ASP B 387 -7.417 36.958 5.729 1.00 52.39 N ANISOU 2496 N ASP B 387 4186 10035 5687 740 -567 -1393 N ATOM 2497 CA ASP B 387 -8.444 36.401 6.605 1.00 56.47 C ANISOU 2497 CA ASP B 387 4618 10549 6289 707 -537 -1406 C ATOM 2498 C ASP B 387 -7.884 36.152 8.012 1.00 49.49 C ANISOU 2498 C ASP B 387 3756 9612 5438 690 -452 -1356 C ATOM 2499 O ASP B 387 -8.577 35.626 8.886 1.00 45.22 O ANISOU 2499 O ASP B 387 3159 9058 4965 660 -408 -1356 O ATOM 2500 CB ASP B 387 -9.026 35.113 6.008 1.00 63.75 C ANISOU 2500 CB ASP B 387 5492 11467 7265 646 -563 -1470 C ATOM 2501 CG ASP B 387 -10.500 34.936 6.320 1.00 72.12 C ANISOU 2501 CG ASP B 387 6438 12561 8405 622 -578 -1492 C ATOM 2502 OD1 ASP B 387 -11.068 35.785 7.041 1.00 79.76 O ANISOU 2502 OD1 ASP B 387 7362 13558 9384 662 -557 -1458 O ATOM 2503 OD2 ASP B 387 -11.093 33.947 5.840 1.00 69.62 O ANISOU 2503 OD2 ASP B 387 6075 12240 8139 565 -614 -1541 O ATOM 2504 N PHE B 388 -6.625 36.536 8.218 1.00 59.70 N ANISOU 2504 N PHE B 388 5132 10870 6681 710 -432 -1309 N ATOM 2505 CA PHE B 388 -5.991 36.463 9.533 1.00 52.31 C ANISOU 2505 CA PHE B 388 4235 9873 5766 704 -367 -1257 C ATOM 2506 C PHE B 388 -5.774 37.859 10.106 1.00 55.60 C ANISOU 2506 C PHE B 388 4700 10288 6135 764 -379 -1194 C ATOM 2507 O PHE B 388 -5.411 38.010 11.271 1.00 57.10 O ANISOU 2507 O PHE B 388 4933 10425 6338 771 -338 -1147 O ATOM 2508 CB PHE B 388 -4.638 35.748 9.460 1.00 47.68 C ANISOU 2508 CB PHE B 388 3707 9238 5172 678 -341 -1247 C ATOM 2509 CG PHE B 388 -4.731 34.297 9.093 1.00 52.87 C ANISOU 2509 CG PHE B 388 4343 9878 5869 624 -326 -1304 C ATOM 2510 CD1 PHE B 388 -5.711 33.489 9.644 1.00 56.77 C ANISOU 2510 CD1 PHE B 388 4780 10359 6429 579 -302 -1336 C ATOM 2511 CD2 PHE B 388 -3.822 33.735 8.215 1.00 55.79 C ANISOU 2511 CD2 PHE B 388 4752 10240 6205 619 -335 -1322 C ATOM 2512 CE1 PHE B 388 -5.792 32.151 9.310 1.00 59.07 C ANISOU 2512 CE1 PHE B 388 5064 10627 6753 524 -299 -1386 C ATOM 2513 CE2 PHE B 388 -3.897 32.400 7.880 1.00 57.96 C ANISOU 2513 CE2 PHE B 388 5025 10492 6505 577 -328 -1375 C ATOM 2514 CZ PHE B 388 -4.883 31.606 8.427 1.00 57.88 C ANISOU 2514 CZ PHE B 388 4966 10464 6560 526 -316 -1408 C ATOM 2515 N THR B 389 -5.986 38.877 9.279 1.00 62.53 N ANISOU 2515 N THR B 389 5586 11217 6955 807 -441 -1194 N ATOM 2516 CA THR B 389 -5.751 40.256 9.691 1.00 64.62 C ANISOU 2516 CA THR B 389 5914 11478 7162 864 -467 -1135 C ATOM 2517 C THR B 389 -6.697 40.693 10.807 1.00 68.06 C ANISOU 2517 C THR B 389 6333 11910 7618 903 -443 -1116 C ATOM 2518 O THR B 389 -7.884 40.364 10.796 1.00 69.04 O ANISOU 2518 O THR B 389 6371 12074 7785 905 -432 -1155 O ATOM 2519 CB THR B 389 -5.887 41.231 8.507 1.00 57.97 C ANISOU 2519 CB THR B 389 5089 10691 6246 902 -543 -1145 C ATOM 2520 OG1 THR B 389 -7.092 40.944 7.790 1.00 56.12 O ANISOU 2520 OG1 THR B 389 4775 10514 6033 906 -573 -1212 O ATOM 2521 CG2 THR B 389 -4.704 41.091 7.566 1.00 53.98 C ANISOU 2521 CG2 THR B 389 4629 10180 5700 879 -556 -1137 C ATOM 2522 N GLY B 390 -6.157 41.435 11.768 1.00 55.59 N ANISOU 2522 N GLY B 390 4837 10278 6007 937 -435 -1050 N ATOM 2523 CA GLY B 390 -6.942 41.942 12.877 1.00 53.45 C ANISOU 2523 CA GLY B 390 4577 9993 5738 992 -409 -1023 C ATOM 2524 C GLY B 390 -7.204 40.885 13.929 1.00 51.93 C ANISOU 2524 C GLY B 390 4355 9757 5621 958 -322 -1027 C ATOM 2525 O GLY B 390 -8.068 41.054 14.789 1.00 50.99 O ANISOU 2525 O GLY B 390 4220 9636 5516 999 -280 -1014 O ATOM 2526 N SER B 391 -6.458 39.788 13.865 1.00 56.53 N ANISOU 2526 N SER B 391 4933 10301 6245 889 -293 -1044 N ATOM 2527 CA SER B 391 -6.638 38.703 14.821 1.00 61.44 C ANISOU 2527 CA SER B 391 5537 10872 6933 849 -214 -1050 C ATOM 2528 C SER B 391 -5.321 38.269 15.459 1.00 62.63 C ANISOU 2528 C SER B 391 5777 10932 7087 821 -196 -1018 C ATOM 2529 O SER B 391 -4.237 38.588 14.968 1.00 63.89 O ANISOU 2529 O SER B 391 5984 11079 7212 817 -241 -997 O ATOM 2530 CB SER B 391 -7.312 37.502 14.153 1.00 60.52 C ANISOU 2530 CB SER B 391 5314 10799 6882 784 -196 -1118 C ATOM 2531 OG SER B 391 -6.375 36.731 13.424 1.00 60.74 O ANISOU 2531 OG SER B 391 5357 10810 6912 732 -214 -1144 O ATOM 2532 N VAL B 392 -5.433 37.542 16.564 1.00 52.62 N ANISOU 2532 N VAL B 392 4529 9600 5862 803 -128 -1011 N ATOM 2533 CA VAL B 392 -4.276 36.960 17.223 1.00 50.54 C ANISOU 2533 CA VAL B 392 4346 9245 5612 775 -110 -989 C ATOM 2534 C VAL B 392 -4.185 35.484 16.859 1.00 49.46 C ANISOU 2534 C VAL B 392 4158 9106 5531 700 -75 -1045 C ATOM 2535 O VAL B 392 -5.076 34.695 17.185 1.00 46.45 O ANISOU 2535 O VAL B 392 3725 8727 5196 669 -22 -1076 O ATOM 2536 CB VAL B 392 -4.364 37.107 18.749 1.00 51.21 C ANISOU 2536 CB VAL B 392 4516 9242 5698 809 -62 -944 C ATOM 2537 CG1 VAL B 392 -3.099 36.583 19.401 1.00 48.24 C ANISOU 2537 CG1 VAL B 392 4231 8765 5333 784 -61 -922 C ATOM 2538 CG2 VAL B 392 -4.597 38.560 19.123 1.00 53.94 C ANISOU 2538 CG2 VAL B 392 4924 9588 5981 892 -99 -891 C ATOM 2539 N LEU B 393 -3.109 35.119 16.172 1.00 57.03 N ANISOU 2539 N LEU B 393 5131 10058 6481 674 -107 -1055 N ATOM 2540 CA LEU B 393 -2.907 33.745 15.736 1.00 57.02 C ANISOU 2540 CA LEU B 393 5099 10049 6516 615 -85 -1108 C ATOM 2541 C LEU B 393 -2.101 32.973 16.769 1.00 57.18 C ANISOU 2541 C LEU B 393 5194 9969 6561 595 -46 -1094 C ATOM 2542 O LEU B 393 -1.320 33.555 17.521 1.00 57.93 O ANISOU 2542 O LEU B 393 5366 10004 6640 627 -57 -1041 O ATOM 2543 CB LEU B 393 -2.202 33.715 14.380 1.00 58.14 C ANISOU 2543 CB LEU B 393 5222 10240 6627 610 -132 -1128 C ATOM 2544 CG LEU B 393 -2.880 34.520 13.269 1.00 52.92 C ANISOU 2544 CG LEU B 393 4505 9670 5931 634 -180 -1144 C ATOM 2545 CD1 LEU B 393 -2.102 34.400 11.970 1.00 50.14 C ANISOU 2545 CD1 LEU B 393 4152 9356 5543 633 -216 -1161 C ATOM 2546 CD2 LEU B 393 -4.320 34.068 13.083 1.00 51.03 C ANISOU 2546 CD2 LEU B 393 4186 9475 5730 610 -170 -1195 C ATOM 2547 N ARG B 394 -2.295 31.660 16.798 1.00 45.18 N ANISOU 2547 N ARG B 394 3659 8427 5080 543 -10 -1143 N ATOM 2548 CA ARG B 394 -1.651 30.811 17.790 1.00 42.01 C ANISOU 2548 CA ARG B 394 3334 7926 4702 522 27 -1140 C ATOM 2549 C ARG B 394 -1.437 29.416 17.222 1.00 42.11 C ANISOU 2549 C ARG B 394 3335 7932 4734 470 34 -1200 C ATOM 2550 O ARG B 394 -2.394 28.672 17.010 1.00 42.58 O ANISOU 2550 O ARG B 394 3346 8011 4821 423 54 -1244 O ATOM 2551 CB ARG B 394 -2.518 30.742 19.049 1.00 47.49 C ANISOU 2551 CB ARG B 394 4052 8569 5421 520 87 -1124 C ATOM 2552 CG ARG B 394 -1.968 29.875 20.170 1.00 44.91 C ANISOU 2552 CG ARG B 394 3819 8129 5114 501 128 -1122 C ATOM 2553 CD ARG B 394 -3.070 29.552 21.165 1.00 50.77 C ANISOU 2553 CD ARG B 394 4568 8839 5885 484 203 -1120 C ATOM 2554 NE ARG B 394 -2.595 28.778 22.307 1.00 57.02 N ANISOU 2554 NE ARG B 394 5466 9513 6687 470 244 -1116 N ATOM 2555 CZ ARG B 394 -3.392 28.104 23.129 1.00 64.95 C ANISOU 2555 CZ ARG B 394 6486 10472 7718 437 318 -1123 C ATOM 2556 NH1 ARG B 394 -4.702 28.101 22.927 1.00 61.78 N ANISOU 2556 NH1 ARG B 394 5987 10142 7345 413 360 -1130 N ATOM 2557 NH2 ARG B 394 -2.880 27.426 24.148 1.00 73.02 N ANISOU 2557 NH2 ARG B 394 7622 11380 8742 429 350 -1120 N ATOM 2558 N LEU B 395 -0.178 29.067 16.973 1.00 44.29 N ANISOU 2558 N LEU B 395 3655 8178 4995 480 15 -1198 N ATOM 2559 CA LEU B 395 0.154 27.781 16.360 1.00 52.33 C ANISOU 2559 CA LEU B 395 4679 9188 6017 447 16 -1254 C ATOM 2560 C LEU B 395 1.281 27.046 17.092 1.00 53.42 C ANISOU 2560 C LEU B 395 4900 9233 6162 451 30 -1249 C ATOM 2561 O LEU B 395 2.143 27.669 17.712 1.00 51.99 O ANISOU 2561 O LEU B 395 4762 9011 5979 487 20 -1197 O ATOM 2562 CB LEU B 395 0.492 27.957 14.871 1.00 53.69 C ANISOU 2562 CB LEU B 395 4806 9441 6153 466 -26 -1272 C ATOM 2563 CG LEU B 395 1.154 29.257 14.400 1.00 52.11 C ANISOU 2563 CG LEU B 395 4591 9290 5918 518 -59 -1217 C ATOM 2564 CD1 LEU B 395 1.911 29.036 13.101 1.00 52.10 C ANISOU 2564 CD1 LEU B 395 4577 9339 5879 539 -80 -1233 C ATOM 2565 CD2 LEU B 395 0.132 30.374 14.232 1.00 49.47 C ANISOU 2565 CD2 LEU B 395 4207 9016 5575 529 -78 -1201 C ATOM 2566 N ASP B 396 1.257 25.717 17.015 1.00 43.87 N ANISOU 2566 N ASP B 396 3718 7988 4961 413 45 -1304 N ATOM 2567 CA ASP B 396 2.259 24.881 17.669 1.00 49.20 C ANISOU 2567 CA ASP B 396 4478 8574 5641 419 56 -1310 C ATOM 2568 C ASP B 396 3.375 24.496 16.704 1.00 49.92 C ANISOU 2568 C ASP B 396 4571 8693 5703 454 29 -1324 C ATOM 2569 O ASP B 396 3.177 23.683 15.803 1.00 48.66 O ANISOU 2569 O ASP B 396 4404 8563 5523 441 22 -1377 O ATOM 2570 CB ASP B 396 1.612 23.619 18.247 1.00 57.85 C ANISOU 2570 CB ASP B 396 5622 9602 6757 361 88 -1359 C ATOM 2571 CG ASP B 396 2.621 22.692 18.910 1.00 65.42 C ANISOU 2571 CG ASP B 396 6680 10463 7713 370 94 -1373 C ATOM 2572 OD1 ASP B 396 3.766 23.127 19.160 1.00 68.01 O ANISOU 2572 OD1 ASP B 396 7036 10767 8036 422 75 -1336 O ATOM 2573 OD2 ASP B 396 2.266 21.525 19.187 1.00 66.41 O ANISOU 2573 OD2 ASP B 396 6857 10533 7844 323 111 -1421 O ATOM 2574 N VAL B 397 4.551 25.080 16.906 1.00 55.53 N ANISOU 2574 N VAL B 397 5296 9392 6413 502 14 -1272 N ATOM 2575 CA VAL B 397 5.697 24.821 16.042 1.00 54.25 C ANISOU 2575 CA VAL B 397 5123 9262 6226 546 0 -1271 C ATOM 2576 C VAL B 397 6.378 23.501 16.396 1.00 61.85 C ANISOU 2576 C VAL B 397 6159 10152 7191 552 11 -1311 C ATOM 2577 O VAL B 397 7.074 22.908 15.570 1.00 60.82 O ANISOU 2577 O VAL B 397 6029 10049 7032 588 9 -1332 O ATOM 2578 CB VAL B 397 6.725 25.965 16.123 1.00 47.67 C ANISOU 2578 CB VAL B 397 4263 8447 5400 589 -22 -1191 C ATOM 2579 CG1 VAL B 397 6.126 27.253 15.584 1.00 42.20 C ANISOU 2579 CG1 VAL B 397 3509 7833 4693 589 -40 -1156 C ATOM 2580 CG2 VAL B 397 7.196 26.151 17.558 1.00 51.20 C ANISOU 2580 CG2 VAL B 397 4774 8795 5886 589 -31 -1152 C ATOM 2581 N ASP B 398 6.172 23.045 17.628 1.00 69.94 N ANISOU 2581 N ASP B 398 7254 11080 8242 524 24 -1320 N ATOM 2582 CA ASP B 398 6.764 21.795 18.092 1.00 71.97 C ANISOU 2582 CA ASP B 398 7595 11252 8497 528 29 -1360 C ATOM 2583 C ASP B 398 5.957 20.587 17.623 1.00 71.69 C ANISOU 2583 C ASP B 398 7590 11212 8438 485 40 -1437 C ATOM 2584 O ASP B 398 5.041 20.136 18.312 1.00 68.44 O ANISOU 2584 O ASP B 398 7216 10745 8041 426 59 -1462 O ATOM 2585 CB ASP B 398 6.885 21.793 19.618 1.00 73.38 C ANISOU 2585 CB ASP B 398 7855 11319 8708 517 35 -1339 C ATOM 2586 CG ASP B 398 7.850 22.847 20.127 1.00 75.09 C ANISOU 2586 CG ASP B 398 8063 11519 8950 561 5 -1264 C ATOM 2587 OD1 ASP B 398 8.475 23.533 19.292 1.00 72.10 O ANISOU 2587 OD1 ASP B 398 7608 11220 8565 596 -15 -1226 O ATOM 2588 OD2 ASP B 398 7.987 22.991 21.361 1.00 78.65 O ANISOU 2588 OD2 ASP B 398 8589 11872 9423 560 -1 -1241 O ATOM 2589 N THR B 399 6.303 20.066 16.449 1.00 80.18 N ANISOU 2589 N THR B 399 8653 12340 9472 515 28 -1470 N ATOM 2590 CA THR B 399 5.596 18.918 15.887 1.00 86.61 C ANISOU 2590 CA THR B 399 9507 13144 10255 477 21 -1542 C ATOM 2591 C THR B 399 6.548 17.856 15.350 1.00 86.92 C ANISOU 2591 C THR B 399 9616 13163 10248 532 10 -1582 C ATOM 2592 O THR B 399 7.624 18.169 14.839 1.00 86.07 O ANISOU 2592 O THR B 399 9482 13098 10122 608 11 -1553 O ATOM 2593 CB THR B 399 4.652 19.330 14.738 1.00 87.28 C ANISOU 2593 CB THR B 399 9518 13321 10323 455 4 -1555 C ATOM 2594 OG1 THR B 399 5.423 19.666 13.577 1.00 84.03 O ANISOU 2594 OG1 THR B 399 9073 12984 9869 526 -7 -1543 O ATOM 2595 CG2 THR B 399 3.800 20.518 15.142 1.00 89.72 C ANISOU 2595 CG2 THR B 399 9749 13667 10674 420 14 -1511 C ATOM 2596 N ASP B 400 6.139 16.597 15.471 1.00 83.61 N ANISOU 2596 N ASP B 400 9285 12677 9806 494 -1 -1645 N ATOM 2597 CA ASP B 400 6.848 15.496 14.835 1.00 89.38 C ANISOU 2597 CA ASP B 400 10096 13387 10477 548 -18 -1692 C ATOM 2598 C ASP B 400 6.196 15.218 13.488 1.00 94.10 C ANISOU 2598 C ASP B 400 10685 14044 11026 542 -46 -1731 C ATOM 2599 O ASP B 400 6.058 14.068 13.072 1.00 98.22 O ANISOU 2599 O ASP B 400 11300 14522 11497 538 -75 -1790 O ATOM 2600 CB ASP B 400 6.820 14.246 15.716 1.00 92.51 C ANISOU 2600 CB ASP B 400 10618 13666 10867 513 -24 -1741 C ATOM 2601 CG ASP B 400 7.780 14.338 16.888 1.00 96.26 C ANISOU 2601 CG ASP B 400 11130 14073 11373 549 -8 -1712 C ATOM 2602 OD1 ASP B 400 8.550 15.320 16.954 1.00 94.05 O ANISOU 2602 OD1 ASP B 400 10776 13838 11120 603 3 -1652 O ATOM 2603 OD2 ASP B 400 7.768 13.427 17.742 1.00101.91 O ANISOU 2603 OD2 ASP B 400 11953 14684 12084 521 -11 -1747 O ATOM 2604 N MET B 401 5.791 16.291 12.817 1.00 97.79 N ANISOU 2604 N MET B 401 11051 14602 11503 542 -46 -1697 N ATOM 2605 CA MET B 401 5.121 16.204 11.526 1.00 96.06 C ANISOU 2605 CA MET B 401 10819 14438 11240 538 -81 -1729 C ATOM 2606 C MET B 401 5.937 16.941 10.471 1.00 92.41 C ANISOU 2606 C MET B 401 10308 14065 10737 633 -68 -1695 C ATOM 2607 O MET B 401 6.593 17.941 10.769 1.00 89.83 O ANISOU 2607 O MET B 401 9912 13780 10441 667 -37 -1632 O ATOM 2608 CB MET B 401 3.721 16.805 11.623 1.00 97.84 C ANISOU 2608 CB MET B 401 10968 14691 11514 448 -96 -1724 C ATOM 2609 CG MET B 401 2.889 16.238 12.762 1.00100.26 C ANISOU 2609 CG MET B 401 11304 14919 11873 352 -91 -1740 C ATOM 2610 SD MET B 401 2.012 14.736 12.298 1.00106.55 S ANISOU 2610 SD MET B 401 12191 15653 12640 278 -149 -1817 S ATOM 2611 CE MET B 401 0.688 15.431 11.309 1.00 92.54 C ANISOU 2611 CE MET B 401 10310 13964 10887 228 -194 -1818 C ATOM 2612 N CYS B 402 5.889 16.450 9.238 1.00 87.44 N ANISOU 2612 N CYS B 402 9725 13461 10036 674 -95 -1734 N ATOM 2613 CA CYS B 402 6.743 16.978 8.180 1.00 85.39 C ANISOU 2613 CA CYS B 402 9441 13280 9724 775 -73 -1704 C ATOM 2614 C CYS B 402 5.957 17.566 7.011 1.00 87.86 C ANISOU 2614 C CYS B 402 9720 13658 10005 770 -105 -1711 C ATOM 2615 O CYS B 402 6.480 18.383 6.253 1.00 90.81 O ANISOU 2615 O CYS B 402 10048 14106 10350 835 -80 -1670 O ATOM 2616 CB CYS B 402 7.691 15.886 7.681 1.00 84.38 C ANISOU 2616 CB CYS B 402 9418 13123 9520 867 -65 -1736 C ATOM 2617 SG CYS B 402 8.599 15.046 8.998 1.00 78.29 S ANISOU 2617 SG CYS B 402 8705 12264 8777 881 -42 -1740 S ATOM 2618 N ASN B 403 4.705 17.147 6.865 1.00 79.78 N ANISOU 2618 N ASN B 403 8720 12605 8988 690 -162 -1761 N ATOM 2619 CA ASN B 403 3.872 17.633 5.774 1.00 74.80 C ANISOU 2619 CA ASN B 403 8064 12026 8331 682 -208 -1775 C ATOM 2620 C ASN B 403 3.340 19.043 6.028 1.00 69.78 C ANISOU 2620 C ASN B 403 7303 11455 7755 644 -197 -1725 C ATOM 2621 O ASN B 403 2.716 19.647 5.156 1.00 68.26 O ANISOU 2621 O ASN B 403 7080 11314 7544 645 -233 -1730 O ATOM 2622 CB ASN B 403 2.718 16.666 5.496 1.00 79.30 C ANISOU 2622 CB ASN B 403 8699 12538 8894 608 -286 -1843 C ATOM 2623 CG ASN B 403 1.668 16.674 6.592 1.00 84.38 C ANISOU 2623 CG ASN B 403 9281 13149 9631 487 -298 -1843 C ATOM 2624 OD1 ASN B 403 1.926 17.109 7.714 1.00 86.49 O ANISOU 2624 OD1 ASN B 403 9493 13411 9956 466 -243 -1802 O ATOM 2625 ND2 ASN B 403 0.474 16.191 6.269 1.00 84.60 N ANISOU 2625 ND2 ASN B 403 9319 13150 9674 407 -370 -1885 N ATOM 2626 N VAL B 404 3.592 19.563 7.226 1.00 71.02 N ANISOU 2626 N VAL B 404 7402 11604 7979 616 -154 -1679 N ATOM 2627 CA VAL B 404 3.131 20.897 7.599 1.00 65.52 C ANISOU 2627 CA VAL B 404 6601 10959 7333 587 -145 -1629 C ATOM 2628 C VAL B 404 4.180 21.640 8.424 1.00 65.68 C ANISOU 2628 C VAL B 404 6586 10987 7384 622 -92 -1560 C ATOM 2629 O VAL B 404 4.972 21.018 9.132 1.00 70.21 O ANISOU 2629 O VAL B 404 7203 11506 7968 637 -65 -1556 O ATOM 2630 CB VAL B 404 1.814 20.835 8.393 1.00 63.82 C ANISOU 2630 CB VAL B 404 6348 10715 7186 488 -166 -1646 C ATOM 2631 CG1 VAL B 404 0.671 20.387 7.495 1.00 59.24 C ANISOU 2631 CG1 VAL B 404 5775 10143 6591 446 -233 -1702 C ATOM 2632 CG2 VAL B 404 1.958 19.906 9.589 1.00 68.63 C ANISOU 2632 CG2 VAL B 404 7009 11237 7832 446 -141 -1659 C ATOM 2633 N PRO B 405 4.190 22.979 8.329 1.00 58.32 N ANISOU 2633 N PRO B 405 5579 10116 6464 634 -86 -1504 N ATOM 2634 CA PRO B 405 5.165 23.807 9.046 1.00 55.03 C ANISOU 2634 CA PRO B 405 5128 9704 6076 662 -52 -1430 C ATOM 2635 C PRO B 405 4.809 23.921 10.522 1.00 49.37 C ANISOU 2635 C PRO B 405 4406 8926 5425 607 -45 -1414 C ATOM 2636 O PRO B 405 5.685 24.120 11.367 1.00 50.48 O ANISOU 2636 O PRO B 405 4555 9032 5595 624 -25 -1368 O ATOM 2637 CB PRO B 405 5.022 25.184 8.377 1.00 55.88 C ANISOU 2637 CB PRO B 405 5173 9893 6167 680 -64 -1385 C ATOM 2638 CG PRO B 405 4.168 24.964 7.159 1.00 56.73 C ANISOU 2638 CG PRO B 405 5291 10038 6225 681 -99 -1439 C ATOM 2639 CD PRO B 405 3.309 23.790 7.477 1.00 55.84 C ANISOU 2639 CD PRO B 405 5218 9866 6131 626 -122 -1508 C ATOM 2640 N TYR B 406 3.521 23.793 10.820 1.00 44.03 N ANISOU 2640 N TYR B 406 3717 8236 4775 544 -61 -1447 N ATOM 2641 CA TYR B 406 3.024 23.945 12.179 1.00 43.86 C ANISOU 2641 CA TYR B 406 3694 8161 4810 496 -45 -1430 C ATOM 2642 C TYR B 406 1.721 23.179 12.351 1.00 51.92 C ANISOU 2642 C TYR B 406 4716 9155 5855 425 -53 -1484 C ATOM 2643 O TYR B 406 1.017 22.911 11.378 1.00 50.09 O ANISOU 2643 O TYR B 406 4465 8962 5603 408 -88 -1525 O ATOM 2644 CB TYR B 406 2.799 25.424 12.496 1.00 45.99 C ANISOU 2644 CB TYR B 406 3906 8472 5097 506 -47 -1369 C ATOM 2645 CG TYR B 406 1.788 26.093 11.591 1.00 46.26 C ANISOU 2645 CG TYR B 406 3879 8584 5114 498 -77 -1381 C ATOM 2646 CD1 TYR B 406 0.432 26.076 11.895 1.00 46.62 C ANISOU 2646 CD1 TYR B 406 3888 8632 5193 447 -83 -1405 C ATOM 2647 CD2 TYR B 406 2.191 26.741 10.430 1.00 46.98 C ANISOU 2647 CD2 TYR B 406 3948 8745 5158 544 -99 -1367 C ATOM 2648 CE1 TYR B 406 -0.495 26.686 11.066 1.00 43.35 C ANISOU 2648 CE1 TYR B 406 3414 8288 4767 445 -119 -1419 C ATOM 2649 CE2 TYR B 406 1.271 27.353 9.595 1.00 50.63 C ANISOU 2649 CE2 TYR B 406 4365 9271 5600 541 -134 -1383 C ATOM 2650 CZ TYR B 406 -0.069 27.322 9.919 1.00 46.85 C ANISOU 2650 CZ TYR B 406 3848 8794 5158 493 -149 -1410 C ATOM 2651 OH TYR B 406 -0.983 27.931 9.092 1.00 46.65 O ANISOU 2651 OH TYR B 406 3774 8832 5118 494 -192 -1427 O ATOM 2652 N SER B 407 1.403 22.830 13.593 1.00 61.72 N ANISOU 2652 N SER B 407 5983 10327 7139 382 -25 -1480 N ATOM 2653 CA SER B 407 0.140 22.174 13.900 1.00 67.69 C ANISOU 2653 CA SER B 407 6731 11059 7931 305 -23 -1517 C ATOM 2654 C SER B 407 -0.721 23.090 14.760 1.00 65.99 C ANISOU 2654 C SER B 407 6458 10856 7760 284 5 -1476 C ATOM 2655 O SER B 407 -0.213 23.994 15.419 1.00 65.78 O ANISOU 2655 O SER B 407 6435 10822 7735 325 24 -1422 O ATOM 2656 CB SER B 407 0.384 20.851 14.624 1.00 75.31 C ANISOU 2656 CB SER B 407 7785 11927 8903 269 -5 -1551 C ATOM 2657 OG SER B 407 0.908 21.075 15.921 1.00 81.91 O ANISOU 2657 OG SER B 407 8663 12697 9761 282 36 -1512 O ATOM 2658 N ILE B 408 -2.028 22.852 14.750 1.00 67.66 N ANISOU 2658 N ILE B 408 6617 11085 8007 222 3 -1497 N ATOM 2659 CA ILE B 408 -2.951 23.646 15.551 1.00 70.78 C ANISOU 2659 CA ILE B 408 6953 11497 8444 208 39 -1457 C ATOM 2660 C ILE B 408 -3.136 23.032 16.934 1.00 71.69 C ANISOU 2660 C ILE B 408 7122 11522 8593 168 100 -1446 C ATOM 2661 O ILE B 408 -3.410 21.838 17.054 1.00 77.31 O ANISOU 2661 O ILE B 408 7869 12185 9323 104 106 -1485 O ATOM 2662 CB ILE B 408 -4.324 23.770 14.867 1.00 69.36 C ANISOU 2662 CB ILE B 408 6672 11389 8294 165 11 -1478 C ATOM 2663 CG1 ILE B 408 -4.164 24.310 13.443 1.00 61.46 C ANISOU 2663 CG1 ILE B 408 5635 10466 7252 206 -55 -1496 C ATOM 2664 CG2 ILE B 408 -5.249 24.655 15.691 1.00 69.82 C ANISOU 2664 CG2 ILE B 408 6663 11473 8391 168 56 -1432 C ATOM 2665 CD1 ILE B 408 -3.577 25.701 13.380 1.00 57.36 C ANISOU 2665 CD1 ILE B 408 5105 9992 6698 284 -56 -1447 C ATOM 2666 N PRO B 409 -2.976 23.847 17.986 1.00 63.42 N ANISOU 2666 N PRO B 409 6096 10448 7553 206 143 -1393 N ATOM 2667 CA PRO B 409 -3.152 23.368 19.361 1.00 63.62 C ANISOU 2667 CA PRO B 409 6187 10382 7603 179 207 -1377 C ATOM 2668 C PRO B 409 -4.592 22.937 19.629 1.00 62.44 C ANISOU 2668 C PRO B 409 5973 10247 7504 106 249 -1384 C ATOM 2669 O PRO B 409 -5.527 23.618 19.205 1.00 62.32 O ANISOU 2669 O PRO B 409 5853 10317 7511 107 244 -1371 O ATOM 2670 CB PRO B 409 -2.800 24.598 20.207 1.00 63.20 C ANISOU 2670 CB PRO B 409 6164 10313 7536 250 229 -1314 C ATOM 2671 CG PRO B 409 -1.968 25.459 19.312 1.00 59.70 C ANISOU 2671 CG PRO B 409 5698 9929 7056 308 169 -1300 C ATOM 2672 CD PRO B 409 -2.528 25.249 17.941 1.00 60.00 C ANISOU 2672 CD PRO B 409 5647 10057 7093 280 128 -1343 C ATOM 2673 N ARG B 410 -4.761 21.813 20.320 1.00 55.00 N ANISOU 2673 N ARG B 410 5091 9223 6582 44 287 -1402 N ATOM 2674 CA ARG B 410 -6.085 21.318 20.675 1.00 60.78 C ANISOU 2674 CA ARG B 410 5762 9961 7369 -36 335 -1400 C ATOM 2675 C ARG B 410 -6.829 22.384 21.469 1.00 64.13 C ANISOU 2675 C ARG B 410 6133 10418 7815 3 402 -1340 C ATOM 2676 O ARG B 410 -8.057 22.502 21.388 1.00 63.30 O ANISOU 2676 O ARG B 410 5917 10374 7759 -35 430 -1326 O ATOM 2677 CB ARG B 410 -5.979 20.037 21.508 1.00 65.64 C ANISOU 2677 CB ARG B 410 6480 10466 7994 -101 376 -1418 C ATOM 2678 CG ARG B 410 -5.126 18.930 20.895 1.00 73.63 C ANISOU 2678 CG ARG B 410 7577 11428 8972 -125 313 -1478 C ATOM 2679 CD ARG B 410 -3.651 19.297 20.897 1.00 81.69 C ANISOU 2679 CD ARG B 410 8684 12418 9938 -34 284 -1478 C ATOM 2680 NE ARG B 410 -3.272 20.014 22.112 1.00 89.76 N ANISOU 2680 NE ARG B 410 9764 13385 10954 21 338 -1427 N ATOM 2681 CZ ARG B 410 -2.128 20.672 22.267 1.00 93.45 C ANISOU 2681 CZ ARG B 410 10285 13833 11389 103 314 -1405 C ATOM 2682 NH1 ARG B 410 -1.241 20.709 21.282 1.00 90.74 N ANISOU 2682 NH1 ARG B 410 9932 13530 11016 140 250 -1427 N ATOM 2683 NH2 ARG B 410 -1.871 21.297 23.409 1.00 96.23 N ANISOU 2683 NH2 ARG B 410 10702 14124 11736 149 353 -1358 N ATOM 2684 N SER B 411 -6.065 23.159 22.233 1.00 77.72 N ANISOU 2684 N SER B 411 7938 12095 9499 84 424 -1301 N ATOM 2685 CA SER B 411 -6.609 24.212 23.080 1.00 79.74 C ANISOU 2685 CA SER B 411 8180 12362 9756 142 485 -1241 C ATOM 2686 C SER B 411 -7.269 25.308 22.255 1.00 73.18 C ANISOU 2686 C SER B 411 7222 11653 8929 181 452 -1227 C ATOM 2687 O SER B 411 -8.141 26.023 22.747 1.00 71.08 O ANISOU 2687 O SER B 411 6905 11425 8677 214 505 -1185 O ATOM 2688 CB SER B 411 -5.506 24.813 23.954 1.00 87.01 C ANISOU 2688 CB SER B 411 9236 13198 10627 223 487 -1207 C ATOM 2689 OG SER B 411 -4.776 23.800 24.625 1.00 92.20 O ANISOU 2689 OG SER B 411 10016 13739 11276 194 501 -1227 O ATOM 2690 N ASN B 412 -6.847 25.438 21.001 1.00 62.54 N ANISOU 2690 N ASN B 412 5832 10368 7565 184 366 -1262 N ATOM 2691 CA ASN B 412 -7.397 26.463 20.119 1.00 54.14 C ANISOU 2691 CA ASN B 412 4660 9414 6497 222 322 -1255 C ATOM 2692 C ASN B 412 -8.906 26.351 19.947 1.00 51.83 C ANISOU 2692 C ASN B 412 4234 9193 6265 175 349 -1256 C ATOM 2693 O ASN B 412 -9.460 25.249 19.961 1.00 54.68 O ANISOU 2693 O ASN B 412 4563 9536 6676 86 368 -1281 O ATOM 2694 CB ASN B 412 -6.702 26.448 18.755 1.00 50.76 C ANISOU 2694 CB ASN B 412 4219 9030 6037 225 229 -1296 C ATOM 2695 CG ASN B 412 -5.459 27.312 18.729 1.00 48.80 C ANISOU 2695 CG ASN B 412 4046 8765 5730 303 196 -1269 C ATOM 2696 OD1 ASN B 412 -4.915 27.663 19.774 1.00 52.01 O ANISOU 2696 OD1 ASN B 412 4538 9102 6120 342 230 -1228 O ATOM 2697 ND2 ASN B 412 -5.004 27.663 17.533 1.00 44.57 N ANISOU 2697 ND2 ASN B 412 3483 8289 5164 324 127 -1288 N ATOM 2698 N PRO B 413 -9.576 27.502 19.793 1.00 45.95 N ANISOU 2698 N PRO B 413 3412 8530 5518 235 347 -1226 N ATOM 2699 CA PRO B 413 -11.027 27.560 19.600 1.00 51.86 C ANISOU 2699 CA PRO B 413 4016 9360 6330 205 369 -1221 C ATOM 2700 C PRO B 413 -11.451 26.815 18.339 1.00 58.43 C ANISOU 2700 C PRO B 413 4758 10242 7201 125 289 -1278 C ATOM 2701 O PRO B 413 -12.515 26.193 18.315 1.00 50.10 O ANISOU 2701 O PRO B 413 3601 9213 6219 50 307 -1282 O ATOM 2702 CB PRO B 413 -11.297 29.059 19.432 1.00 47.31 C ANISOU 2702 CB PRO B 413 3401 8857 5716 308 350 -1189 C ATOM 2703 CG PRO B 413 -10.135 29.736 20.055 1.00 46.94 C ANISOU 2703 CG PRO B 413 3497 8742 5595 384 354 -1158 C ATOM 2704 CD PRO B 413 -8.968 28.842 19.810 1.00 45.57 C ANISOU 2704 CD PRO B 413 3412 8497 5406 337 319 -1193 C ATOM 2705 N HIS B 414 -10.618 26.875 17.304 1.00 61.02 N ANISOU 2705 N HIS B 414 5126 10577 7480 139 201 -1317 N ATOM 2706 CA HIS B 414 -10.978 26.311 16.010 1.00 55.32 C ANISOU 2706 CA HIS B 414 4339 9900 6780 82 113 -1371 C ATOM 2707 C HIS B 414 -10.130 25.108 15.613 1.00 59.92 C ANISOU 2707 C HIS B 414 5014 10411 7342 27 77 -1418 C ATOM 2708 O HIS B 414 -9.879 24.879 14.428 1.00 61.41 O ANISOU 2708 O HIS B 414 5206 10621 7505 21 -8 -1462 O ATOM 2709 CB HIS B 414 -10.914 27.385 14.926 1.00 50.39 C ANISOU 2709 CB HIS B 414 3679 9354 6112 151 34 -1382 C ATOM 2710 CG HIS B 414 -11.820 28.545 15.181 1.00 49.34 C ANISOU 2710 CG HIS B 414 3456 9297 5995 210 55 -1344 C ATOM 2711 ND1 HIS B 414 -13.178 28.402 15.372 1.00 49.66 N ANISOU 2711 ND1 HIS B 414 3367 9387 6115 171 79 -1333 N ATOM 2712 CD2 HIS B 414 -11.569 29.875 15.272 1.00 47.17 C ANISOU 2712 CD2 HIS B 414 3203 9056 5665 308 52 -1311 C ATOM 2713 CE1 HIS B 414 -13.722 29.587 15.574 1.00 50.94 C ANISOU 2713 CE1 HIS B 414 3474 9613 6267 252 95 -1299 C ATOM 2714 NE2 HIS B 414 -12.765 30.498 15.516 1.00 50.07 N ANISOU 2714 NE2 HIS B 414 3463 9491 6072 336 76 -1286 N ATOM 2715 N PHE B 415 -9.690 24.344 16.607 1.00 60.53 N ANISOU 2715 N PHE B 415 5175 10399 7424 -5 141 -1408 N ATOM 2716 CA PHE B 415 -9.030 23.069 16.351 1.00 59.41 C ANISOU 2716 CA PHE B 415 5122 10185 7268 -61 112 -1453 C ATOM 2717 C PHE B 415 -10.063 22.054 15.876 1.00 61.89 C ANISOU 2717 C PHE B 415 5367 10505 7643 -168 74 -1485 C ATOM 2718 O PHE B 415 -11.152 21.964 16.442 1.00 58.35 O ANISOU 2718 O PHE B 415 4831 10075 7266 -221 121 -1458 O ATOM 2719 CB PHE B 415 -8.325 22.560 17.611 1.00 60.35 C ANISOU 2719 CB PHE B 415 5355 10202 7375 -63 187 -1433 C ATOM 2720 CG PHE B 415 -7.711 21.196 17.455 1.00 62.93 C ANISOU 2720 CG PHE B 415 5779 10448 7685 -119 161 -1480 C ATOM 2721 CD1 PHE B 415 -6.428 21.050 16.952 1.00 65.78 C ANISOU 2721 CD1 PHE B 415 6232 10780 7981 -68 118 -1507 C ATOM 2722 CD2 PHE B 415 -8.418 20.061 17.808 1.00 63.00 C ANISOU 2722 CD2 PHE B 415 5787 10408 7741 -221 179 -1495 C ATOM 2723 CE1 PHE B 415 -5.862 19.794 16.808 1.00 66.63 C ANISOU 2723 CE1 PHE B 415 6436 10814 8066 -106 93 -1552 C ATOM 2724 CE2 PHE B 415 -7.859 18.805 17.667 1.00 65.30 C ANISOU 2724 CE2 PHE B 415 6183 10619 8008 -269 148 -1540 C ATOM 2725 CZ PHE B 415 -6.579 18.671 17.167 1.00 66.87 C ANISOU 2725 CZ PHE B 415 6479 10791 8136 -206 104 -1571 C ATOM 2726 N ASN B 416 -9.728 21.306 14.830 1.00 67.37 N ANISOU 2726 N ASN B 416 6102 11185 8310 -197 -12 -1540 N ATOM 2727 CA ASN B 416 -10.643 20.310 14.282 1.00 74.83 C ANISOU 2727 CA ASN B 416 7000 12125 9309 -302 -72 -1573 C ATOM 2728 C ASN B 416 -11.885 20.966 13.673 1.00 73.93 C ANISOU 2728 C ASN B 416 6729 12106 9254 -316 -117 -1564 C ATOM 2729 O ASN B 416 -12.928 20.323 13.519 1.00 72.31 O ANISOU 2729 O ASN B 416 6444 11906 9123 -413 -150 -1569 O ATOM 2730 CB ASN B 416 -11.052 19.306 15.365 1.00 79.56 C ANISOU 2730 CB ASN B 416 7619 12649 9960 -396 -6 -1557 C ATOM 2731 CG ASN B 416 -11.594 18.015 14.790 1.00 86.01 C ANISOU 2731 CG ASN B 416 8444 13426 10811 -510 -83 -1597 C ATOM 2732 OD1 ASN B 416 -10.841 17.193 14.267 1.00 86.21 O ANISOU 2732 OD1 ASN B 416 8589 13389 10778 -516 -142 -1645 O ATOM 2733 ND2 ASN B 416 -12.906 17.819 14.901 1.00 90.69 N ANISOU 2733 ND2 ASN B 416 8910 14051 11497 -602 -84 -1575 N ATOM 2734 N SER B 417 -11.764 22.245 13.319 1.00 73.46 N ANISOU 2734 N SER B 417 6628 12120 9163 -222 -124 -1548 N ATOM 2735 CA SER B 417 -12.890 23.005 12.778 1.00 79.58 C ANISOU 2735 CA SER B 417 7259 12989 9987 -217 -166 -1540 C ATOM 2736 C SER B 417 -12.867 23.087 11.253 1.00 82.07 C ANISOU 2736 C SER B 417 7577 13339 10267 -200 -293 -1592 C ATOM 2737 O SER B 417 -11.877 23.509 10.655 1.00 80.91 O ANISOU 2737 O SER B 417 7517 13191 10034 -124 -320 -1610 O ATOM 2738 CB SER B 417 -12.924 24.412 13.377 1.00 83.63 C ANISOU 2738 CB SER B 417 7730 13561 10486 -120 -99 -1489 C ATOM 2739 OG SER B 417 -14.039 25.137 12.904 1.00 87.79 O ANISOU 2739 OG SER B 417 8117 14178 11059 -108 -138 -1482 O ATOM 2740 N THR B 418 -13.976 22.694 10.635 1.00 81.20 N ANISOU 2740 N THR B 418 7371 13257 10226 -273 -371 -1612 N ATOM 2741 CA THR B 418 -14.111 22.740 9.184 1.00 80.79 C ANISOU 2741 CA THR B 418 7324 13228 10144 -261 -503 -1662 C ATOM 2742 C THR B 418 -15.084 23.838 8.768 1.00 77.38 C ANISOU 2742 C THR B 418 6754 12893 9752 -222 -542 -1650 C ATOM 2743 O THR B 418 -16.003 23.607 7.982 1.00 75.66 O ANISOU 2743 O THR B 418 6461 12700 9588 -272 -645 -1675 O ATOM 2744 CB THR B 418 -14.601 21.394 8.626 1.00 82.00 C ANISOU 2744 CB THR B 418 7493 13324 10338 -373 -597 -1703 C ATOM 2745 OG1 THR B 418 -15.933 21.137 9.091 1.00 78.09 O ANISOU 2745 OG1 THR B 418 6849 12857 9967 -468 -593 -1674 O ATOM 2746 CG2 THR B 418 -13.679 20.268 9.075 1.00 83.66 C ANISOU 2746 CG2 THR B 418 7846 13434 10505 -408 -560 -1717 C ATOM 2747 N ASN B 419 -14.874 25.035 9.307 1.00 59.95 N ANISOU 2747 N ASN B 419 4524 10737 7517 -131 -468 -1610 N ATOM 2748 CA ASN B 419 -15.737 26.172 9.018 1.00 54.85 C ANISOU 2748 CA ASN B 419 3759 10184 6897 -78 -496 -1596 C ATOM 2749 C ASN B 419 -15.006 27.482 9.280 1.00 51.39 C ANISOU 2749 C ASN B 419 3372 9778 6376 43 -444 -1567 C ATOM 2750 O ASN B 419 -15.423 28.547 8.816 1.00 52.17 O ANISOU 2750 O ASN B 419 3418 9946 6459 111 -484 -1565 O ATOM 2751 CB ASN B 419 -17.014 26.100 9.862 1.00 62.97 C ANISOU 2751 CB ASN B 419 4630 11254 8043 -133 -442 -1553 C ATOM 2752 CG ASN B 419 -18.102 27.029 9.357 1.00 70.69 C ANISOU 2752 CG ASN B 419 5466 12329 9065 -92 -499 -1549 C ATOM 2753 OD1 ASN B 419 -18.100 27.431 8.193 1.00 73.58 O ANISOU 2753 OD1 ASN B 419 5847 12719 9390 -55 -611 -1592 O ATOM 2754 ND2 ASN B 419 -19.045 27.368 10.231 1.00 71.66 N ANISOU 2754 ND2 ASN B 419 5453 12506 9268 -93 -421 -1497 N ATOM 2755 N GLN B 420 -13.907 27.391 10.023 1.00 71.15 N ANISOU 2755 N GLN B 420 5984 12224 8826 67 -362 -1545 N ATOM 2756 CA GLN B 420 -13.121 28.563 10.392 1.00 74.29 C ANISOU 2756 CA GLN B 420 6441 12636 9148 169 -315 -1510 C ATOM 2757 C GLN B 420 -11.629 28.254 10.460 1.00 72.20 C ANISOU 2757 C GLN B 420 6321 12302 8807 189 -291 -1513 C ATOM 2758 O GLN B 420 -11.237 27.108 10.682 1.00 71.54 O ANISOU 2758 O GLN B 420 6292 12152 8737 127 -274 -1530 O ATOM 2759 CB GLN B 420 -13.608 29.130 11.726 1.00 73.77 C ANISOU 2759 CB GLN B 420 6323 12587 9120 196 -213 -1449 C ATOM 2760 CG GLN B 420 -14.829 30.022 11.602 1.00 77.46 C ANISOU 2760 CG GLN B 420 6659 13144 9627 235 -231 -1434 C ATOM 2761 CD GLN B 420 -15.607 30.120 12.894 1.00 81.71 C ANISOU 2761 CD GLN B 420 7120 13695 10229 234 -123 -1379 C ATOM 2762 OE1 GLN B 420 -15.871 31.215 13.393 1.00 82.27 O ANISOU 2762 OE1 GLN B 420 7172 13809 10277 322 -83 -1339 O ATOM 2763 NE2 GLN B 420 -15.975 28.972 13.449 1.00 85.58 N ANISOU 2763 NE2 GLN B 420 7577 14146 10795 138 -74 -1374 N ATOM 2764 N PRO B 421 -10.790 29.284 10.266 1.00 52.05 N ANISOU 2764 N PRO B 421 3832 9767 6178 275 -293 -1493 N ATOM 2765 CA PRO B 421 -9.334 29.102 10.275 1.00 50.86 C ANISOU 2765 CA PRO B 421 3803 9561 5960 300 -274 -1488 C ATOM 2766 C PRO B 421 -8.820 28.697 11.653 1.00 49.82 C ANISOU 2766 C PRO B 421 3720 9360 5848 284 -182 -1451 C ATOM 2767 O PRO B 421 -8.979 29.452 12.612 1.00 49.08 O ANISOU 2767 O PRO B 421 3617 9270 5762 320 -128 -1403 O ATOM 2768 CB PRO B 421 -8.797 30.483 9.884 1.00 50.36 C ANISOU 2768 CB PRO B 421 3769 9540 5825 388 -296 -1460 C ATOM 2769 CG PRO B 421 -9.903 31.436 10.151 1.00 50.15 C ANISOU 2769 CG PRO B 421 3654 9575 5826 419 -299 -1439 C ATOM 2770 CD PRO B 421 -11.188 30.685 10.041 1.00 51.04 C ANISOU 2770 CD PRO B 421 3661 9709 6021 352 -317 -1471 C ATOM 2771 N PRO B 422 -8.212 27.507 11.747 1.00 54.30 N ANISOU 2771 N PRO B 422 4354 9860 6418 235 -170 -1476 N ATOM 2772 CA PRO B 422 -7.688 26.949 12.999 1.00 53.18 C ANISOU 2772 CA PRO B 422 4274 9640 6293 215 -92 -1451 C ATOM 2773 C PRO B 422 -6.564 27.789 13.595 1.00 52.72 C ANISOU 2773 C PRO B 422 4291 9556 6184 287 -59 -1403 C ATOM 2774 O PRO B 422 -6.285 27.675 14.786 1.00 57.44 O ANISOU 2774 O PRO B 422 4936 10093 6797 287 4 -1371 O ATOM 2775 CB PRO B 422 -7.144 25.582 12.571 1.00 53.60 C ANISOU 2775 CB PRO B 422 4394 9635 6337 164 -115 -1499 C ATOM 2776 CG PRO B 422 -7.859 25.261 11.306 1.00 53.94 C ANISOU 2776 CG PRO B 422 4386 9723 6386 133 -198 -1548 C ATOM 2777 CD PRO B 422 -8.057 26.572 10.621 1.00 52.95 C ANISOU 2777 CD PRO B 422 4211 9678 6230 199 -237 -1534 C ATOM 2778 N GLU B 423 -5.923 28.619 12.779 1.00 60.89 N ANISOU 2778 N GLU B 423 5341 10631 7161 346 -104 -1396 N ATOM 2779 CA GLU B 423 -4.827 29.448 13.263 1.00 58.34 C ANISOU 2779 CA GLU B 423 5085 10285 6796 406 -86 -1344 C ATOM 2780 C GLU B 423 -5.336 30.564 14.173 1.00 54.26 C ANISOU 2780 C GLU B 423 4552 9779 6286 447 -58 -1291 C ATOM 2781 O GLU B 423 -4.642 30.984 15.103 1.00 56.27 O ANISOU 2781 O GLU B 423 4874 9979 6525 478 -29 -1244 O ATOM 2782 CB GLU B 423 -4.023 30.034 12.095 1.00 60.29 C ANISOU 2782 CB GLU B 423 5350 10575 6981 452 -140 -1344 C ATOM 2783 CG GLU B 423 -3.270 29.001 11.260 1.00 61.26 C ANISOU 2783 CG GLU B 423 5515 10681 7082 436 -157 -1386 C ATOM 2784 CD GLU B 423 -4.134 28.366 10.182 1.00 60.49 C ANISOU 2784 CD GLU B 423 5377 10619 6989 402 -206 -1449 C ATOM 2785 OE1 GLU B 423 -3.682 27.382 9.557 1.00 57.27 O ANISOU 2785 OE1 GLU B 423 5014 10186 6561 388 -222 -1489 O ATOM 2786 OE2 GLU B 423 -5.263 28.853 9.956 1.00 61.11 O ANISOU 2786 OE2 GLU B 423 5384 10747 7089 393 -235 -1458 O ATOM 2787 N VAL B 424 -6.552 31.032 13.906 1.00 47.21 N ANISOU 2787 N VAL B 424 3575 8952 5413 450 -72 -1299 N ATOM 2788 CA VAL B 424 -7.132 32.144 14.658 1.00 47.91 C ANISOU 2788 CA VAL B 424 3646 9060 5496 504 -49 -1252 C ATOM 2789 C VAL B 424 -7.600 31.746 16.061 1.00 48.04 C ANISOU 2789 C VAL B 424 3674 9022 5558 488 35 -1225 C ATOM 2790 O VAL B 424 -8.461 30.875 16.217 1.00 45.44 O ANISOU 2790 O VAL B 424 3281 8695 5288 428 69 -1250 O ATOM 2791 CB VAL B 424 -8.308 32.783 13.891 1.00 47.05 C ANISOU 2791 CB VAL B 424 3438 9045 5394 523 -92 -1270 C ATOM 2792 CG1 VAL B 424 -8.950 33.884 14.716 1.00 47.06 C ANISOU 2792 CG1 VAL B 424 3427 9066 5386 589 -61 -1221 C ATOM 2793 CG2 VAL B 424 -7.831 33.324 12.556 1.00 44.42 C ANISOU 2793 CG2 VAL B 424 3115 8759 5004 550 -173 -1291 C ATOM 2794 N PHE B 425 -7.029 32.390 17.078 1.00 49.17 N ANISOU 2794 N PHE B 425 3904 9109 5670 540 67 -1172 N ATOM 2795 CA PHE B 425 -7.448 32.170 18.459 1.00 49.66 C ANISOU 2795 CA PHE B 425 3998 9111 5760 543 150 -1140 C ATOM 2796 C PHE B 425 -8.537 33.164 18.851 1.00 47.95 C ANISOU 2796 C PHE B 425 3732 8947 5539 605 176 -1106 C ATOM 2797 O PHE B 425 -9.560 32.788 19.425 1.00 45.82 O ANISOU 2797 O PHE B 425 3403 8688 5317 588 245 -1101 O ATOM 2798 CB PHE B 425 -6.260 32.282 19.419 1.00 46.64 C ANISOU 2798 CB PHE B 425 3753 8624 5344 571 164 -1101 C ATOM 2799 CG PHE B 425 -6.596 31.923 20.841 1.00 46.36 C ANISOU 2799 CG PHE B 425 3776 8511 5329 574 250 -1073 C ATOM 2800 CD1 PHE B 425 -6.464 30.618 21.290 1.00 47.31 C ANISOU 2800 CD1 PHE B 425 3922 8565 5489 506 297 -1098 C ATOM 2801 CD2 PHE B 425 -7.051 32.888 21.728 1.00 47.81 C ANISOU 2801 CD2 PHE B 425 4000 8681 5485 650 285 -1020 C ATOM 2802 CE1 PHE B 425 -6.778 30.284 22.596 1.00 49.44 C ANISOU 2802 CE1 PHE B 425 4255 8757 5773 509 381 -1071 C ATOM 2803 CE2 PHE B 425 -7.366 32.558 23.037 1.00 47.12 C ANISOU 2803 CE2 PHE B 425 3979 8517 5409 661 372 -991 C ATOM 2804 CZ PHE B 425 -7.229 31.255 23.469 1.00 47.42 C ANISOU 2804 CZ PHE B 425 4040 8490 5489 588 422 -1016 C ATOM 2805 N ALA B 426 -8.301 34.436 18.540 1.00 48.50 N ANISOU 2805 N ALA B 426 3829 9049 5549 679 122 -1079 N ATOM 2806 CA ALA B 426 -9.287 35.487 18.761 1.00 44.65 C ANISOU 2806 CA ALA B 426 3303 8619 5043 754 132 -1051 C ATOM 2807 C ALA B 426 -8.998 36.659 17.833 1.00 48.70 C ANISOU 2807 C ALA B 426 3825 9186 5491 809 40 -1048 C ATOM 2808 O ALA B 426 -7.864 36.841 17.394 1.00 45.79 O ANISOU 2808 O ALA B 426 3525 8789 5084 802 -15 -1044 O ATOM 2809 CB ALA B 426 -9.271 35.939 20.211 1.00 49.12 C ANISOU 2809 CB ALA B 426 3970 9112 5583 819 198 -991 C ATOM 2810 N HIS B 427 -10.022 37.450 17.532 1.00 46.41 N ANISOU 2810 N HIS B 427 3466 8977 5192 863 25 -1047 N ATOM 2811 CA HIS B 427 -9.856 38.597 16.645 1.00 46.34 C ANISOU 2811 CA HIS B 427 3472 9019 5116 918 -65 -1046 C ATOM 2812 C HIS B 427 -10.548 39.838 17.196 1.00 46.48 C ANISOU 2812 C HIS B 427 3514 9061 5084 1024 -61 -1004 C ATOM 2813 O HIS B 427 -11.284 39.764 18.181 1.00 47.38 O ANISOU 2813 O HIS B 427 3615 9166 5222 1059 18 -979 O ATOM 2814 CB HIS B 427 -10.386 38.276 15.245 1.00 55.79 C ANISOU 2814 CB HIS B 427 4555 10303 6341 875 -122 -1108 C ATOM 2815 CG HIS B 427 -11.854 38.002 15.198 1.00 63.60 C ANISOU 2815 CG HIS B 427 5407 11362 7395 872 -94 -1131 C ATOM 2816 ND1 HIS B 427 -12.457 37.016 15.959 1.00 69.16 N ANISOU 2816 ND1 HIS B 427 6050 12050 8180 822 -8 -1129 N ATOM 2817 CD2 HIS B 427 -12.852 38.566 14.476 1.00 65.43 C ANISOU 2817 CD2 HIS B 427 5546 11684 7631 909 -142 -1153 C ATOM 2818 CE1 HIS B 427 -13.749 36.995 15.713 1.00 71.44 C ANISOU 2818 CE1 HIS B 427 6204 12417 8523 825 -2 -1145 C ATOM 2819 NE2 HIS B 427 -14.017 37.930 14.811 1.00 71.75 N ANISOU 2819 NE2 HIS B 427 6220 12522 8519 880 -86 -1162 N ATOM 2820 N GLY B 428 -10.305 40.977 16.556 1.00 48.33 N ANISOU 2820 N GLY B 428 3794 9325 5244 1080 -145 -995 N ATOM 2821 CA GLY B 428 -10.929 42.224 16.958 1.00 50.88 C ANISOU 2821 CA GLY B 428 4155 9671 5505 1190 -158 -960 C ATOM 2822 C GLY B 428 -9.965 43.393 16.952 1.00 53.68 C ANISOU 2822 C GLY B 428 4658 9978 5760 1242 -236 -916 C ATOM 2823 O GLY B 428 -10.364 44.543 17.143 1.00 52.84 O ANISOU 2823 O GLY B 428 4607 9886 5584 1337 -269 -888 O ATOM 2824 N LEU B 429 -8.689 43.097 16.733 1.00 56.60 N ANISOU 2824 N LEU B 429 5091 10290 6124 1179 -267 -908 N ATOM 2825 CA LEU B 429 -7.661 44.130 16.724 1.00 57.10 C ANISOU 2825 CA LEU B 429 5288 10302 6105 1209 -345 -858 C ATOM 2826 C LEU B 429 -7.715 44.964 15.447 1.00 58.48 C ANISOU 2826 C LEU B 429 5447 10548 6224 1225 -434 -877 C ATOM 2827 O LEU B 429 -8.296 44.549 14.440 1.00 51.82 O ANISOU 2827 O LEU B 429 4493 9784 5412 1197 -442 -935 O ATOM 2828 CB LEU B 429 -6.273 43.510 16.890 1.00 54.59 C ANISOU 2828 CB LEU B 429 5025 9906 5810 1135 -346 -838 C ATOM 2829 CG LEU B 429 -6.038 42.713 18.175 1.00 53.86 C ANISOU 2829 CG LEU B 429 4976 9724 5763 1118 -271 -818 C ATOM 2830 CD1 LEU B 429 -4.674 42.044 18.148 1.00 53.93 C ANISOU 2830 CD1 LEU B 429 5021 9670 5801 1045 -282 -808 C ATOM 2831 CD2 LEU B 429 -6.176 43.606 19.398 1.00 54.52 C ANISOU 2831 CD2 LEU B 429 5189 9737 5791 1207 -270 -757 C ATOM 2832 N HIS B 430 -7.108 46.145 15.504 1.00 57.56 N ANISOU 2832 N HIS B 430 5453 10396 6023 1270 -508 -826 N ATOM 2833 CA HIS B 430 -7.063 47.046 14.362 1.00 51.77 C ANISOU 2833 CA HIS B 430 4733 9716 5223 1287 -597 -835 C ATOM 2834 C HIS B 430 -5.647 47.561 14.162 1.00 59.30 C ANISOU 2834 C HIS B 430 5791 10610 6130 1250 -661 -780 C ATOM 2835 O HIS B 430 -4.897 47.037 13.341 1.00 67.21 O ANISOU 2835 O HIS B 430 6753 11627 7158 1178 -666 -794 O ATOM 2836 CB HIS B 430 -8.027 48.216 14.560 1.00 48.65 C ANISOU 2836 CB HIS B 430 4380 9350 4754 1397 -635 -825 C ATOM 2837 CG HIS B 430 -9.443 47.795 14.794 1.00 57.76 C ANISOU 2837 CG HIS B 430 5419 10569 5957 1441 -570 -868 C ATOM 2838 ND1 HIS B 430 -10.163 47.058 13.878 1.00 64.18 N ANISOU 2838 ND1 HIS B 430 6084 11468 6836 1400 -556 -937 N ATOM 2839 CD2 HIS B 430 -10.278 48.014 15.838 1.00 62.90 C ANISOU 2839 CD2 HIS B 430 6081 11213 6604 1523 -515 -847 C ATOM 2840 CE1 HIS B 430 -11.376 46.837 14.349 1.00 66.43 C ANISOU 2840 CE1 HIS B 430 6279 11798 7164 1446 -498 -954 C ATOM 2841 NE2 HIS B 430 -11.473 47.407 15.537 1.00 66.64 N ANISOU 2841 NE2 HIS B 430 6398 11774 7149 1525 -465 -899 N ATOM 2842 N ASP B 431 -5.284 48.589 14.922 1.00 60.42 N ANISOU 2842 N ASP B 431 6069 10683 6205 1302 -711 -713 N ATOM 2843 CA ASP B 431 -3.941 49.154 14.854 1.00 63.04 C ANISOU 2843 CA ASP B 431 6502 10950 6498 1262 -780 -648 C ATOM 2844 C ASP B 431 -3.224 48.995 16.192 1.00 68.96 C ANISOU 2844 C ASP B 431 7346 11587 7270 1257 -768 -588 C ATOM 2845 O ASP B 431 -3.056 49.964 16.931 1.00 74.08 O ANISOU 2845 O ASP B 431 8132 12163 7852 1310 -828 -529 O ATOM 2846 CB ASP B 431 -4.000 50.630 14.460 1.00 62.17 C ANISOU 2846 CB ASP B 431 6495 10845 6280 1318 -883 -613 C ATOM 2847 CG ASP B 431 -2.636 51.199 14.119 1.00 66.26 C ANISOU 2847 CG ASP B 431 7095 11314 6767 1259 -959 -546 C ATOM 2848 OD1 ASP B 431 -2.571 52.374 13.700 1.00 69.25 O ANISOU 2848 OD1 ASP B 431 7562 11693 7057 1288 -1048 -514 O ATOM 2849 OD2 ASP B 431 -1.629 50.473 14.266 1.00 65.35 O ANISOU 2849 OD2 ASP B 431 6953 11160 6716 1183 -931 -522 O ATOM 2850 N PRO B 432 -2.796 47.764 16.506 1.00 73.19 N ANISOU 2850 N PRO B 432 7819 12099 7893 1194 -696 -606 N ATOM 2851 CA PRO B 432 -2.154 47.471 17.789 1.00 73.84 C ANISOU 2851 CA PRO B 432 7986 12067 8001 1189 -681 -558 C ATOM 2852 C PRO B 432 -0.681 47.849 17.780 1.00 74.73 C ANISOU 2852 C PRO B 432 8175 12111 8109 1136 -758 -489 C ATOM 2853 O PRO B 432 0.066 47.375 16.924 1.00 75.59 O ANISOU 2853 O PRO B 432 8207 12258 8257 1064 -755 -497 O ATOM 2854 CB PRO B 432 -2.283 45.944 17.907 1.00 72.41 C ANISOU 2854 CB PRO B 432 7697 11901 7916 1135 -579 -614 C ATOM 2855 CG PRO B 432 -3.097 45.494 16.708 1.00 72.02 C ANISOU 2855 CG PRO B 432 7507 11972 7887 1117 -547 -688 C ATOM 2856 CD PRO B 432 -2.927 46.555 15.680 1.00 71.89 C ANISOU 2856 CD PRO B 432 7510 12005 7801 1130 -632 -674 C ATOM 2857 N GLY B 433 -0.267 48.692 18.720 1.00 74.31 N ANISOU 2857 N GLY B 433 8270 11955 8008 1172 -827 -418 N ATOM 2858 CA GLY B 433 1.144 48.982 18.893 1.00 74.66 C ANISOU 2858 CA GLY B 433 8385 11920 8065 1116 -905 -344 C ATOM 2859 C GLY B 433 1.830 47.759 19.470 1.00 71.22 C ANISOU 2859 C GLY B 433 7909 11430 7721 1063 -848 -351 C ATOM 2860 O GLY B 433 1.345 46.639 19.310 1.00 67.34 O ANISOU 2860 O GLY B 433 7312 10989 7285 1047 -749 -419 O ATOM 2861 N ARG B 434 2.959 47.958 20.141 1.00 65.84 N ANISOU 2861 N ARG B 434 7317 10642 7058 1033 -916 -280 N ATOM 2862 CA ARG B 434 3.602 46.849 20.828 1.00 65.87 C ANISOU 2862 CA ARG B 434 7305 10580 7143 995 -871 -286 C ATOM 2863 C ARG B 434 2.733 46.439 22.012 1.00 67.53 C ANISOU 2863 C ARG B 434 7585 10727 7346 1060 -809 -315 C ATOM 2864 O ARG B 434 2.480 47.237 22.913 1.00 64.75 O ANISOU 2864 O ARG B 434 7380 10289 6933 1126 -860 -273 O ATOM 2865 CB ARG B 434 5.008 47.222 21.299 1.00 69.31 C ANISOU 2865 CB ARG B 434 7821 10911 7603 952 -973 -198 C ATOM 2866 CG ARG B 434 5.845 46.014 21.694 1.00 71.98 C ANISOU 2866 CG ARG B 434 8110 11202 8035 902 -932 -209 C ATOM 2867 CD ARG B 434 7.219 46.404 22.210 1.00 75.45 C ANISOU 2867 CD ARG B 434 8623 11535 8508 861 -1042 -119 C ATOM 2868 NE ARG B 434 8.086 45.237 22.344 1.00 78.74 N ANISOU 2868 NE ARG B 434 8968 11932 9019 812 -1004 -132 N ATOM 2869 CZ ARG B 434 7.963 44.320 23.299 1.00 82.77 C ANISOU 2869 CZ ARG B 434 9519 12365 9563 832 -955 -170 C ATOM 2870 NH1 ARG B 434 7.003 44.431 24.208 1.00 81.62 N ANISOU 2870 NH1 ARG B 434 9484 12159 9367 898 -930 -193 N ATOM 2871 NH2 ARG B 434 8.796 43.289 23.344 1.00 83.94 N ANISOU 2871 NH2 ARG B 434 9603 12498 9792 790 -928 -183 N ATOM 2872 N CYS B 435 2.265 45.196 21.999 1.00 60.34 N ANISOU 2872 N CYS B 435 6577 9856 6494 1042 -699 -385 N ATOM 2873 CA CYS B 435 1.387 44.707 23.054 1.00 53.84 C ANISOU 2873 CA CYS B 435 5803 8983 5669 1096 -621 -414 C ATOM 2874 C CYS B 435 2.175 44.136 24.228 1.00 48.77 C ANISOU 2874 C CYS B 435 5261 8204 5065 1085 -628 -387 C ATOM 2875 O CYS B 435 3.042 43.279 24.051 1.00 41.53 O ANISOU 2875 O CYS B 435 4288 7275 4217 1018 -620 -398 O ATOM 2876 CB CYS B 435 0.411 43.665 22.505 1.00 52.95 C ANISOU 2876 CB CYS B 435 5542 8975 5599 1078 -505 -499 C ATOM 2877 SG CYS B 435 -0.729 44.304 21.252 1.00 59.19 S ANISOU 2877 SG CYS B 435 6226 9918 6346 1105 -499 -539 S ATOM 2878 N ALA B 436 1.862 44.626 25.425 1.00 44.24 N ANISOU 2878 N ALA B 436 4845 7524 4442 1159 -643 -351 N ATOM 2879 CA ALA B 436 2.498 44.169 26.654 1.00 42.76 C ANISOU 2879 CA ALA B 436 4782 7187 4276 1163 -656 -325 C ATOM 2880 C ALA B 436 2.108 42.728 26.961 1.00 41.91 C ANISOU 2880 C ALA B 436 4607 7087 4231 1138 -530 -391 C ATOM 2881 O ALA B 436 0.975 42.317 26.716 1.00 40.40 O ANISOU 2881 O ALA B 436 4328 6982 4040 1153 -427 -443 O ATOM 2882 CB ALA B 436 2.114 45.078 27.809 1.00 43.97 C ANISOU 2882 CB ALA B 436 5135 7227 4345 1263 -697 -274 C ATOM 2883 N VAL B 437 3.050 41.963 27.503 1.00 44.96 N ANISOU 2883 N VAL B 437 5032 7378 4670 1097 -545 -387 N ATOM 2884 CA VAL B 437 2.804 40.555 27.795 1.00 49.07 C ANISOU 2884 CA VAL B 437 5503 7894 5248 1066 -437 -449 C ATOM 2885 C VAL B 437 3.105 40.184 29.248 1.00 55.69 C ANISOU 2885 C VAL B 437 6512 8566 6083 1099 -436 -429 C ATOM 2886 O VAL B 437 4.251 40.267 29.696 1.00 57.59 O ANISOU 2886 O VAL B 437 6840 8700 6343 1084 -530 -389 O ATOM 2887 CB VAL B 437 3.622 39.638 26.868 1.00 44.94 C ANISOU 2887 CB VAL B 437 4841 7433 4799 978 -435 -485 C ATOM 2888 CG1 VAL B 437 3.298 38.182 27.150 1.00 40.93 C ANISOU 2888 CG1 VAL B 437 4294 6918 4341 946 -329 -552 C ATOM 2889 CG2 VAL B 437 3.345 39.979 25.420 1.00 39.59 C ANISOU 2889 CG2 VAL B 437 4012 6911 4119 949 -435 -505 C ATOM 2890 N ASP B 438 2.070 39.771 29.974 1.00 53.64 N ANISOU 2890 N ASP B 438 6296 8284 5802 1144 -330 -456 N ATOM 2891 CA ASP B 438 2.235 39.297 31.342 1.00 51.89 C ANISOU 2891 CA ASP B 438 6240 7905 5572 1178 -308 -445 C ATOM 2892 C ASP B 438 2.242 37.773 31.372 1.00 49.08 C ANISOU 2892 C ASP B 438 5813 7553 5283 1114 -215 -510 C ATOM 2893 O ASP B 438 1.223 37.132 31.122 1.00 43.58 O ANISOU 2893 O ASP B 438 5018 6940 4600 1099 -98 -558 O ATOM 2894 CB ASP B 438 1.124 39.845 32.238 1.00 53.58 C ANISOU 2894 CB ASP B 438 6573 8076 5708 1280 -243 -423 C ATOM 2895 CG ASP B 438 1.306 39.461 33.695 1.00 51.98 C ANISOU 2895 CG ASP B 438 6570 7697 5481 1327 -224 -405 C ATOM 2896 OD1 ASP B 438 0.424 39.799 34.512 1.00 53.12 O ANISOU 2896 OD1 ASP B 438 6825 7797 5561 1417 -155 -385 O ATOM 2897 OD2 ASP B 438 2.328 38.823 34.026 1.00 49.54 O ANISOU 2897 OD2 ASP B 438 6313 7293 5218 1281 -275 -410 O ATOM 2898 N ARG B 439 3.400 37.201 31.682 1.00 66.19 N ANISOU 2898 N ARG B 439 8031 9625 7492 1076 -275 -509 N ATOM 2899 CA ARG B 439 3.585 35.755 31.637 1.00 73.44 C ANISOU 2899 CA ARG B 439 8892 10542 8470 1014 -208 -571 C ATOM 2900 C ARG B 439 3.191 35.088 32.952 1.00 76.84 C ANISOU 2900 C ARG B 439 9472 10841 8882 1047 -134 -583 C ATOM 2901 O ARG B 439 2.978 33.876 33.007 1.00 73.83 O ANISOU 2901 O ARG B 439 9054 10462 8537 1002 -51 -638 O ATOM 2902 CB ARG B 439 5.037 35.424 31.287 1.00 76.63 C ANISOU 2902 CB ARG B 439 9271 10916 8930 964 -305 -567 C ATOM 2903 CG ARG B 439 5.612 36.306 30.187 1.00 77.74 C ANISOU 2903 CG ARG B 439 9304 11155 9080 942 -394 -532 C ATOM 2904 CD ARG B 439 6.981 35.826 29.743 1.00 79.76 C ANISOU 2904 CD ARG B 439 9502 11404 9400 890 -464 -529 C ATOM 2905 NE ARG B 439 6.915 34.518 29.100 1.00 82.34 N ANISOU 2905 NE ARG B 439 9709 11805 9771 840 -381 -603 N ATOM 2906 CZ ARG B 439 6.729 34.334 27.797 1.00 83.00 C ANISOU 2906 CZ ARG B 439 9629 12037 9869 802 -347 -635 C ATOM 2907 NH1 ARG B 439 6.591 35.379 26.990 1.00 80.03 N ANISOU 2907 NH1 ARG B 439 9184 11753 9470 806 -384 -600 N ATOM 2908 NH2 ARG B 439 6.682 33.106 27.299 1.00 83.99 N ANISOU 2908 NH2 ARG B 439 9673 12211 10027 762 -280 -703 N ATOM 2909 N HIS B 440 3.098 35.890 34.008 1.00 87.07 N ANISOU 2909 N HIS B 440 10951 12017 10116 1129 -166 -529 N ATOM 2910 CA HIS B 440 2.695 35.396 35.320 1.00 90.73 C ANISOU 2910 CA HIS B 440 11583 12346 10546 1177 -93 -531 C ATOM 2911 C HIS B 440 1.574 36.252 35.893 1.00 91.50 C ANISOU 2911 C HIS B 440 11765 12438 10564 1272 -30 -492 C ATOM 2912 O HIS B 440 1.789 37.012 36.835 1.00 97.50 O ANISOU 2912 O HIS B 440 12723 13064 11258 1355 -89 -439 O ATOM 2913 CB HIS B 440 3.885 35.391 36.281 1.00 94.76 C ANISOU 2913 CB HIS B 440 12285 12667 11052 1199 -205 -501 C ATOM 2914 CG HIS B 440 4.948 34.404 35.919 1.00100.02 C ANISOU 2914 CG HIS B 440 12886 13322 11796 1120 -251 -541 C ATOM 2915 ND1 HIS B 440 5.914 34.664 34.970 1.00103.47 N ANISOU 2915 ND1 HIS B 440 13202 13828 12283 1070 -355 -530 N ATOM 2916 CD2 HIS B 440 5.199 33.155 36.377 1.00103.00 C ANISOU 2916 CD2 HIS B 440 13304 13626 12204 1088 -205 -590 C ATOM 2917 CE1 HIS B 440 6.713 33.619 34.859 1.00105.30 C ANISOU 2917 CE1 HIS B 440 13399 14035 12575 1018 -368 -570 C ATOM 2918 NE2 HIS B 440 6.301 32.688 35.703 1.00105.36 N ANISOU 2918 NE2 HIS B 440 13508 13954 12570 1027 -283 -610 N ATOM 2919 N PRO B 441 0.370 36.133 35.321 1.00 79.51 N ANISOU 2919 N PRO B 441 10098 11063 9049 1264 88 -518 N ATOM 2920 CA PRO B 441 -0.772 36.929 35.778 1.00 81.05 C ANISOU 2920 CA PRO B 441 10347 11277 9173 1361 160 -482 C ATOM 2921 C PRO B 441 -1.116 36.612 37.225 1.00 80.39 C ANISOU 2921 C PRO B 441 10463 11042 9039 1432 243 -462 C ATOM 2922 O PRO B 441 -1.092 35.443 37.621 1.00 79.35 O ANISOU 2922 O PRO B 441 10342 10861 8946 1381 317 -499 O ATOM 2923 CB PRO B 441 -1.910 36.472 34.857 1.00 84.01 C ANISOU 2923 CB PRO B 441 10495 11834 9592 1312 277 -526 C ATOM 2924 CG PRO B 441 -1.236 35.858 33.679 1.00 82.59 C ANISOU 2924 CG PRO B 441 10149 11742 9489 1201 222 -575 C ATOM 2925 CD PRO B 441 0.007 35.232 34.217 1.00 80.17 C ANISOU 2925 CD PRO B 441 9959 11298 9205 1168 154 -581 C ATOM 2926 N THR B 442 -1.427 37.645 38.001 1.00 93.23 N ANISOU 2926 N THR B 442 12258 12591 10574 1552 229 -404 N ATOM 2927 CA THR B 442 -1.801 37.473 39.399 1.00 98.44 C ANISOU 2927 CA THR B 442 13130 13102 11169 1640 311 -377 C ATOM 2928 C THR B 442 -3.025 36.571 39.523 1.00 96.09 C ANISOU 2928 C THR B 442 12727 12884 10899 1621 510 -405 C ATOM 2929 O THR B 442 -3.158 35.817 40.488 1.00 95.25 O ANISOU 2929 O THR B 442 12744 12667 10780 1633 599 -408 O ATOM 2930 CB THR B 442 -2.084 38.826 40.083 1.00103.27 C ANISOU 2930 CB THR B 442 13931 13639 11666 1786 271 -308 C ATOM 2931 OG1 THR B 442 -3.139 39.505 39.390 1.00110.92 O ANISOU 2931 OG1 THR B 442 14754 14774 12617 1826 332 -299 O ATOM 2932 CG2 THR B 442 -0.837 39.698 40.078 1.00 99.83 C ANISOU 2932 CG2 THR B 442 13625 13101 11206 1797 62 -272 C ATOM 2933 N ASP B 443 -3.914 36.651 38.537 1.00 76.91 N ANISOU 2933 N ASP B 443 7482 13633 8107 202 667 -582 N ATOM 2934 CA ASP B 443 -5.097 35.800 38.507 1.00 71.55 C ANISOU 2934 CA ASP B 443 6769 13038 7378 77 731 -530 C ATOM 2935 C ASP B 443 -4.687 34.339 38.359 1.00 67.60 C ANISOU 2935 C ASP B 443 6426 12464 6793 -19 670 -336 C ATOM 2936 O ASP B 443 -4.079 33.949 37.361 1.00 60.13 O ANISOU 2936 O ASP B 443 5557 11346 5942 38 583 -243 O ATOM 2937 CB ASP B 443 -6.029 36.211 37.365 1.00 70.36 C ANISOU 2937 CB ASP B 443 6492 12839 7403 133 740 -582 C ATOM 2938 CG ASP B 443 -7.394 35.545 37.452 1.00 72.30 C ANISOU 2938 CG ASP B 443 6663 13205 7603 4 820 -560 C ATOM 2939 OD1 ASP B 443 -7.474 34.394 37.932 1.00 69.19 O ANISOU 2939 OD1 ASP B 443 6365 12861 7063 -135 832 -441 O ATOM 2940 OD2 ASP B 443 -8.390 36.173 37.035 1.00 73.60 O ANISOU 2940 OD2 ASP B 443 6670 13412 7881 38 866 -660 O ATOM 2941 N ILE B 444 -5.021 33.539 39.365 1.00 88.45 N ANISOU 2941 N ILE B 444 9120 15233 9253 -169 718 -278 N ATOM 2942 CA ILE B 444 -4.654 32.127 39.381 1.00 87.85 C ANISOU 2942 CA ILE B 444 9204 15093 9083 -272 656 -93 C ATOM 2943 C ILE B 444 -5.222 31.365 38.182 1.00 85.32 C ANISOU 2943 C ILE B 444 8895 14664 8857 -295 629 0 C ATOM 2944 O ILE B 444 -4.564 30.484 37.628 1.00 83.44 O ANISOU 2944 O ILE B 444 8791 14276 8635 -294 543 136 O ATOM 2945 CB ILE B 444 -5.094 31.450 40.699 1.00 86.84 C ANISOU 2945 CB ILE B 444 9122 15137 8734 -451 717 -53 C ATOM 2946 CG1 ILE B 444 -4.678 29.977 40.711 1.00 88.24 C ANISOU 2946 CG1 ILE B 444 9478 15230 8819 -556 637 147 C ATOM 2947 CG2 ILE B 444 -6.598 31.597 40.907 1.00 83.87 C ANISOU 2947 CG2 ILE B 444 8604 14935 8330 -546 844 -139 C ATOM 2948 CD1 ILE B 444 -3.178 29.765 40.641 1.00 86.82 C ANISOU 2948 CD1 ILE B 444 9433 14893 8663 -468 514 234 C ATOM 2949 N ASN B 445 -6.439 31.719 37.780 1.00 72.83 N ANISOU 2949 N ASN B 445 7172 13157 7343 -314 701 -77 N ATOM 2950 CA ASN B 445 -7.120 31.030 36.686 1.00 72.60 C ANISOU 2950 CA ASN B 445 7145 13044 7394 -355 677 5 C ATOM 2951 C ASN B 445 -6.680 31.476 35.292 1.00 69.91 C ANISOU 2951 C ASN B 445 6802 12515 7246 -214 601 -1 C ATOM 2952 O ASN B 445 -7.230 31.023 34.289 1.00 68.38 O ANISOU 2952 O ASN B 445 6610 12242 7129 -240 576 56 O ATOM 2953 CB ASN B 445 -8.637 31.178 36.821 1.00 76.63 C ANISOU 2953 CB ASN B 445 7498 13717 7901 -445 778 -65 C ATOM 2954 CG ASN B 445 -9.192 30.434 38.022 1.00 84.48 C ANISOU 2954 CG ASN B 445 8516 14889 8692 -626 855 -25 C ATOM 2955 OD1 ASN B 445 -8.460 29.737 38.726 1.00 88.07 O ANISOU 2955 OD1 ASN B 445 9121 15337 9006 -692 820 70 O ATOM 2956 ND2 ASN B 445 -10.492 30.577 38.260 1.00 85.01 N ANISOU 2956 ND2 ASN B 445 8433 15119 8746 -711 956 -95 N ATOM 2957 N ILE B 446 -5.690 32.362 35.236 1.00 61.37 N ANISOU 2957 N ILE B 446 5721 11363 6233 -74 562 -70 N ATOM 2958 CA ILE B 446 -5.178 32.880 33.969 1.00 53.76 C ANISOU 2958 CA ILE B 446 4760 10226 5441 56 491 -84 C ATOM 2959 C ILE B 446 -3.683 32.605 33.840 1.00 54.21 C ANISOU 2959 C ILE B 446 4959 10142 5497 126 410 -9 C ATOM 2960 O ILE B 446 -2.904 32.948 34.729 1.00 57.38 O ANISOU 2960 O ILE B 446 5382 10588 5832 158 406 -39 O ATOM 2961 CB ILE B 446 -5.421 34.394 33.849 1.00 49.02 C ANISOU 2961 CB ILE B 446 4005 9662 4958 172 516 -252 C ATOM 2962 CG1 ILE B 446 -6.915 34.706 33.974 1.00 48.99 C ANISOU 2962 CG1 ILE B 446 3840 9798 4976 116 597 -335 C ATOM 2963 CG2 ILE B 446 -4.859 34.920 32.535 1.00 42.62 C ANISOU 2963 CG2 ILE B 446 3210 8670 4314 292 435 -256 C ATOM 2964 CD1 ILE B 446 -7.226 36.185 34.049 1.00 48.75 C ANISOU 2964 CD1 ILE B 446 3651 9817 5055 229 627 -511 C ATOM 2965 N ASN B 447 -3.286 31.984 32.732 1.00 59.69 N ANISOU 2965 N ASN B 447 5747 10667 6266 147 347 86 N ATOM 2966 CA ASN B 447 -1.892 31.598 32.532 1.00 60.23 C ANISOU 2966 CA ASN B 447 5945 10594 6344 211 276 161 C ATOM 2967 C ASN B 447 -1.116 32.581 31.660 1.00 53.98 C ANISOU 2967 C ASN B 447 5125 9685 5700 354 234 93 C ATOM 2968 O ASN B 447 0.115 32.527 31.595 1.00 53.28 O ANISOU 2968 O ASN B 447 5111 9502 5630 424 183 126 O ATOM 2969 CB ASN B 447 -1.803 30.187 31.945 1.00 62.12 C ANISOU 2969 CB ASN B 447 6326 10715 6562 142 237 311 C ATOM 2970 CG ASN B 447 -0.463 29.526 32.215 1.00 65.95 C ANISOU 2970 CG ASN B 447 6945 11100 7013 178 176 402 C ATOM 2971 OD1 ASN B 447 0.478 30.168 32.686 1.00 70.22 O ANISOU 2971 OD1 ASN B 447 7471 11647 7564 263 154 357 O ATOM 2972 ND2 ASN B 447 -0.372 28.234 31.920 1.00 63.98 N ANISOU 2972 ND2 ASN B 447 6827 10754 6728 114 143 531 N ATOM 2973 N LEU B 448 -1.839 33.475 30.992 1.00 52.11 N ANISOU 2973 N LEU B 448 4776 9454 5568 393 250 -1 N ATOM 2974 CA LEU B 448 -1.214 34.481 30.140 1.00 48.30 C ANISOU 2974 CA LEU B 448 4265 8865 5222 514 207 -69 C ATOM 2975 C LEU B 448 -2.196 35.590 29.761 1.00 46.83 C ANISOU 2975 C LEU B 448 3935 8727 5134 546 227 -188 C ATOM 2976 O LEU B 448 -3.393 35.351 29.593 1.00 51.05 O ANISOU 2976 O LEU B 448 4407 9319 5672 475 259 -188 O ATOM 2977 CB LEU B 448 -0.639 33.832 28.876 1.00 45.56 C ANISOU 2977 CB LEU B 448 4031 8335 4946 531 155 23 C ATOM 2978 CG LEU B 448 -0.063 34.769 27.811 1.00 35.94 C ANISOU 2978 CG LEU B 448 2796 6996 3865 633 111 -35 C ATOM 2979 CD1 LEU B 448 1.084 35.582 28.383 1.00 40.99 C ANISOU 2979 CD1 LEU B 448 3420 7643 4511 727 92 -94 C ATOM 2980 CD2 LEU B 448 0.393 33.984 26.595 1.00 33.41 C ANISOU 2980 CD2 LEU B 448 2596 6508 3592 625 77 57 C ATOM 2981 N THR B 449 -1.680 36.805 29.618 1.00 43.49 N ANISOU 2981 N THR B 449 3456 8273 4795 653 202 -288 N ATOM 2982 CA THR B 449 -2.513 37.943 29.256 1.00 48.96 C ANISOU 2982 CA THR B 449 4015 8992 5597 699 205 -405 C ATOM 2983 C THR B 449 -1.775 38.919 28.337 1.00 54.47 C ANISOU 2983 C THR B 449 4718 9555 6422 803 136 -451 C ATOM 2984 O THR B 449 -0.676 39.372 28.652 1.00 56.12 O ANISOU 2984 O THR B 449 4963 9736 6623 867 114 -475 O ATOM 2985 CB THR B 449 -3.056 38.662 30.512 1.00 50.05 C ANISOU 2985 CB THR B 449 4034 9301 5681 705 272 -526 C ATOM 2986 OG1 THR B 449 -3.450 39.996 30.174 1.00 45.72 O ANISOU 2986 OG1 THR B 449 3368 8744 5261 792 256 -655 O ATOM 2987 CG2 THR B 449 -1.991 38.717 31.590 1.00 57.17 C ANISOU 2987 CG2 THR B 449 4994 10250 6478 725 279 -533 C ATOM 2988 N ILE B 450 -2.388 39.223 27.196 1.00 54.31 N ANISOU 2988 N ILE B 450 4666 9453 6517 809 98 -457 N ATOM 2989 CA ILE B 450 -1.805 40.132 26.214 1.00 51.71 C ANISOU 2989 CA ILE B 450 4348 8991 6307 888 27 -493 C ATOM 2990 C ILE B 450 -2.549 41.463 26.215 1.00 50.78 C ANISOU 2990 C ILE B 450 4092 8909 6294 949 11 -623 C ATOM 2991 O ILE B 450 -3.698 41.535 25.781 1.00 51.53 O ANISOU 2991 O ILE B 450 4107 9018 6453 920 6 -636 O ATOM 2992 CB ILE B 450 -1.865 39.541 24.787 1.00 49.38 C ANISOU 2992 CB ILE B 450 4140 8554 6069 846 -21 -399 C ATOM 2993 CG1 ILE B 450 -1.294 38.123 24.757 1.00 54.49 C ANISOU 2993 CG1 ILE B 450 4922 9159 6620 783 0 -273 C ATOM 2994 CG2 ILE B 450 -1.128 40.435 23.802 1.00 42.11 C ANISOU 2994 CG2 ILE B 450 3250 7497 5252 913 -91 -428 C ATOM 2995 CD1 ILE B 450 0.190 38.058 25.018 1.00 57.90 C ANISOU 2995 CD1 ILE B 450 5438 9541 7020 839 -8 -253 C ATOM 2996 N LEU B 451 -1.894 42.514 26.701 1.00 48.61 N ANISOU 2996 N LEU B 451 3786 8643 6041 1033 -2 -718 N ATOM 2997 CA LEU B 451 -2.502 43.842 26.735 1.00 52.55 C ANISOU 2997 CA LEU B 451 4161 9159 6645 1103 -24 -850 C ATOM 2998 C LEU B 451 -2.019 44.685 25.561 1.00 54.93 C ANISOU 2998 C LEU B 451 4496 9303 7073 1159 -122 -860 C ATOM 2999 O LEU B 451 -0.828 44.971 25.440 1.00 58.38 O ANISOU 2999 O LEU B 451 5010 9670 7500 1195 -155 -850 O ATOM 3000 CB LEU B 451 -2.183 44.548 28.054 1.00 54.35 C ANISOU 3000 CB LEU B 451 4336 9497 6816 1155 21 -962 C ATOM 3001 CG LEU B 451 -3.085 45.717 28.465 1.00 55.04 C ANISOU 3001 CG LEU B 451 4277 9651 6986 1217 36 -1115 C ATOM 3002 CD1 LEU B 451 -2.773 46.158 29.887 1.00 57.35 C ANISOU 3002 CD1 LEU B 451 4540 10068 7183 1244 101 -1216 C ATOM 3003 CD2 LEU B 451 -2.971 46.894 27.506 1.00 51.48 C ANISOU 3003 CD2 LEU B 451 3805 9063 6693 1298 -63 -1171 C ATOM 3004 N CYS B 452 -2.950 45.093 24.705 1.00 59.93 N ANISOU 3004 N CYS B 452 5066 9882 7822 1159 -172 -877 N ATOM 3005 CA CYS B 452 -2.608 45.878 23.526 1.00 56.04 C ANISOU 3005 CA CYS B 452 4611 9236 7445 1194 -275 -877 C ATOM 3006 C CYS B 452 -3.211 47.279 23.570 1.00 54.64 C ANISOU 3006 C CYS B 452 4314 9052 7396 1275 -326 -1006 C ATOM 3007 O CYS B 452 -4.384 47.453 23.901 1.00 54.66 O ANISOU 3007 O CYS B 452 4190 9133 7446 1283 -303 -1065 O ATOM 3008 CB CYS B 452 -3.060 45.154 22.257 1.00 58.44 C ANISOU 3008 CB CYS B 452 4975 9445 7784 1116 -319 -768 C ATOM 3009 SG CYS B 452 -2.394 43.484 22.076 1.00 75.01 S ANISOU 3009 SG CYS B 452 7225 11526 9749 1025 -265 -621 S ATOM 3010 N SER B 453 -2.397 48.275 23.232 1.00 58.06 N ANISOU 3010 N SER B 453 4786 9388 7887 1334 -398 -1049 N ATOM 3011 CA SER B 453 -2.855 49.657 23.159 1.00 66.62 C ANISOU 3011 CA SER B 453 5778 10433 9102 1414 -467 -1166 C ATOM 3012 C SER B 453 -3.260 50.003 21.730 1.00 74.55 C ANISOU 3012 C SER B 453 6803 11291 10231 1395 -583 -1118 C ATOM 3013 O SER B 453 -2.450 50.503 20.948 1.00 74.32 O ANISOU 3013 O SER B 453 6867 11137 10236 1397 -664 -1092 O ATOM 3014 CB SER B 453 -1.759 50.609 23.639 1.00 69.76 C ANISOU 3014 CB SER B 453 6211 10805 9490 1482 -489 -1241 C ATOM 3015 OG SER B 453 -0.567 50.436 22.891 1.00 71.08 O ANISOU 3015 OG SER B 453 6513 10867 9629 1451 -534 -1155 O ATOM 3016 N ASP B 454 -4.517 49.731 21.393 1.00 96.08 N ANISOU 3016 N ASP B 454 9445 14038 13023 1366 -595 -1104 N ATOM 3017 CA ASP B 454 -5.013 49.950 20.038 1.00102.66 C ANISOU 3017 CA ASP B 454 10299 14738 13968 1332 -713 -1046 C ATOM 3018 C ASP B 454 -5.553 51.366 19.859 1.00107.37 C ANISOU 3018 C ASP B 454 10797 15270 14729 1418 -816 -1150 C ATOM 3019 O ASP B 454 -6.363 51.837 20.657 1.00110.98 O ANISOU 3019 O ASP B 454 11106 15816 15246 1487 -782 -1258 O ATOM 3020 CB ASP B 454 -6.094 48.922 19.696 1.00103.79 C ANISOU 3020 CB ASP B 454 10404 14927 14106 1248 -690 -966 C ATOM 3021 CG ASP B 454 -6.355 48.825 18.206 1.00102.13 C ANISOU 3021 CG ASP B 454 10268 14572 13965 1178 -807 -868 C ATOM 3022 OD1 ASP B 454 -5.910 49.723 17.461 1.00 99.01 O ANISOU 3022 OD1 ASP B 454 9927 14047 13647 1202 -915 -878 O ATOM 3023 OD2 ASP B 454 -7.005 47.847 17.779 1.00102.73 O ANISOU 3023 OD2 ASP B 454 10357 14665 14013 1088 -795 -779 O ATOM 3024 N SER B 455 -5.103 52.038 18.803 1.00 95.62 N ANISOU 3024 N SER B 455 9394 13624 13313 1412 -941 -1119 N ATOM 3025 CA SER B 455 -5.516 53.411 18.532 1.00 99.36 C ANISOU 3025 CA SER B 455 9797 14008 13947 1491 -1062 -1206 C ATOM 3026 C SER B 455 -6.585 53.488 17.443 1.00103.54 C ANISOU 3026 C SER B 455 10288 14449 14605 1452 -1181 -1150 C ATOM 3027 O SER B 455 -6.967 54.579 17.014 1.00105.35 O ANISOU 3027 O SER B 455 10471 14577 14981 1506 -1309 -1200 O ATOM 3028 CB SER B 455 -4.308 54.270 18.147 1.00 97.33 C ANISOU 3028 CB SER B 455 9659 13631 13691 1509 -1138 -1216 C ATOM 3029 OG SER B 455 -3.677 53.773 16.979 1.00 94.36 O ANISOU 3029 OG SER B 455 9435 13150 13267 1407 -1188 -1088 O ATOM 3030 N ASN B 456 -7.064 52.328 17.004 1.00101.68 N ANISOU 3030 N ASN B 456 10074 14246 14314 1355 -1148 -1044 N ATOM 3031 CA ASN B 456 -8.102 52.260 15.978 1.00103.75 C ANISOU 3031 CA ASN B 456 10303 14433 14683 1299 -1261 -977 C ATOM 3032 C ASN B 456 -7.787 53.125 14.763 1.00102.61 C ANISOU 3032 C ASN B 456 10256 14101 14629 1280 -1433 -938 C ATOM 3033 O ASN B 456 -8.522 54.062 14.451 1.00102.63 O ANISOU 3033 O ASN B 456 10169 14032 14792 1332 -1558 -983 O ATOM 3034 CB ASN B 456 -9.465 52.651 16.559 1.00106.83 C ANISOU 3034 CB ASN B 456 10478 14906 15206 1374 -1262 -1067 C ATOM 3035 CG ASN B 456 -9.967 51.662 17.595 1.00106.37 C ANISOU 3035 CG ASN B 456 10325 15037 15054 1358 -1098 -1084 C ATOM 3036 OD1 ASN B 456 -9.203 50.853 18.121 1.00108.06 O ANISOU 3036 OD1 ASN B 456 10628 15325 15106 1319 -981 -1052 O ATOM 3037 ND2 ASN B 456 -11.259 51.725 17.895 1.00103.50 N ANISOU 3037 ND2 ASN B 456 9778 14753 14794 1387 -1093 -1133 N ATOM 3038 N ARG B 460 -10.284 58.059 18.833 1.00134.30 N ANISOU 3038 N ARG B 460 13510 18284 19233 1938 -1437 -1685 N ATOM 3039 CA ARG B 460 -10.997 56.850 19.229 1.00134.51 C ANISOU 3039 CA ARG B 460 13449 18473 19183 1877 -1306 -1645 C ATOM 3040 C ARG B 460 -10.027 55.727 19.589 1.00134.02 C ANISOU 3040 C ARG B 460 13526 18503 18892 1782 -1172 -1564 C ATOM 3041 O ARG B 460 -10.060 54.653 18.988 1.00134.81 O ANISOU 3041 O ARG B 460 13699 18612 18910 1667 -1161 -1428 O ATOM 3042 CB ARG B 460 -11.938 56.404 18.119 1.00132.96 C ANISOU 3042 CB ARG B 460 13219 18218 19083 1802 -1415 -1529 C ATOM 3043 N SER B 461 -9.168 55.980 20.572 1.00153.28 N ANISOU 3043 N SER B 461 16003 21005 21230 1830 -1076 -1648 N ATOM 3044 CA SER B 461 -8.175 54.995 20.990 1.00147.02 C ANISOU 3044 CA SER B 461 15338 20293 20231 1753 -960 -1578 C ATOM 3045 C SER B 461 -8.553 54.334 22.313 1.00140.69 C ANISOU 3045 C SER B 461 14438 19694 19323 1757 -783 -1642 C ATOM 3046 O SER B 461 -8.763 55.012 23.319 1.00144.87 O ANISOU 3046 O SER B 461 14867 20300 19879 1847 -722 -1789 O ATOM 3047 CB SER B 461 -6.791 55.640 21.103 1.00146.70 C ANISOU 3047 CB SER B 461 15431 20177 20132 1780 -988 -1601 C ATOM 3048 OG SER B 461 -6.769 56.635 22.112 1.00147.31 O ANISOU 3048 OG SER B 461 15428 20295 20249 1891 -957 -1763 O ATOM 3049 N SER B 462 -8.638 53.008 22.304 1.00100.23 N ANISOU 3049 N SER B 462 9352 14654 14076 1653 -703 -1532 N ATOM 3050 CA SER B 462 -8.933 52.256 23.517 1.00 89.13 C ANISOU 3050 CA SER B 462 7878 13440 12547 1631 -538 -1570 C ATOM 3051 C SER B 462 -7.757 51.366 23.901 1.00 73.74 C ANISOU 3051 C SER B 462 6085 11532 10402 1561 -462 -1487 C ATOM 3052 O SER B 462 -6.599 51.766 23.781 1.00 72.65 O ANISOU 3052 O SER B 462 6064 11310 10228 1583 -503 -1480 O ATOM 3053 CB SER B 462 -10.200 51.416 23.345 1.00 91.32 C ANISOU 3053 CB SER B 462 8045 13802 12850 1564 -502 -1518 C ATOM 3054 OG SER B 462 -10.002 50.371 22.409 1.00 91.29 O ANISOU 3054 OG SER B 462 8165 13739 12784 1448 -540 -1350 O ATOM 3055 N ALA B 463 -8.063 50.158 24.361 1.00 46.92 N ANISOU 3055 N ALA B 463 2685 8259 6884 1477 -357 -1422 N ATOM 3056 CA ALA B 463 -7.038 49.209 24.773 1.00 42.46 C ANISOU 3056 CA ALA B 463 2259 7735 6139 1411 -287 -1337 C ATOM 3057 C ALA B 463 -7.672 47.872 25.111 1.00 46.02 C ANISOU 3057 C ALA B 463 2693 8308 6486 1309 -193 -1258 C ATOM 3058 O ALA B 463 -8.384 47.749 26.107 1.00 52.21 O ANISOU 3058 O ALA B 463 3363 9244 7229 1306 -93 -1331 O ATOM 3059 CB ALA B 463 -6.268 49.743 25.968 1.00 41.69 C ANISOU 3059 CB ALA B 463 2170 7711 5961 1471 -222 -1441 C ATOM 3060 N ARG B 464 -7.419 46.869 24.279 1.00 53.70 N ANISOU 3060 N ARG B 464 3782 9211 7410 1219 -223 -1110 N ATOM 3061 CA ARG B 464 -7.979 45.544 24.509 1.00 56.34 C ANISOU 3061 CA ARG B 464 4122 9642 7642 1112 -147 -1020 C ATOM 3062 C ARG B 464 -6.923 44.554 24.980 1.00 52.68 C ANISOU 3062 C ARG B 464 3806 9202 7009 1057 -88 -934 C ATOM 3063 O ARG B 464 -5.744 44.685 24.657 1.00 52.39 O ANISOU 3063 O ARG B 464 3890 9065 6951 1084 -129 -902 O ATOM 3064 CB ARG B 464 -8.690 45.028 23.258 1.00 59.06 C ANISOU 3064 CB ARG B 464 4481 9901 8060 1038 -222 -916 C ATOM 3065 CG ARG B 464 -8.039 45.442 21.953 1.00 62.52 C ANISOU 3065 CG ARG B 464 5031 10148 8575 1052 -347 -861 C ATOM 3066 CD ARG B 464 -9.026 45.306 20.808 1.00 69.42 C ANISOU 3066 CD ARG B 464 5873 10948 9554 995 -436 -798 C ATOM 3067 NE ARG B 464 -10.290 45.971 21.114 1.00 74.11 N ANISOU 3067 NE ARG B 464 6268 11618 10272 1040 -444 -891 N ATOM 3068 CZ ARG B 464 -10.576 47.222 20.771 1.00 75.58 C ANISOU 3068 CZ ARG B 464 6367 11733 10616 1131 -536 -977 C ATOM 3069 NH1 ARG B 464 -9.691 47.947 20.101 1.00 76.00 N ANISOU 3069 NH1 ARG B 464 6524 11639 10712 1174 -630 -976 N ATOM 3070 NH2 ARG B 464 -11.750 47.748 21.095 1.00 74.57 N ANISOU 3070 NH2 ARG B 464 6046 11680 10608 1178 -535 -1065 N ATOM 3071 N ILE B 465 -7.360 43.566 25.752 1.00 46.32 N ANISOU 3071 N ILE B 465 2986 8528 6087 978 7 -897 N ATOM 3072 CA ILE B 465 -6.456 42.578 26.324 1.00 48.32 C ANISOU 3072 CA ILE B 465 3369 8811 6178 924 59 -815 C ATOM 3073 C ILE B 465 -6.974 41.166 26.062 1.00 50.98 C ANISOU 3073 C ILE B 465 3762 9169 6439 800 86 -685 C ATOM 3074 O ILE B 465 -8.182 40.938 26.032 1.00 52.02 O ANISOU 3074 O ILE B 465 3791 9375 6600 746 109 -688 O ATOM 3075 CB ILE B 465 -6.236 42.831 27.841 1.00 68.07 C ANISOU 3075 CB ILE B 465 5825 11463 8577 949 150 -906 C ATOM 3076 CG1 ILE B 465 -5.482 41.674 28.497 1.00 69.16 C ANISOU 3076 CG1 ILE B 465 6089 11644 8545 875 198 -806 C ATOM 3077 CG2 ILE B 465 -7.562 43.058 28.547 1.00 68.40 C ANISOU 3077 CG2 ILE B 465 5697 11660 8633 932 228 -1001 C ATOM 3078 CD1 ILE B 465 -6.382 40.603 29.074 1.00 71.22 C ANISOU 3078 CD1 ILE B 465 6323 12035 8701 759 277 -752 C ATOM 3079 N LEU B 466 -6.056 40.225 25.860 1.00 55.58 N ANISOU 3079 N LEU B 466 4504 9683 6931 756 79 -571 N ATOM 3080 CA LEU B 466 -6.429 38.842 25.577 1.00 60.03 C ANISOU 3080 CA LEU B 466 5147 10244 7419 638 96 -443 C ATOM 3081 C LEU B 466 -6.201 37.929 26.777 1.00 59.83 C ANISOU 3081 C LEU B 466 5168 10336 7231 575 176 -401 C ATOM 3082 O LEU B 466 -5.080 37.801 27.266 1.00 54.50 O ANISOU 3082 O LEU B 466 4582 9642 6485 608 181 -385 O ATOM 3083 CB LEU B 466 -5.656 38.310 24.368 1.00 59.22 C ANISOU 3083 CB LEU B 466 5203 9964 7336 623 28 -338 C ATOM 3084 CG LEU B 466 -5.924 36.848 24.002 1.00 56.86 C ANISOU 3084 CG LEU B 466 5011 9635 6958 504 38 -203 C ATOM 3085 CD1 LEU B 466 -7.391 36.640 23.643 1.00 56.12 C ANISOU 3085 CD1 LEU B 466 4824 9593 6906 422 34 -189 C ATOM 3086 CD2 LEU B 466 -5.020 36.393 22.865 1.00 51.37 C ANISOU 3086 CD2 LEU B 466 4477 8760 6279 503 -17 -120 C ATOM 3087 N GLN B 467 -7.271 37.290 27.240 1.00 61.02 N ANISOU 3087 N GLN B 467 5256 10607 7323 478 233 -379 N ATOM 3088 CA GLN B 467 -7.187 36.356 28.357 1.00 63.86 C ANISOU 3088 CA GLN B 467 5664 11081 7518 394 304 -329 C ATOM 3089 C GLN B 467 -7.026 34.921 27.871 1.00 61.03 C ANISOU 3089 C GLN B 467 5459 10643 7087 292 282 -171 C ATOM 3090 O GLN B 467 -7.792 34.452 27.028 1.00 64.32 O ANISOU 3090 O GLN B 467 5876 11015 7548 225 257 -112 O ATOM 3091 CB GLN B 467 -8.434 36.456 29.239 1.00 71.09 C ANISOU 3091 CB GLN B 467 6427 12188 8395 333 391 -398 C ATOM 3092 CG GLN B 467 -8.610 37.792 29.941 1.00 76.51 C ANISOU 3092 CG GLN B 467 6965 12971 9133 430 433 -566 C ATOM 3093 CD GLN B 467 -7.623 37.999 31.074 1.00 79.31 C ANISOU 3093 CD GLN B 467 7377 13383 9375 463 469 -607 C ATOM 3094 OE1 GLN B 467 -6.540 37.411 31.089 1.00 79.80 O ANISOU 3094 OE1 GLN B 467 7589 13366 9365 457 433 -516 O ATOM 3095 NE2 GLN B 467 -7.993 38.842 32.031 1.00 78.91 N ANISOU 3095 NE2 GLN B 467 7204 13468 9310 499 540 -747 N ATOM 3096 N ILE B 468 -6.031 34.226 28.412 1.00 54.07 N ANISOU 3096 N ILE B 468 4708 9740 6097 280 286 -102 N ATOM 3097 CA ILE B 468 -5.828 32.815 28.107 1.00 54.97 C ANISOU 3097 CA ILE B 468 4975 9778 6134 187 268 44 C ATOM 3098 C ILE B 468 -5.959 31.971 29.374 1.00 62.29 C ANISOU 3098 C ILE B 468 5935 10834 6898 88 323 94 C ATOM 3099 O ILE B 468 -4.974 31.733 30.076 1.00 68.78 O ANISOU 3099 O ILE B 468 6840 11651 7641 111 318 121 O ATOM 3100 CB ILE B 468 -4.453 32.576 27.463 1.00 52.48 C ANISOU 3100 CB ILE B 468 4805 9288 5847 258 208 101 C ATOM 3101 CG1 ILE B 468 -4.221 33.586 26.340 1.00 59.73 C ANISOU 3101 CG1 ILE B 468 5687 10094 6914 354 158 36 C ATOM 3102 CG2 ILE B 468 -4.347 31.154 26.938 1.00 48.67 C ANISOU 3102 CG2 ILE B 468 4478 8702 5312 170 185 241 C ATOM 3103 CD1 ILE B 468 -2.898 33.417 25.629 1.00 65.03 C ANISOU 3103 CD1 ILE B 468 6489 10600 7619 420 111 81 C ATOM 3104 N ILE B 469 -7.181 31.523 29.658 1.00 52.16 N ANISOU 3104 N ILE B 469 4587 9668 5565 -29 370 111 N ATOM 3105 CA ILE B 469 -7.482 30.772 30.877 1.00 50.00 C ANISOU 3105 CA ILE B 469 4333 9537 5127 -146 429 154 C ATOM 3106 C ILE B 469 -6.664 29.488 31.004 1.00 60.58 C ANISOU 3106 C ILE B 469 5870 10783 6364 -204 387 300 C ATOM 3107 O ILE B 469 -6.561 28.705 30.057 1.00 60.18 O ANISOU 3107 O ILE B 469 5930 10590 6347 -232 335 397 O ATOM 3108 CB ILE B 469 -8.985 30.419 30.975 1.00 47.53 C ANISOU 3108 CB ILE B 469 3917 9354 4786 -277 484 159 C ATOM 3109 CG1 ILE B 469 -9.793 31.609 31.499 1.00 45.24 C ANISOU 3109 CG1 ILE B 469 3417 9226 4547 -236 557 1 C ATOM 3110 CG2 ILE B 469 -9.193 29.226 31.888 1.00 46.61 C ANISOU 3110 CG2 ILE B 469 3889 9329 4491 -433 520 261 C ATOM 3111 CD1 ILE B 469 -9.873 32.777 30.549 1.00 43.64 C ANISOU 3111 CD1 ILE B 469 3110 8940 4531 -102 515 -96 C ATOM 3112 N LYS B 470 -6.091 29.283 32.187 1.00 75.87 N ANISOU 3112 N LYS B 470 7855 12798 8177 -225 406 312 N ATOM 3113 CA LYS B 470 -5.311 28.087 32.486 1.00 77.84 C ANISOU 3113 CA LYS B 470 8284 12967 8326 -279 359 450 C ATOM 3114 C LYS B 470 -6.145 26.811 32.376 1.00 73.87 C ANISOU 3114 C LYS B 470 7856 12470 7741 -441 362 569 C ATOM 3115 O LYS B 470 -7.233 26.715 32.948 1.00 69.21 O ANISOU 3115 O LYS B 470 7183 12040 7074 -559 426 553 O ATOM 3116 CB LYS B 470 -4.706 28.196 33.888 1.00 87.44 C ANISOU 3116 CB LYS B 470 9518 14290 9414 -288 376 436 C ATOM 3117 CG LYS B 470 -4.473 26.860 34.583 1.00 96.25 C ANISOU 3117 CG LYS B 470 10787 15403 10379 -413 347 580 C ATOM 3118 CD LYS B 470 -4.185 27.054 36.068 1.00100.98 C ANISOU 3118 CD LYS B 470 11384 16151 10833 -457 373 557 C ATOM 3119 CE LYS B 470 -4.213 25.732 36.823 1.00104.79 C ANISOU 3119 CE LYS B 470 12010 16655 11151 -613 347 702 C ATOM 3120 NZ LYS B 470 -3.226 24.759 36.279 1.00105.34 N ANISOU 3120 NZ LYS B 470 12250 16519 11257 -575 242 837 N ATOM 3121 N GLY B 471 -5.627 25.838 31.632 1.00 74.93 N ANISOU 3121 N GLY B 471 8147 12429 7893 -449 294 686 N ATOM 3122 CA GLY B 471 -6.261 24.538 31.508 1.00 76.10 C ANISOU 3122 CA GLY B 471 8400 12554 7961 -602 281 812 C ATOM 3123 C GLY B 471 -7.606 24.542 30.806 1.00 77.90 C ANISOU 3123 C GLY B 471 8538 12827 8233 -688 311 799 C ATOM 3124 O GLY B 471 -8.415 23.636 31.008 1.00 80.25 O ANISOU 3124 O GLY B 471 8875 13177 8438 -845 323 883 O ATOM 3125 N LYS B 472 -7.850 25.552 29.977 1.00 81.71 N ANISOU 3125 N LYS B 472 8902 13288 8857 -591 316 700 N ATOM 3126 CA LYS B 472 -9.110 25.644 29.244 1.00 82.80 C ANISOU 3126 CA LYS B 472 8942 13461 9057 -662 330 686 C ATOM 3127 C LYS B 472 -8.974 25.221 27.785 1.00 84.70 C ANISOU 3127 C LYS B 472 9288 13502 9391 -649 260 748 C ATOM 3128 O LYS B 472 -8.094 25.697 27.066 1.00 83.46 O ANISOU 3128 O LYS B 472 9172 13208 9331 -520 221 716 O ATOM 3129 CB LYS B 472 -9.682 27.062 29.315 1.00 78.22 C ANISOU 3129 CB LYS B 472 8146 13001 8574 -581 377 534 C ATOM 3130 CG LYS B 472 -10.954 27.255 28.498 1.00 70.53 C ANISOU 3130 CG LYS B 472 7054 12055 7690 -638 377 516 C ATOM 3131 CD LYS B 472 -11.440 28.694 28.549 1.00 64.80 C ANISOU 3131 CD LYS B 472 6115 11426 7079 -538 412 362 C ATOM 3132 CE LYS B 472 -12.742 28.869 27.781 1.00 57.55 C ANISOU 3132 CE LYS B 472 5067 10540 6260 -595 402 350 C ATOM 3133 NZ LYS B 472 -13.865 28.111 28.400 1.00 57.22 N ANISOU 3133 NZ LYS B 472 4966 10656 6117 -766 462 398 N ATOM 3134 N ASP B 473 -9.854 24.324 27.353 1.00 71.61 N ANISOU 3134 N ASP B 473 7678 11833 7699 -791 247 837 N ATOM 3135 CA ASP B 473 -9.912 23.928 25.953 1.00 70.51 C ANISOU 3135 CA ASP B 473 7634 11518 7640 -802 185 891 C ATOM 3136 C ASP B 473 -10.984 24.741 25.244 1.00 66.12 C ANISOU 3136 C ASP B 473 6914 11016 7194 -810 184 823 C ATOM 3137 O ASP B 473 -12.147 24.341 25.190 1.00 60.44 O ANISOU 3137 O ASP B 473 6137 10378 6449 -944 192 862 O ATOM 3138 CB ASP B 473 -10.207 22.434 25.820 1.00 75.29 C ANISOU 3138 CB ASP B 473 8407 12056 8144 -958 157 1034 C ATOM 3139 CG ASP B 473 -10.279 21.977 24.371 1.00 74.77 C ANISOU 3139 CG ASP B 473 8457 11805 8149 -981 94 1088 C ATOM 3140 OD1 ASP B 473 -9.870 22.744 23.471 1.00 72.55 O ANISOU 3140 OD1 ASP B 473 8154 11428 7985 -868 70 1024 O ATOM 3141 OD2 ASP B 473 -10.745 20.844 24.131 1.00 78.68 O ANISOU 3141 OD2 ASP B 473 9073 12249 8574 -1122 69 1196 O ATOM 3142 N TYR B 474 -10.583 25.889 24.710 1.00 76.78 N ANISOU 3142 N TYR B 474 8186 12318 8669 -667 167 725 N ATOM 3143 CA TYR B 474 -11.499 26.765 23.994 1.00 74.13 C ANISOU 3143 CA TYR B 474 7696 12014 8457 -655 148 658 C ATOM 3144 C TYR B 474 -12.192 26.040 22.845 1.00 69.97 C ANISOU 3144 C TYR B 474 7247 11386 7954 -771 88 750 C ATOM 3145 O TYR B 474 -11.547 25.356 22.042 1.00 70.41 O ANISOU 3145 O TYR B 474 7489 11265 7998 -780 41 823 O ATOM 3146 CB TYR B 474 -10.760 27.996 23.467 1.00 68.92 C ANISOU 3146 CB TYR B 474 6990 11274 7923 -487 119 558 C ATOM 3147 CG TYR B 474 -10.267 28.923 24.553 1.00 63.58 C ANISOU 3147 CG TYR B 474 6205 10712 7242 -375 173 449 C ATOM 3148 CD1 TYR B 474 -10.912 30.123 24.811 1.00 61.00 C ANISOU 3148 CD1 TYR B 474 5675 10500 7002 -314 197 329 C ATOM 3149 CD2 TYR B 474 -9.160 28.596 25.324 1.00 66.79 C ANISOU 3149 CD2 TYR B 474 6714 11105 7559 -331 196 467 C ATOM 3150 CE1 TYR B 474 -10.468 30.975 25.804 1.00 64.38 C ANISOU 3150 CE1 TYR B 474 6014 11028 7421 -216 247 223 C ATOM 3151 CE2 TYR B 474 -8.707 29.443 26.320 1.00 69.12 C ANISOU 3151 CE2 TYR B 474 6918 11503 7841 -239 240 370 C ATOM 3152 CZ TYR B 474 -9.366 30.632 26.555 1.00 66.91 C ANISOU 3152 CZ TYR B 474 6446 11338 7641 -184 269 245 C ATOM 3153 OH TYR B 474 -8.924 31.481 27.543 1.00 64.36 O ANISOU 3153 OH TYR B 474 6042 11112 7301 -97 313 142 O ATOM 3154 N GLU B 475 -13.510 26.188 22.781 1.00 60.64 N ANISOU 3154 N GLU B 475 5919 10318 6805 -861 92 742 N ATOM 3155 CA GLU B 475 -14.293 25.620 21.694 1.00 65.57 C ANISOU 3155 CA GLU B 475 6592 10861 7459 -979 26 824 C ATOM 3156 C GLU B 475 -14.912 26.737 20.861 1.00 63.85 C ANISOU 3156 C GLU B 475 6222 10638 7402 -923 -26 751 C ATOM 3157 O GLU B 475 -15.702 26.488 19.949 1.00 64.76 O ANISOU 3157 O GLU B 475 6338 10704 7563 -1017 -91 806 O ATOM 3158 CB GLU B 475 -15.367 24.673 22.235 1.00 69.64 C ANISOU 3158 CB GLU B 475 7080 11504 7876 -1161 56 903 C ATOM 3159 CG GLU B 475 -14.813 23.440 22.944 1.00 78.23 C ANISOU 3159 CG GLU B 475 8348 12573 8802 -1241 86 998 C ATOM 3160 CD GLU B 475 -13.985 22.546 22.031 1.00 90.15 C ANISOU 3160 CD GLU B 475 10112 13853 10287 -1251 21 1091 C ATOM 3161 OE1 GLU B 475 -12.889 22.970 21.596 1.00 94.42 O ANISOU 3161 OE1 GLU B 475 10729 14263 10883 -1112 3 1050 O ATOM 3162 OE2 GLU B 475 -14.425 21.409 21.761 1.00 94.47 O ANISOU 3162 OE2 GLU B 475 10784 14352 10758 -1402 -7 1202 O ATOM 3163 N SER B 476 -14.539 27.971 21.192 1.00 54.76 N ANISOU 3163 N SER B 476 4942 9530 6334 -771 -6 630 N ATOM 3164 CA SER B 476 -14.930 29.148 20.424 1.00 46.39 C ANISOU 3164 CA SER B 476 3749 8440 5435 -691 -67 553 C ATOM 3165 C SER B 476 -14.062 30.330 20.845 1.00 46.33 C ANISOU 3165 C SER B 476 3680 8438 5487 -514 -44 432 C ATOM 3166 O SER B 476 -13.665 30.429 22.006 1.00 45.24 O ANISOU 3166 O SER B 476 3505 8407 5279 -467 37 382 O ATOM 3167 CB SER B 476 -16.411 29.474 20.629 1.00 42.18 C ANISOU 3167 CB SER B 476 2993 8065 4970 -757 -61 523 C ATOM 3168 OG SER B 476 -16.625 30.128 21.866 1.00 43.79 O ANISOU 3168 OG SER B 476 3017 8450 5171 -692 32 415 O ATOM 3169 N GLU B 477 -13.762 31.218 19.902 1.00 55.46 N ANISOU 3169 N GLU B 477 4832 9474 6765 -424 -119 389 N ATOM 3170 CA GLU B 477 -12.885 32.353 20.175 1.00 53.06 C ANISOU 3170 CA GLU B 477 4486 9153 6521 -262 -111 281 C ATOM 3171 C GLU B 477 -13.373 33.191 21.355 1.00 47.33 C ANISOU 3171 C GLU B 477 3548 8612 5823 -194 -41 162 C ATOM 3172 O GLU B 477 -14.571 33.430 21.505 1.00 41.18 O ANISOU 3172 O GLU B 477 2598 7945 5104 -235 -34 132 O ATOM 3173 CB GLU B 477 -12.738 33.244 18.940 1.00 54.71 C ANISOU 3173 CB GLU B 477 4702 9219 6866 -199 -214 255 C ATOM 3174 CG GLU B 477 -12.235 32.538 17.700 1.00 58.75 C ANISOU 3174 CG GLU B 477 5426 9545 7352 -265 -279 356 C ATOM 3175 CD GLU B 477 -12.005 33.500 16.553 1.00 63.55 C ANISOU 3175 CD GLU B 477 6046 10018 8081 -207 -376 325 C ATOM 3176 OE1 GLU B 477 -12.145 33.085 15.384 1.00 67.99 O ANISOU 3176 OE1 GLU B 477 6729 10454 8652 -292 -449 402 O ATOM 3177 OE2 GLU B 477 -11.692 34.677 16.825 1.00 62.48 O ANISOU 3177 OE2 GLU B 477 5809 9903 8028 -83 -383 224 O ATOM 3178 N PRO B 478 -12.432 33.638 22.198 1.00 43.86 N ANISOU 3178 N PRO B 478 3119 8205 5342 -91 14 91 N ATOM 3179 CA PRO B 478 -12.708 34.519 23.335 1.00 41.25 C ANISOU 3179 CA PRO B 478 2609 8034 5029 -15 85 -37 C ATOM 3180 C PRO B 478 -12.865 35.956 22.867 1.00 40.45 C ANISOU 3180 C PRO B 478 2378 7893 5096 109 27 -149 C ATOM 3181 O PRO B 478 -12.335 36.310 21.815 1.00 47.63 O ANISOU 3181 O PRO B 478 3374 8642 6081 153 -62 -127 O ATOM 3182 CB PRO B 478 -11.438 34.403 24.189 1.00 41.81 C ANISOU 3182 CB PRO B 478 2787 8109 4990 43 138 -51 C ATOM 3183 CG PRO B 478 -10.624 33.298 23.576 1.00 41.25 C ANISOU 3183 CG PRO B 478 2937 7895 4841 -14 102 79 C ATOM 3184 CD PRO B 478 -11.018 33.242 22.148 1.00 41.80 C ANISOU 3184 CD PRO B 478 3048 7829 5005 -50 13 133 C ATOM 3185 N SER B 479 -13.574 36.775 23.634 1.00 41.47 N ANISOU 3185 N SER B 479 2308 8165 5285 162 78 -268 N ATOM 3186 CA SER B 479 -13.720 38.182 23.285 1.00 40.38 C ANISOU 3186 CA SER B 479 2044 7985 5312 290 21 -383 C ATOM 3187 C SER B 479 -12.605 39.011 23.903 1.00 40.86 C ANISOU 3187 C SER B 479 2136 8032 5358 418 46 -478 C ATOM 3188 O SER B 479 -12.323 38.899 25.096 1.00 44.76 O ANISOU 3188 O SER B 479 2615 8648 5743 425 144 -527 O ATOM 3189 CB SER B 479 -15.077 38.722 23.735 1.00 47.10 C ANISOU 3189 CB SER B 479 2652 8984 6259 297 58 -477 C ATOM 3190 OG SER B 479 -15.168 40.116 23.491 1.00 47.29 O ANISOU 3190 OG SER B 479 2556 8962 6449 434 1 -596 O ATOM 3191 N LEU B 480 -11.965 39.835 23.083 1.00 47.17 N ANISOU 3191 N LEU B 480 2985 8681 6257 507 -48 -501 N ATOM 3192 CA LEU B 480 -10.957 40.758 23.579 1.00 51.27 C ANISOU 3192 CA LEU B 480 3522 9178 6781 629 -39 -596 C ATOM 3193 C LEU B 480 -11.604 41.697 24.584 1.00 58.82 C ANISOU 3193 C LEU B 480 4283 10276 7791 706 25 -750 C ATOM 3194 O LEU B 480 -12.623 42.325 24.291 1.00 62.79 O ANISOU 3194 O LEU B 480 4628 10797 8431 735 -9 -811 O ATOM 3195 CB LEU B 480 -10.348 41.563 22.430 1.00 52.00 C ANISOU 3195 CB LEU B 480 3681 9087 6988 699 -159 -596 C ATOM 3196 CG LEU B 480 -9.531 40.789 21.395 1.00 53.52 C ANISOU 3196 CG LEU B 480 4077 9127 7131 637 -215 -465 C ATOM 3197 CD1 LEU B 480 -9.165 41.691 20.233 1.00 50.68 C ANISOU 3197 CD1 LEU B 480 3759 8603 6893 690 -333 -475 C ATOM 3198 CD2 LEU B 480 -8.283 40.194 22.027 1.00 54.95 C ANISOU 3198 CD2 LEU B 480 4394 9313 7171 642 -150 -433 C ATOM 3199 N LEU B 481 -11.019 41.783 25.773 1.00 56.85 N ANISOU 3199 N LEU B 481 4042 10126 7434 738 115 -814 N ATOM 3200 CA LEU B 481 -11.552 42.649 26.814 1.00 55.84 C ANISOU 3200 CA LEU B 481 3745 10137 7336 807 192 -971 C ATOM 3201 C LEU B 481 -11.218 44.103 26.508 1.00 50.84 C ANISOU 3201 C LEU B 481 3062 9407 6848 950 118 -1087 C ATOM 3202 O LEU B 481 -10.047 44.473 26.413 1.00 40.54 O ANISOU 3202 O LEU B 481 1876 8007 5520 1005 77 -1086 O ATOM 3203 CB LEU B 481 -11.005 42.242 28.181 1.00 57.08 C ANISOU 3203 CB LEU B 481 3947 10427 7314 778 307 -997 C ATOM 3204 CG LEU B 481 -11.250 40.780 28.562 1.00 59.14 C ANISOU 3204 CG LEU B 481 4276 10779 7417 630 373 -876 C ATOM 3205 CD1 LEU B 481 -10.780 40.506 29.982 1.00 62.08 C ANISOU 3205 CD1 LEU B 481 4682 11289 7616 600 479 -911 C ATOM 3206 CD2 LEU B 481 -12.721 40.424 28.405 1.00 60.17 C ANISOU 3206 CD2 LEU B 481 4260 11004 7597 550 405 -869 C ATOM 3207 N GLU B 482 -12.252 44.922 26.343 1.00 58.08 N ANISOU 3207 N GLU B 482 3802 10346 7921 1008 97 -1184 N ATOM 3208 CA GLU B 482 -12.065 46.318 25.975 1.00 67.25 C ANISOU 3208 CA GLU B 482 4912 11401 9239 1141 10 -1290 C ATOM 3209 C GLU B 482 -12.246 47.260 27.160 1.00 67.46 C ANISOU 3209 C GLU B 482 4808 11542 9281 1238 97 -1473 C ATOM 3210 O GLU B 482 -13.272 47.233 27.840 1.00 67.48 O ANISOU 3210 O GLU B 482 4649 11694 9297 1228 191 -1553 O ATOM 3211 CB GLU B 482 -13.026 46.708 24.851 1.00 79.47 C ANISOU 3211 CB GLU B 482 6361 12859 10977 1155 -103 -1273 C ATOM 3212 CG GLU B 482 -12.911 48.162 24.421 1.00 89.30 C ANISOU 3212 CG GLU B 482 7553 13981 12396 1290 -210 -1376 C ATOM 3213 CD GLU B 482 -14.027 48.586 23.488 1.00 93.64 C ANISOU 3213 CD GLU B 482 7974 14463 13143 1307 -320 -1372 C ATOM 3214 OE1 GLU B 482 -14.167 49.803 23.242 1.00 95.62 O ANISOU 3214 OE1 GLU B 482 8148 14627 13555 1421 -407 -1469 O ATOM 3215 OE2 GLU B 482 -14.768 47.705 23.004 1.00 93.34 O ANISOU 3215 OE2 GLU B 482 7912 14453 13100 1204 -329 -1269 O ATOM 3216 N PHE B 483 -11.241 48.095 27.398 1.00 57.25 N ANISOU 3216 N PHE B 483 3588 10180 7984 1326 69 -1542 N ATOM 3217 CA PHE B 483 -11.313 49.103 28.448 1.00 63.07 C ANISOU 3217 CA PHE B 483 4223 11000 8741 1424 138 -1723 C ATOM 3218 C PHE B 483 -10.433 50.298 28.100 1.00 64.53 C ANISOU 3218 C PHE B 483 4472 11033 9014 1537 34 -1786 C ATOM 3219 O PHE B 483 -9.476 50.171 27.341 1.00 67.84 O ANISOU 3219 O PHE B 483 5044 11317 9414 1520 -57 -1682 O ATOM 3220 CB PHE B 483 -10.935 48.509 29.811 1.00 67.92 C ANISOU 3220 CB PHE B 483 4876 11780 9148 1366 283 -1748 C ATOM 3221 CG PHE B 483 -9.531 47.974 29.882 1.00 67.43 C ANISOU 3221 CG PHE B 483 5018 11663 8938 1323 263 -1644 C ATOM 3222 CD1 PHE B 483 -9.144 46.890 29.112 1.00 65.46 C ANISOU 3222 CD1 PHE B 483 4898 11343 8632 1233 216 -1467 C ATOM 3223 CD2 PHE B 483 -8.603 48.544 30.737 1.00 69.28 C ANISOU 3223 CD2 PHE B 483 5313 11918 9092 1373 291 -1725 C ATOM 3224 CE1 PHE B 483 -7.853 46.395 29.182 1.00 65.04 C ANISOU 3224 CE1 PHE B 483 5018 11238 8457 1204 199 -1377 C ATOM 3225 CE2 PHE B 483 -7.311 48.052 30.812 1.00 67.87 C ANISOU 3225 CE2 PHE B 483 5308 11692 8789 1337 267 -1627 C ATOM 3226 CZ PHE B 483 -6.936 46.976 30.033 1.00 64.77 C ANISOU 3226 CZ PHE B 483 5030 11227 8353 1257 222 -1454 C ATOM 3227 N LYS B 484 -10.766 51.460 28.651 1.00 77.06 N ANISOU 3227 N LYS B 484 5941 12640 10696 1648 50 -1959 N ATOM 3228 CA LYS B 484 -10.071 52.696 28.311 1.00 83.26 C ANISOU 3228 CA LYS B 484 6775 13277 11584 1756 -58 -2030 C ATOM 3229 C LYS B 484 -9.306 53.263 29.506 1.00 89.00 C ANISOU 3229 C LYS B 484 7540 14068 12205 1804 19 -2152 C ATOM 3230 O LYS B 484 -9.831 54.089 30.253 1.00 93.52 O ANISOU 3230 O LYS B 484 7993 14704 12836 1886 76 -2322 O ATOM 3231 CB LYS B 484 -11.070 53.725 27.774 1.00 87.42 C ANISOU 3231 CB LYS B 484 7145 13728 12343 1858 -140 -2129 C ATOM 3232 CG LYS B 484 -11.842 53.246 26.550 1.00 89.80 C ANISOU 3232 CG LYS B 484 7408 13955 12757 1807 -236 -2006 C ATOM 3233 CD LYS B 484 -13.181 53.959 26.410 1.00 92.77 C ANISOU 3233 CD LYS B 484 7569 14337 13341 1891 -265 -2114 C ATOM 3234 CE LYS B 484 -13.005 55.464 26.290 1.00 95.63 C ANISOU 3234 CE LYS B 484 7902 14567 13866 2035 -366 -2246 C ATOM 3235 NZ LYS B 484 -12.201 55.837 25.094 1.00 95.61 N ANISOU 3235 NZ LYS B 484 8055 14354 13917 2031 -544 -2140 N ATOM 3236 N PRO B 485 -8.054 52.815 29.687 1.00 85.80 N ANISOU 3236 N PRO B 485 7305 13647 11649 1752 18 -2066 N ATOM 3237 CA PRO B 485 -7.201 53.221 30.808 1.00 89.97 C ANISOU 3237 CA PRO B 485 7893 14237 12055 1776 79 -2155 C ATOM 3238 C PRO B 485 -6.434 54.499 30.500 1.00 96.75 C ANISOU 3238 C PRO B 485 8805 14947 13008 1873 -32 -2227 C ATOM 3239 O PRO B 485 -6.611 55.514 31.176 1.00 99.91 O ANISOU 3239 O PRO B 485 9140 15368 13455 1958 -8 -2393 O ATOM 3240 CB PRO B 485 -6.202 52.060 30.927 1.00 84.62 C ANISOU 3240 CB PRO B 485 7372 13586 11195 1670 101 -2000 C ATOM 3241 CG PRO B 485 -6.566 51.069 29.834 1.00 80.04 C ANISOU 3241 CG PRO B 485 6814 12950 10645 1596 57 -1838 C ATOM 3242 CD PRO B 485 -7.389 51.812 28.845 1.00 80.23 C ANISOU 3242 CD PRO B 485 6741 12867 10875 1661 -37 -1875 C ATOM 3243 N PHE B 486 -5.584 54.432 29.481 1.00100.73 N ANISOU 3243 N PHE B 486 9433 15302 13537 1854 -149 -2104 N ATOM 3244 CA PHE B 486 -4.708 55.537 29.109 1.00101.45 C ANISOU 3244 CA PHE B 486 9600 15249 13699 1922 -262 -2144 C ATOM 3245 C PHE B 486 -5.440 56.875 29.080 1.00108.44 C ANISOU 3245 C PHE B 486 10370 16071 14760 2038 -314 -2304 C ATOM 3246 O PHE B 486 -6.491 57.005 28.453 1.00109.73 O ANISOU 3246 O PHE B 486 10427 16198 15070 2067 -354 -2314 O ATOM 3247 CB PHE B 486 -4.057 55.252 27.756 1.00 92.86 C ANISOU 3247 CB PHE B 486 8627 14007 12650 1878 -382 -1988 C ATOM 3248 CG PHE B 486 -3.525 53.852 27.627 1.00 87.41 C ANISOU 3248 CG PHE B 486 8032 13363 11815 1771 -333 -1829 C ATOM 3249 CD1 PHE B 486 -2.415 53.449 28.352 1.00 85.10 C ANISOU 3249 CD1 PHE B 486 7838 13127 11368 1736 -284 -1797 C ATOM 3250 CD2 PHE B 486 -4.138 52.938 26.789 1.00 84.69 C ANISOU 3250 CD2 PHE B 486 7682 13002 11494 1705 -342 -1712 C ATOM 3251 CE1 PHE B 486 -1.925 52.161 28.239 1.00 80.83 C ANISOU 3251 CE1 PHE B 486 7384 12619 10709 1647 -245 -1653 C ATOM 3252 CE2 PHE B 486 -3.651 51.649 26.671 1.00 82.75 C ANISOU 3252 CE2 PHE B 486 7532 12788 11120 1611 -299 -1571 C ATOM 3253 CZ PHE B 486 -2.544 51.261 27.398 1.00 80.49 C ANISOU 3253 CZ PHE B 486 7340 12552 10691 1587 -250 -1543 C ATOM 3254 N SER B 487 -4.872 57.861 29.768 1.00129.36 N ANISOU 3254 N SER B 487 13046 18705 17400 2104 -320 -2429 N ATOM 3255 CA SER B 487 -5.471 59.188 29.866 1.00132.35 C ANISOU 3255 CA SER B 487 13329 19017 17941 2224 -366 -2598 C ATOM 3256 C SER B 487 -5.934 59.706 28.508 1.00133.31 C ANISOU 3256 C SER B 487 13424 18964 18265 2265 -522 -2553 C ATOM 3257 O SER B 487 -7.134 59.763 28.233 1.00134.42 O ANISOU 3257 O SER B 487 13423 19112 18538 2304 -524 -2591 O ATOM 3258 CB SER B 487 -4.484 60.173 30.498 1.00131.48 C ANISOU 3258 CB SER B 487 13305 18863 17787 2271 -393 -2699 C ATOM 3259 OG SER B 487 -4.065 59.723 31.775 1.00131.25 O ANISOU 3259 OG SER B 487 13306 18995 17567 2226 -259 -2740 O ATOM 3260 N ASN B 488 -4.978 60.080 27.662 1.00115.37 N ANISOU 3260 N ASN B 488 11284 16537 16014 2248 -654 -2468 N ATOM 3261 CA ASN B 488 -5.293 60.600 26.336 1.00115.25 C ANISOU 3261 CA ASN B 488 11272 16344 16174 2269 -817 -2413 C ATOM 3262 C ASN B 488 -4.051 60.716 25.453 1.00112.79 C ANISOU 3262 C ASN B 488 11134 15894 15827 2210 -933 -2291 C ATOM 3263 O ASN B 488 -3.030 61.264 25.870 1.00109.39 O ANISOU 3263 O ASN B 488 10793 15438 15332 2221 -946 -2330 O ATOM 3264 CB ASN B 488 -5.991 61.958 26.450 1.00116.34 C ANISOU 3264 CB ASN B 488 11307 16398 16499 2399 -888 -2578 C ATOM 3265 CG ASN B 488 -6.824 62.292 25.228 1.00113.65 C ANISOU 3265 CG ASN B 488 10908 15915 16357 2424 -1035 -2529 C ATOM 3266 OD1 ASN B 488 -7.026 61.451 24.351 1.00112.42 O ANISOU 3266 OD1 ASN B 488 10776 15745 16195 2339 -1067 -2380 O ATOM 3267 ND2 ASN B 488 -7.316 63.524 25.167 1.00111.90 N ANISOU 3267 ND2 ASN B 488 10616 15583 16317 2539 -1131 -2656 N ATOM 3268 N GLY B 489 -4.146 60.195 24.232 1.00126.67 N ANISOU 3268 N GLY B 489 12937 17567 17623 2141 -1013 -2145 N ATOM 3269 CA GLY B 489 -3.046 60.265 23.286 1.00123.47 C ANISOU 3269 CA GLY B 489 12691 17032 17188 2075 -1116 -2028 C ATOM 3270 C GLY B 489 -2.639 58.906 22.747 1.00119.00 C ANISOU 3270 C GLY B 489 12207 16505 16501 1958 -1066 -1861 C ATOM 3271 O GLY B 489 -2.939 57.881 23.359 1.00118.58 O ANISOU 3271 O GLY B 489 12111 16596 16349 1927 -939 -1839 O ATOM 3272 N PRO B 490 -1.959 58.892 21.589 1.00107.87 N ANISOU 3272 N PRO B 490 10922 14966 15098 1890 -1166 -1747 N ATOM 3273 CA PRO B 490 -1.464 57.665 20.954 1.00101.84 C ANISOU 3273 CA PRO B 490 10253 14215 14226 1781 -1126 -1593 C ATOM 3274 C PRO B 490 -0.270 57.080 21.702 1.00 97.80 C ANISOU 3274 C PRO B 490 9815 13793 13550 1752 -1023 -1569 C ATOM 3275 O PRO B 490 0.511 57.829 22.291 1.00 99.92 O ANISOU 3275 O PRO B 490 10110 14058 13796 1793 -1032 -1641 O ATOM 3276 CB PRO B 490 -1.023 58.139 19.562 1.00 99.25 C ANISOU 3276 CB PRO B 490 10035 13710 13963 1727 -1271 -1511 C ATOM 3277 CG PRO B 490 -1.656 59.482 19.375 1.00101.95 C ANISOU 3277 CG PRO B 490 10317 13948 14472 1806 -1400 -1606 C ATOM 3278 CD PRO B 490 -1.731 60.074 20.743 1.00106.02 C ANISOU 3278 CD PRO B 490 10741 14555 14985 1910 -1330 -1759 C ATOM 3279 N LEU B 491 -0.132 55.758 21.675 1.00 86.13 N ANISOU 3279 N LEU B 491 8372 12390 11965 1681 -934 -1466 N ATOM 3280 CA LEU B 491 0.958 55.087 22.375 1.00 77.14 C ANISOU 3280 CA LEU B 491 7297 11334 10678 1655 -842 -1431 C ATOM 3281 C LEU B 491 1.730 54.135 21.469 1.00 61.97 C ANISOU 3281 C LEU B 491 5493 9360 8692 1566 -838 -1287 C ATOM 3282 O LEU B 491 1.139 53.365 20.711 1.00 58.43 O ANISOU 3282 O LEU B 491 5058 8887 8254 1509 -837 -1204 O ATOM 3283 CB LEU B 491 0.432 54.321 23.593 1.00 81.12 C ANISOU 3283 CB LEU B 491 7723 12008 11092 1664 -712 -1465 C ATOM 3284 CG LEU B 491 0.156 55.110 24.874 1.00 85.88 C ANISOU 3284 CG LEU B 491 8235 12702 11693 1744 -670 -1617 C ATOM 3285 CD1 LEU B 491 -1.044 56.025 24.710 1.00 86.45 C ANISOU 3285 CD1 LEU B 491 8194 12736 11916 1813 -723 -1722 C ATOM 3286 CD2 LEU B 491 -0.061 54.159 26.035 1.00 89.03 C ANISOU 3286 CD2 LEU B 491 8595 13272 11959 1720 -534 -1620 C ATOM 3287 N VAL B 492 3.054 54.189 21.560 1.00 45.47 N ANISOU 3287 N VAL B 492 3486 7254 6537 1552 -834 -1262 N ATOM 3288 CA VAL B 492 3.916 53.273 20.822 1.00 38.90 C ANISOU 3288 CA VAL B 492 2759 6381 5640 1478 -812 -1140 C ATOM 3289 C VAL B 492 3.629 51.827 21.214 1.00 43.68 C ANISOU 3289 C VAL B 492 3361 7084 6153 1443 -706 -1069 C ATOM 3290 O VAL B 492 3.342 50.983 20.363 1.00 42.94 O ANISOU 3290 O VAL B 492 3314 6948 6054 1380 -698 -979 O ATOM 3291 CB VAL B 492 5.408 53.575 21.077 1.00 33.09 C ANISOU 3291 CB VAL B 492 2086 5636 4851 1481 -814 -1137 C ATOM 3292 CG1 VAL B 492 6.289 52.453 20.535 1.00 28.28 C ANISOU 3292 CG1 VAL B 492 1564 5012 4170 1417 -762 -1021 C ATOM 3293 CG2 VAL B 492 5.789 54.913 20.467 1.00 31.11 C ANISOU 3293 CG2 VAL B 492 1864 5270 4685 1490 -927 -1183 C ATOM 3294 N GLY B 493 3.708 51.550 22.510 1.00 72.77 N ANISOU 3294 N GLY B 493 6995 10895 9757 1475 -629 -1111 N ATOM 3295 CA GLY B 493 3.463 50.215 23.021 1.00 79.07 C ANISOU 3295 CA GLY B 493 7793 11790 10459 1438 -533 -1046 C ATOM 3296 C GLY B 493 3.771 50.108 24.501 1.00 81.45 C ANISOU 3296 C GLY B 493 8058 12225 10665 1469 -465 -1096 C ATOM 3297 O GLY B 493 4.028 51.110 25.170 1.00 80.97 O ANISOU 3297 O GLY B 493 7961 12188 10616 1522 -486 -1195 O ATOM 3298 N GLY B 494 3.746 48.884 25.016 1.00 53.09 N ANISOU 3298 N GLY B 494 4484 8716 6973 1428 -387 -1027 N ATOM 3299 CA GLY B 494 4.002 48.655 26.423 1.00 50.96 C ANISOU 3299 CA GLY B 494 4191 8575 6596 1438 -325 -1059 C ATOM 3300 C GLY B 494 4.716 47.348 26.687 1.00 50.84 C ANISOU 3300 C GLY B 494 4250 8590 6476 1391 -279 -944 C ATOM 3301 O GLY B 494 5.101 46.639 25.758 1.00 51.87 O ANISOU 3301 O GLY B 494 4451 8634 6622 1359 -289 -847 O ATOM 3302 N PHE B 495 4.891 47.034 27.965 1.00 53.08 N ANISOU 3302 N PHE B 495 4522 8993 6654 1385 -230 -958 N ATOM 3303 CA PHE B 495 5.552 45.802 28.373 1.00 47.13 C ANISOU 3303 CA PHE B 495 3836 8271 5800 1343 -196 -850 C ATOM 3304 C PHE B 495 5.387 45.594 29.871 1.00 53.25 C ANISOU 3304 C PHE B 495 4586 9193 6454 1325 -145 -882 C ATOM 3305 O PHE B 495 5.061 46.527 30.604 1.00 53.97 O ANISOU 3305 O PHE B 495 4615 9354 6536 1353 -137 -998 O ATOM 3306 CB PHE B 495 7.039 45.846 28.017 1.00 39.09 C ANISOU 3306 CB PHE B 495 2883 7171 4797 1366 -243 -798 C ATOM 3307 CG PHE B 495 7.781 46.990 28.652 1.00 37.52 C ANISOU 3307 CG PHE B 495 2661 6995 4601 1412 -284 -884 C ATOM 3308 CD1 PHE B 495 7.956 48.183 27.971 1.00 36.31 C ANISOU 3308 CD1 PHE B 495 2491 6760 4547 1451 -343 -953 C ATOM 3309 CD2 PHE B 495 8.304 46.873 29.930 1.00 38.71 C ANISOU 3309 CD2 PHE B 495 2815 7245 4650 1408 -271 -891 C ATOM 3310 CE1 PHE B 495 8.639 49.239 28.554 1.00 36.77 C ANISOU 3310 CE1 PHE B 495 2535 6833 4604 1487 -385 -1031 C ATOM 3311 CE2 PHE B 495 8.986 47.926 30.517 1.00 37.22 C ANISOU 3311 CE2 PHE B 495 2610 7075 4457 1442 -313 -970 C ATOM 3312 CZ PHE B 495 9.154 49.108 29.827 1.00 35.54 C ANISOU 3312 CZ PHE B 495 2380 6778 4345 1483 -368 -1041 C ATOM 3313 N VAL B 496 5.606 44.362 30.317 1.00 64.87 N ANISOU 3313 N VAL B 496 6112 10708 7829 1272 -113 -781 N ATOM 3314 CA VAL B 496 5.598 44.051 31.738 1.00 66.38 C ANISOU 3314 CA VAL B 496 6302 11034 7887 1237 -73 -791 C ATOM 3315 C VAL B 496 7.034 43.917 32.223 1.00 67.33 C ANISOU 3315 C VAL B 496 6482 11139 7960 1251 -119 -738 C ATOM 3316 O VAL B 496 7.865 43.297 31.558 1.00 66.66 O ANISOU 3316 O VAL B 496 6456 10961 7911 1259 -152 -640 O ATOM 3317 CB VAL B 496 4.838 42.746 32.025 1.00 66.30 C ANISOU 3317 CB VAL B 496 6315 11087 7790 1156 -16 -706 C ATOM 3318 CG1 VAL B 496 5.002 42.346 33.481 1.00 64.68 C ANISOU 3318 CG1 VAL B 496 6130 11013 7433 1105 14 -697 C ATOM 3319 CG2 VAL B 496 3.370 42.902 31.667 1.00 67.87 C ANISOU 3319 CG2 VAL B 496 6436 11320 8032 1136 30 -763 C ATOM 3320 N TYR B 497 7.331 44.510 33.373 1.00 54.47 N ANISOU 3320 N TYR B 497 4838 9604 6255 1253 -122 -807 N ATOM 3321 CA TYR B 497 8.684 44.462 33.909 1.00 54.27 C ANISOU 3321 CA TYR B 497 4862 9573 6186 1262 -177 -759 C ATOM 3322 C TYR B 497 8.890 43.246 34.807 1.00 61.64 C ANISOU 3322 C TYR B 497 5853 10577 6990 1196 -165 -654 C ATOM 3323 O TYR B 497 8.306 43.150 35.887 1.00 63.87 O ANISOU 3323 O TYR B 497 6130 10983 7154 1140 -123 -688 O ATOM 3324 CB TYR B 497 9.021 45.747 34.667 1.00 49.03 C ANISOU 3324 CB TYR B 497 4166 8961 5504 1292 -202 -879 C ATOM 3325 CG TYR B 497 10.440 45.783 35.185 1.00 48.91 C ANISOU 3325 CG TYR B 497 4195 8939 5452 1297 -271 -830 C ATOM 3326 CD1 TYR B 497 11.510 45.937 34.315 1.00 47.68 C ANISOU 3326 CD1 TYR B 497 4051 8669 5395 1342 -332 -781 C ATOM 3327 CD2 TYR B 497 10.710 45.660 36.541 1.00 52.22 C ANISOU 3327 CD2 TYR B 497 4640 9469 5734 1250 -275 -831 C ATOM 3328 CE1 TYR B 497 12.809 45.968 34.780 1.00 49.29 C ANISOU 3328 CE1 TYR B 497 4280 8871 5576 1348 -398 -734 C ATOM 3329 CE2 TYR B 497 12.006 45.690 37.016 1.00 53.71 C ANISOU 3329 CE2 TYR B 497 4863 9649 5894 1252 -350 -779 C ATOM 3330 CZ TYR B 497 13.050 45.845 36.130 1.00 53.42 C ANISOU 3330 CZ TYR B 497 4826 9501 5971 1304 -412 -730 C ATOM 3331 OH TYR B 497 14.344 45.876 36.593 1.00 55.84 O ANISOU 3331 OH TYR B 497 5154 9804 6260 1306 -489 -677 O ATOM 3332 N ARG B 498 9.724 42.319 34.348 1.00 84.50 N ANISOU 3332 N ARG B 498 8806 13389 9909 1199 -202 -528 N ATOM 3333 CA ARG B 498 10.040 41.119 35.109 1.00 91.59 C ANISOU 3333 CA ARG B 498 9770 14329 10702 1142 -212 -412 C ATOM 3334 C ARG B 498 11.519 41.119 35.481 1.00 90.39 C ANISOU 3334 C ARG B 498 9648 14146 10552 1173 -292 -356 C ATOM 3335 O ARG B 498 12.146 40.065 35.574 1.00 93.88 O ANISOU 3335 O ARG B 498 10144 14549 10976 1160 -327 -234 O ATOM 3336 CB ARG B 498 9.704 39.868 34.292 1.00 99.15 C ANISOU 3336 CB ARG B 498 10774 15207 11690 1120 -191 -303 C ATOM 3337 CG ARG B 498 8.214 39.640 34.046 1.00104.30 C ANISOU 3337 CG ARG B 498 11402 15903 12324 1070 -117 -334 C ATOM 3338 CD ARG B 498 7.589 38.752 35.119 1.00107.53 C ANISOU 3338 CD ARG B 498 11847 16425 12583 973 -83 -282 C ATOM 3339 NE ARG B 498 7.051 39.507 36.248 1.00104.14 N ANISOU 3339 NE ARG B 498 11369 16144 12056 938 -44 -388 N ATOM 3340 CZ ARG B 498 5.753 39.708 36.458 1.00 99.32 C ANISOU 3340 CZ ARG B 498 10701 15628 11410 893 33 -464 C ATOM 3341 NH1 ARG B 498 4.860 39.208 35.615 1.00 97.57 N ANISOU 3341 NH1 ARG B 498 10463 15368 11241 873 70 -437 N ATOM 3342 NH2 ARG B 498 5.347 40.403 37.510 1.00 98.26 N ANISOU 3342 NH2 ARG B 498 10522 15626 11185 865 75 -570 N ATOM 3343 N GLY B 499 12.068 42.312 35.692 1.00 60.29 N ANISOU 3343 N GLY B 499 5796 10347 6766 1212 -327 -445 N ATOM 3344 CA GLY B 499 13.486 42.466 35.961 1.00 58.62 C ANISOU 3344 CA GLY B 499 5596 10105 6572 1242 -409 -400 C ATOM 3345 C GLY B 499 13.873 42.327 37.421 1.00 61.78 C ANISOU 3345 C GLY B 499 6028 10611 6833 1187 -450 -376 C ATOM 3346 O GLY B 499 13.027 42.108 38.287 1.00 64.31 O ANISOU 3346 O GLY B 499 6369 11037 7030 1118 -407 -398 O ATOM 3347 N CYS B 500 15.169 42.461 37.690 1.00 73.06 N ANISOU 3347 N CYS B 500 7461 12015 8282 1211 -535 -329 N ATOM 3348 CA CYS B 500 15.704 42.324 39.040 1.00 72.46 C ANISOU 3348 CA CYS B 500 7422 12028 8080 1155 -597 -291 C ATOM 3349 C CYS B 500 16.313 43.640 39.529 1.00 71.17 C ANISOU 3349 C CYS B 500 7231 11903 7908 1167 -646 -387 C ATOM 3350 O CYS B 500 16.426 43.878 40.732 1.00 73.43 O ANISOU 3350 O CYS B 500 7547 12286 8066 1107 -678 -405 O ATOM 3351 CB CYS B 500 16.747 41.204 39.081 1.00 69.14 C ANISOU 3351 CB CYS B 500 7037 11548 7685 1163 -675 -133 C ATOM 3352 SG CYS B 500 17.687 41.090 40.617 1.00101.41 S ANISOU 3352 SG CYS B 500 11168 15720 11645 1102 -788 -65 S ATOM 3353 N GLN B 501 16.697 44.490 38.582 1.00 66.38 N ANISOU 3353 N GLN B 501 6573 11217 7433 1236 -654 -446 N ATOM 3354 CA GLN B 501 17.278 45.795 38.882 1.00 64.78 C ANISOU 3354 CA GLN B 501 6344 11032 7238 1249 -704 -539 C ATOM 3355 C GLN B 501 16.356 46.659 39.735 1.00 65.71 C ANISOU 3355 C GLN B 501 6469 11250 7247 1208 -659 -676 C ATOM 3356 O GLN B 501 16.810 47.359 40.639 1.00 70.59 O ANISOU 3356 O GLN B 501 7103 11930 7790 1177 -708 -727 O ATOM 3357 CB GLN B 501 17.610 46.531 37.581 1.00 63.89 C ANISOU 3357 CB GLN B 501 6181 10810 7283 1319 -706 -583 C ATOM 3358 CG GLN B 501 17.638 48.045 37.708 1.00 63.32 C ANISOU 3358 CG GLN B 501 6086 10750 7223 1330 -727 -719 C ATOM 3359 CD GLN B 501 18.833 48.535 38.490 1.00 63.17 C ANISOU 3359 CD GLN B 501 6073 10763 7165 1309 -824 -705 C ATOM 3360 OE1 GLN B 501 18.816 49.628 39.055 1.00 65.07 O ANISOU 3360 OE1 GLN B 501 6318 11044 7360 1293 -848 -811 O ATOM 3361 NE2 GLN B 501 19.882 47.724 38.528 1.00 60.39 N ANISOU 3361 NE2 GLN B 501 5721 10390 6836 1310 -885 -575 N ATOM 3362 N SER B 502 15.063 46.615 39.437 1.00 56.15 N ANISOU 3362 N SER B 502 5244 10058 6033 1207 -565 -741 N ATOM 3363 CA SER B 502 14.091 47.436 40.147 1.00 63.38 C ANISOU 3363 CA SER B 502 6151 11066 6866 1180 -505 -886 C ATOM 3364 C SER B 502 13.062 46.574 40.869 1.00 72.20 C ANISOU 3364 C SER B 502 7293 12287 7853 1107 -426 -869 C ATOM 3365 O SER B 502 12.617 45.553 40.346 1.00 74.43 O ANISOU 3365 O SER B 502 7579 12541 8158 1100 -391 -782 O ATOM 3366 CB SER B 502 13.389 48.387 39.174 1.00 62.44 C ANISOU 3366 CB SER B 502 5974 10882 6871 1247 -463 -1005 C ATOM 3367 OG SER B 502 12.484 49.243 39.849 1.00 66.02 O ANISOU 3367 OG SER B 502 6408 11415 7262 1235 -406 -1157 O ATOM 3368 N GLU B 503 12.692 46.987 42.076 1.00 60.09 N ANISOU 3368 N GLU B 503 5782 10873 6177 1046 -398 -955 N ATOM 3369 CA GLU B 503 11.642 46.309 42.823 1.00 58.68 C ANISOU 3369 CA GLU B 503 5623 10810 5862 964 -311 -959 C ATOM 3370 C GLU B 503 10.326 47.070 42.690 1.00 56.04 C ANISOU 3370 C GLU B 503 5221 10519 5550 986 -202 -1124 C ATOM 3371 O GLU B 503 9.254 46.472 42.591 1.00 58.28 O ANISOU 3371 O GLU B 503 5481 10851 5812 955 -116 -1122 O ATOM 3372 CB GLU B 503 12.034 46.169 44.296 1.00 63.73 C ANISOU 3372 CB GLU B 503 6337 11566 6312 864 -341 -944 C ATOM 3373 CG GLU B 503 13.130 45.142 44.559 1.00 66.06 C ANISOU 3373 CG GLU B 503 6699 11832 6569 825 -446 -761 C ATOM 3374 CD GLU B 503 13.458 44.991 46.038 1.00 70.80 C ANISOU 3374 CD GLU B 503 7381 12549 6971 712 -486 -738 C ATOM 3375 OE1 GLU B 503 13.396 46.000 46.773 1.00 67.75 O ANISOU 3375 OE1 GLU B 503 7003 12235 6506 686 -472 -869 O ATOM 3376 OE2 GLU B 503 13.786 43.862 46.463 1.00 72.98 O ANISOU 3376 OE2 GLU B 503 7720 12839 7171 645 -537 -589 O ATOM 3377 N ARG B 504 10.419 48.396 42.676 1.00 52.91 N ANISOU 3377 N ARG B 504 4793 10104 5207 1041 -213 -1264 N ATOM 3378 CA ARG B 504 9.242 49.254 42.587 1.00 51.54 C ANISOU 3378 CA ARG B 504 4548 9961 5072 1078 -121 -1434 C ATOM 3379 C ARG B 504 8.629 49.268 41.188 1.00 58.69 C ANISOU 3379 C ARG B 504 5383 10762 6155 1156 -102 -1432 C ATOM 3380 O ARG B 504 7.753 50.086 40.891 1.00 61.44 O ANISOU 3380 O ARG B 504 5662 11104 6580 1208 -52 -1567 O ATOM 3381 CB ARG B 504 9.594 50.681 43.013 1.00 43.95 C ANISOU 3381 CB ARG B 504 3587 8996 4117 1114 -151 -1584 C ATOM 3382 CG ARG B 504 10.821 51.254 42.321 1.00 41.81 C ANISOU 3382 CG ARG B 504 3331 8597 3959 1175 -271 -1542 C ATOM 3383 CD ARG B 504 10.875 52.766 42.452 1.00 45.19 C ANISOU 3383 CD ARG B 504 3744 8994 4431 1225 -292 -1709 C ATOM 3384 NE ARG B 504 11.876 53.353 41.567 1.00 46.31 N ANISOU 3384 NE ARG B 504 3887 9003 4704 1284 -398 -1673 N ATOM 3385 CZ ARG B 504 11.819 54.594 41.093 1.00 52.44 C ANISOU 3385 CZ ARG B 504 4639 9699 5588 1350 -428 -1791 C ATOM 3386 NH1 ARG B 504 10.803 55.381 41.415 1.00 53.64 N ANISOU 3386 NH1 ARG B 504 4755 9882 5742 1379 -360 -1958 N ATOM 3387 NH2 ARG B 504 12.773 55.046 40.289 1.00 53.58 N ANISOU 3387 NH2 ARG B 504 4790 9729 5840 1385 -525 -1744 N ATOM 3388 N LEU B 505 9.091 48.361 40.334 1.00 81.37 N ANISOU 3388 N LEU B 505 8275 13549 9093 1164 -147 -1280 N ATOM 3389 CA LEU B 505 8.609 48.295 38.961 1.00 77.77 C ANISOU 3389 CA LEU B 505 7768 12986 8794 1225 -139 -1262 C ATOM 3390 C LEU B 505 8.196 46.877 38.583 1.00 74.33 C ANISOU 3390 C LEU B 505 7351 12551 8340 1179 -104 -1127 C ATOM 3391 O LEU B 505 7.460 46.673 37.619 1.00 71.11 O ANISOU 3391 O LEU B 505 6902 12088 8030 1203 -74 -1119 O ATOM 3392 CB LEU B 505 9.682 48.801 37.996 1.00 76.60 C ANISOU 3392 CB LEU B 505 7630 12698 8777 1292 -234 -1226 C ATOM 3393 CG LEU B 505 9.257 48.991 36.538 1.00 73.15 C ANISOU 3393 CG LEU B 505 7150 12140 8502 1351 -238 -1226 C ATOM 3394 CD1 LEU B 505 8.196 50.077 36.425 1.00 71.41 C ANISOU 3394 CD1 LEU B 505 6860 11926 8347 1395 -201 -1384 C ATOM 3395 CD2 LEU B 505 10.457 49.318 35.661 1.00 69.59 C ANISOU 3395 CD2 LEU B 505 6723 11564 8154 1394 -327 -1170 C ATOM 3396 N TYR B 506 8.670 45.900 39.348 1.00 69.08 N ANISOU 3396 N TYR B 506 6752 11944 7549 1107 -117 -1018 N ATOM 3397 CA TYR B 506 8.392 44.496 39.057 1.00 66.85 C ANISOU 3397 CA TYR B 506 6505 11654 7242 1057 -97 -880 C ATOM 3398 C TYR B 506 6.894 44.199 39.014 1.00 65.05 C ANISOU 3398 C TYR B 506 6228 11497 6993 1017 5 -926 C ATOM 3399 O TYR B 506 6.196 44.313 40.023 1.00 64.08 O ANISOU 3399 O TYR B 506 6090 11508 6750 956 74 -999 O ATOM 3400 CB TYR B 506 9.081 43.586 40.080 1.00 70.67 C ANISOU 3400 CB TYR B 506 7073 12199 7581 979 -135 -767 C ATOM 3401 CG TYR B 506 8.897 42.111 39.806 1.00 71.75 C ANISOU 3401 CG TYR B 506 7259 12310 7692 928 -129 -616 C ATOM 3402 CD1 TYR B 506 9.728 41.442 38.918 1.00 73.46 C ANISOU 3402 CD1 TYR B 506 7510 12395 8008 973 -193 -494 C ATOM 3403 CD2 TYR B 506 7.891 41.388 40.433 1.00 75.52 C ANISOU 3403 CD2 TYR B 506 7752 12894 8048 832 -57 -599 C ATOM 3404 CE1 TYR B 506 9.563 40.093 38.661 1.00 77.23 C ANISOU 3404 CE1 TYR B 506 8041 12837 8466 930 -190 -361 C ATOM 3405 CE2 TYR B 506 7.719 40.039 40.184 1.00 79.58 C ANISOU 3405 CE2 TYR B 506 8321 13377 8537 779 -59 -458 C ATOM 3406 CZ TYR B 506 8.558 39.397 39.297 1.00 81.95 C ANISOU 3406 CZ TYR B 506 8662 13536 8941 832 -128 -341 C ATOM 3407 OH TYR B 506 8.391 38.054 39.044 1.00 85.80 O ANISOU 3407 OH TYR B 506 9213 13981 9407 783 -133 -206 O ATOM 3408 N GLY B 507 6.409 43.822 37.835 1.00 65.24 N ANISOU 3408 N GLY B 507 6225 11433 7130 1046 16 -883 N ATOM 3409 CA GLY B 507 5.018 43.445 37.667 1.00 63.60 C ANISOU 3409 CA GLY B 507 5965 11282 6917 1005 101 -908 C ATOM 3410 C GLY B 507 4.147 44.567 37.140 1.00 61.11 C ANISOU 3410 C GLY B 507 5547 10956 6718 1070 135 -1053 C ATOM 3411 O GLY B 507 2.939 44.400 36.977 1.00 59.37 O ANISOU 3411 O GLY B 507 5261 10785 6513 1045 204 -1089 O ATOM 3412 N SER B 508 4.760 45.715 36.873 1.00 56.90 N ANISOU 3412 N SER B 508 4996 10353 6270 1153 81 -1135 N ATOM 3413 CA SER B 508 4.026 46.873 36.379 1.00 60.47 C ANISOU 3413 CA SER B 508 5356 10777 6844 1223 94 -1274 C ATOM 3414 C SER B 508 4.005 46.913 34.858 1.00 61.04 C ANISOU 3414 C SER B 508 5418 10698 7077 1275 41 -1224 C ATOM 3415 O SER B 508 4.982 46.550 34.203 1.00 60.41 O ANISOU 3415 O SER B 508 5405 10517 7032 1286 -24 -1122 O ATOM 3416 CB SER B 508 4.639 48.168 36.919 1.00 63.94 C ANISOU 3416 CB SER B 508 5791 11216 7289 1278 58 -1397 C ATOM 3417 OG SER B 508 4.594 48.206 38.335 1.00 74.30 O ANISOU 3417 OG SER B 508 7116 12669 8444 1223 111 -1457 O ATOM 3418 N TYR B 509 2.881 47.344 34.297 1.00 59.06 N ANISOU 3418 N TYR B 509 5081 10436 6924 1302 68 -1298 N ATOM 3419 CA TYR B 509 2.814 47.616 32.872 1.00 53.51 C ANISOU 3419 CA TYR B 509 4368 9588 6375 1349 6 -1271 C ATOM 3420 C TYR B 509 3.473 48.961 32.619 1.00 52.32 C ANISOU 3420 C TYR B 509 4214 9354 6313 1429 -67 -1360 C ATOM 3421 O TYR B 509 3.342 49.884 33.421 1.00 53.50 O ANISOU 3421 O TYR B 509 4321 9561 6445 1462 -51 -1489 O ATOM 3422 CB TYR B 509 1.366 47.642 32.385 1.00 52.88 C ANISOU 3422 CB TYR B 509 4194 9524 6374 1348 46 -1314 C ATOM 3423 CG TYR B 509 0.708 46.282 32.334 1.00 58.33 C ANISOU 3423 CG TYR B 509 4896 10270 6999 1262 102 -1207 C ATOM 3424 CD1 TYR B 509 -0.071 45.828 33.386 1.00 65.04 C ANISOU 3424 CD1 TYR B 509 5701 11277 7737 1201 196 -1239 C ATOM 3425 CD2 TYR B 509 0.864 45.452 31.231 1.00 57.80 C ANISOU 3425 CD2 TYR B 509 4890 10098 6975 1234 63 -1077 C ATOM 3426 CE1 TYR B 509 -0.678 44.586 33.345 1.00 64.38 C ANISOU 3426 CE1 TYR B 509 5632 11242 7588 1111 242 -1137 C ATOM 3427 CE2 TYR B 509 0.260 44.208 31.181 1.00 57.97 C ANISOU 3427 CE2 TYR B 509 4930 10161 6934 1150 109 -979 C ATOM 3428 CZ TYR B 509 -0.509 43.782 32.242 1.00 59.44 C ANISOU 3428 CZ TYR B 509 5070 10502 7011 1088 195 -1006 C ATOM 3429 OH TYR B 509 -1.113 42.547 32.203 1.00 60.13 O ANISOU 3429 OH TYR B 509 5183 10632 7033 995 235 -904 O ATOM 3430 N VAL B 510 4.195 49.070 31.512 1.00 54.19 N ANISOU 3430 N VAL B 510 4499 9452 6639 1452 -144 -1294 N ATOM 3431 CA VAL B 510 4.838 50.326 31.160 1.00 50.17 C ANISOU 3431 CA VAL B 510 3993 8851 6216 1515 -222 -1366 C ATOM 3432 C VAL B 510 4.582 50.665 29.700 1.00 48.52 C ANISOU 3432 C VAL B 510 3782 8503 6152 1538 -284 -1343 C ATOM 3433 O VAL B 510 5.111 50.017 28.801 1.00 50.19 O ANISOU 3433 O VAL B 510 4056 8632 6383 1510 -311 -1230 O ATOM 3434 CB VAL B 510 6.353 50.286 31.422 1.00 42.17 C ANISOU 3434 CB VAL B 510 3060 7816 5148 1509 -267 -1308 C ATOM 3435 CG1 VAL B 510 7.007 51.568 30.933 1.00 39.59 C ANISOU 3435 CG1 VAL B 510 2741 7388 4915 1561 -352 -1373 C ATOM 3436 CG2 VAL B 510 6.623 50.076 32.899 1.00 40.69 C ANISOU 3436 CG2 VAL B 510 2882 7762 4817 1481 -223 -1334 C ATOM 3437 N PHE B 511 3.758 51.681 29.475 1.00 48.50 N ANISOU 3437 N PHE B 511 3708 8470 6250 1588 -309 -1454 N ATOM 3438 CA PHE B 511 3.466 52.142 28.126 1.00 53.33 C ANISOU 3438 CA PHE B 511 4318 8945 7001 1607 -385 -1439 C ATOM 3439 C PHE B 511 3.994 53.558 27.927 1.00 61.31 C ANISOU 3439 C PHE B 511 5337 9865 8094 1664 -474 -1526 C ATOM 3440 O PHE B 511 3.899 54.393 28.825 1.00 68.19 O ANISOU 3440 O PHE B 511 6167 10787 8954 1709 -465 -1648 O ATOM 3441 CB PHE B 511 1.962 52.090 27.857 1.00 55.71 C ANISOU 3441 CB PHE B 511 4526 9267 7374 1613 -361 -1477 C ATOM 3442 CG PHE B 511 1.417 50.696 27.739 1.00 59.72 C ANISOU 3442 CG PHE B 511 5039 9834 7820 1543 -294 -1372 C ATOM 3443 CD1 PHE B 511 1.292 49.890 28.858 1.00 65.67 C ANISOU 3443 CD1 PHE B 511 5782 10730 8441 1504 -199 -1362 C ATOM 3444 CD2 PHE B 511 1.028 50.193 26.511 1.00 56.72 C ANISOU 3444 CD2 PHE B 511 4681 9362 7506 1506 -331 -1280 C ATOM 3445 CE1 PHE B 511 0.792 48.607 28.752 1.00 67.03 C ANISOU 3445 CE1 PHE B 511 5966 10950 8554 1432 -144 -1261 C ATOM 3446 CE2 PHE B 511 0.527 48.910 26.398 1.00 57.54 C ANISOU 3446 CE2 PHE B 511 4797 9514 7551 1436 -274 -1184 C ATOM 3447 CZ PHE B 511 0.408 48.116 27.520 1.00 62.48 C ANISOU 3447 CZ PHE B 511 5412 10279 8050 1401 -181 -1173 C ATOM 3448 N GLY B 512 4.556 53.819 26.751 1.00 56.22 N ANISOU 3448 N GLY B 512 4751 9085 7524 1654 -557 -1465 N ATOM 3449 CA GLY B 512 5.094 55.129 26.439 1.00 56.09 C ANISOU 3449 CA GLY B 512 4756 8970 7586 1693 -652 -1532 C ATOM 3450 C GLY B 512 4.688 55.595 25.056 1.00 56.09 C ANISOU 3450 C GLY B 512 4768 8827 7715 1689 -742 -1508 C ATOM 3451 O GLY B 512 4.255 54.797 24.229 1.00 54.54 O ANISOU 3451 O GLY B 512 4586 8601 7536 1645 -733 -1417 O ATOM 3452 N ASP B 513 4.817 56.895 24.810 1.00 77.43 N ANISOU 3452 N ASP B 513 7474 11438 10507 1729 -837 -1586 N ATOM 3453 CA ASP B 513 4.531 57.455 23.493 1.00 83.97 C ANISOU 3453 CA ASP B 513 8331 12118 11457 1717 -944 -1559 C ATOM 3454 C ASP B 513 5.815 57.937 22.818 1.00 88.17 C ANISOU 3454 C ASP B 513 8963 12549 11988 1677 -1020 -1510 C ATOM 3455 O ASP B 513 6.883 57.947 23.433 1.00 85.36 O ANISOU 3455 O ASP B 513 8640 12240 11552 1671 -994 -1510 O ATOM 3456 CB ASP B 513 3.486 58.577 23.578 1.00 83.79 C ANISOU 3456 CB ASP B 513 8229 12049 11560 1792 -1009 -1682 C ATOM 3457 CG ASP B 513 3.913 59.714 24.489 1.00 83.23 C ANISOU 3457 CG ASP B 513 8149 11984 11491 1855 -1034 -1810 C ATOM 3458 OD1 ASP B 513 5.128 59.865 24.732 1.00 82.67 O ANISOU 3458 OD1 ASP B 513 8151 11914 11348 1828 -1042 -1790 O ATOM 3459 OD2 ASP B 513 3.027 60.460 24.960 1.00 82.07 O ANISOU 3459 OD2 ASP B 513 7920 11841 11423 1931 -1046 -1935 O ATOM 3460 N ARG B 514 5.706 58.329 21.552 1.00 91.19 N ANISOU 3460 N ARG B 514 9393 12797 12456 1642 -1115 -1465 N ATOM 3461 CA ARG B 514 6.876 58.687 20.755 1.00 94.46 C ANISOU 3461 CA ARG B 514 9908 13118 12866 1582 -1179 -1406 C ATOM 3462 C ARG B 514 7.555 59.973 21.227 1.00 95.31 C ANISOU 3462 C ARG B 514 10030 13188 12994 1615 -1252 -1493 C ATOM 3463 O ARG B 514 8.623 60.335 20.735 1.00 94.59 O ANISOU 3463 O ARG B 514 10014 13036 12889 1563 -1300 -1453 O ATOM 3464 CB ARG B 514 6.503 58.788 19.271 1.00 97.44 C ANISOU 3464 CB ARG B 514 10340 13361 13320 1521 -1266 -1335 C ATOM 3465 CG ARG B 514 5.163 59.459 19.008 1.00100.39 C ANISOU 3465 CG ARG B 514 10655 13670 13817 1567 -1349 -1394 C ATOM 3466 CD ARG B 514 4.867 59.529 17.515 1.00100.49 C ANISOU 3466 CD ARG B 514 10738 13548 13896 1491 -1448 -1310 C ATOM 3467 NE ARG B 514 5.808 60.401 16.818 1.00102.83 N ANISOU 3467 NE ARG B 514 11133 13730 14208 1438 -1547 -1292 N ATOM 3468 CZ ARG B 514 5.568 61.674 16.521 1.00107.07 C ANISOU 3468 CZ ARG B 514 11683 14152 14847 1458 -1685 -1346 C ATOM 3469 NH1 ARG B 514 4.410 62.230 16.852 1.00108.82 N ANISOU 3469 NH1 ARG B 514 11816 14354 15177 1543 -1740 -1428 N ATOM 3470 NH2 ARG B 514 6.488 62.391 15.890 1.00108.25 N ANISOU 3470 NH2 ARG B 514 11931 14204 14994 1393 -1770 -1319 N ATOM 3471 N ASN B 515 6.932 60.657 22.180 1.00 95.76 N ANISOU 3471 N ASN B 515 10017 13284 13084 1697 -1256 -1616 N ATOM 3472 CA ASN B 515 7.484 61.896 22.716 1.00 93.23 C ANISOU 3472 CA ASN B 515 9713 12926 12783 1733 -1325 -1712 C ATOM 3473 C ASN B 515 8.439 61.654 23.880 1.00 86.86 C ANISOU 3473 C ASN B 515 8910 12237 11856 1735 -1250 -1732 C ATOM 3474 O ASN B 515 9.278 62.500 24.189 1.00 85.88 O ANISOU 3474 O ASN B 515 8826 12083 11720 1732 -1307 -1775 O ATOM 3475 CB ASN B 515 6.362 62.837 23.155 1.00 98.93 C ANISOU 3475 CB ASN B 515 10363 13618 13608 1824 -1371 -1848 C ATOM 3476 CG ASN B 515 5.489 63.282 22.001 1.00102.97 C ANISOU 3476 CG ASN B 515 10873 13992 14257 1825 -1479 -1830 C ATOM 3477 OD1 ASN B 515 5.665 62.843 20.864 1.00103.39 O ANISOU 3477 OD1 ASN B 515 10987 13979 14319 1748 -1515 -1713 O ATOM 3478 ND2 ASN B 515 4.537 64.162 22.290 1.00103.45 N ANISOU 3478 ND2 ASN B 515 10867 14008 14432 1912 -1534 -1947 N ATOM 3479 N GLY B 516 8.301 60.500 24.525 1.00 66.08 N ANISOU 3479 N GLY B 516 6239 9736 9133 1733 -1132 -1698 N ATOM 3480 CA GLY B 516 9.160 60.143 25.638 1.00 63.65 C ANISOU 3480 CA GLY B 516 5935 9544 8706 1728 -1066 -1702 C ATOM 3481 C GLY B 516 8.427 60.122 26.966 1.00 65.67 C ANISOU 3481 C GLY B 516 6121 9919 8913 1785 -991 -1808 C ATOM 3482 O GLY B 516 9.047 60.077 28.029 1.00 65.17 O ANISOU 3482 O GLY B 516 6065 9947 8751 1783 -953 -1838 O ATOM 3483 N ASN B 517 7.100 60.156 26.904 1.00 71.07 N ANISOU 3483 N ASN B 517 6736 10605 9664 1829 -970 -1866 N ATOM 3484 CA ASN B 517 6.278 60.152 28.108 1.00 71.70 C ANISOU 3484 CA ASN B 517 6739 10802 9702 1880 -887 -1978 C ATOM 3485 C ASN B 517 5.784 58.749 28.434 1.00 71.93 C ANISOU 3485 C ASN B 517 6729 10955 9646 1847 -771 -1907 C ATOM 3486 O ASN B 517 5.166 58.091 27.599 1.00 71.41 O ANISOU 3486 O ASN B 517 6645 10861 9627 1827 -763 -1831 O ATOM 3487 CB ASN B 517 5.092 61.107 27.955 1.00 72.71 C ANISOU 3487 CB ASN B 517 6797 10867 9965 1956 -930 -2102 C ATOM 3488 CG ASN B 517 5.500 62.467 27.420 1.00 74.27 C ANISOU 3488 CG ASN B 517 7043 10911 10264 1983 -1066 -2155 C ATOM 3489 OD1 ASN B 517 5.951 62.590 26.281 1.00 74.27 O ANISOU 3489 OD1 ASN B 517 7104 10794 10319 1941 -1155 -2064 O ATOM 3490 ND2 ASN B 517 5.331 63.500 28.238 1.00 75.99 N ANISOU 3490 ND2 ASN B 517 7241 11128 10505 2048 -1081 -2306 N ATOM 3491 N PHE B 518 6.056 58.294 29.653 1.00 84.38 N ANISOU 3491 N PHE B 518 8301 12667 11092 1834 -687 -1929 N ATOM 3492 CA PHE B 518 5.692 56.941 30.055 1.00 78.41 C ANISOU 3492 CA PHE B 518 7523 12030 10239 1792 -582 -1854 C ATOM 3493 C PHE B 518 4.680 56.910 31.193 1.00 73.83 C ANISOU 3493 C PHE B 518 6865 11582 9607 1815 -486 -1966 C ATOM 3494 O PHE B 518 4.475 57.904 31.890 1.00 76.08 O ANISOU 3494 O PHE B 518 7120 11882 9903 1865 -488 -2109 O ATOM 3495 CB PHE B 518 6.936 56.148 30.452 1.00 75.37 C ANISOU 3495 CB PHE B 518 7210 11696 9730 1735 -565 -1748 C ATOM 3496 CG PHE B 518 7.886 55.912 29.321 1.00 71.56 C ANISOU 3496 CG PHE B 518 6794 11105 9290 1703 -630 -1628 C ATOM 3497 CD1 PHE B 518 7.774 54.782 28.531 1.00 70.11 C ANISOU 3497 CD1 PHE B 518 6628 10902 9109 1663 -601 -1504 C ATOM 3498 CD2 PHE B 518 8.890 56.822 29.044 1.00 71.53 C ANISOU 3498 CD2 PHE B 518 6838 11019 9323 1708 -717 -1643 C ATOM 3499 CE1 PHE B 518 8.648 54.562 27.486 1.00 69.99 C ANISOU 3499 CE1 PHE B 518 6674 10789 9129 1632 -649 -1404 C ATOM 3500 CE2 PHE B 518 9.767 56.610 28.002 1.00 73.72 C ANISOU 3500 CE2 PHE B 518 7170 11205 9635 1672 -766 -1538 C ATOM 3501 CZ PHE B 518 9.646 55.478 27.220 1.00 72.68 C ANISOU 3501 CZ PHE B 518 7053 11057 9504 1635 -727 -1422 C ATOM 3502 N LEU B 519 4.054 55.751 31.368 1.00 48.35 N ANISOU 3502 N LEU B 519 3605 8449 6317 1774 -398 -1903 N ATOM 3503 CA LEU B 519 3.088 55.543 32.436 1.00 49.32 C ANISOU 3503 CA LEU B 519 3652 8715 6372 1775 -291 -1994 C ATOM 3504 C LEU B 519 3.137 54.096 32.906 1.00 57.70 C ANISOU 3504 C LEU B 519 4737 9891 7294 1694 -207 -1880 C ATOM 3505 O LEU B 519 3.735 53.242 32.250 1.00 58.30 O ANISOU 3505 O LEU B 519 4876 9920 7354 1650 -234 -1734 O ATOM 3506 CB LEU B 519 1.676 55.909 31.967 1.00 39.44 C ANISOU 3506 CB LEU B 519 2290 7442 5253 1825 -278 -2073 C ATOM 3507 CG LEU B 519 1.065 55.129 30.801 1.00 37.52 C ANISOU 3507 CG LEU B 519 2026 7143 5086 1796 -295 -1956 C ATOM 3508 CD1 LEU B 519 0.552 53.774 31.262 1.00 37.15 C ANISOU 3508 CD1 LEU B 519 1959 7229 4926 1723 -188 -1881 C ATOM 3509 CD2 LEU B 519 -0.060 55.931 30.166 1.00 39.26 C ANISOU 3509 CD2 LEU B 519 2147 7291 5478 1864 -339 -2043 C ATOM 3510 N THR B 520 2.509 53.828 34.044 1.00 64.57 N ANISOU 3510 N THR B 520 5562 10909 8061 1670 -105 -1950 N ATOM 3511 CA THR B 520 2.465 52.479 34.589 1.00 62.60 C ANISOU 3511 CA THR B 520 5340 10776 7671 1584 -28 -1847 C ATOM 3512 C THR B 520 1.035 52.060 34.904 1.00 58.56 C ANISOU 3512 C THR B 520 4727 10372 7149 1562 75 -1896 C ATOM 3513 O THR B 520 0.279 52.810 35.521 1.00 64.29 O ANISOU 3513 O THR B 520 5371 11165 7893 1601 130 -2050 O ATOM 3514 CB THR B 520 3.352 52.341 35.849 1.00 71.06 C ANISOU 3514 CB THR B 520 6481 11943 8576 1538 -5 -1850 C ATOM 3515 OG1 THR B 520 2.897 51.238 36.642 1.00 77.12 O ANISOU 3515 OG1 THR B 520 7250 12851 9203 1455 89 -1800 O ATOM 3516 CG2 THR B 520 3.295 53.604 36.686 1.00 74.81 C ANISOU 3516 CG2 THR B 520 6930 12452 9042 1586 5 -2028 C ATOM 3517 N LEU B 521 0.668 50.860 34.466 1.00 60.64 N ANISOU 3517 N LEU B 521 4998 10654 7388 1499 103 -1768 N ATOM 3518 CA LEU B 521 -0.662 50.317 34.723 1.00 60.56 C ANISOU 3518 CA LEU B 521 4895 10754 7361 1460 199 -1793 C ATOM 3519 C LEU B 521 -0.606 49.149 35.699 1.00 61.21 C ANISOU 3519 C LEU B 521 5025 10978 7255 1353 282 -1718 C ATOM 3520 O LEU B 521 0.335 48.353 35.681 1.00 61.58 O ANISOU 3520 O LEU B 521 5179 10997 7220 1305 246 -1584 O ATOM 3521 CB LEU B 521 -1.323 49.860 33.423 1.00 56.68 C ANISOU 3521 CB LEU B 521 4369 10174 6993 1458 163 -1707 C ATOM 3522 CG LEU B 521 -1.769 50.954 32.456 1.00 55.03 C ANISOU 3522 CG LEU B 521 4090 9841 6978 1549 86 -1784 C ATOM 3523 CD1 LEU B 521 -2.467 50.337 31.258 1.00 58.80 C ANISOU 3523 CD1 LEU B 521 4543 10249 7551 1522 53 -1684 C ATOM 3524 CD2 LEU B 521 -2.682 51.939 33.162 1.00 56.11 C ANISOU 3524 CD2 LEU B 521 4101 10054 7166 1612 143 -1971 C ATOM 3525 N GLN B 522 -1.621 49.050 36.548 1.00 48.91 N ANISOU 3525 N GLN B 522 3385 9569 5631 1316 393 -1805 N ATOM 3526 CA GLN B 522 -1.702 47.968 37.516 1.00 53.41 C ANISOU 3526 CA GLN B 522 3997 10282 6012 1200 475 -1739 C ATOM 3527 C GLN B 522 -3.158 47.675 37.835 1.00 52.00 C ANISOU 3527 C GLN B 522 3699 10236 5822 1153 590 -1801 C ATOM 3528 O GLN B 522 -3.983 48.588 37.890 1.00 50.26 O ANISOU 3528 O GLN B 522 3355 10043 5697 1219 634 -1956 O ATOM 3529 CB GLN B 522 -0.942 48.336 38.791 1.00 64.11 C ANISOU 3529 CB GLN B 522 5418 11721 7221 1178 497 -1803 C ATOM 3530 CG GLN B 522 -1.091 47.327 39.918 1.00 73.12 C ANISOU 3530 CG GLN B 522 6605 13022 8154 1047 582 -1750 C ATOM 3531 CD GLN B 522 -0.390 47.767 41.184 1.00 76.29 C ANISOU 3531 CD GLN B 522 7073 13506 8406 1018 598 -1821 C ATOM 3532 OE1 GLN B 522 0.640 48.440 41.134 1.00 78.24 O ANISOU 3532 OE1 GLN B 522 7378 13667 8682 1077 512 -1835 O ATOM 3533 NE2 GLN B 522 -0.947 47.391 42.331 1.00 74.23 N ANISOU 3533 NE2 GLN B 522 6807 13417 7979 918 707 -1865 N ATOM 3534 N GLN B 523 -3.472 46.400 38.039 1.00 66.65 N ANISOU 3534 N GLN B 523 5587 12170 7565 1039 638 -1681 N ATOM 3535 CA GLN B 523 -4.844 45.995 38.314 1.00 70.94 C ANISOU 3535 CA GLN B 523 6017 12847 8089 975 748 -1722 C ATOM 3536 C GLN B 523 -5.044 45.674 39.793 1.00 74.05 C ANISOU 3536 C GLN B 523 6424 13434 8278 871 865 -1773 C ATOM 3537 O GLN B 523 -4.338 46.202 40.651 1.00 79.38 O ANISOU 3537 O GLN B 523 7157 14144 8861 881 870 -1842 O ATOM 3538 CB GLN B 523 -5.227 44.796 37.446 1.00 68.36 C ANISOU 3538 CB GLN B 523 5713 12478 7784 905 722 -1555 C ATOM 3539 CG GLN B 523 -6.705 44.717 37.107 1.00 65.29 C ANISOU 3539 CG GLN B 523 5172 12156 7481 886 790 -1602 C ATOM 3540 CD GLN B 523 -7.011 43.605 36.130 1.00 62.08 C ANISOU 3540 CD GLN B 523 4800 11682 7105 819 745 -1435 C ATOM 3541 OE1 GLN B 523 -6.203 42.696 35.936 1.00 60.99 O ANISOU 3541 OE1 GLN B 523 4806 11480 6888 764 692 -1284 O ATOM 3542 NE2 GLN B 523 -8.181 43.670 35.506 1.00 62.11 N ANISOU 3542 NE2 GLN B 523 4672 11697 7230 823 763 -1462 N ATOM 3543 N SER B 524 -6.009 44.809 40.086 1.00 68.90 N ANISOU 3543 N SER B 524 5722 12908 7549 762 957 -1736 N ATOM 3544 CA SER B 524 -6.311 44.436 41.463 1.00 77.27 C ANISOU 3544 CA SER B 524 6794 14162 8403 641 1076 -1779 C ATOM 3545 C SER B 524 -6.934 43.046 41.522 1.00 79.55 C ANISOU 3545 C SER B 524 7102 14536 8587 492 1123 -1640 C ATOM 3546 O SER B 524 -7.869 42.751 40.780 1.00 80.99 O ANISOU 3546 O SER B 524 7186 14712 8874 486 1140 -1617 O ATOM 3547 CB SER B 524 -7.262 45.455 42.091 1.00 81.80 C ANISOU 3547 CB SER B 524 7211 14861 9009 684 1200 -2003 C ATOM 3548 OG SER B 524 -6.836 46.781 41.837 1.00 84.35 O ANISOU 3548 OG SER B 524 7503 15081 9467 834 1146 -2134 O ATOM 3549 N PRO B 525 -6.412 42.185 42.407 1.00 88.19 N ANISOU 3549 N PRO B 525 8328 15707 9473 363 1135 -1542 N ATOM 3550 CA PRO B 525 -6.963 40.838 42.587 1.00 95.94 C ANISOU 3550 CA PRO B 525 9347 16773 10333 205 1176 -1406 C ATOM 3551 C PRO B 525 -8.477 40.882 42.770 1.00100.48 C ANISOU 3551 C PRO B 525 9753 17504 10922 149 1314 -1508 C ATOM 3552 O PRO B 525 -9.182 39.987 42.305 1.00106.70 O ANISOU 3552 O PRO B 525 10515 18307 11718 66 1326 -1406 O ATOM 3553 CB PRO B 525 -6.282 40.359 43.868 1.00102.15 C ANISOU 3553 CB PRO B 525 10273 17657 10882 85 1192 -1360 C ATOM 3554 CG PRO B 525 -4.979 41.078 43.876 1.00 99.24 C ANISOU 3554 CG PRO B 525 9989 17172 10546 194 1091 -1378 C ATOM 3555 CD PRO B 525 -5.250 42.430 43.278 1.00 91.22 C ANISOU 3555 CD PRO B 525 8839 16094 9726 356 1097 -1546 C ATOM 3556 N VAL B 526 -8.960 41.921 43.445 1.00 86.46 N ANISOU 3556 N VAL B 526 7859 15839 9152 195 1419 -1710 N ATOM 3557 CA VAL B 526 -10.392 42.155 43.587 1.00 77.86 C ANISOU 3557 CA VAL B 526 6578 14895 8111 171 1556 -1837 C ATOM 3558 C VAL B 526 -10.746 43.483 42.924 1.00 70.35 C ANISOU 3558 C VAL B 526 5472 13862 7396 356 1544 -2003 C ATOM 3559 O VAL B 526 -9.874 44.330 42.736 1.00 67.92 O ANISOU 3559 O VAL B 526 5216 13431 7160 480 1461 -2053 O ATOM 3560 CB VAL B 526 -10.817 42.176 45.065 1.00 77.73 C ANISOU 3560 CB VAL B 526 6542 15105 7885 48 1717 -1951 C ATOM 3561 CG1 VAL B 526 -10.623 40.804 45.689 1.00 75.86 C ANISOU 3561 CG1 VAL B 526 6453 14953 7417 -154 1725 -1777 C ATOM 3562 CG2 VAL B 526 -10.029 43.230 45.829 1.00 77.76 C ANISOU 3562 CG2 VAL B 526 6597 15109 7839 124 1723 -2093 C ATOM 3563 N THR B 527 -12.018 43.656 42.570 1.00 58.79 N ANISOU 3563 N THR B 527 3818 12465 6056 372 1619 -2082 N ATOM 3564 CA THR B 527 -12.485 44.837 41.834 1.00 58.19 C ANISOU 3564 CA THR B 527 3582 12300 6227 547 1593 -2224 C ATOM 3565 C THR B 527 -11.924 44.893 40.410 1.00 54.62 C ANISOU 3565 C THR B 527 3186 11615 5952 648 1415 -2103 C ATOM 3566 O THR B 527 -12.537 45.474 39.514 1.00 54.73 O ANISOU 3566 O THR B 527 3068 11547 6178 752 1371 -2154 O ATOM 3567 CB THR B 527 -12.181 46.170 42.572 1.00 56.98 C ANISOU 3567 CB THR B 527 3396 12168 6087 658 1642 -2438 C ATOM 3568 OG1 THR B 527 -10.808 46.537 42.385 1.00 56.04 O ANISOU 3568 OG1 THR B 527 3441 11892 5961 729 1512 -2387 O ATOM 3569 CG2 THR B 527 -12.483 46.052 44.058 1.00 60.23 C ANISOU 3569 CG2 THR B 527 3802 12803 6281 539 1813 -2545 C ATOM 3570 N LYS B 528 -10.760 44.281 40.216 1.00 72.02 N ANISOU 3570 N LYS B 528 5585 13713 8066 614 1312 -1944 N ATOM 3571 CA LYS B 528 -10.117 44.185 38.908 1.00 68.74 C ANISOU 3571 CA LYS B 528 5248 13085 7786 686 1154 -1816 C ATOM 3572 C LYS B 528 -10.145 45.507 38.145 1.00 70.09 C ANISOU 3572 C LYS B 528 5326 13124 8180 860 1083 -1936 C ATOM 3573 O LYS B 528 -10.408 45.536 36.944 1.00 71.52 O ANISOU 3573 O LYS B 528 5471 13178 8525 911 992 -1876 O ATOM 3574 CB LYS B 528 -10.765 43.076 38.073 1.00 63.47 C ANISOU 3574 CB LYS B 528 4571 12396 7148 598 1127 -1661 C ATOM 3575 CG LYS B 528 -11.582 42.088 38.890 1.00 64.62 C ANISOU 3575 CG LYS B 528 4686 12735 7130 430 1251 -1625 C ATOM 3576 CD LYS B 528 -11.338 40.653 38.466 1.00 64.74 C ANISOU 3576 CD LYS B 528 4841 12702 7054 304 1194 -1407 C ATOM 3577 CE LYS B 528 -10.024 40.137 39.033 1.00 70.39 C ANISOU 3577 CE LYS B 528 5761 13379 7603 261 1147 -1307 C ATOM 3578 NZ LYS B 528 -9.924 38.654 38.952 1.00 74.52 N ANISOU 3578 NZ LYS B 528 6415 13897 8003 116 1121 -1112 N ATOM 3579 N GLN B 529 -9.872 46.598 38.852 1.00 65.02 N ANISOU 3579 N GLN B 529 4656 12511 7538 943 1119 -2103 N ATOM 3580 CA GLN B 529 -9.829 47.918 38.234 1.00 60.50 C ANISOU 3580 CA GLN B 529 4010 11809 7169 1107 1046 -2224 C ATOM 3581 C GLN B 529 -8.389 48.304 37.917 1.00 61.80 C ANISOU 3581 C GLN B 529 4334 11814 7332 1168 920 -2169 C ATOM 3582 O GLN B 529 -7.450 47.641 38.358 1.00 62.89 O ANISOU 3582 O GLN B 529 4623 11964 7310 1093 905 -2065 O ATOM 3583 CB GLN B 529 -10.462 48.959 39.156 1.00 58.37 C ANISOU 3583 CB GLN B 529 3604 11655 6920 1170 1162 -2457 C ATOM 3584 CG GLN B 529 -11.880 48.620 39.574 1.00 60.09 C ANISOU 3584 CG GLN B 529 3647 12051 7134 1107 1306 -2529 C ATOM 3585 CD GLN B 529 -12.875 48.752 38.439 1.00 56.98 C ANISOU 3585 CD GLN B 529 3097 11585 6967 1170 1253 -2518 C ATOM 3586 OE1 GLN B 529 -12.927 49.776 37.758 1.00 58.65 O ANISOU 3586 OE1 GLN B 529 3244 11663 7379 1313 1167 -2598 O ATOM 3587 NE2 GLN B 529 -13.681 47.716 38.237 1.00 57.27 N ANISOU 3587 NE2 GLN B 529 3078 11711 6973 1055 1298 -2416 N ATOM 3588 N TRP B 530 -8.219 49.380 37.156 1.00 63.21 N ANISOU 3588 N TRP B 530 4477 11844 7695 1303 824 -2238 N ATOM 3589 CA TRP B 530 -6.892 49.828 36.755 1.00 64.44 C ANISOU 3589 CA TRP B 530 4772 11845 7868 1361 701 -2191 C ATOM 3590 C TRP B 530 -6.578 51.226 37.272 1.00 72.38 C ANISOU 3590 C TRP B 530 5754 12826 8921 1469 697 -2373 C ATOM 3591 O TRP B 530 -7.476 52.042 37.481 1.00 76.07 O ANISOU 3591 O TRP B 530 6080 13333 9491 1541 751 -2537 O ATOM 3592 CB TRP B 530 -6.756 49.795 35.230 1.00 57.00 C ANISOU 3592 CB TRP B 530 3851 10719 7090 1406 565 -2078 C ATOM 3593 CG TRP B 530 -6.909 48.429 34.645 1.00 50.38 C ANISOU 3593 CG TRP B 530 3063 9878 6201 1300 556 -1893 C ATOM 3594 CD1 TRP B 530 -8.078 47.790 34.346 1.00 54.05 C ANISOU 3594 CD1 TRP B 530 3428 10408 6702 1243 603 -1859 C ATOM 3595 CD2 TRP B 530 -5.855 47.529 34.281 1.00 43.97 C ANISOU 3595 CD2 TRP B 530 2415 8991 5300 1240 493 -1721 C ATOM 3596 NE1 TRP B 530 -7.816 46.547 33.822 1.00 51.24 N ANISOU 3596 NE1 TRP B 530 3176 10018 6276 1146 571 -1674 N ATOM 3597 CE2 TRP B 530 -6.460 46.363 33.771 1.00 43.45 C ANISOU 3597 CE2 TRP B 530 2350 8942 5216 1147 507 -1591 C ATOM 3598 CE3 TRP B 530 -4.461 47.596 34.337 1.00 43.03 C ANISOU 3598 CE3 TRP B 530 2436 8791 5121 1255 427 -1666 C ATOM 3599 CZ2 TRP B 530 -5.717 45.273 33.320 1.00 40.99 C ANISOU 3599 CZ2 TRP B 530 2182 8562 4829 1077 459 -1415 C ATOM 3600 CZ3 TRP B 530 -3.726 46.513 33.889 1.00 39.92 C ANISOU 3600 CZ3 TRP B 530 2170 8336 4660 1189 382 -1492 C ATOM 3601 CH2 TRP B 530 -4.356 45.367 33.387 1.00 41.71 C ANISOU 3601 CH2 TRP B 530 2402 8574 4871 1105 400 -1372 C ATOM 3602 N GLN B 531 -5.292 51.496 37.469 1.00 76.86 N ANISOU 3602 N GLN B 531 7137 14275 7789 -63 407 -2652 N ATOM 3603 CA GLN B 531 -4.840 52.817 37.886 1.00 84.54 C ANISOU 3603 CA GLN B 531 7995 15227 8900 -99 478 -2820 C ATOM 3604 C GLN B 531 -3.646 53.248 37.043 1.00 87.35 C ANISOU 3604 C GLN B 531 8317 15467 9405 -39 493 -2793 C ATOM 3605 O GLN B 531 -2.770 52.437 36.735 1.00 85.13 O ANISOU 3605 O GLN B 531 8086 15195 9067 -2 422 -2694 O ATOM 3606 CB GLN B 531 -4.473 52.818 39.370 1.00 87.17 C ANISOU 3606 CB GLN B 531 8285 15728 9109 -187 439 -2958 C ATOM 3607 CG GLN B 531 -3.393 51.812 39.737 1.00 89.63 C ANISOU 3607 CG GLN B 531 8637 16136 9281 -187 324 -2894 C ATOM 3608 CD GLN B 531 -3.250 51.634 41.237 1.00 88.53 C ANISOU 3608 CD GLN B 531 8477 16183 8976 -273 271 -3007 C ATOM 3609 OE1 GLN B 531 -3.705 52.472 42.020 1.00 81.41 O ANISOU 3609 OE1 GLN B 531 7512 15331 8088 -334 329 -3167 O ATOM 3610 NE2 GLN B 531 -2.611 50.541 41.646 1.00 90.91 N ANISOU 3610 NE2 GLN B 531 8833 16589 9121 -277 161 -2925 N ATOM 3611 N GLU B 532 -3.624 54.523 36.663 1.00110.26 N ANISOU 3611 N GLU B 532 11130 18254 12508 -27 591 -2877 N ATOM 3612 CA GLU B 532 -2.562 55.057 35.818 1.00109.27 C ANISOU 3612 CA GLU B 532 10963 18003 12550 33 627 -2851 C ATOM 3613 C GLU B 532 -1.650 55.999 36.598 1.00106.62 C ANISOU 3613 C GLU B 532 10503 17689 12320 -18 651 -3025 C ATOM 3614 O GLU B 532 -2.104 56.997 37.160 1.00109.51 O ANISOU 3614 O GLU B 532 10780 18056 12772 -69 718 -3175 O ATOM 3615 CB GLU B 532 -3.157 55.795 34.616 1.00112.63 C ANISOU 3615 CB GLU B 532 11384 18260 13150 98 724 -2790 C ATOM 3616 CG GLU B 532 -4.165 54.985 33.811 1.00119.07 C ANISOU 3616 CG GLU B 532 12316 19045 13879 148 699 -2633 C ATOM 3617 CD GLU B 532 -5.522 54.881 34.488 1.00126.04 C ANISOU 3617 CD GLU B 532 13209 20003 14677 90 699 -2682 C ATOM 3618 OE1 GLU B 532 -5.863 55.774 35.293 1.00129.57 O ANISOU 3618 OE1 GLU B 532 13563 20480 15189 25 757 -2837 O ATOM 3619 OE2 GLU B 532 -6.252 53.904 34.212 1.00126.13 O ANISOU 3619 OE2 GLU B 532 13318 20040 14564 110 644 -2568 O ATOM 3620 N LYS B 533 -0.360 55.683 36.627 1.00 80.89 N ANISOU 3620 N LYS B 533 7231 14440 9061 -3 596 -3008 N ATOM 3621 CA LYS B 533 0.611 56.531 37.305 1.00 80.39 C ANISOU 3621 CA LYS B 533 7046 14388 9111 -45 607 -3169 C ATOM 3622 C LYS B 533 1.697 56.982 36.335 1.00 72.39 C ANISOU 3622 C LYS B 533 5986 13221 8297 25 653 -3117 C ATOM 3623 O LYS B 533 2.236 56.172 35.583 1.00 70.03 O ANISOU 3623 O LYS B 533 5762 12882 7964 88 616 -2965 O ATOM 3624 CB LYS B 533 1.237 55.801 38.499 1.00 86.26 C ANISOU 3624 CB LYS B 533 7796 15306 9674 -107 487 -3227 C ATOM 3625 CG LYS B 533 0.237 55.262 39.517 1.00 89.32 C ANISOU 3625 CG LYS B 533 8237 15857 9844 -175 441 -3267 C ATOM 3626 CD LYS B 533 -0.287 53.886 39.117 1.00 88.86 C ANISOU 3626 CD LYS B 533 8315 15839 9609 -141 377 -3078 C ATOM 3627 CE LYS B 533 0.834 52.854 39.070 1.00 82.52 C ANISOU 3627 CE LYS B 533 7556 15077 8722 -115 269 -2975 C ATOM 3628 NZ LYS B 533 0.339 51.486 38.751 1.00 70.82 N ANISOU 3628 NZ LYS B 533 6200 13637 7073 -86 204 -2801 N ATOM 3629 N PRO B 534 2.014 58.284 36.341 1.00 60.91 N ANISOU 3629 N PRO B 534 4405 11675 7062 16 742 -3244 N ATOM 3630 CA PRO B 534 3.079 58.820 35.487 1.00 59.31 C ANISOU 3630 CA PRO B 534 4141 11320 7072 79 800 -3206 C ATOM 3631 C PRO B 534 4.432 58.200 35.820 1.00 61.08 C ANISOU 3631 C PRO B 534 4356 11593 7259 77 708 -3198 C ATOM 3632 O PRO B 534 4.721 57.966 36.993 1.00 68.60 O ANISOU 3632 O PRO B 534 5278 12687 8100 5 619 -3311 O ATOM 3633 CB PRO B 534 3.086 60.312 35.836 1.00 58.18 C ANISOU 3633 CB PRO B 534 3846 11108 7150 42 896 -3386 C ATOM 3634 CG PRO B 534 1.719 60.588 36.363 1.00 56.22 C ANISOU 3634 CG PRO B 534 3608 10926 6829 -11 922 -3462 C ATOM 3635 CD PRO B 534 1.310 59.342 37.084 1.00 58.97 C ANISOU 3635 CD PRO B 534 4065 11450 6889 -51 806 -3425 C ATOM 3636 N LEU B 535 5.245 57.936 34.801 1.00 46.74 N ANISOU 3636 N LEU B 535 2564 9662 5533 156 730 -3065 N ATOM 3637 CA LEU B 535 6.587 57.399 35.015 1.00 48.19 C ANISOU 3637 CA LEU B 535 2726 9867 5717 160 653 -3050 C ATOM 3638 C LEU B 535 7.651 58.455 34.732 1.00 49.39 C ANISOU 3638 C LEU B 535 2741 9880 6144 182 731 -3124 C ATOM 3639 O LEU B 535 7.962 58.745 33.576 1.00 48.01 O ANISOU 3639 O LEU B 535 2570 9549 6124 261 827 -3017 O ATOM 3640 CB LEU B 535 6.832 56.166 34.144 1.00 46.17 C ANISOU 3640 CB LEU B 535 2599 9589 5354 231 612 -2845 C ATOM 3641 CG LEU B 535 8.114 55.390 34.462 1.00 45.82 C ANISOU 3641 CG LEU B 535 2546 9587 5277 230 515 -2818 C ATOM 3642 CD1 LEU B 535 7.964 54.625 35.764 1.00 46.02 C ANISOU 3642 CD1 LEU B 535 2594 9810 5082 150 375 -2881 C ATOM 3643 CD2 LEU B 535 8.478 54.442 33.336 1.00 44.69 C ANISOU 3643 CD2 LEU B 535 2507 9367 5104 315 518 -2620 C ATOM 3644 N CYS B 536 8.204 59.023 35.799 1.00 68.82 N ANISOU 3644 N CYS B 536 5082 12401 8664 112 690 -3307 N ATOM 3645 CA CYS B 536 9.224 60.060 35.692 1.00 73.44 C ANISOU 3645 CA CYS B 536 5518 12862 9524 121 755 -3402 C ATOM 3646 C CYS B 536 10.568 59.489 35.241 1.00 79.48 C ANISOU 3646 C CYS B 536 6279 13564 10355 171 719 -3305 C ATOM 3647 O CYS B 536 10.921 58.362 35.587 1.00 81.33 O ANISOU 3647 O CYS B 536 6585 13904 10411 161 600 -3242 O ATOM 3648 CB CYS B 536 9.381 60.775 37.037 1.00 71.60 C ANISOU 3648 CB CYS B 536 5162 12724 9320 27 706 -3640 C ATOM 3649 SG CYS B 536 10.773 61.920 37.133 1.00 77.58 S ANISOU 3649 SG CYS B 536 5721 13349 10408 26 751 -3783 S ATOM 3650 N LEU B 537 11.311 60.269 34.461 1.00 86.27 N ANISOU 3650 N LEU B 537 7050 14247 11482 226 828 -3289 N ATOM 3651 CA LEU B 537 12.662 59.885 34.060 1.00 86.36 C ANISOU 3651 CA LEU B 537 7033 14181 11601 271 811 -3216 C ATOM 3652 C LEU B 537 13.576 61.099 33.886 1.00 80.84 C ANISOU 3652 C LEU B 537 6163 13325 11229 284 907 -3313 C ATOM 3653 O LEU B 537 14.680 61.141 34.434 1.00 75.67 O ANISOU 3653 O LEU B 537 5408 12671 10673 258 843 -3397 O ATOM 3654 CB LEU B 537 12.640 59.033 32.785 1.00 86.96 C ANISOU 3654 CB LEU B 537 7246 14180 11616 364 856 -2985 C ATOM 3655 CG LEU B 537 11.754 59.475 31.618 1.00 90.48 C ANISOU 3655 CG LEU B 537 7757 14511 12112 432 996 -2875 C ATOM 3656 CD1 LEU B 537 12.139 60.858 31.110 1.00 91.10 C ANISOU 3656 CD1 LEU B 537 7982 14543 12089 518 1010 -2659 C ATOM 3657 CD2 LEU B 537 11.824 58.452 30.494 1.00 92.89 C ANISOU 3657 CD2 LEU B 537 7928 14640 12725 463 1144 -2927 C ATOM 3658 N HIS B 550 12.623 60.570 19.737 1.00 62.28 N ANISOU 3658 N HIS B 550 4768 9727 9168 1319 2105 -1478 N ATOM 3659 CA HIS B 550 11.354 59.867 19.590 1.00 70.80 C ANISOU 3659 CA HIS B 550 5999 10916 9984 1318 2009 -1429 C ATOM 3660 C HIS B 550 11.494 58.375 19.886 1.00 73.11 C ANISOU 3660 C HIS B 550 6403 11333 10043 1298 1869 -1408 C ATOM 3661 O HIS B 550 12.545 57.782 19.648 1.00 73.30 O ANISOU 3661 O HIS B 550 6441 11324 10086 1329 1883 -1360 O ATOM 3662 CB HIS B 550 10.790 60.076 18.184 1.00 79.61 C ANISOU 3662 CB HIS B 550 7238 11942 11069 1422 2116 -1261 C ATOM 3663 CG HIS B 550 10.390 61.490 17.899 1.00 87.95 C ANISOU 3663 CG HIS B 550 8199 12889 12328 1439 2238 -1269 C ATOM 3664 ND1 HIS B 550 9.089 61.932 18.013 1.00 89.39 N ANISOU 3664 ND1 HIS B 550 8394 13110 12459 1415 2207 -1293 N ATOM 3665 CD2 HIS B 550 11.118 62.561 17.507 1.00 92.45 C ANISOU 3665 CD2 HIS B 550 8653 13309 13165 1478 2394 -1253 C ATOM 3666 CE1 HIS B 550 9.033 63.215 17.702 1.00 91.18 C ANISOU 3666 CE1 HIS B 550 8516 13214 12912 1438 2337 -1290 C ATOM 3667 NE2 HIS B 550 10.252 63.621 17.392 1.00 93.39 N ANISOU 3667 NE2 HIS B 550 8717 13379 13389 1477 2453 -1265 N ATOM 3668 N ILE B 551 10.427 57.773 20.406 1.00 82.75 N ANISOU 3668 N ILE B 551 7697 12691 11054 1247 1740 -1442 N ATOM 3669 CA ILE B 551 10.438 56.353 20.751 1.00 87.47 C ANISOU 3669 CA ILE B 551 8394 13410 11429 1224 1601 -1422 C ATOM 3670 C ILE B 551 10.068 55.481 19.556 1.00 85.94 C ANISOU 3670 C ILE B 551 8386 13199 11068 1313 1610 -1259 C ATOM 3671 O ILE B 551 9.065 55.724 18.885 1.00 87.73 O ANISOU 3671 O ILE B 551 8695 13408 11232 1353 1637 -1195 O ATOM 3672 CB ILE B 551 9.485 56.041 21.923 1.00 93.78 C ANISOU 3672 CB ILE B 551 9185 14368 12079 1126 1458 -1534 C ATOM 3673 CG1 ILE B 551 10.173 56.316 23.262 1.00 98.35 C ANISOU 3673 CG1 ILE B 551 9611 15008 12749 1032 1399 -1694 C ATOM 3674 CG2 ILE B 551 9.037 54.589 21.873 1.00 94.15 C ANISOU 3674 CG2 ILE B 551 9379 14522 11870 1128 1335 -1462 C ATOM 3675 CD1 ILE B 551 10.610 57.752 23.453 1.00102.10 C ANISOU 3675 CD1 ILE B 551 9922 15382 13490 1018 1507 -1790 C ATOM 3676 N LEU B 552 10.883 54.461 19.300 1.00 74.78 N ANISOU 3676 N LEU B 552 7035 11790 9587 1343 1583 -1196 N ATOM 3677 CA LEU B 552 10.663 53.562 18.172 1.00 73.12 C ANISOU 3677 CA LEU B 552 7000 11561 9221 1428 1591 -1051 C ATOM 3678 C LEU B 552 10.231 52.173 18.632 1.00 78.49 C ANISOU 3678 C LEU B 552 7774 12376 9673 1390 1431 -1050 C ATOM 3679 O LEU B 552 9.620 51.421 17.871 1.00 82.68 O ANISOU 3679 O LEU B 552 8452 12921 10039 1442 1403 -956 O ATOM 3680 CB LEU B 552 11.927 53.458 17.315 1.00 63.31 C ANISOU 3680 CB LEU B 552 5770 10198 8088 1507 1710 -963 C ATOM 3681 CG LEU B 552 12.460 54.771 16.741 1.00 57.50 C ANISOU 3681 CG LEU B 552 4945 9312 7589 1557 1886 -942 C ATOM 3682 CD1 LEU B 552 13.767 54.542 15.997 1.00 58.89 C ANISOU 3682 CD1 LEU B 552 5130 9375 7870 1629 2000 -858 C ATOM 3683 CD2 LEU B 552 11.424 55.416 15.834 1.00 53.56 C ANISOU 3683 CD2 LEU B 552 4526 8766 7056 1618 1957 -863 C ATOM 3684 N GLY B 553 10.551 51.837 19.877 1.00 85.51 N ANISOU 3684 N GLY B 553 8575 13362 10553 1299 1325 -1154 N ATOM 3685 CA GLY B 553 10.202 50.540 20.430 1.00 82.30 C ANISOU 3685 CA GLY B 553 8239 13084 9947 1257 1175 -1154 C ATOM 3686 C GLY B 553 10.945 50.232 21.715 1.00 77.93 C ANISOU 3686 C GLY B 553 7575 12614 9421 1171 1081 -1253 C ATOM 3687 O GLY B 553 11.769 51.026 22.172 1.00 78.89 O ANISOU 3687 O GLY B 553 7562 12691 9722 1144 1128 -1330 O ATOM 3688 N PHE B 554 10.655 49.074 22.300 1.00 59.88 N ANISOU 3688 N PHE B 554 5343 10447 6961 1128 943 -1249 N ATOM 3689 CA PHE B 554 11.292 48.668 23.548 1.00 57.37 C ANISOU 3689 CA PHE B 554 4933 10224 6641 1047 837 -1332 C ATOM 3690 C PHE B 554 12.053 47.359 23.387 1.00 52.76 C ANISOU 3690 C PHE B 554 4405 9650 5991 1069 776 -1251 C ATOM 3691 O PHE B 554 11.836 46.616 22.432 1.00 44.97 O ANISOU 3691 O PHE B 554 3544 8627 4917 1137 794 -1142 O ATOM 3692 CB PHE B 554 10.253 48.520 24.660 1.00 56.55 C ANISOU 3692 CB PHE B 554 4820 10272 6395 958 719 -1414 C ATOM 3693 CG PHE B 554 9.335 49.698 24.794 1.00 58.35 C ANISOU 3693 CG PHE B 554 5005 10493 6671 936 774 -1490 C ATOM 3694 CD1 PHE B 554 9.805 50.906 25.278 1.00 60.21 C ANISOU 3694 CD1 PHE B 554 5101 10690 7087 901 835 -1601 C ATOM 3695 CD2 PHE B 554 8.000 49.594 24.444 1.00 61.38 C ANISOU 3695 CD2 PHE B 554 5482 10905 6934 947 763 -1453 C ATOM 3696 CE1 PHE B 554 8.962 51.991 25.405 1.00 63.79 C ANISOU 3696 CE1 PHE B 554 5507 11131 7598 879 890 -1674 C ATOM 3697 CE2 PHE B 554 7.151 50.675 24.569 1.00 63.29 C ANISOU 3697 CE2 PHE B 554 5678 11135 7233 926 815 -1521 C ATOM 3698 CZ PHE B 554 7.632 51.876 25.051 1.00 64.34 C ANISOU 3698 CZ PHE B 554 5672 11229 7547 891 881 -1631 C ATOM 3699 N GLY B 555 12.938 47.080 24.338 1.00 56.16 N ANISOU 3699 N GLY B 555 4739 10132 6466 1012 700 -1308 N ATOM 3700 CA GLY B 555 13.724 45.861 24.324 1.00 53.69 C ANISOU 3700 CA GLY B 555 4458 9830 6112 1025 635 -1239 C ATOM 3701 C GLY B 555 13.825 45.226 25.696 1.00 51.60 C ANISOU 3701 C GLY B 555 4136 9710 5758 934 476 -1299 C ATOM 3702 O GLY B 555 13.287 45.748 26.670 1.00 54.44 O ANISOU 3702 O GLY B 555 4437 10168 6081 861 421 -1401 O ATOM 3703 N GLU B 556 14.518 44.094 25.772 1.00 49.83 N ANISOU 3703 N GLU B 556 3931 9500 5500 939 406 -1235 N ATOM 3704 CA GLU B 556 14.669 43.366 27.027 1.00 50.86 C ANISOU 3704 CA GLU B 556 4016 9769 5540 860 250 -1269 C ATOM 3705 C GLU B 556 15.788 42.338 26.930 1.00 52.00 C ANISOU 3705 C GLU B 556 4150 9878 5727 881 205 -1194 C ATOM 3706 O GLU B 556 15.791 41.496 26.033 1.00 49.60 O ANISOU 3706 O GLU B 556 3944 9516 5383 943 233 -1087 O ATOM 3707 CB GLU B 556 13.365 42.661 27.396 1.00 54.56 C ANISOU 3707 CB GLU B 556 4579 10364 5788 826 158 -1246 C ATOM 3708 CG GLU B 556 13.426 41.911 28.716 1.00 58.46 C ANISOU 3708 CG GLU B 556 5033 11009 6170 745 1 -1272 C ATOM 3709 CD GLU B 556 12.399 40.801 28.802 1.00 62.73 C ANISOU 3709 CD GLU B 556 5682 11641 6511 736 -81 -1198 C ATOM 3710 OE1 GLU B 556 12.298 40.007 27.843 1.00 61.95 O ANISOU 3710 OE1 GLU B 556 5679 11476 6384 800 -56 -1093 O ATOM 3711 OE2 GLU B 556 11.700 40.714 29.833 1.00 68.98 O ANISOU 3711 OE2 GLU B 556 6461 12569 7178 664 -169 -1247 O ATOM 3712 N ASP B 557 16.735 42.400 27.860 1.00 62.74 N ANISOU 3712 N ASP B 557 5391 11274 7173 828 132 -1253 N ATOM 3713 CA ASP B 557 17.852 41.460 27.866 1.00 63.15 C ANISOU 3713 CA ASP B 557 5415 11291 7287 842 81 -1185 C ATOM 3714 C ASP B 557 17.479 40.148 28.552 1.00 55.32 C ANISOU 3714 C ASP B 557 4473 10431 6114 800 -72 -1130 C ATOM 3715 O ASP B 557 16.401 40.020 29.132 1.00 48.70 O ANISOU 3715 O ASP B 557 3681 9718 5106 754 -140 -1152 O ATOM 3716 CB ASP B 557 19.093 42.082 28.519 1.00 66.26 C ANISOU 3716 CB ASP B 557 5652 11654 7871 808 63 -1267 C ATOM 3717 CG ASP B 557 18.828 42.579 29.926 1.00 67.17 C ANISOU 3717 CG ASP B 557 5682 11914 7925 713 -52 -1391 C ATOM 3718 OD1 ASP B 557 19.577 43.462 30.395 1.00 68.64 O ANISOU 3718 OD1 ASP B 557 5739 12071 8269 686 -45 -1491 O ATOM 3719 OD2 ASP B 557 17.872 42.091 30.563 1.00 68.34 O ANISOU 3719 OD2 ASP B 557 5890 12205 7871 667 -148 -1391 O ATOM 3720 N GLU B 558 18.380 39.174 28.480 1.00 59.12 N ANISOU 3720 N GLU B 558 4941 10879 6642 817 -119 -1053 N ATOM 3721 CA GLU B 558 18.120 37.851 29.034 1.00 60.06 C ANISOU 3721 CA GLU B 558 5104 11104 6612 786 -256 -982 C ATOM 3722 C GLU B 558 17.894 37.900 30.542 1.00 64.61 C ANISOU 3722 C GLU B 558 5613 11850 7086 691 -402 -1053 C ATOM 3723 O GLU B 558 17.382 36.949 31.135 1.00 65.20 O ANISOU 3723 O GLU B 558 5730 12039 7004 655 -514 -1002 O ATOM 3724 CB GLU B 558 19.272 36.899 28.700 1.00 61.47 C ANISOU 3724 CB GLU B 558 5259 11200 6899 821 -273 -893 C ATOM 3725 CG GLU B 558 18.995 35.443 29.038 1.00 65.02 C ANISOU 3725 CG GLU B 558 5762 11730 7211 805 -394 -798 C ATOM 3726 CD GLU B 558 20.069 34.504 28.519 1.00 66.87 C ANISOU 3726 CD GLU B 558 5981 11860 7567 850 -388 -706 C ATOM 3727 OE1 GLU B 558 21.061 34.993 27.939 1.00 66.39 O ANISOU 3727 OE1 GLU B 558 5865 11666 7696 892 -291 -718 O ATOM 3728 OE2 GLU B 558 19.920 33.276 28.690 1.00 67.27 O ANISOU 3728 OE2 GLU B 558 6071 11956 7532 843 -477 -621 O ATOM 3729 N LEU B 559 18.270 39.018 31.155 1.00 58.22 N ANISOU 3729 N LEU B 559 4698 11056 6367 650 -397 -1172 N ATOM 3730 CA LEU B 559 18.195 39.159 32.605 1.00 56.24 C ANISOU 3730 CA LEU B 559 4376 10965 6027 560 -533 -1256 C ATOM 3731 C LEU B 559 16.944 39.905 33.066 1.00 54.52 C ANISOU 3731 C LEU B 559 4190 10849 5676 516 -520 -1346 C ATOM 3732 O LEU B 559 16.769 40.157 34.257 1.00 61.71 O ANISOU 3732 O LEU B 559 5049 11896 6501 442 -616 -1431 O ATOM 3733 CB LEU B 559 19.448 39.854 33.135 1.00 60.66 C ANISOU 3733 CB LEU B 559 4790 11490 6769 535 -558 -1344 C ATOM 3734 CG LEU B 559 20.766 39.150 32.814 1.00 65.09 C ANISOU 3734 CG LEU B 559 5298 11951 7482 570 -580 -1263 C ATOM 3735 CD1 LEU B 559 21.932 39.861 33.485 1.00 63.97 C ANISOU 3735 CD1 LEU B 559 5001 11788 7517 536 -625 -1362 C ATOM 3736 CD2 LEU B 559 20.701 37.692 33.243 1.00 68.76 C ANISOU 3736 CD2 LEU B 559 5811 12506 7808 553 -712 -1151 C ATOM 3737 N GLY B 560 16.078 40.260 32.123 1.00 56.54 N ANISOU 3737 N GLY B 560 4531 11037 5915 564 -403 -1328 N ATOM 3738 CA GLY B 560 14.810 40.881 32.456 1.00 57.52 C ANISOU 3738 CA GLY B 560 4691 11244 5919 528 -385 -1399 C ATOM 3739 C GLY B 560 14.795 42.393 32.346 1.00 65.03 C ANISOU 3739 C GLY B 560 5573 12136 7000 525 -281 -1523 C ATOM 3740 O GLY B 560 13.727 43.006 32.329 1.00 71.02 O ANISOU 3740 O GLY B 560 6366 12923 7694 512 -233 -1573 O ATOM 3741 N GLU B 561 15.975 43.001 32.271 1.00 58.05 N ANISOU 3741 N GLU B 561 4584 11162 6312 537 -246 -1571 N ATOM 3742 CA GLU B 561 16.074 44.456 32.172 1.00 60.60 C ANISOU 3742 CA GLU B 561 4824 11414 6788 535 -145 -1690 C ATOM 3743 C GLU B 561 15.492 44.978 30.862 1.00 63.28 C ANISOU 3743 C GLU B 561 5235 11623 7186 609 14 -1642 C ATOM 3744 O GLU B 561 15.736 44.416 29.794 1.00 64.44 O ANISOU 3744 O GLU B 561 5453 11667 7363 684 75 -1525 O ATOM 3745 CB GLU B 561 17.524 44.915 32.331 1.00 59.84 C ANISOU 3745 CB GLU B 561 4594 11235 6907 535 -142 -1742 C ATOM 3746 CG GLU B 561 18.149 44.501 33.649 1.00 59.19 C ANISOU 3746 CG GLU B 561 4432 11281 6777 461 -308 -1798 C ATOM 3747 CD GLU B 561 17.228 44.749 34.830 1.00 56.48 C ANISOU 3747 CD GLU B 561 4090 11117 6255 378 -396 -1901 C ATOM 3748 OE1 GLU B 561 16.529 45.786 34.841 1.00 51.19 O ANISOU 3748 OE1 GLU B 561 3405 10443 5600 364 -318 -1999 O ATOM 3749 OE2 GLU B 561 17.208 43.905 35.750 1.00 56.96 O ANISOU 3749 OE2 GLU B 561 4164 11319 6159 329 -539 -1881 O ATOM 3750 N VAL B 562 14.724 46.058 30.953 1.00 68.47 N ANISOU 3750 N VAL B 562 5872 12286 7858 590 78 -1735 N ATOM 3751 CA VAL B 562 14.059 46.624 29.787 1.00 68.11 C ANISOU 3751 CA VAL B 562 5892 12129 7858 656 219 -1692 C ATOM 3752 C VAL B 562 14.887 47.727 29.134 1.00 71.16 C ANISOU 3752 C VAL B 562 6191 12356 8492 702 354 -1725 C ATOM 3753 O VAL B 562 15.704 48.376 29.788 1.00 76.54 O ANISOU 3753 O VAL B 562 6741 13029 9313 663 340 -1828 O ATOM 3754 CB VAL B 562 12.670 47.172 30.149 1.00 66.35 C ANISOU 3754 CB VAL B 562 5699 11986 7524 616 225 -1759 C ATOM 3755 CG1 VAL B 562 11.758 46.037 30.586 1.00 66.28 C ANISOU 3755 CG1 VAL B 562 5791 12113 7279 586 115 -1702 C ATOM 3756 CG2 VAL B 562 12.786 48.222 31.241 1.00 66.13 C ANISOU 3756 CG2 VAL B 562 5542 12019 7567 539 205 -1927 C ATOM 3757 N TYR B 563 14.665 47.931 27.838 1.00 61.98 N ANISOU 3757 N TYR B 563 5101 11067 7383 785 483 -1636 N ATOM 3758 CA TYR B 563 15.409 48.924 27.074 1.00 56.08 C ANISOU 3758 CA TYR B 563 4283 10156 6868 840 630 -1642 C ATOM 3759 C TYR B 563 14.483 49.806 26.244 1.00 55.25 C ANISOU 3759 C TYR B 563 4226 9979 6787 885 755 -1627 C ATOM 3760 O TYR B 563 13.338 49.445 25.974 1.00 51.23 O ANISOU 3760 O TYR B 563 3829 9524 6113 894 736 -1579 O ATOM 3761 CB TYR B 563 16.409 48.240 26.145 1.00 51.93 C ANISOU 3761 CB TYR B 563 3797 9518 6418 917 683 -1521 C ATOM 3762 CG TYR B 563 17.502 47.479 26.854 1.00 50.81 C ANISOU 3762 CG TYR B 563 3587 9413 6305 882 576 -1529 C ATOM 3763 CD1 TYR B 563 18.758 48.041 27.041 1.00 48.21 C ANISOU 3763 CD1 TYR B 563 3119 8996 6202 879 610 -1583 C ATOM 3764 CD2 TYR B 563 17.283 46.193 27.328 1.00 52.05 C ANISOU 3764 CD2 TYR B 563 3813 9688 6276 853 438 -1479 C ATOM 3765 CE1 TYR B 563 19.764 47.344 27.684 1.00 44.98 C ANISOU 3765 CE1 TYR B 563 2645 8618 5829 848 504 -1588 C ATOM 3766 CE2 TYR B 563 18.283 45.489 27.973 1.00 50.22 C ANISOU 3766 CE2 TYR B 563 3516 9488 6075 822 335 -1478 C ATOM 3767 CZ TYR B 563 19.521 46.069 28.148 1.00 44.56 C ANISOU 3767 CZ TYR B 563 2663 8685 5581 820 366 -1533 C ATOM 3768 OH TYR B 563 20.514 45.369 28.789 1.00 45.67 O ANISOU 3768 OH TYR B 563 2736 8855 5762 790 255 -1529 O ATOM 3769 N ILE B 564 14.998 50.958 25.829 1.00 73.90 N ANISOU 3769 N ILE B 564 6497 12212 9368 915 883 -1663 N ATOM 3770 CA ILE B 564 14.240 51.902 25.020 1.00 78.23 C ANISOU 3770 CA ILE B 564 7074 12677 9973 961 1012 -1643 C ATOM 3771 C ILE B 564 15.001 52.259 23.750 1.00 90.18 C ANISOU 3771 C ILE B 564 8597 14014 11655 1059 1170 -1543 C ATOM 3772 O ILE B 564 16.112 52.784 23.811 1.00 97.77 O ANISOU 3772 O ILE B 564 9440 14883 12825 1064 1230 -1580 O ATOM 3773 CB ILE B 564 13.950 53.195 25.800 1.00 77.50 C ANISOU 3773 CB ILE B 564 6849 12598 10001 898 1032 -1795 C ATOM 3774 CG1 ILE B 564 13.002 52.911 26.965 1.00 90.39 C ANISOU 3774 CG1 ILE B 564 8490 14405 11448 807 897 -1889 C ATOM 3775 CG2 ILE B 564 13.361 54.252 24.882 1.00 72.07 C ANISOU 3775 CG2 ILE B 564 6169 11793 9420 954 1181 -1764 C ATOM 3776 CD1 ILE B 564 12.695 54.126 27.813 1.00 96.61 C ANISOU 3776 CD1 ILE B 564 9150 15218 12341 738 911 -2054 C ATOM 3777 N LEU B 565 14.401 51.969 22.600 1.00 71.09 N ANISOU 3777 N LEU B 565 6319 11547 9146 1137 1238 -1418 N ATOM 3778 CA LEU B 565 14.996 52.326 21.318 1.00 70.00 C ANISOU 3778 CA LEU B 565 6210 11246 9142 1237 1400 -1313 C ATOM 3779 C LEU B 565 14.427 53.647 20.819 1.00 74.53 C ANISOU 3779 C LEU B 565 6751 11734 9832 1266 1526 -1322 C ATOM 3780 O LEU B 565 13.223 53.773 20.605 1.00 77.05 O ANISOU 3780 O LEU B 565 7148 12097 10029 1269 1512 -1304 O ATOM 3781 CB LEU B 565 14.761 51.220 20.291 1.00 65.64 C ANISOU 3781 CB LEU B 565 5834 10685 8420 1312 1404 -1168 C ATOM 3782 CG LEU B 565 15.612 49.967 20.497 1.00 61.31 C ANISOU 3782 CG LEU B 565 5309 10170 7816 1307 1324 -1133 C ATOM 3783 CD1 LEU B 565 15.109 48.823 19.637 1.00 60.02 C ANISOU 3783 CD1 LEU B 565 5325 10026 7455 1367 1301 -1013 C ATOM 3784 CD2 LEU B 565 17.074 50.268 20.202 1.00 59.69 C ANISOU 3784 CD2 LEU B 565 5008 9833 7837 1343 1428 -1119 C ATOM 3785 N SER B 566 15.300 54.632 20.638 1.00 70.26 N ANISOU 3785 N SER B 566 6088 11066 9542 1287 1649 -1347 N ATOM 3786 CA SER B 566 14.863 55.967 20.251 1.00 75.83 C ANISOU 3786 CA SER B 566 6736 11680 10394 1310 1774 -1361 C ATOM 3787 C SER B 566 15.641 56.502 19.056 1.00 83.41 C ANISOU 3787 C SER B 566 7693 12463 11535 1410 1960 -1251 C ATOM 3788 O SER B 566 16.707 55.993 18.714 1.00 82.87 O ANISOU 3788 O SER B 566 7627 12333 11526 1448 1998 -1196 O ATOM 3789 CB SER B 566 14.995 56.933 21.429 1.00 77.82 C ANISOU 3789 CB SER B 566 6805 11956 10806 1220 1744 -1535 C ATOM 3790 OG SER B 566 16.355 57.133 21.773 1.00 79.62 O ANISOU 3790 OG SER B 566 6900 12115 11237 1208 1770 -1587 O ATOM 3791 N SER B 567 15.093 57.536 18.427 1.00117.82 N ANISOU 3791 N SER B 567 12045 16737 15985 1452 2079 -1216 N ATOM 3792 CA SER B 567 15.728 58.170 17.279 1.00121.49 C ANISOU 3792 CA SER B 567 12506 17030 16624 1550 2270 -1104 C ATOM 3793 C SER B 567 16.359 59.500 17.677 1.00123.33 C ANISOU 3793 C SER B 567 12537 17155 17168 1525 2369 -1196 C ATOM 3794 O SER B 567 16.053 60.049 18.737 1.00121.93 O ANISOU 3794 O SER B 567 12239 17037 17053 1437 2295 -1345 O ATOM 3795 CB SER B 567 14.707 58.387 16.159 1.00119.69 C ANISOU 3795 CB SER B 567 12419 16772 16286 1628 2343 -976 C ATOM 3796 OG SER B 567 15.286 59.083 15.069 1.00120.86 O ANISOU 3796 OG SER B 567 12562 16758 16602 1723 2535 -863 O ATOM 3797 N THR B 574 18.724 59.832 9.006 1.00135.32 N ANISOU 3797 N THR B 574 14690 17913 18813 2271 3454 -127 N ATOM 3798 CA THR B 574 18.550 58.417 9.312 1.00133.88 C ANISOU 3798 CA THR B 574 14623 17866 18378 2238 3287 -161 C ATOM 3799 C THR B 574 19.891 57.783 9.684 1.00130.04 C ANISOU 3799 C THR B 574 14062 17342 18007 2219 3297 -202 C ATOM 3800 O THR B 574 20.937 58.427 9.587 1.00129.39 O ANISOU 3800 O THR B 574 13851 17121 18189 2241 3442 -192 O ATOM 3801 CB THR B 574 17.920 57.656 8.124 1.00136.50 C ANISOU 3801 CB THR B 574 15198 18236 18430 2330 3299 -21 C ATOM 3802 OG1 THR B 574 16.869 58.444 7.550 1.00136.19 O ANISOU 3802 OG1 THR B 574 15217 18190 18340 2371 3337 47 O ATOM 3803 CG2 THR B 574 17.352 56.319 8.579 1.00134.69 C ANISOU 3803 CG2 THR B 574 15078 18166 17933 2279 3094 -76 C ATOM 3804 N HIS B 575 19.850 56.523 10.111 1.00114.55 N ANISOU 3804 N HIS B 575 12173 15496 15854 2178 3141 -244 N ATOM 3805 CA HIS B 575 21.047 55.805 10.541 1.00107.92 C ANISOU 3805 CA HIS B 575 11265 14634 15107 2152 3122 -285 C ATOM 3806 C HIS B 575 21.671 56.476 11.761 1.00 99.00 C ANISOU 3806 C HIS B 575 9902 13482 14231 2060 3077 -429 C ATOM 3807 O HIS B 575 22.822 56.907 11.727 1.00 95.78 O ANISOU 3807 O HIS B 575 9368 12944 14080 2076 3197 -430 O ATOM 3808 CB HIS B 575 22.066 55.716 9.401 1.00111.78 C ANISOU 3808 CB HIS B 575 11803 14975 15692 2258 3327 -156 C ATOM 3809 CG HIS B 575 23.216 54.802 9.688 1.00114.03 C ANISOU 3809 CG HIS B 575 12046 15237 16041 2243 3306 -179 C ATOM 3810 ND1 HIS B 575 23.217 53.472 9.330 1.00115.07 N ANISOU 3810 ND1 HIS B 575 12329 15432 15959 2267 3243 -134 N ATOM 3811 CD2 HIS B 575 24.404 55.027 10.299 1.00114.50 C ANISOU 3811 CD2 HIS B 575 11925 15213 16367 2205 3337 -245 C ATOM 3812 CE1 HIS B 575 24.355 52.916 9.708 1.00114.69 C ANISOU 3812 CE1 HIS B 575 12194 15339 16043 2246 3240 -166 C ATOM 3813 NE2 HIS B 575 25.092 53.839 10.298 1.00114.49 N ANISOU 3813 NE2 HIS B 575 11967 15225 16307 2208 3293 -232 N ATOM 3814 N ASN B 576 20.901 56.557 12.842 1.00109.97 N ANISOU 3814 N ASN B 576 11236 14999 15549 1962 2905 -554 N ATOM 3815 CA ASN B 576 21.343 57.255 14.042 1.00106.16 C ANISOU 3815 CA ASN B 576 10541 14513 15283 1870 2849 -705 C ATOM 3816 C ASN B 576 20.587 56.822 15.296 1.00100.49 C ANISOU 3816 C ASN B 576 9803 13974 14406 1760 2624 -840 C ATOM 3817 O ASN B 576 20.720 57.439 16.353 1.00101.48 O ANISOU 3817 O ASN B 576 9766 14122 14669 1677 2559 -980 O ATOM 3818 CB ASN B 576 21.213 58.767 13.844 1.00107.49 C ANISOU 3818 CB ASN B 576 10595 14569 15677 1888 2989 -714 C ATOM 3819 CG ASN B 576 19.892 59.158 13.206 1.00106.68 C ANISOU 3819 CG ASN B 576 10616 14500 15417 1927 3013 -642 C ATOM 3820 OD1 ASN B 576 18.850 58.572 13.500 1.00103.90 O ANISOU 3820 OD1 ASN B 576 10368 14291 14819 1890 2866 -667 O ATOM 3821 ND2 ASN B 576 19.930 60.154 12.327 1.00108.81 N ANISOU 3821 ND2 ASN B 576 10871 14634 15837 2003 3199 -548 N ATOM 3822 N GLY B 577 19.797 55.760 15.172 1.00 90.81 N ANISOU 3822 N GLY B 577 8742 12871 12889 1760 2508 -799 N ATOM 3823 CA GLY B 577 19.027 55.246 16.290 1.00 85.35 C ANISOU 3823 CA GLY B 577 8051 12352 12025 1662 2303 -908 C ATOM 3824 C GLY B 577 19.894 54.928 17.494 1.00 79.50 C ANISOU 3824 C GLY B 577 7170 11658 11380 1577 2188 -1028 C ATOM 3825 O GLY B 577 21.078 54.629 17.352 1.00 77.95 O ANISOU 3825 O GLY B 577 6922 11379 11318 1600 2237 -1003 O ATOM 3826 N LYS B 578 19.302 54.994 18.682 1.00 87.07 N ANISOU 3826 N LYS B 578 8067 12748 12269 1478 2035 -1158 N ATOM 3827 CA LYS B 578 20.032 54.732 19.917 1.00 81.90 C ANISOU 3827 CA LYS B 578 7280 12156 11683 1391 1907 -1281 C ATOM 3828 C LYS B 578 19.313 53.710 20.792 1.00 77.13 C ANISOU 3828 C LYS B 578 6746 11740 10818 1319 1705 -1327 C ATOM 3829 O LYS B 578 18.099 53.529 20.687 1.00 76.06 O ANISOU 3829 O LYS B 578 6721 11692 10485 1314 1660 -1307 O ATOM 3830 CB LYS B 578 20.240 56.029 20.703 1.00 79.93 C ANISOU 3830 CB LYS B 578 6841 11871 11659 1333 1927 -1424 C ATOM 3831 CG LYS B 578 20.871 57.154 19.900 1.00 80.58 C ANISOU 3831 CG LYS B 578 6835 11760 12020 1400 2131 -1383 C ATOM 3832 CD LYS B 578 21.160 58.359 20.780 1.00 80.38 C ANISOU 3832 CD LYS B 578 6606 11701 12235 1335 2135 -1542 C ATOM 3833 CE LYS B 578 21.610 59.554 19.958 1.00 82.95 C ANISOU 3833 CE LYS B 578 6844 11832 12840 1403 2345 -1495 C ATOM 3834 NZ LYS B 578 20.551 60.004 19.013 1.00 83.96 N ANISOU 3834 NZ LYS B 578 7088 11932 12882 1465 2452 -1392 N ATOM 3835 N LEU B 579 20.073 53.042 21.654 1.00 73.20 N ANISOU 3835 N LEU B 579 6182 11303 10330 1263 1585 -1384 N ATOM 3836 CA LEU B 579 19.505 52.091 22.600 1.00 71.15 C ANISOU 3836 CA LEU B 579 5970 11222 9842 1189 1392 -1429 C ATOM 3837 C LEU B 579 19.752 52.544 24.035 1.00 75.10 C ANISOU 3837 C LEU B 579 6315 11807 10412 1086 1274 -1595 C ATOM 3838 O LEU B 579 20.896 52.739 24.445 1.00 79.13 O ANISOU 3838 O LEU B 579 6695 12263 11110 1068 1268 -1649 O ATOM 3839 CB LEU B 579 20.098 50.699 22.391 1.00 66.37 C ANISOU 3839 CB LEU B 579 5443 10635 9141 1213 1329 -1338 C ATOM 3840 CG LEU B 579 19.657 49.659 23.423 1.00 61.05 C ANISOU 3840 CG LEU B 579 4804 10139 8252 1136 1128 -1376 C ATOM 3841 CD1 LEU B 579 18.140 49.560 23.456 1.00 56.69 C ANISOU 3841 CD1 LEU B 579 4366 9698 7475 1119 1080 -1373 C ATOM 3842 CD2 LEU B 579 20.284 48.302 23.143 1.00 59.65 C ANISOU 3842 CD2 LEU B 579 4696 9962 8008 1165 1079 -1277 C ATOM 3843 N TYR B 580 18.675 52.709 24.794 1.00 79.13 N ANISOU 3843 N TYR B 580 6841 12453 10773 1020 1181 -1678 N ATOM 3844 CA TYR B 580 18.778 53.140 26.182 1.00 76.80 C ANISOU 3844 CA TYR B 580 6413 12255 10510 921 1066 -1843 C ATOM 3845 C TYR B 580 18.320 52.047 27.143 1.00 72.01 C ANISOU 3845 C TYR B 580 5868 11838 9656 852 878 -1864 C ATOM 3846 O TYR B 580 17.306 51.392 26.913 1.00 73.51 O ANISOU 3846 O TYR B 580 6194 12106 9630 860 843 -1796 O ATOM 3847 CB TYR B 580 17.955 54.411 26.410 1.00 79.92 C ANISOU 3847 CB TYR B 580 6750 12649 10968 891 1124 -1947 C ATOM 3848 CG TYR B 580 18.538 55.655 25.775 1.00 83.50 C ANISOU 3848 CG TYR B 580 7094 12923 11709 939 1294 -1961 C ATOM 3849 CD1 TYR B 580 19.745 56.182 26.216 1.00 85.89 C ANISOU 3849 CD1 TYR B 580 7231 13149 12252 918 1305 -2048 C ATOM 3850 CD2 TYR B 580 17.875 56.310 24.746 1.00 83.90 C ANISOU 3850 CD2 TYR B 580 7202 12877 11798 1005 1441 -1884 C ATOM 3851 CE1 TYR B 580 20.281 57.320 25.644 1.00 87.60 C ANISOU 3851 CE1 TYR B 580 7341 13195 12750 962 1466 -2058 C ATOM 3852 CE2 TYR B 580 18.403 57.451 24.168 1.00 86.55 C ANISOU 3852 CE2 TYR B 580 7436 13046 12404 1050 1602 -1887 C ATOM 3853 CZ TYR B 580 19.606 57.951 24.621 1.00 89.09 C ANISOU 3853 CZ TYR B 580 7590 13290 12969 1028 1618 -1974 C ATOM 3854 OH TYR B 580 20.137 59.085 24.051 1.00 91.23 O ANISOU 3854 OH TYR B 580 7751 13386 13524 1073 1783 -1974 O ATOM 3855 N LYS B 581 19.076 51.852 28.218 1.00 61.74 N ANISOU 3855 N LYS B 581 4464 10606 8390 786 757 -1956 N ATOM 3856 CA LYS B 581 18.694 50.905 29.258 1.00 54.79 C ANISOU 3856 CA LYS B 581 3625 9910 7283 715 576 -1983 C ATOM 3857 C LYS B 581 18.028 51.640 30.414 1.00 52.13 C ANISOU 3857 C LYS B 581 3219 9696 6893 627 506 -2146 C ATOM 3858 O LYS B 581 18.441 52.741 30.777 1.00 48.30 O ANISOU 3858 O LYS B 581 2599 9160 6594 600 546 -2272 O ATOM 3859 CB LYS B 581 19.915 50.137 29.759 1.00 50.93 C ANISOU 3859 CB LYS B 581 3074 9435 6843 697 471 -1973 C ATOM 3860 CG LYS B 581 19.596 49.089 30.809 1.00 49.44 C ANISOU 3860 CG LYS B 581 2929 9433 6422 630 283 -1980 C ATOM 3861 CD LYS B 581 20.834 48.289 31.171 1.00 50.75 C ANISOU 3861 CD LYS B 581 3037 9597 6650 622 185 -1948 C ATOM 3862 CE LYS B 581 20.490 47.105 32.057 1.00 50.59 C ANISOU 3862 CE LYS B 581 3078 9753 6389 568 8 -1918 C ATOM 3863 NZ LYS B 581 21.677 46.237 32.290 1.00 50.74 N ANISOU 3863 NZ LYS B 581 3048 9758 6473 569 -85 -1862 N ATOM 3864 N ILE B 582 16.991 51.035 30.985 1.00 48.32 N ANISOU 3864 N ILE B 582 2827 9369 6162 581 408 -2147 N ATOM 3865 CA ILE B 582 16.285 51.643 32.108 1.00 52.17 C ANISOU 3865 CA ILE B 582 3263 9985 6573 496 344 -2300 C ATOM 3866 C ILE B 582 16.797 51.090 33.433 1.00 56.62 C ANISOU 3866 C ILE B 582 3773 10697 7043 418 170 -2377 C ATOM 3867 O ILE B 582 16.762 49.882 33.668 1.00 54.32 O ANISOU 3867 O ILE B 582 3563 10500 6578 411 64 -2288 O ATOM 3868 CB ILE B 582 14.767 51.413 32.019 1.00 50.38 C ANISOU 3868 CB ILE B 582 3160 9844 6137 488 347 -2265 C ATOM 3869 CG1 ILE B 582 14.231 51.892 30.669 1.00 48.75 C ANISOU 3869 CG1 ILE B 582 3017 9496 6009 570 505 -2176 C ATOM 3870 CG2 ILE B 582 14.060 52.121 33.162 1.00 49.64 C ANISOU 3870 CG2 ILE B 582 3006 9873 5983 401 300 -2431 C ATOM 3871 CD1 ILE B 582 12.753 51.637 30.474 1.00 46.50 C ANISOU 3871 CD1 ILE B 582 2852 9279 5536 569 507 -2132 C ATOM 3872 N VAL B 583 17.274 51.981 34.294 1.00 80.11 N ANISOU 3872 N VAL B 583 6609 13693 10136 361 140 -2543 N ATOM 3873 CA VAL B 583 17.809 51.581 35.590 1.00 85.28 C ANISOU 3873 CA VAL B 583 7204 14491 10709 286 -30 -2630 C ATOM 3874 C VAL B 583 17.138 52.338 36.735 1.00 77.93 C ANISOU 3874 C VAL B 583 6220 13691 9697 201 -79 -2812 C ATOM 3875 O VAL B 583 16.775 53.506 36.591 1.00 75.26 O ANISOU 3875 O VAL B 583 5820 13287 9487 197 26 -2915 O ATOM 3876 CB VAL B 583 19.337 51.783 35.654 1.00 93.22 C ANISOU 3876 CB VAL B 583 8075 15399 11943 296 -54 -2665 C ATOM 3877 CG1 VAL B 583 20.025 50.932 34.598 1.00 91.42 C ANISOU 3877 CG1 VAL B 583 7902 15051 11783 376 -10 -2485 C ATOM 3878 CG2 VAL B 583 19.691 53.251 35.472 1.00 97.18 C ANISOU 3878 CG2 VAL B 583 8440 15770 12713 300 61 -2795 C ATOM 3879 N ASP B 584 16.971 51.665 37.870 1.00 50.81 N ANISOU 3879 N ASP B 584 2812 10442 6052 134 -234 -2850 N ATOM 3880 CA ASP B 584 16.317 52.269 39.025 1.00 52.89 C ANISOU 3880 CA ASP B 584 3039 10850 6206 51 -286 -3021 C ATOM 3881 C ASP B 584 17.345 52.822 40.006 1.00 52.59 C ANISOU 3881 C ASP B 584 2856 10849 6277 -4 -382 -3187 C ATOM 3882 O ASP B 584 18.116 52.066 40.594 1.00 53.34 O ANISOU 3882 O ASP B 584 2937 11021 6309 -24 -524 -3163 O ATOM 3883 CB ASP B 584 15.416 51.251 39.723 1.00 58.15 C ANISOU 3883 CB ASP B 584 3826 11708 6559 9 -391 -2967 C ATOM 3884 CG ASP B 584 14.536 51.883 40.780 1.00 62.73 C ANISOU 3884 CG ASP B 584 4392 12431 7013 -70 -413 -3132 C ATOM 3885 OD1 ASP B 584 14.573 53.122 40.919 1.00 63.57 O ANISOU 3885 OD1 ASP B 584 4395 12481 7277 -90 -342 -3290 O ATOM 3886 OD2 ASP B 584 13.808 51.140 41.473 1.00 64.57 O ANISOU 3886 OD2 ASP B 584 4713 12828 6994 -111 -494 -3104 O ATOM 3887 N PRO B 585 17.350 54.150 40.189 1.00 66.79 N ANISOU 3887 N PRO B 585 4541 12590 8246 -28 -309 -3359 N ATOM 3888 CA PRO B 585 18.343 54.833 41.028 1.00 69.01 C ANISOU 3888 CA PRO B 585 4668 12881 8671 -75 -388 -3536 C ATOM 3889 C PRO B 585 18.372 54.290 42.454 1.00 78.40 C ANISOU 3889 C PRO B 585 5868 14293 9628 -156 -578 -3621 C ATOM 3890 O PRO B 585 19.400 54.384 43.129 1.00 81.79 O ANISOU 3890 O PRO B 585 6194 14748 10133 -186 -694 -3713 O ATOM 3891 CB PRO B 585 17.858 56.287 41.031 1.00 68.67 C ANISOU 3891 CB PRO B 585 4536 12771 8786 -95 -266 -3704 C ATOM 3892 CG PRO B 585 17.025 56.417 39.798 1.00 66.11 C ANISOU 3892 CG PRO B 585 4294 12324 8499 -28 -97 -3574 C ATOM 3893 CD PRO B 585 16.365 55.088 39.623 1.00 65.09 C ANISOU 3893 CD PRO B 585 4335 12297 8101 -12 -151 -3398 C ATOM 3894 N LYS B 586 17.253 53.727 42.901 1.00 85.16 N ANISOU 3894 N LYS B 586 6847 15306 10204 -188 -611 -3586 N ATOM 3895 CA LYS B 586 17.139 53.210 44.261 1.00 87.68 C ANISOU 3895 CA LYS B 586 7192 15849 10273 -263 -777 -3657 C ATOM 3896 C LYS B 586 17.836 51.861 44.413 1.00 87.39 C ANISOU 3896 C LYS B 586 7206 15875 10122 -250 -920 -3502 C ATOM 3897 O LYS B 586 17.707 51.193 45.438 1.00 97.14 O ANISOU 3897 O LYS B 586 8487 17298 11123 -301 -1062 -3509 O ATOM 3898 CB LYS B 586 15.668 53.097 44.661 1.00 89.75 C ANISOU 3898 CB LYS B 586 7565 16247 10290 -300 -745 -3668 C ATOM 3899 CG LYS B 586 14.917 54.419 44.610 1.00 94.68 C ANISOU 3899 CG LYS B 586 8136 16820 11020 -320 -610 -3829 C ATOM 3900 CD LYS B 586 13.454 54.243 44.976 1.00 99.70 C ANISOU 3900 CD LYS B 586 8880 17581 11420 -354 -574 -3829 C ATOM 3901 CE LYS B 586 12.719 55.574 44.956 1.00102.36 C ANISOU 3901 CE LYS B 586 9154 17862 11877 -376 -441 -3994 C ATOM 3902 NZ LYS B 586 11.275 55.420 45.287 1.00103.25 N ANISOU 3902 NZ LYS B 586 9366 18086 11778 -409 -397 -3993 N ATOM 3903 N ARG B 587 18.579 51.475 43.383 1.00 67.72 N ANISOU 3903 N ARG B 587 4705 13222 7801 -178 -877 -3360 N ATOM 3904 CA ARG B 587 19.296 50.207 43.364 1.00 61.60 C ANISOU 3904 CA ARG B 587 3970 12474 6962 -157 -994 -3202 C ATOM 3905 C ARG B 587 20.575 50.367 42.554 1.00 60.48 C ANISOU 3905 C ARG B 587 3729 12136 7114 -99 -955 -3159 C ATOM 3906 O ARG B 587 20.656 51.236 41.685 1.00 60.96 O ANISOU 3906 O ARG B 587 3738 12026 7397 -56 -803 -3186 O ATOM 3907 CB ARG B 587 18.426 49.124 42.731 1.00 60.84 C ANISOU 3907 CB ARG B 587 4031 12397 6688 -117 -954 -3003 C ATOM 3908 CG ARG B 587 17.150 48.823 43.492 1.00 60.12 C ANISOU 3908 CG ARG B 587 4042 12493 6308 -170 -989 -3021 C ATOM 3909 CD ARG B 587 17.333 47.627 44.399 1.00 64.52 C ANISOU 3909 CD ARG B 587 4652 13224 6640 -206 -1164 -2942 C ATOM 3910 NE ARG B 587 17.391 46.383 43.638 1.00 63.22 N ANISOU 3910 NE ARG B 587 4575 13007 6438 -149 -1169 -2722 N ATOM 3911 CZ ARG B 587 17.479 45.176 44.185 1.00 68.70 C ANISOU 3911 CZ ARG B 587 5327 13823 6952 -165 -1302 -2607 C ATOM 3912 NH1 ARG B 587 17.524 45.044 45.504 1.00 79.09 N ANISOU 3912 NH1 ARG B 587 6628 15327 8095 -235 -1443 -2683 N ATOM 3913 NH2 ARG B 587 17.524 44.098 43.414 1.00 64.53 N ANISOU 3913 NH2 ARG B 587 4872 13229 6415 -111 -1292 -2415 N ATOM 3914 N PRO B 588 21.583 49.530 42.837 1.00 56.35 N ANISOU 3914 N PRO B 588 3178 11633 6600 -97 -1090 -3086 N ATOM 3915 CA PRO B 588 22.827 49.543 42.060 1.00 58.09 C ANISOU 3915 CA PRO B 588 3308 11665 7100 -40 -1054 -3027 C ATOM 3916 C PRO B 588 22.560 49.178 40.600 1.00 57.36 C ANISOU 3916 C PRO B 588 3302 11413 7080 46 -891 -2852 C ATOM 3917 O PRO B 588 21.499 48.630 40.297 1.00 55.01 O ANISOU 3917 O PRO B 588 3141 11174 6588 59 -850 -2755 O ATOM 3918 CB PRO B 588 23.670 48.451 42.729 1.00 57.16 C ANISOU 3918 CB PRO B 588 3179 11638 6903 -60 -1245 -2954 C ATOM 3919 CG PRO B 588 23.089 48.294 44.091 1.00 58.19 C ANISOU 3919 CG PRO B 588 3343 12005 6760 -141 -1393 -3045 C ATOM 3920 CD PRO B 588 21.625 48.550 43.934 1.00 57.36 C ANISOU 3920 CD PRO B 588 3350 11961 6484 -149 -1282 -3055 C ATOM 3921 N LEU B 589 23.504 49.481 39.713 1.00 65.62 N ANISOU 3921 N LEU B 589 4269 12261 8404 106 -799 -2816 N ATOM 3922 CA LEU B 589 23.356 49.153 38.297 1.00 63.51 C ANISOU 3922 CA LEU B 589 4083 11837 8210 192 -641 -2652 C ATOM 3923 C LEU B 589 23.315 47.643 38.085 1.00 54.62 C ANISOU 3923 C LEU B 589 3072 10763 6917 217 -713 -2467 C ATOM 3924 O LEU B 589 22.812 47.157 37.071 1.00 51.30 O ANISOU 3924 O LEU B 589 2763 10274 6454 277 -607 -2330 O ATOM 3925 CB LEU B 589 24.492 49.766 37.474 1.00 64.88 C ANISOU 3925 CB LEU B 589 4140 11791 8720 249 -530 -2652 C ATOM 3926 CG LEU B 589 24.454 51.278 37.243 1.00 67.17 C ANISOU 3926 CG LEU B 589 4328 11972 9223 251 -398 -2794 C ATOM 3927 CD1 LEU B 589 25.724 51.742 36.545 1.00 69.59 C ANISOU 3927 CD1 LEU B 589 4507 12066 9868 304 -308 -2784 C ATOM 3928 CD2 LEU B 589 23.224 51.673 36.438 1.00 66.44 C ANISOU 3928 CD2 LEU B 589 4344 11847 9055 286 -239 -2751 C ATOM 3929 N MET B 590 23.851 46.909 39.053 1.00 53.59 N ANISOU 3929 N MET B 590 2913 10754 6695 170 -896 -2465 N ATOM 3930 CA MET B 590 23.866 45.455 38.995 1.00 53.16 C ANISOU 3930 CA MET B 590 2951 10756 6490 186 -981 -2295 C ATOM 3931 C MET B 590 23.869 44.858 40.396 1.00 53.69 C ANISOU 3931 C MET B 590 3014 11033 6354 110 -1191 -2328 C ATOM 3932 O MET B 590 24.921 44.473 40.909 1.00 56.37 O ANISOU 3932 O MET B 590 3268 11383 6769 94 -1320 -2323 O ATOM 3933 CB MET B 590 25.085 44.962 38.216 1.00 53.56 C ANISOU 3933 CB MET B 590 2950 10639 6762 247 -953 -2187 C ATOM 3934 CG MET B 590 25.112 43.457 38.012 1.00 73.80 C ANISOU 3934 CG MET B 590 5606 13235 9198 271 -1021 -2005 C ATOM 3935 SD MET B 590 23.664 42.871 37.115 1.00 88.26 S ANISOU 3935 SD MET B 590 7630 15080 10823 315 -905 -1879 S ATOM 3936 CE MET B 590 23.838 43.775 35.578 1.00 49.78 C ANISOU 3936 CE MET B 590 2750 9970 6193 401 -665 -1871 C ATOM 3937 N PRO B 591 22.688 44.787 41.024 1.00 63.10 N ANISOU 3937 N PRO B 591 4294 12392 7287 63 -1225 -2360 N ATOM 3938 CA PRO B 591 22.574 44.145 42.334 1.00 65.25 C ANISOU 3938 CA PRO B 591 4583 12876 7333 -5 -1414 -2372 C ATOM 3939 C PRO B 591 23.187 42.752 42.297 1.00 69.15 C ANISOU 3939 C PRO B 591 5104 13377 7793 16 -1521 -2198 C ATOM 3940 O PRO B 591 23.071 42.050 41.297 1.00 72.21 O ANISOU 3940 O PRO B 591 5563 13661 8210 77 -1437 -2047 O ATOM 3941 CB PRO B 591 21.062 44.058 42.546 1.00 62.43 C ANISOU 3941 CB PRO B 591 4352 12647 6721 -30 -1374 -2369 C ATOM 3942 CG PRO B 591 20.517 45.203 41.771 1.00 64.06 C ANISOU 3942 CG PRO B 591 4553 12735 7052 -3 -1193 -2454 C ATOM 3943 CD PRO B 591 21.400 45.328 40.558 1.00 64.78 C ANISOU 3943 CD PRO B 591 4595 12604 7414 73 -1085 -2385 C ATOM 3944 N GLU B 592 23.842 42.368 43.384 1.00 64.77 N ANISOU 3944 N GLU B 592 4490 12944 7177 -33 -1706 -2220 N ATOM 3945 CA GLU B 592 24.529 41.086 43.458 1.00 65.43 C ANISOU 3945 CA GLU B 592 4577 13034 7248 -18 -1823 -2061 C ATOM 3946 C GLU B 592 23.594 39.924 43.129 1.00 60.49 C ANISOU 3946 C GLU B 592 4098 12463 6421 3 -1803 -1888 C ATOM 3947 O GLU B 592 24.030 38.900 42.606 1.00 56.68 O ANISOU 3947 O GLU B 592 3637 11908 5991 45 -1818 -1731 O ATOM 3948 CB GLU B 592 25.153 40.898 44.844 1.00 78.99 C ANISOU 3948 CB GLU B 592 6222 14912 8879 -84 -2041 -2119 C ATOM 3949 CG GLU B 592 26.309 41.855 45.167 1.00 86.89 C ANISOU 3949 CG GLU B 592 7060 15844 10111 -101 -2092 -2274 C ATOM 3950 CD GLU B 592 25.917 43.329 45.111 1.00 85.31 C ANISOU 3950 CD GLU B 592 6817 15610 9989 -117 -1977 -2471 C ATOM 3951 OE1 GLU B 592 25.881 43.894 43.997 1.00 89.60 O ANISOU 3951 OE1 GLU B 592 7350 15972 10721 -64 -1797 -2471 O ATOM 3952 OE2 GLU B 592 25.666 43.929 46.179 1.00 77.32 O ANISOU 3952 OE2 GLU B 592 5777 14749 8853 -183 -2066 -2626 O ATOM 3953 N GLU B 593 22.307 40.087 43.426 1.00 76.60 N ANISOU 3953 N GLU B 593 6235 14624 8246 -26 -1766 -1921 N ATOM 3954 CA GLU B 593 21.329 39.030 43.176 1.00 76.86 C ANISOU 3954 CA GLU B 593 6403 14713 8088 -10 -1748 -1769 C ATOM 3955 C GLU B 593 20.930 38.953 41.706 1.00 76.88 C ANISOU 3955 C GLU B 593 6473 14541 8196 66 -1571 -1685 C ATOM 3956 O GLU B 593 20.327 37.973 41.269 1.00 74.86 O ANISOU 3956 O GLU B 593 6318 14288 7837 93 -1553 -1544 O ATOM 3957 CB GLU B 593 20.088 39.193 44.069 1.00 73.79 C ANISOU 3957 CB GLU B 593 6090 14517 7432 -70 -1774 -1831 C ATOM 3958 CG GLU B 593 19.288 40.474 43.857 1.00 75.56 C ANISOU 3958 CG GLU B 593 6319 14718 7671 -79 -1638 -1984 C ATOM 3959 CD GLU B 593 17.997 40.504 44.669 1.00 84.86 C ANISOU 3959 CD GLU B 593 7580 16078 8586 -134 -1651 -2027 C ATOM 3960 OE1 GLU B 593 17.374 41.582 44.772 1.00 84.37 O ANISOU 3960 OE1 GLU B 593 7509 16027 8521 -157 -1566 -2172 O ATOM 3961 OE2 GLU B 593 17.605 39.448 45.209 1.00 91.41 O ANISOU 3961 OE2 GLU B 593 8479 17033 9219 -153 -1741 -1913 O ATOM 3962 N CYS B 594 21.275 39.988 40.948 1.00 71.54 N ANISOU 3962 N CYS B 594 5741 13713 7729 100 -1443 -1772 N ATOM 3963 CA CYS B 594 20.932 40.053 39.531 1.00 71.72 C ANISOU 3963 CA CYS B 594 5827 13569 7854 175 -1269 -1704 C ATOM 3964 C CYS B 594 22.042 39.475 38.659 1.00 71.04 C ANISOU 3964 C CYS B 594 5705 13317 7969 238 -1242 -1594 C ATOM 3965 O CYS B 594 21.872 39.310 37.450 1.00 64.21 O ANISOU 3965 O CYS B 594 4902 12315 7179 307 -1108 -1514 O ATOM 3966 CB CYS B 594 20.639 41.498 39.119 1.00 71.91 C ANISOU 3966 CB CYS B 594 5815 13513 7994 183 -1129 -1844 C ATOM 3967 SG CYS B 594 19.237 42.239 39.985 1.00 63.12 S ANISOU 3967 SG CYS B 594 4747 12569 6666 114 -1128 -1977 S ATOM 3968 N ARG B 595 23.174 39.166 39.283 1.00 75.69 N ANISOU 3968 N ARG B 595 6194 13920 8643 216 -1369 -1593 N ATOM 3969 CA ARG B 595 24.324 38.627 38.566 1.00 75.71 C ANISOU 3969 CA ARG B 595 6145 13765 8855 270 -1352 -1497 C ATOM 3970 C ARG B 595 24.066 37.230 38.021 1.00 76.46 C ANISOU 3970 C ARG B 595 6341 13844 8866 310 -1356 -1316 C ATOM 3971 O ARG B 595 23.268 36.471 38.570 1.00 80.45 O ANISOU 3971 O ARG B 595 6925 14492 9149 279 -1440 -1255 O ATOM 3972 CB ARG B 595 25.562 38.617 39.460 1.00 77.53 C ANISOU 3972 CB ARG B 595 6238 14023 9197 231 -1505 -1542 C ATOM 3973 CG ARG B 595 26.156 39.988 39.685 1.00 83.91 C ANISOU 3973 CG ARG B 595 6921 14776 10184 213 -1477 -1715 C ATOM 3974 CD ARG B 595 27.656 39.908 39.873 1.00 93.43 C ANISOU 3974 CD ARG B 595 7984 15894 11622 216 -1560 -1719 C ATOM 3975 NE ARG B 595 28.292 41.168 39.510 1.00101.31 N ANISOU 3975 NE ARG B 595 8867 16750 12874 232 -1460 -1848 N ATOM 3976 CZ ARG B 595 28.497 41.561 38.257 1.00104.84 C ANISOU 3976 CZ ARG B 595 9315 17001 13516 302 -1269 -1817 C ATOM 3977 NH1 ARG B 595 29.079 42.726 38.015 1.00106.90 N ANISOU 3977 NH1 ARG B 595 9464 17139 14013 312 -1183 -1935 N ATOM 3978 NH2 ARG B 595 28.116 40.792 37.246 1.00104.17 N ANISOU 3978 NH2 ARG B 595 9344 16844 13391 362 -1164 -1670 N ATOM 3979 N ALA B 596 24.758 36.898 36.937 1.00 72.95 N ANISOU 3979 N ALA B 596 5889 13221 8609 379 -1261 -1232 N ATOM 3980 CA ALA B 596 24.601 35.607 36.284 1.00 68.41 C ANISOU 3980 CA ALA B 596 5402 12604 7987 424 -1249 -1069 C ATOM 3981 C ALA B 596 25.744 35.384 35.303 1.00 72.33 C ANISOU 3981 C ALA B 596 5846 12900 8737 490 -1163 -1007 C ATOM 3982 O ALA B 596 25.803 36.029 34.258 1.00 74.84 O ANISOU 3982 O ALA B 596 6179 13074 9183 547 -995 -1030 O ATOM 3983 CB ALA B 596 23.265 35.542 35.565 1.00 59.05 C ANISOU 3983 CB ALA B 596 4361 11427 6650 454 -1137 -1037 C ATOM 3984 N THR B 597 26.651 34.473 35.644 1.00 71.70 N ANISOU 3984 N THR B 597 5702 12809 8731 485 -1275 -925 N ATOM 3985 CA THR B 597 27.808 34.189 34.800 1.00 71.88 C ANISOU 3985 CA THR B 597 5664 12642 9005 544 -1201 -865 C ATOM 3986 C THR B 597 27.403 34.048 33.337 1.00 74.28 C ANISOU 3986 C THR B 597 6077 12805 9341 625 -1007 -802 C ATOM 3987 O THR B 597 26.368 33.457 33.024 1.00 72.32 O ANISOU 3987 O THR B 597 5957 12613 8910 638 -987 -740 O ATOM 3988 CB THR B 597 28.537 32.915 35.253 1.00 75.05 C ANISOU 3988 CB THR B 597 6018 13059 9437 532 -1344 -749 C ATOM 3989 OG1 THR B 597 28.930 33.053 36.624 1.00 82.03 O ANISOU 3989 OG1 THR B 597 6804 14080 10282 458 -1533 -804 O ATOM 3990 CG2 THR B 597 29.771 32.679 34.401 1.00 73.61 C ANISOU 3990 CG2 THR B 597 5761 12671 9534 591 -1260 -696 C ATOM 3991 N VAL B 598 28.223 34.600 32.446 1.00 84.10 N ANISOU 3991 N VAL B 598 7269 13867 10819 681 -866 -820 N ATOM 3992 CA VAL B 598 27.924 34.601 31.016 1.00 76.78 C ANISOU 3992 CA VAL B 598 6443 12801 9929 763 -670 -769 C ATOM 3993 C VAL B 598 28.461 33.363 30.303 1.00 71.33 C ANISOU 3993 C VAL B 598 5783 12006 9313 816 -644 -638 C ATOM 3994 O VAL B 598 29.663 33.093 30.330 1.00 63.71 O ANISOU 3994 O VAL B 598 4712 10944 8553 825 -663 -610 O ATOM 3995 CB VAL B 598 28.493 35.855 30.321 1.00 74.93 C ANISOU 3995 CB VAL B 598 6148 12415 9909 804 -506 -848 C ATOM 3996 CG1 VAL B 598 28.388 35.716 28.813 1.00 77.74 C ANISOU 3996 CG1 VAL B 598 6605 12617 10316 897 -307 -775 C ATOM 3997 CG2 VAL B 598 27.769 37.102 30.800 1.00 72.23 C ANISOU 3997 CG2 VAL B 598 5797 12159 9488 764 -497 -976 C ATOM 3998 N GLN B 599 27.559 32.617 29.671 1.00 86.23 N ANISOU 3998 N GLN B 599 7812 13910 11041 849 -601 -561 N ATOM 3999 CA GLN B 599 27.935 31.465 28.860 1.00 93.19 C ANISOU 3999 CA GLN B 599 8739 14686 11983 905 -555 -445 C ATOM 4000 C GLN B 599 27.767 31.782 27.378 1.00 91.80 C ANISOU 4000 C GLN B 599 8660 14363 11857 992 -341 -433 C ATOM 4001 O GLN B 599 26.654 31.740 26.854 1.00 89.99 O ANISOU 4001 O GLN B 599 8564 14173 11454 1016 -288 -424 O ATOM 4002 CB GLN B 599 27.092 30.238 29.223 1.00 97.91 C ANISOU 4002 CB GLN B 599 9422 15404 12373 881 -672 -361 C ATOM 4003 CG GLN B 599 27.433 29.602 30.561 1.00105.92 C ANISOU 4003 CG GLN B 599 10346 16543 13355 808 -880 -332 C ATOM 4004 CD GLN B 599 26.730 30.274 31.724 1.00117.06 C ANISOU 4004 CD GLN B 599 11743 18137 14597 732 -993 -416 C ATOM 4005 OE1 GLN B 599 25.729 30.968 31.543 1.00121.04 O ANISOU 4005 OE1 GLN B 599 12328 18693 14970 732 -928 -478 O ATOM 4006 NE2 GLN B 599 27.248 30.064 32.930 1.00120.68 N ANISOU 4006 NE2 GLN B 599 12100 18695 15057 669 -1165 -418 N ATOM 4007 N PRO B 600 28.878 32.099 26.695 1.00 83.57 N ANISOU 4007 N PRO B 600 7549 13150 11053 1042 -218 -431 N ATOM 4008 CA PRO B 600 28.858 32.447 25.270 1.00 87.13 C ANISOU 4008 CA PRO B 600 8088 13454 11565 1130 -3 -415 C ATOM 4009 C PRO B 600 28.112 31.406 24.442 1.00 89.37 C ANISOU 4009 C PRO B 600 8527 13734 11697 1179 36 -332 C ATOM 4010 O PRO B 600 28.126 30.223 24.786 1.00 92.58 O ANISOU 4010 O PRO B 600 8938 14184 12055 1159 -75 -265 O ATOM 4011 CB PRO B 600 30.341 32.457 24.895 1.00 86.64 C ANISOU 4011 CB PRO B 600 7910 13218 11790 1166 79 -396 C ATOM 4012 CG PRO B 600 31.041 32.787 26.165 1.00 85.52 C ANISOU 4012 CG PRO B 600 7603 13135 11755 1091 -74 -451 C ATOM 4013 CD PRO B 600 30.242 32.126 27.251 1.00 83.57 C ANISOU 4013 CD PRO B 600 7384 13085 11284 1019 -278 -440 C ATOM 4014 N ALA B 601 27.465 31.847 23.367 1.00 76.81 N ANISOU 4014 N ALA B 601 7059 12091 10036 1241 189 -336 N ATOM 4015 CA ALA B 601 26.689 30.952 22.514 1.00 69.25 C ANISOU 4015 CA ALA B 601 6256 11129 8926 1291 228 -271 C ATOM 4016 C ALA B 601 27.574 29.886 21.879 1.00 66.88 C ANISOU 4016 C ALA B 601 5953 10704 8755 1340 278 -194 C ATOM 4017 O ALA B 601 28.661 30.184 21.381 1.00 66.29 O ANISOU 4017 O ALA B 601 5812 10486 8889 1380 396 -190 O ATOM 4018 CB ALA B 601 25.957 31.740 21.446 1.00 64.90 C ANISOU 4018 CB ALA B 601 5828 10535 8295 1354 387 -293 C ATOM 4019 N GLN B 602 27.099 28.645 21.894 1.00 67.85 N ANISOU 4019 N GLN B 602 6142 10876 8762 1336 193 -133 N ATOM 4020 CA GLN B 602 27.879 27.524 21.382 1.00 71.22 C ANISOU 4020 CA GLN B 602 6561 11193 9307 1375 224 -61 C ATOM 4021 C GLN B 602 27.230 26.873 20.164 1.00 73.59 C ANISOU 4021 C GLN B 602 7025 11442 9495 1448 325 -25 C ATOM 4022 O GLN B 602 26.017 26.949 19.972 1.00 71.84 O ANISOU 4022 O GLN B 602 6921 11307 9069 1451 308 -40 O ATOM 4023 CB GLN B 602 28.094 26.478 22.480 1.00 70.97 C ANISOU 4023 CB GLN B 602 6442 11243 9280 1308 30 -12 C ATOM 4024 CG GLN B 602 28.922 26.968 23.653 1.00 70.40 C ANISOU 4024 CG GLN B 602 6201 11209 9338 1241 -79 -41 C ATOM 4025 CD GLN B 602 30.365 27.226 23.278 1.00 69.74 C ANISOU 4025 CD GLN B 602 6007 10959 9534 1275 23 -39 C ATOM 4026 OE1 GLN B 602 30.902 26.600 22.364 1.00 70.45 O ANISOU 4026 OE1 GLN B 602 6124 10911 9732 1336 135 10 O ATOM 4027 NE2 GLN B 602 31.005 28.148 23.987 1.00 69.15 N ANISOU 4027 NE2 GLN B 602 5802 10890 9582 1235 -14 -98 N ATOM 4028 N THR B 603 28.059 26.233 19.346 1.00 87.32 N ANISOU 4028 N THR B 603 8769 13038 11372 1507 431 18 N ATOM 4029 CA THR B 603 27.590 25.503 18.175 1.00 85.85 C ANISOU 4029 CA THR B 603 8731 12792 11095 1579 525 48 C ATOM 4030 C THR B 603 26.593 24.421 18.574 1.00 81.32 C ANISOU 4030 C THR B 603 8220 12334 10346 1545 373 78 C ATOM 4031 O THR B 603 26.801 23.711 19.559 1.00 82.29 O ANISOU 4031 O THR B 603 8248 12516 10503 1483 220 114 O ATOM 4032 CB THR B 603 28.768 24.847 17.429 1.00 87.39 C ANISOU 4032 CB THR B 603 8896 12819 11490 1636 644 88 C ATOM 4033 OG1 THR B 603 29.594 25.864 16.849 1.00 85.85 O ANISOU 4033 OG1 THR B 603 8666 12503 11448 1682 818 63 O ATOM 4034 CG2 THR B 603 28.264 23.924 16.332 1.00 89.81 C ANISOU 4034 CG2 THR B 603 9354 13078 11692 1703 716 113 C ATOM 4035 N LEU B 604 25.512 24.298 17.809 1.00 59.52 N ANISOU 4035 N LEU B 604 5614 9599 7402 1587 413 68 N ATOM 4036 CA LEU B 604 24.503 23.275 18.069 1.00 59.78 C ANISOU 4036 CA LEU B 604 5711 9726 7275 1562 282 94 C ATOM 4037 C LEU B 604 25.137 21.896 18.218 1.00 61.32 C ANISOU 4037 C LEU B 604 5848 9868 7582 1556 223 156 C ATOM 4038 O LEU B 604 26.136 21.590 17.569 1.00 60.52 O ANISOU 4038 O LEU B 604 5723 9629 7643 1604 332 174 O ATOM 4039 CB LEU B 604 23.448 23.251 16.960 1.00 60.77 C ANISOU 4039 CB LEU B 604 6014 9847 7229 1626 359 74 C ATOM 4040 CG LEU B 604 22.358 24.320 17.030 1.00 56.97 C ANISOU 4040 CG LEU B 604 5601 9462 6582 1614 353 25 C ATOM 4041 CD1 LEU B 604 22.946 25.693 16.765 1.00 60.62 C ANISOU 4041 CD1 LEU B 604 6031 9868 7134 1637 485 -13 C ATOM 4042 CD2 LEU B 604 21.240 24.013 16.049 1.00 49.77 C ANISOU 4042 CD2 LEU B 604 4858 8556 5495 1670 385 15 C ATOM 4043 N THR B 605 24.552 21.068 19.076 1.00 90.42 N ANISOU 4043 N THR B 605 9508 13660 11189 1497 55 193 N ATOM 4044 CA THR B 605 25.085 19.736 19.326 1.00 92.42 C ANISOU 4044 CA THR B 605 9696 13871 11550 1485 -17 260 C ATOM 4045 C THR B 605 24.001 18.669 19.245 1.00 88.43 C ANISOU 4045 C THR B 605 9275 13422 10901 1483 -103 288 C ATOM 4046 O THR B 605 24.299 17.476 19.211 1.00 84.14 O ANISOU 4046 O THR B 605 8702 12827 10439 1487 -143 341 O ATOM 4047 CB THR B 605 25.767 19.650 20.705 1.00 94.96 C ANISOU 4047 CB THR B 605 9851 14254 11976 1405 -161 300 C ATOM 4048 OG1 THR B 605 24.802 19.891 21.737 1.00 93.52 O ANISOU 4048 OG1 THR B 605 9667 14244 11625 1336 -305 295 O ATOM 4049 CG2 THR B 605 26.889 20.674 20.811 1.00 95.31 C ANISOU 4049 CG2 THR B 605 9797 14233 12185 1406 -85 267 C ATOM 4050 N SER B 606 22.745 19.104 19.215 1.00 84.50 N ANISOU 4050 N SER B 606 8877 13025 10205 1476 -131 251 N ATOM 4051 CA SER B 606 21.615 18.179 19.188 1.00 81.27 C ANISOU 4051 CA SER B 606 8543 12674 9660 1470 -219 272 C ATOM 4052 C SER B 606 21.841 17.051 18.187 1.00 77.16 C ANISOU 4052 C SER B 606 8080 12032 9206 1533 -156 290 C ATOM 4053 O SER B 606 22.458 17.252 17.143 1.00 75.86 O ANISOU 4053 O SER B 606 7964 11746 9114 1602 -6 262 O ATOM 4054 CB SER B 606 20.310 18.919 18.878 1.00 77.07 C ANISOU 4054 CB SER B 606 8133 12222 8927 1481 -207 216 C ATOM 4055 OG SER B 606 20.404 19.645 17.666 1.00 70.81 O ANISOU 4055 OG SER B 606 7441 11343 8122 1557 -45 163 O ATOM 4056 N GLU B 607 21.342 15.865 18.520 1.00 69.98 N ANISOU 4056 N GLU B 607 7162 11153 8275 1509 -267 338 N ATOM 4057 CA GLU B 607 21.501 14.694 17.666 1.00 73.76 C ANISOU 4057 CA GLU B 607 7682 11519 8823 1562 -223 351 C ATOM 4058 C GLU B 607 21.064 14.992 16.237 1.00 71.42 C ANISOU 4058 C GLU B 607 7547 11154 8436 1647 -85 279 C ATOM 4059 O GLU B 607 21.756 14.645 15.283 1.00 74.78 O ANISOU 4059 O GLU B 607 8006 11450 8957 1711 35 263 O ATOM 4060 CB GLU B 607 20.704 13.512 18.220 1.00 80.66 C ANISOU 4060 CB GLU B 607 8541 12454 9654 1523 -368 403 C ATOM 4061 CG GLU B 607 20.976 12.192 17.518 1.00 87.24 C ANISOU 4061 CG GLU B 607 9386 13168 10594 1567 -342 421 C ATOM 4062 CD GLU B 607 19.975 11.114 17.894 1.00 91.29 C ANISOU 4062 CD GLU B 607 9904 13734 11047 1538 -471 460 C ATOM 4063 OE1 GLU B 607 18.814 11.458 18.207 1.00 90.91 O ANISOU 4063 OE1 GLU B 607 9912 13798 10833 1513 -539 443 O ATOM 4064 OE2 GLU B 607 20.350 9.922 17.869 1.00 91.02 O ANISOU 4064 OE2 GLU B 607 9814 13627 11144 1541 -499 507 O ATOM 4065 N CYS B 608 19.912 15.639 16.097 1.00 57.49 N ANISOU 4065 N CYS B 608 5881 9476 6486 1649 -103 236 N ATOM 4066 CA CYS B 608 19.385 15.991 14.783 1.00 59.36 C ANISOU 4066 CA CYS B 608 6277 9663 6613 1729 11 171 C ATOM 4067 C CYS B 608 20.371 16.855 13.997 1.00 66.66 C ANISOU 4067 C CYS B 608 7224 10490 7613 1787 188 142 C ATOM 4068 O CYS B 608 20.824 16.473 12.919 1.00 69.98 O ANISOU 4068 O CYS B 608 7714 10796 8078 1859 307 122 O ATOM 4069 CB CYS B 608 18.042 16.709 14.923 1.00 55.74 C ANISOU 4069 CB CYS B 608 5898 9320 5959 1713 -46 136 C ATOM 4070 SG CYS B 608 17.330 17.278 13.365 1.00 49.25 S ANISOU 4070 SG CYS B 608 5272 8452 4988 1809 79 62 S ATOM 4071 N SER B 609 20.708 18.016 14.548 1.00 79.60 N ANISOU 4071 N SER B 609 8802 12172 9272 1756 208 138 N ATOM 4072 CA SER B 609 21.620 18.944 13.888 1.00 84.52 C ANISOU 4072 CA SER B 609 9433 12704 9977 1807 376 116 C ATOM 4073 C SER B 609 23.024 18.365 13.732 1.00 82.49 C ANISOU 4073 C SER B 609 9088 12319 9937 1825 451 147 C ATOM 4074 O SER B 609 23.879 18.959 13.076 1.00 86.62 O ANISOU 4074 O SER B 609 9617 12743 10554 1876 608 134 O ATOM 4075 CB SER B 609 21.693 20.261 14.663 1.00 91.00 C ANISOU 4075 CB SER B 609 10182 13598 10797 1759 364 104 C ATOM 4076 OG SER B 609 22.379 20.092 15.891 1.00 93.03 O ANISOU 4076 OG SER B 609 10276 13891 11181 1684 262 142 O ATOM 4077 N ARG B 610 23.261 17.207 14.340 1.00 62.86 N ANISOU 4077 N ARG B 610 6515 9831 7538 1785 343 193 N ATOM 4078 CA ARG B 610 24.575 16.580 14.281 1.00 63.12 C ANISOU 4078 CA ARG B 610 6449 9741 7792 1796 398 229 C ATOM 4079 C ARG B 610 24.688 15.634 13.092 1.00 60.09 C ANISOU 4079 C ARG B 610 6160 9240 7432 1871 498 212 C ATOM 4080 O ARG B 610 25.723 15.587 12.425 1.00 57.00 O ANISOU 4080 O ARG B 610 5755 8717 7185 1921 642 208 O ATOM 4081 CB ARG B 610 24.879 15.830 15.580 1.00 67.84 C ANISOU 4081 CB ARG B 610 6892 10391 8495 1714 230 296 C ATOM 4082 CG ARG B 610 26.360 15.551 15.805 1.00 74.94 C ANISOU 4082 CG ARG B 610 7651 11178 9646 1709 271 336 C ATOM 4083 CD ARG B 610 26.595 14.588 16.965 1.00 80.86 C ANISOU 4083 CD ARG B 610 8261 11971 10492 1637 98 413 C ATOM 4084 NE ARG B 610 25.860 14.970 18.169 1.00 85.92 N ANISOU 4084 NE ARG B 610 8862 12780 11005 1559 -66 432 N ATOM 4085 CZ ARG B 610 24.811 14.307 18.646 1.00 88.70 C ANISOU 4085 CZ ARG B 610 9244 13234 11224 1523 -198 459 C ATOM 4086 NH1 ARG B 610 24.375 13.219 18.025 1.00 90.31 N ANISOU 4086 NH1 ARG B 610 9513 13387 11415 1557 -193 468 N ATOM 4087 NH2 ARG B 610 24.201 14.726 19.746 1.00 87.73 N ANISOU 4087 NH2 ARG B 610 9083 13262 10988 1454 -331 474 N ATOM 4088 N LEU B 611 23.623 14.883 12.825 1.00 60.14 N ANISOU 4088 N LEU B 611 6259 9291 7299 1879 425 197 N ATOM 4089 CA LEU B 611 23.642 13.903 11.742 1.00 67.20 C ANISOU 4089 CA LEU B 611 7243 10083 8207 1947 501 170 C ATOM 4090 C LEU B 611 22.316 13.807 10.991 1.00 74.10 C ANISOU 4090 C LEU B 611 8286 11008 8861 1987 485 114 C ATOM 4091 O LEU B 611 21.804 12.711 10.770 1.00 80.11 O ANISOU 4091 O LEU B 611 9082 11757 9601 1994 421 106 O ATOM 4092 CB LEU B 611 24.028 12.519 12.272 1.00 65.38 C ANISOU 4092 CB LEU B 611 6902 9810 8128 1911 406 222 C ATOM 4093 CG LEU B 611 23.163 11.933 13.389 1.00 57.89 C ANISOU 4093 CG LEU B 611 5892 8984 7122 1833 201 268 C ATOM 4094 CD1 LEU B 611 23.064 10.420 13.263 1.00 52.11 C ANISOU 4094 CD1 LEU B 611 5139 8192 6469 1837 143 289 C ATOM 4095 CD2 LEU B 611 23.704 12.331 14.752 1.00 61.02 C ANISOU 4095 CD2 LEU B 611 6128 9449 7608 1752 101 335 C ATOM 4096 N CYS B 612 21.762 14.948 10.594 1.00 66.86 N ANISOU 4096 N CYS B 612 7469 10143 7793 2013 539 77 N ATOM 4097 CA CYS B 612 20.541 14.952 9.795 1.00 56.63 C ANISOU 4097 CA CYS B 612 6337 8888 6291 2059 529 23 C ATOM 4098 C CYS B 612 20.798 15.514 8.405 1.00 56.72 C ANISOU 4098 C CYS B 612 6491 8819 6241 2156 716 -26 C ATOM 4099 O CYS B 612 20.891 16.728 8.219 1.00 52.63 O ANISOU 4099 O CYS B 612 6005 8317 5676 2175 802 -31 O ATOM 4100 CB CYS B 612 19.428 15.738 10.487 1.00 49.33 C ANISOU 4100 CB CYS B 612 5424 8106 5215 2008 415 22 C ATOM 4101 SG CYS B 612 17.917 15.889 9.511 1.00 55.13 S ANISOU 4101 SG CYS B 612 6353 8889 5706 2064 398 -42 S ATOM 4102 N ARG B 613 20.912 14.615 7.433 1.00 74.35 N ANISOU 4102 N ARG B 613 8809 10963 8476 2219 781 -62 N ATOM 4103 CA ARG B 613 21.137 15.001 6.044 1.00 78.14 C ANISOU 4103 CA ARG B 613 9440 11367 8883 2318 960 -109 C ATOM 4104 C ARG B 613 19.891 14.766 5.199 1.00 74.31 C ANISOU 4104 C ARG B 613 9128 10925 8180 2368 918 -171 C ATOM 4105 O ARG B 613 19.064 13.911 5.519 1.00 65.58 O ANISOU 4105 O ARG B 613 8019 9867 7032 2335 769 -184 O ATOM 4106 CB ARG B 613 22.307 14.215 5.453 1.00 80.97 C ANISOU 4106 CB ARG B 613 9776 11582 9405 2362 1091 -115 C ATOM 4107 CG ARG B 613 23.567 14.242 6.296 1.00 82.35 C ANISOU 4107 CG ARG B 613 9766 11700 9822 2312 1116 -54 C ATOM 4108 CD ARG B 613 24.629 13.329 5.710 1.00 88.04 C ANISOU 4108 CD ARG B 613 10462 12274 10716 2354 1235 -62 C ATOM 4109 NE ARG B 613 25.778 13.202 6.599 1.00 92.56 N ANISOU 4109 NE ARG B 613 10843 12790 11535 2299 1230 0 N ATOM 4110 CZ ARG B 613 26.826 12.423 6.356 1.00 96.88 C ANISOU 4110 CZ ARG B 613 11322 13206 12283 2318 1316 8 C ATOM 4111 NH1 ARG B 613 26.874 11.698 5.245 1.00 96.53 N ANISOU 4111 NH1 ARG B 613 11388 13073 12216 2390 1423 -47 N ATOM 4112 NH2 ARG B 613 27.828 12.369 7.224 1.00 98.57 N ANISOU 4112 NH2 ARG B 613 11355 13375 12723 2265 1294 69 N ATOM 4113 N ASN B 614 19.767 15.530 4.119 1.00 75.89 N ANISOU 4113 N ASN B 614 9477 11108 8249 2447 1049 -204 N ATOM 4114 CA ASN B 614 18.641 15.397 3.208 1.00 75.96 C ANISOU 4114 CA ASN B 614 9661 11155 8046 2504 1016 -264 C ATOM 4115 C ASN B 614 17.316 15.639 3.919 1.00 74.45 C ANISOU 4115 C ASN B 614 9462 11090 7734 2446 832 -261 C ATOM 4116 O ASN B 614 16.490 14.736 4.056 1.00 74.35 O ANISOU 4116 O ASN B 614 9461 11110 7677 2426 693 -289 O ATOM 4117 CB ASN B 614 18.667 14.027 2.526 1.00 75.35 C ANISOU 4117 CB ASN B 614 9641 11004 7983 2544 1014 -319 C ATOM 4118 CG ASN B 614 19.969 13.768 1.787 1.00 77.38 C ANISOU 4118 CG ASN B 614 9909 11130 8362 2604 1209 -328 C ATOM 4119 OD1 ASN B 614 20.063 12.848 0.978 1.00 77.30 O ANISOU 4119 OD1 ASN B 614 9977 11051 8343 2656 1253 -385 O ATOM 4120 ND2 ASN B 614 20.980 14.581 2.065 1.00 80.90 N ANISOU 4120 ND2 ASN B 614 10274 11537 8929 2596 1329 -274 N ATOM 4121 N GLY B 615 17.131 16.874 4.373 1.00 78.89 N ANISOU 4121 N GLY B 615 9998 11719 8257 2420 836 -229 N ATOM 4122 CA GLY B 615 15.947 17.249 5.117 1.00 75.32 C ANISOU 4122 CA GLY B 615 9526 11385 7705 2361 678 -223 C ATOM 4123 C GLY B 615 16.299 18.227 6.218 1.00 75.06 C ANISOU 4123 C GLY B 615 9359 11406 7755 2290 668 -172 C ATOM 4124 O GLY B 615 17.477 18.502 6.459 1.00 77.59 O ANISOU 4124 O GLY B 615 9590 11668 8224 2283 767 -141 O ATOM 4125 N TYR B 616 15.280 18.754 6.890 1.00 75.70 N ANISOU 4125 N TYR B 616 9423 11594 7747 2238 548 -168 N ATOM 4126 CA TYR B 616 15.493 19.733 7.948 1.00 72.28 C ANISOU 4126 CA TYR B 616 8868 11221 7373 2170 531 -133 C ATOM 4127 C TYR B 616 15.204 19.143 9.321 1.00 70.88 C ANISOU 4127 C TYR B 616 8554 11121 7255 2070 364 -106 C ATOM 4128 O TYR B 616 14.798 17.986 9.439 1.00 71.93 O ANISOU 4128 O TYR B 616 8686 11258 7387 2056 264 -108 O ATOM 4129 CB TYR B 616 14.634 20.980 7.711 1.00 66.82 C ANISOU 4129 CB TYR B 616 8252 10591 6544 2185 543 -148 C ATOM 4130 CG TYR B 616 13.141 20.740 7.771 1.00 62.45 C ANISOU 4130 CG TYR B 616 7765 10121 5842 2170 400 -174 C ATOM 4131 CD1 TYR B 616 12.400 21.134 8.878 1.00 56.61 C ANISOU 4131 CD1 TYR B 616 6941 9483 5083 2088 279 -164 C ATOM 4132 CD2 TYR B 616 12.469 20.128 6.720 1.00 62.96 C ANISOU 4132 CD2 TYR B 616 7972 10159 5788 2237 386 -213 C ATOM 4133 CE1 TYR B 616 11.036 20.925 8.938 1.00 54.25 C ANISOU 4133 CE1 TYR B 616 6695 9253 4664 2074 155 -186 C ATOM 4134 CE2 TYR B 616 11.101 19.912 6.773 1.00 59.61 C ANISOU 4134 CE2 TYR B 616 7600 9804 5244 2223 251 -239 C ATOM 4135 CZ TYR B 616 10.391 20.314 7.885 1.00 56.17 C ANISOU 4135 CZ TYR B 616 7074 9463 4804 2141 138 -222 C ATOM 4136 OH TYR B 616 9.032 20.107 7.953 1.00 53.80 O ANISOU 4136 OH TYR B 616 6819 9224 4401 2126 10 -246 O ATOM 4137 N CYS B 617 15.427 19.943 10.358 1.00 56.93 N ANISOU 4137 N CYS B 617 6673 9416 5543 2003 337 -80 N ATOM 4138 CA CYS B 617 15.152 19.520 11.722 1.00 45.60 C ANISOU 4138 CA CYS B 617 5112 8068 4146 1908 184 -50 C ATOM 4139 C CYS B 617 14.002 20.330 12.296 1.00 47.72 C ANISOU 4139 C CYS B 617 5388 8451 4293 1863 101 -65 C ATOM 4140 O CYS B 617 14.027 21.560 12.272 1.00 46.51 O ANISOU 4140 O CYS B 617 5239 8316 4115 1867 168 -80 O ATOM 4141 CB CYS B 617 16.389 19.695 12.600 1.00 39.99 C ANISOU 4141 CB CYS B 617 4249 7342 3603 1858 204 -12 C ATOM 4142 SG CYS B 617 17.831 18.757 12.066 1.00 71.08 S ANISOU 4142 SG CYS B 617 8149 11137 7720 1901 301 12 S ATOM 4143 N THR B 618 12.988 19.638 12.802 1.00 69.12 N ANISOU 4143 N THR B 618 8095 11232 6937 1821 -39 -61 N ATOM 4144 CA THR B 618 11.892 20.302 13.489 1.00 72.55 C ANISOU 4144 CA THR B 618 8519 11776 7271 1769 -125 -72 C ATOM 4145 C THR B 618 12.389 20.765 14.852 1.00 73.98 C ANISOU 4145 C THR B 618 8553 12029 7526 1683 -167 -44 C ATOM 4146 O THR B 618 13.368 20.231 15.369 1.00 75.81 O ANISOU 4146 O THR B 618 8689 12238 7879 1656 -177 -7 O ATOM 4147 CB THR B 618 10.686 19.364 13.660 1.00 73.75 C ANISOU 4147 CB THR B 618 8701 11975 7345 1748 -259 -73 C ATOM 4148 OG1 THR B 618 11.065 18.237 14.459 1.00 75.64 O ANISOU 4148 OG1 THR B 618 8840 12222 7678 1698 -343 -25 O ATOM 4149 CG2 THR B 618 10.198 18.879 12.306 1.00 72.44 C ANISOU 4149 CG2 THR B 618 8679 11737 7106 1834 -229 -111 C ATOM 4150 N PRO B 619 11.723 21.771 15.435 1.00 68.40 N ANISOU 4150 N PRO B 619 7828 11410 6750 1641 -195 -65 N ATOM 4151 CA PRO B 619 12.140 22.284 16.745 1.00 70.06 C ANISOU 4151 CA PRO B 619 7906 11699 7016 1559 -238 -51 C ATOM 4152 C PRO B 619 12.147 21.197 17.823 1.00 72.34 C ANISOU 4152 C PRO B 619 8100 12046 7338 1490 -369 -1 C ATOM 4153 O PRO B 619 12.703 21.410 18.901 1.00 73.57 O ANISOU 4153 O PRO B 619 8142 12261 7551 1426 -411 19 O ATOM 4154 CB PRO B 619 11.079 23.345 17.055 1.00 66.92 C ANISOU 4154 CB PRO B 619 7529 11386 6512 1531 -258 -91 C ATOM 4155 CG PRO B 619 10.571 23.769 15.721 1.00 62.70 C ANISOU 4155 CG PRO B 619 7131 10786 5904 1614 -174 -122 C ATOM 4156 CD PRO B 619 10.596 22.535 14.873 1.00 64.07 C ANISOU 4156 CD PRO B 619 7381 10887 6074 1670 -181 -106 C ATOM 4157 N THR B 620 11.543 20.049 17.529 1.00 71.36 N ANISOU 4157 N THR B 620 8024 11908 7182 1505 -434 20 N ATOM 4158 CA THR B 620 11.507 18.935 18.473 1.00 72.63 C ANISOU 4158 CA THR B 620 8100 12116 7381 1446 -553 78 C ATOM 4159 C THR B 620 12.609 17.918 18.194 1.00 76.60 C ANISOU 4159 C THR B 620 8564 12524 8018 1472 -533 120 C ATOM 4160 O THR B 620 12.548 16.781 18.663 1.00 79.66 O ANISOU 4160 O THR B 620 8901 12920 8447 1444 -622 173 O ATOM 4161 CB THR B 620 10.148 18.210 18.455 1.00 71.38 C ANISOU 4161 CB THR B 620 7995 11995 7130 1439 -647 82 C ATOM 4162 OG1 THR B 620 9.789 17.896 17.103 1.00 73.82 O ANISOU 4162 OG1 THR B 620 8427 12214 7408 1521 -595 44 O ATOM 4163 CG2 THR B 620 9.070 19.082 19.077 1.00 67.10 C ANISOU 4163 CG2 THR B 620 7457 11561 6477 1393 -689 55 C ATOM 4164 N GLY B 621 13.608 18.332 17.422 1.00 77.15 N ANISOU 4164 N GLY B 621 8653 12499 8162 1526 -410 99 N ATOM 4165 CA GLY B 621 14.762 17.494 17.149 1.00 78.79 C ANISOU 4165 CA GLY B 621 8815 12607 8514 1551 -373 134 C ATOM 4166 C GLY B 621 14.524 16.377 16.150 1.00 78.10 C ANISOU 4166 C GLY B 621 8811 12431 8432 1612 -359 128 C ATOM 4167 O GLY B 621 15.358 15.481 16.008 1.00 80.81 O ANISOU 4167 O GLY B 621 9109 12693 8901 1626 -344 160 O ATOM 4168 N LYS B 622 13.393 16.420 15.453 1.00 66.81 N ANISOU 4168 N LYS B 622 7501 11012 6873 1649 -365 84 N ATOM 4169 CA LYS B 622 13.094 15.398 14.455 1.00 68.19 C ANISOU 4169 CA LYS B 622 7763 11104 7040 1709 -357 63 C ATOM 4170 C LYS B 622 13.631 15.770 13.080 1.00 68.81 C ANISOU 4170 C LYS B 622 7951 11079 7113 1801 -206 12 C ATOM 4171 O LYS B 622 13.511 16.915 12.645 1.00 67.58 O ANISOU 4171 O LYS B 622 7861 10935 6881 1830 -127 -21 O ATOM 4172 CB LYS B 622 11.590 15.135 14.361 1.00 64.97 C ANISOU 4172 CB LYS B 622 7428 10753 6503 1705 -452 38 C ATOM 4173 CG LYS B 622 11.228 14.196 13.224 1.00 62.37 C ANISOU 4173 CG LYS B 622 7201 10338 6158 1774 -443 -2 C ATOM 4174 CD LYS B 622 9.745 13.902 13.172 1.00 61.85 C ANISOU 4174 CD LYS B 622 7194 10323 5984 1768 -548 -28 C ATOM 4175 CE LYS B 622 9.444 12.880 12.090 1.00 65.30 C ANISOU 4175 CE LYS B 622 7721 10670 6419 1834 -551 -74 C ATOM 4176 NZ LYS B 622 8.011 12.488 12.073 1.00 67.03 N ANISOU 4176 NZ LYS B 622 7983 10929 6557 1826 -665 -99 N ATOM 4177 N CYS B 623 14.218 14.794 12.397 1.00 70.91 N ANISOU 4177 N CYS B 623 8238 11243 7463 1847 -162 9 N ATOM 4178 CA CYS B 623 14.720 15.012 11.048 1.00 74.40 C ANISOU 4178 CA CYS B 623 8792 11584 7893 1939 -13 -39 C ATOM 4179 C CYS B 623 13.678 14.635 10.000 1.00 73.14 C ANISOU 4179 C CYS B 623 8783 11409 7596 2000 -28 -100 C ATOM 4180 O CYS B 623 13.507 13.458 9.676 1.00 72.98 O ANISOU 4180 O CYS B 623 8781 11341 7609 2017 -72 -115 O ATOM 4181 CB CYS B 623 16.005 14.218 10.813 1.00 79.23 C ANISOU 4181 CB CYS B 623 9346 12082 8674 1960 62 -19 C ATOM 4182 SG CYS B 623 16.651 14.347 9.129 1.00 79.04 S ANISOU 4182 SG CYS B 623 9466 11929 8638 2076 259 -78 S ATOM 4183 N CYS B 624 12.981 15.640 9.479 1.00 72.34 N ANISOU 4183 N CYS B 624 8788 11347 7350 2034 4 -137 N ATOM 4184 CA CYS B 624 12.017 15.427 8.407 1.00 67.92 C ANISOU 4184 CA CYS B 624 8381 10775 6651 2099 -8 -198 C ATOM 4185 C CYS B 624 12.742 15.197 7.087 1.00 68.74 C ANISOU 4185 C CYS B 624 8593 10770 6756 2193 134 -238 C ATOM 4186 O CYS B 624 13.594 15.992 6.689 1.00 70.57 O ANISOU 4186 O CYS B 624 8844 10961 7010 2229 276 -230 O ATOM 4187 CB CYS B 624 11.063 16.617 8.291 1.00 64.84 C ANISOU 4187 CB CYS B 624 8063 10461 6113 2105 -20 -216 C ATOM 4188 SG CYS B 624 9.746 16.635 9.532 1.00 65.35 S ANISOU 4188 SG CYS B 624 8049 10649 6132 2012 -202 -196 S ATOM 4189 N CYS B 625 12.400 14.104 6.414 1.00 69.48 N ANISOU 4189 N CYS B 625 8755 10814 6831 2233 98 -283 N ATOM 4190 CA CYS B 625 13.090 13.708 5.193 1.00 67.80 C ANISOU 4190 CA CYS B 625 8643 10497 6623 2319 228 -329 C ATOM 4191 C CYS B 625 12.532 14.408 3.955 1.00 72.85 C ANISOU 4191 C CYS B 625 9466 11138 7076 2406 295 -384 C ATOM 4192 O CYS B 625 11.317 14.532 3.789 1.00 73.49 O ANISOU 4192 O CYS B 625 9620 11280 7023 2411 192 -415 O ATOM 4193 CB CYS B 625 13.017 12.190 5.012 1.00 63.33 C ANISOU 4193 CB CYS B 625 8064 9871 6128 2324 162 -362 C ATOM 4194 SG CYS B 625 13.596 11.242 6.437 1.00136.26 S ANISOU 4194 SG CYS B 625 17086 19103 15585 2226 69 -285 S ATOM 4195 N SER B 626 13.433 14.867 3.093 1.00 73.19 N ANISOU 4195 N SER B 626 9583 11113 7115 2476 470 -392 N ATOM 4196 CA SER B 626 13.046 15.462 1.823 1.00 68.70 C ANISOU 4196 CA SER B 626 9197 10537 6367 2568 552 -437 C ATOM 4197 C SER B 626 12.690 14.354 0.839 1.00 69.72 C ANISOU 4197 C SER B 626 9445 10618 6429 2630 527 -518 C ATOM 4198 O SER B 626 13.117 13.212 1.013 1.00 69.77 O ANISOU 4198 O SER B 626 9385 10566 6557 2613 505 -534 O ATOM 4199 CB SER B 626 14.183 16.321 1.266 1.00 67.38 C ANISOU 4199 CB SER B 626 9063 10310 6229 2622 759 -410 C ATOM 4200 OG SER B 626 15.339 15.540 1.019 1.00 70.47 O ANISOU 4200 OG SER B 626 9418 10600 6759 2642 865 -416 O ATOM 4201 N PRO B 627 11.901 14.686 -0.196 1.00 78.16 N ANISOU 4201 N PRO B 627 10686 11709 7304 2703 526 -569 N ATOM 4202 CA PRO B 627 11.472 13.698 -1.191 1.00 74.86 C ANISOU 4202 CA PRO B 627 10392 11251 6798 2767 492 -660 C ATOM 4203 C PRO B 627 12.635 12.862 -1.716 1.00 75.65 C ANISOU 4203 C PRO B 627 10497 11244 7004 2807 624 -690 C ATOM 4204 O PRO B 627 13.577 13.405 -2.294 1.00 74.30 O ANISOU 4204 O PRO B 627 10376 11022 6832 2860 807 -673 O ATOM 4205 CB PRO B 627 10.895 14.566 -2.310 1.00 76.22 C ANISOU 4205 CB PRO B 627 10754 11455 6750 2853 540 -689 C ATOM 4206 CG PRO B 627 10.394 15.777 -1.609 1.00 76.53 C ANISOU 4206 CG PRO B 627 10742 11577 6760 2807 498 -621 C ATOM 4207 CD PRO B 627 11.354 16.025 -0.477 1.00 77.51 C ANISOU 4207 CD PRO B 627 10685 11689 7075 2730 551 -546 C ATOM 4208 N GLY B 628 12.565 11.551 -1.505 1.00 61.12 N ANISOU 4208 N GLY B 628 8597 9362 5263 2781 537 -733 N ATOM 4209 CA GLY B 628 13.594 10.646 -1.983 1.00 66.10 C ANISOU 4209 CA GLY B 628 9223 9885 6009 2815 651 -770 C ATOM 4210 C GLY B 628 14.463 10.081 -0.877 1.00 73.28 C ANISOU 4210 C GLY B 628 9929 10749 7165 2735 645 -706 C ATOM 4211 O GLY B 628 15.536 9.539 -1.139 1.00 78.23 O ANISOU 4211 O GLY B 628 10523 11278 7921 2757 766 -714 O ATOM 4212 N TRP B 629 14.001 10.201 0.363 1.00 79.37 N ANISOU 4212 N TRP B 629 10564 11592 8003 2644 506 -641 N ATOM 4213 CA TRP B 629 14.762 9.706 1.505 1.00 81.76 C ANISOU 4213 CA TRP B 629 10671 11866 8527 2565 481 -569 C ATOM 4214 C TRP B 629 13.865 9.251 2.650 1.00 85.17 C ANISOU 4214 C TRP B 629 10987 12372 9002 2477 280 -533 C ATOM 4215 O TRP B 629 12.751 9.749 2.815 1.00 87.92 O ANISOU 4215 O TRP B 629 11380 12811 9216 2461 176 -538 O ATOM 4216 CB TRP B 629 15.739 10.775 1.995 1.00 76.51 C ANISOU 4216 CB TRP B 629 9930 11205 7934 2543 597 -489 C ATOM 4217 CG TRP B 629 16.666 11.246 0.924 1.00 71.79 C ANISOU 4217 CG TRP B 629 9435 10529 7314 2628 807 -513 C ATOM 4218 CD1 TRP B 629 16.527 12.360 0.149 1.00 66.38 C ANISOU 4218 CD1 TRP B 629 8886 9869 6468 2691 910 -523 C ATOM 4219 CD2 TRP B 629 17.871 10.605 0.493 1.00 68.46 C ANISOU 4219 CD2 TRP B 629 8986 9985 7039 2661 947 -526 C ATOM 4220 NE1 TRP B 629 17.578 12.458 -0.731 1.00 65.91 N ANISOU 4220 NE1 TRP B 629 8889 9713 6441 2762 1111 -537 N ATOM 4221 CE2 TRP B 629 18.418 11.388 -0.541 1.00 67.92 C ANISOU 4221 CE2 TRP B 629 9045 9874 6886 2745 1139 -543 C ATOM 4222 CE3 TRP B 629 18.546 9.443 0.885 1.00 68.93 C ANISOU 4222 CE3 TRP B 629 8924 9963 7305 2629 933 -520 C ATOM 4223 CZ2 TRP B 629 19.603 11.054 -1.188 1.00 71.48 C ANISOU 4223 CZ2 TRP B 629 9506 10206 7447 2797 1322 -560 C ATOM 4224 CZ3 TRP B 629 19.725 9.110 0.241 1.00 74.27 C ANISOU 4224 CZ3 TRP B 629 9605 10517 8097 2679 1109 -539 C ATOM 4225 CH2 TRP B 629 20.241 9.913 -0.783 1.00 74.14 C ANISOU 4225 CH2 TRP B 629 9719 10462 7989 2762 1304 -561 C ATOM 4226 N GLU B 630 14.361 8.301 3.436 1.00 79.57 N ANISOU 4226 N GLU B 630 10127 11622 8485 2420 230 -492 N ATOM 4227 CA GLU B 630 13.621 7.777 4.578 1.00 80.71 C ANISOU 4227 CA GLU B 630 10149 11829 8688 2335 52 -443 C ATOM 4228 C GLU B 630 14.575 7.346 5.686 1.00 85.46 C ANISOU 4228 C GLU B 630 10563 12406 9504 2264 42 -351 C ATOM 4229 O GLU B 630 15.793 7.401 5.524 1.00 82.28 O ANISOU 4229 O GLU B 630 10121 11927 9213 2282 170 -333 O ATOM 4230 CB GLU B 630 12.738 6.601 4.153 1.00 83.47 C ANISOU 4230 CB GLU B 630 10541 12149 9025 2353 -55 -515 C ATOM 4231 CG GLU B 630 13.506 5.431 3.559 1.00 90.20 C ANISOU 4231 CG GLU B 630 11382 12875 10015 2390 13 -562 C ATOM 4232 CD GLU B 630 12.599 4.296 3.126 1.00 90.92 C ANISOU 4232 CD GLU B 630 11513 12934 10100 2408 -96 -644 C ATOM 4233 OE1 GLU B 630 13.123 3.234 2.725 1.00 93.61 O ANISOU 4233 OE1 GLU B 630 11829 13170 10568 2432 -59 -687 O ATOM 4234 OE2 GLU B 630 11.362 4.465 3.187 1.00 87.10 O ANISOU 4234 OE2 GLU B 630 11077 12523 9493 2399 -219 -667 O ATOM 4235 N GLY B 631 14.014 6.913 6.811 1.00119.47 N ANISOU 4235 N GLY B 631 14751 16775 13868 2185 -109 -291 N ATOM 4236 CA GLY B 631 14.812 6.509 7.952 1.00122.78 C ANISOU 4236 CA GLY B 631 14991 17186 14474 2114 -142 -193 C ATOM 4237 C GLY B 631 14.941 7.629 8.965 1.00122.76 C ANISOU 4237 C GLY B 631 14916 17285 14442 2053 -162 -118 C ATOM 4238 O GLY B 631 14.620 8.779 8.666 1.00122.06 O ANISOU 4238 O GLY B 631 14916 17253 14208 2075 -117 -144 O ATOM 4239 N ASP B 632 15.412 7.292 10.163 1.00125.43 N ANISOU 4239 N ASP B 632 15093 17647 14919 1979 -232 -25 N ATOM 4240 CA ASP B 632 15.567 8.271 11.235 1.00124.22 C ANISOU 4240 CA ASP B 632 14858 17593 14746 1915 -264 43 C ATOM 4241 C ASP B 632 16.141 9.589 10.726 1.00123.09 C ANISOU 4241 C ASP B 632 14782 17448 14540 1954 -127 13 C ATOM 4242 O ASP B 632 15.520 10.643 10.867 1.00123.22 O ANISOU 4242 O ASP B 632 14848 17553 14417 1944 -138 1 O ATOM 4243 CB ASP B 632 16.456 7.716 12.350 1.00124.24 C ANISOU 4243 CB ASP B 632 14682 17586 14935 1849 -315 141 C ATOM 4244 CG ASP B 632 15.798 6.583 13.113 1.00124.42 C ANISOU 4244 CG ASP B 632 14623 17639 15013 1797 -464 196 C ATOM 4245 OD1 ASP B 632 14.765 6.065 12.639 1.00125.63 O ANISOU 4245 OD1 ASP B 632 14852 17791 15091 1819 -516 147 O ATOM 4246 OD2 ASP B 632 16.316 6.211 14.187 1.00123.44 O ANISOU 4246 OD2 ASP B 632 14354 17537 15010 1734 -533 291 O ATOM 4247 N PHE B 633 17.327 9.524 10.130 1.00 81.92 N ANISOU 4247 N PHE B 633 9563 12125 9438 1999 9 3 N ATOM 4248 CA PHE B 633 18.004 10.723 9.652 1.00 78.73 C ANISOU 4248 CA PHE B 633 9208 11702 9005 2037 154 -15 C ATOM 4249 C PHE B 633 18.148 10.750 8.132 1.00 78.13 C ANISOU 4249 C PHE B 633 9287 11533 8863 2138 302 -96 C ATOM 4250 O PHE B 633 19.114 11.296 7.598 1.00 76.79 O ANISOU 4250 O PHE B 633 9137 11294 8747 2182 457 -102 O ATOM 4251 CB PHE B 633 19.365 10.873 10.329 1.00 76.45 C ANISOU 4251 CB PHE B 633 8772 11369 8906 2002 202 49 C ATOM 4252 CG PHE B 633 19.280 11.029 11.818 1.00 73.60 C ANISOU 4252 CG PHE B 633 8268 11111 8585 1907 63 126 C ATOM 4253 CD1 PHE B 633 18.887 12.232 12.379 1.00 71.92 C ANISOU 4253 CD1 PHE B 633 8055 11006 8267 1872 37 131 C ATOM 4254 CD2 PHE B 633 19.585 9.973 12.656 1.00 71.98 C ANISOU 4254 CD2 PHE B 633 7930 10896 8523 1853 -40 193 C ATOM 4255 CE1 PHE B 633 18.804 12.379 13.747 1.00 66.66 C ANISOU 4255 CE1 PHE B 633 7264 10439 7624 1785 -89 194 C ATOM 4256 CE2 PHE B 633 19.504 10.115 14.025 1.00 68.64 C ANISOU 4256 CE2 PHE B 633 7384 10574 8120 1768 -169 267 C ATOM 4257 CZ PHE B 633 19.113 11.319 14.570 1.00 64.96 C ANISOU 4257 CZ PHE B 633 6926 10220 7536 1734 -192 263 C ATOM 4258 N CYS B 634 17.179 10.154 7.446 1.00 83.25 N ANISOU 4258 N CYS B 634 10048 12184 9399 2175 254 -157 N ATOM 4259 CA CYS B 634 17.096 10.235 5.992 1.00 83.49 C ANISOU 4259 CA CYS B 634 10250 12152 9321 2272 375 -242 C ATOM 4260 C CYS B 634 18.378 9.783 5.293 1.00 80.64 C ANISOU 4260 C CYS B 634 9886 11655 9099 2325 534 -258 C ATOM 4261 O CYS B 634 18.940 10.505 4.468 1.00 78.84 O ANISOU 4261 O CYS B 634 9745 11381 8830 2388 695 -282 O ATOM 4262 CB CYS B 634 16.728 11.659 5.569 1.00 84.46 C ANISOU 4262 CB CYS B 634 10482 12335 9274 2306 441 -258 C ATOM 4263 SG CYS B 634 15.307 12.338 6.462 1.00 58.17 S ANISOU 4263 SG CYS B 634 7140 9160 5801 2240 271 -236 S ATOM 4264 N ARG B 635 18.829 8.580 5.631 1.00 68.36 N ANISOU 4264 N ARG B 635 8227 10032 7716 2298 492 -240 N ATOM 4265 CA ARG B 635 20.005 7.988 5.005 1.00 64.75 C ANISOU 4265 CA ARG B 635 7753 9436 7412 2344 635 -259 C ATOM 4266 C ARG B 635 19.582 6.839 4.102 1.00 62.90 C ANISOU 4266 C ARG B 635 7609 9135 7154 2395 630 -345 C ATOM 4267 O ARG B 635 20.209 6.576 3.079 1.00 65.76 O ANISOU 4267 O ARG B 635 8049 9395 7541 2466 779 -405 O ATOM 4268 CB ARG B 635 20.975 7.474 6.068 1.00 65.38 C ANISOU 4268 CB ARG B 635 7631 9474 7738 2275 600 -172 C ATOM 4269 CG ARG B 635 21.378 8.511 7.099 1.00 61.48 C ANISOU 4269 CG ARG B 635 7030 9051 7280 2215 577 -90 C ATOM 4270 CD ARG B 635 22.216 9.613 6.477 1.00 57.74 C ANISOU 4270 CD ARG B 635 6608 8530 6801 2267 763 -103 C ATOM 4271 NE ARG B 635 22.696 10.554 7.483 1.00 51.12 N ANISOU 4271 NE ARG B 635 5650 7746 6026 2207 740 -32 N ATOM 4272 CZ ARG B 635 23.803 10.383 8.196 1.00 52.56 C ANISOU 4272 CZ ARG B 635 5671 7874 6424 2166 749 31 C ATOM 4273 NH1 ARG B 635 24.552 9.303 8.016 1.00 52.77 N ANISOU 4273 NH1 ARG B 635 5633 7785 6631 2177 784 38 N ATOM 4274 NH2 ARG B 635 24.163 11.293 9.091 1.00 55.75 N ANISOU 4274 NH2 ARG B 635 5976 8336 6870 2113 718 83 N ATOM 4275 N THR B 636 18.514 6.153 4.497 1.00 70.22 N ANISOU 4275 N THR B 636 8523 10118 8039 2359 461 -355 N ATOM 4276 CA THR B 636 17.972 5.057 3.708 1.00 76.31 C ANISOU 4276 CA THR B 636 9373 10833 8788 2402 432 -444 C ATOM 4277 C THR B 636 17.397 5.600 2.405 1.00 81.01 C ANISOU 4277 C THR B 636 10181 11442 9156 2490 508 -545 C ATOM 4278 O THR B 636 16.404 6.327 2.409 1.00 76.35 O ANISOU 4278 O THR B 636 9671 10953 8384 2489 434 -554 O ATOM 4279 CB THR B 636 16.876 4.294 4.476 1.00 81.30 C ANISOU 4279 CB THR B 636 9937 11527 9428 2341 228 -426 C ATOM 4280 OG1 THR B 636 17.403 3.817 5.721 1.00 84.87 O ANISOU 4280 OG1 THR B 636 10192 11975 10077 2260 155 -319 O ATOM 4281 CG2 THR B 636 16.373 3.113 3.657 1.00 82.28 C ANISOU 4281 CG2 THR B 636 10128 11579 9556 2386 198 -525 C ATOM 4282 N ALA B 637 18.035 5.245 1.294 1.00104.04 N ANISOU 4282 N ALA B 637 13189 14255 12085 2568 656 -620 N ATOM 4283 CA ALA B 637 17.647 5.752 -0.018 1.00100.18 C ANISOU 4283 CA ALA B 637 12911 13773 11379 2660 748 -713 C ATOM 4284 C ALA B 637 16.238 5.323 -0.417 1.00 98.38 C ANISOU 4284 C ALA B 637 12788 13601 10990 2677 601 -795 C ATOM 4285 O ALA B 637 15.781 4.237 -0.058 1.00101.65 O ANISOU 4285 O ALA B 637 13129 13996 11498 2641 474 -815 O ATOM 4286 CB ALA B 637 18.655 5.315 -1.071 1.00 99.77 C ANISOU 4286 CB ALA B 637 12926 13595 11387 2736 938 -778 C ATOM 4287 N LYS B 638 15.557 6.187 -1.164 1.00125.75 N ANISOU 4287 N LYS B 638 14274 16334 17172 4419 -3582 -3648 N ATOM 4288 CA LYS B 638 14.220 5.893 -1.663 1.00126.39 C ANISOU 4288 CA LYS B 638 14519 16509 16994 4391 -3655 -3865 C ATOM 4289 C LYS B 638 14.301 5.391 -3.100 1.00124.99 C ANISOU 4289 C LYS B 638 14808 16160 16523 4579 -3537 -3274 C ATOM 4290 O LYS B 638 15.163 5.820 -3.868 1.00127.00 O ANISOU 4290 O LYS B 638 15088 16149 17018 4776 -3485 -2737 O ATOM 4291 CB LYS B 638 13.345 7.145 -1.607 1.00127.33 C ANISOU 4291 CB LYS B 638 14170 16452 17757 4416 -3978 -4300 C ATOM 4292 CG LYS B 638 11.877 6.907 -1.924 1.00126.87 C ANISOU 4292 CG LYS B 638 14188 16523 17495 4356 -4086 -4617 C ATOM 4293 CD LYS B 638 11.065 6.709 -0.657 1.00128.88 C ANISOU 4293 CD LYS B 638 14178 17210 17580 4129 -4113 -5344 C ATOM 4294 CE LYS B 638 11.056 7.977 0.185 1.00133.51 C ANISOU 4294 CE LYS B 638 14146 17726 18855 4145 -4341 -5893 C ATOM 4295 NZ LYS B 638 10.214 7.841 1.405 1.00132.13 N ANISOU 4295 NZ LYS B 638 13672 18062 18470 3953 -4349 -6646 N ATOM 4296 N CYS B 639 13.401 4.483 -3.460 1.00123.11 N ANISOU 4296 N CYS B 639 14919 16101 15758 4519 -3503 -3374 N ATOM 4297 CA CYS B 639 13.353 3.958 -4.819 1.00123.99 C ANISOU 4297 CA CYS B 639 15487 16099 15523 4705 -3426 -2919 C ATOM 4298 C CYS B 639 11.975 4.169 -5.436 1.00125.97 C ANISOU 4298 C CYS B 639 15757 16319 15788 4698 -3662 -3136 C ATOM 4299 O CYS B 639 10.959 4.102 -4.745 1.00124.48 O ANISOU 4299 O CYS B 639 15391 16302 15603 4503 -3793 -3657 O ATOM 4300 CB CYS B 639 13.717 2.473 -4.833 1.00121.82 C ANISOU 4300 CB CYS B 639 15697 16014 14574 4674 -3181 -2771 C ATOM 4301 SG CYS B 639 15.378 2.108 -4.229 1.00171.36 S ANISOU 4301 SG CYS B 639 21982 22304 20823 4703 -2903 -2441 S ATOM 4302 N GLU B 640 11.946 4.427 -6.740 1.00153.49 N ANISOU 4302 N GLU B 640 19436 19618 19267 4912 -3716 -2716 N ATOM 4303 CA GLU B 640 10.690 4.659 -7.444 1.00159.99 C ANISOU 4303 CA GLU B 640 20286 20388 20116 4921 -3973 -2849 C ATOM 4304 C GLU B 640 10.746 4.090 -8.859 1.00165.67 C ANISOU 4304 C GLU B 640 21508 21098 20343 5128 -3918 -2386 C ATOM 4305 O GLU B 640 11.335 4.698 -9.752 1.00167.63 O ANISOU 4305 O GLU B 640 21751 21208 20734 5337 -3905 -1873 O ATOM 4306 CB GLU B 640 10.370 6.155 -7.486 1.00159.91 C ANISOU 4306 CB GLU B 640 19751 20111 20898 4960 -4258 -2902 C ATOM 4307 CG GLU B 640 8.921 6.482 -7.821 1.00160.64 C ANISOU 4307 CG GLU B 640 19725 20157 21155 4906 -4570 -3206 C ATOM 4308 CD GLU B 640 7.967 6.149 -6.688 1.00156.70 C ANISOU 4308 CD GLU B 640 19027 19892 20619 4665 -4621 -3916 C ATOM 4309 OE1 GLU B 640 7.149 7.021 -6.325 1.00156.45 O ANISOU 4309 OE1 GLU B 640 18539 19770 21136 4615 -4873 -4320 O ATOM 4310 OE2 GLU B 640 8.035 5.021 -6.156 1.00154.08 O ANISOU 4310 OE2 GLU B 640 18968 19845 19731 4529 -4414 -4057 O ATOM 4311 N PRO B 641 10.128 2.916 -9.069 1.00168.33 N ANISOU 4311 N PRO B 641 22261 21600 20096 5069 -3900 -2564 N ATOM 4312 CA PRO B 641 9.398 2.145 -8.054 1.00169.53 C ANISOU 4312 CA PRO B 641 22398 21936 20079 4798 -3923 -3082 C ATOM 4313 C PRO B 641 10.316 1.594 -6.965 1.00171.07 C ANISOU 4313 C PRO B 641 22562 22270 20167 4680 -3667 -3135 C ATOM 4314 O PRO B 641 11.483 1.305 -7.230 1.00170.32 O ANISOU 4314 O PRO B 641 22666 22133 19915 4836 -3439 -2756 O ATOM 4315 CB PRO B 641 8.793 0.987 -8.858 1.00168.67 C ANISOU 4315 CB PRO B 641 22809 21890 19387 4828 -3973 -3070 C ATOM 4316 CG PRO B 641 8.821 1.439 -10.282 1.00170.18 C ANISOU 4316 CG PRO B 641 23194 21957 19510 5098 -4069 -2682 C ATOM 4317 CD PRO B 641 10.043 2.286 -10.397 1.00170.23 C ANISOU 4317 CD PRO B 641 23002 21868 19812 5272 -3892 -2255 C ATOM 4318 N ALA B 642 9.785 1.453 -5.755 1.00170.06 N ANISOU 4318 N ALA B 642 22163 22339 20112 4408 -3705 -3585 N ATOM 4319 CA ALA B 642 10.562 0.953 -4.626 1.00168.51 C ANISOU 4319 CA ALA B 642 21894 22329 19802 4257 -3503 -3642 C ATOM 4320 C ALA B 642 11.023 -0.483 -4.853 1.00170.77 C ANISOU 4320 C ALA B 642 22675 22665 19545 4261 -3333 -3403 C ATOM 4321 O ALA B 642 10.453 -1.206 -5.670 1.00172.36 O ANISOU 4321 O ALA B 642 23246 22813 19431 4316 -3408 -3358 O ATOM 4322 CB ALA B 642 9.758 1.058 -3.338 1.00165.79 C ANISOU 4322 CB ALA B 642 21152 22281 19558 3960 -3588 -4174 C ATOM 4323 N CYS B 643 12.057 -0.889 -4.124 1.00183.53 N ANISOU 4323 N CYS B 643 24282 24363 21090 4208 -3134 -3268 N ATOM 4324 CA CYS B 643 12.599 -2.237 -4.246 1.00188.35 C ANISOU 4324 CA CYS B 643 25308 24978 21280 4219 -2986 -3042 C ATOM 4325 C CYS B 643 11.652 -3.274 -3.654 1.00191.85 C ANISOU 4325 C CYS B 643 25827 25615 21451 3921 -3095 -3298 C ATOM 4326 O CYS B 643 10.998 -3.028 -2.641 1.00190.05 O ANISOU 4326 O CYS B 643 25241 25650 21320 3647 -3175 -3612 O ATOM 4327 CB CYS B 643 13.965 -2.333 -3.566 1.00185.94 C ANISOU 4327 CB CYS B 643 24913 24694 21041 4228 -2772 -2805 C ATOM 4328 SG CYS B 643 15.260 -1.339 -4.339 1.00233.86 S ANISOU 4328 SG CYS B 643 30920 30513 27421 4581 -2613 -2367 S ATOM 4329 N ARG B 644 11.589 -4.436 -4.295 1.00180.14 N ANISOU 4329 N ARG B 644 24790 24015 19642 3982 -3106 -3164 N ATOM 4330 CA ARG B 644 10.747 -5.528 -3.826 1.00181.41 C ANISOU 4330 CA ARG B 644 25036 24294 19595 3697 -3241 -3321 C ATOM 4331 C ARG B 644 11.544 -6.462 -2.925 1.00179.56 C ANISOU 4331 C ARG B 644 24823 24151 19251 3529 -3116 -3140 C ATOM 4332 O ARG B 644 11.718 -6.196 -1.736 1.00175.55 O ANISOU 4332 O ARG B 644 23952 23922 18827 3291 -3058 -3201 O ATOM 4333 CB ARG B 644 10.181 -6.306 -5.014 1.00183.05 C ANISOU 4333 CB ARG B 644 25700 24274 19575 3846 -3397 -3311 C ATOM 4334 CG ARG B 644 9.237 -5.501 -5.890 1.00183.73 C ANISOU 4334 CG ARG B 644 25770 24297 19740 3966 -3581 -3475 C ATOM 4335 CD ARG B 644 7.873 -5.354 -5.238 1.00185.07 C ANISOU 4335 CD ARG B 644 25621 24662 20036 3641 -3788 -3806 C ATOM 4336 NE ARG B 644 7.268 -6.654 -4.964 1.00187.02 N ANISOU 4336 NE ARG B 644 26032 24934 20094 3398 -3926 -3853 N ATOM 4337 CZ ARG B 644 6.632 -7.387 -5.872 1.00188.27 C ANISOU 4337 CZ ARG B 644 26548 24887 20100 3461 -4148 -3887 C ATOM 4338 NH1 ARG B 644 6.516 -6.948 -7.118 1.00188.03 N ANISOU 4338 NH1 ARG B 644 26766 24671 20008 3767 -4240 -3882 N ATOM 4339 NH2 ARG B 644 6.112 -8.559 -5.536 1.00188.99 N ANISOU 4339 NH2 ARG B 644 26734 24963 20109 3212 -4304 -3909 N ATOM 4340 N HIS B 645 12.026 -7.557 -3.502 1.00224.58 N ANISOU 4340 N HIS B 645 30939 29622 24769 3664 -3093 -2931 N ATOM 4341 CA HIS B 645 12.847 -8.511 -2.769 1.00222.69 C ANISOU 4341 CA HIS B 645 30741 29391 24481 3537 -3003 -2706 C ATOM 4342 C HIS B 645 14.148 -7.858 -2.314 1.00219.29 C ANISOU 4342 C HIS B 645 30115 29009 24197 3648 -2765 -2500 C ATOM 4343 O HIS B 645 15.056 -7.645 -3.116 1.00221.80 O ANISOU 4343 O HIS B 645 30620 29113 24542 3995 -2605 -2302 O ATOM 4344 CB HIS B 645 13.138 -9.738 -3.634 1.00225.03 C ANISOU 4344 CB HIS B 645 31518 29355 24626 3736 -3047 -2574 C ATOM 4345 CG HIS B 645 14.208 -10.628 -3.080 1.00227.01 C ANISOU 4345 CG HIS B 645 31825 29520 24908 3704 -2941 -2296 C ATOM 4346 ND1 HIS B 645 14.045 -11.351 -1.918 1.00227.45 N ANISOU 4346 ND1 HIS B 645 31686 29732 25001 3308 -3041 -2201 N ATOM 4347 CD2 HIS B 645 15.450 -10.915 -3.534 1.00228.08 C ANISOU 4347 CD2 HIS B 645 32162 29441 25056 4017 -2749 -2068 C ATOM 4348 CE1 HIS B 645 15.146 -12.042 -1.677 1.00227.64 C ANISOU 4348 CE1 HIS B 645 31799 29605 25090 3373 -2943 -1918 C ATOM 4349 NE2 HIS B 645 16.012 -11.797 -2.641 1.00228.02 N ANISOU 4349 NE2 HIS B 645 32083 29418 25136 3811 -2758 -1855 N ATOM 4350 N GLY B 646 14.220 -7.548 -1.021 1.00120.22 N ANISOU 4350 N GLY B 646 17172 16774 11731 3350 -2750 -2548 N ATOM 4351 CA GLY B 646 15.362 -6.874 -0.423 1.00118.70 C ANISOU 4351 CA GLY B 646 16733 16657 11713 3400 -2584 -2402 C ATOM 4352 C GLY B 646 16.680 -7.036 -1.156 1.00118.32 C ANISOU 4352 C GLY B 646 16931 16296 11729 3749 -2393 -2053 C ATOM 4353 O GLY B 646 17.391 -8.025 -0.969 1.00117.94 O ANISOU 4353 O GLY B 646 17045 16148 11617 3743 -2333 -1805 O ATOM 4354 N GLY B 647 17.006 -6.055 -1.991 1.00171.47 N ANISOU 4354 N GLY B 647 23657 22878 18614 4053 -2300 -2008 N ATOM 4355 CA GLY B 647 16.138 -4.910 -2.195 1.00167.33 C ANISOU 4355 CA GLY B 647 22914 22426 18238 4048 -2417 -2281 C ATOM 4356 C GLY B 647 16.678 -3.647 -1.554 1.00160.87 C ANISOU 4356 C GLY B 647 21654 21689 17781 4028 -2387 -2315 C ATOM 4357 O GLY B 647 15.920 -2.739 -1.215 1.00159.77 O ANISOU 4357 O GLY B 647 21201 21675 17829 3918 -2528 -2641 O ATOM 4358 N VAL B 648 17.994 -3.591 -1.387 1.00145.76 N ANISOU 4358 N VAL B 648 19694 19681 16007 4145 -2224 -1997 N ATOM 4359 CA VAL B 648 18.640 -2.426 -0.796 1.00142.44 C ANISOU 4359 CA VAL B 648 18852 19281 15987 4138 -2228 -2003 C ATOM 4360 C VAL B 648 18.880 -1.339 -1.843 1.00144.45 C ANISOU 4360 C VAL B 648 19047 19275 16563 4439 -2204 -1828 C ATOM 4361 O VAL B 648 19.727 -1.486 -2.723 1.00147.19 O ANISOU 4361 O VAL B 648 19595 19427 16902 4717 -2022 -1409 O ATOM 4362 CB VAL B 648 19.973 -2.805 -0.113 1.00139.50 C ANISOU 4362 CB VAL B 648 18410 18916 15679 4108 -2096 -1704 C ATOM 4363 CG1 VAL B 648 20.786 -3.737 -1.001 1.00140.61 C ANISOU 4363 CG1 VAL B 648 18946 18827 15654 4370 -1887 -1276 C ATOM 4364 CG2 VAL B 648 20.766 -1.555 0.245 1.00137.94 C ANISOU 4364 CG2 VAL B 648 17806 18645 15960 4166 -2117 -1653 C ATOM 4365 N CYS B 649 18.122 -0.251 -1.745 1.00151.42 N ANISOU 4365 N CYS B 649 19623 20169 17741 4387 -2393 -2136 N ATOM 4366 CA CYS B 649 18.249 0.855 -2.690 1.00152.49 C ANISOU 4366 CA CYS B 649 19640 20045 18255 4632 -2431 -1938 C ATOM 4367 C CYS B 649 19.476 1.708 -2.387 1.00152.81 C ANISOU 4367 C CYS B 649 19345 19929 18789 4713 -2390 -1669 C ATOM 4368 O CYS B 649 19.746 2.037 -1.232 1.00151.96 O ANISOU 4368 O CYS B 649 18908 19926 18902 4525 -2483 -1916 O ATOM 4369 CB CYS B 649 16.991 1.724 -2.678 1.00151.92 C ANISOU 4369 CB CYS B 649 19320 19986 18418 4548 -2692 -2363 C ATOM 4370 SG CYS B 649 17.067 3.149 -3.791 1.00181.05 S ANISOU 4370 SG CYS B 649 22796 23326 22667 4810 -2814 -2074 S ATOM 4371 N VAL B 650 20.214 2.066 -3.433 1.00137.77 N ANISOU 4371 N VAL B 650 17505 17796 17044 4991 -2261 -1154 N ATOM 4372 CA VAL B 650 21.427 2.861 -3.283 1.00138.75 C ANISOU 4372 CA VAL B 650 17300 17735 17685 5079 -2220 -798 C ATOM 4373 C VAL B 650 21.407 4.075 -4.207 1.00143.91 C ANISOU 4373 C VAL B 650 17725 18132 18822 5261 -2326 -500 C ATOM 4374 O VAL B 650 20.940 5.149 -3.828 1.00142.74 O ANISOU 4374 O VAL B 650 17182 17852 19201 5166 -2610 -776 O ATOM 4375 CB VAL B 650 22.685 2.025 -3.587 1.00139.44 C ANISOU 4375 CB VAL B 650 17621 17814 17544 5243 -1902 -291 C ATOM 4376 CG1 VAL B 650 23.941 2.814 -3.248 1.00139.42 C ANISOU 4376 CG1 VAL B 650 17224 17633 18117 5286 -1885 59 C ATOM 4377 CG2 VAL B 650 22.651 0.713 -2.818 1.00137.72 C ANISOU 4377 CG2 VAL B 650 17663 17810 16856 5073 -1822 -514 C ATOM 4378 N ARG B 651 21.918 3.893 -5.421 1.00197.73 N ANISOU 4378 N ARG B 651 24771 24894 25462 5529 -2106 70 N ATOM 4379 CA ARG B 651 21.973 4.965 -6.410 1.00202.56 C ANISOU 4379 CA ARG B 651 25177 25311 26476 5703 -2183 502 C ATOM 4380 C ARG B 651 20.570 5.356 -6.876 1.00205.23 C ANISOU 4380 C ARG B 651 25553 25640 26787 5666 -2438 200 C ATOM 4381 O ARG B 651 19.608 4.632 -6.620 1.00205.73 O ANISOU 4381 O ARG B 651 25879 25875 26412 5547 -2490 -283 O ATOM 4382 CB ARG B 651 22.835 4.541 -7.591 1.00205.27 C ANISOU 4382 CB ARG B 651 25775 25724 26493 6004 -1840 1181 C ATOM 4383 N PRO B 652 20.451 6.509 -7.560 1.00154.57 N ANISOU 4383 N PRO B 652 18842 19007 20879 5756 -2620 522 N ATOM 4384 CA PRO B 652 19.160 7.017 -8.039 1.00153.61 C ANISOU 4384 CA PRO B 652 18692 18829 20846 5728 -2905 296 C ATOM 4385 C PRO B 652 18.255 5.935 -8.630 1.00151.70 C ANISOU 4385 C PRO B 652 18989 18848 19802 5766 -2818 89 C ATOM 4386 O PRO B 652 18.491 5.465 -9.743 1.00154.14 O ANISOU 4386 O PRO B 652 19642 19289 19635 5983 -2621 524 O ATOM 4387 CB PRO B 652 19.569 8.013 -9.124 1.00157.37 C ANISOU 4387 CB PRO B 652 18937 19110 21746 5908 -2964 1016 C ATOM 4388 CG PRO B 652 20.873 8.545 -8.648 1.00157.94 C ANISOU 4388 CG PRO B 652 18640 18998 22374 5914 -2892 1373 C ATOM 4389 CD PRO B 652 21.558 7.420 -7.909 1.00155.19 C ANISOU 4389 CD PRO B 652 18556 18862 21547 5876 -2590 1175 C ATOM 4390 N ASN B 653 17.226 5.555 -7.877 1.00178.42 N ANISOU 4390 N ASN B 653 22422 22325 23047 5560 -2974 -581 N ATOM 4391 CA ASN B 653 16.241 4.573 -8.326 1.00176.78 C ANISOU 4391 CA ASN B 653 22666 22316 22185 5550 -2969 -833 C ATOM 4392 C ASN B 653 16.855 3.295 -8.892 1.00175.89 C ANISOU 4392 C ASN B 653 23077 22388 21366 5712 -2644 -576 C ATOM 4393 O ASN B 653 16.305 2.689 -9.812 1.00178.80 O ANISOU 4393 O ASN B 653 23838 22864 21232 5833 -2637 -544 O ATOM 4394 CB ASN B 653 15.288 5.193 -9.352 1.00179.76 C ANISOU 4394 CB ASN B 653 23038 22610 22653 5636 -3213 -728 C ATOM 4395 CG ASN B 653 14.595 6.435 -8.827 1.00180.72 C ANISOU 4395 CG ASN B 653 22624 22505 23534 5497 -3568 -1031 C ATOM 4396 OD1 ASN B 653 15.244 7.390 -8.400 1.00182.37 O ANISOU 4396 OD1 ASN B 653 22396 22498 24398 5489 -3643 -903 O ATOM 4397 ND2 ASN B 653 13.268 6.432 -8.864 1.00179.96 N ANISOU 4397 ND2 ASN B 653 22540 22438 23399 5395 -3809 -1452 N ATOM 4398 N LYS B 654 17.992 2.890 -8.337 1.00130.96 N ANISOU 4398 N LYS B 654 17376 16722 15661 5725 -2401 -421 N ATOM 4399 CA LYS B 654 18.655 1.666 -8.769 1.00127.92 C ANISOU 4399 CA LYS B 654 17437 16477 14691 5893 -2096 -221 C ATOM 4400 C LYS B 654 18.690 0.641 -7.641 1.00126.56 C ANISOU 4400 C LYS B 654 17374 16391 14321 5678 -2048 -603 C ATOM 4401 O LYS B 654 19.609 0.637 -6.822 1.00127.92 O ANISOU 4401 O LYS B 654 17350 16541 14713 5607 -1935 -516 O ATOM 4402 CB LYS B 654 20.070 1.967 -9.266 1.00127.47 C ANISOU 4402 CB LYS B 654 17284 16383 14765 6138 -1818 409 C ATOM 4403 CG LYS B 654 20.821 0.752 -9.794 1.00131.12 C ANISOU 4403 CG LYS B 654 18171 16994 14655 6371 -1481 606 C ATOM 4404 CD LYS B 654 21.997 1.168 -10.663 1.00131.49 C ANISOU 4404 CD LYS B 654 18124 17081 14755 6676 -1197 1282 C ATOM 4405 CE LYS B 654 22.937 2.097 -9.916 1.00131.95 C ANISOU 4405 CE LYS B 654 17664 16959 15513 6575 -1191 1574 C ATOM 4406 NZ LYS B 654 23.932 2.731 -10.824 1.00136.46 N ANISOU 4406 NZ LYS B 654 18044 17562 16241 6837 -966 2310 N ATOM 4407 N CYS B 655 17.680 -0.223 -7.601 1.00137.70 N ANISOU 4407 N CYS B 655 19080 17902 15339 5561 -2160 -989 N ATOM 4408 CA CYS B 655 17.596 -1.258 -6.577 1.00136.63 C ANISOU 4408 CA CYS B 655 19041 17865 15006 5328 -2148 -1292 C ATOM 4409 C CYS B 655 18.768 -2.227 -6.680 1.00138.30 C ANISOU 4409 C CYS B 655 19506 18064 14979 5489 -1870 -997 C ATOM 4410 O CYS B 655 19.461 -2.272 -7.696 1.00139.12 O ANISOU 4410 O CYS B 655 19791 18126 14942 5810 -1671 -632 O ATOM 4411 CB CYS B 655 16.272 -2.018 -6.682 1.00135.63 C ANISOU 4411 CB CYS B 655 19177 17819 14538 5186 -2339 -1679 C ATOM 4412 SG CYS B 655 14.808 -1.030 -6.295 1.00137.85 S ANISOU 4412 SG CYS B 655 19103 18147 15126 4948 -2668 -2114 S ATOM 4413 N LEU B 656 18.986 -3.002 -5.623 1.00161.31 N ANISOU 4413 N LEU B 656 22406 21039 17848 5267 -1857 -1144 N ATOM 4414 CA LEU B 656 20.095 -3.945 -5.589 1.00164.76 C ANISOU 4414 CA LEU B 656 23034 21428 18142 5396 -1629 -881 C ATOM 4415 C LEU B 656 19.620 -5.331 -5.165 1.00165.29 C ANISOU 4415 C LEU B 656 23377 21523 17904 5221 -1715 -1111 C ATOM 4416 O LEU B 656 19.609 -5.659 -3.978 1.00165.75 O ANISOU 4416 O LEU B 656 23258 21676 18043 4912 -1795 -1221 O ATOM 4417 CB LEU B 656 21.186 -3.448 -4.639 1.00166.71 C ANISOU 4417 CB LEU B 656 22905 21669 18768 5302 -1537 -678 C ATOM 4418 CG LEU B 656 22.586 -4.022 -4.854 1.00171.10 C ANISOU 4418 CG LEU B 656 23560 22132 19317 5533 -1260 -269 C ATOM 4419 CD1 LEU B 656 23.123 -3.611 -6.215 1.00174.42 C ANISOU 4419 CD1 LEU B 656 24089 22490 19691 5940 -1041 94 C ATOM 4420 CD2 LEU B 656 23.524 -3.570 -3.747 1.00170.62 C ANISOU 4420 CD2 LEU B 656 23105 22072 19651 5369 -1244 -120 C ATOM 4421 N CYS B 657 19.229 -6.141 -6.143 1.00150.53 N ANISOU 4421 N CYS B 657 21926 19579 15691 5416 -1722 -1172 N ATOM 4422 CA CYS B 657 18.715 -7.480 -5.877 1.00147.65 C ANISOU 4422 CA CYS B 657 21828 19167 15105 5264 -1859 -1379 C ATOM 4423 C CYS B 657 19.820 -8.420 -5.405 1.00144.49 C ANISOU 4423 C CYS B 657 21485 18665 14750 5297 -1713 -1164 C ATOM 4424 O CYS B 657 20.881 -8.508 -6.023 1.00145.31 O ANISOU 4424 O CYS B 657 21690 18676 14845 5636 -1469 -905 O ATOM 4425 CB CYS B 657 18.039 -8.048 -7.126 1.00148.83 C ANISOU 4425 CB CYS B 657 22406 19226 14916 5500 -1948 -1540 C ATOM 4426 SG CYS B 657 16.771 -6.975 -7.841 1.00151.77 S ANISOU 4426 SG CYS B 657 22731 19695 15238 5497 -2144 -1735 S ATOM 4427 N TYR B 661 18.049 -12.772 -8.183 1.00137.77 N ANISOU 4427 N TYR B 661 22199 17121 13026 5832 -2271 -1980 N ATOM 4428 CA TYR B 661 17.015 -11.974 -8.831 1.00137.57 C ANISOU 4428 CA TYR B 661 22216 17247 12806 5836 -2396 -2162 C ATOM 4429 C TYR B 661 17.615 -10.897 -9.725 1.00138.75 C ANISOU 4429 C TYR B 661 22346 17572 12800 6201 -2112 -1971 C ATOM 4430 O TYR B 661 18.773 -10.509 -9.562 1.00137.37 O ANISOU 4430 O TYR B 661 22002 17447 12746 6351 -1809 -1661 O ATOM 4431 CB TYR B 661 16.095 -11.351 -7.790 1.00134.58 C ANISOU 4431 CB TYR B 661 21482 17025 12625 5356 -2572 -2210 C ATOM 4432 N LEU B 662 16.822 -10.418 -10.675 1.00160.39 N ANISOU 4432 N LEU B 662 25240 20408 15292 6332 -2230 -2116 N ATOM 4433 CA LEU B 662 17.273 -9.364 -11.569 1.00164.66 C ANISOU 4433 CA LEU B 662 25737 21146 15682 6646 -2002 -1870 C ATOM 4434 C LEU B 662 16.134 -8.407 -11.880 1.00166.88 C ANISOU 4434 C LEU B 662 25916 21540 15951 6508 -2227 -1955 C ATOM 4435 O LEU B 662 14.983 -8.657 -11.522 1.00165.55 O ANISOU 4435 O LEU B 662 25757 21307 15840 6216 -2544 -2251 O ATOM 4436 CB LEU B 662 17.831 -9.956 -12.862 1.00168.01 C ANISOU 4436 CB LEU B 662 26553 21613 15672 7148 -1843 -1893 C ATOM 4437 CG LEU B 662 19.173 -10.676 -12.749 1.00169.53 C ANISOU 4437 CG LEU B 662 26790 21725 15900 7397 -1539 -1748 C ATOM 4438 CD1 LEU B 662 19.567 -11.303 -14.081 1.00173.05 C ANISOU 4438 CD1 LEU B 662 27626 22261 15863 7922 -1403 -1886 C ATOM 4439 CD2 LEU B 662 20.255 -9.722 -12.258 1.00169.66 C ANISOU 4439 CD2 LEU B 662 26406 21852 16206 7396 -1208 -1271 C ATOM 4440 N GLY B 663 16.470 -7.310 -12.549 1.00178.15 N ANISOU 4440 N GLY B 663 27213 23133 17342 6715 -2069 -1659 N ATOM 4441 CA GLY B 663 15.494 -6.319 -12.954 1.00180.37 C ANISOU 4441 CA GLY B 663 27371 23500 17660 6628 -2284 -1673 C ATOM 4442 C GLY B 663 15.698 -5.018 -12.204 1.00181.36 C ANISOU 4442 C GLY B 663 26984 23639 18284 6430 -2231 -1434 C ATOM 4443 O GLY B 663 16.472 -4.967 -11.250 1.00178.26 O ANISOU 4443 O GLY B 663 26345 23198 18187 6307 -2068 -1323 O ATOM 4444 N PRO B 664 14.990 -3.955 -12.623 1.00162.23 N ANISOU 4444 N PRO B 664 24383 21264 15993 6396 -2407 -1371 N ATOM 4445 CA PRO B 664 15.111 -2.622 -12.012 1.00160.30 C ANISOU 4445 CA PRO B 664 23626 20984 16298 6237 -2420 -1185 C ATOM 4446 C PRO B 664 14.622 -2.584 -10.568 1.00155.73 C ANISOU 4446 C PRO B 664 22739 20334 16096 5840 -2561 -1533 C ATOM 4447 O PRO B 664 15.180 -1.841 -9.753 1.00153.07 O ANISOU 4447 O PRO B 664 22006 19967 16188 5727 -2483 -1429 O ATOM 4448 CB PRO B 664 14.209 -1.744 -12.898 1.00163.34 C ANISOU 4448 CB PRO B 664 23959 21399 16702 6291 -2664 -1120 C ATOM 4449 CG PRO B 664 14.085 -2.501 -14.172 1.00168.90 C ANISOU 4449 CG PRO B 664 25161 22238 16775 6582 -2654 -1093 C ATOM 4450 CD PRO B 664 14.064 -3.936 -13.766 1.00165.62 C ANISOU 4450 CD PRO B 664 25078 21769 16081 6530 -2633 -1461 C ATOM 4451 N GLN B 665 13.602 -3.391 -10.271 1.00172.52 N ANISOU 4451 N GLN B 665 25036 22461 18053 5636 -2773 -1935 N ATOM 4452 CA GLN B 665 13.048 -3.515 -8.922 1.00171.05 C ANISOU 4452 CA GLN B 665 24573 22303 18114 5251 -2892 -2262 C ATOM 4453 C GLN B 665 13.065 -4.951 -8.400 1.00173.51 C ANISOU 4453 C GLN B 665 25137 22614 18174 5110 -2879 -2417 C ATOM 4454 O GLN B 665 12.387 -5.271 -7.419 1.00173.77 O ANISOU 4454 O GLN B 665 24999 22725 18301 4773 -3014 -2675 O ATOM 4455 CB GLN B 665 11.619 -2.978 -8.881 1.00169.34 C ANISOU 4455 CB GLN B 665 24175 22112 18056 5059 -3203 -2575 C ATOM 4456 CG GLN B 665 11.493 -1.554 -9.363 1.00169.34 C ANISOU 4456 CG GLN B 665 23883 22059 18398 5174 -3284 -2428 C ATOM 4457 CD GLN B 665 11.533 -1.458 -10.868 1.00171.97 C ANISOU 4457 CD GLN B 665 24534 22359 18447 5493 -3308 -2136 C ATOM 4458 OE1 GLN B 665 11.287 -2.441 -11.564 1.00173.69 O ANISOU 4458 OE1 GLN B 665 25194 22604 18196 5604 -3344 -2199 O ATOM 4459 NE2 GLN B 665 11.824 -0.268 -11.382 1.00173.25 N ANISOU 4459 NE2 GLN B 665 24456 22473 18899 5640 -3313 -1814 N ATOM 4460 N CYS B 666 13.851 -5.807 -9.046 1.00180.11 N ANISOU 4460 N CYS B 666 26347 23373 18713 5370 -2721 -2246 N ATOM 4461 CA CYS B 666 13.873 -7.236 -8.720 1.00178.62 C ANISOU 4461 CA CYS B 666 26425 23103 18340 5278 -2759 -2376 C ATOM 4462 C CYS B 666 12.642 -7.963 -9.255 1.00179.56 C ANISOU 4462 C CYS B 666 26830 23152 18244 5213 -3073 -2680 C ATOM 4463 O CYS B 666 11.540 -7.420 -9.318 1.00180.36 O ANISOU 4463 O CYS B 666 26799 23311 18420 5060 -3296 -2861 O ATOM 4464 CB CYS B 666 14.008 -7.471 -7.208 1.00175.99 C ANISOU 4464 CB CYS B 666 25778 22842 18248 4904 -2747 -2412 C ATOM 4465 SG CYS B 666 15.358 -6.550 -6.444 1.00245.74 S ANISOU 4465 SG CYS B 666 34225 31757 27388 4929 -2456 -2110 S ATOM 4466 N GLU B 667 12.726 -9.124 -9.643 1.00180.04 N ANISOU 4466 N GLU B 667 27248 23070 18089 5317 -3134 -2763 N TER 4467 GLU B 667 HETATM 4468 ZN ZN A1192 -13.270 35.489 -6.995 1.00 60.35 ZN HETATM 4469 CA CA A1193 -18.414 44.429 -7.263 1.00 71.86 CA HETATM 4470 CA CA A1194 -14.810 45.306 -9.475 1.00 89.81 CA HETATM 4471 NA NA B1667 11.932 10.333 9.784 1.00 64.33 NA HETATM 4472 NA NA B1668 -10.458 23.235 21.086 1.00 29.19 NA HETATM 4473 NA NA B1669 -1.777 33.092 36.927 1.00 46.28 NA HETATM 4474 CA CA B1670 3.555 48.091 14.898 1.00 72.55 CA CONECT 414 4469 CONECT 415 4469 CONECT 423 4469 4470 CONECT 424 4469 CONECT 455 4469 CONECT 456 4469 CONECT 693 4469 CONECT 704 4469 CONECT 705 4470 CONECT 730 4470 CONECT 820 4468 CONECT 875 4468 CONECT 1161 4468 CONECT 1230 3649 CONECT 2254 4474 CONECT 2476 4468 CONECT 2477 4468 CONECT 2617 4188 CONECT 2676 4472 CONECT 2693 4472 CONECT 2877 3009 CONECT 2922 4473 CONECT 2936 4473 CONECT 2960 4473 CONECT 3009 2877 CONECT 3140 4472 CONECT 3145 4472 CONECT 3161 4472 CONECT 3352 3967 CONECT 3649 1230 CONECT 3967 3352 CONECT 4070 4142 CONECT 4101 4182 CONECT 4142 4070 CONECT 4182 4101 CONECT 4188 2617 CONECT 4194 4263 CONECT 4263 4194 CONECT 4301 4370 CONECT 4328 4412 CONECT 4370 4301 CONECT 4412 4328 CONECT 4426 4465 CONECT 4465 4426 CONECT 4468 820 875 1161 2476 CONECT 4468 2477 CONECT 4469 414 415 423 424 CONECT 4469 455 456 693 704 CONECT 4470 423 705 730 CONECT 4472 2676 2693 3140 3145 CONECT 4472 3161 CONECT 4473 2922 2936 2960 CONECT 4474 2254 MASTER 553 0 7 8 34 0 9 6 4472 2 53 48 END
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Related entries of code: 2wfx
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
2wg4
RCSB PDB
PDBbind
155aa, >2WG4_1|Chain... at 99%
3ho5
RCSB PDB
PDBbind
169aa, >3HO5_2|Chain... *
3mxw
RCSB PDB
PDBbind
169aa, >3MXW_1|Chain... at 100%
4c4n
RCSB PDB
PDBbind
164aa, >4C4N_1|Chains... at 94%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
3h6s
RCSB PDB
PDBbind
152-mer
Entry Information
PDB ID
2wfx
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
HUMAN HEDGEHOG-INTERACTING PROTEIN HIP
Ligand Name
152-mer
EC.Number
E.C.-.-.-.-
Resolution
3.2(Å)
Affinity (Kd/Ki/IC50)
Kd=14nM
Release Year
2009
Protein/NA Sequence
Check fasta file
Primary Reference
(2009) Nat.Struct.Mol.Biol. Vol. 16: pp. 698-703
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):
Q62226
Q96QV1
Entrez Gene ID
NCBI Entrez Gene ID:
20423
64399
ASD
Information of known allosteric effects of PDB entries
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