HEADER SIGNALING PROTEIN 24-JUN-13 4BV0 TITLE HIGH RESOLUTION STRUCTURE OF EVOLVED AGONIST-BOUND NEUROTENSIN TITLE 2 RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUROTENSIN RECEPTOR TYPE 1; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: RESIDUES 50-390; COMPND 5 SYNONYM: NEUROTENSIN RECEPTOR 1 TM86VDIC3B, NT-R-1, NTR1, HIGH- COMPND 6 AFFINITY LEVOCABASTINE-INSENSITIVE NEUROTENSIN RECEPTOR, NTRH; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 OTHER_DETAILS: THERMOSTABLE MUTANT WITH INTRACELLULAR LOOP 3 DELETION COMPND 10 B (T279-I295); COMPND 11 MOL_ID: 2; COMPND 12 MOLECULE: NEUROTENSIN/NEUROMEDIN N; COMPND 13 CHAIN: C, D; COMPND 14 FRAGMENT: C-TERMINUS, RESIDUES 157-162; COMPND 15 SYNONYM: LARGE NEUROMEDIN N, NMN-125, NEUROMEDIN N, NN, NMN, COMPND 16 NEUROTENSIN, NT, TAIL PEPTIDE; COMPND 17 ENGINEERED: YES; COMPND 18 OTHER_DETAILS: THE SEQUENCE RRPYIL CORRESPONDS TO RESIDUES 8-13 OF COMPND 19 THE NEUROTENSIN C-TERMINUS. THE FULL CRYSTALLIZED CONSTRUCT WAS COMPND 20 GPGGRRPYIL (THE N-TERMINAL GPGG IS AN ARTIFICIAL LINKER). SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VARIANT: TUNER; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEP-TM86VDIC3III; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 13 ORGANISM_COMMON: NORWAY RAT; SOURCE 14 ORGANISM_TAXID: 10116; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) KEYWDS SIGNALING PROTEIN, G PROTEIN COUPLED RECEPTOR, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR P.EGLOFF,M.HILLENBRAND,D.J.SCOTT,K.M.SCHLINKMANN,P.HEINE,S.BALADA, AUTHOR 2 A.BATYUK,P.MITTL,M.SCHUETZ,A.PLUECKTHUN REVDAT 4 20-JUN-18 4BV0 1 JRNL REMARK REVDAT 3 26-FEB-14 4BV0 1 JRNL REVDAT 2 05-FEB-14 4BV0 1 JRNL REVDAT 1 29-JAN-14 4BV0 0 JRNL AUTH P.EGLOFF,M.HILLENBRAND,C.KLENK,A.BATYUK,P.HEINE,S.BALADA, JRNL AUTH 2 K.M.SCHLINKMANN,D.J.SCOTT,M.SCHUETZ,A.PLUECKTHUN JRNL TITL STRUCTURE OF SIGNALING-COMPETENT NEUROTENSIN RECEPTOR 1 JRNL TITL 2 OBTAINED BY DIRECTED EVOLUTION IN ESCHERICHIA COLI JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 E655 2014 JRNL REFN ISSN 0027-8424 JRNL PMID 24453215 JRNL DOI 10.1073/PNAS.1317903111 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2 REMARK 3 NUMBER OF REFLECTIONS : 20680 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.284 REMARK 3 FREE R VALUE : 0.311 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1036 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 19.8765 - 5.8862 1.00 3108 164 0.2375 0.2655 REMARK 3 2 5.8862 - 4.6923 1.00 2967 156 0.2628 0.2864 REMARK 3 3 4.6923 - 4.1051 1.00 2934 155 0.2395 0.2904 REMARK 3 4 4.1051 - 3.7325 0.99 2899 151 0.3379 0.3458 REMARK 3 5 3.7325 - 3.4665 0.86 2512 133 0.4268 0.4762 REMARK 3 6 3.4665 - 3.2630 0.92 2635 140 0.4534 0.4471 REMARK 3 7 3.2630 - 3.1002 0.89 2589 137 0.4485 0.4484 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.770 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 45.010 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 4985 REMARK 3 ANGLE : 0.651 6794 REMARK 3 CHIRALITY : 0.046 821 REMARK 3 PLANARITY : 0.003 818 REMARK 3 DIHEDRAL : 10.105 1725 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN A REMARK 3 SELECTION : CHAIN B REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN C REMARK 3 SELECTION : CHAIN D REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: PHENIX AND REFMAC WERE USED REMARK 4 REMARK 4 4BV0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUN-13. REMARK 100 THE DEPOSITION ID IS D_1290057425. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21665 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 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 (%) : 99.2 REMARK 200 DATA REDUNDANCY : 6.300 REMARK 200 R MERGE (I) : 0.10000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.5500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0 REMARK 200 DATA REDUNDANCY IN SHELL : 5.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.510 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: PDB ENTRY 3ZEV REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.03 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% (V/V) PEG600, 0.5 M NACL, 50 MM REMARK 280 GLYCINE PH 9.4 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 30.29000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.29000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.78000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.29000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.29000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.78000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1690 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14650 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.1 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1660 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14950 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.1 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 46 REMARK 465 PRO A 47 REMARK 465 GLY A 48 REMARK 465 SER A 49 REMARK 465 GLY A 50 REMARK 465 PRO A 51 REMARK 465 LYS A 93 REMARK 465 SER A 94 REMARK 465 LEU A 95 REMARK 465 GLN A 96 REMARK 465 SER A 97 REMARK 465 LEU A 98 REMARK 465 GLN A 99 REMARK 465 PHE A 175 REMARK 465 LYS A 176 REMARK 465 HIS A 177 REMARK 465 LYS A 178 REMARK 465 THR A 179 REMARK 465 GLN A 270 REMARK 465 ALA A 271 REMARK 465 ALA A 272 REMARK 465 GLU A 273 REMARK 465 GLN A 274 REMARK 465 GLY A 275 REMARK 465 ARG A 276 REMARK 465 VAL A 277 REMARK 465 CYS A 278 REMARK 465 THR A 279 REMARK 465 GLU A 280 REMARK 465 CYS A 388 REMARK 465 PRO A 389 REMARK 465 GLY A 390 REMARK 465 THR A 391 REMARK 465 ARG A 392 REMARK 465 GLU A 393 REMARK 465 LEU A 394 REMARK 465 GLU A 395 REMARK 465 VAL A 396 REMARK 465 LEU A 397 REMARK 465 PHE A 398 REMARK 465 GLN A 399 REMARK 465 GLY B 46 REMARK 465 PRO B 47 REMARK 465 GLY B 48 REMARK 465 SER B 49 REMARK 465 GLY B 50 REMARK 465 LYS B 92 REMARK 465 LYS B 93 REMARK 465 SER B 94 REMARK 465 LEU B 95 REMARK 465 GLN B 96 REMARK 465 SER B 97 REMARK 465 LEU B 180 REMARK 465 HIS B 269 REMARK 465 GLN B 270 REMARK 465 ALA B 271 REMARK 465 ALA B 272 REMARK 465 GLU B 273 REMARK 465 GLN B 274 REMARK 465 GLY B 275 REMARK 465 ARG B 276 REMARK 465 VAL B 277 REMARK 465 CYS B 278 REMARK 465 THR B 279 REMARK 465 GLU B 280 REMARK 465 PRO B 281 REMARK 465 GLY B 282 REMARK 465 GLY B 390 REMARK 465 THR B 391 REMARK 465 ARG B 392 REMARK 465 GLU B 393 REMARK 465 LEU B 394 REMARK 465 GLU B 395 REMARK 465 VAL B 396 REMARK 465 LEU B 397 REMARK 465 PHE B 398 REMARK 465 GLN B 399 REMARK 465 GLY C 4 REMARK 465 PRO C 5 REMARK 465 GLY C 6 REMARK 465 GLY D 4 REMARK 465 PRO D 5 REMARK 465 GLY D 6 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 58 53.99 -116.94 REMARK 500 ALA A 136 52.81 -118.26 REMARK 500 PHE A 137 -3.81 -143.68 REMARK 500 MET A 181 75.43 53.93 REMARK 500 PHE A 246 -78.91 -131.63 REMARK 500 SER B 53 -172.77 -65.32 REMARK 500 ILE B 129 -49.67 -137.14 REMARK 500 LEU B 213 48.68 -103.05 REMARK 500 PHE B 246 -77.25 -130.49 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3ZEV RELATED DB: PDB REMARK 900 STRUCTURE OF THERMOSTABLE AGONIST-BOUND NEUROTENSIN RECEPTOR 1 REMARK 900 MUTANT WITHOUT LYSOZYME FUSION REMARK 900 RELATED ID: 4BV0 RELATED DB: PDB REMARK 900 HIGH RESOLUTION STRUCTURE OF EVOLVED AGONIST-BOUND NEUROTENSIN REMARK 900 RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION REMARK 900 RELATED ID: 4BWB RELATED DB: PDB REMARK 900 STRUCTURE OF EVOLVED AGONIST-BOUND NEUROTENSIN RECEPTOR 1 MUTANT REMARK 900 WITHOUT LYSOZYME FUSION DBREF 4BV0 A 50 390 UNP P20789 NTR1_RAT 50 390 DBREF 4BV0 B 50 390 UNP P20789 NTR1_RAT 50 390 DBREF 4BV0 C 8 13 UNP P20068 NEUT_RAT 157 162 DBREF 4BV0 D 8 13 UNP P20068 NEUT_RAT 157 162 SEQADV 4BV0 GLY A 46 UNP P20789 EXPRESSION TAG SEQADV 4BV0 PRO A 47 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLY A 48 UNP P20789 EXPRESSION TAG SEQADV 4BV0 SER A 49 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLY A 83 UNP P20789 SER 83 ENGINEERED MUTATION SEQADV 4BV0 LEU A 86 UNP P20789 ALA 86 ENGINEERED MUTATION SEQADV 4BV0 ARG A 101 UNP P20789 THR 101 ENGINEERED MUTATION SEQADV 4BV0 ASP A 103 UNP P20789 HIS 103 ENGINEERED MUTATION SEQADV 4BV0 TYR A 105 UNP P20789 HIS 105 ENGINEERED MUTATION SEQADV 4BV0 PHE A 119 UNP P20789 LEU 119 ENGINEERED MUTATION SEQADV 4BV0 LEU A 121 UNP P20789 MET 121 ENGINEERED MUTATION SEQADV 4BV0 ASP A 124 UNP P20789 GLU 124 ENGINEERED MUTATION SEQADV 4BV0 VAL A 125 UNP P20789 LEU 125 ENGINEERED MUTATION SEQADV 4BV0 LYS A 143 UNP P20789 ARG 143 ENGINEERED MUTATION SEQADV 4BV0 GLU A 150 UNP P20789 ASP 150 ENGINEERED MUTATION SEQADV 4BV0 VAL A 161 UNP P20789 ALA 161 ENGINEERED MUTATION SEQADV 4BV0 LEU A 167 UNP P20789 ARG 167 ENGINEERED MUTATION SEQADV 4BV0 ARG A 172 UNP P20789 CYS 172 ENGINEERED MUTATION SEQADV 4BV0 HIS A 177 UNP P20789 ALA 177 ENGINEERED MUTATION SEQADV 4BV0 VAL A 208 UNP P20789 MET 208 ENGINEERED MUTATION SEQADV 4BV0 LEU A 213 UNP P20789 ARG 213 ENGINEERED MUTATION SEQADV 4BV0 LEU A 234 UNP P20789 VAL 234 ENGINEERED MUTATION SEQADV 4BV0 LEU A 240 UNP P20789 VAL 240 ENGINEERED MUTATION SEQADV 4BV0 ALA A 253 UNP P20789 ILE 253 ENGINEERED MUTATION SEQADV 4BV0 ARG A 262 UNP P20789 ASN 262 ENGINEERED MUTATION SEQADV 4BV0 ARG A 263 UNP P20789 LYS 263 ENGINEERED MUTATION SEQADV 4BV0 A UNP P20789 VAL 280 DELETION SEQADV 4BV0 A UNP P20789 GLY 281 DELETION SEQADV 4BV0 A UNP P20789 THR 282 DELETION SEQADV 4BV0 A UNP P20789 HIS 283 DELETION SEQADV 4BV0 A UNP P20789 ASN 284 DELETION SEQADV 4BV0 A UNP P20789 GLY 285 DELETION SEQADV 4BV0 A UNP P20789 LEU 286 DELETION SEQADV 4BV0 A UNP P20789 GLU 287 DELETION SEQADV 4BV0 A UNP P20789 HIS 288 DELETION SEQADV 4BV0 A UNP P20789 SER 289 DELETION SEQADV 4BV0 A UNP P20789 THR 290 DELETION SEQADV 4BV0 A UNP P20789 PHE 291 DELETION SEQADV 4BV0 A UNP P20789 ASN 292 DELETION SEQADV 4BV0 A UNP P20789 MET 293 DELETION SEQADV 4BV0 A UNP P20789 THR 294 DELETION SEQADV 4BV0 A UNP P20789 ILE 295 DELETION SEQADV 4BV0 ARG A 305 UNP P20789 HIS 305 ENGINEERED MUTATION SEQADV 4BV0 MET A 313 UNP P20789 VAL 313 ENGINEERED MUTATION SEQADV 4BV0 VAL A 332 UNP P20789 CYS 332 ENGINEERED MUTATION SEQADV 4BV0 ALA A 342 UNP P20789 PHE 342 ENGINEERED MUTATION SEQADV 4BV0 SER A 354 UNP P20789 THR 354 ENGINEERED MUTATION SEQADV 4BV0 VAL A 358 UNP P20789 PHE 358 ENGINEERED MUTATION SEQADV 4BV0 ALA A 362 UNP P20789 SER 362 ENGINEERED MUTATION SEQADV 4BV0 THR A 391 UNP P20789 EXPRESSION TAG SEQADV 4BV0 ARG A 392 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLU A 393 UNP P20789 EXPRESSION TAG SEQADV 4BV0 LEU A 394 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLU A 395 UNP P20789 EXPRESSION TAG SEQADV 4BV0 VAL A 396 UNP P20789 EXPRESSION TAG SEQADV 4BV0 LEU A 397 UNP P20789 EXPRESSION TAG SEQADV 4BV0 PHE A 398 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLN A 399 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLY B 46 UNP P20789 EXPRESSION TAG SEQADV 4BV0 PRO B 47 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLY B 48 UNP P20789 EXPRESSION TAG SEQADV 4BV0 SER B 49 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLY B 83 UNP P20789 SER 83 ENGINEERED MUTATION SEQADV 4BV0 LEU B 86 UNP P20789 ALA 86 ENGINEERED MUTATION SEQADV 4BV0 ARG B 101 UNP P20789 THR 101 ENGINEERED MUTATION SEQADV 4BV0 ASP B 103 UNP P20789 HIS 103 ENGINEERED MUTATION SEQADV 4BV0 TYR B 105 UNP P20789 HIS 105 ENGINEERED MUTATION SEQADV 4BV0 PHE B 119 UNP P20789 LEU 119 ENGINEERED MUTATION SEQADV 4BV0 LEU B 121 UNP P20789 MET 121 ENGINEERED MUTATION SEQADV 4BV0 ASP B 124 UNP P20789 GLU 124 ENGINEERED MUTATION SEQADV 4BV0 VAL B 125 UNP P20789 LEU 125 ENGINEERED MUTATION SEQADV 4BV0 LYS B 143 UNP P20789 ARG 143 ENGINEERED MUTATION SEQADV 4BV0 GLU B 150 UNP P20789 ASP 150 ENGINEERED MUTATION SEQADV 4BV0 VAL B 161 UNP P20789 ALA 161 ENGINEERED MUTATION SEQADV 4BV0 LEU B 167 UNP P20789 ARG 167 ENGINEERED MUTATION SEQADV 4BV0 ARG B 172 UNP P20789 CYS 172 ENGINEERED MUTATION SEQADV 4BV0 HIS B 177 UNP P20789 ALA 177 ENGINEERED MUTATION SEQADV 4BV0 VAL B 208 UNP P20789 MET 208 ENGINEERED MUTATION SEQADV 4BV0 LEU B 213 UNP P20789 ARG 213 ENGINEERED MUTATION SEQADV 4BV0 LEU B 234 UNP P20789 VAL 234 ENGINEERED MUTATION SEQADV 4BV0 LEU B 240 UNP P20789 VAL 240 ENGINEERED MUTATION SEQADV 4BV0 ALA B 253 UNP P20789 ILE 253 ENGINEERED MUTATION SEQADV 4BV0 ARG B 262 UNP P20789 ASN 262 ENGINEERED MUTATION SEQADV 4BV0 ARG B 263 UNP P20789 LYS 263 ENGINEERED MUTATION SEQADV 4BV0 B UNP P20789 VAL 280 DELETION SEQADV 4BV0 B UNP P20789 GLY 281 DELETION SEQADV 4BV0 B UNP P20789 THR 282 DELETION SEQADV 4BV0 B UNP P20789 HIS 283 DELETION SEQADV 4BV0 B UNP P20789 ASN 284 DELETION SEQADV 4BV0 B UNP P20789 GLY 285 DELETION SEQADV 4BV0 B UNP P20789 LEU 286 DELETION SEQADV 4BV0 B UNP P20789 GLU 287 DELETION SEQADV 4BV0 B UNP P20789 HIS 288 DELETION SEQADV 4BV0 B UNP P20789 SER 289 DELETION SEQADV 4BV0 B UNP P20789 THR 290 DELETION SEQADV 4BV0 B UNP P20789 PHE 291 DELETION SEQADV 4BV0 B UNP P20789 ASN 292 DELETION SEQADV 4BV0 B UNP P20789 MET 293 DELETION SEQADV 4BV0 B UNP P20789 THR 294 DELETION SEQADV 4BV0 B UNP P20789 ILE 295 DELETION SEQADV 4BV0 ARG B 305 UNP P20789 HIS 305 ENGINEERED MUTATION SEQADV 4BV0 MET B 313 UNP P20789 VAL 313 ENGINEERED MUTATION SEQADV 4BV0 VAL B 332 UNP P20789 CYS 332 ENGINEERED MUTATION SEQADV 4BV0 ALA B 342 UNP P20789 PHE 342 ENGINEERED MUTATION SEQADV 4BV0 SER B 354 UNP P20789 THR 354 ENGINEERED MUTATION SEQADV 4BV0 VAL B 358 UNP P20789 PHE 358 ENGINEERED MUTATION SEQADV 4BV0 ALA B 362 UNP P20789 SER 362 ENGINEERED MUTATION SEQADV 4BV0 THR B 391 UNP P20789 EXPRESSION TAG SEQADV 4BV0 ARG B 392 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLU B 393 UNP P20789 EXPRESSION TAG SEQADV 4BV0 LEU B 394 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLU B 395 UNP P20789 EXPRESSION TAG SEQADV 4BV0 VAL B 396 UNP P20789 EXPRESSION TAG SEQADV 4BV0 LEU B 397 UNP P20789 EXPRESSION TAG SEQADV 4BV0 PHE B 398 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLN B 399 UNP P20789 EXPRESSION TAG SEQADV 4BV0 GLY C 4 UNP P20068 EXPRESSION TAG SEQADV 4BV0 PRO C 5 UNP P20068 EXPRESSION TAG SEQADV 4BV0 GLY C 6 UNP P20068 EXPRESSION TAG SEQADV 4BV0 GLY C 7 UNP P20068 EXPRESSION TAG SEQADV 4BV0 GLY D 4 UNP P20068 EXPRESSION TAG SEQADV 4BV0 PRO D 5 UNP P20068 EXPRESSION TAG SEQADV 4BV0 GLY D 6 UNP P20068 EXPRESSION TAG SEQADV 4BV0 GLY D 7 UNP P20068 EXPRESSION TAG SEQRES 1 A 338 GLY PRO GLY SER GLY PRO ASN SER ASP LEU ASP VAL ASN SEQRES 2 A 338 THR ASP ILE TYR SER LYS VAL LEU VAL THR ALA ILE TYR SEQRES 3 A 338 LEU ALA LEU PHE VAL VAL GLY THR VAL GLY ASN GLY VAL SEQRES 4 A 338 THR LEU PHE THR LEU ALA ARG LYS LYS SER LEU GLN SER SEQRES 5 A 338 LEU GLN SER ARG VAL ASP TYR TYR LEU GLY SER LEU ALA SEQRES 6 A 338 LEU SER ASP LEU LEU ILE LEU LEU PHE ALA LEU PRO VAL SEQRES 7 A 338 ASP VAL TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA SEQRES 8 A 338 PHE GLY ASP ALA GLY CYS LYS GLY TYR TYR PHE LEU ARG SEQRES 9 A 338 GLU ALA CYS THR TYR ALA THR ALA LEU ASN VAL VAL SER SEQRES 10 A 338 LEU SER VAL GLU LEU TYR LEU ALA ILE ARG HIS PRO PHE SEQRES 11 A 338 LYS HIS LYS THR LEU MET SER ARG SER ARG THR LYS LYS SEQRES 12 A 338 PHE ILE SER ALA ILE TRP LEU ALA SER ALA LEU LEU ALA SEQRES 13 A 338 ILE PRO MET LEU PHE THR VAL GLY LEU GLN ASN LEU SER SEQRES 14 A 338 GLY ASP GLY THR HIS PRO GLY GLY LEU VAL CYS THR PRO SEQRES 15 A 338 ILE VAL ASP THR ALA THR LEU LYS VAL VAL ILE GLN LEU SEQRES 16 A 338 ASN THR PHE MET SER PHE LEU PHE PRO MET LEU VAL ALA SEQRES 17 A 338 SER ILE LEU ASN THR VAL ILE ALA ARG ARG LEU THR VAL SEQRES 18 A 338 MET VAL HIS GLN ALA ALA GLU GLN GLY ARG VAL CYS THR SEQRES 19 A 338 GLU PRO GLY ARG VAL GLN ALA LEU ARG ARG GLY VAL LEU SEQRES 20 A 338 VAL LEU ARG ALA MET VAL ILE ALA PHE VAL VAL CYS TRP SEQRES 21 A 338 LEU PRO TYR HIS VAL ARG ARG LEU MET PHE VAL TYR ILE SEQRES 22 A 338 SER ASP GLU GLN TRP THR THR ALA LEU PHE ASP PHE TYR SEQRES 23 A 338 HIS TYR PHE TYR MET LEU SER ASN ALA LEU VAL TYR VAL SEQRES 24 A 338 SER ALA ALA ILE ASN PRO ILE LEU TYR ASN LEU VAL SER SEQRES 25 A 338 ALA ASN PHE ARG GLN VAL PHE LEU SER THR LEU ALA CYS SEQRES 26 A 338 LEU CYS PRO GLY THR ARG GLU LEU GLU VAL LEU PHE GLN SEQRES 1 B 338 GLY PRO GLY SER GLY PRO ASN SER ASP LEU ASP VAL ASN SEQRES 2 B 338 THR ASP ILE TYR SER LYS VAL LEU VAL THR ALA ILE TYR SEQRES 3 B 338 LEU ALA LEU PHE VAL VAL GLY THR VAL GLY ASN GLY VAL SEQRES 4 B 338 THR LEU PHE THR LEU ALA ARG LYS LYS SER LEU GLN SER SEQRES 5 B 338 LEU GLN SER ARG VAL ASP TYR TYR LEU GLY SER LEU ALA SEQRES 6 B 338 LEU SER ASP LEU LEU ILE LEU LEU PHE ALA LEU PRO VAL SEQRES 7 B 338 ASP VAL TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA SEQRES 8 B 338 PHE GLY ASP ALA GLY CYS LYS GLY TYR TYR PHE LEU ARG SEQRES 9 B 338 GLU ALA CYS THR TYR ALA THR ALA LEU ASN VAL VAL SER SEQRES 10 B 338 LEU SER VAL GLU LEU TYR LEU ALA ILE ARG HIS PRO PHE SEQRES 11 B 338 LYS HIS LYS THR LEU MET SER ARG SER ARG THR LYS LYS SEQRES 12 B 338 PHE ILE SER ALA ILE TRP LEU ALA SER ALA LEU LEU ALA SEQRES 13 B 338 ILE PRO MET LEU PHE THR VAL GLY LEU GLN ASN LEU SER SEQRES 14 B 338 GLY ASP GLY THR HIS PRO GLY GLY LEU VAL CYS THR PRO SEQRES 15 B 338 ILE VAL ASP THR ALA THR LEU LYS VAL VAL ILE GLN LEU SEQRES 16 B 338 ASN THR PHE MET SER PHE LEU PHE PRO MET LEU VAL ALA SEQRES 17 B 338 SER ILE LEU ASN THR VAL ILE ALA ARG ARG LEU THR VAL SEQRES 18 B 338 MET VAL HIS GLN ALA ALA GLU GLN GLY ARG VAL CYS THR SEQRES 19 B 338 GLU PRO GLY ARG VAL GLN ALA LEU ARG ARG GLY VAL LEU SEQRES 20 B 338 VAL LEU ARG ALA MET VAL ILE ALA PHE VAL VAL CYS TRP SEQRES 21 B 338 LEU PRO TYR HIS VAL ARG ARG LEU MET PHE VAL TYR ILE SEQRES 22 B 338 SER ASP GLU GLN TRP THR THR ALA LEU PHE ASP PHE TYR SEQRES 23 B 338 HIS TYR PHE TYR MET LEU SER ASN ALA LEU VAL TYR VAL SEQRES 24 B 338 SER ALA ALA ILE ASN PRO ILE LEU TYR ASN LEU VAL SER SEQRES 25 B 338 ALA ASN PHE ARG GLN VAL PHE LEU SER THR LEU ALA CYS SEQRES 26 B 338 LEU CYS PRO GLY THR ARG GLU LEU GLU VAL LEU PHE GLN SEQRES 1 C 10 GLY PRO GLY GLY ARG ARG PRO TYR ILE LEU SEQRES 1 D 10 GLY PRO GLY GLY ARG ARG PRO TYR ILE LEU HELIX 1 1 ASP A 60 LYS A 92 1 33 HELIX 2 2 ARG A 101 ALA A 120 1 20 HELIX 3 3 ALA A 120 PHE A 128 1 9 HELIX 4 4 PHE A 137 HIS A 173 1 37 HELIX 5 5 SER A 182 ALA A 201 1 20 HELIX 6 6 ILE A 202 PHE A 206 5 5 HELIX 7 7 HIS A 219 GLY A 221 5 3 HELIX 8 8 ASP A 230 PHE A 246 1 17 HELIX 9 9 PHE A 246 HIS A 269 1 24 HELIX 10 10 GLY A 298 ILE A 334 1 37 HELIX 11 11 THR A 340 VAL A 372 1 33 HELIX 12 12 ALA A 374 CYS A 386 1 13 HELIX 13 13 ASP B 60 ALA B 90 1 31 HELIX 14 14 LEU B 98 ASN B 127 1 30 HELIX 15 15 GLY B 138 HIS B 173 1 36 HELIX 16 16 SER B 182 ILE B 202 1 21 HELIX 17 17 PRO B 203 THR B 207 1 5 HELIX 18 18 HIS B 219 GLY B 221 5 3 HELIX 19 19 ASP B 230 PHE B 246 1 17 HELIX 20 20 PHE B 246 VAL B 266 1 21 HELIX 21 21 ARG B 299 ILE B 334 1 36 HELIX 22 22 THR B 340 VAL B 372 1 33 HELIX 23 23 ALA B 374 LEU B 387 1 14 SHEET 1 AA 2 VAL A 208 ASN A 212 0 SHEET 2 AA 2 LEU A 223 PRO A 227 -1 O VAL A 224 N GLN A 211 SHEET 1 BA 2 VAL B 208 ASN B 212 0 SHEET 2 BA 2 LEU B 223 PRO B 227 -1 O VAL B 224 N GLN B 211 SSBOND 1 CYS A 142 CYS A 225 1555 1555 2.03 SSBOND 2 CYS B 142 CYS B 225 1555 1555 2.03 CISPEP 1 HIS A 133 PRO A 134 0 -0.35 CISPEP 2 HIS B 133 PRO B 134 0 1.36 CRYST1 60.580 91.560 208.580 90.00 90.00 90.00 P 21 21 21 8 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 0.016507 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010922 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004794 0.00000 MTRIX1 1 -0.488000 -0.155000 -0.859000 -4.46500 1 MTRIX2 1 -0.146400 -0.955600 0.255600 -30.54000 1 MTRIX3 1 -0.860400 0.250500 0.443700 2.75000 1 ATOM 1 N ASN A 52 -36.736 -41.270 49.553 1.00 93.50 N ANISOU 1 N ASN A 52 12288 7698 15538 -1202 2582 1338 N ATOM 2 CA ASN A 52 -36.547 -40.605 48.269 1.00 92.56 C ANISOU 2 CA ASN A 52 11964 7807 15396 -1219 2332 1059 C ATOM 3 C ASN A 52 -35.724 -41.438 47.290 1.00 93.28 C ANISOU 3 C ASN A 52 12261 7678 15504 -1176 2172 838 C ATOM 4 O ASN A 52 -34.623 -41.049 46.900 1.00 92.60 O ANISOU 4 O ASN A 52 12226 7724 15235 -921 2030 705 O ATOM 5 CB ASN A 52 -35.910 -39.227 48.468 1.00 88.62 C ANISOU 5 CB ASN A 52 11331 7694 14645 -947 2253 1047 C ATOM 6 CG ASN A 52 -34.710 -39.265 49.396 1.00 88.44 C ANISOU 6 CG ASN A 52 11565 7648 14389 -589 2297 1166 C ATOM 7 OD1 ASN A 52 -34.095 -40.312 49.595 1.00 90.27 O ANISOU 7 OD1 ASN A 52 12081 7588 14628 -491 2323 1201 O ATOM 8 ND2 ASN A 52 -34.373 -38.118 49.972 1.00 87.17 N ANISOU 8 ND2 ASN A 52 11305 7793 14022 -389 2297 1226 N ATOM 9 N SER A 53 -36.270 -42.583 46.892 1.00117.02 N ANISOU 9 N SER A 53 15383 10345 18736 -1435 2208 792 N ATOM 10 CA SER A 53 -35.583 -43.478 45.968 1.00117.58 C ANISOU 10 CA SER A 53 15672 10159 18842 -1417 2082 573 C ATOM 11 C SER A 53 -35.751 -43.031 44.518 1.00116.89 C ANISOU 11 C SER A 53 15383 10256 18775 -1571 1851 269 C ATOM 12 O SER A 53 -35.250 -43.677 43.598 1.00117.33 O ANISOU 12 O SER A 53 15596 10135 18850 -1581 1735 47 O ATOM 13 CB SER A 53 -36.084 -44.914 46.138 1.00119.80 C ANISOU 13 CB SER A 53 16194 9968 19355 -1641 2218 638 C ATOM 14 OG SER A 53 -37.478 -45.000 45.902 1.00121.93 O ANISOU 14 OG SER A 53 16244 10225 19860 -2055 2260 638 O ATOM 15 N ASP A 54 -36.458 -41.923 44.323 1.00140.30 N ANISOU 15 N ASP A 54 18011 13572 21726 -1680 1787 264 N ATOM 16 CA ASP A 54 -36.666 -41.368 42.992 1.00140.06 C ANISOU 16 CA ASP A 54 17779 13756 21684 -1810 1557 6 C ATOM 17 C ASP A 54 -35.469 -40.515 42.584 1.00138.77 C ANISOU 17 C ASP A 54 17626 13847 21253 -1495 1425 -114 C ATOM 18 O ASP A 54 -35.307 -40.168 41.414 1.00139.31 O ANISOU 18 O ASP A 54 17618 14054 21259 -1541 1236 -345 O ATOM 19 CB ASP A 54 -37.950 -40.535 42.958 1.00142.99 C ANISOU 19 CB ASP A 54 17779 14390 22163 -2043 1540 65 C ATOM 20 CG ASP A 54 -38.322 -40.090 41.557 1.00142.97 C ANISOU 20 CG ASP A 54 17578 14579 22167 -2213 1287 -186 C ATOM 21 OD1 ASP A 54 -38.043 -40.841 40.599 1.00144.10 O ANISOU 21 OD1 ASP A 54 17877 14541 22334 -2312 1161 -408 O ATOM 22 OD2 ASP A 54 -38.895 -38.990 41.414 1.00141.20 O ANISOU 22 OD2 ASP A 54 17054 14680 21915 -2238 1214 -161 O ATOM 23 N LEU A 55 -34.630 -40.185 43.560 1.00 57.81 N ANISOU 23 N LEU A 55 7471 3655 10837 -1184 1526 45 N ATOM 24 CA LEU A 55 -33.450 -39.362 43.316 1.00 54.29 C ANISOU 24 CA LEU A 55 7025 3454 10148 -887 1422 -50 C ATOM 25 C LEU A 55 -32.207 -40.216 43.091 1.00 55.01 C ANISOU 25 C LEU A 55 7403 3327 10171 -670 1402 -161 C ATOM 26 O LEU A 55 -31.145 -39.701 42.740 1.00 52.97 O ANISOU 26 O LEU A 55 7151 3242 9732 -439 1313 -277 O ATOM 27 CB LEU A 55 -33.218 -38.391 44.478 1.00 52.14 C ANISOU 27 CB LEU A 55 6670 3416 9725 -672 1518 161 C ATOM 28 CG LEU A 55 -33.877 -37.011 44.397 1.00 49.92 C ANISOU 28 CG LEU A 55 6083 3492 9394 -737 1472 182 C ATOM 29 CD1 LEU A 55 -35.378 -37.118 44.175 1.00 51.69 C ANISOU 29 CD1 LEU A 55 6106 3695 9841 -1072 1492 213 C ATOM 30 CD2 LEU A 55 -33.575 -36.204 45.649 1.00 48.34 C ANISOU 30 CD2 LEU A 55 5864 3461 9042 -517 1592 385 C ATOM 31 N ASP A 56 -32.344 -41.522 43.296 1.00 75.00 N ANISOU 31 N ASP A 56 10167 5471 12858 -744 1495 -122 N ATOM 32 CA ASP A 56 -31.231 -42.444 43.114 1.00 75.33 C ANISOU 32 CA ASP A 56 10496 5260 12868 -528 1492 -219 C ATOM 33 C ASP A 56 -30.885 -42.600 41.639 1.00 75.35 C ANISOU 33 C ASP A 56 10508 5270 12852 -591 1332 -546 C ATOM 34 O ASP A 56 -31.724 -42.375 40.766 1.00 75.60 O ANISOU 34 O ASP A 56 10385 5390 12950 -875 1232 -685 O ATOM 35 CB ASP A 56 -31.562 -43.819 43.701 1.00 78.41 C ANISOU 35 CB ASP A 56 11153 5194 13445 -614 1640 -90 C ATOM 36 CG ASP A 56 -32.009 -43.748 45.147 1.00 78.98 C ANISOU 36 CG ASP A 56 11246 5237 13526 -573 1820 246 C ATOM 37 OD1 ASP A 56 -31.797 -42.700 45.790 1.00 76.82 O ANISOU 37 OD1 ASP A 56 10832 5277 13080 -396 1827 369 O ATOM 38 OD2 ASP A 56 -32.571 -44.747 45.642 1.00 81.48 O ANISOU 38 OD2 ASP A 56 11736 5209 14013 -726 1962 384 O ATOM 39 N VAL A 57 -29.641 -42.982 41.368 1.00103.56 N ANISOU 39 N VAL A 57 14260 8760 16327 -317 1309 -669 N ATOM 40 CA VAL A 57 -29.220 -43.322 40.016 1.00104.25 C ANISOU 40 CA VAL A 57 14421 8793 16395 -355 1197 -984 C ATOM 41 C VAL A 57 -28.625 -44.725 40.028 1.00105.60 C ANISOU 41 C VAL A 57 14925 8534 16666 -226 1274 -1041 C ATOM 42 O VAL A 57 -28.255 -45.239 41.085 1.00106.39 O ANISOU 42 O VAL A 57 15181 8451 16793 -18 1390 -834 O ATOM 43 CB VAL A 57 -28.179 -42.325 39.465 1.00100.31 C ANISOU 43 CB VAL A 57 13795 8652 15667 -129 1099 -1128 C ATOM 44 CG1 VAL A 57 -28.623 -40.892 39.720 1.00 98.84 C ANISOU 44 CG1 VAL A 57 13315 8868 15372 -182 1051 -1015 C ATOM 45 CG2 VAL A 57 -26.812 -42.588 40.073 1.00 99.91 C ANISOU 45 CG2 VAL A 57 13885 8554 15523 269 1161 -1081 C ATOM 46 N ASN A 58 -28.538 -45.348 38.858 1.00119.23 N ANISOU 46 N ASN A 58 16777 10089 18438 -341 1208 -1322 N ATOM 47 CA ASN A 58 -27.988 -46.695 38.771 1.00120.15 C ANISOU 47 CA ASN A 58 17225 9772 18654 -211 1284 -1406 C ATOM 48 C ASN A 58 -26.714 -46.754 37.935 1.00119.16 C ANISOU 48 C ASN A 58 17178 9709 18389 60 1236 -1664 C ATOM 49 O ASN A 58 -26.618 -47.530 36.984 1.00120.77 O ANISOU 49 O ASN A 58 17560 9686 18643 -21 1214 -1924 O ATOM 50 CB ASN A 58 -29.029 -47.679 38.233 1.00123.29 C ANISOU 50 CB ASN A 58 17778 9800 19269 -583 1291 -1514 C ATOM 51 CG ASN A 58 -28.722 -49.120 38.608 1.00127.19 C ANISOU 51 CG ASN A 58 18642 9771 19914 -468 1418 -1487 C ATOM 52 OD1 ASN A 58 -27.568 -49.486 38.829 1.00127.40 O ANISOU 52 OD1 ASN A 58 18816 9749 19843 -89 1445 -1488 O ATOM 53 ND2 ASN A 58 -29.761 -49.944 38.685 1.00130.32 N ANISOU 53 ND2 ASN A 58 19143 9915 20459 -779 1431 -1425 N ATOM 54 N THR A 59 -25.741 -45.922 38.291 1.00 89.04 N ANISOU 54 N THR A 59 13225 6209 14398 373 1226 -1601 N ATOM 55 CA THR A 59 -24.422 -45.993 37.679 1.00 88.62 C ANISOU 55 CA THR A 59 13230 6218 14226 676 1215 -1810 C ATOM 56 C THR A 59 -23.613 -47.060 38.405 1.00 90.13 C ANISOU 56 C THR A 59 13676 6064 14505 1002 1322 -1714 C ATOM 57 O THR A 59 -23.491 -47.026 39.629 1.00 89.80 O ANISOU 57 O THR A 59 13637 6009 14473 1171 1375 -1432 O ATOM 58 CB THR A 59 -23.687 -44.644 37.754 1.00 84.90 C ANISOU 58 CB THR A 59 12485 6235 13540 859 1158 -1790 C ATOM 59 OG1 THR A 59 -23.577 -44.231 39.121 1.00 84.05 O ANISOU 59 OG1 THR A 59 12293 6232 13409 1025 1199 -1486 O ATOM 60 CG2 THR A 59 -24.444 -43.582 36.971 1.00 84.58 C ANISOU 60 CG2 THR A 59 12217 6514 13405 560 1050 -1884 C ATOM 61 N ASP A 60 -23.073 -48.012 37.649 1.00152.25 N ANISOU 61 N ASP A 60 21769 13651 22427 1098 1352 -1948 N ATOM 62 CA ASP A 60 -22.358 -49.142 38.237 1.00154.87 C ANISOU 62 CA ASP A 60 22326 13734 22785 1393 1378 -1838 C ATOM 63 C ASP A 60 -21.125 -48.704 39.025 1.00153.17 C ANISOU 63 C ASP A 60 21997 13750 22452 1827 1379 -1699 C ATOM 64 O ASP A 60 -20.537 -47.658 38.750 1.00150.18 O ANISOU 64 O ASP A 60 21388 13731 21943 1936 1355 -1787 O ATOM 65 CB ASP A 60 -21.976 -50.163 37.162 1.00159.07 C ANISOU 65 CB ASP A 60 23059 14065 23314 1411 1339 -2114 C ATOM 66 CG ASP A 60 -21.079 -49.577 36.092 1.00157.67 C ANISOU 66 CG ASP A 60 22754 14188 22965 1545 1298 -2398 C ATOM 67 OD1 ASP A 60 -21.609 -48.977 35.133 1.00156.42 O ANISOU 67 OD1 ASP A 60 22506 14179 22748 1268 1259 -2595 O ATOM 68 OD2 ASP A 60 -19.844 -49.721 36.207 1.00158.11 O ANISOU 68 OD2 ASP A 60 22788 14345 22942 1922 1299 -2421 O ATOM 69 N ILE A 61 -20.749 -49.516 40.008 1.00 89.59 N ANISOU 69 N ILE A 61 14095 5500 14445 2059 1393 -1482 N ATOM 70 CA ILE A 61 -19.646 -49.194 40.909 1.00 89.12 C ANISOU 70 CA ILE A 61 13922 5657 14282 2454 1362 -1319 C ATOM 71 C ILE A 61 -18.310 -49.107 40.174 1.00 88.84 C ANISOU 71 C ILE A 61 13767 5838 14150 2741 1301 -1560 C ATOM 72 O ILE A 61 -17.500 -48.220 40.444 1.00 86.19 O ANISOU 72 O ILE A 61 13195 5860 13692 2950 1262 -1538 O ATOM 73 CB ILE A 61 -19.533 -50.223 42.060 1.00 93.30 C ANISOU 73 CB ILE A 61 14654 5908 14886 2627 1373 -1047 C ATOM 74 CG1 ILE A 61 -20.856 -50.333 42.825 1.00 93.89 C ANISOU 74 CG1 ILE A 61 14846 5778 15049 2331 1455 -794 C ATOM 75 CG2 ILE A 61 -18.404 -49.848 43.009 1.00 92.23 C ANISOU 75 CG2 ILE A 61 14376 6032 14636 3014 1312 -883 C ATOM 76 CD1 ILE A 61 -21.756 -51.460 42.355 1.00 96.94 C ANISOU 76 CD1 ILE A 61 15481 5747 15605 2039 1498 -860 C ATOM 77 N TYR A 62 -18.090 -50.028 39.240 1.00137.87 N ANISOU 77 N TYR A 62 20131 11838 20417 2739 1296 -1794 N ATOM 78 CA TYR A 62 -16.849 -50.063 38.473 1.00139.32 C ANISOU 78 CA TYR A 62 20205 12201 20528 2999 1260 -2038 C ATOM 79 C TYR A 62 -16.639 -48.784 37.667 1.00134.88 C ANISOU 79 C TYR A 62 19403 12051 19796 2922 1254 -2221 C ATOM 80 O TYR A 62 -15.511 -48.313 37.517 1.00133.86 O ANISOU 80 O TYR A 62 19064 12225 19572 3170 1226 -2309 O ATOM 81 CB TYR A 62 -16.820 -51.286 37.554 1.00148.75 C ANISOU 81 CB TYR A 62 21635 13069 21813 2972 1269 -2265 C ATOM 82 CG TYR A 62 -16.701 -52.598 38.297 1.00153.98 C ANISOU 82 CG TYR A 62 22513 13349 22645 3129 1276 -2108 C ATOM 83 CD1 TYR A 62 -16.078 -52.659 39.537 1.00154.40 C ANISOU 83 CD1 TYR A 62 22489 13451 22724 3416 1257 -1845 C ATOM 84 CD2 TYR A 62 -17.213 -53.772 37.762 1.00158.24 C ANISOU 84 CD2 TYR A 62 23335 13479 23309 2982 1297 -2218 C ATOM 85 CE1 TYR A 62 -15.967 -53.853 40.223 1.00158.42 C ANISOU 85 CE1 TYR A 62 23209 13610 23374 3561 1266 -1685 C ATOM 86 CE2 TYR A 62 -17.106 -54.972 38.441 1.00162.11 C ANISOU 86 CE2 TYR A 62 24033 13607 23955 3122 1311 -2067 C ATOM 87 CZ TYR A 62 -16.482 -55.006 39.671 1.00162.20 C ANISOU 87 CZ TYR A 62 23972 13672 23984 3416 1299 -1795 C ATOM 88 OH TYR A 62 -16.373 -56.197 40.352 1.00165.58 O ANISOU 88 OH TYR A 62 24622 13738 24554 3559 1314 -1630 O ATOM 89 N SER A 63 -17.731 -48.223 37.155 1.00 97.75 N ANISOU 89 N SER A 63 14705 7361 15074 2557 1280 -2276 N ATOM 90 CA SER A 63 -17.668 -46.959 36.433 1.00 94.66 C ANISOU 90 CA SER A 63 14083 7351 14534 2440 1278 -2423 C ATOM 91 C SER A 63 -17.292 -45.833 37.388 1.00 91.84 C ANISOU 91 C SER A 63 13465 7322 14110 2583 1267 -2222 C ATOM 92 O SER A 63 -16.505 -44.953 37.042 1.00 90.21 O ANISOU 92 O SER A 63 13037 7480 13758 2696 1252 -2318 O ATOM 93 CB SER A 63 -19.005 -46.652 35.758 1.00 95.56 C ANISOU 93 CB SER A 63 14223 7395 14692 1994 1279 -2520 C ATOM 94 OG SER A 63 -20.034 -46.482 36.716 1.00 94.63 O ANISOU 94 OG SER A 63 14100 7150 14707 1814 1296 -2273 O ATOM 95 N LYS A 64 -17.861 -45.871 38.590 1.00 87.88 N ANISOU 95 N LYS A 64 12999 6693 13697 2568 1277 -1936 N ATOM 96 CA LYS A 64 -17.556 -44.882 39.617 1.00 85.60 C ANISOU 96 CA LYS A 64 12500 6691 13331 2708 1259 -1721 C ATOM 97 C LYS A 64 -16.072 -44.901 39.962 1.00 86.24 C ANISOU 97 C LYS A 64 12452 6994 13319 3096 1191 -1722 C ATOM 98 O LYS A 64 -15.427 -43.857 40.007 1.00 84.59 O ANISOU 98 O LYS A 64 11987 7167 12987 3185 1157 -1749 O ATOM 99 CB LYS A 64 -18.378 -45.138 40.882 1.00 85.10 C ANISOU 99 CB LYS A 64 12553 6431 13348 2648 1280 -1397 C ATOM 100 CG LYS A 64 -19.881 -45.020 40.703 1.00 84.74 C ANISOU 100 CG LYS A 64 12538 6290 13367 2212 1285 -1348 C ATOM 101 CD LYS A 64 -20.596 -45.232 42.029 1.00 85.37 C ANISOU 101 CD LYS A 64 12713 6216 13507 2175 1327 -1012 C ATOM 102 CE LYS A 64 -22.105 -45.183 41.869 1.00 85.73 C ANISOU 102 CE LYS A 64 12771 6151 13650 1744 1350 -962 C ATOM 103 NZ LYS A 64 -22.569 -43.875 41.333 1.00 85.02 N ANISOU 103 NZ LYS A 64 12398 6457 13450 1505 1272 -1050 N ATOM 104 N VAL A 65 -15.540 -46.096 40.200 1.00 84.92 N ANISOU 104 N VAL A 65 12433 6586 13246 3299 1170 -1702 N ATOM 105 CA VAL A 65 -14.139 -46.258 40.576 1.00 85.74 C ANISOU 105 CA VAL A 65 12364 6860 13353 3631 1118 -1701 C ATOM 106 C VAL A 65 -13.199 -45.873 39.435 1.00 84.94 C ANISOU 106 C VAL A 65 12042 7017 13214 3676 1145 -2002 C ATOM 107 O VAL A 65 -12.178 -45.220 39.655 1.00 84.16 O ANISOU 107 O VAL A 65 11662 7238 13077 3808 1169 -1979 O ATOM 108 CB VAL A 65 -13.842 -47.704 41.025 1.00 89.29 C ANISOU 108 CB VAL A 65 13025 6949 13952 3816 1116 -1614 C ATOM 109 CG1 VAL A 65 -12.378 -47.857 41.406 1.00 91.01 C ANISOU 109 CG1 VAL A 65 13038 7344 14198 4143 1087 -1598 C ATOM 110 CG2 VAL A 65 -14.741 -48.090 42.189 1.00 89.91 C ANISOU 110 CG2 VAL A 65 13321 6777 14064 3754 1115 -1296 C ATOM 111 N LEU A 66 -13.552 -46.278 38.219 1.00 75.70 N ANISOU 111 N LEU A 66 11026 5706 12030 3543 1169 -2256 N ATOM 112 CA LEU A 66 -12.764 -45.942 37.037 1.00 75.72 C ANISOU 112 CA LEU A 66 10866 5971 11934 3538 1208 -2520 C ATOM 113 C LEU A 66 -12.686 -44.431 36.843 1.00 71.92 C ANISOU 113 C LEU A 66 10313 5874 11140 3442 1402 -2371 C ATOM 114 O LEU A 66 -11.596 -43.853 36.796 1.00 71.49 O ANISOU 114 O LEU A 66 9961 6107 11095 3537 1471 -2395 O ATOM 115 CB LEU A 66 -13.369 -46.596 35.793 1.00 77.34 C ANISOU 115 CB LEU A 66 11442 5944 11999 3424 1234 -2719 C ATOM 116 CG LEU A 66 -12.711 -46.271 34.451 1.00 77.53 C ANISOU 116 CG LEU A 66 11503 6181 11775 3417 1399 -2893 C ATOM 117 CD1 LEU A 66 -11.292 -46.815 34.399 1.00 80.35 C ANISOU 117 CD1 LEU A 66 11814 6554 12160 3664 1659 -2829 C ATOM 118 CD2 LEU A 66 -13.543 -46.813 33.299 1.00 78.84 C ANISOU 118 CD2 LEU A 66 11902 6098 11957 3166 1392 -3146 C ATOM 119 N VAL A 67 -13.853 -43.802 36.737 1.00 69.41 N ANISOU 119 N VAL A 67 10013 5569 10793 3203 1270 -2427 N ATOM 120 CA VAL A 67 -13.950 -42.358 36.550 1.00 65.88 C ANISOU 120 CA VAL A 67 9288 5500 10242 3017 1259 -2438 C ATOM 121 C VAL A 67 -13.272 -41.595 37.690 1.00 64.32 C ANISOU 121 C VAL A 67 8852 5573 10014 3188 1236 -2222 C ATOM 122 O VAL A 67 -12.643 -40.560 37.468 1.00 62.54 O ANISOU 122 O VAL A 67 8377 5723 9661 3156 1227 -2253 O ATOM 123 CB VAL A 67 -15.425 -41.918 36.399 1.00 63.87 C ANISOU 123 CB VAL A 67 9052 5148 10069 2655 1213 -2458 C ATOM 124 CG1 VAL A 67 -15.553 -40.407 36.446 1.00 60.11 C ANISOU 124 CG1 VAL A 67 8304 5071 9465 2505 1160 -2421 C ATOM 125 CG2 VAL A 67 -16.007 -42.462 35.103 1.00 65.32 C ANISOU 125 CG2 VAL A 67 9416 5145 10256 2423 1239 -2695 C ATOM 126 N THR A 68 -13.388 -42.121 38.906 1.00 65.26 N ANISOU 126 N THR A 68 9017 5491 10287 3324 1218 -2013 N ATOM 127 CA THR A 68 -12.734 -41.521 40.065 1.00 64.32 C ANISOU 127 CA THR A 68 8667 5630 10141 3471 1126 -1826 C ATOM 128 C THR A 68 -11.217 -41.563 39.917 1.00 65.87 C ANISOU 128 C THR A 68 8670 6046 10311 3662 1159 -1870 C ATOM 129 O THR A 68 -10.537 -40.558 40.126 1.00 64.28 O ANISOU 129 O THR A 68 8228 6211 9984 3670 1116 -1835 O ATOM 130 CB THR A 68 -13.125 -42.236 41.372 1.00 65.69 C ANISOU 130 CB THR A 68 8994 5562 10405 3600 1038 -1584 C ATOM 131 OG1 THR A 68 -14.550 -42.213 41.522 1.00 64.56 O ANISOU 131 OG1 THR A 68 9062 5197 10272 3400 1058 -1490 O ATOM 132 CG2 THR A 68 -12.479 -41.557 42.570 1.00 64.76 C ANISOU 132 CG2 THR A 68 8687 5735 10185 3743 949 -1377 C ATOM 133 N ALA A 69 -10.696 -42.732 39.554 1.00 69.20 N ANISOU 133 N ALA A 69 9195 6230 10868 3806 1226 -1955 N ATOM 134 CA ALA A 69 -9.263 -42.914 39.351 1.00 71.27 C ANISOU 134 CA ALA A 69 9286 6657 11135 4006 1271 -2006 C ATOM 135 C ALA A 69 -8.744 -41.970 38.273 1.00 69.74 C ANISOU 135 C ALA A 69 8936 6796 10765 3885 1353 -2163 C ATOM 136 O ALA A 69 -7.678 -41.367 38.420 1.00 69.65 O ANISOU 136 O ALA A 69 8676 7097 10691 3966 1329 -2144 O ATOM 137 CB ALA A 69 -8.961 -44.359 38.983 1.00 75.25 C ANISOU 137 CB ALA A 69 9955 6813 11825 4160 1348 -2103 C ATOM 138 N ILE A 70 -9.508 -41.846 37.191 1.00 84.02 N ANISOU 138 N ILE A 70 10903 8539 12484 3682 1421 -2321 N ATOM 139 CA ILE A 70 -9.168 -40.921 36.117 1.00 82.81 C ANISOU 139 CA ILE A 70 10626 8696 12144 3534 1459 -2476 C ATOM 140 C ILE A 70 -9.133 -39.485 36.636 1.00 79.80 C ANISOU 140 C ILE A 70 9993 8680 11649 3413 1354 -2375 C ATOM 141 O ILE A 70 -8.213 -38.725 36.327 1.00 79.14 O ANISOU 141 O ILE A 70 9690 8905 11474 3401 1371 -2413 O ATOM 142 CB ILE A 70 -10.168 -41.020 34.947 1.00 82.26 C ANISOU 142 CB ILE A 70 10778 8492 11988 3308 1482 -2663 C ATOM 143 CG1 ILE A 70 -10.142 -42.423 34.339 1.00 85.55 C ANISOU 143 CG1 ILE A 70 11473 8551 12484 3415 1587 -2787 C ATOM 144 CG2 ILE A 70 -9.855 -39.981 33.882 1.00 80.61 C ANISOU 144 CG2 ILE A 70 10419 8614 11597 3128 1503 -2808 C ATOM 145 CD1 ILE A 70 -11.140 -42.622 33.219 1.00 85.51 C ANISOU 145 CD1 ILE A 70 11698 8398 12397 3179 1565 -2989 C ATOM 146 N TYR A 71 -10.132 -39.128 37.437 1.00 75.04 N ANISOU 146 N TYR A 71 9428 8024 11058 3321 1255 -2245 N ATOM 147 CA TYR A 71 -10.227 -37.786 38.004 1.00 71.67 C ANISOU 147 CA TYR A 71 8795 7909 10528 3202 1161 -2146 C ATOM 148 C TYR A 71 -9.046 -37.471 38.913 1.00 71.59 C ANISOU 148 C TYR A 71 8564 8118 10519 3373 1108 -2022 C ATOM 149 O TYR A 71 -8.573 -36.338 38.952 1.00 68.88 O ANISOU 149 O TYR A 71 8012 8093 10065 3276 1069 -2017 O ATOM 150 CB TYR A 71 -11.534 -37.609 38.782 1.00 68.22 C ANISOU 150 CB TYR A 71 8457 7335 10126 3110 1080 -2021 C ATOM 151 CG TYR A 71 -12.761 -37.416 37.920 1.00 68.33 C ANISOU 151 CG TYR A 71 8589 7243 10130 2856 1084 -2155 C ATOM 152 CD1 TYR A 71 -12.694 -37.534 36.538 1.00 68.88 C ANISOU 152 CD1 TYR A 71 8714 7310 10146 2733 1149 -2372 C ATOM 153 CD2 TYR A 71 -13.988 -37.098 38.490 1.00 69.05 C ANISOU 153 CD2 TYR A 71 8718 7237 10282 2722 1020 -2069 C ATOM 154 CE1 TYR A 71 -13.815 -37.356 35.751 1.00 69.10 C ANISOU 154 CE1 TYR A 71 8831 7245 10178 2472 1135 -2503 C ATOM 155 CE2 TYR A 71 -15.114 -36.915 37.710 1.00 68.97 C ANISOU 155 CE2 TYR A 71 8791 7152 10261 2402 1019 -2125 C ATOM 156 CZ TYR A 71 -15.021 -37.043 36.341 1.00 68.94 C ANISOU 156 CZ TYR A 71 8832 7142 10221 2297 1067 -2372 C ATOM 157 OH TYR A 71 -16.140 -36.864 35.560 1.00 69.22 O ANISOU 157 OH TYR A 71 8949 7119 10231 1981 1039 -2424 O ATOM 158 N LEU A 72 -8.577 -38.476 39.646 1.00 63.43 N ANISOU 158 N LEU A 72 7580 6904 9615 3615 1093 -1928 N ATOM 159 CA LEU A 72 -7.449 -38.297 40.552 1.00 64.53 C ANISOU 159 CA LEU A 72 7516 7242 9761 3794 1007 -1820 C ATOM 160 C LEU A 72 -6.137 -38.199 39.781 1.00 66.18 C ANISOU 160 C LEU A 72 7542 7649 9953 3854 1080 -1956 C ATOM 161 O LEU A 72 -5.243 -37.435 40.152 1.00 65.99 O ANISOU 161 O LEU A 72 7282 7921 9869 3872 1013 -1928 O ATOM 162 CB LEU A 72 -7.385 -39.436 41.571 1.00 67.11 C ANISOU 162 CB LEU A 72 7965 7311 10225 4042 945 -1674 C ATOM 163 CG LEU A 72 -8.584 -39.563 42.513 1.00 65.94 C ANISOU 163 CG LEU A 72 8001 6966 10087 4007 867 -1503 C ATOM 164 CD1 LEU A 72 -8.356 -40.668 43.534 1.00 68.92 C ANISOU 164 CD1 LEU A 72 8504 7115 10567 4263 793 -1338 C ATOM 165 CD2 LEU A 72 -8.872 -38.238 43.204 1.00 62.88 C ANISOU 165 CD2 LEU A 72 7480 6865 9548 3875 771 -1404 C ATOM 166 N ALA A 73 -6.027 -38.977 38.708 1.00 66.69 N ANISOU 166 N ALA A 73 7725 7545 10071 3882 1221 -2109 N ATOM 167 CA ALA A 73 -4.855 -38.918 37.841 1.00 68.49 C ANISOU 167 CA ALA A 73 7803 7943 10280 3935 1323 -2250 C ATOM 168 C ALA A 73 -4.742 -37.535 37.209 1.00 65.95 C ANISOU 168 C ALA A 73 7320 7951 9788 3693 1327 -2322 C ATOM 169 O ALA A 73 -3.682 -36.907 37.240 1.00 66.44 O ANISOU 169 O ALA A 73 7140 8287 9817 3713 1314 -2333 O ATOM 170 CB ALA A 73 -4.936 -39.989 36.767 1.00 70.86 C ANISOU 170 CB ALA A 73 8308 7977 10639 3989 1484 -2409 C ATOM 171 N LEU A 74 -5.849 -37.064 36.644 1.00 63.46 N ANISOU 171 N LEU A 74 7138 7599 9374 3458 1337 -2372 N ATOM 172 CA LEU A 74 -5.906 -35.731 36.056 1.00 60.99 C ANISOU 172 CA LEU A 74 6701 7565 8906 3207 1331 -2427 C ATOM 173 C LEU A 74 -5.707 -34.664 37.127 1.00 59.08 C ANISOU 173 C LEU A 74 6262 7559 8627 3158 1199 -2284 C ATOM 174 O LEU A 74 -5.223 -33.568 36.843 1.00 58.02 O ANISOU 174 O LEU A 74 5956 7693 8396 3013 1194 -2316 O ATOM 175 CB LEU A 74 -7.242 -35.521 35.343 1.00 58.92 C ANISOU 175 CB LEU A 74 6629 7192 8567 2981 1338 -2496 C ATOM 176 CG LEU A 74 -7.507 -36.428 34.140 1.00 60.78 C ANISOU 176 CG LEU A 74 7079 7215 8801 2979 1453 -2673 C ATOM 177 CD1 LEU A 74 -8.956 -36.325 33.697 1.00 59.00 C ANISOU 177 CD1 LEU A 74 7040 6846 8530 2765 1411 -2731 C ATOM 178 CD2 LEU A 74 -6.568 -36.083 32.996 1.00 61.98 C ANISOU 178 CD2 LEU A 74 7134 7564 8851 2935 1567 -2817 C ATOM 179 N PHE A 75 -6.081 -34.996 38.359 1.00 62.89 N ANISOU 179 N PHE A 75 6786 7931 9180 3275 1094 -2129 N ATOM 180 CA PHE A 75 -5.904 -34.089 39.486 1.00 61.43 C ANISOU 180 CA PHE A 75 6446 7950 8946 3251 959 -1997 C ATOM 181 C PHE A 75 -4.427 -33.875 39.780 1.00 63.37 C ANISOU 181 C PHE A 75 6451 8426 9203 3375 924 -2008 C ATOM 182 O PHE A 75 -3.955 -32.742 39.802 1.00 62.26 O ANISOU 182 O PHE A 75 6132 8552 8973 3237 885 -2027 O ATOM 183 CB PHE A 75 -6.617 -34.618 40.733 1.00 61.30 C ANISOU 183 CB PHE A 75 6553 7747 8990 3374 861 -1827 C ATOM 184 CG PHE A 75 -6.325 -33.830 41.979 1.00 60.45 C ANISOU 184 CG PHE A 75 6306 7845 8816 3394 716 -1695 C ATOM 185 CD1 PHE A 75 -6.979 -32.636 42.229 1.00 57.52 C ANISOU 185 CD1 PHE A 75 5903 7619 8333 3184 670 -1658 C ATOM 186 CD2 PHE A 75 -5.401 -34.288 42.905 1.00 62.82 C ANISOU 186 CD2 PHE A 75 6517 8193 9160 3630 620 -1614 C ATOM 187 CE1 PHE A 75 -6.713 -31.910 43.375 1.00 56.94 C ANISOU 187 CE1 PHE A 75 5724 7729 8184 3202 541 -1554 C ATOM 188 CE2 PHE A 75 -5.131 -33.566 44.052 1.00 62.28 C ANISOU 188 CE2 PHE A 75 6338 8323 9005 3650 473 -1509 C ATOM 189 CZ PHE A 75 -5.788 -32.376 44.288 1.00 59.33 C ANISOU 189 CZ PHE A 75 5946 8086 8511 3434 439 -1485 C ATOM 190 N VAL A 76 -3.698 -34.964 40.006 1.00 62.50 N ANISOU 190 N VAL A 76 6335 8202 9212 3635 937 -2001 N ATOM 191 CA VAL A 76 -2.275 -34.852 40.317 1.00 64.83 C ANISOU 191 CA VAL A 76 6384 8713 9537 3781 893 -2014 C ATOM 192 C VAL A 76 -1.465 -34.320 39.133 1.00 65.41 C ANISOU 192 C VAL A 76 6302 8980 9570 3667 1018 -2176 C ATOM 193 O VAL A 76 -0.617 -33.442 39.304 1.00 65.54 O ANISOU 193 O VAL A 76 6087 9274 9541 3608 969 -2197 O ATOM 194 CB VAL A 76 -1.678 -36.181 40.844 1.00 68.45 C ANISOU 194 CB VAL A 76 6866 8996 10145 4109 872 -1961 C ATOM 195 CG1 VAL A 76 -2.173 -36.461 42.255 1.00 68.24 C ANISOU 195 CG1 VAL A 76 6932 8870 10127 4230 707 -1772 C ATOM 196 CG2 VAL A 76 -2.012 -37.339 39.918 1.00 70.02 C ANISOU 196 CG2 VAL A 76 7270 8891 10442 4185 1034 -2050 C ATOM 197 N VAL A 77 -1.740 -34.835 37.938 1.00 65.92 N ANISOU 197 N VAL A 77 6506 8898 9643 3629 1179 -2297 N ATOM 198 CA VAL A 77 -1.037 -34.388 36.737 1.00 66.69 C ANISOU 198 CA VAL A 77 6493 9162 9686 3524 1317 -2449 C ATOM 199 C VAL A 77 -1.280 -32.903 36.475 1.00 63.78 C ANISOU 199 C VAL A 77 6037 9026 9171 3224 1287 -2463 C ATOM 200 O VAL A 77 -0.345 -32.147 36.200 1.00 64.47 O ANISOU 200 O VAL A 77 5914 9357 9224 3153 1314 -2520 O ATOM 201 CB VAL A 77 -1.446 -35.213 35.497 1.00 67.73 C ANISOU 201 CB VAL A 77 6841 9077 9818 3528 1488 -2580 C ATOM 202 CG1 VAL A 77 -0.924 -34.563 34.223 1.00 68.05 C ANISOU 202 CG1 VAL A 77 6801 9301 9753 3371 1626 -2728 C ATOM 203 CG2 VAL A 77 -0.937 -36.641 35.617 1.00 71.34 C ANISOU 203 CG2 VAL A 77 7358 9315 10432 3833 1551 -2595 C ATOM 204 N GLY A 78 -2.538 -32.490 36.579 1.00113.37 N ANISOU 204 N GLY A 78 12478 15219 15376 3051 1235 -2409 N ATOM 205 CA GLY A 78 -2.908 -31.107 36.345 1.00110.49 C ANISOU 205 CA GLY A 78 12063 15035 14882 2771 1207 -2411 C ATOM 206 C GLY A 78 -2.373 -30.147 37.390 1.00109.47 C ANISOU 206 C GLY A 78 11733 15127 14733 2735 1076 -2327 C ATOM 207 O GLY A 78 -1.859 -29.080 37.055 1.00108.96 O ANISOU 207 O GLY A 78 11525 15277 14598 2567 1092 -2377 O ATOM 208 N THR A 79 -2.497 -30.521 38.660 1.00 75.16 N ANISOU 208 N THR A 79 7391 10724 10443 2892 946 -2205 N ATOM 209 CA THR A 79 -2.052 -29.666 39.756 1.00 74.84 C ANISOU 209 CA THR A 79 7184 10887 10365 2872 802 -2134 C ATOM 210 C THR A 79 -0.533 -29.530 39.799 1.00 76.96 C ANISOU 210 C THR A 79 7192 11374 10674 2964 795 -2205 C ATOM 211 O THR A 79 -0.010 -28.435 40.004 1.00 75.85 O ANISOU 211 O THR A 79 6884 11463 10472 2821 746 -2234 O ATOM 212 CB THR A 79 -2.559 -30.167 41.122 1.00 72.98 C ANISOU 212 CB THR A 79 7034 10537 10159 3037 662 -1984 C ATOM 213 OG1 THR A 79 -2.316 -31.574 41.238 1.00 75.83 O ANISOU 213 OG1 THR A 79 7464 10707 10640 3305 682 -1960 O ATOM 214 CG2 THR A 79 -4.049 -29.902 41.266 1.00 69.58 C ANISOU 214 CG2 THR A 79 6806 9958 9672 2895 655 -1907 C ATOM 215 N VAL A 80 0.172 -30.641 39.609 1.00 75.89 N ANISOU 215 N VAL A 80 7020 11164 10652 3202 847 -2237 N ATOM 216 CA VAL A 80 1.629 -30.602 39.567 1.00 78.95 C ANISOU 216 CA VAL A 80 7141 11757 11099 3308 855 -2310 C ATOM 217 C VAL A 80 2.106 -29.832 38.338 1.00 78.97 C ANISOU 217 C VAL A 80 7042 11913 11051 3099 1006 -2447 C ATOM 218 O VAL A 80 2.977 -28.967 38.437 1.00 79.77 O ANISOU 218 O VAL A 80 6914 12261 11133 3007 980 -2496 O ATOM 219 CB VAL A 80 2.245 -32.017 39.575 1.00 82.47 C ANISOU 219 CB VAL A 80 7578 12066 11691 3627 897 -2314 C ATOM 220 CG1 VAL A 80 3.729 -31.958 39.245 1.00 85.82 C ANISOU 220 CG1 VAL A 80 7715 12707 12186 3718 949 -2413 C ATOM 221 CG2 VAL A 80 2.022 -32.685 40.923 1.00 83.11 C ANISOU 221 CG2 VAL A 80 7722 12036 11820 3849 725 -2166 C ATOM 222 N GLY A 81 1.516 -30.142 37.187 1.00107.14 N ANISOU 222 N GLY A 81 10786 15331 14589 3021 1162 -2511 N ATOM 223 CA GLY A 81 1.871 -29.487 35.941 1.00107.29 C ANISOU 223 CA GLY A 81 10752 15472 14540 2830 1317 -2633 C ATOM 224 C GLY A 81 1.690 -27.981 35.979 1.00105.53 C ANISOU 224 C GLY A 81 10465 15428 14204 2537 1269 -2626 C ATOM 225 O GLY A 81 2.634 -27.230 35.732 1.00106.83 O ANISOU 225 O GLY A 81 10422 15808 14358 2441 1310 -2694 O ATOM 226 N ASN A 82 0.477 -27.539 36.297 1.00 94.36 N ANISOU 226 N ASN A 82 9225 13915 12711 2398 1190 -2545 N ATOM 227 CA ASN A 82 0.167 -26.113 36.350 1.00 91.72 C ANISOU 227 CA ASN A 82 8865 13713 12272 2126 1149 -2531 C ATOM 228 C ASN A 82 0.841 -25.399 37.519 1.00 91.91 C ANISOU 228 C ASN A 82 8687 13928 12307 2124 1007 -2498 C ATOM 229 O ASN A 82 1.155 -24.212 37.432 1.00 92.28 O ANISOU 229 O ASN A 82 8627 14141 12293 1918 1011 -2538 O ATOM 230 CB ASN A 82 -1.346 -25.891 36.400 1.00 86.72 C ANISOU 230 CB ASN A 82 8468 12917 11566 2002 1108 -2452 C ATOM 231 CG ASN A 82 -2.052 -26.405 35.161 1.00 86.45 C ANISOU 231 CG ASN A 82 8627 12725 11495 1956 1237 -2509 C ATOM 232 OD1 ASN A 82 -2.141 -25.710 34.149 1.00 85.00 O ANISOU 232 OD1 ASN A 82 8471 12603 11221 1761 1331 -2573 O ATOM 233 ND2 ASN A 82 -2.563 -27.629 35.236 1.00 86.96 N ANISOU 233 ND2 ASN A 82 8835 12582 11623 2133 1240 -2492 N ATOM 234 N GLY A 83 1.056 -26.125 38.611 1.00 62.55 N ANISOU 234 N GLY A 83 4926 10181 8660 2353 881 -2429 N ATOM 235 CA GLY A 83 1.724 -25.568 39.774 1.00 63.35 C ANISOU 235 CA GLY A 83 4838 10472 8761 2383 727 -2408 C ATOM 236 C GLY A 83 3.179 -25.260 39.482 1.00 66.36 C ANISOU 236 C GLY A 83 4937 11083 9194 2384 769 -2519 C ATOM 237 O GLY A 83 3.657 -24.150 39.736 1.00 66.39 O ANISOU 237 O GLY A 83 4789 11284 9153 2216 725 -2566 O ATOM 238 N VAL A 84 3.885 -26.249 38.943 1.00 65.34 N ANISOU 238 N VAL A 84 4736 10925 9166 2576 865 -2567 N ATOM 239 CA VAL A 84 5.275 -26.069 38.544 1.00 68.60 C ANISOU 239 CA VAL A 84 4868 11549 9646 2593 936 -2676 C ATOM 240 C VAL A 84 5.366 -25.038 37.421 1.00 67.87 C ANISOU 240 C VAL A 84 4758 11551 9481 2301 1095 -2769 C ATOM 241 O VAL A 84 6.309 -24.247 37.369 1.00 69.55 O ANISOU 241 O VAL A 84 4738 11983 9706 2187 1116 -2846 O ATOM 242 CB VAL A 84 5.917 -27.405 38.108 1.00 71.84 C ANISOU 242 CB VAL A 84 5227 11884 10187 2876 1032 -2707 C ATOM 243 CG1 VAL A 84 7.303 -27.177 37.527 1.00 75.30 C ANISOU 243 CG1 VAL A 84 5371 12544 10697 2875 1144 -2826 C ATOM 244 CG2 VAL A 84 5.989 -28.365 39.286 1.00 73.16 C ANISOU 244 CG2 VAL A 84 5387 11975 10435 3174 865 -2608 C ATOM 245 N THR A 85 4.370 -25.039 36.538 1.00 94.42 N ANISOU 245 N THR A 85 8366 14744 12765 2179 1203 -2759 N ATOM 246 CA THR A 85 4.294 -24.055 35.461 1.00 94.46 C ANISOU 246 CA THR A 85 8398 14813 12678 1901 1346 -2827 C ATOM 247 C THR A 85 4.272 -22.635 36.019 1.00 93.06 C ANISOU 247 C THR A 85 8146 14781 12433 1660 1255 -2817 C ATOM 248 O THR A 85 5.080 -21.795 35.624 1.00 94.57 O ANISOU 248 O THR A 85 8166 15148 12617 1499 1333 -2897 O ATOM 249 CB THR A 85 3.050 -24.268 34.577 1.00 90.16 C ANISOU 249 CB THR A 85 8151 14059 12045 1815 1433 -2803 C ATOM 250 OG1 THR A 85 3.096 -25.575 33.989 1.00 91.78 O ANISOU 250 OG1 THR A 85 8436 14128 12308 2026 1535 -2839 O ATOM 251 CG2 THR A 85 2.995 -23.225 33.472 1.00 89.68 C ANISOU 251 CG2 THR A 85 8125 14072 11878 1536 1571 -2861 C ATOM 252 N LEU A 86 3.350 -22.377 36.942 1.00100.36 N ANISOU 252 N LEU A 86 9199 15624 13309 1636 1102 -2723 N ATOM 253 CA LEU A 86 3.269 -21.076 37.602 1.00 99.37 C ANISOU 253 CA LEU A 86 9022 15616 13119 1431 1009 -2716 C ATOM 254 C LEU A 86 4.561 -20.750 38.338 1.00102.60 C ANISOU 254 C LEU A 86 9133 16260 13588 1469 929 -2784 C ATOM 255 O LEU A 86 5.007 -19.602 38.347 1.00103.19 O ANISOU 255 O LEU A 86 9090 16487 13630 1252 942 -2848 O ATOM 256 CB LEU A 86 2.094 -21.034 38.581 1.00 92.78 C ANISOU 256 CB LEU A 86 8367 14654 12232 1457 861 -2602 C ATOM 257 CG LEU A 86 0.723 -20.684 38.005 1.00 89.67 C ANISOU 257 CG LEU A 86 8236 14081 11753 1305 916 -2540 C ATOM 258 CD1 LEU A 86 -0.319 -20.627 39.108 1.00 87.61 C ANISOU 258 CD1 LEU A 86 8111 13721 11457 1346 774 -2429 C ATOM 259 CD2 LEU A 86 0.783 -19.363 37.257 1.00 89.34 C ANISOU 259 CD2 LEU A 86 8189 14121 11636 1012 1014 -2595 C ATOM 260 N PHE A 87 5.156 -21.769 38.952 1.00104.72 N ANISOU 260 N PHE A 87 9284 16555 13951 1744 845 -2770 N ATOM 261 CA PHE A 87 6.397 -21.603 39.698 1.00108.39 C ANISOU 261 CA PHE A 87 9450 17251 14485 1818 746 -2829 C ATOM 262 C PHE A 87 7.508 -21.059 38.801 1.00110.91 C ANISOU 262 C PHE A 87 9545 17747 14850 1674 903 -2954 C ATOM 263 O PHE A 87 8.046 -19.973 39.045 1.00111.53 O ANISOU 263 O PHE A 87 9465 18003 14908 1474 879 -3020 O ATOM 264 CB PHE A 87 6.822 -22.937 40.315 1.00110.27 C ANISOU 264 CB PHE A 87 9616 17458 14825 2168 652 -2782 C ATOM 265 CG PHE A 87 7.605 -22.798 41.589 1.00113.33 C ANISOU 265 CG PHE A 87 9784 18037 15240 2279 447 -2784 C ATOM 266 CD1 PHE A 87 6.954 -22.668 42.805 1.00112.09 C ANISOU 266 CD1 PHE A 87 9738 17851 15001 2319 254 -2698 C ATOM 267 CD2 PHE A 87 8.990 -22.805 41.574 1.00117.90 C ANISOU 267 CD2 PHE A 87 10042 18833 15922 2349 445 -2871 C ATOM 268 CE1 PHE A 87 7.668 -22.542 43.981 1.00114.15 C ANISOU 268 CE1 PHE A 87 9808 18298 15266 2426 54 -2703 C ATOM 269 CE2 PHE A 87 9.711 -22.679 42.747 1.00120.02 C ANISOU 269 CE2 PHE A 87 10102 19289 16211 2452 238 -2874 C ATOM 270 CZ PHE A 87 9.049 -22.548 43.952 1.00118.09 C ANISOU 270 CZ PHE A 87 9987 19016 15868 2491 36 -2791 C ATOM 271 N THR A 88 7.837 -21.810 37.754 1.00130.60 N ANISOU 271 N THR A 88 12031 20187 17403 1769 1076 -2988 N ATOM 272 CA THR A 88 8.904 -21.414 36.842 1.00132.60 C ANISOU 272 CA THR A 88 12072 20605 17703 1657 1252 -3101 C ATOM 273 C THR A 88 8.585 -20.123 36.087 1.00131.04 C ANISOU 273 C THR A 88 11958 20430 17399 1306 1373 -3138 C ATOM 274 O THR A 88 9.468 -19.294 35.883 1.00133.31 O ANISOU 274 O THR A 88 12035 20905 17709 1134 1439 -3222 O ATOM 275 CB THR A 88 9.277 -22.542 35.848 1.00132.04 C ANISOU 275 CB THR A 88 11997 20464 17709 1851 1432 -3134 C ATOM 276 OG1 THR A 88 10.292 -22.076 34.951 1.00134.93 O ANISOU 276 OG1 THR A 88 12159 21000 18109 1725 1622 -3241 O ATOM 277 CG2 THR A 88 8.066 -22.987 35.045 1.00129.56 C ANISOU 277 CG2 THR A 88 12022 19899 17306 1839 1526 -3085 C ATOM 278 N LEU A 89 7.326 -19.948 35.687 1.00126.70 N ANISOU 278 N LEU A 89 11712 19689 16739 1199 1400 -3073 N ATOM 279 CA LEU A 89 6.918 -18.738 34.977 1.00125.51 C ANISOU 279 CA LEU A 89 11671 19534 16481 881 1507 -3089 C ATOM 280 C LEU A 89 7.089 -17.500 35.850 1.00125.13 C ANISOU 280 C LEU A 89 11524 19612 16407 683 1393 -3106 C ATOM 281 O LEU A 89 7.491 -16.441 35.368 1.00125.81 O ANISOU 281 O LEU A 89 11545 19795 16463 430 1500 -3166 O ATOM 282 CB LEU A 89 5.472 -18.841 34.488 1.00120.98 C ANISOU 282 CB LEU A 89 11434 18730 15801 832 1526 -3004 C ATOM 283 CG LEU A 89 5.219 -19.693 33.242 1.00121.85 C ANISOU 283 CG LEU A 89 11685 18720 15892 915 1692 -3016 C ATOM 284 CD1 LEU A 89 3.751 -19.637 32.846 1.00117.88 C ANISOU 284 CD1 LEU A 89 11498 18012 15279 833 1684 -2936 C ATOM 285 CD2 LEU A 89 6.108 -19.246 32.091 1.00124.98 C ANISOU 285 CD2 LEU A 89 11967 19245 16276 777 1910 -3111 C ATOM 286 N ALA A 90 6.782 -17.640 37.135 1.00138.75 N ANISOU 286 N ALA A 90 13250 21331 18139 796 1184 -3056 N ATOM 287 CA ALA A 90 6.974 -16.548 38.080 1.00138.68 C ANISOU 287 CA ALA A 90 13144 21448 18101 634 1064 -3088 C ATOM 288 C ALA A 90 8.459 -16.321 38.332 1.00142.66 C ANISOU 288 C ALA A 90 13301 22203 18701 623 1058 -3197 C ATOM 289 O ALA A 90 8.894 -15.191 38.556 1.00143.56 O ANISOU 289 O ALA A 90 13302 22445 18799 389 1060 -3267 O ATOM 290 CB ALA A 90 6.249 -16.834 39.385 1.00145.23 C ANISOU 290 CB ALA A 90 14072 22213 18897 779 848 -3007 C ATOM 291 N ARG A 91 9.236 -17.400 38.288 1.00163.77 N ANISOU 291 N ARG A 91 15802 24939 21483 875 1055 -3212 N ATOM 292 CA ARG A 91 10.675 -17.304 38.518 1.00167.96 C ANISOU 292 CA ARG A 91 15974 25717 22127 896 1046 -3310 C ATOM 293 C ARG A 91 11.446 -16.803 37.295 1.00170.28 C ANISOU 293 C ARG A 91 16134 26106 22457 705 1289 -3398 C ATOM 294 O ARG A 91 12.614 -16.428 37.405 1.00173.78 O ANISOU 294 O ARG A 91 16273 26766 22990 639 1306 -3488 O ATOM 295 CB ARG A 91 11.241 -18.646 38.992 1.00160.27 C ANISOU 295 CB ARG A 91 14850 24778 21266 1257 949 -3285 C ATOM 296 CG ARG A 91 10.805 -19.039 40.394 1.00159.15 C ANISOU 296 CG ARG A 91 14766 24607 21096 1443 688 -3207 C ATOM 297 CD ARG A 91 11.195 -17.979 41.412 1.00159.92 C ANISOU 297 CD ARG A 91 14710 24891 21159 1282 526 -3262 C ATOM 298 NE ARG A 91 10.726 -18.310 42.754 1.00158.93 N ANISOU 298 NE ARG A 91 14659 24745 20981 1456 280 -3186 N ATOM 299 CZ ARG A 91 11.432 -18.999 43.645 1.00161.75 C ANISOU 299 CZ ARG A 91 14824 25226 21406 1709 103 -3173 C ATOM 300 NH1 ARG A 91 12.647 -19.433 43.338 1.00165.75 N ANISOU 300 NH1 ARG A 91 15036 25888 22054 1821 144 -3233 N ATOM 301 NH2 ARG A 91 10.924 -19.255 44.843 1.00160.78 N ANISOU 301 NH2 ARG A 91 14805 25076 21209 1857 -114 -3093 N ATOM 302 N LYS A 92 10.796 -16.797 36.134 1.00134.07 N ANISOU 302 N LYS A 92 11774 21366 17801 616 1475 -3372 N ATOM 303 CA LYS A 92 11.429 -16.302 34.913 1.00136.22 C ANISOU 303 CA LYS A 92 11961 21716 18082 430 1723 -3444 C ATOM 304 C LYS A 92 11.634 -14.792 34.967 1.00136.47 C ANISOU 304 C LYS A 92 11942 21843 18068 79 1758 -3494 C ATOM 305 O LYS A 92 12.218 -14.202 34.057 1.00138.58 O ANISOU 305 O LYS A 92 12124 22190 18341 -114 1962 -3552 O ATOM 306 CB LYS A 92 10.608 -16.675 33.675 1.00126.79 C ANISOU 306 CB LYS A 92 11049 20329 16797 424 1899 -3398 C ATOM 307 CG LYS A 92 10.678 -18.144 33.292 1.00127.78 C ANISOU 307 CG LYS A 92 11188 20378 16984 739 1947 -3385 C ATOM 308 CD LYS A 92 12.109 -18.590 33.044 1.00132.49 C ANISOU 308 CD LYS A 92 11449 21171 17722 864 2056 -3475 C ATOM 309 CE LYS A 92 12.186 -20.091 32.811 1.00133.67 C ANISOU 309 CE LYS A 92 11615 21230 17945 1208 2090 -3462 C ATOM 310 NZ LYS A 92 11.343 -20.524 31.662 1.00131.98 N ANISOU 310 NZ LYS A 92 11703 20820 17625 1207 2255 -3441 N ATOM 311 N SER A 100 8.297 -13.163 27.129 1.00118.63 N ANISOU 311 N SER A 100 11109 18901 15064 -764 2934 -3301 N ATOM 312 CA SER A 100 7.814 -13.046 28.500 1.00116.64 C ANISOU 312 CA SER A 100 10841 18607 14871 -716 2679 -3264 C ATOM 313 C SER A 100 6.418 -12.436 28.544 1.00113.10 C ANISOU 313 C SER A 100 10702 17973 14299 -838 2594 -3159 C ATOM 314 O SER A 100 5.743 -12.480 29.572 1.00112.15 O ANISOU 314 O SER A 100 10634 17777 14201 -763 2392 -3111 O ATOM 315 CB SER A 100 8.781 -12.209 29.340 1.00116.13 C ANISOU 315 CB SER A 100 10506 18712 14907 -857 2637 -3328 C ATOM 316 OG SER A 100 10.057 -12.822 29.411 1.00120.90 O ANISOU 316 OG SER A 100 10794 19498 15644 -721 2692 -3420 O ATOM 317 N ARG A 101 5.994 -11.866 27.422 1.00129.03 N ANISOU 317 N ARG A 101 12922 19923 16181 -1019 2754 -3119 N ATOM 318 CA ARG A 101 4.675 -11.255 27.323 1.00125.56 C ANISOU 318 CA ARG A 101 12777 19311 15620 -1133 2693 -3012 C ATOM 319 C ARG A 101 3.582 -12.316 27.373 1.00121.53 C ANISOU 319 C ARG A 101 12442 18655 15079 -911 2572 -2955 C ATOM 320 O ARG A 101 2.517 -12.100 27.950 1.00119.32 O ANISOU 320 O ARG A 101 12313 18252 14773 -910 2425 -2874 O ATOM 321 CB ARG A 101 4.560 -10.443 26.032 1.00122.85 C ANISOU 321 CB ARG A 101 12610 18940 15129 -1364 2902 -2976 C ATOM 322 CG ARG A 101 3.232 -9.727 25.860 1.00120.46 C ANISOU 322 CG ARG A 101 12611 18464 14694 -1483 2851 -2856 C ATOM 323 CD ARG A 101 3.163 -9.031 24.514 1.00122.25 C ANISOU 323 CD ARG A 101 13025 18667 14759 -1688 3063 -2810 C ATOM 324 NE ARG A 101 4.248 -8.071 24.343 1.00125.89 N ANISOU 324 NE ARG A 101 13348 19238 15248 -1915 3217 -2853 N ATOM 325 CZ ARG A 101 4.493 -7.413 23.214 1.00128.63 C ANISOU 325 CZ ARG A 101 13808 19594 15472 -2108 3434 -2825 C ATOM 326 NH1 ARG A 101 3.728 -7.613 22.150 1.00128.13 N ANISOU 326 NH1 ARG A 101 14004 19446 15234 -2094 3513 -2754 N ATOM 327 NH2 ARG A 101 5.502 -6.556 23.148 1.00131.45 N ANISOU 327 NH2 ARG A 101 14024 20047 15874 -2319 3571 -2866 N ATOM 328 N VAL A 102 3.857 -13.467 26.766 1.00108.14 N ANISOU 328 N VAL A 102 10725 16972 13391 -725 2644 -3003 N ATOM 329 CA VAL A 102 2.896 -14.563 26.733 1.00105.25 C ANISOU 329 CA VAL A 102 10523 16464 13003 -519 2549 -2966 C ATOM 330 C VAL A 102 2.882 -15.342 28.046 1.00104.13 C ANISOU 330 C VAL A 102 10256 16307 13002 -296 2351 -2965 C ATOM 331 O VAL A 102 1.968 -16.127 28.301 1.00102.58 O ANISOU 331 O VAL A 102 10197 15974 12804 -143 2240 -2918 O ATOM 332 CB VAL A 102 3.180 -15.530 25.568 1.00104.86 C ANISOU 332 CB VAL A 102 10525 16419 12900 -402 2713 -3030 C ATOM 333 CG1 VAL A 102 2.986 -14.823 24.235 1.00106.16 C ANISOU 333 CG1 VAL A 102 10874 16577 12885 -608 2895 -3013 C ATOM 334 CG2 VAL A 102 4.586 -16.096 25.678 1.00108.09 C ANISOU 334 CG2 VAL A 102 10652 16984 13434 -277 2806 -3134 C ATOM 335 N ASP A 103 3.895 -15.116 28.878 1.00111.19 N ANISOU 335 N ASP A 103 10892 17343 14012 -285 2307 -3015 N ATOM 336 CA ASP A 103 3.991 -15.792 30.168 1.00111.36 C ANISOU 336 CA ASP A 103 10786 17370 14153 -74 2118 -3010 C ATOM 337 C ASP A 103 2.857 -15.383 31.105 1.00107.37 C ANISOU 337 C ASP A 103 10425 16748 13620 -104 1932 -2915 C ATOM 338 O ASP A 103 2.481 -16.136 32.002 1.00106.62 O ANISOU 338 O ASP A 103 10334 16591 13585 91 1778 -2876 O ATOM 339 CB ASP A 103 5.345 -15.519 30.826 1.00123.13 C ANISOU 339 CB ASP A 103 11961 19063 15758 -76 2108 -3090 C ATOM 340 CG ASP A 103 6.499 -16.149 30.070 1.00127.19 C ANISOU 340 CG ASP A 103 12293 19699 16334 22 2278 -3182 C ATOM 341 OD1 ASP A 103 6.249 -17.058 29.250 1.00127.90 O ANISOU 341 OD1 ASP A 103 12502 19701 16391 156 2373 -3186 O ATOM 342 OD2 ASP A 103 7.657 -15.741 30.302 1.00130.12 O ANISOU 342 OD2 ASP A 103 12398 20254 16788 -34 2320 -3255 O ATOM 343 N TYR A 104 2.319 -14.187 30.892 1.00124.08 N ANISOU 343 N TYR A 104 12668 18831 15648 -343 1960 -2872 N ATOM 344 CA TYR A 104 1.193 -13.706 31.684 1.00121.61 C ANISOU 344 CA TYR A 104 12503 18403 15302 -382 1813 -2782 C ATOM 345 C TYR A 104 -0.095 -14.417 31.281 1.00118.38 C ANISOU 345 C TYR A 104 12330 17813 14836 -278 1780 -2700 C ATOM 346 O TYR A 104 -0.924 -14.749 32.130 1.00115.89 O ANISOU 346 O TYR A 104 12087 17402 14546 -168 1633 -2631 O ATOM 347 CB TYR A 104 1.040 -12.191 31.537 1.00121.63 C ANISOU 347 CB TYR A 104 12569 18414 15232 -666 1872 -2764 C ATOM 348 CG TYR A 104 2.146 -11.403 32.203 1.00124.59 C ANISOU 348 CG TYR A 104 12719 18950 15670 -785 1870 -2848 C ATOM 349 CD1 TYR A 104 2.789 -11.892 33.333 1.00126.40 C ANISOU 349 CD1 TYR A 104 12744 19282 16000 -632 1731 -2898 C ATOM 350 CD2 TYR A 104 2.550 -10.173 31.700 1.00126.49 C ANISOU 350 CD2 TYR A 104 12956 19241 15865 -1055 2008 -2876 C ATOM 351 CE1 TYR A 104 3.801 -11.177 33.946 1.00128.51 C ANISOU 351 CE1 TYR A 104 12794 19713 16321 -746 1719 -2986 C ATOM 352 CE2 TYR A 104 3.562 -9.450 32.306 1.00128.98 C ANISOU 352 CE2 TYR A 104 13061 19703 16243 -1182 2010 -2964 C ATOM 353 CZ TYR A 104 4.183 -9.957 33.428 1.00129.73 C ANISOU 353 CZ TYR A 104 12941 19914 16439 -1027 1859 -3024 C ATOM 354 OH TYR A 104 5.190 -9.242 34.035 1.00131.98 O ANISOU 354 OH TYR A 104 13005 20358 16783 -1158 1849 -3121 O ATOM 355 N TYR A 105 -0.254 -14.651 29.982 1.00 57.14 N ANISOU 355 N TYR A 105 4693 10020 6999 -317 1921 -2712 N ATOM 356 CA TYR A 105 -1.406 -15.386 29.475 1.00 55.50 C ANISOU 356 CA TYR A 105 4699 9659 6730 -228 1899 -2660 C ATOM 357 C TYR A 105 -1.334 -16.843 29.919 1.00 55.71 C ANISOU 357 C TYR A 105 4677 9639 6852 40 1826 -2685 C ATOM 358 O TYR A 105 -2.337 -17.429 30.332 1.00 53.79 O ANISOU 358 O TYR A 105 4557 9261 6619 148 1719 -2626 O ATOM 359 CB TYR A 105 -1.467 -15.311 27.950 1.00 56.75 C ANISOU 359 CB TYR A 105 4993 9811 6758 -333 2072 -2687 C ATOM 360 CG TYR A 105 -1.527 -13.906 27.396 1.00 56.93 C ANISOU 360 CG TYR A 105 5093 9865 6673 -596 2166 -2649 C ATOM 361 CD1 TYR A 105 -2.726 -13.210 27.341 1.00 54.76 C ANISOU 361 CD1 TYR A 105 5015 9482 6309 -706 2112 -2549 C ATOM 362 CD2 TYR A 105 -0.384 -13.279 26.917 1.00 59.53 C ANISOU 362 CD2 TYR A 105 5302 10326 6991 -734 2320 -2709 C ATOM 363 CE1 TYR A 105 -2.784 -11.926 26.834 1.00 55.16 C ANISOU 363 CE1 TYR A 105 5157 9543 6257 -938 2205 -2503 C ATOM 364 CE2 TYR A 105 -0.433 -11.995 26.405 1.00 59.95 C ANISOU 364 CE2 TYR A 105 5446 10388 6944 -982 2419 -2667 C ATOM 365 CZ TYR A 105 -1.636 -11.324 26.366 1.00 57.75 C ANISOU 365 CZ TYR A 105 5381 9988 6573 -1079 2360 -2560 C ATOM 366 OH TYR A 105 -1.690 -10.046 25.859 1.00 58.39 O ANISOU 366 OH TYR A 105 5573 10060 6552 -1317 2465 -2505 O ATOM 367 N LEU A 106 -0.139 -17.420 29.831 1.00 67.97 N ANISOU 367 N LEU A 106 6047 11298 8478 149 1894 -2772 N ATOM 368 CA LEU A 106 0.083 -18.801 30.247 1.00 68.92 C ANISOU 368 CA LEU A 106 6112 11374 8698 417 1842 -2797 C ATOM 369 C LEU A 106 -0.138 -18.965 31.748 1.00 66.80 C ANISOU 369 C LEU A 106 5779 11080 8520 536 1648 -2731 C ATOM 370 O LEU A 106 -0.689 -19.971 32.196 1.00 65.58 O ANISOU 370 O LEU A 106 5703 10801 8413 721 1564 -2691 O ATOM 371 CB LEU A 106 1.492 -19.261 29.866 1.00 71.82 C ANISOU 371 CB LEU A 106 6276 11878 9132 511 1967 -2902 C ATOM 372 CG LEU A 106 1.661 -19.979 28.524 1.00 73.87 C ANISOU 372 CG LEU A 106 6623 12109 9335 563 2149 -2978 C ATOM 373 CD1 LEU A 106 1.178 -19.122 27.363 1.00 72.66 C ANISOU 373 CD1 LEU A 106 6639 11949 9019 326 2270 -2974 C ATOM 374 CD2 LEU A 106 3.112 -20.388 28.322 1.00 77.51 C ANISOU 374 CD2 LEU A 106 6847 12720 9884 672 2272 -3076 C ATOM 375 N GLY A 107 0.296 -17.972 32.516 1.00 52.99 N ANISOU 375 N GLY A 107 3898 9449 6789 424 1585 -2724 N ATOM 376 CA GLY A 107 0.093 -17.975 33.952 1.00 51.80 C ANISOU 376 CA GLY A 107 3695 9292 6693 516 1405 -2667 C ATOM 377 C GLY A 107 -1.378 -17.851 34.297 1.00 48.68 C ANISOU 377 C GLY A 107 3517 8732 6246 492 1315 -2560 C ATOM 378 O GLY A 107 -1.868 -18.498 35.226 1.00 47.66 O ANISOU 378 O GLY A 107 3424 8522 6164 655 1193 -2496 O ATOM 379 N SER A 108 -2.083 -17.014 33.541 1.00 56.54 N ANISOU 379 N SER A 108 4657 9679 7147 292 1384 -2534 N ATOM 380 CA SER A 108 -3.520 -16.845 33.712 1.00 53.66 C ANISOU 380 CA SER A 108 4491 9163 6734 259 1319 -2434 C ATOM 381 C SER A 108 -4.241 -18.163 33.448 1.00 52.95 C ANISOU 381 C SER A 108 4524 8928 6668 433 1303 -2412 C ATOM 382 O SER A 108 -5.152 -18.548 34.186 1.00 51.18 O ANISOU 382 O SER A 108 4386 8591 6472 523 1201 -2333 O ATOM 383 CB SER A 108 -4.043 -15.758 32.771 1.00 52.11 C ANISOU 383 CB SER A 108 4419 8952 6429 25 1413 -2418 C ATOM 384 OG SER A 108 -5.436 -15.559 32.940 1.00 50.20 O ANISOU 384 OG SER A 108 4351 8578 6146 -1 1351 -2322 O ATOM 385 N LEU A 109 -3.819 -18.852 32.391 1.00 59.91 N ANISOU 385 N LEU A 109 5415 9812 7538 477 1417 -2490 N ATOM 386 CA LEU A 109 -4.368 -20.159 32.049 1.00 60.65 C ANISOU 386 CA LEU A 109 5623 9767 7655 638 1421 -2502 C ATOM 387 C LEU A 109 -4.097 -21.176 33.151 1.00 61.61 C ANISOU 387 C LEU A 109 5669 9844 7898 876 1323 -2477 C ATOM 388 O LEU A 109 -4.969 -21.973 33.502 1.00 60.24 O ANISOU 388 O LEU A 109 5613 9519 7759 989 1261 -2429 O ATOM 389 CB LEU A 109 -3.779 -20.655 30.727 1.00 62.26 C ANISOU 389 CB LEU A 109 5844 9997 7815 644 1577 -2611 C ATOM 390 CG LEU A 109 -4.289 -19.979 29.454 1.00 62.28 C ANISOU 390 CG LEU A 109 5992 10001 7671 443 1679 -2631 C ATOM 391 CD1 LEU A 109 -3.473 -20.417 28.250 1.00 64.95 C ANISOU 391 CD1 LEU A 109 6324 10397 7957 456 1848 -2745 C ATOM 392 CD2 LEU A 109 -5.761 -20.295 29.249 1.00 60.21 C ANISOU 392 CD2 LEU A 109 5937 9584 7357 431 1615 -2590 C ATOM 393 N ALA A 110 -2.884 -21.141 33.693 1.00118.78 N ANISOU 393 N ALA A 110 12710 17220 15202 949 1312 -2512 N ATOM 394 CA ALA A 110 -2.487 -22.063 34.751 1.00120.49 C ANISOU 394 CA ALA A 110 12840 17416 15525 1186 1217 -2485 C ATOM 395 C ALA A 110 -3.311 -21.848 36.016 1.00118.21 C ANISOU 395 C ALA A 110 12607 17063 15243 1211 1066 -2371 C ATOM 396 O ALA A 110 -3.708 -22.808 36.678 1.00117.89 O ANISOU 396 O ALA A 110 12626 16903 15264 1396 998 -2313 O ATOM 397 CB ALA A 110 -1.003 -21.923 35.047 1.00118.52 C ANISOU 397 CB ALA A 110 12343 17356 15332 1240 1227 -2552 C ATOM 398 N LEU A 111 -3.563 -20.585 36.349 1.00 62.13 N ANISOU 398 N LEU A 111 5494 10036 8078 1026 1026 -2339 N ATOM 399 CA LEU A 111 -4.414 -20.253 37.485 1.00 59.65 C ANISOU 399 CA LEU A 111 5246 9666 7753 1033 905 -2236 C ATOM 400 C LEU A 111 -5.834 -20.749 37.232 1.00 57.35 C ANISOU 400 C LEU A 111 5161 9177 7452 1047 909 -2162 C ATOM 401 O LEU A 111 -6.459 -21.361 38.105 1.00 55.53 O ANISOU 401 O LEU A 111 4995 8842 7263 1180 831 -2079 O ATOM 402 CB LEU A 111 -4.424 -18.743 37.728 1.00 57.13 C ANISOU 402 CB LEU A 111 4891 9451 7363 818 891 -2236 C ATOM 403 CG LEU A 111 -5.295 -18.250 38.886 1.00 55.39 C ANISOU 403 CG LEU A 111 4739 9186 7119 815 784 -2141 C ATOM 404 CD1 LEU A 111 -4.744 -18.732 40.219 1.00 56.53 C ANISOU 404 CD1 LEU A 111 4770 9404 7303 998 663 -2129 C ATOM 405 CD2 LEU A 111 -5.417 -16.733 38.865 1.00 55.04 C ANISOU 405 CD2 LEU A 111 4700 9210 7004 585 805 -2153 C ATOM 406 N SER A 112 -6.328 -20.482 36.026 1.00 59.24 N ANISOU 406 N SER A 112 5500 9374 7634 907 1003 -2198 N ATOM 407 CA SER A 112 -7.665 -20.902 35.619 1.00 57.71 C ANISOU 407 CA SER A 112 5484 9017 7427 897 1009 -2157 C ATOM 408 C SER A 112 -7.853 -22.409 35.764 1.00 59.02 C ANISOU 408 C SER A 112 5705 9043 7677 1107 998 -2163 C ATOM 409 O SER A 112 -8.903 -22.873 36.208 1.00 57.60 O ANISOU 409 O SER A 112 5630 8722 7531 1163 950 -2097 O ATOM 410 CB SER A 112 -7.939 -20.478 34.174 1.00 57.36 C ANISOU 410 CB SER A 112 5521 8980 7292 729 1112 -2223 C ATOM 411 OG SER A 112 -9.222 -20.906 33.750 1.00 56.13 O ANISOU 411 OG SER A 112 5521 8685 7120 717 1106 -2209 O ATOM 412 N ASP A 113 -6.828 -23.168 35.392 1.00 91.71 N ANISOU 412 N ASP A 113 9773 13215 11859 1226 1053 -2246 N ATOM 413 CA ASP A 113 -6.876 -24.621 35.504 1.00 93.14 C ANISOU 413 CA ASP A 113 10013 13248 12127 1440 1058 -2261 C ATOM 414 C ASP A 113 -6.776 -25.069 36.960 1.00 92.73 C ANISOU 414 C ASP A 113 9916 13161 12156 1620 949 -2159 C ATOM 415 O ASP A 113 -7.496 -25.971 37.391 1.00 91.81 O ANISOU 415 O ASP A 113 9913 12870 12101 1745 919 -2106 O ATOM 416 CB ASP A 113 -5.760 -25.263 34.678 1.00 97.41 C ANISOU 416 CB ASP A 113 10489 13835 12690 1528 1163 -2379 C ATOM 417 CG ASP A 113 -5.863 -24.931 33.202 1.00 98.17 C ANISOU 417 CG ASP A 113 10656 13958 12686 1365 1282 -2481 C ATOM 418 OD1 ASP A 113 -6.988 -24.670 32.726 1.00 97.10 O ANISOU 418 OD1 ASP A 113 10664 13745 12484 1233 1276 -2473 O ATOM 419 OD2 ASP A 113 -4.818 -24.932 32.518 1.00100.74 O ANISOU 419 OD2 ASP A 113 10891 14390 12996 1371 1384 -2571 O ATOM 420 N LEU A 114 -5.882 -24.431 37.711 1.00 46.55 N ANISOU 420 N LEU A 114 3904 7479 6303 1630 890 -2140 N ATOM 421 CA LEU A 114 -5.669 -24.778 39.114 1.00 46.97 C ANISOU 421 CA LEU A 114 3904 7535 6406 1803 774 -2051 C ATOM 422 C LEU A 114 -6.918 -24.574 39.966 1.00 44.85 C ANISOU 422 C LEU A 114 3760 7162 6118 1780 703 -1930 C ATOM 423 O LEU A 114 -7.183 -25.356 40.880 1.00 45.25 O ANISOU 423 O LEU A 114 3860 7112 6221 1958 640 -1845 O ATOM 424 CB LEU A 114 -4.495 -23.991 39.701 1.00 48.01 C ANISOU 424 CB LEU A 114 3830 7896 6517 1785 713 -2081 C ATOM 425 CG LEU A 114 -3.099 -24.561 39.441 1.00 50.97 C ANISOU 425 CG LEU A 114 4036 8372 6956 1924 744 -2168 C ATOM 426 CD1 LEU A 114 -2.037 -23.689 40.085 1.00 52.03 C ANISOU 426 CD1 LEU A 114 3954 8746 7069 1882 668 -2207 C ATOM 427 CD2 LEU A 114 -3.003 -25.990 39.954 1.00 52.60 C ANISOU 427 CD2 LEU A 114 4283 8441 7260 2207 708 -2119 C ATOM 428 N LEU A 115 -7.679 -23.524 39.669 1.00 43.89 N ANISOU 428 N LEU A 115 3691 7063 5923 1569 719 -1916 N ATOM 429 CA LEU A 115 -8.919 -23.263 40.395 1.00 42.09 C ANISOU 429 CA LEU A 115 3572 6740 5681 1540 672 -1805 C ATOM 430 C LEU A 115 -9.900 -24.427 40.261 1.00 42.03 C ANISOU 430 C LEU A 115 3711 6512 5747 1645 699 -1768 C ATOM 431 O LEU A 115 -10.491 -24.871 41.247 1.00 42.11 O ANISOU 431 O LEU A 115 3782 6422 5795 1760 651 -1666 O ATOM 432 CB LEU A 115 -9.567 -21.962 39.916 1.00 40.53 C ANISOU 432 CB LEU A 115 3405 6591 5403 1302 701 -1804 C ATOM 433 CG LEU A 115 -8.819 -20.671 40.252 1.00 40.45 C ANISOU 433 CG LEU A 115 3279 6768 5324 1181 672 -1830 C ATOM 434 CD1 LEU A 115 -9.578 -19.458 39.735 1.00 38.98 C ANISOU 434 CD1 LEU A 115 3156 6584 5069 962 713 -1818 C ATOM 435 CD2 LEU A 115 -8.582 -20.563 41.752 1.00 40.97 C ANISOU 435 CD2 LEU A 115 3287 6896 5383 1295 568 -1770 C ATOM 436 N ILE A 116 -10.058 -24.921 39.037 1.00 68.51 N ANISOU 436 N ILE A 116 7124 9790 9117 1603 779 -1863 N ATOM 437 CA ILE A 116 -10.947 -26.045 38.767 1.00 69.71 C ANISOU 437 CA ILE A 116 7417 9725 9345 1683 808 -1872 C ATOM 438 C ILE A 116 -10.411 -27.337 39.377 1.00 71.40 C ANISOU 438 C ILE A 116 7649 9822 9656 1935 793 -1848 C ATOM 439 O ILE A 116 -11.155 -28.103 39.989 1.00 72.14 O ANISOU 439 O ILE A 116 7848 9734 9825 2047 772 -1774 O ATOM 440 CB ILE A 116 -11.145 -26.254 37.252 1.00 69.07 C ANISOU 440 CB ILE A 116 7401 9605 9238 1573 891 -2014 C ATOM 441 CG1 ILE A 116 -11.735 -24.998 36.610 1.00 68.01 C ANISOU 441 CG1 ILE A 116 7265 9570 9003 1334 902 -2026 C ATOM 442 CG2 ILE A 116 -12.040 -27.455 36.988 1.00 70.64 C ANISOU 442 CG2 ILE A 116 7749 9563 9526 1650 911 -2057 C ATOM 443 CD1 ILE A 116 -12.002 -25.144 35.127 1.00 68.77 C ANISOU 443 CD1 ILE A 116 7441 9641 9046 1218 974 -2166 C ATOM 444 N LEU A 117 -9.115 -27.571 39.208 1.00 56.67 N ANISOU 444 N LEU A 117 5678 8055 7797 2030 808 -1906 N ATOM 445 CA LEU A 117 -8.486 -28.790 39.705 1.00 58.43 C ANISOU 445 CA LEU A 117 5908 8174 8117 2284 796 -1886 C ATOM 446 C LEU A 117 -8.524 -28.894 41.228 1.00 58.76 C ANISOU 446 C LEU A 117 5937 8209 8181 2430 687 -1737 C ATOM 447 O LEU A 117 -8.605 -29.991 41.778 1.00 60.45 O ANISOU 447 O LEU A 117 6239 8247 8481 2633 669 -1673 O ATOM 448 CB LEU A 117 -7.042 -28.880 39.210 1.00 59.48 C ANISOU 448 CB LEU A 117 5894 8450 8256 2351 836 -1983 C ATOM 449 CG LEU A 117 -6.866 -29.107 37.709 1.00 60.29 C ANISOU 449 CG LEU A 117 6035 8531 8341 2274 963 -2134 C ATOM 450 CD1 LEU A 117 -5.477 -28.683 37.268 1.00 61.87 C ANISOU 450 CD1 LEU A 117 6046 8944 8518 2268 1008 -2217 C ATOM 451 CD2 LEU A 117 -7.122 -30.564 37.354 1.00 62.08 C ANISOU 451 CD2 LEU A 117 6418 8506 8662 2444 1025 -2179 C ATOM 452 N LEU A 118 -8.473 -27.752 41.905 1.00 44.38 N ANISOU 452 N LEU A 118 4023 6567 6274 2329 615 -1683 N ATOM 453 CA LEU A 118 -8.391 -27.741 43.364 1.00 44.70 C ANISOU 453 CA LEU A 118 4046 6641 6297 2467 503 -1558 C ATOM 454 C LEU A 118 -9.733 -27.545 44.066 1.00 42.94 C ANISOU 454 C LEU A 118 3957 6307 6051 2429 487 -1437 C ATOM 455 O LEU A 118 -9.966 -28.116 45.131 1.00 43.70 O ANISOU 455 O LEU A 118 4126 6319 6158 2601 427 -1316 O ATOM 456 CB LEU A 118 -7.395 -26.679 43.838 1.00 44.87 C ANISOU 456 CB LEU A 118 3883 6935 6232 2414 422 -1589 C ATOM 457 CG LEU A 118 -5.919 -26.974 43.568 1.00 47.32 C ANISOU 457 CG LEU A 118 4025 7377 6578 2516 411 -1682 C ATOM 458 CD1 LEU A 118 -5.043 -25.831 44.053 1.00 47.50 C ANISOU 458 CD1 LEU A 118 3860 7671 6519 2431 328 -1729 C ATOM 459 CD2 LEU A 118 -5.511 -28.281 44.227 1.00 49.77 C ANISOU 459 CD2 LEU A 118 4363 7576 6972 2809 356 -1616 C ATOM 460 N PHE A 119 -10.614 -26.743 43.477 1.00 47.30 N ANISOU 460 N PHE A 119 4545 6860 6568 2213 542 -1462 N ATOM 461 CA PHE A 119 -11.855 -26.379 44.157 1.00 46.85 C ANISOU 461 CA PHE A 119 4580 6733 6489 2166 536 -1351 C ATOM 462 C PHE A 119 -13.120 -26.902 43.477 1.00 46.56 C ANISOU 462 C PHE A 119 4670 6487 6533 2107 613 -1359 C ATOM 463 O PHE A 119 -14.209 -26.828 44.044 1.00 47.55 O ANISOU 463 O PHE A 119 4872 6521 6673 2104 620 -1262 O ATOM 464 CB PHE A 119 -11.935 -24.861 44.340 1.00 45.46 C ANISOU 464 CB PHE A 119 4327 6744 6203 1978 517 -1353 C ATOM 465 CG PHE A 119 -10.775 -24.283 45.102 1.00 46.76 C ANISOU 465 CG PHE A 119 4364 7114 6288 2027 427 -1367 C ATOM 466 CD1 PHE A 119 -10.793 -24.235 46.486 1.00 48.37 C ANISOU 466 CD1 PHE A 119 4584 7362 6433 2165 343 -1268 C ATOM 467 CD2 PHE A 119 -9.665 -23.793 44.434 1.00 46.28 C ANISOU 467 CD2 PHE A 119 4167 7212 6205 1943 425 -1488 C ATOM 468 CE1 PHE A 119 -9.726 -23.707 47.190 1.00 48.75 C ANISOU 468 CE1 PHE A 119 4505 7620 6398 2217 241 -1305 C ATOM 469 CE2 PHE A 119 -8.595 -23.265 45.132 1.00 47.06 C ANISOU 469 CE2 PHE A 119 4127 7512 6243 1984 334 -1522 C ATOM 470 CZ PHE A 119 -8.626 -23.221 46.511 1.00 48.29 C ANISOU 470 CZ PHE A 119 4290 7720 6338 2121 233 -1439 C ATOM 471 N ALA A 120 -12.977 -27.431 42.267 1.00 51.44 N ANISOU 471 N ALA A 120 5307 7036 7202 2064 669 -1486 N ATOM 472 CA ALA A 120 -14.121 -27.979 41.546 1.00 51.76 C ANISOU 472 CA ALA A 120 5459 6881 7326 1999 723 -1539 C ATOM 473 C ALA A 120 -14.045 -29.499 41.443 1.00 53.81 C ANISOU 473 C ALA A 120 5840 6898 7708 2180 745 -1568 C ATOM 474 O ALA A 120 -15.062 -30.184 41.540 1.00 54.51 O ANISOU 474 O ALA A 120 6092 6744 7875 2121 756 -1472 O ATOM 475 CB ALA A 120 -14.236 -27.353 40.163 1.00 49.24 C ANISOU 475 CB ALA A 120 5107 6647 6956 1786 768 -1681 C ATOM 476 N LEU A 121 -12.836 -30.018 41.253 1.00 42.60 N ANISOU 476 N LEU A 121 4386 5516 6286 2306 751 -1615 N ATOM 477 CA LEU A 121 -12.629 -31.461 41.117 1.00 44.93 C ANISOU 477 CA LEU A 121 4807 5571 6696 2491 782 -1644 C ATOM 478 C LEU A 121 -13.046 -32.285 42.347 1.00 45.94 C ANISOU 478 C LEU A 121 5061 5491 6905 2687 742 -1477 C ATOM 479 O LEU A 121 -13.738 -33.289 42.194 1.00 46.80 O ANISOU 479 O LEU A 121 5351 5307 7125 2720 776 -1471 O ATOM 480 CB LEU A 121 -11.185 -31.777 40.688 1.00 46.84 C ANISOU 480 CB LEU A 121 4957 5914 6925 2599 805 -1723 C ATOM 481 CG LEU A 121 -10.834 -33.217 40.295 1.00 49.54 C ANISOU 481 CG LEU A 121 5425 6019 7382 2779 863 -1785 C ATOM 482 CD1 LEU A 121 -9.772 -33.221 39.207 1.00 50.80 C ANISOU 482 CD1 LEU A 121 5493 6304 7504 2768 936 -1940 C ATOM 483 CD2 LEU A 121 -10.356 -34.028 41.494 1.00 51.49 C ANISOU 483 CD2 LEU A 121 5702 6156 7708 3038 807 -1638 C ATOM 484 N PRO A 122 -12.622 -31.881 43.564 1.00 45.89 N ANISOU 484 N PRO A 122 4986 5619 6832 2789 667 -1327 N ATOM 485 CA PRO A 122 -13.049 -32.672 44.727 1.00 47.08 C ANISOU 485 CA PRO A 122 5294 5569 7026 2976 635 -1141 C ATOM 486 C PRO A 122 -14.562 -32.650 44.943 1.00 44.94 C ANISOU 486 C PRO A 122 5180 5116 6780 2782 679 -1007 C ATOM 487 O PRO A 122 -15.160 -33.692 45.222 1.00 45.87 O ANISOU 487 O PRO A 122 5496 4940 6994 2818 716 -896 O ATOM 488 CB PRO A 122 -12.344 -31.980 45.897 1.00 47.02 C ANISOU 488 CB PRO A 122 5169 5800 6895 3054 534 -1026 C ATOM 489 CG PRO A 122 -11.169 -31.310 45.285 1.00 46.94 C ANISOU 489 CG PRO A 122 4948 6050 6837 2983 513 -1172 C ATOM 490 CD PRO A 122 -11.650 -30.842 43.949 1.00 45.32 C ANISOU 490 CD PRO A 122 4719 5858 6643 2755 603 -1322 C ATOM 491 N VAL A 123 -15.165 -31.472 44.812 1.00 43.49 N ANISOU 491 N VAL A 123 4908 5098 6519 2548 682 -1004 N ATOM 492 CA VAL A 123 -16.607 -31.322 44.977 1.00 42.40 C ANISOU 492 CA VAL A 123 4874 4824 6411 2325 727 -873 C ATOM 493 C VAL A 123 -17.352 -32.156 43.938 1.00 43.06 C ANISOU 493 C VAL A 123 5073 4659 6629 2182 781 -950 C ATOM 494 O VAL A 123 -18.412 -32.719 44.218 1.00 43.57 O ANISOU 494 O VAL A 123 5274 4499 6781 2080 822 -824 O ATOM 495 CB VAL A 123 -17.032 -29.847 44.848 1.00 39.93 C ANISOU 495 CB VAL A 123 4429 4741 6000 2117 719 -887 C ATOM 496 CG1 VAL A 123 -18.496 -29.680 45.216 1.00 39.13 C ANISOU 496 CG1 VAL A 123 4411 4517 5939 1931 766 -730 C ATOM 497 CG2 VAL A 123 -16.158 -28.966 45.727 1.00 39.46 C ANISOU 497 CG2 VAL A 123 4250 4939 5804 2236 658 -863 C ATOM 498 N ASP A 124 -16.780 -32.237 42.741 1.00 49.37 N ANISOU 498 N ASP A 124 5817 5503 7439 2168 785 -1166 N ATOM 499 CA ASP A 124 -17.369 -33.004 41.651 1.00 50.22 C ANISOU 499 CA ASP A 124 6038 5397 7647 2030 823 -1280 C ATOM 500 C ASP A 124 -17.286 -34.498 41.939 1.00 52.85 C ANISOU 500 C ASP A 124 6563 5408 8109 2191 856 -1239 C ATOM 501 O ASP A 124 -18.304 -35.189 41.961 1.00 53.65 O ANISOU 501 O ASP A 124 6816 5250 8317 2059 887 -1162 O ATOM 502 CB ASP A 124 -16.654 -32.683 40.337 1.00 50.09 C ANISOU 502 CB ASP A 124 5928 5528 7575 1999 832 -1527 C ATOM 503 CG ASP A 124 -17.434 -33.136 39.112 1.00 50.58 C ANISOU 503 CG ASP A 124 6097 5431 7689 1791 852 -1659 C ATOM 504 OD1 ASP A 124 -18.089 -34.198 39.164 1.00 52.09 O ANISOU 504 OD1 ASP A 124 6458 5329 8004 1759 869 -1620 O ATOM 505 OD2 ASP A 124 -17.386 -32.422 38.089 1.00 49.64 O ANISOU 505 OD2 ASP A 124 5901 5480 7480 1650 849 -1803 O ATOM 506 N VAL A 125 -16.071 -34.991 42.157 1.00 46.07 N ANISOU 506 N VAL A 125 5693 4564 7249 2478 850 -1291 N ATOM 507 CA VAL A 125 -15.853 -36.415 42.391 1.00 49.08 C ANISOU 507 CA VAL A 125 6267 4628 7753 2676 881 -1262 C ATOM 508 C VAL A 125 -16.616 -36.898 43.624 1.00 49.44 C ANISOU 508 C VAL A 125 6472 4466 7846 2687 889 -992 C ATOM 509 O VAL A 125 -17.030 -38.053 43.690 1.00 51.50 O ANISOU 509 O VAL A 125 6945 4386 8235 2692 939 -940 O ATOM 510 CB VAL A 125 -14.344 -36.766 42.498 1.00 52.24 C ANISOU 510 CB VAL A 125 6592 5114 8142 3024 862 -1348 C ATOM 511 CG1 VAL A 125 -13.729 -36.166 43.750 1.00 52.29 C ANISOU 511 CG1 VAL A 125 6471 5352 8046 3204 783 -1191 C ATOM 512 CG2 VAL A 125 -14.140 -38.272 42.473 1.00 55.83 C ANISOU 512 CG2 VAL A 125 7267 5208 8739 3230 905 -1348 C ATOM 513 N TYR A 126 -16.830 -36.008 44.588 1.00 47.77 N ANISOU 513 N TYR A 126 6171 4451 7528 2676 853 -826 N ATOM 514 CA TYR A 126 -17.609 -36.371 45.765 1.00 48.18 C ANISOU 514 CA TYR A 126 6375 4335 7599 2671 882 -564 C ATOM 515 C TYR A 126 -19.112 -36.336 45.500 1.00 46.44 C ANISOU 515 C TYR A 126 6215 3969 7460 2342 948 -507 C ATOM 516 O TYR A 126 -19.774 -37.372 45.505 1.00 48.16 O ANISOU 516 O TYR A 126 6621 3864 7814 2278 1012 -439 O ATOM 517 CB TYR A 126 -17.271 -35.470 46.956 1.00 47.35 C ANISOU 517 CB TYR A 126 6171 4489 7332 2778 827 -414 C ATOM 518 CG TYR A 126 -18.226 -35.634 48.119 1.00 47.37 C ANISOU 518 CG TYR A 126 6322 4355 7321 2723 882 -149 C ATOM 519 CD1 TYR A 126 -18.164 -36.751 48.942 1.00 50.44 C ANISOU 519 CD1 TYR A 126 6932 4483 7750 2909 910 31 C ATOM 520 CD2 TYR A 126 -19.193 -34.673 48.392 1.00 44.63 C ANISOU 520 CD2 TYR A 126 5903 4134 6922 2490 919 -74 C ATOM 521 CE1 TYR A 126 -19.037 -36.907 50.003 1.00 50.74 C ANISOU 521 CE1 TYR A 126 7118 4396 7764 2848 984 281 C ATOM 522 CE2 TYR A 126 -20.070 -34.821 49.449 1.00 44.89 C ANISOU 522 CE2 TYR A 126 6064 4051 6941 2438 997 162 C ATOM 523 CZ TYR A 126 -19.988 -35.939 50.251 1.00 47.92 C ANISOU 523 CZ TYR A 126 6670 4184 7353 2609 1035 341 C ATOM 524 OH TYR A 126 -20.859 -36.088 51.306 1.00 48.42 O ANISOU 524 OH TYR A 126 6872 4136 7391 2547 1134 584 O ATOM 525 N ASN A 127 -19.639 -35.140 45.254 1.00 49.31 N ANISOU 525 N ASN A 127 6414 4570 7752 2134 932 -537 N ATOM 526 CA ASN A 127 -21.083 -34.921 45.277 1.00 48.58 C ANISOU 526 CA ASN A 127 6333 4400 7726 1852 985 -441 C ATOM 527 C ASN A 127 -21.797 -35.065 43.934 1.00 48.43 C ANISOU 527 C ASN A 127 6295 4296 7810 1596 981 -611 C ATOM 528 O ASN A 127 -22.982 -34.748 43.824 1.00 48.20 O ANISOU 528 O ASN A 127 6226 4250 7839 1353 1002 -552 O ATOM 529 CB ASN A 127 -21.390 -33.546 45.877 1.00 46.65 C ANISOU 529 CB ASN A 127 5936 4437 7354 1782 973 -351 C ATOM 530 CG ASN A 127 -22.642 -33.549 46.732 1.00 47.30 C ANISOU 530 CG ASN A 127 6075 4414 7484 1644 1060 -135 C ATOM 531 OD1 ASN A 127 -23.571 -34.321 46.496 1.00 48.60 O ANISOU 531 OD1 ASN A 127 6330 4337 7801 1486 1120 -93 O ATOM 532 ND2 ASN A 127 -22.670 -32.683 47.737 1.00 46.55 N ANISOU 532 ND2 ASN A 127 5924 4502 7260 1696 1074 -5 N ATOM 533 N PHE A 128 -21.092 -35.545 42.916 1.00 52.87 N ANISOU 533 N PHE A 128 6884 4815 8392 1653 952 -823 N ATOM 534 CA PHE A 128 -21.700 -35.669 41.595 1.00 53.27 C ANISOU 534 CA PHE A 128 6932 4806 8504 1414 932 -1002 C ATOM 535 C PHE A 128 -21.635 -37.073 41.000 1.00 55.28 C ANISOU 535 C PHE A 128 7385 4731 8890 1425 961 -1120 C ATOM 536 O PHE A 128 -22.530 -37.474 40.256 1.00 56.79 O ANISOU 536 O PHE A 128 7639 4759 9182 1182 958 -1182 O ATOM 537 CB PHE A 128 -21.113 -34.640 40.624 1.00 52.55 C ANISOU 537 CB PHE A 128 6677 5015 8277 1383 875 -1189 C ATOM 538 CG PHE A 128 -21.657 -33.252 40.815 1.00 51.20 C ANISOU 538 CG PHE A 128 6336 5104 8015 1243 844 -1106 C ATOM 539 CD1 PHE A 128 -22.976 -33.058 41.191 1.00 53.19 C ANISOU 539 CD1 PHE A 128 6573 5296 8341 1049 855 -958 C ATOM 540 CD2 PHE A 128 -20.850 -32.143 40.624 1.00 48.78 C ANISOU 540 CD2 PHE A 128 5882 5093 7559 1305 812 -1179 C ATOM 541 CE1 PHE A 128 -23.481 -31.784 41.370 1.00 52.53 C ANISOU 541 CE1 PHE A 128 6338 5438 8183 946 834 -884 C ATOM 542 CE2 PHE A 128 -21.350 -30.867 40.802 1.00 48.08 C ANISOU 542 CE2 PHE A 128 5663 5213 7394 1183 789 -1104 C ATOM 543 CZ PHE A 128 -22.667 -30.688 41.176 1.00 49.88 C ANISOU 543 CZ PHE A 128 5884 5373 7696 1017 799 -957 C ATOM 544 N ILE A 129 -20.587 -37.823 41.320 1.00 76.53 N ANISOU 544 N ILE A 129 10172 7320 11585 1705 984 -1159 N ATOM 545 CA ILE A 129 -20.470 -39.177 40.789 1.00 77.71 C ANISOU 545 CA ILE A 129 10534 7128 11864 1745 1024 -1277 C ATOM 546 C ILE A 129 -20.552 -40.250 41.874 1.00 79.06 C ANISOU 546 C ILE A 129 10914 6969 12158 1867 1087 -1070 C ATOM 547 O ILE A 129 -20.980 -41.372 41.606 1.00 79.73 O ANISOU 547 O ILE A 129 11198 6707 12391 1763 1132 -1099 O ATOM 548 CB ILE A 129 -19.189 -39.367 39.939 1.00 74.59 C ANISOU 548 CB ILE A 129 10131 6796 11416 1970 1024 -1510 C ATOM 549 CG1 ILE A 129 -17.929 -39.247 40.799 1.00 74.33 C ANISOU 549 CG1 ILE A 129 10029 6893 11320 2326 1019 -1414 C ATOM 550 CG2 ILE A 129 -19.159 -38.362 38.799 1.00 72.98 C ANISOU 550 CG2 ILE A 129 9759 6884 11086 1815 983 -1716 C ATOM 551 CD1 ILE A 129 -16.657 -39.587 40.059 1.00 74.81 C ANISOU 551 CD1 ILE A 129 10071 6988 11365 2577 1038 -1630 C ATOM 552 N TRP A 130 -20.146 -39.903 43.093 1.00 53.19 N ANISOU 552 N TRP A 130 7606 3792 8811 2079 1088 -862 N ATOM 553 CA TRP A 130 -20.166 -40.853 44.202 1.00 55.89 C ANISOU 553 CA TRP A 130 8161 3839 9237 2205 1149 -630 C ATOM 554 C TRP A 130 -21.451 -40.763 45.026 1.00 54.67 C ANISOU 554 C TRP A 130 8022 3626 9125 1944 1204 -416 C ATOM 555 O TRP A 130 -22.154 -41.762 45.195 1.00 55.94 O ANISOU 555 O TRP A 130 8302 3515 9437 1707 1260 -416 O ATOM 556 CB TRP A 130 -18.919 -40.696 45.086 1.00 56.99 C ANISOU 556 CB TRP A 130 8285 4103 9266 2578 1114 -503 C ATOM 557 CG TRP A 130 -17.718 -41.448 44.568 1.00 59.85 C ANISOU 557 CG TRP A 130 8691 4396 9652 2884 1090 -664 C ATOM 558 CD1 TRP A 130 -16.592 -40.916 44.011 1.00 59.17 C ANISOU 558 CD1 TRP A 130 8402 4608 9470 3047 1030 -845 C ATOM 559 CD2 TRP A 130 -17.534 -42.870 44.560 1.00 64.19 C ANISOU 559 CD2 TRP A 130 9500 4549 10341 3066 1142 -660 C ATOM 560 NE1 TRP A 130 -15.715 -41.916 43.662 1.00 62.79 N ANISOU 560 NE1 TRP A 130 8957 4899 10001 3330 1043 -957 N ATOM 561 CE2 TRP A 130 -16.270 -43.125 43.988 1.00 65.74 C ANISOU 561 CE2 TRP A 130 9613 4852 10513 3342 1096 -848 C ATOM 562 CE3 TRP A 130 -18.313 -43.951 44.983 1.00 67.10 C ANISOU 562 CE3 TRP A 130 10157 4483 10855 3009 1223 -515 C ATOM 563 CZ2 TRP A 130 -15.770 -44.414 43.829 1.00 69.20 C ANISOU 563 CZ2 TRP A 130 10194 5052 11047 3506 1074 -901 C ATOM 564 CZ3 TRP A 130 -17.814 -45.231 44.823 1.00 70.86 C ANISOU 564 CZ3 TRP A 130 10819 4686 11419 3196 1213 -565 C ATOM 565 CH2 TRP A 130 -16.555 -45.451 44.251 1.00 71.70 C ANISOU 565 CH2 TRP A 130 10799 4959 11486 3440 1128 -758 C ATOM 566 N VAL A 131 -21.766 -39.569 45.518 1.00 52.52 N ANISOU 566 N VAL A 131 7622 3609 8722 1981 1193 -246 N ATOM 567 CA VAL A 131 -23.027 -39.344 46.221 1.00 51.37 C ANISOU 567 CA VAL A 131 7464 3447 8606 1749 1265 -48 C ATOM 568 C VAL A 131 -23.846 -38.233 45.560 1.00 47.84 C ANISOU 568 C VAL A 131 6786 3253 8141 1471 1227 -157 C ATOM 569 O VAL A 131 -23.455 -37.068 45.549 1.00 45.28 O ANISOU 569 O VAL A 131 6277 3257 7672 1523 1161 -219 O ATOM 570 CB VAL A 131 -22.809 -39.076 47.727 1.00 51.49 C ANISOU 570 CB VAL A 131 7510 3567 8488 1933 1296 212 C ATOM 571 CG1 VAL A 131 -21.677 -38.088 47.931 1.00 49.90 C ANISOU 571 CG1 VAL A 131 7148 3719 8094 2165 1189 144 C ATOM 572 CG2 VAL A 131 -24.090 -38.584 48.381 1.00 49.85 C ANISOU 572 CG2 VAL A 131 7236 3421 8285 1689 1383 380 C ATOM 573 N HIS A 132 -24.984 -38.614 44.992 1.00 77.41 N ANISOU 573 N HIS A 132 10542 6833 12037 1172 1265 -180 N ATOM 574 CA HIS A 132 -25.788 -37.695 44.200 1.00 77.43 C ANISOU 574 CA HIS A 132 10334 7045 12041 911 1210 -289 C ATOM 575 C HIS A 132 -26.735 -36.883 45.074 1.00 76.84 C ANISOU 575 C HIS A 132 10128 7122 11946 793 1269 -89 C ATOM 576 O HIS A 132 -27.229 -35.835 44.660 1.00 76.55 O ANISOU 576 O HIS A 132 9890 7328 11866 659 1218 -143 O ATOM 577 CB HIS A 132 -26.560 -38.466 43.130 1.00 81.46 C ANISOU 577 CB HIS A 132 10899 7329 12721 645 1193 -437 C ATOM 578 CG HIS A 132 -25.686 -39.316 42.261 1.00 81.99 C ANISOU 578 CG HIS A 132 11115 7229 12807 752 1151 -655 C ATOM 579 ND1 HIS A 132 -25.357 -38.967 40.969 1.00 81.12 N ANISOU 579 ND1 HIS A 132 10926 7260 12636 689 1055 -913 N ATOM 580 CD2 HIS A 132 -25.061 -40.493 42.504 1.00 83.34 C ANISOU 580 CD2 HIS A 132 11520 7100 13045 932 1203 -654 C ATOM 581 CE1 HIS A 132 -24.574 -39.896 40.451 1.00 82.06 C ANISOU 581 CE1 HIS A 132 11217 7179 12783 821 1060 -1073 C ATOM 582 NE2 HIS A 132 -24.377 -40.832 41.362 1.00 83.30 N ANISOU 582 NE2 HIS A 132 11562 7061 13027 978 1146 -922 N ATOM 583 N HIS A 133 -26.979 -37.372 46.286 1.00 65.58 N ANISOU 583 N HIS A 133 8828 5544 10548 853 1386 146 N ATOM 584 CA HIS A 133 -27.860 -36.690 47.227 1.00 65.74 C ANISOU 584 CA HIS A 133 8749 5689 10542 764 1478 347 C ATOM 585 C HIS A 133 -27.616 -37.194 48.647 1.00 65.69 C ANISOU 585 C HIS A 133 8933 5553 10474 948 1594 594 C ATOM 586 O HIS A 133 -27.347 -38.379 48.848 1.00 67.36 O ANISOU 586 O HIS A 133 9368 5467 10759 1026 1638 652 O ATOM 587 CB HIS A 133 -29.326 -36.896 46.835 1.00 65.84 C ANISOU 587 CB HIS A 133 8671 5595 10750 426 1535 366 C ATOM 588 CG HIS A 133 -29.780 -38.320 46.914 1.00 67.89 C ANISOU 588 CG HIS A 133 9129 5467 11198 307 1626 430 C ATOM 589 ND1 HIS A 133 -29.443 -39.262 45.966 1.00 68.65 N ANISOU 589 ND1 HIS A 133 9350 5336 11399 260 1559 248 N ATOM 590 CD2 HIS A 133 -30.547 -38.962 47.826 1.00 69.23 C ANISOU 590 CD2 HIS A 133 9411 5425 11470 219 1792 655 C ATOM 591 CE1 HIS A 133 -29.981 -40.424 46.293 1.00 70.20 C ANISOU 591 CE1 HIS A 133 9729 5181 11762 144 1671 354 C ATOM 592 NE2 HIS A 133 -30.657 -40.268 47.417 1.00 70.66 N ANISOU 592 NE2 HIS A 133 9781 5243 11824 111 1817 609 N ATOM 593 N PRO A 134 -27.709 -36.296 49.640 1.00 61.45 N ANISOU 593 N PRO A 134 8327 5231 9790 1024 1645 743 N ATOM 594 CA PRO A 134 -28.019 -34.875 49.455 1.00 61.00 C ANISOU 594 CA PRO A 134 8028 5500 9648 948 1605 680 C ATOM 595 C PRO A 134 -26.771 -34.030 49.217 1.00 59.31 C ANISOU 595 C PRO A 134 7740 5547 9249 1155 1465 536 C ATOM 596 O PRO A 134 -25.658 -34.477 49.491 1.00 58.47 O ANISOU 596 O PRO A 134 7757 5402 9056 1390 1414 527 O ATOM 597 CB PRO A 134 -28.646 -34.496 50.793 1.00 62.46 C ANISOU 597 CB PRO A 134 8234 5738 9759 958 1756 920 C ATOM 598 CG PRO A 134 -27.925 -35.350 51.774 1.00 62.88 C ANISOU 598 CG PRO A 134 8543 5626 9722 1184 1801 1075 C ATOM 599 CD PRO A 134 -27.642 -36.657 51.067 1.00 63.19 C ANISOU 599 CD PRO A 134 8730 5362 9916 1177 1764 998 C ATOM 600 N TRP A 135 -26.966 -32.818 48.707 1.00 55.03 N ANISOU 600 N TRP A 135 6993 5261 8655 1066 1406 428 N ATOM 601 CA TRP A 135 -25.869 -31.878 48.514 1.00 52.89 C ANISOU 601 CA TRP A 135 6635 5249 8211 1221 1293 299 C ATOM 602 C TRP A 135 -25.376 -31.378 49.867 1.00 52.39 C ANISOU 602 C TRP A 135 6626 5316 7964 1416 1327 442 C ATOM 603 O TRP A 135 -26.162 -30.899 50.686 1.00 53.02 O ANISOU 603 O TRP A 135 6697 5436 8012 1361 1431 592 O ATOM 604 CB TRP A 135 -26.322 -30.706 47.641 1.00 51.76 C ANISOU 604 CB TRP A 135 6286 5315 8065 1057 1238 175 C ATOM 605 CG TRP A 135 -25.283 -29.642 47.452 1.00 49.29 C ANISOU 605 CG TRP A 135 5882 5265 7583 1177 1144 53 C ATOM 606 CD1 TRP A 135 -25.173 -28.473 48.146 1.00 48.52 C ANISOU 606 CD1 TRP A 135 5715 5377 7344 1230 1155 101 C ATOM 607 CD2 TRP A 135 -24.208 -29.648 46.504 1.00 47.79 C ANISOU 607 CD2 TRP A 135 5664 5147 7349 1245 1038 -145 C ATOM 608 NE1 TRP A 135 -24.098 -27.751 47.690 1.00 46.26 N ANISOU 608 NE1 TRP A 135 5355 5283 6939 1310 1056 -52 N ATOM 609 CE2 TRP A 135 -23.488 -28.450 46.682 1.00 45.67 C ANISOU 609 CE2 TRP A 135 5295 5137 6921 1322 990 -200 C ATOM 610 CE3 TRP A 135 -23.785 -30.549 45.522 1.00 48.29 C ANISOU 610 CE3 TRP A 135 5780 5077 7492 1244 992 -289 C ATOM 611 CZ2 TRP A 135 -22.369 -28.130 45.916 1.00 44.01 C ANISOU 611 CZ2 TRP A 135 5020 5066 6638 1386 906 -382 C ATOM 612 CZ3 TRP A 135 -22.673 -30.230 44.763 1.00 46.67 C ANISOU 612 CZ3 TRP A 135 5515 5016 7203 1328 915 -473 C ATOM 613 CH2 TRP A 135 -21.979 -29.031 44.964 1.00 44.62 C ANISOU 613 CH2 TRP A 135 5138 5023 6792 1393 876 -513 C ATOM 614 N ALA A 136 -24.073 -31.493 50.100 1.00 48.25 N ANISOU 614 N ALA A 136 6153 4864 7315 1646 1238 389 N ATOM 615 CA ALA A 136 -23.498 -31.155 51.398 1.00 48.04 C ANISOU 615 CA ALA A 136 6198 4954 7099 1846 1239 517 C ATOM 616 C ALA A 136 -22.489 -30.013 51.318 1.00 45.74 C ANISOU 616 C ALA A 136 5769 4966 6644 1941 1122 377 C ATOM 617 O ALA A 136 -21.358 -30.142 51.788 1.00 45.64 O ANISOU 617 O ALA A 136 5792 5036 6511 2158 1035 366 O ATOM 618 CB ALA A 136 -22.857 -32.385 52.027 1.00 47.99 C ANISOU 618 CB ALA A 136 6394 4757 7083 2061 1230 624 C ATOM 619 N PHE A 137 -22.900 -28.897 50.723 1.00 42.19 N ANISOU 619 N PHE A 137 5159 4678 6196 1778 1116 274 N ATOM 620 CA PHE A 137 -22.040 -27.720 50.630 1.00 40.62 C ANISOU 620 CA PHE A 137 4834 4749 5852 1827 1024 143 C ATOM 621 C PHE A 137 -22.843 -26.430 50.772 1.00 39.06 C ANISOU 621 C PHE A 137 4546 4686 5611 1681 1079 158 C ATOM 622 O PHE A 137 -22.281 -25.335 50.788 1.00 37.85 O ANISOU 622 O PHE A 137 4305 4738 5338 1693 1022 62 O ATOM 623 CB PHE A 137 -21.256 -27.719 49.315 1.00 39.89 C ANISOU 623 CB PHE A 137 4632 4715 5809 1811 929 -72 C ATOM 624 CG PHE A 137 -20.340 -28.898 49.155 1.00 41.56 C ANISOU 624 CG PHE A 137 4918 4810 6063 1986 879 -111 C ATOM 625 CD1 PHE A 137 -19.081 -28.897 49.733 1.00 42.33 C ANISOU 625 CD1 PHE A 137 5006 5036 6042 2211 793 -133 C ATOM 626 CD2 PHE A 137 -20.738 -30.009 48.431 1.00 42.61 C ANISOU 626 CD2 PHE A 137 5128 4704 6360 1930 912 -133 C ATOM 627 CE1 PHE A 137 -18.237 -29.981 49.590 1.00 44.12 C ANISOU 627 CE1 PHE A 137 5291 5155 6320 2401 747 -166 C ATOM 628 CE2 PHE A 137 -19.898 -31.097 48.285 1.00 44.38 C ANISOU 628 CE2 PHE A 137 5435 4798 6629 2110 877 -174 C ATOM 629 CZ PHE A 137 -18.646 -31.082 48.865 1.00 45.14 C ANISOU 629 CZ PHE A 137 5513 5024 6614 2358 798 -185 C ATOM 630 N GLY A 138 -24.161 -26.567 50.873 1.00 42.48 N ANISOU 630 N GLY A 138 4995 4994 6151 1543 1194 274 N ATOM 631 CA GLY A 138 -25.032 -25.425 51.084 1.00 41.48 C ANISOU 631 CA GLY A 138 4784 4973 6003 1430 1265 308 C ATOM 632 C GLY A 138 -25.319 -24.628 49.826 1.00 38.92 C ANISOU 632 C GLY A 138 4302 4731 5752 1278 1209 165 C ATOM 633 O GLY A 138 -24.829 -24.952 48.744 1.00 38.21 O ANISOU 633 O GLY A 138 4172 4627 5718 1243 1119 31 O ATOM 634 N ASP A 139 -26.118 -23.577 49.979 1.00 52.35 N ANISOU 634 N ASP A 139 5927 6518 7444 1198 1269 197 N ATOM 635 CA ASP A 139 -26.508 -22.724 48.864 1.00 49.66 C ANISOU 635 CA ASP A 139 5451 6254 7163 1064 1218 93 C ATOM 636 C ASP A 139 -25.302 -21.958 48.327 1.00 46.89 C ANISOU 636 C ASP A 139 5069 6058 6686 1105 1108 -70 C ATOM 637 O ASP A 139 -25.122 -21.823 47.113 1.00 45.87 O ANISOU 637 O ASP A 139 4875 5955 6599 1019 1030 -189 O ATOM 638 CB ASP A 139 -27.598 -21.747 49.313 1.00 50.34 C ANISOU 638 CB ASP A 139 5474 6387 7264 1012 1319 183 C ATOM 639 CG ASP A 139 -28.342 -21.125 48.149 1.00 48.80 C ANISOU 639 CG ASP A 139 5139 6222 7181 871 1273 127 C ATOM 640 OD1 ASP A 139 -28.433 -21.772 47.086 1.00 49.81 O ANISOU 640 OD1 ASP A 139 5226 6285 7414 775 1192 64 O ATOM 641 OD2 ASP A 139 -28.844 -19.990 48.302 1.00 46.44 O ANISOU 641 OD2 ASP A 139 4782 6005 6858 864 1314 147 O ATOM 642 N ALA A 140 -24.474 -21.468 49.244 1.00 27.58 N ANISOU 642 N ALA A 140 2676 3721 4080 1227 1103 -75 N ATOM 643 CA ALA A 140 -23.285 -20.700 48.891 1.00 27.15 C ANISOU 643 CA ALA A 140 2582 3826 3910 1256 1010 -228 C ATOM 644 C ALA A 140 -22.268 -21.549 48.137 1.00 27.33 C ANISOU 644 C ALA A 140 2589 3838 3957 1299 922 -339 C ATOM 645 O ALA A 140 -21.664 -21.092 47.168 1.00 26.88 O ANISOU 645 O ALA A 140 2457 3870 3884 1241 863 -480 O ATOM 646 CB ALA A 140 -22.655 -20.099 50.138 1.00 27.76 C ANISOU 646 CB ALA A 140 2717 4017 3813 1371 1012 -212 C ATOM 647 N GLY A 141 -22.077 -22.784 48.590 1.00 37.80 N ANISOU 647 N GLY A 141 3995 5048 5320 1406 926 -272 N ATOM 648 CA GLY A 141 -21.190 -23.709 47.910 1.00 38.21 C ANISOU 648 CA GLY A 141 4043 5061 5412 1474 860 -373 C ATOM 649 C GLY A 141 -21.752 -24.080 46.552 1.00 38.05 C ANISOU 649 C GLY A 141 3988 4942 5525 1328 857 -449 C ATOM 650 O GLY A 141 -21.022 -24.133 45.557 1.00 37.36 O ANISOU 650 O GLY A 141 3850 4908 5435 1315 804 -602 O ATOM 651 N CYS A 142 -23.059 -24.325 46.518 1.00 40.81 N ANISOU 651 N CYS A 142 4360 5159 5986 1213 916 -345 N ATOM 652 CA CYS A 142 -23.757 -24.681 45.287 1.00 41.43 C ANISOU 652 CA CYS A 142 4405 5146 6188 1053 897 -408 C ATOM 653 C CYS A 142 -23.570 -23.627 44.202 1.00 39.38 C ANISOU 653 C CYS A 142 4051 5040 5871 951 838 -539 C ATOM 654 O CYS A 142 -23.197 -23.947 43.075 1.00 39.52 O ANISOU 654 O CYS A 142 4061 5054 5899 902 787 -674 O ATOM 655 CB CYS A 142 -25.250 -24.884 45.560 1.00 43.93 C ANISOU 655 CB CYS A 142 4717 5342 6630 935 966 -265 C ATOM 656 SG CYS A 142 -26.234 -25.270 44.095 1.00 46.19 S ANISOU 656 SG CYS A 142 4945 5531 7072 719 914 -335 S ATOM 657 N LYS A 143 -23.824 -22.369 44.548 1.00 26.09 N ANISOU 657 N LYS A 143 2315 3482 4118 923 856 -498 N ATOM 658 CA LYS A 143 -23.722 -21.280 43.579 1.00 25.42 C ANISOU 658 CA LYS A 143 2162 3521 3974 823 811 -593 C ATOM 659 C LYS A 143 -22.270 -20.923 43.253 1.00 25.78 C ANISOU 659 C LYS A 143 2191 3703 3899 877 775 -737 C ATOM 660 O LYS A 143 -21.916 -20.712 42.086 1.00 25.70 O ANISOU 660 O LYS A 143 2156 3747 3861 797 738 -854 O ATOM 661 CB LYS A 143 -24.487 -20.053 44.079 1.00 24.96 C ANISOU 661 CB LYS A 143 2069 3523 3894 786 852 -499 C ATOM 662 CG LYS A 143 -25.968 -20.316 44.315 1.00 25.14 C ANISOU 662 CG LYS A 143 2065 3436 4052 724 898 -363 C ATOM 663 CD LYS A 143 -26.709 -19.060 44.742 1.00 25.11 C ANISOU 663 CD LYS A 143 2013 3494 4032 709 947 -284 C ATOM 664 CE LYS A 143 -28.208 -19.309 44.820 1.00 25.73 C ANISOU 664 CE LYS A 143 2022 3487 4268 641 992 -161 C ATOM 665 NZ LYS A 143 -28.973 -18.055 45.064 1.00 26.02 N ANISOU 665 NZ LYS A 143 1997 3583 4305 643 1038 -96 N ATOM 666 N GLY A 144 -21.434 -20.867 44.285 1.00 39.73 N ANISOU 666 N GLY A 144 3969 5536 5590 1010 786 -727 N ATOM 667 CA GLY A 144 -20.029 -20.538 44.122 1.00 38.52 C ANISOU 667 CA GLY A 144 3767 5530 5338 1065 751 -861 C ATOM 668 C GLY A 144 -19.288 -21.528 43.244 1.00 38.75 C ANISOU 668 C GLY A 144 3786 5531 5406 1103 727 -982 C ATOM 669 O GLY A 144 -18.364 -21.158 42.518 1.00 37.55 O ANISOU 669 O GLY A 144 3569 5502 5196 1080 716 -1120 O ATOM 670 N TYR A 145 -19.700 -22.790 43.312 1.00 44.04 N ANISOU 670 N TYR A 145 4526 6032 6177 1159 733 -932 N ATOM 671 CA TYR A 145 -19.120 -23.844 42.486 1.00 44.72 C ANISOU 671 CA TYR A 145 4630 6049 6313 1207 722 -1050 C ATOM 672 C TYR A 145 -19.287 -23.545 40.994 1.00 43.95 C ANISOU 672 C TYR A 145 4514 5981 6205 1047 716 -1175 C ATOM 673 O TYR A 145 -18.303 -23.356 40.262 1.00 43.64 O ANISOU 673 O TYR A 145 4422 6058 6101 1054 720 -1322 O ATOM 674 CB TYR A 145 -19.775 -25.181 42.839 1.00 46.98 C ANISOU 674 CB TYR A 145 5026 6105 6721 1262 738 -959 C ATOM 675 CG TYR A 145 -19.372 -26.340 41.961 1.00 48.08 C ANISOU 675 CG TYR A 145 5219 6121 6930 1300 736 -1082 C ATOM 676 CD1 TYR A 145 -18.153 -26.979 42.138 1.00 48.01 C ANISOU 676 CD1 TYR A 145 5205 6127 6911 1497 732 -1158 C ATOM 677 CD2 TYR A 145 -20.222 -26.809 40.970 1.00 49.72 C ANISOU 677 CD2 TYR A 145 5481 6194 7216 1147 733 -1128 C ATOM 678 CE1 TYR A 145 -17.785 -28.046 41.342 1.00 48.90 C ANISOU 678 CE1 TYR A 145 5378 6110 7091 1549 745 -1281 C ATOM 679 CE2 TYR A 145 -19.864 -27.874 40.169 1.00 50.77 C ANISOU 679 CE2 TYR A 145 5687 6200 7404 1177 737 -1259 C ATOM 680 CZ TYR A 145 -18.645 -28.488 40.359 1.00 50.15 C ANISOU 680 CZ TYR A 145 5616 6124 7317 1384 753 -1336 C ATOM 681 OH TYR A 145 -18.284 -29.551 39.562 1.00 51.49 O ANISOU 681 OH TYR A 145 5868 6152 7544 1432 771 -1477 O ATOM 682 N TYR A 146 -20.542 -23.497 40.555 1.00 49.00 N ANISOU 682 N TYR A 146 5190 6524 6903 903 705 -1114 N ATOM 683 CA TYR A 146 -20.865 -23.231 39.158 1.00 49.06 C ANISOU 683 CA TYR A 146 5201 6554 6886 748 677 -1213 C ATOM 684 C TYR A 146 -20.327 -21.879 38.696 1.00 46.83 C ANISOU 684 C TYR A 146 4856 6464 6471 685 681 -1269 C ATOM 685 O TYR A 146 -19.865 -21.743 37.557 1.00 45.86 O ANISOU 685 O TYR A 146 4739 6408 6276 619 681 -1399 O ATOM 686 CB TYR A 146 -22.377 -23.314 38.931 1.00 49.45 C ANISOU 686 CB TYR A 146 5272 6491 7024 610 642 -1116 C ATOM 687 CG TYR A 146 -22.932 -24.718 39.033 1.00 51.84 C ANISOU 687 CG TYR A 146 5646 6585 7464 614 641 -1096 C ATOM 688 CD1 TYR A 146 -22.993 -25.543 37.919 1.00 53.98 C ANISOU 688 CD1 TYR A 146 5982 6765 7763 539 605 -1227 C ATOM 689 CD2 TYR A 146 -23.393 -25.218 40.243 1.00 53.28 C ANISOU 689 CD2 TYR A 146 5850 6653 7741 685 685 -948 C ATOM 690 CE1 TYR A 146 -23.499 -26.828 38.006 1.00 56.96 C ANISOU 690 CE1 TYR A 146 6440 6926 8274 526 608 -1219 C ATOM 691 CE2 TYR A 146 -23.900 -26.501 40.341 1.00 56.77 C ANISOU 691 CE2 TYR A 146 6373 6881 8316 672 698 -921 C ATOM 692 CZ TYR A 146 -23.951 -27.301 39.218 1.00 58.46 C ANISOU 692 CZ TYR A 146 6648 6992 8571 588 657 -1060 C ATOM 693 OH TYR A 146 -24.455 -28.580 39.309 1.00 61.73 O ANISOU 693 OH TYR A 146 7157 7170 9126 559 672 -1043 O ATOM 694 N PHE A 147 -20.380 -20.885 39.582 1.00 27.69 N ANISOU 694 N PHE A 147 2389 4120 4010 700 694 -1175 N ATOM 695 CA PHE A 147 -19.820 -19.573 39.271 1.00 27.56 C ANISOU 695 CA PHE A 147 2329 4263 3878 634 708 -1223 C ATOM 696 C PHE A 147 -18.331 -19.687 38.957 1.00 28.95 C ANISOU 696 C PHE A 147 2454 4562 3986 690 737 -1375 C ATOM 697 O PHE A 147 -17.850 -19.132 37.965 1.00 29.24 O ANISOU 697 O PHE A 147 2476 4695 3939 594 760 -1473 O ATOM 698 CB PHE A 147 -20.040 -18.593 40.427 1.00 27.06 C ANISOU 698 CB PHE A 147 2246 4244 3793 658 723 -1114 C ATOM 699 CG PHE A 147 -19.479 -17.221 40.172 1.00 27.02 C ANISOU 699 CG PHE A 147 2214 4373 3679 579 743 -1163 C ATOM 700 CD1 PHE A 147 -20.219 -16.271 39.487 1.00 26.14 C ANISOU 700 CD1 PHE A 147 2136 4256 3540 455 737 -1121 C ATOM 701 CD2 PHE A 147 -18.212 -16.880 40.619 1.00 27.99 C ANISOU 701 CD2 PHE A 147 2276 4624 3734 626 762 -1250 C ATOM 702 CE1 PHE A 147 -19.707 -15.009 39.250 1.00 26.17 C ANISOU 702 CE1 PHE A 147 2142 4354 3449 375 766 -1157 C ATOM 703 CE2 PHE A 147 -17.693 -15.621 40.384 1.00 28.06 C ANISOU 703 CE2 PHE A 147 2265 4742 3656 526 789 -1300 C ATOM 704 CZ PHE A 147 -18.443 -14.684 39.699 1.00 27.14 C ANISOU 704 CZ PHE A 147 2209 4591 3510 398 799 -1250 C ATOM 705 N LEU A 148 -17.611 -20.412 39.810 1.00 39.81 N ANISOU 705 N LEU A 148 3795 5937 5395 849 739 -1388 N ATOM 706 CA LEU A 148 -16.183 -20.634 39.618 1.00 39.55 C ANISOU 706 CA LEU A 148 3684 6023 5322 928 759 -1522 C ATOM 707 C LEU A 148 -15.909 -21.313 38.282 1.00 40.10 C ANISOU 707 C LEU A 148 3774 6070 5393 898 793 -1663 C ATOM 708 O LEU A 148 -15.031 -20.886 37.528 1.00 39.68 O ANISOU 708 O LEU A 148 3696 6122 5258 823 817 -1738 O ATOM 709 CB LEU A 148 -15.607 -21.481 40.754 1.00 39.64 C ANISOU 709 CB LEU A 148 3686 6001 5376 1119 724 -1469 C ATOM 710 CG LEU A 148 -14.140 -21.885 40.582 1.00 40.01 C ANISOU 710 CG LEU A 148 3677 6126 5399 1193 710 -1546 C ATOM 711 CD1 LEU A 148 -13.231 -20.666 40.652 1.00 39.38 C ANISOU 711 CD1 LEU A 148 3514 6222 5226 1091 694 -1569 C ATOM 712 CD2 LEU A 148 -13.733 -22.929 41.610 1.00 41.43 C ANISOU 712 CD2 LEU A 148 3860 6243 5639 1413 672 -1495 C ATOM 713 N ARG A 149 -16.667 -22.370 37.994 1.00 66.54 N ANISOU 713 N ARG A 149 7217 9242 8823 917 776 -1648 N ATOM 714 CA ARG A 149 -16.505 -23.094 36.734 1.00 67.41 C ANISOU 714 CA ARG A 149 7382 9306 8926 884 804 -1791 C ATOM 715 C ARG A 149 -16.690 -22.184 35.518 1.00 66.76 C ANISOU 715 C ARG A 149 7321 9320 8726 695 819 -1849 C ATOM 716 O ARG A 149 -15.847 -22.157 34.614 1.00 66.74 O ANISOU 716 O ARG A 149 7300 9417 8642 676 884 -1996 O ATOM 717 CB ARG A 149 -17.475 -24.274 36.660 1.00 72.09 C ANISOU 717 CB ARG A 149 8095 9669 9628 891 767 -1753 C ATOM 718 CG ARG A 149 -17.227 -25.346 37.705 1.00 73.78 C ANISOU 718 CG ARG A 149 8326 9755 9952 1085 767 -1698 C ATOM 719 CD ARG A 149 -18.088 -26.571 37.449 1.00 76.23 C ANISOU 719 CD ARG A 149 8771 9817 10376 1064 751 -1685 C ATOM 720 NE ARG A 149 -17.800 -27.183 36.155 1.00 77.08 N ANISOU 720 NE ARG A 149 8947 9879 10462 1025 774 -1872 N ATOM 721 CZ ARG A 149 -16.875 -28.116 35.959 1.00 77.74 C ANISOU 721 CZ ARG A 149 9057 9904 10577 1186 824 -1999 C ATOM 722 NH1 ARG A 149 -16.141 -28.550 36.976 1.00 78.19 N ANISOU 722 NH1 ARG A 149 9070 9945 10692 1404 838 -1948 N ATOM 723 NH2 ARG A 149 -16.681 -28.617 34.747 1.00 78.16 N ANISOU 723 NH2 ARG A 149 9187 9915 10594 1140 858 -2181 N ATOM 724 N GLU A 150 -17.789 -21.436 35.510 1.00 41.38 N ANISOU 724 N GLU A 150 4147 6076 5499 566 766 -1728 N ATOM 725 CA GLU A 150 -18.099 -20.537 34.402 1.00 41.57 C ANISOU 725 CA GLU A 150 4214 6176 5405 397 762 -1749 C ATOM 726 C GLU A 150 -17.041 -19.449 34.216 1.00 39.81 C ANISOU 726 C GLU A 150 3924 6137 5067 358 837 -1805 C ATOM 727 O GLU A 150 -16.563 -19.218 33.100 1.00 40.42 O ANISOU 727 O GLU A 150 4032 6296 5031 276 892 -1913 O ATOM 728 CB GLU A 150 -19.476 -19.907 34.601 1.00 43.82 C ANISOU 728 CB GLU A 150 4531 6398 5721 304 683 -1588 C ATOM 729 CG GLU A 150 -20.620 -20.890 34.447 1.00 46.43 C ANISOU 729 CG GLU A 150 4919 6566 6157 280 608 -1550 C ATOM 730 CD GLU A 150 -21.038 -21.079 33.004 1.00 48.94 C ANISOU 730 CD GLU A 150 5325 6877 6394 149 553 -1634 C ATOM 731 OE1 GLU A 150 -21.095 -20.073 32.265 1.00 48.31 O ANISOU 731 OE1 GLU A 150 5269 6899 6187 50 537 -1622 O ATOM 732 OE2 GLU A 150 -21.312 -22.233 32.609 1.00 51.31 O ANISOU 732 OE2 GLU A 150 5687 7061 6749 143 522 -1713 O ATOM 733 N ALA A 151 -16.680 -18.785 35.310 1.00 42.59 N ANISOU 733 N ALA A 151 4190 6550 5439 406 847 -1736 N ATOM 734 CA ALA A 151 -15.642 -17.762 35.266 1.00 42.39 C ANISOU 734 CA ALA A 151 4092 6687 5326 350 913 -1789 C ATOM 735 C ALA A 151 -14.350 -18.344 34.701 1.00 43.09 C ANISOU 735 C ALA A 151 4155 6826 5391 380 948 -1888 C ATOM 736 O ALA A 151 -13.664 -17.704 33.897 1.00 43.42 O ANISOU 736 O ALA A 151 4196 6961 5340 269 1006 -1938 O ATOM 737 CB ALA A 151 -15.407 -17.183 36.650 1.00 49.24 C ANISOU 737 CB ALA A 151 4910 7566 6231 398 871 -1679 C ATOM 738 N CYS A 152 -14.037 -19.569 35.113 1.00 50.57 N ANISOU 738 N CYS A 152 5082 7705 6427 536 925 -1913 N ATOM 739 CA CYS A 152 -12.845 -20.258 34.633 1.00 50.43 C ANISOU 739 CA CYS A 152 5028 7724 6407 601 965 -2007 C ATOM 740 C CYS A 152 -12.876 -20.519 33.128 1.00 51.19 C ANISOU 740 C CYS A 152 5200 7826 6421 517 1039 -2131 C ATOM 741 O CYS A 152 -11.903 -20.227 32.430 1.00 52.11 O ANISOU 741 O CYS A 152 5287 8042 6471 463 1107 -2191 O ATOM 742 CB CYS A 152 -12.626 -21.567 35.395 1.00 50.39 C ANISOU 742 CB CYS A 152 5008 7620 6516 806 930 -2000 C ATOM 743 SG CYS A 152 -11.890 -21.362 37.035 1.00 50.90 S ANISOU 743 SG CYS A 152 4964 7744 6629 929 858 -1893 S ATOM 744 N THR A 153 -13.981 -21.066 32.624 1.00 58.28 N ANISOU 744 N THR A 153 6201 8624 7320 500 1029 -2181 N ATOM 745 CA THR A 153 -14.063 -21.362 31.192 1.00 58.96 C ANISOU 745 CA THR A 153 6392 8713 7299 416 1086 -2315 C ATOM 746 C THR A 153 -14.045 -20.089 30.337 1.00 58.30 C ANISOU 746 C THR A 153 6344 8756 7051 229 1132 -2303 C ATOM 747 O THR A 153 -13.422 -20.060 29.267 1.00 58.15 O ANISOU 747 O THR A 153 6374 8798 6921 165 1208 -2380 O ATOM 748 CB THR A 153 -15.269 -22.275 30.828 1.00 59.60 C ANISOU 748 CB THR A 153 6600 8633 7414 412 1027 -2369 C ATOM 749 OG1 THR A 153 -15.211 -22.613 29.436 1.00 62.25 O ANISOU 749 OG1 THR A 153 7057 8975 7622 333 1073 -2517 O ATOM 750 CG2 THR A 153 -16.596 -21.596 31.122 1.00 59.19 C ANISOU 750 CG2 THR A 153 6597 8519 7373 293 906 -2188 C ATOM 751 N TYR A 154 -14.703 -19.036 30.819 1.00 39.17 N ANISOU 751 N TYR A 154 3905 6366 4613 150 1096 -2199 N ATOM 752 CA TYR A 154 -14.670 -17.748 30.130 1.00 39.15 C ANISOU 752 CA TYR A 154 3950 6466 4459 -19 1144 -2165 C ATOM 753 C TYR A 154 -13.249 -17.196 30.071 1.00 40.01 C ANISOU 753 C TYR A 154 3980 6670 4550 -53 1219 -2157 C ATOM 754 O TYR A 154 -12.769 -16.802 29.003 1.00 41.22 O ANISOU 754 O TYR A 154 4193 6892 4576 -162 1303 -2200 O ATOM 755 CB TYR A 154 -15.599 -16.737 30.805 1.00 36.98 C ANISOU 755 CB TYR A 154 3693 6148 4211 -77 1060 -1990 C ATOM 756 CG TYR A 154 -17.040 -16.822 30.355 1.00 35.37 C ANISOU 756 CG TYR A 154 3619 5821 3996 -131 930 -1887 C ATOM 757 CD1 TYR A 154 -17.430 -16.326 29.119 1.00 35.66 C ANISOU 757 CD1 TYR A 154 3793 5884 3873 -264 914 -1876 C ATOM 758 CD2 TYR A 154 -18.012 -17.388 31.168 1.00 33.77 C ANISOU 758 CD2 TYR A 154 3398 5490 3943 -53 821 -1794 C ATOM 759 CE1 TYR A 154 -18.745 -16.398 28.704 1.00 34.40 C ANISOU 759 CE1 TYR A 154 3729 5634 3707 -308 770 -1784 C ATOM 760 CE2 TYR A 154 -19.330 -17.465 30.762 1.00 32.43 C ANISOU 760 CE2 TYR A 154 3312 5228 3784 -112 699 -1706 C ATOM 761 CZ TYR A 154 -19.691 -16.968 29.529 1.00 32.73 C ANISOU 761 CZ TYR A 154 3465 5304 3666 -236 663 -1704 C ATOM 762 OH TYR A 154 -21.003 -17.041 29.120 1.00 31.65 O ANISOU 762 OH TYR A 154 3388 5094 3542 -289 517 -1618 O ATOM 763 N ALA A 155 -12.581 -17.176 31.222 1.00 34.82 N ANISOU 763 N ALA A 155 3194 6021 4014 37 1185 -2107 N ATOM 764 CA ALA A 155 -11.208 -16.687 31.306 1.00 35.84 C ANISOU 764 CA ALA A 155 3219 6254 4145 4 1241 -2124 C ATOM 765 C ALA A 155 -10.275 -17.471 30.389 1.00 37.83 C ANISOU 765 C ALA A 155 3456 6547 4372 41 1326 -2237 C ATOM 766 O ALA A 155 -9.414 -16.892 29.723 1.00 39.12 O ANISOU 766 O ALA A 155 3590 6808 4467 -61 1422 -2274 O ATOM 767 CB ALA A 155 -10.711 -16.742 32.742 1.00 35.35 C ANISOU 767 CB ALA A 155 3029 6199 4202 114 1165 -2075 C ATOM 768 N THR A 156 -10.457 -18.788 30.355 1.00 40.44 N ANISOU 768 N THR A 156 3811 6795 4761 188 1303 -2295 N ATOM 769 CA THR A 156 -9.646 -19.654 29.507 1.00 42.53 C ANISOU 769 CA THR A 156 4077 7075 5006 250 1391 -2411 C ATOM 770 C THR A 156 -9.854 -19.329 28.030 1.00 43.50 C ANISOU 770 C THR A 156 4338 7231 4960 105 1485 -2472 C ATOM 771 O THR A 156 -8.887 -19.140 27.287 1.00 45.76 O ANISOU 771 O THR A 156 4596 7608 5181 57 1600 -2527 O ATOM 772 CB THR A 156 -9.963 -21.142 29.750 1.00 42.94 C ANISOU 772 CB THR A 156 4168 6995 5152 434 1351 -2465 C ATOM 773 OG1 THR A 156 -9.790 -21.450 31.138 1.00 42.23 O ANISOU 773 OG1 THR A 156 3973 6871 5202 577 1265 -2389 O ATOM 774 CG2 THR A 156 -9.041 -22.024 28.922 1.00 45.37 C ANISOU 774 CG2 THR A 156 4479 7313 5446 517 1456 -2588 C ATOM 775 N ALA A 157 -11.117 -19.259 27.613 1.00 47.40 N ANISOU 775 N ALA A 157 4981 7658 5372 33 1435 -2463 N ATOM 776 CA ALA A 157 -11.448 -18.942 26.226 1.00 48.93 C ANISOU 776 CA ALA A 157 5339 7884 5370 -108 1498 -2509 C ATOM 777 C ALA A 157 -10.857 -17.599 25.794 1.00 48.74 C ANISOU 777 C ALA A 157 5305 7978 5238 -266 1588 -2447 C ATOM 778 O ALA A 157 -10.191 -17.500 24.753 1.00 50.12 O ANISOU 778 O ALA A 157 5534 8217 5293 -330 1706 -2502 O ATOM 779 CB ALA A 157 -12.957 -18.948 26.027 1.00 47.35 C ANISOU 779 CB ALA A 157 5284 7611 5098 -168 1396 -2498 C ATOM 780 N LEU A 158 -11.097 -16.571 26.604 1.00 40.37 N ANISOU 780 N LEU A 158 4183 6935 4219 -328 1543 -2335 N ATOM 781 CA LEU A 158 -10.589 -15.234 26.312 1.00 40.83 C ANISOU 781 CA LEU A 158 4244 7078 4192 -489 1628 -2274 C ATOM 782 C LEU A 158 -9.063 -15.202 26.263 1.00 42.53 C ANISOU 782 C LEU A 158 4314 7386 4460 -485 1736 -2330 C ATOM 783 O LEU A 158 -8.479 -14.498 25.440 1.00 44.03 O ANISOU 783 O LEU A 158 4541 7649 4541 -621 1858 -2334 O ATOM 784 CB LEU A 158 -11.110 -14.220 27.332 1.00 38.98 C ANISOU 784 CB LEU A 158 3975 6823 4013 -539 1558 -2158 C ATOM 785 CG LEU A 158 -12.619 -13.967 27.325 1.00 37.57 C ANISOU 785 CG LEU A 158 3931 6578 3767 -565 1472 -2090 C ATOM 786 CD1 LEU A 158 -12.986 -12.885 28.330 1.00 36.11 C ANISOU 786 CD1 LEU A 158 3705 6374 3640 -605 1435 -1979 C ATOM 787 CD2 LEU A 158 -13.096 -13.594 25.929 1.00 38.72 C ANISOU 787 CD2 LEU A 158 4282 6745 3684 -697 1518 -2088 C ATOM 788 N ASN A 159 -8.422 -15.966 27.143 1.00 59.65 N ANISOU 788 N ASN A 159 6319 9556 6791 -331 1693 -2372 N ATOM 789 CA ASN A 159 -6.968 -16.080 27.127 1.00 61.48 C ANISOU 789 CA ASN A 159 6392 9891 7079 -305 1785 -2442 C ATOM 790 C ASN A 159 -6.464 -16.724 25.838 1.00 63.74 C ANISOU 790 C ASN A 159 6741 10209 7269 -294 1920 -2543 C ATOM 791 O ASN A 159 -5.446 -16.307 25.282 1.00 65.55 O ANISOU 791 O ASN A 159 6908 10542 7456 -375 2055 -2583 O ATOM 792 CB ASN A 159 -6.467 -16.863 28.342 1.00 61.52 C ANISOU 792 CB ASN A 159 6227 9889 7260 -118 1694 -2459 C ATOM 793 CG ASN A 159 -6.411 -16.017 29.599 1.00 60.38 C ANISOU 793 CG ASN A 159 5978 9771 7194 -153 1601 -2383 C ATOM 794 OD1 ASN A 159 -6.053 -14.840 29.553 1.00 60.47 O ANISOU 794 OD1 ASN A 159 5959 9854 7164 -317 1650 -2364 O ATOM 795 ND2 ASN A 159 -6.766 -16.614 30.731 1.00 60.18 N ANISOU 795 ND2 ASN A 159 5911 9681 7274 -2 1472 -2343 N ATOM 796 N VAL A 160 -7.183 -17.739 25.368 1.00 64.93 N ANISOU 796 N VAL A 160 7022 10268 7382 -198 1890 -2591 N ATOM 797 CA VAL A 160 -6.837 -18.402 24.115 1.00 67.11 C ANISOU 797 CA VAL A 160 7398 10557 7545 -181 2014 -2698 C ATOM 798 C VAL A 160 -6.936 -17.438 22.937 1.00 67.84 C ANISOU 798 C VAL A 160 7639 10711 7428 -380 2119 -2673 C ATOM 799 O VAL A 160 -5.994 -17.306 22.149 1.00 70.75 O ANISOU 799 O VAL A 160 7987 11169 7725 -425 2277 -2727 O ATOM 800 CB VAL A 160 -7.736 -19.627 23.850 1.00 66.41 C ANISOU 800 CB VAL A 160 7455 10337 7441 -66 1944 -2765 C ATOM 801 CG1 VAL A 160 -7.537 -20.138 22.430 1.00 69.18 C ANISOU 801 CG1 VAL A 160 7965 10696 7627 -82 2066 -2877 C ATOM 802 CG2 VAL A 160 -7.448 -20.724 24.862 1.00 66.11 C ANISOU 802 CG2 VAL A 160 7290 10227 7601 147 1878 -2798 C ATOM 803 N VAL A 161 -8.077 -16.762 22.824 1.00 48.52 N ANISOU 803 N VAL A 161 5342 8216 4876 -493 2038 -2586 N ATOM 804 CA VAL A 161 -8.285 -15.799 21.744 1.00 49.53 C ANISOU 804 CA VAL A 161 5644 8390 4786 -677 2121 -2535 C ATOM 805 C VAL A 161 -7.235 -14.689 21.778 1.00 50.55 C ANISOU 805 C VAL A 161 5663 8618 4925 -804 2249 -2489 C ATOM 806 O VAL A 161 -6.663 -14.320 20.746 1.00 52.81 O ANISOU 806 O VAL A 161 6026 8972 5068 -905 2401 -2507 O ATOM 807 CB VAL A 161 -9.690 -15.171 21.810 1.00 47.69 C ANISOU 807 CB VAL A 161 5569 8093 4457 -765 1993 -2428 C ATOM 808 CG1 VAL A 161 -9.884 -14.181 20.673 1.00 49.05 C ANISOU 808 CG1 VAL A 161 5943 8307 4386 -943 2073 -2356 C ATOM 809 CG2 VAL A 161 -10.753 -16.254 21.762 1.00 46.97 C ANISOU 809 CG2 VAL A 161 5581 7911 4354 -666 1861 -2488 C ATOM 810 N SER A 162 -6.980 -14.172 22.976 1.00 49.09 N ANISOU 810 N SER A 162 5305 8440 4907 -803 2188 -2438 N ATOM 811 CA SER A 162 -5.989 -13.121 23.165 1.00 50.08 C ANISOU 811 CA SER A 162 5311 8651 5065 -935 2289 -2412 C ATOM 812 C SER A 162 -4.606 -13.589 22.729 1.00 52.77 C ANISOU 812 C SER A 162 5510 9099 5441 -899 2439 -2524 C ATOM 813 O SER A 162 -3.862 -12.840 22.098 1.00 54.78 O ANISOU 813 O SER A 162 5760 9434 5620 -1047 2594 -2524 O ATOM 814 CB SER A 162 -5.955 -12.668 24.625 1.00 48.18 C ANISOU 814 CB SER A 162 4909 8397 5001 -915 2172 -2366 C ATOM 815 OG SER A 162 -5.064 -11.581 24.796 1.00 49.29 O ANISOU 815 OG SER A 162 4951 8613 5165 -1069 2263 -2355 O ATOM 816 N LEU A 163 -4.269 -14.831 23.064 1.00 53.01 N ANISOU 816 N LEU A 163 5429 9128 5586 -700 2403 -2615 N ATOM 817 CA LEU A 163 -3.001 -15.416 22.639 1.00 55.78 C ANISOU 817 CA LEU A 163 5642 9577 5975 -628 2547 -2726 C ATOM 818 C LEU A 163 -2.931 -15.543 21.122 1.00 58.13 C ANISOU 818 C LEU A 163 6117 9899 6070 -687 2714 -2773 C ATOM 819 O LEU A 163 -1.866 -15.371 20.525 1.00 60.84 O ANISOU 819 O LEU A 163 6381 10352 6384 -735 2893 -2830 O ATOM 820 CB LEU A 163 -2.786 -16.782 23.293 1.00 55.63 C ANISOU 820 CB LEU A 163 5505 9521 6109 -380 2467 -2801 C ATOM 821 CG LEU A 163 -2.090 -16.758 24.653 1.00 55.11 C ANISOU 821 CG LEU A 163 5186 9508 6245 -298 2377 -2795 C ATOM 822 CD1 LEU A 163 -2.043 -18.151 25.256 1.00 55.00 C ANISOU 822 CD1 LEU A 163 5105 9432 6362 -41 2291 -2845 C ATOM 823 CD2 LEU A 163 -0.688 -16.183 24.514 1.00 57.70 C ANISOU 823 CD2 LEU A 163 5317 9997 6608 -382 2521 -2848 C ATOM 824 N SER A 164 -4.069 -15.844 20.504 1.00 57.29 N ANISOU 824 N SER A 164 6253 9698 5817 -686 2654 -2754 N ATOM 825 CA SER A 164 -4.143 -15.919 19.049 1.00 59.53 C ANISOU 825 CA SER A 164 6750 10000 5868 -749 2787 -2791 C ATOM 826 C SER A 164 -3.845 -14.558 18.426 1.00 60.78 C ANISOU 826 C SER A 164 6977 10232 5885 -974 2917 -2705 C ATOM 827 O SER A 164 -3.074 -14.457 17.468 1.00 63.70 O ANISOU 827 O SER A 164 7376 10686 6140 -1028 3108 -2752 O ATOM 828 CB SER A 164 -5.516 -16.423 18.600 1.00 58.36 C ANISOU 828 CB SER A 164 6852 9740 5582 -722 2658 -2784 C ATOM 829 OG SER A 164 -5.765 -17.729 19.087 1.00 57.66 O ANISOU 829 OG SER A 164 6722 9569 5619 -526 2561 -2874 O ATOM 830 N VAL A 165 -4.455 -13.514 18.981 1.00 58.78 N ANISOU 830 N VAL A 165 6757 9937 5639 -1100 2823 -2578 N ATOM 831 CA VAL A 165 -4.219 -12.155 18.502 1.00 59.95 C ANISOU 831 CA VAL A 165 6987 10125 5667 -1319 2940 -2482 C ATOM 832 C VAL A 165 -2.756 -11.748 18.676 1.00 62.03 C ANISOU 832 C VAL A 165 7022 10504 6044 -1386 3103 -2533 C ATOM 833 O VAL A 165 -2.131 -11.228 17.748 1.00 64.76 O ANISOU 833 O VAL A 165 7429 10918 6260 -1516 3294 -2529 O ATOM 834 CB VAL A 165 -5.113 -11.133 19.229 1.00 57.45 C ANISOU 834 CB VAL A 165 6734 9726 5368 -1422 2807 -2341 C ATOM 835 CG1 VAL A 165 -4.831 -9.731 18.721 1.00 58.98 C ANISOU 835 CG1 VAL A 165 7034 9936 5440 -1648 2941 -2238 C ATOM 836 CG2 VAL A 165 -6.580 -11.481 19.046 1.00 55.66 C ANISOU 836 CG2 VAL A 165 6721 9402 5027 -1364 2647 -2288 C ATOM 837 N GLU A 166 -2.219 -11.992 19.868 1.00 80.30 N ANISOU 837 N GLU A 166 9074 12844 8593 -1299 3025 -2579 N ATOM 838 CA GLU A 166 -0.833 -11.656 20.183 1.00 82.63 C ANISOU 838 CA GLU A 166 9119 13262 9015 -1356 3147 -2640 C ATOM 839 C GLU A 166 0.147 -12.358 19.249 1.00 85.73 C ANISOU 839 C GLU A 166 9453 13759 9360 -1292 3343 -2752 C ATOM 840 O GLU A 166 1.092 -11.743 18.756 1.00 88.70 O ANISOU 840 O GLU A 166 9759 14238 9705 -1429 3532 -2769 O ATOM 841 CB GLU A 166 -0.510 -12.008 21.638 1.00 80.89 C ANISOU 841 CB GLU A 166 8642 13057 9035 -1233 2994 -2680 C ATOM 842 CG GLU A 166 -1.242 -11.161 22.669 1.00 78.32 C ANISOU 842 CG GLU A 166 8339 12651 8769 -1311 2830 -2581 C ATOM 843 CD GLU A 166 -0.724 -9.737 22.737 1.00 79.54 C ANISOU 843 CD GLU A 166 8474 12840 8907 -1558 2924 -2535 C ATOM 844 OE1 GLU A 166 0.438 -9.505 22.340 1.00 81.95 O ANISOU 844 OE1 GLU A 166 8642 13262 9231 -1648 3087 -2601 O ATOM 845 OE2 GLU A 166 -1.479 -8.851 23.188 1.00 78.21 O ANISOU 845 OE2 GLU A 166 8428 12578 8710 -1664 2843 -2435 O ATOM 846 N LEU A 167 -0.082 -13.646 19.010 1.00 67.79 N ANISOU 846 N LEU A 167 7216 11457 7084 -1084 3308 -2831 N ATOM 847 CA LEU A 167 0.778 -14.413 18.115 1.00 71.06 C ANISOU 847 CA LEU A 167 7595 11957 7447 -993 3498 -2946 C ATOM 848 C LEU A 167 0.672 -13.907 16.681 1.00 73.35 C ANISOU 848 C LEU A 167 8127 12270 7472 -1142 3679 -2919 C ATOM 849 O LEU A 167 1.683 -13.762 15.990 1.00 76.69 O ANISOU 849 O LEU A 167 8481 12810 7848 -1194 3902 -2973 O ATOM 850 CB LEU A 167 0.443 -15.905 18.173 1.00 70.58 C ANISOU 850 CB LEU A 167 7564 11827 7429 -738 3417 -3037 C ATOM 851 CG LEU A 167 1.292 -16.792 17.257 1.00 74.14 C ANISOU 851 CG LEU A 167 7998 12350 7824 -616 3620 -3168 C ATOM 852 CD1 LEU A 167 2.770 -16.655 17.594 1.00 76.63 C ANISOU 852 CD1 LEU A 167 7997 12819 8300 -600 3762 -3227 C ATOM 853 CD2 LEU A 167 0.855 -18.245 17.342 1.00 73.67 C ANISOU 853 CD2 LEU A 167 8005 12184 7800 -371 3532 -3257 C ATOM 854 N TYR A 168 -0.555 -13.639 16.238 1.00 73.50 N ANISOU 854 N TYR A 168 8429 12185 7312 -1207 3583 -2831 N ATOM 855 CA TYR A 168 -0.770 -13.123 14.890 1.00 75.66 C ANISOU 855 CA TYR A 168 8970 12475 7305 -1345 3724 -2784 C ATOM 856 C TYR A 168 -0.052 -11.796 14.682 1.00 77.47 C ANISOU 856 C TYR A 168 9157 12778 7502 -1575 3890 -2704 C ATOM 857 O TYR A 168 0.534 -11.565 13.630 1.00 80.76 O ANISOU 857 O TYR A 168 9657 13272 7756 -1659 4105 -2718 O ATOM 858 CB TYR A 168 -2.260 -12.965 14.580 1.00 74.28 C ANISOU 858 CB TYR A 168 9093 12179 6950 -1378 3556 -2687 C ATOM 859 CG TYR A 168 -2.520 -12.312 13.239 1.00 76.36 C ANISOU 859 CG TYR A 168 9649 12461 6905 -1527 3677 -2613 C ATOM 860 CD1 TYR A 168 -2.439 -13.044 12.061 1.00 79.24 C ANISOU 860 CD1 TYR A 168 10181 12864 7062 -1460 3786 -2703 C ATOM 861 CD2 TYR A 168 -2.839 -10.963 13.150 1.00 76.16 C ANISOU 861 CD2 TYR A 168 9747 12407 6785 -1728 3685 -2451 C ATOM 862 CE1 TYR A 168 -2.671 -12.450 10.833 1.00 82.15 C ANISOU 862 CE1 TYR A 168 10830 13257 7126 -1589 3890 -2628 C ATOM 863 CE2 TYR A 168 -3.071 -10.361 11.927 1.00 79.31 C ANISOU 863 CE2 TYR A 168 10429 12816 6888 -1855 3791 -2365 C ATOM 864 CZ TYR A 168 -2.987 -11.109 10.772 1.00 82.13 C ANISOU 864 CZ TYR A 168 10946 13227 7033 -1784 3888 -2452 C ATOM 865 OH TYR A 168 -3.220 -10.514 9.554 1.00 84.93 O ANISOU 865 OH TYR A 168 11595 13599 7074 -1903 3985 -2361 O ATOM 866 N LEU A 169 -0.101 -10.926 15.685 1.00 83.51 N ANISOU 866 N LEU A 169 9803 13513 8415 -1681 3796 -2625 N ATOM 867 CA LEU A 169 0.577 -9.637 15.598 1.00 85.85 C ANISOU 867 CA LEU A 169 10059 13858 8702 -1915 3945 -2556 C ATOM 868 C LEU A 169 2.089 -9.793 15.718 1.00 89.18 C ANISOU 868 C LEU A 169 10177 14431 9277 -1915 4121 -2672 C ATOM 869 O LEU A 169 2.849 -8.967 15.212 1.00 92.60 O ANISOU 869 O LEU A 169 10588 14934 9660 -2101 4320 -2649 O ATOM 870 CB LEU A 169 0.056 -8.670 16.664 1.00 83.94 C ANISOU 870 CB LEU A 169 9800 13524 8567 -2028 3790 -2449 C ATOM 871 CG LEU A 169 -1.064 -7.720 16.230 1.00 83.07 C ANISOU 871 CG LEU A 169 10015 13292 8257 -2164 3740 -2282 C ATOM 872 CD1 LEU A 169 -2.304 -8.490 15.810 1.00 81.40 C ANISOU 872 CD1 LEU A 169 10013 13002 7912 -2014 3582 -2261 C ATOM 873 CD2 LEU A 169 -1.393 -6.732 17.339 1.00 80.79 C ANISOU 873 CD2 LEU A 169 9682 12919 8095 -2282 3631 -2192 C ATOM 874 N ALA A 170 2.521 -10.858 16.386 1.00 90.97 N ANISOU 874 N ALA A 170 10171 14704 9689 -1705 4048 -2791 N ATOM 875 CA ALA A 170 3.944 -11.127 16.554 1.00 93.88 C ANISOU 875 CA ALA A 170 10230 15226 10213 -1667 4196 -2905 C ATOM 876 C ALA A 170 4.495 -11.930 15.381 1.00 97.00 C ANISOU 876 C ALA A 170 10667 15705 10484 -1567 4412 -2998 C ATOM 877 O ALA A 170 5.682 -12.254 15.344 1.00100.36 O ANISOU 877 O ALA A 170 10845 16267 11017 -1514 4567 -3098 O ATOM 878 CB ALA A 170 4.198 -11.856 17.864 1.00 91.75 C ANISOU 878 CB ALA A 170 9691 14969 10198 -1477 4014 -2977 C ATOM 879 N ILE A 171 3.629 -12.250 14.426 1.00131.08 N ANISOU 879 N ILE A 171 15296 19944 14565 -1538 4420 -2970 N ATOM 880 CA ILE A 171 4.040 -13.015 13.253 1.00134.61 C ANISOU 880 CA ILE A 171 15834 20458 14855 -1440 4620 -3064 C ATOM 881 C ILE A 171 3.719 -12.267 11.957 1.00136.51 C ANISOU 881 C ILE A 171 16384 20697 14787 -1622 4774 -2978 C ATOM 882 O ILE A 171 4.175 -12.646 10.879 1.00139.69 O ANISOU 882 O ILE A 171 16874 21178 15025 -1589 4984 -3045 O ATOM 883 CB ILE A 171 3.385 -14.413 13.239 1.00131.42 C ANISOU 883 CB ILE A 171 15526 19968 14441 -1181 4486 -3151 C ATOM 884 CG1 ILE A 171 4.277 -15.421 12.513 1.00134.86 C ANISOU 884 CG1 ILE A 171 15892 20498 14850 -1010 4695 -3302 C ATOM 885 CG2 ILE A 171 1.990 -14.354 12.628 1.00130.55 C ANISOU 885 CG2 ILE A 171 15784 19730 14088 -1220 4362 -3076 C ATOM 886 CD1 ILE A 171 3.805 -16.847 12.651 1.00133.72 C ANISOU 886 CD1 ILE A 171 15801 20258 14748 -743 4572 -3407 C ATOM 887 N ARG A 172 2.938 -11.197 12.077 1.00114.62 N ANISOU 887 N ARG A 172 13784 17833 11931 -1805 4672 -2827 N ATOM 888 CA ARG A 172 2.569 -10.368 10.934 1.00117.17 C ANISOU 888 CA ARG A 172 14419 18140 11959 -1985 4793 -2713 C ATOM 889 C ARG A 172 3.492 -9.157 10.840 1.00119.98 C ANISOU 889 C ARG A 172 14676 18566 12342 -2228 4994 -2645 C ATOM 890 O ARG A 172 3.782 -8.667 9.748 1.00124.03 O ANISOU 890 O ARG A 172 15362 19126 12638 -2360 5207 -2594 O ATOM 891 CB ARG A 172 1.105 -9.929 11.044 1.00117.00 C ANISOU 891 CB ARG A 172 14676 17966 11813 -2027 4560 -2576 C ATOM 892 CG ARG A 172 0.671 -8.843 10.069 1.00119.09 C ANISOU 892 CG ARG A 172 15256 18193 11799 -2230 4645 -2414 C ATOM 893 CD ARG A 172 0.777 -9.289 8.620 1.00123.15 C ANISOU 893 CD ARG A 172 16004 18775 12011 -2203 4814 -2450 C ATOM 894 NE ARG A 172 0.301 -8.250 7.710 1.00125.03 N ANISOU 894 NE ARG A 172 16567 18972 11965 -2385 4872 -2276 N ATOM 895 CZ ARG A 172 0.367 -8.325 6.385 1.00129.39 C ANISOU 895 CZ ARG A 172 17366 19584 12212 -2410 5030 -2266 C ATOM 896 NH1 ARG A 172 0.897 -9.392 5.804 1.00132.11 N ANISOU 896 NH1 ARG A 172 17666 20031 12496 -2267 5158 -2432 N ATOM 897 NH2 ARG A 172 -0.094 -7.329 5.641 1.00131.28 N ANISOU 897 NH2 ARG A 172 17906 19777 12197 -2571 5063 -2087 N ATOM 898 N HIS A 173 3.969 -8.689 11.990 1.00155.79 N ANISOU 898 N HIS A 173 18938 23111 17143 -2289 4928 -2649 N ATOM 899 CA HIS A 173 4.918 -7.580 12.021 1.00158.96 C ANISOU 899 CA HIS A 173 19210 23579 17606 -2526 5111 -2609 C ATOM 900 C HIS A 173 6.225 -7.901 12.757 1.00160.47 C ANISOU 900 C HIS A 173 18981 23919 18071 -2482 5192 -2747 C ATOM 901 O HIS A 173 6.558 -7.233 13.736 1.00160.44 O ANISOU 901 O HIS A 173 18783 23916 18259 -2599 5125 -2736 O ATOM 902 CB HIS A 173 4.270 -6.349 12.662 1.00150.08 C ANISOU 902 CB HIS A 173 18188 22319 16515 -2711 4969 -2464 C ATOM 903 CG HIS A 173 2.994 -5.925 12.006 1.00148.79 C ANISOU 903 CG HIS A 173 18426 22014 16092 -2762 4889 -2308 C ATOM 904 ND1 HIS A 173 2.947 -4.960 11.023 1.00151.13 N ANISOU 904 ND1 HIS A 173 18979 22276 16166 -2967 5055 -2173 N ATOM 905 CD2 HIS A 173 1.716 -6.330 12.196 1.00145.75 C ANISOU 905 CD2 HIS A 173 18228 21516 15633 -2630 4657 -2259 C ATOM 906 CE1 HIS A 173 1.696 -4.792 10.633 1.00149.50 C ANISOU 906 CE1 HIS A 173 19103 21945 15754 -2949 4916 -2044 C ATOM 907 NE2 HIS A 173 0.929 -5.611 11.329 1.00146.43 N ANISOU 907 NE2 HIS A 173 18671 21513 15453 -2750 4675 -2098 N ATOM 908 N PRO A 174 6.975 -8.919 12.296 1.00146.16 N ANISOU 908 N PRO A 174 17026 22232 16274 -2310 5332 -2880 N ATOM 909 CA PRO A 174 8.268 -9.162 12.931 1.00148.14 C ANISOU 909 CA PRO A 174 16873 22640 16773 -2278 5428 -2998 C ATOM 910 C PRO A 174 9.413 -8.801 11.991 1.00152.97 C ANISOU 910 C PRO A 174 17418 23405 17297 -2397 5777 -3032 C ATOM 911 O PRO A 174 10.426 -8.268 12.444 1.00154.38 O ANISOU 911 O PRO A 174 17335 23693 17630 -2547 5897 -3055 O ATOM 912 CB PRO A 174 8.242 -10.674 13.158 1.00146.27 C ANISOU 912 CB PRO A 174 16516 22420 16640 -1953 5317 -3122 C ATOM 913 CG PRO A 174 7.284 -11.214 12.075 1.00145.38 C ANISOU 913 CG PRO A 174 16770 22208 16259 -1847 5305 -3101 C ATOM 914 CD PRO A 174 6.645 -10.026 11.387 1.00145.68 C ANISOU 914 CD PRO A 174 17129 22169 16051 -2094 5359 -2949 C ATOM 915 N LEU A 180 3.288 -3.495 20.852 1.00138.31 N ANISOU 915 N LEU A 180 15859 20492 16201 -2901 3845 -2459 N ATOM 916 CA LEU A 180 3.126 -2.685 22.054 1.00136.50 C ANISOU 916 CA LEU A 180 15580 20195 16089 -3002 3717 -2451 C ATOM 917 C LEU A 180 2.815 -3.561 23.263 1.00132.95 C ANISOU 917 C LEU A 180 14958 19769 15787 -2771 3473 -2520 C ATOM 918 O LEU A 180 3.508 -4.548 23.513 1.00132.14 O ANISOU 918 O LEU A 180 14608 19806 15795 -2607 3443 -2634 O ATOM 919 CB LEU A 180 2.029 -1.634 21.864 1.00124.37 C ANISOU 919 CB LEU A 180 14382 18456 14419 -3143 3704 -2287 C ATOM 920 CG LEU A 180 2.323 -0.452 20.932 1.00127.47 C ANISOU 920 CG LEU A 180 14970 18785 14680 -3415 3928 -2194 C ATOM 921 CD1 LEU A 180 3.707 0.122 21.206 1.00130.71 C ANISOU 921 CD1 LEU A 180 15138 19307 15219 -3611 4067 -2301 C ATOM 922 CD2 LEU A 180 2.167 -0.830 19.462 1.00129.11 C ANISOU 922 CD2 LEU A 180 15368 19009 14680 -3385 4076 -2127 C ATOM 923 N MET A 181 1.772 -3.192 24.003 1.00154.22 N ANISOU 923 N MET A 181 17793 22324 18481 -2752 3310 -2443 N ATOM 924 CA MET A 181 1.352 -3.928 25.195 1.00152.01 C ANISOU 924 CA MET A 181 17386 22048 18323 -2540 3080 -2487 C ATOM 925 C MET A 181 2.486 -4.116 26.199 1.00152.96 C ANISOU 925 C MET A 181 17175 22322 18621 -2517 3026 -2629 C ATOM 926 O MET A 181 3.043 -5.207 26.318 1.00153.14 O ANISOU 926 O MET A 181 16998 22463 18724 -2321 2979 -2714 O ATOM 927 CB MET A 181 0.755 -5.287 24.816 1.00142.41 C ANISOU 927 CB MET A 181 16208 20832 17071 -2279 3002 -2480 C ATOM 928 CG MET A 181 -0.680 -5.228 24.317 1.00140.22 C ANISOU 928 CG MET A 181 16234 20396 16647 -2245 2950 -2343 C ATOM 929 SD MET A 181 -1.852 -4.820 25.625 1.00136.65 S ANISOU 929 SD MET A 181 15851 19809 16259 -2193 2734 -2270 S ATOM 930 CE MET A 181 -3.404 -4.940 24.738 1.00134.95 C ANISOU 930 CE MET A 181 15968 19450 15858 -2139 2706 -2118 C ATOM 931 N SER A 182 2.824 -3.050 26.917 1.00108.00 N ANISOU 931 N SER A 182 11430 16623 12983 -2715 3030 -2655 N ATOM 932 CA SER A 182 3.858 -3.121 27.943 1.00110.46 C ANISOU 932 CA SER A 182 11432 17088 13449 -2710 2960 -2792 C ATOM 933 C SER A 182 3.409 -4.020 29.091 1.00108.04 C ANISOU 933 C SER A 182 11028 16796 13225 -2454 2720 -2820 C ATOM 934 O SER A 182 2.238 -4.391 29.173 1.00106.09 O ANISOU 934 O SER A 182 10967 16418 12923 -2329 2615 -2728 O ATOM 935 CB SER A 182 4.205 -1.724 28.462 1.00110.70 C ANISOU 935 CB SER A 182 11466 17089 13507 -2993 3009 -2815 C ATOM 936 OG SER A 182 3.065 -1.083 29.009 1.00107.91 O ANISOU 936 OG SER A 182 11340 16555 13106 -3035 2914 -2728 O ATOM 937 N ARG A 183 4.348 -4.367 29.968 1.00132.38 N ANISOU 937 N ARG A 183 13820 20042 16435 -2377 2636 -2940 N ATOM 938 CA ARG A 183 4.083 -5.262 31.092 1.00131.23 C ANISOU 938 CA ARG A 183 13566 19930 16365 -2121 2414 -2966 C ATOM 939 C ARG A 183 2.890 -4.798 31.923 1.00128.17 C ANISOU 939 C ARG A 183 13364 19393 15941 -2118 2272 -2893 C ATOM 940 O ARG A 183 1.989 -5.585 32.234 1.00126.35 O ANISOU 940 O ARG A 183 13222 19085 15699 -1905 2145 -2829 O ATOM 941 CB ARG A 183 5.325 -5.375 31.978 1.00134.09 C ANISOU 941 CB ARG A 183 13601 20493 16856 -2099 2346 -3100 C ATOM 942 CG ARG A 183 6.567 -5.852 31.241 1.00138.28 C ANISOU 942 CG ARG A 183 13907 21188 17446 -2089 2490 -3177 C ATOM 943 CD ARG A 183 7.799 -5.784 32.127 1.00141.55 C ANISOU 943 CD ARG A 183 13986 21807 17991 -2102 2424 -3304 C ATOM 944 NE ARG A 183 7.657 -6.600 33.329 1.00140.94 N ANISOU 944 NE ARG A 183 13799 21778 17976 -1847 2187 -3324 N ATOM 945 CZ ARG A 183 8.022 -7.875 33.414 1.00142.57 C ANISOU 945 CZ ARG A 183 13857 22065 18249 -1569 2124 -3342 C ATOM 946 NH1 ARG A 183 8.553 -8.486 32.363 1.00144.43 N ANISOU 946 NH1 ARG A 183 14028 22349 18502 -1508 2285 -3354 N ATOM 947 NH2 ARG A 183 7.855 -8.541 34.549 1.00141.91 N ANISOU 947 NH2 ARG A 183 13699 22009 18210 -1349 1908 -3344 N ATOM 948 N SER A 184 2.890 -3.515 32.269 1.00125.63 N ANISOU 948 N SER A 184 13103 19025 15604 -2359 2309 -2902 N ATOM 949 CA SER A 184 1.797 -2.917 33.024 1.00122.72 C ANISOU 949 CA SER A 184 12918 18510 15201 -2384 2210 -2838 C ATOM 950 C SER A 184 0.475 -3.063 32.277 1.00119.95 C ANISOU 950 C SER A 184 12850 17976 14750 -2322 2237 -2686 C ATOM 951 O SER A 184 -0.485 -3.615 32.811 1.00117.65 O ANISOU 951 O SER A 184 12632 17613 14457 -2138 2101 -2627 O ATOM 952 CB SER A 184 2.084 -1.440 33.305 1.00121.27 C ANISOU 952 CB SER A 184 12783 18283 15013 -2686 2291 -2873 C ATOM 953 OG SER A 184 2.302 -0.724 32.102 1.00122.44 O ANISOU 953 OG SER A 184 13059 18366 15097 -2902 2499 -2824 O ATOM 954 N ARG A 185 0.441 -2.579 31.038 1.00 97.81 N ANISOU 954 N ARG A 185 10201 15105 11858 -2473 2412 -2621 N ATOM 955 CA ARG A 185 -0.762 -2.645 30.213 1.00 95.41 C ANISOU 955 CA ARG A 185 10168 14643 11439 -2431 2445 -2474 C ATOM 956 C ARG A 185 -1.246 -4.078 30.000 1.00 94.16 C ANISOU 956 C ARG A 185 9989 14505 11281 -2150 2346 -2452 C ATOM 957 O ARG A 185 -2.450 -4.341 29.997 1.00 92.88 O ANISOU 957 O ARG A 185 9994 14225 11073 -2039 2267 -2352 O ATOM 958 CB ARG A 185 -0.530 -1.957 28.865 1.00 98.28 C ANISOU 958 CB ARG A 185 10687 14963 11693 -2632 2655 -2416 C ATOM 959 CG ARG A 185 -0.451 -0.441 28.950 1.00100.27 C ANISOU 959 CG ARG A 185 11076 15107 11916 -2916 2760 -2381 C ATOM 960 CD ARG A 185 -0.306 0.191 27.574 1.00103.30 C ANISOU 960 CD ARG A 185 11652 15427 12171 -3096 2967 -2292 C ATOM 961 NE ARG A 185 1.017 -0.034 26.999 1.00107.74 N ANISOU 961 NE ARG A 185 12022 16150 12765 -3184 3106 -2393 N ATOM 962 CZ ARG A 185 1.396 0.409 25.804 1.00111.52 C ANISOU 962 CZ ARG A 185 12619 16614 13140 -3342 3308 -2339 C ATOM 963 NH1 ARG A 185 0.550 1.100 25.052 1.00111.79 N ANISOU 963 NH1 ARG A 185 12978 16477 13022 -3423 3379 -2179 N ATOM 964 NH2 ARG A 185 2.621 0.160 25.360 1.00114.94 N ANISOU 964 NH2 ARG A 185 12847 17208 13618 -3412 3440 -2438 N ATOM 965 N THR A 186 -0.303 -5.000 29.825 1.00 73.97 N ANISOU 965 N THR A 186 7229 12094 8784 -2038 2357 -2545 N ATOM 966 CA THR A 186 -0.636 -6.409 29.642 1.00 72.76 C ANISOU 966 CA THR A 186 7054 11949 8642 -1776 2276 -2538 C ATOM 967 C THR A 186 -1.298 -6.986 30.890 1.00 70.66 C ANISOU 967 C THR A 186 6750 11646 8452 -1578 2068 -2524 C ATOM 968 O THR A 186 -2.329 -7.657 30.799 1.00 68.63 O ANISOU 968 O THR A 186 6623 11287 8165 -1428 1992 -2446 O ATOM 969 CB THR A 186 0.605 -7.247 29.275 1.00 75.98 C ANISOU 969 CB THR A 186 7243 12516 9111 -1690 2345 -2647 C ATOM 970 OG1 THR A 186 1.073 -6.863 27.976 1.00 77.77 O ANISOU 970 OG1 THR A 186 7541 12763 9244 -1839 2552 -2642 O ATOM 971 CG2 THR A 186 0.266 -8.730 29.262 1.00 75.13 C ANISOU 971 CG2 THR A 186 7110 12399 9038 -1406 2245 -2648 C ATOM 972 N LYS A 187 -0.709 -6.719 32.053 1.00108.58 N ANISOU 972 N LYS A 187 11378 16534 13344 -1585 1980 -2600 N ATOM 973 CA LYS A 187 -1.287 -7.182 33.313 1.00106.18 C ANISOU 973 CA LYS A 187 11044 16204 13095 -1408 1791 -2584 C ATOM 974 C LYS A 187 -2.669 -6.573 33.550 1.00103.19 C ANISOU 974 C LYS A 187 10892 15658 12658 -1447 1753 -2470 C ATOM 975 O LYS A 187 -3.581 -7.249 34.040 1.00101.88 O ANISOU 975 O LYS A 187 10788 15416 12506 -1263 1635 -2405 O ATOM 976 CB LYS A 187 -0.350 -6.886 34.487 1.00105.66 C ANISOU 976 CB LYS A 187 10758 16280 13110 -1433 1711 -2695 C ATOM 977 CG LYS A 187 0.903 -7.752 34.502 1.00108.40 C ANISOU 977 CG LYS A 187 10851 16800 13535 -1320 1706 -2797 C ATOM 978 CD LYS A 187 1.646 -7.648 35.825 1.00109.40 C ANISOU 978 CD LYS A 187 10763 17069 13734 -1280 1571 -2891 C ATOM 979 CE LYS A 187 2.922 -6.834 35.690 1.00112.40 C ANISOU 979 CE LYS A 187 10946 17607 14153 -1484 1664 -3010 C ATOM 980 NZ LYS A 187 2.651 -5.419 35.318 1.00112.82 N ANISOU 980 NZ LYS A 187 11136 17582 14148 -1790 1788 -3002 N ATOM 981 N LYS A 188 -2.820 -5.301 33.190 1.00 57.04 N ANISOU 981 N LYS A 188 5172 9749 6753 -1685 1865 -2442 N ATOM 982 CA LYS A 188 -4.113 -4.629 33.263 1.00 56.37 C ANISOU 982 CA LYS A 188 5313 9498 6607 -1731 1859 -2325 C ATOM 983 C LYS A 188 -5.131 -5.346 32.383 1.00 55.34 C ANISOU 983 C LYS A 188 5346 9272 6410 -1601 1857 -2213 C ATOM 984 O LYS A 188 -6.289 -5.521 32.769 1.00 55.03 O ANISOU 984 O LYS A 188 5420 9129 6362 -1492 1774 -2126 O ATOM 985 CB LYS A 188 -3.994 -3.166 32.828 1.00 56.44 C ANISOU 985 CB LYS A 188 5453 9438 6555 -2015 2008 -2304 C ATOM 986 CG LYS A 188 -3.131 -2.303 33.735 1.00 57.84 C ANISOU 986 CG LYS A 188 5501 9684 6792 -2183 2015 -2418 C ATOM 987 CD LYS A 188 -2.986 -0.894 33.176 1.00 59.47 C ANISOU 987 CD LYS A 188 5870 9787 6941 -2477 2180 -2386 C ATOM 988 CE LYS A 188 -1.837 -0.148 33.837 1.00 61.55 C ANISOU 988 CE LYS A 188 5972 10147 7268 -2674 2213 -2527 C ATOM 989 NZ LYS A 188 -1.987 -0.082 35.316 1.00 60.88 N ANISOU 989 NZ LYS A 188 5773 10108 7250 -2615 2066 -2613 N ATOM 990 N PHE A 189 -4.689 -5.766 31.200 1.00 64.87 N ANISOU 990 N PHE A 189 6560 10523 7566 -1617 1954 -2226 N ATOM 991 CA PHE A 189 -5.563 -6.470 30.268 1.00 63.78 C ANISOU 991 CA PHE A 189 6573 10314 7345 -1514 1959 -2148 C ATOM 992 C PHE A 189 -5.964 -7.848 30.790 1.00 62.32 C ANISOU 992 C PHE A 189 6315 10129 7234 -1255 1815 -2159 C ATOM 993 O PHE A 189 -7.100 -8.281 30.600 1.00 61.43 O ANISOU 993 O PHE A 189 6336 9922 7083 -1159 1757 -2081 O ATOM 994 CB PHE A 189 -4.911 -6.595 28.891 1.00 65.20 C ANISOU 994 CB PHE A 189 6783 10552 7436 -1600 2112 -2175 C ATOM 995 CG PHE A 189 -5.771 -7.297 27.880 1.00 64.41 C ANISOU 995 CG PHE A 189 6851 10395 7226 -1512 2119 -2115 C ATOM 996 CD1 PHE A 189 -6.920 -6.695 27.395 1.00 63.66 C ANISOU 996 CD1 PHE A 189 6993 10188 7005 -1580 2128 -1994 C ATOM 997 CD2 PHE A 189 -5.433 -8.557 27.415 1.00 64.80 C ANISOU 997 CD2 PHE A 189 6828 10503 7289 -1361 2116 -2186 C ATOM 998 CE1 PHE A 189 -7.718 -7.336 26.468 1.00 64.07 C ANISOU 998 CE1 PHE A 189 7199 10207 6936 -1507 2119 -1953 C ATOM 999 CE2 PHE A 189 -6.226 -9.203 26.486 1.00 64.92 C ANISOU 999 CE2 PHE A 189 7007 10468 7191 -1294 2120 -2153 C ATOM 1000 CZ PHE A 189 -7.370 -8.592 26.012 1.00 64.77 C ANISOU 1000 CZ PHE A 189 7216 10357 7038 -1372 2114 -2041 C ATOM 1001 N ILE A 190 -5.027 -8.534 31.439 1.00 50.04 N ANISOU 1001 N ILE A 190 4552 8678 5782 -1146 1759 -2254 N ATOM 1002 CA ILE A 190 -5.319 -9.828 32.049 1.00 48.94 C ANISOU 1002 CA ILE A 190 4351 8523 5719 -900 1626 -2257 C ATOM 1003 C ILE A 190 -6.360 -9.658 33.151 1.00 47.17 C ANISOU 1003 C ILE A 190 4189 8207 5527 -828 1499 -2178 C ATOM 1004 O ILE A 190 -7.323 -10.428 33.240 1.00 45.76 O ANISOU 1004 O ILE A 190 4092 7937 5357 -682 1424 -2116 O ATOM 1005 CB ILE A 190 -4.051 -10.479 32.634 1.00 51.31 C ANISOU 1005 CB ILE A 190 4419 8957 6119 -796 1590 -2363 C ATOM 1006 CG1 ILE A 190 -3.042 -10.769 31.523 1.00 54.02 C ANISOU 1006 CG1 ILE A 190 4688 9395 6443 -839 1731 -2442 C ATOM 1007 CG2 ILE A 190 -4.400 -11.763 33.371 1.00 50.30 C ANISOU 1007 CG2 ILE A 190 4256 8789 6066 -542 1452 -2344 C ATOM 1008 CD1 ILE A 190 -3.539 -11.759 30.495 1.00 54.13 C ANISOU 1008 CD1 ILE A 190 4820 9343 6405 -733 1775 -2425 C ATOM 1009 N SER A 191 -6.162 -8.637 33.981 1.00 44.25 N ANISOU 1009 N SER A 191 3780 7860 5173 -939 1486 -2191 N ATOM 1010 CA SER A 191 -7.118 -8.306 35.031 1.00 44.22 C ANISOU 1010 CA SER A 191 3842 7773 5187 -887 1392 -2123 C ATOM 1011 C SER A 191 -8.494 -8.009 34.437 1.00 43.44 C ANISOU 1011 C SER A 191 3955 7533 5020 -907 1422 -2004 C ATOM 1012 O SER A 191 -9.522 -8.386 35.004 1.00 42.32 O ANISOU 1012 O SER A 191 3872 7306 4902 -774 1337 -1932 O ATOM 1013 CB SER A 191 -6.623 -7.112 35.848 1.00 45.79 C ANISOU 1013 CB SER A 191 3984 8022 5394 -1044 1408 -2180 C ATOM 1014 OG SER A 191 -5.375 -7.396 36.457 1.00 47.19 O ANISOU 1014 OG SER A 191 3947 8355 5629 -1024 1366 -2301 O ATOM 1015 N ALA A 192 -8.502 -7.340 33.287 1.00 46.95 N ANISOU 1015 N ALA A 192 4510 7957 5371 -1073 1547 -1983 N ATOM 1016 CA ALA A 192 -9.743 -7.043 32.579 1.00 46.77 C ANISOU 1016 CA ALA A 192 4692 7824 5257 -1097 1579 -1873 C ATOM 1017 C ALA A 192 -10.431 -8.326 32.117 1.00 45.67 C ANISOU 1017 C ALA A 192 4581 7660 5111 -929 1515 -1854 C ATOM 1018 O ALA A 192 -11.653 -8.460 32.227 1.00 45.81 O ANISOU 1018 O ALA A 192 4696 7596 5115 -856 1461 -1778 O ATOM 1019 CB ALA A 192 -9.473 -6.125 31.396 1.00 46.40 C ANISOU 1019 CB ALA A 192 4771 7772 5087 -1307 1729 -1850 C ATOM 1020 N ILE A 193 -9.639 -9.263 31.601 1.00 37.08 N ANISOU 1020 N ILE A 193 3406 6646 4038 -873 1529 -1934 N ATOM 1021 CA ILE A 193 -10.154 -10.562 31.179 1.00 36.61 C ANISOU 1021 CA ILE A 193 3372 6559 3982 -722 1479 -1945 C ATOM 1022 C ILE A 193 -10.807 -11.286 32.347 1.00 34.97 C ANISOU 1022 C ILE A 193 3115 6290 3885 -544 1345 -1912 C ATOM 1023 O ILE A 193 -11.927 -11.788 32.231 1.00 33.91 O ANISOU 1023 O ILE A 193 3066 6079 3740 -474 1298 -1866 O ATOM 1024 CB ILE A 193 -9.041 -11.463 30.606 1.00 38.27 C ANISOU 1024 CB ILE A 193 3480 6851 4209 -671 1527 -2051 C ATOM 1025 CG1 ILE A 193 -8.494 -10.885 29.301 1.00 40.12 C ANISOU 1025 CG1 ILE A 193 3783 7141 4318 -838 1678 -2078 C ATOM 1026 CG2 ILE A 193 -9.561 -12.873 30.373 1.00 37.86 C ANISOU 1026 CG2 ILE A 193 3457 6749 4181 -503 1471 -2077 C ATOM 1027 CD1 ILE A 193 -7.470 -11.774 28.627 1.00 41.99 C ANISOU 1027 CD1 ILE A 193 3933 7458 4562 -781 1750 -2183 C ATOM 1028 N TRP A 194 -10.101 -11.332 33.473 1.00 50.78 N ANISOU 1028 N TRP A 194 4978 8332 5982 -478 1288 -1939 N ATOM 1029 CA TRP A 194 -10.619 -11.986 34.670 1.00 50.16 C ANISOU 1029 CA TRP A 194 4864 8199 5995 -308 1169 -1896 C ATOM 1030 C TRP A 194 -11.913 -11.344 35.159 1.00 49.73 C ANISOU 1030 C TRP A 194 4914 8051 5931 -320 1139 -1796 C ATOM 1031 O TRP A 194 -12.877 -12.042 35.484 1.00 48.59 O ANISOU 1031 O TRP A 194 4806 7826 5828 -199 1078 -1741 O ATOM 1032 CB TRP A 194 -9.574 -11.985 35.786 1.00 49.97 C ANISOU 1032 CB TRP A 194 4687 8260 6037 -256 1115 -1946 C ATOM 1033 CG TRP A 194 -8.563 -13.081 35.655 1.00 50.53 C ANISOU 1033 CG TRP A 194 4640 8400 6157 -141 1104 -2024 C ATOM 1034 CD1 TRP A 194 -7.255 -12.952 35.290 1.00 52.03 C ANISOU 1034 CD1 TRP A 194 4704 8717 6349 -199 1163 -2121 C ATOM 1035 CD2 TRP A 194 -8.781 -14.478 35.881 1.00 50.14 C ANISOU 1035 CD2 TRP A 194 4589 8293 6170 58 1044 -2012 C ATOM 1036 NE1 TRP A 194 -6.644 -14.183 35.280 1.00 52.37 N ANISOU 1036 NE1 TRP A 194 4660 8787 6450 -34 1140 -2169 N ATOM 1037 CE2 TRP A 194 -7.560 -15.137 35.638 1.00 50.93 C ANISOU 1037 CE2 TRP A 194 4563 8485 6304 125 1069 -2102 C ATOM 1038 CE3 TRP A 194 -9.891 -15.236 36.267 1.00 49.99 C ANISOU 1038 CE3 TRP A 194 4658 8148 6186 182 982 -1935 C ATOM 1039 CZ2 TRP A 194 -7.417 -16.516 35.769 1.00 51.49 C ANISOU 1039 CZ2 TRP A 194 4610 8513 6440 320 1035 -2115 C ATOM 1040 CZ3 TRP A 194 -9.747 -16.606 36.396 1.00 49.55 C ANISOU 1040 CZ3 TRP A 194 4582 8048 6195 358 950 -1952 C ATOM 1041 CH2 TRP A 194 -8.519 -17.232 36.147 1.00 50.22 C ANISOU 1041 CH2 TRP A 194 4556 8214 6309 431 977 -2039 C ATOM 1042 N LEU A 195 -11.933 -10.015 35.203 1.00 35.41 N ANISOU 1042 N LEU A 195 3146 6243 4068 -467 1195 -1775 N ATOM 1043 CA LEU A 195 -13.121 -9.293 35.648 1.00 34.51 C ANISOU 1043 CA LEU A 195 3131 6038 3942 -474 1189 -1683 C ATOM 1044 C LEU A 195 -14.318 -9.566 34.742 1.00 34.05 C ANISOU 1044 C LEU A 195 3185 5920 3833 -463 1204 -1626 C ATOM 1045 O LEU A 195 -15.417 -9.839 35.225 1.00 32.76 O ANISOU 1045 O LEU A 195 3069 5648 3728 -360 1116 -1525 O ATOM 1046 CB LEU A 195 -12.853 -7.790 35.731 1.00 35.65 C ANISOU 1046 CB LEU A 195 3327 6187 4034 -650 1273 -1684 C ATOM 1047 CG LEU A 195 -14.056 -6.942 36.153 1.00 36.05 C ANISOU 1047 CG LEU A 195 3514 6104 4078 -647 1263 -1569 C ATOM 1048 CD1 LEU A 195 -14.590 -7.392 37.505 1.00 35.67 C ANISOU 1048 CD1 LEU A 195 3420 6014 4120 -477 1167 -1534 C ATOM 1049 CD2 LEU A 195 -13.697 -5.466 36.181 1.00 37.93 C ANISOU 1049 CD2 LEU A 195 3840 6300 4272 -825 1342 -1564 C ATOM 1050 N ALA A 196 -14.098 -9.494 33.431 1.00 34.12 N ANISOU 1050 N ALA A 196 3260 5966 3738 -569 1276 -1657 N ATOM 1051 CA ALA A 196 -15.157 -9.763 32.463 1.00 34.34 C ANISOU 1051 CA ALA A 196 3432 5909 3705 -567 1223 -1573 C ATOM 1052 C ALA A 196 -15.672 -11.193 32.600 1.00 33.74 C ANISOU 1052 C ALA A 196 3308 5802 3708 -415 1132 -1596 C ATOM 1053 O ALA A 196 -16.877 -11.444 32.513 1.00 34.30 O ANISOU 1053 O ALA A 196 3456 5766 3810 -368 1028 -1492 O ATOM 1054 CB ALA A 196 -14.659 -9.512 31.050 1.00 35.39 C ANISOU 1054 CB ALA A 196 3654 6111 3683 -708 1325 -1620 C ATOM 1055 N SER A 197 -14.747 -12.122 32.823 1.00 34.02 N ANISOU 1055 N SER A 197 3211 5928 3787 -338 1173 -1732 N ATOM 1056 CA SER A 197 -15.089 -13.524 33.018 1.00 33.58 C ANISOU 1056 CA SER A 197 3119 5823 3818 -190 1103 -1764 C ATOM 1057 C SER A 197 -15.992 -13.681 34.233 1.00 32.10 C ANISOU 1057 C SER A 197 2919 5525 3751 -83 1000 -1644 C ATOM 1058 O SER A 197 -16.996 -14.393 34.186 1.00 31.93 O ANISOU 1058 O SER A 197 2950 5396 3787 -27 919 -1582 O ATOM 1059 CB SER A 197 -13.820 -14.356 33.205 1.00 34.34 C ANISOU 1059 CB SER A 197 3116 5957 3973 -108 1104 -1841 C ATOM 1060 OG SER A 197 -12.872 -14.067 32.194 1.00 35.74 O ANISOU 1060 OG SER A 197 3301 6216 4062 -212 1191 -1911 O ATOM 1061 N ALA A 198 -15.628 -13.005 35.319 1.00 28.86 N ANISOU 1061 N ALA A 198 2442 5146 3375 -65 1011 -1620 N ATOM 1062 CA ALA A 198 -16.423 -13.033 36.541 1.00 27.62 C ANISOU 1062 CA ALA A 198 2285 4899 3309 35 939 -1510 C ATOM 1063 C ALA A 198 -17.804 -12.425 36.312 1.00 26.05 C ANISOU 1063 C ALA A 198 2202 4580 3115 -10 891 -1364 C ATOM 1064 O ALA A 198 -18.798 -12.889 36.872 1.00 25.09 O ANISOU 1064 O ALA A 198 2090 4363 3082 74 831 -1270 O ATOM 1065 CB ALA A 198 -15.699 -12.303 37.659 1.00 27.90 C ANISOU 1065 CB ALA A 198 2263 4990 3348 41 948 -1517 C ATOM 1066 N LEU A 199 -17.858 -11.388 35.482 1.00 27.67 N ANISOU 1066 N LEU A 199 2492 4791 3229 -140 923 -1339 N ATOM 1067 CA LEU A 199 -19.112 -10.704 35.183 1.00 27.41 C ANISOU 1067 CA LEU A 199 2565 4654 3197 -168 870 -1196 C ATOM 1068 C LEU A 199 -20.056 -11.581 34.371 1.00 27.59 C ANISOU 1068 C LEU A 199 2618 4625 3239 -150 782 -1159 C ATOM 1069 O LEU A 199 -21.267 -11.573 34.591 1.00 27.27 O ANISOU 1069 O LEU A 199 2590 4498 3275 -107 707 -1042 O ATOM 1070 CB LEU A 199 -18.844 -9.395 34.437 1.00 28.09 C ANISOU 1070 CB LEU A 199 2755 4750 3168 -305 925 -1172 C ATOM 1071 CG LEU A 199 -18.189 -8.275 35.245 1.00 28.14 C ANISOU 1071 CG LEU A 199 2760 4766 3166 -355 1001 -1188 C ATOM 1072 CD1 LEU A 199 -17.774 -7.136 34.331 1.00 29.20 C ANISOU 1072 CD1 LEU A 199 3009 4903 3181 -516 1077 -1180 C ATOM 1073 CD2 LEU A 199 -19.130 -7.778 36.332 1.00 27.44 C ANISOU 1073 CD2 LEU A 199 2697 4567 3163 -266 964 -1076 C ATOM 1074 N LEU A 200 -19.499 -12.337 33.431 1.00 36.85 N ANISOU 1074 N LEU A 200 3800 5858 4346 -188 794 -1270 N ATOM 1075 CA LEU A 200 -20.305 -13.210 32.584 1.00 38.87 C ANISOU 1075 CA LEU A 200 4100 6068 4602 -193 704 -1267 C ATOM 1076 C LEU A 200 -20.748 -14.474 33.321 1.00 38.95 C ANISOU 1076 C LEU A 200 4034 6006 4760 -85 654 -1273 C ATOM 1077 O LEU A 200 -21.621 -15.203 32.849 1.00 40.86 O ANISOU 1077 O LEU A 200 4299 6182 5044 -94 566 -1255 O ATOM 1078 CB LEU A 200 -19.544 -13.573 31.306 1.00 39.17 C ANISOU 1078 CB LEU A 200 4198 6186 4498 -271 750 -1400 C ATOM 1079 CG LEU A 200 -19.190 -12.400 30.388 1.00 40.18 C ANISOU 1079 CG LEU A 200 4434 6376 4456 -400 808 -1379 C ATOM 1080 CD1 LEU A 200 -18.381 -12.869 29.190 1.00 40.94 C ANISOU 1080 CD1 LEU A 200 4589 6564 4405 -470 882 -1522 C ATOM 1081 CD2 LEU A 200 -20.447 -11.673 29.936 1.00 42.77 C ANISOU 1081 CD2 LEU A 200 4868 6634 4750 -436 695 -1220 C ATOM 1082 N ALA A 201 -20.146 -14.726 34.480 1.00 33.16 N ANISOU 1082 N ALA A 201 3216 5281 4102 10 707 -1296 N ATOM 1083 CA ALA A 201 -20.466 -15.910 35.271 1.00 33.03 C ANISOU 1083 CA ALA A 201 3147 5187 4217 121 679 -1288 C ATOM 1084 C ALA A 201 -21.564 -15.628 36.295 1.00 32.80 C ANISOU 1084 C ALA A 201 3096 5073 4293 169 646 -1133 C ATOM 1085 O ALA A 201 -22.057 -16.540 36.958 1.00 33.00 O ANISOU 1085 O ALA A 201 3093 5015 4431 242 628 -1092 O ATOM 1086 CB ALA A 201 -19.218 -16.439 35.961 1.00 31.34 C ANISOU 1086 CB ALA A 201 2861 5033 4014 219 743 -1387 C ATOM 1087 N ILE A 202 -21.940 -14.358 36.411 1.00 26.55 N ANISOU 1087 N ILE A 202 2325 4295 3466 128 652 -1048 N ATOM 1088 CA ILE A 202 -22.984 -13.921 37.344 1.00 26.08 C ANISOU 1088 CA ILE A 202 2245 4165 3499 181 644 -906 C ATOM 1089 C ILE A 202 -24.342 -14.655 37.263 1.00 26.41 C ANISOU 1089 C ILE A 202 2254 4114 3665 188 574 -818 C ATOM 1090 O ILE A 202 -24.900 -15.008 38.303 1.00 26.23 O ANISOU 1090 O ILE A 202 2185 4033 3749 262 601 -740 O ATOM 1091 CB ILE A 202 -23.191 -12.381 37.286 1.00 25.94 C ANISOU 1091 CB ILE A 202 2276 4157 3422 139 664 -838 C ATOM 1092 CG1 ILE A 202 -21.934 -11.659 37.772 1.00 25.73 C ANISOU 1092 CG1 ILE A 202 2263 4202 3310 128 745 -917 C ATOM 1093 CG2 ILE A 202 -24.389 -11.957 38.119 1.00 25.76 C ANISOU 1093 CG2 ILE A 202 2228 4056 3502 208 664 -697 C ATOM 1094 CD1 ILE A 202 -22.081 -10.155 37.845 1.00 25.79 C ANISOU 1094 CD1 ILE A 202 2343 4189 3268 82 780 -860 C ATOM 1095 N PRO A 203 -24.877 -14.889 36.043 1.00 41.08 N ANISOU 1095 N PRO A 203 4136 5968 5506 103 487 -831 N ATOM 1096 CA PRO A 203 -26.184 -15.558 35.944 1.00 42.72 C ANISOU 1096 CA PRO A 203 4288 6099 5844 88 407 -754 C ATOM 1097 C PRO A 203 -26.293 -16.890 36.689 1.00 42.83 C ANISOU 1097 C PRO A 203 4259 6030 5985 136 434 -763 C ATOM 1098 O PRO A 203 -27.395 -17.268 37.086 1.00 44.59 O ANISOU 1098 O PRO A 203 4412 6184 6345 138 418 -664 O ATOM 1099 CB PRO A 203 -26.334 -15.800 34.441 1.00 44.84 C ANISOU 1099 CB PRO A 203 4610 6395 6033 -19 299 -823 C ATOM 1100 CG PRO A 203 -25.583 -14.698 33.823 1.00 45.11 C ANISOU 1100 CG PRO A 203 4728 6514 5899 -53 326 -851 C ATOM 1101 CD PRO A 203 -24.398 -14.461 34.714 1.00 42.16 C ANISOU 1101 CD PRO A 203 4352 6172 5496 9 454 -905 C ATOM 1102 N MET A 204 -25.176 -17.587 36.872 1.00 58.82 N ANISOU 1102 N MET A 204 6321 8058 7970 176 482 -874 N ATOM 1103 CA MET A 204 -25.188 -18.863 37.581 1.00 59.39 C ANISOU 1103 CA MET A 204 6381 8030 8152 238 512 -874 C ATOM 1104 C MET A 204 -25.543 -18.694 39.054 1.00 58.17 C ANISOU 1104 C MET A 204 6185 7839 8076 329 584 -742 C ATOM 1105 O MET A 204 -26.123 -19.589 39.667 1.00 59.79 O ANISOU 1105 O MET A 204 6370 7940 8406 342 602 -668 O ATOM 1106 CB MET A 204 -23.846 -19.576 37.436 1.00 57.73 C ANISOU 1106 CB MET A 204 6216 7838 7878 300 550 -1013 C ATOM 1107 CG MET A 204 -23.592 -20.075 36.034 1.00 59.91 C ANISOU 1107 CG MET A 204 6547 8120 8094 219 501 -1153 C ATOM 1108 SD MET A 204 -24.919 -21.141 35.444 1.00 65.24 S ANISOU 1108 SD MET A 204 7239 8652 8895 114 405 -1139 S ATOM 1109 CE MET A 204 -24.472 -21.311 33.720 1.00 67.14 C ANISOU 1109 CE MET A 204 7573 8949 8988 10 343 -1319 C ATOM 1110 N LEU A 205 -25.197 -17.540 39.615 1.00 23.65 N ANISOU 1110 N LEU A 205 1813 3549 3622 380 635 -716 N ATOM 1111 CA LEU A 205 -25.544 -17.226 40.994 1.00 23.86 C ANISOU 1111 CA LEU A 205 1822 3556 3686 466 710 -604 C ATOM 1112 C LEU A 205 -27.056 -17.112 41.141 1.00 23.98 C ANISOU 1112 C LEU A 205 1776 3508 3829 433 712 -472 C ATOM 1113 O LEU A 205 -27.600 -17.270 42.233 1.00 24.50 O ANISOU 1113 O LEU A 205 1821 3524 3962 495 790 -370 O ATOM 1114 CB LEU A 205 -24.877 -15.920 41.431 1.00 23.74 C ANISOU 1114 CB LEU A 205 1831 3637 3553 496 750 -622 C ATOM 1115 CG LEU A 205 -23.349 -15.878 41.383 1.00 24.06 C ANISOU 1115 CG LEU A 205 1895 3770 3477 520 754 -753 C ATOM 1116 CD1 LEU A 205 -22.839 -14.493 41.742 1.00 24.03 C ANISOU 1116 CD1 LEU A 205 1912 3846 3374 508 789 -771 C ATOM 1117 CD2 LEU A 205 -22.759 -16.926 42.310 1.00 24.67 C ANISOU 1117 CD2 LEU A 205 1975 3828 3571 634 775 -761 C ATOM 1118 N PHE A 206 -27.729 -16.839 40.029 1.00 26.37 N ANISOU 1118 N PHE A 206 2043 3819 4158 337 626 -472 N ATOM 1119 CA PHE A 206 -29.176 -16.673 40.024 1.00 26.94 C ANISOU 1119 CA PHE A 206 2018 3854 4362 305 607 -354 C ATOM 1120 C PHE A 206 -29.865 -17.863 39.364 1.00 27.41 C ANISOU 1120 C PHE A 206 2028 3845 4540 206 526 -368 C ATOM 1121 O PHE A 206 -31.093 -17.928 39.313 1.00 28.34 O ANISOU 1121 O PHE A 206 2036 3939 4795 158 496 -281 O ATOM 1122 CB PHE A 206 -29.560 -15.381 39.297 1.00 26.68 C ANISOU 1122 CB PHE A 206 1971 3885 4280 282 547 -324 C ATOM 1123 CG PHE A 206 -29.059 -14.131 39.968 1.00 26.36 C ANISOU 1123 CG PHE A 206 1987 3883 4147 363 632 -304 C ATOM 1124 CD1 PHE A 206 -27.737 -13.737 39.836 1.00 25.73 C ANISOU 1124 CD1 PHE A 206 2005 3855 3916 362 651 -409 C ATOM 1125 CD2 PHE A 206 -29.914 -13.344 40.722 1.00 27.02 C ANISOU 1125 CD2 PHE A 206 2021 3947 4300 435 699 -191 C ATOM 1126 CE1 PHE A 206 -27.275 -12.588 40.450 1.00 25.61 C ANISOU 1126 CE1 PHE A 206 2045 3864 3821 410 723 -404 C ATOM 1127 CE2 PHE A 206 -29.458 -12.193 41.336 1.00 26.83 C ANISOU 1127 CE2 PHE A 206 2070 3936 4186 502 778 -190 C ATOM 1128 CZ PHE A 206 -28.136 -11.815 41.200 1.00 26.02 C ANISOU 1128 CZ PHE A 206 2074 3878 3934 479 784 -299 C ATOM 1129 N THR A 207 -29.071 -18.805 38.865 1.00 59.21 N ANISOU 1129 N THR A 207 6131 7841 8523 173 493 -488 N ATOM 1130 CA THR A 207 -29.613 -19.955 38.146 1.00 62.01 C ANISOU 1130 CA THR A 207 6470 8114 8975 64 411 -535 C ATOM 1131 C THR A 207 -29.705 -21.207 39.015 1.00 62.95 C ANISOU 1131 C THR A 207 6604 8096 9216 85 491 -504 C ATOM 1132 O THR A 207 -30.774 -21.804 39.139 1.00 64.84 O ANISOU 1132 O THR A 207 6768 8252 9613 3 482 -437 O ATOM 1133 CB THR A 207 -28.789 -20.275 36.883 1.00 63.89 C ANISOU 1133 CB THR A 207 6805 8382 9088 5 326 -701 C ATOM 1134 OG1 THR A 207 -28.791 -19.142 36.007 1.00 63.37 O ANISOU 1134 OG1 THR A 207 6744 8433 8901 -30 253 -711 O ATOM 1135 CG2 THR A 207 -29.377 -21.473 36.154 1.00 67.02 C ANISOU 1135 CG2 THR A 207 7206 8680 9578 -116 237 -768 C ATOM 1136 N VAL A 208 -28.584 -21.605 39.609 1.00 30.57 N ANISOU 1136 N VAL A 208 2598 3971 5045 193 566 -547 N ATOM 1137 CA VAL A 208 -28.546 -22.806 40.438 1.00 32.18 C ANISOU 1137 CA VAL A 208 2850 4031 5344 238 642 -505 C ATOM 1138 C VAL A 208 -28.872 -22.495 41.896 1.00 31.20 C ANISOU 1138 C VAL A 208 2703 3901 5250 332 765 -347 C ATOM 1139 O VAL A 208 -28.877 -21.335 42.308 1.00 29.66 O ANISOU 1139 O VAL A 208 2469 3817 4982 386 796 -299 O ATOM 1140 CB VAL A 208 -27.172 -23.503 40.371 1.00 32.11 C ANISOU 1140 CB VAL A 208 2957 3993 5250 335 651 -624 C ATOM 1141 CG1 VAL A 208 -26.856 -23.916 38.943 1.00 33.69 C ANISOU 1141 CG1 VAL A 208 3198 4186 5417 246 557 -791 C ATOM 1142 CG2 VAL A 208 -26.086 -22.593 40.924 1.00 29.55 C ANISOU 1142 CG2 VAL A 208 2642 3809 4775 466 690 -641 C ATOM 1143 N GLY A 209 -29.146 -23.539 42.673 1.00 59.49 N ANISOU 1143 N GLY A 209 6329 7342 8933 349 842 -267 N ATOM 1144 CA GLY A 209 -29.428 -23.379 44.087 1.00 59.10 C ANISOU 1144 CA GLY A 209 6287 7279 8889 440 974 -114 C ATOM 1145 C GLY A 209 -29.761 -24.693 44.763 1.00 62.47 C ANISOU 1145 C GLY A 209 6786 7521 9430 433 1058 -23 C ATOM 1146 O GLY A 209 -29.466 -25.763 44.233 1.00 65.14 O ANISOU 1146 O GLY A 209 7199 7731 9821 397 1013 -95 O ATOM 1147 N LEU A 210 -30.376 -24.613 45.938 1.00 42.15 N ANISOU 1147 N LEU A 210 4206 4924 6888 468 1193 138 N ATOM 1148 CA LEU A 210 -30.769 -25.806 46.678 1.00 46.15 C ANISOU 1148 CA LEU A 210 4793 5245 7497 452 1301 256 C ATOM 1149 C LEU A 210 -32.265 -26.062 46.562 1.00 47.81 C ANISOU 1149 C LEU A 210 4869 5386 7912 271 1361 345 C ATOM 1150 O LEU A 210 -33.068 -25.132 46.633 1.00 45.78 O ANISOU 1150 O LEU A 210 4460 5246 7688 235 1391 391 O ATOM 1151 CB LEU A 210 -30.393 -25.672 48.155 1.00 45.39 C ANISOU 1151 CB LEU A 210 4807 5164 7276 616 1430 388 C ATOM 1152 CG LEU A 210 -28.909 -25.679 48.517 1.00 43.79 C ANISOU 1152 CG LEU A 210 4741 5015 6885 805 1373 326 C ATOM 1153 CD1 LEU A 210 -28.737 -25.610 50.025 1.00 44.49 C ANISOU 1153 CD1 LEU A 210 4942 5115 6848 949 1492 473 C ATOM 1154 CD2 LEU A 210 -28.232 -26.916 47.955 1.00 45.39 C ANISOU 1154 CD2 LEU A 210 5045 5067 7135 824 1301 249 C ATOM 1155 N GLN A 211 -32.635 -27.327 46.385 1.00 64.38 N ANISOU 1155 N GLN A 211 7016 7287 10158 157 1381 364 N ATOM 1156 CA GLN A 211 -34.042 -27.720 46.400 1.00 63.95 C ANISOU 1156 CA GLN A 211 6826 7153 10319 -35 1454 456 C ATOM 1157 C GLN A 211 -34.235 -29.096 47.029 1.00 66.08 C ANISOU 1157 C GLN A 211 7233 7177 10698 -91 1577 561 C ATOM 1158 O GLN A 211 -33.475 -30.027 46.758 1.00 67.57 O ANISOU 1158 O GLN A 211 7593 7210 10868 -59 1526 492 O ATOM 1159 CB GLN A 211 -34.647 -27.690 44.992 1.00 64.70 C ANISOU 1159 CB GLN A 211 6770 7278 10535 -221 1288 323 C ATOM 1160 CG GLN A 211 -35.133 -26.317 44.549 1.00 61.51 C ANISOU 1160 CG GLN A 211 6171 7096 10104 -219 1216 304 C ATOM 1161 CD GLN A 211 -35.981 -26.374 43.293 1.00 61.68 C ANISOU 1161 CD GLN A 211 6025 7145 10265 -416 1057 215 C ATOM 1162 OE1 GLN A 211 -36.041 -27.400 42.616 1.00 63.01 O ANISOU 1162 OE1 GLN A 211 6241 7176 10522 -559 977 127 O ATOM 1163 NE2 GLN A 211 -36.648 -25.269 42.980 1.00 60.43 N ANISOU 1163 NE2 GLN A 211 5677 7160 10122 -418 1002 236 N ATOM 1164 N ASN A 212 -35.254 -29.215 47.875 1.00 69.97 N ANISOU 1164 N ASN A 212 7653 7627 11305 -170 1753 730 N ATOM 1165 CA ASN A 212 -35.574 -30.485 48.514 1.00 71.47 C ANISOU 1165 CA ASN A 212 7976 7572 11608 -248 1899 857 C ATOM 1166 C ASN A 212 -36.488 -31.318 47.622 1.00 71.88 C ANISOU 1166 C ASN A 212 7921 7477 11913 -525 1847 798 C ATOM 1167 O ASN A 212 -37.711 -31.194 47.682 1.00 72.01 O ANISOU 1167 O ASN A 212 7728 7529 12105 -700 1922 868 O ATOM 1168 CB ASN A 212 -36.228 -30.246 49.876 1.00 70.76 C ANISOU 1168 CB ASN A 212 7871 7506 11509 -214 2140 1073 C ATOM 1169 CG ASN A 212 -36.174 -31.467 50.776 1.00 72.15 C ANISOU 1169 CG ASN A 212 8270 7433 11711 -220 2307 1233 C ATOM 1170 OD1 ASN A 212 -36.353 -32.597 50.324 1.00 72.79 O ANISOU 1170 OD1 ASN A 212 8417 7286 11954 -375 2293 1215 O ATOM 1171 ND2 ASN A 212 -35.922 -31.242 52.060 1.00 72.09 N ANISOU 1171 ND2 ASN A 212 8401 7458 11534 -50 2466 1391 N ATOM 1172 N LEU A 213 -35.886 -32.168 46.796 1.00 97.68 N ANISOU 1172 N LEU A 213 11327 10584 15201 -565 1719 659 N ATOM 1173 CA LEU A 213 -36.639 -32.947 45.818 1.00 98.54 C ANISOU 1173 CA LEU A 213 11359 10555 15527 -835 1634 558 C ATOM 1174 C LEU A 213 -37.169 -34.266 46.372 1.00100.31 C ANISOU 1174 C LEU A 213 11702 10478 15932 -991 1794 678 C ATOM 1175 O LEU A 213 -37.499 -35.175 45.611 1.00101.81 O ANISOU 1175 O LEU A 213 11917 10481 16285 -1200 1722 574 O ATOM 1176 CB LEU A 213 -35.796 -33.205 44.566 1.00 96.43 C ANISOU 1176 CB LEU A 213 11187 10259 15191 -821 1421 323 C ATOM 1177 CG LEU A 213 -35.431 -31.977 43.731 1.00 94.93 C ANISOU 1177 CG LEU A 213 10868 10349 14851 -737 1249 187 C ATOM 1178 CD1 LEU A 213 -34.790 -32.396 42.417 1.00 95.72 C ANISOU 1178 CD1 LEU A 213 11057 10402 14911 -783 1062 -47 C ATOM 1179 CD2 LEU A 213 -36.655 -31.110 43.483 1.00 93.60 C ANISOU 1179 CD2 LEU A 213 10406 10374 14784 -872 1221 230 C ATOM 1180 N SER A 214 -37.254 -34.370 47.694 1.00 56.59 N ANISOU 1180 N SER A 214 6256 4886 10360 -899 2013 895 N ATOM 1181 CA SER A 214 -37.847 -35.549 48.316 1.00 59.83 C ANISOU 1181 CA SER A 214 6777 5012 10942 -1062 2199 1045 C ATOM 1182 C SER A 214 -39.356 -35.547 48.091 1.00 61.80 C ANISOU 1182 C SER A 214 6734 5298 11449 -1370 2258 1077 C ATOM 1183 O SER A 214 -39.910 -34.578 47.569 1.00 60.57 O ANISOU 1183 O SER A 214 6297 5402 11314 -1407 2164 1010 O ATOM 1184 CB SER A 214 -37.525 -35.600 49.810 1.00 60.26 C ANISOU 1184 CB SER A 214 7019 5020 10857 -872 2423 1282 C ATOM 1185 OG SER A 214 -38.006 -34.448 50.479 1.00 59.09 O ANISOU 1185 OG SER A 214 6688 5138 10625 -798 2525 1382 O ATOM 1186 N GLY A 215 -40.014 -36.633 48.483 1.00 76.99 N ANISOU 1186 N GLY A 215 8719 6959 13574 -1591 2412 1181 N ATOM 1187 CA GLY A 215 -41.443 -36.786 48.271 1.00 77.02 C ANISOU 1187 CA GLY A 215 8431 6977 13853 -1916 2471 1204 C ATOM 1188 C GLY A 215 -42.280 -35.671 48.870 1.00 75.71 C ANISOU 1188 C GLY A 215 7970 7098 13698 -1888 2601 1330 C ATOM 1189 O GLY A 215 -43.205 -35.168 48.231 1.00 75.50 O ANISOU 1189 O GLY A 215 7606 7250 13829 -2050 2511 1257 O ATOM 1190 N ASP A 216 -41.953 -35.281 50.097 1.00 98.36 N ANISOU 1190 N ASP A 216 10968 10014 16392 -1669 2808 1515 N ATOM 1191 CA ASP A 216 -42.698 -34.237 50.792 1.00 97.62 C ANISOU 1191 CA ASP A 216 10634 10171 16288 -1615 2972 1639 C ATOM 1192 C ASP A 216 -41.918 -32.927 50.846 1.00 95.28 C ANISOU 1192 C ASP A 216 10343 10138 15723 -1304 2867 1580 C ATOM 1193 O ASP A 216 -42.439 -31.904 51.289 1.00 94.02 O ANISOU 1193 O ASP A 216 9991 10200 15534 -1225 2969 1644 O ATOM 1194 CB ASP A 216 -43.062 -34.692 52.208 1.00101.77 C ANISOU 1194 CB ASP A 216 11301 10581 16787 -1611 3299 1885 C ATOM 1195 CG ASP A 216 -43.989 -35.894 52.216 1.00106.61 C ANISOU 1195 CG ASP A 216 11911 11012 17586 -1895 3354 1910 C ATOM 1196 OD1 ASP A 216 -43.975 -36.667 51.235 1.00109.17 O ANISOU 1196 OD1 ASP A 216 12226 11178 18075 -2095 3184 1769 O ATOM 1197 OD2 ASP A 216 -44.733 -36.066 53.205 1.00109.53 O ANISOU 1197 OD2 ASP A 216 12295 11395 17926 -1925 3568 2062 O ATOM 1198 N GLY A 217 -40.669 -32.965 50.393 1.00 79.29 N ANISOU 1198 N GLY A 217 8537 8081 13510 -1132 2672 1451 N ATOM 1199 CA GLY A 217 -39.819 -31.788 50.408 1.00 77.68 C ANISOU 1199 CA GLY A 217 8358 8105 13053 -860 2565 1382 C ATOM 1200 C GLY A 217 -39.364 -31.434 51.810 1.00 77.19 C ANISOU 1200 C GLY A 217 8475 8084 12772 -634 2766 1550 C ATOM 1201 O GLY A 217 -39.044 -30.281 52.098 1.00 76.92 O ANISOU 1201 O GLY A 217 8396 8268 12564 -448 2751 1532 O ATOM 1202 N THR A 218 -39.336 -32.434 52.686 1.00 61.62 N ANISOU 1202 N THR A 218 6722 5891 10799 -654 2951 1715 N ATOM 1203 CA THR A 218 -38.942 -32.229 54.075 1.00 61.49 C ANISOU 1203 CA THR A 218 6909 5896 10556 -450 3147 1893 C ATOM 1204 C THR A 218 -37.726 -33.073 54.442 1.00 62.86 C ANISOU 1204 C THR A 218 7444 5880 10558 -285 3097 1929 C ATOM 1205 O THR A 218 -36.964 -32.720 55.343 1.00 62.98 O ANISOU 1205 O THR A 218 7647 5970 10313 -44 3134 2004 O ATOM 1206 CB THR A 218 -40.093 -32.566 55.043 1.00 62.21 C ANISOU 1206 CB THR A 218 6950 5919 10767 -598 3469 2112 C ATOM 1207 OG1 THR A 218 -40.480 -33.936 54.872 1.00 65.02 O ANISOU 1207 OG1 THR A 218 7390 5980 11333 -825 3534 2177 O ATOM 1208 CG2 THR A 218 -41.293 -31.668 54.782 1.00 62.48 C ANISOU 1208 CG2 THR A 218 6601 6166 10972 -723 3533 2085 C ATOM 1209 N HIS A 219 -37.550 -34.188 53.741 1.00 55.36 N ANISOU 1209 N HIS A 219 6592 4686 9758 -408 3005 1870 N ATOM 1210 CA HIS A 219 -36.445 -35.099 54.015 1.00 55.42 C ANISOU 1210 CA HIS A 219 6934 4480 9640 -244 2958 1905 C ATOM 1211 C HIS A 219 -35.112 -34.479 53.605 1.00 51.04 C ANISOU 1211 C HIS A 219 6432 4086 8873 12 2721 1736 C ATOM 1212 O HIS A 219 -34.917 -34.127 52.442 1.00 48.56 O ANISOU 1212 O HIS A 219 5969 3860 8622 -38 2524 1523 O ATOM 1213 CB HIS A 219 -36.658 -36.430 53.291 1.00 58.05 C ANISOU 1213 CB HIS A 219 7354 4493 10211 -450 2927 1862 C ATOM 1214 CG HIS A 219 -35.834 -37.554 53.837 1.00 60.05 C ANISOU 1214 CG HIS A 219 7975 4459 10383 -306 2966 1975 C ATOM 1215 ND1 HIS A 219 -34.482 -37.669 53.601 1.00 57.84 N ANISOU 1215 ND1 HIS A 219 7869 4170 9939 -45 2782 1871 N ATOM 1216 CD2 HIS A 219 -36.173 -38.615 54.607 1.00 64.49 C ANISOU 1216 CD2 HIS A 219 8763 4729 11012 -379 3170 2190 C ATOM 1217 CE1 HIS A 219 -34.021 -38.751 54.203 1.00 60.91 C ANISOU 1217 CE1 HIS A 219 8572 4274 10297 57 2858 2018 C ATOM 1218 NE2 HIS A 219 -35.028 -39.343 54.820 1.00 64.91 N ANISOU 1218 NE2 HIS A 219 9132 4594 10936 -144 3094 2218 N ATOM 1219 N PRO A 220 -34.187 -34.344 54.569 1.00 50.43 N ANISOU 1219 N PRO A 220 6568 4056 8540 280 2740 1832 N ATOM 1220 CA PRO A 220 -32.876 -33.711 54.380 1.00 46.83 C ANISOU 1220 CA PRO A 220 6152 3776 7868 531 2536 1690 C ATOM 1221 C PRO A 220 -31.991 -34.447 53.376 1.00 46.25 C ANISOU 1221 C PRO A 220 6159 3559 7855 574 2343 1524 C ATOM 1222 O PRO A 220 -31.000 -33.885 52.910 1.00 43.54 O ANISOU 1222 O PRO A 220 5785 3377 7384 733 2166 1366 O ATOM 1223 CB PRO A 220 -32.249 -33.782 55.777 1.00 48.17 C ANISOU 1223 CB PRO A 220 6566 3953 7782 772 2626 1875 C ATOM 1224 CG PRO A 220 -33.402 -33.933 56.710 1.00 51.48 C ANISOU 1224 CG PRO A 220 7011 4304 8244 644 2900 2099 C ATOM 1225 CD PRO A 220 -34.396 -34.762 55.965 1.00 53.72 C ANISOU 1225 CD PRO A 220 7196 4371 8845 349 2969 2094 C ATOM 1226 N GLY A 221 -32.343 -35.688 53.056 1.00 64.94 N ANISOU 1226 N GLY A 221 8635 5623 10418 430 2391 1556 N ATOM 1227 CA GLY A 221 -31.593 -36.467 52.089 1.00 64.96 C ANISOU 1227 CA GLY A 221 8732 5456 10492 464 2233 1391 C ATOM 1228 C GLY A 221 -31.951 -36.100 50.662 1.00 65.25 C ANISOU 1228 C GLY A 221 8541 5581 10670 271 2090 1150 C ATOM 1229 O GLY A 221 -31.245 -36.463 49.721 1.00 64.69 O ANISOU 1229 O GLY A 221 8513 5448 10619 313 1940 963 O ATOM 1230 N GLY A 222 -33.055 -35.377 50.503 1.00 56.00 N ANISOU 1230 N GLY A 222 7129 4560 9590 69 2138 1156 N ATOM 1231 CA GLY A 222 -33.508 -34.949 49.192 1.00 54.84 C ANISOU 1231 CA GLY A 222 6754 4522 9560 -115 1992 950 C ATOM 1232 C GLY A 222 -33.058 -33.540 48.861 1.00 53.22 C ANISOU 1232 C GLY A 222 6383 4652 9187 9 1869 838 C ATOM 1233 O GLY A 222 -33.490 -32.957 47.866 1.00 52.93 O ANISOU 1233 O GLY A 222 6146 4750 9214 -124 1755 698 O ATOM 1234 N LEU A 223 -32.189 -32.989 49.702 1.00 57.12 N ANISOU 1234 N LEU A 223 6968 5273 9461 260 1888 902 N ATOM 1235 CA LEU A 223 -31.651 -31.652 49.485 1.00 56.27 C ANISOU 1235 CA LEU A 223 6732 5461 9185 380 1783 798 C ATOM 1236 C LEU A 223 -30.558 -31.687 48.424 1.00 55.20 C ANISOU 1236 C LEU A 223 6622 5362 8989 460 1593 581 C ATOM 1237 O LEU A 223 -29.419 -32.057 48.708 1.00 54.11 O ANISOU 1237 O LEU A 223 6639 5186 8733 661 1555 562 O ATOM 1238 CB LEU A 223 -31.094 -31.083 50.790 1.00 54.84 C ANISOU 1238 CB LEU A 223 6647 5402 8786 602 1865 929 C ATOM 1239 CG LEU A 223 -30.482 -29.683 50.710 1.00 53.41 C ANISOU 1239 CG LEU A 223 6359 5509 8424 723 1769 825 C ATOM 1240 CD1 LEU A 223 -31.533 -28.661 50.308 1.00 53.75 C ANISOU 1240 CD1 LEU A 223 6172 5702 8547 573 1790 802 C ATOM 1241 CD2 LEU A 223 -29.832 -29.303 52.031 1.00 53.10 C ANISOU 1241 CD2 LEU A 223 6452 5562 8160 939 1831 938 C ATOM 1242 N VAL A 224 -30.905 -31.297 47.203 1.00 42.99 N ANISOU 1242 N VAL A 224 4918 3897 7518 309 1476 420 N ATOM 1243 CA VAL A 224 -29.965 -31.372 46.091 1.00 42.09 C ANISOU 1243 CA VAL A 224 4829 3812 7349 354 1318 206 C ATOM 1244 C VAL A 224 -29.628 -30.003 45.506 1.00 39.64 C ANISOU 1244 C VAL A 224 4369 3784 6908 385 1213 89 C ATOM 1245 O VAL A 224 -30.381 -29.038 45.664 1.00 39.19 O ANISOU 1245 O VAL A 224 4162 3874 6853 318 1237 149 O ATOM 1246 CB VAL A 224 -30.496 -32.280 44.965 1.00 43.61 C ANISOU 1246 CB VAL A 224 5027 3822 7718 145 1253 83 C ATOM 1247 CG1 VAL A 224 -30.714 -33.694 45.483 1.00 46.27 C ANISOU 1247 CG1 VAL A 224 5546 3842 8191 111 1357 183 C ATOM 1248 CG2 VAL A 224 -31.783 -31.713 44.390 1.00 43.56 C ANISOU 1248 CG2 VAL A 224 4805 3913 7830 -91 1219 75 C ATOM 1249 N CYS A 225 -28.483 -29.934 44.833 1.00 59.50 N ANISOU 1249 N CYS A 225 6930 6362 9314 492 1109 -74 N ATOM 1250 CA CYS A 225 -28.048 -28.722 44.152 1.00 57.09 C ANISOU 1250 CA CYS A 225 6509 6299 8882 508 1014 -195 C ATOM 1251 C CYS A 225 -28.506 -28.750 42.699 1.00 57.87 C ANISOU 1251 C CYS A 225 6538 6400 9047 325 905 -348 C ATOM 1252 O CYS A 225 -27.910 -29.426 41.861 1.00 58.01 O ANISOU 1252 O CYS A 225 6640 6337 9063 323 843 -498 O ATOM 1253 CB CYS A 225 -26.527 -28.585 44.223 1.00 54.34 C ANISOU 1253 CB CYS A 225 6229 6041 8375 714 975 -289 C ATOM 1254 SG CYS A 225 -25.862 -27.133 43.378 1.00 51.54 S ANISOU 1254 SG CYS A 225 5751 5967 7862 715 882 -439 S ATOM 1255 N THR A 226 -29.568 -28.007 42.410 1.00 45.86 N ANISOU 1255 N THR A 226 4869 4978 7578 181 878 -309 N ATOM 1256 CA THR A 226 -30.190 -28.018 41.093 1.00 47.66 C ANISOU 1256 CA THR A 226 5023 5216 7870 -6 757 -428 C ATOM 1257 C THR A 226 -30.536 -26.592 40.665 1.00 45.45 C ANISOU 1257 C THR A 226 4595 5162 7512 -34 689 -427 C ATOM 1258 O THR A 226 -30.712 -25.715 41.515 1.00 42.54 O ANISOU 1258 O THR A 226 4160 4895 7106 48 764 -306 O ATOM 1259 CB THR A 226 -31.465 -28.899 41.107 1.00 49.93 C ANISOU 1259 CB THR A 226 5267 5329 8373 -199 778 -361 C ATOM 1260 OG1 THR A 226 -32.079 -28.904 39.813 1.00 49.10 O ANISOU 1260 OG1 THR A 226 5084 5252 8320 -389 631 -487 O ATOM 1261 CG2 THR A 226 -32.460 -28.384 42.135 1.00 49.45 C ANISOU 1261 CG2 THR A 226 5076 5313 8399 -218 892 -162 C ATOM 1262 N PRO A 227 -30.599 -26.343 39.344 1.00 44.72 N ANISOU 1262 N PRO A 227 4472 5141 7378 -140 551 -563 N ATOM 1263 CA PRO A 227 -31.068 -25.047 38.841 1.00 41.61 C ANISOU 1263 CA PRO A 227 3951 4935 6924 -176 473 -546 C ATOM 1264 C PRO A 227 -32.460 -24.699 39.364 1.00 40.40 C ANISOU 1264 C PRO A 227 3627 4797 6925 -250 503 -389 C ATOM 1265 O PRO A 227 -33.396 -25.485 39.212 1.00 41.81 O ANISOU 1265 O PRO A 227 3740 4871 7274 -397 482 -367 O ATOM 1266 CB PRO A 227 -31.096 -25.244 37.316 1.00 42.33 C ANISOU 1266 CB PRO A 227 4067 5049 6968 -307 312 -710 C ATOM 1267 CG PRO A 227 -30.903 -26.724 37.091 1.00 44.78 C ANISOU 1267 CG PRO A 227 4498 5160 7356 -367 316 -811 C ATOM 1268 CD PRO A 227 -30.097 -27.192 38.253 1.00 45.84 C ANISOU 1268 CD PRO A 227 4726 5198 7492 -202 465 -748 C ATOM 1269 N ILE A 228 -32.583 -23.525 39.977 1.00 80.17 N ANISOU 1269 N ILE A 228 8589 9962 11909 -151 559 -287 N ATOM 1270 CA ILE A 228 -33.825 -23.116 40.626 1.00 78.94 C ANISOU 1270 CA ILE A 228 8268 9831 11896 -177 626 -133 C ATOM 1271 C ILE A 228 -34.695 -22.237 39.733 1.00 77.98 C ANISOU 1271 C ILE A 228 7986 9835 11807 -251 492 -130 C ATOM 1272 O ILE A 228 -35.748 -21.761 40.158 1.00 77.29 O ANISOU 1272 O ILE A 228 7730 9793 11846 -258 535 -10 O ATOM 1273 CB ILE A 228 -33.542 -22.358 41.936 1.00 75.71 C ANISOU 1273 CB ILE A 228 7882 9471 11414 -9 787 -21 C ATOM 1274 CG1 ILE A 228 -32.659 -21.138 41.661 1.00 73.40 C ANISOU 1274 CG1 ILE A 228 7647 9315 10929 99 741 -84 C ATOM 1275 CG2 ILE A 228 -32.884 -23.277 42.951 1.00 76.85 C ANISOU 1275 CG2 ILE A 228 8170 9492 11539 68 913 12 C ATOM 1276 CD1 ILE A 228 -32.241 -20.388 42.907 1.00 71.95 C ANISOU 1276 CD1 ILE A 228 7508 9178 10652 253 880 -7 C ATOM 1277 N VAL A 229 -34.254 -22.023 38.498 1.00 59.78 N ANISOU 1277 N VAL A 229 5736 7592 9385 -295 332 -258 N ATOM 1278 CA VAL A 229 -34.995 -21.181 37.567 1.00 59.12 C ANISOU 1278 CA VAL A 229 5531 7632 9299 -348 178 -251 C ATOM 1279 C VAL A 229 -35.657 -22.035 36.483 1.00 61.43 C ANISOU 1279 C VAL A 229 5772 7894 9673 -538 4 -340 C ATOM 1280 O VAL A 229 -35.260 -23.179 36.257 1.00 63.57 O ANISOU 1280 O VAL A 229 6154 8046 9954 -621 -4 -448 O ATOM 1281 CB VAL A 229 -34.086 -20.098 36.944 1.00 56.63 C ANISOU 1281 CB VAL A 229 5327 7428 8760 -260 124 -309 C ATOM 1282 CG1 VAL A 229 -33.323 -20.654 35.751 1.00 58.72 C ANISOU 1282 CG1 VAL A 229 5734 7686 8888 -340 9 -479 C ATOM 1283 CG2 VAL A 229 -34.902 -18.874 36.554 1.00 56.57 C ANISOU 1283 CG2 VAL A 229 5195 7539 8759 -235 35 -220 C ATOM 1284 N ASP A 230 -36.671 -21.480 35.823 1.00 87.66 N ANISOU 1284 N ASP A 230 8929 11321 13056 -602 -143 -299 N ATOM 1285 CA ASP A 230 -37.469 -22.230 34.854 1.00 89.89 C ANISOU 1285 CA ASP A 230 9127 11595 13431 -797 -332 -377 C ATOM 1286 C ASP A 230 -36.676 -22.681 33.628 1.00 91.23 C ANISOU 1286 C ASP A 230 9493 11755 13414 -873 -472 -565 C ATOM 1287 O ASP A 230 -35.510 -22.324 33.457 1.00 91.22 O ANISOU 1287 O ASP A 230 9674 11774 13212 -770 -423 -628 O ATOM 1288 CB ASP A 230 -38.696 -21.421 34.423 1.00 91.82 C ANISOU 1288 CB ASP A 230 9137 11984 13767 -820 -480 -284 C ATOM 1289 CG ASP A 230 -38.326 -20.119 33.741 1.00 92.08 C ANISOU 1289 CG ASP A 230 9234 12155 13597 -697 -578 -267 C ATOM 1290 OD1 ASP A 230 -37.254 -19.564 34.059 1.00 91.82 O ANISOU 1290 OD1 ASP A 230 9373 12114 13399 -566 -459 -275 O ATOM 1291 OD2 ASP A 230 -39.110 -19.649 32.889 1.00 93.83 O ANISOU 1291 OD2 ASP A 230 9334 12492 13826 -736 -779 -242 O ATOM 1292 N THR A 231 -37.329 -23.469 32.779 1.00 72.30 N ANISOU 1292 N THR A 231 7053 9332 11087 -1062 -641 -662 N ATOM 1293 CA THR A 231 -36.697 -24.046 31.597 1.00 73.20 C ANISOU 1293 CA THR A 231 7361 9423 11029 -1154 -770 -860 C ATOM 1294 C THR A 231 -36.228 -22.978 30.612 1.00 72.89 C ANISOU 1294 C THR A 231 7414 9549 10734 -1082 -888 -889 C ATOM 1295 O THR A 231 -35.157 -23.100 30.017 1.00 73.50 O ANISOU 1295 O THR A 231 7703 9618 10605 -1054 -870 -1020 O ATOM 1296 CB THR A 231 -37.655 -25.017 30.873 1.00 75.50 C ANISOU 1296 CB THR A 231 7573 9667 11446 -1391 -954 -961 C ATOM 1297 OG1 THR A 231 -38.124 -26.007 31.797 1.00 76.29 O ANISOU 1297 OG1 THR A 231 7592 9597 11798 -1479 -827 -920 O ATOM 1298 CG2 THR A 231 -36.953 -25.707 29.713 1.00 76.70 C ANISOU 1298 CG2 THR A 231 7962 9772 11410 -1482 -1061 -1188 C ATOM 1299 N ALA A 232 -37.031 -21.931 30.451 1.00 47.74 N ANISOU 1299 N ALA A 232 4068 6508 7564 -1044 -997 -760 N ATOM 1300 CA ALA A 232 -36.717 -20.855 29.514 1.00 47.95 C ANISOU 1300 CA ALA A 232 4185 6681 7353 -978 -1117 -755 C ATOM 1301 C ALA A 232 -35.426 -20.131 29.886 1.00 45.99 C ANISOU 1301 C ALA A 232 4110 6435 6932 -818 -935 -743 C ATOM 1302 O ALA A 232 -34.514 -20.004 29.066 1.00 46.40 O ANISOU 1302 O ALA A 232 4358 6523 6752 -820 -956 -852 O ATOM 1303 CB ALA A 232 -37.874 -19.872 29.431 1.00 46.92 C ANISOU 1303 CB ALA A 232 3839 6681 7310 -935 -1251 -591 C ATOM 1304 N THR A 233 -35.355 -19.659 31.127 1.00 33.05 N ANISOU 1304 N THR A 233 2393 4762 5402 -688 -752 -616 N ATOM 1305 CA THR A 233 -34.183 -18.935 31.608 1.00 30.36 C ANISOU 1305 CA THR A 233 2187 4427 4921 -546 -584 -602 C ATOM 1306 C THR A 233 -32.946 -19.828 31.594 1.00 29.16 C ANISOU 1306 C THR A 233 2209 4194 4676 -558 -479 -759 C ATOM 1307 O THR A 233 -31.845 -19.374 31.277 1.00 27.65 O ANISOU 1307 O THR A 233 2162 4046 4298 -501 -416 -821 O ATOM 1308 CB THR A 233 -34.403 -18.395 33.031 1.00 29.59 C ANISOU 1308 CB THR A 233 1977 4301 4967 -417 -412 -453 C ATOM 1309 OG1 THR A 233 -35.647 -17.685 33.089 1.00 31.19 O ANISOU 1309 OG1 THR A 233 1990 4566 5293 -394 -494 -312 O ATOM 1310 CG2 THR A 233 -33.269 -17.465 33.436 1.00 27.33 C ANISOU 1310 CG2 THR A 233 1822 4039 4525 -287 -273 -443 C ATOM 1311 N LEU A 234 -33.140 -21.099 31.937 1.00 35.48 N ANISOU 1311 N LEU A 234 2989 4872 5620 -632 -454 -821 N ATOM 1312 CA LEU A 234 -32.064 -22.081 31.897 1.00 35.21 C ANISOU 1312 CA LEU A 234 3114 4738 5526 -630 -366 -971 C ATOM 1313 C LEU A 234 -31.524 -22.194 30.476 1.00 36.07 C ANISOU 1313 C LEU A 234 3377 4904 5425 -703 -477 -1139 C ATOM 1314 O LEU A 234 -30.309 -22.221 30.260 1.00 35.31 O ANISOU 1314 O LEU A 234 3422 4817 5177 -639 -384 -1244 O ATOM 1315 CB LEU A 234 -32.563 -23.441 32.389 1.00 36.42 C ANISOU 1315 CB LEU A 234 3231 4724 5885 -711 -338 -994 C ATOM 1316 CG LEU A 234 -31.511 -24.535 32.582 1.00 36.35 C ANISOU 1316 CG LEU A 234 3384 4574 5856 -672 -227 -1124 C ATOM 1317 CD1 LEU A 234 -30.434 -24.079 33.552 1.00 34.34 C ANISOU 1317 CD1 LEU A 234 3170 4338 5539 -484 -54 -1069 C ATOM 1318 CD2 LEU A 234 -32.164 -25.819 33.067 1.00 37.91 C ANISOU 1318 CD2 LEU A 234 3556 4578 6270 -768 -204 -1122 C ATOM 1319 N LYS A 235 -32.437 -22.247 29.509 1.00 32.30 N ANISOU 1319 N LYS A 235 2865 4477 4933 -837 -675 -1165 N ATOM 1320 CA LYS A 235 -32.063 -22.239 28.101 1.00 33.59 C ANISOU 1320 CA LYS A 235 3184 4714 4862 -912 -798 -1311 C ATOM 1321 C LYS A 235 -31.248 -20.995 27.775 1.00 31.95 C ANISOU 1321 C LYS A 235 3067 4640 4434 -812 -743 -1269 C ATOM 1322 O LYS A 235 -30.211 -21.083 27.126 1.00 31.90 O ANISOU 1322 O LYS A 235 3228 4659 4234 -805 -683 -1401 O ATOM 1323 CB LYS A 235 -33.301 -22.298 27.202 1.00 36.47 C ANISOU 1323 CB LYS A 235 3475 5142 5240 -1062 -1050 -1313 C ATOM 1324 CG LYS A 235 -33.943 -23.670 27.102 1.00 38.95 C ANISOU 1324 CG LYS A 235 3759 5325 5715 -1222 -1130 -1428 C ATOM 1325 CD LYS A 235 -35.166 -23.642 26.199 1.00 42.11 C ANISOU 1325 CD LYS A 235 4060 5818 6123 -1378 -1406 -1434 C ATOM 1326 CE LYS A 235 -35.828 -25.008 26.125 1.00 44.94 C ANISOU 1326 CE LYS A 235 4380 6037 6660 -1569 -1487 -1558 C ATOM 1327 NZ LYS A 235 -37.051 -24.988 25.277 1.00 48.42 N ANISOU 1327 NZ LYS A 235 4688 6585 7123 -1735 -1778 -1569 N ATOM 1328 N VAL A 236 -31.716 -19.841 28.240 1.00 30.92 N ANISOU 1328 N VAL A 236 2825 4582 4340 -737 -749 -1087 N ATOM 1329 CA VAL A 236 -31.038 -18.577 27.962 1.00 29.53 C ANISOU 1329 CA VAL A 236 2741 4509 3972 -657 -697 -1030 C ATOM 1330 C VAL A 236 -29.602 -18.544 28.491 1.00 27.50 C ANISOU 1330 C VAL A 236 2576 4228 3644 -571 -479 -1098 C ATOM 1331 O VAL A 236 -28.679 -18.161 27.771 1.00 27.44 O ANISOU 1331 O VAL A 236 2712 4291 3426 -577 -435 -1175 O ATOM 1332 CB VAL A 236 -31.823 -17.374 28.523 1.00 28.87 C ANISOU 1332 CB VAL A 236 2524 4469 3974 -572 -720 -821 C ATOM 1333 CG1 VAL A 236 -31.072 -16.078 28.262 1.00 27.47 C ANISOU 1333 CG1 VAL A 236 2470 4364 3604 -503 -651 -767 C ATOM 1334 CG2 VAL A 236 -33.211 -17.315 27.905 1.00 31.22 C ANISOU 1334 CG2 VAL A 236 2707 4820 4336 -640 -952 -750 C ATOM 1335 N VAL A 237 -29.413 -18.955 29.743 1.00 37.46 N ANISOU 1335 N VAL A 237 3753 5402 5077 -494 -346 -1069 N ATOM 1336 CA VAL A 237 -28.084 -18.921 30.353 1.00 36.46 C ANISOU 1336 CA VAL A 237 3684 5269 4899 -399 -162 -1125 C ATOM 1337 C VAL A 237 -27.143 -19.989 29.784 1.00 36.43 C ANISOU 1337 C VAL A 237 3795 5230 4815 -423 -115 -1323 C ATOM 1338 O VAL A 237 -25.952 -19.731 29.581 1.00 35.42 O ANISOU 1338 O VAL A 237 3741 5162 4556 -377 -4 -1406 O ATOM 1339 CB VAL A 237 -28.146 -19.005 31.901 1.00 35.69 C ANISOU 1339 CB VAL A 237 3477 5099 4983 -294 -44 -1026 C ATOM 1340 CG1 VAL A 237 -28.843 -17.779 32.469 1.00 34.78 C ANISOU 1340 CG1 VAL A 237 3271 5026 4916 -244 -46 -851 C ATOM 1341 CG2 VAL A 237 -28.847 -20.274 32.355 1.00 36.37 C ANISOU 1341 CG2 VAL A 237 3503 5056 5261 -328 -66 -1032 C ATOM 1342 N ILE A 238 -27.676 -21.179 29.516 1.00 45.02 N ANISOU 1342 N ILE A 238 4894 6219 5992 -496 -194 -1404 N ATOM 1343 CA ILE A 238 -26.875 -22.246 28.921 1.00 45.29 C ANISOU 1343 CA ILE A 238 5053 6195 5958 -511 -151 -1604 C ATOM 1344 C ILE A 238 -26.439 -21.870 27.505 1.00 45.18 C ANISOU 1344 C ILE A 238 5178 6297 5690 -582 -197 -1721 C ATOM 1345 O ILE A 238 -25.295 -22.109 27.114 1.00 44.57 O ANISOU 1345 O ILE A 238 5198 6248 5487 -541 -82 -1860 O ATOM 1346 CB ILE A 238 -27.625 -23.595 28.922 1.00 45.51 C ANISOU 1346 CB ILE A 238 5083 6062 6146 -592 -226 -1670 C ATOM 1347 CG1 ILE A 238 -27.789 -24.105 30.355 1.00 45.90 C ANISOU 1347 CG1 ILE A 238 5033 5981 6423 -508 -130 -1563 C ATOM 1348 CG2 ILE A 238 -26.880 -24.629 28.094 1.00 45.55 C ANISOU 1348 CG2 ILE A 238 5250 5999 6055 -615 -198 -1897 C ATOM 1349 CD1 ILE A 238 -28.560 -25.399 30.459 1.00 47.65 C ANISOU 1349 CD1 ILE A 238 5261 6020 6824 -601 -180 -1606 C ATOM 1350 N GLN A 239 -27.352 -21.267 26.747 1.00 48.46 N ANISOU 1350 N GLN A 239 5598 6788 6026 -681 -362 -1656 N ATOM 1351 CA GLN A 239 -27.034 -20.760 25.415 1.00 48.71 C ANISOU 1351 CA GLN A 239 5779 6942 5787 -749 -417 -1728 C ATOM 1352 C GLN A 239 -25.998 -19.648 25.504 1.00 48.17 C ANISOU 1352 C GLN A 239 5745 6979 5579 -675 -265 -1679 C ATOM 1353 O GLN A 239 -25.097 -19.563 24.672 1.00 48.59 O ANISOU 1353 O GLN A 239 5933 7104 5425 -697 -185 -1799 O ATOM 1354 CB GLN A 239 -28.291 -20.240 24.714 1.00 50.01 C ANISOU 1354 CB GLN A 239 5925 7171 5903 -845 -645 -1628 C ATOM 1355 CG GLN A 239 -29.229 -21.325 24.214 1.00 51.18 C ANISOU 1355 CG GLN A 239 6072 7251 6121 -969 -825 -1728 C ATOM 1356 CD GLN A 239 -30.590 -20.778 23.831 1.00 52.44 C ANISOU 1356 CD GLN A 239 6137 7486 6300 -1042 -1066 -1597 C ATOM 1357 OE1 GLN A 239 -31.544 -21.533 23.641 1.00 54.05 O ANISOU 1357 OE1 GLN A 239 6273 7643 6618 -1152 -1229 -1642 O ATOM 1358 NE2 GLN A 239 -30.688 -19.458 23.717 1.00 52.59 N ANISOU 1358 NE2 GLN A 239 6146 7617 6217 -982 -1091 -1436 N ATOM 1359 N LEU A 240 -26.139 -18.795 26.515 1.00 28.81 N ANISOU 1359 N LEU A 240 3173 4532 3240 -598 -216 -1510 N ATOM 1360 CA LEU A 240 -25.178 -17.728 26.764 1.00 27.65 C ANISOU 1360 CA LEU A 240 3046 4464 2995 -543 -69 -1464 C ATOM 1361 C LEU A 240 -23.777 -18.302 26.933 1.00 28.20 C ANISOU 1361 C LEU A 240 3140 4541 3034 -491 111 -1624 C ATOM 1362 O LEU A 240 -22.833 -17.868 26.270 1.00 29.47 O ANISOU 1362 O LEU A 240 3389 4796 3012 -516 211 -1699 O ATOM 1363 CB LEU A 240 -25.568 -16.939 28.015 1.00 25.15 C ANISOU 1363 CB LEU A 240 2596 4120 2841 -460 -38 -1287 C ATOM 1364 CG LEU A 240 -24.505 -15.998 28.588 1.00 23.98 C ANISOU 1364 CG LEU A 240 2444 4023 2646 -402 127 -1259 C ATOM 1365 CD1 LEU A 240 -24.304 -14.787 27.689 1.00 24.76 C ANISOU 1365 CD1 LEU A 240 2661 4207 2541 -466 130 -1207 C ATOM 1366 CD2 LEU A 240 -24.869 -15.573 30.001 1.00 21.69 C ANISOU 1366 CD2 LEU A 240 2027 3677 2537 -309 164 -1128 C ATOM 1367 N ASN A 241 -23.655 -19.287 27.818 1.00 72.51 N ANISOU 1367 N ASN A 241 8670 10053 8828 -413 155 -1669 N ATOM 1368 CA ASN A 241 -22.373 -19.938 28.061 1.00 70.85 C ANISOU 1368 CA ASN A 241 8460 9842 8616 -331 310 -1813 C ATOM 1369 C ASN A 241 -21.819 -20.625 26.815 1.00 71.02 C ANISOU 1369 C ASN A 241 8618 9889 8477 -381 338 -2013 C ATOM 1370 O ASN A 241 -20.637 -20.496 26.499 1.00 69.60 O ANISOU 1370 O ASN A 241 8461 9797 8184 -349 482 -2120 O ATOM 1371 CB ASN A 241 -22.493 -20.948 29.205 1.00 73.09 C ANISOU 1371 CB ASN A 241 8657 9991 9121 -228 329 -1805 C ATOM 1372 CG ASN A 241 -21.170 -21.607 29.542 1.00 71.02 C ANISOU 1372 CG ASN A 241 8382 9730 8872 -107 473 -1938 C ATOM 1373 OD1 ASN A 241 -20.104 -21.018 29.362 1.00 69.22 O ANISOU 1373 OD1 ASN A 241 8139 9628 8531 -83 581 -1993 O ATOM 1374 ND2 ASN A 241 -21.231 -22.839 30.034 1.00 71.53 N ANISOU 1374 ND2 ASN A 241 8446 9649 9081 -31 476 -1986 N ATOM 1375 N THR A 242 -22.683 -21.347 26.107 1.00 44.04 N ANISOU 1375 N THR A 242 5285 6400 5048 -466 203 -2070 N ATOM 1376 CA THR A 242 -22.270 -22.109 24.932 1.00 44.30 C ANISOU 1376 CA THR A 242 5472 6436 4925 -517 219 -2278 C ATOM 1377 C THR A 242 -21.772 -21.211 23.800 1.00 44.22 C ANISOU 1377 C THR A 242 5581 6589 4632 -592 262 -2311 C ATOM 1378 O THR A 242 -20.760 -21.503 23.165 1.00 42.74 O ANISOU 1378 O THR A 242 5477 6457 4304 -577 403 -2476 O ATOM 1379 CB THR A 242 -23.412 -23.003 24.410 1.00 47.10 C ANISOU 1379 CB THR A 242 5897 6676 5322 -619 38 -2333 C ATOM 1380 OG1 THR A 242 -23.877 -23.854 25.465 1.00 46.94 O ANISOU 1380 OG1 THR A 242 5777 6490 5569 -565 21 -2294 O ATOM 1381 CG2 THR A 242 -22.933 -23.861 23.250 1.00 47.72 C ANISOU 1381 CG2 THR A 242 6158 6740 5234 -666 65 -2575 C ATOM 1382 N PHE A 243 -22.485 -20.118 23.552 1.00 48.17 N ANISOU 1382 N PHE A 243 6091 7160 5050 -667 151 -2148 N ATOM 1383 CA PHE A 243 -22.101 -19.186 22.499 1.00 48.34 C ANISOU 1383 CA PHE A 243 6249 7323 4797 -744 187 -2140 C ATOM 1384 C PHE A 243 -20.880 -18.351 22.880 1.00 46.63 C ANISOU 1384 C PHE A 243 5980 7195 4541 -696 403 -2118 C ATOM 1385 O PHE A 243 -19.945 -18.213 22.092 1.00 46.03 O ANISOU 1385 O PHE A 243 6002 7216 4270 -731 547 -2229 O ATOM 1386 CB PHE A 243 -23.265 -18.258 22.136 1.00 51.64 C ANISOU 1386 CB PHE A 243 6700 7774 5148 -817 -8 -1953 C ATOM 1387 CG PHE A 243 -24.307 -18.897 21.261 1.00 53.64 C ANISOU 1387 CG PHE A 243 7047 8007 5326 -909 -229 -2007 C ATOM 1388 CD1 PHE A 243 -23.986 -19.339 19.988 1.00 54.47 C ANISOU 1388 CD1 PHE A 243 7354 8171 5173 -989 -233 -2175 C ATOM 1389 CD2 PHE A 243 -25.612 -19.035 21.702 1.00 55.20 C ANISOU 1389 CD2 PHE A 243 7128 8137 5707 -922 -432 -1895 C ATOM 1390 CE1 PHE A 243 -24.943 -19.920 19.177 1.00 56.37 C ANISOU 1390 CE1 PHE A 243 7688 8400 5329 -1087 -456 -2240 C ATOM 1391 CE2 PHE A 243 -26.575 -19.616 20.897 1.00 56.45 C ANISOU 1391 CE2 PHE A 243 7353 8291 5806 -1025 -653 -1954 C ATOM 1392 CZ PHE A 243 -26.240 -20.058 19.633 1.00 57.06 C ANISOU 1392 CZ PHE A 243 7642 8424 5615 -1110 -676 -2130 C ATOM 1393 N MET A 244 -20.891 -17.800 24.090 1.00 58.14 N ANISOU 1393 N MET A 244 7282 8626 6182 -625 430 -1981 N ATOM 1394 CA MET A 244 -19.861 -16.846 24.495 1.00 56.29 C ANISOU 1394 CA MET A 244 6992 8478 5917 -608 603 -1944 C ATOM 1395 C MET A 244 -18.540 -17.482 24.929 1.00 54.34 C ANISOU 1395 C MET A 244 6647 8264 5735 -523 787 -2102 C ATOM 1396 O MET A 244 -17.477 -16.889 24.748 1.00 53.58 O ANISOU 1396 O MET A 244 6534 8279 5544 -548 951 -2144 O ATOM 1397 CB MET A 244 -20.386 -15.924 25.600 1.00 54.35 C ANISOU 1397 CB MET A 244 6637 8193 5822 -572 555 -1748 C ATOM 1398 CG MET A 244 -21.578 -15.066 25.195 1.00 56.59 C ANISOU 1398 CG MET A 244 6997 8458 6045 -632 395 -1573 C ATOM 1399 SD MET A 244 -21.219 -13.923 23.846 1.00 58.29 S ANISOU 1399 SD MET A 244 7415 8779 5952 -755 444 -1532 S ATOM 1400 CE MET A 244 -21.986 -14.765 22.463 1.00 60.05 C ANISOU 1400 CE MET A 244 7800 9019 5998 -825 272 -1614 C ATOM 1401 N SER A 245 -18.601 -18.681 25.501 1.00 74.40 N ANISOU 1401 N SER A 245 9119 10708 8442 -421 762 -2185 N ATOM 1402 CA SER A 245 -17.399 -19.316 26.035 1.00 72.73 C ANISOU 1402 CA SER A 245 8797 10519 8318 -301 914 -2316 C ATOM 1403 C SER A 245 -16.857 -20.430 25.145 1.00 73.34 C ANISOU 1403 C SER A 245 8962 10589 8312 -274 990 -2534 C ATOM 1404 O SER A 245 -15.789 -20.980 25.414 1.00 72.31 O ANISOU 1404 O SER A 245 8744 10490 8239 -161 1129 -2661 O ATOM 1405 CB SER A 245 -17.654 -19.856 27.445 1.00 75.53 C ANISOU 1405 CB SER A 245 9016 10761 8918 -169 861 -2248 C ATOM 1406 OG SER A 245 -18.608 -20.903 27.425 1.00 75.67 O ANISOU 1406 OG SER A 245 9094 10625 9030 -157 739 -2261 O ATOM 1407 N PHE A 246 -17.588 -20.762 24.085 1.00 42.61 N ANISOU 1407 N PHE A 246 5244 6659 4286 -372 896 -2585 N ATOM 1408 CA PHE A 246 -17.180 -21.860 23.214 1.00 44.61 C ANISOU 1408 CA PHE A 246 5615 6884 4451 -352 960 -2808 C ATOM 1409 C PHE A 246 -17.213 -21.495 21.733 1.00 46.92 C ANISOU 1409 C PHE A 246 6106 7278 4444 -492 976 -2881 C ATOM 1410 O PHE A 246 -16.175 -21.211 21.140 1.00 48.47 O ANISOU 1410 O PHE A 246 6324 7574 4518 -490 1141 -2919 O ATOM 1411 CB PHE A 246 -18.039 -23.098 23.474 1.00 44.35 C ANISOU 1411 CB PHE A 246 5624 6655 4574 -317 820 -2853 C ATOM 1412 CG PHE A 246 -17.583 -24.320 22.732 1.00 47.41 C ANISOU 1412 CG PHE A 246 6134 6970 4907 -272 896 -3098 C ATOM 1413 CD1 PHE A 246 -16.390 -24.941 23.063 1.00 48.60 C ANISOU 1413 CD1 PHE A 246 6206 7109 5150 -105 1069 -3204 C ATOM 1414 CD2 PHE A 246 -18.350 -24.855 21.712 1.00 49.18 C ANISOU 1414 CD2 PHE A 246 6554 7130 5001 -389 780 -3203 C ATOM 1415 CE1 PHE A 246 -15.967 -26.068 22.385 1.00 50.91 C ANISOU 1415 CE1 PHE A 246 6622 7296 5428 -39 1124 -3348 C ATOM 1416 CE2 PHE A 246 -17.933 -25.983 21.030 1.00 52.13 C ANISOU 1416 CE2 PHE A 246 7064 7416 5327 -346 854 -3431 C ATOM 1417 CZ PHE A 246 -16.740 -26.590 21.367 1.00 52.67 C ANISOU 1417 CZ PHE A 246 7059 7441 5513 -159 1027 -3468 C ATOM 1418 N LEU A 247 -18.408 -21.504 21.148 1.00 50.84 N ANISOU 1418 N LEU A 247 6736 7724 4857 -603 776 -2828 N ATOM 1419 CA LEU A 247 -18.578 -21.310 19.707 1.00 52.22 C ANISOU 1419 CA LEU A 247 7133 7983 4724 -731 750 -2904 C ATOM 1420 C LEU A 247 -17.888 -20.063 19.151 1.00 52.50 C ANISOU 1420 C LEU A 247 7216 8193 4538 -800 892 -2832 C ATOM 1421 O LEU A 247 -16.931 -20.174 18.392 1.00 54.29 O ANISOU 1421 O LEU A 247 7511 8461 4655 -780 1051 -2885 O ATOM 1422 CB LEU A 247 -20.063 -21.306 19.337 1.00 52.69 C ANISOU 1422 CB LEU A 247 7287 7984 4751 -837 470 -2815 C ATOM 1423 CG LEU A 247 -20.757 -22.665 19.430 1.00 53.93 C ANISOU 1423 CG LEU A 247 7463 7972 5057 -827 342 -2945 C ATOM 1424 CD1 LEU A 247 -22.229 -22.549 19.070 1.00 55.71 C ANISOU 1424 CD1 LEU A 247 7735 8163 5269 -948 55 -2848 C ATOM 1425 CD2 LEU A 247 -20.059 -23.678 18.534 1.00 55.84 C ANISOU 1425 CD2 LEU A 247 7875 8196 5146 -819 463 -3224 C ATOM 1426 N PHE A 248 -18.379 -18.889 19.533 1.00 59.28 N ANISOU 1426 N PHE A 248 8026 9080 5415 -846 808 -2603 N ATOM 1427 CA PHE A 248 -17.828 -17.614 19.062 1.00 59.36 C ANISOU 1427 CA PHE A 248 8099 9222 5230 -928 934 -2504 C ATOM 1428 C PHE A 248 -16.305 -17.446 19.265 1.00 57.62 C ANISOU 1428 C PHE A 248 7765 9067 5061 -876 1203 -2554 C ATOM 1429 O PHE A 248 -15.572 -17.222 18.289 1.00 58.91 O ANISOU 1429 O PHE A 248 8035 9287 5061 -918 1331 -2561 O ATOM 1430 CB PHE A 248 -18.621 -16.442 19.669 1.00 60.62 C ANISOU 1430 CB PHE A 248 8205 9353 5475 -951 798 -2243 C ATOM 1431 CG PHE A 248 -18.086 -15.083 19.316 1.00 60.42 C ANISOU 1431 CG PHE A 248 8250 9422 5282 -1037 927 -2121 C ATOM 1432 CD1 PHE A 248 -18.358 -14.514 18.083 1.00 62.23 C ANISOU 1432 CD1 PHE A 248 8718 9717 5210 -1147 891 -2063 C ATOM 1433 CD2 PHE A 248 -17.336 -14.361 20.231 1.00 58.74 C ANISOU 1433 CD2 PHE A 248 7880 9226 5211 -1015 1076 -2060 C ATOM 1434 CE1 PHE A 248 -17.875 -13.259 17.761 1.00 62.12 C ANISOU 1434 CE1 PHE A 248 8793 9765 5044 -1234 1021 -1935 C ATOM 1435 CE2 PHE A 248 -16.851 -13.106 19.915 1.00 58.99 C ANISOU 1435 CE2 PHE A 248 7987 9323 5103 -1116 1202 -1951 C ATOM 1436 CZ PHE A 248 -17.121 -12.554 18.679 1.00 60.49 C ANISOU 1436 CZ PHE A 248 8425 9559 4999 -1226 1183 -1882 C ATOM 1437 N PRO A 249 -15.816 -17.578 20.517 1.00 62.31 N ANISOU 1437 N PRO A 249 8130 9631 5916 -769 1262 -2550 N ATOM 1438 CA PRO A 249 -14.386 -17.316 20.726 1.00 62.09 C ANISOU 1438 CA PRO A 249 7964 9653 5974 -723 1458 -2539 C ATOM 1439 C PRO A 249 -13.473 -18.351 20.070 1.00 63.37 C ANISOU 1439 C PRO A 249 8143 9805 6132 -641 1569 -2683 C ATOM 1440 O PRO A 249 -12.420 -17.978 19.558 1.00 65.03 O ANISOU 1440 O PRO A 249 8335 10092 6282 -665 1730 -2682 O ATOM 1441 CB PRO A 249 -14.242 -17.372 22.249 1.00 59.67 C ANISOU 1441 CB PRO A 249 7425 9310 5938 -616 1438 -2501 C ATOM 1442 CG PRO A 249 -15.326 -18.275 22.691 1.00 59.81 C ANISOU 1442 CG PRO A 249 7456 9227 6043 -551 1284 -2564 C ATOM 1443 CD PRO A 249 -16.475 -18.002 21.768 1.00 61.05 C ANISOU 1443 CD PRO A 249 7822 9373 6004 -676 1137 -2521 C ATOM 1444 N MET A 250 -13.863 -19.622 20.084 1.00 69.68 N ANISOU 1444 N MET A 250 8977 10502 6995 -549 1493 -2810 N ATOM 1445 CA MET A 250 -13.052 -20.660 19.453 1.00 71.75 C ANISOU 1445 CA MET A 250 9278 10737 7247 -457 1601 -2954 C ATOM 1446 C MET A 250 -13.135 -20.582 17.936 1.00 74.68 C ANISOU 1446 C MET A 250 9889 11153 7330 -557 1637 -3004 C ATOM 1447 O MET A 250 -12.246 -21.059 17.235 1.00 76.68 O ANISOU 1447 O MET A 250 10181 11432 7522 -506 1783 -3098 O ATOM 1448 CB MET A 250 -13.456 -22.054 19.935 1.00 70.03 C ANISOU 1448 CB MET A 250 9051 10368 7189 -330 1515 -3075 C ATOM 1449 CG MET A 250 -13.082 -22.339 21.376 1.00 68.47 C ANISOU 1449 CG MET A 250 8620 10123 7270 -187 1516 -3034 C ATOM 1450 SD MET A 250 -11.325 -22.082 21.699 1.00 69.44 S ANISOU 1450 SD MET A 250 8537 10355 7489 -88 1707 -3007 S ATOM 1451 CE MET A 250 -11.364 -20.556 22.638 1.00 67.41 C ANISOU 1451 CE MET A 250 8120 10199 7294 -180 1673 -2821 C ATOM 1452 N LEU A 251 -14.211 -19.986 17.435 1.00 53.05 N ANISOU 1452 N LEU A 251 7317 8431 4408 -692 1497 -2937 N ATOM 1453 CA LEU A 251 -14.343 -19.746 16.007 1.00 55.53 C ANISOU 1453 CA LEU A 251 7878 8802 4419 -792 1505 -2952 C ATOM 1454 C LEU A 251 -13.332 -18.680 15.616 1.00 56.41 C ANISOU 1454 C LEU A 251 7965 9034 4434 -848 1703 -2856 C ATOM 1455 O LEU A 251 -12.541 -18.870 14.686 1.00 58.94 O ANISOU 1455 O LEU A 251 8370 9404 4622 -840 1855 -2927 O ATOM 1456 CB LEU A 251 -15.763 -19.293 15.665 1.00 55.16 C ANISOU 1456 CB LEU A 251 7997 8755 4209 -916 1273 -2872 C ATOM 1457 CG LEU A 251 -16.167 -19.271 14.192 1.00 57.98 C ANISOU 1457 CG LEU A 251 8638 9151 4242 -1005 1204 -2898 C ATOM 1458 CD1 LEU A 251 -15.793 -20.578 13.516 1.00 60.32 C ANISOU 1458 CD1 LEU A 251 9028 9383 4507 -927 1257 -3102 C ATOM 1459 CD2 LEU A 251 -17.659 -19.015 14.067 1.00 57.58 C ANISOU 1459 CD2 LEU A 251 8702 9088 4088 -1104 914 -2829 C ATOM 1460 N VAL A 252 -13.351 -17.568 16.349 1.00 54.48 N ANISOU 1460 N VAL A 252 7605 8831 4266 -907 1707 -2701 N ATOM 1461 CA VAL A 252 -12.386 -16.493 16.130 1.00 55.25 C ANISOU 1461 CA VAL A 252 7659 9023 4312 -981 1891 -2606 C ATOM 1462 C VAL A 252 -10.947 -17.005 16.225 1.00 56.47 C ANISOU 1462 C VAL A 252 7640 9213 4602 -887 2092 -2708 C ATOM 1463 O VAL A 252 -10.111 -16.711 15.367 1.00 58.84 O ANISOU 1463 O VAL A 252 7996 9593 4769 -935 2264 -2722 O ATOM 1464 CB VAL A 252 -12.587 -15.342 17.136 1.00 52.88 C ANISOU 1464 CB VAL A 252 7234 8730 4128 -1043 1859 -2445 C ATOM 1465 CG1 VAL A 252 -11.482 -14.307 16.993 1.00 53.88 C ANISOU 1465 CG1 VAL A 252 7298 8933 4241 -1129 2056 -2368 C ATOM 1466 CG2 VAL A 252 -13.953 -14.701 16.945 1.00 52.15 C ANISOU 1466 CG2 VAL A 252 7326 8619 3871 -1136 1677 -2326 C ATOM 1467 N ALA A 253 -10.674 -17.787 17.264 1.00 62.06 N ANISOU 1467 N ALA A 253 8143 9868 5570 -749 2066 -2775 N ATOM 1468 CA ALA A 253 -9.342 -18.335 17.494 1.00 62.82 C ANISOU 1468 CA ALA A 253 8054 10000 5815 -636 2224 -2864 C ATOM 1469 C ALA A 253 -8.935 -19.328 16.408 1.00 65.88 C ANISOU 1469 C ALA A 253 8574 10383 6073 -565 2324 -3019 C ATOM 1470 O ALA A 253 -7.756 -19.446 16.080 1.00 68.38 O ANISOU 1470 O ALA A 253 8804 10774 6403 -521 2508 -3079 O ATOM 1471 CB ALA A 253 -9.266 -18.987 18.868 1.00 61.76 C ANISOU 1471 CB ALA A 253 7699 9799 5968 -489 2142 -2882 C ATOM 1472 N SER A 254 -9.911 -20.042 15.857 1.00 86.89 N ANISOU 1472 N SER A 254 11445 12959 8610 -556 2201 -3092 N ATOM 1473 CA SER A 254 -9.639 -20.999 14.790 1.00 89.83 C ANISOU 1473 CA SER A 254 11982 13311 8840 -492 2280 -3251 C ATOM 1474 C SER A 254 -9.292 -20.278 13.492 1.00 92.67 C ANISOU 1474 C SER A 254 12516 13783 8910 -610 2411 -3228 C ATOM 1475 O SER A 254 -8.375 -20.684 12.775 1.00 96.48 O ANISOU 1475 O SER A 254 13023 14318 9319 -553 2594 -3330 O ATOM 1476 CB SER A 254 -10.830 -21.934 14.574 1.00 88.67 C ANISOU 1476 CB SER A 254 12018 13029 8644 -469 2088 -3345 C ATOM 1477 OG SER A 254 -12.002 -21.203 14.261 1.00 88.28 O ANISOU 1477 OG SER A 254 12121 12988 8435 -619 1913 -3245 O ATOM 1478 N ILE A 255 -10.029 -19.212 13.192 1.00 64.46 N ANISOU 1478 N ILE A 255 9072 10249 5171 -767 2323 -3088 N ATOM 1479 CA ILE A 255 -9.727 -18.392 12.023 1.00 66.93 C ANISOU 1479 CA ILE A 255 9559 10667 5206 -887 2446 -3030 C ATOM 1480 C ILE A 255 -8.334 -17.786 12.160 1.00 67.88 C ANISOU 1480 C ILE A 255 9487 10889 5414 -902 2692 -2997 C ATOM 1481 O ILE A 255 -7.504 -17.869 11.244 1.00 70.94 O ANISOU 1481 O ILE A 255 9937 11355 5663 -901 2887 -3064 O ATOM 1482 CB ILE A 255 -10.751 -17.251 11.847 1.00 65.89 C ANISOU 1482 CB ILE A 255 9579 10548 4907 -1041 2300 -2850 C ATOM 1483 CG1 ILE A 255 -12.176 -17.806 11.785 1.00 65.03 C ANISOU 1483 CG1 ILE A 255 9628 10353 4727 -1037 2027 -2878 C ATOM 1484 CG2 ILE A 255 -10.431 -16.430 10.609 1.00 68.76 C ANISOU 1484 CG2 ILE A 255 10144 11009 4972 -1157 2431 -2777 C ATOM 1485 CD1 ILE A 255 -12.361 -18.930 10.792 1.00 67.61 C ANISOU 1485 CD1 ILE A 255 10146 10646 4897 -978 1993 -3057 C ATOM 1486 N LEU A 256 -8.085 -17.189 13.322 1.00 65.43 N ANISOU 1486 N LEU A 256 8941 10581 5338 -918 2680 -2901 N ATOM 1487 CA LEU A 256 -6.800 -16.565 13.612 1.00 66.20 C ANISOU 1487 CA LEU A 256 8827 10773 5553 -952 2878 -2871 C ATOM 1488 C LEU A 256 -5.644 -17.552 13.488 1.00 68.35 C ANISOU 1488 C LEU A 256 8958 11086 5924 -805 3042 -3032 C ATOM 1489 O LEU A 256 -4.625 -17.237 12.882 1.00 70.97 O ANISOU 1489 O LEU A 256 9253 11524 6189 -846 3255 -3054 O ATOM 1490 CB LEU A 256 -6.810 -15.924 15.001 1.00 63.18 C ANISOU 1490 CB LEU A 256 8215 10371 5421 -975 2794 -2768 C ATOM 1491 CG LEU A 256 -7.118 -14.425 15.049 1.00 62.42 C ANISOU 1491 CG LEU A 256 8180 10294 5242 -1163 2788 -2591 C ATOM 1492 CD1 LEU A 256 -8.417 -14.099 14.329 1.00 62.25 C ANISOU 1492 CD1 LEU A 256 8460 10225 4970 -1241 2653 -2505 C ATOM 1493 CD2 LEU A 256 -7.170 -13.944 16.487 1.00 59.51 C ANISOU 1493 CD2 LEU A 256 7591 9893 5126 -1161 2692 -2518 C ATOM 1494 N ASN A 257 -5.808 -18.743 14.056 1.00 85.19 N ANISOU 1494 N ASN A 257 11017 13133 8219 -631 2949 -3140 N ATOM 1495 CA ASN A 257 -4.803 -19.796 13.931 1.00 87.73 C ANISOU 1495 CA ASN A 257 11228 13471 8632 -460 3092 -3293 C ATOM 1496 C ASN A 257 -4.588 -20.205 12.479 1.00 91.26 C ANISOU 1496 C ASN A 257 11903 13956 8815 -455 3239 -3403 C ATOM 1497 O ASN A 257 -3.454 -20.438 12.048 1.00 94.17 O ANISOU 1497 O ASN A 257 12185 14413 9182 -392 3455 -3486 O ATOM 1498 CB ASN A 257 -5.194 -21.017 14.765 1.00 86.03 C ANISOU 1498 CB ASN A 257 10949 13122 8615 -275 2949 -3376 C ATOM 1499 CG ASN A 257 -4.848 -20.858 16.231 1.00 83.69 C ANISOU 1499 CG ASN A 257 10362 12823 8612 -213 2878 -3306 C ATOM 1500 OD1 ASN A 257 -3.822 -21.357 16.693 1.00 84.22 O ANISOU 1500 OD1 ASN A 257 10225 12925 8849 -74 2969 -3365 O ATOM 1501 ND2 ASN A 257 -5.701 -20.160 16.970 1.00 80.88 N ANISOU 1501 ND2 ASN A 257 9991 12430 8309 -307 2711 -3179 N ATOM 1502 N THR A 258 -5.686 -20.289 11.732 1.00 77.54 N ANISOU 1502 N THR A 258 10454 12158 6848 -518 3116 -3407 N ATOM 1503 CA THR A 258 -5.637 -20.634 10.316 1.00 81.34 C ANISOU 1503 CA THR A 258 11195 12675 7037 -526 3221 -3507 C ATOM 1504 C THR A 258 -4.769 -19.648 9.542 1.00 83.92 C ANISOU 1504 C THR A 258 11529 13156 7202 -647 3451 -3441 C ATOM 1505 O THR A 258 -3.927 -20.051 8.738 1.00 87.64 O ANISOU 1505 O THR A 258 12029 13700 7572 -585 3661 -3552 O ATOM 1506 CB THR A 258 -7.046 -20.670 9.692 1.00 79.97 C ANISOU 1506 CB THR A 258 11326 12428 6630 -608 3005 -3492 C ATOM 1507 OG1 THR A 258 -7.837 -21.670 10.346 1.00 77.88 O ANISOU 1507 OG1 THR A 258 11067 12013 6510 -500 2813 -3583 O ATOM 1508 CG2 THR A 258 -6.967 -20.986 8.205 1.00 84.24 C ANISOU 1508 CG2 THR A 258 12147 13024 6836 -628 3104 -3586 C ATOM 1509 N VAL A 259 -4.970 -18.357 9.792 1.00 80.67 N ANISOU 1509 N VAL A 259 11096 12787 6767 -818 3420 -3261 N ATOM 1510 CA VAL A 259 -4.164 -17.330 9.134 1.00 83.04 C ANISOU 1510 CA VAL A 259 11404 13218 6931 -958 3640 -3181 C ATOM 1511 C VAL A 259 -2.712 -17.364 9.618 1.00 84.16 C ANISOU 1511 C VAL A 259 11231 13450 7298 -904 3856 -3233 C ATOM 1512 O VAL A 259 -1.771 -17.203 8.832 1.00 87.59 O ANISOU 1512 O VAL A 259 11664 13997 7619 -932 4101 -3275 O ATOM 1513 CB VAL A 259 -4.746 -15.925 9.370 1.00 81.21 C ANISOU 1513 CB VAL A 259 11230 12983 6646 -1152 3551 -2970 C ATOM 1514 CG1 VAL A 259 -3.988 -14.891 8.553 1.00 84.13 C ANISOU 1514 CG1 VAL A 259 11659 13464 6843 -1309 3784 -2884 C ATOM 1515 CG2 VAL A 259 -6.222 -15.904 9.019 1.00 80.08 C ANISOU 1515 CG2 VAL A 259 11368 12757 6303 -1187 3310 -2912 C ATOM 1516 N ILE A 260 -2.545 -17.580 10.919 1.00103.85 N ANISOU 1516 N ILE A 260 13455 15901 10102 -825 3759 -3230 N ATOM 1517 CA ILE A 260 -1.230 -17.633 11.549 1.00104.74 C ANISOU 1517 CA ILE A 260 13242 16101 10454 -763 3910 -3275 C ATOM 1518 C ILE A 260 -0.351 -18.723 10.940 1.00107.94 C ANISOU 1518 C ILE A 260 13613 16556 10843 -588 4098 -3451 C ATOM 1519 O ILE A 260 0.845 -18.519 10.731 1.00111.46 O ANISOU 1519 O ILE A 260 13884 17130 11333 -594 4322 -3486 O ATOM 1520 CB ILE A 260 -1.352 -17.840 13.078 1.00 98.03 C ANISOU 1520 CB ILE A 260 12143 15184 9920 -677 3726 -3248 C ATOM 1521 CG1 ILE A 260 -1.740 -16.528 13.762 1.00 95.47 C ANISOU 1521 CG1 ILE A 260 11771 14854 9647 -862 3620 -3078 C ATOM 1522 CG2 ILE A 260 -0.051 -18.346 13.669 1.00 99.35 C ANISOU 1522 CG2 ILE A 260 11994 15432 10323 -542 3848 -3336 C ATOM 1523 CD1 ILE A 260 -1.952 -16.660 15.253 1.00 92.03 C ANISOU 1523 CD1 ILE A 260 11121 14357 9490 -785 3430 -3046 C ATOM 1524 N ALA A 261 -0.951 -19.872 10.642 1.00 83.11 N ANISOU 1524 N ALA A 261 10636 13308 7633 -435 4011 -3567 N ATOM 1525 CA ALA A 261 -0.218 -20.983 10.038 1.00 86.48 C ANISOU 1525 CA ALA A 261 11070 13756 8031 -248 4183 -3745 C ATOM 1526 C ALA A 261 0.420 -20.600 8.701 1.00 90.63 C ANISOU 1526 C ALA A 261 11726 14418 8293 -328 4446 -3780 C ATOM 1527 O ALA A 261 1.638 -20.711 8.527 1.00 93.51 O ANISOU 1527 O ALA A 261 11906 14899 8723 -264 4683 -3846 O ATOM 1528 CB ALA A 261 -1.129 -22.190 9.868 1.00 86.04 C ANISOU 1528 CB ALA A 261 11231 13541 7919 -104 4029 -3862 C ATOM 1529 N ARG A 262 -0.405 -20.144 7.763 1.00144.20 N ANISOU 1529 N ARG A 262 18823 21193 14774 -465 4402 -3731 N ATOM 1530 CA ARG A 262 0.084 -19.769 6.439 1.00148.48 C ANISOU 1530 CA ARG A 262 19533 21859 15023 -548 4638 -3751 C ATOM 1531 C ARG A 262 1.027 -18.568 6.499 1.00149.42 C ANISOU 1531 C ARG A 262 19462 22120 15189 -715 4836 -3631 C ATOM 1532 O ARG A 262 1.971 -18.472 5.709 1.00154.55 O ANISOU 1532 O ARG A 262 20093 22900 15727 -727 5112 -3683 O ATOM 1533 CB ARG A 262 -1.077 -19.507 5.474 1.00137.41 C ANISOU 1533 CB ARG A 262 18518 20414 13275 -658 4511 -3708 C ATOM 1534 CG ARG A 262 -2.008 -18.382 5.890 1.00134.62 C ANISOU 1534 CG ARG A 262 18229 20018 12903 -847 4310 -3503 C ATOM 1535 CD ARG A 262 -3.121 -18.187 4.874 1.00136.16 C ANISOU 1535 CD ARG A 262 18805 20185 12742 -934 4177 -3462 C ATOM 1536 NE ARG A 262 -4.004 -17.081 5.234 1.00134.33 N ANISOU 1536 NE ARG A 262 18641 19915 12482 -1100 3995 -3255 N ATOM 1537 CZ ARG A 262 -3.823 -15.824 4.844 1.00135.78 C ANISOU 1537 CZ ARG A 262 18889 20171 12530 -1278 4100 -3088 C ATOM 1538 NH1 ARG A 262 -2.787 -15.508 4.078 1.00139.48 N ANISOU 1538 NH1 ARG A 262 19354 20761 12878 -1328 4390 -3104 N ATOM 1539 NH2 ARG A 262 -4.677 -14.882 5.219 1.00133.76 N ANISOU 1539 NH2 ARG A 262 18707 19859 12257 -1405 3924 -2903 N ATOM 1540 N ARG A 263 0.775 -17.660 7.439 1.00104.51 N ANISOU 1540 N ARG A 263 13636 16405 9669 -848 4702 -3478 N ATOM 1541 CA ARG A 263 1.663 -16.520 7.638 1.00105.42 C ANISOU 1541 CA ARG A 263 13557 16634 9864 -1018 4869 -3373 C ATOM 1542 C ARG A 263 3.038 -17.007 8.088 1.00107.29 C ANISOU 1542 C ARG A 263 13444 16974 10346 -896 5053 -3484 C ATOM 1543 O ARG A 263 4.070 -16.460 7.691 1.00110.37 O ANISOU 1543 O ARG A 263 13710 17503 10721 -990 5303 -3478 O ATOM 1544 CB ARG A 263 1.080 -15.554 8.670 1.00101.49 C ANISOU 1544 CB ARG A 263 12980 16065 9515 -1161 4666 -3208 C ATOM 1545 CG ARG A 263 1.743 -14.186 8.679 1.00102.68 C ANISOU 1545 CG ARG A 263 13029 16303 9682 -1388 4819 -3083 C ATOM 1546 CD ARG A 263 1.470 -13.442 7.382 1.00105.47 C ANISOU 1546 CD ARG A 263 13699 16687 9686 -1555 4949 -2990 C ATOM 1547 NE ARG A 263 0.045 -13.181 7.198 1.00103.98 N ANISOU 1547 NE ARG A 263 13814 16379 9316 -1603 4716 -2879 N ATOM 1548 CZ ARG A 263 -0.482 -12.641 6.104 1.00107.60 C ANISOU 1548 CZ ARG A 263 14600 16841 9443 -1716 4751 -2785 C ATOM 1549 NH1 ARG A 263 0.299 -12.304 5.086 1.00112.57 N ANISOU 1549 NH1 ARG A 263 15310 17582 9879 -1798 5023 -2788 N ATOM 1550 NH2 ARG A 263 -1.790 -12.440 6.027 1.00106.48 N ANISOU 1550 NH2 ARG A 263 14704 16595 9157 -1742 4512 -2683 N ATOM 1551 N LEU A 264 3.040 -18.046 8.917 1.00145.05 N ANISOU 1551 N LEU A 264 18069 21689 15356 -682 4928 -3582 N ATOM 1552 CA LEU A 264 4.277 -18.662 9.375 1.00147.16 C ANISOU 1552 CA LEU A 264 18012 22045 15856 -521 5074 -3692 C ATOM 1553 C LEU A 264 4.995 -19.328 8.212 1.00152.01 C ANISOU 1553 C LEU A 264 18708 22751 16300 -409 5349 -3833 C ATOM 1554 O LEU A 264 6.217 -19.234 8.093 1.00155.50 O ANISOU 1554 O LEU A 264 18918 23340 16825 -393 5589 -3879 O ATOM 1555 CB LEU A 264 3.999 -19.693 10.469 1.00139.42 C ANISOU 1555 CB LEU A 264 16897 20949 15127 -299 4866 -3752 C ATOM 1556 CG LEU A 264 5.220 -20.457 10.986 1.00141.23 C ANISOU 1556 CG LEU A 264 16805 21257 15600 -89 4990 -3862 C ATOM 1557 CD1 LEU A 264 6.218 -19.506 11.631 1.00141.62 C ANISOU 1557 CD1 LEU A 264 16517 21457 15836 -217 5075 -3794 C ATOM 1558 CD2 LEU A 264 4.806 -21.551 11.959 1.00138.81 C ANISOU 1558 CD2 LEU A 264 16436 20806 15499 140 4777 -3910 C ATOM 1559 N THR A 265 4.233 -20.000 7.354 1.00118.96 N ANISOU 1559 N THR A 265 14847 18480 11871 -331 5314 -3909 N ATOM 1560 CA THR A 265 4.821 -20.680 6.203 1.00123.39 C ANISOU 1560 CA THR A 265 15529 19117 12236 -214 5567 -4058 C ATOM 1561 C THR A 265 5.430 -19.698 5.203 1.00125.89 C ANISOU 1561 C THR A 265 15898 19599 12334 -408 5837 -4000 C ATOM 1562 O THR A 265 6.441 -20.001 4.568 1.00129.00 O ANISOU 1562 O THR A 265 16209 20122 12681 -328 6122 -4102 O ATOM 1563 CB THR A 265 3.804 -21.581 5.474 1.00112.96 C ANISOU 1563 CB THR A 265 14578 17665 10676 -111 5448 -4161 C ATOM 1564 OG1 THR A 265 2.738 -20.780 4.948 1.00112.75 O ANISOU 1564 OG1 THR A 265 14842 17603 10392 -319 5311 -4041 O ATOM 1565 CG2 THR A 265 3.237 -22.627 6.422 1.00109.41 C ANISOU 1565 CG2 THR A 265 14084 17040 10445 80 5206 -4227 C ATOM 1566 N VAL A 266 4.820 -18.523 5.063 1.00127.43 N ANISOU 1566 N VAL A 266 16236 19788 12394 -657 5758 -3832 N ATOM 1567 CA VAL A 266 5.339 -17.525 4.130 1.00130.51 C ANISOU 1567 CA VAL A 266 16697 20316 12573 -860 6010 -3753 C ATOM 1568 C VAL A 266 6.494 -16.723 4.738 1.00131.88 C ANISOU 1568 C VAL A 266 16501 20613 12993 -975 6174 -3692 C ATOM 1569 O VAL A 266 7.376 -16.252 4.019 1.00136.04 O ANISOU 1569 O VAL A 266 16976 21288 13422 -1067 6469 -3695 O ATOM 1570 CB VAL A 266 4.228 -16.584 3.591 1.00125.20 C ANISOU 1570 CB VAL A 266 16366 19583 11621 -1076 5881 -3589 C ATOM 1571 CG1 VAL A 266 3.755 -15.622 4.667 1.00120.90 C ANISOU 1571 CG1 VAL A 266 15708 18956 11271 -1230 5664 -3419 C ATOM 1572 CG2 VAL A 266 4.719 -15.820 2.370 1.00129.62 C ANISOU 1572 CG2 VAL A 266 17075 20276 11896 -1245 6167 -3530 C ATOM 1573 N MET A 267 6.499 -16.584 6.061 1.00161.80 N ANISOU 1573 N MET A 267 20031 24348 17097 -973 5982 -3644 N ATOM 1574 CA MET A 267 7.582 -15.874 6.736 1.00162.97 C ANISOU 1574 CA MET A 267 19813 24613 17494 -1079 6102 -3606 C ATOM 1575 C MET A 267 8.845 -16.728 6.833 1.00166.41 C ANISOU 1575 C MET A 267 19942 25177 18110 -874 6303 -3763 C ATOM 1576 O MET A 267 9.959 -16.225 6.681 1.00170.84 O ANISOU 1576 O MET A 267 20273 25899 18740 -965 6547 -3769 O ATOM 1577 CB MET A 267 7.155 -15.424 8.135 1.00162.18 C ANISOU 1577 CB MET A 267 19543 24422 17657 -1137 5821 -3513 C ATOM 1578 CG MET A 267 8.277 -14.772 8.930 1.00164.34 C ANISOU 1578 CG MET A 267 19428 24816 18197 -1240 5911 -3495 C ATOM 1579 SD MET A 267 7.879 -14.492 10.665 1.00160.70 S ANISOU 1579 SD MET A 267 18740 24261 18056 -1244 5574 -3431 S ATOM 1580 CE MET A 267 9.476 -13.970 11.288 1.00162.88 C ANISOU 1580 CE MET A 267 18558 24731 18599 -1335 5746 -3467 C ATOM 1581 N VAL A 268 8.663 -18.021 7.082 1.00136.83 N ANISOU 1581 N VAL A 268 16194 21355 14440 -596 6204 -3889 N ATOM 1582 CA VAL A 268 9.783 -18.926 7.324 1.00140.30 C ANISOU 1582 CA VAL A 268 16339 21890 15078 -357 6358 -4032 C ATOM 1583 C VAL A 268 10.603 -19.198 6.059 1.00146.83 C ANISOU 1583 C VAL A 268 17220 22860 15706 -306 6719 -4137 C ATOM 1584 O VAL A 268 11.751 -19.639 6.141 1.00150.35 O ANISOU 1584 O VAL A 268 17379 23434 16311 -158 6919 -4234 O ATOM 1585 CB VAL A 268 9.301 -20.263 7.940 1.00133.53 C ANISOU 1585 CB VAL A 268 15501 20881 14351 -64 6151 -4129 C ATOM 1586 CG1 VAL A 268 8.664 -21.150 6.878 1.00135.09 C ANISOU 1586 CG1 VAL A 268 16067 20991 14270 70 6194 -4239 C ATOM 1587 CG2 VAL A 268 10.443 -20.980 8.650 1.00135.01 C ANISOU 1587 CG2 VAL A 268 15303 21150 14842 164 6230 -4222 C ATOM 1588 N HIS A 269 10.011 -18.919 4.899 1.00132.36 N ANISOU 1588 N HIS A 269 15755 21014 13523 -422 6800 -4113 N ATOM 1589 CA HIS A 269 10.655 -19.160 3.607 1.00137.78 C ANISOU 1589 CA HIS A 269 16552 21833 13965 -382 7139 -4210 C ATOM 1590 C HIS A 269 11.113 -20.609 3.447 1.00140.25 C ANISOU 1590 C HIS A 269 16817 22145 14327 -41 7239 -4410 C ATOM 1591 O HIS A 269 10.295 -21.527 3.391 1.00138.64 O ANISOU 1591 O HIS A 269 16848 21785 14045 126 7064 -4492 O ATOM 1592 CB HIS A 269 11.833 -18.203 3.389 1.00142.84 C ANISOU 1592 CB HIS A 269 16936 22678 14659 -566 7437 -4154 C ATOM 1593 CG HIS A 269 11.421 -16.791 3.107 1.00143.17 C ANISOU 1593 CG HIS A 269 17135 22723 14542 -907 7431 -3972 C ATOM 1594 ND1 HIS A 269 11.190 -16.325 1.830 1.00147.18 N ANISOU 1594 ND1 HIS A 269 17964 23277 14681 -1047 7616 -3929 N ATOM 1595 CD2 HIS A 269 11.204 -15.742 3.935 1.00139.78 C ANISOU 1595 CD2 HIS A 269 16598 22248 14263 -1129 7267 -3820 C ATOM 1596 CE1 HIS A 269 10.846 -15.051 1.884 1.00145.71 C ANISOU 1596 CE1 HIS A 269 17865 23065 14433 -1337 7567 -3747 C ATOM 1597 NE2 HIS A 269 10.846 -14.673 3.150 1.00141.54 N ANISOU 1597 NE2 HIS A 269 17082 22478 14220 -1392 7359 -3684 N ATOM 1598 N PRO A 297 16.341 -15.722 12.694 1.00161.38 N ANISOU 1598 N PRO A 297 16358 25468 19490 -783 6539 -3982 N ATOM 1599 CA PRO A 297 17.289 -16.842 12.738 1.00164.97 C ANISOU 1599 CA PRO A 297 16531 26044 20105 -475 6666 -4107 C ATOM 1600 C PRO A 297 16.943 -17.846 13.835 1.00162.13 C ANISOU 1600 C PRO A 297 16092 25577 19933 -182 6371 -4135 C ATOM 1601 O PRO A 297 16.906 -19.049 13.578 1.00162.47 O ANISOU 1601 O PRO A 297 16199 25565 19967 120 6410 -4214 O ATOM 1602 CB PRO A 297 18.628 -16.159 13.038 1.00166.78 C ANISOU 1602 CB PRO A 297 16323 26509 20536 -621 6822 -4129 C ATOM 1603 CG PRO A 297 18.265 -14.851 13.661 1.00163.85 C ANISOU 1603 CG PRO A 297 15971 26098 20186 -952 6649 -4023 C ATOM 1604 CD PRO A 297 16.988 -14.436 13.003 1.00160.83 C ANISOU 1604 CD PRO A 297 16072 25521 19514 -1096 6599 -3929 C ATOM 1605 N GLY A 298 16.694 -17.351 15.043 1.00173.44 N ANISOU 1605 N GLY A 298 17401 26974 21526 -270 6085 -4071 N ATOM 1606 CA GLY A 298 16.329 -18.206 16.157 1.00170.84 C ANISOU 1606 CA GLY A 298 17007 26541 21364 -15 5793 -4078 C ATOM 1607 C GLY A 298 14.940 -17.889 16.676 1.00164.99 C ANISOU 1607 C GLY A 298 16568 25589 20531 -111 5495 -3978 C ATOM 1608 O GLY A 298 14.408 -18.594 17.533 1.00161.51 O ANISOU 1608 O GLY A 298 16154 25027 20186 88 5248 -3968 O ATOM 1609 N ARG A 299 14.353 -16.820 16.149 1.00140.45 N ANISOU 1609 N ARG A 299 13691 22436 17239 -412 5528 -3898 N ATOM 1610 CA ARG A 299 13.019 -16.395 16.556 1.00134.83 C ANISOU 1610 CA ARG A 299 13266 21533 16431 -523 5270 -3795 C ATOM 1611 C ARG A 299 11.943 -17.208 15.842 1.00133.07 C ANISOU 1611 C ARG A 299 13420 21132 16008 -382 5244 -3795 C ATOM 1612 O ARG A 299 10.876 -17.465 16.398 1.00128.99 O ANISOU 1612 O ARG A 299 13080 20448 15483 -323 4992 -3743 O ATOM 1613 CB ARG A 299 12.828 -14.902 16.275 1.00132.95 C ANISOU 1613 CB ARG A 299 13131 21307 16077 -892 5320 -3702 C ATOM 1614 CG ARG A 299 11.475 -14.353 16.702 1.00127.78 C ANISOU 1614 CG ARG A 299 12759 20463 15331 -1012 5069 -3589 C ATOM 1615 CD ARG A 299 11.343 -12.875 16.369 1.00128.12 C ANISOU 1615 CD ARG A 299 12916 20506 15260 -1364 5144 -3494 C ATOM 1616 NE ARG A 299 10.027 -12.353 16.727 1.00123.81 N ANISOU 1616 NE ARG A 299 12648 19774 14620 -1461 4918 -3381 N ATOM 1617 CZ ARG A 299 9.651 -11.090 16.552 1.00123.11 C ANISOU 1617 CZ ARG A 299 12717 19633 14429 -1742 4934 -3278 C ATOM 1618 NH1 ARG A 299 10.492 -10.212 16.024 1.00127.16 N ANISOU 1618 NH1 ARG A 299 13144 20256 14916 -1971 5165 -3272 N ATOM 1619 NH2 ARG A 299 8.433 -10.704 16.907 1.00118.89 N ANISOU 1619 NH2 ARG A 299 12424 18930 13820 -1794 4727 -3177 N ATOM 1620 N VAL A 300 12.234 -17.617 14.611 1.00152.67 N ANISOU 1620 N VAL A 300 16023 23657 18326 -331 5509 -3860 N ATOM 1621 CA VAL A 300 11.271 -18.353 13.796 1.00151.30 C ANISOU 1621 CA VAL A 300 16222 23330 17933 -217 5506 -3880 C ATOM 1622 C VAL A 300 10.953 -19.737 14.363 1.00150.03 C ANISOU 1622 C VAL A 300 16067 23049 17890 111 5348 -3947 C ATOM 1623 O VAL A 300 9.851 -20.252 14.176 1.00148.57 O ANISOU 1623 O VAL A 300 16184 22687 17577 179 5215 -3939 O ATOM 1624 CB VAL A 300 11.751 -18.491 12.336 1.00153.38 C ANISOU 1624 CB VAL A 300 16614 23684 17980 -227 5842 -3950 C ATOM 1625 CG1 VAL A 300 11.718 -17.139 11.638 1.00154.31 C ANISOU 1625 CG1 VAL A 300 16849 23865 17917 -565 5979 -3857 C ATOM 1626 CG2 VAL A 300 13.148 -19.091 12.284 1.00158.20 C ANISOU 1626 CG2 VAL A 300 16889 24468 18750 -43 6070 -4067 C ATOM 1627 N GLN A 301 11.919 -20.332 15.057 1.00167.07 N ANISOU 1627 N GLN A 301 17892 25298 20290 312 5362 -4012 N ATOM 1628 CA GLN A 301 11.723 -21.645 15.660 1.00167.16 C ANISOU 1628 CA GLN A 301 17892 25189 20433 635 5224 -4065 C ATOM 1629 C GLN A 301 10.804 -21.552 16.873 1.00161.69 C ANISOU 1629 C GLN A 301 17237 24355 19844 624 4878 -3970 C ATOM 1630 O GLN A 301 9.908 -22.380 17.050 1.00159.02 O ANISOU 1630 O GLN A 301 17109 23831 19481 777 4728 -3972 O ATOM 1631 CB GLN A 301 13.065 -22.264 16.055 1.00173.34 C ANISOU 1631 CB GLN A 301 18298 26119 21447 862 5345 -4148 C ATOM 1632 CG GLN A 301 13.997 -22.517 14.880 1.00179.27 C ANISOU 1632 CG GLN A 301 18999 27008 22110 923 5706 -4254 C ATOM 1633 CD GLN A 301 15.285 -23.201 15.293 1.00183.89 C ANISOU 1633 CD GLN A 301 19200 27732 22939 1180 5820 -4334 C ATOM 1634 OE1 GLN A 301 15.500 -23.486 16.471 1.00183.63 O ANISOU 1634 OE1 GLN A 301 18938 27695 23140 1311 5618 -4307 O ATOM 1635 NE2 GLN A 301 16.150 -23.468 14.322 1.00189.00 N ANISOU 1635 NE2 GLN A 301 19775 28509 23530 1260 6148 -4430 N ATOM 1636 N ALA A 302 11.030 -20.539 17.703 1.00138.88 N ANISOU 1636 N ALA A 302 14149 21554 17067 437 4760 -3892 N ATOM 1637 CA ALA A 302 10.179 -20.293 18.860 1.00133.53 C ANISOU 1637 CA ALA A 302 13506 20761 16469 400 4447 -3797 C ATOM 1638 C ALA A 302 8.784 -19.879 18.405 1.00129.51 C ANISOU 1638 C ALA A 302 13373 20090 15747 237 4353 -3720 C ATOM 1639 O ALA A 302 7.789 -20.168 19.071 1.00126.59 O ANISOU 1639 O ALA A 302 13136 19564 15397 293 4118 -3664 O ATOM 1640 CB ALA A 302 10.790 -19.225 19.751 1.00128.22 C ANISOU 1640 CB ALA A 302 12550 20229 15938 221 4367 -3749 C ATOM 1641 N LEU A 303 8.723 -19.201 17.263 1.00 96.21 N ANISOU 1641 N LEU A 303 9321 15914 11322 38 4541 -3714 N ATOM 1642 CA LEU A 303 7.451 -18.798 16.676 1.00 93.65 C ANISOU 1642 CA LEU A 303 9358 15452 10774 -112 4472 -3641 C ATOM 1643 C LEU A 303 6.673 -20.016 16.193 1.00 93.16 C ANISOU 1643 C LEU A 303 9554 15236 10607 92 4436 -3702 C ATOM 1644 O LEU A 303 5.471 -20.121 16.428 1.00 89.83 O ANISOU 1644 O LEU A 303 9350 14659 10125 78 4238 -3645 O ATOM 1645 CB LEU A 303 7.673 -17.815 15.525 1.00 95.87 C ANISOU 1645 CB LEU A 303 9756 15824 10848 -362 4697 -3615 C ATOM 1646 CG LEU A 303 7.368 -16.345 15.824 1.00 94.03 C ANISOU 1646 CG LEU A 303 9540 15600 10587 -662 4626 -3489 C ATOM 1647 CD1 LEU A 303 8.108 -15.876 17.067 1.00 93.63 C ANISOU 1647 CD1 LEU A 303 9145 15641 10791 -696 4531 -3479 C ATOM 1648 CD2 LEU A 303 7.718 -15.473 14.628 1.00 96.96 C ANISOU 1648 CD2 LEU A 303 10030 16058 10754 -888 4882 -3462 C ATOM 1649 N ARG A 304 7.366 -20.929 15.517 1.00126.31 N ANISOU 1649 N ARG A 304 13727 19478 14788 280 4632 -3825 N ATOM 1650 CA ARG A 304 6.772 -22.187 15.077 1.00126.48 C ANISOU 1650 CA ARG A 304 13983 19348 14726 495 4614 -3911 C ATOM 1651 C ARG A 304 6.256 -22.963 16.282 1.00123.78 C ANISOU 1651 C ARG A 304 13591 18860 14579 679 4359 -3891 C ATOM 1652 O ARG A 304 5.144 -23.500 16.268 1.00122.18 O ANISOU 1652 O ARG A 304 13639 18479 14303 727 4211 -3888 O ATOM 1653 CB ARG A 304 7.808 -23.027 14.329 1.00136.28 C ANISOU 1653 CB ARG A 304 15151 20673 15957 691 4883 -4053 C ATOM 1654 CG ARG A 304 7.302 -24.387 13.876 1.00137.98 C ANISOU 1654 CG ARG A 304 15609 20723 16094 930 4883 -4166 C ATOM 1655 CD ARG A 304 8.457 -25.338 13.596 1.00143.26 C ANISOU 1655 CD ARG A 304 16116 21460 16854 1194 5110 -4300 C ATOM 1656 NE ARG A 304 9.390 -24.801 12.610 1.00147.83 N ANISOU 1656 NE ARG A 304 16618 22238 17313 1099 5411 -4345 N ATOM 1657 CZ ARG A 304 9.380 -25.120 11.319 1.00151.80 C ANISOU 1657 CZ ARG A 304 17360 22749 17569 1123 5621 -4446 C ATOM 1658 NH1 ARG A 304 8.484 -25.979 10.853 1.00151.83 N ANISOU 1658 NH1 ARG A 304 17697 22570 17422 1236 5549 -4523 N ATOM 1659 NH2 ARG A 304 10.269 -24.582 10.495 1.00155.33 N ANISOU 1659 NH2 ARG A 304 17716 23388 17915 1031 5903 -4475 N ATOM 1660 N ARG A 305 7.084 -23.009 17.321 1.00 89.37 N ANISOU 1660 N ARG A 305 8906 14585 10468 777 4310 -3876 N ATOM 1661 CA ARG A 305 6.739 -23.644 18.587 1.00 86.91 C ANISOU 1661 CA ARG A 305 8511 14159 10352 948 4072 -3838 C ATOM 1662 C ARG A 305 5.435 -23.069 19.134 1.00 82.31 C ANISOU 1662 C ARG A 305 8097 13454 9722 788 3825 -3720 C ATOM 1663 O ARG A 305 4.527 -23.809 19.519 1.00 80.15 O ANISOU 1663 O ARG A 305 7982 13004 9468 903 3664 -3708 O ATOM 1664 CB ARG A 305 7.874 -23.427 19.589 1.00 88.13 C ANISOU 1664 CB ARG A 305 8274 14467 10743 1012 4052 -3823 C ATOM 1665 CG ARG A 305 7.745 -24.192 20.892 1.00 86.52 C ANISOU 1665 CG ARG A 305 7958 14170 10745 1229 3833 -3788 C ATOM 1666 CD ARG A 305 8.935 -23.900 21.795 1.00 88.23 C ANISOU 1666 CD ARG A 305 7783 14570 11169 1275 3814 -3779 C ATOM 1667 NE ARG A 305 10.204 -24.215 21.142 1.00 92.99 N ANISOU 1667 NE ARG A 305 8186 15325 11821 1389 4070 -3883 N ATOM 1668 CZ ARG A 305 11.390 -23.786 21.561 1.00 95.52 C ANISOU 1668 CZ ARG A 305 8151 15854 12288 1377 4125 -3899 C ATOM 1669 NH1 ARG A 305 11.477 -23.013 22.636 1.00 93.72 N ANISOU 1669 NH1 ARG A 305 7743 15706 12162 1249 3934 -3826 N ATOM 1670 NH2 ARG A 305 12.491 -24.124 20.903 1.00100.07 N ANISOU 1670 NH2 ARG A 305 8549 16564 12908 1491 4375 -3995 N ATOM 1671 N GLY A 306 5.347 -21.742 19.147 1.00 81.06 N ANISOU 1671 N GLY A 306 7909 13387 9505 521 3808 -3635 N ATOM 1672 CA GLY A 306 4.162 -21.054 19.623 1.00 77.05 C ANISOU 1672 CA GLY A 306 7552 12778 8945 360 3600 -3520 C ATOM 1673 C GLY A 306 2.930 -21.336 18.785 1.00 75.81 C ANISOU 1673 C GLY A 306 7749 12473 8583 322 3573 -3521 C ATOM 1674 O GLY A 306 1.825 -21.450 19.314 1.00 72.67 O ANISOU 1674 O GLY A 306 7481 11938 8194 324 3372 -3459 O ATOM 1675 N VAL A 307 3.119 -21.445 17.473 1.00 85.65 N ANISOU 1675 N VAL A 307 9150 13755 9637 286 3774 -3594 N ATOM 1676 CA VAL A 307 2.020 -21.739 16.560 1.00 85.46 C ANISOU 1676 CA VAL A 307 9472 13608 9389 247 3750 -3613 C ATOM 1677 C VAL A 307 1.460 -23.135 16.817 1.00 85.38 C ANISOU 1677 C VAL A 307 9575 13427 9438 477 3642 -3692 C ATOM 1678 O VAL A 307 0.247 -23.310 16.966 1.00 82.42 O ANISOU 1678 O VAL A 307 9398 12910 9008 446 3466 -3658 O ATOM 1679 CB VAL A 307 2.458 -21.626 15.086 1.00 89.43 C ANISOU 1679 CB VAL A 307 10123 14199 9658 180 3999 -3689 C ATOM 1680 CG1 VAL A 307 1.361 -22.130 14.161 1.00 89.72 C ANISOU 1680 CG1 VAL A 307 10522 14108 9460 180 3954 -3736 C ATOM 1681 CG2 VAL A 307 2.823 -20.190 14.750 1.00 89.93 C ANISOU 1681 CG2 VAL A 307 10139 14400 9630 -80 4103 -3594 C ATOM 1682 N LEU A 308 2.351 -24.122 16.873 1.00 87.28 N ANISOU 1682 N LEU A 308 9690 13677 9796 706 3752 -3798 N ATOM 1683 CA LEU A 308 1.948 -25.499 17.148 1.00 87.52 C ANISOU 1683 CA LEU A 308 9824 13527 9900 941 3672 -3877 C ATOM 1684 C LEU A 308 1.264 -25.623 18.508 1.00 84.32 C ANISOU 1684 C LEU A 308 9347 13009 9682 986 3419 -3779 C ATOM 1685 O LEU A 308 0.219 -26.269 18.628 1.00 83.00 O ANISOU 1685 O LEU A 308 9377 12662 9496 1033 3280 -3790 O ATOM 1686 CB LEU A 308 3.147 -26.449 17.063 1.00 90.77 C ANISOU 1686 CB LEU A 308 10091 13974 10423 1194 3852 -3995 C ATOM 1687 CG LEU A 308 3.456 -27.068 15.695 1.00 94.56 C ANISOU 1687 CG LEU A 308 10766 14453 10710 1265 4078 -4146 C ATOM 1688 CD1 LEU A 308 3.896 -26.017 14.686 1.00 96.37 C ANISOU 1688 CD1 LEU A 308 10993 14872 10749 1057 4267 -4137 C ATOM 1689 CD2 LEU A 308 4.505 -28.164 15.824 1.00 98.21 C ANISOU 1689 CD2 LEU A 308 11093 14902 11321 1567 4222 -4257 C ATOM 1690 N VAL A 309 1.853 -24.998 19.525 1.00 90.73 N ANISOU 1690 N VAL A 309 9879 13929 10664 965 3359 -3688 N ATOM 1691 CA VAL A 309 1.270 -24.999 20.865 1.00 87.49 C ANISOU 1691 CA VAL A 309 9393 13435 10414 1000 3124 -3585 C ATOM 1692 C VAL A 309 -0.130 -24.388 20.868 1.00 83.68 C ANISOU 1692 C VAL A 309 9116 12863 9817 810 2966 -3499 C ATOM 1693 O VAL A 309 -1.062 -24.954 21.442 1.00 81.65 O ANISOU 1693 O VAL A 309 8964 12447 9612 881 2805 -3473 O ATOM 1694 CB VAL A 309 2.162 -24.244 21.877 1.00 88.35 C ANISOU 1694 CB VAL A 309 9182 13702 10686 972 3083 -3509 C ATOM 1695 CG1 VAL A 309 1.379 -23.897 23.136 1.00 84.30 C ANISOU 1695 CG1 VAL A 309 8642 13120 10269 934 2838 -3385 C ATOM 1696 CG2 VAL A 309 3.387 -25.070 22.221 1.00 91.60 C ANISOU 1696 CG2 VAL A 309 9367 14172 11265 1216 3172 -3579 C ATOM 1697 N LEU A 310 -0.272 -23.240 20.213 1.00 68.40 N ANISOU 1697 N LEU A 310 7237 11025 7725 574 3021 -3454 N ATOM 1698 CA LEU A 310 -1.548 -22.535 20.168 1.00 65.53 C ANISOU 1698 CA LEU A 310 7056 10596 7247 391 2883 -3362 C ATOM 1699 C LEU A 310 -2.626 -23.351 19.461 1.00 65.43 C ANISOU 1699 C LEU A 310 7334 10428 7099 424 2837 -3429 C ATOM 1700 O LEU A 310 -3.737 -23.498 19.975 1.00 62.91 O ANISOU 1700 O LEU A 310 7111 9987 6806 411 2659 -3379 O ATOM 1701 CB LEU A 310 -1.391 -21.174 19.488 1.00 65.88 C ANISOU 1701 CB LEU A 310 7126 10770 7138 145 2980 -3301 C ATOM 1702 CG LEU A 310 -2.636 -20.286 19.491 1.00 63.12 C ANISOU 1702 CG LEU A 310 6945 10364 6675 -42 2844 -3187 C ATOM 1703 CD1 LEU A 310 -2.994 -19.855 20.905 1.00 60.06 C ANISOU 1703 CD1 LEU A 310 6411 9946 6464 -45 2660 -3079 C ATOM 1704 CD2 LEU A 310 -2.436 -19.080 18.592 1.00 64.26 C ANISOU 1704 CD2 LEU A 310 7170 10614 6632 -266 2973 -3136 C ATOM 1705 N ARG A 311 -2.297 -23.876 18.283 1.00109.37 N ANISOU 1705 N ARG A 311 13038 16001 12516 462 2997 -3550 N ATOM 1706 CA ARG A 311 -3.232 -24.717 17.539 1.00109.88 C ANISOU 1706 CA ARG A 311 13390 15918 12439 494 2954 -3644 C ATOM 1707 C ARG A 311 -3.639 -25.937 18.359 1.00108.23 C ANISOU 1707 C ARG A 311 13185 15530 12408 689 2827 -3688 C ATOM 1708 O ARG A 311 -4.811 -26.329 18.372 1.00107.07 O ANISOU 1708 O ARG A 311 13220 15238 12223 657 2679 -3697 O ATOM 1709 CB ARG A 311 -2.633 -25.150 16.198 1.00113.08 C ANISOU 1709 CB ARG A 311 13934 16368 12662 534 3162 -3783 C ATOM 1710 CG ARG A 311 -2.647 -24.064 15.132 1.00114.89 C ANISOU 1710 CG ARG A 311 14301 16719 12633 317 3255 -3747 C ATOM 1711 CD ARG A 311 -2.200 -24.604 13.782 1.00119.73 C ANISOU 1711 CD ARG A 311 15091 17361 13040 371 3450 -3895 C ATOM 1712 NE ARG A 311 -0.768 -24.889 13.747 1.00123.12 N ANISOU 1712 NE ARG A 311 15308 17908 13564 495 3675 -3956 N ATOM 1713 CZ ARG A 311 -0.147 -25.468 12.725 1.00127.01 C ANISOU 1713 CZ ARG A 311 15895 18436 13926 593 3879 -4095 C ATOM 1714 NH1 ARG A 311 -0.833 -25.834 11.651 1.00129.26 N ANISOU 1714 NH1 ARG A 311 16500 18643 13968 579 3876 -4195 N ATOM 1715 NH2 ARG A 311 1.160 -25.687 12.778 1.00129.08 N ANISOU 1715 NH2 ARG A 311 15932 18816 14296 709 4084 -4142 N ATOM 1716 N ALA A 312 -2.664 -26.524 19.050 1.00 70.18 N ANISOU 1716 N ALA A 312 8162 10719 7784 887 2885 -3710 N ATOM 1717 CA ALA A 312 -2.924 -27.656 19.932 1.00 69.61 C ANISOU 1717 CA ALA A 312 8082 10472 7895 1090 2778 -3731 C ATOM 1718 C ALA A 312 -3.911 -27.276 21.032 1.00 65.89 C ANISOU 1718 C ALA A 312 7576 9932 7525 1019 2558 -3599 C ATOM 1719 O ALA A 312 -4.824 -28.038 21.346 1.00 64.90 O ANISOU 1719 O ALA A 312 7588 9626 7446 1074 2438 -3618 O ATOM 1720 CB ALA A 312 -1.626 -28.169 20.535 1.00 71.55 C ANISOU 1720 CB ALA A 312 8091 10768 8328 1312 2874 -3749 C ATOM 1721 N MET A 313 -3.725 -26.092 21.608 1.00 77.15 N ANISOU 1721 N MET A 313 8826 11502 8987 893 2513 -3470 N ATOM 1722 CA MET A 313 -4.607 -25.610 22.664 1.00 73.85 C ANISOU 1722 CA MET A 313 8369 11038 8652 824 2321 -3341 C ATOM 1723 C MET A 313 -6.022 -25.368 22.149 1.00 72.36 C ANISOU 1723 C MET A 313 8412 10765 8318 662 2224 -3333 C ATOM 1724 O MET A 313 -7.000 -25.634 22.850 1.00 70.94 O ANISOU 1724 O MET A 313 8277 10464 8215 675 2072 -3287 O ATOM 1725 CB MET A 313 -4.051 -24.332 23.299 1.00 75.86 C ANISOU 1725 CB MET A 313 8408 11462 8952 711 2307 -3223 C ATOM 1726 CG MET A 313 -2.815 -24.551 24.159 1.00 77.22 C ANISOU 1726 CG MET A 313 8322 11717 9302 869 2336 -3214 C ATOM 1727 SD MET A 313 -2.352 -23.092 25.114 1.00 75.52 S ANISOU 1727 SD MET A 313 7876 11667 9150 722 2264 -3085 S ATOM 1728 CE MET A 313 -2.006 -21.919 23.806 1.00 76.27 C ANISOU 1728 CE MET A 313 8018 11907 9053 475 2435 -3109 C ATOM 1729 N VAL A 314 -6.126 -24.866 20.923 1.00 59.13 N ANISOU 1729 N VAL A 314 6882 9158 6428 512 2311 -3375 N ATOM 1730 CA VAL A 314 -7.428 -24.604 20.320 1.00 58.06 C ANISOU 1730 CA VAL A 314 6972 8962 6128 355 2211 -3369 C ATOM 1731 C VAL A 314 -8.183 -25.901 20.041 1.00 58.87 C ANISOU 1731 C VAL A 314 7269 8875 6224 441 2143 -3494 C ATOM 1732 O VAL A 314 -9.340 -26.053 20.448 1.00 57.09 O ANISOU 1732 O VAL A 314 7126 8540 6026 390 1983 -3470 O ATOM 1733 CB VAL A 314 -7.303 -23.783 19.022 1.00 59.55 C ANISOU 1733 CB VAL A 314 7294 9270 6063 183 2318 -3377 C ATOM 1734 CG1 VAL A 314 -8.659 -23.649 18.346 1.00 58.90 C ANISOU 1734 CG1 VAL A 314 7461 9123 5796 42 2191 -3378 C ATOM 1735 CG2 VAL A 314 -6.715 -22.413 19.318 1.00 58.72 C ANISOU 1735 CG2 VAL A 314 7021 9324 5965 62 2375 -3248 C ATOM 1736 N ILE A 315 -7.528 -26.837 19.357 1.00 63.73 N ANISOU 1736 N ILE A 315 7961 9445 6808 569 2269 -3635 N ATOM 1737 CA ILE A 315 -8.165 -28.116 19.051 1.00 64.95 C ANISOU 1737 CA ILE A 315 8323 9399 6957 649 2215 -3772 C ATOM 1738 C ILE A 315 -8.504 -28.896 20.324 1.00 63.48 C ANISOU 1738 C ILE A 315 8053 9047 7019 791 2101 -3742 C ATOM 1739 O ILE A 315 -9.540 -29.562 20.396 1.00 63.06 O ANISOU 1739 O ILE A 315 8153 8817 6988 768 1977 -3794 O ATOM 1740 CB ILE A 315 -7.326 -28.980 18.068 1.00 68.71 C ANISOU 1740 CB ILE A 315 8915 9852 7342 773 2390 -3938 C ATOM 1741 CG1 ILE A 315 -5.955 -29.327 18.655 1.00 69.97 C ANISOU 1741 CG1 ILE A 315 8849 10061 7678 986 2532 -3934 C ATOM 1742 CG2 ILE A 315 -7.167 -28.265 16.734 1.00 70.38 C ANISOU 1742 CG2 ILE A 315 9256 10210 7278 623 2493 -3971 C ATOM 1743 CD1 ILE A 315 -5.858 -30.734 19.216 1.00 71.10 C ANISOU 1743 CD1 ILE A 315 9022 9995 7998 1219 2520 -4014 C ATOM 1744 N ALA A 316 -7.638 -28.794 21.329 1.00 60.92 N ANISOU 1744 N ALA A 316 7489 8781 6877 928 2138 -3655 N ATOM 1745 CA ALA A 316 -7.890 -29.437 22.613 1.00 59.60 C ANISOU 1745 CA ALA A 316 7239 8473 6934 1072 2031 -3597 C ATOM 1746 C ALA A 316 -9.108 -28.818 23.283 1.00 56.45 C ANISOU 1746 C ALA A 316 6836 8049 6562 929 1858 -3487 C ATOM 1747 O ALA A 316 -9.946 -29.526 23.836 1.00 55.73 O ANISOU 1747 O ALA A 316 6824 7776 6577 970 1750 -3496 O ATOM 1748 CB ALA A 316 -6.675 -29.330 23.518 1.00 59.82 C ANISOU 1748 CB ALA A 316 7009 8600 7119 1236 2088 -3514 C ATOM 1749 N PHE A 317 -9.202 -27.493 23.226 1.00 58.01 N ANISOU 1749 N PHE A 317 6951 8422 6670 761 1841 -3385 N ATOM 1750 CA PHE A 317 -10.330 -26.783 23.817 1.00 55.21 C ANISOU 1750 CA PHE A 317 6588 8063 6328 629 1693 -3278 C ATOM 1751 C PHE A 317 -11.633 -27.213 23.156 1.00 55.34 C ANISOU 1751 C PHE A 317 6832 7945 6249 516 1597 -3368 C ATOM 1752 O PHE A 317 -12.604 -27.540 23.839 1.00 53.96 O ANISOU 1752 O PHE A 317 6675 7643 6184 511 1472 -3346 O ATOM 1753 CB PHE A 317 -10.146 -25.269 23.686 1.00 53.97 C ANISOU 1753 CB PHE A 317 6341 8102 6063 465 1713 -3167 C ATOM 1754 CG PHE A 317 -11.062 -24.465 24.570 1.00 51.12 C ANISOU 1754 CG PHE A 317 5920 7750 5755 377 1580 -3035 C ATOM 1755 CD1 PHE A 317 -12.370 -24.212 24.192 1.00 50.20 C ANISOU 1755 CD1 PHE A 317 5948 7588 5538 235 1479 -3038 C ATOM 1756 CD2 PHE A 317 -10.612 -23.964 25.780 1.00 49.63 C ANISOU 1756 CD2 PHE A 317 5532 7617 5708 440 1551 -2912 C ATOM 1757 CE1 PHE A 317 -13.212 -23.472 25.001 1.00 47.82 C ANISOU 1757 CE1 PHE A 317 5586 7297 5288 170 1372 -2923 C ATOM 1758 CE2 PHE A 317 -11.449 -23.224 26.595 1.00 47.22 C ANISOU 1758 CE2 PHE A 317 5184 7315 5444 371 1443 -2794 C ATOM 1759 CZ PHE A 317 -12.751 -22.979 26.204 1.00 46.32 C ANISOU 1759 CZ PHE A 317 5206 7155 5240 243 1365 -2800 C ATOM 1760 N VAL A 318 -11.647 -27.221 21.826 1.00 54.01 N ANISOU 1760 N VAL A 318 6838 7809 5875 419 1653 -3471 N ATOM 1761 CA VAL A 318 -12.837 -27.623 21.082 1.00 54.59 C ANISOU 1761 CA VAL A 318 7141 7771 5830 291 1539 -3565 C ATOM 1762 C VAL A 318 -13.246 -29.061 21.401 1.00 55.58 C ANISOU 1762 C VAL A 318 7362 7650 6105 400 1484 -3680 C ATOM 1763 O VAL A 318 -14.381 -29.313 21.812 1.00 54.52 O ANISOU 1763 O VAL A 318 7278 7389 6049 325 1335 -3682 O ATOM 1764 CB VAL A 318 -12.635 -27.476 19.561 1.00 56.98 C ANISOU 1764 CB VAL A 318 7633 8152 5863 191 1610 -3657 C ATOM 1765 CG1 VAL A 318 -13.844 -28.015 18.812 1.00 57.99 C ANISOU 1765 CG1 VAL A 318 8007 8157 5870 64 1461 -3764 C ATOM 1766 CG2 VAL A 318 -12.384 -26.021 19.199 1.00 56.16 C ANISOU 1766 CG2 VAL A 318 7473 8263 5604 58 1656 -3533 C ATOM 1767 N VAL A 319 -12.312 -29.993 21.223 1.00 57.80 N ANISOU 1767 N VAL A 319 7670 7857 6436 575 1609 -3775 N ATOM 1768 CA VAL A 319 -12.582 -31.412 21.449 1.00 59.29 C ANISOU 1768 CA VAL A 319 7983 7785 6759 692 1581 -3889 C ATOM 1769 C VAL A 319 -13.045 -31.713 22.876 1.00 57.35 C ANISOU 1769 C VAL A 319 7620 7404 6767 778 1488 -3792 C ATOM 1770 O VAL A 319 -14.018 -32.439 23.080 1.00 57.51 O ANISOU 1770 O VAL A 319 7764 7209 6881 734 1382 -3848 O ATOM 1771 CB VAL A 319 -11.351 -32.283 21.109 1.00 62.15 C ANISOU 1771 CB VAL A 319 8374 8105 7137 903 1752 -3988 C ATOM 1772 CG1 VAL A 319 -11.548 -33.712 21.594 1.00 63.56 C ANISOU 1772 CG1 VAL A 319 8662 7993 7494 1059 1730 -4070 C ATOM 1773 CG2 VAL A 319 -11.081 -32.256 19.612 1.00 64.68 C ANISOU 1773 CG2 VAL A 319 8874 8500 7202 824 1841 -4121 C ATOM 1774 N CYS A 320 -12.353 -31.144 23.859 1.00 55.72 N ANISOU 1774 N CYS A 320 7181 7320 6670 887 1525 -3644 N ATOM 1775 CA CYS A 320 -12.670 -31.403 25.262 1.00 54.09 C ANISOU 1775 CA CYS A 320 6863 7002 6686 994 1447 -3533 C ATOM 1776 C CYS A 320 -13.971 -30.741 25.713 1.00 51.60 C ANISOU 1776 C CYS A 320 6529 6683 6395 822 1304 -3459 C ATOM 1777 O CYS A 320 -14.746 -31.334 26.464 1.00 51.09 O ANISOU 1777 O CYS A 320 6494 6423 6496 849 1222 -3443 O ATOM 1778 CB CYS A 320 -11.518 -30.963 26.170 1.00 53.38 C ANISOU 1778 CB CYS A 320 6538 7061 6682 1156 1509 -3394 C ATOM 1779 SG CYS A 320 -9.983 -31.886 25.930 1.00 56.54 S ANISOU 1779 SG CYS A 320 6917 7448 7119 1404 1670 -3467 S ATOM 1780 N TRP A 321 -14.211 -29.516 25.256 1.00 64.30 N ANISOU 1780 N TRP A 321 8093 8493 7843 649 1282 -3411 N ATOM 1781 CA TRP A 321 -15.387 -28.770 25.694 1.00 63.35 C ANISOU 1781 CA TRP A 321 7936 8393 7739 500 1155 -3334 C ATOM 1782 C TRP A 321 -16.624 -29.012 24.831 1.00 64.07 C ANISOU 1782 C TRP A 321 8217 8387 7740 301 1036 -3444 C ATOM 1783 O TRP A 321 -17.697 -28.477 25.116 1.00 63.80 O ANISOU 1783 O TRP A 321 8161 8343 7735 164 880 -3272 O ATOM 1784 CB TRP A 321 -15.082 -27.272 25.785 1.00 62.82 C ANISOU 1784 CB TRP A 321 7728 8577 7562 421 1177 -3200 C ATOM 1785 CG TRP A 321 -14.128 -26.930 26.888 1.00 61.15 C ANISOU 1785 CG TRP A 321 7312 8448 7472 575 1231 -3064 C ATOM 1786 CD1 TRP A 321 -12.774 -26.789 26.790 1.00 61.41 C ANISOU 1786 CD1 TRP A 321 7249 8599 7484 667 1341 -3045 C ATOM 1787 CD2 TRP A 321 -14.456 -26.695 28.263 1.00 59.86 C ANISOU 1787 CD2 TRP A 321 7018 8258 7468 646 1166 -2930 C ATOM 1788 NE1 TRP A 321 -12.239 -26.477 28.016 1.00 60.42 N ANISOU 1788 NE1 TRP A 321 6943 8524 7487 778 1325 -2910 N ATOM 1789 CE2 TRP A 321 -13.251 -26.413 28.938 1.00 59.35 C ANISOU 1789 CE2 TRP A 321 6794 8302 7452 772 1220 -2831 C ATOM 1790 CE3 TRP A 321 -15.652 -26.694 28.988 1.00 59.82 C ANISOU 1790 CE3 TRP A 321 7025 8135 7567 599 1045 -2827 C ATOM 1791 CZ2 TRP A 321 -13.208 -26.133 30.301 1.00 59.24 C ANISOU 1791 CZ2 TRP A 321 6647 8298 7561 863 1165 -2684 C ATOM 1792 CZ3 TRP A 321 -15.607 -26.416 30.342 1.00 59.53 C ANISOU 1792 CZ3 TRP A 321 6856 8102 7660 697 1013 -2661 C ATOM 1793 CH2 TRP A 321 -14.393 -26.139 30.984 1.00 59.32 C ANISOU 1793 CH2 TRP A 321 6678 8203 7655 839 1082 -2630 C ATOM 1794 N LEU A 322 -16.481 -29.817 23.782 1.00 51.26 N ANISOU 1794 N LEU A 322 6780 6680 6015 278 1062 -3598 N ATOM 1795 CA LEU A 322 -17.628 -30.146 22.934 1.00 52.40 C ANISOU 1795 CA LEU A 322 7116 6728 6068 78 920 -3708 C ATOM 1796 C LEU A 322 -18.700 -31.007 23.626 1.00 51.74 C ANISOU 1796 C LEU A 322 7066 6382 6212 38 777 -3661 C ATOM 1797 O LEU A 322 -19.868 -30.621 23.645 1.00 50.13 O ANISOU 1797 O LEU A 322 6853 6174 6020 -138 599 -3533 O ATOM 1798 CB LEU A 322 -17.191 -30.764 21.597 1.00 55.37 C ANISOU 1798 CB LEU A 322 7701 7082 6255 60 977 -3859 C ATOM 1799 CG LEU A 322 -18.324 -31.145 20.642 1.00 57.01 C ANISOU 1799 CG LEU A 322 8119 7198 6343 -153 806 -3972 C ATOM 1800 CD1 LEU A 322 -19.190 -29.936 20.322 1.00 55.60 C ANISOU 1800 CD1 LEU A 322 7906 7205 6013 -355 657 -3874 C ATOM 1801 CD2 LEU A 322 -17.768 -31.761 19.368 1.00 60.15 C ANISOU 1801 CD2 LEU A 322 8734 7577 6543 -137 880 -4123 C ATOM 1802 N PRO A 323 -18.318 -32.168 24.201 1.00 53.09 N ANISOU 1802 N PRO A 323 7271 6328 6573 203 852 -3736 N ATOM 1803 CA PRO A 323 -19.365 -32.982 24.833 1.00 52.55 C ANISOU 1803 CA PRO A 323 7250 5996 6722 139 726 -3655 C ATOM 1804 C PRO A 323 -19.942 -32.319 26.082 1.00 48.79 C ANISOU 1804 C PRO A 323 6582 5558 6400 134 648 -3363 C ATOM 1805 O PRO A 323 -21.053 -32.647 26.499 1.00 47.93 O ANISOU 1805 O PRO A 323 6480 5299 6431 10 524 -3257 O ATOM 1806 CB PRO A 323 -18.625 -34.268 25.224 1.00 55.00 C ANISOU 1806 CB PRO A 323 7644 6064 7189 358 856 -3779 C ATOM 1807 CG PRO A 323 -17.379 -34.272 24.402 1.00 56.96 C ANISOU 1807 CG PRO A 323 7934 6449 7259 488 1007 -3913 C ATOM 1808 CD PRO A 323 -17.006 -32.835 24.272 1.00 54.90 C ANISOU 1808 CD PRO A 323 7507 6519 6833 445 1029 -3813 C ATOM 1809 N TYR A 324 -19.183 -31.398 26.666 1.00 66.50 N ANISOU 1809 N TYR A 324 8653 8001 8613 260 729 -3245 N ATOM 1810 CA TYR A 324 -19.612 -30.679 27.858 1.00 65.85 C ANISOU 1810 CA TYR A 324 8400 7974 8646 269 675 -2985 C ATOM 1811 C TYR A 324 -20.842 -29.818 27.580 1.00 66.12 C ANISOU 1811 C TYR A 324 8404 8098 8622 43 519 -2860 C ATOM 1812 O TYR A 324 -21.844 -29.902 28.291 1.00 66.53 O ANISOU 1812 O TYR A 324 8405 8047 8827 -26 425 -2704 O ATOM 1813 CB TYR A 324 -18.466 -29.812 28.384 1.00 64.31 C ANISOU 1813 CB TYR A 324 8042 7994 8399 427 788 -2924 C ATOM 1814 CG TYR A 324 -18.847 -28.885 29.516 1.00 63.44 C ANISOU 1814 CG TYR A 324 7771 7971 8361 426 736 -2677 C ATOM 1815 CD1 TYR A 324 -18.985 -29.361 30.813 1.00 64.61 C ANISOU 1815 CD1 TYR A 324 7868 7985 8696 548 733 -2537 C ATOM 1816 CD2 TYR A 324 -19.053 -27.530 29.290 1.00 62.45 C ANISOU 1816 CD2 TYR A 324 7567 8056 8107 310 700 -2586 C ATOM 1817 CE1 TYR A 324 -19.328 -28.514 31.852 1.00 64.34 C ANISOU 1817 CE1 TYR A 324 7705 8034 8707 550 699 -2326 C ATOM 1818 CE2 TYR A 324 -19.394 -26.676 30.322 1.00 62.05 C ANISOU 1818 CE2 TYR A 324 7387 8072 8119 317 665 -2378 C ATOM 1819 CZ TYR A 324 -19.531 -27.174 31.601 1.00 62.99 C ANISOU 1819 CZ TYR A 324 7454 8066 8414 435 666 -2256 C ATOM 1820 OH TYR A 324 -19.872 -26.328 32.632 1.00 62.59 O ANISOU 1820 OH TYR A 324 7292 8083 8408 444 642 -2063 O ATOM 1821 N HIS A 325 -20.760 -28.996 26.539 1.00 50.57 N ANISOU 1821 N HIS A 325 6464 6319 6431 -65 497 -2924 N ATOM 1822 CA HIS A 325 -21.845 -28.081 26.197 1.00 50.57 C ANISOU 1822 CA HIS A 325 6432 6426 6357 -250 342 -2798 C ATOM 1823 C HIS A 325 -23.051 -28.794 25.590 1.00 52.15 C ANISOU 1823 C HIS A 325 6738 6487 6591 -431 176 -2859 C ATOM 1824 O HIS A 325 -24.177 -28.305 25.684 1.00 52.80 O ANISOU 1824 O HIS A 325 6747 6601 6715 -561 25 -2718 O ATOM 1825 CB HIS A 325 -21.349 -26.975 25.262 1.00 49.83 C ANISOU 1825 CB HIS A 325 6362 6570 6001 -300 373 -2832 C ATOM 1826 CG HIS A 325 -20.470 -25.968 25.935 1.00 48.17 C ANISOU 1826 CG HIS A 325 6009 6519 5775 -189 494 -2719 C ATOM 1827 ND1 HIS A 325 -19.161 -25.751 25.562 1.00 48.10 N ANISOU 1827 ND1 HIS A 325 6002 6643 5632 -109 659 -2835 N ATOM 1828 CD2 HIS A 325 -20.710 -25.126 26.968 1.00 47.39 C ANISOU 1828 CD2 HIS A 325 5760 6468 5780 -154 476 -2512 C ATOM 1829 CE1 HIS A 325 -18.635 -24.815 26.331 1.00 46.35 C ANISOU 1829 CE1 HIS A 325 5630 6543 5438 -44 725 -2705 C ATOM 1830 NE2 HIS A 325 -19.555 -24.419 27.193 1.00 45.44 N ANISOU 1830 NE2 HIS A 325 5434 6373 5457 -67 614 -2512 N ATOM 1831 N VAL A 326 -22.813 -29.943 24.966 1.00 49.73 N ANISOU 1831 N VAL A 326 6597 6027 6271 -438 202 -3077 N ATOM 1832 CA VAL A 326 -23.900 -30.744 24.412 1.00 51.76 C ANISOU 1832 CA VAL A 326 6965 6129 6575 -624 43 -3166 C ATOM 1833 C VAL A 326 -24.757 -31.314 25.539 1.00 51.36 C ANISOU 1833 C VAL A 326 6820 5880 6817 -647 -5 -3017 C ATOM 1834 O VAL A 326 -25.985 -31.353 25.443 1.00 52.58 O ANISOU 1834 O VAL A 326 6936 5993 7049 -832 -170 -2958 O ATOM 1835 CB VAL A 326 -23.369 -31.891 23.525 1.00 54.57 C ANISOU 1835 CB VAL A 326 7546 6338 6851 -617 105 -3458 C ATOM 1836 CG1 VAL A 326 -24.499 -32.820 23.109 1.00 56.88 C ANISOU 1836 CG1 VAL A 326 7953 6435 7225 -822 -62 -3558 C ATOM 1837 CG2 VAL A 326 -22.665 -31.330 22.300 1.00 55.37 C ANISOU 1837 CG2 VAL A 326 7755 6645 6638 -623 158 -3610 C ATOM 1838 N ARG A 327 -24.098 -31.737 26.613 1.00 49.83 N ANISOU 1838 N ARG A 327 6581 5574 6779 -457 141 -2949 N ATOM 1839 CA ARG A 327 -24.781 -32.311 27.768 1.00 49.61 C ANISOU 1839 CA ARG A 327 6488 5349 7015 -457 133 -2794 C ATOM 1840 C ARG A 327 -25.707 -31.310 28.455 1.00 47.65 C ANISOU 1840 C ARG A 327 6042 5229 6834 -532 50 -2544 C ATOM 1841 O ARG A 327 -26.836 -31.642 28.817 1.00 48.25 O ANISOU 1841 O ARG A 327 6066 5191 7077 -671 -36 -2452 O ATOM 1842 CB ARG A 327 -23.761 -32.842 28.776 1.00 49.19 C ANISOU 1842 CB ARG A 327 6440 5180 7073 -206 303 -2758 C ATOM 1843 CG ARG A 327 -24.381 -33.284 30.087 1.00 48.84 C ANISOU 1843 CG ARG A 327 6335 4955 7268 -187 316 -2558 C ATOM 1844 CD ARG A 327 -23.333 -33.746 31.077 1.00 48.60 C ANISOU 1844 CD ARG A 327 6319 4830 7317 80 462 -2507 C ATOM 1845 NE ARG A 327 -22.331 -32.719 31.346 1.00 46.60 N ANISOU 1845 NE ARG A 327 5940 4834 6933 247 528 -2459 N ATOM 1846 CZ ARG A 327 -22.505 -31.709 32.191 1.00 44.37 C ANISOU 1846 CZ ARG A 327 5497 4713 6649 269 519 -2257 C ATOM 1847 NH1 ARG A 327 -23.649 -31.581 32.849 1.00 43.82 N ANISOU 1847 NH1 ARG A 327 5366 4586 6700 151 460 -2080 N ATOM 1848 NH2 ARG A 327 -21.537 -30.824 32.375 1.00 42.91 N ANISOU 1848 NH2 ARG A 327 5211 4747 6346 403 577 -2242 N ATOM 1849 N ARG A 328 -25.219 -30.088 28.637 1.00 52.99 N ANISOU 1849 N ARG A 328 6607 6137 7389 -443 87 -2442 N ATOM 1850 CA ARG A 328 -25.989 -29.046 29.306 1.00 52.81 C ANISOU 1850 CA ARG A 328 6409 6237 7419 -483 29 -2214 C ATOM 1851 C ARG A 328 -27.208 -28.649 28.480 1.00 53.49 C ANISOU 1851 C ARG A 328 6461 6395 7466 -697 -160 -2204 C ATOM 1852 O ARG A 328 -28.257 -28.308 29.026 1.00 53.79 O ANISOU 1852 O ARG A 328 6359 6437 7641 -772 -233 -2039 O ATOM 1853 CB ARG A 328 -25.100 -27.835 29.592 1.00 50.43 C ANISOU 1853 CB ARG A 328 6027 6148 6984 -346 114 -2136 C ATOM 1854 CG ARG A 328 -23.868 -28.184 30.411 1.00 49.38 C ANISOU 1854 CG ARG A 328 5898 5973 6888 -132 276 -2150 C ATOM 1855 CD ARG A 328 -22.845 -27.062 30.426 1.00 47.18 C ANISOU 1855 CD ARG A 328 5556 5916 6454 -31 356 -2140 C ATOM 1856 NE ARG A 328 -23.266 -25.929 31.243 1.00 46.63 N ANISOU 1856 NE ARG A 328 5350 5959 6406 -27 341 -1938 N ATOM 1857 CZ ARG A 328 -23.700 -24.774 30.752 1.00 46.84 C ANISOU 1857 CZ ARG A 328 5338 6138 6320 -125 275 -1875 C ATOM 1858 NH1 ARG A 328 -23.769 -24.592 29.440 1.00 47.33 N ANISOU 1858 NH1 ARG A 328 5488 6271 6222 -239 211 -1987 N ATOM 1859 NH2 ARG A 328 -24.061 -23.797 31.573 1.00 46.68 N ANISOU 1859 NH2 ARG A 328 5208 6191 6337 -102 277 -1699 N ATOM 1860 N LEU A 329 -27.064 -28.701 27.160 1.00 39.00 N ANISOU 1860 N LEU A 329 4752 4626 5439 -788 -239 -2382 N ATOM 1861 CA LEU A 329 -28.184 -28.473 26.257 1.00 40.73 C ANISOU 1861 CA LEU A 329 4961 4913 5599 -990 -449 -2399 C ATOM 1862 C LEU A 329 -29.110 -29.685 26.266 1.00 43.19 C ANISOU 1862 C LEU A 329 5296 5012 6102 -1147 -542 -2468 C ATOM 1863 O LEU A 329 -30.327 -29.553 26.138 1.00 44.17 O ANISOU 1863 O LEU A 329 5307 5162 6314 -1308 -709 -2396 O ATOM 1864 CB LEU A 329 -27.683 -28.198 24.838 1.00 42.67 C ANISOU 1864 CB LEU A 329 5369 5293 5550 -1037 -500 -2575 C ATOM 1865 CG LEU A 329 -27.004 -26.846 24.610 1.00 40.87 C ANISOU 1865 CG LEU A 329 5119 5294 5116 -945 -440 -2491 C ATOM 1866 CD1 LEU A 329 -26.309 -26.811 23.260 1.00 43.25 C ANISOU 1866 CD1 LEU A 329 5615 5693 5123 -976 -427 -2687 C ATOM 1867 CD2 LEU A 329 -28.020 -25.720 24.717 1.00 39.63 C ANISOU 1867 CD2 LEU A 329 4817 5274 4968 -1009 -590 -2284 C ATOM 1868 N MET A 330 -28.519 -30.865 26.420 1.00 73.30 N ANISOU 1868 N MET A 330 9251 8611 9990 -1098 -431 -2610 N ATOM 1869 CA MET A 330 -29.274 -32.109 26.514 1.00 75.21 C ANISOU 1869 CA MET A 330 9544 8602 10431 -1246 -485 -2682 C ATOM 1870 C MET A 330 -30.102 -32.129 27.794 1.00 75.55 C ANISOU 1870 C MET A 330 9402 8562 10743 -1263 -458 -2449 C ATOM 1871 O MET A 330 -31.213 -32.660 27.824 1.00 76.78 O ANISOU 1871 O MET A 330 9497 8609 11069 -1459 -563 -2433 O ATOM 1872 CB MET A 330 -28.317 -33.304 26.490 1.00 76.33 C ANISOU 1872 CB MET A 330 9896 8512 10594 -1142 -340 -2868 C ATOM 1873 CG MET A 330 -28.975 -34.654 26.715 1.00 78.16 C ANISOU 1873 CG MET A 330 10213 8432 11054 -1278 -358 -2933 C ATOM 1874 SD MET A 330 -27.767 -35.986 26.857 1.00 79.27 S ANISOU 1874 SD MET A 330 10607 8276 11237 -1091 -162 -3116 S ATOM 1875 CE MET A 330 -28.842 -37.402 27.062 1.00 82.08 C ANISOU 1875 CE MET A 330 11061 8260 11868 -1324 -218 -3167 C ATOM 1876 N PHE A 331 -29.550 -31.536 28.847 1.00 75.76 N ANISOU 1876 N PHE A 331 9337 8647 10800 -1066 -312 -2274 N ATOM 1877 CA PHE A 331 -30.194 -31.501 30.155 1.00 75.95 C ANISOU 1877 CA PHE A 331 9207 8604 11046 -1049 -249 -2046 C ATOM 1878 C PHE A 331 -31.494 -30.703 30.143 1.00 75.86 C ANISOU 1878 C PHE A 331 8984 8739 11100 -1200 -390 -1905 C ATOM 1879 O PHE A 331 -32.445 -31.041 30.849 1.00 75.91 O ANISOU 1879 O PHE A 331 8872 8644 11326 -1301 -387 -1785 O ATOM 1880 CB PHE A 331 -29.232 -30.915 31.194 1.00 74.91 C ANISOU 1880 CB PHE A 331 9038 8543 10880 -799 -82 -1910 C ATOM 1881 CG PHE A 331 -29.867 -30.644 32.530 1.00 75.22 C ANISOU 1881 CG PHE A 331 8925 8562 11093 -767 -12 -1667 C ATOM 1882 CD1 PHE A 331 -30.045 -31.666 33.447 1.00 76.63 C ANISOU 1882 CD1 PHE A 331 9153 8503 11462 -753 92 -1597 C ATOM 1883 CD2 PHE A 331 -30.273 -29.364 32.875 1.00 74.21 C ANISOU 1883 CD2 PHE A 331 8624 8643 10929 -746 -36 -1508 C ATOM 1884 CE1 PHE A 331 -30.624 -31.420 34.677 1.00 77.10 C ANISOU 1884 CE1 PHE A 331 9087 8550 11658 -726 175 -1372 C ATOM 1885 CE2 PHE A 331 -30.854 -29.113 34.104 1.00 74.66 C ANISOU 1885 CE2 PHE A 331 8552 8683 11132 -710 47 -1298 C ATOM 1886 CZ PHE A 331 -31.028 -30.142 35.006 1.00 76.00 C ANISOU 1886 CZ PHE A 331 8769 8633 11476 -703 156 -1230 C ATOM 1887 N VAL A 332 -31.534 -29.647 29.336 1.00 49.76 N ANISOU 1887 N VAL A 332 5630 5669 7607 -1209 -505 -1915 N ATOM 1888 CA VAL A 332 -32.649 -28.707 29.374 1.00 49.60 C ANISOU 1888 CA VAL A 332 5397 5812 7636 -1291 -631 -1758 C ATOM 1889 C VAL A 332 -33.631 -28.853 28.205 1.00 51.60 C ANISOU 1889 C VAL A 332 5622 6123 7863 -1515 -875 -1863 C ATOM 1890 O VAL A 332 -34.846 -28.779 28.396 1.00 52.67 O ANISOU 1890 O VAL A 332 5561 6284 8167 -1643 -983 -1761 O ATOM 1891 CB VAL A 332 -32.144 -27.244 29.480 1.00 47.06 C ANISOU 1891 CB VAL A 332 5020 5714 7147 -1131 -597 -1642 C ATOM 1892 CG1 VAL A 332 -31.175 -26.918 28.350 1.00 46.66 C ANISOU 1892 CG1 VAL A 332 5145 5770 6816 -1093 -625 -1802 C ATOM 1893 CG2 VAL A 332 -33.309 -26.269 29.503 1.00 46.95 C ANISOU 1893 CG2 VAL A 332 4797 5854 7190 -1190 -729 -1482 C ATOM 1894 N TYR A 333 -33.109 -29.080 27.003 1.00 62.55 N ANISOU 1894 N TYR A 333 7196 7536 9033 -1562 -962 -2070 N ATOM 1895 CA TYR A 333 -33.940 -29.079 25.800 1.00 63.46 C ANISOU 1895 CA TYR A 333 7308 7748 9056 -1758 -1218 -2176 C ATOM 1896 C TYR A 333 -34.854 -30.294 25.654 1.00 64.94 C ANISOU 1896 C TYR A 333 7477 7758 9439 -1993 -1330 -2286 C ATOM 1897 O TYR A 333 -35.874 -30.225 24.969 1.00 65.54 O ANISOU 1897 O TYR A 333 7451 7928 9522 -2176 -1566 -2316 O ATOM 1898 CB TYR A 333 -33.082 -28.900 24.545 1.00 62.53 C ANISOU 1898 CB TYR A 333 7421 7728 8610 -1735 -1264 -2364 C ATOM 1899 CG TYR A 333 -32.914 -27.455 24.137 1.00 61.47 C ANISOU 1899 CG TYR A 333 7247 7847 8260 -1639 -1318 -2246 C ATOM 1900 CD1 TYR A 333 -33.838 -26.840 23.303 1.00 62.66 C ANISOU 1900 CD1 TYR A 333 7328 8169 8312 -1753 -1571 -2211 C ATOM 1901 CD2 TYR A 333 -31.839 -26.703 24.592 1.00 60.28 C ANISOU 1901 CD2 TYR A 333 7132 7762 8009 -1438 -1124 -2165 C ATOM 1902 CE1 TYR A 333 -33.695 -25.519 22.928 1.00 62.15 C ANISOU 1902 CE1 TYR A 333 7253 8311 8051 -1657 -1618 -2088 C ATOM 1903 CE2 TYR A 333 -31.687 -25.379 24.222 1.00 59.52 C ANISOU 1903 CE2 TYR A 333 7020 7871 7724 -1367 -1162 -2054 C ATOM 1904 CZ TYR A 333 -32.619 -24.793 23.390 1.00 60.60 C ANISOU 1904 CZ TYR A 333 7110 8152 7762 -1471 -1404 -2010 C ATOM 1905 OH TYR A 333 -32.475 -23.477 23.017 1.00 60.89 O ANISOU 1905 OH TYR A 333 7156 8369 7612 -1391 -1439 -1884 O ATOM 1906 N ILE A 334 -34.493 -31.402 26.291 1.00 58.25 N ANISOU 1906 N ILE A 334 6729 6651 8752 -1991 -1169 -2345 N ATOM 1907 CA ILE A 334 -35.325 -32.601 26.236 1.00 60.46 C ANISOU 1907 CA ILE A 334 7009 6721 9242 -2228 -1246 -2446 C ATOM 1908 C ILE A 334 -36.551 -32.446 27.132 1.00 60.73 C ANISOU 1908 C ILE A 334 6748 6762 9563 -2330 -1263 -2232 C ATOM 1909 O ILE A 334 -36.430 -32.127 28.315 1.00 59.41 O ANISOU 1909 O ILE A 334 6478 6574 9522 -2183 -1077 -2030 O ATOM 1910 CB ILE A 334 -34.539 -33.863 26.642 1.00 61.07 C ANISOU 1910 CB ILE A 334 7313 6484 9405 -2183 -1055 -2567 C ATOM 1911 CG1 ILE A 334 -33.333 -34.057 25.722 1.00 61.06 C ANISOU 1911 CG1 ILE A 334 7587 6480 9131 -2071 -1019 -2794 C ATOM 1912 CG2 ILE A 334 -35.440 -35.089 26.601 1.00 64.28 C ANISOU 1912 CG2 ILE A 334 7736 6646 10040 -2452 -1128 -2669 C ATOM 1913 CD1 ILE A 334 -32.541 -35.312 26.011 1.00 62.11 C ANISOU 1913 CD1 ILE A 334 7953 6301 9346 -2004 -844 -2933 C ATOM 1914 N SER A 335 -37.730 -32.667 26.557 1.00142.30 N ANISOU 1914 N SER A 335 16939 17135 19991 -2583 -1487 -2285 N ATOM 1915 CA SER A 335 -38.985 -32.527 27.289 1.00143.21 C ANISOU 1915 CA SER A 335 16738 17285 20389 -2703 -1515 -2098 C ATOM 1916 C SER A 335 -39.080 -33.530 28.434 1.00144.25 C ANISOU 1916 C SER A 335 16876 17131 20800 -2752 -1292 -2027 C ATOM 1917 O SER A 335 -38.431 -34.576 28.410 1.00145.92 O ANISOU 1917 O SER A 335 17340 17084 21018 -2774 -1193 -2171 O ATOM 1918 CB SER A 335 -40.179 -32.690 26.346 1.00142.56 C ANISOU 1918 CB SER A 335 16502 17305 20357 -2984 -1821 -2203 C ATOM 1919 OG SER A 335 -41.403 -32.536 27.043 1.00143.61 O ANISOU 1919 OG SER A 335 16291 17493 20779 -3097 -1842 -2024 O ATOM 1920 N ASP A 336 -39.895 -33.205 29.432 1.00138.91 N ANISOU 1920 N ASP A 336 15933 16497 20352 -2759 -1204 -1800 N ATOM 1921 CA ASP A 336 -40.039 -34.047 30.615 1.00139.11 C ANISOU 1921 CA ASP A 336 15959 16266 20630 -2799 -971 -1689 C ATOM 1922 C ASP A 336 -40.683 -35.393 30.292 1.00140.70 C ANISOU 1922 C ASP A 336 16211 16219 21030 -3117 -1036 -1842 C ATOM 1923 O ASP A 336 -40.470 -36.377 31.001 1.00141.18 O ANISOU 1923 O ASP A 336 16425 15984 21234 -3148 -845 -1829 O ATOM 1924 CB ASP A 336 -40.848 -33.323 31.694 1.00138.66 C ANISOU 1924 CB ASP A 336 15591 16336 20757 -2752 -861 -1419 C ATOM 1925 CG ASP A 336 -40.220 -32.007 32.108 1.00137.28 C ANISOU 1925 CG ASP A 336 15385 16376 20401 -2445 -781 -1271 C ATOM 1926 OD1 ASP A 336 -39.039 -31.779 31.772 1.00136.09 O ANISOU 1926 OD1 ASP A 336 15463 16240 20007 -2263 -763 -1358 O ATOM 1927 OD2 ASP A 336 -40.904 -31.202 32.773 1.00137.13 O ANISOU 1927 OD2 ASP A 336 15110 16504 20488 -2388 -727 -1076 O ATOM 1928 N GLU A 337 -41.469 -35.432 29.222 1.00143.15 N ANISOU 1928 N GLU A 337 16402 16645 21345 -3356 -1312 -1986 N ATOM 1929 CA GLU A 337 -42.136 -36.663 28.814 1.00146.48 C ANISOU 1929 CA GLU A 337 16877 16859 21920 -3679 -1401 -2141 C ATOM 1930 C GLU A 337 -41.205 -37.567 28.011 1.00146.74 C ANISOU 1930 C GLU A 337 17303 16666 21785 -3696 -1424 -2417 C ATOM 1931 O GLU A 337 -41.371 -38.787 27.997 1.00148.85 O ANISOU 1931 O GLU A 337 17751 16658 22150 -3862 -1369 -2498 O ATOM 1932 CB GLU A 337 -43.400 -36.354 28.007 1.00153.06 C ANISOU 1932 CB GLU A 337 17482 17967 22707 -3875 -1678 -2133 C ATOM 1933 CG GLU A 337 -43.156 -35.534 26.751 1.00152.77 C ANISOU 1933 CG GLU A 337 17482 18199 22365 -3803 -1943 -2260 C ATOM 1934 CD GLU A 337 -44.401 -35.399 25.896 1.00155.94 C ANISOU 1934 CD GLU A 337 17713 18832 22705 -4022 -2228 -2281 C ATOM 1935 OE1 GLU A 337 -45.425 -36.032 26.232 1.00157.82 O ANISOU 1935 OE1 GLU A 337 17806 19018 23142 -4249 -2220 -2228 O ATOM 1936 OE2 GLU A 337 -44.357 -34.662 24.889 1.00156.61 O ANISOU 1936 OE2 GLU A 337 17811 19159 22535 -3971 -2456 -2350 O ATOM 1937 N GLN A 338 -40.223 -36.966 27.346 1.00118.04 N ANISOU 1937 N GLN A 338 13828 13166 17855 -3495 -1483 -2529 N ATOM 1938 CA GLN A 338 -39.276 -37.721 26.533 1.00118.92 C ANISOU 1938 CA GLN A 338 14309 13101 17775 -3477 -1490 -2801 C ATOM 1939 C GLN A 338 -38.217 -38.418 27.381 1.00117.74 C ANISOU 1939 C GLN A 338 14410 12653 17672 -3277 -1192 -2772 C ATOM 1940 O GLN A 338 -37.610 -39.397 26.948 1.00119.47 O ANISOU 1940 O GLN A 338 14929 12620 17846 -3303 -1154 -2990 O ATOM 1941 CB GLN A 338 -38.601 -36.813 25.502 1.00118.49 C ANISOU 1941 CB GLN A 338 14347 13319 17355 -3315 -1625 -2902 C ATOM 1942 CG GLN A 338 -39.504 -36.384 24.360 1.00121.00 C ANISOU 1942 CG GLN A 338 14556 13880 17538 -3516 -1958 -3002 C ATOM 1943 CD GLN A 338 -38.756 -35.608 23.293 1.00120.44 C ANISOU 1943 CD GLN A 338 14634 14032 17097 -3373 -2072 -3130 C ATOM 1944 OE1 GLN A 338 -38.411 -34.442 23.483 1.00118.35 O ANISOU 1944 OE1 GLN A 338 14265 14003 16702 -3156 -2038 -2953 O ATOM 1945 NE2 GLN A 338 -38.496 -36.257 22.163 1.00122.24 N ANISOU 1945 NE2 GLN A 338 15159 14196 17090 -3452 -2170 -3356 N ATOM 1946 N TRP A 339 -37.996 -37.908 28.588 1.00 73.18 N ANISOU 1946 N TRP A 339 8652 7041 12112 -3067 -986 -2506 N ATOM 1947 CA TRP A 339 -36.986 -38.467 29.481 1.00 72.58 C ANISOU 1947 CA TRP A 339 8793 6719 12065 -2843 -720 -2444 C ATOM 1948 C TRP A 339 -37.341 -39.870 29.965 1.00 74.98 C ANISOU 1948 C TRP A 339 9231 6625 12633 -3025 -610 -2472 C ATOM 1949 O TRP A 339 -38.359 -40.071 30.628 1.00 76.33 O ANISOU 1949 O TRP A 339 9213 6733 13055 -3218 -578 -2324 O ATOM 1950 CB TRP A 339 -36.751 -37.545 30.680 1.00 70.88 C ANISOU 1950 CB TRP A 339 8416 6652 11862 -2593 -548 -2151 C ATOM 1951 CG TRP A 339 -35.752 -36.459 30.421 1.00 69.01 C ANISOU 1951 CG TRP A 339 8202 6674 11345 -2316 -549 -2145 C ATOM 1952 CD1 TRP A 339 -36.015 -35.143 30.180 1.00 67.68 C ANISOU 1952 CD1 TRP A 339 7826 6839 11050 -2263 -659 -2055 C ATOM 1953 CD2 TRP A 339 -34.327 -36.598 30.378 1.00 68.36 C ANISOU 1953 CD2 TRP A 339 8356 6532 11084 -2057 -427 -2231 C ATOM 1954 NE1 TRP A 339 -34.842 -34.453 29.990 1.00 66.43 N ANISOU 1954 NE1 TRP A 339 7774 6822 10645 -2009 -606 -2079 N ATOM 1955 CE2 TRP A 339 -33.791 -35.324 30.106 1.00 66.82 C ANISOU 1955 CE2 TRP A 339 8078 6648 10661 -1881 -465 -2191 C ATOM 1956 CE3 TRP A 339 -33.453 -37.677 30.542 1.00 69.05 C ANISOU 1956 CE3 TRP A 339 8712 6329 11193 -1950 -287 -2337 C ATOM 1957 CZ2 TRP A 339 -32.420 -35.099 29.995 1.00 65.94 C ANISOU 1957 CZ2 TRP A 339 8121 6583 10349 -1628 -364 -2258 C ATOM 1958 CZ3 TRP A 339 -32.093 -37.451 30.432 1.00 68.12 C ANISOU 1958 CZ3 TRP A 339 8736 6267 10878 -1670 -195 -2403 C ATOM 1959 CH2 TRP A 339 -31.590 -36.173 30.161 1.00 66.55 C ANISOU 1959 CH2 TRP A 339 8429 6398 10460 -1523 -232 -2366 C ATOM 1960 N THR A 340 -36.493 -40.835 29.625 1.00 95.05 N ANISOU 1960 N THR A 340 12102 8892 15121 -2960 -539 -2663 N ATOM 1961 CA THR A 340 -36.655 -42.204 30.098 1.00 97.56 C ANISOU 1961 CA THR A 340 12611 8783 15675 -3095 -411 -2691 C ATOM 1962 C THR A 340 -35.497 -42.573 31.018 1.00 97.13 C ANISOU 1962 C THR A 340 12773 8525 15606 -2763 -160 -2583 C ATOM 1963 O THR A 340 -34.564 -41.789 31.195 1.00 96.83 O ANISOU 1963 O THR A 340 12734 8690 15369 -2453 -107 -2528 O ATOM 1964 CB THR A 340 -36.716 -43.207 28.930 1.00100.78 C ANISOU 1964 CB THR A 340 13258 8989 16044 -3312 -551 -3016 C ATOM 1965 OG1 THR A 340 -35.488 -43.164 28.193 1.00 99.80 O ANISOU 1965 OG1 THR A 340 13373 8880 15668 -3085 -545 -3234 O ATOM 1966 CG2 THR A 340 -37.873 -42.875 28.001 1.00102.16 C ANISOU 1966 CG2 THR A 340 13233 9432 16152 -3598 -834 -3068 C ATOM 1967 N THR A 341 -35.562 -43.764 31.604 1.00 86.78 N ANISOU 1967 N THR A 341 11648 6814 14510 -2832 -12 -2547 N ATOM 1968 CA THR A 341 -34.511 -44.235 32.501 1.00 86.03 C ANISOU 1968 CA THR A 341 11773 6495 14420 -2516 213 -2430 C ATOM 1969 C THR A 341 -33.197 -44.431 31.751 1.00 85.66 C ANISOU 1969 C THR A 341 11975 6414 14158 -2259 213 -2663 C ATOM 1970 O THR A 341 -32.116 -44.150 32.279 1.00 84.17 O ANISOU 1970 O THR A 341 11846 6276 13859 -1908 337 -2569 O ATOM 1971 CB THR A 341 -34.908 -45.553 33.190 1.00 91.60 C ANISOU 1971 CB THR A 341 12668 6736 15399 -2665 360 -2359 C ATOM 1972 OG1 THR A 341 -35.233 -46.535 32.198 1.00 95.75 O ANISOU 1972 OG1 THR A 341 13385 7055 15942 -2905 241 -2614 O ATOM 1973 CG2 THR A 341 -36.113 -45.338 34.093 1.00 92.20 C ANISOU 1973 CG2 THR A 341 12489 6856 15689 -2887 415 -2095 C ATOM 1974 N ALA A 342 -33.302 -44.911 30.515 1.00 77.92 N ANISOU 1974 N ALA A 342 11131 5358 13116 -2439 74 -2973 N ATOM 1975 CA ALA A 342 -32.139 -45.099 29.658 1.00 78.22 C ANISOU 1975 CA ALA A 342 11402 5375 12941 -2224 79 -3228 C ATOM 1976 C ALA A 342 -31.429 -43.771 29.420 1.00 73.53 C ANISOU 1976 C ALA A 342 10640 5219 12078 -1984 41 -3192 C ATOM 1977 O ALA A 342 -30.214 -43.671 29.584 1.00 71.82 O ANISOU 1977 O ALA A 342 10521 5028 11739 -1654 162 -3201 O ATOM 1978 CB ALA A 342 -32.549 -45.728 28.336 1.00 82.02 C ANISOU 1978 CB ALA A 342 12044 5790 13328 -2469 -95 -3513 C ATOM 1979 N LEU A 343 -32.199 -42.753 29.046 1.00 71.82 N ANISOU 1979 N LEU A 343 10163 5342 11781 -2153 -127 -3147 N ATOM 1980 CA LEU A 343 -31.658 -41.416 28.822 1.00 67.58 C ANISOU 1980 CA LEU A 343 9460 5215 11001 -1962 -167 -3089 C ATOM 1981 C LEU A 343 -31.093 -40.813 30.105 1.00 63.47 C ANISOU 1981 C LEU A 343 8819 4789 10507 -1678 -2 -2803 C ATOM 1982 O LEU A 343 -30.192 -39.982 30.061 1.00 60.39 O ANISOU 1982 O LEU A 343 8387 4636 9925 -1436 36 -2784 O ATOM 1983 CB LEU A 343 -32.731 -40.492 28.241 1.00 67.11 C ANISOU 1983 CB LEU A 343 9150 5463 10885 -2203 -385 -3065 C ATOM 1984 CG LEU A 343 -33.080 -40.675 26.763 1.00 70.40 C ANISOU 1984 CG LEU A 343 9664 5934 11150 -2425 -595 -3361 C ATOM 1985 CD1 LEU A 343 -34.235 -39.768 26.370 1.00 70.23 C ANISOU 1985 CD1 LEU A 343 9366 6212 11106 -2647 -823 -3288 C ATOM 1986 CD2 LEU A 343 -31.863 -40.403 25.893 1.00 69.54 C ANISOU 1986 CD2 LEU A 343 9729 5952 10739 -2206 -564 -3549 C ATOM 1987 N PHE A 344 -31.634 -41.241 31.241 1.00 69.18 N ANISOU 1987 N PHE A 344 9496 5329 11463 -1723 98 -2585 N ATOM 1988 CA PHE A 344 -31.202 -40.762 32.550 1.00 66.72 C ANISOU 1988 CA PHE A 344 9091 5084 11176 -1473 252 -2308 C ATOM 1989 C PHE A 344 -29.807 -41.292 32.876 1.00 66.62 C ANISOU 1989 C PHE A 344 9298 4915 11102 -1141 400 -2346 C ATOM 1990 O PHE A 344 -28.847 -40.521 33.055 1.00 64.11 O ANISOU 1990 O PHE A 344 8919 4825 10615 -874 440 -2306 O ATOM 1991 CB PHE A 344 -32.206 -41.230 33.607 1.00 67.93 C ANISOU 1991 CB PHE A 344 9174 5049 11587 -1633 333 -2080 C ATOM 1992 CG PHE A 344 -32.036 -40.580 34.948 1.00 66.49 C ANISOU 1992 CG PHE A 344 8863 4988 11412 -1428 467 -1780 C ATOM 1993 CD1 PHE A 344 -32.590 -39.338 35.204 1.00 65.50 C ANISOU 1993 CD1 PHE A 344 8457 5197 11235 -1456 417 -1633 C ATOM 1994 CD2 PHE A 344 -31.346 -41.223 35.963 1.00 67.07 C ANISOU 1994 CD2 PHE A 344 9110 4835 11541 -1205 641 -1646 C ATOM 1995 CE1 PHE A 344 -32.446 -38.741 36.441 1.00 65.10 C ANISOU 1995 CE1 PHE A 344 8308 5252 11178 -1274 545 -1375 C ATOM 1996 CE2 PHE A 344 -31.200 -40.631 37.203 1.00 66.43 C ANISOU 1996 CE2 PHE A 344 8928 4873 11441 -1023 753 -1378 C ATOM 1997 CZ PHE A 344 -31.749 -39.387 37.441 1.00 65.54 C ANISOU 1997 CZ PHE A 344 8542 5093 11268 -1064 710 -1251 C ATOM 1998 N ASP A 345 -29.705 -42.617 32.949 1.00 84.00 N ANISOU 1998 N ASP A 345 11749 6719 13447 -1159 477 -2428 N ATOM 1999 CA ASP A 345 -28.433 -43.278 33.211 1.00 84.22 C ANISOU 1999 CA ASP A 345 11997 6556 13446 -834 611 -2471 C ATOM 2000 C ASP A 345 -27.382 -42.843 32.193 1.00 82.75 C ANISOU 2000 C ASP A 345 11842 6574 13025 -661 574 -2710 C ATOM 2001 O ASP A 345 -26.253 -42.500 32.558 1.00 81.88 O ANISOU 2001 O ASP A 345 11719 6582 12811 -340 658 -2669 O ATOM 2002 CB ASP A 345 -28.607 -44.798 33.186 1.00 87.82 C ANISOU 2002 CB ASP A 345 12745 6526 14098 -919 681 -2563 C ATOM 2003 CG ASP A 345 -29.625 -45.284 34.201 1.00 89.46 C ANISOU 2003 CG ASP A 345 12939 6509 14544 -1108 746 -2321 C ATOM 2004 OD1 ASP A 345 -30.503 -44.487 34.596 1.00 88.79 O ANISOU 2004 OD1 ASP A 345 12598 6654 14485 -1276 698 -2152 O ATOM 2005 OD2 ASP A 345 -29.547 -46.463 34.607 1.00 91.66 O ANISOU 2005 OD2 ASP A 345 13467 6373 14986 -1084 858 -2297 O ATOM 2006 N PHE A 346 -27.768 -42.839 30.919 1.00 77.10 N ANISOU 2006 N PHE A 346 11159 5914 12220 -882 445 -2958 N ATOM 2007 CA PHE A 346 -26.879 -42.387 29.853 1.00 76.07 C ANISOU 2007 CA PHE A 346 11061 5997 11844 -760 416 -3189 C ATOM 2008 C PHE A 346 -26.451 -40.938 30.050 1.00 74.31 C ANISOU 2008 C PHE A 346 10590 6202 11443 -620 400 -3052 C ATOM 2009 O PHE A 346 -25.329 -40.572 29.713 1.00 73.68 O ANISOU 2009 O PHE A 346 10521 6280 11195 -392 461 -3148 O ATOM 2010 CB PHE A 346 -27.530 -42.554 28.478 1.00 76.75 C ANISOU 2010 CB PHE A 346 11225 6094 11841 -1056 260 -3457 C ATOM 2011 CG PHE A 346 -26.799 -41.844 27.373 1.00 75.62 C ANISOU 2011 CG PHE A 346 11081 6242 11408 -973 219 -3653 C ATOM 2012 CD1 PHE A 346 -25.621 -42.361 26.860 1.00 76.03 C ANISOU 2012 CD1 PHE A 346 11330 6204 11354 -747 340 -3868 C ATOM 2013 CD2 PHE A 346 -27.288 -40.658 26.850 1.00 74.66 C ANISOU 2013 CD2 PHE A 346 10764 6483 11120 -1112 73 -3614 C ATOM 2014 CE1 PHE A 346 -24.944 -41.709 25.846 1.00 75.32 C ANISOU 2014 CE1 PHE A 346 11240 6388 10991 -680 330 -4043 C ATOM 2015 CE2 PHE A 346 -26.616 -40.001 25.837 1.00 73.64 C ANISOU 2015 CE2 PHE A 346 10656 6613 10712 -1044 51 -3777 C ATOM 2016 CZ PHE A 346 -25.443 -40.528 25.334 1.00 73.73 C ANISOU 2016 CZ PHE A 346 10862 6540 10614 -837 187 -3993 C ATOM 2017 N TYR A 347 -27.348 -40.116 30.586 1.00 58.26 N ANISOU 2017 N TYR A 347 8332 4350 9454 -759 327 -2835 N ATOM 2018 CA TYR A 347 -27.015 -38.727 30.875 1.00 54.07 C ANISOU 2018 CA TYR A 347 7579 4192 8773 -637 317 -2691 C ATOM 2019 C TYR A 347 -25.943 -38.659 31.951 1.00 52.38 C ANISOU 2019 C TYR A 347 7354 3982 8566 -307 469 -2547 C ATOM 2020 O TYR A 347 -25.056 -37.806 31.902 1.00 50.29 O ANISOU 2020 O TYR A 347 6996 3974 8135 -127 497 -2551 O ATOM 2021 CB TYR A 347 -28.249 -37.939 31.317 1.00 51.99 C ANISOU 2021 CB TYR A 347 7087 4084 8583 -835 224 -2483 C ATOM 2022 CG TYR A 347 -27.938 -36.542 31.804 1.00 47.80 C ANISOU 2022 CG TYR A 347 6349 3887 7927 -693 236 -2311 C ATOM 2023 CD1 TYR A 347 -27.741 -35.501 30.907 1.00 46.43 C ANISOU 2023 CD1 TYR A 347 6095 4008 7540 -713 144 -2398 C ATOM 2024 CD2 TYR A 347 -27.834 -36.264 33.162 1.00 45.56 C ANISOU 2024 CD2 TYR A 347 5971 3612 7728 -543 342 -2065 C ATOM 2025 CE1 TYR A 347 -27.455 -34.224 31.347 1.00 42.92 C ANISOU 2025 CE1 TYR A 347 5480 3840 6988 -595 162 -2246 C ATOM 2026 CE2 TYR A 347 -27.546 -34.990 33.611 1.00 42.04 C ANISOU 2026 CE2 TYR A 347 5353 3455 7166 -423 352 -1928 C ATOM 2027 CZ TYR A 347 -27.357 -33.973 32.700 1.00 40.73 C ANISOU 2027 CZ TYR A 347 5108 3559 6806 -454 264 -2021 C ATOM 2028 OH TYR A 347 -27.070 -32.702 33.141 1.00 37.54 O ANISOU 2028 OH TYR A 347 4552 3417 6296 -348 280 -1890 O ATOM 2029 N HIS A 348 -26.024 -39.559 32.925 1.00 58.44 N ANISOU 2029 N HIS A 348 8219 4464 9523 -234 563 -2418 N ATOM 2030 CA HIS A 348 -25.024 -39.577 33.992 1.00 57.49 C ANISOU 2030 CA HIS A 348 8101 4337 9406 89 685 -2270 C ATOM 2031 C HIS A 348 -23.657 -40.097 33.525 1.00 58.62 C ANISOU 2031 C HIS A 348 8386 4418 9471 354 759 -2465 C ATOM 2032 O HIS A 348 -22.612 -39.549 33.899 1.00 57.13 O ANISOU 2032 O HIS A 348 8105 4420 9183 614 811 -2421 O ATOM 2033 CB HIS A 348 -25.543 -40.344 35.210 1.00 58.68 C ANISOU 2033 CB HIS A 348 8328 4206 9762 94 764 -2047 C ATOM 2034 CG HIS A 348 -26.695 -39.672 35.891 1.00 57.31 C ANISOU 2034 CG HIS A 348 7972 4149 9654 -98 734 -1822 C ATOM 2035 ND1 HIS A 348 -27.881 -39.395 35.246 1.00 57.60 N ANISOU 2035 ND1 HIS A 348 7908 4242 9734 -420 627 -1868 N ATOM 2036 CD2 HIS A 348 -26.837 -39.205 37.154 1.00 55.83 C ANISOU 2036 CD2 HIS A 348 7679 4044 9490 -4 798 -1555 C ATOM 2037 CE1 HIS A 348 -28.706 -38.793 36.083 1.00 56.37 C ANISOU 2037 CE1 HIS A 348 7579 4196 9645 -507 639 -1638 C ATOM 2038 NE2 HIS A 348 -28.098 -38.667 37.248 1.00 55.27 N ANISOU 2038 NE2 HIS A 348 7444 4069 9486 -262 750 -1448 N ATOM 2039 N TYR A 349 -23.660 -41.139 32.697 1.00 58.40 N ANISOU 2039 N TYR A 349 8571 4126 9491 287 766 -2689 N ATOM 2040 CA TYR A 349 -22.412 -41.635 32.118 1.00 60.75 C ANISOU 2040 CA TYR A 349 9001 4367 9713 533 847 -2905 C ATOM 2041 C TYR A 349 -21.778 -40.577 31.212 1.00 59.07 C ANISOU 2041 C TYR A 349 8651 4533 9262 561 820 -3053 C ATOM 2042 O TYR A 349 -20.558 -40.376 31.223 1.00 59.20 O ANISOU 2042 O TYR A 349 8620 4683 9190 832 904 -3109 O ATOM 2043 CB TYR A 349 -22.642 -42.936 31.343 1.00 65.24 C ANISOU 2043 CB TYR A 349 9849 4566 10374 429 862 -3138 C ATOM 2044 CG TYR A 349 -23.009 -44.117 32.215 1.00 67.83 C ANISOU 2044 CG TYR A 349 10362 4469 10943 451 926 -3011 C ATOM 2045 CD1 TYR A 349 -22.111 -44.621 33.148 1.00 68.82 C ANISOU 2045 CD1 TYR A 349 10558 4445 11146 795 1040 -2885 C ATOM 2046 CD2 TYR A 349 -24.246 -44.737 32.096 1.00 69.74 C ANISOU 2046 CD2 TYR A 349 10709 4454 11333 124 871 -3014 C ATOM 2047 CE1 TYR A 349 -22.440 -45.702 33.945 1.00 71.55 C ANISOU 2047 CE1 TYR A 349 11102 4385 11700 820 1106 -2750 C ATOM 2048 CE2 TYR A 349 -24.584 -45.818 32.888 1.00 72.50 C ANISOU 2048 CE2 TYR A 349 11245 4397 11906 123 948 -2889 C ATOM 2049 CZ TYR A 349 -23.677 -46.297 33.810 1.00 73.38 C ANISOU 2049 CZ TYR A 349 11452 4352 12078 476 1070 -2751 C ATOM 2050 OH TYR A 349 -24.010 -47.374 34.600 1.00 76.48 O ANISOU 2050 OH TYR A 349 12056 4322 12681 480 1152 -2608 O ATOM 2051 N PHE A 350 -22.620 -39.901 30.437 1.00 71.39 N ANISOU 2051 N PHE A 350 10139 6266 10721 278 700 -3108 N ATOM 2052 CA PHE A 350 -22.187 -38.814 29.569 1.00 69.94 C ANISOU 2052 CA PHE A 350 9840 6434 10298 261 667 -3216 C ATOM 2053 C PHE A 350 -21.620 -37.677 30.409 1.00 68.12 C ANISOU 2053 C PHE A 350 9379 6497 10007 428 702 -3012 C ATOM 2054 O PHE A 350 -20.696 -36.980 29.989 1.00 66.31 O ANISOU 2054 O PHE A 350 9068 6514 9611 549 750 -3093 O ATOM 2055 CB PHE A 350 -23.364 -38.305 28.734 1.00 69.47 C ANISOU 2055 CB PHE A 350 9748 6487 10159 -75 506 -3259 C ATOM 2056 CG PHE A 350 -22.976 -37.322 27.666 1.00 68.16 C ANISOU 2056 CG PHE A 350 9526 6643 9729 -112 469 -3386 C ATOM 2057 CD1 PHE A 350 -21.732 -37.387 27.059 1.00 67.06 C ANISOU 2057 CD1 PHE A 350 9459 6578 9441 77 589 -3576 C ATOM 2058 CD2 PHE A 350 -23.857 -36.328 27.272 1.00 68.01 C ANISOU 2058 CD2 PHE A 350 9380 6851 9611 -328 323 -3306 C ATOM 2059 CE1 PHE A 350 -21.377 -36.482 26.078 1.00 66.32 C ANISOU 2059 CE1 PHE A 350 9327 6776 9094 30 576 -3680 C ATOM 2060 CE2 PHE A 350 -23.508 -35.421 26.292 1.00 66.67 C ANISOU 2060 CE2 PHE A 350 9184 6961 9185 -360 293 -3402 C ATOM 2061 CZ PHE A 350 -22.266 -35.497 25.694 1.00 66.27 C ANISOU 2061 CZ PHE A 350 9221 6979 8978 -191 426 -3587 C ATOM 2062 N TYR A 351 -22.187 -37.494 31.597 1.00 62.64 N ANISOU 2062 N TYR A 351 8586 5770 9445 422 684 -2752 N ATOM 2063 CA TYR A 351 -21.691 -36.504 32.543 1.00 60.97 C ANISOU 2063 CA TYR A 351 8179 5798 9188 580 715 -2555 C ATOM 2064 C TYR A 351 -20.268 -36.862 32.948 1.00 60.12 C ANISOU 2064 C TYR A 351 8086 5684 9073 910 828 -2596 C ATOM 2065 O TYR A 351 -19.361 -36.020 32.891 1.00 58.79 O ANISOU 2065 O TYR A 351 7777 5787 8771 1037 860 -2621 O ATOM 2066 CB TYR A 351 -22.601 -36.440 33.771 1.00 63.12 C ANISOU 2066 CB TYR A 351 8386 5989 9607 519 694 -2284 C ATOM 2067 CG TYR A 351 -22.239 -35.361 34.764 1.00 61.95 C ANISOU 2067 CG TYR A 351 8052 6087 9398 651 713 -2086 C ATOM 2068 CD1 TYR A 351 -22.768 -34.084 34.651 1.00 61.43 C ANISOU 2068 CD1 TYR A 351 7822 6281 9238 510 646 -2007 C ATOM 2069 CD2 TYR A 351 -21.376 -35.621 35.821 1.00 61.53 C ANISOU 2069 CD2 TYR A 351 7999 5999 9379 921 789 -1979 C ATOM 2070 CE1 TYR A 351 -22.445 -33.093 35.556 1.00 60.10 C ANISOU 2070 CE1 TYR A 351 7504 6319 9013 620 667 -1844 C ATOM 2071 CE2 TYR A 351 -21.047 -34.637 36.733 1.00 59.98 C ANISOU 2071 CE2 TYR A 351 7644 6030 9115 1027 793 -1816 C ATOM 2072 CZ TYR A 351 -21.584 -33.374 36.595 1.00 58.99 C ANISOU 2072 CZ TYR A 351 7368 6148 8898 869 738 -1756 C ATOM 2073 OH TYR A 351 -21.261 -32.387 37.499 1.00 56.02 O ANISOU 2073 OH TYR A 351 6852 5981 8451 963 746 -1611 O ATOM 2074 N MET A 352 -20.083 -38.119 33.347 1.00 64.62 N ANISOU 2074 N MET A 352 8822 5937 9793 1047 887 -2604 N ATOM 2075 CA MET A 352 -18.761 -38.624 33.707 1.00 64.09 C ANISOU 2075 CA MET A 352 8779 5830 9742 1387 984 -2650 C ATOM 2076 C MET A 352 -17.743 -38.383 32.592 1.00 63.10 C ANISOU 2076 C MET A 352 8623 5885 9467 1473 1040 -2909 C ATOM 2077 O MET A 352 -16.666 -37.833 32.832 1.00 61.75 O ANISOU 2077 O MET A 352 8295 5944 9221 1680 1089 -2909 O ATOM 2078 CB MET A 352 -18.824 -40.117 34.035 1.00 66.35 C ANISOU 2078 CB MET A 352 9301 5696 10211 1496 1037 -2657 C ATOM 2079 CG MET A 352 -19.688 -40.461 35.237 1.00 67.35 C ANISOU 2079 CG MET A 352 9477 5622 10489 1438 1017 -2387 C ATOM 2080 SD MET A 352 -19.667 -42.226 35.608 1.00 69.97 S ANISOU 2080 SD MET A 352 10121 5432 11033 1577 1096 -2387 S ATOM 2081 CE MET A 352 -20.754 -42.290 37.029 1.00 71.74 C ANISOU 2081 CE MET A 352 10357 5512 11387 1459 1086 -2033 C ATOM 2082 N LEU A 353 -18.100 -38.788 31.376 1.00 90.64 N ANISOU 2082 N LEU A 353 12259 9275 12905 1301 1033 -3132 N ATOM 2083 CA LEU A 353 -17.229 -38.630 30.212 1.00 90.94 C ANISOU 2083 CA LEU A 353 12305 9466 12782 1357 1106 -3394 C ATOM 2084 C LEU A 353 -16.855 -37.169 29.954 1.00 88.86 C ANISOU 2084 C LEU A 353 11817 9617 12329 1308 1096 -3363 C ATOM 2085 O LEU A 353 -15.669 -36.814 29.893 1.00 87.57 O ANISOU 2085 O LEU A 353 11536 9664 12072 1495 1180 -3375 O ATOM 2086 CB LEU A 353 -17.906 -39.215 28.971 1.00 92.82 C ANISOU 2086 CB LEU A 353 12758 9541 12967 1125 1072 -3622 C ATOM 2087 CG LEU A 353 -17.207 -38.996 27.628 1.00 94.32 C ANISOU 2087 CG LEU A 353 12999 9929 12910 1111 1121 -3816 C ATOM 2088 CD1 LEU A 353 -15.884 -39.745 27.577 1.00 96.63 C ANISOU 2088 CD1 LEU A 353 13362 10170 13182 1411 1252 -3850 C ATOM 2089 CD2 LEU A 353 -18.112 -39.413 26.478 1.00 95.89 C ANISOU 2089 CD2 LEU A 353 13399 10006 13027 826 1035 -3998 C ATOM 2090 N SER A 354 -17.877 -36.333 29.799 1.00 63.67 N ANISOU 2090 N SER A 354 8570 6553 9068 1038 981 -3262 N ATOM 2091 CA SER A 354 -17.690 -34.916 29.505 1.00 61.77 C ANISOU 2091 CA SER A 354 8153 6669 8649 956 963 -3221 C ATOM 2092 C SER A 354 -16.812 -34.227 30.543 1.00 59.40 C ANISOU 2092 C SER A 354 7644 6560 8367 1161 1014 -3069 C ATOM 2093 O SER A 354 -15.853 -33.537 30.189 1.00 57.98 O ANISOU 2093 O SER A 354 7344 6624 8061 1239 1091 -3148 O ATOM 2094 CB SER A 354 -19.043 -34.208 29.400 1.00 60.76 C ANISOU 2094 CB SER A 354 7997 6602 8487 669 817 -3092 C ATOM 2095 OG SER A 354 -19.823 -34.425 30.562 1.00 61.75 O ANISOU 2095 OG SER A 354 8090 6580 8795 650 759 -2873 O ATOM 2096 N ASN A 355 -17.131 -34.420 31.820 1.00 71.32 N ANISOU 2096 N ASN A 355 9112 7961 10026 1240 975 -2856 N ATOM 2097 CA ASN A 355 -16.327 -33.828 32.886 1.00 69.93 C ANISOU 2097 CA ASN A 355 8752 7957 9860 1435 1001 -2714 C ATOM 2098 C ASN A 355 -14.895 -34.362 32.898 1.00 70.47 C ANISOU 2098 C ASN A 355 8780 8049 9946 1729 1107 -2842 C ATOM 2099 O ASN A 355 -13.944 -33.621 33.180 1.00 69.61 O ANISOU 2099 O ASN A 355 8502 8203 9745 1814 1125 -2759 O ATOM 2100 CB ASN A 355 -16.993 -34.026 34.248 1.00 68.81 C ANISOU 2100 CB ASN A 355 8612 7677 9856 1466 944 -2464 C ATOM 2101 CG ASN A 355 -18.254 -33.199 34.402 1.00 69.48 C ANISOU 2101 CG ASN A 355 8656 7824 9921 1211 856 -2313 C ATOM 2102 OD1 ASN A 355 -18.906 -32.848 33.418 1.00 69.51 O ANISOU 2102 OD1 ASN A 355 8687 7875 9847 991 810 -2397 O ATOM 2103 ND2 ASN A 355 -18.599 -32.875 35.642 1.00 69.80 N ANISOU 2103 ND2 ASN A 355 8629 7871 10022 1249 830 -2089 N ATOM 2104 N ALA A 356 -14.749 -35.647 32.582 1.00 52.96 N ANISOU 2104 N ALA A 356 6745 5570 7808 1830 1151 -2936 N ATOM 2105 CA ALA A 356 -13.430 -36.257 32.465 1.00 55.11 C ANISOU 2105 CA ALA A 356 7022 5870 8049 2065 1234 -2952 C ATOM 2106 C ALA A 356 -12.596 -35.520 31.426 1.00 55.09 C ANISOU 2106 C ALA A 356 6918 6159 7856 1998 1300 -3051 C ATOM 2107 O ALA A 356 -11.434 -35.199 31.672 1.00 55.34 O ANISOU 2107 O ALA A 356 6790 6388 7847 2134 1348 -2984 O ATOM 2108 CB ALA A 356 -13.546 -37.731 32.111 1.00 58.13 C ANISOU 2108 CB ALA A 356 7654 5904 8529 2154 1279 -3060 C ATOM 2109 N LEU A 357 -13.195 -35.241 30.271 1.00 55.00 N ANISOU 2109 N LEU A 357 6999 6169 7730 1774 1300 -3204 N ATOM 2110 CA LEU A 357 -12.506 -34.476 29.232 1.00 55.08 C ANISOU 2110 CA LEU A 357 6939 6444 7545 1687 1368 -3285 C ATOM 2111 C LEU A 357 -12.216 -33.042 29.682 1.00 52.53 C ANISOU 2111 C LEU A 357 6384 6427 7149 1616 1341 -3147 C ATOM 2112 O LEU A 357 -11.161 -32.478 29.362 1.00 52.88 O ANISOU 2112 O LEU A 357 6304 6690 7099 1644 1415 -3139 O ATOM 2113 CB LEU A 357 -13.312 -34.477 27.932 1.00 55.67 C ANISOU 2113 CB LEU A 357 7190 6473 7490 1455 1354 -3461 C ATOM 2114 CG LEU A 357 -13.470 -35.841 27.255 1.00 58.67 C ANISOU 2114 CG LEU A 357 7823 6569 7898 1492 1388 -3628 C ATOM 2115 CD1 LEU A 357 -14.222 -35.710 25.940 1.00 59.31 C ANISOU 2115 CD1 LEU A 357 8069 6656 7811 1239 1349 -3792 C ATOM 2116 CD2 LEU A 357 -12.112 -36.491 27.041 1.00 61.22 C ANISOU 2116 CD2 LEU A 357 8152 6896 8212 1739 1528 -3670 C ATOM 2117 N VAL A 358 -13.156 -32.461 30.425 1.00 57.18 N ANISOU 2117 N VAL A 358 6919 7014 7791 1517 1241 -3042 N ATOM 2118 CA VAL A 358 -12.984 -31.118 30.973 1.00 54.43 C ANISOU 2118 CA VAL A 358 6376 6920 7385 1451 1207 -2901 C ATOM 2119 C VAL A 358 -11.718 -31.036 31.821 1.00 54.03 C ANISOU 2119 C VAL A 358 6164 6989 7375 1645 1233 -2781 C ATOM 2120 O VAL A 358 -10.935 -30.093 31.695 1.00 52.75 O ANISOU 2120 O VAL A 358 5857 7063 7121 1595 1259 -2743 O ATOM 2121 CB VAL A 358 -14.203 -30.681 31.815 1.00 52.43 C ANISOU 2121 CB VAL A 358 6101 6605 7213 1364 1108 -2799 C ATOM 2122 CG1 VAL A 358 -13.886 -29.420 32.607 1.00 50.50 C ANISOU 2122 CG1 VAL A 358 5668 6594 6924 1346 1077 -2634 C ATOM 2123 CG2 VAL A 358 -15.414 -30.463 30.924 1.00 52.99 C ANISOU 2123 CG2 VAL A 358 6294 6622 7217 1115 1054 -2870 C ATOM 2124 N TYR A 359 -11.513 -32.036 32.673 1.00 59.99 N ANISOU 2124 N TYR A 359 6953 7571 8271 1859 1222 -2724 N ATOM 2125 CA TYR A 359 -10.297 -32.099 33.479 1.00 61.15 C ANISOU 2125 CA TYR A 359 6954 7821 8461 2057 1234 -2622 C ATOM 2126 C TYR A 359 -9.078 -32.433 32.619 1.00 63.82 C ANISOU 2126 C TYR A 359 7256 8239 8754 2138 1349 -2737 C ATOM 2127 O TYR A 359 -7.962 -31.971 32.892 1.00 64.16 O ANISOU 2127 O TYR A 359 7115 8480 8785 2198 1369 -2691 O ATOM 2128 CB TYR A 359 -10.458 -33.114 34.611 1.00 62.45 C ANISOU 2128 CB TYR A 359 7185 7765 8779 2272 1191 -2517 C ATOM 2129 CG TYR A 359 -11.537 -32.731 35.595 1.00 61.25 C ANISOU 2129 CG TYR A 359 7044 7555 8674 2211 1093 -2383 C ATOM 2130 CD1 TYR A 359 -11.776 -31.399 35.902 1.00 59.81 C ANISOU 2130 CD1 TYR A 359 6728 7592 8405 2055 1040 -2304 C ATOM 2131 CD2 TYR A 359 -12.319 -33.698 36.213 1.00 63.31 C ANISOU 2131 CD2 TYR A 359 7458 7527 9072 2308 1064 -2332 C ATOM 2132 CE1 TYR A 359 -12.760 -31.037 36.797 1.00 59.46 C ANISOU 2132 CE1 TYR A 359 6691 7499 8403 2010 969 -2182 C ATOM 2133 CE2 TYR A 359 -13.309 -33.345 37.112 1.00 63.25 C ANISOU 2133 CE2 TYR A 359 7454 7463 9118 2254 992 -2207 C ATOM 2134 CZ TYR A 359 -13.524 -32.012 37.399 1.00 60.80 C ANISOU 2134 CZ TYR A 359 6997 7394 8713 2112 949 -2135 C ATOM 2135 OH TYR A 359 -14.504 -31.648 38.290 1.00 60.38 O ANISOU 2135 OH TYR A 359 6960 7289 8695 2041 891 -1974 O ATOM 2136 N VAL A 360 -9.304 -33.231 31.577 1.00 56.42 N ANISOU 2136 N VAL A 360 6495 7146 7796 2132 1424 -2895 N ATOM 2137 CA VAL A 360 -8.252 -33.582 30.627 1.00 58.93 C ANISOU 2137 CA VAL A 360 6807 7526 8058 2203 1556 -3021 C ATOM 2138 C VAL A 360 -7.636 -32.330 30.007 1.00 58.14 C ANISOU 2138 C VAL A 360 6549 7724 7819 2044 1600 -3035 C ATOM 2139 O VAL A 360 -6.427 -32.269 29.814 1.00 59.84 O ANISOU 2139 O VAL A 360 6633 8075 8031 2136 1690 -3059 O ATOM 2140 CB VAL A 360 -8.767 -34.541 29.520 1.00 60.82 C ANISOU 2140 CB VAL A 360 7302 7548 8261 2178 1621 -3204 C ATOM 2141 CG1 VAL A 360 -7.882 -34.481 28.280 1.00 62.97 C ANISOU 2141 CG1 VAL A 360 7573 7943 8410 2175 1766 -3344 C ATOM 2142 CG2 VAL A 360 -8.851 -35.964 30.045 1.00 62.79 C ANISOU 2142 CG2 VAL A 360 7703 7487 8668 2393 1624 -3205 C ATOM 2143 N SER A 361 -8.464 -31.330 29.718 1.00 62.35 N ANISOU 2143 N SER A 361 7092 8349 8249 1807 1542 -3016 N ATOM 2144 CA SER A 361 -7.960 -30.055 29.200 1.00 61.27 C ANISOU 2144 CA SER A 361 6826 8472 7984 1641 1581 -3005 C ATOM 2145 C SER A 361 -7.030 -29.355 30.197 1.00 60.53 C ANISOU 2145 C SER A 361 6493 8558 7950 1699 1549 -2878 C ATOM 2146 O SER A 361 -5.884 -28.999 29.871 1.00 61.29 O ANISOU 2146 O SER A 361 6449 8820 8018 1712 1634 -2909 O ATOM 2147 CB SER A 361 -9.125 -29.130 28.839 1.00 59.21 C ANISOU 2147 CB SER A 361 6637 8249 7614 1393 1514 -2989 C ATOM 2148 OG SER A 361 -8.657 -27.859 28.421 1.00 58.51 O ANISOU 2148 OG SER A 361 6440 8385 7406 1237 1553 -2959 O ATOM 2149 N ALA A 362 -7.535 -29.169 31.414 1.00 71.49 N ANISOU 2149 N ALA A 362 7836 9908 9417 1729 1426 -2743 N ATOM 2150 CA ALA A 362 -6.791 -28.506 32.481 1.00 71.12 C ANISOU 2150 CA ALA A 362 7589 10015 9416 1774 1363 -2624 C ATOM 2151 C ALA A 362 -5.467 -29.206 32.765 1.00 73.90 C ANISOU 2151 C ALA A 362 7815 10403 9858 1995 1413 -2648 C ATOM 2152 O ALA A 362 -4.496 -28.571 33.179 1.00 73.45 O ANISOU 2152 O ALA A 362 7561 10535 9809 1998 1400 -2617 O ATOM 2153 CB ALA A 362 -7.634 -28.430 33.745 1.00 66.38 C ANISOU 2153 CB ALA A 362 7010 9330 8882 1806 1232 -2484 C ATOM 2154 N ALA A 363 -5.431 -30.515 32.539 1.00 67.13 N ANISOU 2154 N ALA A 363 7073 9358 9074 2178 1468 -2712 N ATOM 2155 CA ALA A 363 -4.198 -31.275 32.708 1.00 69.92 C ANISOU 2155 CA ALA A 363 7317 9726 9523 2410 1531 -2742 C ATOM 2156 C ALA A 363 -3.332 -31.249 31.448 1.00 72.08 C ANISOU 2156 C ALA A 363 7548 10108 9731 2383 1693 -2887 C ATOM 2157 O ALA A 363 -2.130 -31.507 31.509 1.00 74.50 O ANISOU 2157 O ALA A 363 7688 10514 10103 2530 1756 -2915 O ATOM 2158 CB ALA A 363 -4.509 -32.709 33.112 1.00 71.44 C ANISOU 2158 CB ALA A 363 7662 9644 9837 2639 1528 -2733 C ATOM 2159 N ILE A 364 -3.944 -30.932 30.310 1.00 76.83 N ANISOU 2159 N ILE A 364 8294 10697 10202 2199 1760 -2980 N ATOM 2160 CA ILE A 364 -3.241 -30.973 29.030 1.00 79.01 C ANISOU 2160 CA ILE A 364 8575 11052 10391 2173 1929 -3122 C ATOM 2161 C ILE A 364 -2.547 -29.652 28.725 1.00 78.76 C ANISOU 2161 C ILE A 364 8356 11290 10277 1999 1970 -3111 C ATOM 2162 O ILE A 364 -1.645 -29.602 27.890 1.00 82.05 O ANISOU 2162 O ILE A 364 8705 11817 10652 2010 2120 -3206 O ATOM 2163 CB ILE A 364 -4.170 -31.364 27.849 1.00 78.33 C ANISOU 2163 CB ILE A 364 8758 10824 10179 2062 1987 -3243 C ATOM 2164 CG1 ILE A 364 -3.414 -32.214 26.825 1.00 81.64 C ANISOU 2164 CG1 ILE A 364 9248 11207 10564 2185 2168 -3400 C ATOM 2165 CG2 ILE A 364 -4.772 -30.132 27.184 1.00 76.80 C ANISOU 2165 CG2 ILE A 364 8593 10765 9823 1773 1966 -3235 C ATOM 2166 CD1 ILE A 364 -3.098 -33.613 27.305 1.00 84.59 C ANISOU 2166 CD1 ILE A 364 9678 11374 11089 2473 2200 -3429 C ATOM 2167 N ASN A 365 -2.968 -28.584 29.397 1.00 89.96 N ANISOU 2167 N ASN A 365 9700 12807 11674 1839 1849 -3000 N ATOM 2168 CA ASN A 365 -2.285 -27.297 29.233 1.00 89.99 C ANISOU 2168 CA ASN A 365 9530 13046 11615 1669 1883 -2986 C ATOM 2169 C ASN A 365 -0.759 -27.299 29.459 1.00 92.48 C ANISOU 2169 C ASN A 365 9594 13527 12018 1790 1953 -3018 C ATOM 2170 O ASN A 365 -0.016 -26.820 28.603 1.00 94.09 O ANISOU 2170 O ASN A 365 9718 13873 12158 1701 2091 -3094 O ATOM 2171 CB ASN A 365 -2.962 -26.189 30.052 1.00 88.21 C ANISOU 2171 CB ASN A 365 9272 12876 11366 1499 1739 -2862 C ATOM 2172 CG ASN A 365 -4.068 -25.493 29.285 1.00 86.34 C ANISOU 2172 CG ASN A 365 9211 12607 10989 1272 1741 -2860 C ATOM 2173 OD1 ASN A 365 -4.149 -25.597 28.061 1.00 86.54 O ANISOU 2173 OD1 ASN A 365 9360 12613 10908 1207 1853 -2956 O ATOM 2174 ND2 ASN A 365 -4.922 -24.770 30.001 1.00 84.41 N ANISOU 2174 ND2 ASN A 365 8979 12359 10733 1156 1618 -2752 N ATOM 2175 N PRO A 366 -0.281 -27.842 30.598 1.00 78.19 N ANISOU 2175 N PRO A 366 7654 11704 10351 1993 1859 -2960 N ATOM 2176 CA PRO A 366 1.166 -27.753 30.834 1.00 80.14 C ANISOU 2176 CA PRO A 366 7633 12134 10683 2095 1909 -2994 C ATOM 2177 C PRO A 366 1.997 -28.802 30.091 1.00 82.95 C ANISOU 2177 C PRO A 366 7968 12453 11094 2300 2079 -3107 C ATOM 2178 O PRO A 366 3.157 -28.534 29.778 1.00 85.64 O ANISOU 2178 O PRO A 366 8103 12973 11464 2316 2186 -3171 O ATOM 2179 CB PRO A 366 1.281 -27.973 32.343 1.00 80.37 C ANISOU 2179 CB PRO A 366 7549 12158 10830 2245 1729 -2887 C ATOM 2180 CG PRO A 366 0.140 -28.862 32.664 1.00 79.65 C ANISOU 2180 CG PRO A 366 7692 11814 10758 2346 1659 -2828 C ATOM 2181 CD PRO A 366 -0.982 -28.447 31.748 1.00 77.85 C ANISOU 2181 CD PRO A 366 7681 11503 10393 2127 1703 -2855 C ATOM 2182 N ILE A 367 1.422 -29.970 29.819 1.00 68.30 N ANISOU 2182 N ILE A 367 6322 10367 9260 2454 2110 -3137 N ATOM 2183 CA ILE A 367 2.163 -31.048 29.165 1.00 71.94 C ANISOU 2183 CA ILE A 367 6792 10762 9779 2674 2276 -3247 C ATOM 2184 C ILE A 367 2.553 -30.676 27.732 1.00 73.48 C ANISOU 2184 C ILE A 367 7017 11060 9843 2546 2480 -3376 C ATOM 2185 O ILE A 367 3.592 -31.108 27.230 1.00 76.93 O ANISOU 2185 O ILE A 367 7343 11562 10324 2689 2643 -3467 O ATOM 2186 CB ILE A 367 1.379 -32.386 29.192 1.00 72.26 C ANISOU 2186 CB ILE A 367 7090 10498 9866 2853 2267 -3261 C ATOM 2187 CG1 ILE A 367 2.227 -33.530 28.628 1.00 76.36 C ANISOU 2187 CG1 ILE A 367 7626 10934 10453 3098 2451 -3380 C ATOM 2188 CG2 ILE A 367 0.074 -32.266 28.433 1.00 69.88 C ANISOU 2188 CG2 ILE A 367 7071 10063 9418 2656 2255 -3291 C ATOM 2189 CD1 ILE A 367 1.477 -34.841 28.502 1.00 77.09 C ANISOU 2189 CD1 ILE A 367 8005 10704 10582 3255 2468 -3419 C ATOM 2190 N LEU A 368 1.727 -29.858 27.086 1.00 71.14 N ANISOU 2190 N LEU A 368 6866 10781 9382 2282 2474 -3379 N ATOM 2191 CA LEU A 368 2.014 -29.395 25.733 1.00 72.50 C ANISOU 2191 CA LEU A 368 7086 11058 9401 2135 2657 -3483 C ATOM 2192 C LEU A 368 3.218 -28.459 25.727 1.00 73.95 C ANISOU 2192 C LEU A 368 6980 11508 9610 2056 2736 -3483 C ATOM 2193 O LEU A 368 3.922 -28.342 24.724 1.00 76.59 O ANISOU 2193 O LEU A 368 7274 11948 9878 2034 2935 -3580 O ATOM 2194 CB LEU A 368 0.796 -28.688 25.134 1.00 69.66 C ANISOU 2194 CB LEU A 368 6948 10657 8864 1871 2606 -3464 C ATOM 2195 CG LEU A 368 -0.443 -29.553 24.897 1.00 68.61 C ANISOU 2195 CG LEU A 368 7112 10274 8681 1905 2545 -3496 C ATOM 2196 CD1 LEU A 368 -1.591 -28.711 24.362 1.00 65.93 C ANISOU 2196 CD1 LEU A 368 6943 9933 8176 1634 2477 -3467 C ATOM 2197 CD2 LEU A 368 -0.126 -30.699 23.951 1.00 71.92 C ANISOU 2197 CD2 LEU A 368 7684 10581 9060 2064 2714 -3650 C ATOM 2198 N TYR A 369 3.449 -27.797 26.856 1.00 87.89 N ANISOU 2198 N TYR A 369 8547 13380 11467 2009 2583 -3380 N ATOM 2199 CA TYR A 369 4.575 -26.882 26.991 1.00 90.02 C ANISOU 2199 CA TYR A 369 8529 13899 11775 1919 2632 -3385 C ATOM 2200 C TYR A 369 5.872 -27.665 27.177 1.00 94.20 C ANISOU 2200 C TYR A 369 8825 14507 12460 2180 2724 -3447 C ATOM 2201 O TYR A 369 6.962 -27.145 26.942 1.00 97.33 O ANISOU 2201 O TYR A 369 8985 15109 12886 2137 2839 -3498 O ATOM 2202 CB TYR A 369 4.362 -25.932 28.173 1.00 82.88 C ANISOU 2202 CB TYR A 369 7506 13074 10911 1791 2426 -3272 C ATOM 2203 CG TYR A 369 3.059 -25.160 28.140 1.00 78.85 C ANISOU 2203 CG TYR A 369 7208 12480 10270 1559 2326 -3197 C ATOM 2204 CD1 TYR A 369 2.429 -24.864 26.938 1.00 78.40 C ANISOU 2204 CD1 TYR A 369 7363 12373 10051 1396 2439 -3237 C ATOM 2205 CD2 TYR A 369 2.461 -24.726 29.316 1.00 76.39 C ANISOU 2205 CD2 TYR A 369 6886 12144 9994 1514 2121 -3086 C ATOM 2206 CE1 TYR A 369 1.239 -24.160 26.909 1.00 75.34 C ANISOU 2206 CE1 TYR A 369 7155 11915 9554 1199 2344 -3164 C ATOM 2207 CE2 TYR A 369 1.273 -24.020 29.297 1.00 73.21 C ANISOU 2207 CE2 TYR A 369 6665 11666 9485 1318 2041 -3016 C ATOM 2208 CZ TYR A 369 0.666 -23.741 28.091 1.00 72.60 C ANISOU 2208 CZ TYR A 369 6781 11541 9262 1164 2150 -3054 C ATOM 2209 OH TYR A 369 -0.517 -23.039 28.067 1.00 70.24 O ANISOU 2209 OH TYR A 369 6650 11172 8865 983 2067 -2980 O ATOM 2210 N ASN A 370 5.742 -28.917 27.606 1.00122.94 N ANISOU 2210 N ASN A 370 12530 17975 16205 2451 2677 -3441 N ATOM 2211 CA ASN A 370 6.895 -29.790 27.796 1.00126.31 C ANISOU 2211 CA ASN A 370 12756 18442 16792 2737 2762 -3492 C ATOM 2212 C ASN A 370 7.247 -30.565 26.530 1.00128.88 C ANISOU 2212 C ASN A 370 13186 18711 17071 2850 3018 -3627 C ATOM 2213 O ASN A 370 8.419 -30.817 26.252 1.00132.67 O ANISOU 2213 O ASN A 370 13449 19324 17635 2984 3172 -3698 O ATOM 2214 CB ASN A 370 6.645 -30.771 28.945 1.00125.51 C ANISOU 2214 CB ASN A 370 12684 18168 16834 2995 2599 -3413 C ATOM 2215 CG ASN A 370 6.617 -30.090 30.300 1.00123.97 C ANISOU 2215 CG ASN A 370 12323 18076 16705 2948 2360 -3291 C ATOM 2216 OD1 ASN A 370 7.349 -29.132 30.542 1.00125.11 O ANISOU 2216 OD1 ASN A 370 12216 18457 16861 2825 2334 -3292 O ATOM 2217 ND2 ASN A 370 5.770 -30.588 31.194 1.00121.77 N ANISOU 2217 ND2 ASN A 370 12189 17615 16463 3044 2189 -3191 N ATOM 2218 N LEU A 371 6.224 -30.933 25.764 1.00138.65 N ANISOU 2218 N LEU A 371 14754 19754 18170 2796 3063 -3668 N ATOM 2219 CA LEU A 371 6.403 -31.769 24.579 1.00141.92 C ANISOU 2219 CA LEU A 371 15332 20075 18515 2918 3291 -3806 C ATOM 2220 C LEU A 371 7.177 -31.083 23.454 1.00144.50 C ANISOU 2220 C LEU A 371 15561 20613 18728 2784 3516 -3899 C ATOM 2221 O LEU A 371 7.664 -31.745 22.538 1.00149.21 O ANISOU 2221 O LEU A 371 16212 21189 19292 2927 3735 -4020 O ATOM 2222 CB LEU A 371 5.050 -32.261 24.058 1.00136.40 C ANISOU 2222 CB LEU A 371 15023 19126 17676 2859 3257 -3837 C ATOM 2223 CG LEU A 371 4.324 -33.289 24.927 1.00135.08 C ANISOU 2223 CG LEU A 371 15004 18694 17626 3048 3110 -3785 C ATOM 2224 CD1 LEU A 371 3.002 -33.691 24.293 1.00133.40 C ANISOU 2224 CD1 LEU A 371 15166 18254 17266 2952 3084 -3838 C ATOM 2225 CD2 LEU A 371 5.204 -34.508 25.160 1.00139.18 C ANISOU 2225 CD2 LEU A 371 15441 19122 18317 3396 3217 -3836 C ATOM 2226 N VAL A 372 7.292 -29.761 23.525 1.00110.63 N ANISOU 2226 N VAL A 372 11139 16519 14376 2514 3474 -3843 N ATOM 2227 CA VAL A 372 8.023 -29.009 22.510 1.00113.42 C ANISOU 2227 CA VAL A 372 11394 17076 14624 2362 3690 -3914 C ATOM 2228 C VAL A 372 9.532 -29.107 22.715 1.00117.80 C ANISOU 2228 C VAL A 372 11587 17826 15348 2521 3820 -3956 C ATOM 2229 O VAL A 372 10.309 -28.545 21.942 1.00120.73 O ANISOU 2229 O VAL A 372 11832 18380 15662 2424 4025 -4020 O ATOM 2230 CB VAL A 372 7.608 -27.528 22.491 1.00108.19 C ANISOU 2230 CB VAL A 372 10724 16538 13845 2011 3613 -3837 C ATOM 2231 CG1 VAL A 372 6.141 -27.398 22.126 1.00104.76 C ANISOU 2231 CG1 VAL A 372 10641 15930 13236 1855 3513 -3803 C ATOM 2232 CG2 VAL A 372 7.888 -26.883 23.838 1.00106.48 C ANISOU 2232 CG2 VAL A 372 10250 16427 13783 1964 3409 -3731 C ATOM 2233 N SER A 373 9.931 -29.819 23.767 1.00193.06 N ANISOU 2233 N SER A 373 20949 27320 25087 2765 3697 -3916 N ATOM 2234 CA SER A 373 11.339 -30.049 24.089 1.00197.87 C ANISOU 2234 CA SER A 373 21194 28103 25885 2958 3787 -3950 C ATOM 2235 C SER A 373 12.119 -28.757 24.318 1.00198.86 C ANISOU 2235 C SER A 373 21004 28516 26039 2733 3783 -3927 C ATOM 2236 O SER A 373 13.340 -28.724 24.161 1.00203.10 O ANISOU 2236 O SER A 373 21235 29244 26690 2822 3924 -3983 O ATOM 2237 CB SER A 373 12.016 -30.899 23.008 1.00198.18 C ANISOU 2237 CB SER A 373 21259 28124 25916 3166 4081 -4084 C ATOM 2238 OG SER A 373 13.374 -31.142 23.329 1.00201.26 O ANISOU 2238 OG SER A 373 21278 28684 26509 3372 4169 -4113 O ATOM 2239 N ALA A 374 11.411 -27.697 24.693 1.00152.70 N ANISOU 2239 N ALA A 374 15231 22693 20093 2442 3627 -3848 N ATOM 2240 CA ALA A 374 12.049 -26.424 25.000 1.00152.40 C ANISOU 2240 CA ALA A 374 14926 22897 20080 2207 3600 -3825 C ATOM 2241 C ALA A 374 12.745 -26.505 26.352 1.00153.50 C ANISOU 2241 C ALA A 374 14755 23139 20428 2350 3405 -3778 C ATOM 2242 O ALA A 374 12.665 -27.523 27.040 1.00153.21 O ANISOU 2242 O ALA A 374 14741 22972 20499 2618 3280 -3743 O ATOM 2243 CB ALA A 374 11.025 -25.302 24.996 1.00151.05 C ANISOU 2243 CB ALA A 374 14954 22689 19748 1878 3485 -3752 C ATOM 2244 N ASN A 375 13.423 -25.428 26.733 1.00131.09 N ANISOU 2244 N ASN A 375 11636 20532 17640 2168 3375 -3777 N ATOM 2245 CA ASN A 375 14.098 -25.375 28.025 1.00132.08 C ANISOU 2245 CA ASN A 375 11456 20786 17943 2277 3174 -3742 C ATOM 2246 C ASN A 375 13.102 -25.324 29.180 1.00128.03 C ANISOU 2246 C ASN A 375 11100 20137 17410 2267 2871 -3631 C ATOM 2247 O ASN A 375 13.469 -25.506 30.345 1.00127.81 O ANISOU 2247 O ASN A 375 10883 20174 17507 2402 2672 -3590 O ATOM 2248 CB ASN A 375 15.055 -24.183 28.084 1.00133.69 C ANISOU 2248 CB ASN A 375 11336 21269 18191 2049 3220 -3783 C ATOM 2249 CG ASN A 375 16.105 -24.228 26.991 1.00137.71 C ANISOU 2249 CG ASN A 375 11667 21929 18730 2058 3535 -3886 C ATOM 2250 OD1 ASN A 375 17.153 -24.855 27.147 1.00142.35 O ANISOU 2250 OD1 ASN A 375 11973 22630 19485 2299 3606 -3936 O ATOM 2251 ND2 ASN A 375 15.828 -23.564 25.875 1.00136.47 N ANISOU 2251 ND2 ASN A 375 11672 21775 18407 1802 3730 -3914 N ATOM 2252 N PHE A 376 11.838 -25.078 28.845 1.00160.84 N ANISOU 2252 N PHE A 376 15599 24111 21401 2111 2841 -3583 N ATOM 2253 CA PHE A 376 10.762 -25.109 29.826 1.00157.46 C ANISOU 2253 CA PHE A 376 15356 23529 20943 2114 2587 -3477 C ATOM 2254 C PHE A 376 10.639 -26.496 30.438 1.00157.69 C ANISOU 2254 C PHE A 376 15430 23400 21085 2463 2493 -3440 C ATOM 2255 O PHE A 376 10.282 -26.633 31.603 1.00156.88 O ANISOU 2255 O PHE A 376 15330 23248 21028 2545 2266 -3353 O ATOM 2256 CB PHE A 376 9.429 -24.700 29.194 1.00153.65 C ANISOU 2256 CB PHE A 376 15229 22877 20276 1903 2600 -3438 C ATOM 2257 CG PHE A 376 8.252 -24.842 30.121 1.00150.03 C ANISOU 2257 CG PHE A 376 14973 22241 19793 1931 2369 -3329 C ATOM 2258 CD1 PHE A 376 7.935 -23.837 31.019 1.00147.26 C ANISOU 2258 CD1 PHE A 376 14582 21952 19419 1762 2184 -3260 C ATOM 2259 CD2 PHE A 376 7.463 -25.983 30.096 1.00149.39 C ANISOU 2259 CD2 PHE A 376 15124 21927 19712 2125 2349 -3302 C ATOM 2260 CE1 PHE A 376 6.856 -23.966 31.874 1.00143.99 C ANISOU 2260 CE1 PHE A 376 14350 21381 18980 1795 1989 -3158 C ATOM 2261 CE2 PHE A 376 6.386 -26.117 30.951 1.00146.39 C ANISOU 2261 CE2 PHE A 376 14919 21387 19316 2147 2152 -3198 C ATOM 2262 CZ PHE A 376 6.080 -25.107 31.838 1.00143.98 C ANISOU 2262 CZ PHE A 376 14566 21155 18985 1985 1975 -3122 C ATOM 2263 N ARG A 377 10.921 -27.523 29.643 1.00124.82 N ANISOU 2263 N ARG A 377 11319 19150 16959 2669 2679 -3507 N ATOM 2264 CA ARG A 377 10.889 -28.896 30.131 1.00125.53 C ANISOU 2264 CA ARG A 377 11459 19069 17170 3013 2623 -3480 C ATOM 2265 C ARG A 377 12.086 -29.149 31.040 1.00128.35 C ANISOU 2265 C ARG A 377 11455 19595 17719 3227 2535 -3473 C ATOM 2266 O ARG A 377 11.990 -29.886 32.023 1.00126.95 O ANISOU 2266 O ARG A 377 11274 19320 17643 3458 2364 -3398 O ATOM 2267 CB ARG A 377 10.887 -29.884 28.963 1.00127.77 C ANISOU 2267 CB ARG A 377 11913 19204 17432 3167 2867 -3571 C ATOM 2268 CG ARG A 377 10.723 -31.338 29.378 1.00128.98 C ANISOU 2268 CG ARG A 377 12183 19124 17701 3509 2829 -3547 C ATOM 2269 CD ARG A 377 10.637 -32.256 28.168 1.00130.84 C ANISOU 2269 CD ARG A 377 12628 19196 17892 3636 3079 -3656 C ATOM 2270 NE ARG A 377 11.853 -32.216 27.361 1.00135.17 N ANISOU 2270 NE ARG A 377 12945 19928 18488 3706 3319 -3767 N ATOM 2271 CZ ARG A 377 12.031 -32.913 26.243 1.00138.46 C ANISOU 2271 CZ ARG A 377 13497 20257 18857 3818 3575 -3882 C ATOM 2272 NH1 ARG A 377 11.069 -33.708 25.794 1.00137.99 N ANISOU 2272 NH1 ARG A 377 13810 19923 18697 3864 3610 -3910 N ATOM 2273 NH2 ARG A 377 13.171 -32.816 25.573 1.00142.93 N ANISOU 2273 NH2 ARG A 377 13827 21010 19470 3883 3799 -3976 N ATOM 2274 N GLN A 378 13.211 -28.526 30.703 1.00130.59 N ANISOU 2274 N GLN A 378 11432 20135 18050 3145 2650 -3549 N ATOM 2275 CA GLN A 378 14.425 -28.635 31.501 1.00134.85 C ANISOU 2275 CA GLN A 378 11584 20879 18772 3315 2565 -3555 C ATOM 2276 C GLN A 378 14.195 -28.055 32.893 1.00132.80 C ANISOU 2276 C GLN A 378 11251 20689 18518 3244 2255 -3462 C ATOM 2277 O GLN A 378 14.495 -28.696 33.903 1.00133.75 O ANISOU 2277 O GLN A 378 11256 20804 18757 3494 2078 -3403 O ATOM 2278 CB GLN A 378 15.582 -27.907 30.814 1.00131.43 C ANISOU 2278 CB GLN A 378 10842 20719 18375 3177 2759 -3658 C ATOM 2279 CG GLN A 378 16.938 -28.154 31.451 1.00136.37 C ANISOU 2279 CG GLN A 378 11038 21566 19211 3384 2715 -3684 C ATOM 2280 CD GLN A 378 17.428 -29.572 31.241 1.00139.63 C ANISOU 2280 CD GLN A 378 11408 21873 19772 3782 2830 -3707 C ATOM 2281 OE1 GLN A 378 17.668 -29.996 30.111 1.00141.60 O ANISOU 2281 OE1 GLN A 378 11707 22081 20011 3844 3110 -3791 O ATOM 2282 NE2 GLN A 378 17.574 -30.315 32.331 1.00140.02 N ANISOU 2282 NE2 GLN A 378 11378 21869 19953 4061 2618 -3632 N ATOM 2283 N VAL A 379 13.651 -26.842 32.941 1.00171.07 N ANISOU 2283 N VAL A 379 16179 25594 23228 2909 2193 -3447 N ATOM 2284 CA VAL A 379 13.357 -26.202 34.219 1.00167.95 C ANISOU 2284 CA VAL A 379 15747 25259 22810 2819 1916 -3370 C ATOM 2285 C VAL A 379 12.149 -26.848 34.900 1.00163.89 C ANISOU 2285 C VAL A 379 15538 24489 22243 2943 1746 -3255 C ATOM 2286 O VAL A 379 11.956 -26.701 36.107 1.00162.31 O ANISOU 2286 O VAL A 379 15311 24314 22047 2982 1507 -3179 O ATOM 2287 CB VAL A 379 13.131 -24.682 34.068 1.00161.96 C ANISOU 2287 CB VAL A 379 14994 24619 21924 2426 1915 -3394 C ATOM 2288 CG1 VAL A 379 14.352 -24.025 33.443 1.00164.65 C ANISOU 2288 CG1 VAL A 379 15028 25209 22324 2288 2092 -3503 C ATOM 2289 CG2 VAL A 379 11.890 -24.403 33.241 1.00158.74 C ANISOU 2289 CG2 VAL A 379 14957 24010 21349 2234 2008 -3366 C ATOM 2290 N PHE A 380 11.344 -27.565 34.120 1.00138.85 N ANISOU 2290 N PHE A 380 12659 21078 19019 3000 1875 -3247 N ATOM 2291 CA PHE A 380 10.207 -28.299 34.663 1.00136.39 C ANISOU 2291 CA PHE A 380 12637 20507 18677 3125 1746 -3143 C ATOM 2292 C PHE A 380 10.712 -29.482 35.471 1.00139.20 C ANISOU 2292 C PHE A 380 12893 20806 19190 3494 1646 -3096 C ATOM 2293 O PHE A 380 10.254 -29.722 36.585 1.00135.95 O ANISOU 2293 O PHE A 380 12551 20320 18786 3594 1434 -2990 O ATOM 2294 CB PHE A 380 9.283 -28.788 33.545 1.00134.46 C ANISOU 2294 CB PHE A 380 12718 20029 18344 3085 1919 -3167 C ATOM 2295 CG PHE A 380 8.042 -29.479 34.039 1.00132.06 C ANISOU 2295 CG PHE A 380 12715 19453 18010 3176 1801 -3067 C ATOM 2296 CD1 PHE A 380 6.919 -28.748 34.386 1.00128.31 C ANISOU 2296 CD1 PHE A 380 12425 18917 17412 2957 1679 -2992 C ATOM 2297 CD2 PHE A 380 7.997 -30.860 34.151 1.00133.49 C ANISOU 2297 CD2 PHE A 380 12995 19432 18295 3478 1824 -3049 C ATOM 2298 CE1 PHE A 380 5.776 -29.378 34.840 1.00126.00 C ANISOU 2298 CE1 PHE A 380 12393 18381 17101 3035 1584 -2899 C ATOM 2299 CE2 PHE A 380 6.857 -31.496 34.604 1.00130.92 C ANISOU 2299 CE2 PHE A 380 12946 18848 17950 3548 1727 -2958 C ATOM 2300 CZ PHE A 380 5.745 -30.754 34.949 1.00127.15 C ANISOU 2300 CZ PHE A 380 12634 18326 17350 3323 1608 -2882 C ATOM 2301 N LEU A 381 11.656 -30.222 34.897 1.00155.11 N ANISOU 2301 N LEU A 381 14751 22853 21329 3703 1807 -3171 N ATOM 2302 CA LEU A 381 12.289 -31.327 35.605 1.00158.28 C ANISOU 2302 CA LEU A 381 15023 23215 21902 4070 1725 -3130 C ATOM 2303 C LEU A 381 13.130 -30.797 36.760 1.00159.80 C ANISOU 2303 C LEU A 381 14891 23665 22161 4103 1503 -3095 C ATOM 2304 O LEU A 381 13.238 -31.436 37.808 1.00160.22 O ANISOU 2304 O LEU A 381 14908 23675 22292 4346 1311 -3005 O ATOM 2305 CB LEU A 381 13.154 -32.160 34.656 1.00160.25 C ANISOU 2305 CB LEU A 381 15162 23452 22275 4283 1971 -3231 C ATOM 2306 CG LEU A 381 12.492 -33.353 33.959 1.00159.91 C ANISOU 2306 CG LEU A 381 15436 23085 22238 4455 2128 -3244 C ATOM 2307 CD1 LEU A 381 11.351 -32.911 33.054 1.00156.21 C ANISOU 2307 CD1 LEU A 381 15292 22484 21577 4175 2238 -3276 C ATOM 2308 CD2 LEU A 381 13.522 -34.155 33.175 1.00164.72 C ANISOU 2308 CD2 LEU A 381 15891 23708 22986 4701 2364 -3348 C ATOM 2309 N SER A 382 13.719 -29.620 36.562 1.00167.77 N ANISOU 2309 N SER A 382 15674 24939 23132 3851 1529 -3169 N ATOM 2310 CA SER A 382 14.532 -28.985 37.594 1.00168.74 C ANISOU 2310 CA SER A 382 15483 25327 23304 3834 1322 -3160 C ATOM 2311 C SER A 382 13.700 -28.613 38.819 1.00164.78 C ANISOU 2311 C SER A 382 15135 24777 22695 3774 1048 -3050 C ATOM 2312 O SER A 382 14.150 -28.765 39.955 1.00164.71 O ANISOU 2312 O SER A 382 14968 24872 22740 3937 824 -2995 O ATOM 2313 CB SER A 382 15.228 -27.741 37.037 1.00175.63 C ANISOU 2313 CB SER A 382 16120 26463 24148 3530 1430 -3271 C ATOM 2314 OG SER A 382 16.060 -28.071 35.938 1.00178.96 O ANISOU 2314 OG SER A 382 16380 26950 24665 3593 1695 -3370 O ATOM 2315 N THR A 383 12.486 -28.126 38.582 1.00156.39 N ANISOU 2315 N THR A 383 14381 23562 21478 3545 1066 -3017 N ATOM 2316 CA THR A 383 11.595 -27.722 39.666 1.00153.04 C ANISOU 2316 CA THR A 383 14123 23082 20940 3472 838 -2915 C ATOM 2317 C THR A 383 10.879 -28.932 40.266 1.00151.70 C ANISOU 2317 C THR A 383 14187 22655 20794 3750 741 -2790 C ATOM 2318 O THR A 383 10.554 -28.951 41.454 1.00149.37 O ANISOU 2318 O THR A 383 13939 22353 20459 3831 518 -2691 O ATOM 2319 CB THR A 383 10.555 -26.691 39.181 1.00144.68 C ANISOU 2319 CB THR A 383 13292 21961 19718 3121 901 -2924 C ATOM 2320 OG1 THR A 383 11.220 -25.626 38.490 1.00145.74 O ANISOU 2320 OG1 THR A 383 13235 22304 19836 2861 1022 -3037 O ATOM 2321 CG2 THR A 383 9.773 -26.116 40.355 1.00141.70 C ANISOU 2321 CG2 THR A 383 13039 21569 19230 3036 675 -2833 C ATOM 2322 N LEU A 384 10.641 -29.943 39.439 1.00159.10 N ANISOU 2322 N LEU A 384 15280 23376 21794 3895 916 -2798 N ATOM 2323 CA LEU A 384 9.971 -31.158 39.888 1.00158.62 C ANISOU 2323 CA LEU A 384 15455 23039 21774 4153 858 -2690 C ATOM 2324 C LEU A 384 10.904 -32.003 40.749 1.00162.25 C ANISOU 2324 C LEU A 384 15716 23552 22379 4501 721 -2638 C ATOM 2325 O LEU A 384 10.455 -32.736 41.631 1.00160.44 O ANISOU 2325 O LEU A 384 15636 23162 22163 4702 572 -2514 O ATOM 2326 CB LEU A 384 9.474 -31.970 38.689 1.00152.56 C ANISOU 2326 CB LEU A 384 14910 22023 21034 4194 1098 -2737 C ATOM 2327 CG LEU A 384 8.621 -33.205 38.987 1.00151.80 C ANISOU 2327 CG LEU A 384 15104 21594 20979 4412 1076 -2641 C ATOM 2328 CD1 LEU A 384 7.372 -32.819 39.763 1.00147.55 C ANISOU 2328 CD1 LEU A 384 14799 20947 20316 4275 915 -2522 C ATOM 2329 CD2 LEU A 384 8.254 -33.924 37.698 1.00151.86 C ANISOU 2329 CD2 LEU A 384 15313 21383 21005 4425 1327 -2726 C ATOM 2330 N ALA A 385 12.203 -31.893 40.488 1.00155.42 N ANISOU 2330 N ALA A 385 14513 22916 21624 4574 772 -2729 N ATOM 2331 CA ALA A 385 13.204 -32.639 41.244 1.00159.33 C ANISOU 2331 CA ALA A 385 14775 23494 22270 4910 640 -2687 C ATOM 2332 C ALA A 385 13.228 -32.222 42.712 1.00158.37 C ANISOU 2332 C ALA A 385 14579 23513 22079 4933 327 -2589 C ATOM 2333 O ALA A 385 13.261 -33.069 43.605 1.00158.31 O ANISOU 2333 O ALA A 385 14615 23413 22121 5219 160 -2473 O ATOM 2334 CB ALA A 385 14.581 -32.466 40.619 1.00157.01 C ANISOU 2334 CB ALA A 385 14105 23443 22109 4950 770 -2813 C ATOM 2335 N CYS A 386 13.208 -30.916 42.958 1.00161.61 N ANISOU 2335 N CYS A 386 14893 24141 22369 4633 250 -2636 N ATOM 2336 CA CYS A 386 13.220 -30.398 44.322 1.00161.82 C ANISOU 2336 CA CYS A 386 14858 24321 22306 4623 -38 -2565 C ATOM 2337 C CYS A 386 11.844 -30.503 44.977 1.00158.18 C ANISOU 2337 C CYS A 386 14766 23637 21697 4593 -144 -2435 C ATOM 2338 O CYS A 386 11.219 -29.494 45.306 1.00153.96 O ANISOU 2338 O CYS A 386 14324 23163 21012 4333 -209 -2438 O ATOM 2339 CB CYS A 386 13.729 -28.953 44.355 1.00160.29 C ANISOU 2339 CB CYS A 386 14428 24429 22044 4307 -70 -2678 C ATOM 2340 SG CYS A 386 12.882 -27.813 43.234 1.00155.55 S ANISOU 2340 SG CYS A 386 14016 23770 21314 3870 153 -2766 S ATOM 2341 N LEU A 387 11.382 -31.735 45.167 1.00131.56 N ANISOU 2341 N LEU A 387 11605 20001 18379 4864 -152 -2321 N ATOM 2342 CA LEU A 387 10.083 -31.987 45.779 1.00128.25 C ANISOU 2342 CA LEU A 387 11537 19349 17842 4865 -236 -2185 C ATOM 2343 C LEU A 387 10.078 -33.349 46.465 1.00130.10 C ANISOU 2343 C LEU A 387 11886 19388 18159 5241 -340 -2042 C ATOM 2344 O LEU A 387 10.703 -34.297 45.989 1.00132.15 O ANISOU 2344 O LEU A 387 12076 19551 18583 5471 -238 -2062 O ATOM 2345 CB LEU A 387 8.972 -31.906 44.725 1.00123.05 C ANISOU 2345 CB LEU A 387 11152 18462 17141 4653 -15 -2215 C ATOM 2346 CG LEU A 387 7.507 -31.923 45.179 1.00119.21 C ANISOU 2346 CG LEU A 387 11016 17746 16531 4579 -64 -2094 C ATOM 2347 CD1 LEU A 387 6.950 -33.341 45.278 1.00120.13 C ANISOU 2347 CD1 LEU A 387 11375 17534 16735 4845 -33 -1983 C ATOM 2348 CD2 LEU A 387 7.324 -31.164 46.490 1.00118.23 C ANISOU 2348 CD2 LEU A 387 10880 17778 16264 4530 -306 -2015 C TER 2349 LEU A 387 ATOM 2350 N PRO B 51 -24.319 23.598 44.619 1.00111.89 N ANISOU 2350 N PRO B 51 19121 8985 14405 -325 3107 -902 N ATOM 2351 CA PRO B 51 -25.396 24.579 44.453 1.00114.15 C ANISOU 2351 CA PRO B 51 19547 9032 14791 36 3128 -679 C ATOM 2352 C PRO B 51 -24.903 25.788 43.671 1.00117.96 C ANISOU 2352 C PRO B 51 20347 9197 15275 -124 3187 -608 C ATOM 2353 O PRO B 51 -25.006 25.837 42.446 1.00118.64 O ANISOU 2353 O PRO B 51 20526 9189 15363 -142 3161 -373 O ATOM 2354 CB PRO B 51 -25.709 25.004 45.895 1.00112.74 C ANISOU 2354 CB PRO B 51 19327 8862 14647 282 3173 -833 C ATOM 2355 CG PRO B 51 -24.924 24.072 46.788 1.00110.26 C ANISOU 2355 CG PRO B 51 18821 8835 14236 89 3150 -1100 C ATOM 2356 CD PRO B 51 -23.759 23.633 45.977 1.00109.70 C ANISOU 2356 CD PRO B 51 18778 8820 14084 -353 3126 -1185 C ATOM 2357 N ASN B 52 -24.373 26.762 44.401 1.00107.58 N ANISOU 2357 N ASN B 52 19201 7723 13952 -242 3265 -809 N ATOM 2358 CA ASN B 52 -23.708 27.912 43.810 1.00111.45 C ANISOU 2358 CA ASN B 52 19990 7918 14439 -458 3334 -793 C ATOM 2359 C ASN B 52 -22.215 27.648 43.736 1.00111.51 C ANISOU 2359 C ASN B 52 19975 8044 14352 -956 3341 -963 C ATOM 2360 O ASN B 52 -21.460 28.428 43.156 1.00113.70 O ANISOU 2360 O ASN B 52 20456 8131 14614 -1216 3398 -951 O ATOM 2361 CB ASN B 52 -23.957 29.143 44.671 1.00113.16 C ANISOU 2361 CB ASN B 52 20399 7899 14700 -343 3415 -938 C ATOM 2362 CG ASN B 52 -23.626 28.900 46.135 1.00111.80 C ANISOU 2362 CG ASN B 52 20144 7882 14455 -542 3424 -1273 C ATOM 2363 OD1 ASN B 52 -24.099 27.932 46.735 1.00108.10 O ANISOU 2363 OD1 ASN B 52 19414 7728 13934 -551 3360 -1375 O ATOM 2364 ND2 ASN B 52 -22.803 29.772 46.713 1.00114.70 N ANISOU 2364 ND2 ASN B 52 20737 8031 14814 -703 3493 -1443 N ATOM 2365 N SER B 53 -21.807 26.517 44.306 1.00151.21 N ANISOU 2365 N SER B 53 24732 13401 19321 -1081 3280 -1119 N ATOM 2366 CA SER B 53 -20.395 26.194 44.503 1.00150.95 C ANISOU 2366 CA SER B 53 24603 13546 19206 -1533 3268 -1333 C ATOM 2367 C SER B 53 -19.596 25.997 43.213 1.00150.57 C ANISOU 2367 C SER B 53 24526 13562 19121 -1813 3268 -1195 C ATOM 2368 O SER B 53 -20.103 26.208 42.111 1.00153.53 O ANISOU 2368 O SER B 53 25062 13754 19519 -1719 3296 -935 O ATOM 2369 CB SER B 53 -20.251 24.966 45.409 1.00147.05 C ANISOU 2369 CB SER B 53 23812 13402 18656 -1542 3187 -1545 C ATOM 2370 OG SER B 53 -20.850 25.201 46.671 1.00148.58 O ANISOU 2370 OG SER B 53 24031 13562 18858 -1299 3195 -1676 O ATOM 2371 N ASP B 54 -18.350 25.557 43.368 1.00167.96 N ANISOU 2371 N ASP B 54 26508 16052 21258 -2149 3229 -1368 N ATOM 2372 CA ASP B 54 -17.405 25.440 42.260 1.00167.36 C ANISOU 2372 CA ASP B 54 26370 16083 21137 -2470 3247 -1285 C ATOM 2373 C ASP B 54 -17.855 24.461 41.175 1.00163.79 C ANISOU 2373 C ASP B 54 25758 15810 20667 -2341 3194 -1082 C ATOM 2374 O ASP B 54 -17.239 24.385 40.115 1.00163.54 O ANISOU 2374 O ASP B 54 25622 15937 20580 -2593 3202 -1023 O ATOM 2375 CB ASP B 54 -16.038 25.007 42.789 1.00168.85 C ANISOU 2375 CB ASP B 54 26342 16537 21275 -2872 3221 -1563 C ATOM 2376 CG ASP B 54 -15.566 25.854 43.950 1.00172.04 C ANISOU 2376 CG ASP B 54 26857 16821 21689 -2974 3235 -1800 C ATOM 2377 OD1 ASP B 54 -16.409 26.507 44.602 1.00176.21 O ANISOU 2377 OD1 ASP B 54 27690 17002 22260 -2896 3315 -1734 O ATOM 2378 OD2 ASP B 54 -14.346 25.861 44.210 1.00171.35 O ANISOU 2378 OD2 ASP B 54 26552 16992 21562 -3125 3157 -2050 O ATOM 2379 N LEU B 55 -18.924 23.717 41.446 1.00 74.48 N ANISOU 2379 N LEU B 55 14416 4482 9400 -1946 3143 -975 N ATOM 2380 CA LEU B 55 -19.432 22.699 40.529 1.00 71.16 C ANISOU 2380 CA LEU B 55 13810 4266 8961 -1780 3061 -770 C ATOM 2381 C LEU B 55 -19.740 23.233 39.134 1.00 73.05 C ANISOU 2381 C LEU B 55 14266 4307 9183 -1754 3095 -454 C ATOM 2382 O LEU B 55 -19.506 22.547 38.141 1.00 70.63 O ANISOU 2382 O LEU B 55 13770 4266 8799 -1784 3019 -307 O ATOM 2383 CB LEU B 55 -20.683 22.034 41.111 1.00 68.23 C ANISOU 2383 CB LEU B 55 13260 4024 8638 -1330 2963 -724 C ATOM 2384 CG LEU B 55 -20.549 20.934 42.172 1.00 64.11 C ANISOU 2384 CG LEU B 55 12355 3925 8080 -1306 2857 -921 C ATOM 2385 CD1 LEU B 55 -19.769 21.389 43.392 1.00 65.79 C ANISOU 2385 CD1 LEU B 55 12594 4140 8260 -1594 2906 -1251 C ATOM 2386 CD2 LEU B 55 -21.931 20.435 42.578 1.00 62.33 C ANISOU 2386 CD2 LEU B 55 12012 3754 7916 -866 2803 -854 C ATOM 2387 N ASP B 56 -20.252 24.459 39.067 1.00 99.74 N ANISOU 2387 N ASP B 56 17938 7361 12599 -1650 3152 -347 N ATOM 2388 CA ASP B 56 -20.604 25.084 37.793 1.00101.70 C ANISOU 2388 CA ASP B 56 18387 7445 12809 -1594 3158 -43 C ATOM 2389 C ASP B 56 -19.395 25.250 36.875 1.00102.88 C ANISOU 2389 C ASP B 56 18542 7696 12852 -2014 3218 -35 C ATOM 2390 O ASP B 56 -18.417 25.911 37.224 1.00102.74 O ANISOU 2390 O ASP B 56 18525 7686 12825 -2350 3296 -248 O ATOM 2391 CB ASP B 56 -21.292 26.436 38.018 1.00108.85 C ANISOU 2391 CB ASP B 56 19592 7982 13785 -1389 3204 45 C ATOM 2392 CG ASP B 56 -20.682 27.223 39.163 1.00111.20 C ANISOU 2392 CG ASP B 56 19984 8144 14122 -1575 3294 -235 C ATOM 2393 OD1 ASP B 56 -19.497 26.992 39.483 1.00111.03 O ANISOU 2393 OD1 ASP B 56 19847 8287 14052 -1951 3328 -455 O ATOM 2394 OD2 ASP B 56 -21.391 28.071 39.747 1.00113.92 O ANISOU 2394 OD2 ASP B 56 20506 8233 14544 -1341 3323 -236 O ATOM 2395 N VAL B 57 -19.470 24.636 35.700 1.00 87.82 N ANISOU 2395 N VAL B 57 16621 5890 10857 -1988 3175 210 N ATOM 2396 CA VAL B 57 -18.389 24.704 34.727 1.00 89.29 C ANISOU 2396 CA VAL B 57 16797 6202 10925 -2352 3241 239 C ATOM 2397 C VAL B 57 -18.775 25.629 33.573 1.00 92.74 C ANISOU 2397 C VAL B 57 17524 6413 11297 -2265 3257 536 C ATOM 2398 O VAL B 57 -19.938 25.688 33.173 1.00 92.41 O ANISOU 2398 O VAL B 57 17595 6243 11271 -1899 3166 769 O ATOM 2399 CB VAL B 57 -18.014 23.297 34.210 1.00 86.77 C ANISOU 2399 CB VAL B 57 16175 6273 10521 -2462 3188 231 C ATOM 2400 CG1 VAL B 57 -19.210 22.632 33.560 1.00 85.66 C ANISOU 2400 CG1 VAL B 57 16023 6178 10344 -2111 3066 498 C ATOM 2401 CG2 VAL B 57 -16.833 23.362 33.246 1.00 87.77 C ANISOU 2401 CG2 VAL B 57 16256 6564 10527 -2837 3275 229 C ATOM 2402 N ASN B 58 -17.795 26.361 33.054 1.00113.37 N ANISOU 2402 N ASN B 58 20247 8984 13843 -2594 3369 526 N ATOM 2403 CA ASN B 58 -18.045 27.375 32.039 1.00117.14 C ANISOU 2403 CA ASN B 58 21036 9207 14264 -2546 3405 782 C ATOM 2404 C ASN B 58 -18.171 26.817 30.626 1.00116.26 C ANISOU 2404 C ASN B 58 20919 9262 13991 -2509 3349 1045 C ATOM 2405 O ASN B 58 -17.222 26.254 30.080 1.00114.87 O ANISOU 2405 O ASN B 58 20584 9353 13708 -2790 3400 990 O ATOM 2406 CB ASN B 58 -16.945 28.436 32.079 1.00119.36 C ANISOU 2406 CB ASN B 58 21467 9331 14553 -2912 3564 659 C ATOM 2407 CG ASN B 58 -16.643 28.904 33.486 1.00119.83 C ANISOU 2407 CG ASN B 58 21509 9276 14745 -3002 3610 366 C ATOM 2408 OD1 ASN B 58 -15.517 28.775 33.966 1.00119.63 O ANISOU 2408 OD1 ASN B 58 21313 9416 14726 -3343 3674 116 O ATOM 2409 ND2 ASN B 58 -17.651 29.447 34.159 1.00120.64 N ANISOU 2409 ND2 ASN B 58 21772 9115 14949 -2685 3570 392 N ATOM 2410 N THR B 59 -19.353 26.977 30.043 1.00106.99 N ANISOU 2410 N THR B 59 19907 7946 12798 -2147 3237 1324 N ATOM 2411 CA THR B 59 -19.567 26.642 28.644 1.00107.79 C ANISOU 2411 CA THR B 59 20066 8163 12727 -2089 3168 1598 C ATOM 2412 C THR B 59 -19.876 27.911 27.868 1.00112.36 C ANISOU 2412 C THR B 59 21003 8415 13276 -2023 3202 1826 C ATOM 2413 O THR B 59 -20.886 28.569 28.123 1.00113.32 O ANISOU 2413 O THR B 59 21286 8274 13498 -1702 3132 1943 O ATOM 2414 CB THR B 59 -20.733 25.654 28.458 1.00101.67 C ANISOU 2414 CB THR B 59 19163 7538 11929 -1707 2968 1767 C ATOM 2415 OG1 THR B 59 -21.940 26.232 28.970 1.00102.21 O ANISOU 2415 OG1 THR B 59 19347 7348 12140 -1318 2879 1862 O ATOM 2416 CG2 THR B 59 -20.449 24.349 29.182 1.00 97.33 C ANISOU 2416 CG2 THR B 59 18270 7307 11405 -1766 2936 1562 C ATOM 2417 N ASP B 60 -18.994 28.262 26.938 1.00118.74 N ANISOU 2417 N ASP B 60 21925 9239 13951 -2321 3317 1883 N ATOM 2418 CA ASP B 60 -19.232 29.391 26.053 1.00122.67 C ANISOU 2418 CA ASP B 60 22769 9451 14391 -2269 3347 2133 C ATOM 2419 C ASP B 60 -20.547 29.150 25.328 1.00122.09 C ANISOU 2419 C ASP B 60 22755 9387 14246 -1850 3139 2436 C ATOM 2420 O ASP B 60 -20.744 28.089 24.737 1.00119.92 O ANISOU 2420 O ASP B 60 22314 9415 13834 -1800 3031 2516 O ATOM 2421 CB ASP B 60 -18.084 29.536 25.052 1.00123.81 C ANISOU 2421 CB ASP B 60 22978 9690 14373 -2645 3495 2163 C ATOM 2422 CG ASP B 60 -18.246 30.741 24.146 1.00129.13 C ANISOU 2422 CG ASP B 60 24028 10060 14976 -2610 3541 2431 C ATOM 2423 OD1 ASP B 60 -18.914 31.713 24.557 1.00131.35 O ANISOU 2423 OD1 ASP B 60 24532 9997 15379 -2396 3517 2512 O ATOM 2424 OD2 ASP B 60 -17.701 30.716 23.022 1.00130.45 O ANISOU 2424 OD2 ASP B 60 24270 10331 14964 -2793 3607 2559 O ATOM 2425 N ILE B 61 -21.451 30.124 25.403 1.00107.07 N ANISOU 2425 N ILE B 61 21073 7164 12442 -1546 3076 2593 N ATOM 2426 CA ILE B 61 -22.788 30.002 24.820 1.00107.43 C ANISOU 2426 CA ILE B 61 21151 7209 12458 -1109 2854 2874 C ATOM 2427 C ILE B 61 -22.707 29.576 23.355 1.00108.32 C ANISOU 2427 C ILE B 61 21310 7526 12321 -1149 2775 3112 C ATOM 2428 O ILE B 61 -23.531 28.793 22.876 1.00106.68 O ANISOU 2428 O ILE B 61 20974 7526 12035 -888 2570 3262 O ATOM 2429 CB ILE B 61 -23.597 31.317 24.961 1.00111.65 C ANISOU 2429 CB ILE B 61 21956 7341 13122 -825 2828 3027 C ATOM 2430 CG1 ILE B 61 -23.879 31.625 26.435 1.00110.61 C ANISOU 2430 CG1 ILE B 61 21751 7045 13229 -703 2873 2795 C ATOM 2431 CG2 ILE B 61 -24.910 31.232 24.200 1.00112.75 C ANISOU 2431 CG2 ILE B 61 22120 7506 13215 -397 2587 3341 C ATOM 2432 CD1 ILE B 61 -22.809 32.451 27.123 1.00112.33 C ANISOU 2432 CD1 ILE B 61 22103 7052 13524 -1055 3102 2553 C ATOM 2433 N TYR B 62 -21.689 30.080 22.665 1.00139.75 N ANISOU 2433 N TYR B 62 25466 11459 16176 -1487 2942 3134 N ATOM 2434 CA TYR B 62 -21.376 29.656 21.307 1.00140.63 C ANISOU 2434 CA TYR B 62 25618 11786 16029 -1599 2917 3311 C ATOM 2435 C TYR B 62 -21.212 28.139 21.256 1.00135.83 C ANISOU 2435 C TYR B 62 24678 11609 15325 -1648 2837 3193 C ATOM 2436 O TYR B 62 -21.850 27.461 20.449 1.00135.11 O ANISOU 2436 O TYR B 62 24538 11721 15079 -1451 2654 3373 O ATOM 2437 CB TYR B 62 -20.082 30.328 20.844 1.00146.66 C ANISOU 2437 CB TYR B 62 26550 12466 16711 -2023 3165 3260 C ATOM 2438 CG TYR B 62 -19.847 30.276 19.353 1.00151.09 C ANISOU 2438 CG TYR B 62 27262 13141 17006 -2105 3167 3496 C ATOM 2439 CD1 TYR B 62 -20.890 30.023 18.472 1.00152.98 C ANISOU 2439 CD1 TYR B 62 27595 13428 17105 -1771 2946 3791 C ATOM 2440 CD2 TYR B 62 -18.578 30.478 18.826 1.00153.40 C ANISOU 2440 CD2 TYR B 62 27594 13508 17185 -2513 3388 3419 C ATOM 2441 CE1 TYR B 62 -20.677 29.976 17.108 1.00155.98 C ANISOU 2441 CE1 TYR B 62 28127 13920 17220 -1845 2945 4003 C ATOM 2442 CE2 TYR B 62 -18.355 30.432 17.464 1.00156.25 C ANISOU 2442 CE2 TYR B 62 28101 13976 17292 -2586 3407 3630 C ATOM 2443 CZ TYR B 62 -19.407 30.181 16.610 1.00157.76 C ANISOU 2443 CZ TYR B 62 28406 14208 17329 -2252 3185 3921 C ATOM 2444 OH TYR B 62 -19.189 30.134 15.252 1.00161.22 O ANISOU 2444 OH TYR B 62 29003 14761 17495 -2324 3200 4127 O ATOM 2445 N SER B 63 -20.362 27.616 22.136 1.00112.55 N ANISOU 2445 N SER B 63 21498 8798 12467 -1909 2967 2885 N ATOM 2446 CA SER B 63 -20.085 26.183 22.194 1.00107.48 C ANISOU 2446 CA SER B 63 20530 8555 11752 -1986 2917 2742 C ATOM 2447 C SER B 63 -21.327 25.374 22.551 1.00103.77 C ANISOU 2447 C SER B 63 19898 8195 11336 -1600 2680 2807 C ATOM 2448 O SER B 63 -21.606 24.351 21.928 1.00102.17 O ANISOU 2448 O SER B 63 19561 8281 10979 -1519 2546 2885 O ATOM 2449 CB SER B 63 -18.969 25.893 23.200 1.00103.97 C ANISOU 2449 CB SER B 63 19864 8208 11431 -2316 3092 2394 C ATOM 2450 OG SER B 63 -17.785 26.599 22.871 1.00107.04 O ANISOU 2450 OG SER B 63 20369 8519 11784 -2681 3305 2322 O ATOM 2451 N LYS B 64 -22.067 25.835 23.556 1.00 94.87 N ANISOU 2451 N LYS B 64 18779 6841 10427 -1362 2633 2767 N ATOM 2452 CA LYS B 64 -23.275 25.145 23.997 1.00 92.28 C ANISOU 2452 CA LYS B 64 18280 6599 10185 -978 2421 2822 C ATOM 2453 C LYS B 64 -24.298 25.035 22.873 1.00 93.93 C ANISOU 2453 C LYS B 64 18571 6870 10248 -674 2192 3140 C ATOM 2454 O LYS B 64 -24.787 23.946 22.576 1.00 91.42 O ANISOU 2454 O LYS B 64 18060 6831 9843 -536 2021 3187 O ATOM 2455 CB LYS B 64 -23.905 25.856 25.197 1.00 92.69 C ANISOU 2455 CB LYS B 64 18359 6365 10494 -751 2429 2742 C ATOM 2456 CG LYS B 64 -25.215 25.231 25.656 1.00 90.48 C ANISOU 2456 CG LYS B 64 17885 6169 10326 -329 2219 2805 C ATOM 2457 CD LYS B 64 -25.949 26.121 26.647 1.00 92.06 C ANISOU 2457 CD LYS B 64 18150 6065 10762 -50 2224 2777 C ATOM 2458 CE LYS B 64 -25.145 26.323 27.919 1.00 90.98 C ANISOU 2458 CE LYS B 64 17988 5812 10768 -282 2429 2461 C ATOM 2459 NZ LYS B 64 -25.871 27.178 28.899 1.00 92.77 N ANISOU 2459 NZ LYS B 64 18291 5750 11208 -9 2444 2418 N ATOM 2460 N VAL B 65 -24.612 26.167 22.250 1.00 98.38 N ANISOU 2460 N VAL B 65 19422 7177 10783 -576 2181 3355 N ATOM 2461 CA VAL B 65 -25.590 26.203 21.166 1.00100.65 C ANISOU 2461 CA VAL B 65 19802 7505 10936 -280 1949 3668 C ATOM 2462 C VAL B 65 -25.131 25.382 19.961 1.00100.25 C ANISOU 2462 C VAL B 65 19730 7773 10587 -454 1902 3749 C ATOM 2463 O VAL B 65 -25.913 24.622 19.386 1.00 99.42 O ANISOU 2463 O VAL B 65 19513 7894 10367 -232 1665 3887 O ATOM 2464 CB VAL B 65 -25.897 27.652 20.730 1.00105.96 C ANISOU 2464 CB VAL B 65 20807 7821 11634 -165 1968 3882 C ATOM 2465 CG1 VAL B 65 -26.794 27.664 19.502 1.00108.63 C ANISOU 2465 CG1 VAL B 65 21236 8235 11803 107 1721 4209 C ATOM 2466 CG2 VAL B 65 -26.545 28.421 21.872 1.00106.65 C ANISOU 2466 CG2 VAL B 65 20908 7605 12010 71 1984 3813 C ATOM 2467 N LEU B 66 -23.861 25.531 19.591 1.00101.04 N ANISOU 2467 N LEU B 66 19923 7902 10566 -852 2127 3651 N ATOM 2468 CA LEU B 66 -23.298 24.780 18.471 1.00100.92 C ANISOU 2468 CA LEU B 66 19888 8191 10267 -1045 2127 3694 C ATOM 2469 C LEU B 66 -23.399 23.273 18.692 1.00 96.24 C ANISOU 2469 C LEU B 66 18972 7971 9625 -1030 2017 3550 C ATOM 2470 O LEU B 66 -23.994 22.558 17.884 1.00 95.99 O ANISOU 2470 O LEU B 66 18893 8169 9408 -875 1812 3688 O ATOM 2471 CB LEU B 66 -21.838 25.173 18.235 1.00102.38 C ANISOU 2471 CB LEU B 66 20167 8349 10383 -1485 2421 3560 C ATOM 2472 CG LEU B 66 -21.064 24.334 17.215 1.00101.95 C ANISOU 2472 CG LEU B 66 20040 8634 10061 -1726 2477 3533 C ATOM 2473 CD1 LEU B 66 -21.707 24.422 15.839 1.00105.04 C ANISOU 2473 CD1 LEU B 66 20632 9084 10195 -1546 2307 3838 C ATOM 2474 CD2 LEU B 66 -19.606 24.764 17.158 1.00103.48 C ANISOU 2474 CD2 LEU B 66 20279 8794 10246 -2151 2782 3373 C ATOM 2475 N VAL B 67 -22.819 22.803 19.792 1.00 92.78 N ANISOU 2475 N VAL B 67 18315 7589 9348 -1195 2149 3269 N ATOM 2476 CA VAL B 67 -22.819 21.381 20.122 1.00 88.38 C ANISOU 2476 CA VAL B 67 17449 7367 8763 -1209 2076 3111 C ATOM 2477 C VAL B 67 -24.241 20.836 20.276 1.00 86.90 C ANISOU 2477 C VAL B 67 17151 7241 8625 -796 1786 3242 C ATOM 2478 O VAL B 67 -24.525 19.707 19.875 1.00 84.82 O ANISOU 2478 O VAL B 67 16725 7280 8223 -739 1636 3245 O ATOM 2479 CB VAL B 67 -21.988 21.100 21.396 1.00 85.35 C ANISOU 2479 CB VAL B 67 16857 7002 8571 -1444 2268 2792 C ATOM 2480 CG1 VAL B 67 -22.118 19.646 21.823 1.00 80.95 C ANISOU 2480 CG1 VAL B 67 15984 6770 8003 -1423 2184 2644 C ATOM 2481 CG2 VAL B 67 -20.528 21.454 21.159 1.00 86.84 C ANISOU 2481 CG2 VAL B 67 17089 7205 8703 -1863 2528 2645 C ATOM 2482 N THR B 68 -25.133 21.646 20.838 1.00 88.25 N ANISOU 2482 N THR B 68 17401 7134 8997 -505 1706 3344 N ATOM 2483 CA THR B 68 -26.533 21.254 20.977 1.00 87.49 C ANISOU 2483 CA THR B 68 17175 7089 8980 -85 1427 3478 C ATOM 2484 C THR B 68 -27.177 21.045 19.610 1.00 89.76 C ANISOU 2484 C THR B 68 17541 7538 9025 74 1184 3736 C ATOM 2485 O THR B 68 -27.843 20.037 19.379 1.00 87.98 O ANISOU 2485 O THR B 68 17126 7574 8728 243 958 3770 O ATOM 2486 CB THR B 68 -27.347 22.297 21.765 1.00 89.25 C ANISOU 2486 CB THR B 68 17462 6978 9472 209 1404 3537 C ATOM 2487 OG1 THR B 68 -26.764 22.483 23.061 1.00 87.30 O ANISOU 2487 OG1 THR B 68 17147 6589 9434 62 1620 3279 O ATOM 2488 CG2 THR B 68 -28.791 21.842 21.924 1.00 88.58 C ANISOU 2488 CG2 THR B 68 17177 6986 9493 648 1118 3658 C ATOM 2489 N ALA B 69 -26.968 22.001 18.709 1.00 93.89 N ANISOU 2489 N ALA B 69 18347 7909 9419 13 1227 3912 N ATOM 2490 CA ALA B 69 -27.500 21.914 17.353 1.00 96.65 C ANISOU 2490 CA ALA B 69 18805 8401 9517 142 1010 4161 C ATOM 2491 C ALA B 69 -26.956 20.687 16.626 1.00 94.64 C ANISOU 2491 C ALA B 69 18442 8528 8990 -68 984 4075 C ATOM 2492 O ALA B 69 -27.694 19.989 15.925 1.00 94.74 O ANISOU 2492 O ALA B 69 18373 8780 8846 110 716 4187 O ATOM 2493 CB ALA B 69 -27.176 23.179 16.575 1.00101.55 C ANISOU 2493 CB ALA B 69 19769 8773 10041 65 1115 4348 C ATOM 2494 N ILE B 70 -25.662 20.434 16.800 1.00 93.04 N ANISOU 2494 N ILE B 70 18222 8390 8741 -447 1258 3860 N ATOM 2495 CA ILE B 70 -25.027 19.250 16.233 1.00 91.02 C ANISOU 2495 CA ILE B 70 17834 8494 8255 -666 1278 3728 C ATOM 2496 C ILE B 70 -25.696 17.987 16.765 1.00 87.08 C ANISOU 2496 C ILE B 70 17042 8238 7807 -501 1077 3625 C ATOM 2497 O ILE B 70 -25.967 17.050 16.012 1.00 86.57 O ANISOU 2497 O ILE B 70 16899 8468 7527 -468 900 3644 O ATOM 2498 CB ILE B 70 -23.520 19.208 16.557 1.00 89.83 C ANISOU 2498 CB ILE B 70 17642 8368 8123 -1083 1619 3478 C ATOM 2499 CG1 ILE B 70 -22.797 20.379 15.890 1.00 94.07 C ANISOU 2499 CG1 ILE B 70 18466 8698 8579 -1274 1817 3581 C ATOM 2500 CG2 ILE B 70 -22.908 17.891 16.106 1.00 87.46 C ANISOU 2500 CG2 ILE B 70 17147 8455 7628 -1276 1642 3307 C ATOM 2501 CD1 ILE B 70 -21.313 20.426 16.180 1.00 93.48 C ANISOU 2501 CD1 ILE B 70 18327 8652 8540 -1681 2140 3338 C ATOM 2502 N TYR B 71 -25.977 17.978 18.064 1.00115.03 N ANISOU 2502 N TYR B 71 20427 11649 11631 -394 1104 3512 N ATOM 2503 CA TYR B 71 -26.617 16.833 18.701 1.00112.51 C ANISOU 2503 CA TYR B 71 19733 11576 11440 -226 917 3367 C ATOM 2504 C TYR B 71 -28.041 16.637 18.198 1.00113.63 C ANISOU 2504 C TYR B 71 19821 11800 11554 154 554 3578 C ATOM 2505 O TYR B 71 -28.530 15.513 18.141 1.00113.27 O ANISOU 2505 O TYR B 71 19445 12076 11518 240 346 3467 O ATOM 2506 CB TYR B 71 -26.615 16.970 20.226 1.00107.88 C ANISOU 2506 CB TYR B 71 18902 10871 11217 -181 1024 3154 C ATOM 2507 CG TYR B 71 -25.279 16.684 20.875 1.00106.40 C ANISOU 2507 CG TYR B 71 18589 10754 11086 -542 1303 2859 C ATOM 2508 CD1 TYR B 71 -24.118 16.606 20.118 1.00106.84 C ANISOU 2508 CD1 TYR B 71 18809 10881 10906 -890 1499 2829 C ATOM 2509 CD2 TYR B 71 -25.183 16.476 22.243 1.00105.09 C ANISOU 2509 CD2 TYR B 71 18128 10599 11204 -531 1367 2610 C ATOM 2510 CE1 TYR B 71 -22.900 16.345 20.707 1.00105.59 C ANISOU 2510 CE1 TYR B 71 18501 10805 10814 -1210 1741 2559 C ATOM 2511 CE2 TYR B 71 -23.967 16.208 22.841 1.00104.31 C ANISOU 2511 CE2 TYR B 71 17900 10581 11152 -848 1592 2344 C ATOM 2512 CZ TYR B 71 -22.829 16.145 22.067 1.00104.44 C ANISOU 2512 CZ TYR B 71 18058 10672 10952 -1184 1774 2318 C ATOM 2513 OH TYR B 71 -21.614 15.882 22.656 1.00103.15 O ANISOU 2513 OH TYR B 71 17735 10607 10851 -1492 1989 2052 O ATOM 2514 N LEU B 72 -28.702 17.733 17.840 1.00 85.88 N ANISOU 2514 N LEU B 72 16583 8011 8035 376 472 3858 N ATOM 2515 CA LEU B 72 -30.053 17.661 17.295 1.00 87.79 C ANISOU 2515 CA LEU B 72 16757 8339 8260 743 114 4070 C ATOM 2516 C LEU B 72 -30.028 17.102 15.877 1.00 89.50 C ANISOU 2516 C LEU B 72 17048 8835 8121 664 -59 4166 C ATOM 2517 O LEU B 72 -30.880 16.293 15.501 1.00 89.24 O ANISOU 2517 O LEU B 72 16842 9049 8018 853 -369 4212 O ATOM 2518 CB LEU B 72 -30.722 19.038 17.311 1.00 91.60 C ANISOU 2518 CB LEU B 72 17394 8504 8905 991 78 4279 C ATOM 2519 CG LEU B 72 -30.952 19.675 18.684 1.00 90.59 C ANISOU 2519 CG LEU B 72 17193 8089 9138 1128 218 4189 C ATOM 2520 CD1 LEU B 72 -31.714 20.986 18.550 1.00 94.88 C ANISOU 2520 CD1 LEU B 72 17887 8347 9817 1398 146 4405 C ATOM 2521 CD2 LEU B 72 -31.680 18.715 19.615 1.00 87.04 C ANISOU 2521 CD2 LEU B 72 16388 7796 8889 1337 88 4063 C ATOM 2522 N ALA B 73 -29.044 17.538 15.095 1.00 91.46 N ANISOU 2522 N ALA B 73 17545 9051 8154 381 145 4183 N ATOM 2523 CA ALA B 73 -28.872 17.043 13.733 1.00 93.30 C ANISOU 2523 CA ALA B 73 17873 9545 8031 274 37 4248 C ATOM 2524 C ALA B 73 -28.572 15.547 13.737 1.00 89.71 C ANISOU 2524 C ALA B 73 17197 9440 7450 130 -12 4023 C ATOM 2525 O ALA B 73 -29.186 14.776 12.997 1.00 90.20 O ANISOU 2525 O ALA B 73 17176 9765 7329 236 -291 4061 O ATOM 2526 CB ALA B 73 -27.762 17.807 13.028 1.00 95.99 C ANISOU 2526 CB ALA B 73 18501 9770 8200 -15 322 4281 C ATOM 2527 N LEU B 74 -27.628 15.143 14.580 1.00 86.32 N ANISOU 2527 N LEU B 74 16662 9012 7124 -116 256 3779 N ATOM 2528 CA LEU B 74 -27.285 13.734 14.724 1.00 82.23 C ANISOU 2528 CA LEU B 74 15840 8834 6571 -258 237 3506 C ATOM 2529 C LEU B 74 -28.459 12.951 15.305 1.00 78.86 C ANISOU 2529 C LEU B 74 15002 8576 6385 23 -72 3423 C ATOM 2530 O LEU B 74 -28.604 11.754 15.054 1.00 76.53 O ANISOU 2530 O LEU B 74 14459 8594 6027 -5 -221 3263 O ATOM 2531 CB LEU B 74 -26.045 13.574 15.605 1.00 78.90 C ANISOU 2531 CB LEU B 74 15269 8397 6313 -553 583 3223 C ATOM 2532 CG LEU B 74 -24.756 14.178 15.044 1.00 81.97 C ANISOU 2532 CG LEU B 74 15972 8683 6488 -888 914 3244 C ATOM 2533 CD1 LEU B 74 -23.661 14.193 16.099 1.00 79.28 C ANISOU 2533 CD1 LEU B 74 15473 8283 6365 -1144 1229 2988 C ATOM 2534 CD2 LEU B 74 -24.302 13.416 13.807 1.00 82.97 C ANISOU 2534 CD2 LEU B 74 16117 9117 6290 -1038 896 3188 C ATOM 2535 N PHE B 75 -29.297 13.637 16.077 1.00 83.47 N ANISOU 2535 N PHE B 75 15522 8942 7250 291 -153 3529 N ATOM 2536 CA PHE B 75 -30.489 13.024 16.650 1.00 83.55 C ANISOU 2536 CA PHE B 75 15147 9089 7509 573 -430 3482 C ATOM 2537 C PHE B 75 -31.496 12.679 15.564 1.00 84.90 C ANISOU 2537 C PHE B 75 15341 9443 7472 769 -804 3670 C ATOM 2538 O PHE B 75 -31.975 11.552 15.500 1.00 84.89 O ANISOU 2538 O PHE B 75 15022 9732 7498 803 -1013 3533 O ATOM 2539 CB PHE B 75 -31.138 13.943 17.689 1.00 83.29 C ANISOU 2539 CB PHE B 75 15071 8765 7810 826 -402 3566 C ATOM 2540 CG PHE B 75 -32.428 13.412 18.249 1.00 83.91 C ANISOU 2540 CG PHE B 75 14757 8974 8150 1132 -669 3546 C ATOM 2541 CD1 PHE B 75 -32.424 12.502 19.292 1.00 83.41 C ANISOU 2541 CD1 PHE B 75 14284 9067 8342 1092 -618 3271 C ATOM 2542 CD2 PHE B 75 -33.646 13.830 17.738 1.00 85.44 C ANISOU 2542 CD2 PHE B 75 14987 9136 8339 1462 -966 3809 C ATOM 2543 CE1 PHE B 75 -33.610 12.014 19.810 1.00 83.55 C ANISOU 2543 CE1 PHE B 75 13936 9202 8605 1355 -838 3256 C ATOM 2544 CE2 PHE B 75 -34.834 13.345 18.251 1.00 85.51 C ANISOU 2544 CE2 PHE B 75 14604 9279 8608 1732 -1199 3786 C ATOM 2545 CZ PHE B 75 -34.815 12.436 19.289 1.00 84.06 C ANISOU 2545 CZ PHE B 75 14016 9246 8678 1668 -1123 3509 C ATOM 2546 N VAL B 76 -31.821 13.648 14.713 1.00 85.20 N ANISOU 2546 N VAL B 76 15762 9307 7302 896 -895 3985 N ATOM 2547 CA VAL B 76 -32.805 13.412 13.659 1.00 88.84 C ANISOU 2547 CA VAL B 76 16263 9942 7550 1102 -1281 4185 C ATOM 2548 C VAL B 76 -32.279 12.471 12.571 1.00 89.15 C ANISOU 2548 C VAL B 76 16377 10287 7210 863 -1343 4089 C ATOM 2549 O VAL B 76 -32.977 11.541 12.160 1.00 88.86 O ANISOU 2549 O VAL B 76 16113 10535 7114 943 -1647 4030 O ATOM 2550 CB VAL B 76 -33.345 14.730 13.044 1.00 93.96 C ANISOU 2550 CB VAL B 76 17153 10373 8172 1307 -1357 4497 C ATOM 2551 CG1 VAL B 76 -34.240 15.451 14.040 1.00 94.16 C ANISOU 2551 CG1 VAL B 76 17027 10165 8587 1629 -1408 4588 C ATOM 2552 CG2 VAL B 76 -32.208 15.634 12.593 1.00 95.80 C ANISOU 2552 CG2 VAL B 76 17752 10403 8245 1052 -1024 4549 C ATOM 2553 N VAL B 77 -31.047 12.701 12.123 1.00 89.62 N ANISOU 2553 N VAL B 77 16707 10298 7046 559 -1036 4042 N ATOM 2554 CA VAL B 77 -30.439 11.857 11.097 1.00 90.00 C ANISOU 2554 CA VAL B 77 16815 10630 6750 323 -1029 3920 C ATOM 2555 C VAL B 77 -30.262 10.428 11.605 1.00 85.17 C ANISOU 2555 C VAL B 77 15844 10287 6233 203 -1053 3594 C ATOM 2556 O VAL B 77 -30.521 9.462 10.884 1.00 85.55 O ANISOU 2556 O VAL B 77 15810 10615 6079 175 -1265 3507 O ATOM 2557 CB VAL B 77 -29.080 12.422 10.628 1.00 91.16 C ANISOU 2557 CB VAL B 77 17229 10678 6731 17 -637 3890 C ATOM 2558 CG1 VAL B 77 -28.390 11.451 9.681 1.00 91.26 C ANISOU 2558 CG1 VAL B 77 17259 10993 6423 -219 -589 3718 C ATOM 2559 CG2 VAL B 77 -29.271 13.775 9.958 1.00 95.74 C ANISOU 2559 CG2 VAL B 77 18092 11034 7250 119 -618 4176 C ATOM 2560 N GLY B 78 -29.837 10.301 12.858 1.00 81.89 N ANISOU 2560 N GLY B 78 15160 9790 6167 136 -830 3385 N ATOM 2561 CA GLY B 78 -29.625 8.999 13.461 1.00 76.79 C ANISOU 2561 CA GLY B 78 14106 9377 5691 32 -813 3054 C ATOM 2562 C GLY B 78 -30.912 8.244 13.741 1.00 75.53 C ANISOU 2562 C GLY B 78 13586 9382 5731 267 -1165 3017 C ATOM 2563 O GLY B 78 -30.995 7.040 13.502 1.00 74.26 O ANISOU 2563 O GLY B 78 13214 9482 5520 192 -1291 2824 O ATOM 2564 N THR B 79 -31.916 8.951 14.252 1.00 74.96 N ANISOU 2564 N THR B 79 13437 9150 5893 548 -1316 3197 N ATOM 2565 CA THR B 79 -33.201 8.338 14.574 1.00 74.03 C ANISOU 2565 CA THR B 79 12951 9181 5998 780 -1639 3180 C ATOM 2566 C THR B 79 -33.942 7.912 13.313 1.00 77.98 C ANISOU 2566 C THR B 79 13519 9900 6208 854 -2008 3295 C ATOM 2567 O THR B 79 -34.459 6.797 13.237 1.00 76.62 O ANISOU 2567 O THR B 79 13056 9978 6078 842 -2219 3136 O ATOM 2568 CB THR B 79 -34.102 9.284 15.392 1.00 74.87 C ANISOU 2568 CB THR B 79 12964 9061 6422 1087 -1696 3356 C ATOM 2569 OG1 THR B 79 -33.454 9.615 16.627 1.00 71.21 O ANISOU 2569 OG1 THR B 79 12418 8408 6229 1016 -1369 3217 O ATOM 2570 CG2 THR B 79 -35.442 8.628 15.689 1.00 74.51 C ANISOU 2570 CG2 THR B 79 12510 9195 6607 1316 -2022 3341 C ATOM 2571 N VAL B 80 -33.995 8.803 12.327 1.00120.92 N ANISOU 2571 N VAL B 80 19356 15240 11347 924 -2091 3573 N ATOM 2572 CA VAL B 80 -34.630 8.476 11.056 1.00122.70 C ANISOU 2572 CA VAL B 80 19701 15677 11242 988 -2451 3697 C ATOM 2573 C VAL B 80 -33.880 7.342 10.363 1.00122.06 C ANISOU 2573 C VAL B 80 19657 15852 10869 695 -2407 3457 C ATOM 2574 O VAL B 80 -34.482 6.347 9.957 1.00122.99 O ANISOU 2574 O VAL B 80 19567 16229 10937 700 -2690 3338 O ATOM 2575 CB VAL B 80 -34.712 9.698 10.120 1.00121.98 C ANISOU 2575 CB VAL B 80 20040 15426 10881 1101 -2494 4034 C ATOM 2576 CG1 VAL B 80 -35.116 9.270 8.718 1.00125.68 C ANISOU 2576 CG1 VAL B 80 20551 16174 11028 1091 -2763 4069 C ATOM 2577 CG2 VAL B 80 -35.693 10.722 10.672 1.00122.79 C ANISOU 2577 CG2 VAL B 80 20049 15313 11294 1440 -2601 4266 C ATOM 2578 N GLY B 81 -32.564 7.493 10.248 1.00 85.57 N ANISOU 2578 N GLY B 81 15293 11153 6070 438 -2044 3378 N ATOM 2579 CA GLY B 81 -31.726 6.489 9.618 1.00 84.92 C ANISOU 2579 CA GLY B 81 15262 11288 5713 164 -1939 3143 C ATOM 2580 C GLY B 81 -31.879 5.108 10.228 1.00 80.33 C ANISOU 2580 C GLY B 81 14241 10909 5369 101 -1999 2816 C ATOM 2581 O GLY B 81 -32.244 4.155 9.538 1.00 81.52 O ANISOU 2581 O GLY B 81 14331 11300 5342 58 -2232 2701 O ATOM 2582 N ASN B 82 -31.611 5.003 11.527 1.00 80.22 N ANISOU 2582 N ASN B 82 13938 10791 5752 94 -1794 2669 N ATOM 2583 CA ASN B 82 -31.691 3.724 12.228 1.00 79.09 C ANISOU 2583 CA ASN B 82 13390 10806 5856 33 -1813 2371 C ATOM 2584 C ASN B 82 -33.106 3.153 12.300 1.00 80.01 C ANISOU 2584 C ASN B 82 13202 11061 6138 223 -2211 2384 C ATOM 2585 O ASN B 82 -33.295 1.941 12.213 1.00 79.24 O ANISOU 2585 O ASN B 82 12903 11164 6041 136 -2338 2171 O ATOM 2586 CB ASN B 82 -31.095 3.836 13.634 1.00 75.19 C ANISOU 2586 CB ASN B 82 12681 10160 5729 -4 -1507 2236 C ATOM 2587 CG ASN B 82 -29.607 4.128 13.616 1.00 74.07 C ANISOU 2587 CG ASN B 82 12749 9942 5452 -245 -1115 2140 C ATOM 2588 OD1 ASN B 82 -28.787 3.225 13.445 1.00 72.86 O ANISOU 2588 OD1 ASN B 82 12543 9936 5204 -438 -979 1904 O ATOM 2589 ND2 ASN B 82 -29.250 5.394 13.796 1.00 74.42 N ANISOU 2589 ND2 ASN B 82 13026 9751 5499 -234 -928 2320 N ATOM 2590 N GLY B 83 -34.094 4.028 12.462 1.00 97.39 N ANISOU 2590 N GLY B 83 15364 13151 8489 481 -2399 2629 N ATOM 2591 CA GLY B 83 -35.481 3.603 12.535 1.00 97.86 C ANISOU 2591 CA GLY B 83 15112 13347 8725 674 -2778 2666 C ATOM 2592 C GLY B 83 -35.973 3.005 11.231 1.00 98.95 C ANISOU 2592 C GLY B 83 15353 13725 8520 639 -3125 2678 C ATOM 2593 O GLY B 83 -36.500 1.885 11.201 1.00 98.01 O ANISOU 2593 O GLY B 83 14959 13808 8473 585 -3328 2493 O ATOM 2594 N VAL B 84 -35.798 3.753 10.144 1.00 94.65 N ANISOU 2594 N VAL B 84 15222 13152 7589 661 -3193 2896 N ATOM 2595 CA VAL B 84 -36.185 3.268 8.825 1.00 97.98 C ANISOU 2595 CA VAL B 84 15806 13802 7618 620 -3519 2917 C ATOM 2596 C VAL B 84 -35.364 2.035 8.460 1.00 96.35 C ANISOU 2596 C VAL B 84 15617 13768 7224 327 -3391 2594 C ATOM 2597 O VAL B 84 -35.867 1.123 7.809 1.00 97.81 O ANISOU 2597 O VAL B 84 15724 14177 7259 272 -3678 2470 O ATOM 2598 CB VAL B 84 -36.035 4.355 7.739 1.00102.16 C ANISOU 2598 CB VAL B 84 16771 14262 7780 689 -3526 3196 C ATOM 2599 CG1 VAL B 84 -36.473 3.818 6.386 1.00105.93 C ANISOU 2599 CG1 VAL B 84 17281 15012 7955 666 -3783 3150 C ATOM 2600 CG2 VAL B 84 -36.856 5.578 8.101 1.00104.00 C ANISOU 2600 CG2 VAL B 84 16973 14306 8235 997 -3619 3504 C ATOM 2601 N THR B 85 -34.106 2.006 8.893 1.00 82.82 N ANISOU 2601 N THR B 85 13995 11945 5527 143 -2965 2450 N ATOM 2602 CA THR B 85 -33.270 0.823 8.711 1.00 80.86 C ANISOU 2602 CA THR B 85 13724 11837 5162 -110 -2801 2128 C ATOM 2603 C THR B 85 -33.935 -0.386 9.361 1.00 77.99 C ANISOU 2603 C THR B 85 12918 11601 5114 -112 -2971 1889 C ATOM 2604 O THR B 85 -34.057 -1.449 8.746 1.00 79.33 O ANISOU 2604 O THR B 85 13067 11960 5117 -232 -3128 1695 O ATOM 2605 CB THR B 85 -31.867 1.014 9.317 1.00 77.32 C ANISOU 2605 CB THR B 85 13353 11245 4778 -276 -2314 2012 C ATOM 2606 OG1 THR B 85 -31.249 2.173 8.744 1.00 80.37 O ANISOU 2606 OG1 THR B 85 14151 11499 4888 -299 -2139 2240 O ATOM 2607 CG2 THR B 85 -30.998 -0.205 9.047 1.00 76.03 C ANISOU 2607 CG2 THR B 85 13174 11234 4481 -509 -2150 1688 C ATOM 2608 N LEU B 86 -34.380 -0.205 10.601 1.00103.88 N ANISOU 2608 N LEU B 86 15862 14765 8843 17 -2931 1905 N ATOM 2609 CA LEU B 86 -35.075 -1.253 11.340 1.00103.56 C ANISOU 2609 CA LEU B 86 15391 14818 9138 26 -3073 1715 C ATOM 2610 C LEU B 86 -36.317 -1.734 10.602 1.00104.35 C ANISOU 2610 C LEU B 86 15388 15115 9146 93 -3537 1750 C ATOM 2611 O LEU B 86 -36.521 -2.936 10.436 1.00103.93 O ANISOU 2611 O LEU B 86 15206 15218 9063 -44 -3667 1518 O ATOM 2612 CB LEU B 86 -35.475 -0.761 12.734 1.00 98.98 C ANISOU 2612 CB LEU B 86 14506 14079 9023 191 -2970 1788 C ATOM 2613 CG LEU B 86 -34.735 -1.331 13.948 1.00 97.61 C ANISOU 2613 CG LEU B 86 14127 13814 9144 92 -2631 1575 C ATOM 2614 CD1 LEU B 86 -34.089 -2.670 13.619 1.00 96.77 C ANISOU 2614 CD1 LEU B 86 13995 13842 8929 -133 -2562 1274 C ATOM 2615 CD2 LEU B 86 -33.699 -0.346 14.458 1.00 96.95 C ANISOU 2615 CD2 LEU B 86 14251 13529 9058 77 -2270 1652 C ATOM 2616 N PHE B 87 -37.146 -0.794 10.157 1.00130.22 N ANISOU 2616 N PHE B 87 18725 18379 12374 306 -3794 2036 N ATOM 2617 CA PHE B 87 -38.402 -1.164 9.507 1.00131.82 C ANISOU 2617 CA PHE B 87 18782 18782 12523 392 -4268 2084 C ATOM 2618 C PHE B 87 -38.254 -1.548 8.032 1.00133.94 C ANISOU 2618 C PHE B 87 19377 19235 12278 261 -4485 2044 C ATOM 2619 O PHE B 87 -39.239 -1.876 7.370 1.00137.18 O ANISOU 2619 O PHE B 87 19621 19830 12673 323 -4797 2017 O ATOM 2620 CB PHE B 87 -39.463 -0.075 9.694 1.00128.38 C ANISOU 2620 CB PHE B 87 18235 18285 12260 698 -4496 2399 C ATOM 2621 CG PHE B 87 -40.066 -0.053 11.070 1.00127.31 C ANISOU 2621 CG PHE B 87 17661 18053 12658 835 -4412 2387 C ATOM 2622 CD1 PHE B 87 -39.804 -1.074 11.970 1.00125.10 C ANISOU 2622 CD1 PHE B 87 17099 17778 12657 678 -4214 2113 C ATOM 2623 CD2 PHE B 87 -40.900 0.980 11.462 1.00128.61 C ANISOU 2623 CD2 PHE B 87 17707 18119 13041 1129 -4522 2651 C ATOM 2624 CE1 PHE B 87 -40.355 -1.063 13.236 1.00124.08 C ANISOU 2624 CE1 PHE B 87 16587 17565 12993 798 -4121 2106 C ATOM 2625 CE2 PHE B 87 -41.457 0.997 12.729 1.00127.48 C ANISOU 2625 CE2 PHE B 87 17168 17893 13375 1256 -4421 2631 C ATOM 2626 CZ PHE B 87 -41.183 -0.027 13.617 1.00125.24 C ANISOU 2626 CZ PHE B 87 16616 17624 13345 1083 -4217 2359 C ATOM 2627 N THR B 88 -37.026 -1.508 7.524 1.00103.68 N ANISOU 2627 N THR B 88 15926 15359 8110 98 -4199 1986 N ATOM 2628 CA THR B 88 -36.737 -2.031 6.191 1.00106.82 C ANISOU 2628 CA THR B 88 16543 15925 8119 -28 -4224 1845 C ATOM 2629 C THR B 88 -36.166 -3.435 6.310 1.00104.59 C ANISOU 2629 C THR B 88 16173 15727 7838 -272 -4113 1477 C ATOM 2630 O THR B 88 -36.423 -4.294 5.466 1.00107.47 O ANISOU 2630 O THR B 88 16525 16263 8046 -354 -4265 1286 O ATOM 2631 CB THR B 88 -35.741 -1.150 5.415 1.00111.78 C ANISOU 2631 CB THR B 88 17621 16471 8380 -63 -3944 1982 C ATOM 2632 OG1 THR B 88 -34.645 -0.795 6.266 1.00108.52 O ANISOU 2632 OG1 THR B 88 17320 15864 8048 -162 -3559 1975 O ATOM 2633 CG2 THR B 88 -36.418 0.110 4.913 1.00115.92 C ANISOU 2633 CG2 THR B 88 18269 16949 8827 174 -4101 2331 C ATOM 2634 N LEU B 89 -35.389 -3.662 7.365 1.00 99.48 N ANISOU 2634 N LEU B 89 15443 14950 7405 -369 -3811 1364 N ATOM 2635 CA LEU B 89 -34.852 -4.990 7.637 1.00 97.37 C ANISOU 2635 CA LEU B 89 15031 14732 7231 -562 -3662 1012 C ATOM 2636 C LEU B 89 -35.949 -5.918 8.153 1.00 96.15 C ANISOU 2636 C LEU B 89 14454 14654 7422 -540 -3944 886 C ATOM 2637 O LEU B 89 -35.778 -7.136 8.194 1.00 95.11 O ANISOU 2637 O LEU B 89 14215 14587 7336 -697 -3937 600 O ATOM 2638 CB LEU B 89 -33.704 -4.914 8.646 1.00 97.50 C ANISOU 2638 CB LEU B 89 14995 14580 7469 -621 -3188 916 C ATOM 2639 CG LEU B 89 -32.465 -4.133 8.204 1.00 97.52 C ANISOU 2639 CG LEU B 89 15377 14506 7169 -693 -2849 994 C ATOM 2640 CD1 LEU B 89 -31.429 -4.096 9.316 1.00 96.05 C ANISOU 2640 CD1 LEU B 89 15060 14170 7264 -745 -2425 889 C ATOM 2641 CD2 LEU B 89 -31.876 -4.724 6.934 1.00 97.70 C ANISOU 2641 CD2 LEU B 89 15723 14679 6718 -864 -2835 837 C ATOM 2642 N ALA B 90 -37.075 -5.330 8.546 1.00122.98 N ANISOU 2642 N ALA B 90 17615 18037 11074 -344 -4181 1102 N ATOM 2643 CA ALA B 90 -38.215 -6.097 9.033 1.00122.83 C ANISOU 2643 CA ALA B 90 17175 18106 11390 -320 -4463 1016 C ATOM 2644 C ALA B 90 -39.053 -6.632 7.876 1.00126.19 C ANISOU 2644 C ALA B 90 17617 18743 11586 -361 -4847 942 C ATOM 2645 O ALA B 90 -39.609 -7.727 7.955 1.00126.36 O ANISOU 2645 O ALA B 90 17383 18853 11774 -470 -4983 715 O ATOM 2646 CB ALA B 90 -39.069 -5.245 9.959 1.00123.35 C ANISOU 2646 CB ALA B 90 16953 18086 11830 -78 -4535 1262 C ATOM 2647 N ARG B 91 -39.139 -5.850 6.803 1.00125.93 N ANISOU 2647 N ARG B 91 17849 18774 11226 -253 -4938 1110 N ATOM 2648 CA ARG B 91 -39.903 -6.241 5.624 1.00130.23 C ANISOU 2648 CA ARG B 91 18392 19523 11566 -251 -5226 1036 C ATOM 2649 C ARG B 91 -39.265 -7.437 4.925 1.00130.52 C ANISOU 2649 C ARG B 91 18588 19636 11368 -485 -5132 700 C ATOM 2650 O ARG B 91 -38.333 -7.282 4.136 1.00131.54 O ANISOU 2650 O ARG B 91 19089 19770 11121 -546 -4952 675 O ATOM 2651 CB ARG B 91 -40.019 -5.068 4.648 1.00137.01 C ANISOU 2651 CB ARG B 91 19534 20425 12099 -80 -5311 1313 C ATOM 2652 CG ARG B 91 -40.737 -3.853 5.213 1.00137.45 C ANISOU 2652 CG ARG B 91 19449 20399 12378 189 -5417 1652 C ATOM 2653 CD ARG B 91 -42.209 -4.141 5.463 1.00139.34 C ANISOU 2653 CD ARG B 91 19233 20778 12933 312 -5764 1657 C ATOM 2654 NE ARG B 91 -42.895 -2.994 6.050 1.00139.74 N ANISOU 2654 NE ARG B 91 19119 20741 13235 593 -5830 1965 N ATOM 2655 CZ ARG B 91 -43.442 -2.008 5.346 1.00143.69 C ANISOU 2655 CZ ARG B 91 19728 21292 13578 815 -5987 2231 C ATOM 2656 NH1 ARG B 91 -43.383 -2.024 4.021 1.00147.61 N ANISOU 2656 NH1 ARG B 91 20497 21937 13651 781 -6105 2239 N ATOM 2657 NH2 ARG B 91 -44.046 -1.004 5.966 1.00143.96 N ANISOU 2657 NH2 ARG B 91 19598 21223 13877 1081 -6016 2492 N ATOM 2658 N LEU B 98 -28.624 -16.027 3.593 1.00123.10 N ANISOU 2658 N LEU B 98 18877 18204 9690 -1657 -2234 -2002 N ATOM 2659 CA LEU B 98 -27.485 -15.384 4.236 1.00120.35 C ANISOU 2659 CA LEU B 98 18534 17796 9398 -1635 -1857 -1909 C ATOM 2660 C LEU B 98 -27.792 -13.919 4.525 1.00119.62 C ANISOU 2660 C LEU B 98 18455 17737 9259 -1596 -1919 -1569 C ATOM 2661 O LEU B 98 -27.296 -13.352 5.499 1.00116.59 O ANISOU 2661 O LEU B 98 17966 17283 9051 -1589 -1722 -1460 O ATOM 2662 CB LEU B 98 -26.235 -15.511 3.357 1.00114.63 C ANISOU 2662 CB LEU B 98 18036 17099 8418 -1629 -1526 -2025 C ATOM 2663 CG LEU B 98 -24.859 -15.242 3.977 1.00112.11 C ANISOU 2663 CG LEU B 98 17674 16712 8212 -1617 -1088 -2035 C ATOM 2664 CD1 LEU B 98 -23.796 -16.057 3.258 1.00113.96 C ANISOU 2664 CD1 LEU B 98 18037 16953 8311 -1607 -821 -2268 C ATOM 2665 CD2 LEU B 98 -24.498 -13.763 3.935 1.00111.81 C ANISOU 2665 CD2 LEU B 98 17726 16708 8051 -1610 -952 -1746 C ATOM 2666 N GLN B 99 -28.615 -13.314 3.675 1.00137.65 N ANISOU 2666 N GLN B 99 20871 20125 11306 -1563 -2195 -1402 N ATOM 2667 CA GLN B 99 -28.957 -11.901 3.810 1.00137.63 C ANISOU 2667 CA GLN B 99 20920 20138 11236 -1501 -2273 -1059 C ATOM 2668 C GLN B 99 -29.743 -11.610 5.086 1.00134.76 C ANISOU 2668 C GLN B 99 20282 19709 11212 -1470 -2455 -920 C ATOM 2669 O GLN B 99 -29.535 -10.582 5.725 1.00133.04 O ANISOU 2669 O GLN B 99 20059 19433 11057 -1429 -2353 -691 O ATOM 2670 CB GLN B 99 -29.727 -11.413 2.580 1.00135.20 C ANISOU 2670 CB GLN B 99 20802 19961 10609 -1449 -2557 -918 C ATOM 2671 CG GLN B 99 -28.904 -11.416 1.300 1.00138.34 C ANISOU 2671 CG GLN B 99 21504 20433 10626 -1472 -2354 -989 C ATOM 2672 CD GLN B 99 -29.673 -10.882 0.108 1.00142.77 C ANISOU 2672 CD GLN B 99 22257 21134 10855 -1416 -2637 -831 C ATOM 2673 OE1 GLN B 99 -30.901 -10.814 0.125 1.00143.90 O ANISOU 2673 OE1 GLN B 99 22276 21339 11062 -1364 -3025 -744 O ATOM 2674 NE2 GLN B 99 -28.949 -10.495 -0.937 1.00145.63 N ANISOU 2674 NE2 GLN B 99 22909 21557 10868 -1423 -2440 -789 N ATOM 2675 N SER B 100 -30.643 -12.517 5.455 1.00188.27 N ANISOU 2675 N SER B 100 26828 26489 18217 -1493 -2715 -1058 N ATOM 2676 CA SER B 100 -31.423 -12.358 6.678 1.00185.56 C ANISOU 2676 CA SER B 100 26188 26092 18225 -1469 -2885 -942 C ATOM 2677 C SER B 100 -30.526 -12.483 7.907 1.00181.04 C ANISOU 2677 C SER B 100 25492 25408 17889 -1511 -2560 -1011 C ATOM 2678 O SER B 100 -30.714 -11.781 8.909 1.00179.51 O ANISOU 2678 O SER B 100 25085 25121 17999 -1404 -2502 -820 O ATOM 2679 CB SER B 100 -32.542 -13.399 6.738 1.00185.98 C ANISOU 2679 CB SER B 100 26006 26175 18483 -1505 -3214 -1092 C ATOM 2680 OG SER B 100 -33.404 -13.286 5.619 1.00189.73 O ANISOU 2680 OG SER B 100 26566 26778 18744 -1465 -3524 -1040 O ATOM 2681 N ARG B 101 -29.549 -13.381 7.813 1.00131.60 N ANISOU 2681 N ARG B 101 19280 19107 11615 -1574 -2283 -1280 N ATOM 2682 CA ARG B 101 -28.604 -13.621 8.896 1.00127.35 C ANISOU 2682 CA ARG B 101 18598 18467 11321 -1583 -1944 -1378 C ATOM 2683 C ARG B 101 -27.883 -12.338 9.293 1.00124.96 C ANISOU 2683 C ARG B 101 18336 18120 11023 -1513 -1684 -1152 C ATOM 2684 O ARG B 101 -27.728 -12.050 10.479 1.00123.73 O ANISOU 2684 O ARG B 101 17937 17854 11220 -1435 -1547 -1074 O ATOM 2685 CB ARG B 101 -27.593 -14.701 8.498 1.00125.98 C ANISOU 2685 CB ARG B 101 18517 18269 11081 -1631 -1686 -1682 C ATOM 2686 CG ARG B 101 -26.602 -15.056 9.595 1.00123.35 C ANISOU 2686 CG ARG B 101 18022 17848 10998 -1630 -1356 -1805 C ATOM 2687 CD ARG B 101 -25.680 -16.194 9.180 1.00123.83 C ANISOU 2687 CD ARG B 101 18138 17857 11054 -1625 -1132 -2090 C ATOM 2688 NE ARG B 101 -26.400 -17.448 8.971 1.00125.56 N ANISOU 2688 NE ARG B 101 18312 18028 11367 -1657 -1357 -2284 N ATOM 2689 CZ ARG B 101 -26.661 -17.972 7.778 1.00128.82 C ANISOU 2689 CZ ARG B 101 18909 18477 11559 -1674 -1493 -2397 C ATOM 2690 NH1 ARG B 101 -26.257 -17.353 6.677 1.00131.14 N ANISOU 2690 NH1 ARG B 101 19445 18868 11515 -1656 -1423 -2329 N ATOM 2691 NH2 ARG B 101 -27.323 -19.117 7.684 1.00129.89 N ANISOU 2691 NH2 ARG B 101 18989 18551 11811 -1716 -1694 -2580 N ATOM 2692 N VAL B 102 -27.454 -11.565 8.300 1.00 82.65 N ANISOU 2692 N VAL B 102 13298 12842 5263 -1549 -1618 -1048 N ATOM 2693 CA VAL B 102 -26.801 -10.288 8.566 1.00 81.65 C ANISOU 2693 CA VAL B 102 13246 12661 5115 -1509 -1379 -824 C ATOM 2694 C VAL B 102 -27.822 -9.173 8.796 1.00 83.47 C ANISOU 2694 C VAL B 102 13431 12848 5437 -1391 -1623 -500 C ATOM 2695 O VAL B 102 -27.502 -8.144 9.394 1.00 83.48 O ANISOU 2695 O VAL B 102 13405 12749 5564 -1331 -1456 -308 O ATOM 2696 CB VAL B 102 -25.814 -9.890 7.446 1.00 87.04 C ANISOU 2696 CB VAL B 102 14232 13392 5446 -1553 -1131 -825 C ATOM 2697 CG1 VAL B 102 -24.672 -10.892 7.367 1.00 86.49 C ANISOU 2697 CG1 VAL B 102 14116 13320 5428 -1595 -820 -1120 C ATOM 2698 CG2 VAL B 102 -26.528 -9.782 6.111 1.00 91.14 C ANISOU 2698 CG2 VAL B 102 14965 14001 5663 -1521 -1395 -749 C ATOM 2699 N ASP B 103 -29.050 -9.383 8.324 1.00100.92 N ANISOU 2699 N ASP B 103 15626 15130 7589 -1355 -2022 -446 N ATOM 2700 CA ASP B 103 -30.141 -8.457 8.612 1.00102.20 C ANISOU 2700 CA ASP B 103 15683 15256 7891 -1213 -2284 -155 C ATOM 2701 C ASP B 103 -30.384 -8.405 10.114 1.00100.75 C ANISOU 2701 C ASP B 103 15126 14935 8217 -1115 -2202 -119 C ATOM 2702 O ASP B 103 -30.709 -7.353 10.665 1.00100.80 O ANISOU 2702 O ASP B 103 15070 14850 8377 -991 -2199 123 O ATOM 2703 CB ASP B 103 -31.431 -8.870 7.896 1.00105.86 C ANISOU 2703 CB ASP B 103 16125 15845 8250 -1197 -2745 -146 C ATOM 2704 CG ASP B 103 -31.442 -8.477 6.433 1.00109.50 C ANISOU 2704 CG ASP B 103 16936 16420 8246 -1205 -2868 -62 C ATOM 2705 OD1 ASP B 103 -30.655 -7.588 6.047 1.00110.82 O ANISOU 2705 OD1 ASP B 103 17358 16549 8199 -1193 -2632 82 O ATOM 2706 OD2 ASP B 103 -32.242 -9.057 5.669 1.00112.60 O ANISOU 2706 OD2 ASP B 103 17296 16923 8563 -1194 -3156 -147 O ATOM 2707 N TYR B 104 -30.225 -9.549 10.772 1.00100.69 N ANISOU 2707 N TYR B 104 14890 14906 8462 -1167 -2128 -362 N ATOM 2708 CA TYR B 104 -30.380 -9.613 12.222 1.00100.04 C ANISOU 2708 CA TYR B 104 14469 14700 8841 -1084 -2029 -348 C ATOM 2709 C TYR B 104 -29.288 -8.832 12.956 1.00 99.33 C ANISOU 2709 C TYR B 104 14401 14501 8840 -1059 -1661 -283 C ATOM 2710 O TYR B 104 -29.570 -8.110 13.916 1.00100.23 O ANISOU 2710 O TYR B 104 14352 14511 9220 -948 -1624 -122 O ATOM 2711 CB TYR B 104 -30.423 -11.068 12.694 1.00 98.83 C ANISOU 2711 CB TYR B 104 14107 14540 8905 -1153 -2030 -617 C ATOM 2712 CG TYR B 104 -31.674 -11.799 12.264 1.00100.22 C ANISOU 2712 CG TYR B 104 14180 14796 9102 -1182 -2409 -668 C ATOM 2713 CD1 TYR B 104 -32.852 -11.107 12.014 1.00103.25 C ANISOU 2713 CD1 TYR B 104 14501 15233 9496 -1092 -2722 -445 C ATOM 2714 CD2 TYR B 104 -31.678 -13.179 12.103 1.00 99.35 C ANISOU 2714 CD2 TYR B 104 14034 14706 9009 -1300 -2458 -942 C ATOM 2715 CE1 TYR B 104 -34.000 -11.767 11.620 1.00104.56 C ANISOU 2715 CE1 TYR B 104 14543 15492 9694 -1131 -3084 -497 C ATOM 2716 CE2 TYR B 104 -32.822 -13.848 11.708 1.00101.60 C ANISOU 2716 CE2 TYR B 104 14220 15062 9322 -1355 -2811 -1001 C ATOM 2717 CZ TYR B 104 -33.979 -13.137 11.468 1.00103.88 C ANISOU 2717 CZ TYR B 104 14420 15425 9623 -1276 -3127 -779 C ATOM 2718 OH TYR B 104 -35.121 -13.797 11.075 1.00104.51 O ANISOU 2718 OH TYR B 104 14372 15595 9742 -1343 -3493 -843 O ATOM 2719 N TYR B 105 -28.047 -8.973 12.498 1.00 77.06 N ANISOU 2719 N TYR B 105 11776 11708 5797 -1165 -1389 -416 N ATOM 2720 CA TYR B 105 -26.929 -8.239 13.085 1.00 75.47 C ANISOU 2720 CA TYR B 105 11598 11424 5654 -1174 -1041 -374 C ATOM 2721 C TYR B 105 -27.098 -6.735 12.896 1.00 76.74 C ANISOU 2721 C TYR B 105 11929 11524 5706 -1118 -1045 -80 C ATOM 2722 O TYR B 105 -26.927 -5.958 13.837 1.00 76.38 O ANISOU 2722 O TYR B 105 11777 11357 5887 -1055 -907 36 O ATOM 2723 CB TYR B 105 -25.597 -8.691 12.482 1.00 74.51 C ANISOU 2723 CB TYR B 105 11650 11372 5290 -1305 -759 -575 C ATOM 2724 CG TYR B 105 -25.216 -10.117 12.811 1.00 73.55 C ANISOU 2724 CG TYR B 105 11363 11272 5309 -1340 -686 -870 C ATOM 2725 CD1 TYR B 105 -24.888 -10.487 14.108 1.00 71.92 C ANISOU 2725 CD1 TYR B 105 10878 10978 5470 -1287 -545 -948 C ATOM 2726 CD2 TYR B 105 -25.169 -11.089 11.821 1.00 74.57 C ANISOU 2726 CD2 TYR B 105 11639 11500 5195 -1420 -757 -1070 C ATOM 2727 CE1 TYR B 105 -24.537 -11.789 14.413 1.00 70.21 C ANISOU 2727 CE1 TYR B 105 10531 10763 5384 -1302 -480 -1200 C ATOM 2728 CE2 TYR B 105 -24.818 -12.393 12.116 1.00 73.25 C ANISOU 2728 CE2 TYR B 105 11343 11324 5166 -1440 -684 -1340 C ATOM 2729 CZ TYR B 105 -24.502 -12.738 13.413 1.00 70.59 C ANISOU 2729 CZ TYR B 105 10728 10889 5203 -1376 -545 -1396 C ATOM 2730 OH TYR B 105 -24.152 -14.035 13.710 1.00 68.80 O ANISOU 2730 OH TYR B 105 10393 10636 5113 -1380 -474 -1648 O ATOM 2731 N LEU B 106 -27.432 -6.331 11.673 1.00 62.94 N ANISOU 2731 N LEU B 106 10462 9853 3600 -1139 -1204 38 N ATOM 2732 CA LEU B 106 -27.662 -4.922 11.371 1.00 64.58 C ANISOU 2732 CA LEU B 106 10873 9990 3675 -1074 -1233 337 C ATOM 2733 C LEU B 106 -28.837 -4.372 12.175 1.00 63.77 C ANISOU 2733 C LEU B 106 10556 9791 3884 -893 -1456 531 C ATOM 2734 O LEU B 106 -28.846 -3.201 12.556 1.00 63.70 O ANISOU 2734 O LEU B 106 10607 9648 3947 -811 -1380 747 O ATOM 2735 CB LEU B 106 -27.898 -4.715 9.872 1.00 68.59 C ANISOU 2735 CB LEU B 106 11731 10612 3720 -1115 -1404 429 C ATOM 2736 CG LEU B 106 -26.683 -4.364 9.009 1.00 71.18 C ANISOU 2736 CG LEU B 106 12400 10975 3670 -1264 -1109 413 C ATOM 2737 CD1 LEU B 106 -25.656 -5.487 9.006 1.00 70.50 C ANISOU 2737 CD1 LEU B 106 12253 10974 3558 -1402 -865 85 C ATOM 2738 CD2 LEU B 106 -27.116 -4.026 7.590 1.00 76.60 C ANISOU 2738 CD2 LEU B 106 13448 11760 3896 -1272 -1321 563 C ATOM 2739 N GLY B 107 -29.823 -5.226 12.431 1.00 59.66 N ANISOU 2739 N GLY B 107 9786 9332 3551 -835 -1721 447 N ATOM 2740 CA GLY B 107 -30.956 -4.854 13.257 1.00 58.27 C ANISOU 2740 CA GLY B 107 9355 9086 3699 -664 -1918 602 C ATOM 2741 C GLY B 107 -30.531 -4.612 14.692 1.00 54.82 C ANISOU 2741 C GLY B 107 8700 8502 3625 -617 -1663 583 C ATOM 2742 O GLY B 107 -30.971 -3.653 15.329 1.00 54.46 O ANISOU 2742 O GLY B 107 8594 8337 3760 -477 -1667 778 O ATOM 2743 N SER B 108 -29.667 -5.487 15.200 1.00 91.76 N ANISOU 2743 N SER B 108 13271 13189 8403 -724 -1443 344 N ATOM 2744 CA SER B 108 -29.135 -5.345 16.551 1.00 91.68 C ANISOU 2744 CA SER B 108 13067 13060 8705 -694 -1199 301 C ATOM 2745 C SER B 108 -28.321 -4.061 16.688 1.00 91.81 C ANISOU 2745 C SER B 108 13272 12964 8649 -703 -956 437 C ATOM 2746 O SER B 108 -28.442 -3.341 17.681 1.00 91.96 O ANISOU 2746 O SER B 108 13188 12851 8902 -607 -880 543 O ATOM 2747 CB SER B 108 -28.276 -6.557 16.919 1.00 90.87 C ANISOU 2747 CB SER B 108 12847 13004 8676 -803 -1023 21 C ATOM 2748 OG SER B 108 -27.806 -6.464 18.253 1.00 90.80 O ANISOU 2748 OG SER B 108 12644 12895 8960 -763 -820 -18 O ATOM 2749 N LEU B 109 -27.495 -3.781 15.684 1.00 54.02 N ANISOU 2749 N LEU B 109 8770 8222 3531 -828 -827 428 N ATOM 2750 CA LEU B 109 -26.687 -2.565 15.663 1.00 54.52 C ANISOU 2750 CA LEU B 109 9045 8176 3493 -874 -591 560 C ATOM 2751 C LEU B 109 -27.558 -1.314 15.641 1.00 56.08 C ANISOU 2751 C LEU B 109 9355 8245 3707 -729 -738 855 C ATOM 2752 O LEU B 109 -27.376 -0.402 16.451 1.00 55.10 O ANISOU 2752 O LEU B 109 9216 7960 3761 -681 -595 955 O ATOM 2753 CB LEU B 109 -25.751 -2.563 14.453 1.00 56.69 C ANISOU 2753 CB LEU B 109 9619 8542 3379 -1040 -445 514 C ATOM 2754 CG LEU B 109 -24.476 -3.399 14.564 1.00 55.36 C ANISOU 2754 CG LEU B 109 9382 8458 3194 -1191 -170 244 C ATOM 2755 CD1 LEU B 109 -23.716 -3.394 13.249 1.00 58.34 C ANISOU 2755 CD1 LEU B 109 10064 8941 3161 -1338 -43 212 C ATOM 2756 CD2 LEU B 109 -23.604 -2.870 15.688 1.00 53.15 C ANISOU 2756 CD2 LEU B 109 8975 8068 3152 -1224 108 218 C ATOM 2757 N ALA B 110 -28.503 -1.279 14.706 1.00 65.57 N ANISOU 2757 N ALA B 110 10674 9516 4721 -654 -1030 988 N ATOM 2758 CA ALA B 110 -29.401 -0.140 14.559 1.00 67.24 C ANISOU 2758 CA ALA B 110 11003 9616 4928 -487 -1202 1282 C ATOM 2759 C ALA B 110 -30.237 0.076 15.817 1.00 67.73 C ANISOU 2759 C ALA B 110 10765 9571 5399 -304 -1276 1338 C ATOM 2760 O ALA B 110 -30.567 1.211 16.164 1.00 68.60 O ANISOU 2760 O ALA B 110 10947 9515 5602 -171 -1264 1546 O ATOM 2761 CB ALA B 110 -30.294 -0.324 13.343 1.00 69.29 C ANISOU 2761 CB ALA B 110 11403 10009 4914 -433 -1541 1390 C ATOM 2762 N LEU B 111 -30.573 -1.015 16.499 1.00 56.55 N ANISOU 2762 N LEU B 111 9024 8239 4224 -296 -1339 1153 N ATOM 2763 CA LEU B 111 -31.277 -0.923 17.773 1.00 54.68 C ANISOU 2763 CA LEU B 111 8489 7913 4375 -143 -1360 1179 C ATOM 2764 C LEU B 111 -30.375 -0.311 18.839 1.00 52.40 C ANISOU 2764 C LEU B 111 8199 7462 4250 -171 -1036 1145 C ATOM 2765 O LEU B 111 -30.793 0.579 19.581 1.00 52.24 O ANISOU 2765 O LEU B 111 8138 7288 4422 -27 -1005 1283 O ATOM 2766 CB LEU B 111 -31.763 -2.298 18.231 1.00 53.08 C ANISOU 2766 CB LEU B 111 7963 7834 4373 -159 -1475 985 C ATOM 2767 CG LEU B 111 -32.398 -2.338 19.623 1.00 51.04 C ANISOU 2767 CG LEU B 111 7389 7495 4511 -24 -1449 988 C ATOM 2768 CD1 LEU B 111 -33.631 -1.448 19.683 1.00 52.97 C ANISOU 2768 CD1 LEU B 111 7575 7678 4873 195 -1649 1230 C ATOM 2769 CD2 LEU B 111 -32.741 -3.766 20.024 1.00 49.60 C ANISOU 2769 CD2 LEU B 111 6921 7422 4504 -78 -1523 791 C ATOM 2770 N SER B 112 -29.135 -0.791 18.904 1.00 77.53 N ANISOU 2770 N SER B 112 11421 10683 7353 -354 -798 953 N ATOM 2771 CA SER B 112 -28.169 -0.299 19.881 1.00 76.04 C ANISOU 2771 CA SER B 112 11218 10370 7302 -412 -500 891 C ATOM 2772 C SER B 112 -27.878 1.185 19.679 1.00 76.60 C ANISOU 2772 C SER B 112 11566 10267 7269 -406 -384 1089 C ATOM 2773 O SER B 112 -27.559 1.897 20.630 1.00 75.93 O ANISOU 2773 O SER B 112 11459 10028 7361 -383 -217 1106 O ATOM 2774 CB SER B 112 -26.870 -1.106 19.813 1.00 73.08 C ANISOU 2774 CB SER B 112 10830 10098 6838 -607 -288 652 C ATOM 2775 OG SER B 112 -26.201 -0.896 18.582 1.00 75.31 O ANISOU 2775 OG SER B 112 11392 10436 6784 -748 -213 671 O ATOM 2776 N ASP B 113 -27.986 1.643 18.436 1.00 96.25 N ANISOU 2776 N ASP B 113 14334 12773 9462 -431 -474 1237 N ATOM 2777 CA ASP B 113 -27.835 3.061 18.133 1.00 96.87 C ANISOU 2777 CA ASP B 113 14713 12665 9426 -413 -388 1461 C ATOM 2778 C ASP B 113 -29.093 3.823 18.539 1.00 97.36 C ANISOU 2778 C ASP B 113 14729 12586 9675 -156 -579 1675 C ATOM 2779 O ASP B 113 -29.017 4.906 19.129 1.00 96.72 O ANISOU 2779 O ASP B 113 14745 12289 9716 -93 -450 1787 O ATOM 2780 CB ASP B 113 -27.556 3.266 16.643 1.00102.29 C ANISOU 2780 CB ASP B 113 15733 13420 9713 -512 -429 1569 C ATOM 2781 CG ASP B 113 -26.291 2.566 16.184 1.00101.14 C ANISOU 2781 CG ASP B 113 15642 13416 9371 -758 -213 1358 C ATOM 2782 OD1 ASP B 113 -25.404 2.323 17.029 1.00 99.62 O ANISOU 2782 OD1 ASP B 113 15287 13216 9346 -865 20 1171 O ATOM 2783 OD2 ASP B 113 -26.184 2.263 14.976 1.00101.40 O ANISOU 2783 OD2 ASP B 113 15879 13573 9075 -836 -277 1378 O ATOM 2784 N LEU B 114 -30.248 3.244 18.220 1.00 50.90 N ANISOU 2784 N LEU B 114 8689 6827 3821 -9 -885 1719 N ATOM 2785 CA LEU B 114 -31.536 3.853 18.537 1.00 52.08 C ANISOU 2785 CA LEU B 114 8748 6885 4157 256 -1093 1917 C ATOM 2786 C LEU B 114 -31.706 4.105 20.032 1.00 48.87 C ANISOU 2786 C LEU B 114 8112 6339 4118 366 -957 1868 C ATOM 2787 O LEU B 114 -32.223 5.145 20.434 1.00 50.32 O ANISOU 2787 O LEU B 114 8352 6338 4429 550 -964 2043 O ATOM 2788 CB LEU B 114 -32.688 2.988 18.020 1.00 53.30 C ANISOU 2788 CB LEU B 114 8701 7240 4310 358 -1441 1923 C ATOM 2789 CG LEU B 114 -33.435 3.516 16.794 1.00 58.43 C ANISOU 2789 CG LEU B 114 9564 7920 4716 479 -1722 2166 C ATOM 2790 CD1 LEU B 114 -34.623 2.626 16.464 1.00 59.69 C ANISOU 2790 CD1 LEU B 114 9457 8285 4938 580 -2080 2148 C ATOM 2791 CD2 LEU B 114 -33.884 4.951 17.018 1.00 60.69 C ANISOU 2791 CD2 LEU B 114 10003 7967 5088 691 -1706 2431 C ATOM 2792 N LEU B 115 -31.269 3.151 20.849 1.00 64.78 N ANISOU 2792 N LEU B 115 9881 8439 6293 263 -834 1630 N ATOM 2793 CA LEU B 115 -31.372 3.282 22.300 1.00 63.85 C ANISOU 2793 CA LEU B 115 9554 8209 6495 353 -696 1564 C ATOM 2794 C LEU B 115 -30.573 4.477 22.812 1.00 63.67 C ANISOU 2794 C LEU B 115 9754 7954 6481 316 -439 1612 C ATOM 2795 O LEU B 115 -31.045 5.235 23.659 1.00 64.23 O ANISOU 2795 O LEU B 115 9809 7849 6745 484 -402 1707 O ATOM 2796 CB LEU B 115 -30.901 2.001 22.993 1.00 61.77 C ANISOU 2796 CB LEU B 115 9033 8083 6353 230 -605 1306 C ATOM 2797 CG LEU B 115 -31.704 0.732 22.704 1.00 62.04 C ANISOU 2797 CG LEU B 115 8829 8319 6422 245 -832 1227 C ATOM 2798 CD1 LEU B 115 -31.144 -0.445 23.487 1.00 60.78 C ANISOU 2798 CD1 LEU B 115 8457 8248 6387 129 -707 984 C ATOM 2799 CD2 LEU B 115 -33.177 0.942 23.019 1.00 62.40 C ANISOU 2799 CD2 LEU B 115 8674 8356 6679 476 -1045 1370 C ATOM 2800 N ILE B 116 -29.362 4.638 22.289 1.00 50.59 N ANISOU 2800 N ILE B 116 8305 6298 4618 88 -256 1538 N ATOM 2801 CA ILE B 116 -28.496 5.743 22.682 1.00 50.91 C ANISOU 2801 CA ILE B 116 8566 6128 4650 -5 -4 1563 C ATOM 2802 C ILE B 116 -29.062 7.082 22.222 1.00 53.99 C ANISOU 2802 C ILE B 116 9240 6298 4977 136 -58 1836 C ATOM 2803 O ILE B 116 -29.114 8.043 22.991 1.00 54.29 O ANISOU 2803 O ILE B 116 9353 6106 5171 219 59 1895 O ATOM 2804 CB ILE B 116 -27.075 5.577 22.109 1.00 50.81 C ANISOU 2804 CB ILE B 116 8708 6187 4410 -293 194 1442 C ATOM 2805 CG1 ILE B 116 -26.443 4.280 22.617 1.00 47.94 C ANISOU 2805 CG1 ILE B 116 8069 6022 4124 -411 263 1171 C ATOM 2806 CG2 ILE B 116 -26.204 6.771 22.475 1.00 51.59 C ANISOU 2806 CG2 ILE B 116 9035 6062 4505 -415 450 1475 C ATOM 2807 CD1 ILE B 116 -25.032 4.054 22.118 1.00 47.92 C ANISOU 2807 CD1 ILE B 116 8168 6109 3929 -675 471 1032 C ATOM 2808 N LEU B 117 -29.492 7.138 20.967 1.00 56.15 N ANISOU 2808 N LEU B 117 9684 6634 5014 171 -241 2002 N ATOM 2809 CA LEU B 117 -29.980 8.387 20.391 1.00 59.49 C ANISOU 2809 CA LEU B 117 10411 6849 5342 313 -307 2285 C ATOM 2810 C LEU B 117 -31.317 8.837 20.982 1.00 60.28 C ANISOU 2810 C LEU B 117 10367 6841 5694 639 -482 2426 C ATOM 2811 O LEU B 117 -31.585 10.033 21.080 1.00 62.35 O ANISOU 2811 O LEU B 117 10840 6846 6003 780 -441 2612 O ATOM 2812 CB LEU B 117 -30.073 8.271 18.868 1.00 62.19 C ANISOU 2812 CB LEU B 117 10984 7310 5335 269 -473 2427 C ATOM 2813 CG LEU B 117 -28.730 8.020 18.179 1.00 62.14 C ANISOU 2813 CG LEU B 117 11173 7383 5052 -45 -261 2317 C ATOM 2814 CD1 LEU B 117 -28.923 7.724 16.705 1.00 64.78 C ANISOU 2814 CD1 LEU B 117 11713 7872 5027 -75 -442 2434 C ATOM 2815 CD2 LEU B 117 -27.798 9.207 18.374 1.00 63.10 C ANISOU 2815 CD2 LEU B 117 11581 7241 5150 -183 36 2382 C ATOM 2816 N LEU B 118 -32.147 7.879 21.381 1.00 56.50 N ANISOU 2816 N LEU B 118 9529 6551 5385 758 -663 2337 N ATOM 2817 CA LEU B 118 -33.461 8.197 21.933 1.00 57.37 C ANISOU 2817 CA LEU B 118 9448 6597 5751 1068 -822 2458 C ATOM 2818 C LEU B 118 -33.412 8.588 23.407 1.00 55.49 C ANISOU 2818 C LEU B 118 9082 6191 5810 1136 -605 2356 C ATOM 2819 O LEU B 118 -34.146 9.473 23.843 1.00 57.07 O ANISOU 2819 O LEU B 118 9317 6193 6172 1373 -608 2498 O ATOM 2820 CB LEU B 118 -34.428 7.022 21.750 1.00 56.94 C ANISOU 2820 CB LEU B 118 9046 6814 5773 1152 -1096 2405 C ATOM 2821 CG LEU B 118 -35.017 6.794 20.358 1.00 59.78 C ANISOU 2821 CG LEU B 118 9489 7331 5894 1199 -1410 2556 C ATOM 2822 CD1 LEU B 118 -35.924 5.575 20.364 1.00 59.16 C ANISOU 2822 CD1 LEU B 118 9028 7512 5939 1246 -1658 2458 C ATOM 2823 CD2 LEU B 118 -35.775 8.026 19.890 1.00 64.07 C ANISOU 2823 CD2 LEU B 118 10235 7699 6410 1459 -1547 2858 C ATOM 2824 N PHE B 119 -32.549 7.929 24.173 1.00 53.97 N ANISOU 2824 N PHE B 119 8747 6078 5682 940 -421 2109 N ATOM 2825 CA PHE B 119 -32.563 8.089 25.624 1.00 52.12 C ANISOU 2825 CA PHE B 119 8356 5732 5716 1004 -244 1989 C ATOM 2826 C PHE B 119 -31.310 8.753 26.200 1.00 51.22 C ANISOU 2826 C PHE B 119 8449 5441 5569 810 50 1877 C ATOM 2827 O PHE B 119 -31.412 9.654 27.029 1.00 51.66 O ANISOU 2827 O PHE B 119 8584 5270 5773 910 186 1895 O ATOM 2828 CB PHE B 119 -32.822 6.741 26.303 1.00 49.42 C ANISOU 2828 CB PHE B 119 7630 5616 5532 989 -290 1802 C ATOM 2829 CG PHE B 119 -34.079 6.062 25.834 1.00 50.45 C ANISOU 2829 CG PHE B 119 7522 5918 5727 1156 -573 1891 C ATOM 2830 CD1 PHE B 119 -35.320 6.623 26.089 1.00 52.36 C ANISOU 2830 CD1 PHE B 119 7661 6078 6155 1445 -688 2054 C ATOM 2831 CD2 PHE B 119 -34.020 4.863 25.143 1.00 49.74 C ANISOU 2831 CD2 PHE B 119 7305 6073 5521 1021 -724 1802 C ATOM 2832 CE1 PHE B 119 -36.479 6.003 25.659 1.00 53.59 C ANISOU 2832 CE1 PHE B 119 7565 6410 6386 1586 -958 2131 C ATOM 2833 CE2 PHE B 119 -35.177 4.237 24.711 1.00 50.94 C ANISOU 2833 CE2 PHE B 119 7231 6386 5738 1149 -997 1870 C ATOM 2834 CZ PHE B 119 -36.408 4.809 24.971 1.00 52.88 C ANISOU 2834 CZ PHE B 119 7350 6565 6176 1426 -1119 2037 C ATOM 2835 N ALA B 120 -30.135 8.308 25.769 1.00 47.23 N ANISOU 2835 N ALA B 120 8026 5042 4875 531 150 1752 N ATOM 2836 CA ALA B 120 -28.886 8.866 26.277 1.00 46.51 C ANISOU 2836 CA ALA B 120 8089 4822 4759 315 419 1626 C ATOM 2837 C ALA B 120 -28.653 10.288 25.769 1.00 49.40 C ANISOU 2837 C ALA B 120 8844 4913 5012 286 519 1803 C ATOM 2838 O ALA B 120 -28.114 11.132 26.485 1.00 49.48 O ANISOU 2838 O ALA B 120 8993 4728 5079 179 730 1737 O ATOM 2839 CB ALA B 120 -27.713 7.968 25.909 1.00 44.81 C ANISOU 2839 CB ALA B 120 7811 4821 4393 39 500 1437 C ATOM 2840 N LEU B 121 -29.062 10.545 24.531 1.00 56.71 N ANISOU 2840 N LEU B 121 9956 5818 5773 378 360 2029 N ATOM 2841 CA LEU B 121 -28.852 11.850 23.905 1.00 59.84 C ANISOU 2841 CA LEU B 121 10757 5944 6038 355 446 2231 C ATOM 2842 C LEU B 121 -29.585 13.019 24.582 1.00 61.58 C ANISOU 2842 C LEU B 121 11100 5846 6454 600 473 2367 C ATOM 2843 O LEU B 121 -28.960 14.037 24.862 1.00 62.79 O ANISOU 2843 O LEU B 121 11518 5728 6612 495 680 2380 O ATOM 2844 CB LEU B 121 -29.147 11.796 22.398 1.00 62.36 C ANISOU 2844 CB LEU B 121 11272 6348 6075 366 269 2438 C ATOM 2845 CG LEU B 121 -28.730 12.997 21.545 1.00 65.79 C ANISOU 2845 CG LEU B 121 12164 6530 6306 289 374 2655 C ATOM 2846 CD1 LEU B 121 -28.255 12.524 20.184 1.00 67.00 C ANISOU 2846 CD1 LEU B 121 12477 6867 6114 104 331 2709 C ATOM 2847 CD2 LEU B 121 -29.871 13.993 21.387 1.00 68.87 C ANISOU 2847 CD2 LEU B 121 12727 6680 6762 615 222 2938 C ATOM 2848 N PRO B 122 -30.904 12.888 24.842 1.00 57.63 N ANISOU 2848 N PRO B 122 10407 5368 6120 925 273 2465 N ATOM 2849 CA PRO B 122 -31.583 14.014 25.496 1.00 60.39 C ANISOU 2849 CA PRO B 122 10876 5407 6661 1180 319 2587 C ATOM 2850 C PRO B 122 -31.015 14.308 26.883 1.00 58.45 C ANISOU 2850 C PRO B 122 10592 5009 6606 1101 571 2376 C ATOM 2851 O PRO B 122 -30.966 15.466 27.297 1.00 61.24 O ANISOU 2851 O PRO B 122 11188 5037 7044 1180 704 2441 O ATOM 2852 CB PRO B 122 -33.029 13.525 25.621 1.00 60.58 C ANISOU 2852 CB PRO B 122 10595 5571 6852 1515 68 2674 C ATOM 2853 CG PRO B 122 -33.177 12.506 24.555 1.00 59.80 C ANISOU 2853 CG PRO B 122 10372 5784 6564 1441 -158 2704 C ATOM 2854 CD PRO B 122 -31.854 11.816 24.494 1.00 56.37 C ANISOU 2854 CD PRO B 122 9939 5496 5983 1077 1 2484 C ATOM 2855 N VAL B 123 -30.592 13.263 27.587 1.00 71.94 N ANISOU 2855 N VAL B 123 12014 6945 8374 949 628 2125 N ATOM 2856 CA VAL B 123 -29.994 13.420 28.906 1.00 71.23 C ANISOU 2856 CA VAL B 123 11874 6756 8434 858 844 1907 C ATOM 2857 C VAL B 123 -28.638 14.114 28.808 1.00 72.09 C ANISOU 2857 C VAL B 123 12277 6696 8417 545 1064 1834 C ATOM 2858 O VAL B 123 -28.343 15.028 29.577 1.00 72.59 O ANISOU 2858 O VAL B 123 12509 6495 8577 525 1235 1777 O ATOM 2859 CB VAL B 123 -29.825 12.062 29.613 1.00 70.27 C ANISOU 2859 CB VAL B 123 11375 6938 8387 780 830 1674 C ATOM 2860 CG1 VAL B 123 -29.126 12.239 30.948 1.00 69.36 C ANISOU 2860 CG1 VAL B 123 11232 6731 8389 676 1040 1452 C ATOM 2861 CG2 VAL B 123 -31.176 11.393 29.799 1.00 70.47 C ANISOU 2861 CG2 VAL B 123 11096 7119 8561 1062 635 1737 C ATOM 2862 N ASP B 124 -27.822 13.686 27.849 1.00 70.18 N ANISOU 2862 N ASP B 124 12093 6611 7959 294 1066 1826 N ATOM 2863 CA ASP B 124 -26.507 14.281 27.639 1.00 69.51 C ANISOU 2863 CA ASP B 124 12256 6405 7748 -32 1280 1761 C ATOM 2864 C ASP B 124 -26.628 15.749 27.240 1.00 70.19 C ANISOU 2864 C ASP B 124 12760 6112 7795 7 1360 1975 C ATOM 2865 O ASP B 124 -25.807 16.577 27.634 1.00 70.19 O ANISOU 2865 O ASP B 124 12972 5885 7813 -193 1570 1903 O ATOM 2866 CB ASP B 124 -25.726 13.506 26.576 1.00 69.55 C ANISOU 2866 CB ASP B 124 12234 6670 7521 -271 1263 1736 C ATOM 2867 CG ASP B 124 -24.320 14.039 26.381 1.00 69.62 C ANISOU 2867 CG ASP B 124 12442 6596 7413 -631 1504 1649 C ATOM 2868 OD1 ASP B 124 -23.740 14.557 27.357 1.00 68.97 O ANISOU 2868 OD1 ASP B 124 12380 6365 7460 -749 1672 1499 O ATOM 2869 OD2 ASP B 124 -23.793 13.941 25.252 1.00 70.19 O ANISOU 2869 OD2 ASP B 124 12648 6759 7260 -802 1529 1725 O ATOM 2870 N VAL B 125 -27.658 16.064 26.462 1.00 71.87 N ANISOU 2870 N VAL B 125 13092 6255 7959 265 1183 2240 N ATOM 2871 CA VAL B 125 -27.919 17.439 26.053 1.00 72.91 C ANISOU 2871 CA VAL B 125 13629 6010 8062 366 1230 2480 C ATOM 2872 C VAL B 125 -28.375 18.279 27.242 1.00 72.43 C ANISOU 2872 C VAL B 125 13617 5648 8254 554 1328 2434 C ATOM 2873 O VAL B 125 -27.893 19.392 27.448 1.00 73.03 O ANISOU 2873 O VAL B 125 14021 5381 8348 451 1514 2457 O ATOM 2874 CB VAL B 125 -28.988 17.510 24.938 1.00 74.21 C ANISOU 2874 CB VAL B 125 13876 6203 8117 644 976 2782 C ATOM 2875 CG1 VAL B 125 -29.479 18.939 24.751 1.00 76.87 C ANISOU 2875 CG1 VAL B 125 14573 6128 8509 873 992 3032 C ATOM 2876 CG2 VAL B 125 -28.437 16.956 23.634 1.00 73.87 C ANISOU 2876 CG2 VAL B 125 13944 6359 7763 427 925 2864 C ATOM 2877 N TYR B 126 -29.294 17.731 28.030 1.00 95.41 N ANISOU 2877 N TYR B 126 16209 8686 11359 818 1215 2360 N ATOM 2878 CA TYR B 126 -29.874 18.467 29.149 1.00 95.12 C ANISOU 2878 CA TYR B 126 16196 8389 11558 1042 1303 2315 C ATOM 2879 C TYR B 126 -28.907 18.674 30.315 1.00 93.81 C ANISOU 2879 C TYR B 126 16040 8135 11469 796 1539 2031 C ATOM 2880 O TYR B 126 -28.651 19.806 30.721 1.00 95.33 O ANISOU 2880 O TYR B 126 16537 7973 11714 752 1708 2023 O ATOM 2881 CB TYR B 126 -31.153 17.786 29.644 1.00 95.62 C ANISOU 2881 CB TYR B 126 15891 8641 11800 1385 1132 2317 C ATOM 2882 CG TYR B 126 -31.738 18.430 30.881 1.00 94.80 C ANISOU 2882 CG TYR B 126 15779 8306 11938 1622 1246 2243 C ATOM 2883 CD1 TYR B 126 -32.465 19.610 30.794 1.00 96.09 C ANISOU 2883 CD1 TYR B 126 16195 8122 12193 1910 1255 2440 C ATOM 2884 CD2 TYR B 126 -31.560 17.861 32.135 1.00 92.88 C ANISOU 2884 CD2 TYR B 126 15287 8187 11818 1570 1350 1978 C ATOM 2885 CE1 TYR B 126 -32.998 20.204 31.922 1.00 95.72 C ANISOU 2885 CE1 TYR B 126 16150 7857 12363 2138 1378 2360 C ATOM 2886 CE2 TYR B 126 -32.089 18.448 33.268 1.00 92.39 C ANISOU 2886 CE2 TYR B 126 15235 7919 11952 1786 1469 1901 C ATOM 2887 CZ TYR B 126 -32.808 19.619 33.156 1.00 93.52 C ANISOU 2887 CZ TYR B 126 15627 7717 12189 2069 1489 2085 C ATOM 2888 OH TYR B 126 -33.337 20.207 34.282 1.00 93.62 O ANISOU 2888 OH TYR B 126 15658 7520 12395 2296 1625 1995 O ATOM 2889 N ASN B 127 -28.376 17.583 30.856 1.00 69.75 N ANISOU 2889 N ASN B 127 12668 5403 8429 639 1542 1796 N ATOM 2890 CA ASN B 127 -27.550 17.661 32.059 1.00 68.61 C ANISOU 2890 CA ASN B 127 12492 5217 8359 434 1729 1518 C ATOM 2891 C ASN B 127 -26.077 17.959 31.810 1.00 69.12 C ANISOU 2891 C ASN B 127 12742 5236 8283 15 1890 1412 C ATOM 2892 O ASN B 127 -25.511 18.878 32.398 1.00 70.40 O ANISOU 2892 O ASN B 127 13151 5111 8487 -123 2064 1333 O ATOM 2893 CB ASN B 127 -27.679 16.383 32.889 1.00 67.80 C ANISOU 2893 CB ASN B 127 11973 5451 8336 466 1669 1314 C ATOM 2894 CG ASN B 127 -28.502 16.586 34.144 1.00 66.82 C ANISOU 2894 CG ASN B 127 11753 5221 8413 737 1705 1240 C ATOM 2895 OD1 ASN B 127 -28.037 17.183 35.115 1.00 65.63 O ANISOU 2895 OD1 ASN B 127 11731 4883 8324 660 1868 1078 O ATOM 2896 ND2 ASN B 127 -29.729 16.081 34.135 1.00 66.60 N ANISOU 2896 ND2 ASN B 127 11497 5321 8485 1048 1557 1351 N ATOM 2897 N PHE B 128 -25.453 17.179 30.940 1.00 89.29 N ANISOU 2897 N PHE B 128 15176 8072 10677 -191 1839 1404 N ATOM 2898 CA PHE B 128 -24.013 17.290 30.747 1.00 89.21 C ANISOU 2898 CA PHE B 128 15247 8096 10553 -598 2001 1263 C ATOM 2899 C PHE B 128 -23.595 18.404 29.789 1.00 90.27 C ANISOU 2899 C PHE B 128 15792 7945 10559 -772 2121 1442 C ATOM 2900 O PHE B 128 -22.433 18.483 29.393 1.00 90.62 O ANISOU 2900 O PHE B 128 15909 8021 10499 -1126 2267 1354 O ATOM 2901 CB PHE B 128 -23.433 15.944 30.314 1.00 92.39 C ANISOU 2901 CB PHE B 128 15343 8916 10845 -746 1929 1156 C ATOM 2902 CG PHE B 128 -23.615 14.855 31.337 1.00 91.41 C ANISOU 2902 CG PHE B 128 14838 9049 10842 -645 1854 952 C ATOM 2903 CD1 PHE B 128 -23.463 15.125 32.687 1.00 90.79 C ANISOU 2903 CD1 PHE B 128 14711 8877 10908 -650 1945 760 C ATOM 2904 CD2 PHE B 128 -23.959 13.567 30.952 1.00 91.40 C ANISOU 2904 CD2 PHE B 128 14551 9372 10802 -550 1694 953 C ATOM 2905 CE1 PHE B 128 -23.632 14.132 33.631 1.00 89.75 C ANISOU 2905 CE1 PHE B 128 14256 8976 10867 -555 1883 590 C ATOM 2906 CE2 PHE B 128 -24.131 12.571 31.893 1.00 90.85 C ANISOU 2906 CE2 PHE B 128 14156 9515 10845 -462 1636 780 C ATOM 2907 CZ PHE B 128 -23.967 12.856 33.233 1.00 89.63 C ANISOU 2907 CZ PHE B 128 13961 9270 10822 -461 1733 608 C ATOM 2908 N ILE B 129 -24.538 19.264 29.424 1.00 66.46 N ANISOU 2908 N ILE B 129 13044 4651 7558 -520 2065 1698 N ATOM 2909 CA ILE B 129 -24.225 20.410 28.579 1.00 71.58 C ANISOU 2909 CA ILE B 129 14130 4975 8092 -654 2183 1897 C ATOM 2910 C ILE B 129 -24.917 21.676 29.062 1.00 75.47 C ANISOU 2910 C ILE B 129 14934 5008 8733 -453 2251 1997 C ATOM 2911 O ILE B 129 -24.281 22.717 29.218 1.00 78.57 O ANISOU 2911 O ILE B 129 15601 5113 9140 -674 2438 1950 O ATOM 2912 CB ILE B 129 -24.592 20.161 27.106 1.00 73.16 C ANISOU 2912 CB ILE B 129 14439 5277 8081 -570 2042 2180 C ATOM 2913 CG1 ILE B 129 -23.691 19.075 26.507 1.00 70.42 C ANISOU 2913 CG1 ILE B 129 13871 5329 7559 -834 2036 2069 C ATOM 2914 CG2 ILE B 129 -24.474 21.453 26.306 1.00 78.97 C ANISOU 2914 CG2 ILE B 129 15665 5634 8708 -644 2155 2425 C ATOM 2915 CD1 ILE B 129 -23.888 18.886 25.034 1.00 72.75 C ANISOU 2915 CD1 ILE B 129 14341 5705 7596 -835 1947 2320 C ATOM 2916 N TRP B 130 -26.219 21.580 29.304 1.00119.98 N ANISOU 2916 N TRP B 130 20488 10608 14493 -32 2092 2113 N ATOM 2917 CA TRP B 130 -26.995 22.735 29.740 1.00122.57 C ANISOU 2917 CA TRP B 130 21062 10525 14984 221 2148 2189 C ATOM 2918 C TRP B 130 -26.909 22.986 31.248 1.00121.13 C ANISOU 2918 C TRP B 130 20764 10272 14989 197 2276 1892 C ATOM 2919 O TRP B 130 -26.411 24.022 31.690 1.00122.15 O ANISOU 2919 O TRP B 130 21046 10234 15134 -88 2454 1713 O ATOM 2920 CB TRP B 130 -28.463 22.604 29.316 1.00123.47 C ANISOU 2920 CB TRP B 130 21089 10656 15171 699 1926 2422 C ATOM 2921 CG TRP B 130 -28.741 22.859 27.866 1.00126.10 C ANISOU 2921 CG TRP B 130 21550 11033 15332 779 1762 2717 C ATOM 2922 CD1 TRP B 130 -27.832 23.089 26.874 1.00128.22 C ANISOU 2922 CD1 TRP B 130 22012 11328 15380 479 1809 2799 C ATOM 2923 CD2 TRP B 130 -30.031 22.902 27.247 1.00128.24 C ANISOU 2923 CD2 TRP B 130 21746 11345 15634 1186 1520 2962 C ATOM 2924 NE1 TRP B 130 -28.480 23.272 25.675 1.00130.76 N ANISOU 2924 NE1 TRP B 130 22413 11696 15577 678 1610 3083 N ATOM 2925 CE2 TRP B 130 -29.831 23.162 25.878 1.00130.90 C ANISOU 2925 CE2 TRP B 130 22263 11725 15748 1109 1418 3187 C ATOM 2926 CE3 TRP B 130 -31.338 22.745 27.721 1.00127.93 C ANISOU 2926 CE3 TRP B 130 21481 11333 15796 1603 1378 3002 C ATOM 2927 CZ2 TRP B 130 -30.889 23.269 24.976 1.00133.45 C ANISOU 2927 CZ2 TRP B 130 22559 12112 16036 1431 1161 3452 C ATOM 2928 CZ3 TRP B 130 -32.388 22.853 26.823 1.00130.49 C ANISOU 2928 CZ3 TRP B 130 21748 11730 16104 1916 1126 3260 C ATOM 2929 CH2 TRP B 130 -32.156 23.112 25.466 1.00133.56 C ANISOU 2929 CH2 TRP B 130 22332 12155 16262 1829 1009 3483 C ATOM 2930 N VAL B 131 -27.401 22.029 32.028 1.00 74.43 N ANISOU 2930 N VAL B 131 14522 4551 9208 489 2160 1817 N ATOM 2931 CA VAL B 131 -27.428 22.139 33.482 1.00 73.15 C ANISOU 2931 CA VAL B 131 14245 4341 9209 532 2263 1555 C ATOM 2932 C VAL B 131 -26.539 21.098 34.145 1.00 68.29 C ANISOU 2932 C VAL B 131 13306 4090 8550 251 2280 1269 C ATOM 2933 O VAL B 131 -26.972 19.979 34.415 1.00 64.36 O ANISOU 2933 O VAL B 131 12441 3938 8075 376 2149 1220 O ATOM 2934 CB VAL B 131 -28.860 22.000 34.001 1.00 72.95 C ANISOU 2934 CB VAL B 131 14024 4342 9354 998 2155 1619 C ATOM 2935 CG1 VAL B 131 -28.942 22.357 35.472 1.00 72.89 C ANISOU 2935 CG1 VAL B 131 13988 4212 9495 1059 2299 1368 C ATOM 2936 CG2 VAL B 131 -29.773 22.898 33.191 1.00 77.64 C ANISOU 2936 CG2 VAL B 131 14862 4651 9989 1320 2085 1926 C ATOM 2937 N HIS B 132 -25.296 21.477 34.418 1.00 88.52 N ANISOU 2937 N HIS B 132 16004 6569 11060 -129 2438 1084 N ATOM 2938 CA HIS B 132 -24.325 20.544 34.978 1.00 87.48 C ANISOU 2938 CA HIS B 132 15580 6775 10885 -405 2452 816 C ATOM 2939 C HIS B 132 -24.686 20.134 36.400 1.00 85.60 C ANISOU 2939 C HIS B 132 15114 6640 10770 -250 2448 595 C ATOM 2940 O HIS B 132 -24.258 19.085 36.878 1.00 83.70 O ANISOU 2940 O HIS B 132 14556 6743 10504 -346 2396 423 O ATOM 2941 CB HIS B 132 -22.918 21.136 34.924 1.00 88.70 C ANISOU 2941 CB HIS B 132 15929 6807 10967 -851 2621 674 C ATOM 2942 CG HIS B 132 -22.507 21.574 33.554 1.00 90.53 C ANISOU 2942 CG HIS B 132 16396 6939 11062 -1035 2661 887 C ATOM 2943 ND1 HIS B 132 -22.676 22.866 33.106 1.00 93.88 N ANISOU 2943 ND1 HIS B 132 17254 6927 11489 -1032 2764 1066 N ATOM 2944 CD2 HIS B 132 -21.954 20.888 32.527 1.00 90.05 C ANISOU 2944 CD2 HIS B 132 16216 7151 10847 -1221 2621 954 C ATOM 2945 CE1 HIS B 132 -22.233 22.960 31.864 1.00 95.51 C ANISOU 2945 CE1 HIS B 132 17590 7160 11539 -1215 2783 1241 C ATOM 2946 NE2 HIS B 132 -21.789 21.774 31.490 1.00 92.89 N ANISOU 2946 NE2 HIS B 132 16937 7250 11106 -1335 2706 1174 N ATOM 2947 N HIS B 133 -25.473 20.970 37.070 1.00 92.39 N ANISOU 2947 N HIS B 133 16153 7195 11757 1 2511 606 N ATOM 2948 CA HIS B 133 -25.967 20.660 38.407 1.00 91.42 C ANISOU 2948 CA HIS B 133 15850 7146 11740 191 2525 423 C ATOM 2949 C HIS B 133 -27.261 21.423 38.677 1.00 93.13 C ANISOU 2949 C HIS B 133 16221 7065 12098 598 2552 556 C ATOM 2950 O HIS B 133 -27.386 22.587 38.297 1.00 97.32 O ANISOU 2950 O HIS B 133 17112 7207 12659 637 2636 672 O ATOM 2951 CB HIS B 133 -24.911 20.986 39.469 1.00 89.24 C ANISOU 2951 CB HIS B 133 15651 6809 11447 -101 2658 112 C ATOM 2952 CG HIS B 133 -24.662 22.451 39.653 1.00 92.87 C ANISOU 2952 CG HIS B 133 16541 6800 11946 -191 2821 77 C ATOM 2953 ND1 HIS B 133 -23.671 23.130 38.977 1.00 95.60 N ANISOU 2953 ND1 HIS B 133 17134 6968 12220 -549 2907 81 N ATOM 2954 CD2 HIS B 133 -25.269 23.365 40.446 1.00 95.31 C ANISOU 2954 CD2 HIS B 133 17086 6765 12363 24 2927 32 C ATOM 2955 CE1 HIS B 133 -23.683 24.399 39.341 1.00 99.19 C ANISOU 2955 CE1 HIS B 133 17886 7079 12724 -551 3013 41 C ATOM 2956 NE2 HIS B 133 -24.644 24.568 40.232 1.00 98.86 N ANISOU 2956 NE2 HIS B 133 17814 6968 12781 -202 3009 7 N ATOM 2957 N PRO B 134 -28.230 20.770 39.338 1.00 66.14 N ANISOU 2957 N PRO B 134 12530 3824 8776 906 2493 541 N ATOM 2958 CA PRO B 134 -28.131 19.399 39.842 1.00 61.36 C ANISOU 2958 CA PRO B 134 11524 3646 8143 868 2407 409 C ATOM 2959 C PRO B 134 -28.599 18.358 38.830 1.00 60.14 C ANISOU 2959 C PRO B 134 11094 3799 7959 956 2217 604 C ATOM 2960 O PRO B 134 -29.228 18.701 37.828 1.00 61.30 O ANISOU 2960 O PRO B 134 11335 3837 8119 1118 2135 852 O ATOM 2961 CB PRO B 134 -29.090 19.415 41.029 1.00 62.21 C ANISOU 2961 CB PRO B 134 11540 3716 8382 1181 2473 325 C ATOM 2962 CG PRO B 134 -30.166 20.349 40.591 1.00 66.38 C ANISOU 2962 CG PRO B 134 12258 3933 9030 1514 2488 547 C ATOM 2963 CD PRO B 134 -29.491 21.411 39.751 1.00 69.39 C ANISOU 2963 CD PRO B 134 13025 3995 9343 1319 2535 640 C ATOM 2964 N TRP B 135 -28.287 17.094 39.101 1.00 58.24 N ANISOU 2964 N TRP B 135 10528 3929 7671 850 2141 488 N ATOM 2965 CA TRP B 135 -28.783 15.983 38.299 1.00 56.37 C ANISOU 2965 CA TRP B 135 10003 3999 7417 935 1961 631 C ATOM 2966 C TRP B 135 -30.285 15.844 38.523 1.00 56.89 C ANISOU 2966 C TRP B 135 9908 4071 7639 1331 1899 765 C ATOM 2967 O TRP B 135 -30.725 15.352 39.561 1.00 55.78 O ANISOU 2967 O TRP B 135 9573 4038 7585 1459 1942 649 O ATOM 2968 CB TRP B 135 -28.054 14.692 38.683 1.00 53.13 C ANISOU 2968 CB TRP B 135 9305 3946 6938 736 1920 449 C ATOM 2969 CG TRP B 135 -28.524 13.471 37.953 1.00 51.22 C ANISOU 2969 CG TRP B 135 8769 4011 6681 803 1746 560 C ATOM 2970 CD1 TRP B 135 -29.389 12.524 38.415 1.00 49.68 C ANISOU 2970 CD1 TRP B 135 8276 4020 6581 1001 1671 564 C ATOM 2971 CD2 TRP B 135 -28.146 13.058 36.633 1.00 50.88 C ANISOU 2971 CD2 TRP B 135 8717 4100 6516 658 1632 672 C ATOM 2972 NE1 TRP B 135 -29.577 11.549 37.467 1.00 48.42 N ANISOU 2972 NE1 TRP B 135 7922 4101 6377 981 1507 664 N ATOM 2973 CE2 TRP B 135 -28.826 11.854 36.362 1.00 49.11 C ANISOU 2973 CE2 TRP B 135 8187 4153 6322 780 1478 727 C ATOM 2974 CE3 TRP B 135 -27.302 13.591 35.654 1.00 52.10 C ANISOU 2974 CE3 TRP B 135 9101 4162 6532 429 1657 728 C ATOM 2975 CZ2 TRP B 135 -28.687 11.174 35.154 1.00 48.55 C ANISOU 2975 CZ2 TRP B 135 8043 4265 6138 687 1339 822 C ATOM 2976 CZ3 TRP B 135 -27.167 12.914 34.455 1.00 51.51 C ANISOU 2976 CZ3 TRP B 135 8953 4283 6338 346 1532 833 C ATOM 2977 CH2 TRP B 135 -27.855 11.718 34.216 1.00 49.75 C ANISOU 2977 CH2 TRP B 135 8432 4332 6139 477 1370 872 C ATOM 2978 N ALA B 136 -31.066 16.286 37.541 1.00 92.67 N ANISOU 2978 N ALA B 136 14516 8492 12200 1525 1798 1014 N ATOM 2979 CA ALA B 136 -32.516 16.395 37.691 1.00 92.83 C ANISOU 2979 CA ALA B 136 14406 8473 12392 1921 1746 1157 C ATOM 2980 C ALA B 136 -33.251 15.056 37.641 1.00 92.01 C ANISOU 2980 C ALA B 136 13882 8732 12346 2033 1593 1191 C ATOM 2981 O ALA B 136 -34.474 15.012 37.771 1.00 91.69 O ANISOU 2981 O ALA B 136 13670 8708 12460 2346 1538 1308 O ATOM 2982 CB ALA B 136 -33.083 17.349 36.647 1.00 98.51 C ANISOU 2982 CB ALA B 136 15361 8941 13126 2106 1675 1419 C ATOM 2983 N PHE B 137 -32.510 13.971 37.452 1.00 82.42 N ANISOU 2983 N PHE B 137 12496 7801 11019 1777 1529 1085 N ATOM 2984 CA PHE B 137 -33.116 12.646 37.400 1.00 81.32 C ANISOU 2984 CA PHE B 137 11979 7990 10930 1843 1390 1101 C ATOM 2985 C PHE B 137 -32.820 11.860 38.673 1.00 79.21 C ANISOU 2985 C PHE B 137 11520 7883 10694 1769 1495 882 C ATOM 2986 O PHE B 137 -32.159 12.361 39.582 1.00 78.91 O ANISOU 2986 O PHE B 137 11639 7718 10626 1672 1658 715 O ATOM 2987 CB PHE B 137 -32.632 11.881 36.166 1.00 81.49 C ANISOU 2987 CB PHE B 137 11944 8217 10800 1644 1219 1166 C ATOM 2988 CG PHE B 137 -32.830 12.629 34.877 1.00 83.25 C ANISOU 2988 CG PHE B 137 12390 8295 10946 1692 1113 1386 C ATOM 2989 CD1 PHE B 137 -34.066 12.645 34.251 1.00 83.49 C ANISOU 2989 CD1 PHE B 137 12311 8350 11063 1965 942 1597 C ATOM 2990 CD2 PHE B 137 -31.780 13.317 34.291 1.00 84.36 C ANISOU 2990 CD2 PHE B 137 12848 8281 10924 1461 1183 1388 C ATOM 2991 CE1 PHE B 137 -34.251 13.333 33.066 1.00 85.09 C ANISOU 2991 CE1 PHE B 137 12735 8421 11173 2024 829 1814 C ATOM 2992 CE2 PHE B 137 -31.959 14.006 33.106 1.00 85.76 C ANISOU 2992 CE2 PHE B 137 13259 8316 11011 1505 1095 1607 C ATOM 2993 CZ PHE B 137 -33.195 14.015 32.493 1.00 86.68 C ANISOU 2993 CZ PHE B 137 13283 8455 11196 1795 910 1825 C ATOM 2994 N GLY B 138 -33.318 10.630 38.739 1.00 63.69 N ANISOU 2994 N GLY B 138 9225 6191 8782 1812 1396 885 N ATOM 2995 CA GLY B 138 -33.099 9.788 39.901 1.00 61.66 C ANISOU 2995 CA GLY B 138 8787 6094 8547 1757 1485 707 C ATOM 2996 C GLY B 138 -31.708 9.189 39.913 1.00 61.84 C ANISOU 2996 C GLY B 138 8846 6243 8407 1440 1493 542 C ATOM 2997 O GLY B 138 -30.897 9.462 39.028 1.00 64.47 O ANISOU 2997 O GLY B 138 9339 6540 8614 1252 1449 556 O ATOM 2998 N ASP B 139 -31.427 8.375 40.924 1.00 85.09 N ANISOU 2998 N ASP B 139 11640 9340 11352 1388 1554 390 N ATOM 2999 CA ASP B 139 -30.153 7.674 41.002 1.00 84.32 C ANISOU 2999 CA ASP B 139 11523 9396 11118 1121 1544 235 C ATOM 3000 C ASP B 139 -30.183 6.487 40.046 1.00 84.87 C ANISOU 3000 C ASP B 139 11389 9696 11162 1049 1380 300 C ATOM 3001 O ASP B 139 -29.178 6.151 39.411 1.00 85.94 O ANISOU 3001 O ASP B 139 11557 9922 11173 833 1333 242 O ATOM 3002 CB ASP B 139 -29.888 7.203 42.433 1.00 81.34 C ANISOU 3002 CB ASP B 139 11069 9097 10738 1118 1652 65 C ATOM 3003 CG ASP B 139 -28.485 6.663 42.619 1.00 80.47 C ANISOU 3003 CG ASP B 139 10966 9120 10490 859 1646 -105 C ATOM 3004 OD1 ASP B 139 -27.589 7.062 41.847 1.00 83.35 O ANISOU 3004 OD1 ASP B 139 11448 9459 10763 669 1612 -120 O ATOM 3005 OD2 ASP B 139 -28.278 5.843 43.538 1.00 77.38 O ANISOU 3005 OD2 ASP B 139 10461 8862 10079 850 1679 -220 O ATOM 3006 N ALA B 140 -31.354 5.865 39.944 1.00 63.70 N ANISOU 3006 N ALA B 140 8493 7107 8605 1227 1300 414 N ATOM 3007 CA ALA B 140 -31.567 4.760 39.020 1.00 64.17 C ANISOU 3007 CA ALA B 140 8364 7362 8654 1173 1132 479 C ATOM 3008 C ALA B 140 -31.559 5.266 37.582 1.00 67.19 C ANISOU 3008 C ALA B 140 8883 7690 8956 1133 1010 609 C ATOM 3009 O ALA B 140 -31.291 4.510 36.649 1.00 68.91 O ANISOU 3009 O ALA B 140 9040 8054 9089 1011 884 623 O ATOM 3010 CB ALA B 140 -32.877 4.057 39.329 1.00 72.58 C ANISOU 3010 CB ALA B 140 9164 8524 9889 1363 1081 564 C ATOM 3011 N GLY B 141 -31.861 6.548 37.411 1.00 64.62 N ANISOU 3011 N GLY B 141 8760 7143 8649 1242 1053 707 N ATOM 3012 CA GLY B 141 -31.783 7.180 36.108 1.00 67.13 C ANISOU 3012 CA GLY B 141 9264 7376 8868 1207 957 846 C ATOM 3013 C GLY B 141 -30.335 7.370 35.705 1.00 68.78 C ANISOU 3013 C GLY B 141 9667 7573 8892 925 1018 743 C ATOM 3014 O GLY B 141 -29.981 7.230 34.536 1.00 70.50 O ANISOU 3014 O GLY B 141 9956 7853 8978 805 924 807 O ATOM 3015 N CYS B 142 -29.496 7.685 36.686 1.00 47.61 N ANISOU 3015 N CYS B 142 7068 4823 6199 817 1180 578 N ATOM 3016 CA CYS B 142 -28.066 7.870 36.469 1.00 48.05 C ANISOU 3016 CA CYS B 142 7270 4879 6108 538 1257 454 C ATOM 3017 C CYS B 142 -27.372 6.547 36.156 1.00 48.12 C ANISOU 3017 C CYS B 142 7087 5161 6036 373 1192 349 C ATOM 3018 O CYS B 142 -26.769 6.374 35.083 1.00 49.54 O ANISOU 3018 O CYS B 142 7328 5413 6085 213 1149 370 O ATOM 3019 CB CYS B 142 -27.434 8.508 37.709 1.00 47.29 C ANISOU 3019 CB CYS B 142 7280 4653 6038 480 1424 291 C ATOM 3020 SG CYS B 142 -25.665 8.202 37.898 1.00 46.50 S ANISOU 3020 SG CYS B 142 7192 4670 5806 143 1504 64 S ATOM 3021 N LYS B 143 -27.458 5.620 37.106 1.00 42.46 N ANISOU 3021 N LYS B 143 6152 4588 5392 420 1195 240 N ATOM 3022 CA LYS B 143 -26.874 4.295 36.948 1.00 40.87 C ANISOU 3022 CA LYS B 143 5763 4626 5139 301 1137 138 C ATOM 3023 C LYS B 143 -27.442 3.608 35.714 1.00 43.21 C ANISOU 3023 C LYS B 143 5977 5034 5405 326 980 257 C ATOM 3024 O LYS B 143 -26.720 2.938 34.982 1.00 42.58 O ANISOU 3024 O LYS B 143 5869 5093 5216 174 940 200 O ATOM 3025 CB LYS B 143 -27.131 3.443 38.191 1.00 38.49 C ANISOU 3025 CB LYS B 143 5262 4428 4936 393 1159 44 C ATOM 3026 CG LYS B 143 -26.492 3.982 39.462 1.00 38.47 C ANISOU 3026 CG LYS B 143 5336 4349 4930 359 1296 -97 C ATOM 3027 CD LYS B 143 -26.933 3.184 40.678 1.00 37.37 C ANISOU 3027 CD LYS B 143 5025 4302 4871 480 1319 -156 C ATOM 3028 CE LYS B 143 -26.229 3.658 41.937 1.00 37.53 C ANISOU 3028 CE LYS B 143 5138 4269 4852 436 1437 -309 C ATOM 3029 NZ LYS B 143 -26.627 2.858 43.127 1.00 36.69 N ANISOU 3029 NZ LYS B 143 4894 4254 4794 557 1467 -354 N ATOM 3030 N GLY B 144 -28.739 3.791 35.485 1.00 36.14 N ANISOU 3030 N GLY B 144 5042 4083 4606 523 890 415 N ATOM 3031 CA GLY B 144 -29.397 3.238 34.316 1.00 36.65 C ANISOU 3031 CA GLY B 144 5034 4249 4641 556 714 534 C ATOM 3032 C GLY B 144 -28.880 3.853 33.030 1.00 38.01 C ANISOU 3032 C GLY B 144 5432 4375 4635 433 680 609 C ATOM 3033 O GLY B 144 -28.765 3.174 32.011 1.00 37.95 O ANISOU 3033 O GLY B 144 5398 4505 4515 345 572 618 O ATOM 3034 N TYR B 145 -28.569 5.144 33.082 1.00 42.39 N ANISOU 3034 N TYR B 145 6225 4725 5157 424 783 661 N ATOM 3035 CA TYR B 145 -28.003 5.854 31.940 1.00 43.99 C ANISOU 3035 CA TYR B 145 6681 4852 5183 293 789 744 C ATOM 3036 C TYR B 145 -26.643 5.275 31.562 1.00 42.91 C ANISOU 3036 C TYR B 145 6550 4857 4897 27 861 591 C ATOM 3037 O TYR B 145 -26.436 4.831 30.424 1.00 43.32 O ANISOU 3037 O TYR B 145 6637 5024 4800 -65 785 626 O ATOM 3038 CB TYR B 145 -27.885 7.348 32.262 1.00 45.81 C ANISOU 3038 CB TYR B 145 7172 4802 5433 319 918 809 C ATOM 3039 CG TYR B 145 -27.057 8.157 31.291 1.00 47.52 C ANISOU 3039 CG TYR B 145 7679 4909 5470 132 985 871 C ATOM 3040 CD1 TYR B 145 -27.602 8.620 30.101 1.00 49.69 C ANISOU 3040 CD1 TYR B 145 8127 5116 5639 202 875 1085 C ATOM 3041 CD2 TYR B 145 -25.737 8.479 31.576 1.00 47.26 C ANISOU 3041 CD2 TYR B 145 7745 4841 5370 -117 1160 722 C ATOM 3042 CE1 TYR B 145 -26.850 9.369 29.215 1.00 51.51 C ANISOU 3042 CE1 TYR B 145 8646 5236 5691 25 956 1158 C ATOM 3043 CE2 TYR B 145 -24.978 9.227 30.698 1.00 49.08 C ANISOU 3043 CE2 TYR B 145 8237 4968 5444 -308 1247 782 C ATOM 3044 CZ TYR B 145 -25.538 9.670 29.518 1.00 51.19 C ANISOU 3044 CZ TYR B 145 8697 5157 5598 -238 1154 1006 C ATOM 3045 OH TYR B 145 -24.783 10.415 28.641 1.00 53.22 O ANISOU 3045 OH TYR B 145 9235 5304 5685 -435 1258 1081 O ATOM 3046 N TYR B 146 -25.720 5.269 32.521 1.00 40.44 N ANISOU 3046 N TYR B 146 6198 4547 4620 -89 1007 415 N ATOM 3047 CA TYR B 146 -24.377 4.750 32.263 1.00 39.64 C ANISOU 3047 CA TYR B 146 6072 4590 4402 -328 1087 259 C ATOM 3048 C TYR B 146 -24.383 3.271 31.862 1.00 38.14 C ANISOU 3048 C TYR B 146 5669 4642 4183 -335 982 189 C ATOM 3049 O TYR B 146 -23.669 2.860 30.935 1.00 38.36 O ANISOU 3049 O TYR B 146 5724 4787 4066 -487 993 146 O ATOM 3050 CB TYR B 146 -23.461 4.991 33.467 1.00 38.88 C ANISOU 3050 CB TYR B 146 5942 4468 4366 -430 1232 80 C ATOM 3051 CG TYR B 146 -22.985 6.423 33.580 1.00 40.72 C ANISOU 3051 CG TYR B 146 6427 4475 4573 -539 1366 98 C ATOM 3052 CD1 TYR B 146 -23.728 7.373 34.271 1.00 41.69 C ANISOU 3052 CD1 TYR B 146 6671 4371 4801 -389 1394 170 C ATOM 3053 CD2 TYR B 146 -21.796 6.827 32.987 1.00 41.74 C ANISOU 3053 CD2 TYR B 146 6674 4607 4579 -796 1478 41 C ATOM 3054 CE1 TYR B 146 -23.295 8.684 34.372 1.00 43.61 C ANISOU 3054 CE1 TYR B 146 7169 4377 5026 -494 1521 179 C ATOM 3055 CE2 TYR B 146 -21.356 8.134 33.083 1.00 43.67 C ANISOU 3055 CE2 TYR B 146 7157 4627 4809 -922 1609 56 C ATOM 3056 CZ TYR B 146 -22.109 9.058 33.776 1.00 44.59 C ANISOU 3056 CZ TYR B 146 7413 4501 5031 -772 1626 124 C ATOM 3057 OH TYR B 146 -21.671 10.361 33.871 1.00 46.74 O ANISOU 3057 OH TYR B 146 7946 4520 5294 -903 1760 131 O ATOM 3058 N PHE B 147 -25.202 2.483 32.555 1.00 47.15 N ANISOU 3058 N PHE B 147 6607 5848 5463 -172 894 178 N ATOM 3059 CA PHE B 147 -25.365 1.065 32.244 1.00 46.33 C ANISOU 3059 CA PHE B 147 6309 5937 5357 -164 788 119 C ATOM 3060 C PHE B 147 -25.872 0.867 30.821 1.00 49.03 C ANISOU 3060 C PHE B 147 6720 6330 5580 -167 648 235 C ATOM 3061 O PHE B 147 -25.393 -0.010 30.102 1.00 48.29 O ANISOU 3061 O PHE B 147 6588 6382 5379 -270 616 156 O ATOM 3062 CB PHE B 147 -26.320 0.402 33.238 1.00 44.52 C ANISOU 3062 CB PHE B 147 5875 5730 5311 11 728 120 C ATOM 3063 CG PHE B 147 -26.754 -0.979 32.837 1.00 44.48 C ANISOU 3063 CG PHE B 147 5693 5881 5326 31 600 95 C ATOM 3064 CD1 PHE B 147 -25.902 -2.059 32.991 1.00 41.34 C ANISOU 3064 CD1 PHE B 147 5191 5617 4901 -66 632 -63 C ATOM 3065 CD2 PHE B 147 -28.021 -1.200 32.320 1.00 47.87 C ANISOU 3065 CD2 PHE B 147 6056 6318 5816 150 443 225 C ATOM 3066 CE1 PHE B 147 -26.299 -3.332 32.626 1.00 41.50 C ANISOU 3066 CE1 PHE B 147 5074 5750 4947 -52 522 -94 C ATOM 3067 CE2 PHE B 147 -28.425 -2.470 31.954 1.00 48.05 C ANISOU 3067 CE2 PHE B 147 5922 6471 5864 145 322 189 C ATOM 3068 CZ PHE B 147 -27.562 -3.538 32.108 1.00 44.71 C ANISOU 3068 CZ PHE B 147 5426 6155 5410 41 368 27 C ATOM 3069 N LEU B 148 -26.845 1.683 30.424 1.00 27.08 N ANISOU 3069 N LEU B 148 4047 3430 2813 -41 563 419 N ATOM 3070 CA LEU B 148 -27.377 1.638 29.067 1.00 28.61 C ANISOU 3070 CA LEU B 148 4332 3667 2873 -30 406 550 C ATOM 3071 C LEU B 148 -26.282 1.932 28.051 1.00 30.46 C ANISOU 3071 C LEU B 148 4775 3925 2873 -232 490 526 C ATOM 3072 O LEU B 148 -26.135 1.213 27.058 1.00 31.01 O ANISOU 3072 O LEU B 148 4849 4137 2796 -310 413 496 O ATOM 3073 CB LEU B 148 -28.522 2.637 28.903 1.00 30.53 C ANISOU 3073 CB LEU B 148 4672 3757 3170 155 312 764 C ATOM 3074 CG LEU B 148 -29.096 2.782 27.493 1.00 32.69 C ANISOU 3074 CG LEU B 148 5072 4065 3284 185 129 927 C ATOM 3075 CD1 LEU B 148 -29.635 1.452 26.994 1.00 32.20 C ANISOU 3075 CD1 LEU B 148 4811 4209 3214 188 -58 875 C ATOM 3076 CD2 LEU B 148 -30.177 3.848 27.465 1.00 35.17 C ANISOU 3076 CD2 LEU B 148 5469 4216 3678 400 39 1143 C ATOM 3077 N ARG B 149 -25.513 2.987 28.310 1.00 52.20 N ANISOU 3077 N ARG B 149 7703 6536 5592 -324 659 530 N ATOM 3078 CA ARG B 149 -24.415 3.359 27.422 1.00 52.63 C ANISOU 3078 CA ARG B 149 7955 6603 5438 -538 779 511 C ATOM 3079 C ARG B 149 -23.412 2.222 27.227 1.00 49.81 C ANISOU 3079 C ARG B 149 7461 6456 5006 -694 843 310 C ATOM 3080 O ARG B 149 -23.126 1.817 26.092 1.00 49.15 O ANISOU 3080 O ARG B 149 7459 6483 4733 -789 822 311 O ATOM 3081 CB ARG B 149 -23.699 4.608 27.938 1.00 53.06 C ANISOU 3081 CB ARG B 149 8180 6467 5513 -638 969 514 C ATOM 3082 CG ARG B 149 -24.537 5.873 27.872 1.00 54.77 C ANISOU 3082 CG ARG B 149 8614 6440 5754 -505 935 727 C ATOM 3083 CD ARG B 149 -23.701 7.100 28.190 1.00 54.89 C ANISOU 3083 CD ARG B 149 8843 6251 5762 -652 1139 718 C ATOM 3084 NE ARG B 149 -22.590 7.264 27.257 1.00 54.65 N ANISOU 3084 NE ARG B 149 8967 6266 5531 -910 1269 695 N ATOM 3085 CZ ARG B 149 -22.663 7.951 26.122 1.00 55.88 C ANISOU 3085 CZ ARG B 149 9402 6323 5507 -959 1275 877 C ATOM 3086 NH1 ARG B 149 -23.798 8.542 25.773 1.00 55.72 N ANISOU 3086 NH1 ARG B 149 9532 6152 5487 -751 1135 1100 N ATOM 3087 NH2 ARG B 149 -21.600 8.046 25.335 1.00 57.10 N ANISOU 3087 NH2 ARG B 149 9683 6533 5479 -1208 1424 843 N ATOM 3088 N GLU B 150 -22.886 1.699 28.332 1.00 62.08 N ANISOU 3088 N GLU B 150 8817 8067 6704 -708 920 140 N ATOM 3089 CA GLU B 150 -21.884 0.639 28.243 1.00 59.38 C ANISOU 3089 CA GLU B 150 8334 7914 6313 -830 986 -52 C ATOM 3090 C GLU B 150 -22.430 -0.659 27.640 1.00 59.54 C ANISOU 3090 C GLU B 150 8239 8083 6298 -762 833 -82 C ATOM 3091 O GLU B 150 -21.751 -1.316 26.846 1.00 58.26 O ANISOU 3091 O GLU B 150 8086 8053 5996 -871 870 -176 O ATOM 3092 CB GLU B 150 -21.215 0.388 29.598 1.00 58.03 C ANISOU 3092 CB GLU B 150 7983 7770 6296 -843 1082 -216 C ATOM 3093 CG GLU B 150 -20.274 1.506 30.020 1.00 59.01 C ANISOU 3093 CG GLU B 150 8214 7795 6411 -992 1255 -253 C ATOM 3094 CD GLU B 150 -19.069 1.000 30.792 1.00 56.61 C ANISOU 3094 CD GLU B 150 7729 7619 6159 -1097 1362 -464 C ATOM 3095 OE1 GLU B 150 -19.086 -0.171 31.225 1.00 54.53 O ANISOU 3095 OE1 GLU B 150 7262 7489 5966 -1009 1297 -565 O ATOM 3096 OE2 GLU B 150 -18.101 1.772 30.956 1.00 56.34 O ANISOU 3096 OE2 GLU B 150 7755 7551 6099 -1269 1505 -527 O ATOM 3097 N ALA B 151 -23.656 -1.021 28.006 1.00 53.68 N ANISOU 3097 N ALA B 151 7393 7317 5688 -588 671 -7 N ATOM 3098 CA ALA B 151 -24.297 -2.197 27.425 1.00 54.67 C ANISOU 3098 CA ALA B 151 7418 7561 5794 -537 509 -29 C ATOM 3099 C ALA B 151 -24.388 -2.044 25.911 1.00 56.51 C ANISOU 3099 C ALA B 151 7846 7838 5790 -607 435 51 C ATOM 3100 O ALA B 151 -24.090 -2.977 25.157 1.00 56.04 O ANISOU 3100 O ALA B 151 7776 7909 5609 -679 406 -52 O ATOM 3101 CB ALA B 151 -25.676 -2.408 28.024 1.00 56.17 C ANISOU 3101 CB ALA B 151 7470 7705 6170 -355 353 65 C ATOM 3102 N CYS B 152 -24.786 -0.852 25.473 1.00 45.74 N ANISOU 3102 N CYS B 152 6676 6354 4349 -580 411 234 N ATOM 3103 CA CYS B 152 -24.881 -0.557 24.049 1.00 47.12 C ANISOU 3103 CA CYS B 152 7075 6557 4270 -640 341 340 C ATOM 3104 C CYS B 152 -23.533 -0.645 23.338 1.00 46.29 C ANISOU 3104 C CYS B 152 7095 6536 3957 -846 527 226 C ATOM 3105 O CYS B 152 -23.447 -1.196 22.238 1.00 47.47 O ANISOU 3105 O CYS B 152 7332 6804 3901 -910 474 198 O ATOM 3106 CB CYS B 152 -25.514 0.817 23.816 1.00 49.25 C ANISOU 3106 CB CYS B 152 7549 6656 4508 -556 295 576 C ATOM 3107 SG CYS B 152 -27.319 0.834 23.930 1.00 52.13 S ANISOU 3107 SG CYS B 152 7805 6986 5015 -303 4 752 S ATOM 3108 N THR B 153 -22.480 -0.112 23.956 1.00 44.12 N ANISOU 3108 N THR B 153 6822 6209 3731 -955 747 152 N ATOM 3109 CA THR B 153 -21.165 -0.154 23.313 1.00 45.00 C ANISOU 3109 CA THR B 153 7020 6412 3665 -1158 947 42 C ATOM 3110 C THR B 153 -20.605 -1.582 23.222 1.00 43.92 C ANISOU 3110 C THR B 153 6700 6468 3520 -1192 966 -177 C ATOM 3111 O THR B 153 -20.020 -1.962 22.198 1.00 45.25 O ANISOU 3111 O THR B 153 6964 6751 3478 -1303 1038 -242 O ATOM 3112 CB THR B 153 -20.144 0.839 23.944 1.00 45.15 C ANISOU 3112 CB THR B 153 7079 6333 3741 -1294 1177 14 C ATOM 3113 OG1 THR B 153 -18.992 0.946 23.099 1.00 46.77 O ANISOU 3113 OG1 THR B 153 7402 6620 3747 -1502 1369 -44 O ATOM 3114 CG2 THR B 153 -19.709 0.401 25.330 1.00 42.87 C ANISOU 3114 CG2 THR B 153 6526 6077 3685 -1268 1233 -157 C ATOM 3115 N TYR B 154 -20.809 -2.376 24.273 1.00 40.22 N ANISOU 3115 N TYR B 154 5984 6026 3272 -1087 909 -286 N ATOM 3116 CA TYR B 154 -20.411 -3.782 24.239 1.00 39.31 C ANISOU 3116 CA TYR B 154 5704 6061 3173 -1084 906 -479 C ATOM 3117 C TYR B 154 -21.176 -4.527 23.148 1.00 40.38 C ANISOU 3117 C TYR B 154 5919 6263 3161 -1051 733 -458 C ATOM 3118 O TYR B 154 -20.597 -5.317 22.394 1.00 41.13 O ANISOU 3118 O TYR B 154 6039 6478 3110 -1124 786 -593 O ATOM 3119 CB TYR B 154 -20.641 -4.463 25.592 1.00 37.03 C ANISOU 3119 CB TYR B 154 5165 5760 3145 -962 859 -563 C ATOM 3120 CG TYR B 154 -19.605 -4.136 26.646 1.00 36.07 C ANISOU 3120 CG TYR B 154 4930 5635 3141 -1010 1029 -660 C ATOM 3121 CD1 TYR B 154 -18.275 -4.501 26.479 1.00 36.41 C ANISOU 3121 CD1 TYR B 154 4910 5800 3126 -1125 1197 -825 C ATOM 3122 CD2 TYR B 154 -19.961 -3.484 27.818 1.00 35.06 C ANISOU 3122 CD2 TYR B 154 4748 5392 3181 -937 1019 -595 C ATOM 3123 CE1 TYR B 154 -17.328 -4.209 27.445 1.00 36.07 C ANISOU 3123 CE1 TYR B 154 4741 5773 3193 -1173 1326 -919 C ATOM 3124 CE2 TYR B 154 -19.024 -3.186 28.787 1.00 34.43 C ANISOU 3124 CE2 TYR B 154 4572 5318 3192 -989 1152 -694 C ATOM 3125 CZ TYR B 154 -17.710 -3.551 28.597 1.00 34.82 C ANISOU 3125 CZ TYR B 154 4546 5499 3186 -1110 1293 -854 C ATOM 3126 OH TYR B 154 -16.777 -3.256 29.564 1.00 35.00 O ANISOU 3126 OH TYR B 154 4452 5545 3302 -1165 1400 -957 O ATOM 3127 N ALA B 155 -22.479 -4.263 23.069 1.00 48.24 N ANISOU 3127 N ALA B 155 6951 7185 4194 -938 525 -298 N ATOM 3128 CA ALA B 155 -23.329 -4.880 22.055 1.00 50.23 C ANISOU 3128 CA ALA B 155 7273 7501 4309 -910 320 -267 C ATOM 3129 C ALA B 155 -22.843 -4.555 20.645 1.00 50.90 C ANISOU 3129 C ALA B 155 7621 7653 4066 -1035 373 -242 C ATOM 3130 O ALA B 155 -22.729 -5.443 19.796 1.00 50.13 O ANISOU 3130 O ALA B 155 7569 7671 3808 -1085 334 -360 O ATOM 3131 CB ALA B 155 -24.773 -4.437 22.235 1.00 53.02 C ANISOU 3131 CB ALA B 155 7609 7770 4767 -768 94 -75 C ATOM 3132 N THR B 156 -22.554 -3.278 20.407 1.00 51.75 N ANISOU 3132 N THR B 156 7917 7676 4068 -1089 475 -92 N ATOM 3133 CA THR B 156 -22.064 -2.827 19.108 1.00 52.10 C ANISOU 3133 CA THR B 156 8241 7767 3787 -1217 556 -38 C ATOM 3134 C THR B 156 -20.740 -3.495 18.744 1.00 50.78 C ANISOU 3134 C THR B 156 8056 7735 3504 -1365 787 -255 C ATOM 3135 O THR B 156 -20.574 -3.989 17.625 1.00 52.53 O ANISOU 3135 O THR B 156 8418 8069 3472 -1429 782 -315 O ATOM 3136 CB THR B 156 -21.896 -1.295 19.069 1.00 53.32 C ANISOU 3136 CB THR B 156 8604 7772 3881 -1261 662 167 C ATOM 3137 OG1 THR B 156 -23.173 -0.667 19.235 1.00 55.12 O ANISOU 3137 OG1 THR B 156 8874 7880 4190 -1098 438 378 O ATOM 3138 CG2 THR B 156 -21.293 -0.855 17.744 1.00 54.79 C ANISOU 3138 CG2 THR B 156 9093 8006 3718 -1411 781 227 C ATOM 3139 N ALA B 157 -19.806 -3.513 19.692 1.00 42.82 N ANISOU 3139 N ALA B 157 6870 6722 2679 -1409 984 -379 N ATOM 3140 CA ALA B 157 -18.508 -4.148 19.466 1.00 44.35 C ANISOU 3140 CA ALA B 157 6994 7052 2806 -1526 1210 -592 C ATOM 3141 C ALA B 157 -18.661 -5.625 19.097 1.00 44.30 C ANISOU 3141 C ALA B 157 6896 7167 2771 -1467 1116 -773 C ATOM 3142 O ALA B 157 -18.122 -6.089 18.080 1.00 47.00 O ANISOU 3142 O ALA B 157 7350 7623 2885 -1550 1216 -881 O ATOM 3143 CB ALA B 157 -17.621 -3.993 20.693 1.00 42.96 C ANISOU 3143 CB ALA B 157 6594 6859 2870 -1551 1379 -694 C ATOM 3144 N LEU B 158 -19.408 -6.353 19.924 1.00 46.93 N ANISOU 3144 N LEU B 158 7039 7462 3333 -1327 937 -808 N ATOM 3145 CA LEU B 158 -19.651 -7.774 19.693 1.00 46.40 C ANISOU 3145 CA LEU B 158 6885 7469 3276 -1272 837 -975 C ATOM 3146 C LEU B 158 -20.304 -8.026 18.337 1.00 48.59 C ANISOU 3146 C LEU B 158 7385 7800 3277 -1303 688 -945 C ATOM 3147 O LEU B 158 -19.950 -8.977 17.639 1.00 49.64 O ANISOU 3147 O LEU B 158 7564 8028 3272 -1340 724 -1120 O ATOM 3148 CB LEU B 158 -20.512 -8.367 20.811 1.00 45.73 C ANISOU 3148 CB LEU B 158 6584 7309 3485 -1131 663 -973 C ATOM 3149 CG LEU B 158 -19.851 -8.493 22.185 1.00 43.86 C ANISOU 3149 CG LEU B 158 6116 7044 3507 -1082 791 -1051 C ATOM 3150 CD1 LEU B 158 -20.797 -9.156 23.175 1.00 44.16 C ANISOU 3150 CD1 LEU B 158 5973 7008 3798 -946 623 -1037 C ATOM 3151 CD2 LEU B 158 -18.545 -9.265 22.084 1.00 42.21 C ANISOU 3151 CD2 LEU B 158 5829 6941 3268 -1127 990 -1270 C ATOM 3152 N ASN B 159 -21.253 -7.171 17.967 1.00 70.94 N ANISOU 3152 N ASN B 159 10362 10569 6021 -1280 515 -728 N ATOM 3153 CA ASN B 159 -21.911 -7.286 16.669 1.00 72.97 C ANISOU 3153 CA ASN B 159 10845 10887 5991 -1307 342 -676 C ATOM 3154 C ASN B 159 -20.950 -7.055 15.505 1.00 73.02 C ANISOU 3154 C ASN B 159 11102 10990 5652 -1448 542 -723 C ATOM 3155 O ASN B 159 -21.027 -7.738 14.484 1.00 73.69 O ANISOU 3155 O ASN B 159 11326 11174 5498 -1488 482 -827 O ATOM 3156 CB ASN B 159 -23.101 -6.330 16.573 1.00 75.89 C ANISOU 3156 CB ASN B 159 11307 11175 6353 -1229 112 -412 C ATOM 3157 CG ASN B 159 -24.272 -6.769 17.429 1.00 77.25 C ANISOU 3157 CG ASN B 159 11247 11292 6813 -1092 -128 -382 C ATOM 3158 OD1 ASN B 159 -24.502 -7.963 17.620 1.00 76.55 O ANISOU 3158 OD1 ASN B 159 11006 11246 6832 -1075 -206 -549 O ATOM 3159 ND2 ASN B 159 -25.020 -5.803 17.949 1.00 78.68 N ANISOU 3159 ND2 ASN B 159 11401 11368 7124 -992 -234 -169 N ATOM 3160 N VAL B 160 -20.046 -6.091 15.664 1.00 51.08 N ANISOU 3160 N VAL B 160 8383 8181 2845 -1533 787 -652 N ATOM 3161 CA VAL B 160 -19.045 -5.813 14.639 1.00 54.82 C ANISOU 3161 CA VAL B 160 9073 8745 3009 -1684 1029 -692 C ATOM 3162 C VAL B 160 -18.112 -7.006 14.439 1.00 55.83 C ANISOU 3162 C VAL B 160 9096 9006 3112 -1724 1204 -981 C ATOM 3163 O VAL B 160 -17.915 -7.472 13.309 1.00 58.66 O ANISOU 3163 O VAL B 160 9619 9451 3220 -1764 1234 -1060 O ATOM 3164 CB VAL B 160 -18.218 -4.554 14.974 1.00 55.33 C ANISOU 3164 CB VAL B 160 9183 8740 3102 -1791 1280 -576 C ATOM 3165 CG1 VAL B 160 -16.987 -4.469 14.085 1.00 58.84 C ANISOU 3165 CG1 VAL B 160 9752 9285 3320 -1945 1575 -662 C ATOM 3166 CG2 VAL B 160 -19.073 -3.304 14.831 1.00 55.61 C ANISOU 3166 CG2 VAL B 160 9418 8633 3078 -1761 1138 -280 C ATOM 3167 N VAL B 161 -17.548 -7.506 15.537 1.00 53.39 N ANISOU 3167 N VAL B 161 8495 8688 3105 -1676 1304 -1124 N ATOM 3168 CA VAL B 161 -16.661 -8.666 15.468 1.00 54.07 C ANISOU 3168 CA VAL B 161 8437 8863 3243 -1660 1453 -1381 C ATOM 3169 C VAL B 161 -17.379 -9.874 14.865 1.00 54.71 C ANISOU 3169 C VAL B 161 8581 8980 3228 -1595 1259 -1511 C ATOM 3170 O VAL B 161 -16.837 -10.573 14.000 1.00 56.59 O ANISOU 3170 O VAL B 161 8870 9256 3375 -1581 1336 -1637 O ATOM 3171 CB VAL B 161 -16.110 -9.042 16.855 1.00 51.45 C ANISOU 3171 CB VAL B 161 7783 8513 3254 -1592 1540 -1494 C ATOM 3172 CG1 VAL B 161 -15.133 -10.203 16.742 1.00 51.91 C ANISOU 3172 CG1 VAL B 161 7679 8609 3435 -1517 1654 -1705 C ATOM 3173 CG2 VAL B 161 -15.438 -7.842 17.494 1.00 50.98 C ANISOU 3173 CG2 VAL B 161 7655 8413 3304 -1668 1707 -1383 C ATOM 3174 N SER B 162 -18.607 -10.103 15.321 1.00 66.72 N ANISOU 3174 N SER B 162 10052 10429 4871 -1511 974 -1438 N ATOM 3175 CA SER B 162 -19.424 -11.201 14.819 1.00 67.37 C ANISOU 3175 CA SER B 162 10178 10524 4896 -1467 751 -1550 C ATOM 3176 C SER B 162 -19.670 -11.071 13.319 1.00 68.60 C ANISOU 3176 C SER B 162 10656 10768 4643 -1555 687 -1532 C ATOM 3177 O SER B 162 -19.697 -12.068 12.599 1.00 68.39 O ANISOU 3177 O SER B 162 10699 10777 4509 -1548 638 -1702 O ATOM 3178 CB SER B 162 -20.758 -11.265 15.564 1.00 66.12 C ANISOU 3178 CB SER B 162 9883 10261 4981 -1367 451 -1425 C ATOM 3179 OG SER B 162 -21.543 -12.350 15.104 1.00 67.79 O ANISOU 3179 OG SER B 162 10122 10483 5154 -1351 232 -1540 O ATOM 3180 N LEU B 163 -19.848 -9.838 12.853 1.00 58.22 N ANISOU 3180 N LEU B 163 9532 9452 3140 -1609 678 -1305 N ATOM 3181 CA LEU B 163 -20.021 -9.585 11.426 1.00 61.91 C ANISOU 3181 CA LEU B 163 10306 9981 3237 -1664 619 -1240 C ATOM 3182 C LEU B 163 -18.738 -9.858 10.654 1.00 63.86 C ANISOU 3182 C LEU B 163 10593 10264 3408 -1684 908 -1362 C ATOM 3183 O LEU B 163 -18.780 -10.313 9.511 1.00 66.56 O ANISOU 3183 O LEU B 163 11106 10657 3526 -1681 864 -1429 O ATOM 3184 CB LEU B 163 -20.495 -8.153 11.176 1.00 62.93 C ANISOU 3184 CB LEU B 163 10642 10079 3191 -1703 545 -941 C ATOM 3185 CG LEU B 163 -22.007 -7.944 11.239 1.00 62.00 C ANISOU 3185 CG LEU B 163 10526 9907 3125 -1604 151 -762 C ATOM 3186 CD1 LEU B 163 -22.362 -6.496 10.950 1.00 63.18 C ANISOU 3186 CD1 LEU B 163 10877 9991 3138 -1598 100 -450 C ATOM 3187 CD2 LEU B 163 -22.707 -8.877 10.265 1.00 64.66 C ANISOU 3187 CD2 LEU B 163 10990 10342 3233 -1612 -98 -882 C ATOM 3188 N SER B 164 -17.598 -9.575 11.278 1.00 67.24 N ANISOU 3188 N SER B 164 10853 10672 4023 -1703 1193 -1393 N ATOM 3189 CA SER B 164 -16.311 -9.888 10.664 1.00 68.87 C ANISOU 3189 CA SER B 164 11040 10923 4204 -1715 1466 -1519 C ATOM 3190 C SER B 164 -16.149 -11.397 10.493 1.00 68.95 C ANISOU 3190 C SER B 164 10960 10956 4282 -1626 1445 -1773 C ATOM 3191 O SER B 164 -15.714 -11.872 9.439 1.00 72.22 O ANISOU 3191 O SER B 164 11504 11421 4517 -1620 1527 -1871 O ATOM 3192 CB SER B 164 -15.160 -9.318 11.494 1.00 66.61 C ANISOU 3192 CB SER B 164 10542 10616 4150 -1753 1734 -1506 C ATOM 3193 OG SER B 164 -15.199 -7.901 11.514 1.00 67.03 O ANISOU 3193 OG SER B 164 10716 10627 4126 -1851 1784 -1278 O ATOM 3194 N VAL B 165 -16.510 -12.144 11.533 1.00 65.27 N ANISOU 3194 N VAL B 165 10285 10442 4071 -1554 1338 -1878 N ATOM 3195 CA VAL B 165 -16.454 -13.602 11.483 1.00 65.52 C ANISOU 3195 CA VAL B 165 10243 10457 4192 -1465 1300 -2108 C ATOM 3196 C VAL B 165 -17.397 -14.153 10.413 1.00 68.34 C ANISOU 3196 C VAL B 165 10841 10830 4294 -1475 1070 -2155 C ATOM 3197 O VAL B 165 -17.009 -15.000 9.601 1.00 70.92 O ANISOU 3197 O VAL B 165 11255 11171 4518 -1440 1128 -2317 O ATOM 3198 CB VAL B 165 -16.818 -14.225 12.842 1.00 62.69 C ANISOU 3198 CB VAL B 165 9635 10029 4153 -1392 1205 -2184 C ATOM 3199 CG1 VAL B 165 -16.730 -15.739 12.771 1.00 63.00 C ANISOU 3199 CG1 VAL B 165 9623 10021 4291 -1300 1180 -2413 C ATOM 3200 CG2 VAL B 165 -15.905 -13.687 13.932 1.00 60.84 C ANISOU 3200 CG2 VAL B 165 9160 9788 4169 -1373 1404 -2140 C ATOM 3201 N GLU B 166 -18.633 -13.661 10.421 1.00 73.07 N ANISOU 3201 N GLU B 166 11541 11429 4793 -1518 799 -2013 N ATOM 3202 CA GLU B 166 -19.639 -14.056 9.440 1.00 75.62 C ANISOU 3202 CA GLU B 166 12071 11778 4882 -1534 526 -2033 C ATOM 3203 C GLU B 166 -19.166 -13.794 8.017 1.00 78.92 C ANISOU 3203 C GLU B 166 12745 12269 4970 -1560 627 -2020 C ATOM 3204 O GLU B 166 -19.390 -14.608 7.121 1.00 81.64 O ANISOU 3204 O GLU B 166 13225 12637 5156 -1544 532 -2162 O ATOM 3205 CB GLU B 166 -20.954 -13.314 9.691 1.00 73.80 C ANISOU 3205 CB GLU B 166 11886 11553 4602 -1571 219 -1831 C ATOM 3206 CG GLU B 166 -21.780 -13.860 10.845 1.00 71.75 C ANISOU 3206 CG GLU B 166 11403 11238 4619 -1550 23 -1879 C ATOM 3207 CD GLU B 166 -22.538 -15.121 10.478 1.00 72.96 C ANISOU 3207 CD GLU B 166 11565 11369 4785 -1545 -217 -2057 C ATOM 3208 OE1 GLU B 166 -22.488 -15.527 9.298 1.00 76.03 O ANISOU 3208 OE1 GLU B 166 12150 11792 4946 -1552 -251 -2141 O ATOM 3209 OE2 GLU B 166 -23.188 -15.705 11.370 1.00 72.26 O ANISOU 3209 OE2 GLU B 166 11288 11228 4939 -1540 -370 -2116 O ATOM 3210 N LEU B 167 -18.511 -12.656 7.813 1.00 70.77 N ANISOU 3210 N LEU B 167 11782 11270 3836 -1607 823 -1852 N ATOM 3211 CA LEU B 167 -18.012 -12.298 6.493 1.00 74.42 C ANISOU 3211 CA LEU B 167 12485 11807 3983 -1642 949 -1816 C ATOM 3212 C LEU B 167 -16.862 -13.211 6.079 1.00 75.84 C ANISOU 3212 C LEU B 167 12619 12013 4184 -1603 1208 -2043 C ATOM 3213 O LEU B 167 -16.787 -13.635 4.922 1.00 79.11 O ANISOU 3213 O LEU B 167 13228 12487 4342 -1596 1210 -2133 O ATOM 3214 CB LEU B 167 -17.575 -10.833 6.451 1.00 74.78 C ANISOU 3214 CB LEU B 167 12606 11858 3950 -1715 1111 -1572 C ATOM 3215 CG LEU B 167 -17.321 -10.268 5.052 1.00 78.85 C ANISOU 3215 CG LEU B 167 13413 12446 4099 -1762 1183 -1470 C ATOM 3216 CD1 LEU B 167 -18.559 -10.419 4.183 1.00 80.96 C ANISOU 3216 CD1 LEU B 167 13908 12757 4098 -1737 836 -1414 C ATOM 3217 CD2 LEU B 167 -16.896 -8.813 5.128 1.00 79.12 C ANISOU 3217 CD2 LEU B 167 13512 12450 4100 -1843 1351 -1223 C ATOM 3218 N TYR B 168 -15.972 -13.515 7.023 1.00 73.62 N ANISOU 3218 N TYR B 168 12077 11691 4204 -1567 1417 -2135 N ATOM 3219 CA TYR B 168 -14.875 -14.438 6.743 1.00 74.95 C ANISOU 3219 CA TYR B 168 12172 11879 4428 -1504 1648 -2347 C ATOM 3220 C TYR B 168 -15.410 -15.794 6.313 1.00 76.06 C ANISOU 3220 C TYR B 168 12389 11989 4521 -1430 1484 -2559 C ATOM 3221 O TYR B 168 -14.950 -16.364 5.326 1.00 79.11 O ANISOU 3221 O TYR B 168 12911 12419 4727 -1401 1588 -2696 O ATOM 3222 CB TYR B 168 -13.950 -14.610 7.952 1.00 72.32 C ANISOU 3222 CB TYR B 168 11518 11505 4455 -1455 1841 -2404 C ATOM 3223 CG TYR B 168 -12.768 -15.520 7.672 1.00 73.97 C ANISOU 3223 CG TYR B 168 11639 11738 4727 -1372 2079 -2603 C ATOM 3224 CD1 TYR B 168 -12.862 -16.896 7.850 1.00 73.84 C ANISOU 3224 CD1 TYR B 168 11571 11660 4826 -1257 2014 -2813 C ATOM 3225 CD2 TYR B 168 -11.562 -15.003 7.219 1.00 75.91 C ANISOU 3225 CD2 TYR B 168 11857 12064 4921 -1410 2368 -2579 C ATOM 3226 CE1 TYR B 168 -11.791 -17.728 7.585 1.00 75.60 C ANISOU 3226 CE1 TYR B 168 11727 11898 5102 -1163 2229 -2986 C ATOM 3227 CE2 TYR B 168 -10.484 -15.829 6.956 1.00 77.68 C ANISOU 3227 CE2 TYR B 168 11992 12322 5202 -1324 2583 -2756 C ATOM 3228 CZ TYR B 168 -10.603 -17.188 7.142 1.00 77.52 C ANISOU 3228 CZ TYR B 168 11929 12237 5287 -1191 2512 -2957 C ATOM 3229 OH TYR B 168 -9.532 -18.011 6.881 1.00 79.51 O ANISOU 3229 OH TYR B 168 12102 12517 5593 -1087 2727 -3127 O ATOM 3230 N LEU B 169 -16.379 -16.311 7.061 1.00 88.13 N ANISOU 3230 N LEU B 169 13830 13438 6217 -1406 1234 -2593 N ATOM 3231 CA LEU B 169 -16.967 -17.604 6.736 1.00 89.52 C ANISOU 3231 CA LEU B 169 14075 13560 6381 -1356 1059 -2797 C ATOM 3232 C LEU B 169 -17.743 -17.551 5.423 1.00 93.49 C ANISOU 3232 C LEU B 169 14872 14130 6523 -1406 857 -2789 C ATOM 3233 O LEU B 169 -17.835 -18.548 4.709 1.00 96.45 O ANISOU 3233 O LEU B 169 15368 14491 6787 -1373 801 -2982 O ATOM 3234 CB LEU B 169 -17.864 -18.092 7.875 1.00 85.46 C ANISOU 3234 CB LEU B 169 13385 12941 6145 -1340 840 -2822 C ATOM 3235 CG LEU B 169 -17.141 -18.412 9.185 1.00 83.15 C ANISOU 3235 CG LEU B 169 12803 12577 6215 -1264 1016 -2869 C ATOM 3236 CD1 LEU B 169 -18.108 -18.982 10.211 1.00 81.58 C ANISOU 3236 CD1 LEU B 169 12458 12275 6264 -1251 794 -2903 C ATOM 3237 CD2 LEU B 169 -15.985 -19.370 8.938 1.00 84.09 C ANISOU 3237 CD2 LEU B 169 12886 12673 6392 -1164 1260 -3063 C ATOM 3238 N ALA B 170 -18.288 -16.381 5.104 1.00 78.63 N ANISOU 3238 N ALA B 170 13108 12316 4452 -1479 744 -2562 N ATOM 3239 CA ALA B 170 -19.047 -16.204 3.870 1.00 82.02 C ANISOU 3239 CA ALA B 170 13810 12826 4526 -1517 531 -2519 C ATOM 3240 C ALA B 170 -18.140 -16.197 2.641 1.00 85.81 C ANISOU 3240 C ALA B 170 14492 13398 4715 -1514 761 -2582 C ATOM 3241 O ALA B 170 -18.518 -16.695 1.581 1.00 89.11 O ANISOU 3241 O ALA B 170 15116 13871 4872 -1512 631 -2685 O ATOM 3242 CB ALA B 170 -19.871 -14.926 3.929 1.00 81.52 C ANISOU 3242 CB ALA B 170 13814 12802 4358 -1574 342 -2234 C ATOM 3243 N ILE B 171 -16.945 -15.633 2.788 1.00 85.56 N ANISOU 3243 N ILE B 171 14390 13388 4729 -1520 1101 -2524 N ATOM 3244 CA ILE B 171 -16.009 -15.540 1.671 1.00 89.25 C ANISOU 3244 CA ILE B 171 15026 13950 4934 -1526 1353 -2567 C ATOM 3245 C ILE B 171 -15.151 -16.796 1.515 1.00 90.36 C ANISOU 3245 C ILE B 171 15102 14073 5159 -1439 1545 -2846 C ATOM 3246 O ILE B 171 -15.084 -17.382 0.434 1.00 93.94 O ANISOU 3246 O ILE B 171 15754 14584 5356 -1416 1555 -2988 O ATOM 3247 CB ILE B 171 -15.087 -14.313 1.808 1.00 89.06 C ANISOU 3247 CB ILE B 171 14957 13964 4916 -1591 1637 -2372 C ATOM 3248 CG1 ILE B 171 -15.916 -13.027 1.850 1.00 88.53 C ANISOU 3248 CG1 ILE B 171 15002 13899 4735 -1667 1458 -2084 C ATOM 3249 CG2 ILE B 171 -14.086 -14.266 0.664 1.00 93.11 C ANISOU 3249 CG2 ILE B 171 15627 14580 5170 -1605 1916 -2424 C ATOM 3250 CD1 ILE B 171 -15.096 -11.780 2.096 1.00 88.08 C ANISOU 3250 CD1 ILE B 171 14897 13841 4729 -1745 1716 -1884 C ATOM 3251 N ARG B 172 -14.500 -17.202 2.600 1.00105.16 N ANISOU 3251 N ARG B 172 16701 15868 7387 -1383 1693 -2920 N ATOM 3252 CA ARG B 172 -13.589 -18.344 2.580 1.00106.57 C ANISOU 3252 CA ARG B 172 16793 16018 7681 -1277 1893 -3161 C ATOM 3253 C ARG B 172 -14.310 -19.666 2.324 1.00107.72 C ANISOU 3253 C ARG B 172 17037 16085 7809 -1213 1678 -3382 C ATOM 3254 O ARG B 172 -13.840 -20.495 1.544 1.00111.76 O ANISOU 3254 O ARG B 172 17664 16611 8188 -1148 1788 -3578 O ATOM 3255 CB ARG B 172 -12.800 -18.414 3.890 1.00105.72 C ANISOU 3255 CB ARG B 172 16354 15845 7969 -1222 2063 -3162 C ATOM 3256 CG ARG B 172 -11.875 -19.616 4.010 1.00106.97 C ANISOU 3256 CG ARG B 172 16398 15961 8284 -1087 2250 -3394 C ATOM 3257 CD ARG B 172 -10.865 -19.665 2.874 1.00111.22 C ANISOU 3257 CD ARG B 172 17063 16611 8585 -1068 2522 -3475 C ATOM 3258 NE ARG B 172 -9.904 -20.750 3.051 1.00113.04 N ANISOU 3258 NE ARG B 172 17160 16806 8986 -921 2720 -3680 N ATOM 3259 CZ ARG B 172 -8.988 -21.091 2.150 1.00116.64 C ANISOU 3259 CZ ARG B 172 17702 17343 9273 -864 2962 -3805 C ATOM 3260 NH1 ARG B 172 -8.908 -20.435 1.001 1.00120.09 N ANISOU 3260 NH1 ARG B 172 18366 17906 9359 -951 3040 -3748 N ATOM 3261 NH2 ARG B 172 -8.153 -22.091 2.397 1.00116.71 N ANISOU 3261 NH2 ARG B 172 17577 17310 9459 -712 3128 -3985 N ATOM 3262 N HIS B 173 -15.450 -19.860 2.979 1.00117.47 N ANISOU 3262 N HIS B 173 18222 17232 9178 -1237 1375 -3355 N ATOM 3263 CA HIS B 173 -16.219 -21.092 2.826 1.00118.75 C ANISOU 3263 CA HIS B 173 18461 17300 9358 -1202 1148 -3559 C ATOM 3264 C HIS B 173 -17.643 -20.809 2.353 1.00120.53 C ANISOU 3264 C HIS B 173 18848 17558 9391 -1294 776 -3481 C ATOM 3265 O HIS B 173 -18.565 -20.742 3.163 1.00118.68 O ANISOU 3265 O HIS B 173 18494 17256 9343 -1332 539 -3406 O ATOM 3266 CB HIS B 173 -16.249 -21.869 4.144 1.00114.63 C ANISOU 3266 CB HIS B 173 17694 16622 9239 -1138 1125 -3640 C ATOM 3267 CG HIS B 173 -14.893 -22.176 4.697 1.00114.19 C ANISOU 3267 CG HIS B 173 17451 16540 9397 -1029 1456 -3707 C ATOM 3268 ND1 HIS B 173 -14.083 -23.163 4.178 1.00117.18 N ANISOU 3268 ND1 HIS B 173 17891 16893 9739 -923 1638 -3920 N ATOM 3269 CD2 HIS B 173 -14.205 -21.628 5.726 1.00111.41 C ANISOU 3269 CD2 HIS B 173 16842 16190 9298 -1004 1624 -3591 C ATOM 3270 CE1 HIS B 173 -12.953 -23.209 4.862 1.00115.13 C ANISOU 3270 CE1 HIS B 173 17411 16627 9706 -831 1899 -3922 C ATOM 3271 NE2 HIS B 173 -13.002 -22.288 5.807 1.00112.02 N ANISOU 3271 NE2 HIS B 173 16817 16252 9492 -883 1891 -3727 N ATOM 3272 N PRO B 174 -17.823 -20.651 1.033 1.00108.40 N ANISOU 3272 N PRO B 174 17574 16135 7478 -1328 720 -3498 N ATOM 3273 CA PRO B 174 -19.115 -20.301 0.429 1.00110.35 C ANISOU 3273 CA PRO B 174 17979 16447 7501 -1406 361 -3408 C ATOM 3274 C PRO B 174 -20.224 -21.312 0.717 1.00110.72 C ANISOU 3274 C PRO B 174 17986 16390 7693 -1422 28 -3559 C ATOM 3275 O PRO B 174 -21.342 -20.913 1.041 1.00107.63 O ANISOU 3275 O PRO B 174 17541 16005 7349 -1482 -273 -3425 O ATOM 3276 CB PRO B 174 -18.804 -20.285 -1.072 1.00117.68 C ANISOU 3276 CB PRO B 174 19193 17509 8009 -1410 430 -3474 C ATOM 3277 CG PRO B 174 -17.340 -20.032 -1.153 1.00117.61 C ANISOU 3277 CG PRO B 174 19154 17534 7996 -1363 857 -3475 C ATOM 3278 CD PRO B 174 -16.755 -20.748 0.024 1.00114.46 C ANISOU 3278 CD PRO B 174 18495 16993 8002 -1288 1006 -3592 C ATOM 3279 N PHE B 175 -19.918 -22.601 0.599 1.00174.54 N ANISOU 3279 N PHE B 175 26090 24374 15852 -1369 81 -3830 N ATOM 3280 CA PHE B 175 -20.937 -23.640 0.730 1.00175.19 C ANISOU 3280 CA PHE B 175 26163 24345 16054 -1402 -225 -3997 C ATOM 3281 C PHE B 175 -21.107 -24.147 2.161 1.00171.13 C ANISOU 3281 C PHE B 175 25393 23652 15976 -1387 -243 -4015 C ATOM 3282 O PHE B 175 -22.224 -24.433 2.594 1.00170.19 O ANISOU 3282 O PHE B 175 25191 23466 16005 -1456 -544 -4011 O ATOM 3283 CB PHE B 175 -20.635 -24.809 -0.212 1.00160.48 C ANISOU 3283 CB PHE B 175 24495 22452 14026 -1364 -187 -4291 C ATOM 3284 CG PHE B 175 -21.617 -25.940 -0.108 1.00160.69 C ANISOU 3284 CG PHE B 175 24520 22343 14192 -1411 -482 -4487 C ATOM 3285 CD1 PHE B 175 -22.875 -25.838 -0.678 1.00162.52 C ANISOU 3285 CD1 PHE B 175 24826 22650 14275 -1516 -862 -4473 C ATOM 3286 CD2 PHE B 175 -21.280 -27.108 0.556 1.00159.53 C ANISOU 3286 CD2 PHE B 175 24291 21992 14331 -1352 -381 -4682 C ATOM 3287 CE1 PHE B 175 -23.781 -26.878 -0.584 1.00163.43 C ANISOU 3287 CE1 PHE B 175 24918 22641 14538 -1580 -1133 -4658 C ATOM 3288 CE2 PHE B 175 -22.181 -28.152 0.653 1.00160.74 C ANISOU 3288 CE2 PHE B 175 24450 22001 14623 -1412 -643 -4859 C ATOM 3289 CZ PHE B 175 -23.433 -28.037 0.082 1.00162.66 C ANISOU 3289 CZ PHE B 175 24752 22321 14728 -1536 -1018 -4852 C ATOM 3290 N LYS B 176 -20.001 -24.263 2.889 1.00162.02 N ANISOU 3290 N LYS B 176 24104 22429 15028 -1296 76 -4033 N ATOM 3291 CA LYS B 176 -20.036 -24.773 4.256 1.00157.83 C ANISOU 3291 CA LYS B 176 23336 21733 14899 -1264 92 -4051 C ATOM 3292 C LYS B 176 -20.763 -23.812 5.193 1.00154.20 C ANISOU 3292 C LYS B 176 22690 21301 14597 -1332 -55 -3810 C ATOM 3293 O LYS B 176 -21.407 -24.231 6.154 1.00152.04 O ANISOU 3293 O LYS B 176 22253 20909 14604 -1357 -196 -3814 O ATOM 3294 CB LYS B 176 -18.617 -25.021 4.771 1.00153.29 C ANISOU 3294 CB LYS B 176 22646 21110 14487 -1134 468 -4108 C ATOM 3295 CG LYS B 176 -18.561 -25.762 6.098 1.00149.41 C ANISOU 3295 CG LYS B 176 21937 20439 14392 -1075 497 -4163 C ATOM 3296 CD LYS B 176 -17.348 -25.346 6.915 1.00146.30 C ANISOU 3296 CD LYS B 176 21326 20072 14190 -977 802 -4064 C ATOM 3297 CE LYS B 176 -16.058 -25.528 6.134 1.00148.99 C ANISOU 3297 CE LYS B 176 21741 20484 14383 -876 1109 -4154 C ATOM 3298 NZ LYS B 176 -14.880 -25.042 6.904 1.00147.24 N ANISOU 3298 NZ LYS B 176 21279 20309 14355 -796 1384 -4049 N ATOM 3299 N HIS B 177 -20.654 -22.520 4.901 1.00153.75 N ANISOU 3299 N HIS B 177 22667 21398 14355 -1364 -14 -3597 N ATOM 3300 CA HIS B 177 -21.257 -21.482 5.731 1.00150.26 C ANISOU 3300 CA HIS B 177 22071 20991 14030 -1417 -132 -3357 C ATOM 3301 C HIS B 177 -22.665 -21.127 5.253 1.00151.88 C ANISOU 3301 C HIS B 177 22364 21264 14082 -1508 -519 -3257 C ATOM 3302 O HIS B 177 -23.425 -20.468 5.965 1.00149.64 O ANISOU 3302 O HIS B 177 21942 20991 13926 -1550 -690 -3080 O ATOM 3303 CB HIS B 177 -20.356 -20.242 5.748 1.00154.71 C ANISOU 3303 CB HIS B 177 22616 21659 14508 -1400 132 -3168 C ATOM 3304 CG HIS B 177 -21.014 -19.016 6.301 1.00153.32 C ANISOU 3304 CG HIS B 177 22370 21540 14346 -1459 -7 -2905 C ATOM 3305 ND1 HIS B 177 -21.495 -18.005 5.497 1.00155.07 N ANISOU 3305 ND1 HIS B 177 22772 21879 14271 -1511 -137 -2727 N ATOM 3306 CD2 HIS B 177 -21.280 -18.642 7.575 1.00150.54 C ANISOU 3306 CD2 HIS B 177 21796 21142 14263 -1465 -37 -2787 C ATOM 3307 CE1 HIS B 177 -22.024 -17.059 6.251 1.00152.99 C ANISOU 3307 CE1 HIS B 177 22405 21626 14098 -1541 -242 -2506 C ATOM 3308 NE2 HIS B 177 -21.906 -17.421 7.516 1.00150.19 N ANISOU 3308 NE2 HIS B 177 21805 21179 14081 -1518 -181 -2545 N ATOM 3309 N LYS B 178 -23.008 -21.590 4.053 1.00197.76 N ANISOU 3309 N LYS B 178 28389 27127 19624 -1531 -661 -3376 N ATOM 3310 CA LYS B 178 -24.295 -21.293 3.423 1.00200.05 C ANISOU 3310 CA LYS B 178 28764 27507 19740 -1605 -1043 -3298 C ATOM 3311 C LYS B 178 -25.488 -21.557 4.343 1.00197.78 C ANISOU 3311 C LYS B 178 28261 27142 19745 -1664 -1344 -3258 C ATOM 3312 O LYS B 178 -26.499 -20.858 4.280 1.00198.16 O ANISOU 3312 O LYS B 178 28273 27280 19739 -1707 -1625 -3081 O ATOM 3313 CB LYS B 178 -24.446 -22.096 2.128 1.00205.03 C ANISOU 3313 CB LYS B 178 29620 28177 20108 -1618 -1149 -3514 C ATOM 3314 CG LYS B 178 -25.632 -21.691 1.268 1.00207.85 C ANISOU 3314 CG LYS B 178 30085 28672 20218 -1682 -1522 -3433 C ATOM 3315 CD LYS B 178 -25.482 -20.268 0.756 1.00208.56 C ANISOU 3315 CD LYS B 178 30294 28925 20027 -1666 -1484 -3163 C ATOM 3316 CE LYS B 178 -26.563 -19.931 -0.258 1.00212.53 C ANISOU 3316 CE LYS B 178 30934 29581 20238 -1704 -1843 -3097 C ATOM 3317 NZ LYS B 178 -27.929 -20.089 0.311 1.00212.03 N ANISOU 3317 NZ LYS B 178 30670 29499 20393 -1756 -2236 -3062 N ATOM 3318 N THR B 179 -25.361 -22.567 5.198 1.00136.58 N ANISOU 3318 N THR B 179 20360 19224 12310 -1658 -1279 -3414 N ATOM 3319 CA THR B 179 -26.395 -22.877 6.178 1.00134.32 C ANISOU 3319 CA THR B 179 19847 18850 12340 -1720 -1514 -3379 C ATOM 3320 C THR B 179 -25.829 -22.860 7.593 1.00131.97 C ANISOU 3320 C THR B 179 19332 18444 12368 -1675 -1281 -3337 C ATOM 3321 O THR B 179 -25.462 -23.900 8.139 1.00132.91 O ANISOU 3321 O THR B 179 19385 18405 12709 -1651 -1167 -3510 O ATOM 3322 CB THR B 179 -27.040 -24.248 5.909 1.00132.68 C ANISOU 3322 CB THR B 179 19654 18520 12238 -1783 -1714 -3619 C ATOM 3323 OG1 THR B 179 -26.026 -25.261 5.895 1.00132.05 O ANISOU 3323 OG1 THR B 179 19664 18302 12206 -1719 -1447 -3844 O ATOM 3324 CG2 THR B 179 -27.764 -24.244 4.571 1.00136.23 C ANISOU 3324 CG2 THR B 179 20274 19097 12391 -1838 -1999 -3666 C ATOM 3325 N MET B 181 -25.838 -20.820 9.940 1.00134.90 N ANISOU 3325 N MET B 181 19272 18885 13099 -1656 -1196 -2889 N ATOM 3326 CA MET B 181 -26.744 -21.212 11.012 1.00132.01 C ANISOU 3326 CA MET B 181 18659 18440 13059 -1702 -1369 -2877 C ATOM 3327 C MET B 181 -28.163 -20.735 10.724 1.00131.02 C ANISOU 3327 C MET B 181 18484 18403 12896 -1780 -1758 -2724 C ATOM 3328 O MET B 181 -28.362 -19.705 10.078 1.00131.89 O ANISOU 3328 O MET B 181 18696 18647 12772 -1769 -1852 -2538 O ATOM 3329 CB MET B 181 -26.256 -20.651 12.350 1.00133.19 C ANISOU 3329 CB MET B 181 18591 18570 13446 -1635 -1161 -2764 C ATOM 3330 CG MET B 181 -26.219 -19.132 12.410 1.00133.04 C ANISOU 3330 CG MET B 181 18561 18655 13334 -1583 -1136 -2477 C ATOM 3331 SD MET B 181 -25.218 -18.502 13.771 1.00132.94 S ANISOU 3331 SD MET B 181 18353 18583 13577 -1450 -786 -2362 S ATOM 3332 CE MET B 181 -23.579 -18.980 13.230 1.00133.16 C ANISOU 3332 CE MET B 181 18582 18664 13349 -1461 -437 -2606 C ATOM 3333 N SER B 182 -29.148 -21.490 11.202 1.00 92.39 N ANISOU 3333 N SER B 182 13428 13430 8247 -1853 -1981 -2792 N ATOM 3334 CA SER B 182 -30.548 -21.133 11.010 1.00 92.79 C ANISOU 3334 CA SER B 182 13369 13566 8324 -1918 -2362 -2649 C ATOM 3335 C SER B 182 -30.878 -19.832 11.734 1.00 91.67 C ANISOU 3335 C SER B 182 13035 13480 8318 -1817 -2378 -2330 C ATOM 3336 O SER B 182 -30.138 -19.403 12.619 1.00 90.19 O ANISOU 3336 O SER B 182 12734 13215 8321 -1707 -2105 -2242 O ATOM 3337 CB SER B 182 -31.463 -22.258 11.498 1.00 91.40 C ANISOU 3337 CB SER B 182 13004 13268 8459 -2014 -2547 -2776 C ATOM 3338 OG SER B 182 -31.250 -22.530 12.872 1.00 89.61 O ANISOU 3338 OG SER B 182 12539 12898 8611 -1963 -2361 -2747 O ATOM 3339 N ARG B 183 -31.990 -19.208 11.353 1.00132.59 N ANISOU 3339 N ARG B 183 18173 18779 13425 -1827 -2694 -2151 N ATOM 3340 CA ARG B 183 -32.401 -17.938 11.946 1.00132.68 C ANISOU 3340 CA ARG B 183 18019 18822 13573 -1693 -2720 -1832 C ATOM 3341 C ARG B 183 -32.635 -18.066 13.449 1.00131.30 C ANISOU 3341 C ARG B 183 17507 18508 13872 -1614 -2603 -1749 C ATOM 3342 O ARG B 183 -32.459 -17.103 14.198 1.00130.81 O ANISOU 3342 O ARG B 183 17340 18421 13940 -1484 -2464 -1539 O ATOM 3343 CB ARG B 183 -33.657 -17.401 11.255 1.00135.41 C ANISOU 3343 CB ARG B 183 18342 19310 13797 -1704 -3121 -1674 C ATOM 3344 CG ARG B 183 -33.460 -17.076 9.782 1.00137.37 C ANISOU 3344 CG ARG B 183 18947 19710 13536 -1760 -3251 -1703 C ATOM 3345 CD ARG B 183 -34.701 -16.431 9.187 1.00140.44 C ANISOU 3345 CD ARG B 183 19276 20229 13854 -1707 -3635 -1509 C ATOM 3346 NE ARG B 183 -34.524 -16.104 7.775 1.00144.09 N ANISOU 3346 NE ARG B 183 20042 20800 13905 -1675 -3691 -1512 N ATOM 3347 CZ ARG B 183 -35.434 -15.481 7.033 1.00147.36 C ANISOU 3347 CZ ARG B 183 20466 21348 14176 -1605 -3992 -1349 C ATOM 3348 NH1 ARG B 183 -36.589 -15.113 7.569 1.00147.24 N ANISOU 3348 NH1 ARG B 183 20156 21371 14418 -1547 -4261 -1172 N ATOM 3349 NH2 ARG B 183 -35.189 -15.224 5.755 1.00150.71 N ANISOU 3349 NH2 ARG B 183 21182 21874 14207 -1581 -4016 -1358 N ATOM 3350 N SER B 184 -33.028 -19.261 13.880 1.00 83.67 N ANISOU 3350 N SER B 184 11326 12379 8086 -1700 -2652 -1918 N ATOM 3351 CA SER B 184 -33.217 -19.548 15.296 1.00 82.22 C ANISOU 3351 CA SER B 184 10853 12055 8332 -1640 -2521 -1860 C ATOM 3352 C SER B 184 -31.915 -19.355 16.065 1.00 79.62 C ANISOU 3352 C SER B 184 10563 11635 8055 -1530 -2141 -1862 C ATOM 3353 O SER B 184 -31.864 -18.596 17.032 1.00 78.76 O ANISOU 3353 O SER B 184 10297 11494 8134 -1409 -2018 -1672 O ATOM 3354 CB SER B 184 -33.734 -20.975 15.487 1.00 82.80 C ANISOU 3354 CB SER B 184 10825 12020 8616 -1777 -2609 -2067 C ATOM 3355 OG SER B 184 -33.864 -21.292 16.861 1.00 80.26 O ANISOU 3355 OG SER B 184 10256 11553 8685 -1719 -2451 -2006 O ATOM 3356 N ARG B 185 -30.864 -20.039 15.622 1.00 74.85 N ANISOU 3356 N ARG B 185 10164 10995 7280 -1571 -1961 -2084 N ATOM 3357 CA ARG B 185 -29.559 -19.948 16.268 1.00 72.54 C ANISOU 3357 CA ARG B 185 9897 10636 7028 -1472 -1612 -2114 C ATOM 3358 C ARG B 185 -28.976 -18.541 16.177 1.00 71.77 C ANISOU 3358 C ARG B 185 9874 10635 6762 -1385 -1485 -1927 C ATOM 3359 O ARG B 185 -28.237 -18.109 17.063 1.00 70.74 O ANISOU 3359 O ARG B 185 9656 10456 6765 -1288 -1248 -1856 O ATOM 3360 CB ARG B 185 -28.583 -20.961 15.662 1.00 72.88 C ANISOU 3360 CB ARG B 185 10147 10641 6903 -1523 -1457 -2400 C ATOM 3361 CG ARG B 185 -28.995 -22.412 15.849 1.00 73.70 C ANISOU 3361 CG ARG B 185 10200 10600 7205 -1599 -1524 -2601 C ATOM 3362 CD ARG B 185 -27.886 -23.359 15.416 1.00 73.73 C ANISOU 3362 CD ARG B 185 10402 10537 7077 -1603 -1316 -2877 C ATOM 3363 NE ARG B 185 -28.256 -24.760 15.601 1.00 74.16 N ANISOU 3363 NE ARG B 185 10438 10418 7322 -1676 -1375 -3072 N ATOM 3364 CZ ARG B 185 -28.790 -25.522 14.652 1.00 75.83 C ANISOU 3364 CZ ARG B 185 10807 10615 7390 -1825 -1566 -3269 C ATOM 3365 NH1 ARG B 185 -29.016 -25.020 13.446 1.00 77.50 N ANISOU 3365 NH1 ARG B 185 11207 10992 7249 -1903 -1724 -3289 N ATOM 3366 NH2 ARG B 185 -29.096 -26.787 14.909 1.00 77.44 N ANISOU 3366 NH2 ARG B 185 10996 10629 7798 -1898 -1598 -3442 N ATOM 3367 N THR B 186 -29.310 -17.831 15.104 1.00 60.93 N ANISOU 3367 N THR B 186 8672 9391 5087 -1426 -1649 -1846 N ATOM 3368 CA THR B 186 -28.837 -16.464 14.918 1.00 61.40 C ANISOU 3368 CA THR B 186 8836 9522 4972 -1360 -1541 -1652 C ATOM 3369 C THR B 186 -29.478 -15.527 15.936 1.00 61.86 C ANISOU 3369 C THR B 186 8670 9538 5296 -1250 -1583 -1393 C ATOM 3370 O THR B 186 -28.789 -14.742 16.586 1.00 60.98 O ANISOU 3370 O THR B 186 8529 9389 5251 -1171 -1363 -1288 O ATOM 3371 CB THR B 186 -29.124 -15.947 13.497 1.00 63.62 C ANISOU 3371 CB THR B 186 9381 9943 4849 -1424 -1722 -1607 C ATOM 3372 OG1 THR B 186 -28.500 -16.809 12.538 1.00 65.59 O ANISOU 3372 OG1 THR B 186 9861 10235 4826 -1525 -1658 -1863 O ATOM 3373 CG2 THR B 186 -28.585 -14.535 13.326 1.00 63.29 C ANISOU 3373 CG2 THR B 186 9469 9945 4633 -1363 -1583 -1394 C ATOM 3374 N LYS B 187 -30.799 -15.616 16.072 1.00 83.82 N ANISOU 3374 N LYS B 187 11286 12326 8234 -1247 -1863 -1302 N ATOM 3375 CA LYS B 187 -31.522 -14.804 17.047 1.00 84.77 C ANISOU 3375 CA LYS B 187 11178 12406 8624 -1129 -1905 -1068 C ATOM 3376 C LYS B 187 -31.103 -15.158 18.472 1.00 82.83 C ANISOU 3376 C LYS B 187 10730 12032 8708 -1068 -1671 -1097 C ATOM 3377 O LYS B 187 -31.001 -14.281 19.337 1.00 82.68 O ANISOU 3377 O LYS B 187 10616 11968 8830 -959 -1548 -935 O ATOM 3378 CB LYS B 187 -33.034 -14.965 16.869 1.00 87.11 C ANISOU 3378 CB LYS B 187 11305 12754 9039 -1144 -2250 -990 C ATOM 3379 CG LYS B 187 -33.564 -14.382 15.566 1.00 89.79 C ANISOU 3379 CG LYS B 187 11823 13233 9058 -1167 -2519 -904 C ATOM 3380 CD LYS B 187 -35.060 -14.610 15.415 1.00 90.96 C ANISOU 3380 CD LYS B 187 11764 13453 9345 -1183 -2880 -843 C ATOM 3381 CE LYS B 187 -35.390 -16.091 15.328 1.00 90.87 C ANISOU 3381 CE LYS B 187 11668 13424 9436 -1344 -2985 -1091 C ATOM 3382 NZ LYS B 187 -36.847 -16.325 15.121 1.00 91.50 N ANISOU 3382 NZ LYS B 187 11526 13590 9648 -1390 -3350 -1045 N ATOM 3383 N LYS B 188 -30.857 -16.444 18.708 1.00 58.62 N ANISOU 3383 N LYS B 188 7621 8901 5752 -1136 -1614 -1304 N ATOM 3384 CA LYS B 188 -30.337 -16.903 19.991 1.00 56.90 C ANISOU 3384 CA LYS B 188 7252 8563 5806 -1076 -1389 -1346 C ATOM 3385 C LYS B 188 -28.978 -16.269 20.266 1.00 55.32 C ANISOU 3385 C LYS B 188 7153 8362 5506 -1010 -1105 -1343 C ATOM 3386 O LYS B 188 -28.680 -15.874 21.395 1.00 55.06 O ANISOU 3386 O LYS B 188 6989 8267 5664 -918 -949 -1257 O ATOM 3387 CB LYS B 188 -30.211 -18.428 20.012 1.00 54.07 C ANISOU 3387 CB LYS B 188 6888 8121 5535 -1159 -1376 -1578 C ATOM 3388 CG LYS B 188 -31.531 -19.176 20.131 1.00 54.91 C ANISOU 3388 CG LYS B 188 6831 8190 5843 -1238 -1611 -1587 C ATOM 3389 CD LYS B 188 -31.301 -20.681 20.166 1.00 54.38 C ANISOU 3389 CD LYS B 188 6792 8002 5870 -1324 -1564 -1820 C ATOM 3390 CE LYS B 188 -32.603 -21.444 20.365 1.00 55.16 C ANISOU 3390 CE LYS B 188 6713 8043 6202 -1431 -1776 -1828 C ATOM 3391 NZ LYS B 188 -33.552 -21.245 19.236 1.00 57.15 N ANISOU 3391 NZ LYS B 188 7001 8424 6289 -1544 -2091 -1832 N ATOM 3392 N PHE B 189 -28.161 -16.171 19.222 1.00 62.39 N ANISOU 3392 N PHE B 189 8280 9332 6094 -1067 -1037 -1442 N ATOM 3393 CA PHE B 189 -26.829 -15.588 19.338 1.00 61.08 C ANISOU 3393 CA PHE B 189 8205 9186 5818 -1033 -764 -1455 C ATOM 3394 C PHE B 189 -26.904 -14.088 19.605 1.00 62.21 C ANISOU 3394 C PHE B 189 8350 9346 5939 -974 -735 -1219 C ATOM 3395 O PHE B 189 -26.081 -13.541 20.338 1.00 61.60 O ANISOU 3395 O PHE B 189 8230 9241 5935 -926 -522 -1184 O ATOM 3396 CB PHE B 189 -26.010 -15.865 18.076 1.00 60.48 C ANISOU 3396 CB PHE B 189 8377 9195 5409 -1119 -687 -1621 C ATOM 3397 CG PHE B 189 -24.585 -15.402 18.164 1.00 59.18 C ANISOU 3397 CG PHE B 189 8278 9063 5146 -1104 -387 -1660 C ATOM 3398 CD1 PHE B 189 -23.670 -16.080 18.952 1.00 57.21 C ANISOU 3398 CD1 PHE B 189 7909 8762 5067 -1051 -179 -1798 C ATOM 3399 CD2 PHE B 189 -24.156 -14.294 17.452 1.00 60.52 C ANISOU 3399 CD2 PHE B 189 8624 9315 5055 -1144 -314 -1555 C ATOM 3400 CE1 PHE B 189 -22.357 -15.659 19.034 1.00 56.36 C ANISOU 3400 CE1 PHE B 189 7825 8705 4885 -1042 87 -1842 C ATOM 3401 CE2 PHE B 189 -22.843 -13.870 17.529 1.00 59.08 C ANISOU 3401 CE2 PHE B 189 8481 9170 4798 -1155 -28 -1597 C ATOM 3402 CZ PHE B 189 -21.943 -14.552 18.322 1.00 56.81 C ANISOU 3402 CZ PHE B 189 8041 8850 4695 -1105 168 -1747 C ATOM 3403 N ILE B 190 -27.892 -13.429 19.007 1.00 78.40 N ANISOU 3403 N ILE B 190 10454 11441 7893 -977 -958 -1062 N ATOM 3404 CA ILE B 190 -28.116 -12.005 19.238 1.00 79.81 C ANISOU 3404 CA ILE B 190 10648 11608 8067 -904 -953 -825 C ATOM 3405 C ILE B 190 -28.532 -11.768 20.685 1.00 79.69 C ANISOU 3405 C ILE B 190 10387 11495 8395 -795 -911 -723 C ATOM 3406 O ILE B 190 -28.016 -10.867 21.355 1.00 79.96 O ANISOU 3406 O ILE B 190 10415 11479 8486 -738 -744 -627 O ATOM 3407 CB ILE B 190 -29.197 -11.441 18.295 1.00 83.37 C ANISOU 3407 CB ILE B 190 11196 12124 8355 -900 -1233 -670 C ATOM 3408 CG1 ILE B 190 -28.752 -11.564 16.837 1.00 84.70 C ANISOU 3408 CG1 ILE B 190 11650 12397 8134 -1007 -1268 -757 C ATOM 3409 CG2 ILE B 190 -29.495 -9.988 18.629 1.00 84.83 C ANISOU 3409 CG2 ILE B 190 11393 12263 8575 -796 -1226 -416 C ATOM 3410 CD1 ILE B 190 -27.485 -10.804 16.520 1.00 84.75 C ANISOU 3410 CD1 ILE B 190 11862 12413 7925 -1042 -997 -746 C ATOM 3411 N SER B 191 -29.465 -12.589 21.163 1.00 43.54 N ANISOU 3411 N SER B 191 5615 6889 4041 -778 -1055 -750 N ATOM 3412 CA SER B 191 -29.907 -12.521 22.551 1.00 42.32 C ANISOU 3412 CA SER B 191 5227 6647 4208 -681 -1002 -668 C ATOM 3413 C SER B 191 -28.733 -12.751 23.499 1.00 39.92 C ANISOU 3413 C SER B 191 4891 6284 3993 -659 -731 -765 C ATOM 3414 O SER B 191 -28.616 -12.090 24.534 1.00 39.87 O ANISOU 3414 O SER B 191 4798 6221 4132 -573 -613 -668 O ATOM 3415 CB SER B 191 -31.007 -13.551 22.814 1.00 42.18 C ANISOU 3415 CB SER B 191 5015 6612 4400 -702 -1176 -708 C ATOM 3416 OG SER B 191 -32.131 -13.321 21.982 1.00 44.50 O ANISOU 3416 OG SER B 191 5300 6981 4629 -721 -1451 -618 O ATOM 3417 N ALA B 192 -27.864 -13.688 23.132 1.00 34.78 N ANISOU 3417 N ALA B 192 4315 5650 3251 -729 -640 -963 N ATOM 3418 CA ALA B 192 -26.669 -13.980 23.916 1.00 33.04 C ANISOU 3418 CA ALA B 192 4060 5396 3100 -699 -400 -1069 C ATOM 3419 C ALA B 192 -25.725 -12.781 23.941 1.00 32.50 C ANISOU 3419 C ALA B 192 4088 5359 2904 -691 -229 -1006 C ATOM 3420 O ALA B 192 -25.116 -12.483 24.969 1.00 30.86 O ANISOU 3420 O ALA B 192 3792 5115 2819 -636 -73 -998 O ATOM 3421 CB ALA B 192 -25.958 -15.205 23.364 1.00 33.75 C ANISOU 3421 CB ALA B 192 4219 5499 3106 -759 -345 -1295 C ATOM 3422 N ILE B 193 -25.611 -12.099 22.805 1.00 64.26 N ANISOU 3422 N ILE B 193 8298 9447 6673 -756 -262 -962 N ATOM 3423 CA ILE B 193 -24.784 -10.901 22.707 1.00 63.98 C ANISOU 3423 CA ILE B 193 8377 9427 6506 -778 -101 -888 C ATOM 3424 C ILE B 193 -25.309 -9.802 23.625 1.00 64.85 C ANISOU 3424 C ILE B 193 8412 9455 6773 -692 -109 -695 C ATOM 3425 O ILE B 193 -24.545 -9.192 24.375 1.00 63.90 O ANISOU 3425 O ILE B 193 8267 9301 6711 -681 66 -685 O ATOM 3426 CB ILE B 193 -24.712 -10.374 21.258 1.00 64.36 C ANISOU 3426 CB ILE B 193 8671 9551 6235 -866 -145 -850 C ATOM 3427 CG1 ILE B 193 -23.833 -11.287 20.402 1.00 63.19 C ANISOU 3427 CG1 ILE B 193 8625 9488 5899 -955 -47 -1064 C ATOM 3428 CG2 ILE B 193 -24.165 -8.955 21.226 1.00 64.70 C ANISOU 3428 CG2 ILE B 193 8838 9572 6174 -889 -7 -711 C ATOM 3429 CD1 ILE B 193 -23.642 -10.792 18.986 1.00 64.89 C ANISOU 3429 CD1 ILE B 193 9104 9786 5765 -1049 -55 -1037 C ATOM 3430 N TRP B 194 -26.616 -9.562 23.567 1.00 43.02 N ANISOU 3430 N TRP B 194 5605 6661 4080 -631 -314 -553 N ATOM 3431 CA TRP B 194 -27.243 -8.555 24.418 1.00 42.71 C ANISOU 3431 CA TRP B 194 5492 6536 4200 -526 -325 -374 C ATOM 3432 C TRP B 194 -27.069 -8.872 25.902 1.00 41.35 C ANISOU 3432 C TRP B 194 5128 6301 4283 -456 -204 -420 C ATOM 3433 O TRP B 194 -26.689 -8.002 26.691 1.00 41.19 O ANISOU 3433 O TRP B 194 5108 6219 4323 -415 -70 -363 O ATOM 3434 CB TRP B 194 -28.728 -8.407 24.083 1.00 45.99 C ANISOU 3434 CB TRP B 194 5853 6950 4670 -456 -576 -229 C ATOM 3435 CG TRP B 194 -28.985 -7.572 22.867 1.00 48.37 C ANISOU 3435 CG TRP B 194 6363 7285 4729 -474 -694 -102 C ATOM 3436 CD1 TRP B 194 -29.455 -8.001 21.660 1.00 49.35 C ANISOU 3436 CD1 TRP B 194 6581 7502 4667 -529 -894 -115 C ATOM 3437 CD2 TRP B 194 -28.780 -6.160 22.739 1.00 49.21 C ANISOU 3437 CD2 TRP B 194 6633 7325 4741 -437 -622 61 C ATOM 3438 NE1 TRP B 194 -29.559 -6.943 20.790 1.00 50.65 N ANISOU 3438 NE1 TRP B 194 6958 7671 4614 -518 -957 44 N ATOM 3439 CE2 TRP B 194 -29.150 -5.802 21.428 1.00 50.54 C ANISOU 3439 CE2 TRP B 194 6994 7549 4659 -461 -786 159 C ATOM 3440 CE3 TRP B 194 -28.320 -5.164 23.607 1.00 49.11 C ANISOU 3440 CE3 TRP B 194 6636 7200 4823 -391 -439 131 C ATOM 3441 CZ2 TRP B 194 -29.074 -4.490 20.964 1.00 51.89 C ANISOU 3441 CZ2 TRP B 194 7379 7655 4680 -433 -762 341 C ATOM 3442 CZ3 TRP B 194 -28.247 -3.863 23.144 1.00 50.34 C ANISOU 3442 CZ3 TRP B 194 7001 7282 4842 -376 -412 295 C ATOM 3443 CH2 TRP B 194 -28.621 -3.538 21.835 1.00 51.75 C ANISOU 3443 CH2 TRP B 194 7377 7507 4780 -393 -568 407 C ATOM 3444 N LEU B 195 -27.344 -10.120 26.272 1.00 38.36 N ANISOU 3444 N LEU B 195 4604 5931 4040 -449 -251 -524 N ATOM 3445 CA LEU B 195 -27.218 -10.552 27.660 1.00 36.88 C ANISOU 3445 CA LEU B 195 4250 5687 4075 -380 -145 -560 C ATOM 3446 C LEU B 195 -25.786 -10.400 28.167 1.00 34.18 C ANISOU 3446 C LEU B 195 3942 5354 3690 -400 66 -663 C ATOM 3447 O LEU B 195 -25.558 -9.846 29.245 1.00 32.77 O ANISOU 3447 O LEU B 195 3704 5129 3620 -339 170 -623 O ATOM 3448 CB LEU B 195 -27.686 -11.999 27.820 1.00 35.60 C ANISOU 3448 CB LEU B 195 3964 5520 4041 -389 -225 -656 C ATOM 3449 CG LEU B 195 -27.551 -12.606 29.219 1.00 33.89 C ANISOU 3449 CG LEU B 195 3601 5242 4035 -319 -114 -688 C ATOM 3450 CD1 LEU B 195 -28.245 -11.737 30.257 1.00 34.21 C ANISOU 3450 CD1 LEU B 195 3547 5227 4226 -217 -89 -531 C ATOM 3451 CD2 LEU B 195 -28.110 -14.020 29.243 1.00 33.54 C ANISOU 3451 CD2 LEU B 195 3464 5166 4113 -344 -196 -767 C ATOM 3452 N ALA B 196 -24.829 -10.890 27.384 1.00 23.62 N ANISOU 3452 N ALA B 196 2696 4087 2192 -486 129 -804 N ATOM 3453 CA ALA B 196 -23.418 -10.774 27.734 1.00 24.23 C ANISOU 3453 CA ALA B 196 2778 4200 2227 -513 323 -913 C ATOM 3454 C ALA B 196 -23.019 -9.312 27.892 1.00 24.36 C ANISOU 3454 C ALA B 196 2878 4199 2180 -540 420 -815 C ATOM 3455 O ALA B 196 -22.275 -8.958 28.806 1.00 24.23 O ANISOU 3455 O ALA B 196 2801 4175 2232 -528 550 -849 O ATOM 3456 CB ALA B 196 -22.552 -11.452 26.687 1.00 26.47 C ANISOU 3456 CB ALA B 196 3148 4571 2339 -597 380 -1074 C ATOM 3457 N SER B 197 -23.528 -8.466 27.000 1.00 51.86 N ANISOU 3457 N SER B 197 6506 7668 5529 -578 347 -692 N ATOM 3458 CA SER B 197 -23.264 -7.033 27.056 1.00 52.73 C ANISOU 3458 CA SER B 197 6730 7725 5578 -608 432 -579 C ATOM 3459 C SER B 197 -23.767 -6.433 28.365 1.00 53.06 C ANISOU 3459 C SER B 197 6676 7664 5819 -502 442 -489 C ATOM 3460 O SER B 197 -23.062 -5.656 29.013 1.00 51.99 O ANISOU 3460 O SER B 197 6558 7490 5704 -528 579 -499 O ATOM 3461 CB SER B 197 -23.917 -6.322 25.870 1.00 54.25 C ANISOU 3461 CB SER B 197 7111 7904 5597 -637 322 -436 C ATOM 3462 OG SER B 197 -23.433 -6.836 24.642 1.00 54.13 O ANISOU 3462 OG SER B 197 7213 7989 5363 -740 325 -524 O ATOM 3463 N ALA B 198 -24.987 -6.799 28.747 1.00 33.49 N ANISOU 3463 N ALA B 198 4094 5146 3485 -392 302 -409 N ATOM 3464 CA ALA B 198 -25.567 -6.332 30.002 1.00 32.57 C ANISOU 3464 CA ALA B 198 3880 4938 3557 -277 321 -328 C ATOM 3465 C ALA B 198 -24.720 -6.780 31.191 1.00 31.04 C ANISOU 3465 C ALA B 198 3576 4757 3459 -267 454 -453 C ATOM 3466 O ALA B 198 -24.450 -5.997 32.106 1.00 30.54 O ANISOU 3466 O ALA B 198 3519 4633 3450 -237 551 -434 O ATOM 3467 CB ALA B 198 -26.996 -6.832 30.146 1.00 18.97 C ANISOU 3467 CB ALA B 198 2032 3197 1980 -173 162 -239 C ATOM 3468 N LEU B 199 -24.300 -8.042 31.163 1.00 28.49 N ANISOU 3468 N LEU B 199 3166 4509 3150 -286 452 -583 N ATOM 3469 CA LEU B 199 -23.451 -8.597 32.213 1.00 27.32 C ANISOU 3469 CA LEU B 199 2915 4386 3079 -261 556 -698 C ATOM 3470 C LEU B 199 -22.140 -7.827 32.324 1.00 27.38 C ANISOU 3470 C LEU B 199 2980 4432 2992 -343 697 -774 C ATOM 3471 O LEU B 199 -21.640 -7.592 33.424 1.00 26.66 O ANISOU 3471 O LEU B 199 2827 4335 2968 -312 774 -814 O ATOM 3472 CB LEU B 199 -23.163 -10.075 31.946 1.00 27.20 C ANISOU 3472 CB LEU B 199 2828 4431 3077 -264 529 -823 C ATOM 3473 CG LEU B 199 -24.348 -11.039 32.000 1.00 27.24 C ANISOU 3473 CG LEU B 199 2754 4392 3203 -207 402 -779 C ATOM 3474 CD1 LEU B 199 -23.904 -12.434 31.596 1.00 27.47 C ANISOU 3474 CD1 LEU B 199 2759 4457 3222 -230 391 -922 C ATOM 3475 CD2 LEU B 199 -24.973 -11.047 33.386 1.00 26.33 C ANISOU 3475 CD2 LEU B 199 2529 4209 3264 -99 420 -701 C ATOM 3476 N LEU B 200 -21.589 -7.434 31.180 1.00 28.85 N ANISOU 3476 N LEU B 200 3284 4662 3016 -459 731 -795 N ATOM 3477 CA LEU B 200 -20.346 -6.672 31.153 1.00 29.29 C ANISOU 3477 CA LEU B 200 3387 4760 2984 -570 878 -866 C ATOM 3478 C LEU B 200 -20.572 -5.228 31.592 1.00 29.57 C ANISOU 3478 C LEU B 200 3522 4684 3029 -589 919 -755 C ATOM 3479 O LEU B 200 -19.639 -4.548 32.019 1.00 29.78 O ANISOU 3479 O LEU B 200 3560 4718 3039 -674 1037 -815 O ATOM 3480 CB LEU B 200 -19.723 -6.711 29.755 1.00 30.67 C ANISOU 3480 CB LEU B 200 3668 5014 2972 -697 926 -917 C ATOM 3481 CG LEU B 200 -19.263 -8.082 29.255 1.00 31.29 C ANISOU 3481 CG LEU B 200 3670 5201 3020 -690 924 -1064 C ATOM 3482 CD1 LEU B 200 -18.796 -8.004 27.810 1.00 33.22 C ANISOU 3482 CD1 LEU B 200 4055 5517 3053 -812 977 -1098 C ATOM 3483 CD2 LEU B 200 -18.167 -8.644 30.147 1.00 31.92 C ANISOU 3483 CD2 LEU B 200 3584 5357 3188 -665 1023 -1214 C ATOM 3484 N ALA B 201 -21.814 -4.766 31.488 1.00 34.05 N ANISOU 3484 N ALA B 201 4156 5147 3634 -508 819 -599 N ATOM 3485 CA ALA B 201 -22.151 -3.394 31.857 1.00 35.59 C ANISOU 3485 CA ALA B 201 4467 5208 3848 -497 855 -485 C ATOM 3486 C ALA B 201 -22.651 -3.284 33.296 1.00 34.44 C ANISOU 3486 C ALA B 201 4227 4990 3868 -369 858 -469 C ATOM 3487 O ALA B 201 -22.894 -2.183 33.792 1.00 35.43 O ANISOU 3487 O ALA B 201 4443 4992 4025 -344 904 -400 O ATOM 3488 CB ALA B 201 -23.174 -2.821 30.891 1.00 42.55 C ANISOU 3488 CB ALA B 201 5488 6013 4664 -463 752 -313 C ATOM 3489 N ILE B 202 -22.807 -4.429 33.956 1.00 32.66 N ANISOU 3489 N ILE B 202 3836 4831 3741 -287 818 -533 N ATOM 3490 CA ILE B 202 -23.199 -4.473 35.371 1.00 31.09 C ANISOU 3490 CA ILE B 202 3550 4585 3679 -169 839 -528 C ATOM 3491 C ILE B 202 -22.425 -3.540 36.332 1.00 29.98 C ANISOU 3491 C ILE B 202 3460 4401 3530 -207 953 -591 C ATOM 3492 O ILE B 202 -23.051 -2.856 37.145 1.00 30.21 O ANISOU 3492 O ILE B 202 3524 4324 3629 -119 977 -529 O ATOM 3493 CB ILE B 202 -23.227 -5.931 35.918 1.00 28.91 C ANISOU 3493 CB ILE B 202 3109 4391 3483 -101 801 -599 C ATOM 3494 CG1 ILE B 202 -24.526 -6.626 35.508 1.00 30.03 C ANISOU 3494 CG1 ILE B 202 3189 4511 3708 -21 685 -499 C ATOM 3495 CG2 ILE B 202 -23.083 -5.954 37.432 1.00 28.20 C ANISOU 3495 CG2 ILE B 202 2957 4286 3471 -20 861 -635 C ATOM 3496 CD1 ILE B 202 -24.720 -7.989 36.137 1.00 28.23 C ANISOU 3496 CD1 ILE B 202 2823 4321 3581 43 660 -544 C ATOM 3497 N PRO B 203 -21.076 -3.499 36.243 1.00 33.01 N ANISOU 3497 N PRO B 203 3843 4868 3832 -341 1026 -723 N ATOM 3498 CA PRO B 203 -20.322 -2.631 37.160 1.00 32.29 C ANISOU 3498 CA PRO B 203 3788 4745 3734 -401 1117 -800 C ATOM 3499 C PRO B 203 -20.736 -1.156 37.149 1.00 34.56 C ANISOU 3499 C PRO B 203 4259 4860 4013 -428 1166 -710 C ATOM 3500 O PRO B 203 -20.502 -0.464 38.140 1.00 34.10 O ANISOU 3500 O PRO B 203 4243 4735 3978 -433 1224 -760 O ATOM 3501 CB PRO B 203 -18.883 -2.764 36.656 1.00 32.59 C ANISOU 3501 CB PRO B 203 3786 4911 3684 -569 1179 -937 C ATOM 3502 CG PRO B 203 -18.829 -4.112 36.068 1.00 32.00 C ANISOU 3502 CG PRO B 203 3594 4958 3605 -525 1122 -972 C ATOM 3503 CD PRO B 203 -20.167 -4.321 35.421 1.00 31.83 C ANISOU 3503 CD PRO B 203 3630 4858 3605 -434 1032 -827 C ATOM 3504 N MET B 204 -21.333 -0.687 36.057 1.00 30.06 N ANISOU 3504 N MET B 204 3809 4212 3400 -440 1138 -583 N ATOM 3505 CA MET B 204 -21.786 0.700 35.973 1.00 30.71 C ANISOU 3505 CA MET B 204 4085 4105 3479 -440 1180 -475 C ATOM 3506 C MET B 204 -22.846 1.018 37.021 1.00 30.49 C ANISOU 3506 C MET B 204 4053 3960 3572 -255 1169 -410 C ATOM 3507 O MET B 204 -22.966 2.158 37.472 1.00 31.47 O ANISOU 3507 O MET B 204 4320 3923 3714 -248 1240 -389 O ATOM 3508 CB MET B 204 -22.320 1.017 34.575 1.00 31.80 C ANISOU 3508 CB MET B 204 4349 4195 3540 -452 1125 -328 C ATOM 3509 CG MET B 204 -21.241 1.278 33.538 1.00 32.81 C ANISOU 3509 CG MET B 204 4576 4373 3519 -662 1198 -372 C ATOM 3510 SD MET B 204 -20.127 2.620 34.003 1.00 34.08 S ANISOU 3510 SD MET B 204 4879 4416 3654 -851 1368 -453 S ATOM 3511 CE MET B 204 -18.664 1.704 34.485 1.00 34.56 C ANISOU 3511 CE MET B 204 4720 4707 3701 -992 1427 -687 C ATOM 3512 N LEU B 205 -23.611 0.003 37.406 1.00 27.75 N ANISOU 3512 N LEU B 205 3547 3686 3311 -111 1093 -384 N ATOM 3513 CA LEU B 205 -24.646 0.161 38.418 1.00 27.64 C ANISOU 3513 CA LEU B 205 3499 3587 3416 68 1101 -325 C ATOM 3514 C LEU B 205 -24.037 0.401 39.796 1.00 27.89 C ANISOU 3514 C LEU B 205 3538 3609 3450 59 1195 -454 C ATOM 3515 O LEU B 205 -24.685 0.953 40.685 1.00 28.42 O ANISOU 3515 O LEU B 205 3655 3565 3578 176 1250 -426 O ATOM 3516 CB LEU B 205 -25.546 -1.075 38.451 1.00 26.75 C ANISOU 3516 CB LEU B 205 3202 3568 3393 189 1011 -271 C ATOM 3517 CG LEU B 205 -26.262 -1.416 37.143 1.00 27.21 C ANISOU 3517 CG LEU B 205 3237 3653 3448 199 888 -157 C ATOM 3518 CD1 LEU B 205 -27.013 -2.732 37.266 1.00 26.45 C ANISOU 3518 CD1 LEU B 205 2948 3652 3448 277 803 -139 C ATOM 3519 CD2 LEU B 205 -27.206 -0.292 36.746 1.00 28.70 C ANISOU 3519 CD2 LEU B 205 3537 3696 3672 297 867 -2 C ATOM 3520 N PHE B 206 -22.786 -0.012 39.967 1.00 48.14 N ANISOU 3520 N PHE B 206 6051 6298 5944 -75 1212 -599 N ATOM 3521 CA PHE B 206 -22.109 0.121 41.251 1.00 46.99 C ANISOU 3521 CA PHE B 206 5897 6177 5781 -92 1269 -733 C ATOM 3522 C PHE B 206 -20.979 1.143 41.196 1.00 48.47 C ANISOU 3522 C PHE B 206 6207 6321 5891 -282 1338 -842 C ATOM 3523 O PHE B 206 -20.340 1.427 42.209 1.00 48.35 O ANISOU 3523 O PHE B 206 6205 6318 5849 -324 1374 -967 O ATOM 3524 CB PHE B 206 -21.565 -1.234 41.711 1.00 45.00 C ANISOU 3524 CB PHE B 206 5464 6110 5523 -73 1219 -821 C ATOM 3525 CG PHE B 206 -22.629 -2.269 41.942 1.00 43.50 C ANISOU 3525 CG PHE B 206 5164 5946 5420 94 1170 -724 C ATOM 3526 CD1 PHE B 206 -23.226 -2.403 43.184 1.00 42.55 C ANISOU 3526 CD1 PHE B 206 5027 5797 5343 230 1204 -709 C ATOM 3527 CD2 PHE B 206 -23.033 -3.109 40.918 1.00 43.55 C ANISOU 3527 CD2 PHE B 206 5090 5999 5458 103 1096 -654 C ATOM 3528 CE1 PHE B 206 -24.206 -3.355 43.400 1.00 41.25 C ANISOU 3528 CE1 PHE B 206 4756 5650 5267 362 1178 -615 C ATOM 3529 CE2 PHE B 206 -24.012 -4.062 41.129 1.00 42.96 C ANISOU 3529 CE2 PHE B 206 4909 5939 5477 229 1051 -572 C ATOM 3530 CZ PHE B 206 -24.599 -4.184 42.372 1.00 41.41 C ANISOU 3530 CZ PHE B 206 4684 5712 5338 354 1099 -548 C ATOM 3531 N THR B 207 -20.738 1.697 40.012 1.00 36.91 N ANISOU 3531 N THR B 207 4837 4805 4382 -406 1354 -793 N ATOM 3532 CA THR B 207 -19.639 2.639 39.820 1.00 38.54 C ANISOU 3532 CA THR B 207 5154 4970 4521 -623 1435 -889 C ATOM 3533 C THR B 207 -20.068 4.090 40.039 1.00 41.30 C ANISOU 3533 C THR B 207 5737 5069 4885 -630 1511 -836 C ATOM 3534 O THR B 207 -19.376 4.853 40.713 1.00 42.23 O ANISOU 3534 O THR B 207 5938 5123 4983 -753 1578 -958 O ATOM 3535 CB THR B 207 -19.009 2.493 38.420 1.00 38.72 C ANISOU 3535 CB THR B 207 5175 5068 4469 -781 1445 -870 C ATOM 3536 OG1 THR B 207 -18.518 1.157 38.250 1.00 36.03 O ANISOU 3536 OG1 THR B 207 4625 4948 4117 -773 1390 -945 O ATOM 3537 CG2 THR B 207 -17.859 3.473 38.245 1.00 41.16 C ANISOU 3537 CG2 THR B 207 5586 5333 4720 -1028 1551 -965 C ATOM 3538 N VAL B 208 -21.210 4.466 39.474 1.00 45.74 N ANISOU 3538 N VAL B 208 6405 5488 5488 -494 1493 -660 N ATOM 3539 CA VAL B 208 -21.695 5.839 39.577 1.00 48.35 C ANISOU 3539 CA VAL B 208 6972 5556 5844 -465 1565 -589 C ATOM 3540 C VAL B 208 -22.876 5.964 40.536 1.00 47.87 C ANISOU 3540 C VAL B 208 6914 5393 5881 -218 1567 -537 C ATOM 3541 O VAL B 208 -23.430 4.962 40.988 1.00 45.91 O ANISOU 3541 O VAL B 208 6484 5279 5682 -73 1509 -527 O ATOM 3542 CB VAL B 208 -22.110 6.394 38.201 1.00 51.32 C ANISOU 3542 CB VAL B 208 7498 5814 6188 -479 1553 -410 C ATOM 3543 CG1 VAL B 208 -20.902 6.495 37.285 1.00 51.95 C ANISOU 3543 CG1 VAL B 208 7619 5963 6156 -743 1598 -463 C ATOM 3544 CG2 VAL B 208 -23.190 5.519 37.581 1.00 51.30 C ANISOU 3544 CG2 VAL B 208 7366 5903 6221 -292 1429 -263 C ATOM 3545 N GLY B 209 -23.253 7.202 40.843 1.00 57.95 N ANISOU 3545 N GLY B 209 8405 6423 7189 -172 1649 -506 N ATOM 3546 CA GLY B 209 -24.383 7.458 41.718 1.00 56.44 C ANISOU 3546 CA GLY B 209 8234 6118 7093 72 1680 -460 C ATOM 3547 C GLY B 209 -24.522 8.922 42.092 1.00 57.08 C ANISOU 3547 C GLY B 209 8588 5906 7194 87 1793 -471 C ATOM 3548 O GLY B 209 -23.727 9.758 41.666 1.00 60.06 O ANISOU 3548 O GLY B 209 9149 6157 7515 -111 1844 -508 O ATOM 3549 N LEU B 210 -25.537 9.233 42.892 1.00 47.65 N ANISOU 3549 N LEU B 210 7425 4595 6086 320 1847 -440 N ATOM 3550 CA LEU B 210 -25.777 10.606 43.324 1.00 48.43 C ANISOU 3550 CA LEU B 210 7794 4392 6215 373 1967 -460 C ATOM 3551 C LEU B 210 -24.919 10.991 44.525 1.00 47.28 C ANISOU 3551 C LEU B 210 7753 4211 5999 232 2055 -698 C ATOM 3552 O LEU B 210 -24.799 10.231 45.485 1.00 45.32 O ANISOU 3552 O LEU B 210 7359 4142 5717 261 2045 -813 O ATOM 3553 CB LEU B 210 -27.256 10.820 43.655 1.00 47.77 C ANISOU 3553 CB LEU B 210 7697 4193 6259 702 2003 -332 C ATOM 3554 CG LEU B 210 -28.223 10.923 42.475 1.00 49.42 C ANISOU 3554 CG LEU B 210 7880 4347 6552 864 1920 -88 C ATOM 3555 CD1 LEU B 210 -29.627 11.244 42.961 1.00 48.54 C ANISOU 3555 CD1 LEU B 210 7744 4114 6585 1194 1975 12 C ATOM 3556 CD2 LEU B 210 -27.743 11.971 41.484 1.00 51.95 C ANISOU 3556 CD2 LEU B 210 8463 4454 6823 730 1927 -12 C ATOM 3557 N GLN B 211 -24.323 12.177 44.460 1.00 63.00 N ANISOU 3557 N GLN B 211 10009 5967 7962 74 2136 -768 N ATOM 3558 CA GLN B 211 -23.548 12.716 45.572 1.00 62.31 C ANISOU 3558 CA GLN B 211 10054 5813 7809 -73 2213 -1006 C ATOM 3559 C GLN B 211 -23.796 14.212 45.731 1.00 63.56 C ANISOU 3559 C GLN B 211 10553 5589 8006 -53 2342 -1022 C ATOM 3560 O GLN B 211 -23.993 14.926 44.748 1.00 65.33 O ANISOU 3560 O GLN B 211 10938 5609 8275 -62 2363 -872 O ATOM 3561 CB GLN B 211 -22.053 12.454 45.378 1.00 62.10 C ANISOU 3561 CB GLN B 211 9960 5951 7684 -414 2164 -1155 C ATOM 3562 CG GLN B 211 -21.630 11.010 45.594 1.00 60.08 C ANISOU 3562 CG GLN B 211 9390 6059 7377 -431 2053 -1208 C ATOM 3563 CD GLN B 211 -20.125 10.835 45.555 1.00 60.31 C ANISOU 3563 CD GLN B 211 9342 6249 7322 -746 2013 -1381 C ATOM 3564 OE1 GLN B 211 -19.384 11.784 45.294 1.00 61.21 O ANISOU 3564 OE1 GLN B 211 9625 6212 7419 -981 2074 -1458 O ATOM 3565 NE2 GLN B 211 -19.663 9.618 45.819 1.00 59.37 N ANISOU 3565 NE2 GLN B 211 8961 6436 7160 -754 1916 -1441 N ATOM 3566 N ASN B 212 -23.785 14.680 46.974 1.00 57.87 N ANISOU 3566 N ASN B 212 9961 4766 7259 -20 2428 -1203 N ATOM 3567 CA ASN B 212 -23.978 16.095 47.258 1.00 59.22 C ANISOU 3567 CA ASN B 212 10478 4555 7465 -4 2562 -1255 C ATOM 3568 C ASN B 212 -22.648 16.776 47.565 1.00 60.44 C ANISOU 3568 C ASN B 212 10807 4623 7532 -366 2591 -1484 C ATOM 3569 O ASN B 212 -22.092 16.614 48.651 1.00 61.29 O ANISOU 3569 O ASN B 212 10894 4842 7551 -466 2585 -1712 O ATOM 3570 CB ASN B 212 -24.956 16.278 48.421 1.00 60.29 C ANISOU 3570 CB ASN B 212 10677 4599 7631 287 2661 -1315 C ATOM 3571 CG ASN B 212 -25.581 17.661 48.449 1.00 63.70 C ANISOU 3571 CG ASN B 212 11447 4608 8148 427 2806 -1287 C ATOM 3572 OD1 ASN B 212 -24.980 18.639 48.004 1.00 65.41 O ANISOU 3572 OD1 ASN B 212 11920 4568 8363 228 2849 -1319 O ATOM 3573 ND2 ASN B 212 -26.797 17.748 48.976 1.00 64.43 N ANISOU 3573 ND2 ASN B 212 11540 4619 8321 775 2892 -1224 N ATOM 3574 N LEU B 213 -22.143 17.537 46.599 1.00 66.05 N ANISOU 3574 N LEU B 213 11690 5139 8265 -569 2620 -1418 N ATOM 3575 CA LEU B 213 -20.851 18.198 46.738 1.00 66.99 C ANISOU 3575 CA LEU B 213 11956 5172 8323 -952 2654 -1622 C ATOM 3576 C LEU B 213 -21.031 19.682 47.043 1.00 70.51 C ANISOU 3576 C LEU B 213 12810 5164 8814 -973 2801 -1688 C ATOM 3577 O LEU B 213 -20.407 20.534 46.413 1.00 72.58 O ANISOU 3577 O LEU B 213 13283 5204 9091 -1230 2862 -1686 O ATOM 3578 CB LEU B 213 -20.031 18.025 45.459 1.00 66.49 C ANISOU 3578 CB LEU B 213 11806 5210 8245 -1218 2610 -1521 C ATOM 3579 CG LEU B 213 -19.986 16.610 44.877 1.00 64.74 C ANISOU 3579 CG LEU B 213 11218 5384 7996 -1160 2479 -1408 C ATOM 3580 CD1 LEU B 213 -19.165 16.578 43.597 1.00 66.54 C ANISOU 3580 CD1 LEU B 213 11409 5675 8199 -1422 2471 -1318 C ATOM 3581 CD2 LEU B 213 -19.440 15.621 45.894 1.00 62.76 C ANISOU 3581 CD2 LEU B 213 10700 5471 7675 -1196 2388 -1606 C ATOM 3582 N SER B 214 -21.883 19.983 48.016 1.00 91.33 N ANISOU 3582 N SER B 214 15569 7657 11474 -704 2872 -1749 N ATOM 3583 CA SER B 214 -22.217 21.366 48.339 1.00 94.71 C ANISOU 3583 CA SER B 214 16324 7712 11949 -652 2982 -1767 C ATOM 3584 C SER B 214 -21.160 22.042 49.206 1.00 96.88 C ANISOU 3584 C SER B 214 16695 7976 12137 -966 2972 -2023 C ATOM 3585 O SER B 214 -21.176 23.260 49.380 1.00101.37 O ANISOU 3585 O SER B 214 17517 8262 12736 -1024 3040 -2037 O ATOM 3586 CB SER B 214 -23.579 21.434 49.036 1.00 93.35 C ANISOU 3586 CB SER B 214 16147 7492 11828 -229 3027 -1698 C ATOM 3587 OG SER B 214 -24.600 20.891 48.217 1.00 92.08 O ANISOU 3587 OG SER B 214 15876 7342 11769 72 3024 -1448 O ATOM 3588 N GLY B 215 -20.240 21.248 49.744 1.00 96.44 N ANISOU 3588 N GLY B 215 16430 8237 11976 -1161 2876 -2222 N ATOM 3589 CA GLY B 215 -19.267 21.749 50.696 1.00 98.14 C ANISOU 3589 CA GLY B 215 16689 8497 12104 -1427 2832 -2472 C ATOM 3590 C GLY B 215 -19.673 21.324 52.092 1.00 97.62 C ANISOU 3590 C GLY B 215 16537 8607 11945 -1231 2784 -2611 C ATOM 3591 O GLY B 215 -18.841 21.188 52.988 1.00 97.74 O ANISOU 3591 O GLY B 215 16480 8807 11851 -1417 2689 -2826 O ATOM 3592 N ASP B 216 -20.974 21.121 52.267 1.00100.14 N ANISOU 3592 N ASP B 216 16859 8880 12309 -847 2846 -2473 N ATOM 3593 CA ASP B 216 -21.519 20.559 53.494 1.00 99.46 C ANISOU 3593 CA ASP B 216 16663 8991 12137 -622 2818 -2553 C ATOM 3594 C ASP B 216 -22.508 19.459 53.128 1.00 95.46 C ANISOU 3594 C ASP B 216 15944 8642 11682 -316 2829 -2358 C ATOM 3595 O ASP B 216 -22.961 18.702 53.987 1.00 93.52 O ANISOU 3595 O ASP B 216 15546 8616 11369 -131 2804 -2380 O ATOM 3596 CB ASP B 216 -22.200 21.641 54.335 1.00102.56 C ANISOU 3596 CB ASP B 216 17290 9143 12535 -453 2913 -2607 C ATOM 3597 CG ASP B 216 -23.307 22.354 53.584 1.00104.47 C ANISOU 3597 CG ASP B 216 17685 9073 12935 -200 3041 -2390 C ATOM 3598 OD1 ASP B 216 -23.187 22.513 52.351 1.00104.92 O ANISOU 3598 OD1 ASP B 216 17787 8993 13085 -280 3056 -2240 O ATOM 3599 OD2 ASP B 216 -24.299 22.755 54.228 1.00106.16 O ANISOU 3599 OD2 ASP B 216 17970 9191 13176 82 3123 -2366 O ATOM 3600 N GLY B 217 -22.834 19.382 51.841 1.00 64.76 N ANISOU 3600 N GLY B 217 12051 4641 7914 -272 2865 -2160 N ATOM 3601 CA GLY B 217 -23.711 18.350 51.318 1.00 61.97 C ANISOU 3601 CA GLY B 217 11487 4431 7627 -10 2863 -1968 C ATOM 3602 C GLY B 217 -25.137 18.434 51.827 1.00 62.54 C ANISOU 3602 C GLY B 217 11536 4451 7774 385 2938 -1839 C ATOM 3603 O GLY B 217 -25.754 17.413 52.129 1.00 60.50 O ANISOU 3603 O GLY B 217 11042 4431 7515 584 2917 -1770 O ATOM 3604 N THR B 218 -25.666 19.651 51.918 1.00 71.15 N ANISOU 3604 N THR B 218 12857 5242 8936 494 3027 -1803 N ATOM 3605 CA THR B 218 -27.002 19.859 52.472 1.00 72.32 C ANISOU 3605 CA THR B 218 12976 5343 9158 855 3105 -1703 C ATOM 3606 C THR B 218 -27.922 20.626 51.526 1.00 73.93 C ANISOU 3606 C THR B 218 13286 5272 9531 1071 3164 -1477 C ATOM 3607 O THR B 218 -29.087 20.864 51.843 1.00 75.19 O ANISOU 3607 O THR B 218 13399 5392 9778 1378 3225 -1378 O ATOM 3608 CB THR B 218 -26.941 20.622 53.809 1.00 75.08 C ANISOU 3608 CB THR B 218 13486 5626 9415 846 3160 -1904 C ATOM 3609 OG1 THR B 218 -26.457 21.951 53.583 1.00 78.16 O ANISOU 3609 OG1 THR B 218 14179 5694 9823 685 3204 -1976 O ATOM 3610 CG2 THR B 218 -26.021 19.913 54.789 1.00 73.89 C ANISOU 3610 CG2 THR B 218 13239 5754 9083 644 3074 -2119 C ATOM 3611 N HIS B 219 -27.397 21.011 50.368 1.00 68.52 N ANISOU 3611 N HIS B 219 12735 4412 8888 907 3140 -1391 N ATOM 3612 CA HIS B 219 -28.150 21.819 49.415 1.00 70.44 C ANISOU 3612 CA HIS B 219 13110 4385 9271 1091 3171 -1165 C ATOM 3613 C HIS B 219 -28.398 21.037 48.127 1.00 68.13 C ANISOU 3613 C HIS B 219 12661 4173 9052 1164 3092 -930 C ATOM 3614 O HIS B 219 -27.451 20.599 47.474 1.00 66.47 O ANISOU 3614 O HIS B 219 12456 4015 8783 897 3041 -950 O ATOM 3615 CB HIS B 219 -27.393 23.121 49.127 1.00 73.42 C ANISOU 3615 CB HIS B 219 13822 4446 9628 848 3211 -1227 C ATOM 3616 CG HIS B 219 -28.178 24.132 48.347 1.00 76.18 C ANISOU 3616 CG HIS B 219 14348 4497 10102 1050 3246 -1010 C ATOM 3617 ND1 HIS B 219 -27.869 25.477 48.357 1.00 79.56 N ANISOU 3617 ND1 HIS B 219 15089 4609 10531 897 3301 -1040 N ATOM 3618 CD2 HIS B 219 -29.246 24.001 47.525 1.00 76.33 C ANISOU 3618 CD2 HIS B 219 14258 4496 10247 1393 3220 -758 C ATOM 3619 CE1 HIS B 219 -28.718 26.128 47.584 1.00 81.65 C ANISOU 3619 CE1 HIS B 219 15448 4665 10911 1149 3310 -811 C ATOM 3620 NE2 HIS B 219 -29.563 25.255 47.064 1.00 79.77 N ANISOU 3620 NE2 HIS B 219 14949 4609 10750 1453 3253 -639 N ATOM 3621 N PRO B 220 -29.681 20.855 47.768 1.00102.26 N ANISOU 3621 N PRO B 220 16831 8521 13504 1519 3075 -711 N ATOM 3622 CA PRO B 220 -30.144 20.143 46.569 1.00100.59 C ANISOU 3622 CA PRO B 220 16456 8387 13375 1647 2978 -460 C ATOM 3623 C PRO B 220 -29.451 20.574 45.275 1.00101.01 C ANISOU 3623 C PRO B 220 16722 8252 13405 1434 2932 -343 C ATOM 3624 O PRO B 220 -29.373 19.783 44.335 1.00 99.22 O ANISOU 3624 O PRO B 220 16283 8265 13152 1364 2784 -194 O ATOM 3625 CB PRO B 220 -31.627 20.509 46.510 1.00103.32 C ANISOU 3625 CB PRO B 220 16713 8678 13868 2035 2975 -270 C ATOM 3626 CG PRO B 220 -32.011 20.676 47.933 1.00104.42 C ANISOU 3626 CG PRO B 220 16793 8891 13992 2136 3072 -446 C ATOM 3627 CD PRO B 220 -30.810 21.273 48.620 1.00104.65 C ANISOU 3627 CD PRO B 220 17066 8822 13874 1820 3141 -712 C ATOM 3628 N GLY B 221 -28.961 21.808 45.230 1.00 76.20 N ANISOU 3628 N GLY B 221 13889 4829 10234 1278 2992 -391 N ATOM 3629 CA GLY B 221 -28.285 22.316 44.051 1.00 77.53 C ANISOU 3629 CA GLY B 221 14273 4816 10367 1050 2965 -271 C ATOM 3630 C GLY B 221 -26.979 21.600 43.761 1.00 75.06 C ANISOU 3630 C GLY B 221 13874 4715 9928 649 2915 -390 C ATOM 3631 O GLY B 221 -26.532 21.547 42.615 1.00 75.85 O ANISOU 3631 O GLY B 221 13989 4850 9978 473 2842 -243 O ATOM 3632 N GLY B 222 -26.365 21.047 44.802 1.00 65.96 N ANISOU 3632 N GLY B 222 12579 3779 8704 502 2926 -648 N ATOM 3633 CA GLY B 222 -25.097 20.355 44.661 1.00 63.05 C ANISOU 3633 CA GLY B 222 12049 3694 8211 125 2849 -781 C ATOM 3634 C GLY B 222 -25.248 18.861 44.448 1.00 58.19 C ANISOU 3634 C GLY B 222 11020 3525 7564 183 2700 -711 C ATOM 3635 O GLY B 222 -24.264 18.123 44.464 1.00 55.66 O ANISOU 3635 O GLY B 222 10520 3477 7148 -80 2631 -828 O ATOM 3636 N LEU B 223 -26.484 18.414 44.248 1.00 58.33 N ANISOU 3636 N LEU B 223 10880 3613 7670 529 2650 -522 N ATOM 3637 CA LEU B 223 -26.759 16.999 44.022 1.00 54.33 C ANISOU 3637 CA LEU B 223 9992 3499 7151 601 2512 -448 C ATOM 3638 C LEU B 223 -26.444 16.603 42.583 1.00 53.40 C ANISOU 3638 C LEU B 223 9795 3503 6990 468 2390 -268 C ATOM 3639 O LEU B 223 -27.244 16.834 41.677 1.00 54.29 O ANISOU 3639 O LEU B 223 9944 3521 7161 651 2338 -34 O ATOM 3640 CB LEU B 223 -28.218 16.679 44.356 1.00 54.45 C ANISOU 3640 CB LEU B 223 9853 3547 7289 1000 2511 -324 C ATOM 3641 CG LEU B 223 -28.663 15.229 44.164 1.00 51.31 C ANISOU 3641 CG LEU B 223 9067 3526 6902 1088 2377 -240 C ATOM 3642 CD1 LEU B 223 -27.752 14.285 44.929 1.00 49.01 C ANISOU 3642 CD1 LEU B 223 8608 3513 6501 875 2354 -447 C ATOM 3643 CD2 LEU B 223 -30.110 15.050 44.597 1.00 51.99 C ANISOU 3643 CD2 LEU B 223 9007 3618 7129 1463 2407 -137 C ATOM 3644 N VAL B 224 -25.277 16.001 42.380 1.00 48.74 N ANISOU 3644 N VAL B 224 9095 3132 6292 157 2343 -382 N ATOM 3645 CA VAL B 224 -24.824 15.642 41.040 1.00 47.22 C ANISOU 3645 CA VAL B 224 8852 3057 6033 -4 2256 -245 C ATOM 3646 C VAL B 224 -24.654 14.136 40.864 1.00 42.96 C ANISOU 3646 C VAL B 224 7955 2919 5449 -31 2128 -260 C ATOM 3647 O VAL B 224 -24.613 13.386 41.838 1.00 41.31 O ANISOU 3647 O VAL B 224 7550 2901 5244 7 2113 -403 O ATOM 3648 CB VAL B 224 -23.491 16.333 40.696 1.00 48.93 C ANISOU 3648 CB VAL B 224 9268 3161 6164 -379 2336 -349 C ATOM 3649 CG1 VAL B 224 -23.658 17.838 40.728 1.00 53.55 C ANISOU 3649 CG1 VAL B 224 10240 3310 6796 -375 2468 -324 C ATOM 3650 CG2 VAL B 224 -22.399 15.891 41.659 1.00 47.71 C ANISOU 3650 CG2 VAL B 224 8968 3208 5951 -616 2349 -627 C ATOM 3651 N CYS B 225 -24.558 13.706 39.609 1.00 54.49 N ANISOU 3651 N CYS B 225 9353 4495 6856 -94 2039 -110 N ATOM 3652 CA CYS B 225 -24.327 12.303 39.284 1.00 54.01 C ANISOU 3652 CA CYS B 225 8986 4789 6747 -137 1923 -125 C ATOM 3653 C CYS B 225 -22.854 12.082 38.954 1.00 54.00 C ANISOU 3653 C CYS B 225 8957 4928 6633 -482 1949 -261 C ATOM 3654 O CYS B 225 -22.358 12.554 37.931 1.00 55.11 O ANISOU 3654 O CYS B 225 9245 4994 6702 -653 1978 -181 O ATOM 3655 CB CYS B 225 -25.207 11.873 38.110 1.00 55.68 C ANISOU 3655 CB CYS B 225 9126 5067 6963 26 1797 109 C ATOM 3656 SG CYS B 225 -25.067 10.128 37.672 1.00 56.16 S ANISOU 3656 SG CYS B 225 8832 5530 6978 -6 1654 84 S ATOM 3657 N THR B 226 -22.164 11.357 39.827 1.00 57.46 N ANISOU 3657 N THR B 226 9200 5577 7055 -576 1941 -462 N ATOM 3658 CA THR B 226 -20.718 11.194 39.732 1.00 57.96 C ANISOU 3658 CA THR B 226 9209 5778 7036 -892 1975 -625 C ATOM 3659 C THR B 226 -20.319 9.776 40.141 1.00 56.02 C ANISOU 3659 C THR B 226 8643 5872 6770 -886 1886 -740 C ATOM 3660 O THR B 226 -21.055 9.116 40.879 1.00 54.06 O ANISOU 3660 O THR B 226 8260 5706 6573 -668 1828 -739 O ATOM 3661 CB THR B 226 -20.005 12.229 40.638 1.00 57.07 C ANISOU 3661 CB THR B 226 9275 5483 6927 -1067 2086 -807 C ATOM 3662 OG1 THR B 226 -18.592 11.997 40.640 1.00 56.51 O ANISOU 3662 OG1 THR B 226 9093 5584 6792 -1375 2105 -983 O ATOM 3663 CG2 THR B 226 -20.528 12.139 42.062 1.00 55.48 C ANISOU 3663 CG2 THR B 226 9037 5268 6774 -882 2081 -919 C ATOM 3664 N PRO B 227 -19.170 9.288 39.638 1.00 61.49 N ANISOU 3664 N PRO B 227 9212 6757 7393 -1118 1884 -831 N ATOM 3665 CA PRO B 227 -18.635 8.002 40.101 1.00 58.23 C ANISOU 3665 CA PRO B 227 8510 6649 6967 -1119 1807 -960 C ATOM 3666 C PRO B 227 -18.447 7.983 41.615 1.00 55.46 C ANISOU 3666 C PRO B 227 8110 6326 6637 -1081 1802 -1132 C ATOM 3667 O PRO B 227 -17.746 8.834 42.163 1.00 55.90 O ANISOU 3667 O PRO B 227 8281 6282 6675 -1253 1867 -1271 O ATOM 3668 CB PRO B 227 -17.278 7.902 39.386 1.00 56.75 C ANISOU 3668 CB PRO B 227 8251 6602 6710 -1406 1850 -1052 C ATOM 3669 CG PRO B 227 -17.022 9.268 38.801 1.00 60.14 C ANISOU 3669 CG PRO B 227 8951 6780 7117 -1593 1969 -1001 C ATOM 3670 CD PRO B 227 -18.374 9.833 38.528 1.00 61.94 C ANISOU 3670 CD PRO B 227 9385 6767 7382 -1369 1958 -797 C ATOM 3671 N ILE B 228 -19.076 7.017 42.278 1.00 31.88 N ANISOU 3671 N ILE B 228 4962 3473 3677 -865 1725 -1122 N ATOM 3672 CA ILE B 228 -19.082 6.958 43.736 1.00 32.60 C ANISOU 3672 CA ILE B 228 5033 3588 3767 -786 1720 -1254 C ATOM 3673 C ILE B 228 -18.015 6.022 44.292 1.00 32.55 C ANISOU 3673 C ILE B 228 4805 3855 3707 -877 1648 -1417 C ATOM 3674 O ILE B 228 -17.930 5.820 45.503 1.00 33.12 O ANISOU 3674 O ILE B 228 4845 3990 3750 -812 1621 -1527 O ATOM 3675 CB ILE B 228 -20.453 6.509 44.271 1.00 31.72 C ANISOU 3675 CB ILE B 228 4895 3442 3716 -486 1701 -1136 C ATOM 3676 CG1 ILE B 228 -20.805 5.122 43.729 1.00 29.79 C ANISOU 3676 CG1 ILE B 228 4422 3400 3496 -376 1608 -1036 C ATOM 3677 CG2 ILE B 228 -21.524 7.523 43.902 1.00 32.25 C ANISOU 3677 CG2 ILE B 228 5171 3236 3849 -366 1769 -988 C ATOM 3678 CD1 ILE B 228 -22.148 4.604 44.195 1.00 29.11 C ANISOU 3678 CD1 ILE B 228 4279 3297 3486 -110 1594 -917 C ATOM 3679 N VAL B 229 -17.206 5.451 43.409 1.00 31.91 N ANISOU 3679 N VAL B 229 4578 3939 3606 -1017 1618 -1432 N ATOM 3680 CA VAL B 229 -16.147 4.543 43.831 1.00 32.05 C ANISOU 3680 CA VAL B 229 4368 4223 3589 -1087 1547 -1580 C ATOM 3681 C VAL B 229 -14.808 5.266 43.907 1.00 33.88 C ANISOU 3681 C VAL B 229 4599 4490 3784 -1374 1584 -1756 C ATOM 3682 O VAL B 229 -14.675 6.395 43.435 1.00 34.98 O ANISOU 3682 O VAL B 229 4920 4443 3927 -1542 1677 -1749 O ATOM 3683 CB VAL B 229 -16.019 3.342 42.878 1.00 30.84 C ANISOU 3683 CB VAL B 229 4019 4255 3444 -1043 1496 -1510 C ATOM 3684 CG1 VAL B 229 -17.342 2.598 42.783 1.00 29.25 C ANISOU 3684 CG1 VAL B 229 3805 4018 3289 -788 1452 -1344 C ATOM 3685 CG2 VAL B 229 -15.554 3.801 41.504 1.00 31.30 C ANISOU 3685 CG2 VAL B 229 4122 4286 3486 -1234 1565 -1469 C ATOM 3686 N ASP B 230 -13.818 4.610 44.505 1.00 73.42 N ANISOU 3686 N ASP B 230 9398 9735 8764 -1429 1507 -1911 N ATOM 3687 CA ASP B 230 -12.485 5.190 44.633 1.00 75.59 C ANISOU 3687 CA ASP B 230 9613 10089 9019 -1708 1523 -2097 C ATOM 3688 C ASP B 230 -11.750 5.210 43.296 1.00 76.62 C ANISOU 3688 C ASP B 230 9661 10284 9168 -1906 1600 -2077 C ATOM 3689 O ASP B 230 -12.252 4.698 42.297 1.00 76.12 O ANISOU 3689 O ASP B 230 9589 10220 9114 -1813 1624 -1928 O ATOM 3690 CB ASP B 230 -11.666 4.442 45.689 1.00 75.40 C ANISOU 3690 CB ASP B 230 9369 10323 8959 -1682 1395 -2262 C ATOM 3691 CG ASP B 230 -11.735 2.934 45.526 1.00 74.94 C ANISOU 3691 CG ASP B 230 9090 10476 8911 -1476 1311 -2196 C ATOM 3692 OD1 ASP B 230 -11.826 2.456 44.377 1.00 75.75 O ANISOU 3692 OD1 ASP B 230 9133 10601 9049 -1463 1355 -2091 O ATOM 3693 OD2 ASP B 230 -11.700 2.225 46.554 1.00 75.01 O ANISOU 3693 OD2 ASP B 230 8999 10619 8883 -1329 1201 -2249 O ATOM 3694 N THR B 231 -10.560 5.800 43.290 1.00101.81 N ANISOU 3694 N THR B 231 12788 13536 12358 -2188 1640 -2234 N ATOM 3695 CA THR B 231 -9.767 5.934 42.073 1.00104.06 C ANISOU 3695 CA THR B 231 12999 13883 12655 -2412 1748 -2230 C ATOM 3696 C THR B 231 -9.377 4.577 41.489 1.00103.27 C ANISOU 3696 C THR B 231 12624 14054 12558 -2308 1706 -2218 C ATOM 3697 O THR B 231 -9.439 4.372 40.275 1.00104.31 O ANISOU 3697 O THR B 231 12767 14187 12677 -2334 1791 -2113 O ATOM 3698 CB THR B 231 -8.492 6.765 42.329 1.00105.56 C ANISOU 3698 CB THR B 231 13128 14118 12862 -2750 1798 -2425 C ATOM 3699 OG1 THR B 231 -8.850 8.031 42.897 1.00106.33 O ANISOU 3699 OG1 THR B 231 13506 13937 12957 -2851 1839 -2452 O ATOM 3700 CG2 THR B 231 -7.728 6.994 41.036 1.00106.86 C ANISOU 3700 CG2 THR B 231 13238 14326 13038 -2997 1948 -2405 C ATOM 3701 N ALA B 232 -8.989 3.652 42.362 1.00 63.54 N ANISOU 3701 N ALA B 232 7366 9244 7534 -2179 1574 -2325 N ATOM 3702 CA ALA B 232 -8.515 2.334 41.946 1.00 62.91 C ANISOU 3702 CA ALA B 232 7019 9416 7469 -2066 1530 -2338 C ATOM 3703 C ALA B 232 -9.558 1.539 41.161 1.00 62.04 C ANISOU 3703 C ALA B 232 6981 9243 7350 -1846 1534 -2153 C ATOM 3704 O ALA B 232 -9.329 1.170 40.007 1.00 62.80 O ANISOU 3704 O ALA B 232 7022 9400 7438 -1890 1611 -2111 O ATOM 3705 CB ALA B 232 -8.041 1.538 43.155 1.00 64.22 C ANISOU 3705 CB ALA B 232 6971 9790 7638 -1931 1371 -2463 C ATOM 3706 N THR B 233 -10.700 1.276 41.789 1.00 34.72 N ANISOU 3706 N THR B 233 3639 5666 3888 -1618 1456 -2052 N ATOM 3707 CA THR B 233 -11.748 0.477 41.161 1.00 33.27 C ANISOU 3707 CA THR B 233 3502 5432 3710 -1413 1439 -1887 C ATOM 3708 C THR B 233 -12.372 1.195 39.965 1.00 33.20 C ANISOU 3708 C THR B 233 3697 5239 3678 -1495 1540 -1745 C ATOM 3709 O THR B 233 -12.886 0.555 39.044 1.00 32.59 O ANISOU 3709 O THR B 233 3622 5173 3589 -1407 1539 -1639 O ATOM 3710 CB THR B 233 -12.849 0.081 42.165 1.00 31.74 C ANISOU 3710 CB THR B 233 3368 5162 3531 -1163 1345 -1809 C ATOM 3711 OG1 THR B 233 -13.544 1.252 42.607 1.00 31.57 O ANISOU 3711 OG1 THR B 233 3575 4916 3504 -1178 1385 -1756 O ATOM 3712 CG2 THR B 233 -12.243 -0.632 43.365 1.00 32.05 C ANISOU 3712 CG2 THR B 233 3236 5378 3565 -1077 1241 -1933 C ATOM 3713 N LEU B 234 -12.327 2.524 39.982 1.00 54.63 N ANISOU 3713 N LEU B 234 6596 7780 6380 -1663 1620 -1744 N ATOM 3714 CA LEU B 234 -12.780 3.307 38.839 1.00 56.61 C ANISOU 3714 CA LEU B 234 7058 7852 6597 -1756 1719 -1605 C ATOM 3715 C LEU B 234 -11.851 3.054 37.661 1.00 57.35 C ANISOU 3715 C LEU B 234 7054 8090 6645 -1932 1810 -1638 C ATOM 3716 O LEU B 234 -12.302 2.874 36.528 1.00 56.41 O ANISOU 3716 O LEU B 234 7021 7938 6473 -1906 1843 -1510 O ATOM 3717 CB LEU B 234 -12.819 4.799 39.172 1.00 58.01 C ANISOU 3717 CB LEU B 234 7468 7795 6778 -1908 1797 -1608 C ATOM 3718 CG LEU B 234 -13.324 5.705 38.047 1.00 59.97 C ANISOU 3718 CG LEU B 234 7975 7824 6988 -1984 1896 -1439 C ATOM 3719 CD1 LEU B 234 -14.726 5.300 37.624 1.00 58.30 C ANISOU 3719 CD1 LEU B 234 7849 7526 6776 -1722 1821 -1244 C ATOM 3720 CD2 LEU B 234 -13.290 7.165 38.472 1.00 62.60 C ANISOU 3720 CD2 LEU B 234 8549 7898 7338 -2130 1979 -1454 C ATOM 3721 N LYS B 235 -10.550 3.038 37.937 1.00 37.72 N ANISOU 3721 N LYS B 235 4381 5777 4176 -2110 1849 -1815 N ATOM 3722 CA LYS B 235 -9.566 2.668 36.929 1.00 39.80 C ANISOU 3722 CA LYS B 235 4496 6217 4406 -2263 1951 -1873 C ATOM 3723 C LYS B 235 -9.834 1.251 36.440 1.00 38.76 C ANISOU 3723 C LYS B 235 4226 6239 4261 -2052 1888 -1840 C ATOM 3724 O LYS B 235 -9.681 0.957 35.259 1.00 39.73 O ANISOU 3724 O LYS B 235 4360 6414 4320 -2102 1973 -1797 O ATOM 3725 CB LYS B 235 -8.144 2.770 37.487 1.00 42.02 C ANISOU 3725 CB LYS B 235 4538 6690 4736 -2455 1980 -2084 C ATOM 3726 CG LYS B 235 -7.631 4.190 37.639 1.00 44.15 C ANISOU 3726 CG LYS B 235 4938 6823 5016 -2751 2084 -2138 C ATOM 3727 CD LYS B 235 -6.230 4.210 38.229 1.00 46.74 C ANISOU 3727 CD LYS B 235 4984 7371 5404 -2943 2085 -2362 C ATOM 3728 CE LYS B 235 -5.693 5.628 38.327 1.00 49.62 C ANISOU 3728 CE LYS B 235 5476 7590 5786 -3277 2197 -2428 C ATOM 3729 NZ LYS B 235 -4.339 5.672 38.945 1.00 52.47 N ANISOU 3729 NZ LYS B 235 5548 8176 6212 -3461 2167 -2653 N ATOM 3730 N VAL B 236 -10.246 0.380 37.357 1.00 46.50 N ANISOU 3730 N VAL B 236 5097 7280 5293 -1821 1744 -1860 N ATOM 3731 CA VAL B 236 -10.554 -1.005 37.012 1.00 43.80 C ANISOU 3731 CA VAL B 236 4639 7050 4952 -1615 1676 -1833 C ATOM 3732 C VAL B 236 -11.705 -1.108 36.009 1.00 42.54 C ANISOU 3732 C VAL B 236 4673 6751 4738 -1530 1675 -1657 C ATOM 3733 O VAL B 236 -11.569 -1.757 34.969 1.00 41.62 O ANISOU 3733 O VAL B 236 4526 6718 4569 -1527 1714 -1648 O ATOM 3734 CB VAL B 236 -10.876 -1.846 38.265 1.00 41.93 C ANISOU 3734 CB VAL B 236 4287 6866 4780 -1388 1527 -1864 C ATOM 3735 CG1 VAL B 236 -11.392 -3.218 37.870 1.00 39.19 C ANISOU 3735 CG1 VAL B 236 3875 6572 4444 -1180 1463 -1809 C ATOM 3736 CG2 VAL B 236 -9.645 -1.971 39.149 1.00 43.77 C ANISOU 3736 CG2 VAL B 236 4293 7289 5050 -1445 1497 -2044 C ATOM 3737 N VAL B 237 -12.828 -0.463 36.310 1.00 34.42 N ANISOU 3737 N VAL B 237 3843 5518 3719 -1458 1630 -1523 N ATOM 3738 CA VAL B 237 -13.990 -0.527 35.423 1.00 33.33 C ANISOU 3738 CA VAL B 237 3870 5257 3537 -1364 1600 -1350 C ATOM 3739 C VAL B 237 -13.770 0.220 34.104 1.00 34.84 C ANISOU 3739 C VAL B 237 4227 5391 3620 -1546 1715 -1280 C ATOM 3740 O VAL B 237 -14.235 -0.220 33.048 1.00 34.70 O ANISOU 3740 O VAL B 237 4277 5381 3525 -1504 1699 -1192 O ATOM 3741 CB VAL B 237 -15.286 -0.036 36.114 1.00 31.57 C ANISOU 3741 CB VAL B 237 3788 4839 3368 -1213 1522 -1220 C ATOM 3742 CG1 VAL B 237 -15.691 -0.995 37.222 1.00 30.22 C ANISOU 3742 CG1 VAL B 237 3471 4730 3282 -1011 1415 -1254 C ATOM 3743 CG2 VAL B 237 -15.114 1.372 36.659 1.00 32.26 C ANISOU 3743 CG2 VAL B 237 4025 4769 3465 -1335 1592 -1227 C ATOM 3744 N ILE B 238 -13.054 1.340 34.162 1.00 35.50 N ANISOU 3744 N ILE B 238 4388 5414 3688 -1757 1831 -1320 N ATOM 3745 CA ILE B 238 -12.747 2.102 32.955 1.00 37.49 C ANISOU 3745 CA ILE B 238 4812 5604 3828 -1952 1965 -1247 C ATOM 3746 C ILE B 238 -11.836 1.306 32.024 1.00 39.18 C ANISOU 3746 C ILE B 238 4885 6036 3967 -2043 2053 -1337 C ATOM 3747 O ILE B 238 -12.101 1.205 30.826 1.00 39.90 O ANISOU 3747 O ILE B 238 5106 6121 3934 -2066 2095 -1242 O ATOM 3748 CB ILE B 238 -12.114 3.470 33.280 1.00 39.32 C ANISOU 3748 CB ILE B 238 5159 5705 4074 -2186 2087 -1279 C ATOM 3749 CG1 ILE B 238 -13.163 4.407 33.880 1.00 38.02 C ANISOU 3749 CG1 ILE B 238 5220 5273 3955 -2091 2029 -1156 C ATOM 3750 CG2 ILE B 238 -11.524 4.098 32.029 1.00 42.12 C ANISOU 3750 CG2 ILE B 238 5656 6039 4311 -2422 2258 -1226 C ATOM 3751 CD1 ILE B 238 -12.642 5.790 34.192 1.00 39.97 C ANISOU 3751 CD1 ILE B 238 5626 5344 4219 -2318 2148 -1186 C ATOM 3752 N GLN B 239 -10.772 0.734 32.580 1.00 39.99 N ANISOU 3752 N GLN B 239 4722 6337 4137 -2082 2077 -1523 N ATOM 3753 CA GLN B 239 -9.870 -0.114 31.806 1.00 41.57 C ANISOU 3753 CA GLN B 239 4755 6744 4294 -2124 2150 -1624 C ATOM 3754 C GLN B 239 -10.596 -1.345 31.279 1.00 40.10 C ANISOU 3754 C GLN B 239 4557 6610 4069 -1908 2053 -1581 C ATOM 3755 O GLN B 239 -10.298 -1.826 30.188 1.00 40.95 O ANISOU 3755 O GLN B 239 4684 6778 4097 -1919 2087 -1577 O ATOM 3756 CB GLN B 239 -8.659 -0.535 32.641 1.00 42.00 C ANISOU 3756 CB GLN B 239 4529 6953 4476 -2123 2096 -1801 C ATOM 3757 CG GLN B 239 -7.668 0.584 32.907 1.00 44.14 C ANISOU 3757 CG GLN B 239 4779 7215 4776 -2380 2201 -1881 C ATOM 3758 CD GLN B 239 -6.610 0.190 33.918 1.00 44.58 C ANISOU 3758 CD GLN B 239 4552 7438 4947 -2362 2118 -2060 C ATOM 3759 OE1 GLN B 239 -5.938 1.043 34.495 1.00 46.07 O ANISOU 3759 OE1 GLN B 239 4696 7631 5177 -2550 2161 -2151 O ATOM 3760 NE2 GLN B 239 -6.459 -1.112 34.138 1.00 43.49 N ANISOU 3760 NE2 GLN B 239 4235 7433 4858 -2137 1992 -2108 N ATOM 3761 N LEU B 240 -11.545 -1.853 32.061 1.00 37.70 N ANISOU 3761 N LEU B 240 4237 6250 3839 -1698 1898 -1539 N ATOM 3762 CA LEU B 240 -12.388 -2.954 31.614 1.00 36.26 C ANISOU 3762 CA LEU B 240 4066 6077 3633 -1509 1790 -1486 C ATOM 3763 C LEU B 240 -13.140 -2.551 30.353 1.00 36.41 C ANISOU 3763 C LEU B 240 4332 5993 3509 -1553 1803 -1334 C ATOM 3764 O LEU B 240 -13.159 -3.286 29.363 1.00 37.05 O ANISOU 3764 O LEU B 240 4433 6155 3490 -1537 1816 -1348 O ATOM 3765 CB LEU B 240 -13.388 -3.349 32.700 1.00 33.73 C ANISOU 3765 CB LEU B 240 3718 5671 3429 -1299 1623 -1430 C ATOM 3766 CG LEU B 240 -14.483 -4.324 32.258 1.00 32.17 C ANISOU 3766 CG LEU B 240 3559 5439 3223 -1127 1502 -1348 C ATOM 3767 CD1 LEU B 240 -13.920 -5.725 32.066 1.00 32.70 C ANISOU 3767 CD1 LEU B 240 3454 5662 3308 -1046 1495 -1480 C ATOM 3768 CD2 LEU B 240 -15.642 -4.328 33.241 1.00 29.97 C ANISOU 3768 CD2 LEU B 240 3306 5031 3050 -965 1372 -1244 C ATOM 3769 N ASN B 241 -13.753 -1.372 30.397 1.00 54.47 N ANISOU 3769 N ASN B 241 6820 8099 5780 -1602 1796 -1191 N ATOM 3770 CA ASN B 241 -14.511 -0.864 29.259 1.00 56.05 C ANISOU 3770 CA ASN B 241 7270 8188 5839 -1627 1787 -1022 C ATOM 3771 C ASN B 241 -13.647 -0.626 28.023 1.00 56.71 C ANISOU 3771 C ASN B 241 7443 8354 5750 -1827 1958 -1044 C ATOM 3772 O ASN B 241 -14.013 -1.022 26.919 1.00 57.14 O ANISOU 3772 O ASN B 241 7611 8442 5658 -1808 1937 -985 O ATOM 3773 CB ASN B 241 -15.258 0.417 29.638 1.00 58.53 C ANISOU 3773 CB ASN B 241 7779 8275 6186 -1623 1758 -865 C ATOM 3774 CG ASN B 241 -16.079 0.971 28.491 1.00 61.74 C ANISOU 3774 CG ASN B 241 8449 8562 6448 -1622 1726 -669 C ATOM 3775 OD1 ASN B 241 -15.662 1.906 27.808 1.00 63.73 O ANISOU 3775 OD1 ASN B 241 8890 8740 6586 -1792 1853 -600 O ATOM 3776 ND2 ASN B 241 -17.253 0.391 28.269 1.00 63.16 N ANISOU 3776 ND2 ASN B 241 8644 8724 6631 -1435 1552 -572 N ATOM 3777 N THR B 242 -12.498 0.015 28.210 1.00 41.30 N ANISOU 3777 N THR B 242 5439 6441 3811 -2028 2129 -1133 N ATOM 3778 CA THR B 242 -11.620 0.336 27.089 1.00 44.48 C ANISOU 3778 CA THR B 242 5923 6920 4056 -2243 2330 -1150 C ATOM 3779 C THR B 242 -10.991 -0.913 26.474 1.00 44.87 C ANISOU 3779 C THR B 242 5802 7162 4087 -2176 2326 -1279 C ATOM 3780 O THR B 242 -10.791 -0.983 25.263 1.00 46.50 O ANISOU 3780 O THR B 242 6129 7399 4141 -2236 2395 -1242 O ATOM 3781 CB THR B 242 -10.503 1.315 27.498 1.00 46.37 C ANISOU 3781 CB THR B 242 6118 7131 4371 -2466 2474 -1215 C ATOM 3782 OG1 THR B 242 -9.638 0.689 28.454 1.00 45.70 O ANISOU 3782 OG1 THR B 242 5717 7184 4463 -2419 2422 -1404 O ATOM 3783 CG2 THR B 242 -11.095 2.578 28.103 1.00 46.03 C ANISOU 3783 CG2 THR B 242 6269 6853 4367 -2523 2468 -1094 C ATOM 3784 N PHE B 243 -10.681 -1.896 27.312 1.00 43.40 N ANISOU 3784 N PHE B 243 5350 7079 4062 -2032 2230 -1418 N ATOM 3785 CA PHE B 243 -10.079 -3.137 26.836 1.00 43.62 C ANISOU 3785 CA PHE B 243 5221 7245 4107 -1932 2204 -1532 C ATOM 3786 C PHE B 243 -11.091 -4.038 26.135 1.00 42.81 C ANISOU 3786 C PHE B 243 5229 7152 3886 -1796 2122 -1490 C ATOM 3787 O PHE B 243 -10.843 -4.517 25.030 1.00 44.16 O ANISOU 3787 O PHE B 243 5468 7378 3932 -1812 2172 -1507 O ATOM 3788 CB PHE B 243 -9.419 -3.899 27.988 1.00 42.55 C ANISOU 3788 CB PHE B 243 4797 7195 4175 -1809 2115 -1671 C ATOM 3789 CG PHE B 243 -8.022 -3.440 28.300 1.00 44.21 C ANISOU 3789 CG PHE B 243 4846 7479 4473 -1941 2197 -1775 C ATOM 3790 CD1 PHE B 243 -7.145 -3.102 27.283 1.00 46.66 C ANISOU 3790 CD1 PHE B 243 5184 7841 4705 -2093 2345 -1796 C ATOM 3791 CD2 PHE B 243 -7.586 -3.349 29.612 1.00 43.58 C ANISOU 3791 CD2 PHE B 243 4586 7429 4542 -1916 2126 -1855 C ATOM 3792 CE1 PHE B 243 -5.859 -2.682 27.568 1.00 48.46 C ANISOU 3792 CE1 PHE B 243 5247 8150 5017 -2223 2425 -1901 C ATOM 3793 CE2 PHE B 243 -6.302 -2.929 29.903 1.00 45.37 C ANISOU 3793 CE2 PHE B 243 4655 7745 4839 -2048 2189 -1965 C ATOM 3794 CZ PHE B 243 -5.437 -2.595 28.880 1.00 47.83 C ANISOU 3794 CZ PHE B 243 4980 8108 5086 -2204 2340 -1989 C ATOM 3795 N MET B 244 -12.234 -4.260 26.777 1.00 40.84 N ANISOU 3795 N MET B 244 5000 6851 3668 -1669 2001 -1444 N ATOM 3796 CA MET B 244 -13.208 -5.228 26.283 1.00 39.74 C ANISOU 3796 CA MET B 244 4924 6710 3464 -1524 1870 -1421 C ATOM 3797 C MET B 244 -14.170 -4.678 25.231 1.00 39.84 C ANISOU 3797 C MET B 244 5219 6619 3298 -1557 1804 -1244 C ATOM 3798 O MET B 244 -14.668 -5.429 24.392 1.00 40.01 O ANISOU 3798 O MET B 244 5321 6675 3205 -1500 1728 -1249 O ATOM 3799 CB MET B 244 -13.986 -5.844 27.448 1.00 36.90 C ANISOU 3799 CB MET B 244 4437 6286 3297 -1328 1686 -1412 C ATOM 3800 CG MET B 244 -13.112 -6.649 28.392 1.00 37.04 C ANISOU 3800 CG MET B 244 4190 6418 3464 -1253 1718 -1582 C ATOM 3801 SD MET B 244 -12.272 -7.997 27.539 1.00 38.18 S ANISOU 3801 SD MET B 244 4247 6663 3596 -1188 1733 -1714 S ATOM 3802 CE MET B 244 -10.774 -8.127 28.510 1.00 38.61 C ANISOU 3802 CE MET B 244 4048 6783 3839 -1170 1754 -1814 C ATOM 3803 N SER B 245 -14.431 -3.376 25.269 1.00 63.91 N ANISOU 3803 N SER B 245 8429 9537 6319 -1645 1825 -1091 N ATOM 3804 CA SER B 245 -15.375 -2.777 24.329 1.00 67.58 C ANISOU 3804 CA SER B 245 9168 9894 6618 -1652 1744 -899 C ATOM 3805 C SER B 245 -14.697 -2.064 23.162 1.00 68.99 C ANISOU 3805 C SER B 245 9552 10102 6560 -1851 1928 -856 C ATOM 3806 O SER B 245 -15.360 -1.672 22.202 1.00 71.38 O ANISOU 3806 O SER B 245 10099 10352 6673 -1857 1866 -708 O ATOM 3807 CB SER B 245 -16.326 -1.816 25.047 1.00 70.49 C ANISOU 3807 CB SER B 245 9622 10067 7097 -1581 1630 -726 C ATOM 3808 OG SER B 245 -17.117 -1.099 24.118 1.00 72.65 O ANISOU 3808 OG SER B 245 10165 10233 7206 -1592 1569 -527 O ATOM 3809 N PHE B 246 -13.380 -1.899 23.235 1.00 46.34 N ANISOU 3809 N PHE B 246 6583 7325 3698 -2015 2155 -979 N ATOM 3810 CA PHE B 246 -12.664 -1.174 22.190 1.00 49.59 C ANISOU 3810 CA PHE B 246 7173 7746 3922 -2212 2345 -929 C ATOM 3811 C PHE B 246 -11.436 -1.909 21.655 1.00 50.84 C ANISOU 3811 C PHE B 246 7160 8047 4113 -2233 2440 -1092 C ATOM 3812 O PHE B 246 -11.481 -2.480 20.568 1.00 52.05 O ANISOU 3812 O PHE B 246 7410 8268 4098 -2207 2442 -1102 O ATOM 3813 CB PHE B 246 -12.270 0.223 22.675 1.00 50.50 C ANISOU 3813 CB PHE B 246 7357 7720 4110 -2373 2461 -846 C ATOM 3814 CG PHE B 246 -11.790 1.131 21.580 1.00 53.51 C ANISOU 3814 CG PHE B 246 7971 8034 4328 -2546 2603 -731 C ATOM 3815 CD1 PHE B 246 -12.694 1.792 20.765 1.00 54.76 C ANISOU 3815 CD1 PHE B 246 8477 8067 4263 -2559 2569 -509 C ATOM 3816 CD2 PHE B 246 -10.436 1.326 21.367 1.00 55.34 C ANISOU 3816 CD2 PHE B 246 8076 8326 4624 -2688 2762 -837 C ATOM 3817 CE1 PHE B 246 -12.255 2.629 19.756 1.00 57.76 C ANISOU 3817 CE1 PHE B 246 9083 8374 4490 -2705 2696 -391 C ATOM 3818 CE2 PHE B 246 -9.992 2.161 20.361 1.00 58.35 C ANISOU 3818 CE2 PHE B 246 8671 8644 4855 -2852 2907 -732 C ATOM 3819 CZ PHE B 246 -10.902 2.813 19.554 1.00 59.55 C ANISOU 3819 CZ PHE B 246 9179 8661 4787 -2858 2876 -506 C ATOM 3820 N LEU B 247 -10.347 -1.881 22.419 1.00 50.14 N ANISOU 3820 N LEU B 247 6821 8002 4229 -2278 2514 -1219 N ATOM 3821 CA LEU B 247 -9.059 -2.411 21.967 1.00 51.73 C ANISOU 3821 CA LEU B 247 6851 8333 4471 -2308 2622 -1362 C ATOM 3822 C LEU B 247 -9.123 -3.847 21.456 1.00 51.23 C ANISOU 3822 C LEU B 247 6705 8380 4382 -2136 2551 -1470 C ATOM 3823 O LEU B 247 -8.856 -4.100 20.288 1.00 53.15 O ANISOU 3823 O LEU B 247 7056 8677 4462 -2159 2629 -1479 O ATOM 3824 CB LEU B 247 -8.002 -2.295 23.069 1.00 51.55 C ANISOU 3824 CB LEU B 247 6547 8356 4684 -2352 2658 -1489 C ATOM 3825 CG LEU B 247 -7.239 -0.971 23.172 1.00 53.49 C ANISOU 3825 CG LEU B 247 6830 8539 4954 -2583 2801 -1455 C ATOM 3826 CD1 LEU B 247 -8.114 0.138 23.738 1.00 52.59 C ANISOU 3826 CD1 LEU B 247 6899 8247 4836 -2649 2764 -1317 C ATOM 3827 CD2 LEU B 247 -5.978 -1.143 24.005 1.00 53.94 C ANISOU 3827 CD2 LEU B 247 6574 8708 5214 -2615 2829 -1627 C ATOM 3828 N PHE B 248 -9.476 -4.776 22.337 1.00 79.82 N ANISOU 3828 N PHE B 248 10146 12022 8159 -1966 2410 -1553 N ATOM 3829 CA PHE B 248 -9.562 -6.195 21.990 1.00 79.90 C ANISOU 3829 CA PHE B 248 10076 12108 8175 -1801 2341 -1665 C ATOM 3830 C PHE B 248 -10.486 -6.494 20.789 1.00 80.62 C ANISOU 3830 C PHE B 248 10418 12189 8025 -1775 2294 -1610 C ATOM 3831 O PHE B 248 -10.026 -7.047 19.781 1.00 82.40 O ANISOU 3831 O PHE B 248 10665 12481 8161 -1743 2345 -1693 O ATOM 3832 CB PHE B 248 -9.947 -7.011 23.237 1.00 76.39 C ANISOU 3832 CB PHE B 248 9426 11658 7939 -1626 2191 -1736 C ATOM 3833 CG PHE B 248 -10.014 -8.496 23.014 1.00 76.18 C ANISOU 3833 CG PHE B 248 9328 11678 7939 -1457 2123 -1849 C ATOM 3834 CD1 PHE B 248 -8.857 -9.252 22.918 1.00 77.12 C ANISOU 3834 CD1 PHE B 248 9281 11878 8141 -1403 2198 -1976 C ATOM 3835 CD2 PHE B 248 -11.238 -9.143 22.946 1.00 75.85 C ANISOU 3835 CD2 PHE B 248 9387 11592 7841 -1355 1987 -1833 C ATOM 3836 CE1 PHE B 248 -8.920 -10.620 22.728 1.00 77.70 C ANISOU 3836 CE1 PHE B 248 9313 11968 8242 -1244 2147 -2078 C ATOM 3837 CE2 PHE B 248 -11.307 -10.509 22.756 1.00 75.54 C ANISOU 3837 CE2 PHE B 248 9299 11570 7831 -1215 1930 -1947 C ATOM 3838 CZ PHE B 248 -10.147 -11.249 22.647 1.00 76.42 C ANISOU 3838 CZ PHE B 248 9266 11742 8026 -1155 2015 -2065 C ATOM 3839 N PRO B 249 -11.779 -6.115 20.871 1.00 52.56 N ANISOU 3839 N PRO B 249 7060 8556 4354 -1787 2190 -1474 N ATOM 3840 CA PRO B 249 -12.685 -6.491 19.779 1.00 53.96 C ANISOU 3840 CA PRO B 249 7474 8745 4284 -1765 2111 -1434 C ATOM 3841 C PRO B 249 -12.354 -5.816 18.450 1.00 56.20 C ANISOU 3841 C PRO B 249 7989 9041 4325 -1898 2237 -1354 C ATOM 3842 O PRO B 249 -12.554 -6.430 17.407 1.00 57.50 O ANISOU 3842 O PRO B 249 8269 9259 4317 -1868 2222 -1402 O ATOM 3843 CB PRO B 249 -14.054 -6.018 20.281 1.00 52.49 C ANISOU 3843 CB PRO B 249 7424 8483 4038 -1745 1954 -1297 C ATOM 3844 CG PRO B 249 -13.744 -4.891 21.184 1.00 52.40 C ANISOU 3844 CG PRO B 249 7354 8392 4164 -1818 2028 -1213 C ATOM 3845 CD PRO B 249 -12.470 -5.289 21.879 1.00 50.69 C ANISOU 3845 CD PRO B 249 6841 8226 4191 -1799 2120 -1365 C ATOM 3846 N MET B 250 -11.862 -4.581 18.482 1.00 53.16 N ANISOU 3846 N MET B 250 7677 8597 3924 -2045 2362 -1237 N ATOM 3847 CA MET B 250 -11.537 -3.874 17.246 1.00 56.19 C ANISOU 3847 CA MET B 250 8300 8976 4075 -2177 2489 -1137 C ATOM 3848 C MET B 250 -10.192 -4.305 16.674 1.00 58.28 C ANISOU 3848 C MET B 250 8439 9346 4358 -2218 2675 -1275 C ATOM 3849 O MET B 250 -9.949 -4.169 15.477 1.00 60.95 O ANISOU 3849 O MET B 250 8965 9717 4477 -2282 2771 -1236 O ATOM 3850 CB MET B 250 -11.580 -2.358 17.444 1.00 56.96 C ANISOU 3850 CB MET B 250 8548 8944 4148 -2325 2562 -953 C ATOM 3851 CG MET B 250 -12.973 -1.815 17.707 1.00 55.78 C ANISOU 3851 CG MET B 250 8608 8679 3908 -2282 2392 -771 C ATOM 3852 SD MET B 250 -14.185 -2.365 16.486 1.00 56.78 S ANISOU 3852 SD MET B 250 9015 8848 3713 -2189 2199 -686 S ATOM 3853 CE MET B 250 -15.104 -3.585 17.427 1.00 53.49 C ANISOU 3853 CE MET B 250 8402 8484 3437 -2014 1975 -812 C ATOM 3854 N LEU B 251 -9.318 -4.818 17.533 1.00 57.28 N ANISOU 3854 N LEU B 251 8001 9277 4485 -2174 2721 -1430 N ATOM 3855 CA LEU B 251 -8.073 -5.408 17.071 1.00 59.26 C ANISOU 3855 CA LEU B 251 8103 9640 4771 -2181 2881 -1572 C ATOM 3856 C LEU B 251 -8.423 -6.687 16.323 1.00 59.75 C ANISOU 3856 C LEU B 251 8231 9765 4705 -2043 2828 -1667 C ATOM 3857 O LEU B 251 -7.953 -6.913 15.201 1.00 62.44 O ANISOU 3857 O LEU B 251 8678 10171 4877 -2078 2958 -1699 O ATOM 3858 CB LEU B 251 -7.138 -5.701 18.246 1.00 58.07 C ANISOU 3858 CB LEU B 251 7605 9539 4920 -2137 2896 -1706 C ATOM 3859 CG LEU B 251 -5.710 -6.145 17.922 1.00 60.38 C ANISOU 3859 CG LEU B 251 7708 9954 5281 -2156 3071 -1843 C ATOM 3860 CD1 LEU B 251 -5.101 -5.245 16.861 1.00 63.66 C ANISOU 3860 CD1 LEU B 251 8281 10384 5522 -2350 3278 -1769 C ATOM 3861 CD2 LEU B 251 -4.852 -6.141 19.180 1.00 59.43 C ANISOU 3861 CD2 LEU B 251 7270 9872 5437 -2143 3058 -1935 C ATOM 3862 N VAL B 252 -9.268 -7.510 16.942 1.00 57.31 N ANISOU 3862 N VAL B 252 7870 9431 4474 -1892 2638 -1716 N ATOM 3863 CA VAL B 252 -9.754 -8.724 16.288 1.00 57.64 C ANISOU 3863 CA VAL B 252 7994 9503 4403 -1767 2555 -1813 C ATOM 3864 C VAL B 252 -10.441 -8.398 14.959 1.00 59.60 C ANISOU 3864 C VAL B 252 8583 9745 4319 -1834 2527 -1709 C ATOM 3865 O VAL B 252 -10.151 -9.013 13.931 1.00 61.82 O ANISOU 3865 O VAL B 252 8972 10084 4435 -1811 2587 -1788 O ATOM 3866 CB VAL B 252 -10.722 -9.516 17.194 1.00 54.72 C ANISOU 3866 CB VAL B 252 7530 9085 4175 -1622 2343 -1861 C ATOM 3867 CG1 VAL B 252 -11.381 -10.645 16.419 1.00 55.34 C ANISOU 3867 CG1 VAL B 252 7746 9171 4110 -1526 2236 -1952 C ATOM 3868 CG2 VAL B 252 -9.989 -10.058 18.415 1.00 53.18 C ANISOU 3868 CG2 VAL B 252 7014 8904 4288 -1523 2359 -1971 C ATOM 3869 N ALA B 253 -11.333 -7.412 14.988 1.00 59.01 N ANISOU 3869 N ALA B 253 8686 9596 4138 -1907 2429 -1529 N ATOM 3870 CA ALA B 253 -12.095 -7.014 13.808 1.00 60.96 C ANISOU 3870 CA ALA B 253 9270 9832 4060 -1958 2360 -1397 C ATOM 3871 C ALA B 253 -11.206 -6.478 12.690 1.00 64.42 C ANISOU 3871 C ALA B 253 9848 10314 4313 -2073 2575 -1359 C ATOM 3872 O ALA B 253 -11.468 -6.721 11.514 1.00 66.75 O ANISOU 3872 O ALA B 253 10370 10651 4340 -2069 2557 -1348 O ATOM 3873 CB ALA B 253 -13.155 -5.986 14.182 1.00 59.83 C ANISOU 3873 CB ALA B 253 9278 9591 3864 -2003 2221 -1188 C ATOM 3874 N SER B 254 -10.160 -5.746 13.060 1.00 64.96 N ANISOU 3874 N SER B 254 9781 10379 4523 -2179 2773 -1344 N ATOM 3875 CA SER B 254 -9.219 -5.212 12.081 1.00 68.41 C ANISOU 3875 CA SER B 254 10320 10862 4813 -2305 3003 -1313 C ATOM 3876 C SER B 254 -8.424 -6.344 11.442 1.00 70.15 C ANISOU 3876 C SER B 254 10445 11204 5005 -2232 3122 -1507 C ATOM 3877 O SER B 254 -8.237 -6.372 10.221 1.00 73.24 O ANISOU 3877 O SER B 254 11036 11649 5141 -2269 3223 -1494 O ATOM 3878 CB SER B 254 -8.271 -4.204 12.732 1.00 68.64 C ANISOU 3878 CB SER B 254 10199 10854 5028 -2451 3174 -1270 C ATOM 3879 OG SER B 254 -7.494 -4.815 13.747 1.00 66.95 O ANISOU 3879 OG SER B 254 9630 10693 5115 -2391 3203 -1441 O ATOM 3880 N ILE B 255 -7.957 -7.271 12.276 1.00 68.45 N ANISOU 3880 N ILE B 255 9933 11028 5047 -2120 3111 -1682 N ATOM 3881 CA ILE B 255 -7.269 -8.464 11.790 1.00 69.93 C ANISOU 3881 CA ILE B 255 10023 11311 5235 -2014 3205 -1872 C ATOM 3882 C ILE B 255 -8.129 -9.193 10.765 1.00 71.05 C ANISOU 3882 C ILE B 255 10426 11462 5109 -1935 3092 -1902 C ATOM 3883 O ILE B 255 -7.703 -9.432 9.628 1.00 74.21 O ANISOU 3883 O ILE B 255 10970 11933 5295 -1950 3226 -1946 O ATOM 3884 CB ILE B 255 -6.955 -9.443 12.935 1.00 67.47 C ANISOU 3884 CB ILE B 255 9393 11006 5236 -1866 3138 -2028 C ATOM 3885 CG1 ILE B 255 -5.863 -8.878 13.842 1.00 67.16 C ANISOU 3885 CG1 ILE B 255 9072 10996 5450 -1935 3262 -2040 C ATOM 3886 CG2 ILE B 255 -6.528 -10.794 12.379 1.00 68.93 C ANISOU 3886 CG2 ILE B 255 9540 11256 5396 -1723 3190 -2214 C ATOM 3887 CD1 ILE B 255 -5.614 -9.721 15.072 1.00 64.71 C ANISOU 3887 CD1 ILE B 255 8463 10686 5439 -1787 3162 -2158 C ATOM 3888 N LEU B 256 -9.347 -9.532 11.176 1.00 68.58 N ANISOU 3888 N LEU B 256 10173 11081 4802 -1855 2841 -1883 N ATOM 3889 CA LEU B 256 -10.275 -10.249 10.313 1.00 69.51 C ANISOU 3889 CA LEU B 256 10527 11202 4683 -1786 2682 -1922 C ATOM 3890 C LEU B 256 -10.568 -9.478 9.031 1.00 72.53 C ANISOU 3890 C LEU B 256 11240 11609 4709 -1891 2706 -1778 C ATOM 3891 O LEU B 256 -10.694 -10.073 7.968 1.00 74.95 O ANISOU 3891 O LEU B 256 11732 11967 4780 -1855 2694 -1851 O ATOM 3892 CB LEU B 256 -11.576 -10.563 11.056 1.00 66.51 C ANISOU 3892 CB LEU B 256 10142 10745 4384 -1715 2398 -1900 C ATOM 3893 CG LEU B 256 -11.453 -11.539 12.227 1.00 63.77 C ANISOU 3893 CG LEU B 256 9506 10366 4358 -1589 2343 -2048 C ATOM 3894 CD1 LEU B 256 -12.817 -11.828 12.832 1.00 61.30 C ANISOU 3894 CD1 LEU B 256 9219 9984 4089 -1538 2068 -2019 C ATOM 3895 CD2 LEU B 256 -10.775 -12.826 11.785 1.00 65.28 C ANISOU 3895 CD2 LEU B 256 9636 10596 4574 -1479 2434 -2258 C ATOM 3896 N ASN B 257 -10.664 -8.156 9.134 1.00 75.73 N ANISOU 3896 N ASN B 257 11730 11970 5073 -2015 2739 -1574 N ATOM 3897 CA ASN B 257 -10.923 -7.319 7.966 1.00 78.79 C ANISOU 3897 CA ASN B 257 12444 12366 5127 -2110 2763 -1405 C ATOM 3898 C ASN B 257 -9.779 -7.329 6.955 1.00 82.52 C ANISOU 3898 C ASN B 257 12970 12929 5452 -2173 3041 -1461 C ATOM 3899 O ASN B 257 -10.012 -7.378 5.746 1.00 85.56 O ANISOU 3899 O ASN B 257 13626 13364 5518 -2183 3040 -1426 O ATOM 3900 CB ASN B 257 -11.267 -5.887 8.379 1.00 78.12 C ANISOU 3900 CB ASN B 257 12448 12180 5052 -2220 2738 -1162 C ATOM 3901 CG ASN B 257 -12.743 -5.708 8.679 1.00 76.30 C ANISOU 3901 CG ASN B 257 12355 11877 4757 -2161 2429 -1035 C ATOM 3902 OD1 ASN B 257 -13.524 -5.331 7.804 1.00 78.25 O ANISOU 3902 OD1 ASN B 257 12895 12119 4717 -2165 2293 -891 O ATOM 3903 ND2 ASN B 257 -13.134 -5.985 9.917 1.00 72.76 N ANISOU 3903 ND2 ASN B 257 11692 11381 4573 -2098 2308 -1083 N ATOM 3904 N THR B 258 -8.547 -7.281 7.452 1.00 79.36 N ANISOU 3904 N THR B 258 12310 12563 5280 -2213 3271 -1550 N ATOM 3905 CA THR B 258 -7.383 -7.394 6.580 1.00 82.95 C ANISOU 3905 CA THR B 258 12767 13120 5629 -2262 3550 -1628 C ATOM 3906 C THR B 258 -7.370 -8.761 5.905 1.00 84.28 C ANISOU 3906 C THR B 258 12971 13369 5682 -2119 3536 -1828 C ATOM 3907 O THR B 258 -7.204 -8.869 4.682 1.00 87.82 O ANISOU 3907 O THR B 258 13640 13890 5838 -2135 3638 -1839 O ATOM 3908 CB THR B 258 -6.069 -7.205 7.360 1.00 82.60 C ANISOU 3908 CB THR B 258 12388 13107 5888 -2319 3767 -1704 C ATOM 3909 OG1 THR B 258 -6.005 -5.871 7.879 1.00 82.02 O ANISOU 3909 OG1 THR B 258 12313 12953 5898 -2476 3803 -1527 O ATOM 3910 CG2 THR B 258 -4.870 -7.446 6.454 1.00 86.49 C ANISOU 3910 CG2 THR B 258 12858 13724 6282 -2352 4057 -1803 C ATOM 3911 N VAL B 259 -7.564 -9.802 6.711 1.00 81.59 N ANISOU 3911 N VAL B 259 12426 13006 5567 -1978 3410 -1985 N ATOM 3912 CA VAL B 259 -7.552 -11.173 6.213 1.00 82.65 C ANISOU 3912 CA VAL B 259 12581 13184 5637 -1831 3388 -2191 C ATOM 3913 C VAL B 259 -8.615 -11.420 5.139 1.00 84.34 C ANISOU 3913 C VAL B 259 13142 13400 5504 -1812 3210 -2170 C ATOM 3914 O VAL B 259 -8.344 -12.079 4.138 1.00 87.37 O ANISOU 3914 O VAL B 259 13663 13853 5681 -1763 3294 -2292 O ATOM 3915 CB VAL B 259 -7.715 -12.194 7.358 1.00 79.31 C ANISOU 3915 CB VAL B 259 11901 12703 5530 -1686 3253 -2335 C ATOM 3916 CG1 VAL B 259 -7.847 -13.599 6.803 1.00 80.56 C ANISOU 3916 CG1 VAL B 259 12131 12871 5607 -1538 3207 -2539 C ATOM 3917 CG2 VAL B 259 -6.533 -12.111 8.310 1.00 78.37 C ANISOU 3917 CG2 VAL B 259 11436 12611 5732 -1681 3429 -2384 C ATOM 3918 N ILE B 260 -9.815 -10.882 5.340 1.00110.06 N ANISOU 3918 N ILE B 260 16540 16588 8690 -1846 2958 -2017 N ATOM 3919 CA ILE B 260 -10.890 -11.057 4.365 1.00111.61 C ANISOU 3919 CA ILE B 260 17053 16796 8558 -1830 2746 -1983 C ATOM 3920 C ILE B 260 -10.703 -10.159 3.149 1.00115.33 C ANISOU 3920 C ILE B 260 17805 17331 8683 -1936 2864 -1830 C ATOM 3921 O ILE B 260 -11.169 -10.483 2.057 1.00118.18 O ANISOU 3921 O ILE B 260 18428 17747 8729 -1914 2771 -1853 O ATOM 3922 CB ILE B 260 -12.293 -10.833 4.980 1.00109.09 C ANISOU 3922 CB ILE B 260 16778 16393 8279 -1816 2409 -1869 C ATOM 3923 CG1 ILE B 260 -12.455 -9.399 5.488 1.00107.84 C ANISOU 3923 CG1 ILE B 260 16631 16178 8164 -1923 2414 -1614 C ATOM 3924 CG2 ILE B 260 -12.543 -11.819 6.099 1.00105.73 C ANISOU 3924 CG2 ILE B 260 16100 15905 8167 -1711 2287 -2025 C ATOM 3925 CD1 ILE B 260 -13.255 -8.501 4.577 1.00109.77 C ANISOU 3925 CD1 ILE B 260 17209 16425 8072 -1983 2278 -1397 C ATOM 3926 N ALA B 261 -10.032 -9.027 3.342 1.00 95.70 N ANISOU 3926 N ALA B 261 15271 14835 6256 -2057 3063 -1676 N ATOM 3927 CA ALA B 261 -9.693 -8.158 2.223 1.00 99.66 C ANISOU 3927 CA ALA B 261 16025 15387 6452 -2168 3225 -1530 C ATOM 3928 C ALA B 261 -8.768 -8.921 1.286 1.00103.18 C ANISOU 3928 C ALA B 261 16501 15954 6747 -2135 3455 -1712 C ATOM 3929 O ALA B 261 -8.976 -8.949 0.071 1.00106.75 O ANISOU 3929 O ALA B 261 17239 16477 6844 -2142 3457 -1690 O ATOM 3930 CB ALA B 261 -9.025 -6.886 2.715 1.00 99.41 C ANISOU 3930 CB ALA B 261 15904 15304 6563 -2314 3418 -1360 C ATOM 3931 N ARG B 262 -7.757 -9.558 1.869 1.00124.53 N ANISOU 3931 N ARG B 262 18908 18686 9721 -2088 3641 -1894 N ATOM 3932 CA ARG B 262 -6.812 -10.363 1.105 1.00128.13 C ANISOU 3932 CA ARG B 262 19352 19254 10079 -2033 3876 -2084 C ATOM 3933 C ARG B 262 -7.477 -11.600 0.500 1.00129.58 C ANISOU 3933 C ARG B 262 19701 19459 10075 -1893 3698 -2256 C ATOM 3934 O ARG B 262 -7.181 -11.986 -0.630 1.00134.78 O ANISOU 3934 O ARG B 262 20582 20208 10421 -1882 3792 -2318 O ATOM 3935 CB ARG B 262 -5.648 -10.784 2.001 1.00124.61 C ANISOU 3935 CB ARG B 262 18522 18822 10001 -1986 4066 -2231 C ATOM 3936 CG ARG B 262 -4.523 -11.507 1.284 1.00128.10 C ANISOU 3936 CG ARG B 262 18910 19383 10378 -1932 4355 -2408 C ATOM 3937 CD ARG B 262 -3.364 -11.797 2.230 1.00126.76 C ANISOU 3937 CD ARG B 262 18343 19234 10586 -1892 4528 -2516 C ATOM 3938 NE ARG B 262 -2.773 -10.575 2.774 1.00126.72 N ANISOU 3938 NE ARG B 262 18186 19225 10735 -2062 4656 -2357 N ATOM 3939 CZ ARG B 262 -3.043 -10.081 3.979 1.00123.24 C ANISOU 3939 CZ ARG B 262 17567 18692 10566 -2103 4513 -2270 C ATOM 3940 NH1 ARG B 262 -3.900 -10.703 4.778 1.00119.78 N ANISOU 3940 NH1 ARG B 262 17070 18165 10277 -1984 4243 -2315 N ATOM 3941 NH2 ARG B 262 -2.457 -8.963 4.386 1.00123.55 N ANISOU 3941 NH2 ARG B 262 17491 18726 10726 -2269 4643 -2143 N ATOM 3942 N ARG B 263 -8.378 -12.213 1.262 1.00131.70 N ANISOU 3942 N ARG B 263 19865 19640 10534 -1795 3438 -2335 N ATOM 3943 CA ARG B 263 -9.041 -13.445 0.848 1.00132.26 C ANISOU 3943 CA ARG B 263 20062 19702 10491 -1672 3239 -2515 C ATOM 3944 C ARG B 263 -9.997 -13.206 -0.316 1.00135.87 C ANISOU 3944 C ARG B 263 20887 20200 10537 -1709 3048 -2434 C ATOM 3945 O ARG B 263 -10.161 -14.065 -1.183 1.00139.49 O ANISOU 3945 O ARG B 263 21515 20706 10779 -1640 3004 -2597 O ATOM 3946 CB ARG B 263 -9.801 -14.064 2.024 1.00126.98 C ANISOU 3946 CB ARG B 263 19208 18917 10123 -1592 2986 -2571 C ATOM 3947 CG ARG B 263 -10.401 -15.430 1.732 1.00127.34 C ANISOU 3947 CG ARG B 263 19343 18928 10114 -1472 2794 -2783 C ATOM 3948 CD ARG B 263 -9.324 -16.498 1.639 1.00128.93 C ANISOU 3948 CD ARG B 263 19425 19149 10415 -1354 3019 -3021 C ATOM 3949 NE ARG B 263 -8.674 -16.727 2.927 1.00126.47 N ANISOU 3949 NE ARG B 263 18765 18778 10511 -1291 3112 -3062 N ATOM 3950 CZ ARG B 263 -7.652 -17.556 3.111 1.00128.12 C ANISOU 3950 CZ ARG B 263 18803 18998 10879 -1175 3318 -3235 C ATOM 3951 NH1 ARG B 263 -7.155 -18.236 2.087 1.00132.47 N ANISOU 3951 NH1 ARG B 263 19503 19615 11217 -1111 3469 -3391 N ATOM 3952 NH2 ARG B 263 -7.123 -17.703 4.318 1.00125.57 N ANISOU 3952 NH2 ARG B 263 18164 18628 10921 -1115 3368 -3250 N ATOM 3953 N LEU B 264 -10.630 -12.039 -0.328 1.00 98.59 N ANISOU 3953 N LEU B 264 16293 15456 5709 -1811 2924 -2182 N ATOM 3954 CA LEU B 264 -11.571 -11.696 -1.387 1.00101.32 C ANISOU 3954 CA LEU B 264 16984 15849 5665 -1839 2720 -2072 C ATOM 3955 C LEU B 264 -10.852 -11.125 -2.604 1.00106.04 C ANISOU 3955 C LEU B 264 17801 16556 5932 -1914 2975 -2000 C ATOM 3956 O LEU B 264 -11.246 -11.382 -3.742 1.00109.63 O ANISOU 3956 O LEU B 264 18529 17095 6030 -1895 2898 -2038 O ATOM 3957 CB LEU B 264 -12.624 -10.709 -0.878 1.00 99.08 C ANISOU 3957 CB LEU B 264 16756 15489 5401 -1891 2457 -1820 C ATOM 3958 CG LEU B 264 -13.677 -10.262 -1.896 1.00101.87 C ANISOU 3958 CG LEU B 264 17448 15891 5369 -1907 2201 -1670 C ATOM 3959 CD1 LEU B 264 -15.081 -10.444 -1.342 1.00 99.28 C ANISOU 3959 CD1 LEU B 264 17105 15498 5118 -1856 1790 -1622 C ATOM 3960 CD2 LEU B 264 -13.444 -8.816 -2.305 1.00103.88 C ANISOU 3960 CD2 LEU B 264 17872 16150 5447 -2016 2336 -1386 C ATOM 3961 N THR B 265 -9.795 -10.354 -2.362 1.00154.22 N ANISOU 3961 N THR B 265 23780 22661 12154 -2006 3278 -1901 N ATOM 3962 CA THR B 265 -9.032 -9.750 -3.451 1.00158.50 C ANISOU 3962 CA THR B 265 24511 23302 12409 -2096 3554 -1821 C ATOM 3963 C THR B 265 -8.327 -10.809 -4.298 1.00161.64 C ANISOU 3963 C THR B 265 24948 23816 12649 -2017 3743 -2072 C ATOM 3964 O THR B 265 -8.207 -10.664 -5.515 1.00166.52 O ANISOU 3964 O THR B 265 25844 24536 12889 -2045 3825 -2050 O ATOM 3965 CB THR B 265 -7.991 -8.741 -2.927 1.00155.65 C ANISOU 3965 CB THR B 265 23977 22913 12248 -2228 3848 -1680 C ATOM 3966 OG1 THR B 265 -8.623 -7.817 -2.033 1.00152.79 O ANISOU 3966 OG1 THR B 265 23576 22426 12049 -2289 3671 -1467 O ATOM 3967 CG2 THR B 265 -7.360 -7.972 -4.080 1.00160.25 C ANISOU 3967 CG2 THR B 265 24792 23585 12510 -2342 4111 -1559 C ATOM 3968 N VAL B 266 -7.871 -11.878 -3.651 1.00137.08 N ANISOU 3968 N VAL B 266 21575 20687 9821 -1910 3804 -2307 N ATOM 3969 CA VAL B 266 -7.155 -12.942 -4.347 1.00139.75 C ANISOU 3969 CA VAL B 266 21934 21118 10046 -1812 3991 -2558 C ATOM 3970 C VAL B 266 -8.094 -13.741 -5.253 1.00142.52 C ANISOU 3970 C VAL B 266 22582 21504 10065 -1736 3751 -2678 C ATOM 3971 O VAL B 266 -7.654 -14.403 -6.193 1.00146.56 O ANISOU 3971 O VAL B 266 23244 22116 10326 -1688 3903 -2833 O ATOM 3972 CB VAL B 266 -6.433 -13.889 -3.355 1.00134.65 C ANISOU 3972 CB VAL B 266 20934 20425 9800 -1693 4091 -2771 C ATOM 3973 CG1 VAL B 266 -7.426 -14.812 -2.668 1.00130.64 C ANISOU 3973 CG1 VAL B 266 20373 19803 9460 -1582 3757 -2886 C ATOM 3974 CG2 VAL B 266 -5.356 -14.696 -4.068 1.00138.61 C ANISOU 3974 CG2 VAL B 266 21428 21032 10206 -1606 4387 -2990 C ATOM 3975 N MET B 267 -9.391 -13.661 -4.974 1.00115.39 N ANISOU 3975 N MET B 267 19228 17991 6624 -1728 3374 -2608 N ATOM 3976 CA MET B 267 -10.390 -14.368 -5.768 1.00117.50 C ANISOU 3976 CA MET B 267 19759 18292 6595 -1672 3096 -2716 C ATOM 3977 C MET B 267 -10.810 -13.556 -6.989 1.00121.60 C ANISOU 3977 C MET B 267 20629 18917 6657 -1756 3045 -2536 C ATOM 3978 O MET B 267 -10.994 -14.105 -8.076 1.00125.60 O ANISOU 3978 O MET B 267 21379 19521 6824 -1721 3009 -2663 O ATOM 3979 CB MET B 267 -11.610 -14.707 -4.911 1.00113.55 C ANISOU 3979 CB MET B 267 19176 17675 6294 -1631 2702 -2724 C ATOM 3980 CG MET B 267 -11.371 -15.829 -3.915 1.00110.49 C ANISOU 3980 CG MET B 267 18516 17186 6281 -1523 2703 -2953 C ATOM 3981 SD MET B 267 -12.608 -15.869 -2.604 1.00104.93 S ANISOU 3981 SD MET B 267 17617 16329 5922 -1513 2340 -2883 S ATOM 3982 CE MET B 267 -14.122 -15.851 -3.559 1.00106.81 C ANISOU 3982 CE MET B 267 18166 16611 5807 -1557 1921 -2781 C ATOM 3983 N VAL B 268 -10.958 -12.249 -6.805 1.00129.76 N ANISOU 3983 N VAL B 268 21697 19927 7678 -1862 3038 -2242 N ATOM 3984 CA VAL B 268 -11.335 -11.360 -7.898 1.00133.69 C ANISOU 3984 CA VAL B 268 22530 20509 7756 -1938 2994 -2030 C ATOM 3985 C VAL B 268 -10.105 -10.859 -8.648 1.00137.64 C ANISOU 3985 C VAL B 268 23117 21106 8076 -2015 3414 -1984 C ATOM 3986 O VAL B 268 -9.769 -11.365 -9.718 1.00141.98 O ANISOU 3986 O VAL B 268 23849 21777 8319 -1988 3540 -2124 O ATOM 3987 CB VAL B 268 -12.146 -10.152 -7.394 1.00131.44 C ANISOU 3987 CB VAL B 268 22278 20138 7526 -2006 2784 -1712 C ATOM 3988 CG1 VAL B 268 -11.355 -9.381 -6.350 1.00128.21 C ANISOU 3988 CG1 VAL B 268 21601 19628 7484 -2080 3019 -1596 C ATOM 3989 CG2 VAL B 268 -12.526 -9.248 -8.557 1.00135.89 C ANISOU 3989 CG2 VAL B 268 23201 20781 7651 -2070 2745 -1477 C ATOM 3990 N ARG B 299 -22.884 -12.420 -6.831 1.00182.78 N ANISOU 3990 N ARG B 299 28921 26649 13877 -1643 -720 -1679 N ATOM 3991 CA ARG B 299 -22.596 -12.609 -5.415 1.00177.32 C ANISOU 3991 CA ARG B 299 27931 25800 13642 -1645 -597 -1720 C ATOM 3992 C ARG B 299 -21.316 -11.882 -5.013 1.00175.85 C ANISOU 3992 C ARG B 299 27717 25548 13552 -1677 -153 -1608 C ATOM 3993 O ARG B 299 -21.190 -11.405 -3.884 1.00173.43 O ANISOU 3993 O ARG B 299 27214 25127 13555 -1684 -76 -1491 O ATOM 3994 CB ARG B 299 -22.482 -14.100 -5.085 1.00176.14 C ANISOU 3994 CB ARG B 299 27627 25599 13701 -1636 -596 -2078 C ATOM 3995 CG ARG B 299 -22.206 -14.392 -3.619 1.00170.98 C ANISOU 3995 CG ARG B 299 26667 24788 13511 -1631 -479 -2131 C ATOM 3996 CD ARG B 299 -22.054 -15.880 -3.357 1.00170.38 C ANISOU 3996 CD ARG B 299 26465 24643 13627 -1613 -470 -2474 C ATOM 3997 NE ARG B 299 -21.724 -16.151 -1.961 1.00165.63 N ANISOU 3997 NE ARG B 299 25579 23895 13459 -1600 -340 -2513 N ATOM 3998 CZ ARG B 299 -21.557 -17.369 -1.455 1.00164.37 C ANISOU 3998 CZ ARG B 299 25274 23636 13544 -1575 -315 -2771 C ATOM 3999 NH1 ARG B 299 -21.691 -18.436 -2.230 1.00167.44 N ANISOU 3999 NH1 ARG B 299 25780 24043 13795 -1565 -408 -3022 N ATOM 4000 NH2 ARG B 299 -21.258 -17.520 -0.172 1.00160.18 N ANISOU 4000 NH2 ARG B 299 24489 22980 13391 -1558 -198 -2779 N ATOM 4001 N VAL B 300 -20.373 -11.799 -5.947 1.00140.00 N ANISOU 4001 N VAL B 300 23366 21084 8742 -1702 138 -1649 N ATOM 4002 CA VAL B 300 -19.086 -11.160 -5.695 1.00138.65 C ANISOU 4002 CA VAL B 300 23159 20867 8652 -1748 575 -1565 C ATOM 4003 C VAL B 300 -19.253 -9.688 -5.324 1.00137.81 C ANISOU 4003 C VAL B 300 23087 20703 8571 -1783 581 -1208 C ATOM 4004 O VAL B 300 -18.601 -9.193 -4.402 1.00135.20 O ANISOU 4004 O VAL B 300 22582 20269 8518 -1820 813 -1132 O ATOM 4005 CB VAL B 300 -18.156 -11.273 -6.919 1.00144.71 C ANISOU 4005 CB VAL B 300 24152 21751 9080 -1774 860 -1650 C ATOM 4006 CG1 VAL B 300 -16.784 -10.695 -6.603 1.00143.63 C ANISOU 4006 CG1 VAL B 300 23925 21571 9076 -1831 1319 -1592 C ATOM 4007 CG2 VAL B 300 -18.036 -12.724 -7.360 1.00146.51 C ANISOU 4007 CG2 VAL B 300 24385 22031 9251 -1727 838 -2003 C ATOM 4008 N GLN B 301 -20.134 -8.998 -6.041 1.00115.29 N ANISOU 4008 N GLN B 301 20459 17915 5430 -1766 316 -992 N ATOM 4009 CA GLN B 301 -20.399 -7.586 -5.786 1.00114.94 C ANISOU 4009 CA GLN B 301 20488 17802 5383 -1779 290 -636 C ATOM 4010 C GLN B 301 -21.001 -7.364 -4.401 1.00110.04 C ANISOU 4010 C GLN B 301 19611 17047 5152 -1748 124 -553 C ATOM 4011 O GLN B 301 -20.653 -6.405 -3.711 1.00108.01 O ANISOU 4011 O GLN B 301 19297 16676 5067 -1781 285 -358 O ATOM 4012 CB GLN B 301 -21.319 -7.002 -6.864 1.00119.38 C ANISOU 4012 CB GLN B 301 21340 18466 5554 -1736 -2 -425 C ATOM 4013 CG GLN B 301 -20.635 -6.718 -8.197 1.00124.57 C ANISOU 4013 CG GLN B 301 22300 19237 5794 -1781 218 -390 C ATOM 4014 CD GLN B 301 -20.283 -7.979 -8.965 1.00126.93 C ANISOU 4014 CD GLN B 301 22647 19666 5914 -1782 271 -726 C ATOM 4015 OE1 GLN B 301 -20.781 -9.064 -8.665 1.00125.34 O ANISOU 4015 OE1 GLN B 301 22293 19477 5853 -1741 63 -969 O ATOM 4016 NE2 GLN B 301 -19.419 -7.840 -9.964 1.00130.96 N ANISOU 4016 NE2 GLN B 301 23376 20266 6116 -1830 555 -741 N ATOM 4017 N ALA B 302 -21.901 -8.255 -3.998 1.00133.51 N ANISOU 4017 N ALA B 302 22432 20032 8266 -1693 -194 -708 N ATOM 4018 CA ALA B 302 -22.526 -8.169 -2.682 1.00129.56 C ANISOU 4018 CA ALA B 302 21678 19418 8132 -1662 -363 -652 C ATOM 4019 C ALA B 302 -21.515 -8.477 -1.581 1.00125.36 C ANISOU 4019 C ALA B 302 20898 18780 7954 -1707 -34 -794 C ATOM 4020 O ALA B 302 -21.540 -7.871 -0.507 1.00121.70 O ANISOU 4020 O ALA B 302 20280 18205 7755 -1712 0 -661 O ATOM 4021 CB ALA B 302 -23.714 -9.114 -2.596 1.00131.75 C ANISOU 4021 CB ALA B 302 21846 19744 8470 -1608 -775 -797 C ATOM 4022 N LEU B 303 -20.624 -9.424 -1.855 1.00158.75 N ANISOU 4022 N LEU B 303 25086 23047 12184 -1730 202 -1066 N ATOM 4023 CA LEU B 303 -19.588 -9.789 -0.899 1.00155.42 C ANISOU 4023 CA LEU B 303 24418 22544 12091 -1755 515 -1213 C ATOM 4024 C LEU B 303 -18.607 -8.642 -0.682 1.00155.14 C ANISOU 4024 C LEU B 303 24393 22460 12095 -1825 854 -1027 C ATOM 4025 O LEU B 303 -18.289 -8.300 0.457 1.00152.51 O ANISOU 4025 O LEU B 303 23847 22028 12073 -1845 970 -984 O ATOM 4026 CB LEU B 303 -18.850 -11.051 -1.351 1.00156.29 C ANISOU 4026 CB LEU B 303 24499 22706 12180 -1739 684 -1534 C ATOM 4027 CG LEU B 303 -19.262 -12.350 -0.652 1.00154.19 C ANISOU 4027 CG LEU B 303 24021 22385 12179 -1687 523 -1786 C ATOM 4028 CD1 LEU B 303 -20.762 -12.580 -0.766 1.00154.17 C ANISOU 4028 CD1 LEU B 303 24064 22401 12113 -1661 66 -1754 C ATOM 4029 CD2 LEU B 303 -18.491 -13.535 -1.215 1.00156.06 C ANISOU 4029 CD2 LEU B 303 24272 22657 12369 -1656 704 -2086 C ATOM 4030 N ARG B 304 -18.139 -8.042 -1.773 1.00105.02 N ANISOU 4030 N ARG B 304 18293 16180 5431 -1869 1010 -918 N ATOM 4031 CA ARG B 304 -17.196 -6.933 -1.674 1.00105.38 C ANISOU 4031 CA ARG B 304 18363 16172 5502 -1956 1335 -740 C ATOM 4032 C ARG B 304 -17.858 -5.676 -1.109 1.00104.02 C ANISOU 4032 C ARG B 304 18233 15888 5400 -1966 1193 -428 C ATOM 4033 O ARG B 304 -17.212 -4.888 -0.415 1.00102.35 O ANISOU 4033 O ARG B 304 17922 15577 5388 -2035 1418 -319 O ATOM 4034 CB ARG B 304 -16.532 -6.641 -3.024 1.00110.32 C ANISOU 4034 CB ARG B 304 19253 16898 5763 -2009 1546 -702 C ATOM 4035 CG ARG B 304 -17.475 -6.136 -4.101 1.00114.13 C ANISOU 4035 CG ARG B 304 20062 17445 5855 -1979 1284 -505 C ATOM 4036 CD ARG B 304 -16.718 -5.759 -5.364 1.00119.07 C ANISOU 4036 CD ARG B 304 20950 18165 6127 -2043 1537 -449 C ATOM 4037 NE ARG B 304 -17.607 -5.234 -6.396 1.00123.02 N ANISOU 4037 NE ARG B 304 21768 18732 6240 -2007 1282 -246 N ATOM 4038 CZ ARG B 304 -17.968 -3.959 -6.493 1.00124.17 C ANISOU 4038 CZ ARG B 304 22080 18804 6296 -2022 1220 85 C ATOM 4039 NH1 ARG B 304 -17.517 -3.072 -5.616 1.00121.63 N ANISOU 4039 NH1 ARG B 304 21643 18328 6243 -2085 1400 240 N ATOM 4040 NH2 ARG B 304 -18.781 -3.569 -7.465 1.00128.08 N ANISOU 4040 NH2 ARG B 304 22857 19375 6432 -1969 971 261 N ATOM 4041 N ARG B 305 -19.144 -5.491 -1.398 1.00118.34 N ANISOU 4041 N ARG B 305 20185 17717 7063 -1892 814 -288 N ATOM 4042 CA ARG B 305 -19.871 -4.359 -0.835 1.00117.45 C ANISOU 4042 CA ARG B 305 20107 17489 7029 -1867 647 9 C ATOM 4043 C ARG B 305 -20.029 -4.560 0.671 1.00112.40 C ANISOU 4043 C ARG B 305 19162 16745 6800 -1852 612 -54 C ATOM 4044 O ARG B 305 -19.981 -3.601 1.445 1.00110.95 O ANISOU 4044 O ARG B 305 18936 16432 6789 -1874 682 134 O ATOM 4045 CB ARG B 305 -21.226 -4.150 -1.530 1.00121.14 C ANISOU 4045 CB ARG B 305 20769 18014 7247 -1767 226 175 C ATOM 4046 CG ARG B 305 -22.393 -4.928 -0.943 1.00118.90 C ANISOU 4046 CG ARG B 305 20302 17747 7127 -1676 -161 79 C ATOM 4047 CD ARG B 305 -23.711 -4.542 -1.598 1.00121.62 C ANISOU 4047 CD ARG B 305 20807 18151 7253 -1573 -581 281 C ATOM 4048 NE ARG B 305 -23.683 -4.726 -3.046 1.00126.22 N ANISOU 4048 NE ARG B 305 21650 18878 7431 -1575 -616 263 N ATOM 4049 CZ ARG B 305 -24.737 -4.562 -3.839 1.00129.45 C ANISOU 4049 CZ ARG B 305 22206 19385 7594 -1488 -977 392 C ATOM 4050 NH1 ARG B 305 -25.909 -4.215 -3.324 1.00128.46 N ANISOU 4050 NH1 ARG B 305 21973 19227 7610 -1384 -1339 549 N ATOM 4051 NH2 ARG B 305 -24.621 -4.748 -5.146 1.00134.09 N ANISOU 4051 NH2 ARG B 305 23037 20113 7799 -1499 -981 361 N ATOM 4052 N GLY B 306 -20.188 -5.817 1.082 1.00 92.17 N ANISOU 4052 N GLY B 306 16397 14231 4393 -1816 517 -323 N ATOM 4053 CA GLY B 306 -20.231 -6.154 2.491 1.00 87.58 C ANISOU 4053 CA GLY B 306 15518 13566 4193 -1806 513 -416 C ATOM 4054 C GLY B 306 -18.885 -5.896 3.138 1.00 85.86 C ANISOU 4054 C GLY B 306 15143 13289 4189 -1888 919 -474 C ATOM 4055 O GLY B 306 -18.808 -5.443 4.282 1.00 82.75 O ANISOU 4055 O GLY B 306 14581 12796 4066 -1904 973 -407 O ATOM 4056 N VAL B 307 -17.820 -6.185 2.394 1.00 88.13 N ANISOU 4056 N VAL B 307 15480 13647 4357 -1939 1199 -601 N ATOM 4057 CA VAL B 307 -16.459 -5.925 2.850 1.00 87.26 C ANISOU 4057 CA VAL B 307 15211 13505 4439 -2022 1584 -659 C ATOM 4058 C VAL B 307 -16.250 -4.438 3.117 1.00 87.44 C ANISOU 4058 C VAL B 307 15315 13421 4487 -2107 1707 -386 C ATOM 4059 O VAL B 307 -15.768 -4.049 4.184 1.00 84.73 O ANISOU 4059 O VAL B 307 14765 12992 4436 -2152 1847 -378 O ATOM 4060 CB VAL B 307 -15.417 -6.403 1.816 1.00 90.56 C ANISOU 4060 CB VAL B 307 15703 14030 4674 -2057 1848 -811 C ATOM 4061 CG1 VAL B 307 -14.034 -5.871 2.161 1.00 90.50 C ANISOU 4061 CG1 VAL B 307 15553 13997 4834 -2160 2234 -811 C ATOM 4062 CG2 VAL B 307 -15.410 -7.920 1.727 1.00 90.09 C ANISOU 4062 CG2 VAL B 307 15524 14042 4663 -1972 1788 -1112 C ATOM 4063 N LEU B 308 -16.620 -3.610 2.145 1.00 97.69 N ANISOU 4063 N LEU B 308 16920 14718 5480 -2125 1646 -163 N ATOM 4064 CA LEU B 308 -16.463 -2.165 2.274 1.00 98.48 C ANISOU 4064 CA LEU B 308 17146 14691 5582 -2201 1757 113 C ATOM 4065 C LEU B 308 -17.332 -1.583 3.389 1.00 95.35 C ANISOU 4065 C LEU B 308 16673 14155 5400 -2149 1549 269 C ATOM 4066 O LEU B 308 -16.890 -0.703 4.130 1.00 94.10 O ANISOU 4066 O LEU B 308 16452 13866 5436 -2222 1714 378 O ATOM 4067 CB LEU B 308 -16.747 -1.460 0.944 1.00103.71 C ANISOU 4067 CB LEU B 308 18172 15377 5855 -2210 1714 328 C ATOM 4068 CG LEU B 308 -15.550 -1.238 0.013 1.00107.49 C ANISOU 4068 CG LEU B 308 18765 15919 6158 -2328 2065 300 C ATOM 4069 CD1 LEU B 308 -14.488 -0.395 0.705 1.00106.63 C ANISOU 4069 CD1 LEU B 308 18520 15695 6299 -2468 2393 348 C ATOM 4070 CD2 LEU B 308 -14.958 -2.555 -0.467 1.00108.30 C ANISOU 4070 CD2 LEU B 308 18763 16186 6202 -2309 2168 -7 C ATOM 4071 N VAL B 309 -18.564 -2.076 3.505 1.00 87.46 N ANISOU 4071 N VAL B 309 15678 13184 4369 -2026 1187 275 N ATOM 4072 CA VAL B 309 -19.452 -1.646 4.584 1.00 84.55 C ANISOU 4072 CA VAL B 309 15220 12697 4207 -1958 973 410 C ATOM 4073 C VAL B 309 -18.853 -1.972 5.951 1.00 80.42 C ANISOU 4073 C VAL B 309 14376 12126 4055 -2001 1143 244 C ATOM 4074 O VAL B 309 -18.791 -1.113 6.836 1.00 78.75 O ANISOU 4074 O VAL B 309 14114 11776 4032 -2028 1215 378 O ATOM 4075 CB VAL B 309 -20.851 -2.291 4.467 1.00 84.29 C ANISOU 4075 CB VAL B 309 15197 12732 4099 -1822 543 408 C ATOM 4076 CG1 VAL B 309 -21.613 -2.167 5.779 1.00 80.66 C ANISOU 4076 CG1 VAL B 309 14553 12176 3918 -1757 360 468 C ATOM 4077 CG2 VAL B 309 -21.637 -1.657 3.332 1.00 88.27 C ANISOU 4077 CG2 VAL B 309 16005 13255 4278 -1754 317 649 C ATOM 4078 N LEU B 310 -18.404 -3.214 6.110 1.00 99.70 N ANISOU 4078 N LEU B 310 16607 14675 6599 -1997 1207 -47 N ATOM 4079 CA LEU B 310 -17.807 -3.665 7.362 1.00 96.24 C ANISOU 4079 CA LEU B 310 15845 14213 6508 -2018 1356 -225 C ATOM 4080 C LEU B 310 -16.569 -2.849 7.720 1.00 97.05 C ANISOU 4080 C LEU B 310 15873 14249 6753 -2138 1705 -193 C ATOM 4081 O LEU B 310 -16.418 -2.402 8.859 1.00 95.84 O ANISOU 4081 O LEU B 310 15551 14004 6859 -2163 1769 -168 O ATOM 4082 CB LEU B 310 -17.444 -5.148 7.279 1.00 94.22 C ANISOU 4082 CB LEU B 310 15409 14073 6315 -1977 1379 -534 C ATOM 4083 CG LEU B 310 -16.852 -5.752 8.554 1.00 91.15 C ANISOU 4083 CG LEU B 310 14674 13670 6289 -1966 1503 -725 C ATOM 4084 CD1 LEU B 310 -17.900 -5.813 9.655 1.00 88.49 C ANISOU 4084 CD1 LEU B 310 14221 13273 6126 -1902 1256 -678 C ATOM 4085 CD2 LEU B 310 -16.270 -7.127 8.281 1.00 91.91 C ANISOU 4085 CD2 LEU B 310 14635 13858 6429 -1919 1578 -1009 C ATOM 4086 N ARG B 311 -15.690 -2.660 6.740 1.00 86.50 N ANISOU 4086 N ARG B 311 14658 12963 5245 -2218 1927 -200 N ATOM 4087 CA ARG B 311 -14.479 -1.868 6.927 1.00 86.71 C ANISOU 4087 CA ARG B 311 14620 12938 5390 -2355 2254 -172 C ATOM 4088 C ARG B 311 -14.822 -0.447 7.361 1.00 85.62 C ANISOU 4088 C ARG B 311 14615 12624 5293 -2412 2242 96 C ATOM 4089 O ARG B 311 -14.192 0.110 8.265 1.00 83.84 O ANISOU 4089 O ARG B 311 14227 12311 5319 -2497 2410 91 O ATOM 4090 CB ARG B 311 -13.662 -1.838 5.634 1.00 92.15 C ANISOU 4090 CB ARG B 311 15471 13714 5830 -2430 2464 -189 C ATOM 4091 CG ARG B 311 -12.378 -1.030 5.722 1.00 93.94 C ANISOU 4091 CG ARG B 311 15634 13898 6163 -2591 2801 -159 C ATOM 4092 CD ARG B 311 -11.680 -0.973 4.374 1.00 98.39 C ANISOU 4092 CD ARG B 311 16385 14554 6447 -2663 3000 -154 C ATOM 4093 NE ARG B 311 -11.395 -2.306 3.853 1.00 99.61 N ANISOU 4093 NE ARG B 311 16447 14871 6530 -2582 3021 -399 N ATOM 4094 CZ ARG B 311 -10.880 -2.544 2.651 1.00103.68 C ANISOU 4094 CZ ARG B 311 17118 15496 6782 -2609 3170 -441 C ATOM 4095 NH1 ARG B 311 -10.593 -1.535 1.839 1.00108.11 N ANISOU 4095 NH1 ARG B 311 17929 16028 7120 -2720 3312 -246 N ATOM 4096 NH2 ARG B 311 -10.655 -3.790 2.259 1.00103.80 N ANISOU 4096 NH2 ARG B 311 17048 15640 6753 -2521 3184 -676 N ATOM 4097 N ALA B 312 -15.831 0.128 6.713 1.00 93.69 N ANISOU 4097 N ALA B 312 15934 13589 6073 -2353 2031 328 N ATOM 4098 CA ALA B 312 -16.292 1.471 7.040 1.00 94.51 C ANISOU 4098 CA ALA B 312 16206 13501 6202 -2369 1987 607 C ATOM 4099 C ALA B 312 -16.786 1.550 8.481 1.00 90.76 C ANISOU 4099 C ALA B 312 15534 12925 6023 -2315 1878 602 C ATOM 4100 O ALA B 312 -16.463 2.493 9.204 1.00 89.72 O ANISOU 4100 O ALA B 312 15381 12637 6072 -2389 2008 698 O ATOM 4101 CB ALA B 312 -17.386 1.907 6.077 1.00 96.40 C ANISOU 4101 CB ALA B 312 16777 13716 6133 -2268 1728 851 C ATOM 4102 N MET B 313 -17.564 0.554 8.897 1.00 87.15 N ANISOU 4102 N MET B 313 14941 12557 5616 -2194 1641 483 N ATOM 4103 CA MET B 313 -18.091 0.519 10.259 1.00 83.54 C ANISOU 4103 CA MET B 313 14295 12024 5421 -2135 1531 472 C ATOM 4104 C MET B 313 -16.989 0.350 11.303 1.00 81.01 C ANISOU 4104 C MET B 313 13667 11704 5409 -2229 1793 274 C ATOM 4105 O MET B 313 -17.055 0.937 12.384 1.00 79.51 O ANISOU 4105 O MET B 313 13390 11390 5431 -2242 1823 332 O ATOM 4106 CB MET B 313 -19.143 -0.583 10.410 1.00 81.25 C ANISOU 4106 CB MET B 313 13918 11842 5112 -2000 1218 376 C ATOM 4107 CG MET B 313 -20.441 -0.303 9.669 1.00 83.66 C ANISOU 4107 CG MET B 313 14477 12131 5177 -1883 881 598 C ATOM 4108 SD MET B 313 -21.720 -1.528 10.007 1.00 83.25 S ANISOU 4108 SD MET B 313 14255 12187 5188 -1736 479 484 S ATOM 4109 CE MET B 313 -20.921 -3.021 9.428 1.00 82.35 C ANISOU 4109 CE MET B 313 14015 12268 5006 -1803 609 126 C ATOM 4110 N VAL B 314 -15.978 -0.450 10.977 1.00 69.52 N ANISOU 4110 N VAL B 314 12048 10386 3981 -2281 1970 44 N ATOM 4111 CA VAL B 314 -14.851 -0.656 11.883 1.00 67.76 C ANISOU 4111 CA VAL B 314 11512 10182 4051 -2354 2198 -144 C ATOM 4112 C VAL B 314 -14.031 0.622 12.044 1.00 69.15 C ANISOU 4112 C VAL B 314 11737 10231 4305 -2509 2428 -27 C ATOM 4113 O VAL B 314 -13.752 1.055 13.168 1.00 67.23 O ANISOU 4113 O VAL B 314 11324 9905 4316 -2551 2493 -50 O ATOM 4114 CB VAL B 314 -13.934 -1.800 11.404 1.00 68.38 C ANISOU 4114 CB VAL B 314 11417 10427 4137 -2351 2328 -396 C ATOM 4115 CG1 VAL B 314 -12.663 -1.852 12.239 1.00 67.26 C ANISOU 4115 CG1 VAL B 314 10960 10304 4290 -2424 2555 -556 C ATOM 4116 CG2 VAL B 314 -14.670 -3.128 11.465 1.00 66.73 C ANISOU 4116 CG2 VAL B 314 11122 10315 3919 -2206 2112 -547 C ATOM 4117 N ILE B 315 -13.654 1.223 10.918 1.00 72.69 N ANISOU 4117 N ILE B 315 12424 10663 4532 -2598 2546 91 N ATOM 4118 CA ILE B 315 -12.908 2.477 10.928 1.00 74.61 C ANISOU 4118 CA ILE B 315 12749 10772 4826 -2763 2763 211 C ATOM 4119 C ILE B 315 -13.672 3.562 11.684 1.00 73.65 C ANISOU 4119 C ILE B 315 12759 10431 4793 -2750 2660 422 C ATOM 4120 O ILE B 315 -13.102 4.271 12.518 1.00 73.12 O ANISOU 4120 O ILE B 315 12592 10246 4943 -2861 2800 417 O ATOM 4121 CB ILE B 315 -12.588 2.958 9.497 1.00 78.94 C ANISOU 4121 CB ILE B 315 13584 11330 5080 -2844 2881 340 C ATOM 4122 CG1 ILE B 315 -11.609 1.996 8.820 1.00 80.32 C ANISOU 4122 CG1 ILE B 315 13613 11703 5201 -2883 3057 122 C ATOM 4123 CG2 ILE B 315 -12.008 4.363 9.517 1.00 81.13 C ANISOU 4123 CG2 ILE B 315 14001 11425 5399 -3010 3068 507 C ATOM 4124 CD1 ILE B 315 -10.273 1.888 9.525 1.00 79.61 C ANISOU 4124 CD1 ILE B 315 13200 11654 5396 -3003 3295 -66 C ATOM 4125 N ALA B 316 -14.968 3.671 11.401 1.00 73.62 N ANISOU 4125 N ALA B 316 12977 10371 4626 -2608 2404 603 N ATOM 4126 CA ALA B 316 -15.827 4.636 12.081 1.00 72.88 C ANISOU 4126 CA ALA B 316 13022 10058 4611 -2551 2280 820 C ATOM 4127 C ALA B 316 -15.854 4.395 13.587 1.00 69.11 C ANISOU 4127 C ALA B 316 12263 9551 4444 -2529 2271 687 C ATOM 4128 O ALA B 316 -15.730 5.335 14.374 1.00 68.72 O ANISOU 4128 O ALA B 316 12224 9317 4571 -2588 2354 763 O ATOM 4129 CB ALA B 316 -17.237 4.591 11.511 1.00 73.60 C ANISOU 4129 CB ALA B 316 13355 10130 4479 -2369 1967 1021 C ATOM 4130 N PHE B 317 -16.012 3.134 13.981 1.00 94.01 N ANISOU 4130 N PHE B 317 15173 12882 7663 -2443 2172 484 N ATOM 4131 CA PHE B 317 -16.053 2.776 15.395 1.00 91.42 C ANISOU 4131 CA PHE B 317 14565 12556 7615 -2406 2156 346 C ATOM 4132 C PHE B 317 -14.762 3.172 16.103 1.00 89.79 C ANISOU 4132 C PHE B 317 14147 12319 7651 -2560 2410 210 C ATOM 4133 O PHE B 317 -14.795 3.803 17.159 1.00 89.20 O ANISOU 4133 O PHE B 317 14017 12105 7770 -2586 2440 240 O ATOM 4134 CB PHE B 317 -16.310 1.276 15.572 1.00 89.49 C ANISOU 4134 CB PHE B 317 14086 12516 7401 -2295 2029 128 C ATOM 4135 CG PHE B 317 -16.568 0.867 16.997 1.00 87.89 C ANISOU 4135 CG PHE B 317 13546 12277 7572 -2159 1913 13 C ATOM 4136 CD1 PHE B 317 -15.519 0.545 17.844 1.00 86.22 C ANISOU 4136 CD1 PHE B 317 13059 12134 7566 -2243 2101 -193 C ATOM 4137 CD2 PHE B 317 -17.861 0.805 17.491 1.00 89.44 C ANISOU 4137 CD2 PHE B 317 13696 12378 7907 -1946 1615 115 C ATOM 4138 CE1 PHE B 317 -15.753 0.169 19.153 1.00 85.42 C ANISOU 4138 CE1 PHE B 317 12674 12003 7778 -2115 1991 -288 C ATOM 4139 CE2 PHE B 317 -18.101 0.430 18.800 1.00 88.52 C ANISOU 4139 CE2 PHE B 317 13288 12230 8115 -1826 1529 17 C ATOM 4140 CZ PHE B 317 -17.046 0.112 19.631 1.00 86.30 C ANISOU 4140 CZ PHE B 317 12765 12012 8011 -1910 1715 -181 C ATOM 4141 N VAL B 318 -13.627 2.800 15.518 1.00 64.25 N ANISOU 4141 N VAL B 318 10795 9215 4403 -2661 2583 58 N ATOM 4142 CA VAL B 318 -12.332 3.115 16.114 1.00 64.41 C ANISOU 4142 CA VAL B 318 10593 9235 4647 -2811 2799 -81 C ATOM 4143 C VAL B 318 -12.113 4.623 16.228 1.00 66.33 C ANISOU 4143 C VAL B 318 11031 9256 4915 -2962 2917 90 C ATOM 4144 O VAL B 318 -11.849 5.140 17.318 1.00 65.16 O ANISOU 4144 O VAL B 318 10757 9008 4992 -3025 2963 46 O ATOM 4145 CB VAL B 318 -11.171 2.482 15.323 1.00 66.24 C ANISOU 4145 CB VAL B 318 10693 9643 4834 -2884 2964 -245 C ATOM 4146 CG1 VAL B 318 -9.833 2.969 15.860 1.00 67.04 C ANISOU 4146 CG1 VAL B 318 10585 9739 5147 -3055 3172 -360 C ATOM 4147 CG2 VAL B 318 -11.256 0.965 15.384 1.00 64.33 C ANISOU 4147 CG2 VAL B 318 10228 9591 4625 -2731 2863 -445 C ATOM 4148 N VAL B 319 -12.240 5.321 15.101 1.00 72.55 N ANISOU 4148 N VAL B 319 12137 9959 5470 -3014 2958 283 N ATOM 4149 CA VAL B 319 -12.024 6.766 15.052 1.00 74.95 C ANISOU 4149 CA VAL B 319 12662 10032 5782 -3157 3078 456 C ATOM 4150 C VAL B 319 -12.930 7.533 16.017 1.00 73.42 C ANISOU 4150 C VAL B 319 12575 9606 5714 -3085 2958 597 C ATOM 4151 O VAL B 319 -12.476 8.437 16.720 1.00 73.80 O ANISOU 4151 O VAL B 319 12609 9489 5940 -3211 3071 593 O ATOM 4152 CB VAL B 319 -12.208 7.314 13.618 1.00 78.74 C ANISOU 4152 CB VAL B 319 13496 10457 5962 -3184 3110 668 C ATOM 4153 CG1 VAL B 319 -12.214 8.836 13.617 1.00 81.20 C ANISOU 4153 CG1 VAL B 319 14075 10488 6288 -3293 3197 879 C ATOM 4154 CG2 VAL B 319 -11.116 6.781 12.703 1.00 80.89 C ANISOU 4154 CG2 VAL B 319 13676 10927 6130 -3295 3295 529 C ATOM 4155 N CYS B 320 -14.206 7.161 16.060 1.00 75.18 N ANISOU 4155 N CYS B 320 12901 9816 5850 -2883 2727 711 N ATOM 4156 CA CYS B 320 -15.167 7.859 16.911 1.00 73.72 C ANISOU 4156 CA CYS B 320 12837 9402 5773 -2779 2604 868 C ATOM 4157 C CYS B 320 -15.006 7.536 18.396 1.00 71.74 C ANISOU 4157 C CYS B 320 12286 9166 5805 -2776 2618 682 C ATOM 4158 O CYS B 320 -15.069 8.429 19.240 1.00 71.43 O ANISOU 4158 O CYS B 320 12300 8909 5931 -2809 2659 737 O ATOM 4159 CB CYS B 320 -16.602 7.566 16.464 1.00 73.67 C ANISOU 4159 CB CYS B 320 13026 9386 5580 -2551 2332 1061 C ATOM 4160 SG CYS B 320 -17.024 8.217 14.831 1.00 76.74 S ANISOU 4160 SG CYS B 320 13818 9701 5638 -2513 2261 1339 S ATOM 4161 N TRP B 321 -14.798 6.261 18.712 1.00 64.49 N ANISOU 4161 N TRP B 321 11063 8497 4944 -2727 2581 459 N ATOM 4162 CA TRP B 321 -14.752 5.826 20.106 1.00 61.32 C ANISOU 4162 CA TRP B 321 10330 8126 4846 -2645 2517 278 C ATOM 4163 C TRP B 321 -13.373 5.945 20.756 1.00 61.30 C ANISOU 4163 C TRP B 321 10100 8187 5003 -2860 2745 70 C ATOM 4164 O TRP B 321 -13.237 5.731 21.960 1.00 59.52 O ANISOU 4164 O TRP B 321 9634 7974 5005 -2826 2716 -71 O ATOM 4165 CB TRP B 321 -15.276 4.393 20.247 1.00 59.81 C ANISOU 4165 CB TRP B 321 9890 8134 4700 -2435 2311 145 C ATOM 4166 CG TRP B 321 -16.749 4.261 20.006 1.00 62.17 C ANISOU 4166 CG TRP B 321 10303 8357 4962 -2186 2018 316 C ATOM 4167 CD1 TRP B 321 -17.365 4.001 18.816 1.00 65.85 C ANISOU 4167 CD1 TRP B 321 10968 8878 5171 -2123 1898 439 C ATOM 4168 CD2 TRP B 321 -17.792 4.379 20.981 1.00 61.57 C ANISOU 4168 CD2 TRP B 321 10132 8149 5110 -1967 1808 376 C ATOM 4169 NE1 TRP B 321 -18.727 3.951 18.990 1.00 66.72 N ANISOU 4169 NE1 TRP B 321 11093 8908 5350 -1882 1611 573 N ATOM 4170 CE2 TRP B 321 -19.015 4.179 20.309 1.00 64.80 C ANISOU 4170 CE2 TRP B 321 10665 8548 5405 -1781 1564 539 C ATOM 4171 CE3 TRP B 321 -17.811 4.633 22.355 1.00 59.10 C ANISOU 4171 CE3 TRP B 321 9642 7736 5075 -1912 1805 304 C ATOM 4172 CZ2 TRP B 321 -20.244 4.227 20.965 1.00 65.56 C ANISOU 4172 CZ2 TRP B 321 10688 8542 5680 -1543 1333 633 C ATOM 4173 CZ3 TRP B 321 -19.032 4.680 23.005 1.00 59.75 C ANISOU 4173 CZ3 TRP B 321 9679 7708 5313 -1672 1590 398 C ATOM 4174 CH2 TRP B 321 -20.231 4.478 22.310 1.00 62.86 C ANISOU 4174 CH2 TRP B 321 10174 8098 5611 -1491 1364 561 C ATOM 4175 N LEU B 322 -12.356 6.280 19.967 1.00 61.47 N ANISOU 4175 N LEU B 322 10148 8242 4965 -3025 2902 39 N ATOM 4176 CA LEU B 322 -11.010 6.458 20.521 1.00 61.98 C ANISOU 4176 CA LEU B 322 9964 8363 5223 -3199 3059 -158 C ATOM 4177 C LEU B 322 -10.902 7.579 21.570 1.00 62.06 C ANISOU 4177 C LEU B 322 10010 8156 5416 -3308 3109 -144 C ATOM 4178 O LEU B 322 -10.458 7.323 22.690 1.00 60.36 O ANISOU 4178 O LEU B 322 9522 8008 5405 -3321 3099 -327 O ATOM 4179 CB LEU B 322 -9.957 6.623 19.413 1.00 65.16 C ANISOU 4179 CB LEU B 322 10400 8842 5517 -3361 3232 -182 C ATOM 4180 CG LEU B 322 -8.484 6.633 19.839 1.00 66.05 C ANISOU 4180 CG LEU B 322 10222 9065 5812 -3532 3384 -399 C ATOM 4181 CD1 LEU B 322 -7.633 5.908 18.808 1.00 67.85 C ANISOU 4181 CD1 LEU B 322 10346 9500 5935 -3566 3493 -491 C ATOM 4182 CD2 LEU B 322 -7.969 8.053 20.040 1.00 68.50 C ANISOU 4182 CD2 LEU B 322 10672 9167 6189 -3755 3523 -338 C ATOM 4183 N PRO B 323 -11.307 8.820 21.225 1.00 74.26 N ANISOU 4183 N PRO B 323 11897 9431 6886 -3377 3153 71 N ATOM 4184 CA PRO B 323 -11.111 9.888 22.214 1.00 74.66 C ANISOU 4184 CA PRO B 323 11991 9258 7118 -3494 3213 58 C ATOM 4185 C PRO B 323 -12.073 9.781 23.393 1.00 73.63 C ANISOU 4185 C PRO B 323 11829 9030 7115 -3333 3079 67 C ATOM 4186 O PRO B 323 -11.781 10.301 24.471 1.00 73.11 O ANISOU 4186 O PRO B 323 11683 8860 7236 -3415 3115 -36 O ATOM 4187 CB PRO B 323 -11.406 11.156 21.412 1.00 76.07 C ANISOU 4187 CB PRO B 323 12576 9158 7168 -3562 3278 306 C ATOM 4188 CG PRO B 323 -12.380 10.718 20.386 1.00 75.99 C ANISOU 4188 CG PRO B 323 12764 9183 6925 -3377 3155 503 C ATOM 4189 CD PRO B 323 -11.964 9.327 20.004 1.00 74.69 C ANISOU 4189 CD PRO B 323 12320 9358 6699 -3336 3134 329 C ATOM 4190 N TYR B 324 -13.205 9.116 23.181 1.00 66.51 N ANISOU 4190 N TYR B 324 10987 8166 6117 -3099 2913 182 N ATOM 4191 CA TYR B 324 -14.191 8.899 24.234 1.00 65.04 C ANISOU 4191 CA TYR B 324 10684 7906 6121 -2823 2679 170 C ATOM 4192 C TYR B 324 -13.581 8.132 25.400 1.00 63.20 C ANISOU 4192 C TYR B 324 10065 7859 6086 -2823 2664 -100 C ATOM 4193 O TYR B 324 -13.907 8.380 26.561 1.00 63.97 O ANISOU 4193 O TYR B 324 10082 7851 6370 -2726 2581 -155 O ATOM 4194 CB TYR B 324 -15.397 8.143 23.671 1.00 67.00 C ANISOU 4194 CB TYR B 324 10958 8223 6274 -2538 2443 294 C ATOM 4195 CG TYR B 324 -16.355 7.610 24.714 1.00 66.75 C ANISOU 4195 CG TYR B 324 10729 8190 6440 -2258 2216 251 C ATOM 4196 CD1 TYR B 324 -17.337 8.422 25.265 1.00 68.45 C ANISOU 4196 CD1 TYR B 324 11089 8154 6765 -2087 2107 398 C ATOM 4197 CD2 TYR B 324 -16.287 6.287 25.135 1.00 65.11 C ANISOU 4197 CD2 TYR B 324 10201 8226 6311 -2158 2122 70 C ATOM 4198 CE1 TYR B 324 -18.218 7.935 26.213 1.00 68.48 C ANISOU 4198 CE1 TYR B 324 10907 8166 6945 -1837 1926 361 C ATOM 4199 CE2 TYR B 324 -17.161 5.792 26.083 1.00 64.86 C ANISOU 4199 CE2 TYR B 324 10000 8190 6454 -1917 1935 43 C ATOM 4200 CZ TYR B 324 -18.124 6.619 26.618 1.00 66.60 C ANISOU 4200 CZ TYR B 324 10354 8175 6774 -1763 1843 187 C ATOM 4201 OH TYR B 324 -18.997 6.128 27.561 1.00 67.11 O ANISOU 4201 OH TYR B 324 10243 8245 7010 -1530 1683 160 O ATOM 4202 N HIS B 325 -12.687 7.202 25.081 1.00 53.90 N ANISOU 4202 N HIS B 325 8660 6961 4860 -2920 2748 -265 N ATOM 4203 CA HIS B 325 -12.026 6.389 26.092 1.00 52.08 C ANISOU 4203 CA HIS B 325 8058 6928 4799 -2910 2731 -515 C ATOM 4204 C HIS B 325 -10.811 7.099 26.681 1.00 54.36 C ANISOU 4204 C HIS B 325 8258 7205 5191 -3192 2920 -656 C ATOM 4205 O HIS B 325 -10.503 6.940 27.861 1.00 52.86 O ANISOU 4205 O HIS B 325 7847 7058 5177 -3171 2864 -816 O ATOM 4206 CB HIS B 325 -11.628 5.034 25.506 1.00 51.81 C ANISOU 4206 CB HIS B 325 7811 7190 4684 -2861 2731 -635 C ATOM 4207 CG HIS B 325 -12.796 4.163 25.164 1.00 49.25 C ANISOU 4207 CG HIS B 325 7511 6897 4303 -2585 2513 -550 C ATOM 4208 ND1 HIS B 325 -12.875 3.447 23.989 1.00 50.20 N ANISOU 4208 ND1 HIS B 325 7687 7155 4230 -2560 2515 -525 N ATOM 4209 CD2 HIS B 325 -13.935 3.894 25.845 1.00 46.02 C ANISOU 4209 CD2 HIS B 325 7076 6402 4006 -2335 2290 -490 C ATOM 4210 CE1 HIS B 325 -14.013 2.777 23.960 1.00 47.64 C ANISOU 4210 CE1 HIS B 325 7367 6826 3909 -2317 2288 -459 C ATOM 4211 NE2 HIS B 325 -14.673 3.029 25.076 1.00 45.08 N ANISOU 4211 NE2 HIS B 325 6983 6370 3776 -2179 2154 -431 N ATOM 4212 N VAL B 326 -10.126 7.883 25.853 1.00 67.90 N ANISOU 4212 N VAL B 326 10122 8844 6833 -3383 3052 -604 N ATOM 4213 CA VAL B 326 -8.993 8.679 26.310 1.00 68.60 C ANISOU 4213 CA VAL B 326 10134 8887 7044 -3617 3167 -733 C ATOM 4214 C VAL B 326 -9.463 9.708 27.334 1.00 69.88 C ANISOU 4214 C VAL B 326 10454 8781 7317 -3667 3163 -696 C ATOM 4215 O VAL B 326 -8.768 9.997 28.309 1.00 70.22 O ANISOU 4215 O VAL B 326 10334 8837 7510 -3791 3182 -872 O ATOM 4216 CB VAL B 326 -8.293 9.393 25.133 1.00 71.09 C ANISOU 4216 CB VAL B 326 10623 9143 7243 -3808 3323 -653 C ATOM 4217 CG1 VAL B 326 -7.163 10.280 25.634 1.00 73.44 C ANISOU 4217 CG1 VAL B 326 10850 9385 7668 -4063 3443 -786 C ATOM 4218 CG2 VAL B 326 -7.768 8.375 24.134 1.00 71.39 C ANISOU 4218 CG2 VAL B 326 10507 9442 7176 -3764 3347 -708 C ATOM 4219 N ARG B 327 -10.659 10.245 27.109 1.00 59.13 N ANISOU 4219 N ARG B 327 9416 7173 5878 -3558 3128 -468 N ATOM 4220 CA ARG B 327 -11.260 11.211 28.021 1.00 58.89 C ANISOU 4220 CA ARG B 327 9567 6843 5965 -3530 3091 -416 C ATOM 4221 C ARG B 327 -11.528 10.596 29.390 1.00 55.11 C ANISOU 4221 C ARG B 327 8822 6456 5661 -3332 2913 -584 C ATOM 4222 O ARG B 327 -11.160 11.162 30.419 1.00 55.44 O ANISOU 4222 O ARG B 327 8827 6401 5835 -3432 2933 -714 O ATOM 4223 CB ARG B 327 -12.567 11.747 27.441 1.00 58.76 C ANISOU 4223 CB ARG B 327 9902 6567 5859 -3319 2997 -135 C ATOM 4224 CG ARG B 327 -13.282 12.721 28.355 1.00 58.30 C ANISOU 4224 CG ARG B 327 10024 6189 5938 -3209 2931 -82 C ATOM 4225 CD ARG B 327 -14.642 13.096 27.803 1.00 58.14 C ANISOU 4225 CD ARG B 327 10295 5951 5846 -2944 2810 194 C ATOM 4226 NE ARG B 327 -15.495 11.929 27.605 1.00 54.66 N ANISOU 4226 NE ARG B 327 9680 5717 5371 -2647 2602 234 N ATOM 4227 CZ ARG B 327 -16.216 11.361 28.566 1.00 51.00 C ANISOU 4227 CZ ARG B 327 9021 5307 5051 -2395 2431 162 C ATOM 4228 NH1 ARG B 327 -16.184 11.850 29.797 1.00 50.47 N ANISOU 4228 NH1 ARG B 327 8917 5109 5149 -2389 2443 43 N ATOM 4229 NH2 ARG B 327 -16.967 10.302 28.297 1.00 49.22 N ANISOU 4229 NH2 ARG B 327 8645 5262 4795 -2159 2254 204 N ATOM 4230 N ARG B 328 -12.178 9.436 29.392 1.00 52.80 N ANISOU 4230 N ARG B 328 8360 6345 5358 -3058 2742 -581 N ATOM 4231 CA ARG B 328 -12.492 8.730 30.628 1.00 49.36 C ANISOU 4231 CA ARG B 328 7677 6012 5067 -2855 2578 -720 C ATOM 4232 C ARG B 328 -11.217 8.282 31.338 1.00 49.90 C ANISOU 4232 C ARG B 328 7430 6311 5219 -3026 2635 -979 C ATOM 4233 O ARG B 328 -11.176 8.194 32.565 1.00 48.34 O ANISOU 4233 O ARG B 328 7091 6132 5145 -2961 2548 -1113 O ATOM 4234 CB ARG B 328 -13.413 7.540 30.344 1.00 46.39 C ANISOU 4234 CB ARG B 328 7192 5780 4656 -2561 2403 -653 C ATOM 4235 CG ARG B 328 -14.775 7.952 29.801 1.00 45.67 C ANISOU 4235 CG ARG B 328 7363 5480 4509 -2358 2300 -408 C ATOM 4236 CD ARG B 328 -15.497 6.809 29.101 1.00 43.85 C ANISOU 4236 CD ARG B 328 7046 5417 4200 -2155 2156 -338 C ATOM 4237 NE ARG B 328 -16.000 5.799 30.028 1.00 40.57 N ANISOU 4237 NE ARG B 328 6384 5120 3913 -1932 1998 -429 N ATOM 4238 CZ ARG B 328 -15.443 4.606 30.209 1.00 39.61 C ANISOU 4238 CZ ARG B 328 5992 5248 3812 -1916 1971 -589 C ATOM 4239 NH1 ARG B 328 -14.359 4.265 29.524 1.00 41.56 N ANISOU 4239 NH1 ARG B 328 6158 5666 3966 -2099 2094 -688 N ATOM 4240 NH2 ARG B 328 -15.973 3.751 31.072 1.00 37.02 N ANISOU 4240 NH2 ARG B 328 5477 4990 3598 -1712 1833 -645 N ATOM 4241 N LEU B 329 -10.175 8.009 30.558 1.00 51.37 N ANISOU 4241 N LEU B 329 7505 6682 5332 -3237 2782 -1048 N ATOM 4242 CA LEU B 329 -8.866 7.691 31.115 1.00 52.69 C ANISOU 4242 CA LEU B 329 7359 7077 5585 -3421 2852 -1288 C ATOM 4243 C LEU B 329 -8.206 8.947 31.674 1.00 55.30 C ANISOU 4243 C LEU B 329 7778 7241 5994 -3699 2959 -1364 C ATOM 4244 O LEU B 329 -7.465 8.886 32.653 1.00 55.44 O ANISOU 4244 O LEU B 329 7567 7374 6125 -3773 2916 -1566 O ATOM 4245 CB LEU B 329 -7.967 7.048 30.056 1.00 54.02 C ANISOU 4245 CB LEU B 329 7379 7467 5680 -3472 2912 -1336 C ATOM 4246 CG LEU B 329 -8.248 5.582 29.718 1.00 51.86 C ANISOU 4246 CG LEU B 329 6922 7416 5368 -3229 2804 -1355 C ATOM 4247 CD1 LEU B 329 -7.354 5.110 28.583 1.00 53.49 C ANISOU 4247 CD1 LEU B 329 7040 7781 5503 -3280 2872 -1391 C ATOM 4248 CD2 LEU B 329 -8.062 4.708 30.947 1.00 49.81 C ANISOU 4248 CD2 LEU B 329 6352 7329 5245 -3083 2669 -1528 C ATOM 4249 N MET B 330 -8.483 10.084 31.045 1.00 63.81 N ANISOU 4249 N MET B 330 9200 8038 7007 -3820 3063 -1200 N ATOM 4250 CA MET B 330 -7.960 11.366 31.501 1.00 65.32 C ANISOU 4250 CA MET B 330 9532 8016 7270 -4052 3144 -1257 C ATOM 4251 C MET B 330 -8.698 11.822 32.756 1.00 65.62 C ANISOU 4251 C MET B 330 9672 7848 7415 -3974 3057 -1287 C ATOM 4252 O MET B 330 -8.147 12.535 33.594 1.00 66.30 O ANISOU 4252 O MET B 330 9751 7844 7595 -4164 3088 -1437 O ATOM 4253 CB MET B 330 -8.097 12.416 30.397 1.00 67.54 C ANISOU 4253 CB MET B 330 10175 8041 7446 -4160 3270 -1053 C ATOM 4254 CG MET B 330 -7.516 13.778 30.742 1.00 70.20 C ANISOU 4254 CG MET B 330 10678 8144 7850 -4399 3365 -1104 C ATOM 4255 SD MET B 330 -7.788 14.994 29.439 1.00 74.32 S ANISOU 4255 SD MET B 330 11647 8346 8244 -4488 3506 -836 S ATOM 4256 CE MET B 330 -6.997 14.184 28.051 1.00 75.63 C ANISOU 4256 CE MET B 330 11635 8825 8275 -4538 3583 -824 C ATOM 4257 N PHE B 331 -9.951 11.396 32.877 1.00 67.85 N ANISOU 4257 N PHE B 331 10036 8066 7680 -3622 2895 -1156 N ATOM 4258 CA PHE B 331 -10.795 11.772 34.006 1.00 68.57 C ANISOU 4258 CA PHE B 331 10228 7964 7861 -3428 2767 -1166 C ATOM 4259 C PHE B 331 -10.286 11.204 35.329 1.00 67.63 C ANISOU 4259 C PHE B 331 9809 8047 7840 -3405 2661 -1412 C ATOM 4260 O PHE B 331 -10.484 11.804 36.386 1.00 67.88 O ANISOU 4260 O PHE B 331 9926 7923 7943 -3392 2618 -1498 O ATOM 4261 CB PHE B 331 -12.236 11.313 33.757 1.00 68.94 C ANISOU 4261 CB PHE B 331 10374 7946 7874 -3056 2625 -968 C ATOM 4262 CG PHE B 331 -13.149 11.498 34.936 1.00 69.15 C ANISOU 4262 CG PHE B 331 10450 7827 7997 -2817 2502 -985 C ATOM 4263 CD1 PHE B 331 -13.718 12.732 35.201 1.00 70.47 C ANISOU 4263 CD1 PHE B 331 10935 7640 8201 -2806 2549 -901 C ATOM 4264 CD2 PHE B 331 -13.449 10.434 35.772 1.00 68.35 C ANISOU 4264 CD2 PHE B 331 10091 7934 7946 -2597 2352 -1083 C ATOM 4265 CE1 PHE B 331 -14.562 12.903 36.281 1.00 70.27 C ANISOU 4265 CE1 PHE B 331 10956 7484 8259 -2577 2459 -926 C ATOM 4266 CE2 PHE B 331 -14.290 10.601 36.855 1.00 69.13 C ANISOU 4266 CE2 PHE B 331 10241 7907 8119 -2382 2264 -1096 C ATOM 4267 CZ PHE B 331 -14.848 11.837 37.110 1.00 69.59 C ANISOU 4267 CZ PHE B 331 10604 7625 8211 -2370 2321 -1023 C ATOM 4268 N VAL B 332 -9.625 10.053 35.268 1.00 68.63 N ANISOU 4268 N VAL B 332 9600 8516 7961 -3391 2618 -1526 N ATOM 4269 CA VAL B 332 -9.236 9.341 36.482 1.00 68.54 C ANISOU 4269 CA VAL B 332 9298 8721 8025 -3309 2484 -1729 C ATOM 4270 C VAL B 332 -7.719 9.291 36.709 1.00 68.92 C ANISOU 4270 C VAL B 332 9075 8998 8116 -3602 2550 -1954 C ATOM 4271 O VAL B 332 -7.258 9.295 37.852 1.00 69.34 O ANISOU 4271 O VAL B 332 8980 9136 8233 -3638 2460 -2138 O ATOM 4272 CB VAL B 332 -9.838 7.910 36.506 1.00 67.00 C ANISOU 4272 CB VAL B 332 8911 8733 7815 -2983 2336 -1686 C ATOM 4273 CG1 VAL B 332 -9.274 7.063 35.373 1.00 65.93 C ANISOU 4273 CG1 VAL B 332 8606 8829 7618 -3031 2402 -1672 C ATOM 4274 CG2 VAL B 332 -9.605 7.243 37.853 1.00 66.18 C ANISOU 4274 CG2 VAL B 332 8570 8801 7776 -2858 2189 -1858 C ATOM 4275 N TYR B 333 -6.945 9.266 35.628 1.00 76.71 N ANISOU 4275 N TYR B 333 9995 10090 9061 -3814 2706 -1940 N ATOM 4276 CA TYR B 333 -5.495 9.113 35.741 1.00 76.97 C ANISOU 4276 CA TYR B 333 9735 10372 9137 -4003 2732 -2137 C ATOM 4277 C TYR B 333 -4.755 10.406 36.079 1.00 78.19 C ANISOU 4277 C TYR B 333 9996 10380 9331 -4279 2800 -2231 C ATOM 4278 O TYR B 333 -3.683 10.369 36.683 1.00 78.59 O ANISOU 4278 O TYR B 333 9800 10623 9437 -4375 2748 -2420 O ATOM 4279 CB TYR B 333 -4.911 8.475 34.478 1.00 75.27 C ANISOU 4279 CB TYR B 333 9407 10339 8853 -3974 2796 -2086 C ATOM 4280 CG TYR B 333 -4.848 6.967 34.538 1.00 73.55 C ANISOU 4280 CG TYR B 333 8893 10410 8643 -3724 2674 -2143 C ATOM 4281 CD1 TYR B 333 -5.913 6.188 34.106 1.00 72.55 C ANISOU 4281 CD1 TYR B 333 8837 10273 8456 -3490 2632 -2002 C ATOM 4282 CD2 TYR B 333 -3.724 6.322 35.036 1.00 72.71 C ANISOU 4282 CD2 TYR B 333 8447 10575 8604 -3707 2592 -2332 C ATOM 4283 CE1 TYR B 333 -5.857 4.808 34.164 1.00 71.53 C ANISOU 4283 CE1 TYR B 333 8463 10376 8340 -3251 2514 -2054 C ATOM 4284 CE2 TYR B 333 -3.658 4.945 35.098 1.00 71.48 C ANISOU 4284 CE2 TYR B 333 8052 10646 8462 -3457 2474 -2373 C ATOM 4285 CZ TYR B 333 -4.727 4.193 34.661 1.00 71.30 C ANISOU 4285 CZ TYR B 333 8120 10586 8385 -3233 2436 -2236 C ATOM 4286 OH TYR B 333 -4.663 2.821 34.723 1.00 70.59 O ANISOU 4286 OH TYR B 333 7818 10688 8315 -2981 2314 -2274 O ATOM 4287 N ILE B 334 -5.318 11.543 35.687 1.00 90.88 N ANISOU 4287 N ILE B 334 11974 11645 10909 -4388 2910 -2090 N ATOM 4288 CA ILE B 334 -4.706 12.830 36.001 1.00 92.55 C ANISOU 4288 CA ILE B 334 12327 11679 11158 -4638 2980 -2166 C ATOM 4289 C ILE B 334 -4.855 13.140 37.489 1.00 93.11 C ANISOU 4289 C ILE B 334 12390 11682 11306 -4636 2856 -2329 C ATOM 4290 O ILE B 334 -5.962 13.123 38.026 1.00 93.13 O ANISOU 4290 O ILE B 334 12564 11501 11318 -4484 2794 -2276 O ATOM 4291 CB ILE B 334 -5.314 13.972 35.165 1.00 91.89 C ANISOU 4291 CB ILE B 334 12674 11220 11019 -4721 3126 -1955 C ATOM 4292 CG1 ILE B 334 -5.145 13.686 33.672 1.00 92.35 C ANISOU 4292 CG1 ILE B 334 12762 11351 10974 -4719 3236 -1792 C ATOM 4293 CG2 ILE B 334 -4.669 15.300 35.528 1.00 95.67 C ANISOU 4293 CG2 ILE B 334 13297 11509 11544 -4975 3200 -2039 C ATOM 4294 CD1 ILE B 334 -3.705 13.531 33.237 1.00 94.64 C ANISOU 4294 CD1 ILE B 334 12783 11905 11270 -4890 3302 -1920 C ATOM 4295 N SER B 335 -3.734 13.417 38.147 1.00123.66 N ANISOU 4295 N SER B 335 16061 15700 15223 -4799 2817 -2527 N ATOM 4296 CA SER B 335 -3.720 13.655 39.588 1.00124.15 C ANISOU 4296 CA SER B 335 16088 15750 15335 -4794 2676 -2703 C ATOM 4297 C SER B 335 -4.418 14.957 39.969 1.00125.85 C ANISOU 4297 C SER B 335 16712 15548 15556 -4862 2727 -2658 C ATOM 4298 O SER B 335 -4.525 15.876 39.158 1.00127.65 O ANISOU 4298 O SER B 335 17216 15518 15768 -4985 2882 -2521 O ATOM 4299 CB SER B 335 -2.283 13.660 40.113 1.00118.16 C ANISOU 4299 CB SER B 335 15014 15262 14619 -4957 2617 -2909 C ATOM 4300 OG SER B 335 -1.639 12.425 39.854 1.00117.03 O ANISOU 4300 OG SER B 335 14495 15494 14479 -4849 2556 -2957 O ATOM 4301 N ASP B 336 -4.886 15.025 41.213 1.00105.46 N ANISOU 4301 N ASP B 336 14180 12899 12989 -4758 2594 -2772 N ATOM 4302 CA ASP B 336 -5.557 16.215 41.726 1.00106.71 C ANISOU 4302 CA ASP B 336 14723 12665 13155 -4776 2628 -2755 C ATOM 4303 C ASP B 336 -4.605 17.404 41.769 1.00110.66 C ANISOU 4303 C ASP B 336 15299 13064 13683 -5068 2710 -2836 C ATOM 4304 O ASP B 336 -5.001 18.541 41.514 1.00112.25 O ANISOU 4304 O ASP B 336 15855 12904 13890 -5143 2826 -2743 O ATOM 4305 CB ASP B 336 -6.118 15.950 43.124 1.00101.94 C ANISOU 4305 CB ASP B 336 14124 12065 12543 -4587 2459 -2892 C ATOM 4306 CG ASP B 336 -7.122 14.816 43.144 1.00 98.50 C ANISOU 4306 CG ASP B 336 13637 11702 12084 -4295 2381 -2821 C ATOM 4307 OD1 ASP B 336 -7.035 13.929 42.270 1.00 97.65 O ANISOU 4307 OD1 ASP B 336 13340 11787 11973 -4249 2404 -2721 O ATOM 4308 OD2 ASP B 336 -7.997 14.811 44.036 1.00 97.55 O ANISOU 4308 OD2 ASP B 336 13664 11458 11941 -4080 2297 -2856 O ATOM 4309 N GLU B 337 -3.346 17.129 42.092 1.00150.99 N ANISOU 4309 N GLU B 337 20068 18487 18814 -5224 2644 -3008 N ATOM 4310 CA GLU B 337 -2.316 18.160 42.140 1.00154.79 C ANISOU 4310 CA GLU B 337 20563 18914 19336 -5525 2711 -3106 C ATOM 4311 C GLU B 337 -1.914 18.589 40.733 1.00156.37 C ANISOU 4311 C GLU B 337 20845 19033 19535 -5697 2916 -2957 C ATOM 4312 O GLU B 337 -1.187 19.566 40.554 1.00160.28 O ANISOU 4312 O GLU B 337 21421 19413 20065 -5959 3014 -2995 O ATOM 4313 CB GLU B 337 -1.091 17.648 42.900 1.00148.46 C ANISOU 4313 CB GLU B 337 19346 18496 18566 -5617 2565 -3325 C ATOM 4314 CG GLU B 337 -0.516 16.355 42.341 1.00146.69 C ANISOU 4314 CG GLU B 337 18733 18662 18340 -5526 2536 -3317 C ATOM 4315 CD GLU B 337 0.665 15.843 43.142 1.00148.13 C ANISOU 4315 CD GLU B 337 18510 19213 18561 -5576 2375 -3523 C ATOM 4316 OE1 GLU B 337 1.103 16.547 44.076 1.00150.78 O ANISOU 4316 OE1 GLU B 337 18862 19506 18920 -5719 2290 -3673 O ATOM 4317 OE2 GLU B 337 1.154 14.735 42.838 1.00146.83 O ANISOU 4317 OE2 GLU B 337 18014 19373 18401 -5462 2328 -3533 O ATOM 4318 N GLN B 338 -2.396 17.852 39.738 1.00133.03 N ANISOU 4318 N GLN B 338 17876 16137 16533 -5550 2976 -2787 N ATOM 4319 CA GLN B 338 -2.063 18.121 38.347 1.00134.49 C ANISOU 4319 CA GLN B 338 18135 16277 16688 -5677 3159 -2634 C ATOM 4320 C GLN B 338 -3.273 18.676 37.598 1.00133.73 C ANISOU 4320 C GLN B 338 18472 15802 16539 -5572 3266 -2385 C ATOM 4321 O GLN B 338 -3.144 19.207 36.495 1.00135.29 O ANISOU 4321 O GLN B 338 18844 15865 16698 -5685 3423 -2234 O ATOM 4322 CB GLN B 338 -1.555 16.844 37.675 1.00126.45 C ANISOU 4322 CB GLN B 338 16766 15636 15643 -5589 3145 -2628 C ATOM 4323 CG GLN B 338 -0.705 17.074 36.438 1.00129.12 C ANISOU 4323 CG GLN B 338 17053 16045 15963 -5779 3315 -2566 C ATOM 4324 CD GLN B 338 -0.003 15.811 35.977 1.00127.96 C ANISOU 4324 CD GLN B 338 16507 16303 15810 -5695 3281 -2626 C ATOM 4325 OE1 GLN B 338 -0.210 14.734 36.536 1.00125.03 O ANISOU 4325 OE1 GLN B 338 15907 16154 15448 -5483 3127 -2698 O ATOM 4326 NE2 GLN B 338 0.837 15.939 34.956 1.00130.47 N ANISOU 4326 NE2 GLN B 338 16749 16709 16115 -5853 3428 -2595 N ATOM 4327 N TRP B 339 -4.449 18.553 38.208 1.00103.19 N ANISOU 4327 N TRP B 339 14776 11763 12667 -5342 3178 -2337 N ATOM 4328 CA TRP B 339 -5.682 19.066 37.617 1.00103.14 C ANISOU 4328 CA TRP B 339 15176 11390 12623 -5195 3253 -2096 C ATOM 4329 C TRP B 339 -5.799 20.579 37.766 1.00107.23 C ANISOU 4329 C TRP B 339 16064 11510 13167 -5321 3345 -2064 C ATOM 4330 O TRP B 339 -6.201 21.076 38.817 1.00109.11 O ANISOU 4330 O TRP B 339 16442 11565 13450 -5260 3278 -2160 O ATOM 4331 CB TRP B 339 -6.904 18.398 38.252 1.00 97.86 C ANISOU 4331 CB TRP B 339 14553 10669 11959 -4892 3130 -2064 C ATOM 4332 CG TRP B 339 -7.415 17.205 37.503 1.00 93.95 C ANISOU 4332 CG TRP B 339 13920 10360 11414 -4709 3106 -1925 C ATOM 4333 CD1 TRP B 339 -7.277 15.895 37.856 1.00 90.29 C ANISOU 4333 CD1 TRP B 339 13103 10245 10957 -4602 2989 -2030 C ATOM 4334 CD2 TRP B 339 -8.152 17.214 36.274 1.00 92.87 C ANISOU 4334 CD2 TRP B 339 14004 10076 11207 -4602 3191 -1651 C ATOM 4335 NE1 TRP B 339 -7.882 15.087 36.923 1.00 88.51 N ANISOU 4335 NE1 TRP B 339 12860 10094 10676 -4448 3008 -1845 N ATOM 4336 CE2 TRP B 339 -8.425 15.873 35.941 1.00 89.88 C ANISOU 4336 CE2 TRP B 339 13382 9974 10792 -4445 3126 -1609 C ATOM 4337 CE3 TRP B 339 -8.606 18.226 35.423 1.00 95.14 C ANISOU 4337 CE3 TRP B 339 14671 10029 11449 -4611 3306 -1430 C ATOM 4338 CZ2 TRP B 339 -9.131 15.517 34.794 1.00 90.12 C ANISOU 4338 CZ2 TRP B 339 13537 9970 10732 -4305 3167 -1359 C ATOM 4339 CZ3 TRP B 339 -9.307 17.870 34.284 1.00 93.50 C ANISOU 4339 CZ3 TRP B 339 14587 9788 11149 -4460 3335 -1175 C ATOM 4340 CH2 TRP B 339 -9.563 16.528 33.980 1.00 90.85 C ANISOU 4340 CH2 TRP B 339 14004 9744 10768 -4314 3264 -1144 C ATOM 4341 N THR B 340 -5.453 21.308 36.710 1.00148.21 N ANISOU 4341 N THR B 340 21421 16565 18327 -5488 3499 -1932 N ATOM 4342 CA THR B 340 -5.614 22.757 36.702 1.00151.84 C ANISOU 4342 CA THR B 340 22260 16622 18810 -5597 3599 -1869 C ATOM 4343 C THR B 340 -6.959 23.133 36.087 1.00151.64 C ANISOU 4343 C THR B 340 22627 16248 18740 -5349 3637 -1592 C ATOM 4344 O THR B 340 -7.733 22.261 35.692 1.00149.10 O ANISOU 4344 O THR B 340 22269 16011 18369 -5113 3581 -1458 O ATOM 4345 CB THR B 340 -4.479 23.453 35.927 1.00153.81 C ANISOU 4345 CB THR B 340 22503 16881 19057 -5920 3752 -1868 C ATOM 4346 OG1 THR B 340 -4.471 22.995 34.569 1.00152.95 O ANISOU 4346 OG1 THR B 340 22387 16870 18858 -5893 3842 -1672 O ATOM 4347 CG2 THR B 340 -3.132 23.150 36.567 1.00154.37 C ANISOU 4347 CG2 THR B 340 22175 17290 19189 -6155 3706 -2139 C ATOM 4348 N THR B 341 -7.235 24.431 36.010 1.00123.39 N ANISOU 4348 N THR B 341 19419 12281 15184 -5394 3724 -1506 N ATOM 4349 CA THR B 341 -8.491 24.916 35.444 1.00123.21 C ANISOU 4349 CA THR B 341 19779 11907 15127 -5137 3749 -1235 C ATOM 4350 C THR B 341 -8.508 24.769 33.924 1.00123.33 C ANISOU 4350 C THR B 341 19872 11951 15036 -5134 3835 -981 C ATOM 4351 O THR B 341 -9.555 24.497 33.320 1.00121.34 O ANISOU 4351 O THR B 341 19773 11606 14725 -4860 3794 -751 O ATOM 4352 CB THR B 341 -8.743 26.388 35.816 1.00123.69 C ANISOU 4352 CB THR B 341 20213 11538 15246 -5174 3817 -1221 C ATOM 4353 OG1 THR B 341 -7.616 27.180 35.421 1.00127.60 O ANISOU 4353 OG1 THR B 341 20716 12014 15751 -5532 3942 -1289 O ATOM 4354 CG2 THR B 341 -8.950 26.528 37.317 1.00122.99 C ANISOU 4354 CG2 THR B 341 20106 11384 15239 -5091 3718 -1440 C ATOM 4355 N ALA B 342 -7.341 24.955 33.315 1.00112.71 N ANISOU 4355 N ALA B 342 18419 10744 13664 -5434 3948 -1023 N ATOM 4356 CA ALA B 342 -7.186 24.799 31.875 1.00113.79 C ANISOU 4356 CA ALA B 342 18609 10944 13683 -5464 4041 -811 C ATOM 4357 C ALA B 342 -7.582 23.391 31.452 1.00109.47 C ANISOU 4357 C ALA B 342 17829 10708 13058 -5263 3947 -750 C ATOM 4358 O ALA B 342 -8.418 23.214 30.569 1.00107.25 O ANISOU 4358 O ALA B 342 17728 10347 12678 -5059 3933 -500 O ATOM 4359 CB ALA B 342 -5.756 25.097 31.459 1.00115.07 C ANISOU 4359 CB ALA B 342 18619 11258 13846 -5828 4179 -920 C ATOM 4360 N LEU B 343 -6.988 22.395 32.103 1.00122.47 N ANISOU 4360 N LEU B 343 19074 12710 14748 -5312 3872 -978 N ATOM 4361 CA LEU B 343 -7.293 20.995 31.824 1.00118.28 C ANISOU 4361 CA LEU B 343 18288 12493 14160 -5132 3780 -955 C ATOM 4362 C LEU B 343 -8.740 20.655 32.170 1.00115.44 C ANISOU 4362 C LEU B 343 18079 11981 13802 -4797 3658 -823 C ATOM 4363 O LEU B 343 -9.299 19.694 31.649 1.00113.61 O ANISOU 4363 O LEU B 343 17764 11906 13496 -4612 3597 -705 O ATOM 4364 CB LEU B 343 -6.344 20.068 32.590 1.00114.09 C ANISOU 4364 CB LEU B 343 17299 12353 13696 -5236 3712 -1239 C ATOM 4365 CG LEU B 343 -4.965 19.768 31.991 1.00115.85 C ANISOU 4365 CG LEU B 343 17237 12883 13899 -5472 3802 -1347 C ATOM 4366 CD1 LEU B 343 -4.078 21.005 31.958 1.00120.55 C ANISOU 4366 CD1 LEU B 343 17953 13315 14536 -5777 3940 -1401 C ATOM 4367 CD2 LEU B 343 -4.289 18.642 32.760 1.00113.71 C ANISOU 4367 CD2 LEU B 343 16504 13009 13691 -5466 3690 -1593 C ATOM 4368 N PHE B 344 -9.336 21.450 33.053 1.00 91.70 N ANISOU 4368 N PHE B 344 15291 8668 10882 -4716 3627 -848 N ATOM 4369 CA PHE B 344 -10.719 21.258 33.478 1.00 88.90 C ANISOU 4369 CA PHE B 344 15090 8132 10553 -4386 3522 -734 C ATOM 4370 C PHE B 344 -11.680 21.636 32.350 1.00 90.13 C ANISOU 4370 C PHE B 344 15572 8052 10618 -4184 3539 -400 C ATOM 4371 O PHE B 344 -12.435 20.793 31.834 1.00 88.56 O ANISOU 4371 O PHE B 344 15336 7960 10353 -3964 3462 -241 O ATOM 4372 CB PHE B 344 -10.991 22.113 34.719 1.00 90.49 C ANISOU 4372 CB PHE B 344 15446 8064 10870 -4356 3500 -872 C ATOM 4373 CG PHE B 344 -12.266 21.773 35.434 1.00 88.55 C ANISOU 4373 CG PHE B 344 15278 7686 10679 -4019 3391 -831 C ATOM 4374 CD1 PHE B 344 -13.459 22.382 35.082 1.00 89.23 C ANISOU 4374 CD1 PHE B 344 15702 7433 10765 -3743 3387 -588 C ATOM 4375 CD2 PHE B 344 -12.268 20.860 36.475 1.00 85.44 C ANISOU 4375 CD2 PHE B 344 14612 7511 10340 -3961 3288 -1037 C ATOM 4376 CE1 PHE B 344 -14.631 22.076 35.746 1.00 86.64 C ANISOU 4376 CE1 PHE B 344 15425 6989 10502 -3409 3294 -553 C ATOM 4377 CE2 PHE B 344 -13.436 20.550 37.142 1.00 83.06 C ANISOU 4377 CE2 PHE B 344 14382 7081 10093 -3646 3202 -1007 C ATOM 4378 CZ PHE B 344 -14.619 21.157 36.776 1.00 83.97 C ANISOU 4378 CZ PHE B 344 14823 6861 10219 -3366 3211 -765 C ATOM 4379 N ASP B 345 -11.646 22.908 31.964 1.00110.55 N ANISOU 4379 N ASP B 345 18479 10327 13199 -4255 3632 -290 N ATOM 4380 CA ASP B 345 -12.500 23.384 30.880 1.00112.02 C ANISOU 4380 CA ASP B 345 18985 10284 13293 -4062 3637 33 C ATOM 4381 C ASP B 345 -12.200 22.641 29.580 1.00111.66 C ANISOU 4381 C ASP B 345 18835 10503 13087 -4109 3654 171 C ATOM 4382 O ASP B 345 -13.114 22.296 28.822 1.00111.24 O ANISOU 4382 O ASP B 345 18893 10436 12936 -3862 3574 410 O ATOM 4383 CB ASP B 345 -12.352 24.894 30.693 1.00113.92 C ANISOU 4383 CB ASP B 345 19572 10155 13557 -4162 3744 110 C ATOM 4384 CG ASP B 345 -12.891 25.680 31.874 1.00115.18 C ANISOU 4384 CG ASP B 345 19894 10012 13857 -4037 3716 15 C ATOM 4385 OD1 ASP B 345 -14.102 25.984 31.884 1.00116.15 O ANISOU 4385 OD1 ASP B 345 20238 9893 14002 -3704 3644 196 O ATOM 4386 OD2 ASP B 345 -12.105 25.990 32.793 1.00115.61 O ANISOU 4386 OD2 ASP B 345 19846 10084 13997 -4259 3759 -245 O ATOM 4387 N PHE B 346 -10.917 22.382 29.336 1.00112.04 N ANISOU 4387 N PHE B 346 18659 10805 13107 -4415 3752 14 N ATOM 4388 CA PHE B 346 -10.506 21.584 28.187 1.00111.11 C ANISOU 4388 CA PHE B 346 18396 10979 12841 -4467 3780 93 C ATOM 4389 C PHE B 346 -11.123 20.194 28.252 1.00106.47 C ANISOU 4389 C PHE B 346 17577 10661 12215 -4244 3642 98 C ATOM 4390 O PHE B 346 -11.527 19.646 27.230 1.00104.39 O ANISOU 4390 O PHE B 346 17349 10511 11805 -4121 3607 278 O ATOM 4391 CB PHE B 346 -8.982 21.477 28.103 1.00110.98 C ANISOU 4391 CB PHE B 346 18118 11213 12837 -4808 3904 -121 C ATOM 4392 CG PHE B 346 -8.500 20.445 27.124 1.00109.91 C ANISOU 4392 CG PHE B 346 17756 11431 12573 -4836 3925 -104 C ATOM 4393 CD1 PHE B 346 -8.514 20.702 25.763 1.00111.68 C ANISOU 4393 CD1 PHE B 346 18185 11616 12635 -4852 4006 114 C ATOM 4394 CD2 PHE B 346 -8.029 19.218 27.564 1.00106.59 C ANISOU 4394 CD2 PHE B 346 16927 11383 12191 -4835 3862 -309 C ATOM 4395 CE1 PHE B 346 -8.072 19.754 24.860 1.00110.42 C ANISOU 4395 CE1 PHE B 346 17830 11776 12349 -4869 4031 115 C ATOM 4396 CE2 PHE B 346 -7.586 18.267 26.667 1.00105.70 C ANISOU 4396 CE2 PHE B 346 16612 11585 11966 -4839 3883 -306 C ATOM 4397 CZ PHE B 346 -7.607 18.535 25.313 1.00107.50 C ANISOU 4397 CZ PHE B 346 17052 11766 12028 -4859 3971 -99 C ATOM 4398 N TYR B 347 -11.193 19.629 29.455 1.00 75.88 N ANISOU 4398 N TYR B 347 13473 6890 8467 -4197 3563 -103 N ATOM 4399 CA TYR B 347 -11.831 18.332 29.646 1.00 71.92 C ANISOU 4399 CA TYR B 347 12757 6620 7950 -3985 3436 -102 C ATOM 4400 C TYR B 347 -13.296 18.402 29.247 1.00 71.24 C ANISOU 4400 C TYR B 347 12945 6317 7805 -3663 3340 182 C ATOM 4401 O TYR B 347 -13.818 17.478 28.624 1.00 69.37 O ANISOU 4401 O TYR B 347 12636 6264 7458 -3506 3261 305 O ATOM 4402 CB TYR B 347 -11.709 17.855 31.098 1.00 69.54 C ANISOU 4402 CB TYR B 347 12202 6419 7802 -3985 3371 -357 C ATOM 4403 CG TYR B 347 -12.466 16.577 31.393 1.00 65.10 C ANISOU 4403 CG TYR B 347 11408 6088 7240 -3703 3209 -357 C ATOM 4404 CD1 TYR B 347 -11.870 15.337 31.207 1.00 62.92 C ANISOU 4404 CD1 TYR B 347 10762 6223 6924 -3728 3169 -482 C ATOM 4405 CD2 TYR B 347 -13.776 16.612 31.858 1.00 62.63 C ANISOU 4405 CD2 TYR B 347 11197 5624 6976 -3331 3050 -247 C ATOM 4406 CE1 TYR B 347 -12.557 14.169 31.473 1.00 58.46 C ANISOU 4406 CE1 TYR B 347 9960 5889 6364 -3408 2974 -494 C ATOM 4407 CE2 TYR B 347 -14.469 15.450 32.122 1.00 58.13 C ANISOU 4407 CE2 TYR B 347 10368 5303 6415 -3022 2860 -258 C ATOM 4408 CZ TYR B 347 -13.856 14.231 31.929 1.00 56.06 C ANISOU 4408 CZ TYR B 347 9764 5427 6110 -3069 2822 -381 C ATOM 4409 OH TYR B 347 -14.544 13.071 32.194 1.00 51.93 O ANISOU 4409 OH TYR B 347 9002 5126 5601 -2774 2640 -390 O ATOM 4410 N HIS B 348 -13.963 19.494 29.609 1.00 81.30 N ANISOU 4410 N HIS B 348 14527 7210 9154 -3550 3336 281 N ATOM 4411 CA HIS B 348 -15.382 19.631 29.269 1.00 81.24 C ANISOU 4411 CA HIS B 348 14765 6990 9114 -3203 3226 555 C ATOM 4412 C HIS B 348 -15.651 19.819 27.767 1.00 83.09 C ANISOU 4412 C HIS B 348 15201 7212 9157 -3140 3214 834 C ATOM 4413 O HIS B 348 -16.564 19.195 27.207 1.00 82.24 O ANISOU 4413 O HIS B 348 15113 7182 8951 -2894 3085 1022 O ATOM 4414 CB HIS B 348 -16.044 20.730 30.102 1.00 84.06 C ANISOU 4414 CB HIS B 348 15373 6950 9616 -3053 3219 572 C ATOM 4415 CG HIS B 348 -16.305 20.329 31.521 1.00 82.27 C ANISOU 4415 CG HIS B 348 14962 6749 9548 -2950 3158 359 C ATOM 4416 ND1 HIS B 348 -15.297 20.176 32.449 1.00 81.59 N ANISOU 4416 ND1 HIS B 348 14649 6812 9541 -3209 3215 53 N ATOM 4417 CD2 HIS B 348 -17.458 20.032 32.166 1.00 81.57 C ANISOU 4417 CD2 HIS B 348 14804 6641 9547 -2557 2995 385 C ATOM 4418 CE1 HIS B 348 -15.819 19.811 33.607 1.00 80.00 C ANISOU 4418 CE1 HIS B 348 14277 6670 9449 -2979 3091 -94 C ATOM 4419 NE2 HIS B 348 -17.128 19.717 33.462 1.00 80.23 N ANISOU 4419 NE2 HIS B 348 14396 6598 9491 -2588 2970 102 N ATOM 4420 N TYR B 349 -14.862 20.666 27.111 1.00 78.07 N ANISOU 4420 N TYR B 349 14714 6488 8460 -3365 3342 859 N ATOM 4421 CA TYR B 349 -14.999 20.834 25.665 1.00 80.25 C ANISOU 4421 CA TYR B 349 15180 6771 8539 -3336 3344 1106 C ATOM 4422 C TYR B 349 -14.678 19.527 24.939 1.00 78.11 C ANISOU 4422 C TYR B 349 14659 6906 8116 -3374 3312 1079 C ATOM 4423 O TYR B 349 -15.364 19.138 23.986 1.00 78.08 O ANISOU 4423 O TYR B 349 14752 6970 7944 -3194 3210 1292 O ATOM 4424 CB TYR B 349 -14.102 21.963 25.152 1.00 84.48 C ANISOU 4424 CB TYR B 349 15904 7147 9048 -3605 3516 1115 C ATOM 4425 CG TYR B 349 -14.535 23.343 25.594 1.00 87.34 C ANISOU 4425 CG TYR B 349 16582 7081 9524 -3537 3542 1195 C ATOM 4426 CD1 TYR B 349 -15.738 23.886 25.161 1.00 88.74 C ANISOU 4426 CD1 TYR B 349 17054 7002 9662 -3226 3433 1477 C ATOM 4427 CD2 TYR B 349 -13.737 24.108 26.434 1.00 88.94 C ANISOU 4427 CD2 TYR B 349 16780 7144 9870 -3776 3666 984 C ATOM 4428 CE1 TYR B 349 -16.138 25.148 25.559 1.00 91.61 C ANISOU 4428 CE1 TYR B 349 17698 6973 10136 -3142 3460 1545 C ATOM 4429 CE2 TYR B 349 -14.128 25.370 26.838 1.00 91.80 C ANISOU 4429 CE2 TYR B 349 17438 7110 10330 -3713 3695 1045 C ATOM 4430 CZ TYR B 349 -15.328 25.886 26.397 1.00 93.11 C ANISOU 4430 CZ TYR B 349 17895 7019 10464 -3390 3598 1325 C ATOM 4431 OH TYR B 349 -15.720 27.143 26.796 1.00 96.18 O ANISOU 4431 OH TYR B 349 18571 7013 10959 -3306 3630 1381 O ATOM 4432 N PHE B 350 -13.637 18.849 25.412 1.00 76.53 N ANISOU 4432 N PHE B 350 14126 6980 7973 -3596 3388 808 N ATOM 4433 CA PHE B 350 -13.242 17.553 24.876 1.00 74.47 C ANISOU 4433 CA PHE B 350 13581 7116 7597 -3625 3367 731 C ATOM 4434 C PHE B 350 -14.344 16.526 25.107 1.00 71.02 C ANISOU 4434 C PHE B 350 13052 6795 7136 -3336 3189 800 C ATOM 4435 O PHE B 350 -14.476 15.564 24.352 1.00 69.87 O ANISOU 4435 O PHE B 350 12805 6906 6839 -3264 3127 846 O ATOM 4436 CB PHE B 350 -11.932 17.092 25.519 1.00 73.61 C ANISOU 4436 CB PHE B 350 13110 7261 7599 -3879 3464 412 C ATOM 4437 CG PHE B 350 -11.408 15.795 24.978 1.00 71.93 C ANISOU 4437 CG PHE B 350 12590 7450 7290 -3902 3456 308 C ATOM 4438 CD1 PHE B 350 -11.292 15.594 23.613 1.00 73.41 C ANISOU 4438 CD1 PHE B 350 12877 7742 7275 -3897 3485 451 C ATOM 4439 CD2 PHE B 350 -11.008 14.785 25.836 1.00 69.13 C ANISOU 4439 CD2 PHE B 350 11852 7369 7047 -3919 3418 59 C ATOM 4440 CE1 PHE B 350 -10.804 14.401 23.114 1.00 72.09 C ANISOU 4440 CE1 PHE B 350 12438 7930 7024 -3903 3482 339 C ATOM 4441 CE2 PHE B 350 -10.515 13.592 25.343 1.00 67.83 C ANISOU 4441 CE2 PHE B 350 11404 7560 6808 -3912 3407 -45 C ATOM 4442 CZ PHE B 350 -10.414 13.400 23.982 1.00 69.29 C ANISOU 4442 CZ PHE B 350 11699 7832 6798 -3903 3442 89 C ATOM 4443 N TYR B 351 -15.133 16.738 26.156 1.00 71.22 N ANISOU 4443 N TYR B 351 13119 6627 7314 -3171 3113 800 N ATOM 4444 CA TYR B 351 -16.296 15.901 26.423 1.00 67.14 C ANISOU 4444 CA TYR B 351 12440 6235 6834 -2788 2860 841 C ATOM 4445 C TYR B 351 -17.355 16.139 25.357 1.00 68.64 C ANISOU 4445 C TYR B 351 12909 6305 6866 -2560 2743 1157 C ATOM 4446 O TYR B 351 -17.910 15.185 24.796 1.00 66.53 O ANISOU 4446 O TYR B 351 12506 6278 6495 -2378 2577 1213 O ATOM 4447 CB TYR B 351 -16.864 16.184 27.816 1.00 64.99 C ANISOU 4447 CB TYR B 351 12096 5807 6791 -2602 2772 735 C ATOM 4448 CG TYR B 351 -18.158 15.461 28.110 1.00 62.16 C ANISOU 4448 CG TYR B 351 11581 5546 6493 -2199 2525 796 C ATOM 4449 CD1 TYR B 351 -18.153 14.158 28.587 1.00 58.89 C ANISOU 4449 CD1 TYR B 351 10780 5466 6129 -2107 2408 620 C ATOM 4450 CD2 TYR B 351 -19.386 16.082 27.915 1.00 63.38 C ANISOU 4450 CD2 TYR B 351 11967 5453 6661 -1911 2414 1034 C ATOM 4451 CE1 TYR B 351 -19.330 13.491 28.857 1.00 56.88 C ANISOU 4451 CE1 TYR B 351 10376 5296 5939 -1767 2198 675 C ATOM 4452 CE2 TYR B 351 -20.570 15.423 28.181 1.00 61.41 C ANISOU 4452 CE2 TYR B 351 11542 5307 6483 -1558 2196 1085 C ATOM 4453 CZ TYR B 351 -20.535 14.128 28.653 1.00 58.15 C ANISOU 4453 CZ TYR B 351 10747 5227 6122 -1501 2095 903 C ATOM 4454 OH TYR B 351 -21.708 13.463 28.921 1.00 56.94 O ANISOU 4454 OH TYR B 351 10412 5174 6048 -1177 1893 953 O ATOM 4455 N MET B 352 -17.632 17.414 25.088 1.00 70.99 N ANISOU 4455 N MET B 352 13603 6225 7145 -2571 2822 1361 N ATOM 4456 CA MET B 352 -18.552 17.785 24.014 1.00 73.42 C ANISOU 4456 CA MET B 352 14217 6392 7285 -2367 2716 1687 C ATOM 4457 C MET B 352 -18.164 17.106 22.701 1.00 73.99 C ANISOU 4457 C MET B 352 14258 6752 7100 -2463 2707 1746 C ATOM 4458 O MET B 352 -18.991 16.450 22.060 1.00 73.12 O ANISOU 4458 O MET B 352 14149 6782 6852 -2243 2521 1891 O ATOM 4459 CB MET B 352 -18.582 19.303 23.822 1.00 77.38 C ANISOU 4459 CB MET B 352 15047 6524 7828 -2378 2788 1822 C ATOM 4460 CG MET B 352 -19.327 20.067 24.905 1.00 77.54 C ANISOU 4460 CG MET B 352 15180 6214 8068 -2165 2746 1839 C ATOM 4461 SD MET B 352 -19.330 21.844 24.591 1.00 82.59 S ANISOU 4461 SD MET B 352 16206 6432 8743 -2183 2837 1987 S ATOM 4462 CE MET B 352 -20.459 22.417 25.857 1.00 82.24 C ANISOU 4462 CE MET B 352 16238 6069 8942 -1821 2736 2011 C ATOM 4463 N LEU B 353 -16.898 17.254 22.320 1.00 88.09 N ANISOU 4463 N LEU B 353 15987 8644 8839 -2775 2892 1610 N ATOM 4464 CA LEU B 353 -16.385 16.656 21.088 1.00 89.01 C ANISOU 4464 CA LEU B 353 16066 9029 8724 -2882 2921 1632 C ATOM 4465 C LEU B 353 -16.507 15.130 21.081 1.00 86.16 C ANISOU 4465 C LEU B 353 15413 9032 8291 -2813 2822 1512 C ATOM 4466 O LEU B 353 -16.977 14.534 20.103 1.00 85.64 O ANISOU 4466 O LEU B 353 15402 9124 8012 -2694 2702 1636 O ATOM 4467 CB LEU B 353 -14.924 17.058 20.875 1.00 89.79 C ANISOU 4467 CB LEU B 353 16098 9179 8837 -3227 3156 1467 C ATOM 4468 CG LEU B 353 -14.210 16.448 19.668 1.00 90.73 C ANISOU 4468 CG LEU B 353 16153 9577 8743 -3358 3230 1450 C ATOM 4469 CD1 LEU B 353 -14.802 16.974 18.368 1.00 94.03 C ANISOU 4469 CD1 LEU B 353 16922 9872 8930 -3254 3178 1748 C ATOM 4470 CD2 LEU B 353 -12.715 16.720 19.733 1.00 91.96 C ANISOU 4470 CD2 LEU B 353 16149 9815 8974 -3687 3461 1236 C ATOM 4471 N SER B 354 -16.079 14.508 22.176 1.00 89.05 N ANISOU 4471 N SER B 354 15472 9534 8830 -2889 2865 1261 N ATOM 4472 CA SER B 354 -16.096 13.054 22.300 1.00 87.00 C ANISOU 4472 CA SER B 354 14861 9634 8561 -2801 2755 1091 C ATOM 4473 C SER B 354 -17.500 12.489 22.125 1.00 86.23 C ANISOU 4473 C SER B 354 14734 9585 8444 -2430 2453 1219 C ATOM 4474 O SER B 354 -17.723 11.612 21.286 1.00 85.71 O ANISOU 4474 O SER B 354 14614 9748 8205 -2362 2351 1242 O ATOM 4475 CB SER B 354 -15.521 12.623 23.650 1.00 85.20 C ANISOU 4475 CB SER B 354 14271 9518 8585 -2857 2780 797 C ATOM 4476 OG SER B 354 -14.190 13.085 23.808 1.00 85.36 O ANISOU 4476 OG SER B 354 14265 9533 8636 -3207 3036 655 O ATOM 4477 N ASN B 355 -18.446 12.993 22.912 1.00 67.14 N ANISOU 4477 N ASN B 355 12350 6954 6207 -2196 2314 1294 N ATOM 4478 CA ASN B 355 -19.827 12.537 22.796 1.00 66.07 C ANISOU 4478 CA ASN B 355 12163 6857 6086 -1843 2029 1421 C ATOM 4479 C ASN B 355 -20.426 12.864 21.430 1.00 68.83 C ANISOU 4479 C ASN B 355 12827 7146 6180 -1756 1934 1708 C ATOM 4480 O ASN B 355 -21.271 12.121 20.917 1.00 68.20 O ANISOU 4480 O ASN B 355 12665 7228 6020 -1546 1700 1779 O ATOM 4481 CB ASN B 355 -20.692 13.097 23.927 1.00 65.33 C ANISOU 4481 CB ASN B 355 12043 6538 6244 -1612 1936 1444 C ATOM 4482 CG ASN B 355 -20.389 12.451 25.264 1.00 64.01 C ANISOU 4482 CG ASN B 355 11521 6500 6301 -1613 1946 1169 C ATOM 4483 OD1 ASN B 355 -19.275 11.984 25.503 1.00 63.43 O ANISOU 4483 OD1 ASN B 355 11278 6597 6228 -1848 2083 958 O ATOM 4484 ND2 ASN B 355 -21.385 12.411 26.141 1.00 65.10 N ANISOU 4484 ND2 ASN B 355 11542 6567 6628 -1340 1801 1174 N ATOM 4485 N ALA B 356 -19.974 13.970 20.841 1.00 68.13 N ANISOU 4485 N ALA B 356 13105 6824 5959 -1927 2110 1872 N ATOM 4486 CA ALA B 356 -20.377 14.321 19.484 1.00 71.98 C ANISOU 4486 CA ALA B 356 13931 7259 6160 -1880 2046 2152 C ATOM 4487 C ALA B 356 -20.002 13.210 18.511 1.00 71.66 C ANISOU 4487 C ALA B 356 13787 7569 5871 -1975 2023 2079 C ATOM 4488 O ALA B 356 -20.824 12.789 17.699 1.00 72.09 O ANISOU 4488 O ALA B 356 13903 7735 5752 -1788 1798 2218 O ATOM 4489 CB ALA B 356 -19.753 15.642 19.057 1.00 76.53 C ANISOU 4489 CB ALA B 356 14849 7556 6673 -2073 2260 2285 C ATOM 4490 N LEU B 357 -18.765 12.730 18.605 1.00 71.16 N ANISOU 4490 N LEU B 357 13559 7683 5795 -2261 2249 1849 N ATOM 4491 CA LEU B 357 -18.323 11.616 17.766 1.00 70.98 C ANISOU 4491 CA LEU B 357 13421 7995 5554 -2351 2259 1740 C ATOM 4492 C LEU B 357 -19.088 10.329 18.087 1.00 66.50 C ANISOU 4492 C LEU B 357 12517 7672 5080 -2109 1987 1604 C ATOM 4493 O LEU B 357 -19.430 9.549 17.186 1.00 66.82 O ANISOU 4493 O LEU B 357 12569 7914 4907 -2040 1850 1627 O ATOM 4494 CB LEU B 357 -16.817 11.391 17.919 1.00 70.95 C ANISOU 4494 CB LEU B 357 13201 8136 5619 -2645 2527 1479 C ATOM 4495 CG LEU B 357 -15.923 12.548 17.470 1.00 74.43 C ANISOU 4495 CG LEU B 357 13815 8407 6059 -2855 2738 1528 C ATOM 4496 CD1 LEU B 357 -14.454 12.191 17.630 1.00 74.25 C ANISOU 4496 CD1 LEU B 357 13515 8572 6123 -3115 2963 1252 C ATOM 4497 CD2 LEU B 357 -16.232 12.934 16.033 1.00 77.93 C ANISOU 4497 CD2 LEU B 357 14566 8820 6224 -2809 2692 1761 C ATOM 4498 N VAL B 358 -19.351 10.119 19.375 1.00 62.64 N ANISOU 4498 N VAL B 358 11744 7157 4901 -1992 1915 1460 N ATOM 4499 CA VAL B 358 -20.109 8.957 19.832 1.00 58.47 C ANISOU 4499 CA VAL B 358 10896 6819 4500 -1766 1673 1342 C ATOM 4500 C VAL B 358 -21.470 8.879 19.145 1.00 59.02 C ANISOU 4500 C VAL B 358 11086 6877 4460 -1504 1379 1560 C ATOM 4501 O VAL B 358 -21.883 7.814 18.685 1.00 57.75 O ANISOU 4501 O VAL B 358 10787 6943 4211 -1418 1205 1501 O ATOM 4502 CB VAL B 358 -20.298 8.969 21.364 1.00 54.89 C ANISOU 4502 CB VAL B 358 10184 6285 4386 -1664 1650 1206 C ATOM 4503 CG1 VAL B 358 -21.317 7.922 21.790 1.00 51.13 C ANISOU 4503 CG1 VAL B 358 9431 5956 4040 -1405 1388 1149 C ATOM 4504 CG2 VAL B 358 -18.968 8.739 22.062 1.00 54.08 C ANISOU 4504 CG2 VAL B 358 9885 6276 4387 -1905 1882 950 C ATOM 4505 N TYR B 359 -22.157 10.014 19.065 1.00 62.65 N ANISOU 4505 N TYR B 359 11804 7071 4929 -1376 1319 1807 N ATOM 4506 CA TYR B 359 -23.430 10.071 18.354 1.00 64.24 C ANISOU 4506 CA TYR B 359 12129 7260 5019 -1120 1030 2038 C ATOM 4507 C TYR B 359 -23.217 9.992 16.843 1.00 67.37 C ANISOU 4507 C TYR B 359 12803 7766 5028 -1223 1017 2167 C ATOM 4508 O TYR B 359 -24.053 9.450 16.109 1.00 67.90 O ANISOU 4508 O TYR B 359 12870 7981 4948 -1068 755 2249 O ATOM 4509 CB TYR B 359 -24.195 11.341 18.727 1.00 66.00 C ANISOU 4509 CB TYR B 359 12551 7154 5370 -929 977 2270 C ATOM 4510 CG TYR B 359 -24.590 11.387 20.184 1.00 63.51 C ANISOU 4510 CG TYR B 359 11972 6741 5417 -786 965 2149 C ATOM 4511 CD1 TYR B 359 -24.853 10.218 20.884 1.00 60.26 C ANISOU 4511 CD1 TYR B 359 11165 6554 5176 -704 853 1941 C ATOM 4512 CD2 TYR B 359 -24.691 12.594 20.863 1.00 64.62 C ANISOU 4512 CD2 TYR B 359 12277 6556 5718 -737 1078 2238 C ATOM 4513 CE1 TYR B 359 -25.211 10.247 22.214 1.00 58.20 C ANISOU 4513 CE1 TYR B 359 10680 6213 5219 -576 856 1836 C ATOM 4514 CE2 TYR B 359 -25.049 12.633 22.197 1.00 62.56 C ANISOU 4514 CE2 TYR B 359 11793 6212 5763 -605 1078 2116 C ATOM 4515 CZ TYR B 359 -25.307 11.455 22.866 1.00 59.35 C ANISOU 4515 CZ TYR B 359 10994 6050 5504 -525 969 1920 C ATOM 4516 OH TYR B 359 -25.663 11.478 24.193 1.00 57.48 O ANISOU 4516 OH TYR B 359 10551 5739 5549 -396 982 1805 O ATOM 4517 N VAL B 360 -22.085 10.528 16.391 1.00 69.46 N ANISOU 4517 N VAL B 360 13300 7965 5124 -1497 1304 2177 N ATOM 4518 CA VAL B 360 -21.732 10.523 14.974 1.00 73.59 C ANISOU 4518 CA VAL B 360 14121 8585 5254 -1630 1355 2295 C ATOM 4519 C VAL B 360 -21.682 9.110 14.400 1.00 72.13 C ANISOU 4519 C VAL B 360 13743 8748 4912 -1644 1246 2115 C ATOM 4520 O VAL B 360 -22.218 8.867 13.324 1.00 74.61 O ANISOU 4520 O VAL B 360 14239 9168 4941 -1567 1066 2246 O ATOM 4521 CB VAL B 360 -20.395 11.264 14.704 1.00 76.34 C ANISOU 4521 CB VAL B 360 14636 8837 5534 -1940 1718 2269 C ATOM 4522 CG1 VAL B 360 -19.699 10.712 13.467 1.00 78.10 C ANISOU 4522 CG1 VAL B 360 14873 9305 5496 -2083 1799 2186 C ATOM 4523 CG2 VAL B 360 -20.634 12.758 14.561 1.00 79.54 C ANISOU 4523 CG2 VAL B 360 15335 8907 5979 -1889 1749 2520 C ATOM 4524 N SER B 361 -21.057 8.180 15.119 1.00103.77 N ANISOU 4524 N SER B 361 17397 12928 9101 -1733 1342 1814 N ATOM 4525 CA SER B 361 -20.987 6.793 14.648 1.00103.12 C ANISOU 4525 CA SER B 361 17133 13152 8896 -1741 1252 1621 C ATOM 4526 C SER B 361 -22.375 6.157 14.524 1.00104.23 C ANISOU 4526 C SER B 361 17164 13378 9061 -1470 864 1677 C ATOM 4527 O SER B 361 -22.716 5.550 13.495 1.00104.48 O ANISOU 4527 O SER B 361 17294 13579 8822 -1445 707 1696 O ATOM 4528 CB SER B 361 -20.109 5.951 15.577 1.00102.10 C ANISOU 4528 CB SER B 361 16635 13160 8996 -1852 1418 1302 C ATOM 4529 OG SER B 361 -20.702 5.820 16.857 1.00102.31 O ANISOU 4529 OG SER B 361 16377 13123 9374 -1679 1279 1233 O ATOM 4530 N ALA B 362 -23.168 6.309 15.582 1.00 75.62 N ANISOU 4530 N ALA B 362 13333 9640 5761 -1276 717 1695 N ATOM 4531 CA ALA B 362 -24.520 5.764 15.636 1.00 77.10 C ANISOU 4531 CA ALA B 362 13364 9896 6036 -1021 363 1748 C ATOM 4532 C ALA B 362 -25.385 6.301 14.502 1.00 78.90 C ANISOU 4532 C ALA B 362 13896 10090 5994 -895 134 2028 C ATOM 4533 O ALA B 362 -26.225 5.582 13.959 1.00 79.80 O ANISOU 4533 O ALA B 362 13942 10369 6010 -777 -151 2036 O ATOM 4534 CB ALA B 362 -25.160 6.070 16.982 1.00 80.86 C ANISOU 4534 CB ALA B 362 13606 10220 6896 -842 303 1752 C ATOM 4535 N ALA B 363 -25.177 7.566 14.148 1.00 68.73 N ANISOU 4535 N ALA B 363 12948 8582 4584 -923 252 2261 N ATOM 4536 CA ALA B 363 -25.892 8.159 13.023 1.00 73.47 C ANISOU 4536 CA ALA B 363 13883 9136 4894 -804 50 2554 C ATOM 4537 C ALA B 363 -25.273 7.738 11.690 1.00 76.81 C ANISOU 4537 C ALA B 363 14551 9749 4884 -989 105 2537 C ATOM 4538 O ALA B 363 -25.919 7.811 10.644 1.00 80.41 O ANISOU 4538 O ALA B 363 15224 10274 5052 -889 -133 2714 O ATOM 4539 CB ALA B 363 -25.914 9.674 13.146 1.00 76.46 C ANISOU 4539 CB ALA B 363 14570 9184 5297 -760 165 2821 C ATOM 4540 N ILE B 364 -24.022 7.291 11.740 1.00 76.51 N ANISOU 4540 N ILE B 364 14469 9803 4797 -1252 419 2317 N ATOM 4541 CA ILE B 364 -23.280 6.914 10.539 1.00 79.61 C ANISOU 4541 CA ILE B 364 15058 10370 4819 -1439 546 2262 C ATOM 4542 C ILE B 364 -23.698 5.544 10.020 1.00 79.05 C ANISOU 4542 C ILE B 364 14861 10588 4586 -1399 317 2095 C ATOM 4543 O ILE B 364 -23.837 5.352 8.811 1.00 81.99 O ANISOU 4543 O ILE B 364 15380 11084 4689 -1379 207 2140 O ATOM 4544 CB ILE B 364 -21.745 6.957 10.776 1.00 78.81 C ANISOU 4544 CB ILE B 364 14864 10280 4799 -1709 968 2053 C ATOM 4545 CG1 ILE B 364 -21.184 8.324 10.383 1.00 81.84 C ANISOU 4545 CG1 ILE B 364 15487 10441 5168 -1804 1190 2234 C ATOM 4546 CG2 ILE B 364 -21.029 5.867 9.991 1.00 79.24 C ANISOU 4546 CG2 ILE B 364 14833 10608 4669 -1832 1058 1819 C ATOM 4547 CD1 ILE B 364 -19.682 8.434 10.537 1.00 81.62 C ANISOU 4547 CD1 ILE B 364 15351 10429 5232 -2071 1578 2039 C ATOM 4548 N ASN B 365 -23.911 4.601 10.936 1.00 92.94 N ANISOU 4548 N ASN B 365 16219 12446 6647 -1343 241 1854 N ATOM 4549 CA ASN B 365 -24.284 3.229 10.559 1.00 93.28 C ANISOU 4549 CA ASN B 365 16095 12740 6605 -1316 40 1652 C ATOM 4550 C ASN B 365 -25.315 3.034 9.424 1.00 95.18 C ANISOU 4550 C ASN B 365 16529 13096 6538 -1196 -320 1796 C ATOM 4551 O ASN B 365 -25.090 2.217 8.532 1.00 95.65 O ANISOU 4551 O ASN B 365 16682 13354 6305 -1290 -350 1662 O ATOM 4552 CB ASN B 365 -24.676 2.406 11.793 1.00 93.36 C ANISOU 4552 CB ASN B 365 15656 12785 7032 -1216 -56 1445 C ATOM 4553 CG ASN B 365 -23.472 1.952 12.593 1.00 91.62 C ANISOU 4553 CG ASN B 365 15224 12585 7000 -1376 272 1190 C ATOM 4554 OD1 ASN B 365 -22.380 1.782 12.049 1.00 92.22 O ANISOU 4554 OD1 ASN B 365 15427 12740 6870 -1571 536 1086 O ATOM 4555 ND2 ASN B 365 -23.665 1.751 13.892 1.00 88.84 N ANISOU 4555 ND2 ASN B 365 14544 12173 7039 -1289 259 1089 N ATOM 4556 N PRO B 366 -26.441 3.775 9.447 1.00 79.36 N ANISOU 4556 N PRO B 366 14585 10975 4593 -981 -599 2060 N ATOM 4557 CA PRO B 366 -27.420 3.546 8.375 1.00 82.94 C ANISOU 4557 CA PRO B 366 15197 11567 4752 -866 -970 2185 C ATOM 4558 C PRO B 366 -27.027 4.124 7.012 1.00 87.51 C ANISOU 4558 C PRO B 366 16106 12163 4979 -921 -878 2318 C ATOM 4559 O PRO B 366 -27.369 3.529 5.990 1.00 89.84 O ANISOU 4559 O PRO B 366 16448 12651 5036 -903 -1063 2264 O ATOM 4560 CB PRO B 366 -28.677 4.247 8.898 1.00 82.80 C ANISOU 4560 CB PRO B 366 15068 11409 4983 -591 -1263 2420 C ATOM 4561 CG PRO B 366 -28.163 5.303 9.803 1.00 81.29 C ANISOU 4561 CG PRO B 366 14892 10949 5045 -591 -980 2517 C ATOM 4562 CD PRO B 366 -26.961 4.703 10.468 1.00 77.77 C ANISOU 4562 CD PRO B 366 14264 10540 4744 -812 -629 2221 C ATOM 4563 N ILE B 367 -26.333 5.258 6.992 1.00 87.18 N ANISOU 4563 N ILE B 367 16260 11925 4941 -984 -593 2475 N ATOM 4564 CA ILE B 367 -25.993 5.909 5.727 1.00 91.54 C ANISOU 4564 CA ILE B 367 17102 12477 5202 -1024 -499 2621 C ATOM 4565 C ILE B 367 -24.924 5.141 4.952 1.00 92.17 C ANISOU 4565 C ILE B 367 17205 12743 5074 -1235 -251 2377 C ATOM 4566 O ILE B 367 -24.759 5.337 3.748 1.00 95.97 O ANISOU 4566 O ILE B 367 17905 13300 5261 -1261 -233 2452 O ATOM 4567 CB ILE B 367 -25.553 7.381 5.925 1.00 93.03 C ANISOU 4567 CB ILE B 367 17496 12381 5472 -1043 -263 2861 C ATOM 4568 CG1 ILE B 367 -24.123 7.463 6.464 1.00 91.03 C ANISOU 4568 CG1 ILE B 367 17187 12051 5350 -1297 185 2684 C ATOM 4569 CG2 ILE B 367 -26.530 8.114 6.834 1.00 92.19 C ANISOU 4569 CG2 ILE B 367 17346 12062 5620 -819 -469 3073 C ATOM 4570 CD1 ILE B 367 -23.112 7.974 5.454 1.00 94.40 C ANISOU 4570 CD1 ILE B 367 17832 12478 5556 -1475 477 2712 C ATOM 4571 N LEU B 368 -24.203 4.267 5.647 1.00 88.67 N ANISOU 4571 N LEU B 368 16529 12372 4789 -1373 -59 2089 N ATOM 4572 CA LEU B 368 -23.207 3.419 5.004 1.00 89.10 C ANISOU 4572 CA LEU B 368 16552 12605 4697 -1539 168 1829 C ATOM 4573 C LEU B 368 -23.888 2.343 4.169 1.00 90.45 C ANISOU 4573 C LEU B 368 16711 13003 4652 -1463 -124 1708 C ATOM 4574 O LEU B 368 -23.301 1.804 3.232 1.00 92.52 O ANISOU 4574 O LEU B 368 17054 13409 4691 -1549 -5 1569 O ATOM 4575 CB LEU B 368 -22.294 2.771 6.047 1.00 85.08 C ANISOU 4575 CB LEU B 368 15761 12111 4455 -1673 428 1553 C ATOM 4576 CG LEU B 368 -21.325 3.696 6.786 1.00 84.08 C ANISOU 4576 CG LEU B 368 15615 11798 4533 -1803 779 1597 C ATOM 4577 CD1 LEU B 368 -20.525 2.914 7.814 1.00 80.25 C ANISOU 4577 CD1 LEU B 368 14809 11371 4313 -1908 982 1305 C ATOM 4578 CD2 LEU B 368 -20.400 4.396 5.803 1.00 87.74 C ANISOU 4578 CD2 LEU B 368 16295 12235 4806 -1936 1052 1674 C ATOM 4579 N TYR B 369 -25.135 2.038 4.515 1.00 90.29 N ANISOU 4579 N TYR B 369 16583 13012 4713 -1302 -510 1756 N ATOM 4580 CA TYR B 369 -25.901 1.020 3.809 1.00 91.61 C ANISOU 4580 CA TYR B 369 16704 13387 4717 -1233 -830 1632 C ATOM 4581 C TYR B 369 -26.475 1.587 2.514 1.00 96.52 C ANISOU 4581 C TYR B 369 17594 14062 5018 -1136 -1027 1853 C ATOM 4582 O TYR B 369 -26.948 0.844 1.654 1.00 98.71 O ANISOU 4582 O TYR B 369 17894 14525 5085 -1107 -1245 1751 O ATOM 4583 CB TYR B 369 -27.030 0.487 4.695 1.00 89.02 C ANISOU 4583 CB TYR B 369 16122 13075 4627 -1106 -1182 1603 C ATOM 4584 CG TYR B 369 -26.579 -0.004 6.056 1.00 84.30 C ANISOU 4584 CG TYR B 369 15265 12419 4347 -1184 -1016 1418 C ATOM 4585 CD1 TYR B 369 -25.308 -0.535 6.242 1.00 82.62 C ANISOU 4585 CD1 TYR B 369 14984 12235 4172 -1358 -641 1172 C ATOM 4586 CD2 TYR B 369 -27.426 0.067 7.155 1.00 81.78 C ANISOU 4586 CD2 TYR B 369 14753 12022 4299 -1071 -1237 1494 C ATOM 4587 CE1 TYR B 369 -24.895 -0.981 7.484 1.00 78.57 C ANISOU 4587 CE1 TYR B 369 14222 11685 3947 -1419 -494 1004 C ATOM 4588 CE2 TYR B 369 -27.021 -0.378 8.400 1.00 76.69 C ANISOU 4588 CE2 TYR B 369 13766 11318 4053 -1097 -1057 1304 C ATOM 4589 CZ TYR B 369 -25.755 -0.901 8.559 1.00 75.31 C ANISOU 4589 CZ TYR B 369 13557 11183 3874 -1279 -699 1067 C ATOM 4590 OH TYR B 369 -25.348 -1.344 9.797 1.00 70.50 O ANISOU 4590 OH TYR B 369 12602 10522 3664 -1286 -537 884 O ATOM 4591 N ASN B 370 -26.427 2.909 2.385 1.00135.21 N ANISOU 4591 N ASN B 370 22697 18791 9884 -1088 -947 2153 N ATOM 4592 CA ASN B 370 -26.967 3.591 1.214 1.00140.20 C ANISOU 4592 CA ASN B 370 23595 19454 10221 -984 -1121 2401 C ATOM 4593 C ASN B 370 -25.898 3.889 0.167 1.00143.46 C ANISOU 4593 C ASN B 370 24268 19900 10339 -1136 -802 2398 C ATOM 4594 O ASN B 370 -26.116 3.694 -1.029 1.00147.16 O ANISOU 4594 O ASN B 370 24901 20530 10482 -1116 -926 2409 O ATOM 4595 CB ASN B 370 -27.657 4.891 1.628 1.00139.67 C ANISOU 4595 CB ASN B 370 23613 19168 10288 -817 -1237 2750 C ATOM 4596 CG ASN B 370 -28.754 4.669 2.649 1.00137.79 C ANISOU 4596 CG ASN B 370 23112 18899 10342 -636 -1567 2779 C ATOM 4597 OD1 ASN B 370 -29.503 3.695 2.572 1.00137.61 O ANISOU 4597 OD1 ASN B 370 22905 19063 10316 -571 -1876 2640 O ATOM 4598 ND2 ASN B 370 -28.852 5.572 3.617 1.00136.80 N ANISOU 4598 ND2 ASN B 370 22961 18532 10486 -555 -1498 2953 N ATOM 4599 N LEU B 371 -24.746 4.366 0.626 1.00104.42 N ANISOU 4599 N LEU B 371 19350 14809 5516 -1292 -394 2381 N ATOM 4600 CA LEU B 371 -23.657 4.749 -0.266 1.00107.50 C ANISOU 4600 CA LEU B 371 19963 15210 5674 -1449 -57 2393 C ATOM 4601 C LEU B 371 -23.078 3.556 -1.019 1.00108.22 C ANISOU 4601 C LEU B 371 20018 15538 5562 -1549 32 2097 C ATOM 4602 O LEU B 371 -22.633 3.685 -2.159 1.00112.21 O ANISOU 4602 O LEU B 371 20750 16131 5752 -1606 144 2132 O ATOM 4603 CB LEU B 371 -22.544 5.445 0.521 1.00105.62 C ANISOU 4603 CB LEU B 371 19685 14776 5671 -1611 354 2392 C ATOM 4604 CG LEU B 371 -22.908 6.746 1.238 1.00105.33 C ANISOU 4604 CG LEU B 371 19721 14463 5838 -1540 343 2674 C ATOM 4605 CD1 LEU B 371 -21.705 7.296 1.987 1.00103.51 C ANISOU 4605 CD1 LEU B 371 19420 14065 5844 -1735 758 2608 C ATOM 4606 CD2 LEU B 371 -23.444 7.769 0.251 1.00110.34 C ANISOU 4606 CD2 LEU B 371 20686 15020 6218 -1438 221 3008 C ATOM 4607 N VAL B 372 -23.089 2.394 -0.375 1.00181.04 N ANISOU 4607 N VAL B 372 28962 24856 14968 -1563 -16 1808 N ATOM 4608 CA VAL B 372 -22.451 1.208 -0.932 1.00182.44 C ANISOU 4608 CA VAL B 372 29077 25224 15018 -1653 108 1496 C ATOM 4609 C VAL B 372 -23.401 0.387 -1.805 1.00185.48 C ANISOU 4609 C VAL B 372 29521 25803 15149 -1547 -257 1424 C ATOM 4610 O VAL B 372 -23.003 -0.134 -2.848 1.00190.16 O ANISOU 4610 O VAL B 372 30244 26544 15464 -1598 -177 1295 O ATOM 4611 CB VAL B 372 -21.856 0.325 0.182 1.00170.38 C ANISOU 4611 CB VAL B 372 27220 23693 13822 -1726 269 1203 C ATOM 4612 CG1 VAL B 372 -21.062 -0.817 -0.413 1.00170.82 C ANISOU 4612 CG1 VAL B 372 27219 23916 13767 -1804 436 889 C ATOM 4613 CG2 VAL B 372 -20.969 1.159 1.092 1.00168.40 C ANISOU 4613 CG2 VAL B 372 26892 23263 13828 -1834 608 1268 C ATOM 4614 N SER B 373 -24.657 0.279 -1.382 1.00140.84 N ANISOU 4614 N SER B 373 23766 20152 9595 -1401 -659 1504 N ATOM 4615 CA SER B 373 -25.647 -0.489 -2.133 1.00143.40 C ANISOU 4615 CA SER B 373 24100 20663 9721 -1306 -1042 1425 C ATOM 4616 C SER B 373 -26.758 0.402 -2.683 1.00147.60 C ANISOU 4616 C SER B 373 24795 21195 10092 -1143 -1388 1751 C ATOM 4617 O SER B 373 -27.274 1.270 -1.981 1.00146.61 O ANISOU 4617 O SER B 373 24622 20915 10166 -1042 -1490 1986 O ATOM 4618 CB SER B 373 -26.241 -1.594 -1.260 1.00136.64 C ANISOU 4618 CB SER B 373 22925 19853 9139 -1277 -1255 1183 C ATOM 4619 OG SER B 373 -27.175 -2.372 -1.988 1.00140.02 O ANISOU 4619 OG SER B 373 23343 20460 9397 -1209 -1619 1079 O ATOM 4620 N ALA B 374 -27.124 0.175 -3.941 1.00144.11 N ANISOU 4620 N ALA B 374 24538 20926 9291 -1107 -1568 1763 N ATOM 4621 CA ALA B 374 -28.140 0.985 -4.608 1.00148.18 C ANISOU 4621 CA ALA B 374 25211 21472 9618 -944 -1901 2070 C ATOM 4622 C ALA B 374 -29.545 0.421 -4.413 1.00147.60 C ANISOU 4622 C ALA B 374 24908 21513 9660 -798 -2393 2032 C ATOM 4623 O ALA B 374 -30.524 1.167 -4.393 1.00149.39 O ANISOU 4623 O ALA B 374 25120 21704 9937 -626 -2683 2301 O ATOM 4624 CB ALA B 374 -27.821 1.120 -6.090 1.00153.64 C ANISOU 4624 CB ALA B 374 26224 22306 9847 -978 -1856 2122 C ATOM 4625 N ASN B 375 -29.637 -0.898 -4.281 1.00138.17 N ANISOU 4625 N ASN B 375 23525 20454 8522 -865 -2481 1694 N ATOM 4626 CA ASN B 375 -30.914 -1.561 -4.043 1.00138.02 C ANISOU 4626 CA ASN B 375 23248 20549 8647 -764 -2927 1609 C ATOM 4627 C ASN B 375 -31.495 -1.156 -2.692 1.00134.68 C ANISOU 4627 C ASN B 375 22561 19968 8643 -662 -3039 1740 C ATOM 4628 O ASN B 375 -32.645 -0.712 -2.596 1.00135.74 O ANISOU 4628 O ASN B 375 22592 20122 8862 -489 -3393 1943 O ATOM 4629 CB ASN B 375 -30.736 -3.080 -4.107 1.00137.54 C ANISOU 4629 CB ASN B 375 23038 20609 8614 -888 -2920 1197 C ATOM 4630 CG ASN B 375 -32.035 -3.833 -3.891 1.00137.26 C ANISOU 4630 CG ASN B 375 22731 20696 8726 -816 -3373 1081 C ATOM 4631 OD1 ASN B 375 -33.121 -3.305 -4.132 1.00139.94 O ANISOU 4631 OD1 ASN B 375 23031 21104 9038 -668 -3730 1293 O ATOM 4632 ND2 ASN B 375 -31.928 -5.076 -3.434 1.00134.46 N ANISOU 4632 ND2 ASN B 375 22174 20369 8546 -919 -3356 740 N ATOM 4633 N PHE B 376 -30.681 -1.302 -1.652 1.00139.94 N ANISOU 4633 N PHE B 376 23111 20484 9574 -764 -2729 1623 N ATOM 4634 CA PHE B 376 -31.088 -0.964 -0.296 1.00136.82 C ANISOU 4634 CA PHE B 376 22476 19931 9576 -687 -2782 1720 C ATOM 4635 C PHE B 376 -31.286 0.545 -0.174 1.00138.28 C ANISOU 4635 C PHE B 376 22814 19947 9776 -551 -2762 2107 C ATOM 4636 O PHE B 376 -32.054 1.020 0.665 1.00136.85 O ANISOU 4636 O PHE B 376 22461 19663 9872 -404 -2944 2271 O ATOM 4637 CB PHE B 376 -30.050 -1.459 0.715 1.00125.85 C ANISOU 4637 CB PHE B 376 20959 18434 8422 -842 -2423 1498 C ATOM 4638 CG PHE B 376 -29.675 -2.909 0.542 1.00125.63 C ANISOU 4638 CG PHE B 376 20824 18541 8366 -977 -2367 1117 C ATOM 4639 CD1 PHE B 376 -30.600 -3.832 0.078 1.00127.63 C ANISOU 4639 CD1 PHE B 376 20960 18963 8569 -944 -2722 963 C ATOM 4640 CD2 PHE B 376 -28.395 -3.347 0.840 1.00123.66 C ANISOU 4640 CD2 PHE B 376 20579 18245 8160 -1130 -1956 907 C ATOM 4641 CE1 PHE B 376 -30.254 -5.161 -0.085 1.00127.23 C ANISOU 4641 CE1 PHE B 376 20830 19005 8506 -1062 -2661 609 C ATOM 4642 CE2 PHE B 376 -28.044 -4.674 0.679 1.00123.28 C ANISOU 4642 CE2 PHE B 376 20435 18300 8105 -1227 -1896 561 C ATOM 4643 CZ PHE B 376 -28.975 -5.582 0.217 1.00125.27 C ANISOU 4643 CZ PHE B 376 20601 18693 8301 -1193 -2246 412 C ATOM 4644 N ARG B 377 -30.588 1.291 -1.024 1.00138.71 N ANISOU 4644 N ARG B 377 23192 19967 9544 -598 -2532 2251 N ATOM 4645 CA ARG B 377 -30.762 2.734 -1.108 1.00139.91 C ANISOU 4645 CA ARG B 377 23536 19953 9670 -474 -2513 2624 C ATOM 4646 C ARG B 377 -32.172 3.052 -1.588 1.00142.49 C ANISOU 4646 C ARG B 377 23824 20377 9938 -244 -2980 2838 C ATOM 4647 O ARG B 377 -32.837 3.947 -1.063 1.00141.82 O ANISOU 4647 O ARG B 377 23678 20150 10055 -62 -3117 3096 O ATOM 4648 CB ARG B 377 -29.747 3.334 -2.081 1.00143.66 C ANISOU 4648 CB ARG B 377 24366 20401 9818 -591 -2190 2715 C ATOM 4649 CG ARG B 377 -29.778 4.851 -2.161 1.00145.98 C ANISOU 4649 CG ARG B 377 24885 20486 10095 -493 -2113 3093 C ATOM 4650 CD ARG B 377 -29.257 5.343 -3.503 1.00150.91 C ANISOU 4650 CD ARG B 377 25869 21162 10308 -557 -1970 3224 C ATOM 4651 NE ARG B 377 -28.022 4.672 -3.898 1.00150.72 N ANISOU 4651 NE ARG B 377 25916 21235 10115 -785 -1632 2955 N ATOM 4652 CZ ARG B 377 -27.334 4.963 -4.997 1.00154.58 C ANISOU 4652 CZ ARG B 377 26699 21766 10267 -884 -1414 3016 C ATOM 4653 NH1 ARG B 377 -27.757 5.919 -5.813 1.00158.95 N ANISOU 4653 NH1 ARG B 377 27523 22267 10605 -786 -1501 3344 N ATOM 4654 NH2 ARG B 377 -26.221 4.300 -5.281 1.00154.62 N ANISOU 4654 NH2 ARG B 377 26725 21864 10160 -1074 -1105 2753 N ATOM 4655 N GLN B 378 -32.623 2.305 -2.591 1.00165.80 N ANISOU 4655 N GLN B 378 26799 23577 12621 -246 -3223 2719 N ATOM 4656 CA GLN B 378 -33.939 2.530 -3.176 1.00169.74 C ANISOU 4656 CA GLN B 378 27245 24215 13035 -40 -3677 2899 C ATOM 4657 C GLN B 378 -35.072 2.009 -2.299 1.00167.75 C ANISOU 4657 C GLN B 378 26581 24011 13147 84 -4019 2827 C ATOM 4658 O GLN B 378 -36.175 2.556 -2.326 1.00170.67 O ANISOU 4658 O GLN B 378 26836 24404 13606 301 -4340 3054 O ATOM 4659 CB GLN B 378 -34.023 1.939 -4.585 1.00163.60 C ANISOU 4659 CB GLN B 378 26640 23694 11827 -91 -3823 2796 C ATOM 4660 CG GLN B 378 -33.229 2.721 -5.621 1.00167.54 C ANISOU 4660 CG GLN B 378 27557 24162 11940 -138 -3582 2984 C ATOM 4661 CD GLN B 378 -33.674 4.170 -5.725 1.00170.13 C ANISOU 4661 CD GLN B 378 28030 24332 12280 49 -3646 3410 C ATOM 4662 OE1 GLN B 378 -34.855 4.482 -5.574 1.00171.44 O ANISOU 4662 OE1 GLN B 378 28026 24530 12585 262 -4011 3584 O ATOM 4663 NE2 GLN B 378 -32.725 5.063 -5.981 1.00171.08 N ANISOU 4663 NE2 GLN B 378 28453 24276 12274 -30 -3283 3576 N ATOM 4664 N VAL B 379 -34.815 0.960 -1.522 1.00131.08 N ANISOU 4664 N VAL B 379 21701 19379 8727 -49 -3946 2518 N ATOM 4665 CA VAL B 379 -35.820 0.526 -0.554 1.00128.64 C ANISOU 4665 CA VAL B 379 20988 19084 8807 54 -4225 2461 C ATOM 4666 C VAL B 379 -35.873 1.526 0.603 1.00125.57 C ANISOU 4666 C VAL B 379 20520 18443 8750 189 -4119 2699 C ATOM 4667 O VAL B 379 -36.926 1.733 1.211 1.00124.70 O ANISOU 4667 O VAL B 379 20134 18323 8924 378 -4391 2817 O ATOM 4668 CB VAL B 379 -35.599 -0.924 -0.044 1.00124.16 C ANISOU 4668 CB VAL B 379 20181 18595 8402 -125 -4196 2067 C ATOM 4669 CG1 VAL B 379 -35.345 -1.866 -1.211 1.00127.05 C ANISOU 4669 CG1 VAL B 379 20682 19166 8426 -269 -4223 1815 C ATOM 4670 CG2 VAL B 379 -34.465 -0.994 0.963 1.00119.02 C ANISOU 4670 CG2 VAL B 379 19530 17750 7944 -263 -3792 1958 C ATOM 4671 N PHE B 380 -34.735 2.161 0.878 1.00158.58 N ANISOU 4671 N PHE B 380 24936 22419 12897 92 -3713 2764 N ATOM 4672 CA PHE B 380 -34.666 3.219 1.879 1.00157.08 C ANISOU 4672 CA PHE B 380 24737 21963 12983 205 -3569 2992 C ATOM 4673 C PHE B 380 -35.510 4.408 1.433 1.00161.10 C ANISOU 4673 C PHE B 380 25346 22415 13448 456 -3777 3359 C ATOM 4674 O PHE B 380 -36.316 4.930 2.203 1.00159.72 O ANISOU 4674 O PHE B 380 24970 22132 13582 665 -3935 3523 O ATOM 4675 CB PHE B 380 -33.215 3.657 2.099 1.00148.08 C ANISOU 4675 CB PHE B 380 23848 20635 11781 18 -3077 2970 C ATOM 4676 CG PHE B 380 -33.050 4.727 3.145 1.00145.45 C ANISOU 4676 CG PHE B 380 23524 20009 11729 105 -2897 3173 C ATOM 4677 CD1 PHE B 380 -33.890 4.781 4.244 1.00143.43 C ANISOU 4677 CD1 PHE B 380 22979 19672 11845 279 -3091 3227 C ATOM 4678 CD2 PHE B 380 -32.055 5.683 3.023 1.00145.04 C ANISOU 4678 CD2 PHE B 380 23765 19759 11582 9 -2524 3300 C ATOM 4679 CE1 PHE B 380 -33.739 5.765 5.204 1.00141.14 C ANISOU 4679 CE1 PHE B 380 22713 19101 11813 370 -2915 3400 C ATOM 4680 CE2 PHE B 380 -31.899 6.669 3.980 1.00143.04 C ANISOU 4680 CE2 PHE B 380 23531 19222 11594 78 -2351 3468 C ATOM 4681 CZ PHE B 380 -32.743 6.710 5.071 1.00141.06 C ANISOU 4681 CZ PHE B 380 23012 18885 11698 265 -2546 3515 C ATOM 4682 N LEU B 381 -35.321 4.828 0.186 1.00192.25 N ANISOU 4682 N LEU B 381 29597 26433 17014 444 -3769 3486 N ATOM 4683 CA LEU B 381 -36.080 5.945 -0.369 1.00196.40 C ANISOU 4683 CA LEU B 381 30246 26918 17457 677 -3967 3842 C ATOM 4684 C LEU B 381 -37.570 5.626 -0.463 1.00197.87 C ANISOU 4684 C LEU B 381 30114 27302 17766 897 -4453 3885 C ATOM 4685 O LEU B 381 -38.415 6.470 -0.158 1.00199.44 O ANISOU 4685 O LEU B 381 30206 27408 18165 1147 -4624 4148 O ATOM 4686 CB LEU B 381 -35.541 6.333 -1.748 1.00206.30 C ANISOU 4686 CB LEU B 381 31894 28241 18247 598 -3868 3950 C ATOM 4687 CG LEU B 381 -34.134 6.931 -1.797 1.00205.04 C ANISOU 4687 CG LEU B 381 32066 27875 17965 408 -3382 3984 C ATOM 4688 CD1 LEU B 381 -33.747 7.268 -3.229 1.00209.95 C ANISOU 4688 CD1 LEU B 381 33050 28594 18125 350 -3329 4102 C ATOM 4689 CD2 LEU B 381 -34.044 8.163 -0.909 1.00203.64 C ANISOU 4689 CD2 LEU B 381 31934 27366 18074 516 -3211 4234 C ATOM 4690 N SER B 382 -37.885 4.405 -0.887 1.00186.73 N ANISOU 4690 N SER B 382 28538 26163 16250 801 -4664 3617 N ATOM 4691 CA SER B 382 -39.272 3.982 -1.040 1.00189.00 C ANISOU 4691 CA SER B 382 28495 26671 16646 970 -5122 3615 C ATOM 4692 C SER B 382 -39.993 3.951 0.303 1.00185.49 C ANISOU 4692 C SER B 382 27640 26131 16708 1110 -5223 3615 C ATOM 4693 O SER B 382 -41.122 4.425 0.419 1.00186.46 O ANISOU 4693 O SER B 382 27540 26296 17013 1359 -5504 3809 O ATOM 4694 CB SER B 382 -39.351 2.607 -1.707 1.00187.45 C ANISOU 4694 CB SER B 382 28213 26758 16254 794 -5284 3282 C ATOM 4695 OG SER B 382 -38.864 1.594 -0.846 1.00182.35 O ANISOU 4695 OG SER B 382 27381 26076 15829 607 -5125 2961 O ATOM 4696 N THR B 383 -39.336 3.394 1.316 1.00146.59 N ANISOU 4696 N THR B 383 22605 21082 12010 956 -4985 3399 N ATOM 4697 CA THR B 383 -39.924 3.332 2.650 1.00142.54 C ANISOU 4697 CA THR B 383 21713 20470 11978 1074 -5046 3387 C ATOM 4698 C THR B 383 -39.951 4.703 3.320 1.00141.18 C ANISOU 4698 C THR B 383 21616 20015 12013 1282 -4902 3699 C ATOM 4699 O THR B 383 -40.768 4.952 4.207 1.00138.61 O ANISOU 4699 O THR B 383 20975 19623 12069 1479 -5021 3779 O ATOM 4700 CB THR B 383 -39.185 2.334 3.552 1.00134.79 C ANISOU 4700 CB THR B 383 20604 19441 11170 845 -4835 3072 C ATOM 4701 OG1 THR B 383 -37.778 2.600 3.503 1.00133.66 O ANISOU 4701 OG1 THR B 383 20819 19138 10828 659 -4426 3041 O ATOM 4702 CG2 THR B 383 -39.447 0.908 3.088 1.00134.75 C ANISOU 4702 CG2 THR B 383 20423 19699 11078 679 -5029 2753 C ATOM 4703 N LEU B 384 -39.055 5.588 2.895 1.00188.67 N ANISOU 4703 N LEU B 384 28043 25853 17788 1235 -4627 3864 N ATOM 4704 CA LEU B 384 -39.054 6.960 3.390 1.00189.56 C ANISOU 4704 CA LEU B 384 28279 25676 18069 1421 -4482 4167 C ATOM 4705 C LEU B 384 -40.224 7.716 2.774 1.00195.17 C ANISOU 4705 C LEU B 384 28939 26457 18761 1710 -4801 4461 C ATOM 4706 O LEU B 384 -40.774 8.636 3.381 1.00195.01 O ANISOU 4706 O LEU B 384 28826 26250 19018 1950 -4819 4688 O ATOM 4707 CB LEU B 384 -37.733 7.658 3.063 1.00182.68 C ANISOU 4707 CB LEU B 384 27857 24595 16956 1249 -4077 4239 C ATOM 4708 CG LEU B 384 -37.538 9.055 3.654 1.00182.51 C ANISOU 4708 CG LEU B 384 27995 24224 17125 1385 -3859 4507 C ATOM 4709 CD1 LEU B 384 -37.706 9.025 5.165 1.00178.32 C ANISOU 4709 CD1 LEU B 384 27178 23527 17048 1470 -3793 4434 C ATOM 4710 CD2 LEU B 384 -36.176 9.613 3.275 1.00182.19 C ANISOU 4710 CD2 LEU B 384 28369 24005 16848 1159 -3443 4529 C ATOM 4711 N ALA B 385 -40.601 7.318 1.563 1.00165.39 N ANISOU 4711 N ALA B 385 25224 22957 14659 1690 -5048 4450 N ATOM 4712 CA ALA B 385 -41.783 7.866 0.911 1.00170.07 C ANISOU 4712 CA ALA B 385 25722 23681 15215 1954 -5400 4704 C ATOM 4713 C ALA B 385 -43.038 7.293 1.560 1.00168.17 C ANISOU 4713 C ALA B 385 24950 23606 15342 2121 -5716 4619 C ATOM 4714 O ALA B 385 -44.120 7.873 1.468 1.00170.58 O ANISOU 4714 O ALA B 385 25065 23962 15788 2394 -5966 4845 O ATOM 4715 CB ALA B 385 -41.763 7.557 -0.576 1.00174.47 C ANISOU 4715 CB ALA B 385 26506 24496 15290 1865 -5567 4696 C ATOM 4716 N CYS B 386 -42.885 6.146 2.214 1.00150.94 N ANISOU 4716 N CYS B 386 22519 21507 13324 1950 -5691 4291 N ATOM 4717 CA CYS B 386 -43.980 5.531 2.952 1.00149.79 C ANISOU 4717 CA CYS B 386 21849 21494 13568 2068 -5931 4175 C ATOM 4718 C CYS B 386 -44.051 6.105 4.362 1.00147.37 C ANISOU 4718 C CYS B 386 21365 20915 13713 2214 -5741 4259 C ATOM 4719 O CYS B 386 -45.049 5.938 5.062 1.00146.44 O ANISOU 4719 O CYS B 386 20812 20860 13969 2385 -5902 4246 O ATOM 4720 CB CYS B 386 -43.804 4.013 3.014 1.00144.78 C ANISOU 4720 CB CYS B 386 21030 21053 12926 1804 -5982 3782 C ATOM 4721 SG CYS B 386 -43.909 3.177 1.414 1.00149.00 S ANISOU 4721 SG CYS B 386 21704 21931 12977 1638 -6236 3623 S ATOM 4722 N LEU B 387 -42.985 6.786 4.771 1.00269.53 N ANISOU 4722 N LEU B 387 37171 36088 29151 2141 -5384 4335 N ATOM 4723 CA LEU B 387 -42.918 7.368 6.106 1.00266.78 C ANISOU 4723 CA LEU B 387 36710 35453 29200 2262 -5170 4402 C ATOM 4724 C LEU B 387 -43.100 8.885 6.061 1.00268.78 C ANISOU 4724 C LEU B 387 37172 35456 29497 2502 -5087 4758 C ATOM 4725 O LEU B 387 -43.082 9.554 7.094 1.00266.41 O ANISOU 4725 O LEU B 387 36832 34880 29510 2624 -4894 4841 O ATOM 4726 CB LEU B 387 -41.597 6.999 6.789 1.00249.20 C ANISOU 4726 CB LEU B 387 34664 33055 26967 1996 -4814 4194 C ATOM 4727 CG LEU B 387 -41.551 7.137 8.314 1.00245.03 C ANISOU 4727 CG LEU B 387 33922 32302 26875 2073 -4635 4151 C ATOM 4728 CD1 LEU B 387 -42.715 6.396 8.953 1.00244.74 C ANISOU 4728 CD1 LEU B 387 33339 32440 27210 2223 -4899 4055 C ATOM 4729 CD2 LEU B 387 -40.229 6.634 8.863 1.00240.22 C ANISOU 4729 CD2 LEU B 387 33470 31588 26216 1783 -4325 3921 C ATOM 4730 N CYS B 388 -43.280 9.426 4.860 1.00200.65 N ANISOU 4730 N CYS B 388 28772 26912 20555 2567 -5233 4965 N ATOM 4731 CA CYS B 388 -43.570 10.852 4.718 1.00204.28 C ANISOU 4731 CA CYS B 388 29405 27145 21066 2808 -5206 5321 C ATOM 4732 C CYS B 388 -44.896 11.304 5.363 1.00205.91 C ANISOU 4732 C CYS B 388 29192 27343 21700 3145 -5412 5474 C ATOM 4733 O CYS B 388 -45.010 12.461 5.769 1.00207.23 O ANISOU 4733 O CYS B 388 29452 27222 22063 3337 -5298 5712 O ATOM 4734 CB CYS B 388 -43.457 11.320 3.257 1.00198.03 C ANISOU 4734 CB CYS B 388 28967 26447 19827 2796 -5318 5521 C ATOM 4735 SG CYS B 388 -44.825 10.890 2.156 1.00203.73 S ANISOU 4735 SG CYS B 388 29422 27592 20395 2968 -5839 5602 S ATOM 4736 N PRO B 389 -45.903 10.410 5.462 1.00190.02 N ANISOU 4736 N PRO B 389 26713 25641 19848 3212 -5699 5330 N ATOM 4737 CA PRO B 389 -47.025 10.863 6.289 1.00190.77 C ANISOU 4737 CA PRO B 389 26387 25689 20408 3510 -5794 5447 C ATOM 4738 C PRO B 389 -46.841 10.458 7.749 1.00185.21 C ANISOU 4738 C PRO B 389 25421 24862 20089 3464 -5581 5221 C ATOM 4739 O PRO B 389 -46.157 9.469 8.017 1.00181.30 O ANISOU 4739 O PRO B 389 24923 24454 19509 3208 -5498 4932 O ATOM 4740 CB PRO B 389 -48.215 10.120 5.686 1.00183.58 C ANISOU 4740 CB PRO B 389 25091 25193 19470 3607 -6197 5408 C ATOM 4741 CG PRO B 389 -47.633 8.847 5.205 1.00181.64 C ANISOU 4741 CG PRO B 389 24919 25180 18918 3294 -6248 5098 C ATOM 4742 CD PRO B 389 -46.249 9.184 4.714 1.00180.37 C ANISOU 4742 CD PRO B 389 25324 24813 18396 3073 -5978 5119 C TER 4743 PRO B 389 ATOM 4744 N GLY C 7 -40.593 -40.029 32.313 1.00105.82 N ANISOU 4744 N GLY C 7 12422 10475 17310 -3548 -441 -1901 N ATOM 4745 CA GLY C 7 -40.859 -40.607 33.617 1.00106.61 C ANISOU 4745 CA GLY C 7 12516 10346 17646 -3577 -183 -1679 C ATOM 4746 C GLY C 7 -40.116 -39.898 34.732 1.00104.58 C ANISOU 4746 C GLY C 7 12273 10180 17282 -3219 31 -1435 C ATOM 4747 O GLY C 7 -40.688 -39.604 35.782 1.00104.55 O ANISOU 4747 O GLY C 7 12085 10221 17416 -3217 189 -1191 O ATOM 4748 N ARG C 8 -38.836 -39.624 34.503 1.00130.99 N ANISOU 4748 N ARG C 8 15834 13561 20376 -2921 40 -1510 N ATOM 4749 CA ARG C 8 -38.006 -38.946 35.493 1.00129.34 C ANISOU 4749 CA ARG C 8 15655 13451 20039 -2576 214 -1312 C ATOM 4750 C ARG C 8 -36.961 -38.057 34.825 1.00128.12 C ANISOU 4750 C ARG C 8 15558 13534 19586 -2322 112 -1427 C ATOM 4751 O ARG C 8 -36.445 -38.384 33.757 1.00128.14 O ANISOU 4751 O ARG C 8 15725 13496 19467 -2342 -14 -1668 O ATOM 4752 CB ARG C 8 -37.334 -39.964 36.416 1.00131.92 C ANISOU 4752 CB ARG C 8 16260 13428 20434 -2452 440 -1222 C ATOM 4753 CG ARG C 8 -36.526 -41.028 35.690 1.00132.21 C ANISOU 4753 CG ARG C 8 16626 13181 20427 -2438 406 -1459 C ATOM 4754 CD ARG C 8 -35.986 -42.060 36.665 1.00132.90 C ANISOU 4754 CD ARG C 8 16982 12905 20609 -2308 627 -1339 C ATOM 4755 NE ARG C 8 -35.176 -41.446 37.712 1.00131.91 N ANISOU 4755 NE ARG C 8 16866 12904 20349 -1961 767 -1131 N ATOM 4756 CZ ARG C 8 -34.640 -42.112 38.730 1.00132.20 C ANISOU 4756 CZ ARG C 8 17109 12696 20426 -1785 954 -971 C ATOM 4757 NH1 ARG C 8 -34.829 -43.419 38.842 1.00133.49 N ANISOU 4757 NH1 ARG C 8 17499 12453 20769 -1919 1041 -984 N ATOM 4758 NH2 ARG C 8 -33.916 -41.470 39.637 1.00131.20 N ANISOU 4758 NH2 ARG C 8 16973 12724 20154 -1476 1047 -796 N ATOM 4759 N ARG C 9 -36.651 -36.933 35.464 1.00 88.51 N ANISOU 4759 N ARG C 9 10417 8761 14452 -2091 179 -1257 N ATOM 4760 CA ARG C 9 -35.751 -35.941 34.885 1.00 87.07 C ANISOU 4760 CA ARG C 9 10248 8833 14001 -1878 91 -1339 C ATOM 4761 C ARG C 9 -34.555 -35.661 35.794 1.00 85.97 C ANISOU 4761 C ARG C 9 10229 8701 13732 -1549 261 -1228 C ATOM 4762 O ARG C 9 -34.715 -35.519 37.006 1.00 86.07 O ANISOU 4762 O ARG C 9 10186 8694 13823 -1461 417 -1009 O ATOM 4763 CB ARG C 9 -36.518 -34.646 34.607 1.00 84.89 C ANISOU 4763 CB ARG C 9 9681 8889 13685 -1927 -39 -1266 C ATOM 4764 CG ARG C 9 -35.700 -33.555 33.939 1.00 84.38 C ANISOU 4764 CG ARG C 9 9629 9083 13347 -1745 -135 -1342 C ATOM 4765 CD ARG C 9 -36.522 -32.294 33.748 1.00 83.24 C ANISOU 4765 CD ARG C 9 9213 9232 13182 -1780 -255 -1244 C ATOM 4766 NE ARG C 9 -35.785 -31.268 33.017 1.00 82.19 N ANISOU 4766 NE ARG C 9 9117 9324 12787 -1630 -347 -1313 N ATOM 4767 CZ ARG C 9 -35.785 -31.151 31.693 1.00 82.17 C ANISOU 4767 CZ ARG C 9 9163 9419 12639 -1725 -544 -1491 C ATOM 4768 NH1 ARG C 9 -36.485 -31.998 30.950 1.00 83.15 N ANISOU 4768 NH1 ARG C 9 9299 9441 12852 -1969 -689 -1635 N ATOM 4769 NH2 ARG C 9 -35.085 -30.187 31.111 1.00 81.56 N ANISOU 4769 NH2 ARG C 9 9131 9538 12319 -1585 -595 -1528 N ATOM 4770 N PRO C 10 -33.349 -35.588 35.205 1.00 54.79 N ANISOU 4770 N PRO C 10 6445 4792 9583 -1369 231 -1383 N ATOM 4771 CA PRO C 10 -32.113 -35.284 35.937 1.00 52.66 C ANISOU 4771 CA PRO C 10 6267 4563 9179 -1057 361 -1309 C ATOM 4772 C PRO C 10 -32.174 -33.951 36.676 1.00 50.01 C ANISOU 4772 C PRO C 10 5739 4497 8765 -932 399 -1119 C ATOM 4773 O PRO C 10 -32.859 -33.028 36.235 1.00 49.26 O ANISOU 4773 O PRO C 10 5459 4619 8641 -1032 292 -1106 O ATOM 4774 CB PRO C 10 -31.062 -35.215 34.825 1.00 52.20 C ANISOU 4774 CB PRO C 10 6336 4578 8919 -959 280 -1544 C ATOM 4775 CG PRO C 10 -31.593 -36.101 33.761 1.00 54.92 C ANISOU 4775 CG PRO C 10 6780 4759 9330 -1194 169 -1748 C ATOM 4776 CD PRO C 10 -33.083 -35.919 33.794 1.00 55.99 C ANISOU 4776 CD PRO C 10 6716 4931 9629 -1465 81 -1655 C ATOM 4777 N TYR C 11 -31.458 -33.861 37.793 1.00 54.60 N ANISOU 4777 N TYR C 11 6376 5059 9309 -707 544 -978 N ATOM 4778 CA TYR C 11 -31.397 -32.630 38.574 1.00 54.14 C ANISOU 4778 CA TYR C 11 6174 5237 9161 -571 594 -816 C ATOM 4779 C TYR C 11 -29.972 -32.089 38.640 1.00 53.06 C ANISOU 4779 C TYR C 11 6111 5232 8819 -316 611 -872 C ATOM 4780 O TYR C 11 -29.734 -31.000 39.161 1.00 53.09 O ANISOU 4780 O TYR C 11 6016 5439 8716 -201 637 -779 O ATOM 4781 CB TYR C 11 -31.953 -32.852 39.985 1.00 54.26 C ANISOU 4781 CB TYR C 11 6164 5151 9303 -549 753 -580 C ATOM 4782 CG TYR C 11 -31.376 -34.055 40.702 1.00 55.29 C ANISOU 4782 CG TYR C 11 6515 5006 9487 -442 873 -532 C ATOM 4783 CD1 TYR C 11 -30.179 -33.964 41.401 1.00 54.73 C ANISOU 4783 CD1 TYR C 11 6559 4960 9278 -166 938 -488 C ATOM 4784 CD2 TYR C 11 -32.033 -35.279 40.685 1.00 56.30 C ANISOU 4784 CD2 TYR C 11 6737 4844 9809 -619 914 -526 C ATOM 4785 CE1 TYR C 11 -29.649 -35.060 42.059 1.00 54.83 C ANISOU 4785 CE1 TYR C 11 6777 4720 9335 -42 1032 -429 C ATOM 4786 CE2 TYR C 11 -31.511 -36.379 41.340 1.00 56.82 C ANISOU 4786 CE2 TYR C 11 7030 4633 9926 -509 1026 -466 C ATOM 4787 CZ TYR C 11 -30.320 -36.264 42.025 1.00 55.87 C ANISOU 4787 CZ TYR C 11 7024 4546 9657 -207 1081 -412 C ATOM 4788 OH TYR C 11 -29.797 -37.357 42.678 1.00 56.02 O ANISOU 4788 OH TYR C 11 7273 4289 9723 -73 1179 -339 O ATOM 4789 N ILE C 12 -29.028 -32.858 38.105 1.00 56.84 N ANISOU 4789 N ILE C 12 6757 5592 9248 -234 601 -1033 N ATOM 4790 CA ILE C 12 -27.628 -32.454 38.084 1.00 55.27 C ANISOU 4790 CA ILE C 12 6607 5519 8874 0 620 -1107 C ATOM 4791 C ILE C 12 -27.284 -31.739 36.780 1.00 54.55 C ANISOU 4791 C ILE C 12 6471 5624 8630 -52 512 -1291 C ATOM 4792 O ILE C 12 -27.566 -32.244 35.692 1.00 54.16 O ANISOU 4792 O ILE C 12 6484 5502 8592 -198 432 -1453 O ATOM 4793 CB ILE C 12 -26.688 -33.664 38.256 1.00 53.68 C ANISOU 4793 CB ILE C 12 6602 5091 8703 160 686 -1179 C ATOM 4794 CG1 ILE C 12 -26.968 -34.373 39.583 1.00 54.84 C ANISOU 4794 CG1 ILE C 12 6824 5035 8975 232 798 -972 C ATOM 4795 CG2 ILE C 12 -25.232 -33.230 38.178 1.00 51.51 C ANISOU 4795 CG2 ILE C 12 6335 4976 8261 397 698 -1272 C ATOM 4796 CD1 ILE C 12 -26.083 -35.576 39.830 1.00 55.11 C ANISOU 4796 CD1 ILE C 12 7065 4823 9049 414 859 -1013 C ATOM 4797 N LEU C 13 -26.679 -30.562 36.896 1.00 65.36 N ANISOU 4797 N LEU C 13 7749 7238 9848 59 514 -1266 N ATOM 4798 CA LEU C 13 -26.263 -29.795 35.727 1.00 64.38 C ANISOU 4798 CA LEU C 13 7599 7306 9559 20 436 -1417 C ATOM 4799 C LEU C 13 -24.753 -29.888 35.528 1.00 62.31 C ANISOU 4799 C LEU C 13 7406 7098 9170 210 494 -1548 C ATOM 4800 O LEU C 13 -23.997 -30.032 36.489 1.00 60.83 O ANISOU 4800 O LEU C 13 7225 6894 8993 400 575 -1479 O ATOM 4801 CB LEU C 13 -26.693 -28.333 35.866 1.00 64.76 C ANISOU 4801 CB LEU C 13 7493 7584 9531 -18 399 -1304 C ATOM 4802 CG LEU C 13 -26.368 -27.406 34.693 1.00 63.52 C ANISOU 4802 CG LEU C 13 7317 7625 9195 -71 321 -1422 C ATOM 4803 CD1 LEU C 13 -26.982 -27.933 33.405 1.00 64.66 C ANISOU 4803 CD1 LEU C 13 7523 7712 9333 -253 204 -1564 C ATOM 4804 CD2 LEU C 13 -26.845 -25.990 34.978 1.00 63.18 C ANISOU 4804 CD2 LEU C 13 7141 7764 9102 -89 297 -1283 C ATOM 4805 OXT LEU C 13 -24.251 -29.824 34.406 1.00 62.89 O ANISOU 4805 OXT LEU C 13 7526 7244 9127 182 462 -1727 O TER 4806 LEU C 13 ATOM 4807 N GLY D 7 -6.749 23.000 41.190 1.00105.43 N ANISOU 4807 N GLY D 7 16410 10573 13077 -5256 3192 -2427 N ATOM 4808 CA GLY D 7 -6.729 21.758 41.940 1.00102.10 C ANISOU 4808 CA GLY D 7 15659 10493 12641 -5117 3028 -2566 C ATOM 4809 C GLY D 7 -8.045 21.011 41.854 1.00 98.47 C ANISOU 4809 C GLY D 7 15282 9974 12160 -4772 2984 -2422 C ATOM 4810 O GLY D 7 -8.175 19.900 42.368 1.00 95.65 O ANISOU 4810 O GLY D 7 14666 9889 11787 -4631 2858 -2506 O ATOM 4811 N ARG D 8 -9.024 21.624 41.197 1.00115.17 N ANISOU 4811 N ARG D 8 17754 11730 14275 -4626 3084 -2200 N ATOM 4812 CA ARG D 8 -10.351 21.033 41.067 1.00112.71 C ANISOU 4812 CA ARG D 8 17548 11320 13958 -4285 3049 -2042 C ATOM 4813 C ARG D 8 -10.378 19.911 40.033 1.00110.77 C ANISOU 4813 C ARG D 8 17098 11316 13675 -4249 3049 -1899 C ATOM 4814 O ARG D 8 -9.631 19.932 39.055 1.00112.87 O ANISOU 4814 O ARG D 8 17284 11696 13906 -4448 3131 -1828 O ATOM 4815 CB ARG D 8 -11.382 22.106 40.711 1.00114.87 C ANISOU 4815 CB ARG D 8 18259 11135 14252 -4113 3141 -1836 C ATOM 4816 CG ARG D 8 -11.063 22.871 39.437 1.00117.51 C ANISOU 4816 CG ARG D 8 18781 11308 14562 -4273 3278 -1636 C ATOM 4817 CD ARG D 8 -12.103 23.943 39.163 1.00119.60 C ANISOU 4817 CD ARG D 8 19471 11124 14848 -4066 3345 -1432 C ATOM 4818 NE ARG D 8 -13.444 23.383 39.028 1.00117.39 N ANISOU 4818 NE ARG D 8 19268 10761 14575 -3685 3287 -1253 N ATOM 4819 CZ ARG D 8 -14.526 24.098 38.739 1.00118.11 C ANISOU 4819 CZ ARG D 8 19679 10506 14691 -3416 3316 -1045 C ATOM 4820 NH1 ARG D 8 -14.428 25.407 38.553 1.00121.88 N ANISOU 4820 NH1 ARG D 8 20446 10678 15185 -3492 3407 -991 N ATOM 4821 NH2 ARG D 8 -15.708 23.505 38.636 1.00115.50 N ANISOU 4821 NH2 ARG D 8 19367 10141 14377 -3062 3251 -888 N ATOM 4822 N ARG D 9 -11.248 18.932 40.261 1.00 84.61 N ANISOU 4822 N ARG D 9 13697 8088 10362 -3979 2957 -1860 N ATOM 4823 CA ARG D 9 -11.387 17.790 39.366 1.00 82.49 C ANISOU 4823 CA ARG D 9 13182 8124 10036 -3827 2902 -1700 C ATOM 4824 C ARG D 9 -12.832 17.652 38.899 1.00 81.52 C ANISOU 4824 C ARG D 9 13225 7854 9894 -3428 2857 -1429 C ATOM 4825 O ARG D 9 -13.759 17.829 39.690 1.00 80.37 O ANISOU 4825 O ARG D 9 13191 7558 9786 -3159 2795 -1427 O ATOM 4826 CB ARG D 9 -10.940 16.507 40.075 1.00 79.90 C ANISOU 4826 CB ARG D 9 12427 8234 9698 -3750 2747 -1877 C ATOM 4827 CG ARG D 9 -11.233 15.226 39.307 1.00 79.51 C ANISOU 4827 CG ARG D 9 12131 8481 9596 -3535 2671 -1731 C ATOM 4828 CD ARG D 9 -10.899 13.994 40.128 1.00 78.45 C ANISOU 4828 CD ARG D 9 11620 8726 9462 -3416 2514 -1897 C ATOM 4829 NE ARG D 9 -9.469 13.887 40.399 1.00 78.08 N ANISOU 4829 NE ARG D 9 11327 8906 9431 -3736 2526 -2128 N ATOM 4830 CZ ARG D 9 -8.610 13.235 39.623 1.00 77.30 C ANISOU 4830 CZ ARG D 9 10973 9080 9318 -3883 2564 -2143 C ATOM 4831 NH1 ARG D 9 -9.034 12.630 38.522 1.00 76.27 N ANISOU 4831 NH1 ARG D 9 10825 9017 9136 -3745 2593 -1947 N ATOM 4832 NH2 ARG D 9 -7.325 13.189 39.948 1.00 77.19 N ANISOU 4832 NH2 ARG D 9 10713 9276 9338 -4165 2571 -2362 N ATOM 4833 N PRO D 10 -13.029 17.347 37.606 1.00 60.65 N ANISOU 4833 N PRO D 10 10595 5261 7187 -3388 2888 -1203 N ATOM 4834 CA PRO D 10 -14.372 17.116 37.064 1.00 58.34 C ANISOU 4834 CA PRO D 10 10416 4879 6872 -3015 2815 -944 C ATOM 4835 C PRO D 10 -15.082 15.964 37.768 1.00 53.64 C ANISOU 4835 C PRO D 10 9548 4535 6297 -2683 2641 -984 C ATOM 4836 O PRO D 10 -14.434 15.129 38.399 1.00 51.83 O ANISOU 4836 O PRO D 10 9015 4608 6069 -2742 2573 -1174 O ATOM 4837 CB PRO D 10 -14.098 16.743 35.605 1.00 58.64 C ANISOU 4837 CB PRO D 10 10429 5045 6805 -3107 2860 -767 C ATOM 4838 CG PRO D 10 -12.797 17.390 35.291 1.00 62.71 C ANISOU 4838 CG PRO D 10 10997 5523 7307 -3547 3032 -872 C ATOM 4839 CD PRO D 10 -11.997 17.306 36.556 1.00 62.77 C ANISOU 4839 CD PRO D 10 10796 5658 7396 -3707 3005 -1180 C ATOM 4840 N TYR D 11 -16.405 15.931 37.663 1.00 64.54 N ANISOU 4840 N TYR D 11 11035 5787 7700 -2335 2571 -800 N ATOM 4841 CA TYR D 11 -17.196 14.856 38.248 1.00 63.78 C ANISOU 4841 CA TYR D 11 10693 5909 7631 -2021 2423 -807 C ATOM 4842 C TYR D 11 -18.048 14.189 37.175 1.00 64.03 C ANISOU 4842 C TYR D 11 10668 6038 7621 -1803 2336 -568 C ATOM 4843 O TYR D 11 -18.812 13.265 37.455 1.00 63.06 O ANISOU 4843 O TYR D 11 10346 6088 7526 -1546 2214 -537 O ATOM 4844 CB TYR D 11 -18.075 15.386 39.384 1.00 61.50 C ANISOU 4844 CB TYR D 11 10535 5406 7427 -1787 2414 -844 C ATOM 4845 CG TYR D 11 -18.931 16.576 39.008 1.00 62.46 C ANISOU 4845 CG TYR D 11 11015 5128 7590 -1659 2488 -658 C ATOM 4846 CD1 TYR D 11 -18.447 17.873 39.134 1.00 63.08 C ANISOU 4846 CD1 TYR D 11 11404 4878 7687 -1872 2626 -716 C ATOM 4847 CD2 TYR D 11 -20.225 16.403 38.533 1.00 62.78 C ANISOU 4847 CD2 TYR D 11 11081 5114 7660 -1321 2413 -425 C ATOM 4848 CE1 TYR D 11 -19.225 18.963 38.793 1.00 64.28 C ANISOU 4848 CE1 TYR D 11 11902 4640 7882 -1735 2696 -539 C ATOM 4849 CE2 TYR D 11 -21.011 17.488 38.189 1.00 63.52 C ANISOU 4849 CE2 TYR D 11 11492 4844 7798 -1174 2469 -247 C ATOM 4850 CZ TYR D 11 -20.506 18.765 38.322 1.00 64.33 C ANISOU 4850 CZ TYR D 11 11921 4607 7916 -1372 2614 -300 C ATOM 4851 OH TYR D 11 -21.285 19.847 37.982 1.00 65.54 O ANISOU 4851 OH TYR D 11 12410 4374 8119 -1207 2673 -114 O ATOM 4852 N ILE D 12 -17.902 14.665 35.943 1.00 65.29 N ANISOU 4852 N ILE D 12 11013 6086 7708 -1921 2400 -400 N ATOM 4853 CA ILE D 12 -18.653 14.134 34.813 1.00 65.94 C ANISOU 4853 CA ILE D 12 11082 6251 7722 -1744 2310 -172 C ATOM 4854 C ILE D 12 -17.761 13.311 33.891 1.00 66.15 C ANISOU 4854 C ILE D 12 10939 6563 7631 -1948 2321 -199 C ATOM 4855 O ILE D 12 -16.860 13.846 33.247 1.00 67.04 O ANISOU 4855 O ILE D 12 11179 6623 7671 -2234 2456 -202 O ATOM 4856 CB ILE D 12 -19.301 15.266 33.992 1.00 65.30 C ANISOU 4856 CB ILE D 12 11368 5831 7612 -1680 2358 75 C ATOM 4857 CG1 ILE D 12 -20.303 16.042 34.849 1.00 65.56 C ANISOU 4857 CG1 ILE D 12 11562 5576 7772 -1420 2346 117 C ATOM 4858 CG2 ILE D 12 -19.974 14.705 32.750 1.00 65.57 C ANISOU 4858 CG2 ILE D 12 11390 5981 7542 -1532 2248 303 C ATOM 4859 CD1 ILE D 12 -20.927 17.225 34.140 1.00 66.42 C ANISOU 4859 CD1 ILE D 12 12048 5318 7871 -1332 2395 358 C ATOM 4860 N LEU D 13 -18.013 12.007 33.833 1.00 91.66 N ANISOU 4860 N LEU D 13 13889 10091 10849 -1804 2194 -223 N ATOM 4861 CA LEU D 13 -17.275 11.131 32.931 1.00 91.04 C ANISOU 4861 CA LEU D 13 13650 10283 10658 -1952 2202 -250 C ATOM 4862 C LEU D 13 -18.206 10.543 31.875 1.00 91.25 C ANISOU 4862 C LEU D 13 13696 10379 10598 -1754 2082 -46 C ATOM 4863 O LEU D 13 -17.760 10.013 30.858 1.00 90.16 O ANISOU 4863 O LEU D 13 13525 10404 10331 -1863 2100 -17 O ATOM 4864 CB LEU D 13 -16.575 10.007 33.701 1.00 86.74 C ANISOU 4864 CB LEU D 13 12755 10043 10159 -1985 2160 -480 C ATOM 4865 CG LEU D 13 -17.375 8.734 33.993 1.00 85.05 C ANISOU 4865 CG LEU D 13 12309 10025 9982 -1710 1992 -471 C ATOM 4866 CD1 LEU D 13 -16.453 7.630 34.488 1.00 82.88 C ANISOU 4866 CD1 LEU D 13 11722 10048 9722 -1783 1974 -679 C ATOM 4867 CD2 LEU D 13 -18.482 8.995 35.002 1.00 86.02 C ANISOU 4867 CD2 LEU D 13 12468 9996 10221 -1455 1914 -431 C ATOM 4868 OXT LEU D 13 -19.428 10.585 32.018 1.00 88.83 O ANISOU 4868 OXT LEU D 13 13432 9973 10348 -1481 1962 86 O TER 4869 LEU D 13 CONECT 656 1254 CONECT 1254 656 CONECT 3020 3656 CONECT 3656 3020 MASTER 349 0 0 23 4 0 0 9 4865 4 4 54 END