HEADER SIGNALING PROTEIN, HYDROLASE/ANTIBIOTIC 12-AUG-10 3OE0 TITLE CRYSTAL STRUCTURE OF THE CXCR4 CHEMOKINE RECEPTOR IN COMPLEX WITH A TITLE 2 CYCLIC PEPTIDE ANTAGONIST CVX15 COMPND MOL_ID: 1; COMPND 2 MOLECULE: C-X-C CHEMOKINE RECEPTOR TYPE 4, LYSOZYME CHIMERA; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CXCR4 RESIDUES 2-228, LYSOZYME RESIDUES 1002-1161, CXCR4 COMPND 5 RESIDUES 231-319; COMPND 6 SYNONYM: CXC-R4, CXCR-4, STROMAL CELL-DERIVED FACTOR 1 RECEPTOR, SDF- COMPND 7 1 RECEPTOR, FUSIN, LEUKOCYTE-DERIVED SEVEN TRANSMEMBRANE DOMAIN COMPND 8 RECEPTOR, LESTR, LCR1, FB22, NPYRL, HM89, LYSIS PROTEIN, MURAMIDASE, COMPND 9 ENDOLYSIN; COMPND 10 EC: 3.2.1.17; COMPND 11 ENGINEERED: YES; COMPND 12 MUTATION: YES; COMPND 13 MOL_ID: 2; COMPND 14 MOLECULE: POLYPHEMUSIN ANALOG, CXC CHEMOKINE RECEPTOR ANTAGONIST; COMPND 15 CHAIN: I; COMPND 16 ENGINEERED: YES; COMPND 17 OTHER_DETAILS: CYCLIC PEPTIDE CVX15 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_TAXID: 9606, 10665; SOURCE 4 GENE: CXCR4, CXCR4_HUMAN, E; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 OTHER_DETAILS: SYNTHETIC ANALOG AND DERIVATIVE OF POLYPHEMUSIN FROM SOURCE 13 LIMULUS POLYPHEMUS (HORSESHOE CRAB) KEYWDS STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED KEYWDS 2 TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D, 7TM, G KEYWDS 3 PROTEIN-COUPLED RECEPTOR, GPCR, SIGNAL TRANSDUCTION, HYDROLASE, KEYWDS 4 CANCER, HIV-1 CO-RECEPTOR, CHEMOKINE, CXCL12, CHIMERA, T4L FUSION, KEYWDS 5 MEMBRANE PROTEIN, TRANSMEMBRANE, ANTIMICROBIAL, ANTIBIOTIC, KEYWDS 6 POLYPHEMUSIN, SIGNALING PROTEIN, HYDROLASE-ANTIBIOTIC COMPLEX, PSI- KEYWDS 7 BIOLOGY, GPCR NETWORK EXPDTA X-RAY DIFFRACTION AUTHOR B.WU,C.D.MOL,G.W.HAN,V.KATRITCH,E.Y.T.CHIEN,W.LIU,V.CHEREZOV, AUTHOR 2 R.C.STEVENS,ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE AUTHOR 3 (ATCG3D),GPCR NETWORK (GPCR) REVDAT 7 06-OCT-21 3OE0 1 SEQADV LINK REVDAT 6 26-JUL-17 3OE0 1 SOURCE REMARK REVDAT 5 02-MAY-12 3OE0 1 REMARK VERSN REVDAT 4 16-FEB-11 3OE0 1 HEADER REVDAT 3 05-JAN-11 3OE0 1 JRNL REVDAT 2 01-DEC-10 3OE0 1 COMPND LINK REMARK REVDAT 1 27-OCT-10 3OE0 0 JRNL AUTH B.WU,E.Y.CHIEN,C.D.MOL,G.FENALTI,W.LIU,V.KATRITCH,R.ABAGYAN, JRNL AUTH 2 A.BROOUN,P.WELLS,F.C.BI,D.J.HAMEL,P.KUHN,T.M.HANDEL, JRNL AUTH 3 V.CHEREZOV,R.C.STEVENS JRNL TITL STRUCTURES OF THE CXCR4 CHEMOKINE GPCR WITH SMALL-MOLECULE JRNL TITL 2 AND CYCLIC PEPTIDE ANTAGONISTS. JRNL REF SCIENCE V. 330 1066 2010 JRNL REFN ISSN 0036-8075 JRNL PMID 20929726 JRNL DOI 10.1126/SCIENCE.1194396 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0088 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.93 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2 REMARK 3 NUMBER OF REFLECTIONS : 16707 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.215 REMARK 3 FREE R VALUE : 0.267 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 898 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98 REMARK 3 REFLECTION IN BIN (WORKING SET) : 961 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.60 REMARK 3 BIN R VALUE (WORKING SET) : 0.3400 REMARK 3 BIN FREE R VALUE SET COUNT : 40 REMARK 3 BIN FREE R VALUE : 0.3970 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3634 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 6 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.05 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.10000 REMARK 3 B22 (A**2) : -0.41000 REMARK 3 B33 (A**2) : 0.41000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.20000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.839 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.374 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.309 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.246 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3728 ; 0.009 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 2530 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5053 ; 1.101 ; 1.956 REMARK 3 BOND ANGLES OTHERS (DEGREES): 6125 ; 0.855 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 441 ; 5.801 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 162 ;37.366 ;22.840 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 625 ;18.646 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;15.924 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 572 ; 0.060 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4046 ; 0.004 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 822 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2232 ; 0.385 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 901 ; 0.045 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3608 ; 0.733 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1496 ; 0.802 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1445 ; 1.419 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 25 A 228 REMARK 3 ORIGIN FOR THE GROUP (A): 56.8558 15.0034 6.2863 REMARK 3 T TENSOR REMARK 3 T11: 0.0526 T22: 0.1669 REMARK 3 T33: 0.2390 T12: -0.0106 REMARK 3 T13: 0.0657 T23: -0.0696 REMARK 3 L TENSOR REMARK 3 L11: 0.1326 L22: 1.6844 REMARK 3 L33: 1.1636 L12: 0.2962 REMARK 3 L13: 0.2334 L23: -0.2676 REMARK 3 S TENSOR REMARK 3 S11: -0.0594 S12: 0.0472 S13: -0.0348 REMARK 3 S21: -0.1450 S22: 0.1410 S23: -0.2135 REMARK 3 S31: -0.0219 S32: 0.1337 S33: -0.0817 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1002 A 1161 REMARK 3 ORIGIN FOR THE GROUP (A): 35.2422 -20.8302 24.5296 REMARK 3 T TENSOR REMARK 3 T11: 0.1686 T22: 0.0892 REMARK 3 T33: 0.1050 T12: -0.0329 REMARK 3 T13: -0.0135 T23: 0.0187 REMARK 3 L TENSOR REMARK 3 L11: 4.4070 L22: 0.3599 REMARK 3 L33: 1.9082 L12: 0.9320 REMARK 3 L13: 0.7447 L23: -0.3647 REMARK 3 S TENSOR REMARK 3 S11: -0.2832 S12: 0.0474 S13: -0.0242 REMARK 3 S21: -0.1104 S22: 0.0112 S23: -0.0591 REMARK 3 S31: 0.0904 S32: 0.0806 S33: 0.2720 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 231 A 303 REMARK 3 ORIGIN FOR THE GROUP (A): 50.1136 16.3673 15.7284 REMARK 3 T TENSOR REMARK 3 T11: 0.1509 T22: 0.1712 REMARK 3 T33: 0.1511 T12: -0.0758 REMARK 3 T13: 0.0310 T23: -0.0263 REMARK 3 L TENSOR REMARK 3 L11: 0.4506 L22: 3.7115 REMARK 3 L33: 1.0419 L12: -0.6918 REMARK 3 L13: -0.4711 L23: 0.5601 REMARK 3 S TENSOR REMARK 3 S11: 0.0483 S12: -0.0562 S13: 0.0183 REMARK 3 S21: 0.4368 S22: -0.1400 S23: 0.0068 REMARK 3 S31: 0.0942 S32: -0.0059 S33: 0.0917 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3OE0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-10. REMARK 100 THE DEPOSITION ID IS D_1000060996. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-JUN-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 14 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0330 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17656 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9 REMARK 200 DATA REDUNDANCY : 6.000 REMARK 200 R MERGE (I) : 0.12000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 73.6 REMARK 200 DATA REDUNDANCY IN SHELL : 3.90 REMARK 200 R MERGE FOR SHELL (I) : 0.63000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.01 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: LIPIDIC CUBIC PHASE MADE OF MONOOLEIN REMARK 280 AND CHOLESTEROL, 25% PEG400, 0.3M POTASSIUM SODIUM TARTRATE, 0.1 REMARK 280 M TRIS PH 7.0, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 41.04000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.43000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 41.04000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 72.43000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 82.08000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 400 REMARK 400 COMPOUND REMARK 400 REMARK 400 THE POLYPHEMUSIN ANALOG, CXC CHEMOKINE RECEPTOR ANTAGONIST IS REMARK 400 OLIGOPEPTIDE, A MEMBER OF ANTAGONIST CLASS. REMARK 400 REMARK 400 GROUP: 1 REMARK 400 NAME: POLYPHEMUSIN ANALOG, CXC CHEMOKINE RECEPTOR ANTAGONIST REMARK 400 CHAIN: I REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER REMARK 400 DESCRIPTION: NULL 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 ASP A -9 REMARK 465 TYR A -8 REMARK 465 LYS A -7 REMARK 465 ASP A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ALA A -2 REMARK 465 GLY A -1 REMARK 465 ALA A 0 REMARK 465 PRO A 1 REMARK 465 GLU A 2 REMARK 465 GLY A 3 REMARK 465 ILE A 4 REMARK 465 SER A 5 REMARK 465 ILE A 6 REMARK 465 TYR A 7 REMARK 465 THR A 8 REMARK 465 SER A 9 REMARK 465 ASP A 10 REMARK 465 ASN A 11 REMARK 465 TYR A 12 REMARK 465 THR A 13 REMARK 465 GLU A 14 REMARK 465 GLU A 15 REMARK 465 MET A 16 REMARK 465 GLY A 17 REMARK 465 SER A 18 REMARK 465 GLY A 19 REMARK 465 ASP A 20 REMARK 465 TYR A 21 REMARK 465 ASP A 22 REMARK 465 SER A 23 REMARK 465 MET A 24 REMARK 465 LYS A 67 REMARK 465 LYS A 68 REMARK 465 LEU A 69 REMARK 465 ARG A 70 REMARK 465 SER A 1200 REMARK 465 GLY A 1201 REMARK 465 SER A 1202 REMARK 465 PHE A 304 REMARK 465 LEU A 305 REMARK 465 GLY A 306 REMARK 465 ALA A 307 REMARK 465 LYS A 308 REMARK 465 PHE A 309 REMARK 465 LYS A 310 REMARK 465 THR A 311 REMARK 465 SER A 312 REMARK 465 ALA A 313 REMARK 465 GLN A 314 REMARK 465 HIS A 315 REMARK 465 ALA A 316 REMARK 465 LEU A 317 REMARK 465 THR A 318 REMARK 465 SER A 319 REMARK 465 GLY A 320 REMARK 465 ARG A 321 REMARK 465 PRO A 322 REMARK 465 LEU A 323 REMARK 465 GLU A 324 REMARK 465 VAL A 325 REMARK 465 LEU A 326 REMARK 465 PHE A 327 REMARK 465 GLN A 328 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 GLN A 233 CG CD OE1 NE2 REMARK 470 LYS A 234 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG I 2 CA - C - N ANGL. DEV. = 17.3 DEGREES REMARK 500 ARG I 2 O - C - N ANGL. DEV. = -16.3 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR A 65 -165.19 -111.28 REMARK 500 ALA A 100 -74.07 -115.86 REMARK 500 VAL A 160 -63.58 -124.08 REMARK 500 ARG A1080 40.34 -109.31 REMARK 500 GLN A 233 77.07 42.60 REMARK 500 LYS A 234 48.31 -142.01 REMARK 500 GLN A 272 23.36 -148.90 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF POLYPHEMUSIN ANALOG, REMARK 800 CXC CHEMOKINE RECEPTOR ANTAGONIST REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ATCG3D_11 RELATED DB: TARGETDB REMARK 900 RELATED ID: 3ODU RELATED DB: PDB REMARK 900 SAME PROTEIN AT 2.5 A IN P21 SPACEGROUP REMARK 900 RELATED ID: 3OE6 RELATED DB: PDB REMARK 900 SAME PROTEIN IN I222 SPACEGROUP REMARK 900 RELATED ID: 3OE8 RELATED DB: PDB REMARK 900 SAME PROTEIN IN P1 SPACEGROUP WITH 3 MOLECULES PER ASYMMETRIC UNIT REMARK 900 RELATED ID: 3OE9 RELATED DB: PDB REMARK 900 SAME PROTEIN IN P1 SPACEGROUP WITH 2 MOLECULES PER ASYMMETRIC UNIT REMARK 900 RELATED ID: GPCR-34 RELATED DB: TARGETTRACK REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE PROTEIN IS A FUSION PROTEIN WITH RESIDUES ASN1002-TYR1161 OF T4 REMARK 999 LYSOZYME INSERTED BETWEEN HIS228 AND GLY231 OF CXCR4, AS INDICATED REMARK 999 AS CXCR4-3 IN THE PUBLICATION. THE SMALL CYCLIC PEPTIDE NAMED CVX15 REMARK 999 IS CXC CHEMOKINE RECEPTOR (CXCR)4 ANTAGONIST, AS WELL AS ANALOG OF REMARK 999 POLYPHEMUSIN FROM LIMULUS POLYPHEMUS (HORSESHOE CRAB). PART OF THE REMARK 999 SEQUENCE OF THE SMALL PEPTIDE HAS SIMILARITY TO UNITPROT ENTRY REMARK 999 P14215 WITH SEQUENCE RRWCFRVCYRGFCYRKCR DBREF 3OE0 A 2 228 UNP P61073 CXCR4_HUMAN 2 228 DBREF 3OE0 A 1002 1161 UNP P00720 LYS_BPT4 1002 1161 DBREF 3OE0 A 231 319 UNP P61073 CXCR4_HUMAN 231 319 DBREF 3OE0 I 1 16 PDB 3OE0 3OE0 1 16 SEQADV 3OE0 ASP A -9 UNP P61073 EXPRESSION TAG SEQADV 3OE0 TYR A -8 UNP P61073 EXPRESSION TAG SEQADV 3OE0 LYS A -7 UNP P61073 EXPRESSION TAG SEQADV 3OE0 ASP A -6 UNP P61073 EXPRESSION TAG SEQADV 3OE0 ASP A -5 UNP P61073 EXPRESSION TAG SEQADV 3OE0 ASP A -4 UNP P61073 EXPRESSION TAG SEQADV 3OE0 ASP A -3 UNP P61073 EXPRESSION TAG SEQADV 3OE0 ALA A -2 UNP P61073 EXPRESSION TAG SEQADV 3OE0 GLY A -1 UNP P61073 EXPRESSION TAG SEQADV 3OE0 ALA A 0 UNP P61073 EXPRESSION TAG SEQADV 3OE0 PRO A 1 UNP P61073 EXPRESSION TAG SEQADV 3OE0 TRP A 125 UNP P61073 LEU 125 ENGINEERED MUTATION SEQADV 3OE0 THR A 1054 UNP P00720 CYS 1054 ENGINEERED MUTATION SEQADV 3OE0 ALA A 1097 UNP P00720 CYS 1097 ENGINEERED MUTATION SEQADV 3OE0 SER A 1200 UNP P61073 LINKER SEQADV 3OE0 GLY A 1201 UNP P61073 LINKER SEQADV 3OE0 SER A 1202 UNP P61073 LINKER SEQADV 3OE0 PRO A 240 UNP P61073 THR 240 ENGINEERED MUTATION SEQADV 3OE0 GLY A 320 UNP P61073 EXPRESSION TAG SEQADV 3OE0 ARG A 321 UNP P61073 EXPRESSION TAG SEQADV 3OE0 PRO A 322 UNP P61073 EXPRESSION TAG SEQADV 3OE0 LEU A 323 UNP P61073 EXPRESSION TAG SEQADV 3OE0 GLU A 324 UNP P61073 EXPRESSION TAG SEQADV 3OE0 VAL A 325 UNP P61073 EXPRESSION TAG SEQADV 3OE0 LEU A 326 UNP P61073 EXPRESSION TAG SEQADV 3OE0 PHE A 327 UNP P61073 EXPRESSION TAG SEQADV 3OE0 GLN A 328 UNP P61073 EXPRESSION TAG SEQRES 1 A 499 ASP TYR LYS ASP ASP ASP ASP ALA GLY ALA PRO GLU GLY SEQRES 2 A 499 ILE SER ILE TYR THR SER ASP ASN TYR THR GLU GLU MET SEQRES 3 A 499 GLY SER GLY ASP TYR ASP SER MET LYS GLU PRO CYS PHE SEQRES 4 A 499 ARG GLU GLU ASN ALA ASN PHE ASN LYS ILE PHE LEU PRO SEQRES 5 A 499 THR ILE TYR SER ILE ILE PHE LEU THR GLY ILE VAL GLY SEQRES 6 A 499 ASN GLY LEU VAL ILE LEU VAL MET GLY TYR GLN LYS LYS SEQRES 7 A 499 LEU ARG SER MET THR ASP LYS TYR ARG LEU HIS LEU SER SEQRES 8 A 499 VAL ALA ASP LEU LEU PHE VAL ILE THR LEU PRO PHE TRP SEQRES 9 A 499 ALA VAL ASP ALA VAL ALA ASN TRP TYR PHE GLY ASN PHE SEQRES 10 A 499 LEU CYS LYS ALA VAL HIS VAL ILE TYR THR VAL ASN LEU SEQRES 11 A 499 TYR SER SER VAL TRP ILE LEU ALA PHE ILE SER LEU ASP SEQRES 12 A 499 ARG TYR LEU ALA ILE VAL HIS ALA THR ASN SER GLN ARG SEQRES 13 A 499 PRO ARG LYS LEU LEU ALA GLU LYS VAL VAL TYR VAL GLY SEQRES 14 A 499 VAL TRP ILE PRO ALA LEU LEU LEU THR ILE PRO ASP PHE SEQRES 15 A 499 ILE PHE ALA ASN VAL SER GLU ALA ASP ASP ARG TYR ILE SEQRES 16 A 499 CYS ASP ARG PHE TYR PRO ASN ASP LEU TRP VAL VAL VAL SEQRES 17 A 499 PHE GLN PHE GLN HIS ILE MET VAL GLY LEU ILE LEU PRO SEQRES 18 A 499 GLY ILE VAL ILE LEU SER CYS TYR CYS ILE ILE ILE SER SEQRES 19 A 499 LYS LEU SER HIS ASN ILE PHE GLU MET LEU ARG ILE ASP SEQRES 20 A 499 GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY SEQRES 21 A 499 TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER SEQRES 22 A 499 PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA SEQRES 23 A 499 ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU SEQRES 24 A 499 ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL SEQRES 25 A 499 ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR SEQRES 26 A 499 ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN SEQRES 27 A 499 MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE SEQRES 28 A 499 THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP SEQRES 29 A 499 GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN SEQRES 30 A 499 GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE SEQRES 31 A 499 ARG THR GLY THR TRP ASP ALA TYR SER GLY SER GLY HIS SEQRES 32 A 499 GLN LYS ARG LYS ALA LEU LYS PRO THR VAL ILE LEU ILE SEQRES 33 A 499 LEU ALA PHE PHE ALA CYS TRP LEU PRO TYR TYR ILE GLY SEQRES 34 A 499 ILE SER ILE ASP SER PHE ILE LEU LEU GLU ILE ILE LYS SEQRES 35 A 499 GLN GLY CYS GLU PHE GLU ASN THR VAL HIS LYS TRP ILE SEQRES 36 A 499 SER ILE THR GLU ALA LEU ALA PHE PHE HIS CYS CYS LEU SEQRES 37 A 499 ASN PRO ILE LEU TYR ALA PHE LEU GLY ALA LYS PHE LYS SEQRES 38 A 499 THR SER ALA GLN HIS ALA LEU THR SER GLY ARG PRO LEU SEQRES 39 A 499 GLU VAL LEU PHE GLN SEQRES 1 I 16 ARG ARG ALN CYS TYR GLN LYS DPR PRO TYR ARG CIR CYS SEQRES 2 I 16 ARG GLY DPR MODRES 3OE0 ALN I 3 ALA NAPHTHALEN-2-YL-3-ALANINE MODRES 3OE0 CIR I 12 ARG CITRULLINE HET ALN I 3 15 HET DPR I 8 7 HET CIR I 12 11 HET DPR I 16 8 HETNAM ALN NAPHTHALEN-2-YL-3-ALANINE HETNAM DPR D-PROLINE HETNAM CIR CITRULLINE FORMUL 2 ALN C13 H13 N O2 FORMUL 2 DPR 2(C5 H9 N O2) FORMUL 2 CIR C6 H13 N3 O3 FORMUL 3 HOH *6(H2 O) HELIX 1 1 ASN A 33 ILE A 39 1 7 HELIX 2 2 ILE A 39 MET A 63 1 25 HELIX 3 3 SER A 71 ILE A 89 1 19 HELIX 4 4 THR A 90 ALA A 100 1 11 HELIX 5 5 PHE A 104 HIS A 140 1 37 HELIX 6 6 ALA A 141 ASN A 143 5 3 HELIX 7 7 SER A 144 LYS A 154 1 11 HELIX 8 8 LYS A 154 VAL A 160 1 7 HELIX 9 9 VAL A 160 THR A 168 1 9 HELIX 10 10 THR A 168 PHE A 174 1 7 HELIX 11 11 ASN A 192 LEU A 208 1 17 HELIX 12 12 LEU A 208 GLU A 1011 1 31 HELIX 13 13 SER A 1038 GLY A 1051 1 14 HELIX 14 14 THR A 1059 ARG A 1080 1 22 HELIX 15 15 LYS A 1083 LEU A 1091 1 9 HELIX 16 16 ASP A 1092 GLY A 1113 1 22 HELIX 17 17 PHE A 1114 GLN A 1123 1 10 HELIX 18 18 ARG A 1125 LYS A 1135 1 11 HELIX 19 19 SER A 1136 THR A 1142 1 7 HELIX 20 20 THR A 1142 GLY A 1156 1 15 HELIX 21 21 LEU A 238 LEU A 267 1 30 HELIX 22 22 GLN A 272 PHE A 292 1 21 HELIX 23 23 PHE A 293 TYR A 302 1 10 SHEET 1 A 3 ALA A 175 GLU A 179 0 SHEET 2 A 3 TYR A 184 TYR A 190 -1 O ILE A 185 N SER A 178 SHEET 3 A 3 CYS I 4 TYR I 5 1 O CYS I 4 N ARG A 188 SHEET 1 B 3 LEU A1013 LYS A1019 0 SHEET 2 B 3 TYR A1025 ILE A1029 -1 O GLY A1028 N ARG A1014 SHEET 3 B 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025 SSBOND 1 CYS A 28 CYS A 274 1555 1555 2.04 SSBOND 2 CYS A 109 CYS A 186 1555 1555 2.05 SSBOND 3 CYS I 4 CYS I 13 1555 1555 2.06 LINK C HIS A 228 N ASN A1002 1555 1555 1.33 LINK C ARG I 2 N ALN I 3 1555 1555 1.34 LINK C ALN I 3 N CYS I 4 1555 1555 1.33 LINK C LYS I 7 N DPR I 8 1555 1555 1.35 LINK C DPR I 8 N PRO I 9 1555 1555 1.34 LINK C ARG I 11 N2 CIR I 12 1555 1555 1.34 LINK C1 CIR I 12 N CYS I 13 1555 1555 1.33 LINK C GLY I 15 N DPR I 16 1555 1555 1.34 SITE 1 AC1 23 HIS A 113 TYR A 116 THR A 117 ASP A 171 SITE 2 AC1 23 ASP A 187 ARG A 188 PHE A 189 TYR A 190 SITE 3 AC1 23 PRO A 191 ASP A 193 VAL A 196 PHE A 199 SITE 4 AC1 23 GLN A 200 ASP A 262 LEU A 266 GLU A 277 SITE 5 AC1 23 HIS A 281 ILE A 284 SER A 285 GLU A 288 SITE 6 AC1 23 HOH I1601 HOH I1602 HOH I1604 CRYST1 82.080 144.860 73.990 90.00 104.54 90.00 C 1 2 1 4 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 0.012183 0.000000 0.003160 0.00000 SCALE2 0.000000 0.006903 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013963 0.00000 ATOM 1 N LYS A 25 41.308 47.731 9.332 1.00 90.95 N ANISOU 1 N LYS A 25 12855 10049 11652 1201 263 -51 N ATOM 2 CA LYS A 25 41.877 46.590 10.113 1.00 89.83 C ANISOU 2 CA LYS A 25 12602 10010 11518 1144 337 -84 C ATOM 3 C LYS A 25 43.361 46.401 9.793 1.00 88.52 C ANISOU 3 C LYS A 25 12494 9869 11269 943 293 -132 C ATOM 4 O LYS A 25 43.727 45.684 8.856 1.00 87.80 O ANISOU 4 O LYS A 25 12303 9850 11204 823 251 -126 O ATOM 5 CB LYS A 25 41.098 45.293 9.833 1.00 89.43 C ANISOU 5 CB LYS A 25 12308 10079 11592 1174 364 -43 C ATOM 6 CG LYS A 25 41.466 44.112 10.739 1.00 89.12 C ANISOU 6 CG LYS A 25 12153 10137 11569 1147 445 -71 C ATOM 7 CD LYS A 25 40.845 44.230 12.146 1.00 90.71 C ANISOU 7 CD LYS A 25 12369 10315 11780 1304 556 -75 C ATOM 8 CE LYS A 25 39.460 43.559 12.257 1.00 91.24 C ANISOU 8 CE LYS A 25 12244 10445 11976 1437 617 -17 C ATOM 9 NZ LYS A 25 38.351 44.371 11.676 1.00 92.35 N ANISOU 9 NZ LYS A 25 12382 10526 12181 1562 586 36 N ATOM 10 N GLU A 26 44.206 47.067 10.574 1.00 88.15 N ANISOU 10 N GLU A 26 12612 9756 11122 907 303 -177 N ATOM 11 CA GLU A 26 45.649 46.808 10.560 1.00 86.87 C ANISOU 11 CA GLU A 26 12484 9627 10895 727 277 -222 C ATOM 12 C GLU A 26 45.927 45.436 11.203 1.00 84.96 C ANISOU 12 C GLU A 26 12073 9501 10706 705 338 -239 C ATOM 13 O GLU A 26 45.194 45.012 12.103 1.00 85.16 O ANISOU 13 O GLU A 26 12036 9547 10774 831 412 -230 O ATOM 14 CB GLU A 26 46.400 47.931 11.299 1.00 87.70 C ANISOU 14 CB GLU A 26 12816 9622 10882 699 260 -258 C ATOM 15 CG GLU A 26 46.012 48.093 12.786 1.00 88.66 C ANISOU 15 CG GLU A 26 13006 9698 10980 835 338 -272 C ATOM 16 CD GLU A 26 45.861 49.553 13.219 1.00 90.68 C ANISOU 16 CD GLU A 26 13510 9801 11141 908 322 -279 C ATOM 17 OE1 GLU A 26 45.218 50.340 12.479 1.00 91.34 O ANISOU 17 OE1 GLU A 26 13657 9818 11230 968 283 -250 O ATOM 18 OE2 GLU A 26 46.373 49.903 14.311 1.00 90.57 O ANISOU 18 OE2 GLU A 26 13636 9729 11046 907 344 -312 O ATOM 19 N PRO A 27 46.979 44.735 10.746 1.00 82.84 N ANISOU 19 N PRO A 27 11733 9306 10434 547 312 -263 N ATOM 20 CA PRO A 27 47.237 43.390 11.275 1.00 81.21 C ANISOU 20 CA PRO A 27 11367 9206 10283 528 361 -277 C ATOM 21 C PRO A 27 47.648 43.379 12.751 1.00 80.37 C ANISOU 21 C PRO A 27 11325 9078 10133 561 404 -309 C ATOM 22 O PRO A 27 48.192 44.360 13.249 1.00 80.95 O ANISOU 22 O PRO A 27 11575 9062 10120 538 380 -332 O ATOM 23 CB PRO A 27 48.375 42.866 10.386 1.00 80.51 C ANISOU 23 CB PRO A 27 11217 9180 10190 352 319 -299 C ATOM 24 CG PRO A 27 49.027 44.075 9.822 1.00 81.51 C ANISOU 24 CG PRO A 27 11511 9223 10235 260 259 -309 C ATOM 25 CD PRO A 27 47.980 45.147 9.745 1.00 82.73 C ANISOU 25 CD PRO A 27 11785 9278 10369 382 244 -277 C ATOM 26 N CYS A 28 47.365 42.277 13.439 1.00 78.76 N ANISOU 26 N CYS A 28 10992 8948 9984 609 462 -310 N ATOM 27 CA CYS A 28 47.779 42.113 14.826 1.00 77.93 C ANISOU 27 CA CYS A 28 10946 8826 9837 629 498 -339 C ATOM 28 C CYS A 28 49.276 41.946 14.894 1.00 76.75 C ANISOU 28 C CYS A 28 10821 8694 9647 470 443 -378 C ATOM 29 O CYS A 28 49.847 41.138 14.169 1.00 75.95 O ANISOU 29 O CYS A 28 10587 8675 9594 371 420 -384 O ATOM 30 CB CYS A 28 47.131 40.886 15.462 1.00 77.44 C ANISOU 30 CB CYS A 28 10736 8844 9844 706 570 -327 C ATOM 31 SG CYS A 28 45.413 41.101 15.878 1.00 78.05 S ANISOU 31 SG CYS A 28 10794 8895 9966 907 659 -284 S ATOM 32 N PHE A 29 49.906 42.703 15.784 1.00 76.56 N ANISOU 32 N PHE A 29 10964 8587 9537 448 422 -403 N ATOM 33 CA PHE A 29 51.342 42.615 15.980 1.00 75.63 C ANISOU 33 CA PHE A 29 10871 8478 9386 299 361 -435 C ATOM 34 C PHE A 29 51.654 41.649 17.105 1.00 74.71 C ANISOU 34 C PHE A 29 10699 8402 9284 307 382 -452 C ATOM 35 O PHE A 29 51.050 41.733 18.171 1.00 74.89 O ANISOU 35 O PHE A 29 10802 8376 9273 413 430 -451 O ATOM 36 CB PHE A 29 51.924 43.983 16.323 1.00 76.46 C ANISOU 36 CB PHE A 29 11200 8464 9385 251 306 -448 C ATOM 37 CG PHE A 29 53.399 43.957 16.539 1.00 76.09 C ANISOU 37 CG PHE A 29 11174 8425 9312 90 235 -474 C ATOM 38 CD1 PHE A 29 53.921 43.878 17.817 1.00 76.26 C ANISOU 38 CD1 PHE A 29 11277 8409 9288 80 215 -492 C ATOM 39 CD2 PHE A 29 54.267 43.971 15.455 1.00 75.85 C ANISOU 39 CD2 PHE A 29 11073 8440 9304 -52 188 -478 C ATOM 40 CE1 PHE A 29 55.277 43.830 18.014 1.00 76.38 C ANISOU 40 CE1 PHE A 29 11295 8433 9292 -69 138 -509 C ATOM 41 CE2 PHE A 29 55.622 43.927 15.638 1.00 75.61 C ANISOU 41 CE2 PHE A 29 11038 8424 9266 -199 127 -497 C ATOM 42 CZ PHE A 29 56.133 43.856 16.919 1.00 76.50 C ANISOU 42 CZ PHE A 29 11220 8500 9343 -207 95 -511 C ATOM 43 N ARG A 30 52.594 40.738 16.860 1.00 73.48 N ANISOU 43 N ARG A 30 10410 8329 9177 198 350 -468 N ATOM 44 CA ARG A 30 53.139 39.884 17.910 1.00 72.86 C ANISOU 44 CA ARG A 30 10295 8278 9107 181 344 -486 C ATOM 45 C ARG A 30 54.619 40.155 18.061 1.00 72.61 C ANISOU 45 C ARG A 30 10307 8231 9049 34 257 -510 C ATOM 46 O ARG A 30 55.299 40.444 17.088 1.00 72.54 O ANISOU 46 O ARG A 30 10260 8244 9055 -71 220 -513 O ATOM 47 CB ARG A 30 52.924 38.406 17.600 1.00 72.00 C ANISOU 47 CB ARG A 30 9977 8285 9094 194 379 -481 C ATOM 48 CG ARG A 30 52.928 37.523 18.843 1.00 72.35 C ANISOU 48 CG ARG A 30 10004 8342 9141 235 396 -490 C ATOM 49 CD ARG A 30 52.533 36.080 18.541 1.00 72.34 C ANISOU 49 CD ARG A 30 9810 8445 9228 262 436 -481 C ATOM 50 NE ARG A 30 53.673 35.260 18.107 1.00 72.25 N ANISOU 50 NE ARG A 30 9675 8503 9272 150 384 -502 N ATOM 51 CZ ARG A 30 54.068 35.083 16.847 1.00 71.52 C ANISOU 51 CZ ARG A 30 9479 8467 9229 78 372 -504 C ATOM 52 NH1 ARG A 30 55.112 34.310 16.600 1.00 70.99 N ANISOU 52 NH1 ARG A 30 9302 8457 9212 -9 337 -524 N ATOM 53 NH2 ARG A 30 53.437 35.660 15.830 1.00 72.43 N ANISOU 53 NH2 ARG A 30 9600 8576 9342 94 394 -485 N ATOM 54 N GLU A 31 55.111 40.046 19.287 1.00 72.61 N ANISOU 54 N GLU A 31 10386 8191 9009 23 225 -523 N ATOM 55 CA GLU A 31 56.517 40.281 19.565 1.00 72.82 C ANISOU 55 CA GLU A 31 10450 8200 9018 -115 130 -539 C ATOM 56 C GLU A 31 57.261 38.998 19.247 1.00 71.91 C ANISOU 56 C GLU A 31 10121 8195 9003 -182 113 -549 C ATOM 57 O GLU A 31 56.714 37.900 19.394 1.00 71.22 O ANISOU 57 O GLU A 31 9918 8170 8970 -109 164 -547 O ATOM 58 CB GLU A 31 56.786 40.664 21.030 1.00 73.55 C ANISOU 58 CB GLU A 31 10725 8196 9025 -108 85 -547 C ATOM 59 CG GLU A 31 55.577 40.849 21.935 1.00 74.27 C ANISOU 59 CG GLU A 31 10947 8218 9051 43 161 -542 C ATOM 60 CD GLU A 31 55.163 39.562 22.633 1.00 74.51 C ANISOU 60 CD GLU A 31 10876 8306 9125 113 209 -543 C ATOM 61 OE1 GLU A 31 55.966 39.046 23.431 1.00 75.23 O ANISOU 61 OE1 GLU A 31 10975 8394 9212 52 145 -554 O ATOM 62 OE2 GLU A 31 54.037 39.068 22.401 1.00 74.90 O ANISOU 62 OE2 GLU A 31 10842 8401 9215 226 305 -530 O ATOM 63 N GLU A 32 58.506 39.137 18.806 1.00 71.78 N ANISOU 63 N GLU A 32 10056 8202 9015 -321 45 -558 N ATOM 64 CA GLU A 32 59.401 38.000 18.734 1.00 71.31 C ANISOU 64 CA GLU A 32 9814 8230 9048 -385 18 -570 C ATOM 65 C GLU A 32 59.911 37.767 20.167 1.00 71.33 C ANISOU 65 C GLU A 32 9890 8186 9024 -393 -52 -575 C ATOM 66 O GLU A 32 60.083 38.716 20.934 1.00 72.11 O ANISOU 66 O GLU A 32 10176 8185 9035 -415 -106 -572 O ATOM 67 CB GLU A 32 60.548 38.265 17.752 1.00 71.76 C ANISOU 67 CB GLU A 32 9785 8328 9150 -529 -17 -575 C ATOM 68 CG GLU A 32 60.882 37.080 16.833 1.00 72.10 C ANISOU 68 CG GLU A 32 9601 8488 9304 -551 24 -586 C ATOM 69 CD GLU A 32 60.016 37.030 15.575 1.00 72.87 C ANISOU 69 CD GLU A 32 9652 8624 9411 -509 108 -579 C ATOM 70 OE1 GLU A 32 60.103 37.969 14.751 1.00 74.05 O ANISOU 70 OE1 GLU A 32 9865 8747 9523 -570 111 -574 O ATOM 71 OE2 GLU A 32 59.260 36.046 15.398 1.00 72.52 O ANISOU 71 OE2 GLU A 32 9512 8633 9409 -422 164 -578 O ATOM 72 N ASN A 33 60.115 36.505 20.532 1.00 70.43 N ANISOU 72 N ASN A 33 9643 8135 8981 -372 -55 -582 N ATOM 73 CA ASN A 33 60.537 36.132 21.882 1.00 70.32 C ANISOU 73 CA ASN A 33 9694 8077 8945 -374 -126 -585 C ATOM 74 C ASN A 33 61.957 35.605 21.816 1.00 70.44 C ANISOU 74 C ASN A 33 9573 8141 9047 -489 -217 -592 C ATOM 75 O ASN A 33 62.236 34.643 21.096 1.00 69.74 O ANISOU 75 O ASN A 33 9287 8149 9060 -496 -189 -600 O ATOM 76 CB ASN A 33 59.588 35.065 22.443 1.00 69.67 C ANISOU 76 CB ASN A 33 9577 8021 8873 -254 -62 -585 C ATOM 77 CG ASN A 33 59.788 34.803 23.927 1.00 69.31 C ANISOU 77 CG ASN A 33 9650 7909 8776 -242 -125 -586 C ATOM 78 OD1 ASN A 33 60.716 34.110 24.326 1.00 68.99 O ANISOU 78 OD1 ASN A 33 9536 7889 8787 -301 -209 -591 O ATOM 79 ND2 ASN A 33 58.886 35.326 24.746 1.00 68.65 N ANISOU 79 ND2 ASN A 33 9752 7740 8589 -159 -81 -580 N ATOM 80 N ALA A 34 62.860 36.242 22.554 1.00 71.27 N ANISOU 80 N ALA A 34 9784 8177 9115 -579 -328 -587 N ATOM 81 CA ALA A 34 64.262 35.853 22.532 1.00 71.73 C ANISOU 81 CA ALA A 34 9710 8277 9266 -694 -426 -587 C ATOM 82 C ALA A 34 64.448 34.433 23.073 1.00 71.50 C ANISOU 82 C ALA A 34 9553 8297 9314 -649 -449 -594 C ATOM 83 O ALA A 34 64.836 33.540 22.331 1.00 71.04 O ANISOU 83 O ALA A 34 9289 8335 9368 -656 -420 -603 O ATOM 84 CB ALA A 34 65.086 36.832 23.310 1.00 72.81 C ANISOU 84 CB ALA A 34 10002 8320 9342 -799 -553 -573 C ATOM 85 N ASN A 35 64.136 34.224 24.349 1.00 71.93 N ANISOU 85 N ASN A 35 9745 8281 9304 -600 -495 -590 N ATOM 86 CA ASN A 35 64.312 32.917 24.998 1.00 72.04 C ANISOU 86 CA ASN A 35 9670 8324 9376 -562 -532 -594 C ATOM 87 C ASN A 35 63.771 31.741 24.192 1.00 70.88 C ANISOU 87 C ASN A 35 9335 8281 9312 -483 -428 -606 C ATOM 88 O ASN A 35 64.338 30.636 24.209 1.00 70.64 O ANISOU 88 O ASN A 35 9154 8306 9377 -486 -465 -612 O ATOM 89 CB ASN A 35 63.656 32.922 26.382 1.00 72.54 C ANISOU 89 CB ASN A 35 9944 8289 9327 -498 -554 -588 C ATOM 90 CG ASN A 35 64.412 33.784 27.376 1.00 74.74 C ANISOU 90 CG ASN A 35 10407 8457 9531 -587 -691 -575 C ATOM 91 OD1 ASN A 35 65.537 34.222 27.113 1.00 76.35 O ANISOU 91 OD1 ASN A 35 10555 8666 9787 -704 -789 -567 O ATOM 92 ND2 ASN A 35 63.798 34.033 28.526 1.00 76.25 N ANISOU 92 ND2 ASN A 35 10825 8546 9599 -537 -697 -572 N ATOM 93 N PHE A 36 62.666 31.986 23.497 1.00 70.11 N ANISOU 93 N PHE A 36 9254 8205 9179 -412 -306 -607 N ATOM 94 CA PHE A 36 62.070 30.990 22.620 1.00 69.12 C ANISOU 94 CA PHE A 36 8967 8172 9121 -347 -208 -615 C ATOM 95 C PHE A 36 62.981 30.699 21.420 1.00 68.88 C ANISOU 95 C PHE A 36 8742 8227 9201 -419 -205 -626 C ATOM 96 O PHE A 36 63.339 29.550 21.170 1.00 68.24 O ANISOU 96 O PHE A 36 8506 8210 9209 -407 -204 -637 O ATOM 97 CB PHE A 36 60.691 31.463 22.149 1.00 68.56 C ANISOU 97 CB PHE A 36 8967 8095 8987 -264 -93 -607 C ATOM 98 CG PHE A 36 60.006 30.490 21.254 1.00 67.53 C ANISOU 98 CG PHE A 36 8687 8051 8919 -204 -3 -608 C ATOM 99 CD1 PHE A 36 59.998 30.679 19.878 1.00 66.89 C ANISOU 99 CD1 PHE A 36 8509 8026 8880 -232 49 -611 C ATOM 100 CD2 PHE A 36 59.399 29.361 21.784 1.00 67.30 C ANISOU 100 CD2 PHE A 36 8623 8043 8902 -128 21 -605 C ATOM 101 CE1 PHE A 36 59.388 29.769 19.041 1.00 66.10 C ANISOU 101 CE1 PHE A 36 8285 7998 8830 -185 121 -610 C ATOM 102 CE2 PHE A 36 58.780 28.447 20.955 1.00 66.95 C ANISOU 102 CE2 PHE A 36 8449 8074 8912 -82 94 -603 C ATOM 103 CZ PHE A 36 58.777 28.652 19.577 1.00 66.31 C ANISOU 103 CZ PHE A 36 8277 8046 8872 -110 142 -606 C ATOM 104 N ASN A 37 63.351 31.754 20.698 1.00 69.31 N ANISOU 104 N ASN A 37 8817 8274 9242 -494 -201 -624 N ATOM 105 CA ASN A 37 64.218 31.646 19.522 1.00 69.54 C ANISOU 105 CA ASN A 37 8681 8378 9363 -574 -183 -634 C ATOM 106 C ASN A 37 65.672 31.308 19.850 1.00 70.50 C ANISOU 106 C ASN A 37 8692 8518 9577 -660 -282 -638 C ATOM 107 O ASN A 37 66.354 30.652 19.069 1.00 70.43 O ANISOU 107 O ASN A 37 8501 8586 9671 -690 -255 -650 O ATOM 108 CB ASN A 37 64.193 32.958 18.732 1.00 69.78 C ANISOU 108 CB ASN A 37 8789 8384 9341 -639 -154 -628 C ATOM 109 CG ASN A 37 62.975 33.090 17.837 1.00 69.30 C ANISOU 109 CG ASN A 37 8752 8339 9238 -568 -45 -626 C ATOM 110 OD1 ASN A 37 61.951 32.443 18.048 1.00 68.50 O ANISOU 110 OD1 ASN A 37 8656 8246 9123 -463 4 -623 O ATOM 111 ND2 ASN A 37 63.088 33.938 16.819 1.00 70.39 N ANISOU 111 ND2 ASN A 37 8906 8479 9358 -632 -12 -624 N ATOM 112 N LYS A 38 66.139 31.763 21.007 1.00 71.59 N ANISOU 112 N LYS A 38 8941 8581 9675 -700 -396 -625 N ATOM 113 CA LYS A 38 67.553 31.697 21.360 1.00 72.85 C ANISOU 113 CA LYS A 38 9012 8746 9919 -799 -513 -618 C ATOM 114 C LYS A 38 67.926 30.481 22.210 1.00 73.05 C ANISOU 114 C LYS A 38 8960 8780 10013 -756 -588 -621 C ATOM 115 O LYS A 38 69.052 29.986 22.105 1.00 73.70 O ANISOU 115 O LYS A 38 8880 8906 10215 -810 -650 -621 O ATOM 116 CB LYS A 38 67.953 32.968 22.113 1.00 73.96 C ANISOU 116 CB LYS A 38 9332 8792 9978 -887 -618 -597 C ATOM 117 CG LYS A 38 67.754 34.268 21.335 1.00 74.52 C ANISOU 117 CG LYS A 38 9492 8840 9979 -946 -568 -592 C ATOM 118 CD LYS A 38 68.939 34.596 20.433 1.00 75.51 C ANISOU 118 CD LYS A 38 9467 9024 10198 -1075 -581 -589 C ATOM 119 CE LYS A 38 68.821 36.009 19.887 1.00 76.31 C ANISOU 119 CE LYS A 38 9703 9080 10211 -1152 -561 -578 C ATOM 120 NZ LYS A 38 69.659 36.209 18.681 1.00 77.02 N ANISOU 120 NZ LYS A 38 9635 9244 10382 -1259 -516 -580 N ATOM 121 N ILE A 39 67.004 30.021 23.061 1.00 72.56 N ANISOU 121 N ILE A 39 9016 8674 9878 -661 -583 -620 N ATOM 122 CA ILE A 39 67.275 28.900 23.969 1.00 72.69 C ANISOU 122 CA ILE A 39 8995 8682 9939 -621 -663 -620 C ATOM 123 C ILE A 39 66.389 27.689 23.687 1.00 71.51 C ANISOU 123 C ILE A 39 8776 8586 9809 -509 -565 -635 C ATOM 124 O ILE A 39 66.891 26.594 23.449 1.00 71.42 O ANISOU 124 O ILE A 39 8602 8631 9902 -490 -578 -646 O ATOM 125 CB ILE A 39 67.052 29.273 25.452 1.00 73.35 C ANISOU 125 CB ILE A 39 9302 8653 9914 -619 -763 -604 C ATOM 126 CG1 ILE A 39 67.777 30.568 25.828 1.00 74.23 C ANISOU 126 CG1 ILE A 39 9531 8692 9979 -731 -865 -586 C ATOM 127 CG2 ILE A 39 67.515 28.123 26.346 1.00 73.81 C ANISOU 127 CG2 ILE A 39 9317 8700 10027 -596 -865 -601 C ATOM 128 CD1 ILE A 39 67.384 31.094 27.204 1.00 74.25 C ANISOU 128 CD1 ILE A 39 9799 8570 9843 -724 -941 -572 C ATOM 129 N PHE A 40 65.075 27.890 23.737 1.00 70.59 N ANISOU 129 N PHE A 40 8782 8447 9591 -434 -472 -634 N ATOM 130 CA PHE A 40 64.126 26.785 23.652 1.00 69.58 C ANISOU 130 CA PHE A 40 8614 8357 9465 -333 -392 -641 C ATOM 131 C PHE A 40 64.251 25.950 22.373 1.00 68.73 C ANISOU 131 C PHE A 40 8304 8348 9460 -318 -315 -657 C ATOM 132 O PHE A 40 64.488 24.746 22.440 1.00 68.58 O ANISOU 132 O PHE A 40 8182 8363 9510 -284 -332 -666 O ATOM 133 CB PHE A 40 62.706 27.312 23.771 1.00 69.14 C ANISOU 133 CB PHE A 40 8705 8268 9297 -264 -295 -631 C ATOM 134 CG PHE A 40 61.667 26.254 23.598 1.00 69.39 C ANISOU 134 CG PHE A 40 8688 8342 9333 -172 -208 -631 C ATOM 135 CD1 PHE A 40 61.055 26.055 22.360 1.00 68.88 C ANISOU 135 CD1 PHE A 40 8521 8348 9301 -143 -103 -634 C ATOM 136 CD2 PHE A 40 61.312 25.430 24.666 1.00 70.44 C ANISOU 136 CD2 PHE A 40 8884 8443 9435 -122 -237 -626 C ATOM 137 CE1 PHE A 40 60.092 25.063 22.188 1.00 68.09 C ANISOU 137 CE1 PHE A 40 8377 8287 9207 -68 -32 -629 C ATOM 138 CE2 PHE A 40 60.345 24.435 24.506 1.00 70.06 C ANISOU 138 CE2 PHE A 40 8791 8436 9391 -47 -158 -622 C ATOM 139 CZ PHE A 40 59.736 24.251 23.256 1.00 68.78 C ANISOU 139 CZ PHE A 40 8520 8346 9266 -21 -58 -622 C ATOM 140 N LEU A 41 64.071 26.588 21.216 1.00 68.22 N ANISOU 140 N LEU A 41 8201 8322 9398 -343 -232 -661 N ATOM 141 CA LEU A 41 64.117 25.892 19.916 1.00 67.42 C ANISOU 141 CA LEU A 41 7935 8305 9375 -333 -147 -677 C ATOM 142 C LEU A 41 65.459 25.212 19.630 1.00 67.86 C ANISOU 142 C LEU A 41 7819 8408 9556 -378 -194 -694 C ATOM 143 O LEU A 41 65.489 24.042 19.258 1.00 67.40 O ANISOU 143 O LEU A 41 7648 8397 9563 -332 -163 -708 O ATOM 144 CB LEU A 41 63.744 26.837 18.755 1.00 67.02 C ANISOU 144 CB LEU A 41 7899 8274 9292 -366 -60 -676 C ATOM 145 CG LEU A 41 62.290 27.327 18.674 1.00 65.96 C ANISOU 145 CG LEU A 41 7890 8112 9059 -302 10 -659 C ATOM 146 CD1 LEU A 41 62.121 28.343 17.566 1.00 65.22 C ANISOU 146 CD1 LEU A 41 7817 8025 8938 -347 68 -657 C ATOM 147 CD2 LEU A 41 61.320 26.184 18.474 1.00 64.80 C ANISOU 147 CD2 LEU A 41 7695 8003 8922 -215 73 -657 C ATOM 148 N PRO A 42 66.575 25.938 19.791 1.00 68.90 N ANISOU 148 N PRO A 42 7928 8524 9724 -468 -269 -690 N ATOM 149 CA PRO A 42 67.850 25.251 19.533 1.00 69.65 C ANISOU 149 CA PRO A 42 7839 8668 9955 -503 -309 -703 C ATOM 150 C PRO A 42 68.042 24.016 20.416 1.00 69.68 C ANISOU 150 C PRO A 42 7802 8661 10009 -440 -387 -706 C ATOM 151 O PRO A 42 68.549 22.996 19.950 1.00 69.70 O ANISOU 151 O PRO A 42 7650 8715 10115 -411 -368 -723 O ATOM 152 CB PRO A 42 68.919 26.322 19.827 1.00 70.73 C ANISOU 152 CB PRO A 42 7982 8777 10113 -615 -400 -688 C ATOM 153 CG PRO A 42 68.192 27.486 20.432 1.00 70.75 C ANISOU 153 CG PRO A 42 8200 8702 9978 -632 -424 -669 C ATOM 154 CD PRO A 42 66.755 27.380 20.039 1.00 69.44 C ANISOU 154 CD PRO A 42 8120 8539 9725 -545 -310 -674 C ATOM 155 N THR A 43 67.626 24.107 21.674 1.00 69.65 N ANISOU 155 N THR A 43 7948 8584 9928 -417 -471 -689 N ATOM 156 CA THR A 43 67.698 22.969 22.577 1.00 69.82 C ANISOU 156 CA THR A 43 7965 8584 9978 -360 -549 -688 C ATOM 157 C THR A 43 66.965 21.783 21.970 1.00 69.12 C ANISOU 157 C THR A 43 7808 8545 9906 -272 -451 -705 C ATOM 158 O THR A 43 67.568 20.745 21.699 1.00 69.34 O ANISOU 158 O THR A 43 7697 8611 10037 -245 -464 -721 O ATOM 159 CB THR A 43 67.089 23.304 23.948 1.00 69.85 C ANISOU 159 CB THR A 43 8179 8496 9863 -346 -623 -668 C ATOM 160 OG1 THR A 43 67.980 24.169 24.659 1.00 70.91 O ANISOU 160 OG1 THR A 43 8373 8573 9995 -432 -750 -651 O ATOM 161 CG2 THR A 43 66.852 22.048 24.763 1.00 69.44 C ANISOU 161 CG2 THR A 43 8146 8422 9816 -277 -674 -668 C ATOM 162 N ILE A 44 65.666 21.957 21.740 1.00 68.39 N ANISOU 162 N ILE A 44 7816 8451 9716 -228 -354 -701 N ATOM 163 CA ILE A 44 64.827 20.893 21.187 1.00 67.55 C ANISOU 163 CA ILE A 44 7667 8387 9612 -153 -266 -710 C ATOM 164 C ILE A 44 65.412 20.368 19.867 1.00 67.56 C ANISOU 164 C ILE A 44 7494 8461 9714 -160 -200 -734 C ATOM 165 O ILE A 44 65.640 19.162 19.731 1.00 67.73 O ANISOU 165 O ILE A 44 7427 8506 9800 -115 -203 -748 O ATOM 166 CB ILE A 44 63.363 21.359 20.981 1.00 66.63 C ANISOU 166 CB ILE A 44 7665 8263 9387 -117 -170 -695 C ATOM 167 CG1 ILE A 44 62.556 21.209 22.271 1.00 66.95 C ANISOU 167 CG1 ILE A 44 7854 8242 9339 -72 -204 -675 C ATOM 168 CG2 ILE A 44 62.683 20.518 19.941 1.00 65.82 C ANISOU 168 CG2 ILE A 44 7483 8218 9304 -72 -71 -702 C ATOM 169 CD1 ILE A 44 63.087 21.984 23.438 1.00 68.39 C ANISOU 169 CD1 ILE A 44 8156 8350 9477 -113 -307 -666 C ATOM 170 N TYR A 45 65.685 21.267 18.917 1.00 67.50 N ANISOU 170 N TYR A 45 7448 8483 9715 -218 -139 -739 N ATOM 171 CA TYR A 45 66.216 20.862 17.609 1.00 67.48 C ANISOU 171 CA TYR A 45 7299 8545 9795 -231 -58 -763 C ATOM 172 C TYR A 45 67.471 19.973 17.742 1.00 68.43 C ANISOU 172 C TYR A 45 7269 8687 10045 -225 -115 -782 C ATOM 173 O TYR A 45 67.664 19.033 16.967 1.00 68.62 O ANISOU 173 O TYR A 45 7187 8752 10131 -188 -52 -805 O ATOM 174 CB TYR A 45 66.529 22.081 16.723 1.00 67.63 C ANISOU 174 CB TYR A 45 7310 8583 9803 -313 -2 -764 C ATOM 175 CG TYR A 45 65.339 22.894 16.225 1.00 66.63 C ANISOU 175 CG TYR A 45 7305 8444 9567 -313 71 -749 C ATOM 176 CD1 TYR A 45 64.031 22.434 16.346 1.00 65.96 C ANISOU 176 CD1 TYR A 45 7299 8348 9413 -240 106 -737 C ATOM 177 CD2 TYR A 45 65.536 24.120 15.594 1.00 66.52 C ANISOU 177 CD2 TYR A 45 7322 8428 9523 -390 103 -745 C ATOM 178 CE1 TYR A 45 62.947 23.188 15.877 1.00 65.04 C ANISOU 178 CE1 TYR A 45 7279 8220 9210 -235 168 -720 C ATOM 179 CE2 TYR A 45 64.462 24.877 15.119 1.00 65.71 C ANISOU 179 CE2 TYR A 45 7331 8308 9326 -385 162 -730 C ATOM 180 CZ TYR A 45 63.166 24.403 15.269 1.00 64.82 C ANISOU 180 CZ TYR A 45 7286 8187 9157 -304 192 -717 C ATOM 181 OH TYR A 45 62.083 25.128 14.817 1.00 63.18 O ANISOU 181 OH TYR A 45 7175 7961 8868 -291 243 -698 O ATOM 182 N SER A 46 68.310 20.259 18.730 1.00 69.06 N ANISOU 182 N SER A 46 7344 8732 10163 -259 -237 -770 N ATOM 183 CA SER A 46 69.495 19.451 18.970 1.00 69.94 C ANISOU 183 CA SER A 46 7308 8856 10407 -248 -310 -781 C ATOM 184 C SER A 46 69.146 18.064 19.522 1.00 69.39 C ANISOU 184 C SER A 46 7247 8769 10349 -156 -348 -787 C ATOM 185 O SER A 46 69.520 17.055 18.935 1.00 69.58 O ANISOU 185 O SER A 46 7151 8828 10457 -108 -308 -811 O ATOM 186 CB SER A 46 70.432 20.179 19.930 1.00 71.12 C ANISOU 186 CB SER A 46 7464 8967 10592 -318 -450 -759 C ATOM 187 OG SER A 46 70.472 21.561 19.624 1.00 71.52 O ANISOU 187 OG SER A 46 7568 9015 10591 -406 -426 -747 O ATOM 188 N ILE A 47 68.430 18.011 20.639 1.00 68.76 N ANISOU 188 N ILE A 47 7317 8630 10179 -131 -421 -767 N ATOM 189 CA ILE A 47 68.030 16.734 21.222 1.00 68.64 C ANISOU 189 CA ILE A 47 7331 8591 10159 -53 -461 -769 C ATOM 190 C ILE A 47 67.451 15.811 20.141 1.00 68.21 C ANISOU 190 C ILE A 47 7218 8584 10112 4 -338 -791 C ATOM 191 O ILE A 47 67.836 14.640 20.026 1.00 68.40 O ANISOU 191 O ILE A 47 7160 8616 10210 58 -354 -808 O ATOM 192 CB ILE A 47 66.970 16.912 22.333 1.00 68.15 C ANISOU 192 CB ILE A 47 7464 8465 9964 -38 -501 -744 C ATOM 193 CG1 ILE A 47 67.555 17.631 23.548 1.00 69.00 C ANISOU 193 CG1 ILE A 47 7658 8506 10052 -90 -639 -723 C ATOM 194 CG2 ILE A 47 66.415 15.564 22.782 1.00 67.60 C ANISOU 194 CG2 ILE A 47 7430 8376 9877 35 -519 -746 C ATOM 195 CD1 ILE A 47 66.543 17.799 24.685 1.00 68.89 C ANISOU 195 CD1 ILE A 47 7852 8422 9901 -74 -668 -702 C ATOM 196 N ILE A 48 66.530 16.356 19.348 1.00 67.66 N ANISOU 196 N ILE A 48 7200 8541 9966 -8 -224 -789 N ATOM 197 CA ILE A 48 65.864 15.600 18.283 1.00 67.12 C ANISOU 197 CA ILE A 48 7101 8511 9887 33 -112 -803 C ATOM 198 C ILE A 48 66.862 15.130 17.243 1.00 67.99 C ANISOU 198 C ILE A 48 7054 8667 10109 35 -59 -836 C ATOM 199 O ILE A 48 66.795 13.995 16.776 1.00 67.57 O ANISOU 199 O ILE A 48 6958 8626 10087 90 -23 -855 O ATOM 200 CB ILE A 48 64.783 16.445 17.589 1.00 66.20 C ANISOU 200 CB ILE A 48 7065 8411 9677 8 -13 -790 C ATOM 201 CG1 ILE A 48 63.600 16.657 18.534 1.00 65.61 C ANISOU 201 CG1 ILE A 48 7139 8294 9494 30 -38 -758 C ATOM 202 CG2 ILE A 48 64.300 15.763 16.326 1.00 65.66 C ANISOU 202 CG2 ILE A 48 6955 8382 9610 32 92 -804 C ATOM 203 CD1 ILE A 48 62.577 17.636 18.025 1.00 64.83 C ANISOU 203 CD1 ILE A 48 7117 8203 9311 11 40 -740 C ATOM 204 N PHE A 49 67.785 16.020 16.893 1.00 69.19 N ANISOU 204 N PHE A 49 7129 8842 10319 -27 -52 -842 N ATOM 205 CA PHE A 49 68.807 15.732 15.902 1.00 70.32 C ANISOU 205 CA PHE A 49 7115 9031 10571 -34 13 -872 C ATOM 206 C PHE A 49 69.706 14.583 16.349 1.00 71.78 C ANISOU 206 C PHE A 49 7190 9209 10873 26 -57 -888 C ATOM 207 O PHE A 49 69.905 13.624 15.598 1.00 71.99 O ANISOU 207 O PHE A 49 7142 9257 10953 79 13 -917 O ATOM 208 CB PHE A 49 69.640 16.982 15.624 1.00 70.92 C ANISOU 208 CB PHE A 49 7131 9128 10684 -126 20 -868 C ATOM 209 CG PHE A 49 70.874 16.714 14.823 1.00 72.04 C ANISOU 209 CG PHE A 49 7094 9318 10959 -138 77 -895 C ATOM 210 CD1 PHE A 49 72.094 16.534 15.447 1.00 73.10 C ANISOU 210 CD1 PHE A 49 7100 9452 11221 -141 -17 -894 C ATOM 211 CD2 PHE A 49 70.814 16.629 13.444 1.00 72.03 C ANISOU 211 CD2 PHE A 49 7053 9358 10956 -146 227 -921 C ATOM 212 CE1 PHE A 49 73.231 16.276 14.707 1.00 74.66 C ANISOU 212 CE1 PHE A 49 7116 9698 11553 -146 46 -917 C ATOM 213 CE2 PHE A 49 71.948 16.375 12.698 1.00 72.95 C ANISOU 213 CE2 PHE A 49 7007 9517 11193 -154 298 -948 C ATOM 214 CZ PHE A 49 73.158 16.197 13.328 1.00 74.35 C ANISOU 214 CZ PHE A 49 7040 9701 11507 -150 213 -946 C ATOM 215 N LEU A 50 70.253 14.687 17.563 1.00 73.02 N ANISOU 215 N LEU A 50 7347 9329 11068 19 -200 -869 N ATOM 216 CA LEU A 50 71.130 13.644 18.111 1.00 74.27 C ANISOU 216 CA LEU A 50 7406 9470 11342 78 -293 -879 C ATOM 217 C LEU A 50 70.380 12.329 18.097 1.00 73.92 C ANISOU 217 C LEU A 50 7419 9405 11259 167 -274 -891 C ATOM 218 O LEU A 50 70.734 11.410 17.353 1.00 74.46 O ANISOU 218 O LEU A 50 7395 9495 11398 225 -210 -921 O ATOM 219 CB LEU A 50 71.566 13.957 19.552 1.00 74.89 C ANISOU 219 CB LEU A 50 7526 9493 11433 53 -471 -848 C ATOM 220 CG LEU A 50 72.679 14.984 19.792 1.00 76.37 C ANISOU 220 CG LEU A 50 7625 9689 11701 -31 -542 -832 C ATOM 221 CD1 LEU A 50 72.685 15.431 21.270 1.00 76.36 C ANISOU 221 CD1 LEU A 50 7746 9615 11650 -67 -715 -796 C ATOM 222 CD2 LEU A 50 74.047 14.433 19.366 1.00 77.08 C ANISOU 222 CD2 LEU A 50 7491 9818 11976 -8 -550 -849 C ATOM 223 N THR A 51 69.318 12.263 18.893 1.00 73.24 N ANISOU 223 N THR A 51 7495 9277 11056 176 -322 -868 N ATOM 224 CA THR A 51 68.581 11.026 19.067 1.00 73.09 C ANISOU 224 CA THR A 51 7545 9231 10993 249 -326 -872 C ATOM 225 C THR A 51 68.003 10.580 17.729 1.00 72.72 C ANISOU 225 C THR A 51 7484 9225 10921 271 -178 -894 C ATOM 226 O THR A 51 67.810 9.398 17.495 1.00 72.76 O ANISOU 226 O THR A 51 7491 9219 10935 334 -164 -909 O ATOM 227 CB THR A 51 67.458 11.172 20.102 1.00 72.34 C ANISOU 227 CB THR A 51 7628 9090 10768 241 -381 -839 C ATOM 228 OG1 THR A 51 66.443 12.030 19.581 1.00 72.52 O ANISOU 228 OG1 THR A 51 7727 9137 10690 201 -280 -826 O ATOM 229 CG2 THR A 51 67.988 11.759 21.412 1.00 72.91 C ANISOU 229 CG2 THR A 51 7746 9112 10844 206 -523 -816 C ATOM 230 N GLY A 52 67.744 11.531 16.841 1.00 72.79 N ANISOU 230 N GLY A 52 7488 9274 10893 216 -74 -895 N ATOM 231 CA GLY A 52 67.297 11.212 15.490 1.00 72.71 C ANISOU 231 CA GLY A 52 7468 9298 10859 225 60 -915 C ATOM 232 C GLY A 52 68.391 10.714 14.557 1.00 73.87 C ANISOU 232 C GLY A 52 7472 9474 11120 250 129 -955 C ATOM 233 O GLY A 52 68.264 9.637 13.973 1.00 73.94 O ANISOU 233 O GLY A 52 7476 9478 11137 307 180 -978 O ATOM 234 N ILE A 53 69.459 11.498 14.403 1.00 74.94 N ANISOU 234 N ILE A 53 7493 9637 11341 205 136 -963 N ATOM 235 CA ILE A 53 70.499 11.189 13.420 1.00 76.20 C ANISOU 235 CA ILE A 53 7507 9834 11611 220 229 -1001 C ATOM 236 C ILE A 53 71.087 9.796 13.666 1.00 76.98 C ANISOU 236 C ILE A 53 7532 9909 11804 320 189 -1024 C ATOM 237 O ILE A 53 71.361 9.067 12.715 1.00 77.53 O ANISOU 237 O ILE A 53 7552 9992 11914 367 293 -1059 O ATOM 238 CB ILE A 53 71.620 12.282 13.380 1.00 77.28 C ANISOU 238 CB ILE A 53 7519 10005 11837 147 228 -997 C ATOM 239 CG1 ILE A 53 72.534 12.121 12.140 1.00 78.22 C ANISOU 239 CG1 ILE A 53 7496 10170 12050 148 369 -1035 C ATOM 240 CG2 ILE A 53 72.423 12.290 14.678 1.00 78.49 C ANISOU 240 CG2 ILE A 53 7606 10135 12081 155 66 -978 C ATOM 241 CD1 ILE A 53 73.665 11.085 12.266 1.00 78.96 C ANISOU 241 CD1 ILE A 53 7431 10266 12302 233 350 -1061 C ATOM 242 N VAL A 54 71.252 9.418 14.931 1.00 77.13 N ANISOU 242 N VAL A 54 7563 9889 11854 353 38 -1005 N ATOM 243 CA VAL A 54 71.753 8.084 15.257 1.00 77.83 C ANISOU 243 CA VAL A 54 7599 9944 12026 452 -19 -1024 C ATOM 244 C VAL A 54 70.639 7.042 15.085 1.00 77.08 C ANISOU 244 C VAL A 54 7642 9815 11827 505 5 -1029 C ATOM 245 O VAL A 54 70.815 6.050 14.381 1.00 77.64 O ANISOU 245 O VAL A 54 7686 9880 11933 573 73 -1062 O ATOM 246 CB VAL A 54 72.350 8.018 16.686 1.00 78.41 C ANISOU 246 CB VAL A 54 7646 9977 12166 464 -204 -999 C ATOM 247 CG1 VAL A 54 72.937 6.642 16.956 1.00 78.48 C ANISOU 247 CG1 VAL A 54 7594 9948 12273 571 -267 -1019 C ATOM 248 CG2 VAL A 54 73.418 9.092 16.867 1.00 79.09 C ANISOU 248 CG2 VAL A 54 7600 10095 12353 397 -241 -986 C ATOM 249 N GLY A 55 69.490 7.285 15.701 1.00 76.05 N ANISOU 249 N GLY A 55 7663 9661 11569 472 -42 -996 N ATOM 250 CA GLY A 55 68.393 6.320 15.698 1.00 75.50 C ANISOU 250 CA GLY A 55 7725 9559 11403 510 -38 -990 C ATOM 251 C GLY A 55 67.968 5.814 14.329 1.00 75.48 C ANISOU 251 C GLY A 55 7740 9573 11363 525 100 -1016 C ATOM 252 O GLY A 55 67.803 4.612 14.131 1.00 75.60 O ANISOU 252 O GLY A 55 7793 9556 11373 588 102 -1032 O ATOM 253 N ASN A 56 67.769 6.728 13.386 1.00 75.47 N ANISOU 253 N ASN A 56 7731 9616 11328 463 210 -1018 N ATOM 254 CA ASN A 56 67.370 6.350 12.039 1.00 75.55 C ANISOU 254 CA ASN A 56 7775 9637 11293 465 340 -1041 C ATOM 255 C ASN A 56 68.557 5.772 11.292 1.00 77.35 C ANISOU 255 C ASN A 56 7884 9872 11633 519 415 -1090 C ATOM 256 O ASN A 56 68.411 4.811 10.533 1.00 77.58 O ANISOU 256 O ASN A 56 7952 9879 11644 566 482 -1116 O ATOM 257 CB ASN A 56 66.808 7.550 11.280 1.00 74.85 C ANISOU 257 CB ASN A 56 7723 9585 11129 378 426 -1026 C ATOM 258 CG ASN A 56 65.520 8.076 11.887 1.00 73.67 C ANISOU 258 CG ASN A 56 7694 9427 10869 336 371 -977 C ATOM 259 OD1 ASN A 56 65.439 9.242 12.269 1.00 73.45 O ANISOU 259 OD1 ASN A 56 7667 9417 10823 281 350 -955 O ATOM 260 ND2 ASN A 56 64.506 7.220 11.980 1.00 72.64 N ANISOU 260 ND2 ASN A 56 7664 9268 10664 360 349 -960 N ATOM 261 N GLY A 57 69.731 6.362 11.517 1.00 78.96 N ANISOU 261 N GLY A 57 7944 10104 11953 512 405 -1100 N ATOM 262 CA GLY A 57 70.980 5.870 10.945 1.00 80.82 C ANISOU 262 CA GLY A 57 8035 10351 12320 570 475 -1144 C ATOM 263 C GLY A 57 71.224 4.405 11.249 1.00 82.01 C ANISOU 263 C GLY A 57 8185 10451 12521 682 425 -1166 C ATOM 264 O GLY A 57 71.546 3.631 10.354 1.00 82.49 O ANISOU 264 O GLY A 57 8229 10502 12611 741 528 -1206 O ATOM 265 N LEU A 58 71.062 4.022 12.512 1.00 82.68 N ANISOU 265 N LEU A 58 8305 10498 12611 711 267 -1139 N ATOM 266 CA LEU A 58 71.193 2.622 12.902 1.00 84.06 C ANISOU 266 CA LEU A 58 8504 10614 12819 813 200 -1155 C ATOM 267 C LEU A 58 70.122 1.768 12.229 1.00 84.43 C ANISOU 267 C LEU A 58 8709 10628 12742 830 262 -1163 C ATOM 268 O LEU A 58 70.406 0.672 11.758 1.00 85.38 O ANISOU 268 O LEU A 58 8836 10712 12892 913 301 -1197 O ATOM 269 CB LEU A 58 71.128 2.456 14.424 1.00 83.79 C ANISOU 269 CB LEU A 58 8503 10539 12792 824 12 -1120 C ATOM 270 CG LEU A 58 72.419 2.757 15.195 1.00 84.65 C ANISOU 270 CG LEU A 58 8453 10653 13056 845 -89 -1116 C ATOM 271 CD1 LEU A 58 72.186 2.627 16.686 1.00 83.80 C ANISOU 271 CD1 LEU A 58 8423 10493 12923 841 -279 -1078 C ATOM 272 CD2 LEU A 58 73.559 1.845 14.760 1.00 85.64 C ANISOU 272 CD2 LEU A 58 8438 10767 13334 953 -58 -1158 C ATOM 273 N VAL A 59 68.897 2.275 12.168 1.00 84.46 N ANISOU 273 N VAL A 59 8841 10641 12608 752 271 -1129 N ATOM 274 CA VAL A 59 67.826 1.579 11.459 1.00 84.81 C ANISOU 274 CA VAL A 59 9031 10659 12533 748 327 -1129 C ATOM 275 C VAL A 59 68.171 1.368 9.989 1.00 86.58 C ANISOU 275 C VAL A 59 9237 10892 12765 763 485 -1172 C ATOM 276 O VAL A 59 67.800 0.354 9.417 1.00 86.92 O ANISOU 276 O VAL A 59 9375 10892 12758 802 521 -1190 O ATOM 277 CB VAL A 59 66.469 2.333 11.558 1.00 83.39 C ANISOU 277 CB VAL A 59 8965 10498 12220 655 319 -1080 C ATOM 278 CG1 VAL A 59 65.504 1.857 10.489 1.00 82.46 C ANISOU 278 CG1 VAL A 59 8968 10366 11995 633 401 -1079 C ATOM 279 CG2 VAL A 59 65.855 2.154 12.933 1.00 82.46 C ANISOU 279 CG2 VAL A 59 8916 10352 12060 652 179 -1039 C ATOM 280 N ILE A 60 68.883 2.315 9.381 1.00 88.52 N ANISOU 280 N ILE A 60 9374 11190 13069 726 580 -1190 N ATOM 281 CA ILE A 60 69.183 2.239 7.944 1.00 90.34 C ANISOU 281 CA ILE A 60 9602 11428 13293 726 745 -1231 C ATOM 282 C ILE A 60 70.331 1.291 7.597 1.00 93.01 C ANISOU 282 C ILE A 60 9848 11743 13749 834 805 -1285 C ATOM 283 O ILE A 60 70.313 0.676 6.536 1.00 93.83 O ANISOU 283 O ILE A 60 10014 11819 13815 863 923 -1320 O ATOM 284 CB ILE A 60 69.438 3.646 7.327 1.00 90.25 C ANISOU 284 CB ILE A 60 9527 11479 13285 634 839 -1228 C ATOM 285 CG1 ILE A 60 68.097 4.268 6.916 1.00 89.33 C ANISOU 285 CG1 ILE A 60 9557 11367 13016 540 850 -1191 C ATOM 286 CG2 ILE A 60 70.340 3.558 6.100 1.00 90.84 C ANISOU 286 CG2 ILE A 60 9532 11566 13414 653 1007 -1280 C ATOM 287 CD1 ILE A 60 68.190 5.733 6.543 1.00 89.44 C ANISOU 287 CD1 ILE A 60 9531 11433 13019 444 905 -1177 C ATOM 288 N LEU A 61 71.325 1.178 8.472 1.00 95.23 N ANISOU 288 N LEU A 61 9983 12028 14169 895 725 -1289 N ATOM 289 CA LEU A 61 72.483 0.314 8.204 1.00 97.83 C ANISOU 289 CA LEU A 61 10200 12337 14633 1010 778 -1338 C ATOM 290 C LEU A 61 72.206 -1.118 8.674 1.00 98.81 C ANISOU 290 C LEU A 61 10420 12382 14741 1110 687 -1346 C ATOM 291 O LEU A 61 72.713 -2.082 8.085 1.00 99.98 O ANISOU 291 O LEU A 61 10564 12490 14934 1207 763 -1391 O ATOM 292 CB LEU A 61 73.757 0.873 8.864 1.00 98.93 C ANISOU 292 CB LEU A 61 10121 12519 14949 1028 729 -1336 C ATOM 293 CG LEU A 61 74.156 2.324 8.509 1.00 99.16 C ANISOU 293 CG LEU A 61 10042 12625 15006 923 804 -1325 C ATOM 294 CD1 LEU A 61 75.197 2.876 9.516 1.00 99.95 C ANISOU 294 CD1 LEU A 61 9954 12758 15264 922 690 -1303 C ATOM 295 CD2 LEU A 61 74.685 2.462 7.056 1.00 99.72 C ANISOU 295 CD2 LEU A 61 10065 12725 15097 919 1022 -1371 C ATOM 296 N VAL A 62 71.398 -1.248 9.726 1.00 98.68 N ANISOU 296 N VAL A 62 10498 12339 14654 1084 531 -1302 N ATOM 297 CA VAL A 62 71.014 -2.552 10.249 1.00 99.47 C ANISOU 297 CA VAL A 62 10711 12362 14720 1159 432 -1301 C ATOM 298 C VAL A 62 69.926 -3.164 9.373 1.00 99.83 C ANISOU 298 C VAL A 62 10947 12369 14612 1136 503 -1305 C ATOM 299 O VAL A 62 70.136 -4.194 8.741 1.00100.72 O ANISOU 299 O VAL A 62 11113 12428 14725 1215 562 -1344 O ATOM 300 CB VAL A 62 70.515 -2.449 11.707 1.00 98.53 C ANISOU 300 CB VAL A 62 10637 12227 14573 1129 245 -1250 C ATOM 301 CG1 VAL A 62 69.870 -3.747 12.158 1.00 98.07 C ANISOU 301 CG1 VAL A 62 10731 12088 14441 1180 152 -1242 C ATOM 302 CG2 VAL A 62 71.658 -2.071 12.625 1.00 99.19 C ANISOU 302 CG2 VAL A 62 10549 12326 14810 1163 148 -1246 C ATOM 303 N MET A 63 68.771 -2.510 9.328 1.00 99.72 N ANISOU 303 N MET A 63 11036 12381 14470 1027 494 -1263 N ATOM 304 CA MET A 63 67.604 -3.032 8.613 1.00 99.92 C ANISOU 304 CA MET A 63 11245 12371 14347 987 532 -1252 C ATOM 305 C MET A 63 67.810 -2.919 7.106 1.00101.17 C ANISOU 305 C MET A 63 11423 12537 14481 976 706 -1292 C ATOM 306 O MET A 63 67.180 -3.648 6.345 1.00101.17 O ANISOU 306 O MET A 63 11572 12487 14381 973 748 -1299 O ATOM 307 CB MET A 63 66.330 -2.271 9.032 1.00 98.54 C ANISOU 307 CB MET A 63 11151 12227 14059 875 472 -1190 C ATOM 308 CG MET A 63 65.019 -3.071 8.967 1.00 98.19 C ANISOU 308 CG MET A 63 11289 12136 13879 842 425 -1157 C ATOM 309 SD MET A 63 64.671 -4.182 10.371 1.00 99.28 S ANISOU 309 SD MET A 63 11502 12212 14006 889 253 -1129 S ATOM 310 CE MET A 63 64.817 -3.088 11.790 1.00 98.21 C ANISOU 310 CE MET A 63 11265 12127 13923 855 152 -1092 C ATOM 311 N GLY A 64 68.687 -2.008 6.680 1.00102.72 N ANISOU 311 N GLY A 64 11476 12789 14761 964 803 -1315 N ATOM 312 CA GLY A 64 68.961 -1.795 5.255 1.00104.11 C ANISOU 312 CA GLY A 64 11669 12974 14914 946 981 -1354 C ATOM 313 C GLY A 64 69.779 -2.899 4.610 1.00106.38 C ANISOU 313 C GLY A 64 11955 13206 15256 1060 1075 -1416 C ATOM 314 O GLY A 64 69.485 -3.315 3.487 1.00106.86 O ANISOU 314 O GLY A 64 12145 13228 15229 1053 1187 -1441 O ATOM 315 N TYR A 65 70.817 -3.357 5.314 1.00108.26 N ANISOU 315 N TYR A 65 12054 13437 15642 1166 1029 -1438 N ATOM 316 CA TYR A 65 71.667 -4.465 4.851 1.00110.46 C ANISOU 316 CA TYR A 65 12315 13658 15995 1298 1109 -1497 C ATOM 317 C TYR A 65 71.429 -5.682 5.759 1.00110.67 C ANISOU 317 C TYR A 65 12418 13609 16021 1385 955 -1488 C ATOM 318 O TYR A 65 70.432 -5.718 6.484 1.00109.60 O ANISOU 318 O TYR A 65 12386 13462 15794 1324 819 -1438 O ATOM 319 CB TYR A 65 73.140 -4.023 4.831 1.00112.06 C ANISOU 319 CB TYR A 65 12278 13912 16385 1360 1191 -1531 C ATOM 320 CG TYR A 65 73.344 -2.602 4.296 1.00112.91 C ANISOU 320 CG TYR A 65 12292 14107 16500 1249 1296 -1522 C ATOM 321 CD1 TYR A 65 74.309 -1.752 4.848 1.00114.30 C ANISOU 321 CD1 TYR A 65 12245 14353 16828 1240 1276 -1513 C ATOM 322 CD2 TYR A 65 72.555 -2.102 3.247 1.00112.87 C ANISOU 322 CD2 TYR A 65 12430 14108 16346 1146 1403 -1519 C ATOM 323 CE1 TYR A 65 74.488 -0.448 4.361 1.00114.28 C ANISOU 323 CE1 TYR A 65 12169 14425 16824 1131 1368 -1503 C ATOM 324 CE2 TYR A 65 72.722 -0.806 2.762 1.00112.82 C ANISOU 324 CE2 TYR A 65 12353 14173 16338 1042 1492 -1510 C ATOM 325 CZ TYR A 65 73.687 0.014 3.319 1.00113.51 C ANISOU 325 CZ TYR A 65 12223 14330 16573 1034 1477 -1503 C ATOM 326 OH TYR A 65 73.841 1.292 2.832 1.00113.06 O ANISOU 326 OH TYR A 65 12109 14338 16507 924 1561 -1492 O ATOM 327 N GLN A 66 72.308 -6.684 5.704 1.00112.28 N ANISOU 327 N GLN A 66 12579 13758 16324 1524 981 -1535 N ATOM 328 CA GLN A 66 72.274 -7.825 6.642 1.00112.59 C ANISOU 328 CA GLN A 66 12671 13721 16385 1617 825 -1529 C ATOM 329 C GLN A 66 70.867 -8.331 7.011 1.00111.12 C ANISOU 329 C GLN A 66 12708 13485 16027 1548 705 -1484 C ATOM 330 O GLN A 66 69.983 -8.454 6.160 1.00110.30 O ANISOU 330 O GLN A 66 12771 13360 15778 1481 773 -1481 O ATOM 331 CB GLN A 66 73.051 -7.468 7.924 1.00112.98 C ANISOU 331 CB GLN A 66 12529 13806 16591 1653 686 -1506 C ATOM 332 CG GLN A 66 72.733 -6.080 8.506 1.00111.72 C ANISOU 332 CG GLN A 66 12292 13734 16422 1523 627 -1455 C ATOM 333 CD GLN A 66 73.467 -5.782 9.798 1.00112.21 C ANISOU 333 CD GLN A 66 12194 13816 16623 1551 474 -1430 C ATOM 334 OE1 GLN A 66 74.322 -4.899 9.849 1.00112.53 O ANISOU 334 OE1 GLN A 66 12046 13922 16785 1535 507 -1430 O ATOM 335 NE2 GLN A 66 73.127 -6.511 10.853 1.00112.25 N ANISOU 335 NE2 GLN A 66 12283 13760 16606 1585 301 -1404 N ATOM 336 N SER A 71 60.192 -9.448 6.205 1.00 79.92 N ANISOU 336 N SER A 71 10016 9416 10932 739 293 -1077 N ATOM 337 CA SER A 71 58.985 -8.926 6.850 1.00 78.85 C ANISOU 337 CA SER A 71 9882 9332 10744 633 212 -998 C ATOM 338 C SER A 71 58.506 -7.596 6.224 1.00 77.91 C ANISOU 338 C SER A 71 9702 9291 10609 546 282 -971 C ATOM 339 O SER A 71 59.196 -6.575 6.295 1.00 77.87 O ANISOU 339 O SER A 71 9559 9346 10682 567 341 -996 O ATOM 340 CB SER A 71 59.243 -8.750 8.350 1.00 78.64 C ANISOU 340 CB SER A 71 9754 9334 10789 669 123 -983 C ATOM 341 OG SER A 71 58.289 -7.883 8.947 1.00 77.76 O ANISOU 341 OG SER A 71 9603 9291 10650 579 84 -917 O ATOM 342 N MET A 72 57.312 -7.612 5.635 1.00 77.08 N ANISOU 342 N MET A 72 9702 9180 10402 444 264 -917 N ATOM 343 CA MET A 72 56.769 -6.443 4.927 1.00 76.03 C ANISOU 343 CA MET A 72 9536 9106 10244 359 318 -887 C ATOM 344 C MET A 72 56.706 -5.194 5.804 1.00 74.41 C ANISOU 344 C MET A 72 9179 8990 10103 345 308 -861 C ATOM 345 O MET A 72 56.970 -4.090 5.335 1.00 73.89 O ANISOU 345 O MET A 72 9036 8973 10064 325 380 -872 O ATOM 346 CB MET A 72 55.351 -6.735 4.407 1.00 76.01 C ANISOU 346 CB MET A 72 9662 9083 10133 249 263 -816 C ATOM 347 CG MET A 72 55.231 -7.891 3.407 1.00 77.66 C ANISOU 347 CG MET A 72 10055 9197 10256 237 266 -832 C ATOM 348 SD MET A 72 55.939 -7.577 1.768 1.00 80.01 S ANISOU 348 SD MET A 72 10415 9460 10523 243 405 -895 S ATOM 349 CE MET A 72 55.451 -9.102 0.941 1.00 80.48 C ANISOU 349 CE MET A 72 10724 9395 10458 214 363 -892 C ATOM 350 N THR A 73 56.340 -5.370 7.072 1.00 73.28 N ANISOU 350 N THR A 73 9006 8861 9976 350 219 -825 N ATOM 351 CA THR A 73 56.133 -4.237 7.970 1.00 72.00 C ANISOU 351 CA THR A 73 8727 8772 9857 330 203 -793 C ATOM 352 C THR A 73 57.445 -3.522 8.266 1.00 71.84 C ANISOU 352 C THR A 73 8577 8781 9935 401 251 -851 C ATOM 353 O THR A 73 57.458 -2.309 8.480 1.00 71.35 O ANISOU 353 O THR A 73 8425 8780 9904 377 277 -839 O ATOM 354 CB THR A 73 55.476 -4.653 9.290 1.00 71.58 C ANISOU 354 CB THR A 73 8688 8717 9788 320 104 -745 C ATOM 355 OG1 THR A 73 54.497 -5.664 9.039 1.00 71.91 O ANISOU 355 OG1 THR A 73 8859 8716 9748 266 52 -701 O ATOM 356 CG2 THR A 73 54.802 -3.457 9.943 1.00 70.63 C ANISOU 356 CG2 THR A 73 8490 8668 9676 272 101 -695 C ATOM 357 N ASP A 74 58.550 -4.264 8.272 1.00 72.07 N ANISOU 357 N ASP A 74 8597 8767 10019 488 261 -910 N ATOM 358 CA ASP A 74 59.866 -3.631 8.349 1.00 71.90 C ANISOU 358 CA ASP A 74 8441 8773 10101 552 315 -965 C ATOM 359 C ASP A 74 60.187 -2.857 7.068 1.00 71.35 C ANISOU 359 C ASP A 74 8344 8731 10032 523 438 -993 C ATOM 360 O ASP A 74 60.702 -1.740 7.138 1.00 71.32 O ANISOU 360 O ASP A 74 8229 8782 10085 514 480 -1003 O ATOM 361 CB ASP A 74 60.960 -4.659 8.645 1.00 72.91 C ANISOU 361 CB ASP A 74 8556 8846 10299 659 295 -1019 C ATOM 362 CG ASP A 74 60.974 -5.090 10.101 1.00 73.24 C ANISOU 362 CG ASP A 74 8587 8870 10368 693 171 -998 C ATOM 363 OD1 ASP A 74 61.081 -4.211 10.993 1.00 72.41 O ANISOU 363 OD1 ASP A 74 8395 8812 10305 678 133 -978 O ATOM 364 OD2 ASP A 74 60.882 -6.311 10.347 1.00 74.41 O ANISOU 364 OD2 ASP A 74 8831 8951 10490 732 109 -1001 O ATOM 365 N LYS A 75 59.869 -3.432 5.906 1.00 70.83 N ANISOU 365 N LYS A 75 8393 8622 9894 502 491 -1003 N ATOM 366 CA LYS A 75 60.167 -2.772 4.630 1.00 70.39 C ANISOU 366 CA LYS A 75 8338 8580 9825 469 611 -1031 C ATOM 367 C LYS A 75 59.653 -1.345 4.631 1.00 68.65 C ANISOU 367 C LYS A 75 8058 8430 9595 389 621 -990 C ATOM 368 O LYS A 75 60.376 -0.426 4.261 1.00 68.98 O ANISOU 368 O LYS A 75 8013 8509 9684 386 701 -1019 O ATOM 369 CB LYS A 75 59.603 -3.535 3.418 1.00 70.85 C ANISOU 369 CB LYS A 75 8566 8575 9779 433 646 -1031 C ATOM 370 CG LYS A 75 60.642 -4.391 2.679 1.00 73.00 C ANISOU 370 CG LYS A 75 8879 8786 10071 515 737 -1106 C ATOM 371 CD LYS A 75 60.353 -4.529 1.173 1.00 74.00 C ANISOU 371 CD LYS A 75 9154 8865 10097 461 826 -1119 C ATOM 372 CE LYS A 75 61.641 -4.720 0.367 1.00 75.68 C ANISOU 372 CE LYS A 75 9349 9050 10356 538 972 -1201 C ATOM 373 NZ LYS A 75 62.512 -3.481 0.316 1.00 76.15 N ANISOU 373 NZ LYS A 75 9240 9186 10506 539 1065 -1227 N ATOM 374 N TYR A 76 58.415 -1.156 5.071 1.00 66.68 N ANISOU 374 N TYR A 76 7851 8196 9288 326 541 -922 N ATOM 375 CA TYR A 76 57.831 0.179 5.094 1.00 65.01 C ANISOU 375 CA TYR A 76 7591 8043 9066 258 545 -881 C ATOM 376 C TYR A 76 58.589 1.100 6.041 1.00 64.05 C ANISOU 376 C TYR A 76 7331 7973 9032 291 543 -895 C ATOM 377 O TYR A 76 58.772 2.274 5.763 1.00 63.41 O ANISOU 377 O TYR A 76 7192 7932 8966 257 591 -896 O ATOM 378 CB TYR A 76 56.351 0.112 5.466 1.00 64.15 C ANISOU 378 CB TYR A 76 7543 7940 8891 196 461 -803 C ATOM 379 CG TYR A 76 55.468 -0.408 4.349 1.00 64.33 C ANISOU 379 CG TYR A 76 7697 7922 8822 131 460 -773 C ATOM 380 CD1 TYR A 76 55.373 0.269 3.140 1.00 64.43 C ANISOU 380 CD1 TYR A 76 7746 7935 8796 76 524 -776 C ATOM 381 CD2 TYR A 76 54.715 -1.570 4.506 1.00 65.08 C ANISOU 381 CD2 TYR A 76 7889 7972 8864 116 387 -739 C ATOM 382 CE1 TYR A 76 54.560 -0.202 2.115 1.00 65.14 C ANISOU 382 CE1 TYR A 76 7970 7979 8798 9 510 -745 C ATOM 383 CE2 TYR A 76 53.897 -2.047 3.487 1.00 64.94 C ANISOU 383 CE2 TYR A 76 7999 7913 8762 46 372 -707 C ATOM 384 CZ TYR A 76 53.828 -1.361 2.296 1.00 65.07 C ANISOU 384 CZ TYR A 76 8053 7928 8742 -5 431 -710 C ATOM 385 OH TYR A 76 53.025 -1.830 1.284 1.00 65.71 O ANISOU 385 OH TYR A 76 8272 7959 8734 -80 404 -675 O ATOM 386 N ARG A 77 59.045 0.552 7.154 1.00 63.74 N ANISOU 386 N ARG A 77 7247 7924 9047 354 479 -906 N ATOM 387 CA ARG A 77 59.768 1.337 8.141 1.00 63.45 C ANISOU 387 CA ARG A 77 7092 7925 9090 382 457 -916 C ATOM 388 C ARG A 77 61.176 1.673 7.665 1.00 63.92 C ANISOU 388 C ARG A 77 7054 7997 9236 421 536 -978 C ATOM 389 O ARG A 77 61.772 2.650 8.124 1.00 64.01 O ANISOU 389 O ARG A 77 6964 8047 9306 416 538 -983 O ATOM 390 CB ARG A 77 59.797 0.613 9.485 1.00 63.42 C ANISOU 390 CB ARG A 77 7087 7897 9110 431 353 -905 C ATOM 391 CG ARG A 77 58.406 0.461 10.074 1.00 62.99 C ANISOU 391 CG ARG A 77 7113 7842 8977 383 286 -839 C ATOM 392 CD ARG A 77 58.389 -0.359 11.340 1.00 63.36 C ANISOU 392 CD ARG A 77 7184 7856 9031 422 189 -827 C ATOM 393 NE ARG A 77 58.888 0.399 12.485 1.00 63.81 N ANISOU 393 NE ARG A 77 7167 7935 9140 439 146 -827 N ATOM 394 CZ ARG A 77 58.935 -0.068 13.729 1.00 64.33 C ANISOU 394 CZ ARG A 77 7254 7973 9212 467 56 -815 C ATOM 395 NH1 ARG A 77 58.518 -1.307 14.002 1.00 64.50 N ANISOU 395 NH1 ARG A 77 7365 7947 9194 480 1 -802 N ATOM 396 NH2 ARG A 77 59.409 0.702 14.702 1.00 64.30 N ANISOU 396 NH2 ARG A 77 7196 7984 9249 475 17 -814 N ATOM 397 N LEU A 78 61.706 0.881 6.739 1.00 64.19 N ANISOU 397 N LEU A 78 7119 7995 9274 457 604 -1023 N ATOM 398 CA LEU A 78 62.934 1.260 6.069 1.00 64.67 C ANISOU 398 CA LEU A 78 7089 8072 9409 483 708 -1078 C ATOM 399 C LEU A 78 62.699 2.594 5.376 1.00 63.98 C ANISOU 399 C LEU A 78 6989 8029 9288 398 777 -1064 C ATOM 400 O LEU A 78 63.352 3.580 5.690 1.00 63.85 O ANISOU 400 O LEU A 78 6864 8057 9336 385 792 -1070 O ATOM 401 CB LEU A 78 63.357 0.190 5.068 1.00 65.65 C ANISOU 401 CB LEU A 78 7277 8142 9522 531 788 -1126 C ATOM 402 CG LEU A 78 64.675 0.413 4.332 1.00 66.75 C ANISOU 402 CG LEU A 78 7322 8294 9743 570 916 -1188 C ATOM 403 CD1 LEU A 78 65.820 0.717 5.302 1.00 66.83 C ANISOU 403 CD1 LEU A 78 7156 8340 9895 629 882 -1207 C ATOM 404 CD2 LEU A 78 64.968 -0.815 3.480 1.00 67.43 C ANISOU 404 CD2 LEU A 78 7497 8313 9807 631 988 -1234 C ATOM 405 N HIS A 79 61.737 2.623 4.458 1.00 63.48 N ANISOU 405 N HIS A 79 7046 7950 9122 335 806 -1039 N ATOM 406 CA HIS A 79 61.277 3.875 3.839 1.00 62.86 C ANISOU 406 CA HIS A 79 6981 7905 8995 248 848 -1014 C ATOM 407 C HIS A 79 61.066 4.998 4.863 1.00 61.77 C ANISOU 407 C HIS A 79 6765 7816 8888 224 784 -977 C ATOM 408 O HIS A 79 61.669 6.066 4.757 1.00 62.26 O ANISOU 408 O HIS A 79 6753 7914 8987 196 829 -990 O ATOM 409 CB HIS A 79 59.950 3.655 3.111 1.00 62.39 C ANISOU 409 CB HIS A 79 7066 7817 8822 185 829 -969 C ATOM 410 CG HIS A 79 60.079 2.925 1.816 1.00 63.08 C ANISOU 410 CG HIS A 79 7261 7852 8853 177 908 -1002 C ATOM 411 ND1 HIS A 79 60.080 3.572 0.601 1.00 63.17 N ANISOU 411 ND1 HIS A 79 7331 7859 8811 112 995 -1010 N ATOM 412 CD2 HIS A 79 60.189 1.605 1.542 1.00 63.52 C ANISOU 412 CD2 HIS A 79 7396 7851 8888 224 913 -1027 C ATOM 413 CE1 HIS A 79 60.193 2.682 -0.368 1.00 64.40 C ANISOU 413 CE1 HIS A 79 7599 7955 8913 118 1054 -1041 C ATOM 414 NE2 HIS A 79 60.262 1.481 0.177 1.00 64.68 N ANISOU 414 NE2 HIS A 79 7649 7957 8967 188 1006 -1052 N ATOM 415 N LEU A 80 60.204 4.746 5.844 1.00 60.29 N ANISOU 415 N LEU A 80 6603 7626 8677 231 682 -931 N ATOM 416 CA LEU A 80 59.862 5.738 6.861 1.00 59.07 C ANISOU 416 CA LEU A 80 6400 7507 8535 212 623 -894 C ATOM 417 C LEU A 80 61.108 6.365 7.463 1.00 59.20 C ANISOU 417 C LEU A 80 6298 7549 8644 238 629 -928 C ATOM 418 O LEU A 80 61.219 7.584 7.590 1.00 58.38 O ANISOU 418 O LEU A 80 6156 7476 8548 197 639 -917 O ATOM 419 CB LEU A 80 59.039 5.081 7.972 1.00 58.51 C ANISOU 419 CB LEU A 80 6367 7422 8442 235 524 -853 C ATOM 420 CG LEU A 80 58.478 5.974 9.079 1.00 57.41 C ANISOU 420 CG LEU A 80 6207 7309 8297 219 466 -810 C ATOM 421 CD1 LEU A 80 57.659 7.111 8.505 1.00 56.07 C ANISOU 421 CD1 LEU A 80 6062 7164 8077 157 499 -774 C ATOM 422 CD2 LEU A 80 57.645 5.149 10.047 1.00 56.53 C ANISOU 422 CD2 LEU A 80 6146 7177 8154 238 386 -772 C ATOM 423 N SER A 81 62.056 5.509 7.815 1.00 59.91 N ANISOU 423 N SER A 81 6333 7621 8806 305 616 -967 N ATOM 424 CA SER A 81 63.281 5.955 8.461 1.00 60.41 C ANISOU 424 CA SER A 81 6273 7705 8972 333 602 -994 C ATOM 425 C SER A 81 64.199 6.714 7.518 1.00 60.78 C ANISOU 425 C SER A 81 6246 7781 9063 302 709 -1029 C ATOM 426 O SER A 81 65.020 7.508 7.972 1.00 61.30 O ANISOU 426 O SER A 81 6213 7877 9201 291 699 -1036 O ATOM 427 CB SER A 81 64.030 4.776 9.072 1.00 61.00 C ANISOU 427 CB SER A 81 6305 7749 9121 419 552 -1023 C ATOM 428 OG SER A 81 64.828 5.233 10.142 1.00 61.80 O ANISOU 428 OG SER A 81 6308 7864 9307 437 480 -1023 O ATOM 429 N VAL A 82 64.072 6.469 6.216 1.00 60.87 N ANISOU 429 N VAL A 82 6314 7783 9030 282 810 -1049 N ATOM 430 CA VAL A 82 64.796 7.263 5.218 1.00 61.30 C ANISOU 430 CA VAL A 82 6322 7863 9104 236 925 -1078 C ATOM 431 C VAL A 82 64.145 8.638 5.087 1.00 60.64 C ANISOU 431 C VAL A 82 6276 7805 8958 148 921 -1039 C ATOM 432 O VAL A 82 64.831 9.637 4.921 1.00 60.87 O ANISOU 432 O VAL A 82 6237 7865 9024 105 965 -1050 O ATOM 433 CB VAL A 82 64.881 6.538 3.852 1.00 61.86 C ANISOU 433 CB VAL A 82 6464 7903 9134 241 1040 -1114 C ATOM 434 CG1 VAL A 82 65.057 7.525 2.717 1.00 61.73 C ANISOU 434 CG1 VAL A 82 6466 7906 9080 161 1152 -1124 C ATOM 435 CG2 VAL A 82 66.021 5.524 3.873 1.00 62.24 C ANISOU 435 CG2 VAL A 82 6430 7937 9281 332 1082 -1167 C ATOM 436 N ALA A 83 62.821 8.679 5.195 1.00 60.06 N ANISOU 436 N ALA A 83 6308 7717 8794 123 865 -993 N ATOM 437 CA ALA A 83 62.074 9.932 5.128 1.00 59.56 C ANISOU 437 CA ALA A 83 6286 7670 8671 53 851 -952 C ATOM 438 C ALA A 83 62.389 10.837 6.310 1.00 59.69 C ANISOU 438 C ALA A 83 6231 7712 8735 52 785 -936 C ATOM 439 O ALA A 83 62.443 12.051 6.159 1.00 59.37 O ANISOU 439 O ALA A 83 6186 7688 8680 -3 802 -925 O ATOM 440 CB ALA A 83 60.598 9.653 5.073 1.00 58.57 C ANISOU 440 CB ALA A 83 6270 7524 8457 40 801 -902 C ATOM 441 N ASP A 84 62.588 10.238 7.484 1.00 60.30 N ANISOU 441 N ASP A 84 6266 7783 8861 111 704 -935 N ATOM 442 CA ASP A 84 62.869 10.993 8.706 1.00 60.68 C ANISOU 442 CA ASP A 84 6267 7843 8945 110 628 -918 C ATOM 443 C ASP A 84 64.330 11.420 8.749 1.00 61.71 C ANISOU 443 C ASP A 84 6279 7995 9173 103 650 -954 C ATOM 444 O ASP A 84 64.656 12.506 9.253 1.00 61.68 O ANISOU 444 O ASP A 84 6245 8004 9184 63 619 -942 O ATOM 445 CB ASP A 84 62.551 10.160 9.949 1.00 60.64 C ANISOU 445 CB ASP A 84 6276 7814 8948 169 528 -902 C ATOM 446 CG ASP A 84 61.069 9.783 10.055 1.00 61.54 C ANISOU 446 CG ASP A 84 6496 7913 8972 170 502 -858 C ATOM 447 OD1 ASP A 84 60.185 10.661 9.822 1.00 61.08 O ANISOU 447 OD1 ASP A 84 6490 7864 8851 126 516 -824 O ATOM 448 OD2 ASP A 84 60.801 8.595 10.395 1.00 63.72 O ANISOU 448 OD2 ASP A 84 6799 8166 9245 214 463 -857 O ATOM 449 N LEU A 85 65.212 10.565 8.230 1.00 62.62 N ANISOU 449 N LEU A 85 6325 8109 9356 142 703 -997 N ATOM 450 CA LEU A 85 66.632 10.876 8.209 1.00 63.54 C ANISOU 450 CA LEU A 85 6308 8251 9583 139 733 -1029 C ATOM 451 C LEU A 85 66.821 12.130 7.401 1.00 63.64 C ANISOU 451 C LEU A 85 6317 8292 9571 51 813 -1028 C ATOM 452 O LEU A 85 67.394 13.103 7.888 1.00 64.11 O ANISOU 452 O LEU A 85 6317 8371 9671 7 780 -1019 O ATOM 453 CB LEU A 85 67.452 9.734 7.612 1.00 64.43 C ANISOU 453 CB LEU A 85 6352 8358 9769 203 802 -1076 C ATOM 454 CG LEU A 85 68.969 9.923 7.708 1.00 66.15 C ANISOU 454 CG LEU A 85 6402 8605 10126 213 827 -1105 C ATOM 455 CD1 LEU A 85 69.404 10.105 9.166 1.00 66.35 C ANISOU 455 CD1 LEU A 85 6358 8628 10224 232 682 -1083 C ATOM 456 CD2 LEU A 85 69.726 8.757 7.059 1.00 67.74 C ANISOU 456 CD2 LEU A 85 6539 8797 10402 290 911 -1154 C ATOM 457 N LEU A 86 66.289 12.115 6.182 1.00 63.46 N ANISOU 457 N LEU A 86 6375 8264 9473 19 909 -1035 N ATOM 458 CA LEU A 86 66.434 13.234 5.257 1.00 63.86 C ANISOU 458 CA LEU A 86 6443 8332 9487 -68 994 -1036 C ATOM 459 C LEU A 86 65.984 14.536 5.903 1.00 63.32 C ANISOU 459 C LEU A 86 6410 8269 9378 -125 921 -995 C ATOM 460 O LEU A 86 66.510 15.600 5.595 1.00 63.89 O ANISOU 460 O LEU A 86 6457 8359 9458 -196 958 -996 O ATOM 461 CB LEU A 86 65.665 12.974 3.954 1.00 63.65 C ANISOU 461 CB LEU A 86 6538 8284 9362 -95 1080 -1039 C ATOM 462 CG LEU A 86 66.151 13.731 2.706 1.00 64.80 C ANISOU 462 CG LEU A 86 6696 8440 9482 -176 1203 -1059 C ATOM 463 CD1 LEU A 86 67.657 13.506 2.420 1.00 66.26 C ANISOU 463 CD1 LEU A 86 6741 8653 9779 -165 1299 -1108 C ATOM 464 CD2 LEU A 86 65.306 13.348 1.490 1.00 64.23 C ANISOU 464 CD2 LEU A 86 6767 8333 9302 -199 1267 -1058 C ATOM 465 N PHE A 87 65.029 14.440 6.817 1.00 62.77 N ANISOU 465 N PHE A 87 6404 8180 9264 -92 822 -960 N ATOM 466 CA PHE A 87 64.565 15.592 7.588 1.00 62.61 C ANISOU 466 CA PHE A 87 6427 8156 9205 -128 750 -922 C ATOM 467 C PHE A 87 65.548 16.006 8.669 1.00 63.39 C ANISOU 467 C PHE A 87 6437 8263 9385 -130 679 -925 C ATOM 468 O PHE A 87 65.893 17.179 8.768 1.00 63.74 O ANISOU 468 O PHE A 87 6478 8314 9426 -193 671 -915 O ATOM 469 CB PHE A 87 63.215 15.281 8.238 1.00 61.68 C ANISOU 469 CB PHE A 87 6403 8014 9018 -87 681 -884 C ATOM 470 CG PHE A 87 62.664 16.398 9.076 1.00 61.07 C ANISOU 470 CG PHE A 87 6380 7925 8896 -108 617 -847 C ATOM 471 CD1 PHE A 87 62.719 16.339 10.458 1.00 60.73 C ANISOU 471 CD1 PHE A 87 6330 7869 8874 -72 526 -834 C ATOM 472 CD2 PHE A 87 62.063 17.496 8.485 1.00 60.98 C ANISOU 472 CD2 PHE A 87 6441 7910 8818 -162 647 -825 C ATOM 473 CE1 PHE A 87 62.189 17.362 11.243 1.00 60.07 C ANISOU 473 CE1 PHE A 87 6315 7767 8741 -87 477 -802 C ATOM 474 CE2 PHE A 87 61.531 18.525 9.262 1.00 60.44 C ANISOU 474 CE2 PHE A 87 6433 7824 8707 -171 593 -793 C ATOM 475 CZ PHE A 87 61.600 18.454 10.646 1.00 59.85 C ANISOU 475 CZ PHE A 87 6354 7735 8650 -133 513 -783 C ATOM 476 N VAL A 88 65.992 15.057 9.493 1.00 63.93 N ANISOU 476 N VAL A 88 6442 8326 9522 -64 618 -936 N ATOM 477 CA VAL A 88 66.805 15.423 10.656 1.00 64.49 C ANISOU 477 CA VAL A 88 6445 8394 9662 -66 522 -930 C ATOM 478 C VAL A 88 68.059 16.159 10.222 1.00 65.62 C ANISOU 478 C VAL A 88 6480 8568 9884 -130 564 -948 C ATOM 479 O VAL A 88 68.397 17.177 10.822 1.00 66.03 O ANISOU 479 O VAL A 88 6529 8617 9941 -184 504 -929 O ATOM 480 CB VAL A 88 67.189 14.230 11.567 1.00 64.74 C ANISOU 480 CB VAL A 88 6424 8409 9764 13 441 -939 C ATOM 481 CG1 VAL A 88 65.951 13.476 12.014 1.00 63.44 C ANISOU 481 CG1 VAL A 88 6370 8215 9519 66 402 -919 C ATOM 482 CG2 VAL A 88 68.178 13.303 10.871 1.00 66.32 C ANISOU 482 CG2 VAL A 88 6503 8628 10065 52 506 -981 C ATOM 483 N ILE A 89 68.723 15.701 9.158 1.00 66.39 N ANISOU 483 N ILE A 89 6496 8692 10036 -129 672 -983 N ATOM 484 CA ILE A 89 69.933 16.402 8.698 1.00 67.49 C ANISOU 484 CA ILE A 89 6520 8867 10256 -197 728 -998 C ATOM 485 C ILE A 89 69.626 17.839 8.229 1.00 67.17 C ANISOU 485 C ILE A 89 6558 8829 10133 -300 761 -978 C ATOM 486 O ILE A 89 70.536 18.601 7.930 1.00 68.17 O ANISOU 486 O ILE A 89 6608 8982 10311 -375 796 -982 O ATOM 487 CB ILE A 89 70.740 15.620 7.614 1.00 68.46 C ANISOU 487 CB ILE A 89 6539 9017 10454 -173 860 -1043 C ATOM 488 CG1 ILE A 89 69.877 15.265 6.403 1.00 68.43 C ANISOU 488 CG1 ILE A 89 6650 9001 10348 -170 972 -1057 C ATOM 489 CG2 ILE A 89 71.335 14.364 8.197 1.00 68.35 C ANISOU 489 CG2 ILE A 89 6422 8998 10549 -73 813 -1062 C ATOM 490 CD1 ILE A 89 70.709 14.987 5.158 1.00 70.06 C ANISOU 490 CD1 ILE A 89 6784 9231 10602 -185 1129 -1099 C ATOM 491 N THR A 90 68.350 18.209 8.188 1.00 65.89 N ANISOU 491 N THR A 90 6546 8640 9850 -305 745 -953 N ATOM 492 CA THR A 90 67.964 19.576 7.890 1.00 65.57 C ANISOU 492 CA THR A 90 6595 8590 9728 -390 754 -930 C ATOM 493 C THR A 90 67.865 20.452 9.137 1.00 65.17 C ANISOU 493 C THR A 90 6586 8515 9660 -409 633 -898 C ATOM 494 O THR A 90 67.794 21.671 9.025 1.00 65.21 O ANISOU 494 O THR A 90 6653 8508 9613 -483 629 -880 O ATOM 495 CB THR A 90 66.618 19.614 7.154 1.00 64.68 C ANISOU 495 CB THR A 90 6622 8456 9497 -384 797 -916 C ATOM 496 OG1 THR A 90 66.642 20.663 6.185 1.00 65.68 O ANISOU 496 OG1 THR A 90 6802 8583 9569 -474 866 -913 O ATOM 497 CG2 THR A 90 65.454 19.843 8.117 1.00 64.10 C ANISOU 497 CG2 THR A 90 6653 8349 9353 -344 701 -879 C ATOM 498 N LEU A 91 67.870 19.842 10.321 1.00 64.90 N ANISOU 498 N LEU A 91 6532 8465 9662 -345 533 -890 N ATOM 499 CA LEU A 91 67.628 20.581 11.576 1.00 64.42 C ANISOU 499 CA LEU A 91 6543 8367 9565 -355 417 -860 C ATOM 500 C LEU A 91 68.722 21.580 11.977 1.00 65.41 C ANISOU 500 C LEU A 91 6617 8493 9741 -439 363 -852 C ATOM 501 O LEU A 91 68.410 22.683 12.404 1.00 65.10 O ANISOU 501 O LEU A 91 6679 8422 9633 -487 316 -828 O ATOM 502 CB LEU A 91 67.347 19.613 12.729 1.00 63.92 C ANISOU 502 CB LEU A 91 6487 8279 9517 -270 325 -853 C ATOM 503 CG LEU A 91 66.009 18.874 12.614 1.00 62.25 C ANISOU 503 CG LEU A 91 6366 8055 9229 -201 353 -845 C ATOM 504 CD1 LEU A 91 65.905 17.768 13.639 1.00 61.49 C ANISOU 504 CD1 LEU A 91 6263 7939 9159 -124 273 -844 C ATOM 505 CD2 LEU A 91 64.862 19.837 12.784 1.00 60.85 C ANISOU 505 CD2 LEU A 91 6328 7850 8940 -217 349 -814 C ATOM 506 N PRO A 92 70.007 21.210 11.845 1.00 66.73 N ANISOU 506 N PRO A 92 6626 8696 10033 -458 368 -871 N ATOM 507 CA PRO A 92 71.036 22.206 12.131 1.00 67.83 C ANISOU 507 CA PRO A 92 6709 8839 10223 -553 318 -858 C ATOM 508 C PRO A 92 70.771 23.557 11.469 1.00 68.06 C ANISOU 508 C PRO A 92 6831 8861 10164 -650 370 -845 C ATOM 509 O PRO A 92 70.997 24.588 12.094 1.00 68.65 O ANISOU 509 O PRO A 92 6962 8906 10213 -718 288 -820 O ATOM 510 CB PRO A 92 72.298 21.566 11.562 1.00 68.88 C ANISOU 510 CB PRO A 92 6643 9026 10501 -559 376 -884 C ATOM 511 CG PRO A 92 72.070 20.125 11.751 1.00 68.55 C ANISOU 511 CG PRO A 92 6561 8984 10499 -443 374 -904 C ATOM 512 CD PRO A 92 70.601 19.900 11.525 1.00 67.23 C ANISOU 512 CD PRO A 92 6553 8790 10199 -392 410 -901 C ATOM 513 N PHE A 93 70.281 23.556 10.232 1.00 67.94 N ANISOU 513 N PHE A 93 6850 8865 10098 -658 495 -860 N ATOM 514 CA PHE A 93 69.977 24.806 9.539 1.00 68.31 C ANISOU 514 CA PHE A 93 7000 8899 10056 -748 542 -848 C ATOM 515 C PHE A 93 68.859 25.513 10.288 1.00 67.83 C ANISOU 515 C PHE A 93 7113 8779 9880 -727 462 -818 C ATOM 516 O PHE A 93 69.011 26.658 10.722 1.00 67.91 O ANISOU 516 O PHE A 93 7195 8756 9849 -795 402 -796 O ATOM 517 CB PHE A 93 69.570 24.553 8.085 1.00 68.19 C ANISOU 517 CB PHE A 93 7005 8904 9997 -753 683 -869 C ATOM 518 CG PHE A 93 70.652 23.905 7.254 1.00 69.61 C ANISOU 518 CG PHE A 93 7029 9137 10281 -773 787 -902 C ATOM 519 CD1 PHE A 93 71.581 24.681 6.569 1.00 70.42 C ANISOU 519 CD1 PHE A 93 7075 9267 10415 -884 854 -906 C ATOM 520 CD2 PHE A 93 70.744 22.517 7.161 1.00 69.54 C ANISOU 520 CD2 PHE A 93 6934 9150 10338 -679 823 -929 C ATOM 521 CE1 PHE A 93 72.578 24.088 5.813 1.00 71.38 C ANISOU 521 CE1 PHE A 93 7046 9438 10635 -897 966 -937 C ATOM 522 CE2 PHE A 93 71.741 21.924 6.409 1.00 70.44 C ANISOU 522 CE2 PHE A 93 6906 9307 10548 -685 929 -961 C ATOM 523 CZ PHE A 93 72.660 22.708 5.737 1.00 71.27 C ANISOU 523 CZ PHE A 93 6946 9442 10688 -792 1006 -966 C ATOM 524 N TRP A 94 67.752 24.799 10.466 1.00 67.36 N ANISOU 524 N TRP A 94 7118 8704 9770 -631 462 -816 N ATOM 525 CA TRP A 94 66.621 25.274 11.260 1.00 67.09 C ANISOU 525 CA TRP A 94 7233 8618 9639 -589 398 -788 C ATOM 526 C TRP A 94 67.061 25.944 12.560 1.00 67.46 C ANISOU 526 C TRP A 94 7318 8624 9686 -615 281 -770 C ATOM 527 O TRP A 94 66.450 26.923 12.992 1.00 67.42 O ANISOU 527 O TRP A 94 7452 8570 9593 -627 243 -748 O ATOM 528 CB TRP A 94 65.687 24.106 11.617 1.00 66.68 C ANISOU 528 CB TRP A 94 7194 8564 9575 -479 394 -788 C ATOM 529 CG TRP A 94 64.605 23.770 10.620 1.00 67.39 C ANISOU 529 CG TRP A 94 7335 8663 9608 -446 477 -786 C ATOM 530 CD1 TRP A 94 64.695 22.915 9.558 1.00 68.10 C ANISOU 530 CD1 TRP A 94 7359 8787 9726 -437 560 -809 C ATOM 531 CD2 TRP A 94 63.256 24.249 10.636 1.00 68.87 C ANISOU 531 CD2 TRP A 94 7650 8817 9700 -414 477 -758 C ATOM 532 NE1 TRP A 94 63.495 22.853 8.898 1.00 68.19 N ANISOU 532 NE1 TRP A 94 7457 8787 9662 -413 601 -793 N ATOM 533 CE2 TRP A 94 62.592 23.662 9.540 1.00 69.13 C ANISOU 533 CE2 TRP A 94 7684 8868 9712 -396 550 -760 C ATOM 534 CE3 TRP A 94 62.542 25.128 11.473 1.00 70.13 C ANISOU 534 CE3 TRP A 94 7925 8930 9791 -397 423 -729 C ATOM 535 CZ2 TRP A 94 61.231 23.924 9.254 1.00 70.07 C ANISOU 535 CZ2 TRP A 94 7902 8965 9755 -364 560 -730 C ATOM 536 CZ3 TRP A 94 61.184 25.387 11.192 1.00 69.90 C ANISOU 536 CZ3 TRP A 94 7990 8880 9689 -354 447 -703 C ATOM 537 CH2 TRP A 94 60.549 24.785 10.092 1.00 69.61 C ANISOU 537 CH2 TRP A 94 7936 8867 9644 -340 510 -701 C ATOM 538 N ALA A 95 68.099 25.398 13.193 1.00 68.12 N ANISOU 538 N ALA A 95 7287 8724 9869 -619 218 -778 N ATOM 539 CA ALA A 95 68.548 25.875 14.506 1.00 68.68 C ANISOU 539 CA ALA A 95 7399 8749 9943 -642 88 -758 C ATOM 540 C ALA A 95 69.337 27.179 14.411 1.00 69.65 C ANISOU 540 C ALA A 95 7540 8859 10063 -763 57 -745 C ATOM 541 O ALA A 95 69.060 28.134 15.146 1.00 69.86 O ANISOU 541 O ALA A 95 7707 8825 10010 -792 -16 -722 O ATOM 542 CB ALA A 95 69.369 24.807 15.211 1.00 68.93 C ANISOU 542 CB ALA A 95 7304 8798 10087 -605 16 -767 C ATOM 543 N VAL A 96 70.310 27.225 13.506 1.00 70.30 N ANISOU 543 N VAL A 96 7486 8994 10228 -835 116 -758 N ATOM 544 CA VAL A 96 71.102 28.434 13.320 1.00 71.20 C ANISOU 544 CA VAL A 96 7607 9102 10344 -964 94 -742 C ATOM 545 C VAL A 96 70.235 29.559 12.733 1.00 70.68 C ANISOU 545 C VAL A 96 7710 8998 10144 -1002 144 -732 C ATOM 546 O VAL A 96 70.522 30.734 12.937 1.00 71.00 O ANISOU 546 O VAL A 96 7835 8999 10139 -1093 92 -712 O ATOM 547 CB VAL A 96 72.369 28.157 12.466 1.00 72.40 C ANISOU 547 CB VAL A 96 7557 9326 10624 -1033 162 -758 C ATOM 548 CG1 VAL A 96 73.115 29.448 12.158 1.00 73.27 C ANISOU 548 CG1 VAL A 96 7679 9432 10728 -1180 152 -739 C ATOM 549 CG2 VAL A 96 73.292 27.180 13.196 1.00 72.57 C ANISOU 549 CG2 VAL A 96 7412 9373 10786 -996 87 -761 C ATOM 550 N ASP A 97 69.168 29.192 12.026 1.00 69.89 N ANISOU 550 N ASP A 97 7664 8904 9984 -931 235 -744 N ATOM 551 CA ASP A 97 68.150 30.157 11.587 1.00 69.52 C ANISOU 551 CA ASP A 97 7788 8813 9811 -940 266 -731 C ATOM 552 C ASP A 97 67.432 30.750 12.784 1.00 69.13 C ANISOU 552 C ASP A 97 7898 8690 9678 -897 171 -707 C ATOM 553 O ASP A 97 67.167 31.951 12.831 1.00 69.19 O ANISOU 553 O ASP A 97 8045 8643 9600 -945 146 -690 O ATOM 554 CB ASP A 97 67.111 29.477 10.688 1.00 68.73 C ANISOU 554 CB ASP A 97 7702 8735 9677 -863 364 -742 C ATOM 555 CG ASP A 97 66.002 30.424 10.234 1.00 68.73 C ANISOU 555 CG ASP A 97 7869 8686 9558 -862 386 -724 C ATOM 556 OD1 ASP A 97 64.830 29.989 10.185 1.00 67.85 O ANISOU 556 OD1 ASP A 97 7812 8564 9403 -770 407 -717 O ATOM 557 OD2 ASP A 97 66.297 31.598 9.921 1.00 70.06 O ANISOU 557 OD2 ASP A 97 8113 8824 9679 -954 379 -713 O ATOM 558 N ALA A 98 67.107 29.884 13.738 1.00 68.71 N ANISOU 558 N ALA A 98 7831 8630 9645 -805 122 -708 N ATOM 559 CA ALA A 98 66.379 30.276 14.935 1.00 68.50 C ANISOU 559 CA ALA A 98 7956 8531 9536 -752 47 -689 C ATOM 560 C ALA A 98 67.147 31.289 15.779 1.00 69.61 C ANISOU 560 C ALA A 98 8174 8616 9656 -837 -60 -673 C ATOM 561 O ALA A 98 66.566 32.268 16.243 1.00 70.00 O ANISOU 561 O ALA A 98 8398 8594 9604 -837 -90 -657 O ATOM 562 CB ALA A 98 66.054 29.057 15.765 1.00 67.90 C ANISOU 562 CB ALA A 98 7840 8463 9493 -652 18 -694 C ATOM 563 N VAL A 99 68.444 31.062 15.975 1.00 70.49 N ANISOU 563 N VAL A 99 8159 8756 9867 -910 -119 -675 N ATOM 564 CA VAL A 99 69.234 31.893 16.890 1.00 71.41 C ANISOU 564 CA VAL A 99 8341 8816 9973 -998 -244 -654 C ATOM 565 C VAL A 99 69.816 33.133 16.215 1.00 72.22 C ANISOU 565 C VAL A 99 8475 8911 10054 -1129 -237 -643 C ATOM 566 O VAL A 99 69.734 34.231 16.764 1.00 72.74 O ANISOU 566 O VAL A 99 8706 8900 10031 -1180 -308 -623 O ATOM 567 CB VAL A 99 70.393 31.094 17.583 1.00 72.12 C ANISOU 567 CB VAL A 99 8280 8932 10188 -1020 -341 -652 C ATOM 568 CG1 VAL A 99 69.850 29.872 18.314 1.00 71.30 C ANISOU 568 CG1 VAL A 99 8163 8827 10099 -897 -359 -662 C ATOM 569 CG2 VAL A 99 71.471 30.689 16.585 1.00 72.66 C ANISOU 569 CG2 VAL A 99 8126 9089 10391 -1083 -284 -664 C ATOM 570 N ALA A 100 70.379 32.961 15.020 1.00 72.51 N ANISOU 570 N ALA A 100 8365 9021 10163 -1185 -148 -656 N ATOM 571 CA ALA A 100 71.272 33.966 14.430 1.00 73.39 C ANISOU 571 CA ALA A 100 8459 9138 10286 -1332 -149 -643 C ATOM 572 C ALA A 100 70.744 34.610 13.131 1.00 72.92 C ANISOU 572 C ALA A 100 8464 9086 10153 -1366 -32 -650 C ATOM 573 O ALA A 100 70.311 35.768 13.142 1.00 73.21 O ANISOU 573 O ALA A 100 8681 9055 10080 -1408 -56 -634 O ATOM 574 CB ALA A 100 72.657 33.345 14.202 1.00 74.28 C ANISOU 574 CB ALA A 100 8336 9328 10558 -1399 -153 -647 C ATOM 575 N ASN A 101 70.782 33.862 12.029 1.00 72.19 N ANISOU 575 N ASN A 101 8242 9068 10119 -1346 89 -674 N ATOM 576 CA ASN A 101 70.550 34.408 10.692 1.00 72.00 C ANISOU 576 CA ASN A 101 8258 9056 10043 -1404 197 -680 C ATOM 577 C ASN A 101 70.483 33.260 9.686 1.00 71.53 C ANISOU 577 C ASN A 101 8060 9071 10047 -1350 324 -709 C ATOM 578 O ASN A 101 70.830 32.141 10.037 1.00 71.56 O ANISOU 578 O ASN A 101 7922 9120 10148 -1286 322 -724 O ATOM 579 CB ASN A 101 71.689 35.378 10.346 1.00 73.36 C ANISOU 579 CB ASN A 101 8404 9233 10236 -1571 184 -665 C ATOM 580 CG ASN A 101 71.764 35.706 8.863 1.00 73.65 C ANISOU 580 CG ASN A 101 8436 9300 10247 -1648 313 -675 C ATOM 581 OD1 ASN A 101 70.874 36.348 8.302 1.00 73.27 O ANISOU 581 OD1 ASN A 101 8549 9205 10084 -1643 345 -672 O ATOM 582 ND2 ASN A 101 72.837 35.267 8.223 1.00 74.35 N ANISOU 582 ND2 ASN A 101 8340 9464 10445 -1720 388 -688 N ATOM 583 N TRP A 102 70.015 33.509 8.462 1.00 71.32 N ANISOU 583 N TRP A 102 8088 9049 9960 -1373 428 -718 N ATOM 584 CA TRP A 102 70.100 32.496 7.400 1.00 71.31 C ANISOU 584 CA TRP A 102 7969 9113 10013 -1345 553 -747 C ATOM 585 C TRP A 102 71.338 32.716 6.518 1.00 72.85 C ANISOU 585 C TRP A 102 8047 9358 10272 -1475 637 -757 C ATOM 586 O TRP A 102 71.316 33.499 5.558 1.00 72.96 O ANISOU 586 O TRP A 102 8144 9359 10218 -1567 702 -753 O ATOM 587 CB TRP A 102 68.817 32.441 6.554 1.00 70.43 C ANISOU 587 CB TRP A 102 7982 8977 9801 -1287 618 -750 C ATOM 588 CG TRP A 102 68.816 31.283 5.570 1.00 69.61 C ANISOU 588 CG TRP A 102 7778 8927 9741 -1248 735 -779 C ATOM 589 CD1 TRP A 102 69.160 31.333 4.256 1.00 69.70 C ANISOU 589 CD1 TRP A 102 7777 8962 9741 -1323 852 -795 C ATOM 590 CD2 TRP A 102 68.484 29.916 5.842 1.00 68.27 C ANISOU 590 CD2 TRP A 102 7523 8788 9628 -1128 746 -796 C ATOM 591 NE1 TRP A 102 69.058 30.095 3.689 1.00 69.00 N ANISOU 591 NE1 TRP A 102 7607 8913 9695 -1256 936 -822 N ATOM 592 CE2 TRP A 102 68.644 29.202 4.641 1.00 68.47 C ANISOU 592 CE2 TRP A 102 7491 8851 9671 -1136 870 -823 C ATOM 593 CE3 TRP A 102 68.056 29.227 6.980 1.00 67.53 C ANISOU 593 CE3 TRP A 102 7408 8687 9563 -1020 665 -791 C ATOM 594 CZ2 TRP A 102 68.394 27.825 4.542 1.00 67.51 C ANISOU 594 CZ2 TRP A 102 7294 8758 9597 -1036 909 -845 C ATOM 595 CZ3 TRP A 102 67.810 27.854 6.880 1.00 66.92 C ANISOU 595 CZ3 TRP A 102 7249 8643 9534 -925 703 -811 C ATOM 596 CH2 TRP A 102 67.982 27.174 5.669 1.00 66.44 C ANISOU 596 CH2 TRP A 102 7134 8617 9491 -933 821 -838 C ATOM 597 N TYR A 103 72.409 31.996 6.851 1.00 73.91 N ANISOU 597 N TYR A 103 7988 9550 10543 -1479 638 -768 N ATOM 598 CA TYR A 103 73.710 32.158 6.198 1.00 75.64 C ANISOU 598 CA TYR A 103 8062 9826 10851 -1597 714 -774 C ATOM 599 C TYR A 103 73.846 31.394 4.859 1.00 75.70 C ANISOU 599 C TYR A 103 7990 9886 10886 -1588 889 -809 C ATOM 600 O TYR A 103 74.838 31.581 4.148 1.00 77.14 O ANISOU 600 O TYR A 103 8068 10114 11128 -1690 982 -816 O ATOM 601 CB TYR A 103 74.853 31.692 7.145 1.00 76.75 C ANISOU 601 CB TYR A 103 8009 10006 11145 -1601 635 -767 C ATOM 602 CG TYR A 103 75.095 32.526 8.405 1.00 77.81 C ANISOU 602 CG TYR A 103 8203 10090 11269 -1651 463 -729 C ATOM 603 CD1 TYR A 103 74.484 32.194 9.616 1.00 77.34 C ANISOU 603 CD1 TYR A 103 8213 9986 11188 -1548 339 -721 C ATOM 604 CD2 TYR A 103 75.970 33.621 8.394 1.00 79.80 C ANISOU 604 CD2 TYR A 103 8449 10339 11533 -1809 426 -701 C ATOM 605 CE1 TYR A 103 74.710 32.942 10.776 1.00 78.05 C ANISOU 605 CE1 TYR A 103 8378 10020 11257 -1596 182 -687 C ATOM 606 CE2 TYR A 103 76.201 34.377 9.552 1.00 80.62 C ANISOU 606 CE2 TYR A 103 8625 10387 11619 -1861 260 -665 C ATOM 607 CZ TYR A 103 75.566 34.027 10.738 1.00 79.84 C ANISOU 607 CZ TYR A 103 8606 10237 11491 -1752 139 -660 C ATOM 608 OH TYR A 103 75.774 34.760 11.884 1.00 80.87 O ANISOU 608 OH TYR A 103 8831 10303 11592 -1803 -21 -626 O ATOM 609 N PHE A 104 72.861 30.573 4.491 1.00 74.44 N ANISOU 609 N PHE A 104 7888 9717 10677 -1475 936 -829 N ATOM 610 CA PHE A 104 73.104 29.475 3.539 1.00 74.62 C ANISOU 610 CA PHE A 104 7807 9790 10754 -1433 1079 -867 C ATOM 611 C PHE A 104 72.600 29.636 2.091 1.00 74.42 C ANISOU 611 C PHE A 104 7898 9751 10626 -1476 1211 -882 C ATOM 612 O PHE A 104 72.516 28.648 1.355 1.00 74.13 O ANISOU 612 O PHE A 104 7822 9737 10606 -1420 1318 -913 O ATOM 613 CB PHE A 104 72.530 28.179 4.113 1.00 73.77 C ANISOU 613 CB PHE A 104 7658 9686 10684 -1277 1042 -882 C ATOM 614 CG PHE A 104 72.835 27.972 5.566 1.00 73.85 C ANISOU 614 CG PHE A 104 7591 9694 10772 -1226 900 -866 C ATOM 615 CD1 PHE A 104 71.960 28.438 6.544 1.00 73.19 C ANISOU 615 CD1 PHE A 104 7643 9555 10611 -1187 771 -838 C ATOM 616 CD2 PHE A 104 73.985 27.302 5.958 1.00 74.55 C ANISOU 616 CD2 PHE A 104 7478 9833 11014 -1214 896 -877 C ATOM 617 CE1 PHE A 104 72.232 28.244 7.893 1.00 73.25 C ANISOU 617 CE1 PHE A 104 7602 9551 10678 -1146 639 -823 C ATOM 618 CE2 PHE A 104 74.266 27.103 7.303 1.00 74.72 C ANISOU 618 CE2 PHE A 104 7441 9845 11104 -1172 751 -859 C ATOM 619 CZ PHE A 104 73.388 27.575 8.274 1.00 74.05 C ANISOU 619 CZ PHE A 104 7510 9699 10927 -1141 622 -833 C ATOM 620 N GLY A 105 72.285 30.856 1.666 1.00 74.47 N ANISOU 620 N GLY A 105 8057 9714 10523 -1576 1202 -860 N ATOM 621 CA GLY A 105 71.862 31.080 0.276 1.00 74.61 C ANISOU 621 CA GLY A 105 8199 9711 10439 -1631 1318 -871 C ATOM 622 C GLY A 105 70.454 30.579 -0.025 1.00 73.25 C ANISOU 622 C GLY A 105 8162 9495 10172 -1528 1303 -871 C ATOM 623 O GLY A 105 69.781 30.031 0.854 1.00 72.43 O ANISOU 623 O GLY A 105 8051 9383 10085 -1411 1212 -864 O ATOM 624 N ASN A 106 70.008 30.755 -1.269 1.00 73.03 N ANISOU 624 N ASN A 106 8262 9439 10047 -1577 1389 -877 N ATOM 625 CA ASN A 106 68.599 30.533 -1.618 1.00 71.68 C ANISOU 625 CA ASN A 106 8243 9216 9775 -1503 1354 -865 C ATOM 626 C ASN A 106 68.258 29.098 -2.056 1.00 70.93 C ANISOU 626 C ASN A 106 8104 9141 9704 -1408 1420 -892 C ATOM 627 O ASN A 106 67.122 28.661 -1.913 1.00 69.88 O ANISOU 627 O ASN A 106 8044 8979 9527 -1318 1359 -877 O ATOM 628 CB ASN A 106 68.156 31.527 -2.696 1.00 72.00 C ANISOU 628 CB ASN A 106 8472 9199 9685 -1605 1382 -848 C ATOM 629 CG ASN A 106 66.731 32.009 -2.489 1.00 71.32 C ANISOU 629 CG ASN A 106 8548 9046 9504 -1547 1267 -812 C ATOM 630 OD1 ASN A 106 66.433 32.681 -1.501 1.00 71.69 O ANISOU 630 OD1 ASN A 106 8619 9070 9550 -1518 1156 -786 O ATOM 631 ND2 ASN A 106 65.843 31.670 -3.419 1.00 70.68 N ANISOU 631 ND2 ASN A 106 8580 8928 9345 -1528 1292 -808 N ATOM 632 N PHE A 107 69.236 28.379 -2.595 1.00 71.42 N ANISOU 632 N PHE A 107 8049 9251 9836 -1428 1547 -929 N ATOM 633 CA PHE A 107 69.039 26.992 -2.988 1.00 70.92 C ANISOU 633 CA PHE A 107 7946 9202 9798 -1338 1615 -959 C ATOM 634 C PHE A 107 68.804 26.131 -1.745 1.00 69.41 C ANISOU 634 C PHE A 107 7647 9033 9693 -1206 1516 -957 C ATOM 635 O PHE A 107 67.920 25.266 -1.729 1.00 68.44 O ANISOU 635 O PHE A 107 7568 8892 9544 -1114 1488 -956 O ATOM 636 CB PHE A 107 70.252 26.483 -3.791 1.00 72.52 C ANISOU 636 CB PHE A 107 8041 9447 10063 -1386 1785 -1003 C ATOM 637 CG PHE A 107 70.185 25.017 -4.138 1.00 73.78 C ANISOU 637 CG PHE A 107 8158 9619 10257 -1286 1860 -1038 C ATOM 638 CD1 PHE A 107 70.917 24.080 -3.408 1.00 75.05 C ANISOU 638 CD1 PHE A 107 8129 9829 10556 -1198 1866 -1062 C ATOM 639 CD2 PHE A 107 69.376 24.569 -5.181 1.00 75.05 C ANISOU 639 CD2 PHE A 107 8476 9731 10307 -1281 1913 -1046 C ATOM 640 CE1 PHE A 107 70.851 22.721 -3.716 1.00 75.87 C ANISOU 640 CE1 PHE A 107 8204 9934 10686 -1102 1931 -1096 C ATOM 641 CE2 PHE A 107 69.302 23.211 -5.498 1.00 75.55 C ANISOU 641 CE2 PHE A 107 8516 9795 10392 -1193 1976 -1078 C ATOM 642 CZ PHE A 107 70.042 22.286 -4.763 1.00 76.03 C ANISOU 642 CZ PHE A 107 8390 9905 10590 -1101 1989 -1104 C ATOM 643 N LEU A 108 69.598 26.365 -0.704 1.00 68.92 N ANISOU 643 N LEU A 108 7450 9005 9730 -1205 1459 -953 N ATOM 644 CA LEU A 108 69.462 25.593 0.521 1.00 67.69 C ANISOU 644 CA LEU A 108 7200 8865 9653 -1089 1361 -950 C ATOM 645 C LEU A 108 68.230 26.022 1.293 1.00 65.95 C ANISOU 645 C LEU A 108 7099 8599 9358 -1040 1226 -912 C ATOM 646 O LEU A 108 67.690 25.231 2.057 1.00 65.56 O ANISOU 646 O LEU A 108 7026 8548 9333 -935 1159 -908 O ATOM 647 CB LEU A 108 70.707 25.700 1.406 1.00 68.51 C ANISOU 647 CB LEU A 108 7129 9014 9887 -1107 1328 -954 C ATOM 648 CG LEU A 108 71.977 24.973 0.947 1.00 69.65 C ANISOU 648 CG LEU A 108 7098 9213 10150 -1114 1449 -992 C ATOM 649 CD1 LEU A 108 73.081 25.188 1.969 1.00 70.53 C ANISOU 649 CD1 LEU A 108 7039 9363 10395 -1132 1379 -982 C ATOM 650 CD2 LEU A 108 71.743 23.484 0.739 1.00 68.73 C ANISOU 650 CD2 LEU A 108 6941 9104 10067 -995 1500 -1023 C ATOM 651 N CYS A 109 67.785 27.263 1.101 1.00 65.07 N ANISOU 651 N CYS A 109 7118 8449 9156 -1113 1191 -884 N ATOM 652 CA CYS A 109 66.532 27.728 1.706 1.00 63.51 C ANISOU 652 CA CYS A 109 7044 8202 8882 -1060 1081 -848 C ATOM 653 C CYS A 109 65.364 26.962 1.132 1.00 61.92 C ANISOU 653 C CYS A 109 6921 7981 8624 -990 1095 -843 C ATOM 654 O CYS A 109 64.467 26.575 1.863 1.00 61.07 O ANISOU 654 O CYS A 109 6832 7861 8511 -898 1018 -823 O ATOM 655 CB CYS A 109 66.324 29.228 1.482 1.00 63.87 C ANISOU 655 CB CYS A 109 7223 8203 8842 -1151 1048 -821 C ATOM 656 SG CYS A 109 64.703 29.906 1.976 1.00 63.94 S ANISOU 656 SG CYS A 109 7398 8143 8751 -1083 936 -776 S ATOM 657 N LYS A 110 65.385 26.742 -0.178 1.00 61.54 N ANISOU 657 N LYS A 110 6922 7927 8531 -1039 1193 -859 N ATOM 658 CA LYS A 110 64.340 25.976 -0.850 1.00 60.38 C ANISOU 658 CA LYS A 110 6857 7756 8327 -989 1205 -852 C ATOM 659 C LYS A 110 64.378 24.519 -0.441 1.00 59.53 C ANISOU 659 C LYS A 110 6646 7680 8290 -890 1213 -874 C ATOM 660 O LYS A 110 63.337 23.903 -0.208 1.00 58.62 O ANISOU 660 O LYS A 110 6570 7549 8152 -814 1157 -853 O ATOM 661 CB LYS A 110 64.484 26.081 -2.368 1.00 61.03 C ANISOU 661 CB LYS A 110 7030 7817 8338 -1077 1311 -867 C ATOM 662 CG LYS A 110 64.014 27.403 -2.920 1.00 61.35 C ANISOU 662 CG LYS A 110 7222 7806 8279 -1162 1282 -836 C ATOM 663 CD LYS A 110 64.095 27.461 -4.433 1.00 62.15 C ANISOU 663 CD LYS A 110 7437 7877 8298 -1254 1381 -849 C ATOM 664 CE LYS A 110 63.849 28.887 -4.939 1.00 62.92 C ANISOU 664 CE LYS A 110 7682 7922 8302 -1353 1351 -821 C ATOM 665 NZ LYS A 110 62.555 29.478 -4.451 1.00 62.21 N ANISOU 665 NZ LYS A 110 7685 7785 8165 -1297 1214 -771 N ATOM 666 N ALA A 111 65.590 23.983 -0.351 1.00 59.72 N ANISOU 666 N ALA A 111 6537 7748 8405 -893 1282 -912 N ATOM 667 CA ALA A 111 65.801 22.572 -0.061 1.00 59.27 C ANISOU 667 CA ALA A 111 6382 7717 8421 -802 1301 -938 C ATOM 668 C ALA A 111 65.293 22.238 1.323 1.00 58.11 C ANISOU 668 C ALA A 111 6192 7572 8312 -710 1178 -916 C ATOM 669 O ALA A 111 64.820 21.129 1.568 1.00 57.71 O ANISOU 669 O ALA A 111 6127 7521 8277 -626 1158 -919 O ATOM 670 CB ALA A 111 67.285 22.226 -0.179 1.00 60.38 C ANISOU 670 CB ALA A 111 6374 7903 8664 -823 1395 -981 C ATOM 671 N VAL A 112 65.393 23.205 2.225 1.00 57.51 N ANISOU 671 N VAL A 112 6108 7494 8246 -730 1098 -893 N ATOM 672 CA VAL A 112 64.953 23.013 3.592 1.00 56.85 C ANISOU 672 CA VAL A 112 6002 7407 8190 -651 987 -872 C ATOM 673 C VAL A 112 63.419 22.877 3.668 1.00 56.01 C ANISOU 673 C VAL A 112 6008 7267 8004 -596 934 -837 C ATOM 674 O VAL A 112 62.888 22.005 4.378 1.00 55.49 O ANISOU 674 O VAL A 112 5921 7204 7959 -511 885 -830 O ATOM 675 CB VAL A 112 65.495 24.147 4.494 1.00 56.93 C ANISOU 675 CB VAL A 112 5996 7413 8220 -696 918 -858 C ATOM 676 CG1 VAL A 112 64.580 24.439 5.664 1.00 55.93 C ANISOU 676 CG1 VAL A 112 5935 7256 8059 -636 808 -824 C ATOM 677 CG2 VAL A 112 66.880 23.771 4.979 1.00 58.14 C ANISOU 677 CG2 VAL A 112 5994 7606 8490 -704 923 -884 C ATOM 678 N HIS A 113 62.712 23.720 2.927 1.00 55.69 N ANISOU 678 N HIS A 113 6085 7195 7878 -644 942 -814 N ATOM 679 CA HIS A 113 61.257 23.660 2.920 1.00 54.88 C ANISOU 679 CA HIS A 113 6077 7063 7712 -596 892 -775 C ATOM 680 C HIS A 113 60.753 22.463 2.107 1.00 54.73 C ANISOU 680 C HIS A 113 6071 7044 7678 -568 932 -780 C ATOM 681 O HIS A 113 59.731 21.854 2.449 1.00 54.18 O ANISOU 681 O HIS A 113 6021 6967 7596 -503 882 -753 O ATOM 682 CB HIS A 113 60.671 24.962 2.383 1.00 54.83 C ANISOU 682 CB HIS A 113 6191 7015 7624 -653 877 -745 C ATOM 683 CG HIS A 113 60.776 26.105 3.339 1.00 54.29 C ANISOU 683 CG HIS A 113 6143 6930 7552 -658 815 -728 C ATOM 684 ND1 HIS A 113 59.706 26.553 4.079 1.00 52.80 N ANISOU 684 ND1 HIS A 113 6016 6713 7332 -597 743 -690 N ATOM 685 CD2 HIS A 113 61.825 26.888 3.680 1.00 54.34 C ANISOU 685 CD2 HIS A 113 6122 6941 7582 -720 815 -744 C ATOM 686 CE1 HIS A 113 60.090 27.572 4.825 1.00 53.02 C ANISOU 686 CE1 HIS A 113 6068 6720 7353 -617 704 -686 C ATOM 687 NE2 HIS A 113 61.371 27.796 4.601 1.00 53.27 N ANISOU 687 NE2 HIS A 113 6049 6773 7418 -696 739 -717 N ATOM 688 N VAL A 114 61.473 22.135 1.034 1.00 55.06 N ANISOU 688 N VAL A 114 6108 7093 7718 -621 1024 -814 N ATOM 689 CA VAL A 114 61.122 20.995 0.199 1.00 54.63 C ANISOU 689 CA VAL A 114 6083 7030 7642 -603 1068 -825 C ATOM 690 C VAL A 114 61.130 19.731 1.051 1.00 54.25 C ANISOU 690 C VAL A 114 5948 7004 7659 -511 1038 -836 C ATOM 691 O VAL A 114 60.084 19.078 1.239 1.00 53.32 O ANISOU 691 O VAL A 114 5868 6872 7516 -460 984 -807 O ATOM 692 CB VAL A 114 62.103 20.842 -0.967 1.00 55.42 C ANISOU 692 CB VAL A 114 6186 7133 7736 -670 1190 -869 C ATOM 693 CG1 VAL A 114 61.946 19.481 -1.637 1.00 54.93 C ANISOU 693 CG1 VAL A 114 6146 7061 7664 -636 1240 -890 C ATOM 694 CG2 VAL A 114 61.894 21.971 -1.961 1.00 56.18 C ANISOU 694 CG2 VAL A 114 6403 7196 7746 -768 1216 -853 C ATOM 695 N ILE A 115 62.306 19.421 1.602 1.00 54.35 N ANISOU 695 N ILE A 115 5843 7049 7757 -492 1065 -873 N ATOM 696 CA ILE A 115 62.475 18.222 2.419 1.00 53.71 C ANISOU 696 CA ILE A 115 5679 6984 7743 -406 1033 -887 C ATOM 697 C ILE A 115 61.343 18.113 3.446 1.00 52.51 C ANISOU 697 C ILE A 115 5558 6821 7572 -347 927 -843 C ATOM 698 O ILE A 115 60.797 17.030 3.665 1.00 52.17 O ANISOU 698 O ILE A 115 5519 6772 7529 -289 900 -837 O ATOM 699 CB ILE A 115 63.835 18.201 3.130 1.00 54.10 C ANISOU 699 CB ILE A 115 5592 7066 7896 -394 1041 -920 C ATOM 700 CG1 ILE A 115 64.966 17.970 2.120 1.00 55.26 C ANISOU 700 CG1 ILE A 115 5685 7230 8081 -433 1165 -967 C ATOM 701 CG2 ILE A 115 63.861 17.101 4.171 1.00 53.70 C ANISOU 701 CG2 ILE A 115 5474 7021 7907 -302 977 -925 C ATOM 702 CD1 ILE A 115 66.368 17.989 2.732 1.00 55.36 C ANISOU 702 CD1 ILE A 115 5542 7280 8213 -428 1175 -995 C ATOM 703 N TYR A 116 60.976 19.240 4.044 1.00 51.64 N ANISOU 703 N TYR A 116 5477 6705 7439 -364 872 -813 N ATOM 704 CA TYR A 116 59.969 19.245 5.084 1.00 50.72 C ANISOU 704 CA TYR A 116 5386 6578 7307 -307 787 -773 C ATOM 705 C TYR A 116 58.634 18.774 4.516 1.00 50.04 C ANISOU 705 C TYR A 116 5375 6474 7162 -291 776 -737 C ATOM 706 O TYR A 116 57.946 17.929 5.125 1.00 49.44 O ANISOU 706 O TYR A 116 5292 6399 7092 -232 733 -718 O ATOM 707 CB TYR A 116 59.881 20.649 5.697 1.00 50.82 C ANISOU 707 CB TYR A 116 5431 6578 7299 -331 746 -751 C ATOM 708 CG TYR A 116 58.924 20.849 6.879 1.00 50.98 C ANISOU 708 CG TYR A 116 5484 6584 7302 -270 672 -713 C ATOM 709 CD1 TYR A 116 58.305 19.780 7.545 1.00 50.78 C ANISOU 709 CD1 TYR A 116 5440 6564 7289 -201 639 -699 C ATOM 710 CD2 TYR A 116 58.666 22.129 7.344 1.00 50.61 C ANISOU 710 CD2 TYR A 116 5493 6514 7221 -284 641 -691 C ATOM 711 CE1 TYR A 116 57.441 20.011 8.612 1.00 50.37 C ANISOU 711 CE1 TYR A 116 5420 6498 7218 -151 587 -664 C ATOM 712 CE2 TYR A 116 57.820 22.350 8.404 1.00 50.45 C ANISOU 712 CE2 TYR A 116 5510 6477 7181 -226 590 -659 C ATOM 713 CZ TYR A 116 57.206 21.309 9.028 1.00 49.95 C ANISOU 713 CZ TYR A 116 5422 6422 7132 -161 568 -645 C ATOM 714 OH TYR A 116 56.371 21.606 10.080 1.00 49.66 O ANISOU 714 OH TYR A 116 5428 6368 7072 -107 532 -613 O ATOM 715 N THR A 117 58.280 19.299 3.344 1.00 49.75 N ANISOU 715 N THR A 117 5415 6418 7068 -349 811 -726 N ATOM 716 CA THR A 117 57.020 18.942 2.714 1.00 49.12 C ANISOU 716 CA THR A 117 5409 6317 6934 -346 788 -686 C ATOM 717 C THR A 117 57.017 17.458 2.362 1.00 49.11 C ANISOU 717 C THR A 117 5397 6317 6943 -322 806 -702 C ATOM 718 O THR A 117 56.020 16.783 2.546 1.00 48.69 O ANISOU 718 O THR A 117 5364 6259 6877 -289 758 -666 O ATOM 719 CB THR A 117 56.753 19.760 1.448 1.00 49.33 C ANISOU 719 CB THR A 117 5531 6314 6896 -421 813 -673 C ATOM 720 OG1 THR A 117 56.891 21.149 1.733 1.00 48.40 O ANISOU 720 OG1 THR A 117 5433 6189 6767 -447 799 -663 O ATOM 721 CG2 THR A 117 55.350 19.510 0.944 1.00 49.51 C ANISOU 721 CG2 THR A 117 5627 6312 6872 -417 763 -619 C ATOM 722 N VAL A 118 58.146 16.947 1.888 1.00 49.77 N ANISOU 722 N VAL A 118 5448 6409 7053 -337 877 -755 N ATOM 723 CA VAL A 118 58.235 15.538 1.512 1.00 49.97 C ANISOU 723 CA VAL A 118 5474 6426 7083 -310 902 -777 C ATOM 724 C VAL A 118 58.005 14.690 2.755 1.00 49.81 C ANISOU 724 C VAL A 118 5392 6420 7111 -232 838 -768 C ATOM 725 O VAL A 118 57.090 13.856 2.792 1.00 49.54 O ANISOU 725 O VAL A 118 5397 6373 7052 -208 795 -738 O ATOM 726 CB VAL A 118 59.604 15.166 0.880 1.00 50.64 C ANISOU 726 CB VAL A 118 5521 6518 7202 -325 1003 -841 C ATOM 727 CG1 VAL A 118 59.513 13.826 0.183 1.00 50.51 C ANISOU 727 CG1 VAL A 118 5552 6476 7163 -306 1038 -860 C ATOM 728 CG2 VAL A 118 60.068 16.228 -0.110 1.00 51.28 C ANISOU 728 CG2 VAL A 118 5646 6591 7245 -410 1075 -854 C ATOM 729 N ASN A 119 58.818 14.933 3.780 1.00 50.11 N ANISOU 729 N ASN A 119 5342 6483 7214 -200 825 -789 N ATOM 730 CA ASN A 119 58.733 14.177 5.032 1.00 50.10 C ANISOU 730 CA ASN A 119 5290 6488 7255 -130 761 -784 C ATOM 731 C ASN A 119 57.319 14.096 5.596 1.00 49.36 C ANISOU 731 C ASN A 119 5244 6388 7122 -108 692 -726 C ATOM 732 O ASN A 119 56.803 13.001 5.777 1.00 48.85 O ANISOU 732 O ASN A 119 5193 6315 7051 -76 664 -714 O ATOM 733 CB ASN A 119 59.679 14.737 6.104 1.00 50.38 C ANISOU 733 CB ASN A 119 5243 6542 7355 -113 737 -803 C ATOM 734 CG ASN A 119 59.376 14.184 7.491 1.00 51.10 C ANISOU 734 CG ASN A 119 5313 6632 7470 -51 657 -786 C ATOM 735 OD1 ASN A 119 58.482 14.690 8.196 1.00 52.42 O ANISOU 735 OD1 ASN A 119 5518 6793 7603 -42 609 -745 O ATOM 736 ND2 ASN A 119 60.107 13.136 7.891 1.00 51.03 N ANISOU 736 ND2 ASN A 119 5247 6622 7517 -5 645 -818 N ATOM 737 N LEU A 120 56.694 15.237 5.868 1.00 49.06 N ANISOU 737 N LEU A 120 5232 6350 7057 -125 668 -690 N ATOM 738 CA LEU A 120 55.419 15.201 6.577 1.00 49.08 C ANISOU 738 CA LEU A 120 5258 6350 7037 -93 612 -635 C ATOM 739 C LEU A 120 54.306 14.517 5.767 1.00 49.01 C ANISOU 739 C LEU A 120 5302 6331 6988 -108 601 -597 C ATOM 740 O LEU A 120 53.390 13.909 6.345 1.00 48.74 O ANISOU 740 O LEU A 120 5269 6299 6950 -78 559 -557 O ATOM 741 CB LEU A 120 55.001 16.594 7.079 1.00 49.22 C ANISOU 741 CB LEU A 120 5295 6367 7039 -95 595 -607 C ATOM 742 CG LEU A 120 54.627 17.660 6.062 1.00 49.87 C ANISOU 742 CG LEU A 120 5432 6436 7081 -146 615 -588 C ATOM 743 CD1 LEU A 120 53.179 17.457 5.670 1.00 51.06 C ANISOU 743 CD1 LEU A 120 5622 6578 7200 -141 586 -529 C ATOM 744 CD2 LEU A 120 54.865 19.073 6.621 1.00 49.59 C ANISOU 744 CD2 LEU A 120 5408 6392 7040 -151 609 -587 C ATOM 745 N TYR A 121 54.403 14.577 4.440 1.00 49.21 N ANISOU 745 N TYR A 121 5375 6341 6981 -160 638 -606 N ATOM 746 CA TYR A 121 53.484 13.819 3.579 1.00 49.02 C ANISOU 746 CA TYR A 121 5412 6297 6915 -185 619 -572 C ATOM 747 C TYR A 121 53.868 12.351 3.459 1.00 48.49 C ANISOU 747 C TYR A 121 5347 6220 6854 -168 628 -601 C ATOM 748 O TYR A 121 53.056 11.479 3.762 1.00 48.55 O ANISOU 748 O TYR A 121 5367 6223 6854 -151 580 -566 O ATOM 749 CB TYR A 121 53.362 14.470 2.200 1.00 49.51 C ANISOU 749 CB TYR A 121 5550 6335 6927 -254 645 -566 C ATOM 750 CG TYR A 121 52.672 15.821 2.248 1.00 51.48 C ANISOU 750 CG TYR A 121 5815 6583 7162 -268 617 -523 C ATOM 751 CD1 TYR A 121 51.649 16.072 3.170 1.00 53.67 C ANISOU 751 CD1 TYR A 121 6059 6873 7457 -224 562 -469 C ATOM 752 CD2 TYR A 121 53.020 16.842 1.370 1.00 53.39 C ANISOU 752 CD2 TYR A 121 6109 6806 7371 -324 648 -534 C ATOM 753 CE1 TYR A 121 51.011 17.300 3.224 1.00 54.82 C ANISOU 753 CE1 TYR A 121 6220 7013 7594 -224 540 -431 C ATOM 754 CE2 TYR A 121 52.378 18.085 1.418 1.00 54.73 C ANISOU 754 CE2 TYR A 121 6302 6965 7525 -331 615 -494 C ATOM 755 CZ TYR A 121 51.373 18.302 2.352 1.00 55.17 C ANISOU 755 CZ TYR A 121 6320 7033 7606 -276 562 -443 C ATOM 756 OH TYR A 121 50.706 19.505 2.431 1.00 56.29 O ANISOU 756 OH TYR A 121 6485 7162 7739 -269 533 -404 O ATOM 757 N SER A 122 55.099 12.067 3.046 1.00 48.04 N ANISOU 757 N SER A 122 5277 6158 6815 -169 690 -664 N ATOM 758 CA SER A 122 55.537 10.678 2.952 1.00 47.74 C ANISOU 758 CA SER A 122 5245 6104 6787 -139 703 -697 C ATOM 759 C SER A 122 55.390 9.986 4.297 1.00 46.84 C ANISOU 759 C SER A 122 5079 6003 6714 -77 644 -687 C ATOM 760 O SER A 122 54.803 8.909 4.392 1.00 46.56 O ANISOU 760 O SER A 122 5079 5950 6660 -64 605 -666 O ATOM 761 CB SER A 122 56.988 10.578 2.476 1.00 48.37 C ANISOU 761 CB SER A 122 5294 6182 6900 -134 789 -768 C ATOM 762 OG SER A 122 57.859 11.243 3.359 1.00 48.49 O ANISOU 762 OG SER A 122 5211 6229 6981 -108 794 -792 O ATOM 763 N SER A 123 55.897 10.628 5.345 1.00 46.03 N ANISOU 763 N SER A 123 4902 5926 6660 -46 632 -697 N ATOM 764 CA SER A 123 55.907 10.013 6.669 1.00 45.20 C ANISOU 764 CA SER A 123 4757 5825 6589 9 577 -693 C ATOM 765 C SER A 123 54.527 9.489 7.068 1.00 43.72 C ANISOU 765 C SER A 123 4613 5634 6365 11 520 -632 C ATOM 766 O SER A 123 54.426 8.361 7.520 1.00 43.67 O ANISOU 766 O SER A 123 4617 5615 6362 39 486 -632 O ATOM 767 CB SER A 123 56.499 10.952 7.741 1.00 45.15 C ANISOU 767 CB SER A 123 4689 5839 6626 30 562 -703 C ATOM 768 OG SER A 123 55.757 12.158 7.893 1.00 46.27 O ANISOU 768 OG SER A 123 4849 5991 6738 5 554 -663 O ATOM 769 N VAL A 124 53.465 10.265 6.884 1.00 42.48 N ANISOU 769 N VAL A 124 4477 5486 6175 -18 509 -579 N ATOM 770 CA VAL A 124 52.157 9.771 7.315 1.00 41.78 C ANISOU 770 CA VAL A 124 4409 5400 6065 -17 459 -517 C ATOM 771 C VAL A 124 51.644 8.728 6.333 1.00 41.90 C ANISOU 771 C VAL A 124 4484 5391 6044 -53 445 -499 C ATOM 772 O VAL A 124 51.146 7.678 6.742 1.00 41.98 O ANISOU 772 O VAL A 124 4511 5393 6046 -45 404 -476 O ATOM 773 CB VAL A 124 51.091 10.887 7.545 1.00 41.49 C ANISOU 773 CB VAL A 124 4363 5381 6018 -26 449 -458 C ATOM 774 CG1 VAL A 124 50.815 11.664 6.271 1.00 41.80 C ANISOU 774 CG1 VAL A 124 4437 5413 6032 -76 466 -444 C ATOM 775 CG2 VAL A 124 49.803 10.281 8.090 1.00 40.05 C ANISOU 775 CG2 VAL A 124 4181 5207 5827 -22 407 -393 C ATOM 776 N TRP A 125 51.787 8.990 5.039 1.00 41.73 N ANISOU 776 N TRP A 125 4508 5353 5994 -98 475 -511 N ATOM 777 CA TRP A 125 51.201 8.089 4.059 1.00 41.85 C ANISOU 777 CA TRP A 125 4602 5336 5962 -143 453 -487 C ATOM 778 C TRP A 125 51.844 6.689 4.049 1.00 42.27 C ANISOU 778 C TRP A 125 4688 5359 6011 -119 457 -530 C ATOM 779 O TRP A 125 51.143 5.712 3.801 1.00 42.70 O ANISOU 779 O TRP A 125 4804 5389 6031 -142 411 -497 O ATOM 780 CB TRP A 125 51.103 8.742 2.664 1.00 42.05 C ANISOU 780 CB TRP A 125 4691 5340 5944 -204 478 -483 C ATOM 781 CG TRP A 125 49.831 9.580 2.530 1.00 41.36 C ANISOU 781 CG TRP A 125 4603 5265 5847 -238 428 -407 C ATOM 782 CD1 TRP A 125 49.723 10.932 2.682 1.00 41.15 C ANISOU 782 CD1 TRP A 125 4540 5258 5837 -234 440 -395 C ATOM 783 CD2 TRP A 125 48.495 9.099 2.288 1.00 40.04 C ANISOU 783 CD2 TRP A 125 4464 5088 5659 -275 355 -331 C ATOM 784 NE1 TRP A 125 48.407 11.324 2.535 1.00 41.02 N ANISOU 784 NE1 TRP A 125 4524 5244 5815 -257 383 -317 N ATOM 785 CE2 TRP A 125 47.637 10.219 2.292 1.00 40.26 C ANISOU 785 CE2 TRP A 125 4460 5134 5701 -285 329 -275 C ATOM 786 CE3 TRP A 125 47.945 7.836 2.078 1.00 40.43 C ANISOU 786 CE3 TRP A 125 4563 5115 5683 -303 306 -302 C ATOM 787 CZ2 TRP A 125 46.259 10.115 2.073 1.00 40.74 C ANISOU 787 CZ2 TRP A 125 4520 5195 5761 -319 256 -189 C ATOM 788 CZ3 TRP A 125 46.566 7.733 1.861 1.00 41.43 C ANISOU 788 CZ3 TRP A 125 4696 5242 5803 -348 229 -215 C ATOM 789 CH2 TRP A 125 45.743 8.868 1.862 1.00 40.94 C ANISOU 789 CH2 TRP A 125 4584 5202 5765 -354 206 -159 C ATOM 790 N ILE A 126 53.138 6.584 4.358 1.00 42.47 N ANISOU 790 N ILE A 126 4674 5385 6076 -71 503 -599 N ATOM 791 CA ILE A 126 53.781 5.277 4.552 1.00 42.95 C ANISOU 791 CA ILE A 126 4753 5417 6147 -28 501 -640 C ATOM 792 C ILE A 126 53.070 4.495 5.672 1.00 42.93 C ANISOU 792 C ILE A 126 4746 5416 6147 -6 425 -599 C ATOM 793 O ILE A 126 52.800 3.298 5.524 1.00 43.00 O ANISOU 793 O ILE A 126 4820 5389 6126 -8 393 -593 O ATOM 794 CB ILE A 126 55.308 5.412 4.855 1.00 43.44 C ANISOU 794 CB ILE A 126 4744 5486 6273 27 557 -714 C ATOM 795 CG1 ILE A 126 56.069 5.915 3.618 1.00 43.93 C ANISOU 795 CG1 ILE A 126 4822 5541 6327 0 647 -758 C ATOM 796 CG2 ILE A 126 55.909 4.083 5.309 1.00 42.83 C ANISOU 796 CG2 ILE A 126 4672 5379 6222 87 538 -750 C ATOM 797 CD1 ILE A 126 57.127 7.004 3.941 1.00 43.64 C ANISOU 797 CD1 ILE A 126 4686 5541 6354 14 696 -796 C ATOM 798 N LEU A 127 52.744 5.173 6.771 1.00 42.77 N ANISOU 798 N LEU A 127 4662 5432 6156 11 400 -571 N ATOM 799 CA LEU A 127 51.929 4.561 7.826 1.00 43.03 C ANISOU 799 CA LEU A 127 4697 5468 6182 20 339 -525 C ATOM 800 C LEU A 127 50.624 3.976 7.250 1.00 43.47 C ANISOU 800 C LEU A 127 4815 5513 6188 -38 299 -459 C ATOM 801 O LEU A 127 50.298 2.820 7.525 1.00 43.83 O ANISOU 801 O LEU A 127 4906 5534 6212 -41 254 -443 O ATOM 802 CB LEU A 127 51.604 5.552 8.963 1.00 42.61 C ANISOU 802 CB LEU A 127 4582 5452 6153 39 332 -498 C ATOM 803 CG LEU A 127 52.741 6.252 9.730 1.00 42.96 C ANISOU 803 CG LEU A 127 4569 5507 6244 86 352 -548 C ATOM 804 CD1 LEU A 127 52.202 7.015 10.951 1.00 42.09 C ANISOU 804 CD1 LEU A 127 4434 5420 6138 101 336 -513 C ATOM 805 CD2 LEU A 127 53.851 5.271 10.170 1.00 43.06 C ANISOU 805 CD2 LEU A 127 4578 5492 6288 134 332 -603 C ATOM 806 N ALA A 128 49.887 4.756 6.449 1.00 43.59 N ANISOU 806 N ALA A 128 4835 5542 6184 -87 305 -418 N ATOM 807 CA ALA A 128 48.660 4.247 5.793 1.00 43.91 C ANISOU 807 CA ALA A 128 4930 5569 6184 -152 255 -350 C ATOM 808 C ALA A 128 48.915 2.933 5.051 1.00 44.40 C ANISOU 808 C ALA A 128 5092 5576 6202 -175 236 -372 C ATOM 809 O ALA A 128 48.139 1.981 5.157 1.00 44.49 O ANISOU 809 O ALA A 128 5148 5570 6185 -209 177 -325 O ATOM 810 CB ALA A 128 48.072 5.283 4.833 1.00 43.73 C ANISOU 810 CB ALA A 128 4909 5555 6149 -201 261 -314 C ATOM 811 N PHE A 129 50.014 2.876 4.313 1.00 44.82 N ANISOU 811 N PHE A 129 5182 5599 6246 -157 290 -442 N ATOM 812 CA PHE A 129 50.358 1.661 3.576 1.00 45.63 C ANISOU 812 CA PHE A 129 5392 5641 6303 -166 286 -472 C ATOM 813 C PHE A 129 50.598 0.474 4.516 1.00 45.67 C ANISOU 813 C PHE A 129 5406 5626 6318 -120 249 -487 C ATOM 814 O PHE A 129 50.142 -0.653 4.250 1.00 45.50 O ANISOU 814 O PHE A 129 5479 5559 6249 -150 200 -465 O ATOM 815 CB PHE A 129 51.557 1.919 2.666 1.00 45.96 C ANISOU 815 CB PHE A 129 5461 5659 6342 -146 372 -549 C ATOM 816 CG PHE A 129 51.173 2.512 1.356 1.00 46.93 C ANISOU 816 CG PHE A 129 5653 5764 6414 -217 391 -530 C ATOM 817 CD1 PHE A 129 50.491 3.724 1.303 1.00 46.94 C ANISOU 817 CD1 PHE A 129 5604 5805 6424 -255 376 -482 C ATOM 818 CD2 PHE A 129 51.450 1.851 0.172 1.00 48.89 C ANISOU 818 CD2 PHE A 129 6029 5948 6597 -247 418 -559 C ATOM 819 CE1 PHE A 129 50.109 4.275 0.093 1.00 46.89 C ANISOU 819 CE1 PHE A 129 5671 5775 6368 -324 379 -460 C ATOM 820 CE2 PHE A 129 51.068 2.404 -1.046 1.00 49.27 C ANISOU 820 CE2 PHE A 129 6161 5971 6588 -322 427 -539 C ATOM 821 CZ PHE A 129 50.396 3.619 -1.077 1.00 48.00 C ANISOU 821 CZ PHE A 129 5945 5850 6440 -361 402 -488 C ATOM 822 N ILE A 130 51.289 0.740 5.623 1.00 45.43 N ANISOU 822 N ILE A 130 5289 5625 6347 -52 265 -520 N ATOM 823 CA ILE A 130 51.441 -0.255 6.683 1.00 45.76 C ANISOU 823 CA ILE A 130 5338 5649 6400 -10 218 -525 C ATOM 824 C ILE A 130 50.055 -0.750 7.123 1.00 46.06 C ANISOU 824 C ILE A 130 5406 5692 6401 -68 145 -442 C ATOM 825 O ILE A 130 49.817 -1.952 7.200 1.00 46.24 O ANISOU 825 O ILE A 130 5509 5672 6388 -80 96 -430 O ATOM 826 CB ILE A 130 52.195 0.303 7.894 1.00 45.18 C ANISOU 826 CB ILE A 130 5167 5608 6390 55 229 -557 C ATOM 827 CG1 ILE A 130 53.643 0.623 7.538 1.00 45.47 C ANISOU 827 CG1 ILE A 130 5160 5638 6475 111 292 -637 C ATOM 828 CG2 ILE A 130 52.197 -0.694 8.988 1.00 45.96 C ANISOU 828 CG2 ILE A 130 5289 5683 6491 87 168 -552 C ATOM 829 CD1 ILE A 130 54.371 1.409 8.600 1.00 44.27 C ANISOU 829 CD1 ILE A 130 4909 5521 6389 159 297 -660 C ATOM 830 N SER A 131 49.138 0.184 7.368 1.00 46.21 N ANISOU 830 N SER A 131 5364 5762 6431 -103 142 -382 N ATOM 831 CA SER A 131 47.770 -0.157 7.748 1.00 46.60 C ANISOU 831 CA SER A 131 5419 5827 6459 -161 85 -296 C ATOM 832 C SER A 131 47.033 -0.965 6.671 1.00 47.53 C ANISOU 832 C SER A 131 5632 5905 6521 -239 36 -254 C ATOM 833 O SER A 131 46.267 -1.865 6.991 1.00 47.52 O ANISOU 833 O SER A 131 5672 5890 6493 -282 -23 -202 O ATOM 834 CB SER A 131 46.976 1.110 8.086 1.00 46.42 C ANISOU 834 CB SER A 131 5302 5865 6467 -173 105 -244 C ATOM 835 OG SER A 131 47.612 1.859 9.108 1.00 45.76 O ANISOU 835 OG SER A 131 5150 5809 6425 -107 145 -280 O ATOM 836 N LEU A 132 47.253 -0.641 5.401 1.00 48.40 N ANISOU 836 N LEU A 132 5787 5992 6607 -265 58 -273 N ATOM 837 CA LEU A 132 46.676 -1.441 4.313 1.00 49.53 C ANISOU 837 CA LEU A 132 6048 6084 6687 -342 6 -239 C ATOM 838 C LEU A 132 47.327 -2.813 4.267 1.00 50.47 C ANISOU 838 C LEU A 132 6276 6134 6764 -319 -8 -287 C ATOM 839 O LEU A 132 46.655 -3.822 4.039 1.00 50.65 O ANISOU 839 O LEU A 132 6393 6114 6735 -379 -78 -243 O ATOM 840 CB LEU A 132 46.853 -0.751 2.961 1.00 49.77 C ANISOU 840 CB LEU A 132 6122 6095 6692 -374 37 -254 C ATOM 841 CG LEU A 132 45.869 0.382 2.694 1.00 49.52 C ANISOU 841 CG LEU A 132 6022 6109 6681 -424 17 -184 C ATOM 842 CD1 LEU A 132 46.409 1.302 1.623 1.00 49.66 C ANISOU 842 CD1 LEU A 132 6067 6114 6684 -430 70 -222 C ATOM 843 CD2 LEU A 132 44.509 -0.180 2.304 1.00 50.18 C ANISOU 843 CD2 LEU A 132 6152 6179 6735 -519 -80 -87 C ATOM 844 N ASP A 133 48.640 -2.843 4.485 1.00 51.11 N ANISOU 844 N ASP A 133 6345 6201 6871 -232 53 -375 N ATOM 845 CA ASP A 133 49.364 -4.104 4.510 1.00 52.31 C ANISOU 845 CA ASP A 133 6591 6285 6996 -190 45 -427 C ATOM 846 C ASP A 133 48.743 -5.083 5.509 1.00 52.74 C ANISOU 846 C ASP A 133 6671 6329 7037 -205 -35 -382 C ATOM 847 O ASP A 133 48.549 -6.260 5.182 1.00 53.11 O ANISOU 847 O ASP A 133 6844 6310 7025 -234 -86 -374 O ATOM 848 CB ASP A 133 50.833 -3.888 4.847 1.00 52.43 C ANISOU 848 CB ASP A 133 6548 6303 7070 -85 118 -519 C ATOM 849 CG ASP A 133 51.627 -5.170 4.783 1.00 53.76 C ANISOU 849 CG ASP A 133 6811 6396 7219 -28 113 -576 C ATOM 850 OD1 ASP A 133 52.180 -5.597 5.820 1.00 54.62 O ANISOU 850 OD1 ASP A 133 6881 6502 7370 39 92 -602 O ATOM 851 OD2 ASP A 133 51.674 -5.768 3.691 1.00 55.65 O ANISOU 851 OD2 ASP A 133 7173 6572 7397 -52 126 -592 O ATOM 852 N ARG A 134 48.432 -4.580 6.710 1.00 52.65 N ANISOU 852 N ARG A 134 6553 6378 7074 -189 -44 -352 N ATOM 853 CA ARG A 134 47.767 -5.368 7.761 1.00 53.06 C ANISOU 853 CA ARG A 134 6622 6427 7111 -212 -111 -302 C ATOM 854 C ARG A 134 46.368 -5.789 7.360 1.00 53.19 C ANISOU 854 C ARG A 134 6687 6441 7079 -323 -177 -209 C ATOM 855 O ARG A 134 45.951 -6.915 7.609 1.00 53.67 O ANISOU 855 O ARG A 134 6834 6460 7095 -364 -242 -179 O ATOM 856 CB ARG A 134 47.658 -4.578 9.064 1.00 52.82 C ANISOU 856 CB ARG A 134 6473 6461 7134 -179 -93 -287 C ATOM 857 CG ARG A 134 48.976 -4.191 9.728 1.00 54.07 C ANISOU 857 CG ARG A 134 6577 6622 7344 -79 -51 -366 C ATOM 858 CD ARG A 134 49.747 -5.393 10.205 1.00 56.34 C ANISOU 858 CD ARG A 134 6941 6844 7620 -27 -91 -412 C ATOM 859 NE ARG A 134 50.362 -6.112 9.096 1.00 58.40 N ANISOU 859 NE ARG A 134 7291 7043 7856 -10 -83 -461 N ATOM 860 CZ ARG A 134 51.213 -7.122 9.240 1.00 60.49 C ANISOU 860 CZ ARG A 134 7623 7240 8117 52 -105 -514 C ATOM 861 NH1 ARG A 134 51.589 -7.536 10.453 1.00 61.18 N ANISOU 861 NH1 ARG A 134 7702 7314 8228 100 -149 -526 N ATOM 862 NH2 ARG A 134 51.705 -7.701 8.152 1.00 61.30 N ANISOU 862 NH2 ARG A 134 7811 7285 8193 68 -82 -558 N ATOM 863 N TYR A 135 45.634 -4.872 6.756 1.00 52.93 N ANISOU 863 N TYR A 135 6597 6453 7060 -375 -166 -160 N ATOM 864 CA TYR A 135 44.302 -5.189 6.286 1.00 53.35 C ANISOU 864 CA TYR A 135 6682 6507 7081 -485 -236 -65 C ATOM 865 C TYR A 135 44.363 -6.405 5.348 1.00 53.49 C ANISOU 865 C TYR A 135 6868 6435 7020 -535 -293 -72 C ATOM 866 O TYR A 135 43.574 -7.338 5.477 1.00 53.54 O ANISOU 866 O TYR A 135 6940 6415 6985 -610 -371 -11 O ATOM 867 CB TYR A 135 43.675 -3.964 5.610 1.00 53.36 C ANISOU 867 CB TYR A 135 6603 6558 7113 -521 -219 -21 C ATOM 868 CG TYR A 135 42.708 -4.315 4.519 1.00 55.27 C ANISOU 868 CG TYR A 135 6918 6770 7311 -630 -296 50 C ATOM 869 CD1 TYR A 135 41.475 -4.878 4.813 1.00 56.84 C ANISOU 869 CD1 TYR A 135 7107 6982 7506 -718 -375 147 C ATOM 870 CD2 TYR A 135 43.026 -4.096 3.194 1.00 57.21 C ANISOU 870 CD2 TYR A 135 7249 6970 7518 -653 -293 23 C ATOM 871 CE1 TYR A 135 40.580 -5.210 3.812 1.00 57.88 C ANISOU 871 CE1 TYR A 135 7306 7082 7601 -827 -461 221 C ATOM 872 CE2 TYR A 135 42.139 -4.425 2.185 1.00 58.92 C ANISOU 872 CE2 TYR A 135 7549 7149 7687 -760 -377 93 C ATOM 873 CZ TYR A 135 40.918 -4.981 2.502 1.00 58.85 C ANISOU 873 CZ TYR A 135 7524 7155 7682 -848 -468 193 C ATOM 874 OH TYR A 135 40.039 -5.308 1.497 1.00 60.64 O ANISOU 874 OH TYR A 135 7832 7341 7866 -963 -566 267 O ATOM 875 N LEU A 136 45.330 -6.398 4.439 1.00 53.20 N ANISOU 875 N LEU A 136 6906 6348 6957 -493 -249 -148 N ATOM 876 CA LEU A 136 45.490 -7.492 3.485 1.00 53.76 C ANISOU 876 CA LEU A 136 7156 6324 6946 -529 -288 -166 C ATOM 877 C LEU A 136 45.959 -8.781 4.164 1.00 53.90 C ANISOU 877 C LEU A 136 7259 6283 6934 -489 -319 -199 C ATOM 878 O LEU A 136 45.427 -9.859 3.902 1.00 53.96 O ANISOU 878 O LEU A 136 7399 6227 6873 -557 -397 -161 O ATOM 879 CB LEU A 136 46.463 -7.098 2.355 1.00 53.83 C ANISOU 879 CB LEU A 136 7222 6294 6935 -487 -211 -244 C ATOM 880 CG LEU A 136 45.912 -6.162 1.267 1.00 53.34 C ANISOU 880 CG LEU A 136 7159 6248 6859 -558 -208 -206 C ATOM 881 CD1 LEU A 136 47.026 -5.596 0.410 1.00 52.21 C ANISOU 881 CD1 LEU A 136 7044 6081 6710 -503 -107 -293 C ATOM 882 CD2 LEU A 136 44.897 -6.885 0.402 1.00 53.52 C ANISOU 882 CD2 LEU A 136 7323 6209 6800 -680 -310 -133 C ATOM 883 N ALA A 137 46.951 -8.664 5.035 1.00 53.63 N ANISOU 883 N ALA A 137 7157 6265 6953 -380 -265 -267 N ATOM 884 CA ALA A 137 47.518 -9.836 5.685 1.00 54.26 C ANISOU 884 CA ALA A 137 7319 6284 7013 -327 -296 -306 C ATOM 885 C ALA A 137 46.475 -10.540 6.563 1.00 54.72 C ANISOU 885 C ALA A 137 7398 6346 7045 -403 -387 -224 C ATOM 886 O ALA A 137 46.455 -11.766 6.657 1.00 55.20 O ANISOU 886 O ALA A 137 7592 6332 7048 -419 -450 -223 O ATOM 887 CB ALA A 137 48.734 -9.447 6.501 1.00 53.64 C ANISOU 887 CB ALA A 137 7143 6228 7008 -202 -234 -384 C ATOM 888 N ILE A 138 45.594 -9.759 7.180 1.00 54.74 N ANISOU 888 N ILE A 138 7275 6435 7089 -450 -389 -155 N ATOM 889 CA ILE A 138 44.633 -10.286 8.143 1.00 55.01 C ANISOU 889 CA ILE A 138 7302 6487 7110 -517 -452 -77 C ATOM 890 C ILE A 138 43.266 -10.561 7.543 1.00 56.12 C ANISOU 890 C ILE A 138 7477 6632 7211 -655 -522 24 C ATOM 891 O ILE A 138 42.781 -11.681 7.658 1.00 57.11 O ANISOU 891 O ILE A 138 7712 6706 7278 -724 -600 65 O ATOM 892 CB ILE A 138 44.478 -9.353 9.344 1.00 54.20 C ANISOU 892 CB ILE A 138 7044 6472 7076 -482 -405 -61 C ATOM 893 CG1 ILE A 138 45.788 -9.345 10.136 1.00 53.49 C ANISOU 893 CG1 ILE A 138 6943 6364 7017 -361 -368 -152 C ATOM 894 CG2 ILE A 138 43.310 -9.806 10.208 1.00 54.00 C ANISOU 894 CG2 ILE A 138 7009 6474 7035 -568 -455 29 C ATOM 895 CD1 ILE A 138 45.741 -8.561 11.390 1.00 52.36 C ANISOU 895 CD1 ILE A 138 6683 6286 6924 -326 -332 -142 C ATOM 896 N VAL A 139 42.634 -9.573 6.913 1.00 56.49 N ANISOU 896 N VAL A 139 7436 6737 7292 -699 -504 69 N ATOM 897 CA VAL A 139 41.293 -9.811 6.363 1.00 57.47 C ANISOU 897 CA VAL A 139 7576 6866 7391 -833 -584 176 C ATOM 898 C VAL A 139 41.348 -10.802 5.207 1.00 59.05 C ANISOU 898 C VAL A 139 7967 6965 7501 -895 -656 172 C ATOM 899 O VAL A 139 40.467 -11.647 5.091 1.00 59.82 O ANISOU 899 O VAL A 139 8143 7032 7553 -1005 -749 248 O ATOM 900 CB VAL A 139 40.570 -8.522 5.913 1.00 57.12 C ANISOU 900 CB VAL A 139 7394 6899 7408 -864 -562 231 C ATOM 901 CG1 VAL A 139 39.175 -8.841 5.384 1.00 56.84 C ANISOU 901 CG1 VAL A 139 7367 6868 7359 -1006 -660 349 C ATOM 902 CG2 VAL A 139 40.478 -7.536 7.055 1.00 55.99 C ANISOU 902 CG2 VAL A 139 7078 6849 7347 -801 -487 236 C ATOM 903 N HIS A 140 42.385 -10.718 4.376 1.00 60.22 N ANISOU 903 N HIS A 140 8198 7058 7622 -827 -609 83 N ATOM 904 CA HIS A 140 42.506 -11.583 3.193 1.00 61.99 C ANISOU 904 CA HIS A 140 8623 7177 7753 -877 -661 69 C ATOM 905 C HIS A 140 43.712 -12.526 3.254 1.00 63.96 C ANISOU 905 C HIS A 140 9009 7336 7955 -783 -633 -29 C ATOM 906 O HIS A 140 44.393 -12.775 2.262 1.00 63.96 O ANISOU 906 O HIS A 140 9138 7260 7903 -753 -604 -91 O ATOM 907 CB HIS A 140 42.548 -10.721 1.947 1.00 61.68 C ANISOU 907 CB HIS A 140 8590 7135 7707 -895 -632 61 C ATOM 908 CG HIS A 140 41.318 -9.894 1.755 1.00 60.00 C ANISOU 908 CG HIS A 140 8263 6994 7537 -990 -680 165 C ATOM 909 ND1 HIS A 140 40.080 -10.451 1.525 1.00 59.23 N ANISOU 909 ND1 HIS A 140 8209 6884 7411 -1127 -798 273 N ATOM 910 CD2 HIS A 140 41.136 -8.554 1.753 1.00 57.97 C ANISOU 910 CD2 HIS A 140 7849 6820 7356 -967 -629 179 C ATOM 911 CE1 HIS A 140 39.188 -9.486 1.390 1.00 58.93 C ANISOU 911 CE1 HIS A 140 8032 6920 7436 -1178 -818 350 C ATOM 912 NE2 HIS A 140 39.802 -8.326 1.529 1.00 57.48 N ANISOU 912 NE2 HIS A 140 7731 6792 7313 -1080 -715 294 N ATOM 913 N ALA A 141 43.926 -13.090 4.437 1.00 66.28 N ANISOU 913 N ALA A 141 9282 7634 8267 -738 -643 -40 N ATOM 914 CA ALA A 141 45.110 -13.895 4.729 1.00 68.35 C ANISOU 914 CA ALA A 141 9640 7821 8509 -629 -618 -134 C ATOM 915 C ALA A 141 45.308 -15.086 3.776 1.00 71.07 C ANISOU 915 C ALA A 141 10218 8036 8749 -654 -666 -158 C ATOM 916 O ALA A 141 46.443 -15.425 3.446 1.00 71.68 O ANISOU 916 O ALA A 141 10372 8046 8813 -548 -609 -253 O ATOM 917 CB ALA A 141 45.053 -14.380 6.178 1.00 68.02 C ANISOU 917 CB ALA A 141 9556 7796 8489 -606 -652 -119 C ATOM 918 N THR A 142 44.206 -15.701 3.341 1.00 73.69 N ANISOU 918 N THR A 142 10659 8330 9007 -794 -769 -71 N ATOM 919 CA THR A 142 44.237 -16.938 2.540 1.00 76.17 C ANISOU 919 CA THR A 142 11222 8512 9207 -838 -835 -80 C ATOM 920 C THR A 142 45.077 -16.819 1.257 1.00 77.67 C ANISOU 920 C THR A 142 11527 8630 9354 -780 -762 -162 C ATOM 921 O THR A 142 45.920 -17.685 0.988 1.00 78.70 O ANISOU 921 O THR A 142 11815 8656 9429 -703 -741 -238 O ATOM 922 CB THR A 142 42.810 -17.398 2.164 1.00 76.93 C ANISOU 922 CB THR A 142 11399 8592 9239 -1021 -965 40 C ATOM 923 OG1 THR A 142 42.133 -16.345 1.462 1.00 76.90 O ANISOU 923 OG1 THR A 142 11296 8655 9267 -1094 -961 96 O ATOM 924 CG2 THR A 142 42.020 -17.776 3.420 1.00 77.09 C ANISOU 924 CG2 THR A 142 11341 8664 9285 -1083 -1033 118 C ATOM 925 N ASN A 143 44.831 -15.776 0.460 1.00 78.44 N ANISOU 925 N ASN A 143 11556 8776 9470 -817 -723 -145 N ATOM 926 CA ASN A 143 45.796 -15.366 -0.570 1.00 79.44 C ANISOU 926 CA ASN A 143 11741 8861 9579 -741 -616 -235 C ATOM 927 C ASN A 143 45.754 -13.881 -0.921 1.00 79.20 C ANISOU 927 C ASN A 143 11547 8927 9618 -742 -545 -229 C ATOM 928 O ASN A 143 44.968 -13.427 -1.758 1.00 79.26 O ANISOU 928 O ASN A 143 11585 8937 9591 -850 -589 -167 O ATOM 929 CB ASN A 143 45.741 -16.253 -1.818 1.00 80.67 C ANISOU 929 CB ASN A 143 12168 8878 9602 -801 -655 -244 C ATOM 930 CG ASN A 143 46.969 -17.158 -1.930 1.00 82.25 C ANISOU 930 CG ASN A 143 12513 8975 9763 -671 -585 -354 C ATOM 931 OD1 ASN A 143 46.853 -18.377 -2.085 1.00 83.81 O ANISOU 931 OD1 ASN A 143 12915 9060 9867 -697 -656 -351 O ATOM 932 ND2 ASN A 143 48.159 -16.556 -1.816 1.00 82.79 N ANISOU 932 ND2 ASN A 143 12467 9080 9909 -527 -447 -450 N ATOM 933 N SER A 144 46.606 -13.151 -0.208 1.00 79.04 N ANISOU 933 N SER A 144 11353 8982 9696 -622 -445 -291 N ATOM 934 CA SER A 144 46.921 -11.763 -0.478 1.00 78.86 C ANISOU 934 CA SER A 144 11182 9038 9740 -589 -354 -314 C ATOM 935 C SER A 144 48.436 -11.567 -0.417 1.00 79.14 C ANISOU 935 C SER A 144 11178 9068 9823 -441 -223 -432 C ATOM 936 O SER A 144 48.925 -10.452 -0.285 1.00 78.55 O ANISOU 936 O SER A 144 10951 9070 9825 -389 -139 -463 O ATOM 937 CB SER A 144 46.250 -10.893 0.570 1.00 78.06 C ANISOU 937 CB SER A 144 10868 9059 9732 -608 -377 -249 C ATOM 938 OG SER A 144 46.602 -11.340 1.873 1.00 78.45 O ANISOU 938 OG SER A 144 10847 9129 9828 -535 -381 -269 O ATOM 939 N GLN A 145 49.180 -12.658 -0.531 1.00 80.43 N ANISOU 939 N GLN A 145 11478 9137 9943 -372 -206 -496 N ATOM 940 CA GLN A 145 50.634 -12.600 -0.514 1.00 81.04 C ANISOU 940 CA GLN A 145 11517 9200 10072 -227 -84 -606 C ATOM 941 C GLN A 145 51.138 -11.794 -1.717 1.00 81.33 C ANISOU 941 C GLN A 145 11572 9233 10093 -224 29 -652 C ATOM 942 O GLN A 145 52.134 -11.081 -1.619 1.00 81.16 O ANISOU 942 O GLN A 145 11424 9259 10151 -132 140 -719 O ATOM 943 CB GLN A 145 51.205 -14.027 -0.534 1.00 82.28 C ANISOU 943 CB GLN A 145 11845 9242 10177 -159 -97 -659 C ATOM 944 CG GLN A 145 52.428 -14.243 0.355 1.00 83.03 C ANISOU 944 CG GLN A 145 11835 9344 10365 -2 -40 -739 C ATOM 945 CD GLN A 145 52.546 -15.688 0.846 1.00 84.88 C ANISOU 945 CD GLN A 145 12208 9481 10558 40 -116 -751 C ATOM 946 OE1 GLN A 145 52.226 -16.640 0.120 1.00 86.24 O ANISOU 946 OE1 GLN A 145 12600 9547 10621 -3 -155 -745 O ATOM 947 NE2 GLN A 145 53.006 -15.853 2.087 1.00 84.72 N ANISOU 947 NE2 GLN A 145 12076 9492 10621 123 -144 -767 N ATOM 948 N ARG A 146 50.435 -11.919 -2.844 1.00 81.97 N ANISOU 948 N ARG A 146 11818 9255 10070 -333 -5 -613 N ATOM 949 CA ARG A 146 50.739 -11.175 -4.074 1.00 82.39 C ANISOU 949 CA ARG A 146 11925 9293 10085 -357 87 -644 C ATOM 950 C ARG A 146 50.537 -9.663 -3.936 1.00 80.84 C ANISOU 950 C ARG A 146 11536 9212 9966 -383 118 -615 C ATOM 951 O ARG A 146 51.508 -8.908 -3.985 1.00 80.56 O ANISOU 951 O ARG A 146 11396 9219 9993 -305 240 -682 O ATOM 952 CB ARG A 146 49.882 -11.678 -5.243 1.00 83.51 C ANISOU 952 CB ARG A 146 12305 9337 10088 -486 13 -594 C ATOM 953 CG ARG A 146 50.413 -12.880 -5.980 1.00 86.73 C ANISOU 953 CG ARG A 146 12957 9604 10390 -453 46 -655 C ATOM 954 CD ARG A 146 49.591 -13.120 -7.254 1.00 90.31 C ANISOU 954 CD ARG A 146 13649 9962 10700 -594 -22 -604 C ATOM 955 NE ARG A 146 48.144 -13.020 -7.010 1.00 92.04 N ANISOU 955 NE ARG A 146 13844 10218 10909 -738 -192 -479 N ATOM 956 CZ ARG A 146 47.360 -14.007 -6.560 1.00 93.70 C ANISOU 956 CZ ARG A 146 14132 10390 11080 -801 -330 -415 C ATOM 957 NH1 ARG A 146 47.845 -15.221 -6.288 1.00 94.53 N ANISOU 957 NH1 ARG A 146 14363 10409 11143 -736 -330 -462 N ATOM 958 NH2 ARG A 146 46.063 -13.775 -6.384 1.00 93.81 N ANISOU 958 NH2 ARG A 146 14093 10449 11099 -934 -470 -298 N ATOM 959 N PRO A 147 49.277 -9.211 -3.783 1.00 79.71 N ANISOU 959 N PRO A 147 11347 9118 9821 -494 7 -514 N ATOM 960 CA PRO A 147 49.040 -7.775 -3.745 1.00 78.71 C ANISOU 960 CA PRO A 147 11059 9087 9758 -518 33 -486 C ATOM 961 C PRO A 147 49.797 -7.046 -2.630 1.00 77.46 C ANISOU 961 C PRO A 147 10680 9026 9723 -411 106 -528 C ATOM 962 O PRO A 147 50.057 -5.851 -2.756 1.00 76.79 O ANISOU 962 O PRO A 147 10486 9003 9687 -401 170 -540 O ATOM 963 CB PRO A 147 47.520 -7.676 -3.539 1.00 78.49 C ANISOU 963 CB PRO A 147 11010 9091 9721 -638 -109 -365 C ATOM 964 CG PRO A 147 47.129 -8.966 -2.964 1.00 78.81 C ANISOU 964 CG PRO A 147 11125 9087 9731 -652 -198 -337 C ATOM 965 CD PRO A 147 48.016 -9.951 -3.626 1.00 79.94 C ANISOU 965 CD PRO A 147 11458 9118 9795 -602 -143 -418 C ATOM 966 N ARG A 148 50.143 -7.759 -1.558 1.00 76.88 N ANISOU 966 N ARG A 148 10556 8958 9695 -336 88 -549 N ATOM 967 CA ARG A 148 50.967 -7.194 -0.492 1.00 75.91 C ANISOU 967 CA ARG A 148 10247 8911 9682 -232 147 -594 C ATOM 968 C ARG A 148 52.387 -6.927 -0.978 1.00 76.19 C ANISOU 968 C ARG A 148 10266 8931 9748 -139 284 -696 C ATOM 969 O ARG A 148 52.999 -5.925 -0.603 1.00 75.53 O ANISOU 969 O ARG A 148 10029 8920 9748 -91 350 -725 O ATOM 970 CB ARG A 148 50.965 -8.103 0.746 1.00 75.64 C ANISOU 970 CB ARG A 148 10186 8872 9678 -183 81 -588 C ATOM 971 CG ARG A 148 49.677 -7.995 1.558 1.00 74.58 C ANISOU 971 CG ARG A 148 9993 8792 9551 -262 -24 -489 C ATOM 972 CD ARG A 148 49.664 -8.885 2.794 1.00 74.27 C ANISOU 972 CD ARG A 148 9942 8745 9531 -224 -87 -481 C ATOM 973 NE ARG A 148 50.602 -8.420 3.818 1.00 73.27 N ANISOU 973 NE ARG A 148 9673 8668 9497 -117 -37 -534 N ATOM 974 CZ ARG A 148 51.656 -9.100 4.265 1.00 73.00 C ANISOU 974 CZ ARG A 148 9653 8591 9492 -16 -18 -603 C ATOM 975 NH1 ARG A 148 51.939 -10.318 3.811 1.00 74.04 N ANISOU 975 NH1 ARG A 148 9939 8626 9565 5 -37 -634 N ATOM 976 NH2 ARG A 148 52.435 -8.558 5.189 1.00 72.42 N ANISOU 976 NH2 ARG A 148 9440 8567 9507 66 12 -641 N ATOM 977 N LYS A 149 52.897 -7.817 -1.823 1.00 77.29 N ANISOU 977 N LYS A 149 10568 8975 9821 -115 328 -748 N ATOM 978 CA LYS A 149 54.224 -7.643 -2.420 1.00 78.11 C ANISOU 978 CA LYS A 149 10668 9059 9951 -29 473 -844 C ATOM 979 C LYS A 149 54.284 -6.415 -3.330 1.00 77.52 C ANISOU 979 C LYS A 149 10570 9018 9864 -85 554 -847 C ATOM 980 O LYS A 149 55.182 -5.587 -3.201 1.00 77.26 O ANISOU 980 O LYS A 149 10403 9042 9910 -28 653 -896 O ATOM 981 CB LYS A 149 54.658 -8.898 -3.204 1.00 79.68 C ANISOU 981 CB LYS A 149 11070 9136 10067 5 510 -896 C ATOM 982 CG LYS A 149 55.346 -9.969 -2.349 1.00 81.20 C ANISOU 982 CG LYS A 149 11249 9293 10309 122 496 -942 C ATOM 983 CD LYS A 149 56.248 -10.903 -3.187 1.00 83.82 C ANISOU 983 CD LYS A 149 11736 9516 10594 202 595 -1025 C ATOM 984 CE LYS A 149 57.471 -11.368 -2.381 1.00 84.54 C ANISOU 984 CE LYS A 149 11714 9608 10797 360 644 -1098 C ATOM 985 NZ LYS A 149 58.339 -10.212 -1.970 1.00 84.17 N ANISOU 985 NZ LYS A 149 11433 9666 10881 417 732 -1131 N ATOM 986 N LEU A 150 53.324 -6.296 -4.241 1.00 77.19 N ANISOU 986 N LEU A 150 10664 8940 9723 -201 504 -791 N ATOM 987 CA LEU A 150 53.307 -5.164 -5.162 1.00 76.91 C ANISOU 987 CA LEU A 150 10634 8923 9662 -263 567 -789 C ATOM 988 C LEU A 150 53.079 -3.840 -4.443 1.00 75.44 C ANISOU 988 C LEU A 150 10245 8851 9567 -272 551 -752 C ATOM 989 O LEU A 150 53.557 -2.803 -4.889 1.00 75.50 O ANISOU 989 O LEU A 150 10201 8892 9594 -278 637 -778 O ATOM 990 CB LEU A 150 52.270 -5.354 -6.285 1.00 77.55 C ANISOU 990 CB LEU A 150 10916 8931 9615 -391 494 -729 C ATOM 991 CG LEU A 150 52.773 -6.064 -7.562 1.00 78.76 C ANISOU 991 CG LEU A 150 11303 8966 9655 -399 574 -787 C ATOM 992 CD1 LEU A 150 52.370 -7.556 -7.597 1.00 78.62 C ANISOU 992 CD1 LEU A 150 11462 8851 9558 -408 491 -773 C ATOM 993 CD2 LEU A 150 52.267 -5.337 -8.809 1.00 78.67 C ANISOU 993 CD2 LEU A 150 11419 8920 9550 -516 575 -755 C ATOM 994 N LEU A 151 52.360 -3.870 -3.329 1.00 74.35 N ANISOU 994 N LEU A 151 10002 8766 9479 -274 447 -692 N ATOM 995 CA LEU A 151 52.137 -2.655 -2.553 1.00 73.04 C ANISOU 995 CA LEU A 151 9653 8699 9396 -273 435 -659 C ATOM 996 C LEU A 151 53.479 -2.189 -1.989 1.00 72.85 C ANISOU 996 C LEU A 151 9490 8721 9466 -170 540 -738 C ATOM 997 O LEU A 151 53.799 -0.997 -2.027 1.00 72.46 O ANISOU 997 O LEU A 151 9343 8727 9459 -173 594 -748 O ATOM 998 CB LEU A 151 51.104 -2.887 -1.435 1.00 72.27 C ANISOU 998 CB LEU A 151 9483 8644 9330 -293 314 -582 C ATOM 999 CG LEU A 151 50.249 -1.688 -1.009 1.00 70.96 C ANISOU 999 CG LEU A 151 9195 8557 9207 -337 271 -512 C ATOM 1000 CD1 LEU A 151 49.354 -1.213 -2.139 1.00 70.15 C ANISOU 1000 CD1 LEU A 151 9183 8432 9039 -443 230 -455 C ATOM 1001 CD2 LEU A 151 49.414 -2.056 0.194 1.00 70.32 C ANISOU 1001 CD2 LEU A 151 9042 8515 9162 -338 179 -450 C ATOM 1002 N ALA A 152 54.271 -3.146 -1.504 1.00 73.09 N ANISOU 1002 N ALA A 152 9518 8723 9527 -81 562 -792 N ATOM 1003 CA ALA A 152 55.556 -2.855 -0.868 1.00 73.05 C ANISOU 1003 CA ALA A 152 9372 8758 9624 20 642 -861 C ATOM 1004 C ALA A 152 56.678 -2.565 -1.873 1.00 73.77 C ANISOU 1004 C ALA A 152 9482 8828 9718 48 787 -937 C ATOM 1005 O ALA A 152 57.479 -1.649 -1.666 1.00 73.54 O ANISOU 1005 O ALA A 152 9318 8857 9765 80 860 -970 O ATOM 1006 CB ALA A 152 55.955 -4.010 0.041 1.00 73.28 C ANISOU 1006 CB ALA A 152 9391 8760 9692 106 599 -885 C ATOM 1007 N GLU A 153 56.734 -3.349 -2.949 1.00 74.61 N ANISOU 1007 N GLU A 153 9761 8848 9736 34 832 -964 N ATOM 1008 CA GLU A 153 57.819 -3.248 -3.938 1.00 75.62 C ANISOU 1008 CA GLU A 153 9928 8945 9857 67 987 -1042 C ATOM 1009 C GLU A 153 57.569 -2.207 -5.045 1.00 75.24 C ANISOU 1009 C GLU A 153 9942 8901 9744 -30 1046 -1028 C ATOM 1010 O GLU A 153 58.516 -1.601 -5.540 1.00 75.60 O ANISOU 1010 O GLU A 153 9941 8964 9819 -11 1179 -1083 O ATOM 1011 CB GLU A 153 58.131 -4.626 -4.563 1.00 77.02 C ANISOU 1011 CB GLU A 153 10278 9017 9969 113 1026 -1088 C ATOM 1012 CG GLU A 153 59.453 -5.283 -4.082 1.00 78.76 C ANISOU 1012 CG GLU A 153 10410 9227 10286 256 1108 -1168 C ATOM 1013 CD GLU A 153 59.263 -6.444 -3.101 1.00 79.96 C ANISOU 1013 CD GLU A 153 10570 9347 10461 322 996 -1157 C ATOM 1014 OE1 GLU A 153 59.685 -6.296 -1.930 1.00 79.83 O ANISOU 1014 OE1 GLU A 153 10384 9390 10558 389 955 -1159 O ATOM 1015 OE2 GLU A 153 58.715 -7.506 -3.503 1.00 81.05 O ANISOU 1015 OE2 GLU A 153 10898 9395 10501 303 947 -1145 O ATOM 1016 N LYS A 154 56.309 -1.998 -5.420 1.00 74.36 N ANISOU 1016 N LYS A 154 9931 8774 9548 -136 946 -953 N ATOM 1017 CA LYS A 154 55.971 -1.111 -6.535 1.00 74.34 C ANISOU 1017 CA LYS A 154 10019 8758 9469 -236 981 -934 C ATOM 1018 C LYS A 154 55.101 0.091 -6.152 1.00 72.71 C ANISOU 1018 C LYS A 154 9715 8623 9287 -304 893 -860 C ATOM 1019 O LYS A 154 55.548 1.231 -6.255 1.00 72.71 O ANISOU 1019 O LYS A 154 9629 8673 9325 -314 959 -875 O ATOM 1020 CB LYS A 154 55.271 -1.906 -7.639 1.00 75.38 C ANISOU 1020 CB LYS A 154 10397 8783 9460 -312 943 -912 C ATOM 1021 CG LYS A 154 56.208 -2.547 -8.678 1.00 77.86 C ANISOU 1021 CG LYS A 154 10865 9010 9708 -280 1088 -995 C ATOM 1022 CD LYS A 154 56.882 -3.835 -8.187 1.00 79.34 C ANISOU 1022 CD LYS A 154 11056 9158 9929 -165 1119 -1051 C ATOM 1023 CE LYS A 154 57.172 -4.790 -9.355 1.00 80.96 C ANISOU 1023 CE LYS A 154 11507 9239 10016 -166 1201 -1100 C ATOM 1024 NZ LYS A 154 57.937 -4.130 -10.447 1.00 81.87 N ANISOU 1024 NZ LYS A 154 11680 9335 10091 -185 1371 -1156 N ATOM 1025 N VAL A 155 53.865 -0.156 -5.729 1.00 71.33 N ANISOU 1025 N VAL A 155 9555 8451 9093 -351 749 -779 N ATOM 1026 CA VAL A 155 52.904 0.931 -5.495 1.00 70.04 C ANISOU 1026 CA VAL A 155 9320 8345 8947 -416 665 -702 C ATOM 1027 C VAL A 155 53.442 2.022 -4.581 1.00 68.98 C ANISOU 1027 C VAL A 155 8987 8302 8918 -363 705 -718 C ATOM 1028 O VAL A 155 53.181 3.200 -4.796 1.00 68.77 O ANISOU 1028 O VAL A 155 8923 8308 8895 -408 705 -692 O ATOM 1029 CB VAL A 155 51.571 0.420 -4.896 1.00 69.59 C ANISOU 1029 CB VAL A 155 9262 8293 8884 -454 512 -613 C ATOM 1030 CG1 VAL A 155 50.658 1.579 -4.524 1.00 67.92 C ANISOU 1030 CG1 VAL A 155 8947 8147 8712 -498 441 -539 C ATOM 1031 CG2 VAL A 155 50.871 -0.504 -5.878 1.00 70.27 C ANISOU 1031 CG2 VAL A 155 9554 8285 8858 -534 448 -580 C ATOM 1032 N VAL A 156 54.200 1.634 -3.567 1.00 68.32 N ANISOU 1032 N VAL A 156 8788 8253 8918 -269 733 -761 N ATOM 1033 CA VAL A 156 54.729 2.599 -2.610 1.00 67.43 C ANISOU 1033 CA VAL A 156 8495 8220 8903 -221 757 -774 C ATOM 1034 C VAL A 156 55.386 3.799 -3.302 1.00 67.25 C ANISOU 1034 C VAL A 156 8451 8217 8882 -250 855 -806 C ATOM 1035 O VAL A 156 55.281 4.922 -2.823 1.00 66.85 O ANISOU 1035 O VAL A 156 8301 8223 8875 -260 841 -784 O ATOM 1036 CB VAL A 156 55.727 1.928 -1.637 1.00 67.55 C ANISOU 1036 CB VAL A 156 8411 8251 9001 -116 786 -830 C ATOM 1037 CG1 VAL A 156 56.999 1.520 -2.364 1.00 68.64 C ANISOU 1037 CG1 VAL A 156 8581 8352 9143 -71 914 -914 C ATOM 1038 CG2 VAL A 156 56.032 2.847 -0.468 1.00 66.69 C ANISOU 1038 CG2 VAL A 156 8131 8219 8986 -78 772 -825 C ATOM 1039 N TYR A 157 56.035 3.561 -4.437 1.00 67.60 N ANISOU 1039 N TYR A 157 8601 8209 8873 -267 955 -858 N ATOM 1040 CA TYR A 157 56.694 4.625 -5.195 1.00 67.48 C ANISOU 1040 CA TYR A 157 8584 8205 8848 -306 1060 -890 C ATOM 1041 C TYR A 157 55.702 5.481 -5.985 1.00 66.80 C ANISOU 1041 C TYR A 157 8598 8102 8682 -411 1007 -829 C ATOM 1042 O TYR A 157 55.831 6.698 -6.046 1.00 66.16 O ANISOU 1042 O TYR A 157 8464 8056 8617 -444 1029 -822 O ATOM 1043 CB TYR A 157 57.725 4.018 -6.137 1.00 68.55 C ANISOU 1043 CB TYR A 157 8806 8287 8951 -286 1199 -967 C ATOM 1044 CG TYR A 157 58.832 3.296 -5.417 1.00 69.43 C ANISOU 1044 CG TYR A 157 8802 8417 9158 -174 1260 -1030 C ATOM 1045 CD1 TYR A 157 58.747 1.932 -5.147 1.00 70.61 C ANISOU 1045 CD1 TYR A 157 9004 8521 9301 -114 1224 -1041 C ATOM 1046 CD2 TYR A 157 59.965 3.977 -4.997 1.00 70.59 C ANISOU 1046 CD2 TYR A 157 8790 8625 9406 -131 1346 -1074 C ATOM 1047 CE1 TYR A 157 59.771 1.262 -4.478 1.00 71.49 C ANISOU 1047 CE1 TYR A 157 9011 8644 9506 -4 1271 -1097 C ATOM 1048 CE2 TYR A 157 60.997 3.319 -4.329 1.00 71.79 C ANISOU 1048 CE2 TYR A 157 8825 8793 9658 -26 1391 -1128 C ATOM 1049 CZ TYR A 157 60.895 1.965 -4.074 1.00 72.30 C ANISOU 1049 CZ TYR A 157 8943 8808 9716 40 1352 -1140 C ATOM 1050 OH TYR A 157 61.918 1.324 -3.411 1.00 73.75 O ANISOU 1050 OH TYR A 157 9014 9003 10005 149 1388 -1190 O ATOM 1051 N VAL A 158 54.716 4.831 -6.591 1.00 66.76 N ANISOU 1051 N VAL A 158 8740 8034 8589 -466 928 -783 N ATOM 1052 CA VAL A 158 53.678 5.520 -7.369 1.00 66.59 C ANISOU 1052 CA VAL A 158 8821 7985 8492 -568 853 -717 C ATOM 1053 C VAL A 158 52.650 6.275 -6.518 1.00 65.26 C ANISOU 1053 C VAL A 158 8541 7876 8378 -576 733 -638 C ATOM 1054 O VAL A 158 51.985 7.181 -7.012 1.00 65.03 O ANISOU 1054 O VAL A 158 8550 7841 8317 -643 685 -589 O ATOM 1055 CB VAL A 158 52.907 4.512 -8.280 1.00 67.38 C ANISOU 1055 CB VAL A 158 9122 7995 8484 -631 789 -685 C ATOM 1056 CG1 VAL A 158 51.513 5.067 -8.694 1.00 66.67 C ANISOU 1056 CG1 VAL A 158 9096 7888 8346 -727 651 -588 C ATOM 1057 CG2 VAL A 158 53.758 4.151 -9.496 1.00 68.07 C ANISOU 1057 CG2 VAL A 158 9373 8005 8483 -654 916 -754 C ATOM 1058 N GLY A 159 52.508 5.893 -5.253 1.00 64.31 N ANISOU 1058 N GLY A 159 8290 7807 8337 -506 687 -626 N ATOM 1059 CA GLY A 159 51.446 6.437 -4.401 1.00 63.42 C ANISOU 1059 CA GLY A 159 8080 7744 8271 -508 580 -549 C ATOM 1060 C GLY A 159 51.888 7.222 -3.180 1.00 62.50 C ANISOU 1060 C GLY A 159 7794 7704 8249 -440 604 -564 C ATOM 1061 O GLY A 159 51.055 7.833 -2.503 1.00 61.91 O ANISOU 1061 O GLY A 159 7644 7667 8209 -437 534 -505 O ATOM 1062 N VAL A 160 53.188 7.213 -2.893 1.00 62.23 N ANISOU 1062 N VAL A 160 7699 7686 8257 -384 700 -640 N ATOM 1063 CA VAL A 160 53.714 7.905 -1.734 1.00 61.36 C ANISOU 1063 CA VAL A 160 7440 7641 8234 -325 716 -657 C ATOM 1064 C VAL A 160 54.799 8.897 -2.147 1.00 61.37 C ANISOU 1064 C VAL A 160 7412 7655 8249 -336 815 -710 C ATOM 1065 O VAL A 160 54.623 10.104 -1.987 1.00 61.53 O ANISOU 1065 O VAL A 160 7392 7703 8281 -359 805 -687 O ATOM 1066 CB VAL A 160 54.258 6.913 -0.712 1.00 61.27 C ANISOU 1066 CB VAL A 160 7356 7643 8280 -245 714 -690 C ATOM 1067 CG1 VAL A 160 54.583 7.622 0.569 1.00 61.20 C ANISOU 1067 CG1 VAL A 160 7210 7692 8350 -194 702 -692 C ATOM 1068 CG2 VAL A 160 53.240 5.799 -0.465 1.00 61.24 C ANISOU 1068 CG2 VAL A 160 7406 7615 8247 -248 624 -641 C ATOM 1069 N TRP A 161 55.905 8.410 -2.698 1.00 61.45 N ANISOU 1069 N TRP A 161 7443 7644 8258 -322 915 -779 N ATOM 1070 CA TRP A 161 57.026 9.297 -3.031 1.00 61.29 C ANISOU 1070 CA TRP A 161 7378 7644 8263 -334 1019 -830 C ATOM 1071 C TRP A 161 56.698 10.278 -4.155 1.00 61.16 C ANISOU 1071 C TRP A 161 7464 7602 8170 -427 1043 -810 C ATOM 1072 O TRP A 161 56.580 11.470 -3.900 1.00 61.06 O ANISOU 1072 O TRP A 161 7407 7619 8173 -452 1023 -787 O ATOM 1073 CB TRP A 161 58.285 8.498 -3.353 1.00 61.99 C ANISOU 1073 CB TRP A 161 7453 7719 8380 -291 1131 -906 C ATOM 1074 CG TRP A 161 58.768 7.733 -2.170 1.00 61.49 C ANISOU 1074 CG TRP A 161 7274 7683 8407 -197 1104 -928 C ATOM 1075 CD1 TRP A 161 58.624 6.403 -1.959 1.00 61.84 C ANISOU 1075 CD1 TRP A 161 7353 7695 8448 -145 1073 -935 C ATOM 1076 CD2 TRP A 161 59.437 8.255 -1.008 1.00 60.55 C ANISOU 1076 CD2 TRP A 161 6997 7620 8387 -149 1090 -940 C ATOM 1077 NE1 TRP A 161 59.178 6.050 -0.750 1.00 61.33 N ANISOU 1077 NE1 TRP A 161 7162 7663 8477 -64 1043 -953 N ATOM 1078 CE2 TRP A 161 59.682 7.169 -0.146 1.00 60.32 C ANISOU 1078 CE2 TRP A 161 6916 7590 8413 -66 1050 -955 C ATOM 1079 CE3 TRP A 161 59.853 9.533 -0.617 1.00 60.36 C ANISOU 1079 CE3 TRP A 161 6885 7642 8407 -172 1100 -937 C ATOM 1080 CZ2 TRP A 161 60.325 7.314 1.082 1.00 59.80 C ANISOU 1080 CZ2 TRP A 161 6713 7564 8444 -8 1017 -967 C ATOM 1081 CZ3 TRP A 161 60.499 9.677 0.605 1.00 60.13 C ANISOU 1081 CZ3 TRP A 161 6720 7654 8472 -116 1069 -950 C ATOM 1082 CH2 TRP A 161 60.729 8.571 1.438 1.00 59.78 C ANISOU 1082 CH2 TRP A 161 6626 7605 8481 -35 1025 -964 C ATOM 1083 N ILE A 162 56.542 9.790 -5.384 1.00 61.18 N ANISOU 1083 N ILE A 162 7617 7543 8085 -479 1078 -817 N ATOM 1084 CA ILE A 162 56.230 10.673 -6.511 1.00 60.94 C ANISOU 1084 CA ILE A 162 7707 7476 7970 -574 1094 -798 C ATOM 1085 C ILE A 162 55.195 11.733 -6.113 1.00 59.79 C ANISOU 1085 C ILE A 162 7535 7352 7828 -602 982 -725 C ATOM 1086 O ILE A 162 55.456 12.922 -6.273 1.00 59.90 O ANISOU 1086 O ILE A 162 7537 7380 7841 -639 1009 -726 O ATOM 1087 CB ILE A 162 55.746 9.906 -7.775 1.00 61.62 C ANISOU 1087 CB ILE A 162 7990 7479 7944 -634 1094 -790 C ATOM 1088 CG1 ILE A 162 56.867 9.061 -8.373 1.00 62.32 C ANISOU 1088 CG1 ILE A 162 8128 7534 8013 -611 1234 -870 C ATOM 1089 CG2 ILE A 162 55.262 10.880 -8.840 1.00 62.04 C ANISOU 1089 CG2 ILE A 162 8174 7489 7907 -737 1079 -756 C ATOM 1090 CD1 ILE A 162 56.521 8.509 -9.734 1.00 62.68 C ANISOU 1090 CD1 ILE A 162 8396 7487 7930 -683 1254 -869 C ATOM 1091 N PRO A 163 54.027 11.318 -5.579 1.00 58.71 N ANISOU 1091 N PRO A 163 7388 7218 7699 -584 861 -662 N ATOM 1092 CA PRO A 163 53.087 12.367 -5.164 1.00 57.90 C ANISOU 1092 CA PRO A 163 7247 7138 7614 -597 770 -595 C ATOM 1093 C PRO A 163 53.637 13.279 -4.063 1.00 57.25 C ANISOU 1093 C PRO A 163 7022 7118 7611 -545 792 -613 C ATOM 1094 O PRO A 163 53.361 14.469 -4.074 1.00 57.34 O ANISOU 1094 O PRO A 163 7031 7135 7619 -571 769 -586 O ATOM 1095 CB PRO A 163 51.851 11.595 -4.691 1.00 57.29 C ANISOU 1095 CB PRO A 163 7160 7060 7545 -578 655 -529 C ATOM 1096 CG PRO A 163 52.270 10.179 -4.599 1.00 57.74 C ANISOU 1096 CG PRO A 163 7233 7102 7601 -545 684 -567 C ATOM 1097 CD PRO A 163 53.418 9.981 -5.511 1.00 58.60 C ANISOU 1097 CD PRO A 163 7419 7177 7668 -565 803 -641 C ATOM 1098 N ALA A 164 54.420 12.753 -3.129 1.00 56.82 N ANISOU 1098 N ALA A 164 6860 7102 7626 -476 830 -656 N ATOM 1099 CA ALA A 164 55.096 13.627 -2.179 1.00 56.34 C ANISOU 1099 CA ALA A 164 6683 7091 7633 -440 853 -677 C ATOM 1100 C ALA A 164 55.996 14.614 -2.946 1.00 57.04 C ANISOU 1100 C ALA A 164 6800 7172 7699 -498 939 -715 C ATOM 1101 O ALA A 164 55.903 15.828 -2.753 1.00 57.04 O ANISOU 1101 O ALA A 164 6786 7184 7702 -520 921 -696 O ATOM 1102 CB ALA A 164 55.900 12.822 -1.183 1.00 56.05 C ANISOU 1102 CB ALA A 164 6540 7086 7671 -364 875 -720 C ATOM 1103 N LEU A 165 56.833 14.098 -3.843 1.00 57.65 N ANISOU 1103 N LEU A 165 6927 7227 7750 -525 1036 -767 N ATOM 1104 CA LEU A 165 57.731 14.945 -4.620 1.00 58.34 C ANISOU 1104 CA LEU A 165 7043 7308 7814 -588 1134 -805 C ATOM 1105 C LEU A 165 56.990 16.027 -5.428 1.00 58.26 C ANISOU 1105 C LEU A 165 7151 7262 7723 -671 1097 -760 C ATOM 1106 O LEU A 165 57.378 17.190 -5.394 1.00 58.42 O ANISOU 1106 O LEU A 165 7153 7294 7747 -707 1117 -763 O ATOM 1107 CB LEU A 165 58.645 14.089 -5.513 1.00 59.44 C ANISOU 1107 CB LEU A 165 7229 7423 7932 -598 1256 -867 C ATOM 1108 CG LEU A 165 59.800 13.414 -4.743 1.00 60.30 C ANISOU 1108 CG LEU A 165 7193 7574 8142 -519 1320 -923 C ATOM 1109 CD1 LEU A 165 60.254 12.067 -5.360 1.00 60.47 C ANISOU 1109 CD1 LEU A 165 7265 7561 8149 -488 1401 -970 C ATOM 1110 CD2 LEU A 165 60.987 14.383 -4.579 1.00 60.66 C ANISOU 1110 CD2 LEU A 165 7139 7662 8247 -543 1401 -959 C ATOM 1111 N LEU A 166 55.918 15.664 -6.123 1.00 58.20 N ANISOU 1111 N LEU A 166 7263 7204 7643 -703 1030 -715 N ATOM 1112 CA LEU A 166 55.148 16.651 -6.897 1.00 58.48 C ANISOU 1112 CA LEU A 166 7414 7198 7606 -779 976 -667 C ATOM 1113 C LEU A 166 54.502 17.753 -6.031 1.00 57.88 C ANISOU 1113 C LEU A 166 7268 7150 7572 -753 887 -617 C ATOM 1114 O LEU A 166 54.331 18.885 -6.482 1.00 58.19 O ANISOU 1114 O LEU A 166 7371 7164 7571 -807 870 -596 O ATOM 1115 CB LEU A 166 54.083 15.957 -7.762 1.00 58.72 C ANISOU 1115 CB LEU A 166 7582 7167 7560 -818 903 -621 C ATOM 1116 CG LEU A 166 54.606 15.050 -8.889 1.00 59.43 C ANISOU 1116 CG LEU A 166 7802 7203 7574 -864 989 -665 C ATOM 1117 CD1 LEU A 166 53.452 14.530 -9.720 1.00 58.84 C ANISOU 1117 CD1 LEU A 166 7879 7059 7417 -917 890 -608 C ATOM 1118 CD2 LEU A 166 55.624 15.770 -9.776 1.00 59.48 C ANISOU 1118 CD2 LEU A 166 7881 7188 7528 -935 1114 -716 C ATOM 1119 N LEU A 167 54.165 17.428 -4.788 1.00 57.24 N ANISOU 1119 N LEU A 167 7066 7114 7566 -670 834 -600 N ATOM 1120 CA LEU A 167 53.602 18.413 -3.860 1.00 56.86 C ANISOU 1120 CA LEU A 167 6953 7091 7560 -632 765 -558 C ATOM 1121 C LEU A 167 54.618 19.458 -3.362 1.00 57.23 C ANISOU 1121 C LEU A 167 6943 7165 7637 -635 821 -597 C ATOM 1122 O LEU A 167 54.233 20.460 -2.768 1.00 57.06 O ANISOU 1122 O LEU A 167 6900 7149 7630 -617 773 -567 O ATOM 1123 CB LEU A 167 52.954 17.710 -2.656 1.00 56.08 C ANISOU 1123 CB LEU A 167 6753 7028 7524 -547 704 -530 C ATOM 1124 CG LEU A 167 51.681 16.921 -2.975 1.00 55.47 C ANISOU 1124 CG LEU A 167 6720 6928 7424 -548 621 -470 C ATOM 1125 CD1 LEU A 167 51.450 15.816 -1.961 1.00 54.79 C ANISOU 1125 CD1 LEU A 167 6547 6877 7392 -479 598 -465 C ATOM 1126 CD2 LEU A 167 50.487 17.841 -3.056 1.00 54.64 C ANISOU 1126 CD2 LEU A 167 6640 6807 7312 -556 534 -397 C ATOM 1127 N THR A 168 55.908 19.234 -3.584 1.00 58.01 N ANISOU 1127 N THR A 168 7014 7278 7748 -657 921 -661 N ATOM 1128 CA THR A 168 56.907 20.218 -3.177 1.00 58.29 C ANISOU 1128 CA THR A 168 6994 7338 7815 -675 969 -693 C ATOM 1129 C THR A 168 57.004 21.367 -4.174 1.00 59.43 C ANISOU 1129 C THR A 168 7249 7444 7887 -768 993 -687 C ATOM 1130 O THR A 168 57.669 22.368 -3.893 1.00 59.59 O ANISOU 1130 O THR A 168 7244 7476 7921 -797 1016 -701 O ATOM 1131 CB THR A 168 58.298 19.592 -3.010 1.00 58.50 C ANISOU 1131 CB THR A 168 6928 7399 7897 -664 1067 -759 C ATOM 1132 OG1 THR A 168 58.729 19.038 -4.260 1.00 59.05 O ANISOU 1132 OG1 THR A 168 7075 7441 7917 -717 1157 -792 O ATOM 1133 CG2 THR A 168 58.267 18.511 -1.949 1.00 57.16 C ANISOU 1133 CG2 THR A 168 6655 7263 7800 -570 1033 -765 C ATOM 1134 N ILE A 169 56.357 21.230 -5.335 1.00 60.22 N ANISOU 1134 N ILE A 169 7481 7491 7907 -822 981 -663 N ATOM 1135 CA ILE A 169 56.431 22.272 -6.366 1.00 61.25 C ANISOU 1135 CA ILE A 169 7740 7574 7957 -919 1000 -656 C ATOM 1136 C ILE A 169 56.345 23.704 -5.781 1.00 61.33 C ANISOU 1136 C ILE A 169 7738 7585 7976 -924 950 -633 C ATOM 1137 O ILE A 169 57.238 24.522 -6.018 1.00 61.82 O ANISOU 1137 O ILE A 169 7818 7647 8022 -988 1012 -661 O ATOM 1138 CB ILE A 169 55.396 22.043 -7.500 1.00 61.47 C ANISOU 1138 CB ILE A 169 7922 7535 7897 -967 943 -613 C ATOM 1139 CG1 ILE A 169 56.003 21.141 -8.574 1.00 62.54 C ANISOU 1139 CG1 ILE A 169 8140 7645 7977 -1021 1042 -657 C ATOM 1140 CG2 ILE A 169 54.977 23.368 -8.137 1.00 61.84 C ANISOU 1140 CG2 ILE A 169 8091 7529 7875 -1038 894 -577 C ATOM 1141 CD1 ILE A 169 55.035 20.742 -9.674 1.00 63.23 C ANISOU 1141 CD1 ILE A 169 8391 7660 7973 -1072 980 -616 C ATOM 1142 N PRO A 170 55.294 24.001 -4.999 1.00 60.87 N ANISOU 1142 N PRO A 170 7652 7529 7946 -856 844 -581 N ATOM 1143 CA PRO A 170 55.146 25.312 -4.369 1.00 60.95 C ANISOU 1143 CA PRO A 170 7662 7532 7964 -845 796 -559 C ATOM 1144 C PRO A 170 56.340 25.754 -3.522 1.00 61.07 C ANISOU 1144 C PRO A 170 7585 7588 8028 -843 852 -603 C ATOM 1145 O PRO A 170 56.638 26.948 -3.439 1.00 61.05 O ANISOU 1145 O PRO A 170 7624 7568 8004 -884 845 -601 O ATOM 1146 CB PRO A 170 53.923 25.122 -3.474 1.00 60.36 C ANISOU 1146 CB PRO A 170 7533 7467 7933 -746 700 -506 C ATOM 1147 CG PRO A 170 53.134 24.114 -4.165 1.00 60.29 C ANISOU 1147 CG PRO A 170 7560 7442 7904 -747 670 -479 C ATOM 1148 CD PRO A 170 54.108 23.164 -4.768 1.00 60.40 C ANISOU 1148 CD PRO A 170 7576 7468 7904 -792 764 -535 C ATOM 1149 N ASP A 171 57.005 24.799 -2.885 1.00 61.01 N ANISOU 1149 N ASP A 171 7460 7633 8088 -799 896 -641 N ATOM 1150 CA ASP A 171 58.173 25.123 -2.086 1.00 61.31 C ANISOU 1150 CA ASP A 171 7402 7709 8182 -801 937 -679 C ATOM 1151 C ASP A 171 59.275 25.665 -3.010 1.00 62.05 C ANISOU 1151 C ASP A 171 7535 7795 8243 -910 1029 -716 C ATOM 1152 O ASP A 171 59.836 26.720 -2.744 1.00 62.42 O ANISOU 1152 O ASP A 171 7586 7841 8288 -956 1030 -720 O ATOM 1153 CB ASP A 171 58.654 23.906 -1.277 1.00 61.30 C ANISOU 1153 CB ASP A 171 7268 7758 8262 -730 958 -709 C ATOM 1154 CG ASP A 171 57.610 23.408 -0.251 1.00 61.29 C ANISOU 1154 CG ASP A 171 7229 7766 8291 -629 872 -673 C ATOM 1155 OD1 ASP A 171 56.616 22.751 -0.653 1.00 61.72 O ANISOU 1155 OD1 ASP A 171 7324 7805 8321 -604 841 -643 O ATOM 1156 OD2 ASP A 171 57.803 23.648 0.966 1.00 62.09 O ANISOU 1156 OD2 ASP A 171 7261 7888 8440 -580 837 -673 O ATOM 1157 N PHE A 172 59.556 24.970 -4.110 1.00 62.47 N ANISOU 1157 N PHE A 172 7631 7841 8264 -955 1109 -740 N ATOM 1158 CA PHE A 172 60.515 25.471 -5.107 1.00 63.32 C ANISOU 1158 CA PHE A 172 7792 7936 8329 -1066 1211 -772 C ATOM 1159 C PHE A 172 60.169 26.883 -5.555 1.00 63.53 C ANISOU 1159 C PHE A 172 7948 7912 8276 -1143 1169 -740 C ATOM 1160 O PHE A 172 61.046 27.722 -5.695 1.00 63.90 O ANISOU 1160 O PHE A 172 7999 7962 8315 -1223 1220 -758 O ATOM 1161 CB PHE A 172 60.577 24.562 -6.342 1.00 63.82 C ANISOU 1161 CB PHE A 172 7930 7977 8341 -1102 1296 -796 C ATOM 1162 CG PHE A 172 61.313 23.286 -6.110 1.00 63.91 C ANISOU 1162 CG PHE A 172 7822 8033 8425 -1047 1375 -842 C ATOM 1163 CD1 PHE A 172 60.623 22.093 -5.933 1.00 63.61 C ANISOU 1163 CD1 PHE A 172 7773 7993 8400 -966 1335 -834 C ATOM 1164 CD2 PHE A 172 62.700 23.278 -6.047 1.00 64.27 C ANISOU 1164 CD2 PHE A 172 7763 8122 8533 -1074 1485 -891 C ATOM 1165 CE1 PHE A 172 61.310 20.909 -5.706 1.00 64.02 C ANISOU 1165 CE1 PHE A 172 7725 8079 8519 -909 1403 -878 C ATOM 1166 CE2 PHE A 172 63.395 22.105 -5.820 1.00 64.62 C ANISOU 1166 CE2 PHE A 172 7691 8204 8654 -1013 1555 -934 C ATOM 1167 CZ PHE A 172 62.703 20.915 -5.651 1.00 64.54 C ANISOU 1167 CZ PHE A 172 7684 8185 8650 -927 1513 -929 C ATOM 1168 N ILE A 173 58.885 27.141 -5.774 1.00 63.23 N ANISOU 1168 N ILE A 173 8013 7825 8184 -1121 1073 -690 N ATOM 1169 CA ILE A 173 58.449 28.445 -6.253 1.00 63.77 C ANISOU 1169 CA ILE A 173 8219 7834 8176 -1185 1021 -656 C ATOM 1170 C ILE A 173 58.548 29.525 -5.160 1.00 63.72 C ANISOU 1170 C ILE A 173 8172 7834 8202 -1159 961 -642 C ATOM 1171 O ILE A 173 59.292 30.502 -5.326 1.00 64.33 O ANISOU 1171 O ILE A 173 8291 7899 8252 -1243 992 -655 O ATOM 1172 CB ILE A 173 57.019 28.372 -6.843 1.00 63.61 C ANISOU 1172 CB ILE A 173 8314 7755 8097 -1163 925 -601 C ATOM 1173 CG1 ILE A 173 57.043 27.545 -8.138 1.00 64.05 C ANISOU 1173 CG1 ILE A 173 8462 7783 8091 -1226 984 -615 C ATOM 1174 CG2 ILE A 173 56.461 29.777 -7.102 1.00 63.57 C ANISOU 1174 CG2 ILE A 173 8437 7686 8029 -1203 846 -560 C ATOM 1175 CD1 ILE A 173 55.672 27.221 -8.710 1.00 63.96 C ANISOU 1175 CD1 ILE A 173 8549 7718 8033 -1207 882 -560 C ATOM 1176 N PHE A 174 57.843 29.318 -4.044 1.00 62.87 N ANISOU 1176 N PHE A 174 7990 7746 8151 -1047 883 -618 N ATOM 1177 CA PHE A 174 57.618 30.372 -3.043 1.00 62.71 C ANISOU 1177 CA PHE A 174 7972 7712 8143 -1009 813 -595 C ATOM 1178 C PHE A 174 58.611 30.444 -1.880 1.00 62.71 C ANISOU 1178 C PHE A 174 7854 7759 8211 -992 833 -627 C ATOM 1179 O PHE A 174 58.590 31.425 -1.129 1.00 62.71 O ANISOU 1179 O PHE A 174 7880 7737 8206 -981 781 -613 O ATOM 1180 CB PHE A 174 56.213 30.251 -2.443 1.00 62.13 C ANISOU 1180 CB PHE A 174 7898 7623 8086 -897 718 -546 C ATOM 1181 CG PHE A 174 55.114 30.233 -3.462 1.00 62.57 C ANISOU 1181 CG PHE A 174 8058 7628 8087 -906 670 -503 C ATOM 1182 CD1 PHE A 174 54.280 29.124 -3.586 1.00 62.15 C ANISOU 1182 CD1 PHE A 174 7965 7590 8058 -849 645 -481 C ATOM 1183 CD2 PHE A 174 54.908 31.324 -4.299 1.00 63.18 C ANISOU 1183 CD2 PHE A 174 8280 7638 8087 -977 640 -481 C ATOM 1184 CE1 PHE A 174 53.265 29.104 -4.529 1.00 62.11 C ANISOU 1184 CE1 PHE A 174 8055 7535 8006 -865 586 -435 C ATOM 1185 CE2 PHE A 174 53.898 31.314 -5.242 1.00 63.40 C ANISOU 1185 CE2 PHE A 174 8408 7613 8066 -988 580 -437 C ATOM 1186 CZ PHE A 174 53.071 30.200 -5.357 1.00 63.09 C ANISOU 1186 CZ PHE A 174 8321 7591 8057 -933 550 -412 C ATOM 1187 N ALA A 175 59.446 29.421 -1.701 1.00 62.82 N ANISOU 1187 N ALA A 175 7748 7832 8290 -986 899 -666 N ATOM 1188 CA ALA A 175 60.469 29.444 -0.645 1.00 63.16 C ANISOU 1188 CA ALA A 175 7674 7917 8404 -977 909 -694 C ATOM 1189 C ALA A 175 61.638 30.312 -1.085 1.00 64.38 C ANISOU 1189 C ALA A 175 7845 8071 8544 -1099 964 -716 C ATOM 1190 O ALA A 175 62.380 29.924 -1.980 1.00 64.89 O ANISOU 1190 O ALA A 175 7889 8156 8610 -1168 1060 -746 O ATOM 1191 CB ALA A 175 60.957 28.049 -0.336 1.00 62.89 C ANISOU 1191 CB ALA A 175 7504 7941 8451 -925 954 -726 C ATOM 1192 N ASN A 176 61.792 31.485 -0.470 1.00 65.06 N ANISOU 1192 N ASN A 176 7976 8130 8612 -1126 908 -700 N ATOM 1193 CA ASN A 176 62.863 32.423 -0.829 1.00 66.48 C ANISOU 1193 CA ASN A 176 8180 8304 8772 -1253 948 -714 C ATOM 1194 C ASN A 176 63.430 33.163 0.390 1.00 66.99 C ANISOU 1194 C ASN A 176 8210 8370 8873 -1259 883 -709 C ATOM 1195 O ASN A 176 62.764 33.286 1.421 1.00 66.37 O ANISOU 1195 O ASN A 176 8146 8272 8800 -1168 800 -689 O ATOM 1196 CB ASN A 176 62.365 33.431 -1.879 1.00 66.90 C ANISOU 1196 CB ASN A 176 8411 8290 8716 -1332 942 -691 C ATOM 1197 CG ASN A 176 62.179 32.804 -3.268 1.00 67.45 C ANISOU 1197 CG ASN A 176 8530 8355 8743 -1373 1021 -701 C ATOM 1198 OD1 ASN A 176 63.036 32.938 -4.138 1.00 69.43 O ANISOU 1198 OD1 ASN A 176 8796 8613 8971 -1483 1114 -724 O ATOM 1199 ND2 ASN A 176 61.061 32.118 -3.473 1.00 66.77 N ANISOU 1199 ND2 ASN A 176 8473 8254 8642 -1288 986 -682 N ATOM 1200 N VAL A 177 64.667 33.641 0.267 1.00 68.38 N ANISOU 1200 N VAL A 177 8343 8566 9071 -1370 925 -726 N ATOM 1201 CA VAL A 177 65.318 34.397 1.338 1.00 69.05 C ANISOU 1201 CA VAL A 177 8403 8645 9184 -1401 857 -719 C ATOM 1202 C VAL A 177 64.886 35.851 1.277 1.00 70.05 C ANISOU 1202 C VAL A 177 8710 8694 9211 -1455 794 -689 C ATOM 1203 O VAL A 177 64.827 36.435 0.196 1.00 70.45 O ANISOU 1203 O VAL A 177 8865 8713 9188 -1541 834 -684 O ATOM 1204 CB VAL A 177 66.859 34.348 1.235 1.00 69.90 C ANISOU 1204 CB VAL A 177 8381 8809 9369 -1509 920 -743 C ATOM 1205 CG1 VAL A 177 67.495 35.353 2.190 1.00 70.10 C ANISOU 1205 CG1 VAL A 177 8417 8813 9402 -1570 835 -726 C ATOM 1206 CG2 VAL A 177 67.369 32.955 1.519 1.00 69.42 C ANISOU 1206 CG2 VAL A 177 8133 8820 9421 -1440 967 -772 C ATOM 1207 N SER A 178 64.595 36.427 2.443 1.00 70.89 N ANISOU 1207 N SER A 178 8861 8763 9308 -1404 695 -671 N ATOM 1208 CA SER A 178 64.193 37.832 2.564 1.00 71.99 C ANISOU 1208 CA SER A 178 9179 8819 9354 -1440 626 -643 C ATOM 1209 C SER A 178 65.036 38.539 3.632 1.00 73.31 C ANISOU 1209 C SER A 178 9343 8971 9538 -1494 558 -639 C ATOM 1210 O SER A 178 65.325 37.975 4.690 1.00 73.15 O ANISOU 1210 O SER A 178 9223 8982 9589 -1436 522 -646 O ATOM 1211 CB SER A 178 62.707 37.941 2.933 1.00 71.19 C ANISOU 1211 CB SER A 178 9180 8663 9205 -1304 566 -618 C ATOM 1212 OG SER A 178 62.021 36.713 2.720 1.00 70.83 O ANISOU 1212 OG SER A 178 9047 8660 9201 -1205 602 -623 O ATOM 1213 N GLU A 179 65.420 39.780 3.350 1.00 75.05 N ANISOU 1213 N GLU A 179 9686 9137 9689 -1610 533 -625 N ATOM 1214 CA GLU A 179 66.181 40.598 4.293 1.00 76.26 C ANISOU 1214 CA GLU A 179 9871 9263 9843 -1678 455 -615 C ATOM 1215 C GLU A 179 65.187 41.314 5.198 1.00 76.13 C ANISOU 1215 C GLU A 179 10016 9156 9752 -1580 360 -594 C ATOM 1216 O GLU A 179 64.291 42.000 4.717 1.00 75.77 O ANISOU 1216 O GLU A 179 10126 9043 9619 -1553 348 -578 O ATOM 1217 CB GLU A 179 67.066 41.589 3.524 1.00 77.58 C ANISOU 1217 CB GLU A 179 10100 9410 9964 -1859 476 -608 C ATOM 1218 CG GLU A 179 67.975 42.455 4.380 1.00 79.31 C ANISOU 1218 CG GLU A 179 10348 9601 10184 -1960 392 -594 C ATOM 1219 CD GLU A 179 67.579 43.928 4.377 1.00 80.97 C ANISOU 1219 CD GLU A 179 10798 9700 10266 -2013 319 -568 C ATOM 1220 OE1 GLU A 179 67.448 44.505 3.271 1.00 81.41 O ANISOU 1220 OE1 GLU A 179 10956 9726 10250 -2092 361 -562 O ATOM 1221 OE2 GLU A 179 67.419 44.506 5.481 1.00 81.81 O ANISOU 1221 OE2 GLU A 179 11001 9743 10339 -1977 218 -554 O ATOM 1222 N ALA A 180 65.338 41.131 6.507 1.00 76.66 N ANISOU 1222 N ALA A 180 10050 9220 9855 -1522 294 -593 N ATOM 1223 CA ALA A 180 64.401 41.694 7.484 1.00 76.81 C ANISOU 1223 CA ALA A 180 10218 9156 9809 -1414 218 -577 C ATOM 1224 C ALA A 180 65.052 41.917 8.855 1.00 77.67 C ANISOU 1224 C ALA A 180 10335 9240 9932 -1430 132 -575 C ATOM 1225 O ALA A 180 65.419 40.952 9.535 1.00 77.66 O ANISOU 1225 O ALA A 180 10194 9296 10016 -1389 126 -586 O ATOM 1226 CB ALA A 180 63.196 40.777 7.627 1.00 75.67 C ANISOU 1226 CB ALA A 180 10032 9031 9686 -1247 249 -579 C ATOM 1227 N ASP A 181 65.178 43.184 9.259 1.00 78.68 N ANISOU 1227 N ASP A 181 10642 9277 9975 -1490 59 -558 N ATOM 1228 CA ASP A 181 65.675 43.547 10.597 1.00 79.39 C ANISOU 1228 CA ASP A 181 10790 9320 10055 -1506 -38 -550 C ATOM 1229 C ASP A 181 67.166 43.174 10.757 1.00 79.68 C ANISOU 1229 C ASP A 181 10664 9424 10186 -1641 -63 -554 C ATOM 1230 O ASP A 181 67.558 42.460 11.688 1.00 79.35 O ANISOU 1230 O ASP A 181 10523 9412 10212 -1607 -105 -558 O ATOM 1231 CB ASP A 181 64.786 42.905 11.692 1.00 78.90 C ANISOU 1231 CB ASP A 181 10738 9241 9997 -1336 -53 -555 C ATOM 1232 CG ASP A 181 64.541 43.831 12.897 1.00 80.75 C ANISOU 1232 CG ASP A 181 11180 9362 10139 -1306 -143 -543 C ATOM 1233 OD1 ASP A 181 63.784 43.411 13.807 1.00 81.85 O ANISOU 1233 OD1 ASP A 181 11352 9478 10269 -1170 -146 -546 O ATOM 1234 OD2 ASP A 181 65.086 44.966 12.942 1.00 83.06 O ANISOU 1234 OD2 ASP A 181 11612 9584 10364 -1420 -206 -529 O ATOM 1235 N ASP A 182 67.972 43.671 9.812 1.00 80.18 N ANISOU 1235 N ASP A 182 10700 9509 10252 -1794 -35 -549 N ATOM 1236 CA ASP A 182 69.439 43.460 9.732 1.00 80.73 C ANISOU 1236 CA ASP A 182 10604 9648 10419 -1942 -44 -547 C ATOM 1237 C ASP A 182 69.919 41.990 9.724 1.00 79.74 C ANISOU 1237 C ASP A 182 10220 9637 10438 -1895 12 -568 C ATOM 1238 O ASP A 182 71.072 41.692 10.060 1.00 80.19 O ANISOU 1238 O ASP A 182 10129 9745 10593 -1980 -20 -563 O ATOM 1239 CB ASP A 182 70.162 44.304 10.794 1.00 81.80 C ANISOU 1239 CB ASP A 182 10835 9717 10527 -2037 -177 -522 C ATOM 1240 CG ASP A 182 70.189 45.792 10.437 1.00 83.37 C ANISOU 1240 CG ASP A 182 11249 9823 10605 -2154 -218 -500 C ATOM 1241 OD1 ASP A 182 69.221 46.269 9.803 1.00 83.71 O ANISOU 1241 OD1 ASP A 182 11435 9815 10554 -2097 -173 -503 O ATOM 1242 OD2 ASP A 182 71.175 46.488 10.782 1.00 85.39 O ANISOU 1242 OD2 ASP A 182 11533 10053 10859 -2305 -300 -477 O ATOM 1243 N ARG A 183 69.029 41.096 9.293 1.00 78.06 N ANISOU 1243 N ARG A 183 9957 9461 10238 -1763 94 -588 N ATOM 1244 CA ARG A 183 69.339 39.681 9.136 1.00 77.21 C ANISOU 1244 CA ARG A 183 9628 9453 10253 -1707 159 -611 C ATOM 1245 C ARG A 183 68.566 39.104 7.954 1.00 75.97 C ANISOU 1245 C ARG A 183 9449 9333 10083 -1644 277 -629 C ATOM 1246 O ARG A 183 67.679 39.761 7.398 1.00 75.49 O ANISOU 1246 O ARG A 183 9544 9216 9922 -1626 294 -620 O ATOM 1247 CB ARG A 183 69.018 38.888 10.417 1.00 76.59 C ANISOU 1247 CB ARG A 183 9513 9372 10214 -1580 92 -614 C ATOM 1248 CG ARG A 183 67.551 38.939 10.882 1.00 75.49 C ANISOU 1248 CG ARG A 183 9527 9170 9985 -1432 80 -611 C ATOM 1249 CD ARG A 183 67.217 37.774 11.831 1.00 74.52 C ANISOU 1249 CD ARG A 183 9321 9073 9920 -1303 59 -621 C ATOM 1250 NE ARG A 183 67.103 36.497 11.113 1.00 73.56 N ANISOU 1250 NE ARG A 183 9031 9039 9879 -1245 151 -643 N ATOM 1251 CZ ARG A 183 67.157 35.288 11.671 1.00 72.00 C ANISOU 1251 CZ ARG A 183 8709 8886 9760 -1164 146 -655 C ATOM 1252 NH1 ARG A 183 67.045 34.209 10.907 1.00 71.31 N ANISOU 1252 NH1 ARG A 183 8491 8869 9735 -1119 233 -675 N ATOM 1253 NH2 ARG A 183 67.335 35.141 12.978 1.00 71.87 N ANISOU 1253 NH2 ARG A 183 8711 8839 9756 -1131 52 -648 N ATOM 1254 N TYR A 184 68.926 37.878 7.575 1.00 75.16 N ANISOU 1254 N TYR A 184 9157 9317 10082 -1612 352 -652 N ATOM 1255 CA TYR A 184 68.228 37.138 6.526 1.00 73.99 C ANISOU 1255 CA TYR A 184 8981 9203 9928 -1547 458 -669 C ATOM 1256 C TYR A 184 67.275 36.084 7.118 1.00 71.91 C ANISOU 1256 C TYR A 184 8686 8949 9684 -1381 447 -677 C ATOM 1257 O TYR A 184 67.555 35.476 8.160 1.00 71.32 O ANISOU 1257 O TYR A 184 8529 8892 9675 -1327 392 -680 O ATOM 1258 CB TYR A 184 69.225 36.453 5.581 1.00 74.80 C ANISOU 1258 CB TYR A 184 8910 9389 10119 -1622 567 -693 C ATOM 1259 CG TYR A 184 70.145 37.385 4.824 1.00 76.52 C ANISOU 1259 CG TYR A 184 9145 9608 10320 -1793 606 -686 C ATOM 1260 CD1 TYR A 184 69.643 38.485 4.135 1.00 77.44 C ANISOU 1260 CD1 TYR A 184 9447 9659 10315 -1859 610 -670 C ATOM 1261 CD2 TYR A 184 71.516 37.140 4.763 1.00 78.43 C ANISOU 1261 CD2 TYR A 184 9209 9916 10672 -1889 641 -693 C ATOM 1262 CE1 TYR A 184 70.486 39.333 3.429 1.00 79.15 C ANISOU 1262 CE1 TYR A 184 9688 9875 10509 -2025 648 -663 C ATOM 1263 CE2 TYR A 184 72.368 37.978 4.060 1.00 79.86 C ANISOU 1263 CE2 TYR A 184 9396 10103 10841 -2054 686 -684 C ATOM 1264 CZ TYR A 184 71.847 39.073 3.395 1.00 80.54 C ANISOU 1264 CZ TYR A 184 9683 10122 10795 -2126 691 -669 C ATOM 1265 OH TYR A 184 72.684 39.909 2.694 1.00 82.56 O ANISOU 1265 OH TYR A 184 9957 10381 11031 -2298 736 -659 O ATOM 1266 N ILE A 185 66.148 35.887 6.435 1.00 70.14 N ANISOU 1266 N ILE A 185 8534 8710 9403 -1309 495 -676 N ATOM 1267 CA ILE A 185 65.134 34.919 6.850 1.00 68.36 C ANISOU 1267 CA ILE A 185 8286 8494 9190 -1162 492 -677 C ATOM 1268 C ILE A 185 64.719 34.075 5.641 1.00 67.11 C ANISOU 1268 C ILE A 185 8079 8377 9041 -1139 588 -691 C ATOM 1269 O ILE A 185 64.839 34.510 4.496 1.00 67.18 O ANISOU 1269 O ILE A 185 8135 8381 9009 -1221 645 -693 O ATOM 1270 CB ILE A 185 63.904 35.611 7.542 1.00 67.85 C ANISOU 1270 CB ILE A 185 8386 8353 9040 -1074 426 -651 C ATOM 1271 CG1 ILE A 185 62.985 36.289 6.518 1.00 67.65 C ANISOU 1271 CG1 ILE A 185 8491 8283 8928 -1077 454 -635 C ATOM 1272 CG2 ILE A 185 64.380 36.625 8.591 1.00 67.98 C ANISOU 1272 CG2 ILE A 185 8492 8312 9025 -1118 336 -639 C ATOM 1273 CD1 ILE A 185 61.958 37.223 7.126 1.00 67.60 C ANISOU 1273 CD1 ILE A 185 8650 8193 8841 -1006 392 -608 C ATOM 1274 N CYS A 186 64.259 32.858 5.912 1.00 65.47 N ANISOU 1274 N CYS A 186 7787 8205 8882 -1034 601 -700 N ATOM 1275 CA CYS A 186 63.905 31.907 4.873 1.00 64.41 C ANISOU 1275 CA CYS A 186 7605 8107 8759 -1009 682 -713 C ATOM 1276 C CYS A 186 62.467 31.479 5.094 1.00 63.06 C ANISOU 1276 C CYS A 186 7491 7914 8554 -890 655 -692 C ATOM 1277 O CYS A 186 62.195 30.561 5.869 1.00 62.61 O ANISOU 1277 O CYS A 186 7365 7880 8543 -800 633 -695 O ATOM 1278 CB CYS A 186 64.850 30.708 4.929 1.00 64.49 C ANISOU 1278 CB CYS A 186 7442 8186 8874 -1003 729 -745 C ATOM 1279 SG CYS A 186 64.391 29.299 3.910 1.00 63.94 S ANISOU 1279 SG CYS A 186 7317 8153 8821 -947 819 -765 S ATOM 1280 N ASP A 187 61.555 32.175 4.418 1.00 62.31 N ANISOU 1280 N ASP A 187 7523 7772 8379 -894 652 -668 N ATOM 1281 CA ASP A 187 60.122 31.956 4.541 1.00 61.06 C ANISOU 1281 CA ASP A 187 7421 7588 8189 -790 623 -639 C ATOM 1282 C ASP A 187 59.493 31.549 3.207 1.00 60.26 C ANISOU 1282 C ASP A 187 7349 7488 8057 -802 668 -631 C ATOM 1283 O ASP A 187 60.035 31.857 2.145 1.00 60.68 O ANISOU 1283 O ASP A 187 7436 7538 8082 -900 715 -643 O ATOM 1284 CB ASP A 187 59.466 33.253 5.003 1.00 61.37 C ANISOU 1284 CB ASP A 187 7597 7558 8162 -770 562 -609 C ATOM 1285 CG ASP A 187 59.925 33.686 6.378 1.00 62.62 C ANISOU 1285 CG ASP A 187 7759 7699 8333 -752 508 -613 C ATOM 1286 OD1 ASP A 187 59.616 34.841 6.772 1.00 64.41 O ANISOU 1286 OD1 ASP A 187 8110 7861 8499 -750 463 -594 O ATOM 1287 OD2 ASP A 187 60.584 32.877 7.068 1.00 63.62 O ANISOU 1287 OD2 ASP A 187 7776 7871 8525 -738 507 -633 O ATOM 1288 N ARG A 188 58.350 30.856 3.274 1.00 58.89 N ANISOU 1288 N ARG A 188 7169 7317 7889 -709 650 -608 N ATOM 1289 CA ARG A 188 57.446 30.711 2.119 1.00 58.09 C ANISOU 1289 CA ARG A 188 7131 7194 7745 -713 658 -584 C ATOM 1290 C ARG A 188 56.539 31.935 2.020 1.00 57.64 C ANISOU 1290 C ARG A 188 7202 7070 7626 -698 601 -543 C ATOM 1291 O ARG A 188 55.734 32.206 2.921 1.00 56.83 O ANISOU 1291 O ARG A 188 7113 6949 7531 -606 554 -517 O ATOM 1292 CB ARG A 188 56.574 29.462 2.230 1.00 57.36 C ANISOU 1292 CB ARG A 188 6974 7131 7688 -626 652 -569 C ATOM 1293 CG ARG A 188 57.339 28.171 2.132 1.00 57.34 C ANISOU 1293 CG ARG A 188 6863 7183 7738 -635 707 -606 C ATOM 1294 CD ARG A 188 56.444 26.998 1.753 1.00 56.32 C ANISOU 1294 CD ARG A 188 6712 7069 7619 -583 704 -588 C ATOM 1295 NE ARG A 188 55.336 26.807 2.684 1.00 55.04 N ANISOU 1295 NE ARG A 188 6532 6905 7476 -484 647 -550 N ATOM 1296 CZ ARG A 188 54.572 25.721 2.727 1.00 53.61 C ANISOU 1296 CZ ARG A 188 6308 6744 7317 -429 635 -531 C ATOM 1297 NH1 ARG A 188 54.787 24.713 1.888 1.00 53.67 N ANISOU 1297 NH1 ARG A 188 6298 6766 7325 -462 670 -547 N ATOM 1298 NH2 ARG A 188 53.580 25.650 3.607 1.00 52.24 N ANISOU 1298 NH2 ARG A 188 6116 6571 7162 -345 592 -494 N ATOM 1299 N PHE A 189 56.678 32.670 0.925 1.00 57.54 N ANISOU 1299 N PHE A 189 7290 7018 7552 -787 610 -539 N ATOM 1300 CA PHE A 189 55.883 33.856 0.706 1.00 57.48 C ANISOU 1300 CA PHE A 189 7415 6938 7484 -779 552 -502 C ATOM 1301 C PHE A 189 55.010 33.633 -0.511 1.00 56.98 C ANISOU 1301 C PHE A 189 7413 6848 7386 -791 538 -471 C ATOM 1302 O PHE A 189 55.498 33.614 -1.637 1.00 57.53 O ANISOU 1302 O PHE A 189 7534 6909 7413 -892 576 -485 O ATOM 1303 CB PHE A 189 56.778 35.087 0.512 1.00 58.31 C ANISOU 1303 CB PHE A 189 7613 7004 7536 -883 555 -516 C ATOM 1304 CG PHE A 189 56.017 36.380 0.506 1.00 58.96 C ANISOU 1304 CG PHE A 189 7840 7003 7557 -861 487 -480 C ATOM 1305 CD1 PHE A 189 55.595 36.952 -0.683 1.00 59.71 C ANISOU 1305 CD1 PHE A 189 8058 7043 7586 -918 466 -457 C ATOM 1306 CD2 PHE A 189 55.687 37.007 1.698 1.00 59.07 C ANISOU 1306 CD2 PHE A 189 7878 6989 7577 -779 441 -469 C ATOM 1307 CE1 PHE A 189 54.868 38.146 -0.680 1.00 60.67 C ANISOU 1307 CE1 PHE A 189 8315 7081 7656 -888 396 -422 C ATOM 1308 CE2 PHE A 189 54.965 38.195 1.707 1.00 59.67 C ANISOU 1308 CE2 PHE A 189 8091 6981 7597 -745 382 -437 C ATOM 1309 CZ PHE A 189 54.555 38.764 0.522 1.00 60.20 C ANISOU 1309 CZ PHE A 189 8271 6994 7607 -797 357 -413 C ATOM 1310 N TYR A 190 53.718 33.461 -0.274 1.00 56.07 N ANISOU 1310 N TYR A 190 7294 6718 7289 -690 483 -427 N ATOM 1311 CA TYR A 190 52.750 33.258 -1.342 1.00 55.89 C ANISOU 1311 CA TYR A 190 7328 6666 7242 -694 445 -387 C ATOM 1312 C TYR A 190 52.192 34.609 -1.790 1.00 56.18 C ANISOU 1312 C TYR A 190 7507 6618 7220 -705 380 -352 C ATOM 1313 O TYR A 190 52.408 35.604 -1.118 1.00 56.28 O ANISOU 1313 O TYR A 190 7565 6599 7216 -688 366 -356 O ATOM 1314 CB TYR A 190 51.615 32.380 -0.839 1.00 55.39 C ANISOU 1314 CB TYR A 190 7173 6632 7240 -581 413 -351 C ATOM 1315 CG TYR A 190 52.031 31.006 -0.369 1.00 54.53 C ANISOU 1315 CG TYR A 190 6934 6596 7186 -561 464 -381 C ATOM 1316 CD1 TYR A 190 51.978 29.918 -1.223 1.00 55.29 C ANISOU 1316 CD1 TYR A 190 7009 6715 7283 -600 483 -383 C ATOM 1317 CD2 TYR A 190 52.438 30.787 0.934 1.00 53.82 C ANISOU 1317 CD2 TYR A 190 6758 6547 7144 -502 487 -405 C ATOM 1318 CE1 TYR A 190 52.332 28.639 -0.797 1.00 55.13 C ANISOU 1318 CE1 TYR A 190 6880 6755 7311 -575 525 -410 C ATOM 1319 CE2 TYR A 190 52.803 29.514 1.373 1.00 54.22 C ANISOU 1319 CE2 TYR A 190 6696 6658 7244 -480 525 -430 C ATOM 1320 CZ TYR A 190 52.746 28.442 0.501 1.00 54.59 C ANISOU 1320 CZ TYR A 190 6720 6726 7293 -515 544 -433 C ATOM 1321 OH TYR A 190 53.094 27.173 0.914 1.00 53.93 O ANISOU 1321 OH TYR A 190 6537 6695 7257 -489 578 -458 O ATOM 1322 N PRO A 191 51.478 34.654 -2.927 1.00 56.44 N ANISOU 1322 N PRO A 191 7622 6607 7216 -737 334 -315 N ATOM 1323 CA PRO A 191 50.909 35.917 -3.403 1.00 57.04 C ANISOU 1323 CA PRO A 191 7839 6594 7236 -744 260 -277 C ATOM 1324 C PRO A 191 49.898 36.588 -2.474 1.00 56.99 C ANISOU 1324 C PRO A 191 7824 6558 7270 -610 198 -237 C ATOM 1325 O PRO A 191 50.003 37.797 -2.266 1.00 57.56 O ANISOU 1325 O PRO A 191 7998 6569 7301 -609 171 -235 O ATOM 1326 CB PRO A 191 50.240 35.526 -4.722 1.00 57.32 C ANISOU 1326 CB PRO A 191 7940 6596 7241 -792 212 -241 C ATOM 1327 CG PRO A 191 51.055 34.400 -5.218 1.00 57.23 C ANISOU 1327 CG PRO A 191 7880 6641 7224 -872 294 -283 C ATOM 1328 CD PRO A 191 51.437 33.624 -3.982 1.00 56.72 C ANISOU 1328 CD PRO A 191 7652 6659 7238 -797 352 -315 C ATOM 1329 N ASN A 192 48.936 35.837 -1.931 1.00 56.46 N ANISOU 1329 N ASN A 192 7643 6528 7278 -499 180 -205 N ATOM 1330 CA ASN A 192 47.904 36.428 -1.050 1.00 56.43 C ANISOU 1330 CA ASN A 192 7621 6498 7318 -362 137 -164 C ATOM 1331 C ASN A 192 47.141 35.422 -0.187 1.00 55.57 C ANISOU 1331 C ASN A 192 7358 6456 7300 -251 154 -143 C ATOM 1332 O ASN A 192 47.315 34.214 -0.322 1.00 55.28 O ANISOU 1332 O ASN A 192 7231 6482 7291 -280 185 -155 O ATOM 1333 CB ASN A 192 46.907 37.229 -1.886 1.00 57.07 C ANISOU 1333 CB ASN A 192 7802 6498 7381 -344 43 -106 C ATOM 1334 CG ASN A 192 46.294 36.407 -2.978 1.00 57.79 C ANISOU 1334 CG ASN A 192 7876 6597 7485 -385 -4 -67 C ATOM 1335 OD1 ASN A 192 45.657 35.388 -2.716 1.00 58.95 O ANISOU 1335 OD1 ASN A 192 7897 6799 7702 -330 -4 -42 O ATOM 1336 ND2 ASN A 192 46.484 36.834 -4.218 1.00 59.21 N ANISOU 1336 ND2 ASN A 192 8192 6715 7590 -491 -49 -59 N ATOM 1337 N ASP A 193 46.283 35.931 0.693 1.00 55.37 N ANISOU 1337 N ASP A 193 7309 6411 7316 -124 138 -112 N ATOM 1338 CA ASP A 193 45.472 35.072 1.570 1.00 54.58 C ANISOU 1338 CA ASP A 193 7068 6370 7300 -16 161 -87 C ATOM 1339 C ASP A 193 44.692 33.978 0.850 1.00 54.20 C ANISOU 1339 C ASP A 193 6933 6360 7301 -27 125 -42 C ATOM 1340 O ASP A 193 44.434 32.923 1.438 1.00 53.70 O ANISOU 1340 O ASP A 193 6748 6363 7292 10 158 -38 O ATOM 1341 CB ASP A 193 44.503 35.899 2.443 1.00 55.07 C ANISOU 1341 CB ASP A 193 7131 6394 7399 125 152 -51 C ATOM 1342 CG ASP A 193 43.623 36.858 1.640 1.00 55.94 C ANISOU 1342 CG ASP A 193 7321 6425 7506 155 68 3 C ATOM 1343 OD1 ASP A 193 43.498 36.719 0.404 1.00 56.04 O ANISOU 1343 OD1 ASP A 193 7372 6419 7502 74 5 27 O ATOM 1344 OD2 ASP A 193 43.044 37.766 2.269 1.00 57.31 O ANISOU 1344 OD2 ASP A 193 7528 6550 7695 265 66 22 O ATOM 1345 N LEU A 194 44.295 34.220 -0.399 1.00 54.38 N ANISOU 1345 N LEU A 194 7024 6336 7299 -84 50 -5 N ATOM 1346 CA LEU A 194 43.543 33.210 -1.135 1.00 54.21 C ANISOU 1346 CA LEU A 194 6937 6340 7317 -106 0 41 C ATOM 1347 C LEU A 194 44.395 31.960 -1.235 1.00 53.36 C ANISOU 1347 C LEU A 194 6783 6297 7195 -186 59 -5 C ATOM 1348 O LEU A 194 43.962 30.884 -0.819 1.00 53.27 O ANISOU 1348 O LEU A 194 6655 6343 7239 -150 72 10 O ATOM 1349 CB LEU A 194 43.115 33.695 -2.528 1.00 55.06 C ANISOU 1349 CB LEU A 194 7157 6375 7386 -173 -99 85 C ATOM 1350 CG LEU A 194 42.006 34.751 -2.611 1.00 55.43 C ANISOU 1350 CG LEU A 194 7236 6355 7468 -85 -185 150 C ATOM 1351 CD1 LEU A 194 41.482 34.872 -4.021 1.00 54.90 C ANISOU 1351 CD1 LEU A 194 7258 6225 7375 -159 -300 203 C ATOM 1352 CD2 LEU A 194 40.869 34.404 -1.676 1.00 55.86 C ANISOU 1352 CD2 LEU A 194 7134 6455 7636 52 -183 201 C ATOM 1353 N TRP A 195 45.613 32.113 -1.753 1.00 52.82 N ANISOU 1353 N TRP A 195 6801 6216 7051 -291 99 -63 N ATOM 1354 CA TRP A 195 46.575 31.016 -1.809 1.00 52.04 C ANISOU 1354 CA TRP A 195 6659 6173 6939 -358 168 -117 C ATOM 1355 C TRP A 195 46.748 30.337 -0.469 1.00 51.25 C ANISOU 1355 C TRP A 195 6433 6142 6898 -282 227 -141 C ATOM 1356 O TRP A 195 46.655 29.114 -0.356 1.00 50.82 O ANISOU 1356 O TRP A 195 6294 6138 6877 -279 244 -142 O ATOM 1357 CB TRP A 195 47.946 31.526 -2.227 1.00 52.14 C ANISOU 1357 CB TRP A 195 6763 6167 6879 -460 222 -180 C ATOM 1358 CG TRP A 195 48.115 31.736 -3.681 1.00 52.70 C ANISOU 1358 CG TRP A 195 6961 6185 6876 -572 194 -175 C ATOM 1359 CD1 TRP A 195 47.815 32.861 -4.396 1.00 53.44 C ANISOU 1359 CD1 TRP A 195 7186 6200 6917 -606 132 -146 C ATOM 1360 CD2 TRP A 195 48.664 30.802 -4.607 1.00 51.84 C ANISOU 1360 CD2 TRP A 195 6875 6090 6731 -667 231 -201 C ATOM 1361 NE1 TRP A 195 48.141 32.675 -5.718 1.00 54.05 N ANISOU 1361 NE1 TRP A 195 7372 6242 6922 -724 127 -152 N ATOM 1362 CE2 TRP A 195 48.663 31.418 -5.872 1.00 52.80 C ANISOU 1362 CE2 TRP A 195 7151 6139 6772 -762 193 -187 C ATOM 1363 CE3 TRP A 195 49.153 29.498 -4.489 1.00 51.51 C ANISOU 1363 CE3 TRP A 195 6750 6109 6713 -679 294 -236 C ATOM 1364 CZ2 TRP A 195 49.129 30.775 -7.012 1.00 53.43 C ANISOU 1364 CZ2 TRP A 195 7306 6204 6789 -869 223 -207 C ATOM 1365 CZ3 TRP A 195 49.622 28.858 -5.620 1.00 52.01 C ANISOU 1365 CZ3 TRP A 195 6883 6157 6719 -777 325 -257 C ATOM 1366 CH2 TRP A 195 49.608 29.498 -6.867 1.00 53.05 C ANISOU 1366 CH2 TRP A 195 7172 6216 6766 -873 294 -244 C ATOM 1367 N VAL A 196 47.009 31.145 0.547 1.00 51.16 N ANISOU 1367 N VAL A 196 6423 6123 6892 -223 254 -161 N ATOM 1368 CA VAL A 196 47.436 30.614 1.825 1.00 50.76 C ANISOU 1368 CA VAL A 196 6282 6125 6876 -170 313 -194 C ATOM 1369 C VAL A 196 46.380 29.697 2.421 1.00 50.89 C ANISOU 1369 C VAL A 196 6186 6185 6962 -85 305 -152 C ATOM 1370 O VAL A 196 46.702 28.586 2.815 1.00 50.43 O ANISOU 1370 O VAL A 196 6052 6180 6928 -89 339 -174 O ATOM 1371 CB VAL A 196 47.802 31.726 2.819 1.00 50.69 C ANISOU 1371 CB VAL A 196 6320 6087 6851 -123 333 -216 C ATOM 1372 CG1 VAL A 196 48.146 31.132 4.158 1.00 50.12 C ANISOU 1372 CG1 VAL A 196 6166 6063 6813 -68 381 -245 C ATOM 1373 CG2 VAL A 196 48.973 32.527 2.300 1.00 50.88 C ANISOU 1373 CG2 VAL A 196 6445 6076 6809 -223 343 -260 C ATOM 1374 N VAL A 197 45.127 30.145 2.460 1.00 51.85 N ANISOU 1374 N VAL A 197 6297 6283 7119 -9 260 -89 N ATOM 1375 CA VAL A 197 44.054 29.353 3.064 1.00 52.27 C ANISOU 1375 CA VAL A 197 6234 6380 7245 70 258 -41 C ATOM 1376 C VAL A 197 43.851 28.015 2.362 1.00 52.60 C ANISOU 1376 C VAL A 197 6219 6460 7304 11 234 -23 C ATOM 1377 O VAL A 197 43.568 27.011 3.008 1.00 52.13 O ANISOU 1377 O VAL A 197 6066 6452 7286 42 257 -15 O ATOM 1378 CB VAL A 197 42.706 30.113 3.081 1.00 53.18 C ANISOU 1378 CB VAL A 197 6337 6461 7408 160 212 30 C ATOM 1379 CG1 VAL A 197 42.245 30.432 1.676 1.00 53.78 C ANISOU 1379 CG1 VAL A 197 6472 6491 7470 103 123 73 C ATOM 1380 CG2 VAL A 197 41.643 29.304 3.823 1.00 52.88 C ANISOU 1380 CG2 VAL A 197 6164 6476 7451 242 227 79 C ATOM 1381 N VAL A 198 44.005 28.001 1.042 1.00 53.65 N ANISOU 1381 N VAL A 198 6425 6562 7397 -79 186 -17 N ATOM 1382 CA VAL A 198 43.779 26.790 0.259 1.00 54.17 C ANISOU 1382 CA VAL A 198 6467 6650 7466 -142 154 2 C ATOM 1383 C VAL A 198 44.819 25.723 0.539 1.00 54.13 C ANISOU 1383 C VAL A 198 6433 6689 7443 -183 220 -61 C ATOM 1384 O VAL A 198 44.492 24.567 0.771 1.00 53.55 O ANISOU 1384 O VAL A 198 6288 6656 7403 -175 220 -47 O ATOM 1385 CB VAL A 198 43.780 27.104 -1.232 1.00 54.74 C ANISOU 1385 CB VAL A 198 6651 6663 7482 -236 91 18 C ATOM 1386 CG1 VAL A 198 43.715 25.814 -2.053 1.00 54.74 C ANISOU 1386 CG1 VAL A 198 6653 6676 7468 -312 65 27 C ATOM 1387 CG2 VAL A 198 42.602 28.018 -1.551 1.00 55.95 C ANISOU 1387 CG2 VAL A 198 6822 6770 7666 -190 4 92 C ATOM 1388 N PHE A 199 46.080 26.125 0.522 1.00 55.28 N ANISOU 1388 N PHE A 199 6635 6826 7541 -227 275 -129 N ATOM 1389 CA PHE A 199 47.176 25.198 0.762 1.00 55.83 C ANISOU 1389 CA PHE A 199 6674 6934 7603 -261 338 -192 C ATOM 1390 C PHE A 199 47.245 24.746 2.211 1.00 55.99 C ANISOU 1390 C PHE A 199 6598 7001 7671 -182 375 -207 C ATOM 1391 O PHE A 199 47.605 23.602 2.490 1.00 55.68 O ANISOU 1391 O PHE A 199 6506 6999 7649 -186 400 -230 O ATOM 1392 CB PHE A 199 48.485 25.821 0.311 1.00 56.05 C ANISOU 1392 CB PHE A 199 6776 6941 7577 -333 385 -254 C ATOM 1393 CG PHE A 199 48.691 25.714 -1.156 1.00 57.85 C ANISOU 1393 CG PHE A 199 7096 7134 7749 -430 375 -256 C ATOM 1394 CD1 PHE A 199 49.694 24.909 -1.673 1.00 59.81 C ANISOU 1394 CD1 PHE A 199 7355 7398 7972 -496 434 -310 C ATOM 1395 CD2 PHE A 199 47.837 26.364 -2.030 1.00 59.79 C ANISOU 1395 CD2 PHE A 199 7424 7327 7966 -454 304 -203 C ATOM 1396 CE1 PHE A 199 49.868 24.789 -3.040 1.00 61.01 C ANISOU 1396 CE1 PHE A 199 7608 7511 8061 -587 436 -313 C ATOM 1397 CE2 PHE A 199 47.999 26.250 -3.396 1.00 61.22 C ANISOU 1397 CE2 PHE A 199 7710 7465 8083 -551 290 -203 C ATOM 1398 CZ PHE A 199 49.021 25.460 -3.904 1.00 62.01 C ANISOU 1398 CZ PHE A 199 7831 7580 8148 -620 362 -260 C ATOM 1399 N GLN A 200 46.883 25.647 3.118 1.00 56.96 N ANISOU 1399 N GLN A 200 6713 7115 7812 -109 377 -192 N ATOM 1400 CA GLN A 200 46.762 25.333 4.534 1.00 57.50 C ANISOU 1400 CA GLN A 200 6710 7217 7919 -29 408 -197 C ATOM 1401 C GLN A 200 45.631 24.323 4.759 1.00 58.06 C ANISOU 1401 C GLN A 200 6698 7321 8038 10 388 -142 C ATOM 1402 O GLN A 200 45.689 23.513 5.678 1.00 58.25 O ANISOU 1402 O GLN A 200 6663 7382 8086 44 416 -153 O ATOM 1403 CB GLN A 200 46.515 26.620 5.329 1.00 57.95 C ANISOU 1403 CB GLN A 200 6803 7242 7973 38 417 -189 C ATOM 1404 CG GLN A 200 46.852 26.551 6.807 1.00 58.60 C ANISOU 1404 CG GLN A 200 6857 7342 8066 99 460 -216 C ATOM 1405 CD GLN A 200 47.002 27.934 7.417 1.00 60.43 C ANISOU 1405 CD GLN A 200 7165 7526 8269 139 470 -227 C ATOM 1406 OE1 GLN A 200 46.017 28.627 7.713 1.00 61.24 O ANISOU 1406 OE1 GLN A 200 7280 7602 8383 215 467 -185 O ATOM 1407 NE2 GLN A 200 48.246 28.346 7.606 1.00 61.66 N ANISOU 1407 NE2 GLN A 200 7372 7668 8388 89 482 -282 N ATOM 1408 N PHE A 201 44.609 24.373 3.910 1.00 59.08 N ANISOU 1408 N PHE A 201 6828 7436 8182 1 333 -81 N ATOM 1409 CA PHE A 201 43.518 23.398 3.935 1.00 59.60 C ANISOU 1409 CA PHE A 201 6814 7533 8296 19 301 -21 C ATOM 1410 C PHE A 201 43.961 22.083 3.287 1.00 59.11 C ANISOU 1410 C PHE A 201 6754 7488 8215 -57 290 -40 C ATOM 1411 O PHE A 201 43.742 21.021 3.858 1.00 58.95 O ANISOU 1411 O PHE A 201 6671 7506 8221 -42 300 -33 O ATOM 1412 CB PHE A 201 42.290 23.986 3.238 1.00 60.65 C ANISOU 1412 CB PHE A 201 6945 7639 8459 33 233 56 C ATOM 1413 CG PHE A 201 41.073 23.112 3.285 1.00 62.86 C ANISOU 1413 CG PHE A 201 7129 7951 8801 49 193 130 C ATOM 1414 CD1 PHE A 201 40.555 22.554 2.112 1.00 65.34 C ANISOU 1414 CD1 PHE A 201 7458 8253 9115 -22 111 177 C ATOM 1415 CD2 PHE A 201 40.427 22.859 4.493 1.00 64.96 C ANISOU 1415 CD2 PHE A 201 7298 8258 9123 131 235 156 C ATOM 1416 CE1 PHE A 201 39.408 21.741 2.140 1.00 66.89 C ANISOU 1416 CE1 PHE A 201 7562 8478 9372 -18 62 253 C ATOM 1417 CE2 PHE A 201 39.278 22.044 4.540 1.00 66.69 C ANISOU 1417 CE2 PHE A 201 7421 8512 9405 138 201 230 C ATOM 1418 CZ PHE A 201 38.766 21.485 3.356 1.00 67.40 C ANISOU 1418 CZ PHE A 201 7516 8591 9501 60 109 281 C ATOM 1419 N GLN A 202 44.598 22.154 2.115 1.00 59.14 N ANISOU 1419 N GLN A 202 6841 7460 8167 -139 275 -67 N ATOM 1420 CA GLN A 202 45.259 20.980 1.512 1.00 59.01 C ANISOU 1420 CA GLN A 202 6847 7451 8120 -208 285 -103 C ATOM 1421 C GLN A 202 46.189 20.290 2.503 1.00 58.23 C ANISOU 1421 C GLN A 202 6701 7389 8031 -180 349 -163 C ATOM 1422 O GLN A 202 46.227 19.067 2.572 1.00 57.98 O ANISOU 1422 O GLN A 202 6644 7379 8007 -192 349 -169 O ATOM 1423 CB GLN A 202 46.071 21.381 0.275 1.00 59.48 C ANISOU 1423 CB GLN A 202 7015 7469 8115 -292 292 -141 C ATOM 1424 CG GLN A 202 46.756 20.208 -0.493 1.00 60.66 C ANISOU 1424 CG GLN A 202 7206 7615 8226 -361 314 -180 C ATOM 1425 CD GLN A 202 48.085 20.614 -1.191 1.00 62.53 C ANISOU 1425 CD GLN A 202 7520 7828 8408 -423 378 -250 C ATOM 1426 OE1 GLN A 202 48.219 20.514 -2.419 1.00 62.93 O ANISOU 1426 OE1 GLN A 202 7668 7839 8401 -500 372 -253 O ATOM 1427 NE2 GLN A 202 49.063 21.071 -0.397 1.00 63.02 N ANISOU 1427 NE2 GLN A 202 7543 7913 8486 -395 440 -304 N ATOM 1428 N HIS A 203 46.940 21.088 3.260 1.00 58.07 N ANISOU 1428 N HIS A 203 6679 7371 8011 -147 394 -207 N ATOM 1429 CA HIS A 203 47.874 20.581 4.274 1.00 57.62 C ANISOU 1429 CA HIS A 203 6581 7343 7968 -120 441 -262 C ATOM 1430 C HIS A 203 47.174 19.751 5.349 1.00 57.04 C ANISOU 1430 C HIS A 203 6436 7302 7933 -60 435 -232 C ATOM 1431 O HIS A 203 47.636 18.681 5.708 1.00 56.94 O ANISOU 1431 O HIS A 203 6396 7309 7928 -62 448 -260 O ATOM 1432 CB HIS A 203 48.637 21.746 4.929 1.00 57.80 C ANISOU 1432 CB HIS A 203 6623 7354 7982 -99 472 -300 C ATOM 1433 CG HIS A 203 49.638 21.320 5.966 1.00 58.31 C ANISOU 1433 CG HIS A 203 6650 7440 8062 -78 505 -352 C ATOM 1434 ND1 HIS A 203 50.802 20.650 5.651 1.00 58.11 N ANISOU 1434 ND1 HIS A 203 6615 7426 8037 -121 531 -407 N ATOM 1435 CD2 HIS A 203 49.652 21.484 7.313 1.00 58.35 C ANISOU 1435 CD2 HIS A 203 6631 7453 8084 -18 513 -356 C ATOM 1436 CE1 HIS A 203 51.483 20.411 6.758 1.00 58.03 C ANISOU 1436 CE1 HIS A 203 6566 7431 8050 -88 542 -440 C ATOM 1437 NE2 HIS A 203 50.806 20.902 7.781 1.00 58.40 N ANISOU 1437 NE2 HIS A 203 6612 7473 8101 -29 529 -410 N ATOM 1438 N ILE A 204 46.071 20.253 5.872 1.00 56.76 N ANISOU 1438 N ILE A 204 6372 7269 7923 -6 421 -176 N ATOM 1439 CA ILE A 204 45.325 19.522 6.864 1.00 56.55 C ANISOU 1439 CA ILE A 204 6280 7273 7931 44 425 -143 C ATOM 1440 C ILE A 204 44.813 18.243 6.254 1.00 56.49 C ANISOU 1440 C ILE A 204 6249 7281 7931 1 388 -110 C ATOM 1441 O ILE A 204 44.938 17.169 6.824 1.00 55.83 O ANISOU 1441 O ILE A 204 6137 7219 7855 5 395 -120 O ATOM 1442 CB ILE A 204 44.135 20.347 7.346 1.00 57.23 C ANISOU 1442 CB ILE A 204 6336 7358 8048 110 425 -82 C ATOM 1443 CG1 ILE A 204 44.626 21.465 8.276 1.00 57.81 C ANISOU 1443 CG1 ILE A 204 6444 7412 8107 165 469 -116 C ATOM 1444 CG2 ILE A 204 43.099 19.459 8.037 1.00 57.10 C ANISOU 1444 CG2 ILE A 204 6243 7377 8073 143 427 -28 C ATOM 1445 CD1 ILE A 204 43.642 22.637 8.423 1.00 59.27 C ANISOU 1445 CD1 ILE A 204 6631 7577 8312 229 472 -68 C ATOM 1446 N MET A 205 44.244 18.373 5.070 1.00 57.30 N ANISOU 1446 N MET A 205 6376 7365 8028 -44 340 -70 N ATOM 1447 CA MET A 205 43.509 17.280 4.467 1.00 58.04 C ANISOU 1447 CA MET A 205 6455 7465 8130 -89 288 -22 C ATOM 1448 C MET A 205 44.459 16.126 4.156 1.00 57.15 C ANISOU 1448 C MET A 205 6381 7350 7982 -137 299 -77 C ATOM 1449 O MET A 205 44.256 15.003 4.605 1.00 57.07 O ANISOU 1449 O MET A 205 6341 7359 7982 -136 291 -68 O ATOM 1450 CB MET A 205 42.758 17.758 3.212 1.00 58.96 C ANISOU 1450 CB MET A 205 6607 7551 8241 -135 221 32 C ATOM 1451 CG MET A 205 41.314 17.236 3.121 1.00 62.36 C ANISOU 1451 CG MET A 205 6973 7999 8721 -140 155 126 C ATOM 1452 SD MET A 205 40.249 17.688 4.538 1.00 68.88 S ANISOU 1452 SD MET A 205 7676 8868 9626 -37 190 181 S ATOM 1453 CE MET A 205 38.720 16.789 4.172 1.00 68.66 C ANISOU 1453 CE MET A 205 7567 8864 9657 -75 107 291 C ATOM 1454 N VAL A 206 45.521 16.422 3.424 1.00 56.71 N ANISOU 1454 N VAL A 206 6392 7268 7885 -175 323 -137 N ATOM 1455 CA VAL A 206 46.473 15.402 3.016 1.00 56.06 C ANISOU 1455 CA VAL A 206 6349 7178 7773 -213 345 -193 C ATOM 1456 C VAL A 206 47.299 14.916 4.195 1.00 55.38 C ANISOU 1456 C VAL A 206 6216 7117 7708 -163 389 -245 C ATOM 1457 O VAL A 206 47.653 13.742 4.257 1.00 55.35 O ANISOU 1457 O VAL A 206 6216 7114 7699 -170 390 -268 O ATOM 1458 CB VAL A 206 47.400 15.935 1.934 1.00 56.27 C ANISOU 1458 CB VAL A 206 6453 7172 7755 -265 374 -242 C ATOM 1459 CG1 VAL A 206 48.476 14.902 1.602 1.00 56.82 C ANISOU 1459 CG1 VAL A 206 6551 7233 7801 -289 417 -306 C ATOM 1460 CG2 VAL A 206 46.587 16.301 0.691 1.00 56.17 C ANISOU 1460 CG2 VAL A 206 6509 7123 7710 -325 318 -189 C ATOM 1461 N GLY A 207 47.575 15.827 5.129 1.00 54.85 N ANISOU 1461 N GLY A 207 6115 7062 7661 -113 417 -260 N ATOM 1462 CA GLY A 207 48.391 15.563 6.333 1.00 54.11 C ANISOU 1462 CA GLY A 207 5986 6985 7586 -67 448 -307 C ATOM 1463 C GLY A 207 47.813 14.692 7.449 1.00 53.55 C ANISOU 1463 C GLY A 207 5874 6936 7537 -26 434 -280 C ATOM 1464 O GLY A 207 48.545 13.830 7.954 1.00 53.16 O ANISOU 1464 O GLY A 207 5818 6889 7491 -15 440 -321 O ATOM 1465 N LEU A 208 46.553 14.940 7.871 1.00 53.20 N ANISOU 1465 N LEU A 208 5799 6904 7508 0 419 -214 N ATOM 1466 CA LEU A 208 45.802 13.997 8.755 1.00 52.91 C ANISOU 1466 CA LEU A 208 5726 6889 7488 21 409 -175 C ATOM 1467 C LEU A 208 44.554 13.415 8.135 1.00 52.45 C ANISOU 1467 C LEU A 208 5648 6841 7441 -12 366 -101 C ATOM 1468 O LEU A 208 44.392 12.201 8.101 1.00 53.09 O ANISOU 1468 O LEU A 208 5731 6924 7515 -41 340 -90 O ATOM 1469 CB LEU A 208 45.295 14.621 10.059 1.00 53.03 C ANISOU 1469 CB LEU A 208 5711 6917 7519 85 440 -153 C ATOM 1470 CG LEU A 208 45.929 15.824 10.737 1.00 54.18 C ANISOU 1470 CG LEU A 208 5880 7049 7658 128 477 -192 C ATOM 1471 CD1 LEU A 208 44.847 16.511 11.588 1.00 54.21 C ANISOU 1471 CD1 LEU A 208 5859 7060 7675 186 508 -140 C ATOM 1472 CD2 LEU A 208 47.123 15.367 11.585 1.00 54.92 C ANISOU 1472 CD2 LEU A 208 5993 7134 7738 138 483 -255 C ATOM 1473 N ILE A 209 43.634 14.270 7.710 1.00 51.62 N ANISOU 1473 N ILE A 209 5520 6737 7354 -9 353 -46 N ATOM 1474 CA ILE A 209 42.262 13.819 7.593 1.00 51.64 C ANISOU 1474 CA ILE A 209 5471 6759 7389 -24 315 38 C ATOM 1475 C ILE A 209 42.143 12.637 6.672 1.00 51.25 C ANISOU 1475 C ILE A 209 5454 6698 7319 -100 256 54 C ATOM 1476 O ILE A 209 41.466 11.661 6.996 1.00 51.75 O ANISOU 1476 O ILE A 209 5487 6779 7395 -119 231 99 O ATOM 1477 CB ILE A 209 41.300 14.913 7.129 1.00 52.17 C ANISOU 1477 CB ILE A 209 5505 6825 7490 -9 297 99 C ATOM 1478 CG1 ILE A 209 41.103 15.938 8.248 1.00 53.01 C ANISOU 1478 CG1 ILE A 209 5575 6943 7621 76 360 98 C ATOM 1479 CG2 ILE A 209 39.957 14.303 6.757 1.00 52.34 C ANISOU 1479 CG2 ILE A 209 5468 6866 7553 -44 239 191 C ATOM 1480 CD1 ILE A 209 39.783 16.731 8.129 1.00 55.03 C ANISOU 1480 CD1 ILE A 209 5765 7208 7933 113 348 179 C ATOM 1481 N LEU A 210 42.796 12.724 5.524 1.00 50.35 N ANISOU 1481 N LEU A 210 5410 6550 7167 -147 237 19 N ATOM 1482 CA LEU A 210 42.696 11.667 4.538 1.00 50.09 C ANISOU 1482 CA LEU A 210 5434 6494 7104 -221 182 33 C ATOM 1483 C LEU A 210 43.390 10.418 5.040 1.00 49.21 C ANISOU 1483 C LEU A 210 5346 6381 6970 -220 198 -13 C ATOM 1484 O LEU A 210 42.736 9.386 5.222 1.00 49.33 O ANISOU 1484 O LEU A 210 5352 6402 6987 -248 158 29 O ATOM 1485 CB LEU A 210 43.259 12.105 3.169 1.00 50.31 C ANISOU 1485 CB LEU A 210 5549 6478 7086 -271 170 2 C ATOM 1486 CG LEU A 210 42.432 13.140 2.394 1.00 50.62 C ANISOU 1486 CG LEU A 210 5591 6504 7138 -292 123 61 C ATOM 1487 CD1 LEU A 210 43.004 13.351 1.002 1.00 49.44 C ANISOU 1487 CD1 LEU A 210 5554 6303 6928 -358 108 31 C ATOM 1488 CD2 LEU A 210 40.950 12.737 2.323 1.00 50.93 C ANISOU 1488 CD2 LEU A 210 5574 6557 7219 -317 44 164 C ATOM 1489 N PRO A 211 44.711 10.501 5.289 1.00 48.09 N ANISOU 1489 N PRO A 211 5231 6229 6810 -190 251 -99 N ATOM 1490 CA PRO A 211 45.367 9.263 5.701 1.00 47.54 C ANISOU 1490 CA PRO A 211 5185 6151 6725 -185 256 -141 C ATOM 1491 C PRO A 211 44.745 8.703 6.976 1.00 46.84 C ANISOU 1491 C PRO A 211 5044 6090 6661 -155 248 -105 C ATOM 1492 O PRO A 211 44.757 7.489 7.171 1.00 47.00 O ANISOU 1492 O PRO A 211 5093 6100 6665 -172 223 -105 O ATOM 1493 CB PRO A 211 46.833 9.678 5.902 1.00 47.24 C ANISOU 1493 CB PRO A 211 5157 6106 6686 -147 315 -230 C ATOM 1494 CG PRO A 211 46.791 11.168 6.093 1.00 47.25 C ANISOU 1494 CG PRO A 211 5123 6122 6706 -122 343 -226 C ATOM 1495 CD PRO A 211 45.653 11.635 5.255 1.00 47.80 C ANISOU 1495 CD PRO A 211 5199 6188 6772 -162 303 -156 C ATOM 1496 N GLY A 212 44.183 9.579 7.810 1.00 45.94 N ANISOU 1496 N GLY A 212 4867 6007 6580 -113 272 -73 N ATOM 1497 CA GLY A 212 43.478 9.155 9.010 1.00 45.68 C ANISOU 1497 CA GLY A 212 4788 6001 6567 -88 278 -32 C ATOM 1498 C GLY A 212 42.324 8.236 8.661 1.00 45.69 C ANISOU 1498 C GLY A 212 4777 6010 6572 -146 224 44 C ATOM 1499 O GLY A 212 42.224 7.131 9.184 1.00 45.41 O ANISOU 1499 O GLY A 212 4756 5973 6522 -162 206 52 O ATOM 1500 N ILE A 213 41.463 8.707 7.761 1.00 45.62 N ANISOU 1500 N ILE A 213 4745 6005 6582 -181 188 104 N ATOM 1501 CA ILE A 213 40.325 7.934 7.287 1.00 45.69 C ANISOU 1501 CA ILE A 213 4737 6019 6601 -249 121 188 C ATOM 1502 C ILE A 213 40.816 6.621 6.725 1.00 45.47 C ANISOU 1502 C ILE A 213 4802 5954 6521 -307 75 161 C ATOM 1503 O ILE A 213 40.200 5.599 6.973 1.00 46.25 O ANISOU 1503 O ILE A 213 4900 6055 6615 -349 35 207 O ATOM 1504 CB ILE A 213 39.513 8.674 6.186 1.00 46.16 C ANISOU 1504 CB ILE A 213 4776 6076 6687 -285 70 249 C ATOM 1505 CG1 ILE A 213 38.736 9.848 6.769 1.00 46.14 C ANISOU 1505 CG1 ILE A 213 4672 6110 6748 -225 107 295 C ATOM 1506 CG2 ILE A 213 38.541 7.739 5.485 1.00 45.82 C ANISOU 1506 CG2 ILE A 213 4740 6025 6645 -374 -21 329 C ATOM 1507 CD1 ILE A 213 38.248 10.816 5.700 1.00 45.77 C ANISOU 1507 CD1 ILE A 213 4617 6048 6723 -241 61 335 C ATOM 1508 N VAL A 214 41.914 6.610 5.981 1.00 44.80 N ANISOU 1508 N VAL A 214 4798 5829 6393 -310 83 87 N ATOM 1509 CA VAL A 214 42.378 5.324 5.474 1.00 45.04 C ANISOU 1509 CA VAL A 214 4924 5817 6372 -354 48 59 C ATOM 1510 C VAL A 214 42.667 4.424 6.673 1.00 45.35 C ANISOU 1510 C VAL A 214 4957 5863 6410 -321 64 38 C ATOM 1511 O VAL A 214 42.160 3.294 6.746 1.00 45.47 O ANISOU 1511 O VAL A 214 5005 5865 6404 -368 14 75 O ATOM 1512 CB VAL A 214 43.620 5.407 4.524 1.00 44.77 C ANISOU 1512 CB VAL A 214 4978 5736 6294 -352 76 -24 C ATOM 1513 CG1 VAL A 214 44.334 4.054 4.441 1.00 43.87 C ANISOU 1513 CG1 VAL A 214 4951 5580 6136 -360 68 -72 C ATOM 1514 CG2 VAL A 214 43.202 5.832 3.136 1.00 44.06 C ANISOU 1514 CG2 VAL A 214 4942 5618 6179 -417 36 8 C ATOM 1515 N ILE A 215 43.439 4.941 7.627 1.00 45.34 N ANISOU 1515 N ILE A 215 4920 5878 6426 -247 126 -17 N ATOM 1516 CA ILE A 215 43.902 4.117 8.743 1.00 45.83 C ANISOU 1516 CA ILE A 215 4995 5937 6481 -214 134 -48 C ATOM 1517 C ILE A 215 42.693 3.583 9.497 1.00 47.00 C ANISOU 1517 C ILE A 215 5107 6111 6639 -244 109 32 C ATOM 1518 O ILE A 215 42.559 2.375 9.664 1.00 47.62 O ANISOU 1518 O ILE A 215 5235 6167 6689 -279 68 44 O ATOM 1519 CB ILE A 215 44.859 4.873 9.711 1.00 45.29 C ANISOU 1519 CB ILE A 215 4896 5879 6433 -136 193 -111 C ATOM 1520 CG1 ILE A 215 46.162 5.278 9.003 1.00 45.81 C ANISOU 1520 CG1 ILE A 215 4990 5921 6494 -113 220 -192 C ATOM 1521 CG2 ILE A 215 45.219 4.001 10.879 1.00 44.05 C ANISOU 1521 CG2 ILE A 215 4759 5710 6264 -109 186 -132 C ATOM 1522 CD1 ILE A 215 46.840 6.521 9.590 1.00 45.55 C ANISOU 1522 CD1 ILE A 215 4910 5906 6488 -57 271 -232 C ATOM 1523 N LEU A 216 41.793 4.475 9.914 1.00 47.93 N ANISOU 1523 N LEU A 216 5139 6273 6798 -232 137 88 N ATOM 1524 CA LEU A 216 40.627 4.063 10.692 1.00 48.90 C ANISOU 1524 CA LEU A 216 5211 6429 6939 -257 132 167 C ATOM 1525 C LEU A 216 39.810 2.995 9.968 1.00 49.98 C ANISOU 1525 C LEU A 216 5372 6554 7062 -349 54 233 C ATOM 1526 O LEU A 216 39.340 2.045 10.596 1.00 50.06 O ANISOU 1526 O LEU A 216 5392 6568 7059 -385 34 270 O ATOM 1527 CB LEU A 216 39.745 5.264 11.077 1.00 49.12 C ANISOU 1527 CB LEU A 216 5136 6505 7022 -223 182 219 C ATOM 1528 CG LEU A 216 40.209 6.075 12.306 1.00 49.63 C ANISOU 1528 CG LEU A 216 5182 6581 7092 -139 264 176 C ATOM 1529 CD1 LEU A 216 39.151 7.103 12.705 1.00 50.43 C ANISOU 1529 CD1 LEU A 216 5188 6724 7245 -105 317 238 C ATOM 1530 CD2 LEU A 216 40.558 5.199 13.518 1.00 49.00 C ANISOU 1530 CD2 LEU A 216 5148 6490 6978 -129 278 153 C ATOM 1531 N SER A 217 39.660 3.136 8.652 1.00 50.84 N ANISOU 1531 N SER A 217 5505 6644 7167 -395 4 249 N ATOM 1532 CA SER A 217 38.944 2.141 7.866 1.00 51.94 C ANISOU 1532 CA SER A 217 5688 6760 7283 -492 -84 311 C ATOM 1533 C SER A 217 39.599 0.788 8.027 1.00 52.59 C ANISOU 1533 C SER A 217 5881 6796 7305 -512 -112 268 C ATOM 1534 O SER A 217 38.919 -0.183 8.373 1.00 53.35 O ANISOU 1534 O SER A 217 5990 6891 7388 -571 -156 323 O ATOM 1535 CB SER A 217 38.914 2.529 6.401 1.00 52.07 C ANISOU 1535 CB SER A 217 5747 6747 7288 -534 -133 319 C ATOM 1536 OG SER A 217 38.299 3.790 6.264 1.00 52.47 O ANISOU 1536 OG SER A 217 5699 6836 7398 -511 -116 361 O ATOM 1537 N CYS A 218 40.913 0.728 7.799 1.00 52.78 N ANISOU 1537 N CYS A 218 5981 6778 7293 -463 -84 171 N ATOM 1538 CA CYS A 218 41.681 -0.513 8.000 1.00 53.48 C ANISOU 1538 CA CYS A 218 6173 6815 7329 -460 -105 118 C ATOM 1539 C CYS A 218 41.455 -1.117 9.398 1.00 54.15 C ANISOU 1539 C CYS A 218 6239 6917 7418 -447 -98 135 C ATOM 1540 O CYS A 218 41.179 -2.314 9.525 1.00 54.33 O ANISOU 1540 O CYS A 218 6332 6909 7402 -498 -152 160 O ATOM 1541 CB CYS A 218 43.186 -0.277 7.787 1.00 53.11 C ANISOU 1541 CB CYS A 218 6172 6736 7270 -386 -56 10 C ATOM 1542 SG CYS A 218 43.695 0.005 6.081 1.00 53.17 S ANISOU 1542 SG CYS A 218 6255 6700 7246 -412 -58 -26 S ATOM 1543 N TYR A 219 41.572 -0.280 10.433 1.00 54.64 N ANISOU 1543 N TYR A 219 6220 7021 7517 -382 -32 122 N ATOM 1544 CA TYR A 219 41.370 -0.709 11.826 1.00 55.47 C ANISOU 1544 CA TYR A 219 6317 7140 7619 -368 -14 136 C ATOM 1545 C TYR A 219 40.001 -1.372 12.007 1.00 56.19 C ANISOU 1545 C TYR A 219 6385 7254 7709 -454 -52 237 C ATOM 1546 O TYR A 219 39.921 -2.528 12.414 1.00 56.39 O ANISOU 1546 O TYR A 219 6481 7250 7694 -495 -93 249 O ATOM 1547 CB TYR A 219 41.520 0.479 12.791 1.00 55.48 C ANISOU 1547 CB TYR A 219 6240 7183 7657 -294 64 118 C ATOM 1548 CG TYR A 219 41.343 0.117 14.258 1.00 57.88 C ANISOU 1548 CG TYR A 219 6550 7492 7946 -279 90 129 C ATOM 1549 CD1 TYR A 219 40.218 0.539 14.972 1.00 59.75 C ANISOU 1549 CD1 TYR A 219 6712 7779 8209 -293 139 201 C ATOM 1550 CD2 TYR A 219 42.302 -0.666 14.928 1.00 60.37 C ANISOU 1550 CD2 TYR A 219 6954 7760 8223 -251 68 69 C ATOM 1551 CE1 TYR A 219 40.048 0.193 16.315 1.00 61.72 C ANISOU 1551 CE1 TYR A 219 6985 8030 8435 -286 172 211 C ATOM 1552 CE2 TYR A 219 42.149 -1.018 16.271 1.00 61.43 C ANISOU 1552 CE2 TYR A 219 7115 7891 8334 -245 84 80 C ATOM 1553 CZ TYR A 219 41.018 -0.585 16.961 1.00 63.10 C ANISOU 1553 CZ TYR A 219 7263 8152 8561 -266 140 150 C ATOM 1554 OH TYR A 219 40.857 -0.930 18.296 1.00 65.34 O ANISOU 1554 OH TYR A 219 7588 8427 8811 -265 167 161 O ATOM 1555 N CYS A 220 38.940 -0.635 11.676 1.00 56.67 N ANISOU 1555 N CYS A 220 6346 7365 7819 -484 -41 312 N ATOM 1556 CA CYS A 220 37.569 -1.136 11.760 1.00 57.79 C ANISOU 1556 CA CYS A 220 6437 7539 7980 -571 -75 418 C ATOM 1557 C CYS A 220 37.372 -2.509 11.142 1.00 57.71 C ANISOU 1557 C CYS A 220 6527 7481 7918 -666 -172 447 C ATOM 1558 O CYS A 220 36.771 -3.384 11.768 1.00 58.50 O ANISOU 1558 O CYS A 220 6641 7585 8002 -726 -194 499 O ATOM 1559 CB CYS A 220 36.591 -0.167 11.102 1.00 58.23 C ANISOU 1559 CB CYS A 220 6376 7642 8104 -588 -73 490 C ATOM 1560 SG CYS A 220 36.007 1.098 12.232 1.00 61.93 S ANISOU 1560 SG CYS A 220 6703 8183 8644 -510 41 517 S ATOM 1561 N ILE A 221 37.868 -2.705 9.923 1.00 56.87 N ANISOU 1561 N ILE A 221 6501 7325 7780 -686 -229 414 N ATOM 1562 CA ILE A 221 37.628 -3.971 9.226 1.00 56.78 C ANISOU 1562 CA ILE A 221 6602 7259 7713 -781 -326 445 C ATOM 1563 C ILE A 221 38.374 -5.122 9.901 1.00 56.07 C ANISOU 1563 C ILE A 221 6630 7115 7559 -766 -337 390 C ATOM 1564 O ILE A 221 37.851 -6.231 9.988 1.00 56.51 O ANISOU 1564 O ILE A 221 6752 7143 7575 -849 -404 439 O ATOM 1565 CB ILE A 221 37.980 -3.906 7.716 1.00 56.84 C ANISOU 1565 CB ILE A 221 6691 7215 7690 -806 -378 421 C ATOM 1566 CG1 ILE A 221 37.365 -2.653 7.076 1.00 57.23 C ANISOU 1566 CG1 ILE A 221 6631 7310 7801 -809 -370 467 C ATOM 1567 CG2 ILE A 221 37.489 -5.172 7.004 1.00 57.24 C ANISOU 1567 CG2 ILE A 221 6861 7207 7680 -920 -488 471 C ATOM 1568 CD1 ILE A 221 37.003 -2.802 5.610 1.00 58.46 C ANISOU 1568 CD1 ILE A 221 6860 7422 7930 -893 -461 504 C ATOM 1569 N ILE A 222 39.578 -4.847 10.401 1.00 54.85 N ANISOU 1569 N ILE A 222 6498 6943 7398 -663 -279 293 N ATOM 1570 CA ILE A 222 40.386 -5.870 11.072 1.00 54.30 C ANISOU 1570 CA ILE A 222 6536 6818 7277 -634 -295 236 C ATOM 1571 C ILE A 222 39.708 -6.415 12.347 1.00 54.70 C ANISOU 1571 C ILE A 222 6573 6889 7319 -670 -295 290 C ATOM 1572 O ILE A 222 39.589 -7.636 12.511 1.00 54.71 O ANISOU 1572 O ILE A 222 6678 6841 7265 -726 -359 307 O ATOM 1573 CB ILE A 222 41.806 -5.354 11.388 1.00 53.36 C ANISOU 1573 CB ILE A 222 6421 6682 7169 -515 -237 127 C ATOM 1574 CG1 ILE A 222 42.583 -5.139 10.088 1.00 53.19 C ANISOU 1574 CG1 ILE A 222 6445 6624 7140 -490 -237 68 C ATOM 1575 CG2 ILE A 222 42.558 -6.343 12.258 1.00 52.56 C ANISOU 1575 CG2 ILE A 222 6413 6526 7029 -479 -260 78 C ATOM 1576 CD1 ILE A 222 43.918 -4.408 10.253 1.00 52.12 C ANISOU 1576 CD1 ILE A 222 6281 6486 7033 -381 -172 -29 C ATOM 1577 N ILE A 223 39.242 -5.526 13.228 1.00 54.47 N ANISOU 1577 N ILE A 223 6429 6928 7339 -643 -223 319 N ATOM 1578 CA ILE A 223 38.662 -5.974 14.499 1.00 55.01 C ANISOU 1578 CA ILE A 223 6491 7014 7393 -673 -204 364 C ATOM 1579 C ILE A 223 37.407 -6.793 14.219 1.00 55.62 C ANISOU 1579 C ILE A 223 6569 7103 7460 -801 -263 469 C ATOM 1580 O ILE A 223 37.088 -7.728 14.951 1.00 56.10 O ANISOU 1580 O ILE A 223 6691 7145 7478 -857 -287 500 O ATOM 1581 CB ILE A 223 38.378 -4.807 15.525 1.00 55.04 C ANISOU 1581 CB ILE A 223 6380 7085 7447 -615 -98 373 C ATOM 1582 CG1 ILE A 223 37.171 -3.961 15.119 1.00 56.02 C ANISOU 1582 CG1 ILE A 223 6361 7283 7639 -649 -63 458 C ATOM 1583 CG2 ILE A 223 39.620 -3.914 15.731 1.00 54.32 C ANISOU 1583 CG2 ILE A 223 6290 6982 7368 -498 -51 274 C ATOM 1584 CD1 ILE A 223 35.846 -4.446 15.707 1.00 58.40 C ANISOU 1584 CD1 ILE A 223 6609 7627 7953 -739 -53 563 C ATOM 1585 N SER A 224 36.713 -6.445 13.143 1.00 55.71 N ANISOU 1585 N SER A 224 6517 7140 7508 -854 -295 524 N ATOM 1586 CA SER A 224 35.583 -7.233 12.672 1.00 56.46 C ANISOU 1586 CA SER A 224 6616 7238 7596 -985 -374 626 C ATOM 1587 C SER A 224 36.033 -8.626 12.252 1.00 56.70 C ANISOU 1587 C SER A 224 6826 7178 7539 -1041 -472 603 C ATOM 1588 O SER A 224 35.353 -9.598 12.537 1.00 57.15 O ANISOU 1588 O SER A 224 6929 7221 7562 -1140 -526 669 O ATOM 1589 CB SER A 224 34.878 -6.530 11.513 1.00 56.53 C ANISOU 1589 CB SER A 224 6533 7281 7662 -1024 -405 684 C ATOM 1590 OG SER A 224 34.204 -7.466 10.698 1.00 57.79 O ANISOU 1590 OG SER A 224 6757 7407 7792 -1151 -518 756 O ATOM 1591 N LYS A 225 37.171 -8.716 11.569 1.00 56.56 N ANISOU 1591 N LYS A 225 6909 7095 7483 -976 -490 510 N ATOM 1592 CA LYS A 225 37.732 -10.016 11.186 1.00 57.21 C ANISOU 1592 CA LYS A 225 7174 7081 7480 -1005 -572 474 C ATOM 1593 C LYS A 225 38.276 -10.770 12.395 1.00 57.65 C ANISOU 1593 C LYS A 225 7308 7101 7494 -970 -563 434 C ATOM 1594 O LYS A 225 38.155 -11.998 12.474 1.00 58.20 O ANISOU 1594 O LYS A 225 7507 7107 7495 -1036 -639 453 O ATOM 1595 CB LYS A 225 38.853 -9.851 10.159 1.00 56.70 C ANISOU 1595 CB LYS A 225 7189 6959 7395 -932 -572 380 C ATOM 1596 CG LYS A 225 39.392 -11.169 9.593 1.00 57.32 C ANISOU 1596 CG LYS A 225 7463 6930 7386 -957 -651 343 C ATOM 1597 CD LYS A 225 38.436 -11.787 8.572 1.00 59.08 C ANISOU 1597 CD LYS A 225 7759 7119 7566 -1093 -750 427 C ATOM 1598 CE LYS A 225 38.693 -13.279 8.374 1.00 60.35 C ANISOU 1598 CE LYS A 225 8125 7173 7630 -1139 -836 413 C ATOM 1599 NZ LYS A 225 39.976 -13.548 7.681 1.00 59.97 N ANISOU 1599 NZ LYS A 225 8208 7040 7538 -1045 -821 303 N ATOM 1600 N LEU A 226 38.891 -10.037 13.325 1.00 57.45 N ANISOU 1600 N LEU A 226 7217 7108 7503 -868 -480 378 N ATOM 1601 CA LEU A 226 39.479 -10.656 14.505 1.00 57.60 C ANISOU 1601 CA LEU A 226 7314 7088 7482 -828 -478 337 C ATOM 1602 C LEU A 226 38.412 -11.425 15.273 1.00 58.55 C ANISOU 1602 C LEU A 226 7457 7220 7570 -938 -505 428 C ATOM 1603 O LEU A 226 38.659 -12.550 15.711 1.00 59.40 O ANISOU 1603 O LEU A 226 7701 7258 7609 -965 -564 418 O ATOM 1604 CB LEU A 226 40.175 -9.620 15.405 1.00 56.94 C ANISOU 1604 CB LEU A 226 7149 7041 7442 -714 -388 277 C ATOM 1605 CG LEU A 226 41.532 -9.047 14.923 1.00 56.77 C ANISOU 1605 CG LEU A 226 7130 6994 7445 -597 -366 172 C ATOM 1606 CD1 LEU A 226 42.223 -8.235 16.026 1.00 56.14 C ANISOU 1606 CD1 LEU A 226 6997 6936 7395 -502 -300 119 C ATOM 1607 CD2 LEU A 226 42.504 -10.125 14.405 1.00 56.67 C ANISOU 1607 CD2 LEU A 226 7263 6885 7384 -568 -435 105 C ATOM 1608 N SER A 227 37.218 -10.847 15.403 1.00 58.78 N ANISOU 1608 N SER A 227 7352 7332 7648 -1004 -463 518 N ATOM 1609 CA SER A 227 36.166 -11.470 16.201 1.00 59.44 C ANISOU 1609 CA SER A 227 7432 7439 7711 -1111 -468 609 C ATOM 1610 C SER A 227 35.466 -12.579 15.434 1.00 60.36 C ANISOU 1610 C SER A 227 7630 7518 7786 -1247 -578 681 C ATOM 1611 O SER A 227 34.973 -13.533 16.033 1.00 61.19 O ANISOU 1611 O SER A 227 7808 7600 7839 -1338 -615 733 O ATOM 1612 CB SER A 227 35.163 -10.432 16.696 1.00 59.43 C ANISOU 1612 CB SER A 227 7248 7544 7789 -1122 -369 680 C ATOM 1613 OG SER A 227 34.331 -10.025 15.649 1.00 59.47 O ANISOU 1613 OG SER A 227 7147 7596 7853 -1180 -393 749 O ATOM 1614 N HIS A 228 35.427 -12.471 14.114 1.00 60.67 N ANISOU 1614 N HIS A 228 7670 7542 7837 -1267 -634 686 N ATOM 1615 CA HIS A 228 34.931 -13.577 13.288 1.00 61.82 C ANISOU 1615 CA HIS A 228 7930 7630 7926 -1392 -754 743 C ATOM 1616 C HIS A 228 35.885 -14.766 13.349 1.00 61.85 C ANISOU 1616 C HIS A 228 8150 7519 7832 -1370 -821 670 C ATOM 1617 O HIS A 228 35.448 -15.905 13.275 1.00 62.55 O ANISOU 1617 O HIS A 228 8360 7552 7853 -1479 -911 720 O ATOM 1618 CB HIS A 228 34.730 -13.150 11.834 1.00 61.91 C ANISOU 1618 CB HIS A 228 7915 7641 7965 -1416 -801 760 C ATOM 1619 CG HIS A 228 34.107 -14.209 10.973 1.00 64.05 C ANISOU 1619 CG HIS A 228 8305 7851 8177 -1559 -932 829 C ATOM 1620 ND1 HIS A 228 34.853 -15.138 10.276 1.00 65.44 N ANISOU 1620 ND1 HIS A 228 8689 7914 8261 -1557 -1010 770 N ATOM 1621 CD2 HIS A 228 32.811 -14.483 10.689 1.00 66.03 C ANISOU 1621 CD2 HIS A 228 8501 8137 8449 -1708 -1000 954 C ATOM 1622 CE1 HIS A 228 34.044 -15.939 9.606 1.00 66.09 C ANISOU 1622 CE1 HIS A 228 8854 7957 8300 -1703 -1124 855 C ATOM 1623 NE2 HIS A 228 32.800 -15.562 9.838 1.00 66.90 N ANISOU 1623 NE2 HIS A 228 8795 8150 8473 -1801 -1126 970 N ATOM 1624 N ASN A1002 37.183 -14.511 13.478 1.00 58.00 N ANISOU 1624 N ASN A1002 7295 8061 6680 -1507 -875 1189 N ATOM 1625 CA ASN A1002 38.132 -15.602 13.632 1.00 57.91 C ANISOU 1625 CA ASN A1002 7305 8141 6557 -1436 -679 1034 C ATOM 1626 C ASN A1002 37.853 -16.400 14.906 1.00 56.81 C ANISOU 1626 C ASN A1002 7288 7772 6522 -1243 -565 836 C ATOM 1627 O ASN A1002 37.847 -17.634 14.890 1.00 56.76 O ANISOU 1627 O ASN A1002 7321 7797 6446 -1182 -387 659 O ATOM 1628 CB ASN A1002 39.569 -15.084 13.624 1.00 58.58 C ANISOU 1628 CB ASN A1002 7315 8321 6621 -1473 -725 1169 C ATOM 1629 CG ASN A1002 40.050 -14.690 12.238 1.00 60.07 C ANISOU 1629 CG ASN A1002 7355 8833 6634 -1677 -778 1342 C ATOM 1630 OD1 ASN A1002 39.475 -15.085 11.223 1.00 61.19 O ANISOU 1630 OD1 ASN A1002 7444 9178 6624 -1781 -730 1312 O ATOM 1631 ND2 ASN A1002 41.118 -13.911 12.193 1.00 60.06 N ANISOU 1631 ND2 ASN A1002 7273 8909 6638 -1749 -881 1530 N ATOM 1632 N ILE A1003 37.598 -15.697 16.003 1.00 56.34 N ANISOU 1632 N ILE A1003 7279 7489 6637 -1155 -674 864 N ATOM 1633 CA ILE A1003 37.208 -16.358 17.241 1.00 55.48 C ANISOU 1633 CA ILE A1003 7263 7204 6611 -995 -587 703 C ATOM 1634 C ILE A1003 36.013 -17.267 16.960 1.00 55.75 C ANISOU 1634 C ILE A1003 7346 7242 6595 -989 -489 571 C ATOM 1635 O ILE A1003 36.039 -18.440 17.307 1.00 55.36 O ANISOU 1635 O ILE A1003 7345 7169 6518 -913 -334 432 O ATOM 1636 CB ILE A1003 36.853 -15.342 18.364 1.00 55.08 C ANISOU 1636 CB ILE A1003 7236 6954 6738 -922 -735 728 C ATOM 1637 CG1 ILE A1003 38.077 -14.494 18.764 1.00 55.66 C ANISOU 1637 CG1 ILE A1003 7269 7007 6873 -933 -831 837 C ATOM 1638 CG2 ILE A1003 36.340 -16.061 19.590 1.00 53.56 C ANISOU 1638 CG2 ILE A1003 7113 6645 6591 -779 -643 569 C ATOM 1639 CD1 ILE A1003 37.727 -13.155 19.409 1.00 55.94 C ANISOU 1639 CD1 ILE A1003 7295 6862 7096 -921 -1030 883 C ATOM 1640 N PHE A1004 34.989 -16.728 16.296 1.00 56.85 N ANISOU 1640 N PHE A1004 7459 7410 6730 -1079 -588 631 N ATOM 1641 CA PHE A1004 33.764 -17.483 15.977 1.00 57.18 C ANISOU 1641 CA PHE A1004 7536 7473 6716 -1096 -514 522 C ATOM 1642 C PHE A1004 34.028 -18.779 15.225 1.00 57.83 C ANISOU 1642 C PHE A1004 7625 7699 6648 -1142 -334 393 C ATOM 1643 O PHE A1004 33.367 -19.779 15.481 1.00 57.76 O ANISOU 1643 O PHE A1004 7677 7633 6633 -1099 -225 247 O ATOM 1644 CB PHE A1004 32.787 -16.622 15.167 1.00 58.06 C ANISOU 1644 CB PHE A1004 7585 7646 6827 -1211 -659 647 C ATOM 1645 CG PHE A1004 31.641 -17.396 14.564 1.00 59.29 C ANISOU 1645 CG PHE A1004 7754 7892 6881 -1273 -584 556 C ATOM 1646 CD1 PHE A1004 30.501 -17.677 15.310 1.00 60.24 C ANISOU 1646 CD1 PHE A1004 7930 7887 7071 -1190 -573 463 C ATOM 1647 CD2 PHE A1004 31.694 -17.838 13.249 1.00 61.15 C ANISOU 1647 CD2 PHE A1004 7931 8367 6935 -1427 -525 559 C ATOM 1648 CE1 PHE A1004 29.421 -18.402 14.750 1.00 60.93 C ANISOU 1648 CE1 PHE A1004 8025 8065 7058 -1264 -509 386 C ATOM 1649 CE2 PHE A1004 30.631 -18.559 12.689 1.00 62.63 C ANISOU 1649 CE2 PHE A1004 8126 8648 7020 -1501 -458 461 C ATOM 1650 CZ PHE A1004 29.493 -18.842 13.442 1.00 61.44 C ANISOU 1650 CZ PHE A1004 8042 8349 6951 -1420 -453 382 C ATOM 1651 N GLU A1005 34.971 -18.747 14.288 1.00 59.07 N ANISOU 1651 N GLU A1005 7707 8049 6688 -1234 -309 441 N ATOM 1652 CA GLU A1005 35.332 -19.929 13.519 1.00 60.22 C ANISOU 1652 CA GLU A1005 7837 8349 6695 -1272 -136 282 C ATOM 1653 C GLU A1005 36.123 -20.890 14.377 1.00 59.80 C ANISOU 1653 C GLU A1005 7841 8161 6717 -1117 3 150 C ATOM 1654 O GLU A1005 36.102 -22.089 14.146 1.00 60.51 O ANISOU 1654 O GLU A1005 7955 8253 6780 -1091 154 -30 O ATOM 1655 CB GLU A1005 36.154 -19.559 12.279 1.00 61.86 C ANISOU 1655 CB GLU A1005 7918 8851 6735 -1417 -151 368 C ATOM 1656 CG GLU A1005 35.362 -18.846 11.171 1.00 64.11 C ANISOU 1656 CG GLU A1005 8115 9337 6905 -1607 -270 504 C ATOM 1657 CD GLU A1005 34.236 -19.698 10.573 1.00 66.86 C ANISOU 1657 CD GLU A1005 8485 9763 7155 -1675 -182 342 C ATOM 1658 OE1 GLU A1005 34.322 -20.950 10.625 1.00 68.31 O ANISOU 1658 OE1 GLU A1005 8722 9919 7313 -1616 -7 100 O ATOM 1659 OE2 GLU A1005 33.253 -19.112 10.050 1.00 68.65 O ANISOU 1659 OE2 GLU A1005 8668 10069 7345 -1792 -295 461 O ATOM 1660 N MET A1006 36.832 -20.367 15.364 1.00 59.27 N ANISOU 1660 N MET A1006 7786 7975 6758 -1017 -52 244 N ATOM 1661 CA MET A1006 37.649 -21.207 16.228 1.00 59.22 C ANISOU 1661 CA MET A1006 7813 7858 6828 -873 64 163 C ATOM 1662 C MET A1006 36.753 -22.089 17.099 1.00 58.80 C ANISOU 1662 C MET A1006 7851 7612 6875 -781 129 54 C ATOM 1663 O MET A1006 36.906 -23.306 17.127 1.00 59.19 O ANISOU 1663 O MET A1006 7925 7609 6954 -724 269 -76 O ATOM 1664 CB MET A1006 38.573 -20.335 17.091 1.00 58.63 C ANISOU 1664 CB MET A1006 7715 7733 6825 -813 -28 306 C ATOM 1665 CG MET A1006 39.604 -21.090 17.911 1.00 57.59 C ANISOU 1665 CG MET A1006 7586 7538 6755 -678 79 268 C ATOM 1666 SD MET A1006 40.363 -20.003 19.123 1.00 54.93 S ANISOU 1666 SD MET A1006 7233 7135 6501 -624 -49 424 S ATOM 1667 CE MET A1006 41.393 -21.176 19.985 1.00 55.09 C ANISOU 1667 CE MET A1006 7242 7108 6578 -472 100 381 C ATOM 1668 N LEU A1007 35.805 -21.475 17.794 1.00 58.46 N ANISOU 1668 N LEU A1007 7848 7468 6895 -769 23 109 N ATOM 1669 CA LEU A1007 34.897 -22.230 18.668 1.00 58.44 C ANISOU 1669 CA LEU A1007 7914 7322 6969 -700 70 31 C ATOM 1670 C LEU A1007 33.922 -23.081 17.861 1.00 59.30 C ANISOU 1670 C LEU A1007 8051 7458 7020 -780 144 -87 C ATOM 1671 O LEU A1007 33.388 -24.063 18.373 1.00 59.08 O ANISOU 1671 O LEU A1007 8074 7321 7051 -739 219 -167 O ATOM 1672 CB LEU A1007 34.136 -21.308 19.624 1.00 57.50 C ANISOU 1672 CB LEU A1007 7804 7129 6914 -664 -60 98 C ATOM 1673 CG LEU A1007 35.026 -20.719 20.717 1.00 56.97 C ANISOU 1673 CG LEU A1007 7716 7012 6917 -573 -113 169 C ATOM 1674 CD1 LEU A1007 35.697 -19.473 20.221 1.00 57.46 C ANISOU 1674 CD1 LEU A1007 7727 7136 6970 -629 -232 275 C ATOM 1675 CD2 LEU A1007 34.223 -20.411 21.955 1.00 57.37 C ANISOU 1675 CD2 LEU A1007 7777 6988 7030 -505 -174 155 C ATOM 1676 N ARG A1008 33.708 -22.703 16.602 1.00 60.50 N ANISOU 1676 N ARG A1008 8160 7769 7055 -909 115 -87 N ATOM 1677 CA ARG A1008 32.980 -23.538 15.651 1.00 61.78 C ANISOU 1677 CA ARG A1008 8332 8009 7132 -1010 197 -222 C ATOM 1678 C ARG A1008 33.609 -24.927 15.543 1.00 62.66 C ANISOU 1678 C ARG A1008 8466 8065 7278 -960 365 -393 C ATOM 1679 O ARG A1008 32.900 -25.929 15.588 1.00 62.97 O ANISOU 1679 O ARG A1008 8556 8010 7357 -970 440 -518 O ATOM 1680 CB ARG A1008 32.958 -22.889 14.270 1.00 62.82 C ANISOU 1680 CB ARG A1008 8380 8382 7104 -1167 145 -177 C ATOM 1681 CG ARG A1008 31.942 -23.490 13.339 1.00 64.87 C ANISOU 1681 CG ARG A1008 8638 8754 7254 -1298 192 -295 C ATOM 1682 CD ARG A1008 32.156 -23.008 11.925 1.00 67.56 C ANISOU 1682 CD ARG A1008 8870 9392 7407 -1465 163 -257 C ATOM 1683 NE ARG A1008 31.074 -23.454 11.051 1.00 69.43 N ANISOU 1683 NE ARG A1008 9091 9768 7521 -1612 188 -352 N ATOM 1684 CZ ARG A1008 30.771 -22.896 9.882 1.00 70.82 C ANISOU 1684 CZ ARG A1008 9161 10227 7521 -1790 123 -272 C ATOM 1685 NH1 ARG A1008 31.465 -21.855 9.430 1.00 70.84 N ANISOU 1685 NH1 ARG A1008 9062 10392 7460 -1848 21 -78 N ATOM 1686 NH2 ARG A1008 29.761 -23.379 9.164 1.00 71.76 N ANISOU 1686 NH2 ARG A1008 9265 10477 7522 -1925 153 -370 N ATOM 1687 N ILE A1009 34.932 -24.981 15.401 1.00 63.27 N ANISOU 1687 N ILE A1009 8495 8191 7353 -906 418 -397 N ATOM 1688 CA ILE A1009 35.643 -26.256 15.339 1.00 64.50 C ANISOU 1688 CA ILE A1009 8653 8274 7579 -828 574 -563 C ATOM 1689 C ILE A1009 35.649 -26.949 16.703 1.00 64.31 C ANISOU 1689 C ILE A1009 8693 7992 7748 -686 603 -535 C ATOM 1690 O ILE A1009 35.280 -28.115 16.802 1.00 65.11 O ANISOU 1690 O ILE A1009 8838 7949 7952 -663 691 -661 O ATOM 1691 CB ILE A1009 37.102 -26.092 14.827 1.00 65.32 C ANISOU 1691 CB ILE A1009 8663 8530 7624 -798 623 -567 C ATOM 1692 CG1 ILE A1009 37.108 -25.710 13.345 1.00 66.38 C ANISOU 1692 CG1 ILE A1009 8709 8965 7546 -961 622 -624 C ATOM 1693 CG2 ILE A1009 37.906 -27.379 15.035 1.00 65.92 C ANISOU 1693 CG2 ILE A1009 8734 8480 7832 -668 774 -724 C ATOM 1694 CD1 ILE A1009 38.484 -25.747 12.695 1.00 67.89 C ANISOU 1694 CD1 ILE A1009 8784 9358 7649 -947 695 -670 C ATOM 1695 N ASP A1010 36.051 -26.226 17.744 1.00 63.60 N ANISOU 1695 N ASP A1010 8600 7855 7710 -605 521 -365 N ATOM 1696 CA ASP A1010 36.255 -26.816 19.066 1.00 63.60 C ANISOU 1696 CA ASP A1010 8627 7671 7866 -478 544 -306 C ATOM 1697 C ASP A1010 34.943 -27.191 19.751 1.00 63.81 C ANISOU 1697 C ASP A1010 8716 7581 7948 -498 515 -299 C ATOM 1698 O ASP A1010 34.724 -28.353 20.078 1.00 64.53 O ANISOU 1698 O ASP A1010 8836 7525 8157 -465 589 -351 O ATOM 1699 CB ASP A1010 37.068 -25.861 19.946 1.00 62.61 C ANISOU 1699 CB ASP A1010 8463 7579 7746 -409 462 -141 C ATOM 1700 CG ASP A1010 38.548 -25.814 19.556 1.00 63.29 C ANISOU 1700 CG ASP A1010 8478 7754 7816 -362 512 -129 C ATOM 1701 OD1 ASP A1010 39.025 -26.779 18.934 1.00 64.90 O ANISOU 1701 OD1 ASP A1010 8659 7946 8053 -332 634 -255 O ATOM 1702 OD2 ASP A1010 39.248 -24.829 19.878 1.00 61.87 O ANISOU 1702 OD2 ASP A1010 8256 7656 7596 -354 432 -4 O ATOM 1703 N GLU A1011 34.071 -26.208 19.946 1.00 63.77 N ANISOU 1703 N GLU A1011 8719 7642 7866 -553 402 -230 N ATOM 1704 CA GLU A1011 32.800 -26.401 20.661 1.00 64.02 C ANISOU 1704 CA GLU A1011 8788 7612 7925 -571 362 -211 C ATOM 1705 C GLU A1011 31.658 -26.845 19.731 1.00 64.67 C ANISOU 1705 C GLU A1011 8903 7720 7947 -692 385 -321 C ATOM 1706 O GLU A1011 30.657 -27.391 20.192 1.00 64.82 O ANISOU 1706 O GLU A1011 8952 7677 7998 -717 384 -328 O ATOM 1707 CB GLU A1011 32.408 -25.096 21.374 1.00 63.30 C ANISOU 1707 CB GLU A1011 8670 7586 7793 -554 229 -109 C ATOM 1708 CG GLU A1011 31.358 -25.228 22.494 1.00 64.77 C ANISOU 1708 CG GLU A1011 8859 7743 8005 -532 190 -77 C ATOM 1709 CD GLU A1011 31.942 -25.097 23.909 1.00 67.35 C ANISOU 1709 CD GLU A1011 9146 8058 8384 -432 169 13 C ATOM 1710 OE1 GLU A1011 32.747 -24.157 24.159 1.00 68.20 O ANISOU 1710 OE1 GLU A1011 9220 8210 8483 -387 110 55 O ATOM 1711 OE2 GLU A1011 31.576 -25.931 24.779 1.00 69.30 O ANISOU 1711 OE2 GLU A1011 9386 8268 8676 -413 203 50 O ATOM 1712 N GLY A1012 31.791 -26.588 18.431 1.00 65.49 N ANISOU 1712 N GLY A1012 8990 7945 7948 -780 398 -396 N ATOM 1713 CA GLY A1012 30.771 -26.995 17.451 1.00 66.40 C ANISOU 1713 CA GLY A1012 9121 8124 7981 -915 421 -508 C ATOM 1714 C GLY A1012 29.581 -26.054 17.273 1.00 65.81 C ANISOU 1714 C GLY A1012 9032 8161 7812 -998 304 -434 C ATOM 1715 O GLY A1012 28.979 -25.598 18.257 1.00 64.76 O ANISOU 1715 O GLY A1012 8903 7981 7723 -944 227 -342 O ATOM 1716 N LEU A1013 29.233 -25.796 16.009 1.00 66.61 N ANISOU 1716 N LEU A1013 9100 8428 7781 -1132 292 -478 N ATOM 1717 CA LEU A1013 28.054 -25.003 15.648 1.00 66.59 C ANISOU 1717 CA LEU A1013 9065 8542 7693 -1225 184 -403 C ATOM 1718 C LEU A1013 26.783 -25.868 15.555 1.00 67.60 C ANISOU 1718 C LEU A1013 9229 8658 7798 -1311 222 -493 C ATOM 1719 O LEU A1013 26.744 -26.851 14.805 1.00 68.31 O ANISOU 1719 O LEU A1013 9338 8771 7844 -1403 321 -645 O ATOM 1720 CB LEU A1013 28.294 -24.293 14.313 1.00 67.16 C ANISOU 1720 CB LEU A1013 9060 8834 7622 -1349 140 -366 C ATOM 1721 CG LEU A1013 27.157 -23.445 13.740 1.00 66.72 C ANISOU 1721 CG LEU A1013 8946 8922 7481 -1460 19 -258 C ATOM 1722 CD1 LEU A1013 26.869 -22.278 14.646 1.00 65.63 C ANISOU 1722 CD1 LEU A1013 8791 8691 7453 -1355 -122 -99 C ATOM 1723 CD2 LEU A1013 27.495 -22.957 12.342 1.00 67.27 C ANISOU 1723 CD2 LEU A1013 8921 9242 7393 -1611 -11 -210 C ATOM 1724 N ARG A1014 25.749 -25.473 16.307 1.00 67.61 N ANISOU 1724 N ARG A1014 9228 8633 7826 -1284 141 -409 N ATOM 1725 CA ARG A1014 24.452 -26.167 16.337 1.00 68.71 C ANISOU 1725 CA ARG A1014 9387 8782 7937 -1369 157 -459 C ATOM 1726 C ARG A1014 23.320 -25.247 15.919 1.00 68.60 C ANISOU 1726 C ARG A1014 9307 8926 7831 -1441 44 -370 C ATOM 1727 O ARG A1014 22.885 -24.411 16.704 1.00 67.78 O ANISOU 1727 O ARG A1014 9167 8808 7777 -1350 -50 -269 O ATOM 1728 CB ARG A1014 24.145 -26.674 17.747 1.00 68.57 C ANISOU 1728 CB ARG A1014 9403 8618 8030 -1271 167 -429 C ATOM 1729 CG ARG A1014 24.926 -27.903 18.153 1.00 70.89 C ANISOU 1729 CG ARG A1014 9757 8740 8437 -1230 278 -503 C ATOM 1730 CD ARG A1014 24.344 -29.156 17.538 1.00 74.65 C ANISOU 1730 CD ARG A1014 10275 9174 8913 -1362 357 -634 C ATOM 1731 NE ARG A1014 25.342 -30.221 17.446 1.00 77.90 N ANISOU 1731 NE ARG A1014 10731 9417 9449 -1327 465 -745 N ATOM 1732 CZ ARG A1014 25.064 -31.513 17.261 1.00 80.84 C ANISOU 1732 CZ ARG A1014 11150 9655 9911 -1401 538 -866 C ATOM 1733 NH1 ARG A1014 26.060 -32.396 17.194 1.00 82.45 N ANISOU 1733 NH1 ARG A1014 11379 9682 10264 -1340 629 -970 N ATOM 1734 NH2 ARG A1014 23.802 -31.936 17.145 1.00 81.52 N ANISOU 1734 NH2 ARG A1014 11248 9770 9954 -1534 515 -884 N ATOM 1735 N LEU A1015 22.818 -25.422 14.701 1.00 69.71 N ANISOU 1735 N LEU A1015 9419 9226 7841 -1604 54 -416 N ATOM 1736 CA LEU A1015 21.745 -24.566 14.190 1.00 69.90 C ANISOU 1736 CA LEU A1015 9361 9419 7778 -1684 -57 -307 C ATOM 1737 C LEU A1015 20.334 -25.015 14.605 1.00 70.08 C ANISOU 1737 C LEU A1015 9382 9460 7782 -1727 -68 -317 C ATOM 1738 O LEU A1015 19.364 -24.317 14.313 1.00 70.33 O ANISOU 1738 O LEU A1015 9335 9626 7758 -1773 -163 -219 O ATOM 1739 CB LEU A1015 21.850 -24.446 12.668 1.00 71.15 C ANISOU 1739 CB LEU A1015 9458 9797 7777 -1859 -56 -318 C ATOM 1740 CG LEU A1015 23.074 -23.658 12.187 1.00 70.82 C ANISOU 1740 CG LEU A1015 9372 9809 7728 -1835 -90 -242 C ATOM 1741 CD1 LEU A1015 23.425 -24.005 10.748 1.00 72.55 C ANISOU 1741 CD1 LEU A1015 9536 10265 7763 -2018 -32 -320 C ATOM 1742 CD2 LEU A1015 22.843 -22.167 12.333 1.00 70.05 C ANISOU 1742 CD2 LEU A1015 9192 9734 7689 -1782 -260 -21 C ATOM 1743 N LYS A1016 20.224 -26.164 15.279 1.00 70.20 N ANISOU 1743 N LYS A1016 9473 9346 7853 -1717 21 -415 N ATOM 1744 CA LYS A1016 18.947 -26.659 15.817 1.00 70.37 C ANISOU 1744 CA LYS A1016 9488 9386 7860 -1762 11 -408 C ATOM 1745 C LYS A1016 19.090 -26.870 17.309 1.00 69.62 C ANISOU 1745 C LYS A1016 9419 9143 7888 -1615 18 -372 C ATOM 1746 O LYS A1016 20.146 -27.285 17.768 1.00 69.39 O ANISOU 1746 O LYS A1016 9446 8962 7956 -1534 78 -404 O ATOM 1747 CB LYS A1016 18.568 -27.992 15.169 1.00 71.66 C ANISOU 1747 CB LYS A1016 9704 9550 7970 -1936 104 -548 C ATOM 1748 CG LYS A1016 18.498 -27.968 13.635 1.00 73.24 C ANISOU 1748 CG LYS A1016 9870 9937 8018 -2110 118 -623 C ATOM 1749 CD LYS A1016 17.994 -29.293 13.055 1.00 74.89 C ANISOU 1749 CD LYS A1016 10126 10150 8179 -2293 204 -796 C ATOM 1750 CE LYS A1016 17.979 -29.278 11.531 1.00 76.31 C ANISOU 1750 CE LYS A1016 10254 10561 8179 -2478 226 -898 C ATOM 1751 NZ LYS A1016 19.358 -29.273 10.960 1.00 76.92 N ANISOU 1751 NZ LYS A1016 10341 10625 8261 -2440 295 -1004 N ATOM 1752 N ILE A1017 18.038 -26.604 18.074 1.00 69.63 N ANISOU 1752 N ILE A1017 9363 9215 7876 -1585 -42 -302 N ATOM 1753 CA ILE A1017 18.079 -26.877 19.515 1.00 69.47 C ANISOU 1753 CA ILE A1017 9342 9117 7937 -1474 -34 -265 C ATOM 1754 C ILE A1017 18.523 -28.324 19.793 1.00 70.70 C ANISOU 1754 C ILE A1017 9582 9114 8165 -1530 65 -313 C ATOM 1755 O ILE A1017 18.096 -29.272 19.122 1.00 72.10 O ANISOU 1755 O ILE A1017 9802 9273 8318 -1682 113 -380 O ATOM 1756 CB ILE A1017 16.726 -26.610 20.198 1.00 69.51 C ANISOU 1756 CB ILE A1017 9254 9273 7882 -1470 -98 -206 C ATOM 1757 CG1 ILE A1017 16.441 -25.105 20.244 1.00 68.95 C ANISOU 1757 CG1 ILE A1017 9086 9303 7808 -1353 -206 -164 C ATOM 1758 CG2 ILE A1017 16.719 -27.191 21.604 1.00 68.74 C ANISOU 1758 CG2 ILE A1017 9144 9141 7830 -1409 -74 -168 C ATOM 1759 CD1 ILE A1017 15.084 -24.738 20.873 1.00 69.23 C ANISOU 1759 CD1 ILE A1017 9003 9510 7788 -1325 -269 -131 C ATOM 1760 N TYR A1018 19.370 -28.482 20.801 1.00 70.75 N ANISOU 1760 N TYR A1018 9603 9003 8273 -1410 87 -274 N ATOM 1761 CA TYR A1018 20.122 -29.711 21.011 1.00 71.84 C ANISOU 1761 CA TYR A1018 9814 8950 8531 -1427 172 -299 C ATOM 1762 C TYR A1018 20.087 -30.081 22.493 1.00 71.85 C ANISOU 1762 C TYR A1018 9776 8927 8596 -1361 159 -180 C ATOM 1763 O TYR A1018 20.292 -29.221 23.348 1.00 71.37 O ANISOU 1763 O TYR A1018 9651 8951 8513 -1238 111 -118 O ATOM 1764 CB TYR A1018 21.554 -29.440 20.548 1.00 71.63 C ANISOU 1764 CB TYR A1018 9829 8822 8566 -1341 214 -354 C ATOM 1765 CG TYR A1018 22.525 -30.583 20.669 1.00 73.88 C ANISOU 1765 CG TYR A1018 10175 8896 9000 -1323 304 -394 C ATOM 1766 CD1 TYR A1018 23.695 -30.454 21.423 1.00 75.12 C ANISOU 1766 CD1 TYR A1018 10326 8962 9253 -1181 318 -330 C ATOM 1767 CD2 TYR A1018 22.299 -31.784 20.010 1.00 76.93 C ANISOU 1767 CD2 TYR A1018 10617 9167 9446 -1446 370 -502 C ATOM 1768 CE1 TYR A1018 24.613 -31.513 21.530 1.00 76.74 C ANISOU 1768 CE1 TYR A1018 10571 8964 9620 -1149 397 -354 C ATOM 1769 CE2 TYR A1018 23.207 -32.849 20.108 1.00 79.01 C ANISOU 1769 CE2 TYR A1018 10926 9201 9891 -1412 447 -552 C ATOM 1770 CZ TYR A1018 24.360 -32.709 20.868 1.00 78.68 C ANISOU 1770 CZ TYR A1018 10870 9070 9952 -1257 460 -468 C ATOM 1771 OH TYR A1018 25.250 -33.764 20.955 1.00 80.24 O ANISOU 1771 OH TYR A1018 11098 9037 10352 -1210 531 -505 O ATOM 1772 N LYS A1019 19.816 -31.341 22.808 1.00 72.88 N ANISOU 1772 N LYS A1019 9931 8951 8806 -1452 195 -144 N ATOM 1773 CA LYS A1019 19.898 -31.797 24.191 1.00 73.27 C ANISOU 1773 CA LYS A1019 9929 8989 8920 -1410 180 4 C ATOM 1774 C LYS A1019 21.269 -32.442 24.441 1.00 73.82 C ANISOU 1774 C LYS A1019 10046 8835 9167 -1333 237 29 C ATOM 1775 O LYS A1019 21.534 -33.536 23.943 1.00 75.34 O ANISOU 1775 O LYS A1019 10306 8818 9500 -1402 290 -18 O ATOM 1776 CB LYS A1019 18.771 -32.782 24.482 1.00 74.52 C ANISOU 1776 CB LYS A1019 10065 9171 9077 -1567 164 80 C ATOM 1777 CG LYS A1019 18.539 -33.019 25.952 1.00 75.16 C ANISOU 1777 CG LYS A1019 10045 9357 9154 -1550 122 268 C ATOM 1778 CD LYS A1019 17.270 -33.816 26.204 1.00 77.19 C ANISOU 1778 CD LYS A1019 10255 9700 9371 -1724 89 363 C ATOM 1779 CE LYS A1019 17.185 -34.267 27.661 1.00 78.77 C ANISOU 1779 CE LYS A1019 10343 10003 9582 -1735 50 583 C ATOM 1780 NZ LYS A1019 15.981 -35.100 27.919 1.00 80.77 N ANISOU 1780 NZ LYS A1019 10541 10348 9799 -1925 8 706 N ATOM 1781 N ASP A1020 22.143 -31.767 25.198 1.00 73.09 N ANISOU 1781 N ASP A1020 9910 8781 9078 -1188 223 91 N ATOM 1782 CA ASP A1020 23.529 -32.251 25.408 1.00 73.43 C ANISOU 1782 CA ASP A1020 9983 8636 9280 -1099 274 124 C ATOM 1783 C ASP A1020 23.569 -33.433 26.374 1.00 74.80 C ANISOU 1783 C ASP A1020 10122 8703 9596 -1134 275 295 C ATOM 1784 O ASP A1020 22.520 -33.926 26.785 1.00 75.46 O ANISOU 1784 O ASP A1020 10166 8854 9649 -1247 238 381 O ATOM 1785 CB ASP A1020 24.501 -31.113 25.817 1.00 72.17 C ANISOU 1785 CB ASP A1020 9785 8562 9072 -949 255 135 C ATOM 1786 CG ASP A1020 24.153 -30.451 27.155 1.00 72.19 C ANISOU 1786 CG ASP A1020 9678 8776 8974 -898 187 248 C ATOM 1787 OD1 ASP A1020 23.341 -30.990 27.936 1.00 73.64 O ANISOU 1787 OD1 ASP A1020 9797 9050 9130 -968 162 356 O ATOM 1788 OD2 ASP A1020 24.713 -29.366 27.427 1.00 71.62 O ANISOU 1788 OD2 ASP A1020 9572 8794 8844 -794 157 221 O ATOM 1789 N THR A1021 24.766 -33.903 26.724 1.00 75.49 N ANISOU 1789 N THR A1021 10209 8629 9842 -1047 310 363 N ATOM 1790 CA THR A1021 24.886 -35.147 27.500 1.00 77.48 C ANISOU 1790 CA THR A1021 10426 8730 10281 -1087 305 548 C ATOM 1791 C THR A1021 24.343 -35.034 28.930 1.00 77.77 C ANISOU 1791 C THR A1021 10334 8995 10219 -1118 231 777 C ATOM 1792 O THR A1021 24.088 -36.052 29.582 1.00 79.61 O ANISOU 1792 O THR A1021 10517 9158 10573 -1202 201 970 O ATOM 1793 CB THR A1021 26.341 -35.662 27.571 1.00 78.05 C ANISOU 1793 CB THR A1021 10508 8582 10565 -970 354 588 C ATOM 1794 OG1 THR A1021 27.143 -34.720 28.289 1.00 77.33 O ANISOU 1794 OG1 THR A1021 10349 8660 10372 -847 338 661 O ATOM 1795 CG2 THR A1021 26.921 -35.872 26.173 1.00 78.42 C ANISOU 1795 CG2 THR A1021 10659 8431 10706 -940 437 344 C ATOM 1796 N GLU A1022 24.165 -33.803 29.408 1.00 76.32 N ANISOU 1796 N GLU A1022 10084 9091 9822 -1057 196 754 N ATOM 1797 CA GLU A1022 23.653 -33.548 30.754 1.00 76.49 C ANISOU 1797 CA GLU A1022 9960 9397 9706 -1079 133 921 C ATOM 1798 C GLU A1022 22.158 -33.190 30.747 1.00 75.92 C ANISOU 1798 C GLU A1022 9842 9551 9451 -1176 91 873 C ATOM 1799 O GLU A1022 21.582 -32.866 31.789 1.00 76.21 O ANISOU 1799 O GLU A1022 9740 9879 9334 -1195 42 967 O ATOM 1800 CB GLU A1022 24.486 -32.442 31.409 1.00 75.58 C ANISOU 1800 CB GLU A1022 9777 9452 9486 -941 121 904 C ATOM 1801 CG GLU A1022 25.986 -32.630 31.186 1.00 76.64 C ANISOU 1801 CG GLU A1022 9965 9374 9781 -837 168 918 C ATOM 1802 CD GLU A1022 26.831 -31.985 32.262 1.00 78.41 C ANISOU 1802 CD GLU A1022 10080 9780 9929 -746 143 1009 C ATOM 1803 OE1 GLU A1022 26.869 -30.732 32.324 1.00 78.14 O ANISOU 1803 OE1 GLU A1022 10028 9912 9748 -678 120 873 O ATOM 1804 OE2 GLU A1022 27.464 -32.739 33.041 1.00 80.77 O ANISOU 1804 OE2 GLU A1022 10306 10051 10328 -747 141 1220 O ATOM 1805 N GLY A1023 21.534 -33.262 29.573 1.00 75.23 N ANISOU 1805 N GLY A1023 9856 9356 9370 -1239 111 721 N ATOM 1806 CA GLY A1023 20.104 -32.996 29.428 1.00 74.92 C ANISOU 1806 CA GLY A1023 9775 9516 9173 -1336 73 679 C ATOM 1807 C GLY A1023 19.730 -31.529 29.286 1.00 73.18 C ANISOU 1807 C GLY A1023 9515 9512 8776 -1241 45 529 C ATOM 1808 O GLY A1023 18.549 -31.193 29.293 1.00 73.42 O ANISOU 1808 O GLY A1023 9482 9742 8671 -1295 9 500 O ATOM 1809 N TYR A1024 20.717 -30.650 29.143 1.00 71.51 N ANISOU 1809 N TYR A1024 9333 9255 8581 -1101 56 439 N ATOM 1810 CA TYR A1024 20.440 -29.223 29.023 1.00 70.08 C ANISOU 1810 CA TYR A1024 9111 9234 8281 -1004 14 305 C ATOM 1811 C TYR A1024 20.194 -28.859 27.574 1.00 68.75 C ANISOU 1811 C TYR A1024 9041 8956 8123 -1030 21 171 C ATOM 1812 O TYR A1024 20.795 -29.438 26.671 1.00 68.70 O ANISOU 1812 O TYR A1024 9144 8740 8217 -1069 73 140 O ATOM 1813 CB TYR A1024 21.587 -28.392 29.602 1.00 69.55 C ANISOU 1813 CB TYR A1024 9016 9179 8229 -861 4 283 C ATOM 1814 CG TYR A1024 21.971 -28.813 30.998 1.00 71.51 C ANISOU 1814 CG TYR A1024 9157 9554 8457 -850 1 429 C ATOM 1815 CD1 TYR A1024 23.297 -28.786 31.413 1.00 72.56 C ANISOU 1815 CD1 TYR A1024 9297 9608 8664 -771 20 482 C ATOM 1816 CD2 TYR A1024 21.003 -29.265 31.903 1.00 73.53 C ANISOU 1816 CD2 TYR A1024 9289 10040 8609 -933 -24 534 C ATOM 1817 CE1 TYR A1024 23.652 -29.181 32.701 1.00 74.10 C ANISOU 1817 CE1 TYR A1024 9375 9951 8828 -776 10 640 C ATOM 1818 CE2 TYR A1024 21.344 -29.664 33.180 1.00 75.34 C ANISOU 1818 CE2 TYR A1024 9396 10430 8799 -945 -34 695 C ATOM 1819 CZ TYR A1024 22.670 -29.625 33.579 1.00 75.83 C ANISOU 1819 CZ TYR A1024 9464 10410 8936 -868 -18 751 C ATOM 1820 OH TYR A1024 22.996 -30.019 34.863 1.00 78.19 O ANISOU 1820 OH TYR A1024 9621 10903 9181 -894 -34 934 O ATOM 1821 N TYR A1025 19.300 -27.900 27.361 1.00 67.54 N ANISOU 1821 N TYR A1025 8832 8963 7867 -1009 -32 93 N ATOM 1822 CA TYR A1025 18.947 -27.473 26.023 1.00 66.61 C ANISOU 1822 CA TYR A1025 8775 8793 7739 -1047 -42 1 C ATOM 1823 C TYR A1025 19.866 -26.341 25.614 1.00 65.42 C ANISOU 1823 C TYR A1025 8649 8574 7631 -929 -70 -66 C ATOM 1824 O TYR A1025 20.024 -25.368 26.341 1.00 64.96 O ANISOU 1824 O TYR A1025 8516 8601 7564 -811 -123 -89 O ATOM 1825 CB TYR A1025 17.483 -27.056 25.970 1.00 66.93 C ANISOU 1825 CB TYR A1025 8726 9037 7666 -1088 -97 -18 C ATOM 1826 CG TYR A1025 16.527 -28.205 26.247 1.00 67.75 C ANISOU 1826 CG TYR A1025 8804 9219 7717 -1236 -76 62 C ATOM 1827 CD1 TYR A1025 16.126 -28.507 27.548 1.00 68.36 C ANISOU 1827 CD1 TYR A1025 8768 9468 7734 -1235 -90 151 C ATOM 1828 CD2 TYR A1025 16.037 -28.998 25.214 1.00 67.74 C ANISOU 1828 CD2 TYR A1025 8879 9137 7718 -1393 -47 51 C ATOM 1829 CE1 TYR A1025 15.259 -29.553 27.807 1.00 69.08 C ANISOU 1829 CE1 TYR A1025 8826 9639 7781 -1389 -84 255 C ATOM 1830 CE2 TYR A1025 15.170 -30.046 25.470 1.00 68.99 C ANISOU 1830 CE2 TYR A1025 9015 9351 7845 -1544 -40 130 C ATOM 1831 CZ TYR A1025 14.785 -30.314 26.768 1.00 69.71 C ANISOU 1831 CZ TYR A1025 8994 9602 7887 -1542 -63 246 C ATOM 1832 OH TYR A1025 13.927 -31.348 27.034 1.00 70.85 O ANISOU 1832 OH TYR A1025 9105 9811 8002 -1710 -68 355 O ATOM 1833 N THR A1026 20.474 -26.485 24.443 1.00 65.02 N ANISOU 1833 N THR A1026 8695 8380 7627 -972 -36 -103 N ATOM 1834 CA THR A1026 21.550 -25.604 23.998 1.00 64.28 C ANISOU 1834 CA THR A1026 8629 8210 7582 -888 -56 -135 C ATOM 1835 C THR A1026 21.421 -25.356 22.511 1.00 64.11 C ANISOU 1835 C THR A1026 8650 8175 7532 -972 -62 -177 C ATOM 1836 O THR A1026 20.944 -26.214 21.776 1.00 64.81 O ANISOU 1836 O THR A1026 8781 8257 7587 -1099 -12 -205 O ATOM 1837 CB THR A1026 22.953 -26.226 24.291 1.00 64.34 C ANISOU 1837 CB THR A1026 8694 8072 7679 -845 14 -109 C ATOM 1838 OG1 THR A1026 23.848 -26.001 23.188 1.00 64.16 O ANISOU 1838 OG1 THR A1026 8732 7961 7683 -854 36 -152 O ATOM 1839 CG2 THR A1026 22.850 -27.740 24.532 1.00 65.39 C ANISOU 1839 CG2 THR A1026 8864 8120 7859 -925 92 -69 C ATOM 1840 N ILE A1027 21.853 -24.185 22.069 1.00 63.40 N ANISOU 1840 N ILE A1027 8539 8092 7457 -915 -130 -177 N ATOM 1841 CA ILE A1027 21.893 -23.888 20.652 1.00 63.67 C ANISOU 1841 CA ILE A1027 8591 8146 7452 -1006 -145 -184 C ATOM 1842 C ILE A1027 23.154 -23.093 20.303 1.00 63.47 C ANISOU 1842 C ILE A1027 8575 8063 7478 -950 -176 -159 C ATOM 1843 O ILE A1027 23.784 -22.493 21.171 1.00 62.90 O ANISOU 1843 O ILE A1027 8484 7940 7476 -832 -214 -139 O ATOM 1844 CB ILE A1027 20.634 -23.099 20.232 1.00 63.97 C ANISOU 1844 CB ILE A1027 8551 8312 7439 -1041 -242 -155 C ATOM 1845 CG1 ILE A1027 20.331 -23.300 18.736 1.00 64.22 C ANISOU 1845 CG1 ILE A1027 8594 8422 7382 -1200 -232 -153 C ATOM 1846 CG2 ILE A1027 20.793 -21.620 20.585 1.00 63.79 C ANISOU 1846 CG2 ILE A1027 8457 8281 7498 -915 -364 -116 C ATOM 1847 CD1 ILE A1027 18.892 -23.010 18.356 1.00 63.49 C ANISOU 1847 CD1 ILE A1027 8426 8477 7220 -1270 -298 -117 C ATOM 1848 N GLY A1028 23.518 -23.108 19.027 1.00 64.13 N ANISOU 1848 N GLY A1028 8675 8180 7510 -1049 -160 -160 N ATOM 1849 CA GLY A1028 24.647 -22.329 18.525 1.00 64.16 C ANISOU 1849 CA GLY A1028 8667 8171 7537 -1028 -199 -112 C ATOM 1850 C GLY A1028 25.996 -22.877 18.962 1.00 63.97 C ANISOU 1850 C GLY A1028 8693 8048 7563 -961 -112 -143 C ATOM 1851 O GLY A1028 26.214 -24.100 18.987 1.00 64.25 O ANISOU 1851 O GLY A1028 8781 8031 7599 -983 4 -218 O ATOM 1852 N ILE A1029 26.902 -21.965 19.304 1.00 63.51 N ANISOU 1852 N ILE A1029 8610 7954 7564 -880 -176 -81 N ATOM 1853 CA ILE A1029 28.199 -22.339 19.849 1.00 63.31 C ANISOU 1853 CA ILE A1029 8613 7851 7588 -804 -109 -88 C ATOM 1854 C ILE A1029 28.115 -22.395 21.382 1.00 62.60 C ANISOU 1854 C ILE A1029 8519 7697 7568 -688 -117 -84 C ATOM 1855 O ILE A1029 28.290 -21.387 22.069 1.00 62.38 O ANISOU 1855 O ILE A1029 8450 7662 7587 -613 -209 -52 O ATOM 1856 CB ILE A1029 29.314 -21.371 19.387 1.00 63.45 C ANISOU 1856 CB ILE A1029 8598 7891 7616 -800 -173 -13 C ATOM 1857 CG1 ILE A1029 29.249 -21.167 17.870 1.00 64.39 C ANISOU 1857 CG1 ILE A1029 8688 8137 7639 -938 -189 10 C ATOM 1858 CG2 ILE A1029 30.678 -21.916 19.786 1.00 63.25 C ANISOU 1858 CG2 ILE A1029 8593 7814 7622 -734 -86 -23 C ATOM 1859 CD1 ILE A1029 30.433 -20.412 17.304 1.00 65.29 C ANISOU 1859 CD1 ILE A1029 8757 8308 7741 -964 -238 101 C ATOM 1860 N GLY A1030 27.810 -23.582 21.901 1.00 62.56 N ANISOU 1860 N GLY A1030 8545 7655 7569 -686 -25 -119 N ATOM 1861 CA GLY A1030 27.794 -23.838 23.337 1.00 62.10 C ANISOU 1861 CA GLY A1030 8464 7578 7552 -601 -20 -92 C ATOM 1862 C GLY A1030 26.971 -22.875 24.176 1.00 61.66 C ANISOU 1862 C GLY A1030 8342 7603 7483 -549 -122 -95 C ATOM 1863 O GLY A1030 27.280 -22.673 25.353 1.00 61.87 O ANISOU 1863 O GLY A1030 8323 7655 7527 -469 -139 -81 O ATOM 1864 N HIS A1031 25.923 -22.290 23.591 1.00 61.42 N ANISOU 1864 N HIS A1031 8289 7627 7421 -592 -189 -119 N ATOM 1865 CA HIS A1031 25.047 -21.359 24.316 1.00 61.19 C ANISOU 1865 CA HIS A1031 8179 7670 7398 -527 -286 -150 C ATOM 1866 C HIS A1031 23.885 -22.109 24.955 1.00 61.37 C ANISOU 1866 C HIS A1031 8168 7790 7357 -549 -250 -169 C ATOM 1867 O HIS A1031 22.957 -22.532 24.264 1.00 62.01 O ANISOU 1867 O HIS A1031 8261 7908 7390 -637 -236 -169 O ATOM 1868 CB HIS A1031 24.506 -20.277 23.380 1.00 61.37 C ANISOU 1868 CB HIS A1031 8172 7698 7445 -549 -393 -144 C ATOM 1869 CG HIS A1031 23.633 -19.273 24.063 1.00 61.52 C ANISOU 1869 CG HIS A1031 8097 7765 7510 -461 -498 -196 C ATOM 1870 ND1 HIS A1031 24.108 -18.063 24.518 1.00 61.80 N ANISOU 1870 ND1 HIS A1031 8085 7741 7652 -365 -601 -228 N ATOM 1871 CD2 HIS A1031 22.318 -19.304 24.375 1.00 61.40 C ANISOU 1871 CD2 HIS A1031 8017 7854 7458 -450 -516 -240 C ATOM 1872 CE1 HIS A1031 23.121 -17.388 25.077 1.00 62.05 C ANISOU 1872 CE1 HIS A1031 8025 7826 7724 -287 -675 -309 C ATOM 1873 NE2 HIS A1031 22.025 -18.120 25.003 1.00 62.02 N ANISOU 1873 NE2 HIS A1031 8004 7935 7624 -334 -623 -312 N ATOM 1874 N LEU A1032 23.935 -22.269 26.274 1.00 61.10 N ANISOU 1874 N LEU A1032 8079 7824 7310 -484 -239 -175 N ATOM 1875 CA LEU A1032 22.882 -22.979 26.998 1.00 61.29 C ANISOU 1875 CA LEU A1032 8047 7979 7259 -517 -212 -168 C ATOM 1876 C LEU A1032 21.591 -22.131 27.084 1.00 61.16 C ANISOU 1876 C LEU A1032 7937 8094 7205 -485 -293 -241 C ATOM 1877 O LEU A1032 21.615 -20.985 27.519 1.00 60.71 O ANISOU 1877 O LEU A1032 7810 8069 7187 -381 -372 -320 O ATOM 1878 CB LEU A1032 23.401 -23.436 28.375 1.00 61.58 C ANISOU 1878 CB LEU A1032 8030 8092 7274 -475 -178 -126 C ATOM 1879 CG LEU A1032 22.436 -23.520 29.565 1.00 62.95 C ANISOU 1879 CG LEU A1032 8075 8493 7348 -466 -195 -138 C ATOM 1880 CD1 LEU A1032 22.746 -24.715 30.479 1.00 63.56 C ANISOU 1880 CD1 LEU A1032 8124 8632 7393 -518 -133 -6 C ATOM 1881 CD2 LEU A1032 22.460 -22.195 30.345 1.00 64.12 C ANISOU 1881 CD2 LEU A1032 8117 8760 7485 -345 -273 -265 C ATOM 1882 N LEU A1033 20.478 -22.720 26.644 1.00 61.38 N ANISOU 1882 N LEU A1033 7961 8191 7170 -576 -274 -221 N ATOM 1883 CA LEU A1033 19.162 -22.051 26.596 1.00 61.83 C ANISOU 1883 CA LEU A1033 7919 8383 7187 -554 -344 -275 C ATOM 1884 C LEU A1033 18.366 -22.218 27.899 1.00 62.46 C ANISOU 1884 C LEU A1033 7870 8685 7176 -518 -341 -307 C ATOM 1885 O LEU A1033 17.845 -21.248 28.444 1.00 62.65 O ANISOU 1885 O LEU A1033 7776 8826 7201 -410 -408 -410 O ATOM 1886 CB LEU A1033 18.332 -22.578 25.411 1.00 61.83 C ANISOU 1886 CB LEU A1033 7963 8383 7143 -687 -328 -230 C ATOM 1887 CG LEU A1033 18.810 -22.204 23.996 1.00 61.42 C ANISOU 1887 CG LEU A1033 7991 8201 7145 -736 -350 -208 C ATOM 1888 CD1 LEU A1033 18.331 -23.219 22.950 1.00 61.16 C ANISOU 1888 CD1 LEU A1033 8023 8174 7039 -906 -289 -174 C ATOM 1889 CD2 LEU A1033 18.386 -20.776 23.608 1.00 60.31 C ANISOU 1889 CD2 LEU A1033 7770 8076 7068 -657 -471 -225 C ATOM 1890 N THR A1034 18.267 -23.454 28.379 1.00 62.90 N ANISOU 1890 N THR A1034 7936 8803 7159 -613 -269 -220 N ATOM 1891 CA THR A1034 17.622 -23.737 29.654 1.00 63.97 C ANISOU 1891 CA THR A1034 7934 9188 7183 -608 -265 -213 C ATOM 1892 C THR A1034 18.098 -25.069 30.231 1.00 64.89 C ANISOU 1892 C THR A1034 8080 9297 7276 -708 -196 -66 C ATOM 1893 O THR A1034 18.428 -25.994 29.480 1.00 64.67 O ANISOU 1893 O THR A1034 8175 9080 7314 -807 -148 17 O ATOM 1894 CB THR A1034 16.093 -23.776 29.515 1.00 64.68 C ANISOU 1894 CB THR A1034 7929 9467 7176 -659 -289 -226 C ATOM 1895 OG1 THR A1034 15.499 -23.872 30.814 1.00 65.43 O ANISOU 1895 OG1 THR A1034 7858 9856 7143 -641 -291 -237 O ATOM 1896 CG2 THR A1034 15.647 -24.962 28.666 1.00 64.14 C ANISOU 1896 CG2 THR A1034 7956 9321 7090 -835 -243 -112 C ATOM 1897 N LYS A1035 18.146 -25.141 31.565 1.00 66.29 N ANISOU 1897 N LYS A1035 8129 9688 7369 -680 -197 -39 N ATOM 1898 CA LYS A1035 18.433 -26.384 32.303 1.00 67.49 C ANISOU 1898 CA LYS A1035 8261 9888 7494 -783 -154 142 C ATOM 1899 C LYS A1035 17.144 -27.161 32.569 1.00 69.07 C ANISOU 1899 C LYS A1035 8372 10287 7582 -915 -156 238 C ATOM 1900 O LYS A1035 17.177 -28.334 32.931 1.00 70.03 O ANISOU 1900 O LYS A1035 8491 10406 7712 -1039 -133 423 O ATOM 1901 CB LYS A1035 19.125 -26.097 33.650 1.00 68.03 C ANISOU 1901 CB LYS A1035 8206 10142 7497 -716 -161 156 C ATOM 1902 CG LYS A1035 20.660 -26.063 33.624 1.00 67.42 C ANISOU 1902 CG LYS A1035 8222 9857 7538 -657 -139 189 C ATOM 1903 CD LYS A1035 21.261 -26.729 34.878 1.00 69.00 C ANISOU 1903 CD LYS A1035 8316 10217 7683 -696 -124 358 C ATOM 1904 CE LYS A1035 21.892 -25.766 35.863 1.00 69.24 C ANISOU 1904 CE LYS A1035 8230 10444 7632 -594 -152 254 C ATOM 1905 NZ LYS A1035 23.328 -25.488 35.510 1.00 68.47 N ANISOU 1905 NZ LYS A1035 8245 10103 7666 -523 -139 250 N ATOM 1906 N SER A1036 16.010 -26.496 32.392 1.00 69.94 N ANISOU 1906 N SER A1036 8400 10571 7602 -891 -192 124 N ATOM 1907 CA SER A1036 14.714 -27.070 32.720 1.00 71.55 C ANISOU 1907 CA SER A1036 8488 11027 7671 -1008 -201 202 C ATOM 1908 C SER A1036 14.384 -28.250 31.792 1.00 72.05 C ANISOU 1908 C SER A1036 8681 10893 7802 -1184 -176 334 C ATOM 1909 O SER A1036 14.837 -28.268 30.656 1.00 71.18 O ANISOU 1909 O SER A1036 8733 10496 7816 -1185 -157 285 O ATOM 1910 CB SER A1036 13.650 -25.973 32.622 1.00 71.94 C ANISOU 1910 CB SER A1036 8418 11282 7632 -913 -246 27 C ATOM 1911 OG SER A1036 14.085 -24.788 33.291 1.00 71.40 O ANISOU 1911 OG SER A1036 8257 11311 7558 -734 -273 -145 O ATOM 1912 N PRO A1037 13.620 -29.247 32.283 1.00 73.95 N ANISOU 1912 N PRO A1037 8840 11296 7960 -1343 -180 497 N ATOM 1913 CA PRO A1037 13.191 -30.393 31.472 1.00 74.82 C ANISOU 1913 CA PRO A1037 9059 11227 8141 -1529 -167 608 C ATOM 1914 C PRO A1037 12.423 -30.025 30.207 1.00 74.93 C ANISOU 1914 C PRO A1037 9143 11178 8146 -1553 -173 483 C ATOM 1915 O PRO A1037 12.545 -30.716 29.193 1.00 75.34 O ANISOU 1915 O PRO A1037 9342 10978 8303 -1661 -148 491 O ATOM 1916 CB PRO A1037 12.256 -31.159 32.409 1.00 76.44 C ANISOU 1916 CB PRO A1037 9102 11728 8213 -1681 -196 791 C ATOM 1917 CG PRO A1037 12.724 -30.834 33.754 1.00 76.91 C ANISOU 1917 CG PRO A1037 9008 12030 8182 -1599 -206 841 C ATOM 1918 CD PRO A1037 13.240 -29.420 33.696 1.00 75.46 C ANISOU 1918 CD PRO A1037 8824 11854 7991 -1376 -201 603 C ATOM 1919 N SER A1038 11.637 -28.954 30.268 1.00 75.23 N ANISOU 1919 N SER A1038 9062 11454 8065 -1455 -208 364 N ATOM 1920 CA SER A1038 10.781 -28.544 29.151 1.00 75.19 C ANISOU 1920 CA SER A1038 9084 11448 8036 -1481 -228 279 C ATOM 1921 C SER A1038 11.535 -28.259 27.835 1.00 74.22 C ANISOU 1921 C SER A1038 9140 11008 8049 -1452 -210 191 C ATOM 1922 O SER A1038 12.465 -27.458 27.793 1.00 73.20 O ANISOU 1922 O SER A1038 9053 10758 8002 -1302 -212 106 O ATOM 1923 CB SER A1038 9.966 -27.313 29.564 1.00 75.46 C ANISOU 1923 CB SER A1038 8938 11772 7960 -1335 -276 162 C ATOM 1924 OG SER A1038 9.264 -26.760 28.466 1.00 75.56 O ANISOU 1924 OG SER A1038 8966 11766 7977 -1332 -306 93 O ATOM 1925 N LEU A1039 11.130 -28.944 26.769 1.00 74.94 N ANISOU 1925 N LEU A1039 9326 10991 8154 -1613 -195 211 N ATOM 1926 CA LEU A1039 11.461 -28.537 25.398 1.00 74.33 C ANISOU 1926 CA LEU A1039 9364 10737 8139 -1611 -190 119 C ATOM 1927 C LEU A1039 10.838 -27.168 25.104 1.00 74.31 C ANISOU 1927 C LEU A1039 9257 10894 8082 -1488 -255 47 C ATOM 1928 O LEU A1039 11.475 -26.309 24.502 1.00 73.60 O ANISOU 1928 O LEU A1039 9212 10682 8067 -1385 -274 -17 O ATOM 1929 CB LEU A1039 10.939 -29.577 24.400 1.00 75.07 C ANISOU 1929 CB LEU A1039 9543 10759 8219 -1832 -164 139 C ATOM 1930 CG LEU A1039 11.069 -29.310 22.894 1.00 74.72 C ANISOU 1930 CG LEU A1039 9589 10613 8186 -1886 -157 49 C ATOM 1931 CD1 LEU A1039 12.498 -28.983 22.492 1.00 72.83 C ANISOU 1931 CD1 LEU A1039 9458 10147 8065 -1781 -122 -20 C ATOM 1932 CD2 LEU A1039 10.554 -30.516 22.102 1.00 75.66 C ANISOU 1932 CD2 LEU A1039 9782 10680 8285 -2127 -124 46 C ATOM 1933 N ASN A1040 9.594 -26.978 25.550 1.00 75.44 N ANISOU 1933 N ASN A1040 9246 11309 8105 -1499 -294 71 N ATOM 1934 CA ASN A1040 8.862 -25.715 25.382 1.00 75.66 C ANISOU 1934 CA ASN A1040 9143 11498 8104 -1368 -363 6 C ATOM 1935 C ASN A1040 9.464 -24.513 26.088 1.00 75.22 C ANISOU 1935 C ASN A1040 9020 11428 8130 -1131 -399 -94 C ATOM 1936 O ASN A1040 9.220 -23.384 25.671 1.00 75.53 O ANISOU 1936 O ASN A1040 8997 11471 8229 -1008 -465 -156 O ATOM 1937 CB ASN A1040 7.408 -25.861 25.851 1.00 77.03 C ANISOU 1937 CB ASN A1040 9143 11995 8127 -1422 -389 46 C ATOM 1938 CG ASN A1040 6.515 -26.495 24.805 1.00 77.59 C ANISOU 1938 CG ASN A1040 9241 12117 8120 -1629 -391 117 C ATOM 1939 OD1 ASN A1040 6.699 -26.291 23.599 1.00 76.81 O ANISOU 1939 OD1 ASN A1040 9232 11883 8068 -1677 -401 104 O ATOM 1940 ND2 ASN A1040 5.526 -27.258 25.263 1.00 78.50 N ANISOU 1940 ND2 ASN A1040 9265 12457 8103 -1768 -387 199 N ATOM 1941 N ALA A1041 10.212 -24.748 27.164 1.00 75.01 N ANISOU 1941 N ALA A1041 8993 11390 8114 -1073 -365 -104 N ATOM 1942 CA ALA A1041 10.963 -23.680 27.837 1.00 74.68 C ANISOU 1942 CA ALA A1041 8906 11312 8156 -867 -394 -217 C ATOM 1943 C ALA A1041 12.167 -23.285 26.983 1.00 73.61 C ANISOU 1943 C ALA A1041 8930 10868 8171 -829 -398 -233 C ATOM 1944 O ALA A1041 12.391 -22.102 26.707 1.00 73.56 O ANISOU 1944 O ALA A1041 8898 10785 8266 -693 -463 -312 O ATOM 1945 CB ALA A1041 11.420 -24.128 29.221 1.00 74.90 C ANISOU 1945 CB ALA A1041 8876 11460 8123 -847 -356 -206 C ATOM 1946 N ALA A1042 12.927 -24.292 26.556 1.00 73.03 N ANISOU 1946 N ALA A1042 9008 10619 8120 -954 -333 -154 N ATOM 1947 CA ALA A1042 14.046 -24.105 25.640 1.00 72.00 C ANISOU 1947 CA ALA A1042 9021 10231 8102 -949 -323 -162 C ATOM 1948 C ALA A1042 13.617 -23.373 24.377 1.00 72.09 C ANISOU 1948 C ALA A1042 9036 10216 8139 -964 -382 -170 C ATOM 1949 O ALA A1042 14.370 -22.562 23.829 1.00 71.70 O ANISOU 1949 O ALA A1042 9028 10029 8186 -895 -421 -189 O ATOM 1950 CB ALA A1042 14.646 -25.449 25.278 1.00 71.77 C ANISOU 1950 CB ALA A1042 9130 10054 8086 -1096 -239 -96 C ATOM 1951 N LYS A1043 12.405 -23.677 23.920 1.00 72.94 N ANISOU 1951 N LYS A1043 9088 10471 8152 -1071 -394 -135 N ATOM 1952 CA LYS A1043 11.837 -23.075 22.715 1.00 73.33 C ANISOU 1952 CA LYS A1043 9114 10545 8202 -1112 -454 -111 C ATOM 1953 C LYS A1043 11.515 -21.613 23.008 1.00 73.92 C ANISOU 1953 C LYS A1043 9055 10666 8364 -922 -559 -152 C ATOM 1954 O LYS A1043 11.673 -20.743 22.161 1.00 73.84 O ANISOU 1954 O LYS A1043 9037 10576 8441 -890 -632 -121 O ATOM 1955 CB LYS A1043 10.559 -23.832 22.318 1.00 74.15 C ANISOU 1955 CB LYS A1043 9174 10829 8170 -1280 -440 -60 C ATOM 1956 CG LYS A1043 10.463 -24.272 20.863 1.00 73.94 C ANISOU 1956 CG LYS A1043 9226 10772 8095 -1466 -426 -21 C ATOM 1957 CD LYS A1043 9.698 -25.592 20.762 1.00 74.08 C ANISOU 1957 CD LYS A1043 9269 10884 7993 -1672 -368 1 C ATOM 1958 CE LYS A1043 9.091 -25.801 19.394 1.00 74.58 C ANISOU 1958 CE LYS A1043 9339 11031 7965 -1857 -379 26 C ATOM 1959 NZ LYS A1043 7.902 -24.940 19.202 1.00 75.10 N ANISOU 1959 NZ LYS A1043 9241 11319 7972 -1822 -469 90 N ATOM 1960 N SER A1044 11.076 -21.367 24.236 1.00 74.87 N ANISOU 1960 N SER A1044 9057 10922 8467 -801 -568 -222 N ATOM 1961 CA SER A1044 10.612 -20.054 24.672 1.00 76.02 C ANISOU 1961 CA SER A1044 9049 11129 8707 -606 -662 -308 C ATOM 1962 C SER A1044 11.760 -19.077 24.935 1.00 75.80 C ANISOU 1962 C SER A1044 9054 10895 8850 -452 -710 -383 C ATOM 1963 O SER A1044 11.592 -17.863 24.825 1.00 76.36 O ANISOU 1963 O SER A1044 9035 10907 9068 -311 -813 -433 O ATOM 1964 CB SER A1044 9.732 -20.221 25.920 1.00 76.86 C ANISOU 1964 CB SER A1044 8997 11500 8704 -542 -642 -388 C ATOM 1965 OG SER A1044 9.685 -19.041 26.683 1.00 77.93 O ANISOU 1965 OG SER A1044 8998 11665 8946 -324 -708 -538 O ATOM 1966 N GLU A1045 12.923 -19.609 25.282 1.00 75.37 N ANISOU 1966 N GLU A1045 9121 10722 8791 -482 -643 -384 N ATOM 1967 CA GLU A1045 14.099 -18.780 25.521 1.00 75.54 C ANISOU 1967 CA GLU A1045 9183 10558 8960 -363 -684 -443 C ATOM 1968 C GLU A1045 14.755 -18.377 24.212 1.00 75.11 C ANISOU 1968 C GLU A1045 9226 10305 9005 -420 -731 -345 C ATOM 1969 O GLU A1045 15.021 -17.199 23.977 1.00 75.40 O ANISOU 1969 O GLU A1045 9223 10221 9203 -318 -837 -359 O ATOM 1970 CB GLU A1045 15.102 -19.514 26.413 1.00 75.04 C ANISOU 1970 CB GLU A1045 9193 10474 8844 -376 -596 -461 C ATOM 1971 CG GLU A1045 14.839 -19.310 27.904 1.00 77.22 C ANISOU 1971 CG GLU A1045 9333 10936 9068 -263 -591 -587 C ATOM 1972 CD GLU A1045 15.273 -17.929 28.392 1.00 79.51 C ANISOU 1972 CD GLU A1045 9550 11150 9508 -81 -679 -739 C ATOM 1973 OE1 GLU A1045 16.500 -17.662 28.421 1.00 80.03 O ANISOU 1973 OE1 GLU A1045 9704 11042 9660 -58 -685 -740 O ATOM 1974 OE2 GLU A1045 14.388 -17.117 28.751 1.00 81.80 O ANISOU 1974 OE2 GLU A1045 9689 11551 9839 39 -744 -867 O ATOM 1975 N LEU A1046 15.009 -19.370 23.366 1.00 74.70 N ANISOU 1975 N LEU A1046 9290 10229 8861 -590 -657 -249 N ATOM 1976 CA LEU A1046 15.574 -19.146 22.040 1.00 74.65 C ANISOU 1976 CA LEU A1046 9358 10105 8896 -680 -686 -155 C ATOM 1977 C LEU A1046 14.883 -17.996 21.293 1.00 76.05 C ANISOU 1977 C LEU A1046 9431 10296 9168 -644 -821 -90 C ATOM 1978 O LEU A1046 15.542 -17.207 20.615 1.00 76.33 O ANISOU 1978 O LEU A1046 9477 10208 9314 -638 -900 -18 O ATOM 1979 CB LEU A1046 15.485 -20.433 21.215 1.00 74.27 C ANISOU 1979 CB LEU A1046 9405 10105 8708 -878 -587 -103 C ATOM 1980 CG LEU A1046 16.111 -20.407 19.818 1.00 73.94 C ANISOU 1980 CG LEU A1046 9431 10005 8658 -999 -592 -29 C ATOM 1981 CD1 LEU A1046 17.608 -20.161 19.885 1.00 72.49 C ANISOU 1981 CD1 LEU A1046 9324 9660 8556 -946 -578 -37 C ATOM 1982 CD2 LEU A1046 15.818 -21.709 19.101 1.00 74.29 C ANISOU 1982 CD2 LEU A1046 9545 10121 8559 -1191 -491 -34 C ATOM 1983 N ASP A1047 13.560 -17.906 21.416 1.00 77.39 N ANISOU 1983 N ASP A1047 9484 10620 9298 -627 -852 -96 N ATOM 1984 CA ASP A1047 12.798 -16.839 20.765 1.00 78.89 C ANISOU 1984 CA ASP A1047 9549 10827 9597 -580 -987 -19 C ATOM 1985 C ASP A1047 13.143 -15.488 21.401 1.00 79.48 C ANISOU 1985 C ASP A1047 9546 10747 9907 -370 -1103 -92 C ATOM 1986 O ASP A1047 13.386 -14.497 20.708 1.00 79.89 O ANISOU 1986 O ASP A1047 9561 10666 10126 -344 -1228 6 O ATOM 1987 CB ASP A1047 11.286 -17.116 20.850 1.00 79.92 C ANISOU 1987 CB ASP A1047 9558 11180 9628 -598 -986 -19 C ATOM 1988 CG ASP A1047 10.849 -18.371 20.049 1.00 80.75 C ANISOU 1988 CG ASP A1047 9731 11430 9518 -833 -895 60 C ATOM 1989 OD1 ASP A1047 11.497 -18.731 19.031 1.00 80.18 O ANISOU 1989 OD1 ASP A1047 9760 11302 9399 -983 -869 138 O ATOM 1990 OD2 ASP A1047 9.827 -18.995 20.440 1.00 82.86 O ANISOU 1990 OD2 ASP A1047 9938 11883 9659 -874 -851 35 O ATOM 1991 N LYS A1048 13.196 -15.472 22.728 1.00 79.60 N ANISOU 1991 N LYS A1048 9528 10783 9932 -233 -1065 -265 N ATOM 1992 CA LYS A1048 13.508 -14.258 23.468 1.00 80.65 C ANISOU 1992 CA LYS A1048 9582 10780 10281 -33 -1164 -392 C ATOM 1993 C LYS A1048 14.955 -13.819 23.190 1.00 79.95 C ANISOU 1993 C LYS A1048 9605 10458 10313 -46 -1201 -346 C ATOM 1994 O LYS A1048 15.264 -12.628 23.210 1.00 81.03 O ANISOU 1994 O LYS A1048 9688 10417 10682 66 -1331 -368 O ATOM 1995 CB LYS A1048 13.257 -14.471 24.975 1.00 80.94 C ANISOU 1995 CB LYS A1048 9547 10960 10247 86 -1097 -605 C ATOM 1996 CG LYS A1048 12.615 -13.273 25.691 1.00 83.52 C ANISOU 1996 CG LYS A1048 9692 11287 10755 306 -1201 -787 C ATOM 1997 CD LYS A1048 13.578 -12.508 26.625 1.00 84.55 C ANISOU 1997 CD LYS A1048 9819 11272 11031 444 -1238 -972 C ATOM 1998 CE LYS A1048 13.483 -13.003 28.080 1.00 84.99 C ANISOU 1998 CE LYS A1048 9807 11566 10917 502 -1135 -1177 C ATOM 1999 NZ LYS A1048 14.219 -12.135 29.049 1.00 85.34 N ANISOU 1999 NZ LYS A1048 9805 11519 11099 648 -1182 -1400 N ATOM 2000 N ALA A1049 15.828 -14.784 22.910 1.00 78.49 N ANISOU 2000 N ALA A1049 9566 10272 9985 -186 -1093 -280 N ATOM 2001 CA ALA A1049 17.235 -14.501 22.623 1.00 77.74 C ANISOU 2001 CA ALA A1049 9572 9997 9968 -213 -1111 -227 C ATOM 2002 C ALA A1049 17.439 -13.918 21.221 1.00 78.23 C ANISOU 2002 C ALA A1049 9637 9971 10116 -310 -1215 -33 C ATOM 2003 O ALA A1049 18.195 -12.962 21.055 1.00 78.78 O ANISOU 2003 O ALA A1049 9701 9870 10360 -269 -1324 14 O ATOM 2004 CB ALA A1049 18.069 -15.764 22.792 1.00 76.30 C ANISOU 2004 CB ALA A1049 9523 9854 9612 -316 -958 -227 C ATOM 2005 N ILE A1050 16.772 -14.493 20.221 1.00 78.24 N ANISOU 2005 N ILE A1050 9635 10105 9984 -453 -1186 86 N ATOM 2006 CA ILE A1050 16.925 -14.060 18.829 1.00 78.69 C ANISOU 2006 CA ILE A1050 9676 10152 10070 -581 -1275 290 C ATOM 2007 C ILE A1050 15.945 -12.954 18.440 1.00 80.59 C ANISOU 2007 C ILE A1050 9761 10373 10484 -518 -1444 393 C ATOM 2008 O ILE A1050 16.230 -12.178 17.525 1.00 81.44 O ANISOU 2008 O ILE A1050 9822 10414 10706 -579 -1572 583 O ATOM 2009 CB ILE A1050 16.734 -15.228 17.862 1.00 78.19 C ANISOU 2009 CB ILE A1050 9673 10269 9765 -788 -1163 359 C ATOM 2010 CG1 ILE A1050 17.739 -16.340 18.169 1.00 76.62 C ANISOU 2010 CG1 ILE A1050 9618 10055 9435 -841 -1003 261 C ATOM 2011 CG2 ILE A1050 16.895 -14.755 16.424 1.00 78.86 C ANISOU 2011 CG2 ILE A1050 9712 10402 9846 -936 -1256 571 C ATOM 2012 CD1 ILE A1050 19.182 -15.915 18.021 1.00 76.04 C ANISOU 2012 CD1 ILE A1050 9603 9848 9439 -836 -1026 302 C ATOM 2013 N GLY A1051 14.792 -12.906 19.114 1.00 81.33 N ANISOU 2013 N GLY A1051 9760 10542 10597 -403 -1446 285 N ATOM 2014 CA GLY A1051 13.811 -11.825 18.935 1.00 83.28 C ANISOU 2014 CA GLY A1051 9839 10755 11048 -296 -1607 351 C ATOM 2015 C GLY A1051 12.690 -12.078 17.931 1.00 84.20 C ANISOU 2015 C GLY A1051 9866 11070 11055 -419 -1631 519 C ATOM 2016 O GLY A1051 11.908 -11.171 17.629 1.00 85.95 O ANISOU 2016 O GLY A1051 9934 11264 11457 -342 -1776 620 O ATOM 2017 N ARG A1052 12.606 -13.304 17.413 1.00 83.21 N ANISOU 2017 N ARG A1052 9827 11139 10648 -611 -1495 547 N ATOM 2018 CA ARG A1052 11.561 -13.682 16.457 1.00 83.85 C ANISOU 2018 CA ARG A1052 9831 11446 10583 -762 -1502 690 C ATOM 2019 C ARG A1052 10.961 -15.033 16.848 1.00 82.89 C ANISOU 2019 C ARG A1052 9769 11518 10206 -846 -1336 559 C ATOM 2020 O ARG A1052 11.307 -15.589 17.886 1.00 81.75 O ANISOU 2020 O ARG A1052 9708 11330 10022 -773 -1231 383 O ATOM 2021 CB ARG A1052 12.133 -13.714 15.030 1.00 84.04 C ANISOU 2021 CB ARG A1052 9880 11529 10522 -979 -1536 904 C ATOM 2022 CG ARG A1052 13.267 -14.697 14.815 1.00 82.33 C ANISOU 2022 CG ARG A1052 9836 11319 10124 -1118 -1391 832 C ATOM 2023 CD ARG A1052 13.731 -14.711 13.361 1.00 82.92 C ANISOU 2023 CD ARG A1052 9899 11520 10086 -1339 -1423 1026 C ATOM 2024 NE ARG A1052 14.555 -15.882 13.064 1.00 81.91 N ANISOU 2024 NE ARG A1052 9916 11460 9745 -1484 -1257 915 N ATOM 2025 CZ ARG A1052 14.086 -17.121 12.895 1.00 82.33 C ANISOU 2025 CZ ARG A1052 10028 11670 9582 -1612 -1118 802 C ATOM 2026 NH1 ARG A1052 12.783 -17.380 12.986 1.00 82.85 N ANISOU 2026 NH1 ARG A1052 10023 11870 9585 -1631 -1121 799 N ATOM 2027 NH2 ARG A1052 14.931 -18.120 12.640 1.00 82.15 N ANISOU 2027 NH2 ARG A1052 10130 11663 9418 -1721 -978 686 N ATOM 2028 N ASN A1053 10.052 -15.551 16.031 1.00 83.50 N ANISOU 2028 N ASN A1053 9793 11816 10116 -1009 -1322 661 N ATOM 2029 CA ASN A1053 9.477 -16.868 16.277 1.00 82.89 C ANISOU 2029 CA ASN A1053 9774 11914 9806 -1125 -1178 560 C ATOM 2030 C ASN A1053 10.188 -17.935 15.465 1.00 81.80 C ANISOU 2030 C ASN A1053 9783 11817 9480 -1354 -1066 561 C ATOM 2031 O ASN A1053 9.736 -18.312 14.390 1.00 82.56 O ANISOU 2031 O ASN A1053 9850 12091 9426 -1551 -1065 657 O ATOM 2032 CB ASN A1053 7.979 -16.869 15.960 1.00 84.44 C ANISOU 2032 CB ASN A1053 9817 12343 9923 -1172 -1224 641 C ATOM 2033 CG ASN A1053 7.171 -16.026 16.941 1.00 86.16 C ANISOU 2033 CG ASN A1053 9878 12550 10305 -928 -1302 580 C ATOM 2034 OD1 ASN A1053 7.296 -16.179 18.162 1.00 86.08 O ANISOU 2034 OD1 ASN A1053 9892 12491 10323 -787 -1242 401 O ATOM 2035 ND2 ASN A1053 6.331 -15.137 16.410 1.00 88.70 N ANISOU 2035 ND2 ASN A1053 10024 12939 10739 -878 -1439 725 N ATOM 2036 N THR A1054 11.318 -18.407 15.978 1.00 80.26 N ANISOU 2036 N THR A1054 9732 11466 9296 -1325 -974 444 N ATOM 2037 CA THR A1054 11.971 -19.601 15.440 1.00 79.38 C ANISOU 2037 CA THR A1054 9761 11374 9025 -1509 -844 386 C ATOM 2038 C THR A1054 11.085 -20.782 15.780 1.00 79.16 C ANISOU 2038 C THR A1054 9757 11470 8850 -1606 -746 301 C ATOM 2039 O THR A1054 10.190 -20.661 16.626 1.00 79.73 O ANISOU 2039 O THR A1054 9748 11603 8942 -1508 -769 282 O ATOM 2040 CB THR A1054 13.331 -19.857 16.105 1.00 78.17 C ANISOU 2040 CB THR A1054 9740 11016 8945 -1422 -768 280 C ATOM 2041 OG1 THR A1054 13.143 -20.061 17.514 1.00 77.62 O ANISOU 2041 OG1 THR A1054 9678 10884 8929 -1274 -730 174 O ATOM 2042 CG2 THR A1054 14.275 -18.684 15.893 1.00 78.23 C ANISOU 2042 CG2 THR A1054 9726 10888 9107 -1327 -869 362 C ATOM 2043 N ASN A1055 11.321 -21.923 15.147 1.00 78.55 N ANISOU 2043 N ASN A1055 9778 11434 8631 -1801 -642 243 N ATOM 2044 CA ASN A1055 10.662 -23.149 15.583 1.00 78.29 C ANISOU 2044 CA ASN A1055 9790 11459 8495 -1899 -549 157 C ATOM 2045 C ASN A1055 11.703 -24.076 16.179 1.00 77.09 C ANISOU 2045 C ASN A1055 9788 11113 8387 -1882 -435 36 C ATOM 2046 O ASN A1055 11.556 -25.298 16.135 1.00 77.57 O ANISOU 2046 O ASN A1055 9924 11167 8379 -2022 -346 -39 O ATOM 2047 CB ASN A1055 9.924 -23.827 14.427 1.00 79.52 C ANISOU 2047 CB ASN A1055 9929 11811 8474 -2151 -527 170 C ATOM 2048 CG ASN A1055 8.851 -24.806 14.901 1.00 80.15 C ANISOU 2048 CG ASN A1055 10001 11989 8460 -2252 -481 131 C ATOM 2049 OD1 ASN A1055 8.650 -25.002 16.099 1.00 79.70 O ANISOU 2049 OD1 ASN A1055 9945 11876 8461 -2139 -465 107 O ATOM 2050 ND2 ASN A1055 8.157 -25.422 13.951 1.00 81.79 N ANISOU 2050 ND2 ASN A1055 10191 12371 8511 -2484 -465 129 N ATOM 2051 N GLY A1056 12.755 -23.483 16.742 1.00 75.57 N ANISOU 2051 N GLY A1056 9630 10754 8326 -1713 -446 25 N ATOM 2052 CA GLY A1056 13.885 -24.236 17.257 1.00 74.30 C ANISOU 2052 CA GLY A1056 9597 10411 8224 -1681 -348 -64 C ATOM 2053 C GLY A1056 15.051 -24.348 16.295 1.00 73.85 C ANISOU 2053 C GLY A1056 9617 10278 8165 -1745 -305 -98 C ATOM 2054 O GLY A1056 16.004 -25.068 16.584 1.00 73.51 O ANISOU 2054 O GLY A1056 9672 10086 8171 -1727 -216 -179 O ATOM 2055 N VAL A1057 14.984 -23.658 15.155 1.00 74.02 N ANISOU 2055 N VAL A1057 9577 10420 8127 -1824 -369 -29 N ATOM 2056 CA VAL A1057 16.155 -23.510 14.284 1.00 73.86 C ANISOU 2056 CA VAL A1057 9592 10374 8094 -1869 -347 -40 C ATOM 2057 C VAL A1057 16.522 -22.054 14.112 1.00 73.43 C ANISOU 2057 C VAL A1057 9455 10320 8122 -1771 -476 104 C ATOM 2058 O VAL A1057 15.660 -21.182 14.116 1.00 73.69 O ANISOU 2058 O VAL A1057 9381 10428 8187 -1734 -592 219 O ATOM 2059 CB VAL A1057 15.949 -24.104 12.879 1.00 75.04 C ANISOU 2059 CB VAL A1057 9733 10707 8072 -2101 -302 -84 C ATOM 2060 CG1 VAL A1057 15.631 -25.577 12.972 1.00 76.10 C ANISOU 2060 CG1 VAL A1057 9954 10806 8155 -2213 -181 -248 C ATOM 2061 CG2 VAL A1057 14.862 -23.350 12.124 1.00 76.13 C ANISOU 2061 CG2 VAL A1057 9734 11073 8116 -2198 -415 61 C ATOM 2062 N ILE A1058 17.815 -21.806 13.945 1.00 73.02 N ANISOU 2062 N ILE A1058 9445 10179 8117 -1732 -461 101 N ATOM 2063 CA ILE A1058 18.322 -20.465 13.675 1.00 73.17 C ANISOU 2063 CA ILE A1058 9390 10185 8225 -1670 -590 252 C ATOM 2064 C ILE A1058 19.311 -20.495 12.512 1.00 73.86 C ANISOU 2064 C ILE A1058 9474 10373 8214 -1803 -566 281 C ATOM 2065 O ILE A1058 19.762 -21.565 12.105 1.00 73.83 O ANISOU 2065 O ILE A1058 9538 10413 8100 -1898 -432 139 O ATOM 2066 CB ILE A1058 18.975 -19.838 14.936 1.00 72.08 C ANISOU 2066 CB ILE A1058 9282 9831 8274 -1455 -628 242 C ATOM 2067 CG1 ILE A1058 20.242 -20.593 15.347 1.00 71.09 C ANISOU 2067 CG1 ILE A1058 9269 9586 8156 -1417 -505 129 C ATOM 2068 CG2 ILE A1058 17.985 -19.826 16.095 1.00 71.61 C ANISOU 2068 CG2 ILE A1058 9200 9728 8280 -1331 -644 192 C ATOM 2069 CD1 ILE A1058 20.895 -20.047 16.607 1.00 69.71 C ANISOU 2069 CD1 ILE A1058 9116 9234 8136 -1226 -536 115 C ATOM 2070 N THR A1059 19.642 -19.313 11.993 1.00 74.71 N ANISOU 2070 N THR A1059 9489 10523 8373 -1809 -700 463 N ATOM 2071 CA THR A1059 20.506 -19.173 10.812 1.00 75.81 C ANISOU 2071 CA THR A1059 9583 10825 8395 -1958 -703 536 C ATOM 2072 C THR A1059 21.964 -18.996 11.219 1.00 75.40 C ANISOU 2072 C THR A1059 9590 10630 8428 -1861 -675 511 C ATOM 2073 O THR A1059 22.257 -18.856 12.398 1.00 74.34 O ANISOU 2073 O THR A1059 9523 10270 8450 -1683 -672 458 O ATOM 2074 CB THR A1059 20.100 -17.951 9.984 1.00 77.03 C ANISOU 2074 CB THR A1059 9582 11120 8564 -2042 -886 803 C ATOM 2075 OG1 THR A1059 20.548 -16.763 10.642 1.00 76.65 O ANISOU 2075 OG1 THR A1059 9512 10864 8748 -1886 -1024 934 O ATOM 2076 CG2 THR A1059 18.592 -17.892 9.818 1.00 77.34 C ANISOU 2076 CG2 THR A1059 9545 11266 8573 -2089 -945 863 C ATOM 2077 N LYS A1060 22.871 -18.987 10.244 1.00 76.74 N ANISOU 2077 N LYS A1060 9717 10962 8476 -1987 -655 552 N ATOM 2078 CA LYS A1060 24.310 -18.797 10.519 1.00 76.64 C ANISOU 2078 CA LYS A1060 9741 10855 8524 -1913 -631 546 C ATOM 2079 C LYS A1060 24.586 -17.392 11.081 1.00 76.29 C ANISOU 2079 C LYS A1060 9654 10646 8686 -1801 -809 744 C ATOM 2080 O LYS A1060 25.333 -17.244 12.044 1.00 75.10 O ANISOU 2080 O LYS A1060 9571 10293 8669 -1652 -797 693 O ATOM 2081 CB LYS A1060 25.145 -19.008 9.240 1.00 78.38 C ANISOU 2081 CB LYS A1060 9888 11348 8544 -2091 -584 561 C ATOM 2082 CG LYS A1060 26.632 -19.425 9.456 1.00 78.61 C ANISOU 2082 CG LYS A1060 9970 11326 8571 -2026 -475 450 C ATOM 2083 CD LYS A1060 27.679 -18.487 8.766 1.00 80.67 C ANISOU 2083 CD LYS A1060 10118 11744 8788 -2110 -573 653 C ATOM 2084 CE LYS A1060 27.388 -18.087 7.284 1.00 83.16 C ANISOU 2084 CE LYS A1060 10268 12433 8896 -2354 -650 818 C ATOM 2085 NZ LYS A1060 27.626 -19.163 6.275 1.00 84.71 N ANISOU 2085 NZ LYS A1060 10425 12934 8827 -2506 -486 615 N ATOM 2086 N ASP A1061 23.990 -16.369 10.464 1.00 77.51 N ANISOU 2086 N ASP A1061 9685 10887 8876 -1880 -980 970 N ATOM 2087 CA ASP A1061 24.128 -14.978 10.925 1.00 77.74 C ANISOU 2087 CA ASP A1061 9661 10731 9146 -1781 -1173 1159 C ATOM 2088 C ASP A1061 23.732 -14.829 12.379 1.00 76.26 C ANISOU 2088 C ASP A1061 9551 10264 9160 -1557 -1178 1027 C ATOM 2089 O ASP A1061 24.385 -14.117 13.133 1.00 76.06 O ANISOU 2089 O ASP A1061 9544 10039 9314 -1436 -1251 1043 O ATOM 2090 CB ASP A1061 23.248 -14.031 10.104 1.00 79.56 C ANISOU 2090 CB ASP A1061 9738 11070 9419 -1886 -1358 1418 C ATOM 2091 CG ASP A1061 23.887 -13.621 8.789 1.00 82.18 C ANISOU 2091 CG ASP A1061 9946 11658 9619 -2102 -1435 1651 C ATOM 2092 OD1 ASP A1061 24.977 -13.005 8.822 1.00 82.37 O ANISOU 2092 OD1 ASP A1061 9956 11615 9725 -2099 -1504 1760 O ATOM 2093 OD2 ASP A1061 23.281 -13.897 7.723 1.00 84.91 O ANISOU 2093 OD2 ASP A1061 10195 12296 9769 -2286 -1432 1734 O ATOM 2094 N GLU A1062 22.648 -15.496 12.757 1.00 75.55 N ANISOU 2094 N GLU A1062 9492 10186 9026 -1517 -1104 895 N ATOM 2095 CA GLU A1062 22.071 -15.357 14.093 1.00 74.46 C ANISOU 2095 CA GLU A1062 9393 9852 9045 -1322 -1112 774 C ATOM 2096 C GLU A1062 22.921 -16.047 15.161 1.00 72.72 C ANISOU 2096 C GLU A1062 9293 9505 8831 -1208 -979 590 C ATOM 2097 O GLU A1062 23.205 -15.464 16.208 1.00 72.24 O ANISOU 2097 O GLU A1062 9244 9271 8931 -1055 -1031 546 O ATOM 2098 CB GLU A1062 20.642 -15.897 14.095 1.00 74.62 C ANISOU 2098 CB GLU A1062 9389 9974 8987 -1341 -1075 715 C ATOM 2099 CG GLU A1062 19.696 -15.079 13.229 1.00 76.07 C ANISOU 2099 CG GLU A1062 9432 10268 9202 -1421 -1228 915 C ATOM 2100 CD GLU A1062 18.318 -15.695 13.125 1.00 76.98 C ANISOU 2100 CD GLU A1062 9516 10527 9206 -1465 -1182 865 C ATOM 2101 OE1 GLU A1062 18.225 -16.923 12.869 1.00 76.67 O ANISOU 2101 OE1 GLU A1062 9549 10615 8966 -1575 -1029 741 O ATOM 2102 OE2 GLU A1062 17.326 -14.942 13.293 1.00 77.83 O ANISOU 2102 OE2 GLU A1062 9518 10613 9439 -1391 -1305 949 O ATOM 2103 N ALA A1063 23.329 -17.281 14.881 1.00 71.85 N ANISOU 2103 N ALA A1063 9259 9484 8554 -1286 -814 480 N ATOM 2104 CA ALA A1063 24.284 -17.996 15.720 1.00 70.62 C ANISOU 2104 CA ALA A1063 9202 9222 8406 -1198 -690 346 C ATOM 2105 C ALA A1063 25.481 -17.114 16.079 1.00 70.43 C ANISOU 2105 C ALA A1063 9172 9085 8503 -1124 -766 416 C ATOM 2106 O ALA A1063 25.930 -17.110 17.227 1.00 69.89 O ANISOU 2106 O ALA A1063 9148 8882 8524 -990 -744 338 O ATOM 2107 CB ALA A1063 24.760 -19.261 15.017 1.00 70.49 C ANISOU 2107 CB ALA A1063 9241 9314 8226 -1311 -530 250 C ATOM 2108 N GLU A1064 25.980 -16.361 15.099 1.00 71.25 N ANISOU 2108 N GLU A1064 9208 9263 8598 -1227 -864 577 N ATOM 2109 CA GLU A1064 27.173 -15.522 15.281 1.00 71.36 C ANISOU 2109 CA GLU A1064 9207 9190 8715 -1194 -947 670 C ATOM 2110 C GLU A1064 26.892 -14.269 16.123 1.00 71.04 C ANISOU 2110 C GLU A1064 9129 8953 8909 -1070 -1115 718 C ATOM 2111 O GLU A1064 27.678 -13.922 17.006 1.00 70.59 O ANISOU 2111 O GLU A1064 9103 8760 8958 -970 -1132 672 O ATOM 2112 CB GLU A1064 27.768 -15.112 13.920 1.00 72.91 C ANISOU 2112 CB GLU A1064 9321 9562 8819 -1369 -1009 853 C ATOM 2113 CG GLU A1064 29.303 -15.090 13.883 1.00 73.56 C ANISOU 2113 CG GLU A1064 9414 9660 8873 -1383 -975 880 C ATOM 2114 CD GLU A1064 29.879 -14.111 12.873 1.00 76.14 C ANISOU 2114 CD GLU A1064 9628 10109 9193 -1530 -1122 1128 C ATOM 2115 OE1 GLU A1064 29.277 -13.948 11.787 1.00 78.28 O ANISOU 2115 OE1 GLU A1064 9808 10567 9367 -1680 -1179 1257 O ATOM 2116 OE2 GLU A1064 30.942 -13.513 13.166 1.00 76.47 O ANISOU 2116 OE2 GLU A1064 9659 10077 9316 -1510 -1186 1207 O ATOM 2117 N LYS A1065 25.785 -13.586 15.840 1.00 71.34 N ANISOU 2117 N LYS A1065 9089 8980 9035 -1077 -1241 801 N ATOM 2118 CA LYS A1065 25.386 -12.422 16.622 1.00 71.60 C ANISOU 2118 CA LYS A1065 9074 8813 9319 -942 -1400 807 C ATOM 2119 C LYS A1065 25.305 -12.809 18.097 1.00 70.02 C ANISOU 2119 C LYS A1065 8938 8511 9155 -771 -1311 576 C ATOM 2120 O LYS A1065 25.771 -12.075 18.981 1.00 70.07 O ANISOU 2120 O LYS A1065 8940 8359 9324 -660 -1386 517 O ATOM 2121 CB LYS A1065 24.029 -11.905 16.151 1.00 72.90 C ANISOU 2121 CB LYS A1065 9139 9001 9558 -953 -1514 897 C ATOM 2122 CG LYS A1065 23.676 -10.531 16.704 1.00 75.49 C ANISOU 2122 CG LYS A1065 9386 9105 10191 -823 -1711 929 C ATOM 2123 CD LYS A1065 22.176 -10.233 16.621 1.00 77.79 C ANISOU 2123 CD LYS A1065 9582 9409 10563 -768 -1784 940 C ATOM 2124 CE LYS A1065 21.844 -8.939 17.365 1.00 79.70 C ANISOU 2124 CE LYS A1065 9743 9399 11141 -595 -1962 899 C ATOM 2125 NZ LYS A1065 20.384 -8.659 17.383 1.00 81.20 N ANISOU 2125 NZ LYS A1065 9825 9603 11423 -511 -2025 884 N ATOM 2126 N LEU A1066 24.714 -13.977 18.338 1.00 68.48 N ANISOU 2126 N LEU A1066 8792 8425 8800 -768 -1156 452 N ATOM 2127 CA LEU A1066 24.561 -14.530 19.672 1.00 67.02 C ANISOU 2127 CA LEU A1066 8652 8206 8606 -638 -1060 264 C ATOM 2128 C LEU A1066 25.905 -14.908 20.273 1.00 65.68 C ANISOU 2128 C LEU A1066 8552 7991 8409 -609 -978 215 C ATOM 2129 O LEU A1066 26.131 -14.735 21.473 1.00 65.30 O ANISOU 2129 O LEU A1066 8506 7878 8426 -492 -975 104 O ATOM 2130 CB LEU A1066 23.686 -15.775 19.612 1.00 66.61 C ANISOU 2130 CB LEU A1066 8633 8289 8388 -683 -923 192 C ATOM 2131 CG LEU A1066 23.132 -16.230 20.955 1.00 66.42 C ANISOU 2131 CG LEU A1066 8611 8270 8355 -566 -857 38 C ATOM 2132 CD1 LEU A1066 22.012 -15.298 21.394 1.00 67.74 C ANISOU 2132 CD1 LEU A1066 8673 8424 8640 -464 -976 -4 C ATOM 2133 CD2 LEU A1066 22.643 -17.653 20.855 1.00 66.05 C ANISOU 2133 CD2 LEU A1066 8617 8334 8142 -645 -710 -2 C ATOM 2134 N PHE A1067 26.784 -15.454 19.440 1.00 64.82 N ANISOU 2134 N PHE A1067 8487 7946 8194 -718 -906 290 N ATOM 2135 CA PHE A1067 28.137 -15.788 19.875 1.00 63.81 C ANISOU 2135 CA PHE A1067 8409 7787 8045 -694 -833 269 C ATOM 2136 C PHE A1067 28.922 -14.544 20.240 1.00 63.84 C ANISOU 2136 C PHE A1067 8378 7676 8201 -650 -973 326 C ATOM 2137 O PHE A1067 29.645 -14.546 21.232 1.00 63.39 O ANISOU 2137 O PHE A1067 8342 7565 8178 -569 -947 255 O ATOM 2138 CB PHE A1067 28.901 -16.567 18.802 1.00 63.79 C ANISOU 2138 CB PHE A1067 8438 7896 7903 -815 -731 323 C ATOM 2139 CG PHE A1067 30.344 -16.796 19.140 1.00 62.96 C ANISOU 2139 CG PHE A1067 8361 7770 7789 -786 -670 323 C ATOM 2140 CD1 PHE A1067 30.718 -17.850 19.963 1.00 62.88 C ANISOU 2140 CD1 PHE A1067 8406 7740 7744 -711 -530 219 C ATOM 2141 CD2 PHE A1067 31.327 -15.953 18.653 1.00 62.95 C ANISOU 2141 CD2 PHE A1067 8319 7776 7821 -839 -762 447 C ATOM 2142 CE1 PHE A1067 32.060 -18.065 20.286 1.00 62.45 C ANISOU 2142 CE1 PHE A1067 8363 7675 7688 -677 -476 234 C ATOM 2143 CE2 PHE A1067 32.668 -16.161 18.966 1.00 63.02 C ANISOU 2143 CE2 PHE A1067 8343 7787 7812 -814 -705 454 C ATOM 2144 CZ PHE A1067 33.035 -17.221 19.782 1.00 62.20 C ANISOU 2144 CZ PHE A1067 8292 7667 7674 -726 -559 343 C ATOM 2145 N ASN A1068 28.792 -13.487 19.443 1.00 64.42 N ANISOU 2145 N ASN A1068 8388 7714 8373 -714 -1130 465 N ATOM 2146 CA ASN A1068 29.497 -12.247 19.746 1.00 64.99 C ANISOU 2146 CA ASN A1068 8422 7645 8625 -688 -1287 529 C ATOM 2147 C ASN A1068 29.108 -11.700 21.109 1.00 65.21 C ANISOU 2147 C ASN A1068 8437 7536 8804 -531 -1341 362 C ATOM 2148 O ASN A1068 29.977 -11.276 21.869 1.00 65.47 O ANISOU 2148 O ASN A1068 8476 7488 8909 -484 -1373 312 O ATOM 2149 CB ASN A1068 29.254 -11.196 18.681 1.00 66.19 C ANISOU 2149 CB ASN A1068 8493 7763 8892 -788 -1468 733 C ATOM 2150 CG ASN A1068 29.854 -11.573 17.366 1.00 66.16 C ANISOU 2150 CG ASN A1068 8474 7939 8724 -961 -1431 906 C ATOM 2151 OD1 ASN A1068 30.894 -12.238 17.302 1.00 64.29 O ANISOU 2151 OD1 ASN A1068 8280 7797 8351 -996 -1313 888 O ATOM 2152 ND2 ASN A1068 29.200 -11.159 16.291 1.00 67.88 N ANISOU 2152 ND2 ASN A1068 8614 8231 8946 -1072 -1531 1075 N ATOM 2153 N GLN A1069 27.815 -11.722 21.426 1.00 65.24 N ANISOU 2153 N GLN A1069 8409 7541 8839 -457 -1347 263 N ATOM 2154 CA GLN A1069 27.362 -11.329 22.759 1.00 65.43 C ANISOU 2154 CA GLN A1069 8399 7494 8967 -305 -1374 63 C ATOM 2155 C GLN A1069 28.024 -12.131 23.863 1.00 64.11 C ANISOU 2155 C GLN A1069 8281 7403 8674 -254 -1234 -65 C ATOM 2156 O GLN A1069 28.391 -11.574 24.888 1.00 64.55 O ANISOU 2156 O GLN A1069 8308 7402 8815 -170 -1279 -190 O ATOM 2157 CB GLN A1069 25.849 -11.454 22.886 1.00 65.93 C ANISOU 2157 CB GLN A1069 8409 7610 9031 -241 -1370 -21 C ATOM 2158 CG GLN A1069 25.137 -10.146 22.648 1.00 68.18 C ANISOU 2158 CG GLN A1069 8596 7746 9561 -184 -1562 0 C ATOM 2159 CD GLN A1069 23.805 -10.343 22.005 1.00 69.56 C ANISOU 2159 CD GLN A1069 8718 8005 9705 -199 -1568 52 C ATOM 2160 OE1 GLN A1069 23.135 -11.358 22.248 1.00 68.79 O ANISOU 2160 OE1 GLN A1069 8640 8072 9423 -198 -1430 -24 O ATOM 2161 NE2 GLN A1069 23.401 -9.380 21.162 1.00 70.95 N ANISOU 2161 NE2 GLN A1069 8816 8074 10066 -226 -1738 207 N ATOM 2162 N ASP A1070 28.171 -13.433 23.656 1.00 62.76 N ANISOU 2162 N ASP A1070 8172 7362 8310 -309 -1070 -36 N ATOM 2163 CA ASP A1070 28.820 -14.283 24.648 1.00 61.95 C ANISOU 2163 CA ASP A1070 8104 7331 8100 -269 -942 -113 C ATOM 2164 C ASP A1070 30.337 -14.046 24.700 1.00 61.54 C ANISOU 2164 C ASP A1070 8078 7238 8067 -296 -952 -46 C ATOM 2165 O ASP A1070 30.962 -14.258 25.733 1.00 61.61 O ANISOU 2165 O ASP A1070 8081 7280 8045 -244 -905 -112 O ATOM 2166 CB ASP A1070 28.501 -15.767 24.401 1.00 61.32 C ANISOU 2166 CB ASP A1070 8077 7364 7855 -317 -777 -94 C ATOM 2167 CG ASP A1070 27.000 -16.091 24.528 1.00 62.25 C ANISOU 2167 CG ASP A1070 8164 7552 7935 -298 -760 -162 C ATOM 2168 OD1 ASP A1070 26.189 -15.163 24.774 1.00 64.97 O ANISOU 2168 OD1 ASP A1070 8436 7870 8377 -235 -870 -227 O ATOM 2169 OD2 ASP A1070 26.630 -17.280 24.370 1.00 61.05 O ANISOU 2169 OD2 ASP A1070 8051 7477 7666 -348 -641 -152 O ATOM 2170 N VAL A1071 30.939 -13.601 23.606 1.00 61.50 N ANISOU 2170 N VAL A1071 8083 7187 8098 -387 -1016 97 N ATOM 2171 CA VAL A1071 32.338 -13.185 23.665 1.00 61.46 C ANISOU 2171 CA VAL A1071 8080 7148 8121 -417 -1052 168 C ATOM 2172 C VAL A1071 32.445 -11.922 24.531 1.00 62.21 C ANISOU 2172 C VAL A1071 8125 7118 8392 -353 -1204 84 C ATOM 2173 O VAL A1071 33.259 -11.866 25.456 1.00 62.01 O ANISOU 2173 O VAL A1071 8095 7105 8359 -317 -1188 21 O ATOM 2174 CB VAL A1071 32.934 -12.938 22.258 1.00 61.80 C ANISOU 2174 CB VAL A1071 8120 7209 8149 -548 -1098 357 C ATOM 2175 CG1 VAL A1071 34.326 -12.348 22.349 1.00 62.14 C ANISOU 2175 CG1 VAL A1071 8148 7226 8234 -587 -1161 443 C ATOM 2176 CG2 VAL A1071 32.995 -14.221 21.488 1.00 61.41 C ANISOU 2176 CG2 VAL A1071 8110 7298 7921 -606 -934 387 C ATOM 2177 N ASP A1072 31.605 -10.927 24.232 1.00 63.14 N ANISOU 2177 N ASP A1072 8197 7116 8676 -339 -1353 77 N ATOM 2178 CA ASP A1072 31.570 -9.663 24.972 1.00 64.33 C ANISOU 2178 CA ASP A1072 8291 7108 9040 -270 -1514 -35 C ATOM 2179 C ASP A1072 31.560 -9.910 26.472 1.00 63.83 C ANISOU 2179 C ASP A1072 8209 7117 8925 -161 -1442 -263 C ATOM 2180 O ASP A1072 32.494 -9.517 27.173 1.00 64.33 O ANISOU 2180 O ASP A1072 8262 7159 9018 -159 -1474 -317 O ATOM 2181 CB ASP A1072 30.346 -8.837 24.576 1.00 65.71 C ANISOU 2181 CB ASP A1072 8406 7157 9401 -229 -1651 -51 C ATOM 2182 CG ASP A1072 30.550 -8.078 23.280 1.00 67.76 C ANISOU 2182 CG ASP A1072 8645 7305 9795 -345 -1802 192 C ATOM 2183 OD1 ASP A1072 30.024 -8.515 22.231 1.00 68.27 O ANISOU 2183 OD1 ASP A1072 8710 7458 9769 -421 -1771 339 O ATOM 2184 OD2 ASP A1072 31.239 -7.035 23.315 1.00 70.98 O ANISOU 2184 OD2 ASP A1072 9025 7548 10395 -375 -1959 244 O ATOM 2185 N ALA A1073 30.517 -10.586 26.950 1.00 62.92 N ANISOU 2185 N ALA A1073 8078 7117 8711 -89 -1345 -383 N ATOM 2186 CA ALA A1073 30.387 -10.935 28.363 1.00 62.52 C ANISOU 2186 CA ALA A1073 7985 7200 8569 -3 -1267 -581 C ATOM 2187 C ALA A1073 31.635 -11.634 28.914 1.00 61.60 C ANISOU 2187 C ALA A1073 7901 7196 8308 -42 -1164 -530 C ATOM 2188 O ALA A1073 32.092 -11.324 30.018 1.00 62.21 O ANISOU 2188 O ALA A1073 7927 7332 8377 -4 -1178 -661 O ATOM 2189 CB ALA A1073 29.173 -11.806 28.569 1.00 61.86 C ANISOU 2189 CB ALA A1073 7882 7263 8357 37 -1161 -640 C ATOM 2190 N ALA A1074 32.181 -12.575 28.148 1.00 60.31 N ANISOU 2190 N ALA A1074 7808 7072 8031 -117 -1061 -348 N ATOM 2191 CA ALA A1074 33.353 -13.331 28.586 1.00 59.58 C ANISOU 2191 CA ALA A1074 7737 7080 7819 -142 -957 -278 C ATOM 2192 C ALA A1074 34.547 -12.412 28.768 1.00 60.04 C ANISOU 2192 C ALA A1074 7778 7071 7960 -173 -1057 -257 C ATOM 2193 O ALA A1074 35.270 -12.508 29.760 1.00 60.03 O ANISOU 2193 O ALA A1074 7743 7165 7901 -157 -1029 -304 O ATOM 2194 CB ALA A1074 33.684 -14.424 27.588 1.00 58.68 C ANISOU 2194 CB ALA A1074 7692 6993 7608 -205 -838 -114 C ATOM 2195 N VAL A1075 34.735 -11.522 27.799 1.00 60.55 N ANISOU 2195 N VAL A1075 7858 6986 8160 -232 -1183 -169 N ATOM 2196 CA VAL A1075 35.834 -10.556 27.820 1.00 61.36 C ANISOU 2196 CA VAL A1075 7944 7002 8368 -286 -1305 -121 C ATOM 2197 C VAL A1075 35.690 -9.558 28.975 1.00 62.89 C ANISOU 2197 C VAL A1075 8075 7133 8686 -226 -1418 -336 C ATOM 2198 O VAL A1075 36.678 -9.209 29.606 1.00 63.34 O ANISOU 2198 O VAL A1075 8108 7214 8742 -253 -1451 -361 O ATOM 2199 CB VAL A1075 35.963 -9.810 26.455 1.00 61.80 C ANISOU 2199 CB VAL A1075 8012 6918 8549 -383 -1434 56 C ATOM 2200 CG1 VAL A1075 36.934 -8.645 26.553 1.00 62.03 C ANISOU 2200 CG1 VAL A1075 8012 6828 8727 -449 -1597 101 C ATOM 2201 CG2 VAL A1075 36.400 -10.789 25.363 1.00 60.15 C ANISOU 2201 CG2 VAL A1075 7845 6826 8181 -460 -1313 244 C ATOM 2202 N ARG A1076 34.466 -9.114 29.254 1.00 63.86 N ANISOU 2202 N ARG A1076 8160 7193 8911 -144 -1474 -505 N ATOM 2203 CA ARG A1076 34.206 -8.260 30.411 1.00 65.67 C ANISOU 2203 CA ARG A1076 8311 7392 9247 -68 -1561 -769 C ATOM 2204 C ARG A1076 34.575 -8.962 31.720 1.00 65.40 C ANISOU 2204 C ARG A1076 8234 7608 9007 -39 -1435 -891 C ATOM 2205 O ARG A1076 35.184 -8.358 32.603 1.00 66.53 O ANISOU 2205 O ARG A1076 8322 7776 9178 -42 -1493 -1033 O ATOM 2206 CB ARG A1076 32.740 -7.822 30.443 1.00 66.78 C ANISOU 2206 CB ARG A1076 8401 7458 9513 33 -1618 -936 C ATOM 2207 CG ARG A1076 32.374 -6.821 29.363 1.00 68.77 C ANISOU 2207 CG ARG A1076 8659 7441 10029 13 -1790 -838 C ATOM 2208 CD ARG A1076 31.094 -6.097 29.704 1.00 72.23 C ANISOU 2208 CD ARG A1076 9013 7778 10651 140 -1880 -1062 C ATOM 2209 NE ARG A1076 30.550 -5.366 28.558 1.00 75.70 N ANISOU 2209 NE ARG A1076 9447 7984 11328 124 -2029 -912 N ATOM 2210 CZ ARG A1076 29.743 -5.881 27.621 1.00 76.90 C ANISOU 2210 CZ ARG A1076 9618 8178 11421 107 -1987 -748 C ATOM 2211 NH1 ARG A1076 29.358 -7.163 27.655 1.00 75.33 N ANISOU 2211 NH1 ARG A1076 9455 8220 10945 103 -1798 -724 N ATOM 2212 NH2 ARG A1076 29.316 -5.100 26.629 1.00 78.71 N ANISOU 2212 NH2 ARG A1076 9820 8206 11880 82 -2145 -595 N ATOM 2213 N GLY A1077 34.212 -10.236 31.837 1.00 64.22 N ANISOU 2213 N GLY A1077 8099 7646 8656 -23 -1271 -826 N ATOM 2214 CA GLY A1077 34.648 -11.060 32.956 1.00 64.05 C ANISOU 2214 CA GLY A1077 8029 7875 8431 -18 -1151 -856 C ATOM 2215 C GLY A1077 36.163 -11.079 33.125 1.00 64.12 C ANISOU 2215 C GLY A1077 8048 7918 8395 -90 -1147 -735 C ATOM 2216 O GLY A1077 36.674 -10.901 34.233 1.00 65.05 O ANISOU 2216 O GLY A1077 8089 8185 8441 -94 -1151 -844 O ATOM 2217 N ILE A1078 36.886 -11.279 32.028 1.00 63.48 N ANISOU 2217 N ILE A1078 8047 7729 8342 -154 -1140 -515 N ATOM 2218 CA ILE A1078 38.346 -11.350 32.064 1.00 63.60 C ANISOU 2218 CA ILE A1078 8065 7792 8309 -222 -1131 -376 C ATOM 2219 C ILE A1078 38.964 -10.033 32.534 1.00 65.68 C ANISOU 2219 C ILE A1078 8283 7977 8694 -263 -1288 -490 C ATOM 2220 O ILE A1078 39.843 -10.019 33.395 1.00 66.21 O ANISOU 2220 O ILE A1078 8296 8182 8678 -293 -1278 -511 O ATOM 2221 CB ILE A1078 38.912 -11.740 30.689 1.00 62.63 C ANISOU 2221 CB ILE A1078 8016 7586 8191 -282 -1099 -141 C ATOM 2222 CG1 ILE A1078 38.566 -13.207 30.385 1.00 61.46 C ANISOU 2222 CG1 ILE A1078 7904 7535 7912 -248 -924 -48 C ATOM 2223 CG2 ILE A1078 40.411 -11.524 30.656 1.00 62.43 C ANISOU 2223 CG2 ILE A1078 7975 7600 8145 -355 -1123 -11 C ATOM 2224 CD1 ILE A1078 38.535 -13.576 28.913 1.00 59.94 C ANISOU 2224 CD1 ILE A1078 7779 7261 7733 -291 -891 95 C ATOM 2225 N LEU A1079 38.482 -8.923 31.987 1.00 67.35 N ANISOU 2225 N LEU A1079 8509 7962 9116 -269 -1442 -560 N ATOM 2226 CA LEU A1079 38.942 -7.598 32.396 1.00 69.52 C ANISOU 2226 CA LEU A1079 8744 8106 9564 -309 -1615 -690 C ATOM 2227 C LEU A1079 38.636 -7.287 33.866 1.00 71.36 C ANISOU 2227 C LEU A1079 8883 8469 9761 -249 -1621 -997 C ATOM 2228 O LEU A1079 39.236 -6.378 34.440 1.00 73.08 O ANISOU 2228 O LEU A1079 9055 8640 10071 -293 -1735 -1131 O ATOM 2229 CB LEU A1079 38.309 -6.510 31.525 1.00 70.52 C ANISOU 2229 CB LEU A1079 8892 7937 9966 -313 -1788 -699 C ATOM 2230 CG LEU A1079 38.563 -6.544 30.021 1.00 69.79 C ANISOU 2230 CG LEU A1079 8862 7726 9926 -399 -1825 -402 C ATOM 2231 CD1 LEU A1079 37.918 -5.322 29.370 1.00 70.82 C ANISOU 2231 CD1 LEU A1079 8983 7568 10358 -408 -2029 -411 C ATOM 2232 CD2 LEU A1079 40.057 -6.613 29.731 1.00 70.19 C ANISOU 2232 CD2 LEU A1079 8925 7845 9899 -520 -1825 -195 C ATOM 2233 N ARG A1080 37.691 -8.012 34.463 1.00 71.52 N ANISOU 2233 N ARG A1080 8864 8665 9645 -161 -1505 -1116 N ATOM 2234 CA ARG A1080 37.320 -7.802 35.865 1.00 73.44 C ANISOU 2234 CA ARG A1080 8990 9103 9809 -110 -1496 -1412 C ATOM 2235 C ARG A1080 37.781 -8.953 36.747 1.00 72.79 C ANISOU 2235 C ARG A1080 8852 9368 9437 -132 -1338 -1332 C ATOM 2236 O ARG A1080 37.052 -9.369 37.652 1.00 73.63 O ANISOU 2236 O ARG A1080 8865 9709 9400 -82 -1266 -1481 O ATOM 2237 CB ARG A1080 35.806 -7.661 35.992 1.00 73.95 C ANISOU 2237 CB ARG A1080 9012 9151 9933 2 -1498 -1621 C ATOM 2238 CG ARG A1080 35.255 -6.515 35.208 1.00 76.55 C ANISOU 2238 CG ARG A1080 9372 9140 10573 40 -1663 -1700 C ATOM 2239 CD ARG A1080 33.745 -6.632 35.019 1.00 79.09 C ANISOU 2239 CD ARG A1080 9665 9447 10937 152 -1641 -1809 C ATOM 2240 NE ARG A1080 33.310 -5.892 33.835 1.00 81.06 N ANISOU 2240 NE ARG A1080 9971 9364 11463 165 -1775 -1717 N ATOM 2241 CZ ARG A1080 33.277 -4.561 33.742 1.00 84.59 C ANISOU 2241 CZ ARG A1080 10388 9535 12218 189 -1964 -1861 C ATOM 2242 NH1 ARG A1080 32.869 -4.000 32.607 1.00 85.57 N ANISOU 2242 NH1 ARG A1080 10552 9376 12583 188 -2086 -1711 N ATOM 2243 NH2 ARG A1080 33.640 -3.781 34.769 1.00 86.69 N ANISOU 2243 NH2 ARG A1080 10573 9802 12560 207 -2039 -2151 N ATOM 2244 N ASN A1081 38.985 -9.458 36.495 1.00 71.70 N ANISOU 2244 N ASN A1081 8751 9274 9215 -210 -1291 -1085 N ATOM 2245 CA ASN A1081 39.477 -10.634 37.204 1.00 70.98 C ANISOU 2245 CA ASN A1081 8604 9480 8883 -228 -1148 -947 C ATOM 2246 C ASN A1081 40.974 -10.505 37.482 1.00 71.48 C ANISOU 2246 C ASN A1081 8641 9625 8891 -317 -1168 -826 C ATOM 2247 O ASN A1081 41.796 -10.684 36.585 1.00 70.98 O ANISOU 2247 O ASN A1081 8653 9441 8873 -358 -1163 -599 O ATOM 2248 CB ASN A1081 39.159 -11.880 36.377 1.00 69.10 C ANISOU 2248 CB ASN A1081 8446 9214 8592 -197 -1019 -706 C ATOM 2249 CG ASN A1081 39.476 -13.175 37.100 1.00 68.35 C ANISOU 2249 CG ASN A1081 8287 9387 8295 -202 -879 -551 C ATOM 2250 OD1 ASN A1081 40.636 -13.585 37.199 1.00 66.94 O ANISOU 2250 OD1 ASN A1081 8093 9287 8054 -245 -840 -371 O ATOM 2251 ND2 ASN A1081 38.433 -13.853 37.568 1.00 68.20 N ANISOU 2251 ND2 ASN A1081 8222 9506 8183 -159 -806 -596 N ATOM 2252 N ALA A1082 41.323 -10.196 38.730 1.00 72.96 N ANISOU 2252 N ALA A1082 8706 10048 8966 -354 -1189 -983 N ATOM 2253 CA ALA A1082 42.716 -9.919 39.125 1.00 73.62 C ANISOU 2253 CA ALA A1082 8742 10235 8992 -453 -1227 -902 C ATOM 2254 C ALA A1082 43.760 -10.823 38.443 1.00 72.29 C ANISOU 2254 C ALA A1082 8624 10072 8768 -481 -1140 -542 C ATOM 2255 O ALA A1082 44.831 -10.350 38.053 1.00 72.44 O ANISOU 2255 O ALA A1082 8665 10017 8841 -556 -1206 -437 O ATOM 2256 CB ALA A1082 42.857 -10.002 40.645 1.00 75.02 C ANISOU 2256 CB ALA A1082 8756 10785 8964 -490 -1200 -1051 C ATOM 2257 N LYS A1083 43.438 -12.111 38.305 1.00 71.01 N ANISOU 2257 N LYS A1083 8473 9997 8510 -421 -998 -365 N ATOM 2258 CA LYS A1083 44.336 -13.089 37.679 1.00 69.87 C ANISOU 2258 CA LYS A1083 8361 9853 8330 -421 -901 -55 C ATOM 2259 C LYS A1083 44.412 -12.943 36.161 1.00 68.65 C ANISOU 2259 C LYS A1083 8339 9416 8326 -412 -920 47 C ATOM 2260 O LYS A1083 45.501 -12.863 35.595 1.00 68.69 O ANISOU 2260 O LYS A1083 8358 9390 8349 -459 -932 207 O ATOM 2261 CB LYS A1083 43.902 -14.526 38.019 1.00 69.33 C ANISOU 2261 CB LYS A1083 8257 9932 8152 -359 -755 87 C ATOM 2262 CG LYS A1083 44.542 -15.106 39.270 1.00 70.38 C ANISOU 2262 CG LYS A1083 8238 10392 8110 -392 -706 192 C ATOM 2263 CD LYS A1083 44.198 -14.300 40.515 1.00 72.03 C ANISOU 2263 CD LYS A1083 8326 10830 8210 -446 -782 -57 C ATOM 2264 CE LYS A1083 44.606 -15.031 41.796 1.00 73.24 C ANISOU 2264 CE LYS A1083 8303 11369 8154 -490 -724 69 C ATOM 2265 NZ LYS A1083 46.085 -15.168 41.952 1.00 73.69 N ANISOU 2265 NZ LYS A1083 8299 11535 8162 -547 -722 282 N ATOM 2266 N LEU A1084 43.259 -12.926 35.505 1.00 67.74 N ANISOU 2266 N LEU A1084 8304 9130 8301 -361 -922 -36 N ATOM 2267 CA LEU A1084 43.221 -12.985 34.047 1.00 66.72 C ANISOU 2267 CA LEU A1084 8283 8789 8277 -360 -920 80 C ATOM 2268 C LEU A1084 43.511 -11.654 33.346 1.00 67.36 C ANISOU 2268 C LEU A1084 8402 8680 8509 -433 -1081 45 C ATOM 2269 O LEU A1084 44.144 -11.645 32.281 1.00 67.11 O ANISOU 2269 O LEU A1084 8413 8570 8513 -480 -1089 214 O ATOM 2270 CB LEU A1084 41.884 -13.549 33.582 1.00 65.74 C ANISOU 2270 CB LEU A1084 8219 8581 8179 -292 -858 32 C ATOM 2271 CG LEU A1084 41.714 -15.017 33.962 1.00 65.25 C ANISOU 2271 CG LEU A1084 8134 8658 8000 -238 -700 138 C ATOM 2272 CD1 LEU A1084 40.281 -15.457 33.753 1.00 65.29 C ANISOU 2272 CD1 LEU A1084 8180 8608 8018 -189 -659 55 C ATOM 2273 CD2 LEU A1084 42.666 -15.900 33.169 1.00 64.42 C ANISOU 2273 CD2 LEU A1084 8059 8533 7884 -236 -604 356 C ATOM 2274 N LYS A1085 43.075 -10.538 33.931 1.00 68.26 N ANISOU 2274 N LYS A1085 8489 8728 8718 -449 -1214 -170 N ATOM 2275 CA LYS A1085 43.284 -9.236 33.297 1.00 69.16 C ANISOU 2275 CA LYS A1085 8633 8621 9024 -522 -1391 -195 C ATOM 2276 C LYS A1085 44.747 -9.040 32.862 1.00 69.35 C ANISOU 2276 C LYS A1085 8648 8673 9029 -630 -1428 12 C ATOM 2277 O LYS A1085 45.022 -8.882 31.677 1.00 68.90 O ANISOU 2277 O LYS A1085 8638 8503 9038 -683 -1466 184 O ATOM 2278 CB LYS A1085 42.817 -8.073 34.188 1.00 70.84 C ANISOU 2278 CB LYS A1085 8795 8761 9359 -521 -1531 -485 C ATOM 2279 CG LYS A1085 42.479 -6.813 33.388 1.00 72.14 C ANISOU 2279 CG LYS A1085 9001 8611 9795 -558 -1721 -527 C ATOM 2280 CD LYS A1085 42.887 -5.507 34.064 1.00 74.22 C ANISOU 2280 CD LYS A1085 9212 8767 10218 -622 -1898 -722 C ATOM 2281 CE LYS A1085 42.332 -4.317 33.269 1.00 75.72 C ANISOU 2281 CE LYS A1085 9437 8603 10728 -639 -2095 -757 C ATOM 2282 NZ LYS A1085 42.973 -3.011 33.594 1.00 77.80 N ANISOU 2282 NZ LYS A1085 9666 8689 11202 -737 -2297 -866 N ATOM 2283 N PRO A1086 45.697 -9.078 33.810 1.00 70.16 N ANISOU 2283 N PRO A1086 8674 8961 9020 -671 -1414 10 N ATOM 2284 CA PRO A1086 47.069 -8.829 33.366 1.00 70.73 C ANISOU 2284 CA PRO A1086 8728 9069 9076 -779 -1459 211 C ATOM 2285 C PRO A1086 47.538 -9.746 32.223 1.00 69.69 C ANISOU 2285 C PRO A1086 8629 8975 8872 -767 -1343 471 C ATOM 2286 O PRO A1086 48.240 -9.281 31.323 1.00 70.21 O ANISOU 2286 O PRO A1086 8702 8988 8986 -861 -1417 628 O ATOM 2287 CB PRO A1086 47.901 -9.055 34.638 1.00 71.25 C ANISOU 2287 CB PRO A1086 8693 9389 8988 -804 -1419 184 C ATOM 2288 CG PRO A1086 47.000 -9.756 35.592 1.00 70.68 C ANISOU 2288 CG PRO A1086 8587 9454 8815 -701 -1313 33 C ATOM 2289 CD PRO A1086 45.627 -9.327 35.260 1.00 70.62 C ANISOU 2289 CD PRO A1086 8644 9239 8949 -640 -1365 -150 C ATOM 2290 N VAL A1087 47.144 -11.018 32.250 1.00 68.45 N ANISOU 2290 N VAL A1087 8482 8916 8608 -660 -1170 508 N ATOM 2291 CA VAL A1087 47.603 -11.976 31.246 1.00 67.68 C ANISOU 2291 CA VAL A1087 8403 8864 8447 -635 -1045 706 C ATOM 2292 C VAL A1087 46.996 -11.676 29.888 1.00 67.34 C ANISOU 2292 C VAL A1087 8435 8653 8497 -662 -1090 737 C ATOM 2293 O VAL A1087 47.681 -11.683 28.869 1.00 67.57 O ANISOU 2293 O VAL A1087 8457 8709 8508 -723 -1089 897 O ATOM 2294 CB VAL A1087 47.239 -13.420 31.623 1.00 66.86 C ANISOU 2294 CB VAL A1087 8292 8861 8248 -514 -862 721 C ATOM 2295 CG1 VAL A1087 47.552 -14.361 30.476 1.00 65.99 C ANISOU 2295 CG1 VAL A1087 8208 8752 8113 -477 -740 866 C ATOM 2296 CG2 VAL A1087 47.991 -13.842 32.865 1.00 67.89 C ANISOU 2296 CG2 VAL A1087 8324 9199 8272 -499 -813 762 C ATOM 2297 N TYR A1088 45.697 -11.420 29.882 1.00 67.04 N ANISOU 2297 N TYR A1088 8450 8473 8546 -622 -1129 590 N ATOM 2298 CA TYR A1088 44.979 -11.095 28.653 1.00 66.72 C ANISOU 2298 CA TYR A1088 8469 8285 8597 -653 -1183 623 C ATOM 2299 C TYR A1088 45.533 -9.826 27.995 1.00 67.61 C ANISOU 2299 C TYR A1088 8565 8297 8826 -788 -1370 724 C ATOM 2300 O TYR A1088 45.652 -9.762 26.776 1.00 67.71 O ANISOU 2300 O TYR A1088 8584 8300 8841 -858 -1391 876 O ATOM 2301 CB TYR A1088 43.497 -10.937 28.982 1.00 66.51 C ANISOU 2301 CB TYR A1088 8480 8136 8651 -581 -1208 437 C ATOM 2302 CG TYR A1088 42.596 -10.627 27.819 1.00 66.49 C ANISOU 2302 CG TYR A1088 8525 7991 8743 -605 -1266 468 C ATOM 2303 CD1 TYR A1088 42.176 -11.626 26.945 1.00 65.39 C ANISOU 2303 CD1 TYR A1088 8424 7902 8516 -580 -1136 535 C ATOM 2304 CD2 TYR A1088 42.122 -9.338 27.622 1.00 68.00 C ANISOU 2304 CD2 TYR A1088 8715 7996 9125 -653 -1458 423 C ATOM 2305 CE1 TYR A1088 41.324 -11.334 25.885 1.00 65.90 C ANISOU 2305 CE1 TYR A1088 8518 7872 8648 -617 -1193 570 C ATOM 2306 CE2 TYR A1088 41.268 -9.038 26.572 1.00 68.28 C ANISOU 2306 CE2 TYR A1088 8775 7913 9252 -678 -1522 480 C ATOM 2307 CZ TYR A1088 40.873 -10.032 25.707 1.00 67.04 C ANISOU 2307 CZ TYR A1088 8650 7847 8973 -667 -1388 558 C ATOM 2308 OH TYR A1088 40.030 -9.700 24.666 1.00 67.91 O ANISOU 2308 OH TYR A1088 8770 7872 9158 -710 -1459 625 O ATOM 2309 N ASP A1089 45.893 -8.836 28.812 1.00 68.48 N ANISOU 2309 N ASP A1089 8641 8348 9027 -838 -1508 644 N ATOM 2310 CA ASP A1089 46.419 -7.557 28.320 1.00 69.58 C ANISOU 2310 CA ASP A1089 8760 8358 9316 -980 -1713 741 C ATOM 2311 C ASP A1089 47.787 -7.673 27.647 1.00 69.52 C ANISOU 2311 C ASP A1089 8704 8506 9202 -1093 -1703 989 C ATOM 2312 O ASP A1089 48.066 -6.951 26.692 1.00 70.39 O ANISOU 2312 O ASP A1089 8798 8552 9395 -1221 -1835 1156 O ATOM 2313 CB ASP A1089 46.501 -6.537 29.462 1.00 71.00 C ANISOU 2313 CB ASP A1089 8913 8436 9627 -1005 -1857 555 C ATOM 2314 CG ASP A1089 45.138 -6.003 29.881 1.00 71.65 C ANISOU 2314 CG ASP A1089 9023 8321 9880 -919 -1930 309 C ATOM 2315 OD1 ASP A1089 44.176 -6.083 29.088 1.00 72.08 O ANISOU 2315 OD1 ASP A1089 9117 8262 10005 -878 -1932 335 O ATOM 2316 OD2 ASP A1089 45.031 -5.485 31.011 1.00 73.30 O ANISOU 2316 OD2 ASP A1089 9199 8505 10147 -894 -1988 78 O ATOM 2317 N SER A1090 48.632 -8.571 28.148 1.00 68.57 N ANISOU 2317 N SER A1090 8544 8605 8902 -1048 -1552 1026 N ATOM 2318 CA SER A1090 49.962 -8.793 27.581 1.00 68.59 C ANISOU 2318 CA SER A1090 8480 8794 8786 -1132 -1520 1246 C ATOM 2319 C SER A1090 49.910 -9.533 26.260 1.00 67.93 C ANISOU 2319 C SER A1090 8398 8798 8612 -1123 -1411 1379 C ATOM 2320 O SER A1090 50.795 -9.376 25.425 1.00 68.66 O ANISOU 2320 O SER A1090 8428 9020 8641 -1228 -1436 1567 O ATOM 2321 CB SER A1090 50.806 -9.613 28.541 1.00 68.30 C ANISOU 2321 CB SER A1090 8387 8964 8600 -1062 -1383 1243 C ATOM 2322 OG SER A1090 50.250 -10.902 28.707 1.00 66.86 O ANISOU 2322 OG SER A1090 8230 8838 8334 -908 -1191 1179 O ATOM 2323 N LEU A1091 48.877 -10.355 26.090 1.00 66.76 N ANISOU 2323 N LEU A1091 8311 8605 8448 -1004 -1288 1272 N ATOM 2324 CA LEU A1091 48.738 -11.198 24.910 1.00 66.24 C ANISOU 2324 CA LEU A1091 8246 8634 8286 -985 -1162 1344 C ATOM 2325 C LEU A1091 48.306 -10.419 23.677 1.00 66.96 C ANISOU 2325 C LEU A1091 8339 8663 8439 -1113 -1293 1449 C ATOM 2326 O LEU A1091 47.767 -9.318 23.769 1.00 67.59 O ANISOU 2326 O LEU A1091 8441 8557 8681 -1181 -1476 1440 O ATOM 2327 CB LEU A1091 47.728 -12.319 25.168 1.00 64.92 C ANISOU 2327 CB LEU A1091 8144 8426 8094 -834 -1001 1192 C ATOM 2328 CG LEU A1091 48.101 -13.332 26.250 1.00 64.41 C ANISOU 2328 CG LEU A1091 8063 8447 7962 -707 -854 1133 C ATOM 2329 CD1 LEU A1091 46.844 -14.024 26.743 1.00 64.26 C ANISOU 2329 CD1 LEU A1091 8113 8332 7972 -595 -772 979 C ATOM 2330 CD2 LEU A1091 49.128 -14.349 25.770 1.00 63.82 C ANISOU 2330 CD2 LEU A1091 7924 8552 7773 -665 -699 1237 C ATOM 2331 N ASP A1092 48.549 -11.038 22.525 1.00 67.17 N ANISOU 2331 N ASP A1092 8326 8857 8337 -1143 -1195 1545 N ATOM 2332 CA ASP A1092 48.181 -10.518 21.205 1.00 67.92 C ANISOU 2332 CA ASP A1092 8393 8978 8434 -1277 -1290 1673 C ATOM 2333 C ASP A1092 46.756 -10.929 20.796 1.00 67.02 C ANISOU 2333 C ASP A1092 8352 8762 8349 -1216 -1241 1557 C ATOM 2334 O ASP A1092 46.058 -11.607 21.543 1.00 65.92 O ANISOU 2334 O ASP A1092 8287 8526 8233 -1073 -1136 1377 O ATOM 2335 CB ASP A1092 49.180 -11.053 20.178 1.00 68.70 C ANISOU 2335 CB ASP A1092 8388 9375 8338 -1345 -1191 1807 C ATOM 2336 CG ASP A1092 49.266 -12.562 20.190 1.00 68.44 C ANISOU 2336 CG ASP A1092 8362 9462 8176 -1188 -940 1665 C ATOM 2337 OD1 ASP A1092 50.231 -13.080 20.799 1.00 69.53 O ANISOU 2337 OD1 ASP A1092 8460 9696 8262 -1111 -845 1659 O ATOM 2338 OD2 ASP A1092 48.354 -13.221 19.631 1.00 67.77 O ANISOU 2338 OD2 ASP A1092 8322 9362 8063 -1142 -847 1561 O ATOM 2339 N ALA A1093 46.341 -10.521 19.598 1.00 67.70 N ANISOU 2339 N ALA A1093 8402 8897 8424 -1340 -1322 1679 N ATOM 2340 CA ALA A1093 45.008 -10.828 19.073 1.00 67.05 C ANISOU 2340 CA ALA A1093 8370 8749 8357 -1312 -1292 1599 C ATOM 2341 C ALA A1093 44.702 -12.324 19.043 1.00 65.82 C ANISOU 2341 C ALA A1093 8257 8686 8064 -1182 -1049 1425 C ATOM 2342 O ALA A1093 43.611 -12.745 19.454 1.00 64.96 O ANISOU 2342 O ALA A1093 8228 8442 8009 -1083 -998 1274 O ATOM 2343 CB ALA A1093 44.853 -10.244 17.673 1.00 68.44 C ANISOU 2343 CB ALA A1093 8463 9048 8492 -1494 -1406 1803 C ATOM 2344 N VAL A1094 45.659 -13.113 18.552 1.00 65.77 N ANISOU 2344 N VAL A1094 8187 8908 7893 -1184 -907 1445 N ATOM 2345 CA VAL A1094 45.469 -14.560 18.361 1.00 64.90 C ANISOU 2345 CA VAL A1094 8101 8878 7677 -1071 -683 1279 C ATOM 2346 C VAL A1094 45.491 -15.328 19.685 1.00 63.61 C ANISOU 2346 C VAL A1094 8008 8577 7583 -893 -573 1139 C ATOM 2347 O VAL A1094 44.720 -16.274 19.885 1.00 63.03 O ANISOU 2347 O VAL A1094 8000 8428 7520 -793 -453 993 O ATOM 2348 CB VAL A1094 46.543 -15.151 17.405 1.00 65.98 C ANISOU 2348 CB VAL A1094 8125 9308 7635 -1116 -565 1320 C ATOM 2349 CG1 VAL A1094 46.671 -16.657 17.585 1.00 65.49 C ANISOU 2349 CG1 VAL A1094 8085 9269 7530 -956 -335 1129 C ATOM 2350 CG2 VAL A1094 46.212 -14.809 15.960 1.00 66.52 C ANISOU 2350 CG2 VAL A1094 8118 9570 7585 -1286 -618 1409 C ATOM 2351 N ARG A1095 46.376 -14.919 20.585 1.00 63.17 N ANISOU 2351 N ARG A1095 7926 8506 7568 -870 -623 1201 N ATOM 2352 CA ARG A1095 46.508 -15.592 21.868 1.00 61.98 C ANISOU 2352 CA ARG A1095 7812 8274 7463 -723 -532 1108 C ATOM 2353 C ARG A1095 45.393 -15.209 22.823 1.00 60.63 C ANISOU 2353 C ARG A1095 7722 7905 7407 -678 -610 1011 C ATOM 2354 O ARG A1095 44.999 -16.020 23.647 1.00 60.10 O ANISOU 2354 O ARG A1095 7693 7783 7358 -563 -511 911 O ATOM 2355 CB ARG A1095 47.885 -15.324 22.475 1.00 62.64 C ANISOU 2355 CB ARG A1095 7819 8457 7523 -726 -553 1212 C ATOM 2356 CG ARG A1095 49.017 -15.925 21.641 1.00 63.80 C ANISOU 2356 CG ARG A1095 7865 8828 7545 -733 -441 1283 C ATOM 2357 CD ARG A1095 50.184 -16.365 22.493 1.00 64.97 C ANISOU 2357 CD ARG A1095 7947 9060 7677 -647 -370 1330 C ATOM 2358 NE ARG A1095 51.292 -16.867 21.681 1.00 67.07 N ANISOU 2358 NE ARG A1095 8096 9555 7830 -645 -269 1390 N ATOM 2359 CZ ARG A1095 52.230 -16.107 21.115 1.00 68.69 C ANISOU 2359 CZ ARG A1095 8201 9950 7947 -774 -352 1539 C ATOM 2360 NH1 ARG A1095 52.214 -14.782 21.255 1.00 69.06 N ANISOU 2360 NH1 ARG A1095 8259 9951 8030 -924 -553 1656 N ATOM 2361 NH2 ARG A1095 53.191 -16.680 20.394 1.00 69.83 N ANISOU 2361 NH2 ARG A1095 8224 10333 7976 -754 -238 1567 N ATOM 2362 N ARG A1096 44.880 -13.985 22.711 1.00 60.41 N ANISOU 2362 N ARG A1096 7708 7777 7467 -768 -789 1044 N ATOM 2363 CA ARG A1096 43.640 -13.616 23.393 1.00 59.64 C ANISOU 2363 CA ARG A1096 7675 7505 7481 -720 -859 922 C ATOM 2364 C ARG A1096 42.554 -14.628 23.049 1.00 58.38 C ANISOU 2364 C ARG A1096 7570 7329 7283 -655 -731 819 C ATOM 2365 O ARG A1096 41.911 -15.179 23.937 1.00 57.48 O ANISOU 2365 O ARG A1096 7494 7156 7189 -557 -667 703 O ATOM 2366 CB ARG A1096 43.180 -12.215 22.999 1.00 60.55 C ANISOU 2366 CB ARG A1096 7782 7498 7723 -824 -1069 980 C ATOM 2367 CG ARG A1096 43.904 -11.100 23.719 1.00 62.61 C ANISOU 2367 CG ARG A1096 8010 7692 8087 -872 -1226 1018 C ATOM 2368 CD ARG A1096 43.362 -9.728 23.325 1.00 66.26 C ANISOU 2368 CD ARG A1096 8463 7980 8731 -966 -1449 1072 C ATOM 2369 NE ARG A1096 43.960 -8.669 24.143 1.00 69.37 N ANISOU 2369 NE ARG A1096 8831 8267 9258 -1006 -1604 1060 N ATOM 2370 CZ ARG A1096 44.997 -7.905 23.792 1.00 72.82 C ANISOU 2370 CZ ARG A1096 9211 8726 9728 -1142 -1730 1233 C ATOM 2371 NH1 ARG A1096 45.587 -8.027 22.601 1.00 74.21 N ANISOU 2371 NH1 ARG A1096 9337 9056 9800 -1259 -1723 1449 N ATOM 2372 NH2 ARG A1096 45.453 -6.995 24.647 1.00 74.72 N ANISOU 2372 NH2 ARG A1096 9436 8853 10100 -1175 -1868 1184 N ATOM 2373 N ALA A1097 42.379 -14.879 21.752 1.00 58.26 N ANISOU 2373 N ALA A1097 7545 7390 7199 -727 -698 867 N ATOM 2374 CA ALA A1097 41.453 -15.903 21.257 1.00 57.46 C ANISOU 2374 CA ALA A1097 7489 7296 7046 -690 -571 767 C ATOM 2375 C ALA A1097 41.679 -17.255 21.925 1.00 56.72 C ANISOU 2375 C ALA A1097 7419 7208 6923 -567 -393 674 C ATOM 2376 O ALA A1097 40.721 -17.946 22.262 1.00 56.41 O ANISOU 2376 O ALA A1097 7433 7095 6905 -507 -327 572 O ATOM 2377 CB ALA A1097 41.576 -16.048 19.756 1.00 57.99 C ANISOU 2377 CB ALA A1097 7513 7512 7006 -800 -544 828 C ATOM 2378 N ALA A1098 42.938 -17.634 22.110 1.00 56.67 N ANISOU 2378 N ALA A1098 7361 7290 6879 -533 -323 725 N ATOM 2379 CA ALA A1098 43.259 -18.864 22.822 1.00 56.36 C ANISOU 2379 CA ALA A1098 7326 7239 6850 -410 -174 674 C ATOM 2380 C ALA A1098 42.662 -18.862 24.220 1.00 55.51 C ANISOU 2380 C ALA A1098 7250 7031 6809 -339 -204 635 C ATOM 2381 O ALA A1098 41.966 -19.796 24.610 1.00 55.02 O ANISOU 2381 O ALA A1098 7225 6908 6772 -274 -117 568 O ATOM 2382 CB ALA A1098 44.759 -19.055 22.899 1.00 57.15 C ANISOU 2382 CB ALA A1098 7344 7456 6914 -382 -124 761 C ATOM 2383 N LEU A1099 42.927 -17.801 24.969 1.00 55.46 N ANISOU 2383 N LEU A1099 7220 7022 6829 -364 -331 673 N ATOM 2384 CA LEU A1099 42.438 -17.703 26.343 1.00 55.27 C ANISOU 2384 CA LEU A1099 7199 6959 6841 -308 -363 617 C ATOM 2385 C LEU A1099 40.909 -17.689 26.395 1.00 54.90 C ANISOU 2385 C LEU A1099 7208 6824 6825 -299 -386 505 C ATOM 2386 O LEU A1099 40.305 -18.334 27.252 1.00 54.71 O ANISOU 2386 O LEU A1099 7187 6800 6798 -238 -331 454 O ATOM 2387 CB LEU A1099 42.981 -16.444 27.008 1.00 55.66 C ANISOU 2387 CB LEU A1099 7207 7024 6916 -352 -508 637 C ATOM 2388 CG LEU A1099 42.948 -16.423 28.536 1.00 55.82 C ANISOU 2388 CG LEU A1099 7188 7090 6931 -300 -520 584 C ATOM 2389 CD1 LEU A1099 44.089 -17.251 29.097 1.00 55.81 C ANISOU 2389 CD1 LEU A1099 7123 7209 6872 -256 -420 692 C ATOM 2390 CD2 LEU A1099 43.029 -14.990 29.055 1.00 56.80 C ANISOU 2390 CD2 LEU A1099 7287 7184 7108 -357 -689 524 C ATOM 2391 N ILE A1100 40.296 -16.958 25.467 1.00 54.96 N ANISOU 2391 N ILE A1100 7244 6777 6860 -369 -473 490 N ATOM 2392 CA ILE A1100 38.847 -16.841 25.409 1.00 54.68 C ANISOU 2392 CA ILE A1100 7247 6671 6857 -364 -506 396 C ATOM 2393 C ILE A1100 38.224 -18.211 25.182 1.00 54.87 C ANISOU 2393 C ILE A1100 7310 6702 6835 -330 -359 357 C ATOM 2394 O ILE A1100 37.168 -18.516 25.732 1.00 54.64 O ANISOU 2394 O ILE A1100 7297 6649 6813 -295 -346 282 O ATOM 2395 CB ILE A1100 38.395 -15.866 24.306 1.00 54.86 C ANISOU 2395 CB ILE A1100 7276 6644 6924 -453 -628 429 C ATOM 2396 CG1 ILE A1100 38.880 -14.441 24.619 1.00 55.59 C ANISOU 2396 CG1 ILE A1100 7329 6678 7111 -491 -802 466 C ATOM 2397 CG2 ILE A1100 36.877 -15.868 24.189 1.00 54.31 C ANISOU 2397 CG2 ILE A1100 7234 6516 6882 -441 -650 343 C ATOM 2398 CD1 ILE A1100 39.095 -13.555 23.395 1.00 55.68 C ANISOU 2398 CD1 ILE A1100 7319 6671 7164 -609 -924 595 C ATOM 2399 N ASN A1101 38.885 -19.043 24.383 1.00 55.65 N ANISOU 2399 N ASN A1101 7415 6838 6892 -342 -251 398 N ATOM 2400 CA ASN A1101 38.410 -20.397 24.141 1.00 56.10 C ANISOU 2400 CA ASN A1101 7507 6872 6936 -312 -113 345 C ATOM 2401 C ASN A1101 38.308 -21.134 25.456 1.00 56.63 C ANISOU 2401 C ASN A1101 7563 6918 7035 -229 -59 347 C ATOM 2402 O ASN A1101 37.253 -21.694 25.780 1.00 56.64 O ANISOU 2402 O ASN A1101 7591 6883 7045 -220 -31 298 O ATOM 2403 CB ASN A1101 39.363 -21.129 23.200 1.00 56.76 C ANISOU 2403 CB ASN A1101 7575 7002 6989 -319 -4 361 C ATOM 2404 CG ASN A1101 38.947 -22.555 22.921 1.00 57.00 C ANISOU 2404 CG ASN A1101 7638 6974 7042 -286 134 281 C ATOM 2405 OD1 ASN A1101 38.465 -23.265 23.801 1.00 57.18 O ANISOU 2405 OD1 ASN A1101 7679 6922 7122 -230 173 273 O ATOM 2406 ND2 ASN A1101 39.171 -22.996 21.691 1.00 57.72 N ANISOU 2406 ND2 ASN A1101 7726 7111 7090 -329 208 219 N ATOM 2407 N MET A1102 39.406 -21.113 26.216 1.00 57.47 N ANISOU 2407 N MET A1102 7615 7071 7148 -183 -53 424 N ATOM 2408 CA MET A1102 39.492 -21.841 27.489 1.00 57.99 C ANISOU 2408 CA MET A1102 7641 7157 7232 -116 -5 470 C ATOM 2409 C MET A1102 38.412 -21.404 28.460 1.00 57.87 C ANISOU 2409 C MET A1102 7616 7175 7196 -121 -77 415 C ATOM 2410 O MET A1102 37.747 -22.244 29.070 1.00 58.02 O ANISOU 2410 O MET A1102 7626 7199 7218 -101 -28 425 O ATOM 2411 CB MET A1102 40.857 -21.650 28.138 1.00 58.43 C ANISOU 2411 CB MET A1102 7623 7295 7281 -83 -11 572 C ATOM 2412 CG MET A1102 41.989 -22.316 27.390 1.00 59.47 C ANISOU 2412 CG MET A1102 7735 7422 7438 -50 82 633 C ATOM 2413 SD MET A1102 43.505 -22.261 28.350 1.00 61.99 S ANISOU 2413 SD MET A1102 7946 7857 7748 -2 81 779 S ATOM 2414 CE MET A1102 43.081 -23.390 29.673 1.00 61.66 C ANISOU 2414 CE MET A1102 7860 7811 7756 61 136 858 C ATOM 2415 N VAL A1103 38.233 -20.091 28.593 1.00 57.92 N ANISOU 2415 N VAL A1103 7612 7205 7188 -150 -199 355 N ATOM 2416 CA VAL A1103 37.162 -19.560 29.419 1.00 58.06 C ANISOU 2416 CA VAL A1103 7605 7264 7189 -143 -270 258 C ATOM 2417 C VAL A1103 35.847 -20.171 28.987 1.00 58.37 C ANISOU 2417 C VAL A1103 7691 7259 7227 -154 -229 208 C ATOM 2418 O VAL A1103 35.172 -20.790 29.786 1.00 58.94 O ANISOU 2418 O VAL A1103 7731 7394 7267 -138 -193 202 O ATOM 2419 CB VAL A1103 37.043 -18.046 29.325 1.00 58.04 C ANISOU 2419 CB VAL A1103 7594 7233 7224 -167 -414 172 C ATOM 2420 CG1 VAL A1103 35.680 -17.602 29.837 1.00 57.93 C ANISOU 2420 CG1 VAL A1103 7560 7236 7215 -146 -473 35 C ATOM 2421 CG2 VAL A1103 38.163 -17.379 30.099 1.00 57.93 C ANISOU 2421 CG2 VAL A1103 7519 7286 7204 -166 -472 192 C ATOM 2422 N PHE A1104 35.497 -20.028 27.718 1.00 58.79 N ANISOU 2422 N PHE A1104 7806 7228 7304 -197 -236 186 N ATOM 2423 CA PHE A1104 34.241 -20.591 27.209 1.00 59.34 C ANISOU 2423 CA PHE A1104 7916 7266 7362 -225 -200 138 C ATOM 2424 C PHE A1104 34.005 -22.020 27.670 1.00 59.61 C ANISOU 2424 C PHE A1104 7954 7306 7388 -211 -87 178 C ATOM 2425 O PHE A1104 32.880 -22.391 28.015 1.00 59.94 O ANISOU 2425 O PHE A1104 7990 7375 7406 -224 -81 145 O ATOM 2426 CB PHE A1104 34.190 -20.559 25.679 1.00 59.54 C ANISOU 2426 CB PHE A1104 7996 7233 7390 -290 -191 138 C ATOM 2427 CG PHE A1104 33.271 -19.518 25.132 1.00 60.77 C ANISOU 2427 CG PHE A1104 8151 7377 7558 -330 -304 94 C ATOM 2428 CD1 PHE A1104 32.002 -19.869 24.664 1.00 62.29 C ANISOU 2428 CD1 PHE A1104 8367 7573 7727 -368 -290 49 C ATOM 2429 CD2 PHE A1104 33.664 -18.181 25.089 1.00 61.97 C ANISOU 2429 CD2 PHE A1104 8272 7508 7763 -334 -434 110 C ATOM 2430 CE1 PHE A1104 31.140 -18.897 24.153 1.00 62.83 C ANISOU 2430 CE1 PHE A1104 8417 7633 7820 -398 -401 29 C ATOM 2431 CE2 PHE A1104 32.813 -17.195 24.577 1.00 62.80 C ANISOU 2431 CE2 PHE A1104 8364 7575 7921 -364 -554 90 C ATOM 2432 CZ PHE A1104 31.550 -17.550 24.110 1.00 63.09 C ANISOU 2432 CZ PHE A1104 8414 7625 7930 -390 -536 54 C ATOM 2433 N GLN A1105 35.058 -22.824 27.664 1.00 59.85 N ANISOU 2433 N GLN A1105 7983 7305 7449 -186 -4 258 N ATOM 2434 CA GLN A1105 34.904 -24.224 28.002 1.00 60.48 C ANISOU 2434 CA GLN A1105 8064 7344 7571 -174 91 315 C ATOM 2435 C GLN A1105 34.658 -24.401 29.497 1.00 60.94 C ANISOU 2435 C GLN A1105 8040 7512 7599 -152 69 386 C ATOM 2436 O GLN A1105 33.696 -25.064 29.900 1.00 61.14 O ANISOU 2436 O GLN A1105 8055 7556 7617 -180 86 403 O ATOM 2437 CB GLN A1105 36.132 -25.014 27.570 1.00 60.94 C ANISOU 2437 CB GLN A1105 8126 7325 7702 -136 181 376 C ATOM 2438 CG GLN A1105 35.942 -26.511 27.636 1.00 61.48 C ANISOU 2438 CG GLN A1105 8206 7284 7870 -125 275 419 C ATOM 2439 CD GLN A1105 37.114 -27.269 27.061 1.00 62.64 C ANISOU 2439 CD GLN A1105 8349 7333 8117 -69 366 438 C ATOM 2440 OE1 GLN A1105 38.156 -26.685 26.749 1.00 62.73 O ANISOU 2440 OE1 GLN A1105 8336 7398 8100 -38 362 443 O ATOM 2441 NE2 GLN A1105 36.956 -28.581 26.915 1.00 64.23 N ANISOU 2441 NE2 GLN A1105 8565 7388 8448 -56 445 443 N ATOM 2442 N MET A1106 35.512 -23.781 30.309 1.00 61.10 N ANISOU 2442 N MET A1106 7993 7633 7589 -117 27 430 N ATOM 2443 CA MET A1106 35.580 -24.104 31.733 1.00 61.72 C ANISOU 2443 CA MET A1106 7968 7858 7624 -104 21 526 C ATOM 2444 C MET A1106 35.298 -22.952 32.702 1.00 61.75 C ANISOU 2444 C MET A1106 7892 8047 7524 -107 -72 440 C ATOM 2445 O MET A1106 35.426 -23.123 33.914 1.00 62.30 O ANISOU 2445 O MET A1106 7853 8294 7523 -110 -80 508 O ATOM 2446 CB MET A1106 36.934 -24.747 32.043 1.00 62.28 C ANISOU 2446 CB MET A1106 7992 7918 7751 -64 74 682 C ATOM 2447 CG MET A1106 38.137 -23.923 31.700 1.00 62.18 C ANISOU 2447 CG MET A1106 7979 7909 7734 -39 48 668 C ATOM 2448 SD MET A1106 39.647 -24.843 32.055 1.00 65.16 S ANISOU 2448 SD MET A1106 8284 8287 8185 19 121 866 S ATOM 2449 CE MET A1106 40.053 -25.565 30.470 1.00 63.00 C ANISOU 2449 CE MET A1106 8103 7798 8035 55 218 824 C ATOM 2450 N GLY A1107 34.896 -21.795 32.181 1.00 61.42 N ANISOU 2450 N GLY A1107 7889 7969 7476 -109 -147 287 N ATOM 2451 CA GLY A1107 34.552 -20.643 33.014 1.00 61.89 C ANISOU 2451 CA GLY A1107 7874 8167 7474 -100 -243 155 C ATOM 2452 C GLY A1107 35.799 -19.999 33.567 1.00 62.61 C ANISOU 2452 C GLY A1107 7912 8324 7552 -90 -284 171 C ATOM 2453 O GLY A1107 36.810 -20.669 33.764 1.00 63.21 O ANISOU 2453 O GLY A1107 7966 8421 7627 -88 -227 322 O ATOM 2454 N GLU A1108 35.745 -18.702 33.841 1.00 63.27 N ANISOU 2454 N GLU A1108 7965 8437 7637 -85 -388 16 N ATOM 2455 CA GLU A1108 36.979 -17.964 34.121 1.00 63.97 C ANISOU 2455 CA GLU A1108 8022 8546 7734 -95 -442 22 C ATOM 2456 C GLU A1108 37.720 -18.384 35.399 1.00 64.82 C ANISOU 2456 C GLU A1108 8012 8881 7732 -106 -410 105 C ATOM 2457 O GLU A1108 38.958 -18.358 35.431 1.00 65.08 O ANISOU 2457 O GLU A1108 8031 8926 7769 -119 -407 211 O ATOM 2458 CB GLU A1108 36.736 -16.456 34.093 1.00 64.57 C ANISOU 2458 CB GLU A1108 8093 8562 7876 -94 -576 -172 C ATOM 2459 CG GLU A1108 35.852 -15.914 35.182 1.00 66.62 C ANISOU 2459 CG GLU A1108 8252 8980 8079 -69 -626 -377 C ATOM 2460 CD GLU A1108 35.708 -14.416 35.064 1.00 68.85 C ANISOU 2460 CD GLU A1108 8531 9143 8484 -55 -766 -580 C ATOM 2461 OE1 GLU A1108 36.141 -13.698 36.003 1.00 70.80 O ANISOU 2461 OE1 GLU A1108 8691 9503 8706 -62 -828 -718 O ATOM 2462 OE2 GLU A1108 35.188 -13.967 34.011 1.00 68.69 O ANISOU 2462 OE2 GLU A1108 8591 8913 8595 -44 -820 -594 O ATOM 2463 N THR A1109 36.992 -18.780 36.443 1.00 65.53 N ANISOU 2463 N THR A1109 8003 9180 7715 -109 -390 76 N ATOM 2464 CA THR A1109 37.653 -19.286 37.649 1.00 66.41 C ANISOU 2464 CA THR A1109 7980 9545 7705 -138 -360 197 C ATOM 2465 C THR A1109 38.487 -20.479 37.219 1.00 65.94 C ANISOU 2465 C THR A1109 7956 9393 7704 -130 -271 462 C ATOM 2466 O THR A1109 39.694 -20.540 37.485 1.00 66.35 O ANISOU 2466 O THR A1109 7962 9502 7746 -137 -265 584 O ATOM 2467 CB THR A1109 36.666 -19.738 38.761 1.00 67.40 C ANISOU 2467 CB THR A1109 7975 9944 7688 -162 -342 175 C ATOM 2468 OG1 THR A1109 35.494 -18.914 38.750 1.00 68.00 O ANISOU 2468 OG1 THR A1109 8050 10032 7755 -140 -398 -80 O ATOM 2469 CG2 THR A1109 37.339 -19.666 40.135 1.00 68.20 C ANISOU 2469 CG2 THR A1109 7902 10379 7631 -211 -358 217 C ATOM 2470 N GLY A1110 37.828 -21.409 36.529 1.00 65.09 N ANISOU 2470 N GLY A1110 7925 9136 7667 -114 -205 535 N ATOM 2471 CA GLY A1110 38.490 -22.584 35.983 1.00 64.86 C ANISOU 2471 CA GLY A1110 7938 8969 7738 -91 -119 742 C ATOM 2472 C GLY A1110 39.826 -22.247 35.355 1.00 64.28 C ANISOU 2472 C GLY A1110 7902 8795 7725 -65 -116 784 C ATOM 2473 O GLY A1110 40.851 -22.781 35.767 1.00 65.17 O ANISOU 2473 O GLY A1110 7942 8972 7845 -50 -81 956 O ATOM 2474 N VAL A1111 39.822 -21.336 34.386 1.00 62.97 N ANISOU 2474 N VAL A1111 7831 8492 7600 -67 -161 645 N ATOM 2475 CA VAL A1111 41.050 -20.978 33.672 1.00 62.53 C ANISOU 2475 CA VAL A1111 7806 8360 7592 -60 -164 692 C ATOM 2476 C VAL A1111 42.076 -20.286 34.587 1.00 62.91 C ANISOU 2476 C VAL A1111 7752 8582 7566 -85 -224 726 C ATOM 2477 O VAL A1111 43.287 -20.472 34.431 1.00 62.73 O ANISOU 2477 O VAL A1111 7699 8576 7559 -74 -197 854 O ATOM 2478 CB VAL A1111 40.738 -20.098 32.436 1.00 61.90 C ANISOU 2478 CB VAL A1111 7831 8122 7563 -82 -218 564 C ATOM 2479 CG1 VAL A1111 42.017 -19.694 31.707 1.00 61.36 C ANISOU 2479 CG1 VAL A1111 7772 8018 7521 -96 -230 631 C ATOM 2480 CG2 VAL A1111 39.786 -20.837 31.488 1.00 61.45 C ANISOU 2480 CG2 VAL A1111 7863 7924 7559 -72 -153 536 C ATOM 2481 N ALA A1112 41.588 -19.521 35.561 1.00 63.26 N ANISOU 2481 N ALA A1112 7732 8775 7527 -119 -302 601 N ATOM 2482 CA ALA A1112 42.466 -18.795 36.484 1.00 64.16 C ANISOU 2482 CA ALA A1112 7743 9075 7558 -161 -367 592 C ATOM 2483 C ALA A1112 43.287 -19.737 37.355 1.00 65.01 C ANISOU 2483 C ALA A1112 7729 9376 7597 -159 -304 812 C ATOM 2484 O ALA A1112 44.286 -19.322 37.942 1.00 65.74 O ANISOU 2484 O ALA A1112 7734 9622 7623 -197 -341 862 O ATOM 2485 CB ALA A1112 41.656 -17.840 37.357 1.00 64.69 C ANISOU 2485 CB ALA A1112 7753 9273 7551 -194 -456 365 C ATOM 2486 N GLY A1113 42.858 -20.997 37.435 1.00 65.25 N ANISOU 2486 N GLY A1113 7745 9394 7653 -123 -218 955 N ATOM 2487 CA GLY A1113 43.547 -22.022 38.215 1.00 66.33 C ANISOU 2487 CA GLY A1113 7755 9681 7764 -115 -164 1208 C ATOM 2488 C GLY A1113 44.911 -22.446 37.694 1.00 66.59 C ANISOU 2488 C GLY A1113 7783 9634 7884 -68 -116 1384 C ATOM 2489 O GLY A1113 45.730 -22.936 38.463 1.00 67.56 O ANISOU 2489 O GLY A1113 7772 9923 7973 -70 -101 1586 O ATOM 2490 N PHE A1114 45.180 -22.265 36.405 1.00 65.98 N ANISOU 2490 N PHE A1114 7826 9331 7908 -29 -93 1318 N ATOM 2491 CA PHE A1114 46.473 -22.666 35.855 1.00 66.61 C ANISOU 2491 CA PHE A1114 7884 9361 8060 22 -41 1464 C ATOM 2492 C PHE A1114 47.549 -21.658 36.245 1.00 67.32 C ANISOU 2492 C PHE A1114 7903 9623 8053 -34 -114 1474 C ATOM 2493 O PHE A1114 48.222 -21.092 35.396 1.00 66.94 O ANISOU 2493 O PHE A1114 7901 9504 8027 -41 -130 1439 O ATOM 2494 CB PHE A1114 46.400 -22.830 34.336 1.00 65.84 C ANISOU 2494 CB PHE A1114 7917 9023 8075 69 12 1381 C ATOM 2495 CG PHE A1114 45.406 -23.863 33.888 1.00 65.84 C ANISOU 2495 CG PHE A1114 7988 8849 8178 115 86 1359 C ATOM 2496 CD1 PHE A1114 45.620 -25.210 34.150 1.00 66.97 C ANISOU 2496 CD1 PHE A1114 8072 8940 8434 185 167 1529 C ATOM 2497 CD2 PHE A1114 44.255 -23.493 33.205 1.00 64.88 C ANISOU 2497 CD2 PHE A1114 7986 8608 8057 82 66 1179 C ATOM 2498 CE1 PHE A1114 44.700 -26.174 33.739 1.00 67.04 C ANISOU 2498 CE1 PHE A1114 8147 8767 8556 212 225 1504 C ATOM 2499 CE2 PHE A1114 43.333 -24.449 32.796 1.00 64.91 C ANISOU 2499 CE2 PHE A1114 8051 8463 8146 108 130 1157 C ATOM 2500 CZ PHE A1114 43.560 -25.791 33.060 1.00 66.03 C ANISOU 2500 CZ PHE A1114 8142 8542 8403 168 209 1313 C ATOM 2501 N THR A1115 47.701 -21.452 37.549 1.00 68.79 N ANISOU 2501 N THR A1115 7961 10056 8118 -89 -162 1527 N ATOM 2502 CA THR A1115 48.683 -20.530 38.113 1.00 69.86 C ANISOU 2502 CA THR A1115 8009 10389 8145 -164 -238 1531 C ATOM 2503 C THR A1115 49.976 -20.445 37.324 1.00 70.42 C ANISOU 2503 C THR A1115 8080 10407 8266 -140 -219 1637 C ATOM 2504 O THR A1115 50.383 -19.355 36.923 1.00 70.16 O ANISOU 2504 O THR A1115 8088 10361 8208 -207 -297 1533 O ATOM 2505 CB THR A1115 49.042 -20.973 39.534 1.00 71.25 C ANISOU 2505 CB THR A1115 8000 10868 8202 -201 -241 1700 C ATOM 2506 OG1 THR A1115 48.010 -20.547 40.426 1.00 71.56 O ANISOU 2506 OG1 THR A1115 8005 11061 8123 -268 -294 1542 O ATOM 2507 CG2 THR A1115 50.378 -20.399 39.984 1.00 72.01 C ANISOU 2507 CG2 THR A1115 7985 11170 8206 -263 -289 1788 C ATOM 2508 N ASN A1116 50.605 -21.604 37.116 1.00 71.67 N ANISOU 2508 N ASN A1116 8183 10539 8509 -46 -121 1847 N ATOM 2509 CA ASN A1116 51.958 -21.695 36.540 1.00 72.76 C ANISOU 2509 CA ASN A1116 8269 10693 8680 -8 -88 1978 C ATOM 2510 C ASN A1116 52.001 -21.313 35.070 1.00 72.31 C ANISOU 2510 C ASN A1116 8339 10444 8689 7 -73 1853 C ATOM 2511 O ASN A1116 52.736 -20.406 34.667 1.00 72.42 O ANISOU 2511 O ASN A1116 8351 10516 8649 -60 -134 1832 O ATOM 2512 CB ASN A1116 52.517 -23.119 36.698 1.00 73.88 C ANISOU 2512 CB ASN A1116 8306 10831 8933 113 16 2218 C ATOM 2513 CG ASN A1116 52.964 -23.426 38.118 1.00 75.28 C ANISOU 2513 CG ASN A1116 8302 11272 9028 80 -10 2431 C ATOM 2514 OD1 ASN A1116 53.351 -22.531 38.868 1.00 76.02 O ANISOU 2514 OD1 ASN A1116 8323 11601 8959 -31 -95 2416 O ATOM 2515 ND2 ASN A1116 52.929 -24.703 38.486 1.00 76.16 N ANISOU 2515 ND2 ASN A1116 8328 11349 9257 169 54 2637 N ATOM 2516 N SER A1117 51.205 -22.028 34.281 1.00 72.25 N ANISOU 2516 N SER A1117 8431 10228 8793 82 1 1783 N ATOM 2517 CA SER A1117 51.075 -21.775 32.852 1.00 71.89 C ANISOU 2517 CA SER A1117 8495 10025 8792 87 23 1659 C ATOM 2518 C SER A1117 50.730 -20.316 32.577 1.00 71.61 C ANISOU 2518 C SER A1117 8536 9988 8681 -37 -104 1512 C ATOM 2519 O SER A1117 51.284 -19.714 31.666 1.00 71.43 O ANISOU 2519 O SER A1117 8532 9961 8644 -82 -133 1501 O ATOM 2520 CB SER A1117 50.006 -22.695 32.257 1.00 71.48 C ANISOU 2520 CB SER A1117 8538 9768 8850 158 106 1573 C ATOM 2521 OG SER A1117 50.203 -24.037 32.675 1.00 71.99 O ANISOU 2521 OG SER A1117 8530 9799 9023 266 201 1712 O ATOM 2522 N LEU A1118 49.822 -19.757 33.373 1.00 72.16 N ANISOU 2522 N LEU A1118 8635 10067 8712 -94 -184 1406 N ATOM 2523 CA LEU A1118 49.446 -18.347 33.251 1.00 72.68 C ANISOU 2523 CA LEU A1118 8762 10102 8749 -201 -319 1255 C ATOM 2524 C LEU A1118 50.652 -17.438 33.429 1.00 74.26 C ANISOU 2524 C LEU A1118 8890 10433 8890 -289 -407 1320 C ATOM 2525 O LEU A1118 50.871 -16.525 32.627 1.00 74.42 O ANISOU 2525 O LEU A1118 8958 10386 8933 -365 -491 1283 O ATOM 2526 CB LEU A1118 48.375 -17.953 34.277 1.00 72.56 C ANISOU 2526 CB LEU A1118 8752 10115 8700 -229 -383 1113 C ATOM 2527 CG LEU A1118 46.912 -18.263 33.970 1.00 71.78 C ANISOU 2527 CG LEU A1118 8748 9870 8654 -190 -356 985 C ATOM 2528 CD1 LEU A1118 46.041 -17.822 35.130 1.00 72.24 C ANISOU 2528 CD1 LEU A1118 8769 10027 8652 -219 -419 848 C ATOM 2529 CD2 LEU A1118 46.462 -17.584 32.702 1.00 71.36 C ANISOU 2529 CD2 LEU A1118 8808 9631 8673 -220 -407 885 C ATOM 2530 N ARG A1119 51.432 -17.680 34.478 1.00 75.97 N ANISOU 2530 N ARG A1119 8983 10849 9032 -292 -398 1435 N ATOM 2531 CA ARG A1119 52.578 -16.832 34.754 1.00 77.64 C ANISOU 2531 CA ARG A1119 9116 11208 9176 -390 -485 1497 C ATOM 2532 C ARG A1119 53.610 -16.925 33.630 1.00 78.23 C ANISOU 2532 C ARG A1119 9176 11278 9269 -383 -450 1628 C ATOM 2533 O ARG A1119 54.311 -15.950 33.366 1.00 78.84 O ANISOU 2533 O ARG A1119 9235 11403 9316 -494 -551 1646 O ATOM 2534 CB ARG A1119 53.210 -17.174 36.103 1.00 78.85 C ANISOU 2534 CB ARG A1119 9118 11613 9225 -399 -473 1613 C ATOM 2535 CG ARG A1119 54.288 -16.176 36.546 1.00 81.07 C ANISOU 2535 CG ARG A1119 9315 12068 9419 -529 -582 1646 C ATOM 2536 CD ARG A1119 54.786 -16.427 37.976 1.00 84.02 C ANISOU 2536 CD ARG A1119 9528 12732 9663 -563 -583 1740 C ATOM 2537 NE ARG A1119 55.292 -17.793 38.178 1.00 85.87 N ANISOU 2537 NE ARG A1119 9657 13069 9899 -447 -454 1987 N ATOM 2538 CZ ARG A1119 54.574 -18.830 38.631 1.00 87.12 C ANISOU 2538 CZ ARG A1119 9794 13219 10086 -356 -372 2041 C ATOM 2539 NH1 ARG A1119 55.152 -20.023 38.768 1.00 88.00 N ANISOU 2539 NH1 ARG A1119 9800 13392 10242 -252 -274 2287 N ATOM 2540 NH2 ARG A1119 53.283 -18.700 38.948 1.00 86.89 N ANISOU 2540 NH2 ARG A1119 9838 13117 10056 -366 -393 1861 N ATOM 2541 N MET A1120 53.702 -18.083 32.971 1.00 78.59 N ANISOU 2541 N MET A1120 9219 11274 9366 -260 -311 1710 N ATOM 2542 CA MET A1120 54.588 -18.238 31.803 1.00 79.40 C ANISOU 2542 CA MET A1120 9295 11396 9475 -242 -260 1795 C ATOM 2543 C MET A1120 54.072 -17.469 30.593 1.00 78.98 C ANISOU 2543 C MET A1120 9351 11212 9445 -320 -324 1685 C ATOM 2544 O MET A1120 54.838 -16.797 29.894 1.00 79.33 O ANISOU 2544 O MET A1120 9362 11332 9446 -409 -382 1748 O ATOM 2545 CB MET A1120 54.740 -19.706 31.397 1.00 79.88 C ANISOU 2545 CB MET A1120 9320 11421 9610 -77 -91 1861 C ATOM 2546 CG MET A1120 55.900 -20.426 32.033 1.00 81.90 C ANISOU 2546 CG MET A1120 9416 11845 9858 2 -24 2054 C ATOM 2547 SD MET A1120 55.390 -21.768 33.109 1.00 84.21 S ANISOU 2547 SD MET A1120 9660 12088 10245 133 61 2139 S ATOM 2548 CE MET A1120 57.020 -22.380 33.587 1.00 86.14 C ANISOU 2548 CE MET A1120 9690 12550 10488 213 117 2402 C ATOM 2549 N LEU A1121 52.774 -17.594 30.332 1.00 78.35 N ANISOU 2549 N LEU A1121 9387 10954 9427 -295 -315 1543 N ATOM 2550 CA LEU A1121 52.154 -16.857 29.241 1.00 78.18 C ANISOU 2550 CA LEU A1121 9459 10811 9432 -375 -387 1454 C ATOM 2551 C LEU A1121 52.469 -15.364 29.390 1.00 78.90 C ANISOU 2551 C LEU A1121 9546 10920 9512 -531 -571 1461 C ATOM 2552 O LEU A1121 53.097 -14.770 28.515 1.00 79.49 O ANISOU 2552 O LEU A1121 9596 11041 9565 -626 -632 1543 O ATOM 2553 CB LEU A1121 50.637 -17.117 29.187 1.00 77.18 C ANISOU 2553 CB LEU A1121 9447 10506 9371 -333 -370 1302 C ATOM 2554 CG LEU A1121 50.194 -18.493 28.651 1.00 76.47 C ANISOU 2554 CG LEU A1121 9385 10352 9318 -212 -207 1277 C ATOM 2555 CD1 LEU A1121 48.682 -18.673 28.749 1.00 74.39 C ANISOU 2555 CD1 LEU A1121 9224 9934 9107 -192 -208 1139 C ATOM 2556 CD2 LEU A1121 50.656 -18.715 27.212 1.00 76.40 C ANISOU 2556 CD2 LEU A1121 9364 10373 9288 -220 -146 1296 C ATOM 2557 N GLN A1122 52.073 -14.783 30.518 1.00 79.28 N ANISOU 2557 N GLN A1122 9603 10944 9576 -564 -662 1373 N ATOM 2558 CA GLN A1122 52.389 -13.386 30.841 1.00 80.33 C ANISOU 2558 CA GLN A1122 9723 11068 9728 -707 -844 1348 C ATOM 2559 C GLN A1122 53.846 -13.018 30.542 1.00 81.37 C ANISOU 2559 C GLN A1122 9761 11360 9796 -801 -885 1524 C ATOM 2560 O GLN A1122 54.122 -11.964 29.967 1.00 81.73 O ANISOU 2560 O GLN A1122 9814 11357 9881 -938 -1026 1562 O ATOM 2561 CB GLN A1122 52.092 -13.119 32.317 1.00 80.74 C ANISOU 2561 CB GLN A1122 9747 11165 9763 -708 -890 1226 C ATOM 2562 CG GLN A1122 52.200 -11.660 32.719 1.00 82.18 C ANISOU 2562 CG GLN A1122 9928 11294 10002 -848 -1084 1127 C ATOM 2563 CD GLN A1122 51.366 -11.326 33.947 1.00 83.25 C ANISOU 2563 CD GLN A1122 10062 11421 10148 -832 -1130 904 C ATOM 2564 OE1 GLN A1122 51.065 -12.195 34.769 1.00 83.67 O ANISOU 2564 OE1 GLN A1122 10073 11605 10112 -746 -1020 882 O ATOM 2565 NE2 GLN A1122 50.988 -10.060 34.075 1.00 84.08 N ANISOU 2565 NE2 GLN A1122 10199 11378 10369 -919 -1298 739 N ATOM 2566 N GLN A1123 54.759 -13.907 30.930 1.00 81.92 N ANISOU 2566 N GLN A1123 9730 11619 9775 -729 -766 1648 N ATOM 2567 CA GLN A1123 56.199 -13.702 30.752 1.00 83.29 C ANISOU 2567 CA GLN A1123 9788 11990 9868 -801 -784 1827 C ATOM 2568 C GLN A1123 56.698 -14.069 29.348 1.00 83.80 C ANISOU 2568 C GLN A1123 9826 12109 9905 -788 -712 1936 C ATOM 2569 O GLN A1123 57.897 -13.980 29.079 1.00 84.92 O ANISOU 2569 O GLN A1123 9854 12443 9966 -838 -712 2090 O ATOM 2570 CB GLN A1123 56.984 -14.496 31.813 1.00 83.79 C ANISOU 2570 CB GLN A1123 9729 12255 9850 -723 -691 1927 C ATOM 2571 CG GLN A1123 56.877 -13.920 33.234 1.00 84.18 C ANISOU 2571 CG GLN A1123 9751 12364 9867 -794 -787 1851 C ATOM 2572 CD GLN A1123 57.489 -14.818 34.303 1.00 84.11 C ANISOU 2572 CD GLN A1123 9611 12575 9772 -717 -692 1972 C ATOM 2573 OE1 GLN A1123 58.252 -15.738 34.000 1.00 83.93 O ANISOU 2573 OE1 GLN A1123 9500 12659 9729 -619 -574 2141 O ATOM 2574 NE2 GLN A1123 57.154 -14.549 35.565 1.00 83.91 N ANISOU 2574 NE2 GLN A1123 9553 12628 9697 -761 -746 1884 N ATOM 2575 N LYS A1124 55.786 -14.487 28.469 1.00 83.37 N ANISOU 2575 N LYS A1124 9858 11916 9900 -726 -648 1849 N ATOM 2576 CA LYS A1124 56.086 -14.792 27.055 1.00 83.87 C ANISOU 2576 CA LYS A1124 9892 12050 9921 -728 -581 1909 C ATOM 2577 C LYS A1124 56.993 -16.017 26.834 1.00 84.69 C ANISOU 2577 C LYS A1124 9881 12330 9964 -589 -398 1982 C ATOM 2578 O LYS A1124 57.606 -16.147 25.780 1.00 85.35 O ANISOU 2578 O LYS A1124 9890 12560 9978 -608 -351 2042 O ATOM 2579 CB LYS A1124 56.627 -13.550 26.318 1.00 84.61 C ANISOU 2579 CB LYS A1124 9951 12215 9982 -929 -745 2023 C ATOM 2580 CG LYS A1124 55.614 -12.401 26.244 1.00 84.52 C ANISOU 2580 CG LYS A1124 10051 11979 10082 -1050 -926 1946 C ATOM 2581 CD LYS A1124 56.014 -11.317 25.241 1.00 85.61 C ANISOU 2581 CD LYS A1124 10149 12162 10214 -1249 -1086 2092 C ATOM 2582 CE LYS A1124 55.104 -10.094 25.331 1.00 85.45 C ANISOU 2582 CE LYS A1124 10225 11885 10357 -1364 -1292 2034 C ATOM 2583 NZ LYS A1124 53.680 -10.425 25.057 1.00 84.08 N ANISOU 2583 NZ LYS A1124 10162 11520 10262 -1271 -1247 1881 N ATOM 2584 N ARG A1125 57.043 -16.919 27.815 1.00 84.99 N ANISOU 2584 N ARG A1125 9893 12362 10037 -448 -299 1977 N ATOM 2585 CA ARG A1125 57.795 -18.176 27.701 1.00 86.20 C ANISOU 2585 CA ARG A1125 9935 12625 10189 -284 -127 2039 C ATOM 2586 C ARG A1125 56.852 -19.274 27.227 1.00 85.85 C ANISOU 2586 C ARG A1125 9970 12408 10241 -142 7 1898 C ATOM 2587 O ARG A1125 56.369 -20.092 28.015 1.00 85.60 O ANISOU 2587 O ARG A1125 9962 12263 10299 -28 72 1875 O ATOM 2588 CB ARG A1125 58.448 -18.548 29.038 1.00 86.84 C ANISOU 2588 CB ARG A1125 9919 12802 10273 -221 -112 2158 C ATOM 2589 CG ARG A1125 59.674 -17.694 29.359 1.00 88.43 C ANISOU 2589 CG ARG A1125 10002 13232 10364 -347 -212 2313 C ATOM 2590 CD ARG A1125 59.792 -17.323 30.837 1.00 89.41 C ANISOU 2590 CD ARG A1125 10095 13412 10462 -402 -297 2367 C ATOM 2591 NE ARG A1125 60.804 -18.101 31.556 1.00 90.76 N ANISOU 2591 NE ARG A1125 10102 13774 10607 -304 -216 2539 N ATOM 2592 CZ ARG A1125 60.557 -19.016 32.494 1.00 91.71 C ANISOU 2592 CZ ARG A1125 10184 13876 10784 -184 -144 2582 C ATOM 2593 NH1 ARG A1125 61.580 -19.637 33.076 1.00 93.25 N ANISOU 2593 NH1 ARG A1125 10207 14260 10961 -108 -87 2775 N ATOM 2594 NH2 ARG A1125 59.308 -19.321 32.864 1.00 90.80 N ANISOU 2594 NH2 ARG A1125 10185 13571 10743 -145 -133 2456 N ATOM 2595 N TRP A1126 56.618 -19.287 25.918 1.00 86.20 N ANISOU 2595 N TRP A1126 10039 12452 10258 -167 44 1816 N ATOM 2596 CA TRP A1126 55.512 -20.034 25.324 1.00 85.80 C ANISOU 2596 CA TRP A1126 10090 12227 10283 -91 134 1649 C ATOM 2597 C TRP A1126 55.627 -21.536 25.518 1.00 86.63 C ANISOU 2597 C TRP A1126 10150 12264 10498 109 306 1608 C ATOM 2598 O TRP A1126 54.684 -22.164 25.999 1.00 86.14 O ANISOU 2598 O TRP A1126 10176 12007 10544 180 341 1535 O ATOM 2599 CB TRP A1126 55.387 -19.722 23.826 1.00 86.26 C ANISOU 2599 CB TRP A1126 10150 12366 10257 -180 138 1581 C ATOM 2600 CG TRP A1126 55.409 -18.261 23.518 1.00 86.15 C ANISOU 2600 CG TRP A1126 10152 12421 10159 -386 -42 1668 C ATOM 2601 CD1 TRP A1126 56.338 -17.596 22.782 1.00 87.05 C ANISOU 2601 CD1 TRP A1126 10158 12764 10153 -508 -99 1786 C ATOM 2602 CD2 TRP A1126 54.472 -17.278 23.971 1.00 85.71 C ANISOU 2602 CD2 TRP A1126 10215 12195 10154 -494 -201 1651 C ATOM 2603 NE1 TRP A1126 56.035 -16.259 22.734 1.00 87.07 N ANISOU 2603 NE1 TRP A1126 10210 12724 10147 -696 -294 1863 N ATOM 2604 CE2 TRP A1126 54.893 -16.036 23.456 1.00 86.19 C ANISOU 2604 CE2 TRP A1126 10238 12357 10151 -680 -358 1768 C ATOM 2605 CE3 TRP A1126 53.313 -17.327 24.762 1.00 84.77 C ANISOU 2605 CE3 TRP A1126 10218 11855 10135 -452 -229 1546 C ATOM 2606 CZ2 TRP A1126 54.196 -14.848 23.703 1.00 86.20 C ANISOU 2606 CZ2 TRP A1126 10325 12206 10219 -811 -545 1773 C ATOM 2607 CZ3 TRP A1126 52.618 -16.146 25.007 1.00 84.29 C ANISOU 2607 CZ3 TRP A1126 10234 11675 10114 -574 -402 1532 C ATOM 2608 CH2 TRP A1126 53.063 -14.924 24.477 1.00 85.20 C ANISOU 2608 CH2 TRP A1126 10315 11856 10198 -745 -559 1639 C ATOM 2609 N ASP A1127 56.775 -22.106 25.154 1.00 88.23 N ANISOU 2609 N ASP A1127 10209 12625 10690 202 406 1660 N ATOM 2610 CA ASP A1127 56.927 -23.565 25.156 1.00 89.47 C ANISOU 2610 CA ASP A1127 10310 12690 10995 408 570 1603 C ATOM 2611 C ASP A1127 56.730 -24.168 26.540 1.00 89.18 C ANISOU 2611 C ASP A1127 10276 12513 11092 502 569 1709 C ATOM 2612 O ASP A1127 56.170 -25.263 26.669 1.00 89.46 O ANISOU 2612 O ASP A1127 10344 12352 11292 628 657 1642 O ATOM 2613 CB ASP A1127 58.275 -24.006 24.559 1.00 91.58 C ANISOU 2613 CB ASP A1127 10392 13169 11233 504 673 1635 C ATOM 2614 CG ASP A1127 58.111 -24.762 23.239 1.00 93.24 C ANISOU 2614 CG ASP A1127 10584 13374 11467 582 811 1415 C ATOM 2615 OD1 ASP A1127 57.308 -25.724 23.198 1.00 93.79 O ANISOU 2615 OD1 ASP A1127 10731 13206 11699 689 894 1270 O ATOM 2616 OD2 ASP A1127 58.787 -24.405 22.248 1.00 94.82 O ANISOU 2616 OD2 ASP A1127 10682 13825 11520 528 834 1382 O ATOM 2617 N GLU A1128 57.178 -23.445 27.565 1.00 88.66 N ANISOU 2617 N GLU A1128 10168 12562 10954 424 462 1876 N ATOM 2618 CA GLU A1128 56.997 -23.880 28.950 1.00 88.46 C ANISOU 2618 CA GLU A1128 10123 12474 11011 476 442 1999 C ATOM 2619 C GLU A1128 55.532 -23.834 29.347 1.00 86.58 C ANISOU 2619 C GLU A1128 10040 12043 10811 427 395 1896 C ATOM 2620 O GLU A1128 55.071 -24.676 30.107 1.00 86.85 O ANISOU 2620 O GLU A1128 10071 11965 10960 507 430 1947 O ATOM 2621 CB GLU A1128 57.843 -23.028 29.901 1.00 88.80 C ANISOU 2621 CB GLU A1128 10072 12734 10931 379 335 2178 C ATOM 2622 CG GLU A1128 59.332 -23.366 29.838 1.00 91.26 C ANISOU 2622 CG GLU A1128 10193 13247 11231 461 394 2334 C ATOM 2623 CD GLU A1128 60.212 -22.328 30.513 1.00 92.28 C ANISOU 2623 CD GLU A1128 10236 13623 11204 322 276 2488 C ATOM 2624 OE1 GLU A1128 60.645 -22.576 31.660 1.00 93.40 O ANISOU 2624 OE1 GLU A1128 10274 13862 11350 346 258 2656 O ATOM 2625 OE2 GLU A1128 60.468 -21.267 29.898 1.00 92.36 O ANISOU 2625 OE2 GLU A1128 10270 13734 11087 177 194 2452 O ATOM 2626 N ALA A1129 54.807 -22.849 28.824 1.00 84.84 N ANISOU 2626 N ALA A1129 9940 11793 10500 292 310 1769 N ATOM 2627 CA ALA A1129 53.369 -22.747 29.048 1.00 83.23 C ANISOU 2627 CA ALA A1129 9876 11419 10326 249 268 1650 C ATOM 2628 C ALA A1129 52.641 -23.932 28.422 1.00 83.06 C ANISOU 2628 C ALA A1129 9914 11207 10436 356 389 1537 C ATOM 2629 O ALA A1129 51.669 -24.445 28.979 1.00 82.45 O ANISOU 2629 O ALA A1129 9898 10991 10435 380 396 1512 O ATOM 2630 CB ALA A1129 52.841 -21.440 28.479 1.00 82.11 C ANISOU 2630 CB ALA A1129 9830 11279 10087 95 150 1549 C ATOM 2631 N ALA A1130 53.131 -24.366 27.264 1.00 83.61 N ANISOU 2631 N ALA A1130 9952 11289 10527 413 484 1464 N ATOM 2632 CA ALA A1130 52.514 -25.452 26.507 1.00 83.89 C ANISOU 2632 CA ALA A1130 10037 11150 10685 504 601 1313 C ATOM 2633 C ALA A1130 52.751 -26.832 27.131 1.00 84.95 C ANISOU 2633 C ALA A1130 10102 11152 11023 670 697 1386 C ATOM 2634 O ALA A1130 51.890 -27.711 27.044 1.00 85.11 O ANISOU 2634 O ALA A1130 10191 10965 11182 721 751 1297 O ATOM 2635 CB ALA A1130 53.018 -25.430 25.076 1.00 84.59 C ANISOU 2635 CB ALA A1130 10088 11340 10710 501 672 1187 C ATOM 2636 N VAL A1131 53.913 -27.022 27.754 1.00 85.73 N ANISOU 2636 N VAL A1131 10056 11365 11149 748 709 1563 N ATOM 2637 CA VAL A1131 54.259 -28.312 28.355 1.00 87.04 C ANISOU 2637 CA VAL A1131 10127 11407 11536 912 786 1676 C ATOM 2638 C VAL A1131 53.498 -28.532 29.673 1.00 86.39 C ANISOU 2638 C VAL A1131 10072 11242 11507 879 715 1825 C ATOM 2639 O VAL A1131 53.094 -29.661 29.974 1.00 87.54 O ANISOU 2639 O VAL A1131 10210 11190 11860 971 763 1867 O ATOM 2640 CB VAL A1131 55.793 -28.464 28.589 1.00 88.53 C ANISOU 2640 CB VAL A1131 10126 11768 11742 1012 821 1842 C ATOM 2641 CG1 VAL A1131 56.116 -29.876 29.046 1.00 90.29 C ANISOU 2641 CG1 VAL A1131 10242 11821 12243 1201 901 1953 C ATOM 2642 CG2 VAL A1131 56.579 -28.133 27.322 1.00 88.82 C ANISOU 2642 CG2 VAL A1131 10111 11956 11681 1024 883 1704 C ATOM 2643 N ASN A1132 53.311 -27.459 30.450 1.00 84.69 N ANISOU 2643 N ASN A1132 9878 11190 11111 742 598 1901 N ATOM 2644 CA ASN A1132 52.523 -27.512 31.687 1.00 83.84 C ANISOU 2644 CA ASN A1132 9782 11074 10997 684 526 2011 C ATOM 2645 C ASN A1132 51.090 -27.898 31.394 1.00 82.98 C ANISOU 2645 C ASN A1132 9815 10759 10954 659 538 1863 C ATOM 2646 O ASN A1132 50.563 -28.866 31.950 1.00 83.60 O ANISOU 2646 O ASN A1132 9877 10708 11177 704 558 1953 O ATOM 2647 CB ASN A1132 52.520 -26.156 32.393 1.00 82.61 C ANISOU 2647 CB ASN A1132 9630 11136 10621 535 402 2033 C ATOM 2648 CG ASN A1132 53.800 -25.883 33.144 1.00 83.37 C ANISOU 2648 CG ASN A1132 9566 11463 10647 535 370 2234 C ATOM 2649 OD1 ASN A1132 54.264 -26.717 33.915 1.00 84.56 O ANISOU 2649 OD1 ASN A1132 9587 11649 10891 612 398 2440 O ATOM 2650 ND2 ASN A1132 54.368 -24.700 32.941 1.00 82.77 N ANISOU 2650 ND2 ASN A1132 9487 11548 10410 435 300 2193 N ATOM 2651 N LEU A1133 50.472 -27.117 30.510 1.00 81.58 N ANISOU 2651 N LEU A1133 9763 10561 10670 575 515 1657 N ATOM 2652 CA LEU A1133 49.086 -27.331 30.103 1.00 80.76 C ANISOU 2652 CA LEU A1133 9795 10290 10598 533 520 1501 C ATOM 2653 C LEU A1133 48.876 -28.700 29.447 1.00 81.87 C ANISOU 2653 C LEU A1133 9952 10202 10949 641 634 1436 C ATOM 2654 O LEU A1133 47.805 -29.294 29.586 1.00 81.80 O ANISOU 2654 O LEU A1133 10014 10040 11025 625 639 1399 O ATOM 2655 CB LEU A1133 48.619 -26.204 29.166 1.00 79.42 C ANISOU 2655 CB LEU A1133 9732 10158 10282 427 470 1317 C ATOM 2656 CG LEU A1133 48.136 -24.913 29.848 1.00 78.12 C ANISOU 2656 CG LEU A1133 9601 10113 9967 305 337 1314 C ATOM 2657 CD1 LEU A1133 48.091 -23.753 28.871 1.00 76.81 C ANISOU 2657 CD1 LEU A1133 9500 9988 9695 211 275 1192 C ATOM 2658 CD2 LEU A1133 46.760 -25.108 30.495 1.00 77.58 C ANISOU 2658 CD2 LEU A1133 9596 9971 9911 270 305 1274 C ATOM 2659 N ALA A1134 49.907 -29.190 28.755 1.00 83.03 N ANISOU 2659 N ALA A1134 10027 10336 11185 749 723 1414 N ATOM 2660 CA ALA A1134 49.890 -30.510 28.115 1.00 84.56 C ANISOU 2660 CA ALA A1134 10213 10304 11609 872 836 1320 C ATOM 2661 C ALA A1134 49.604 -31.649 29.093 1.00 85.82 C ANISOU 2661 C ALA A1134 10326 10283 11998 943 837 1496 C ATOM 2662 O ALA A1134 49.113 -32.703 28.688 1.00 87.03 O ANISOU 2662 O ALA A1134 10516 10189 12362 1002 899 1404 O ATOM 2663 CB ALA A1134 51.207 -30.763 27.403 1.00 86.02 C ANISOU 2663 CB ALA A1134 10284 10554 11844 992 926 1280 C ATOM 2664 N LYS A1135 49.929 -31.452 30.369 1.00 85.79 N ANISOU 2664 N LYS A1135 10230 10409 11957 925 763 1754 N ATOM 2665 CA LYS A1135 49.547 -32.410 31.403 1.00 86.99 C ANISOU 2665 CA LYS A1135 10322 10440 12289 951 737 1970 C ATOM 2666 C LYS A1135 48.603 -31.778 32.434 1.00 85.23 C ANISOU 2666 C LYS A1135 10132 10367 11885 800 630 2066 C ATOM 2667 O LYS A1135 49.031 -31.187 33.428 1.00 85.03 O ANISOU 2667 O LYS A1135 10010 10579 11715 750 561 2239 O ATOM 2668 CB LYS A1135 50.781 -33.051 32.062 1.00 89.26 C ANISOU 2668 CB LYS A1135 10422 10754 12736 1078 753 2230 C ATOM 2669 CG LYS A1135 51.740 -32.109 32.814 1.00 89.39 C ANISOU 2669 CG LYS A1135 10324 11097 12542 1038 693 2402 C ATOM 2670 CD LYS A1135 52.449 -32.842 33.972 1.00 92.16 C ANISOU 2670 CD LYS A1135 10482 11497 13037 1106 664 2754 C ATOM 2671 CE LYS A1135 51.497 -33.175 35.148 1.00 92.33 C ANISOU 2671 CE LYS A1135 10482 11538 13061 1003 580 2957 C ATOM 2672 NZ LYS A1135 52.203 -33.759 36.337 1.00 93.90 N ANISOU 2672 NZ LYS A1135 10468 11853 13357 1036 533 3342 N ATOM 2673 N SER A1136 47.311 -31.903 32.163 1.00 83.99 N ANISOU 2673 N SER A1136 10100 10086 11726 726 620 1931 N ATOM 2674 CA SER A1136 46.268 -31.395 33.038 1.00 82.56 C ANISOU 2674 CA SER A1136 9945 10039 11384 593 531 1981 C ATOM 2675 C SER A1136 45.038 -32.268 32.857 1.00 82.95 C ANISOU 2675 C SER A1136 10075 9873 11570 561 543 1936 C ATOM 2676 O SER A1136 45.004 -33.116 31.964 1.00 83.82 O ANISOU 2676 O SER A1136 10238 9726 11882 631 618 1827 O ATOM 2677 CB SER A1136 45.955 -29.931 32.707 1.00 80.44 C ANISOU 2677 CB SER A1136 9764 9942 10856 498 481 1787 C ATOM 2678 OG SER A1136 45.860 -29.712 31.311 1.00 78.90 O ANISOU 2678 OG SER A1136 9683 9628 10665 512 535 1549 O ATOM 2679 N ARG A1137 44.036 -32.076 33.708 1.00 82.52 N ANISOU 2679 N ARG A1137 10016 9933 11401 450 470 2009 N ATOM 2680 CA ARG A1137 42.785 -32.837 33.606 1.00 83.00 C ANISOU 2680 CA ARG A1137 10146 9825 11563 394 469 1984 C ATOM 2681 C ARG A1137 42.013 -32.358 32.381 1.00 81.35 C ANISOU 2681 C ARG A1137 10103 9523 11281 357 501 1672 C ATOM 2682 O ARG A1137 41.288 -33.122 31.751 1.00 81.95 O ANISOU 2682 O ARG A1137 10259 9382 11494 344 537 1578 O ATOM 2683 CB ARG A1137 41.938 -32.697 34.885 1.00 83.15 C ANISOU 2683 CB ARG A1137 10089 10060 11443 276 380 2153 C ATOM 2684 CG ARG A1137 40.665 -33.556 34.902 1.00 84.54 C ANISOU 2684 CG ARG A1137 10309 10089 11723 201 368 2180 C ATOM 2685 CD ARG A1137 39.762 -33.283 36.116 1.00 85.18 C ANISOU 2685 CD ARG A1137 10301 10452 11612 72 282 2319 C ATOM 2686 NE ARG A1137 39.958 -34.249 37.196 1.00 87.82 N ANISOU 2686 NE ARG A1137 10469 10831 12064 44 239 2676 N ATOM 2687 CZ ARG A1137 39.545 -35.516 37.167 1.00 89.93 C ANISOU 2687 CZ ARG A1137 10727 10857 12585 26 234 2837 C ATOM 2688 NH1 ARG A1137 39.768 -36.312 38.207 1.00 91.97 N ANISOU 2688 NH1 ARG A1137 10813 11182 12950 -10 176 3204 N ATOM 2689 NH2 ARG A1137 38.912 -36.001 36.102 1.00 90.46 N ANISOU 2689 NH2 ARG A1137 10945 10619 12806 34 280 2643 N ATOM 2690 N TRP A1138 42.181 -31.081 32.058 1.00 79.60 N ANISOU 2690 N TRP A1138 9923 9469 10849 330 478 1526 N ATOM 2691 CA TRP A1138 41.665 -30.504 30.822 1.00 78.26 C ANISOU 2691 CA TRP A1138 9887 9243 10604 297 500 1262 C ATOM 2692 C TRP A1138 42.154 -31.275 29.581 1.00 79.70 C ANISOU 2692 C TRP A1138 10113 9212 10954 374 602 1133 C ATOM 2693 O TRP A1138 41.351 -31.634 28.720 1.00 79.47 O ANISOU 2693 O TRP A1138 10179 9048 10966 336 637 965 O ATOM 2694 CB TRP A1138 42.077 -29.027 30.757 1.00 76.52 C ANISOU 2694 CB TRP A1138 9670 9227 10177 266 444 1187 C ATOM 2695 CG TRP A1138 41.811 -28.349 29.461 1.00 73.89 C ANISOU 2695 CG TRP A1138 9441 8861 9771 231 454 970 C ATOM 2696 CD1 TRP A1138 40.637 -28.330 28.769 1.00 72.34 C ANISOU 2696 CD1 TRP A1138 9344 8589 9550 165 453 820 C ATOM 2697 CD2 TRP A1138 42.737 -27.565 28.706 1.00 71.40 C ANISOU 2697 CD2 TRP A1138 9124 8618 9384 243 457 904 C ATOM 2698 NE1 TRP A1138 40.779 -27.590 27.623 1.00 71.05 N ANISOU 2698 NE1 TRP A1138 9236 8452 9307 136 454 674 N ATOM 2699 CE2 TRP A1138 42.060 -27.107 27.564 1.00 70.44 C ANISOU 2699 CE2 TRP A1138 9097 8467 9200 178 454 727 C ATOM 2700 CE3 TRP A1138 44.075 -27.210 28.884 1.00 71.07 C ANISOU 2700 CE3 TRP A1138 8998 8685 9320 291 457 995 C ATOM 2701 CZ2 TRP A1138 42.674 -26.309 26.609 1.00 69.55 C ANISOU 2701 CZ2 TRP A1138 8990 8433 9001 153 445 654 C ATOM 2702 CZ3 TRP A1138 44.682 -26.425 27.935 1.00 70.28 C ANISOU 2702 CZ3 TRP A1138 8910 8656 9136 268 451 910 C ATOM 2703 CH2 TRP A1138 43.984 -25.983 26.810 1.00 69.79 C ANISOU 2703 CH2 TRP A1138 8937 8567 9013 196 443 748 C ATOM 2704 N TYR A1139 43.461 -31.543 29.519 1.00 81.32 N ANISOU 2704 N TYR A1139 10235 9409 11252 481 650 1202 N ATOM 2705 CA TYR A1139 44.075 -32.272 28.396 1.00 83.10 C ANISOU 2705 CA TYR A1139 10468 9467 11637 576 755 1058 C ATOM 2706 C TYR A1139 43.565 -33.713 28.224 1.00 85.18 C ANISOU 2706 C TYR A1139 10752 9439 12170 615 809 1034 C ATOM 2707 O TYR A1139 43.370 -34.166 27.102 1.00 85.84 O ANISOU 2707 O TYR A1139 10899 9383 12332 628 883 805 O ATOM 2708 CB TYR A1139 45.602 -32.297 28.532 1.00 84.15 C ANISOU 2708 CB TYR A1139 10478 9672 11822 695 792 1164 C ATOM 2709 CG TYR A1139 46.312 -32.663 27.245 1.00 86.20 C ANISOU 2709 CG TYR A1139 10730 9858 12161 785 900 960 C ATOM 2710 CD1 TYR A1139 46.830 -31.675 26.411 1.00 86.21 C ANISOU 2710 CD1 TYR A1139 10738 10056 11960 752 910 832 C ATOM 2711 CD2 TYR A1139 46.463 -33.998 26.852 1.00 89.14 C ANISOU 2711 CD2 TYR A1139 11077 9975 12816 897 988 887 C ATOM 2712 CE1 TYR A1139 47.484 -32.000 25.221 1.00 87.67 C ANISOU 2712 CE1 TYR A1139 10891 10235 12183 823 1013 638 C ATOM 2713 CE2 TYR A1139 47.110 -34.334 25.660 1.00 90.46 C ANISOU 2713 CE2 TYR A1139 11219 10106 13044 984 1096 656 C ATOM 2714 CZ TYR A1139 47.618 -33.329 24.851 1.00 89.68 C ANISOU 2714 CZ TYR A1139 11115 10256 12702 943 1112 532 C ATOM 2715 OH TYR A1139 48.254 -33.638 23.669 1.00 91.03 O ANISOU 2715 OH TYR A1139 11238 10453 12896 1015 1221 299 O ATOM 2716 N ASN A1140 43.371 -34.444 29.316 1.00 86.57 N ANISOU 2716 N ASN A1140 10863 9531 12495 623 765 1272 N ATOM 2717 CA ASN A1140 42.869 -35.815 29.207 1.00 88.84 C ANISOU 2717 CA ASN A1140 11166 9513 13074 645 794 1277 C ATOM 2718 C ASN A1140 41.397 -35.873 28.800 1.00 88.35 C ANISOU 2718 C ASN A1140 11232 9384 12952 510 775 1129 C ATOM 2719 O ASN A1140 41.008 -36.717 27.991 1.00 89.75 O ANISOU 2719 O ASN A1140 11471 9320 13307 514 830 956 O ATOM 2720 CB ASN A1140 43.087 -36.588 30.511 1.00 90.54 C ANISOU 2720 CB ASN A1140 11255 9668 13476 674 736 1625 C ATOM 2721 CG ASN A1140 44.539 -36.977 30.721 1.00 92.34 C ANISOU 2721 CG ASN A1140 11345 9860 13877 835 772 1763 C ATOM 2722 OD1 ASN A1140 45.454 -36.275 30.283 1.00 91.81 O ANISOU 2722 OD1 ASN A1140 11255 9946 13680 900 816 1666 O ATOM 2723 ND2 ASN A1140 44.757 -38.100 31.398 1.00 94.60 N ANISOU 2723 ND2 ASN A1140 11527 9948 14467 895 748 2012 N ATOM 2724 N GLN A1141 40.589 -34.966 29.346 1.00 86.68 N ANISOU 2724 N GLN A1141 11050 9392 12491 391 696 1181 N ATOM 2725 CA GLN A1141 39.133 -34.990 29.133 1.00 86.19 C ANISOU 2725 CA GLN A1141 11086 9303 12357 260 665 1084 C ATOM 2726 C GLN A1141 38.729 -34.571 27.698 1.00 85.00 C ANISOU 2726 C GLN A1141 11055 9139 12103 220 719 766 C ATOM 2727 O GLN A1141 37.759 -35.107 27.141 1.00 85.39 O ANISOU 2727 O GLN A1141 11182 9055 12206 143 734 639 O ATOM 2728 CB GLN A1141 38.424 -34.104 30.180 1.00 84.97 C ANISOU 2728 CB GLN A1141 10902 9416 11966 162 568 1219 C ATOM 2729 CG GLN A1141 37.245 -34.778 30.919 1.00 86.62 C ANISOU 2729 CG GLN A1141 11095 9594 12221 56 511 1363 C ATOM 2730 CD GLN A1141 37.680 -35.714 32.062 1.00 89.47 C ANISOU 2730 CD GLN A1141 11322 9905 12768 80 475 1688 C ATOM 2731 OE1 GLN A1141 38.661 -35.451 32.773 1.00 89.11 O ANISOU 2731 OE1 GLN A1141 11167 9992 12698 146 459 1854 O ATOM 2732 NE2 GLN A1141 36.930 -36.804 32.248 1.00 91.37 N ANISOU 2732 NE2 GLN A1141 11559 9961 13193 11 452 1798 N ATOM 2733 N THR A1142 39.470 -33.619 27.119 1.00 83.54 N ANISOU 2733 N THR A1142 10869 9107 11762 258 741 657 N ATOM 2734 CA THR A1142 39.224 -33.123 25.751 1.00 82.58 C ANISOU 2734 CA THR A1142 10830 9030 11516 209 783 393 C ATOM 2735 C THR A1142 40.560 -32.813 25.046 1.00 82.58 C ANISOU 2735 C THR A1142 10779 9102 11494 302 847 309 C ATOM 2736 O THR A1142 40.954 -31.651 24.918 1.00 80.94 O ANISOU 2736 O THR A1142 10557 9102 11091 279 807 317 O ATOM 2737 CB THR A1142 38.295 -31.879 25.748 1.00 80.61 C ANISOU 2737 CB THR A1142 10634 8980 11012 94 699 364 C ATOM 2738 OG1 THR A1142 38.712 -30.945 26.756 1.00 79.64 O ANISOU 2738 OG1 THR A1142 10450 9035 10773 112 623 528 O ATOM 2739 CG2 THR A1142 36.847 -32.290 26.008 1.00 80.42 C ANISOU 2739 CG2 THR A1142 10665 8893 10996 -7 662 366 C ATOM 2740 N PRO A1143 41.255 -33.865 24.572 1.00 84.35 N ANISOU 2740 N PRO A1143 10964 9152 11931 405 942 223 N ATOM 2741 CA PRO A1143 42.672 -33.764 24.195 1.00 84.84 C ANISOU 2741 CA PRO A1143 10936 9287 12011 523 1006 195 C ATOM 2742 C PRO A1143 42.973 -33.104 22.858 1.00 84.03 C ANISOU 2742 C PRO A1143 10844 9363 11721 483 1056 -30 C ATOM 2743 O PRO A1143 44.038 -32.507 22.703 1.00 83.93 O ANISOU 2743 O PRO A1143 10753 9522 11613 533 1067 4 O ATOM 2744 CB PRO A1143 43.140 -35.232 24.163 1.00 87.57 C ANISOU 2744 CB PRO A1143 11228 9354 12689 654 1090 157 C ATOM 2745 CG PRO A1143 41.945 -36.062 24.575 1.00 88.33 C ANISOU 2745 CG PRO A1143 11395 9223 12943 584 1054 194 C ATOM 2746 CD PRO A1143 40.745 -35.225 24.333 1.00 86.37 C ANISOU 2746 CD PRO A1143 11250 9123 12441 417 994 130 C ATOM 2747 N ASN A1144 42.070 -33.228 21.896 1.00 83.54 N ANISOU 2747 N ASN A1144 10861 9282 11599 383 1082 -245 N ATOM 2748 CA ASN A1144 42.308 -32.642 20.587 1.00 83.01 C ANISOU 2748 CA ASN A1144 10781 9421 11336 323 1125 -443 C ATOM 2749 C ASN A1144 42.081 -31.138 20.626 1.00 80.17 C ANISOU 2749 C ASN A1144 10442 9303 10713 210 1016 -327 C ATOM 2750 O ASN A1144 42.933 -30.378 20.170 1.00 80.11 O ANISOU 2750 O ASN A1144 10369 9502 10565 206 1012 -315 O ATOM 2751 CB ASN A1144 41.453 -33.332 19.529 1.00 84.31 C ANISOU 2751 CB ASN A1144 11005 9507 11522 244 1190 -715 C ATOM 2752 CG ASN A1144 41.857 -34.784 19.325 1.00 86.94 C ANISOU 2752 CG ASN A1144 11301 9590 12142 366 1302 -882 C ATOM 2753 OD1 ASN A1144 43.009 -35.079 19.009 1.00 88.70 O ANISOU 2753 OD1 ASN A1144 11422 9842 12436 492 1384 -962 O ATOM 2754 ND2 ASN A1144 40.917 -35.695 19.520 1.00 88.12 N ANISOU 2754 ND2 ASN A1144 11524 9486 12471 331 1301 -934 N ATOM 2755 N ARG A1145 40.960 -30.711 21.204 1.00 77.82 N ANISOU 2755 N ARG A1145 10225 8979 10365 121 922 -235 N ATOM 2756 CA ARG A1145 40.717 -29.288 21.444 1.00 75.33 C ANISOU 2756 CA ARG A1145 9922 8842 9856 37 803 -116 C ATOM 2757 C ARG A1145 41.884 -28.649 22.195 1.00 74.48 C ANISOU 2757 C ARG A1145 9737 8830 9729 110 762 56 C ATOM 2758 O ARG A1145 42.412 -27.616 21.779 1.00 74.01 O ANISOU 2758 O ARG A1145 9644 8950 9526 63 712 85 O ATOM 2759 CB ARG A1145 39.433 -29.099 22.243 1.00 74.08 C ANISOU 2759 CB ARG A1145 9834 8618 9694 -24 717 -40 C ATOM 2760 CG ARG A1145 39.149 -27.664 22.661 1.00 72.14 C ANISOU 2760 CG ARG A1145 9592 8517 9299 -85 589 64 C ATOM 2761 CD ARG A1145 37.744 -27.544 23.218 1.00 71.29 C ANISOU 2761 CD ARG A1145 9541 8368 9175 -146 522 81 C ATOM 2762 NE ARG A1145 37.336 -26.163 23.457 1.00 69.86 N ANISOU 2762 NE ARG A1145 9361 8306 8874 -199 399 129 N ATOM 2763 CZ ARG A1145 36.089 -25.789 23.746 1.00 69.83 C ANISOU 2763 CZ ARG A1145 9391 8311 8830 -254 330 118 C ATOM 2764 NH1 ARG A1145 35.117 -26.689 23.835 1.00 70.23 N ANISOU 2764 NH1 ARG A1145 9478 8278 8925 -281 369 77 N ATOM 2765 NH2 ARG A1145 35.806 -24.507 23.943 1.00 69.65 N ANISOU 2765 NH2 ARG A1145 9356 8373 8734 -282 215 145 N ATOM 2766 N ALA A1146 42.279 -29.278 23.297 1.00 74.36 N ANISOU 2766 N ALA A1146 9686 8704 9862 211 774 187 N ATOM 2767 CA ALA A1146 43.387 -28.806 24.123 1.00 73.74 C ANISOU 2767 CA ALA A1146 9522 8723 9773 278 739 363 C ATOM 2768 C ALA A1146 44.656 -28.567 23.320 1.00 74.15 C ANISOU 2768 C ALA A1146 9493 8909 9769 319 792 321 C ATOM 2769 O ALA A1146 45.259 -27.498 23.421 1.00 73.30 O ANISOU 2769 O ALA A1146 9346 8973 9530 279 721 412 O ATOM 2770 CB ALA A1146 43.666 -29.797 25.234 1.00 74.67 C ANISOU 2770 CB ALA A1146 9589 8703 10079 382 765 508 C ATOM 2771 N LYS A1147 45.039 -29.566 22.524 1.00 75.46 N ANISOU 2771 N LYS A1147 9627 9003 10042 392 913 173 N ATOM 2772 CA LYS A1147 46.283 -29.537 21.733 1.00 76.47 C ANISOU 2772 CA LYS A1147 9649 9280 10126 449 987 108 C ATOM 2773 C LYS A1147 46.325 -28.386 20.721 1.00 75.28 C ANISOU 2773 C LYS A1147 9494 9378 9730 313 941 53 C ATOM 2774 O LYS A1147 47.366 -27.751 20.548 1.00 75.11 O ANISOU 2774 O LYS A1147 9381 9551 9605 313 925 130 O ATOM 2775 CB LYS A1147 46.477 -30.872 20.998 1.00 78.82 C ANISOU 2775 CB LYS A1147 9911 9441 10593 552 1131 -104 C ATOM 2776 CG LYS A1147 47.883 -31.108 20.450 1.00 81.04 C ANISOU 2776 CG LYS A1147 10049 9857 10884 665 1226 -166 C ATOM 2777 CD LYS A1147 47.888 -32.107 19.288 1.00 84.04 C ANISOU 2777 CD LYS A1147 10396 10185 11350 718 1365 -480 C ATOM 2778 CE LYS A1147 47.360 -33.489 19.690 1.00 85.90 C ANISOU 2778 CE LYS A1147 10677 10059 11902 820 1419 -560 C ATOM 2779 NZ LYS A1147 47.365 -34.439 18.527 1.00 88.53 N ANISOU 2779 NZ LYS A1147 10975 10331 12329 867 1553 -913 N ATOM 2780 N ARG A1148 45.193 -28.142 20.058 1.00 74.25 N ANISOU 2780 N ARG A1148 9450 9248 9512 190 912 -59 N ATOM 2781 CA ARG A1148 45.047 -27.023 19.121 1.00 73.34 C ANISOU 2781 CA ARG A1148 9328 9359 9179 39 843 -71 C ATOM 2782 C ARG A1148 45.146 -25.691 19.849 1.00 71.58 C ANISOU 2782 C ARG A1148 9114 9205 8876 -24 690 140 C ATOM 2783 O ARG A1148 45.888 -24.799 19.433 1.00 71.31 O ANISOU 2783 O ARG A1148 9010 9366 8716 -89 635 221 O ATOM 2784 CB ARG A1148 43.695 -27.088 18.406 1.00 73.05 C ANISOU 2784 CB ARG A1148 9378 9290 9087 -77 832 -207 C ATOM 2785 CG ARG A1148 43.537 -28.256 17.452 1.00 74.63 C ANISOU 2785 CG ARG A1148 9565 9461 9329 -57 973 -462 C ATOM 2786 CD ARG A1148 42.257 -28.130 16.633 1.00 74.01 C ANISOU 2786 CD ARG A1148 9554 9422 9144 -208 948 -580 C ATOM 2787 NE ARG A1148 41.046 -28.272 17.448 1.00 72.53 N ANISOU 2787 NE ARG A1148 9481 9022 9052 -222 887 -524 N ATOM 2788 CZ ARG A1148 40.283 -29.367 17.536 1.00 72.83 C ANISOU 2788 CZ ARG A1148 9584 8863 9225 -203 951 -654 C ATOM 2789 NH1 ARG A1148 40.575 -30.476 16.861 1.00 74.91 N ANISOU 2789 NH1 ARG A1148 9817 9071 9575 -158 1082 -876 N ATOM 2790 NH2 ARG A1148 39.208 -29.354 18.319 1.00 71.50 N ANISOU 2790 NH2 ARG A1148 9501 8551 9112 -231 881 -568 N ATOM 2791 N VAL A1149 44.382 -25.569 20.935 1.00 70.29 N ANISOU 2791 N VAL A1149 9028 8888 8789 -12 618 221 N ATOM 2792 CA VAL A1149 44.425 -24.384 21.786 1.00 68.96 C ANISOU 2792 CA VAL A1149 8866 8760 8576 -56 477 381 C ATOM 2793 C VAL A1149 45.833 -24.151 22.334 1.00 69.43 C ANISOU 2793 C VAL A1149 8829 8916 8635 4 473 513 C ATOM 2794 O VAL A1149 46.292 -23.011 22.370 1.00 69.02 O ANISOU 2794 O VAL A1149 8745 8983 8494 -71 366 612 O ATOM 2795 CB VAL A1149 43.416 -24.467 22.948 1.00 67.98 C ANISOU 2795 CB VAL A1149 8812 8487 8527 -37 424 415 C ATOM 2796 CG1 VAL A1149 43.699 -23.379 23.979 1.00 67.28 C ANISOU 2796 CG1 VAL A1149 8702 8453 8407 -55 298 546 C ATOM 2797 CG2 VAL A1149 41.983 -24.356 22.424 1.00 66.77 C ANISOU 2797 CG2 VAL A1149 8745 8278 8344 -123 392 312 C ATOM 2798 N ILE A1150 46.518 -25.225 22.738 1.00 70.52 N ANISOU 2798 N ILE A1150 8911 8997 8884 137 581 522 N ATOM 2799 CA ILE A1150 47.931 -25.137 23.164 1.00 71.19 C ANISOU 2799 CA ILE A1150 8883 9197 8969 206 594 649 C ATOM 2800 C ILE A1150 48.882 -24.730 22.030 1.00 72.08 C ANISOU 2800 C ILE A1150 8907 9522 8959 163 620 623 C ATOM 2801 O ILE A1150 49.746 -23.874 22.230 1.00 72.15 O ANISOU 2801 O ILE A1150 8847 9684 8881 118 547 757 O ATOM 2802 CB ILE A1150 48.454 -26.460 23.770 1.00 72.33 C ANISOU 2802 CB ILE A1150 8968 9224 9289 370 706 677 C ATOM 2803 CG1 ILE A1150 47.871 -26.686 25.164 1.00 71.78 C ANISOU 2803 CG1 ILE A1150 8933 9028 9310 396 653 798 C ATOM 2804 CG2 ILE A1150 49.964 -26.425 23.879 1.00 73.22 C ANISOU 2804 CG2 ILE A1150 8941 9489 9389 444 738 785 C ATOM 2805 CD1 ILE A1150 48.500 -27.849 25.901 1.00 73.24 C ANISOU 2805 CD1 ILE A1150 9032 9118 9676 542 730 903 C ATOM 2806 N THR A1151 48.739 -25.347 20.854 1.00 73.08 N ANISOU 2806 N THR A1151 9021 9678 9067 167 723 448 N ATOM 2807 CA THR A1151 49.567 -24.984 19.691 1.00 74.04 C ANISOU 2807 CA THR A1151 9035 10057 9036 108 753 410 C ATOM 2808 C THR A1151 49.414 -23.507 19.384 1.00 73.16 C ANISOU 2808 C THR A1151 8936 10095 8763 -74 595 533 C ATOM 2809 O THR A1151 50.386 -22.837 19.016 1.00 73.70 O ANISOU 2809 O THR A1151 8900 10387 8715 -137 555 636 O ATOM 2810 CB THR A1151 49.180 -25.745 18.414 1.00 75.14 C ANISOU 2810 CB THR A1151 9164 10242 9144 100 872 169 C ATOM 2811 OG1 THR A1151 49.155 -27.151 18.665 1.00 76.72 O ANISOU 2811 OG1 THR A1151 9367 10240 9541 266 1007 29 O ATOM 2812 CG2 THR A1151 50.177 -25.461 17.321 1.00 76.31 C ANISOU 2812 CG2 THR A1151 9163 10711 9119 51 916 135 C ATOM 2813 N THR A1152 48.178 -23.021 19.529 1.00 71.85 N ANISOU 2813 N THR A1152 8890 9803 8606 -160 500 527 N ATOM 2814 CA THR A1152 47.855 -21.609 19.352 1.00 71.02 C ANISOU 2814 CA THR A1152 8806 9767 8409 -322 329 647 C ATOM 2815 C THR A1152 48.649 -20.765 20.341 1.00 70.41 C ANISOU 2815 C THR A1152 8696 9705 8350 -326 219 825 C ATOM 2816 O THR A1152 49.289 -19.794 19.952 1.00 70.53 O ANISOU 2816 O THR A1152 8644 9878 8275 -440 120 948 O ATOM 2817 CB THR A1152 46.340 -21.350 19.544 1.00 69.95 C ANISOU 2817 CB THR A1152 8798 9456 8323 -372 254 598 C ATOM 2818 OG1 THR A1152 45.582 -22.284 18.762 1.00 70.48 O ANISOU 2818 OG1 THR A1152 8900 9495 8385 -363 365 424 O ATOM 2819 CG2 THR A1152 45.973 -19.928 19.137 1.00 69.67 C ANISOU 2819 CG2 THR A1152 8767 9481 8222 -535 76 711 C ATOM 2820 N PHE A1153 48.622 -21.151 21.614 1.00 69.90 N ANISOU 2820 N PHE A1153 8667 9495 8397 -217 233 846 N ATOM 2821 CA PHE A1153 49.404 -20.451 22.636 1.00 69.79 C ANISOU 2821 CA PHE A1153 8610 9517 8390 -221 141 995 C ATOM 2822 C PHE A1153 50.890 -20.468 22.306 1.00 71.54 C ANISOU 2822 C PHE A1153 8696 9947 8539 -211 183 1089 C ATOM 2823 O PHE A1153 51.576 -19.482 22.536 1.00 71.55 O ANISOU 2823 O PHE A1153 8646 10053 8484 -302 68 1223 O ATOM 2824 CB PHE A1153 49.188 -21.038 24.041 1.00 68.98 C ANISOU 2824 CB PHE A1153 8535 9280 8393 -107 169 1006 C ATOM 2825 CG PHE A1153 47.965 -20.518 24.742 1.00 66.39 C ANISOU 2825 CG PHE A1153 8307 8814 8104 -147 69 965 C ATOM 2826 CD1 PHE A1153 47.796 -19.164 24.962 1.00 64.72 C ANISOU 2826 CD1 PHE A1153 8113 8610 7864 -258 -92 1002 C ATOM 2827 CD2 PHE A1153 46.992 -21.389 25.205 1.00 65.23 C ANISOU 2827 CD2 PHE A1153 8222 8527 8033 -74 135 886 C ATOM 2828 CE1 PHE A1153 46.668 -18.687 25.613 1.00 63.44 C ANISOU 2828 CE1 PHE A1153 8025 8330 7749 -277 -178 933 C ATOM 2829 CE2 PHE A1153 45.864 -20.917 25.854 1.00 63.58 C ANISOU 2829 CE2 PHE A1153 8084 8229 7843 -107 49 839 C ATOM 2830 CZ PHE A1153 45.705 -19.565 26.060 1.00 62.73 C ANISOU 2830 CZ PHE A1153 7987 8140 7705 -200 -102 851 C ATOM 2831 N ARG A1154 51.390 -21.571 21.761 1.00 73.48 N ANISOU 2831 N ARG A1154 8872 10254 8791 -104 342 1012 N ATOM 2832 CA ARG A1154 52.818 -21.647 21.446 1.00 75.75 C ANISOU 2832 CA ARG A1154 9009 10764 9007 -76 395 1090 C ATOM 2833 C ARG A1154 53.196 -20.784 20.240 1.00 76.51 C ANISOU 2833 C ARG A1154 9034 11102 8933 -238 333 1130 C ATOM 2834 O ARG A1154 54.143 -20.001 20.325 1.00 77.13 O ANISOU 2834 O ARG A1154 9022 11352 8929 -319 250 1289 O ATOM 2835 CB ARG A1154 53.293 -23.091 21.219 1.00 77.43 C ANISOU 2835 CB ARG A1154 9146 10969 9302 106 586 975 C ATOM 2836 CG ARG A1154 54.808 -23.253 21.476 1.00 80.18 C ANISOU 2836 CG ARG A1154 9330 11504 9631 188 633 1093 C ATOM 2837 CD ARG A1154 55.443 -24.422 20.714 1.00 83.93 C ANISOU 2837 CD ARG A1154 9685 12058 10147 341 815 946 C ATOM 2838 NE ARG A1154 54.598 -25.619 20.740 1.00 85.31 N ANISOU 2838 NE ARG A1154 9941 11970 10502 469 923 766 N ATOM 2839 CZ ARG A1154 53.954 -26.132 19.690 1.00 87.11 C ANISOU 2839 CZ ARG A1154 10201 12174 10720 460 1007 536 C ATOM 2840 NH1 ARG A1154 54.049 -25.584 18.475 1.00 87.77 N ANISOU 2840 NH1 ARG A1154 10231 12512 10603 330 1004 458 N ATOM 2841 NH2 ARG A1154 53.210 -27.222 19.856 1.00 87.94 N ANISOU 2841 NH2 ARG A1154 10383 12013 11016 570 1090 391 N ATOM 2842 N THR A1155 52.456 -20.927 19.137 1.00 76.76 N ANISOU 2842 N THR A1155 9095 11164 8906 -301 366 1001 N ATOM 2843 CA THR A1155 52.822 -20.304 17.853 1.00 77.79 C ANISOU 2843 CA THR A1155 9124 11579 8853 -460 329 1041 C ATOM 2844 C THR A1155 52.316 -18.874 17.690 1.00 76.97 C ANISOU 2844 C THR A1155 9068 11474 8703 -666 118 1199 C ATOM 2845 O THR A1155 52.996 -18.037 17.103 1.00 77.78 O ANISOU 2845 O THR A1155 9064 11805 8682 -815 25 1353 O ATOM 2846 CB THR A1155 52.295 -21.127 16.647 1.00 78.81 C ANISOU 2846 CB THR A1155 9234 11797 8914 -453 462 826 C ATOM 2847 OG1 THR A1155 50.891 -21.369 16.801 1.00 77.42 O ANISOU 2847 OG1 THR A1155 9213 11370 8833 -448 451 715 O ATOM 2848 CG2 THR A1155 53.026 -22.458 16.529 1.00 80.38 C ANISOU 2848 CG2 THR A1155 9338 12045 9155 -262 666 656 C ATOM 2849 N GLY A1156 51.119 -18.602 18.195 1.00 75.58 N ANISOU 2849 N GLY A1156 9038 11041 8638 -675 39 1165 N ATOM 2850 CA GLY A1156 50.470 -17.305 17.988 1.00 75.16 C ANISOU 2850 CA GLY A1156 9031 10939 8587 -849 -160 1287 C ATOM 2851 C GLY A1156 49.861 -17.174 16.602 1.00 75.82 C ANISOU 2851 C GLY A1156 9083 11170 8555 -983 -171 1267 C ATOM 2852 O GLY A1156 49.655 -16.065 16.109 1.00 76.21 O ANISOU 2852 O GLY A1156 9106 11272 8575 -1158 -341 1427 O ATOM 2853 N THR A1157 49.560 -18.317 15.988 1.00 76.13 N ANISOU 2853 N THR A1157 9114 11271 8539 -906 3 1073 N ATOM 2854 CA THR A1157 49.039 -18.389 14.630 1.00 77.08 C ANISOU 2854 CA THR A1157 9181 11588 8514 -1031 26 1017 C ATOM 2855 C THR A1157 47.865 -19.337 14.621 1.00 76.27 C ANISOU 2855 C THR A1157 9192 11306 8479 -942 134 795 C ATOM 2856 O THR A1157 47.541 -19.907 15.655 1.00 75.15 O ANISOU 2856 O THR A1157 9156 10901 8493 -791 185 710 O ATOM 2857 CB THR A1157 50.091 -18.962 13.689 1.00 79.10 C ANISOU 2857 CB THR A1157 9267 12196 8590 -1040 161 955 C ATOM 2858 OG1 THR A1157 50.485 -20.256 14.166 1.00 79.57 O ANISOU 2858 OG1 THR A1157 9336 12164 8731 -823 355 751 O ATOM 2859 CG2 THR A1157 51.301 -18.055 13.630 1.00 79.84 C ANISOU 2859 CG2 THR A1157 9228 12514 8593 -1145 56 1191 C ATOM 2860 N TRP A1158 47.240 -19.527 13.462 1.00 77.22 N ANISOU 2860 N TRP A1158 9277 11590 8472 -1050 167 709 N ATOM 2861 CA TRP A1158 46.103 -20.452 13.356 1.00 77.07 C ANISOU 2861 CA TRP A1158 9358 11420 8504 -990 268 489 C ATOM 2862 C TRP A1158 46.467 -21.787 12.702 1.00 79.03 C ANISOU 2862 C TRP A1158 9540 11800 8685 -907 483 226 C ATOM 2863 O TRP A1158 45.622 -22.426 12.068 1.00 79.40 O ANISOU 2863 O TRP A1158 9615 11857 8693 -938 558 41 O ATOM 2864 CB TRP A1158 44.955 -19.811 12.585 1.00 76.86 C ANISOU 2864 CB TRP A1158 9348 11451 8401 -1165 155 548 C ATOM 2865 CG TRP A1158 44.521 -18.510 13.121 1.00 74.78 C ANISOU 2865 CG TRP A1158 9136 11039 8235 -1238 -59 779 C ATOM 2866 CD1 TRP A1158 44.957 -17.287 12.732 1.00 74.83 C ANISOU 2866 CD1 TRP A1158 9052 11188 8188 -1394 -229 1027 C ATOM 2867 CD2 TRP A1158 43.546 -18.287 14.139 1.00 72.31 C ANISOU 2867 CD2 TRP A1158 8966 10402 8106 -1161 -133 776 C ATOM 2868 NE1 TRP A1158 44.312 -16.306 13.442 1.00 73.74 N ANISOU 2868 NE1 TRP A1158 8999 10801 8217 -1408 -408 1162 N ATOM 2869 CE2 TRP A1158 43.437 -16.894 14.313 1.00 72.03 C ANISOU 2869 CE2 TRP A1158 8920 10312 8134 -1262 -346 999 C ATOM 2870 CE3 TRP A1158 42.751 -19.127 14.921 1.00 70.90 C ANISOU 2870 CE3 TRP A1158 8910 9983 8045 -1021 -44 608 C ATOM 2871 CZ2 TRP A1158 42.568 -16.322 15.238 1.00 70.66 C ANISOU 2871 CZ2 TRP A1158 8850 9861 8136 -1210 -462 1022 C ATOM 2872 CZ3 TRP A1158 41.883 -18.555 15.843 1.00 69.37 C ANISOU 2872 CZ3 TRP A1158 8812 9548 7994 -985 -159 656 C ATOM 2873 CH2 TRP A1158 41.801 -17.168 15.992 1.00 69.21 C ANISOU 2873 CH2 TRP A1158 8775 9488 8033 -1071 -360 842 C ATOM 2874 N ASP A1159 47.711 -22.221 12.889 1.00 80.46 N ANISOU 2874 N ASP A1159 9629 12071 8869 -796 579 197 N ATOM 2875 CA ASP A1159 48.190 -23.484 12.316 1.00 82.76 C ANISOU 2875 CA ASP A1159 9837 12473 9133 -689 784 -72 C ATOM 2876 C ASP A1159 47.319 -24.696 12.685 1.00 82.44 C ANISOU 2876 C ASP A1159 9923 12124 9274 -556 898 -310 C ATOM 2877 O ASP A1159 47.207 -25.641 11.902 1.00 84.17 O ANISOU 2877 O ASP A1159 10096 12423 9459 -534 1041 -577 O ATOM 2878 CB ASP A1159 49.644 -23.738 12.730 1.00 83.87 C ANISOU 2878 CB ASP A1159 9866 12693 9306 -552 856 -38 C ATOM 2879 CG ASP A1159 50.596 -22.654 12.233 1.00 85.93 C ANISOU 2879 CG ASP A1159 9974 13306 9366 -698 758 180 C ATOM 2880 OD1 ASP A1159 51.620 -22.395 12.919 1.00 87.87 O ANISOU 2880 OD1 ASP A1159 10168 13559 9657 -626 734 326 O ATOM 2881 OD2 ASP A1159 50.316 -22.055 11.167 1.00 87.69 O ANISOU 2881 OD2 ASP A1159 10121 13810 9386 -899 695 225 O ATOM 2882 N ALA A1160 46.691 -24.672 13.857 1.00 80.44 N ANISOU 2882 N ALA A1160 9819 11535 9209 -481 833 -220 N ATOM 2883 CA ALA A1160 45.781 -25.745 14.230 1.00 80.12 C ANISOU 2883 CA ALA A1160 9894 11208 9336 -387 915 -399 C ATOM 2884 C ALA A1160 44.388 -25.570 13.610 1.00 79.72 C ANISOU 2884 C ALA A1160 9922 11159 9207 -537 866 -465 C ATOM 2885 O ALA A1160 43.470 -26.316 13.951 1.00 79.47 O ANISOU 2885 O ALA A1160 9997 10892 9304 -492 905 -581 O ATOM 2886 CB ALA A1160 45.678 -25.832 15.732 1.00 78.59 C ANISOU 2886 CB ALA A1160 9800 10709 9348 -260 867 -265 C ATOM 2887 N TYR A1161 44.231 -24.588 12.717 1.00 79.83 N ANISOU 2887 N TYR A1161 9872 11444 9016 -722 771 -369 N ATOM 2888 CA TYR A1161 42.941 -24.279 12.085 1.00 79.56 C ANISOU 2888 CA TYR A1161 9886 11450 8891 -880 704 -386 C ATOM 2889 C TYR A1161 43.153 -23.693 10.683 1.00 80.98 C ANISOU 2889 C TYR A1161 9918 12041 8807 -1076 676 -360 C ATOM 2890 O TYR A1161 42.999 -24.368 9.670 1.00 82.55 O ANISOU 2890 O TYR A1161 10048 12439 8875 -1140 787 -580 O ATOM 2891 CB TYR A1161 42.160 -23.244 12.915 1.00 77.68 C ANISOU 2891 CB TYR A1161 9750 11029 8735 -915 524 -156 C ATOM 2892 CG TYR A1161 42.000 -23.516 14.413 1.00 75.97 C ANISOU 2892 CG TYR A1161 9651 10475 8738 -752 515 -119 C ATOM 2893 CD1 TYR A1161 40.841 -24.100 14.914 1.00 75.78 C ANISOU 2893 CD1 TYR A1161 9742 10225 8824 -713 532 -207 C ATOM 2894 CD2 TYR A1161 42.980 -23.138 15.325 1.00 75.07 C ANISOU 2894 CD2 TYR A1161 9518 10304 8701 -656 478 19 C ATOM 2895 CE1 TYR A1161 40.673 -24.328 16.279 1.00 74.42 C ANISOU 2895 CE1 TYR A1161 9652 9798 8824 -585 517 -154 C ATOM 2896 CE2 TYR A1161 42.823 -23.367 16.692 1.00 74.00 C ANISOU 2896 CE2 TYR A1161 9466 9913 8736 -528 465 62 C ATOM 2897 CZ TYR A1161 41.666 -23.963 17.158 1.00 73.89 C ANISOU 2897 CZ TYR A1161 9556 9699 8820 -494 485 -22 C ATOM 2898 OH TYR A1161 41.489 -24.197 18.501 1.00 73.74 O ANISOU 2898 OH TYR A1161 9597 9475 8943 -386 469 34 O ATOM 2899 N GLY A 231 48.593 -24.195 5.340 1.00111.39 N ANISOU 2899 N GLY A 231 16444 11894 13982 -1029 2119 -597 N ATOM 2900 CA GLY A 231 49.177 -22.962 5.857 1.00110.02 C ANISOU 2900 CA GLY A 231 16178 11878 13745 -942 2026 -490 C ATOM 2901 C GLY A 231 49.870 -23.208 7.184 1.00110.14 C ANISOU 2901 C GLY A 231 16348 11850 13649 -880 2145 -339 C ATOM 2902 O GLY A 231 49.265 -23.759 8.105 1.00111.27 O ANISOU 2902 O GLY A 231 16590 11866 13820 -975 2319 -363 O ATOM 2903 N HIS A 232 51.144 -22.820 7.277 1.00109.18 N ANISOU 2903 N HIS A 232 16258 11819 13407 -714 2052 -190 N ATOM 2904 CA HIS A 232 51.951 -23.085 8.481 1.00109.53 C ANISOU 2904 CA HIS A 232 16466 11817 13331 -622 2117 -44 C ATOM 2905 C HIS A 232 53.055 -22.033 8.751 1.00107.76 C ANISOU 2905 C HIS A 232 16161 11741 13042 -478 1958 77 C ATOM 2906 O HIS A 232 53.588 -21.426 7.818 1.00106.72 O ANISOU 2906 O HIS A 232 15894 11722 12933 -406 1827 88 O ATOM 2907 CB HIS A 232 52.513 -24.537 8.497 1.00110.97 C ANISOU 2907 CB HIS A 232 16884 11846 13433 -555 2234 19 C ATOM 2908 CG HIS A 232 52.802 -25.127 7.140 1.00112.17 C ANISOU 2908 CG HIS A 232 17033 11983 13602 -515 2198 -12 C ATOM 2909 ND1 HIS A 232 54.050 -25.615 6.794 1.00113.23 N ANISOU 2909 ND1 HIS A 232 17263 12106 13652 -348 2171 106 N ATOM 2910 CD2 HIS A 232 52.003 -25.350 6.063 1.00113.42 C ANISOU 2910 CD2 HIS A 232 17124 12119 13851 -614 2189 -154 C ATOM 2911 CE1 HIS A 232 54.013 -26.088 5.559 1.00113.43 C ANISOU 2911 CE1 HIS A 232 17293 12103 13701 -347 2164 45 C ATOM 2912 NE2 HIS A 232 52.783 -25.938 5.093 1.00113.79 N ANISOU 2912 NE2 HIS A 232 17249 12141 13843 -505 2162 -114 N ATOM 2913 N GLN A 233 53.359 -21.823 10.038 1.00107.26 N ANISOU 2913 N GLN A 233 16192 11660 12900 -438 1976 161 N ATOM 2914 CA GLN A 233 54.301 -20.791 10.513 1.00105.68 C ANISOU 2914 CA GLN A 233 15916 11583 12654 -319 1819 260 C ATOM 2915 C GLN A 233 54.130 -19.445 9.790 1.00103.53 C ANISOU 2915 C GLN A 233 15386 11479 12471 -348 1683 206 C ATOM 2916 O GLN A 233 54.933 -19.099 8.923 1.00102.94 O ANISOU 2916 O GLN A 233 15205 11487 12418 -253 1578 244 O ATOM 2917 CB GLN A 233 55.750 -21.287 10.390 1.00105.86 C ANISOU 2917 CB GLN A 233 16013 11593 12612 -134 1747 389 C ATOM 2918 N LYS A 234 53.097 -18.686 10.161 1.00102.22 N ANISOU 2918 N LYS A 234 15128 11351 12358 -472 1702 121 N ATOM 2919 CA LYS A 234 52.730 -17.471 9.430 1.00100.17 C ANISOU 2919 CA LYS A 234 14638 11233 12186 -511 1588 52 C ATOM 2920 C LYS A 234 52.261 -16.316 10.320 1.00 98.93 C ANISOU 2920 C LYS A 234 14400 11146 12043 -567 1558 36 C ATOM 2921 O LYS A 234 51.237 -15.706 10.023 1.00 98.64 O ANISOU 2921 O LYS A 234 14226 11151 12102 -675 1561 -72 O ATOM 2922 CB LYS A 234 51.613 -17.815 8.438 1.00100.34 C ANISOU 2922 CB LYS A 234 14589 11224 12312 -630 1633 -93 C ATOM 2923 N ARG A 235 53.001 -15.995 11.386 1.00 98.07 N ANISOU 2923 N ARG A 235 14375 11044 11842 -487 1518 138 N ATOM 2924 CA ARG A 235 52.519 -15.011 12.387 1.00 97.15 C ANISOU 2924 CA ARG A 235 14235 10962 11714 -541 1513 124 C ATOM 2925 C ARG A 235 52.605 -13.578 11.906 1.00 95.03 C ANISOU 2925 C ARG A 235 13741 10854 11510 -534 1367 102 C ATOM 2926 O ARG A 235 53.660 -13.149 11.442 1.00 94.46 O ANISOU 2926 O ARG A 235 13591 10865 11435 -425 1234 170 O ATOM 2927 CB ARG A 235 53.285 -15.101 13.718 1.00 97.88 C ANISOU 2927 CB ARG A 235 14522 10998 11668 -448 1493 232 C ATOM 2928 CG ARG A 235 52.951 -13.940 14.685 1.00 97.61 C ANISOU 2928 CG ARG A 235 14471 11009 11606 -483 1459 224 C ATOM 2929 CD ARG A 235 53.335 -14.221 16.127 1.00 98.88 C ANISOU 2929 CD ARG A 235 14900 11061 11606 -416 1481 303 C ATOM 2930 NE ARG A 235 52.813 -13.193 17.036 1.00 99.30 N ANISOU 2930 NE ARG A 235 14969 11132 11626 -468 1488 279 N ATOM 2931 CZ ARG A 235 53.431 -12.051 17.369 1.00 98.88 C ANISOU 2931 CZ ARG A 235 14838 11182 11549 -405 1308 313 C ATOM 2932 NH1 ARG A 235 54.629 -11.737 16.877 1.00 98.57 N ANISOU 2932 NH1 ARG A 235 14674 11240 11535 -289 1105 372 N ATOM 2933 NH2 ARG A 235 52.839 -11.207 18.211 1.00 98.81 N ANISOU 2933 NH2 ARG A 235 14873 11168 11501 -461 1344 284 N ATOM 2934 N LYS A 236 51.513 -12.832 12.074 1.00 93.72 N ANISOU 2934 N LYS A 236 13477 10719 11414 -648 1406 11 N ATOM 2935 CA LYS A 236 51.473 -11.421 11.707 1.00 91.85 C ANISOU 2935 CA LYS A 236 13042 10622 11232 -647 1281 -13 C ATOM 2936 C LYS A 236 50.984 -10.555 12.866 1.00 91.09 C ANISOU 2936 C LYS A 236 12961 10533 11115 -700 1309 -22 C ATOM 2937 O LYS A 236 49.841 -10.668 13.296 1.00 91.72 O ANISOU 2937 O LYS A 236 13059 10544 11244 -814 1447 -103 O ATOM 2938 CB LYS A 236 50.621 -11.231 10.445 1.00 91.49 C ANISOU 2938 CB LYS A 236 12831 10623 11308 -714 1265 -129 C ATOM 2939 CG LYS A 236 51.413 -10.790 9.187 1.00 90.89 C ANISOU 2939 CG LYS A 236 12647 10644 11242 -616 1128 -101 C ATOM 2940 CD LYS A 236 52.723 -11.560 8.919 1.00 91.41 C ANISOU 2940 CD LYS A 236 12812 10679 11239 -493 1108 7 C ATOM 2941 CE LYS A 236 53.761 -10.715 8.176 1.00 90.88 C ANISOU 2941 CE LYS A 236 12636 10711 11184 -384 991 70 C ATOM 2942 NZ LYS A 236 55.155 -11.034 8.590 1.00 91.16 N ANISOU 2942 NZ LYS A 236 12731 10726 11178 -264 960 194 N ATOM 2943 N ALA A 237 51.872 -9.689 13.359 1.00 89.62 N ANISOU 2943 N ALA A 237 12764 10419 10867 -616 1183 55 N ATOM 2944 CA ALA A 237 51.625 -8.892 14.560 1.00 89.03 C ANISOU 2944 CA ALA A 237 12751 10339 10737 -641 1192 63 C ATOM 2945 C ALA A 237 51.119 -7.490 14.241 1.00 87.31 C ANISOU 2945 C ALA A 237 12333 10238 10604 -689 1129 3 C ATOM 2946 O ALA A 237 51.483 -6.893 13.226 1.00 86.17 O ANISOU 2946 O ALA A 237 12016 10199 10524 -651 1016 -1 O ATOM 2947 CB ALA A 237 52.892 -8.801 15.403 1.00 89.37 C ANISOU 2947 CB ALA A 237 12923 10374 10658 -518 1070 175 C ATOM 2948 N LEU A 238 50.286 -6.984 15.149 1.00 86.91 N ANISOU 2948 N LEU A 238 12326 10150 10543 -765 1220 -37 N ATOM 2949 CA LEU A 238 49.655 -5.664 15.070 1.00 85.43 C ANISOU 2949 CA LEU A 238 11978 10050 10431 -817 1190 -98 C ATOM 2950 C LEU A 238 50.183 -4.682 16.128 1.00 84.61 C ANISOU 2950 C LEU A 238 11949 9969 10228 -774 1114 -41 C ATOM 2951 O LEU A 238 50.385 -3.493 15.848 1.00 83.81 O ANISOU 2951 O LEU A 238 11702 9975 10165 -756 1000 -46 O ATOM 2952 CB LEU A 238 48.151 -5.824 15.299 1.00 86.18 C ANISOU 2952 CB LEU A 238 12052 10068 10624 -948 1378 -207 C ATOM 2953 CG LEU A 238 47.397 -6.787 14.379 1.00 86.34 C ANISOU 2953 CG LEU A 238 11994 10041 10768 -1016 1459 -294 C ATOM 2954 CD1 LEU A 238 46.430 -7.673 15.168 1.00 87.47 C ANISOU 2954 CD1 LEU A 238 12267 10019 10948 -1120 1700 -347 C ATOM 2955 CD2 LEU A 238 46.673 -5.992 13.309 1.00 85.90 C ANISOU 2955 CD2 LEU A 238 11687 10084 10864 -1052 1378 -397 C ATOM 2956 N LYS A 239 50.403 -5.192 17.340 1.00 84.59 N ANISOU 2956 N LYS A 239 12193 9854 10092 -752 1176 10 N ATOM 2957 CA LYS A 239 50.645 -4.357 18.530 1.00 84.06 C ANISOU 2957 CA LYS A 239 12256 9769 9912 -724 1132 44 C ATOM 2958 C LYS A 239 51.717 -3.281 18.283 1.00 81.95 C ANISOU 2958 C LYS A 239 11856 9628 9649 -642 898 87 C ATOM 2959 O LYS A 239 51.481 -2.102 18.560 1.00 81.27 O ANISOU 2959 O LYS A 239 11704 9597 9577 -668 861 61 O ATOM 2960 CB LYS A 239 50.985 -5.218 19.775 1.00 85.72 C ANISOU 2960 CB LYS A 239 12800 9826 9942 -673 1192 109 C ATOM 2961 CG LYS A 239 50.250 -6.597 19.858 1.00 87.31 C ANISOU 2961 CG LYS A 239 13150 9883 10141 -731 1422 87 C ATOM 2962 CD LYS A 239 51.115 -7.792 19.329 1.00 87.64 C ANISOU 2962 CD LYS A 239 13239 9903 10156 -649 1359 147 C ATOM 2963 CE LYS A 239 50.441 -8.665 18.242 1.00 86.99 C ANISOU 2963 CE LYS A 239 13028 9809 10215 -729 1485 83 C ATOM 2964 NZ LYS A 239 48.939 -8.627 18.186 1.00 87.01 N ANISOU 2964 NZ LYS A 239 12958 9758 10343 -880 1699 -27 N ATOM 2965 N PRO A 240 52.881 -3.673 17.726 1.00 80.36 N ANISOU 2965 N PRO A 240 11606 9468 9458 -547 756 148 N ATOM 2966 CA PRO A 240 53.911 -2.662 17.467 1.00 78.73 C ANISOU 2966 CA PRO A 240 11254 9364 9294 -477 557 182 C ATOM 2967 C PRO A 240 53.467 -1.584 16.478 1.00 76.23 C ANISOU 2967 C PRO A 240 10691 9165 9106 -529 550 126 C ATOM 2968 O PRO A 240 53.839 -0.419 16.629 1.00 76.17 O ANISOU 2968 O PRO A 240 10598 9221 9120 -515 445 129 O ATOM 2969 CB PRO A 240 55.077 -3.478 16.887 1.00 78.84 C ANISOU 2969 CB PRO A 240 11240 9379 9335 -376 463 247 C ATOM 2970 CG PRO A 240 54.813 -4.887 17.297 1.00 80.46 C ANISOU 2970 CG PRO A 240 11658 9462 9448 -371 578 266 C ATOM 2971 CD PRO A 240 53.324 -5.014 17.303 1.00 80.78 C ANISOU 2971 CD PRO A 240 11726 9466 9501 -498 781 187 C ATOM 2972 N THR A 241 52.675 -1.964 15.481 1.00 74.02 N ANISOU 2972 N THR A 241 10310 8904 8909 -584 652 72 N ATOM 2973 CA THR A 241 52.202 -1.001 14.496 1.00 71.60 C ANISOU 2973 CA THR A 241 9798 8696 8710 -617 635 16 C ATOM 2974 C THR A 241 51.228 -0.006 15.118 1.00 70.46 C ANISOU 2974 C THR A 241 9637 8561 8571 -692 688 -43 C ATOM 2975 O THR A 241 51.408 1.201 14.968 1.00 70.18 O ANISOU 2975 O THR A 241 9493 8601 8567 -681 608 -47 O ATOM 2976 CB THR A 241 51.555 -1.689 13.281 1.00 71.29 C ANISOU 2976 CB THR A 241 9676 8660 8749 -646 703 -39 C ATOM 2977 OG1 THR A 241 52.541 -1.875 12.261 1.00 70.53 O ANISOU 2977 OG1 THR A 241 9512 8605 8681 -561 622 9 O ATOM 2978 CG2 THR A 241 50.431 -0.846 12.716 1.00 70.82 C ANISOU 2978 CG2 THR A 241 9475 8655 8778 -710 729 -133 C ATOM 2979 N VAL A 242 50.211 -0.502 15.820 1.00 69.55 N ANISOU 2979 N VAL A 242 9632 8359 8433 -768 838 -89 N ATOM 2980 CA VAL A 242 49.218 0.375 16.452 1.00 68.40 C ANISOU 2980 CA VAL A 242 9478 8204 8307 -841 922 -149 C ATOM 2981 C VAL A 242 49.882 1.447 17.344 1.00 67.34 C ANISOU 2981 C VAL A 242 9410 8092 8083 -801 822 -102 C ATOM 2982 O VAL A 242 49.469 2.608 17.330 1.00 66.56 O ANISOU 2982 O VAL A 242 9212 8047 8028 -827 809 -140 O ATOM 2983 CB VAL A 242 48.142 -0.435 17.253 1.00 69.58 C ANISOU 2983 CB VAL A 242 9770 8219 8446 -926 1138 -195 C ATOM 2984 CG1 VAL A 242 47.281 0.482 18.096 1.00 69.41 C ANISOU 2984 CG1 VAL A 242 9773 8166 8431 -986 1242 -241 C ATOM 2985 CG2 VAL A 242 47.257 -1.246 16.312 1.00 68.91 C ANISOU 2985 CG2 VAL A 242 9566 8116 8501 -988 1232 -276 C ATOM 2986 N ILE A 243 50.924 1.070 18.083 1.00 66.73 N ANISOU 2986 N ILE A 243 9497 7969 7886 -731 735 -25 N ATOM 2987 CA ILE A 243 51.638 2.028 18.937 1.00 66.07 C ANISOU 2987 CA ILE A 243 9485 7896 7721 -687 605 9 C ATOM 2988 C ILE A 243 52.370 3.084 18.119 1.00 64.02 C ANISOU 2988 C ILE A 243 9008 7758 7559 -650 448 17 C ATOM 2989 O ILE A 243 52.353 4.265 18.462 1.00 63.72 O ANISOU 2989 O ILE A 243 8935 7753 7521 -663 398 0 O ATOM 2990 CB ILE A 243 52.658 1.338 19.858 1.00 67.25 C ANISOU 2990 CB ILE A 243 9855 7962 7732 -602 505 80 C ATOM 2991 CG1 ILE A 243 51.946 0.454 20.875 1.00 68.71 C ANISOU 2991 CG1 ILE A 243 10318 8002 7787 -631 676 79 C ATOM 2992 CG2 ILE A 243 53.488 2.368 20.611 1.00 67.27 C ANISOU 2992 CG2 ILE A 243 9902 7980 7676 -550 322 102 C ATOM 2993 CD1 ILE A 243 52.894 -0.404 21.667 1.00 70.31 C ANISOU 2993 CD1 ILE A 243 10764 8109 7841 -530 578 150 C ATOM 2994 N LEU A 244 53.020 2.656 17.048 1.00 62.30 N ANISOU 2994 N LEU A 244 8658 7590 7421 -604 389 44 N ATOM 2995 CA LEU A 244 53.698 3.587 16.155 1.00 60.73 C ANISOU 2995 CA LEU A 244 8262 7487 7326 -569 283 53 C ATOM 2996 C LEU A 244 52.741 4.667 15.642 1.00 59.38 C ANISOU 2996 C LEU A 244 7964 7378 7219 -627 342 -10 C ATOM 2997 O LEU A 244 52.997 5.862 15.791 1.00 58.96 O ANISOU 2997 O LEU A 244 7848 7365 7186 -625 275 -13 O ATOM 2998 CB LEU A 244 54.331 2.831 14.978 1.00 60.29 C ANISOU 2998 CB LEU A 244 8110 7453 7344 -515 269 86 C ATOM 2999 CG LEU A 244 55.011 3.657 13.884 1.00 58.70 C ANISOU 2999 CG LEU A 244 7722 7325 7254 -473 208 100 C ATOM 3000 CD1 LEU A 244 55.878 4.744 14.493 1.00 57.94 C ANISOU 3000 CD1 LEU A 244 7583 7245 7185 -451 86 122 C ATOM 3001 CD2 LEU A 244 55.828 2.745 12.980 1.00 57.37 C ANISOU 3001 CD2 LEU A 244 7515 7145 7137 -404 205 148 C ATOM 3002 N ILE A 245 51.631 4.239 15.056 1.00 58.45 N ANISOU 3002 N ILE A 245 7808 7259 7139 -677 458 -67 N ATOM 3003 CA ILE A 245 50.669 5.172 14.483 1.00 57.44 C ANISOU 3003 CA ILE A 245 7554 7185 7086 -717 498 -136 C ATOM 3004 C ILE A 245 50.063 6.113 15.527 1.00 57.15 C ANISOU 3004 C ILE A 245 7566 7131 7015 -766 538 -167 C ATOM 3005 O ILE A 245 50.136 7.328 15.365 1.00 56.60 O ANISOU 3005 O ILE A 245 7412 7116 6976 -758 485 -176 O ATOM 3006 CB ILE A 245 49.574 4.429 13.701 1.00 57.57 C ANISOU 3006 CB ILE A 245 7516 7189 7169 -756 590 -206 C ATOM 3007 CG1 ILE A 245 50.123 4.026 12.329 1.00 57.15 C ANISOU 3007 CG1 ILE A 245 7383 7176 7156 -694 528 -188 C ATOM 3008 CG2 ILE A 245 48.346 5.299 13.538 1.00 57.53 C ANISOU 3008 CG2 ILE A 245 7408 7209 7239 -806 639 -293 C ATOM 3009 CD1 ILE A 245 49.329 2.956 11.642 1.00 57.58 C ANISOU 3009 CD1 ILE A 245 7428 7195 7253 -721 590 -248 C ATOM 3010 N LEU A 246 49.487 5.569 16.598 1.00 57.30 N ANISOU 3010 N LEU A 246 7739 7062 6968 -814 644 -181 N ATOM 3011 CA LEU A 246 48.928 6.416 17.662 1.00 57.19 C ANISOU 3011 CA LEU A 246 7809 7010 6908 -856 706 -207 C ATOM 3012 C LEU A 246 49.953 7.430 18.163 1.00 56.50 C ANISOU 3012 C LEU A 246 7756 6953 6757 -811 559 -161 C ATOM 3013 O LEU A 246 49.664 8.616 18.273 1.00 56.20 O ANISOU 3013 O LEU A 246 7663 6948 6742 -827 552 -189 O ATOM 3014 CB LEU A 246 48.425 5.579 18.840 1.00 58.39 C ANISOU 3014 CB LEU A 246 8183 7034 6966 -896 851 -209 C ATOM 3015 CG LEU A 246 47.130 4.781 18.640 1.00 59.03 C ANISOU 3015 CG LEU A 246 8235 7054 7139 -972 1049 -279 C ATOM 3016 CD1 LEU A 246 46.845 3.904 19.862 1.00 60.18 C ANISOU 3016 CD1 LEU A 246 8641 7048 7175 -1002 1211 -263 C ATOM 3017 CD2 LEU A 246 45.942 5.682 18.346 1.00 58.29 C ANISOU 3017 CD2 LEU A 246 7979 6989 7178 -1028 1133 -367 C ATOM 3018 N ALA A 247 51.154 6.961 18.460 1.00 56.40 N ANISOU 3018 N ALA A 247 7826 6923 6680 -751 436 -95 N ATOM 3019 CA ALA A 247 52.234 7.849 18.887 1.00 56.19 C ANISOU 3019 CA ALA A 247 7806 6916 6626 -707 270 -62 C ATOM 3020 C ALA A 247 52.459 8.971 17.875 1.00 54.91 C ANISOU 3020 C ALA A 247 7423 6851 6586 -701 214 -75 C ATOM 3021 O ALA A 247 52.603 10.137 18.254 1.00 54.74 O ANISOU 3021 O ALA A 247 7389 6843 6564 -710 161 -89 O ATOM 3022 CB ALA A 247 53.517 7.058 19.092 1.00 56.59 C ANISOU 3022 CB ALA A 247 7920 6937 6642 -632 131 0 C ATOM 3023 N PHE A 248 52.478 8.603 16.592 1.00 53.97 N ANISOU 3023 N PHE A 248 7157 6786 6563 -682 235 -72 N ATOM 3024 CA PHE A 248 52.721 9.551 15.494 1.00 52.88 C ANISOU 3024 CA PHE A 248 6841 6722 6528 -660 201 -76 C ATOM 3025 C PHE A 248 51.673 10.667 15.460 1.00 52.05 C ANISOU 3025 C PHE A 248 6689 6644 6440 -703 266 -135 C ATOM 3026 O PHE A 248 52.002 11.830 15.242 1.00 51.24 O ANISOU 3026 O PHE A 248 6514 6576 6379 -692 220 -135 O ATOM 3027 CB PHE A 248 52.758 8.820 14.137 1.00 52.44 C ANISOU 3027 CB PHE A 248 6691 6696 6537 -625 233 -67 C ATOM 3028 CG PHE A 248 53.022 9.726 12.974 1.00 52.06 C ANISOU 3028 CG PHE A 248 6507 6701 6572 -588 217 -66 C ATOM 3029 CD1 PHE A 248 54.305 9.887 12.484 1.00 53.50 C ANISOU 3029 CD1 PHE A 248 6623 6886 6817 -533 158 -10 C ATOM 3030 CD2 PHE A 248 51.990 10.443 12.388 1.00 52.19 C ANISOU 3030 CD2 PHE A 248 6466 6751 6611 -603 267 -122 C ATOM 3031 CE1 PHE A 248 54.562 10.749 11.416 1.00 53.61 C ANISOU 3031 CE1 PHE A 248 6539 6926 6901 -497 176 -5 C ATOM 3032 CE2 PHE A 248 52.227 11.302 11.331 1.00 52.32 C ANISOU 3032 CE2 PHE A 248 6396 6801 6681 -556 258 -117 C ATOM 3033 CZ PHE A 248 53.521 11.457 10.838 1.00 53.05 C ANISOU 3033 CZ PHE A 248 6446 6887 6822 -505 225 -55 C ATOM 3034 N PHE A 249 50.413 10.301 15.666 1.00 51.80 N ANISOU 3034 N PHE A 249 6695 6590 6396 -751 381 -189 N ATOM 3035 CA PHE A 249 49.331 11.273 15.619 1.00 51.48 C ANISOU 3035 CA PHE A 249 6596 6568 6395 -785 449 -252 C ATOM 3036 C PHE A 249 49.234 12.090 16.897 1.00 51.73 C ANISOU 3036 C PHE A 249 6739 6558 6356 -818 465 -258 C ATOM 3037 O PHE A 249 48.939 13.275 16.838 1.00 51.52 O ANISOU 3037 O PHE A 249 6657 6559 6359 -822 465 -283 O ATOM 3038 CB PHE A 249 48.011 10.592 15.277 1.00 51.64 C ANISOU 3038 CB PHE A 249 6577 6571 6473 -823 565 -320 C ATOM 3039 CG PHE A 249 47.884 10.261 13.820 1.00 51.50 C ANISOU 3039 CG PHE A 249 6430 6603 6534 -782 527 -340 C ATOM 3040 CD1 PHE A 249 48.486 9.124 13.300 1.00 52.26 C ANISOU 3040 CD1 PHE A 249 6546 6691 6616 -755 499 -303 C ATOM 3041 CD2 PHE A 249 47.196 11.104 12.961 1.00 51.42 C ANISOU 3041 CD2 PHE A 249 6300 6639 6598 -759 512 -394 C ATOM 3042 CE1 PHE A 249 48.386 8.815 11.941 1.00 52.39 C ANISOU 3042 CE1 PHE A 249 6477 6740 6686 -710 463 -323 C ATOM 3043 CE2 PHE A 249 47.089 10.809 11.613 1.00 52.25 C ANISOU 3043 CE2 PHE A 249 6326 6775 6750 -707 461 -415 C ATOM 3044 CZ PHE A 249 47.687 9.657 11.098 1.00 52.40 C ANISOU 3044 CZ PHE A 249 6379 6782 6747 -684 439 -380 C ATOM 3045 N ALA A 250 49.498 11.465 18.040 1.00 52.35 N ANISOU 3045 N ALA A 250 6997 6561 6330 -833 476 -233 N ATOM 3046 CA ALA A 250 49.608 12.196 19.292 1.00 53.10 C ANISOU 3046 CA ALA A 250 7245 6601 6327 -849 464 -233 C ATOM 3047 C ALA A 250 50.625 13.317 19.104 1.00 52.93 C ANISOU 3047 C ALA A 250 7149 6629 6331 -816 310 -210 C ATOM 3048 O ALA A 250 50.356 14.462 19.437 1.00 53.00 O ANISOU 3048 O ALA A 250 7162 6639 6336 -835 319 -238 O ATOM 3049 CB ALA A 250 50.013 11.275 20.434 1.00 53.84 C ANISOU 3049 CB ALA A 250 7575 6599 6283 -840 455 -199 C ATOM 3050 N CYS A 251 51.777 13.002 18.528 1.00 52.96 N ANISOU 3050 N CYS A 251 7074 6666 6380 -770 185 -165 N ATOM 3051 CA CYS A 251 52.758 14.041 18.214 1.00 53.28 C ANISOU 3051 CA CYS A 251 7010 6743 6489 -746 63 -150 C ATOM 3052 C CYS A 251 52.143 15.204 17.436 1.00 52.61 C ANISOU 3052 C CYS A 251 6795 6711 6480 -759 128 -183 C ATOM 3053 O CYS A 251 52.240 16.343 17.864 1.00 53.05 O ANISOU 3053 O CYS A 251 6863 6758 6533 -775 98 -200 O ATOM 3054 CB CYS A 251 53.948 13.482 17.428 1.00 53.10 C ANISOU 3054 CB CYS A 251 6878 6745 6553 -694 -29 -101 C ATOM 3055 SG CYS A 251 55.144 12.559 18.433 1.00 56.07 S ANISOU 3055 SG CYS A 251 7380 7052 6869 -653 -185 -61 S ATOM 3056 N TRP A 252 51.504 14.928 16.302 1.00 51.99 N ANISOU 3056 N TRP A 252 6607 6679 6465 -745 207 -195 N ATOM 3057 CA TRP A 252 51.080 16.008 15.406 1.00 51.09 C ANISOU 3057 CA TRP A 252 6379 6611 6421 -730 241 -219 C ATOM 3058 C TRP A 252 49.764 16.652 15.783 1.00 51.38 C ANISOU 3058 C TRP A 252 6436 6641 6443 -764 334 -280 C ATOM 3059 O TRP A 252 49.500 17.768 15.353 1.00 51.25 O ANISOU 3059 O TRP A 252 6357 6648 6466 -749 345 -299 O ATOM 3060 CB TRP A 252 50.992 15.533 13.959 1.00 50.41 C ANISOU 3060 CB TRP A 252 6187 6565 6398 -681 261 -212 C ATOM 3061 CG TRP A 252 52.305 15.453 13.295 1.00 49.45 C ANISOU 3061 CG TRP A 252 6012 6449 6328 -636 199 -154 C ATOM 3062 CD1 TRP A 252 53.001 14.324 13.006 1.00 49.86 C ANISOU 3062 CD1 TRP A 252 6063 6489 6390 -609 174 -114 C ATOM 3063 CD2 TRP A 252 53.098 16.547 12.839 1.00 48.94 C ANISOU 3063 CD2 TRP A 252 5880 6384 6329 -611 176 -131 C ATOM 3064 NE1 TRP A 252 54.187 14.641 12.396 1.00 50.49 N ANISOU 3064 NE1 TRP A 252 6069 6563 6549 -568 141 -68 N ATOM 3065 CE2 TRP A 252 54.273 16.004 12.283 1.00 49.91 C ANISOU 3065 CE2 TRP A 252 5953 6492 6515 -572 148 -79 C ATOM 3066 CE3 TRP A 252 52.934 17.938 12.849 1.00 49.17 C ANISOU 3066 CE3 TRP A 252 5887 6414 6378 -618 191 -151 C ATOM 3067 CZ2 TRP A 252 55.284 16.804 11.739 1.00 49.55 C ANISOU 3067 CZ2 TRP A 252 5829 6426 6569 -547 148 -48 C ATOM 3068 CZ3 TRP A 252 53.944 18.737 12.309 1.00 48.81 C ANISOU 3068 CZ3 TRP A 252 5776 6350 6418 -594 184 -119 C ATOM 3069 CH2 TRP A 252 55.100 18.164 11.760 1.00 49.37 C ANISOU 3069 CH2 TRP A 252 5790 6399 6566 -562 169 -70 C ATOM 3070 N LEU A 253 48.942 15.979 16.583 1.00 51.96 N ANISOU 3070 N LEU A 253 6601 6671 6467 -806 415 -309 N ATOM 3071 CA LEU A 253 47.553 16.423 16.745 1.00 52.28 C ANISOU 3071 CA LEU A 253 6623 6700 6540 -834 534 -375 C ATOM 3072 C LEU A 253 47.442 17.853 17.251 1.00 52.13 C ANISOU 3072 C LEU A 253 6629 6672 6505 -842 541 -391 C ATOM 3073 O LEU A 253 46.654 18.623 16.716 1.00 52.10 O ANISOU 3073 O LEU A 253 6531 6693 6569 -826 585 -433 O ATOM 3074 CB LEU A 253 46.740 15.477 17.642 1.00 53.29 C ANISOU 3074 CB LEU A 253 6857 6756 6633 -887 658 -404 C ATOM 3075 CG LEU A 253 45.240 15.535 17.358 1.00 54.04 C ANISOU 3075 CG LEU A 253 6853 6841 6835 -911 789 -484 C ATOM 3076 CD1 LEU A 253 44.933 14.942 15.977 1.00 53.74 C ANISOU 3076 CD1 LEU A 253 6654 6860 6903 -877 746 -512 C ATOM 3077 CD2 LEU A 253 44.467 14.809 18.458 1.00 56.05 C ANISOU 3077 CD2 LEU A 253 7234 6995 7066 -974 956 -513 C ATOM 3078 N PRO A 254 48.234 18.217 18.274 1.00 52.54 N ANISOU 3078 N PRO A 254 6814 6680 6466 -860 485 -362 N ATOM 3079 CA PRO A 254 48.188 19.588 18.802 1.00 52.74 C ANISOU 3079 CA PRO A 254 6882 6687 6470 -871 486 -380 C ATOM 3080 C PRO A 254 48.465 20.661 17.750 1.00 51.95 C ANISOU 3080 C PRO A 254 6637 6645 6454 -833 438 -377 C ATOM 3081 O PRO A 254 47.750 21.646 17.691 1.00 52.27 O ANISOU 3081 O PRO A 254 6653 6685 6520 -830 501 -412 O ATOM 3082 CB PRO A 254 49.275 19.586 19.875 1.00 53.21 C ANISOU 3082 CB PRO A 254 7098 6691 6425 -884 375 -350 C ATOM 3083 CG PRO A 254 49.371 18.178 20.293 1.00 53.55 C ANISOU 3083 CG PRO A 254 7239 6699 6405 -887 381 -328 C ATOM 3084 CD PRO A 254 49.159 17.377 19.053 1.00 52.92 C ANISOU 3084 CD PRO A 254 6997 6685 6424 -865 407 -320 C ATOM 3085 N TYR A 255 49.485 20.465 16.928 1.00 51.31 N ANISOU 3085 N TYR A 255 6474 6601 6419 -800 345 -334 N ATOM 3086 CA TYR A 255 49.758 21.370 15.811 1.00 51.03 C ANISOU 3086 CA TYR A 255 6324 6602 6461 -756 331 -324 C ATOM 3087 C TYR A 255 48.517 21.573 14.939 1.00 50.87 C ANISOU 3087 C TYR A 255 6229 6616 6483 -716 410 -365 C ATOM 3088 O TYR A 255 48.156 22.701 14.590 1.00 50.85 O ANISOU 3088 O TYR A 255 6197 6617 6506 -689 435 -384 O ATOM 3089 CB TYR A 255 50.899 20.794 14.960 1.00 50.65 C ANISOU 3089 CB TYR A 255 6206 6574 6465 -720 263 -272 C ATOM 3090 CG TYR A 255 51.288 21.580 13.726 1.00 49.65 C ANISOU 3090 CG TYR A 255 5990 6463 6411 -667 276 -252 C ATOM 3091 CD1 TYR A 255 52.173 22.650 13.809 1.00 50.59 C ANISOU 3091 CD1 TYR A 255 6092 6551 6577 -676 251 -236 C ATOM 3092 CD2 TYR A 255 50.827 21.215 12.472 1.00 48.98 C ANISOU 3092 CD2 TYR A 255 5855 6409 6346 -603 313 -250 C ATOM 3093 CE1 TYR A 255 52.578 23.359 12.665 1.00 50.63 C ANISOU 3093 CE1 TYR A 255 6039 6549 6650 -626 295 -211 C ATOM 3094 CE2 TYR A 255 51.211 21.919 11.320 1.00 49.80 C ANISOU 3094 CE2 TYR A 255 5923 6506 6492 -540 339 -225 C ATOM 3095 CZ TYR A 255 52.092 22.995 11.421 1.00 50.26 C ANISOU 3095 CZ TYR A 255 5971 6526 6598 -552 345 -202 C ATOM 3096 OH TYR A 255 52.487 23.705 10.294 1.00 49.38 O ANISOU 3096 OH TYR A 255 5846 6387 6529 -490 403 -174 O ATOM 3097 N TYR A 256 47.862 20.474 14.597 1.00 51.00 N ANISOU 3097 N TYR A 256 6215 6648 6514 -710 438 -385 N ATOM 3098 CA TYR A 256 46.784 20.519 13.622 1.00 51.09 C ANISOU 3098 CA TYR A 256 6136 6688 6586 -661 469 -433 C ATOM 3099 C TYR A 256 45.522 21.131 14.201 1.00 51.70 C ANISOU 3099 C TYR A 256 6206 6744 6693 -681 553 -499 C ATOM 3100 O TYR A 256 44.837 21.888 13.519 1.00 51.97 O ANISOU 3100 O TYR A 256 6172 6795 6780 -625 555 -536 O ATOM 3101 CB TYR A 256 46.518 19.139 13.043 1.00 51.03 C ANISOU 3101 CB TYR A 256 6090 6694 6602 -651 460 -444 C ATOM 3102 CG TYR A 256 47.482 18.766 11.939 1.00 50.22 C ANISOU 3102 CG TYR A 256 5967 6616 6495 -593 391 -392 C ATOM 3103 CD1 TYR A 256 47.387 19.355 10.683 1.00 50.20 C ANISOU 3103 CD1 TYR A 256 5925 6632 6515 -508 364 -395 C ATOM 3104 CD2 TYR A 256 48.472 17.821 12.146 1.00 49.59 C ANISOU 3104 CD2 TYR A 256 5925 6528 6388 -613 362 -338 C ATOM 3105 CE1 TYR A 256 48.254 19.010 9.658 1.00 50.84 C ANISOU 3105 CE1 TYR A 256 6015 6715 6585 -450 331 -345 C ATOM 3106 CE2 TYR A 256 49.342 17.458 11.130 1.00 50.56 C ANISOU 3106 CE2 TYR A 256 6028 6660 6521 -557 325 -290 C ATOM 3107 CZ TYR A 256 49.234 18.053 9.884 1.00 51.43 C ANISOU 3107 CZ TYR A 256 6109 6781 6648 -478 321 -292 C ATOM 3108 OH TYR A 256 50.112 17.695 8.873 1.00 52.71 O ANISOU 3108 OH TYR A 256 6280 6933 6813 -418 313 -241 O ATOM 3109 N ILE A 257 45.223 20.838 15.458 1.00 52.25 N ANISOU 3109 N ILE A 257 6359 6766 6727 -750 627 -514 N ATOM 3110 CA ILE A 257 44.220 21.632 16.143 1.00 53.20 C ANISOU 3110 CA ILE A 257 6494 6847 6871 -771 729 -566 C ATOM 3111 C ILE A 257 44.654 23.108 16.050 1.00 53.14 C ANISOU 3111 C ILE A 257 6503 6847 6840 -740 692 -548 C ATOM 3112 O ILE A 257 43.841 23.999 15.789 1.00 53.75 O ANISOU 3112 O ILE A 257 6526 6924 6972 -704 735 -589 O ATOM 3113 CB ILE A 257 44.033 21.225 17.626 1.00 53.98 C ANISOU 3113 CB ILE A 257 6740 6867 6899 -846 833 -571 C ATOM 3114 CG1 ILE A 257 43.471 19.809 17.727 1.00 54.33 C ANISOU 3114 CG1 ILE A 257 6774 6886 6982 -880 905 -595 C ATOM 3115 CG2 ILE A 257 43.082 22.207 18.342 1.00 54.40 C ANISOU 3115 CG2 ILE A 257 6827 6868 6975 -861 959 -620 C ATOM 3116 CD1 ILE A 257 43.232 19.347 19.157 1.00 55.73 C ANISOU 3116 CD1 ILE A 257 7131 6962 7079 -945 1038 -597 C ATOM 3117 N GLY A 258 45.944 23.354 16.248 1.00 52.76 N ANISOU 3117 N GLY A 258 6522 6797 6724 -751 612 -490 N ATOM 3118 CA GLY A 258 46.487 24.707 16.211 1.00 52.56 C ANISOU 3118 CA GLY A 258 6517 6764 6688 -736 583 -473 C ATOM 3119 C GLY A 258 46.148 25.394 14.913 1.00 52.04 C ANISOU 3119 C GLY A 258 6349 6734 6687 -655 577 -481 C ATOM 3120 O GLY A 258 45.446 26.405 14.904 1.00 52.68 O ANISOU 3120 O GLY A 258 6425 6802 6789 -628 627 -514 O ATOM 3121 N ILE A 259 46.607 24.821 13.807 1.00 51.09 N ANISOU 3121 N ILE A 259 6168 6650 6591 -606 520 -451 N ATOM 3122 CA ILE A 259 46.452 25.480 12.511 1.00 50.48 C ANISOU 3122 CA ILE A 259 6043 6589 6546 -512 506 -449 C ATOM 3123 C ILE A 259 44.990 25.522 12.016 1.00 50.50 C ANISOU 3123 C ILE A 259 5982 6608 6598 -451 523 -518 C ATOM 3124 O ILE A 259 44.632 26.402 11.244 1.00 50.61 O ANISOU 3124 O ILE A 259 5986 6619 6625 -366 513 -531 O ATOM 3125 CB ILE A 259 47.397 24.886 11.443 1.00 49.83 C ANISOU 3125 CB ILE A 259 5945 6522 6464 -468 457 -396 C ATOM 3126 CG1 ILE A 259 47.093 23.418 11.184 1.00 49.65 C ANISOU 3126 CG1 ILE A 259 5887 6527 6447 -470 428 -409 C ATOM 3127 CG2 ILE A 259 48.806 24.999 11.900 1.00 49.03 C ANISOU 3127 CG2 ILE A 259 5873 6395 6360 -521 440 -340 C ATOM 3128 CD1 ILE A 259 47.233 23.061 9.748 1.00 50.08 C ANISOU 3128 CD1 ILE A 259 5929 6593 6503 -378 392 -393 C ATOM 3129 N SER A 260 44.163 24.574 12.451 1.00 50.53 N ANISOU 3129 N SER A 260 5942 6618 6640 -489 546 -568 N ATOM 3130 CA SER A 260 42.708 24.678 12.260 1.00 51.24 C ANISOU 3130 CA SER A 260 5943 6705 6819 -450 571 -652 C ATOM 3131 C SER A 260 42.191 26.000 12.814 1.00 51.56 C ANISOU 3131 C SER A 260 6001 6715 6874 -442 638 -676 C ATOM 3132 O SER A 260 41.703 26.850 12.081 1.00 51.70 O ANISOU 3132 O SER A 260 5984 6734 6923 -350 608 -700 O ATOM 3133 CB SER A 260 41.961 23.540 12.966 1.00 51.43 C ANISOU 3133 CB SER A 260 5923 6713 6905 -524 634 -703 C ATOM 3134 OG SER A 260 42.225 22.310 12.347 1.00 51.08 O ANISOU 3134 OG SER A 260 5850 6693 6865 -522 573 -696 O ATOM 3135 N ILE A 261 42.321 26.175 14.117 1.00 51.87 N ANISOU 3135 N ILE A 261 6117 6715 6876 -530 726 -667 N ATOM 3136 CA ILE A 261 41.842 27.380 14.753 1.00 52.95 C ANISOU 3136 CA ILE A 261 6290 6810 7016 -529 805 -690 C ATOM 3137 C ILE A 261 42.395 28.620 14.033 1.00 53.39 C ANISOU 3137 C ILE A 261 6375 6872 7036 -457 753 -654 C ATOM 3138 O ILE A 261 41.669 29.594 13.805 1.00 53.86 O ANISOU 3138 O ILE A 261 6411 6915 7137 -393 781 -688 O ATOM 3139 CB ILE A 261 42.172 27.364 16.259 1.00 53.14 C ANISOU 3139 CB ILE A 261 6448 6779 6964 -632 892 -675 C ATOM 3140 CG1 ILE A 261 41.226 26.386 16.974 1.00 53.69 C ANISOU 3140 CG1 ILE A 261 6499 6811 7088 -685 1003 -725 C ATOM 3141 CG2 ILE A 261 42.034 28.744 16.855 1.00 53.39 C ANISOU 3141 CG2 ILE A 261 6556 6762 6965 -630 956 -682 C ATOM 3142 CD1 ILE A 261 41.773 25.806 18.255 1.00 53.83 C ANISOU 3142 CD1 ILE A 261 6683 6773 6994 -774 1058 -694 C ATOM 3143 N ASP A 262 43.666 28.556 13.636 1.00 53.51 N ANISOU 3143 N ASP A 262 6439 6902 6989 -463 686 -588 N ATOM 3144 CA ASP A 262 44.314 29.637 12.874 1.00 53.84 C ANISOU 3144 CA ASP A 262 6516 6931 7006 -401 661 -548 C ATOM 3145 C ASP A 262 43.589 29.925 11.555 1.00 53.85 C ANISOU 3145 C ASP A 262 6469 6948 7042 -268 623 -571 C ATOM 3146 O ASP A 262 43.395 31.073 11.186 1.00 54.12 O ANISOU 3146 O ASP A 262 6539 6953 7070 -198 642 -572 O ATOM 3147 CB ASP A 262 45.775 29.254 12.613 1.00 53.77 C ANISOU 3147 CB ASP A 262 6539 6925 6963 -434 613 -480 C ATOM 3148 CG ASP A 262 46.600 30.381 11.982 1.00 55.44 C ANISOU 3148 CG ASP A 262 6795 7098 7168 -394 626 -436 C ATOM 3149 OD1 ASP A 262 47.350 30.066 11.019 1.00 58.02 O ANISOU 3149 OD1 ASP A 262 7117 7426 7499 -352 604 -391 O ATOM 3150 OD2 ASP A 262 46.521 31.548 12.450 1.00 55.75 O ANISOU 3150 OD2 ASP A 262 6885 7095 7200 -405 674 -446 O ATOM 3151 N SER A 263 43.182 28.879 10.853 1.00 53.80 N ANISOU 3151 N SER A 263 6395 6979 7067 -227 560 -595 N ATOM 3152 CA SER A 263 42.460 29.046 9.603 1.00 54.41 C ANISOU 3152 CA SER A 263 6441 7062 7168 -90 488 -630 C ATOM 3153 C SER A 263 40.998 29.444 9.827 1.00 55.63 C ANISOU 3153 C SER A 263 6508 7209 7417 -45 494 -719 C ATOM 3154 O SER A 263 40.392 30.087 8.964 1.00 56.17 O ANISOU 3154 O SER A 263 6574 7265 7502 84 433 -749 O ATOM 3155 CB SER A 263 42.543 27.774 8.771 1.00 54.14 C ANISOU 3155 CB SER A 263 6374 7060 7134 -61 403 -634 C ATOM 3156 OG SER A 263 42.121 26.663 9.527 1.00 53.70 O ANISOU 3156 OG SER A 263 6237 7027 7140 -156 419 -675 O ATOM 3157 N PHE A 264 40.428 29.064 10.971 1.00 56.11 N ANISOU 3157 N PHE A 264 6507 7266 7546 -144 574 -761 N ATOM 3158 CA PHE A 264 39.093 29.553 11.356 1.00 57.35 C ANISOU 3158 CA PHE A 264 6573 7397 7820 -115 623 -844 C ATOM 3159 C PHE A 264 39.138 31.054 11.621 1.00 57.46 C ANISOU 3159 C PHE A 264 6665 7372 7793 -77 682 -824 C ATOM 3160 O PHE A 264 38.137 31.747 11.434 1.00 58.14 O ANISOU 3160 O PHE A 264 6690 7436 7964 8 683 -882 O ATOM 3161 CB PHE A 264 38.530 28.815 12.585 1.00 57.81 C ANISOU 3161 CB PHE A 264 6574 7434 7957 -235 741 -888 C ATOM 3162 CG PHE A 264 37.715 27.591 12.240 1.00 59.50 C ANISOU 3162 CG PHE A 264 6643 7661 8300 -237 702 -963 C ATOM 3163 CD1 PHE A 264 36.372 27.512 12.585 1.00 61.64 C ANISOU 3163 CD1 PHE A 264 6769 7895 8755 -237 771 -1063 C ATOM 3164 CD2 PHE A 264 38.289 26.527 11.552 1.00 59.97 C ANISOU 3164 CD2 PHE A 264 6705 7761 8318 -241 603 -939 C ATOM 3165 CE1 PHE A 264 35.617 26.393 12.260 1.00 62.96 C ANISOU 3165 CE1 PHE A 264 6785 8062 9072 -249 735 -1144 C ATOM 3166 CE2 PHE A 264 37.547 25.402 11.233 1.00 61.08 C ANISOU 3166 CE2 PHE A 264 6719 7906 8583 -249 564 -1015 C ATOM 3167 CZ PHE A 264 36.204 25.335 11.585 1.00 62.62 C ANISOU 3167 CZ PHE A 264 6758 8061 8973 -257 626 -1121 C ATOM 3168 N ILE A 265 40.298 31.544 12.062 1.00 56.74 N ANISOU 3168 N ILE A 265 6703 7266 7588 -140 725 -747 N ATOM 3169 CA ILE A 265 40.490 32.968 12.277 1.00 56.99 C ANISOU 3169 CA ILE A 265 6825 7252 7575 -114 781 -723 C ATOM 3170 C ILE A 265 40.612 33.671 10.942 1.00 57.49 C ANISOU 3170 C ILE A 265 6926 7309 7607 27 706 -701 C ATOM 3171 O ILE A 265 40.009 34.733 10.743 1.00 58.49 O ANISOU 3171 O ILE A 265 7072 7400 7750 117 725 -724 O ATOM 3172 CB ILE A 265 41.733 33.257 13.111 1.00 56.36 C ANISOU 3172 CB ILE A 265 6864 7148 7403 -227 830 -661 C ATOM 3173 CG1 ILE A 265 41.520 32.747 14.535 1.00 56.54 C ANISOU 3173 CG1 ILE A 265 6904 7152 7427 -347 909 -686 C ATOM 3174 CG2 ILE A 265 42.038 34.755 13.122 1.00 56.25 C ANISOU 3174 CG2 ILE A 265 6945 7078 7348 -195 877 -638 C ATOM 3175 CD1 ILE A 265 42.693 32.974 15.460 1.00 56.04 C ANISOU 3175 CD1 ILE A 265 6966 7054 7269 -452 921 -640 C ATOM 3176 N LEU A 266 41.369 33.070 10.025 1.00 57.11 N ANISOU 3176 N LEU A 266 6905 7285 7507 57 631 -657 N ATOM 3177 CA LEU A 266 41.590 33.653 8.697 1.00 57.56 C ANISOU 3177 CA LEU A 266 7046 7316 7507 199 576 -626 C ATOM 3178 C LEU A 266 40.274 33.856 7.954 1.00 58.99 C ANISOU 3178 C LEU A 266 7173 7496 7742 353 485 -700 C ATOM 3179 O LEU A 266 40.021 34.922 7.390 1.00 59.69 O ANISOU 3179 O LEU A 266 7343 7537 7797 476 477 -696 O ATOM 3180 CB LEU A 266 42.528 32.767 7.874 1.00 56.85 C ANISOU 3180 CB LEU A 266 6995 7243 7362 204 525 -573 C ATOM 3181 CG LEU A 266 43.086 33.365 6.583 1.00 56.35 C ANISOU 3181 CG LEU A 266 7073 7126 7212 333 517 -519 C ATOM 3182 CD1 LEU A 266 43.762 34.702 6.838 1.00 55.36 C ANISOU 3182 CD1 LEU A 266 7050 6931 7052 315 633 -468 C ATOM 3183 CD2 LEU A 266 44.058 32.382 5.949 1.00 54.88 C ANISOU 3183 CD2 LEU A 266 6919 6947 6983 315 501 -466 C ATOM 3184 N LEU A 267 39.430 32.830 7.994 1.00 59.82 N ANISOU 3184 N LEU A 267 7140 7643 7943 345 413 -773 N ATOM 3185 CA LEU A 267 38.094 32.886 7.409 1.00 61.43 C ANISOU 3185 CA LEU A 267 7246 7844 8247 479 302 -868 C ATOM 3186 C LEU A 267 37.160 33.884 8.112 1.00 63.30 C ANISOU 3186 C LEU A 267 7421 8048 8580 500 374 -919 C ATOM 3187 O LEU A 267 36.137 34.286 7.538 1.00 64.90 O ANISOU 3187 O LEU A 267 7561 8232 8864 642 278 -991 O ATOM 3188 CB LEU A 267 37.466 31.487 7.419 1.00 61.19 C ANISOU 3188 CB LEU A 267 7058 7856 8332 435 227 -943 C ATOM 3189 CG LEU A 267 38.086 30.518 6.412 1.00 59.71 C ANISOU 3189 CG LEU A 267 6930 7693 8063 468 116 -916 C ATOM 3190 CD1 LEU A 267 37.894 29.067 6.793 1.00 57.68 C ANISOU 3190 CD1 LEU A 267 6548 7475 7893 358 105 -959 C ATOM 3191 CD2 LEU A 267 37.511 30.793 5.044 1.00 60.36 C ANISOU 3191 CD2 LEU A 267 7058 7750 8123 669 -60 -962 C ATOM 3192 N GLU A 268 37.514 34.275 9.339 1.00 63.75 N ANISOU 3192 N GLU A 268 7504 8090 8627 367 533 -887 N ATOM 3193 CA GLU A 268 36.686 35.149 10.191 1.00 65.39 C ANISOU 3193 CA GLU A 268 7667 8256 8921 364 638 -932 C ATOM 3194 C GLU A 268 35.490 34.428 10.825 1.00 66.41 C ANISOU 3194 C GLU A 268 7603 8389 9239 320 675 -1031 C ATOM 3195 O GLU A 268 34.539 35.073 11.252 1.00 67.36 O ANISOU 3195 O GLU A 268 7648 8467 9476 358 743 -1089 O ATOM 3196 CB GLU A 268 36.230 36.422 9.447 1.00 66.54 C ANISOU 3196 CB GLU A 268 7869 8357 9054 537 590 -941 C ATOM 3197 CG GLU A 268 37.319 37.490 9.331 1.00 67.29 C ANISOU 3197 CG GLU A 268 8167 8411 8988 541 656 -845 C ATOM 3198 CD GLU A 268 37.427 38.079 7.935 1.00 69.49 C ANISOU 3198 CD GLU A 268 8563 8658 9182 726 548 -819 C ATOM 3199 OE1 GLU A 268 36.990 39.236 7.735 1.00 70.40 O ANISOU 3199 OE1 GLU A 268 8743 8716 9287 841 565 -825 O ATOM 3200 OE2 GLU A 268 37.948 37.369 7.039 1.00 70.90 O ANISOU 3200 OE2 GLU A 268 8787 8859 9292 761 454 -791 O ATOM 3201 N ILE A 269 35.556 33.099 10.906 1.00 66.59 N ANISOU 3201 N ILE A 269 7547 8449 9303 236 649 -1049 N ATOM 3202 CA ILE A 269 34.577 32.326 11.668 1.00 67.88 C ANISOU 3202 CA ILE A 269 7546 8598 9648 159 734 -1134 C ATOM 3203 C ILE A 269 34.666 32.713 13.138 1.00 68.78 C ANISOU 3203 C ILE A 269 7732 8661 9740 34 949 -1110 C ATOM 3204 O ILE A 269 33.651 32.745 13.829 1.00 70.09 O ANISOU 3204 O ILE A 269 7792 8775 10063 12 1075 -1181 O ATOM 3205 CB ILE A 269 34.795 30.795 11.553 1.00 67.34 C ANISOU 3205 CB ILE A 269 7416 8568 9602 76 688 -1145 C ATOM 3206 CG1 ILE A 269 34.544 30.305 10.121 1.00 67.40 C ANISOU 3206 CG1 ILE A 269 7350 8612 9645 201 470 -1190 C ATOM 3207 CG2 ILE A 269 33.883 30.038 12.532 1.00 67.45 C ANISOU 3207 CG2 ILE A 269 7289 8540 9796 -28 834 -1223 C ATOM 3208 CD1 ILE A 269 34.910 28.833 9.895 1.00 66.04 C ANISOU 3208 CD1 ILE A 269 7149 8476 9467 125 417 -1190 C ATOM 3209 N ILE A 270 35.882 32.992 13.615 1.00 68.76 N ANISOU 3209 N ILE A 270 7914 8661 9550 -42 993 -1015 N ATOM 3210 CA ILE A 270 36.095 33.439 14.998 1.00 69.50 C ANISOU 3210 CA ILE A 270 8126 8696 9583 -150 1168 -991 C ATOM 3211 C ILE A 270 36.914 34.733 15.058 1.00 69.66 C ANISOU 3211 C ILE A 270 8311 8695 9461 -130 1172 -925 C ATOM 3212 O ILE A 270 38.086 34.766 14.666 1.00 68.76 O ANISOU 3212 O ILE A 270 8293 8610 9222 -146 1091 -855 O ATOM 3213 CB ILE A 270 36.720 32.310 15.899 1.00 69.00 C ANISOU 3213 CB ILE A 270 8136 8632 9449 -297 1230 -959 C ATOM 3214 CG1 ILE A 270 38.218 32.118 15.653 1.00 67.32 C ANISOU 3214 CG1 ILE A 270 8048 8462 9067 -336 1125 -870 C ATOM 3215 CG2 ILE A 270 35.982 30.982 15.685 1.00 69.17 C ANISOU 3215 CG2 ILE A 270 7997 8670 9614 -315 1224 -1022 C ATOM 3216 CD1 ILE A 270 38.743 30.813 16.216 1.00 66.62 C ANISOU 3216 CD1 ILE A 270 7995 8384 8932 -443 1134 -848 C ATOM 3217 N LYS A 271 36.263 35.798 15.530 1.00 71.28 N ANISOU 3217 N LYS A 271 8537 8838 9706 -94 1277 -954 N ATOM 3218 CA LYS A 271 36.903 37.095 15.758 1.00 71.85 C ANISOU 3218 CA LYS A 271 8770 8868 9660 -86 1312 -905 C ATOM 3219 C LYS A 271 37.004 37.348 17.253 1.00 72.38 C ANISOU 3219 C LYS A 271 8970 8863 9668 -203 1473 -903 C ATOM 3220 O LYS A 271 35.987 37.377 17.939 1.00 73.39 O ANISOU 3220 O LYS A 271 9055 8936 9892 -208 1612 -959 O ATOM 3221 CB LYS A 271 36.093 38.214 15.116 1.00 72.94 C ANISOU 3221 CB LYS A 271 8863 8978 9872 61 1305 -937 C ATOM 3222 CG LYS A 271 35.768 37.971 13.654 1.00 74.43 C ANISOU 3222 CG LYS A 271 8940 9219 10118 204 1136 -955 C ATOM 3223 CD LYS A 271 35.341 39.274 12.969 1.00 76.99 C ANISOU 3223 CD LYS A 271 9299 9504 10450 364 1107 -961 C ATOM 3224 CE LYS A 271 34.432 38.998 11.766 1.00 79.17 C ANISOU 3224 CE LYS A 271 9432 9808 10842 532 945 -1024 C ATOM 3225 NZ LYS A 271 33.190 38.226 12.128 1.00 80.82 N ANISOU 3225 NZ LYS A 271 9416 10020 11269 523 961 -1128 N ATOM 3226 N GLN A 272 38.229 37.533 17.751 1.00 72.11 N ANISOU 3226 N GLN A 272 9099 8816 9481 -293 1453 -845 N ATOM 3227 CA GLN A 272 38.473 37.624 19.194 1.00 72.72 C ANISOU 3227 CA GLN A 272 9342 8819 9469 -404 1567 -845 C ATOM 3228 C GLN A 272 39.663 38.537 19.572 1.00 72.58 C ANISOU 3228 C GLN A 272 9503 8760 9311 -457 1527 -801 C ATOM 3229 O GLN A 272 40.244 38.403 20.660 1.00 72.59 O ANISOU 3229 O GLN A 272 9662 8711 9206 -556 1548 -794 O ATOM 3230 CB GLN A 272 38.669 36.203 19.759 1.00 72.59 C ANISOU 3230 CB GLN A 272 9331 8819 9429 -496 1567 -843 C ATOM 3231 CG GLN A 272 37.961 35.936 21.081 1.00 74.04 C ANISOU 3231 CG GLN A 272 9612 8911 9606 -559 1752 -880 C ATOM 3232 CD GLN A 272 36.462 36.060 20.955 1.00 75.51 C ANISOU 3232 CD GLN A 272 9647 9066 9975 -492 1895 -947 C ATOM 3233 OE1 GLN A 272 35.845 35.446 20.080 1.00 75.68 O ANISOU 3233 OE1 GLN A 272 9458 9147 10148 -436 1843 -980 O ATOM 3234 NE2 GLN A 272 35.865 36.872 21.819 1.00 77.00 N ANISOU 3234 NE2 GLN A 272 9938 9153 10164 -492 2070 -975 N ATOM 3235 N GLY A 273 40.009 39.474 18.689 1.00 72.47 N ANISOU 3235 N GLY A 273 9477 8756 9302 -386 1470 -777 N ATOM 3236 CA GLY A 273 41.071 40.434 18.970 1.00 72.71 C ANISOU 3236 CA GLY A 273 9654 8734 9239 -437 1447 -747 C ATOM 3237 C GLY A 273 42.453 39.818 18.892 1.00 72.27 C ANISOU 3237 C GLY A 273 9616 8710 9131 -519 1320 -705 C ATOM 3238 O GLY A 273 42.597 38.661 18.498 1.00 71.74 O ANISOU 3238 O GLY A 273 9455 8714 9089 -525 1249 -691 O ATOM 3239 N CYS A 274 43.467 40.587 19.288 1.00 72.83 N ANISOU 3239 N CYS A 274 9804 8722 9146 -585 1290 -693 N ATOM 3240 CA CYS A 274 44.867 40.187 19.090 1.00 72.79 C ANISOU 3240 CA CYS A 274 9788 8734 9133 -654 1165 -659 C ATOM 3241 C CYS A 274 45.464 39.271 20.168 1.00 72.82 C ANISOU 3241 C CYS A 274 9862 8732 9072 -758 1086 -669 C ATOM 3242 O CYS A 274 46.385 38.508 19.863 1.00 72.38 O ANISOU 3242 O CYS A 274 9743 8718 9038 -791 975 -642 O ATOM 3243 CB CYS A 274 45.757 41.418 18.922 1.00 73.23 C ANISOU 3243 CB CYS A 274 9907 8718 9198 -679 1159 -651 C ATOM 3244 SG CYS A 274 45.410 42.409 17.441 1.00 75.17 S ANISOU 3244 SG CYS A 274 10098 8957 9504 -547 1234 -620 S ATOM 3245 N GLU A 275 44.968 39.337 21.407 1.00 73.44 N ANISOU 3245 N GLU A 275 10086 8750 9067 -799 1145 -707 N ATOM 3246 CA GLU A 275 45.486 38.472 22.480 1.00 73.71 C ANISOU 3246 CA GLU A 275 10235 8760 9011 -879 1068 -717 C ATOM 3247 C GLU A 275 45.223 36.997 22.152 1.00 72.29 C ANISOU 3247 C GLU A 275 9947 8662 8856 -864 1048 -695 C ATOM 3248 O GLU A 275 46.057 36.129 22.415 1.00 72.13 O ANISOU 3248 O GLU A 275 9945 8658 8803 -910 929 -679 O ATOM 3249 CB GLU A 275 44.900 38.857 23.854 1.00 75.27 C ANISOU 3249 CB GLU A 275 10653 8853 9090 -910 1166 -759 C ATOM 3250 CG GLU A 275 43.394 38.542 24.061 1.00 77.50 C ANISOU 3250 CG GLU A 275 10929 9129 9389 -860 1359 -777 C ATOM 3251 CD GLU A 275 42.811 39.094 25.396 1.00 81.51 C ANISOU 3251 CD GLU A 275 11679 9507 9783 -884 1499 -817 C ATOM 3252 OE1 GLU A 275 43.247 40.176 25.861 1.00 83.79 O ANISOU 3252 OE1 GLU A 275 12111 9718 10005 -908 1477 -836 O ATOM 3253 OE2 GLU A 275 41.898 38.452 25.975 1.00 82.80 O ANISOU 3253 OE2 GLU A 275 11897 9635 9928 -878 1646 -832 O ATOM 3254 N PHE A 276 44.067 36.735 21.550 1.00 71.11 N ANISOU 3254 N PHE A 276 9681 8558 8778 -795 1156 -699 N ATOM 3255 CA PHE A 276 43.683 35.393 21.135 1.00 69.82 C ANISOU 3255 CA PHE A 276 9400 8466 8660 -778 1149 -689 C ATOM 3256 C PHE A 276 44.536 34.949 19.953 1.00 68.29 C ANISOU 3256 C PHE A 276 9066 8355 8526 -755 1018 -646 C ATOM 3257 O PHE A 276 45.225 33.925 20.007 1.00 67.77 O ANISOU 3257 O PHE A 276 8987 8320 8440 -793 928 -623 O ATOM 3258 CB PHE A 276 42.197 35.382 20.751 1.00 69.92 C ANISOU 3258 CB PHE A 276 9303 8492 8768 -707 1285 -723 C ATOM 3259 CG PHE A 276 41.635 34.012 20.553 1.00 69.44 C ANISOU 3259 CG PHE A 276 9138 8478 8766 -705 1302 -732 C ATOM 3260 CD1 PHE A 276 40.972 33.367 21.584 1.00 70.81 C ANISOU 3260 CD1 PHE A 276 9396 8591 8915 -751 1429 -761 C ATOM 3261 CD2 PHE A 276 41.768 33.362 19.340 1.00 68.20 C ANISOU 3261 CD2 PHE A 276 8816 8411 8685 -657 1205 -714 C ATOM 3262 CE1 PHE A 276 40.451 32.092 21.408 1.00 70.45 C ANISOU 3262 CE1 PHE A 276 9252 8575 8938 -758 1461 -774 C ATOM 3263 CE2 PHE A 276 41.257 32.093 19.155 1.00 68.11 C ANISOU 3263 CE2 PHE A 276 8709 8435 8732 -661 1216 -730 C ATOM 3264 CZ PHE A 276 40.597 31.456 20.188 1.00 69.31 C ANISOU 3264 CZ PHE A 276 8928 8528 8878 -716 1346 -761 C ATOM 3265 N GLU A 277 44.486 35.741 18.886 1.00 67.42 N ANISOU 3265 N GLU A 277 8867 8266 8480 -685 1020 -634 N ATOM 3266 CA GLU A 277 45.208 35.436 17.658 1.00 66.23 C ANISOU 3266 CA GLU A 277 8608 8174 8382 -646 933 -591 C ATOM 3267 C GLU A 277 46.657 35.157 18.026 1.00 65.12 C ANISOU 3267 C GLU A 277 8507 8018 8217 -728 828 -564 C ATOM 3268 O GLU A 277 47.214 34.138 17.632 1.00 64.72 O ANISOU 3268 O GLU A 277 8387 8014 8187 -736 754 -535 O ATOM 3269 CB GLU A 277 45.115 36.602 16.649 1.00 66.59 C ANISOU 3269 CB GLU A 277 8627 8204 8468 -560 966 -579 C ATOM 3270 CG GLU A 277 44.787 36.175 15.204 1.00 67.80 C ANISOU 3270 CG GLU A 277 8669 8418 8672 -452 938 -559 C ATOM 3271 CD GLU A 277 45.557 36.958 14.111 1.00 70.32 C ANISOU 3271 CD GLU A 277 9004 8709 9004 -394 934 -514 C ATOM 3272 OE1 GLU A 277 44.907 37.413 13.133 1.00 72.46 O ANISOU 3272 OE1 GLU A 277 9265 8980 9285 -272 955 -514 O ATOM 3273 OE2 GLU A 277 46.805 37.090 14.205 1.00 70.11 O ANISOU 3273 OE2 GLU A 277 9002 8650 8985 -464 912 -482 O ATOM 3274 N ASN A 278 47.249 36.046 18.822 1.00 64.52 N ANISOU 3274 N ASN A 278 8540 7868 8106 -789 814 -579 N ATOM 3275 CA ASN A 278 48.651 35.916 19.180 1.00 63.74 C ANISOU 3275 CA ASN A 278 8459 7740 8017 -864 691 -569 C ATOM 3276 C ASN A 278 48.918 34.699 20.034 1.00 62.99 C ANISOU 3276 C ASN A 278 8414 7658 7860 -913 603 -573 C ATOM 3277 O ASN A 278 49.983 34.111 19.926 1.00 63.10 O ANISOU 3277 O ASN A 278 8377 7684 7914 -942 487 -553 O ATOM 3278 CB ASN A 278 49.170 37.167 19.888 1.00 64.56 C ANISOU 3278 CB ASN A 278 8672 7749 8107 -920 678 -602 C ATOM 3279 CG ASN A 278 49.436 38.324 18.932 1.00 64.65 C ANISOU 3279 CG ASN A 278 8628 7731 8203 -887 741 -587 C ATOM 3280 OD1 ASN A 278 49.419 38.171 17.707 1.00 65.01 O ANISOU 3280 OD1 ASN A 278 8567 7821 8313 -819 780 -546 O ATOM 3281 ND2 ASN A 278 49.701 39.491 19.497 1.00 65.14 N ANISOU 3281 ND2 ASN A 278 8786 7704 8258 -931 755 -621 N ATOM 3282 N THR A 279 47.965 34.312 20.876 1.00 62.22 N ANISOU 3282 N THR A 279 8420 7546 7672 -916 670 -598 N ATOM 3283 CA THR A 279 48.140 33.119 21.708 1.00 61.54 C ANISOU 3283 CA THR A 279 8418 7455 7508 -952 609 -597 C ATOM 3284 C THR A 279 48.134 31.862 20.851 1.00 59.85 C ANISOU 3284 C THR A 279 8061 7327 7351 -921 588 -561 C ATOM 3285 O THR A 279 48.834 30.894 21.141 1.00 59.62 O ANISOU 3285 O THR A 279 8049 7305 7296 -945 487 -543 O ATOM 3286 CB THR A 279 47.050 33.009 22.785 1.00 62.17 C ANISOU 3286 CB THR A 279 8663 7476 7480 -961 733 -631 C ATOM 3287 OG1 THR A 279 47.202 34.077 23.722 1.00 62.90 O ANISOU 3287 OG1 THR A 279 8933 7474 7492 -994 734 -665 O ATOM 3288 CG2 THR A 279 47.158 31.695 23.522 1.00 62.19 C ANISOU 3288 CG2 THR A 279 8768 7465 7396 -985 696 -623 C ATOM 3289 N VAL A 280 47.353 31.890 19.782 1.00 58.41 N ANISOU 3289 N VAL A 280 7744 7202 7244 -859 674 -554 N ATOM 3290 CA VAL A 280 47.246 30.740 18.895 1.00 57.17 C ANISOU 3290 CA VAL A 280 7460 7120 7139 -822 656 -528 C ATOM 3291 C VAL A 280 48.542 30.560 18.110 1.00 56.22 C ANISOU 3291 C VAL A 280 7255 7028 7077 -819 547 -484 C ATOM 3292 O VAL A 280 49.026 29.447 17.938 1.00 55.52 O ANISOU 3292 O VAL A 280 7126 6971 6996 -824 483 -458 O ATOM 3293 CB VAL A 280 46.048 30.890 17.956 1.00 56.73 C ANISOU 3293 CB VAL A 280 7296 7106 7151 -746 748 -545 C ATOM 3294 CG1 VAL A 280 45.956 29.717 17.024 1.00 55.65 C ANISOU 3294 CG1 VAL A 280 7044 7037 7062 -709 712 -528 C ATOM 3295 CG2 VAL A 280 44.776 31.018 18.782 1.00 57.27 C ANISOU 3295 CG2 VAL A 280 7423 7135 7200 -754 873 -595 C ATOM 3296 N HIS A 281 49.108 31.671 17.662 1.00 55.95 N ANISOU 3296 N HIS A 281 7198 6967 7092 -811 542 -476 N ATOM 3297 CA HIS A 281 50.409 31.661 17.001 1.00 55.79 C ANISOU 3297 CA HIS A 281 7099 6943 7153 -817 470 -439 C ATOM 3298 C HIS A 281 51.487 31.065 17.900 1.00 55.90 C ANISOU 3298 C HIS A 281 7145 6930 7162 -886 339 -440 C ATOM 3299 O HIS A 281 52.337 30.306 17.452 1.00 55.08 O ANISOU 3299 O HIS A 281 6957 6846 7123 -883 274 -409 O ATOM 3300 CB HIS A 281 50.788 33.080 16.575 1.00 56.28 C ANISOU 3300 CB HIS A 281 7157 6952 7274 -810 516 -439 C ATOM 3301 CG HIS A 281 50.005 33.587 15.397 1.00 57.14 C ANISOU 3301 CG HIS A 281 7231 7082 7397 -716 621 -424 C ATOM 3302 ND1 HIS A 281 48.765 33.089 15.053 1.00 57.22 N ANISOU 3302 ND1 HIS A 281 7225 7147 7368 -650 661 -436 N ATOM 3303 CD2 HIS A 281 50.284 34.555 14.489 1.00 58.48 C ANISOU 3303 CD2 HIS A 281 7390 7212 7618 -669 687 -403 C ATOM 3304 CE1 HIS A 281 48.318 33.721 13.982 1.00 57.37 C ANISOU 3304 CE1 HIS A 281 7226 7164 7405 -557 720 -425 C ATOM 3305 NE2 HIS A 281 49.218 34.617 13.621 1.00 58.51 N ANISOU 3305 NE2 HIS A 281 7390 7249 7590 -564 747 -400 N ATOM 3306 N LYS A 282 51.422 31.385 19.183 1.00 56.87 N ANISOU 3306 N LYS A 282 7404 6999 7204 -938 297 -480 N ATOM 3307 CA LYS A 282 52.403 30.891 20.139 1.00 57.79 C ANISOU 3307 CA LYS A 282 7584 7074 7296 -989 140 -492 C ATOM 3308 C LYS A 282 52.302 29.376 20.322 1.00 57.41 C ANISOU 3308 C LYS A 282 7551 7067 7193 -973 101 -468 C ATOM 3309 O LYS A 282 53.322 28.685 20.313 1.00 57.41 O ANISOU 3309 O LYS A 282 7500 7069 7244 -979 -22 -451 O ATOM 3310 CB LYS A 282 52.274 31.632 21.479 1.00 58.92 C ANISOU 3310 CB LYS A 282 7917 7135 7334 -1035 101 -545 C ATOM 3311 CG LYS A 282 52.571 33.136 21.374 1.00 59.90 C ANISOU 3311 CG LYS A 282 8031 7202 7523 -1061 119 -574 C ATOM 3312 CD LYS A 282 53.255 33.694 22.624 1.00 62.77 C ANISOU 3312 CD LYS A 282 8543 7468 7837 -1121 -25 -632 C ATOM 3313 CE LYS A 282 53.578 35.205 22.503 1.00 63.95 C ANISOU 3313 CE LYS A 282 8678 7551 8067 -1157 -2 -668 C ATOM 3314 NZ LYS A 282 52.426 36.117 22.792 1.00 63.04 N ANISOU 3314 NZ LYS A 282 8693 7408 7850 -1143 151 -686 N ATOM 3315 N TRP A 283 51.074 28.875 20.468 1.00 57.03 N ANISOU 3315 N TRP A 283 7564 7044 7060 -952 216 -471 N ATOM 3316 CA TRP A 283 50.792 27.424 20.563 1.00 56.94 C ANISOU 3316 CA TRP A 283 7569 7064 7001 -939 218 -451 C ATOM 3317 C TRP A 283 51.337 26.652 19.349 1.00 55.57 C ANISOU 3317 C TRP A 283 7222 6958 6931 -904 187 -406 C ATOM 3318 O TRP A 283 51.944 25.584 19.488 1.00 55.61 O ANISOU 3318 O TRP A 283 7230 6970 6930 -903 104 -383 O ATOM 3319 CB TRP A 283 49.281 27.237 20.699 1.00 57.11 C ANISOU 3319 CB TRP A 283 7636 7091 6971 -927 383 -472 C ATOM 3320 CG TRP A 283 48.707 25.831 20.730 1.00 59.16 C ANISOU 3320 CG TRP A 283 7904 7370 7202 -920 436 -463 C ATOM 3321 CD1 TRP A 283 48.312 25.067 19.647 1.00 59.94 C ANISOU 3321 CD1 TRP A 283 7854 7539 7381 -885 475 -448 C ATOM 3322 CD2 TRP A 283 48.359 25.070 21.897 1.00 62.10 C ANISOU 3322 CD2 TRP A 283 8462 7678 7456 -947 476 -473 C ATOM 3323 NE1 TRP A 283 47.773 23.870 20.077 1.00 60.69 N ANISOU 3323 NE1 TRP A 283 8009 7618 7432 -899 533 -452 N ATOM 3324 CE2 TRP A 283 47.790 23.843 21.449 1.00 62.38 C ANISOU 3324 CE2 TRP A 283 8431 7746 7523 -936 547 -463 C ATOM 3325 CE3 TRP A 283 48.492 25.292 23.276 1.00 64.05 C ANISOU 3325 CE3 TRP A 283 8946 7826 7562 -974 460 -490 C ATOM 3326 CZ2 TRP A 283 47.360 22.845 22.334 1.00 63.43 C ANISOU 3326 CZ2 TRP A 283 8720 7815 7563 -957 623 -466 C ATOM 3327 CZ3 TRP A 283 48.057 24.296 24.160 1.00 65.33 C ANISOU 3327 CZ3 TRP A 283 9288 7921 7611 -984 534 -489 C ATOM 3328 CH2 TRP A 283 47.499 23.088 23.680 1.00 65.06 C ANISOU 3328 CH2 TRP A 283 9175 7920 7624 -978 624 -475 C ATOM 3329 N ILE A 284 51.156 27.225 18.164 1.00 54.21 N ANISOU 3329 N ILE A 284 6923 6825 6848 -866 255 -394 N ATOM 3330 CA ILE A 284 51.595 26.590 16.935 1.00 52.77 C ANISOU 3330 CA ILE A 284 6608 6690 6749 -822 250 -353 C ATOM 3331 C ILE A 284 53.113 26.447 16.928 1.00 53.36 C ANISOU 3331 C ILE A 284 6627 6739 6906 -841 137 -327 C ATOM 3332 O ILE A 284 53.623 25.402 16.528 1.00 53.45 O ANISOU 3332 O ILE A 284 6582 6773 6951 -821 98 -294 O ATOM 3333 CB ILE A 284 51.056 27.340 15.691 1.00 51.97 C ANISOU 3333 CB ILE A 284 6429 6614 6701 -761 346 -348 C ATOM 3334 CG1 ILE A 284 49.526 27.227 15.666 1.00 51.42 C ANISOU 3334 CG1 ILE A 284 6380 6573 6581 -732 431 -383 C ATOM 3335 CG2 ILE A 284 51.625 26.756 14.410 1.00 50.26 C ANISOU 3335 CG2 ILE A 284 6115 6426 6553 -708 347 -302 C ATOM 3336 CD1 ILE A 284 48.826 28.207 14.809 1.00 50.26 C ANISOU 3336 CD1 ILE A 284 6199 6433 6464 -668 501 -396 C ATOM 3337 N SER A 285 53.838 27.459 17.407 1.00 54.04 N ANISOU 3337 N SER A 285 6725 6768 7039 -881 80 -348 N ATOM 3338 CA SER A 285 55.306 27.391 17.415 1.00 54.77 C ANISOU 3338 CA SER A 285 6732 6822 7256 -903 -33 -338 C ATOM 3339 C SER A 285 55.809 26.313 18.350 1.00 55.35 C ANISOU 3339 C SER A 285 6863 6885 7281 -917 -181 -342 C ATOM 3340 O SER A 285 56.605 25.473 17.954 1.00 55.47 O ANISOU 3340 O SER A 285 6785 6910 7379 -896 -237 -311 O ATOM 3341 CB SER A 285 55.914 28.710 17.835 1.00 55.64 C ANISOU 3341 CB SER A 285 6841 6860 7439 -953 -75 -377 C ATOM 3342 OG SER A 285 55.396 29.760 17.062 1.00 56.14 O ANISOU 3342 OG SER A 285 6883 6920 7526 -935 67 -373 O ATOM 3343 N ILE A 286 55.339 26.341 19.591 1.00 55.97 N ANISOU 3343 N ILE A 286 7115 6933 7219 -943 -237 -378 N ATOM 3344 CA ILE A 286 55.624 25.267 20.532 1.00 56.80 C ANISOU 3344 CA ILE A 286 7333 7015 7231 -939 -364 -379 C ATOM 3345 C ILE A 286 55.301 23.912 19.921 1.00 55.88 C ANISOU 3345 C ILE A 286 7175 6958 7097 -897 -302 -331 C ATOM 3346 O ILE A 286 56.157 23.025 19.870 1.00 56.28 O ANISOU 3346 O ILE A 286 7178 7007 7198 -875 -405 -307 O ATOM 3347 CB ILE A 286 54.776 25.357 21.819 1.00 57.55 C ANISOU 3347 CB ILE A 286 7671 7063 7131 -956 -355 -414 C ATOM 3348 CG1 ILE A 286 55.055 26.651 22.593 1.00 59.41 C ANISOU 3348 CG1 ILE A 286 7996 7226 7351 -996 -430 -468 C ATOM 3349 CG2 ILE A 286 55.061 24.151 22.702 1.00 58.10 C ANISOU 3349 CG2 ILE A 286 7889 7097 7087 -936 -469 -405 C ATOM 3350 CD1 ILE A 286 56.536 26.866 22.943 1.00 61.63 C ANISOU 3350 CD1 ILE A 286 8222 7453 7742 -1012 -661 -498 C ATOM 3351 N THR A 287 54.062 23.764 19.458 1.00 54.71 N ANISOU 3351 N THR A 287 7039 6855 6891 -885 -139 -325 N ATOM 3352 CA THR A 287 53.550 22.456 19.078 1.00 53.93 C ANISOU 3352 CA THR A 287 6936 6798 6756 -857 -78 -296 C ATOM 3353 C THR A 287 54.153 21.954 17.772 1.00 53.37 C ANISOU 3353 C THR A 287 6694 6774 6809 -817 -72 -254 C ATOM 3354 O THR A 287 54.241 20.742 17.571 1.00 53.05 O ANISOU 3354 O THR A 287 6649 6751 6755 -794 -80 -226 O ATOM 3355 CB THR A 287 52.008 22.436 19.009 1.00 53.36 C ANISOU 3355 CB THR A 287 6911 6746 6615 -859 83 -319 C ATOM 3356 OG1 THR A 287 51.549 23.433 18.096 1.00 52.82 O ANISOU 3356 OG1 THR A 287 6736 6712 6621 -843 164 -329 O ATOM 3357 CG2 THR A 287 51.413 22.704 20.381 1.00 53.58 C ANISOU 3357 CG2 THR A 287 7137 6707 6512 -895 109 -355 C ATOM 3358 N GLU A 288 54.578 22.865 16.895 1.00 53.36 N ANISOU 3358 N GLU A 288 6572 6780 6922 -807 -43 -246 N ATOM 3359 CA GLU A 288 55.322 22.459 15.694 1.00 53.34 C ANISOU 3359 CA GLU A 288 6432 6796 7039 -765 -23 -203 C ATOM 3360 C GLU A 288 56.650 21.860 16.117 1.00 54.13 C ANISOU 3360 C GLU A 288 6489 6860 7218 -769 -158 -186 C ATOM 3361 O GLU A 288 57.032 20.793 15.656 1.00 53.80 O ANISOU 3361 O GLU A 288 6401 6832 7205 -734 -164 -150 O ATOM 3362 CB GLU A 288 55.590 23.629 14.732 1.00 53.43 C ANISOU 3362 CB GLU A 288 6353 6793 7155 -750 56 -196 C ATOM 3363 CG GLU A 288 56.453 23.211 13.488 1.00 54.28 C ANISOU 3363 CG GLU A 288 6345 6892 7386 -702 106 -146 C ATOM 3364 CD GLU A 288 56.795 24.350 12.503 1.00 54.53 C ANISOU 3364 CD GLU A 288 6317 6883 7517 -680 216 -132 C ATOM 3365 OE1 GLU A 288 56.534 24.188 11.283 1.00 52.86 O ANISOU 3365 OE1 GLU A 288 6103 6679 7299 -614 325 -100 O ATOM 3366 OE2 GLU A 288 57.344 25.389 12.944 1.00 55.65 O ANISOU 3366 OE2 GLU A 288 6431 6972 7741 -726 195 -156 O ATOM 3367 N ALA A 289 57.354 22.567 16.992 1.00 55.50 N ANISOU 3367 N ALA A 289 6675 6980 7431 -808 -275 -218 N ATOM 3368 CA ALA A 289 58.666 22.136 17.446 1.00 56.79 C ANISOU 3368 CA ALA A 289 6778 7097 7700 -807 -439 -219 C ATOM 3369 C ALA A 289 58.572 20.768 18.117 1.00 57.15 C ANISOU 3369 C ALA A 289 6936 7150 7628 -779 -524 -204 C ATOM 3370 O ALA A 289 59.404 19.884 17.855 1.00 57.44 O ANISOU 3370 O ALA A 289 6892 7180 7751 -742 -588 -174 O ATOM 3371 CB ALA A 289 59.271 23.168 18.389 1.00 57.77 C ANISOU 3371 CB ALA A 289 6921 7155 7871 -854 -577 -276 C ATOM 3372 N LEU A 290 57.547 20.586 18.953 1.00 57.20 N ANISOU 3372 N LEU A 290 7131 7159 7443 -793 -505 -222 N ATOM 3373 CA LEU A 290 57.385 19.330 19.690 1.00 57.93 C ANISOU 3373 CA LEU A 290 7371 7236 7403 -768 -563 -208 C ATOM 3374 C LEU A 290 57.028 18.186 18.766 1.00 57.50 C ANISOU 3374 C LEU A 290 7259 7231 7354 -734 -450 -162 C ATOM 3375 O LEU A 290 57.374 17.041 19.041 1.00 57.83 O ANISOU 3375 O LEU A 290 7354 7257 7359 -701 -512 -137 O ATOM 3376 CB LEU A 290 56.348 19.454 20.812 1.00 58.08 C ANISOU 3376 CB LEU A 290 7624 7220 7222 -794 -527 -239 C ATOM 3377 CG LEU A 290 56.819 20.262 22.035 1.00 59.44 C ANISOU 3377 CG LEU A 290 7932 7315 7334 -812 -687 -287 C ATOM 3378 CD1 LEU A 290 55.678 20.473 23.019 1.00 59.20 C ANISOU 3378 CD1 LEU A 290 8148 7240 7103 -835 -595 -313 C ATOM 3379 CD2 LEU A 290 58.015 19.595 22.726 1.00 59.63 C ANISOU 3379 CD2 LEU A 290 8006 7283 7367 -770 -923 -288 C ATOM 3380 N ALA A 291 56.352 18.503 17.664 1.00 57.23 N ANISOU 3380 N ALA A 291 7129 7252 7364 -736 -295 -154 N ATOM 3381 CA ALA A 291 55.972 17.503 16.668 1.00 56.93 C ANISOU 3381 CA ALA A 291 7038 7256 7335 -702 -195 -121 C ATOM 3382 C ALA A 291 57.188 16.781 16.085 1.00 58.00 C ANISOU 3382 C ALA A 291 7065 7383 7589 -657 -256 -77 C ATOM 3383 O ALA A 291 57.150 15.568 15.874 1.00 58.06 O ANISOU 3383 O ALA A 291 7098 7397 7564 -627 -240 -49 O ATOM 3384 CB ALA A 291 55.182 18.148 15.572 1.00 55.83 C ANISOU 3384 CB ALA A 291 6823 7162 7228 -696 -60 -129 C ATOM 3385 N PHE A 292 58.278 17.518 15.866 1.00 59.49 N ANISOU 3385 N PHE A 292 7130 7546 7928 -654 -316 -74 N ATOM 3386 CA PHE A 292 59.477 16.962 15.224 1.00 60.46 C ANISOU 3386 CA PHE A 292 7118 7647 8207 -611 -345 -35 C ATOM 3387 C PHE A 292 60.015 15.718 15.946 1.00 62.14 C ANISOU 3387 C PHE A 292 7388 7835 8387 -578 -474 -19 C ATOM 3388 O PHE A 292 60.825 14.987 15.382 1.00 62.37 O ANISOU 3388 O PHE A 292 7321 7849 8527 -531 -478 17 O ATOM 3389 CB PHE A 292 60.590 18.016 15.112 1.00 61.23 C ANISOU 3389 CB PHE A 292 7066 7696 8502 -627 -393 -50 C ATOM 3390 CG PHE A 292 60.234 19.246 14.289 1.00 60.13 C ANISOU 3390 CG PHE A 292 6872 7562 8411 -648 -250 -57 C ATOM 3391 CD1 PHE A 292 59.159 19.266 13.413 1.00 58.44 C ANISOU 3391 CD1 PHE A 292 6712 7395 8095 -627 -96 -42 C ATOM 3392 CD2 PHE A 292 61.032 20.384 14.373 1.00 61.23 C ANISOU 3392 CD2 PHE A 292 6907 7646 8711 -682 -278 -84 C ATOM 3393 CE1 PHE A 292 58.876 20.395 12.662 1.00 58.14 C ANISOU 3393 CE1 PHE A 292 6647 7350 8093 -628 20 -46 C ATOM 3394 CE2 PHE A 292 60.760 21.520 13.621 1.00 60.31 C ANISOU 3394 CE2 PHE A 292 6759 7518 8636 -695 -135 -86 C ATOM 3395 CZ PHE A 292 59.685 21.527 12.768 1.00 59.55 C ANISOU 3395 CZ PHE A 292 6739 7470 8417 -662 12 -63 C ATOM 3396 N PHE A 293 59.566 15.471 17.181 1.00 63.80 N ANISOU 3396 N PHE A 293 7772 8028 8440 -594 -568 -44 N ATOM 3397 CA PHE A 293 59.873 14.208 17.870 1.00 65.60 C ANISOU 3397 CA PHE A 293 8111 8223 8590 -551 -671 -24 C ATOM 3398 C PHE A 293 59.301 12.969 17.163 1.00 65.57 C ANISOU 3398 C PHE A 293 8136 8249 8526 -524 -538 16 C ATOM 3399 O PHE A 293 59.606 11.846 17.556 1.00 66.56 O ANISOU 3399 O PHE A 293 8343 8343 8601 -481 -600 41 O ATOM 3400 CB PHE A 293 59.395 14.221 19.336 1.00 66.41 C ANISOU 3400 CB PHE A 293 8449 8281 8502 -567 -767 -56 C ATOM 3401 CG PHE A 293 60.427 14.721 20.311 1.00 69.02 C ANISOU 3401 CG PHE A 293 8800 8548 8877 -550 -1002 -90 C ATOM 3402 CD1 PHE A 293 61.577 13.974 20.568 1.00 71.36 C ANISOU 3402 CD1 PHE A 293 9057 8800 9255 -483 -1181 -77 C ATOM 3403 CD2 PHE A 293 60.252 15.934 20.981 1.00 70.58 C ANISOU 3403 CD2 PHE A 293 9056 8722 9039 -597 -1058 -143 C ATOM 3404 CE1 PHE A 293 62.547 14.435 21.471 1.00 73.56 C ANISOU 3404 CE1 PHE A 293 9343 9011 9593 -460 -1436 -124 C ATOM 3405 CE2 PHE A 293 61.217 16.408 21.887 1.00 72.68 C ANISOU 3405 CE2 PHE A 293 9344 8918 9350 -582 -1302 -189 C ATOM 3406 CZ PHE A 293 62.365 15.656 22.133 1.00 74.10 C ANISOU 3406 CZ PHE A 293 9475 9055 9623 -513 -1502 -183 C ATOM 3407 N HIS A 294 58.480 13.148 16.132 1.00 65.25 N ANISOU 3407 N HIS A 294 8041 8260 8488 -543 -369 19 N ATOM 3408 CA HIS A 294 57.988 11.997 15.373 1.00 65.20 C ANISOU 3408 CA HIS A 294 8053 8274 8444 -518 -260 46 C ATOM 3409 C HIS A 294 59.112 11.230 14.647 1.00 65.93 C ANISOU 3409 C HIS A 294 8038 8349 8661 -454 -281 95 C ATOM 3410 O HIS A 294 58.978 10.031 14.404 1.00 65.95 O ANISOU 3410 O HIS A 294 8094 8345 8616 -425 -242 121 O ATOM 3411 CB HIS A 294 56.856 12.401 14.414 1.00 64.20 C ANISOU 3411 CB HIS A 294 7895 8197 8297 -541 -109 25 C ATOM 3412 CG HIS A 294 57.320 13.070 13.163 1.00 63.95 C ANISOU 3412 CG HIS A 294 7722 8182 8390 -512 -51 41 C ATOM 3413 ND1 HIS A 294 57.625 12.365 12.021 1.00 64.60 N ANISOU 3413 ND1 HIS A 294 7754 8264 8524 -460 18 76 N ATOM 3414 CD2 HIS A 294 57.505 14.377 12.864 1.00 64.23 C ANISOU 3414 CD2 HIS A 294 7682 8222 8500 -524 -34 29 C ATOM 3415 CE1 HIS A 294 57.990 13.210 11.073 1.00 65.12 C ANISOU 3415 CE1 HIS A 294 7731 8327 8684 -437 83 88 C ATOM 3416 NE2 HIS A 294 57.930 14.437 11.559 1.00 64.80 N ANISOU 3416 NE2 HIS A 294 7669 8289 8663 -476 54 60 N ATOM 3417 N CYS A 295 60.214 11.905 14.325 1.00 66.88 N ANISOU 3417 N CYS A 295 8008 8451 8952 -436 -329 105 N ATOM 3418 CA CYS A 295 61.378 11.227 13.745 1.00 68.11 C ANISOU 3418 CA CYS A 295 8048 8572 9257 -373 -342 148 C ATOM 3419 C CYS A 295 61.777 10.009 14.541 1.00 69.18 C ANISOU 3419 C CYS A 295 8271 8673 9339 -329 -460 167 C ATOM 3420 O CYS A 295 61.893 8.920 13.988 1.00 69.48 O ANISOU 3420 O CYS A 295 8320 8704 9376 -283 -399 206 O ATOM 3421 CB CYS A 295 62.575 12.155 13.708 1.00 68.99 C ANISOU 3421 CB CYS A 295 7984 8643 9584 -370 -408 140 C ATOM 3422 SG CYS A 295 62.198 13.653 12.866 1.00 69.56 S ANISOU 3422 SG CYS A 295 7979 8733 9715 -416 -265 121 S ATOM 3423 N CYS A 296 61.960 10.206 15.845 1.00 70.26 N ANISOU 3423 N CYS A 296 8495 8781 9417 -338 -630 139 N ATOM 3424 CA CYS A 296 62.570 9.205 16.721 1.00 71.67 C ANISOU 3424 CA CYS A 296 8767 8907 9557 -276 -788 154 C ATOM 3425 C CYS A 296 61.657 8.050 17.129 1.00 71.52 C ANISOU 3425 C CYS A 296 8972 8881 9321 -269 -728 173 C ATOM 3426 O CYS A 296 62.143 6.956 17.407 1.00 72.35 O ANISOU 3426 O CYS A 296 9142 8941 9403 -202 -795 205 O ATOM 3427 CB CYS A 296 63.092 9.888 17.979 1.00 73.01 C ANISOU 3427 CB CYS A 296 8983 9032 9724 -276 -1010 109 C ATOM 3428 SG CYS A 296 63.814 11.506 17.659 1.00 74.09 S ANISOU 3428 SG CYS A 296 8885 9171 10094 -323 -1054 64 S ATOM 3429 N LEU A 297 60.348 8.286 17.183 1.00 70.86 N ANISOU 3429 N LEU A 297 9001 8830 9093 -336 -598 150 N ATOM 3430 CA LEU A 297 59.384 7.226 17.517 1.00 70.85 C ANISOU 3430 CA LEU A 297 9196 8808 8916 -346 -503 158 C ATOM 3431 C LEU A 297 59.744 5.901 16.840 1.00 71.03 C ANISOU 3431 C LEU A 297 9200 8816 8972 -289 -455 205 C ATOM 3432 O LEU A 297 59.705 4.840 17.467 1.00 71.63 O ANISOU 3432 O LEU A 297 9444 8836 8937 -254 -476 226 O ATOM 3433 CB LEU A 297 57.963 7.622 17.096 1.00 69.59 C ANISOU 3433 CB LEU A 297 9053 8694 8691 -425 -324 122 C ATOM 3434 CG LEU A 297 57.293 8.808 17.792 1.00 69.65 C ANISOU 3434 CG LEU A 297 9115 8709 8638 -486 -323 74 C ATOM 3435 CD1 LEU A 297 55.928 9.097 17.149 1.00 68.39 C ANISOU 3435 CD1 LEU A 297 8926 8596 8463 -548 -144 38 C ATOM 3436 CD2 LEU A 297 57.152 8.559 19.286 1.00 70.18 C ANISOU 3436 CD2 LEU A 297 9425 8698 8541 -483 -394 66 C ATOM 3437 N ASN A 298 60.097 5.976 15.559 1.00 70.56 N ANISOU 3437 N ASN A 298 8958 8795 9055 -274 -379 223 N ATOM 3438 CA ASN A 298 60.389 4.787 14.773 1.00 70.76 C ANISOU 3438 CA ASN A 298 8966 8803 9113 -222 -310 265 C ATOM 3439 C ASN A 298 61.598 4.000 15.352 1.00 72.13 C ANISOU 3439 C ASN A 298 9157 8914 9335 -132 -456 305 C ATOM 3440 O ASN A 298 61.434 2.847 15.759 1.00 72.69 O ANISOU 3440 O ASN A 298 9383 8940 9296 -99 -452 328 O ATOM 3441 CB ASN A 298 60.508 5.164 13.273 1.00 70.02 C ANISOU 3441 CB ASN A 298 8706 8750 9148 -218 -188 273 C ATOM 3442 CG ASN A 298 60.874 3.978 12.372 1.00 70.10 C ANISOU 3442 CG ASN A 298 8707 8732 9194 -157 -107 317 C ATOM 3443 OD1 ASN A 298 60.586 2.816 12.687 1.00 69.97 O ANISOU 3443 OD1 ASN A 298 8822 8684 9078 -143 -95 330 O ATOM 3444 ND2 ASN A 298 61.493 4.280 11.228 1.00 68.85 N ANISOU 3444 ND2 ASN A 298 8410 8575 9175 -121 -32 339 N ATOM 3445 N PRO A 299 62.790 4.617 15.429 1.00 72.90 N ANISOU 3445 N PRO A 299 9096 8997 9603 -90 -588 308 N ATOM 3446 CA PRO A 299 63.916 3.945 16.084 1.00 74.63 C ANISOU 3446 CA PRO A 299 9320 9150 9884 3 -765 332 C ATOM 3447 C PRO A 299 63.666 3.501 17.529 1.00 75.89 C ANISOU 3447 C PRO A 299 9729 9258 9847 27 -911 322 C ATOM 3448 O PRO A 299 63.901 2.346 17.858 1.00 76.56 O ANISOU 3448 O PRO A 299 9940 9287 9861 100 -949 357 O ATOM 3449 CB PRO A 299 65.017 5.002 16.055 1.00 75.45 C ANISOU 3449 CB PRO A 299 9199 9248 10220 16 -890 308 C ATOM 3450 CG PRO A 299 64.700 5.856 14.905 1.00 74.23 C ANISOU 3450 CG PRO A 299 8898 9147 10160 -46 -709 302 C ATOM 3451 CD PRO A 299 63.232 5.780 14.645 1.00 72.55 C ANISOU 3451 CD PRO A 299 8838 8986 9742 -114 -551 294 C ATOM 3452 N ILE A 300 63.202 4.411 18.380 1.00 76.59 N ANISOU 3452 N ILE A 300 9909 9350 9838 -25 -982 277 N ATOM 3453 CA ILE A 300 62.936 4.088 19.788 1.00 78.20 C ANISOU 3453 CA ILE A 300 10394 9485 9831 1 -1105 267 C ATOM 3454 C ILE A 300 62.097 2.818 19.938 1.00 78.53 C ANISOU 3454 C ILE A 300 10667 9487 9680 7 -960 300 C ATOM 3455 O ILE A 300 62.463 1.915 20.689 1.00 79.89 O ANISOU 3455 O ILE A 300 11027 9577 9749 93 -1062 327 O ATOM 3456 CB ILE A 300 62.200 5.233 20.517 1.00 78.01 C ANISOU 3456 CB ILE A 300 10471 9472 9696 -77 -1115 214 C ATOM 3457 CG1 ILE A 300 63.126 6.438 20.688 1.00 78.73 C ANISOU 3457 CG1 ILE A 300 10385 9572 9955 -74 -1306 172 C ATOM 3458 CG2 ILE A 300 61.693 4.766 21.880 1.00 78.89 C ANISOU 3458 CG2 ILE A 300 10932 9495 9548 -51 -1168 211 C ATOM 3459 CD1 ILE A 300 62.502 7.584 21.456 1.00 78.86 C ANISOU 3459 CD1 ILE A 300 10513 9588 9862 -143 -1332 119 C ATOM 3460 N LEU A 301 60.981 2.754 19.212 1.00 77.73 N ANISOU 3460 N LEU A 301 10553 9436 9543 -79 -726 294 N ATOM 3461 CA LEU A 301 60.047 1.623 19.311 1.00 77.97 C ANISOU 3461 CA LEU A 301 10783 9422 9418 -98 -560 311 C ATOM 3462 C LEU A 301 60.698 0.263 19.088 1.00 78.86 C ANISOU 3462 C LEU A 301 10940 9482 9541 -7 -578 364 C ATOM 3463 O LEU A 301 60.156 -0.752 19.510 1.00 79.45 O ANISOU 3463 O LEU A 301 11234 9486 9468 -1 -487 382 O ATOM 3464 CB LEU A 301 58.852 1.795 18.365 1.00 76.57 C ANISOU 3464 CB LEU A 301 10521 9310 9262 -202 -335 281 C ATOM 3465 CG LEU A 301 57.628 2.471 18.988 1.00 76.51 C ANISOU 3465 CG LEU A 301 10626 9300 9143 -295 -236 230 C ATOM 3466 CD1 LEU A 301 56.657 2.929 17.907 1.00 75.32 C ANISOU 3466 CD1 LEU A 301 10314 9228 9075 -380 -75 189 C ATOM 3467 CD2 LEU A 301 56.939 1.520 19.966 1.00 77.49 C ANISOU 3467 CD2 LEU A 301 11042 9317 9083 -300 -144 236 C ATOM 3468 N TYR A 302 61.854 0.235 18.436 1.00 79.35 N ANISOU 3468 N TYR A 302 10797 9566 9784 63 -677 390 N ATOM 3469 CA TYR A 302 62.708 -0.946 18.490 1.00 80.72 C ANISOU 3469 CA TYR A 302 11020 9673 9976 176 -750 441 C ATOM 3470 C TYR A 302 63.384 -1.027 19.869 1.00 82.56 C ANISOU 3470 C TYR A 302 11428 9821 10117 272 -994 444 C ATOM 3471 O TYR A 302 64.564 -0.714 20.019 1.00 83.50 O ANISOU 3471 O TYR A 302 11408 9931 10388 354 -1206 442 O ATOM 3472 CB TYR A 302 63.727 -0.910 17.359 1.00 80.76 C ANISOU 3472 CB TYR A 302 10743 9714 10225 225 -759 464 C ATOM 3473 CG TYR A 302 63.098 -1.094 15.987 1.00 80.22 C ANISOU 3473 CG TYR A 302 10573 9701 10204 161 -525 469 C ATOM 3474 CD1 TYR A 302 62.675 -2.355 15.569 1.00 81.39 C ANISOU 3474 CD1 TYR A 302 10838 9813 10271 173 -388 497 C ATOM 3475 CD2 TYR A 302 62.933 -0.023 15.107 1.00 79.38 C ANISOU 3475 CD2 TYR A 302 10274 9671 10216 95 -448 441 C ATOM 3476 CE1 TYR A 302 62.099 -2.553 14.316 1.00 80.38 C ANISOU 3476 CE1 TYR A 302 10638 9724 10176 122 -200 490 C ATOM 3477 CE2 TYR A 302 62.360 -0.210 13.842 1.00 78.68 C ANISOU 3477 CE2 TYR A 302 10127 9619 10148 56 -257 441 C ATOM 3478 CZ TYR A 302 61.946 -1.484 13.455 1.00 79.33 C ANISOU 3478 CZ TYR A 302 10328 9664 10147 70 -144 462 C ATOM 3479 OH TYR A 302 61.378 -1.720 12.217 1.00 78.65 O ANISOU 3479 OH TYR A 302 10207 9603 10071 38 18 453 O ATOM 3480 N ALA A 303 62.592 -1.429 20.867 1.00 83.08 N ANISOU 3480 N ALA A 303 11808 9815 9941 261 -957 443 N ATOM 3481 CA ALA A 303 63.002 -1.501 22.275 1.00 84.78 C ANISOU 3481 CA ALA A 303 12280 9930 10000 353 -1172 442 C ATOM 3482 C ALA A 303 62.272 -2.678 22.906 1.00 85.44 C ANISOU 3482 C ALA A 303 12717 9904 9841 375 -1037 476 C ATOM 3483 O ALA A 303 61.367 -3.250 22.290 1.00 84.44 O ANISOU 3483 O ALA A 303 12602 9790 9689 293 -779 485 O ATOM 3484 CB ALA A 303 62.649 -0.212 23.010 1.00 84.51 C ANISOU 3484 CB ALA A 303 12296 9910 9901 292 -1249 386 C TER 3485 ALA A 303 ATOM 3486 N ARG I 1 59.475 30.324 8.423 1.00 63.70 N ATOM 3487 CA ARG I 1 58.018 30.456 8.673 1.00 63.86 C ATOM 3488 C ARG I 1 57.290 30.051 7.418 1.00 63.70 C ATOM 3489 O ARG I 1 57.517 30.636 6.365 1.00 63.93 O ATOM 3490 CB ARG I 1 57.654 31.892 9.049 1.00 63.93 C ATOM 3491 CG ARG I 1 57.462 32.117 10.558 1.00 65.11 C ATOM 3492 CD ARG I 1 56.987 33.539 10.884 1.00 66.75 C ATOM 3493 NE ARG I 1 57.597 34.538 9.985 1.00 68.29 N ATOM 3494 CZ ARG I 1 57.964 35.776 10.331 1.00 68.69 C ATOM 3495 NH1 ARG I 1 58.507 36.578 9.419 1.00 68.63 N ATOM 3496 NH2 ARG I 1 57.801 36.224 11.573 1.00 69.22 N ATOM 3497 N ARG I 2 56.402 29.065 7.532 1.00 63.45 N ATOM 3498 CA ARG I 2 55.756 28.462 6.362 1.00 63.21 C ATOM 3499 C ARG I 2 54.552 29.237 5.849 1.00 62.61 C ATOM 3500 O ARG I 2 54.118 28.990 4.727 1.00 62.39 O ATOM 3501 CB ARG I 2 55.351 27.020 6.666 1.00 63.37 C ATOM 3502 CG ARG I 2 56.545 26.083 6.696 1.00 64.15 C ATOM 3503 CD ARG I 2 56.156 24.623 6.871 1.00 65.00 C ATOM 3504 NE ARG I 2 55.820 23.921 5.634 1.00 65.69 N ATOM 3505 CZ ARG I 2 56.678 23.651 4.650 1.00 67.22 C ATOM 3506 NH1 ARG I 2 57.953 24.041 4.704 1.00 67.63 N ATOM 3507 NH2 ARG I 2 56.250 22.996 3.580 1.00 68.08 N HETATM 3508 N ALN I 3 53.803 30.235 6.333 1.00 61.31 N HETATM 3509 CA ALN I 3 52.575 30.652 5.675 1.00 60.83 C HETATM 3510 C ALN I 3 52.613 32.142 5.546 1.00 61.47 C HETATM 3511 O ALN I 3 51.736 32.820 6.117 1.00 61.29 O HETATM 3512 CB ALN I 3 51.352 30.218 6.478 1.00 60.59 C HETATM 3513 CG1 ALN I 3 51.257 28.723 6.695 1.00 59.11 C HETATM 3514 CD1 ALN I 3 51.482 28.197 7.960 1.00 58.84 C HETATM 3515 CE1 ALN I 3 51.406 26.832 8.232 1.00 58.40 C HETATM 3516 CD2 ALN I 3 50.910 27.781 5.613 1.00 58.17 C HETATM 3517 CE2 ALN I 3 50.842 26.342 5.950 1.00 57.98 C HETATM 3518 CZ1 ALN I 3 51.086 25.914 7.242 1.00 58.42 C HETATM 3519 CG2 ALN I 3 50.653 28.191 4.310 1.00 58.14 C HETATM 3520 CD3 ALN I 3 50.345 27.247 3.341 1.00 57.86 C HETATM 3521 CE3 ALN I 3 50.283 25.892 3.667 1.00 58.62 C HETATM 3522 CZ2 ALN I 3 50.528 25.434 4.962 1.00 58.08 C ATOM 3523 N CYS I 4 53.594 32.733 4.867 1.00 63.18 N ATOM 3524 CA CYS I 4 53.597 34.193 4.753 1.00 63.78 C ATOM 3525 C CYS I 4 52.883 34.636 3.495 1.00 63.35 C ATOM 3526 O CYS I 4 52.649 33.838 2.601 1.00 63.49 O ATOM 3527 CB CYS I 4 55.025 34.738 4.764 1.00 64.06 C ATOM 3528 SG CYS I 4 55.921 34.276 6.251 1.00 65.90 S ATOM 3529 N TYR I 5 52.529 35.913 3.432 1.00 63.11 N ATOM 3530 CA TYR I 5 51.786 36.420 2.296 1.00 62.86 C ATOM 3531 C TYR I 5 51.643 37.932 2.301 1.00 63.25 C ATOM 3532 O TYR I 5 51.992 38.586 3.278 1.00 62.85 O ATOM 3533 CB TYR I 5 50.404 35.769 2.249 1.00 62.60 C ATOM 3534 CG TYR I 5 49.511 36.049 3.437 1.00 60.76 C ATOM 3535 CD1 TYR I 5 49.726 35.438 4.663 1.00 58.61 C ATOM 3536 CD2 TYR I 5 48.418 36.897 3.309 1.00 59.72 C ATOM 3537 CE1 TYR I 5 48.887 35.685 5.738 1.00 58.73 C ATOM 3538 CE2 TYR I 5 47.574 37.149 4.371 1.00 59.17 C ATOM 3539 CZ TYR I 5 47.804 36.541 5.582 1.00 59.09 C ATOM 3540 OH TYR I 5 46.942 36.807 6.629 1.00 59.31 O ATOM 3541 N GLN I 6 51.122 38.460 1.193 1.00 63.91 N ATOM 3542 CA GLN I 6 50.915 39.894 1.003 1.00 64.60 C ATOM 3543 C GLN I 6 49.451 40.262 1.234 1.00 64.66 C ATOM 3544 O GLN I 6 48.578 39.769 0.525 1.00 64.43 O ATOM 3545 CB GLN I 6 51.317 40.289 -0.427 1.00 64.96 C ATOM 3546 CG GLN I 6 51.309 41.790 -0.718 1.00 65.85 C ATOM 3547 CD GLN I 6 52.394 42.533 0.036 1.00 67.10 C ATOM 3548 OE1 GLN I 6 53.580 42.246 -0.120 1.00 68.12 O ATOM 3549 NE2 GLN I 6 51.993 43.498 0.855 1.00 67.83 N ATOM 3550 N LYS I 7 49.192 41.121 2.222 1.00 65.07 N ATOM 3551 CA LYS I 7 47.857 41.696 2.438 1.00 65.67 C ATOM 3552 C LYS I 7 47.908 43.205 2.198 1.00 65.97 C ATOM 3553 O LYS I 7 48.346 43.954 3.077 1.00 65.86 O ATOM 3554 CB LYS I 7 47.352 41.400 3.855 1.00 65.96 C ATOM 3555 CG LYS I 7 45.880 41.792 4.125 1.00 66.62 C ATOM 3556 CD LYS I 7 44.879 40.869 3.420 1.00 67.72 C ATOM 3557 CE LYS I 7 43.454 41.101 3.942 1.00 68.79 C ATOM 3558 NZ LYS I 7 42.391 40.432 3.111 1.00 69.79 N HETATM 3559 N DPR I 8 47.480 43.659 0.999 1.00 66.45 N HETATM 3560 CA DPR I 8 47.619 45.076 0.650 1.00 66.74 C HETATM 3561 CB DPR I 8 47.127 45.126 -0.803 1.00 66.82 C HETATM 3562 CG DPR I 8 47.313 43.742 -1.318 1.00 66.67 C HETATM 3563 CD DPR I 8 46.982 42.874 -0.148 1.00 66.51 C HETATM 3564 C DPR I 8 49.080 45.527 0.717 1.00 66.94 C HETATM 3565 O DPR I 8 49.932 44.913 0.072 1.00 66.91 O ATOM 3566 N PRO I 9 49.374 46.581 1.498 1.00 67.26 N ATOM 3567 CA PRO I 9 50.762 47.004 1.648 1.00 67.54 C ATOM 3568 C PRO I 9 51.536 46.158 2.662 1.00 67.76 C ATOM 3569 O PRO I 9 52.758 46.304 2.759 1.00 67.79 O ATOM 3570 CB PRO I 9 50.628 48.441 2.153 1.00 67.52 C ATOM 3571 CG PRO I 9 49.390 48.412 2.968 1.00 67.40 C ATOM 3572 CD PRO I 9 48.462 47.422 2.295 1.00 67.28 C ATOM 3573 N TYR I 10 50.834 45.274 3.383 1.00 67.93 N ATOM 3574 CA TYR I 10 51.419 44.488 4.479 1.00 68.09 C ATOM 3575 C TYR I 10 51.986 43.135 4.047 1.00 67.85 C ATOM 3576 O TYR I 10 51.486 42.509 3.119 1.00 67.65 O ATOM 3577 CB TYR I 10 50.369 44.269 5.576 1.00 68.24 C ATOM 3578 CG TYR I 10 49.811 45.568 6.104 1.00 69.65 C ATOM 3579 CD1 TYR I 10 50.466 46.266 7.121 1.00 70.78 C ATOM 3580 CD2 TYR I 10 48.650 46.122 5.569 1.00 70.66 C ATOM 3581 CE1 TYR I 10 49.975 47.464 7.597 1.00 71.10 C ATOM 3582 CE2 TYR I 10 48.152 47.325 6.041 1.00 71.05 C ATOM 3583 CZ TYR I 10 48.820 47.988 7.052 1.00 71.54 C ATOM 3584 OH TYR I 10 48.337 49.180 7.524 1.00 73.43 O ATOM 3585 N ARG I 11 53.051 42.711 4.719 1.00 67.87 N ATOM 3586 CA ARG I 11 53.492 41.322 4.685 1.00 68.15 C ATOM 3587 C ARG I 11 52.932 40.655 5.928 1.00 68.01 C ATOM 3588 O ARG I 11 52.891 41.276 6.992 1.00 67.87 O ATOM 3589 CB ARG I 11 55.019 41.193 4.690 1.00 68.38 C ATOM 3590 CG ARG I 11 55.661 41.403 3.334 1.00 69.76 C ATOM 3591 CD ARG I 11 57.036 40.744 3.238 1.00 71.58 C ATOM 3592 NE ARG I 11 57.480 40.645 1.841 1.00 72.88 N ATOM 3593 CZ ARG I 11 58.433 39.823 1.394 1.00 73.14 C ATOM 3594 NH1 ARG I 11 58.739 39.818 0.101 1.00 73.49 N ATOM 3595 NH2 ARG I 11 59.080 39.001 2.218 1.00 72.61 N HETATM 3596 C1 CIR I 12 52.374 37.407 7.200 1.00 67.17 C HETATM 3597 O1 CIR I 12 52.710 36.947 6.091 1.00 65.82 O HETATM 3598 C2 CIR I 12 51.720 38.746 7.180 1.00 68.09 C HETATM 3599 N2 CIR I 12 52.274 39.502 6.077 1.00 68.09 N HETATM 3600 C3 CIR I 12 50.240 38.559 6.934 1.00 69.11 C HETATM 3601 C4 CIR I 12 49.481 39.850 7.164 1.00 70.48 C HETATM 3602 C5 CIR I 12 48.532 39.701 8.345 1.00 72.75 C HETATM 3603 N6 CIR I 12 47.200 40.189 8.039 1.00 74.81 N HETATM 3604 C7 CIR I 12 46.208 40.045 8.917 1.00 77.13 C HETATM 3605 O7 CIR I 12 46.395 39.472 9.988 1.00 78.19 O HETATM 3606 N8 CIR I 12 45.008 40.553 8.607 1.00 78.06 N ATOM 3607 N CYS I 13 52.472 36.771 8.361 1.00 67.45 N ATOM 3608 CA CYS I 13 52.455 35.315 8.272 1.00 67.71 C ATOM 3609 C CYS I 13 51.417 34.722 9.225 1.00 67.55 C ATOM 3610 O CYS I 13 51.064 35.327 10.237 1.00 67.66 O ATOM 3611 CB CYS I 13 53.853 34.744 8.554 1.00 67.81 C ATOM 3612 SG CYS I 13 55.237 35.601 7.666 1.00 68.93 S ATOM 3613 N ARG I 14 50.930 33.532 8.888 1.00 67.31 N ATOM 3614 CA ARG I 14 49.870 32.886 9.652 1.00 66.92 C ATOM 3615 C ARG I 14 50.363 32.241 10.950 1.00 67.02 C ATOM 3616 O ARG I 14 49.552 31.806 11.785 1.00 67.18 O ATOM 3617 CB ARG I 14 49.161 31.850 8.788 1.00 66.70 C ATOM 3618 CG ARG I 14 47.997 32.390 8.015 1.00 66.19 C ATOM 3619 CD ARG I 14 46.860 32.790 8.936 1.00 65.62 C ATOM 3620 NE ARG I 14 46.700 34.237 9.029 1.00 64.91 N ATOM 3621 CZ ARG I 14 45.828 34.840 9.829 1.00 64.70 C ATOM 3622 NH1 ARG I 14 45.749 36.164 9.845 1.00 65.18 N ATOM 3623 NH2 ARG I 14 45.042 34.129 10.626 1.00 64.55 N ATOM 3624 N GLY I 15 51.676 32.176 11.134 1.00 66.92 N ATOM 3625 CA GLY I 15 52.222 31.743 12.418 1.00 67.07 C ATOM 3626 C GLY I 15 52.390 30.240 12.462 1.00 66.91 C ATOM 3627 O GLY I 15 51.419 29.494 12.329 1.00 66.71 O HETATM 3628 N DPR I 16 53.628 29.794 12.697 1.00 66.95 N HETATM 3629 CA DPR I 16 54.089 28.513 12.204 1.00 67.11 C HETATM 3630 CB DPR I 16 55.128 28.084 13.248 1.00 67.00 C HETATM 3631 CG DPR I 16 55.209 29.210 14.240 1.00 66.69 C HETATM 3632 CD DPR I 16 54.610 30.397 13.608 1.00 66.77 C HETATM 3633 C DPR I 16 54.735 28.735 10.833 1.00 67.39 C HETATM 3634 O DPR I 16 55.506 27.915 10.321 1.00 67.72 O HETATM 3635 OXT DPR I 16 54.502 29.772 10.197 1.00 67.52 O TER 3636 DPR I 16 HETATM 3637 O HOH A1600 51.996 18.773 17.684 1.00 36.01 O HETATM 3638 O HOH A1603 52.741 14.448 8.911 1.00 49.65 O HETATM 3639 O HOH A1605 49.135 -24.575 35.419 1.00 30.25 O HETATM 3640 O HOH I1601 54.372 25.545 10.342 1.00 53.07 O HETATM 3641 O HOH I1602 58.577 37.594 4.253 1.00 46.34 O HETATM 3642 O HOH I1604 57.675 27.030 10.941 1.00 39.92 O CONECT 31 3244 CONECT 656 1279 CONECT 1279 656 CONECT 1616 1624 CONECT 1624 1616 CONECT 3244 31 CONECT 3499 3508 CONECT 3508 3499 3509 CONECT 3509 3508 3510 3512 CONECT 3510 3509 3511 3523 CONECT 3511 3510 CONECT 3512 3509 3513 CONECT 3513 3512 3514 3516 CONECT 3514 3513 3515 CONECT 3515 3514 3518 CONECT 3516 3513 3517 3519 CONECT 3517 3516 3518 3522 CONECT 3518 3515 3517 CONECT 3519 3516 3520 CONECT 3520 3519 3521 CONECT 3521 3520 3522 CONECT 3522 3517 3521 CONECT 3523 3510 CONECT 3528 3612 CONECT 3552 3559 CONECT 3559 3552 3560 3563 CONECT 3560 3559 3561 3564 CONECT 3561 3560 3562 CONECT 3562 3561 3563 CONECT 3563 3559 3562 CONECT 3564 3560 3565 3566 CONECT 3565 3564 CONECT 3566 3564 CONECT 3587 3599 CONECT 3596 3597 3598 3607 CONECT 3597 3596 CONECT 3598 3596 3599 3600 CONECT 3599 3587 3598 CONECT 3600 3598 3601 CONECT 3601 3600 3602 CONECT 3602 3601 3603 CONECT 3603 3602 3604 CONECT 3604 3603 3605 3606 CONECT 3605 3604 CONECT 3606 3604 CONECT 3607 3596 CONECT 3612 3528 CONECT 3626 3628 CONECT 3628 3626 3629 3632 CONECT 3629 3628 3630 3633 CONECT 3630 3629 3631 CONECT 3631 3630 3632 CONECT 3632 3628 3631 CONECT 3633 3629 3634 3635 CONECT 3634 3633 CONECT 3635 3633 MASTER 455 0 4 23 6 0 6 6 3640 2 56 41 END