HEADER SIGNALING PROTEIN 07-DEC-12 3ZEV TITLE STRUCTURE OF THERMOSTABLE AGONIST-BOUND NEUROTENSIN TITLE 2 RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUROTENSIN RECEPTOR 1 TM86V; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 OTHER_DETAILS: THERMOSTABLE MUTANT; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: NEUROTENSIN; COMPND 9 CHAIN: C, D; COMPND 10 FRAGMENT: C-TERMINUS, RESIDUES 157-162; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: RESIDUES 8-13 CORRESPOND TO NEUROTENSIN C-TERMINUS. COMPND 13 RESIDUES 6-7 DO NOT CORRESPOND TO NEUROTENSIN SEQUENCE 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, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR P.EGLOFF,M.HILLENBRAND,K.M.SCHLINKMANN,A.BATYUK,P.MITTL,A.PLUECKTHUN REVDAT 3 26-FEB-14 3ZEV 1 JRNL REVDAT 2 05-FEB-14 3ZEV 1 JRNL REVDAT 1 29-JAN-14 3ZEV 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. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-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) : 3.000 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.935 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.33 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.94 REMARK 3 NUMBER OF REFLECTIONS : 22639 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.2436 REMARK 3 R VALUE (WORKING SET) : 0.2418 REMARK 3 FREE R VALUE : 0.2792 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 1129 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 19.9355 - 5.9536 1.00 2867 152 0.2334 0.2581 REMARK 3 2 5.9536 - 4.7466 1.00 2750 145 0.2511 0.2766 REMARK 3 3 4.7466 - 4.1527 1.00 2725 140 0.2046 0.2758 REMARK 3 4 4.1527 - 3.7759 1.00 2708 147 0.2266 0.2581 REMARK 3 5 3.7759 - 3.5068 1.00 2666 135 0.2504 0.2909 REMARK 3 6 3.5068 - 3.3010 1.00 2682 144 0.2864 0.3480 REMARK 3 7 3.3010 - 3.1364 1.00 2687 123 0.3342 0.3764 REMARK 3 8 3.1364 - 3.0003 0.92 2425 143 0.3676 0.3955 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) : 0.39 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.74 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 115.97 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 125.70 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 5073 REMARK 3 ANGLE : 0.735 6912 REMARK 3 CHIRALITY : 0.047 838 REMARK 3 PLANARITY : 0.003 834 REMARK 3 DIHEDRAL : 10.791 1748 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND RESSEQ 51:386) REMARK 3 ORIGIN FOR THE GROUP (A): -11.1522 24.3030 -31.2116 REMARK 3 T TENSOR REMARK 3 T11: 0.7062 T22: 0.7279 REMARK 3 T33: 0.7648 T12: -0.1382 REMARK 3 T13: -0.0670 T23: -0.1449 REMARK 3 L TENSOR REMARK 3 L11: 2.4436 L22: 3.5722 REMARK 3 L33: 4.0092 L12: 0.3318 REMARK 3 L13: 0.0901 L23: 0.2509 REMARK 3 S TENSOR REMARK 3 S11: -0.0903 S12: -0.1211 S13: 0.4025 REMARK 3 S21: 0.1720 S22: 0.1230 S23: -0.4874 REMARK 3 S31: -0.2129 S32: 0.7034 S33: -0.0414 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN B AND RESSEQ 51:386) REMARK 3 ORIGIN FOR THE GROUP (A): -20.9055 -4.0160 -20.5944 REMARK 3 T TENSOR REMARK 3 T11: 0.7273 T22: 0.7416 REMARK 3 T33: 0.5979 T12: 0.0421 REMARK 3 T13: -0.0985 T23: 0.1356 REMARK 3 L TENSOR REMARK 3 L11: 3.9697 L22: 4.9029 REMARK 3 L33: 4.9490 L12: 0.6582 REMARK 3 L13: 0.7986 L23: 0.7879 REMARK 3 S TENSOR REMARK 3 S11: 0.0122 S12: -0.6609 S13: -0.2816 REMARK 3 S21: 1.0301 S22: 0.1063 S23: 0.0347 REMARK 3 S31: 0.6645 S32: 0.0142 S33: -0.1713 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3ZEV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-NOV-13. REMARK 100 THE PDBE ID CODE IS EBI-55025. 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 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M) REMARK 200 DETECTOR MANUFACTURER : DECTRIS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22942 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.00 REMARK 200 RESOLUTION RANGE LOW (A) : 50.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.72 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 6.9 REMARK 200 R MERGE (I) : 0.01 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.68 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NONE REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.54 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.28% (W/V) NONYL-GLUCOSIDE, REMARK 280 0.5% (W/V) DECYL-GLUCOSIDE, 0.01% (W/V) DODECYL-GLUCOSIDE, REMARK 280 0.1% (W/V) CHOLESTERYLHEMISUCCINATE, 10MM HEPES PH 8, 1.15 REMARK 280 MM NACL, 2 MM DTT, 100 NM NTI, 26% (V/V) PEG 600, 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 29.27500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.68000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.09000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.68000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.27500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.09000 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: 1750 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15060 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.1 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 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: 1670 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15360 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.9 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 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 SER A 94 REMARK 465 LEU A 95 REMARK 465 GLN A 96 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 LEU A 387 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 ARG B 91 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 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 LEU B 387 REMARK 465 CYS B 388 REMARK 465 PRO B 389 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 6 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 HIS A 269 CG ND1 CD2 CE1 NE2 REMARK 470 GLN A 270 CG CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 NE2 GLN A 239 OH TYR A 333 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 52 51.12 -114.32 REMARK 500 ASN A 58 59.26 -90.79 REMARK 500 TRP A 130 -70.16 -96.51 REMARK 500 PHE A 246 -76.00 -130.12 REMARK 500 TRP B 130 -72.52 -97.53 REMARK 500 PHE B 246 -74.84 -129.40 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1387 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1388 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1389 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1390 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1391 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4BUO RELATED DB: PDB REMARK 900 HIGH RESOLUTION STRUCTURE OF THERMOSTABLE AGONIST-BOUND REMARK 900 NEUROTENSIN RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION REMARK 900 RELATED ID: 4BV0 RELATED DB: PDB REMARK 900 HIGH RESOLUTION STRUCTURE OF EVOLVED AGONIST-BOUND REMARK 900 NEUROTENSIN RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION REMARK 900 RELATED ID: 4BWB RELATED DB: PDB REMARK 900 STRUCTURE OF EVOLVED AGONIST-BOUND NEUROTENSIN RECEPTOR REMARK 900 1 MUTANT WITHOUT LYSOZYME FUSION DBREF 3ZEV A 50 390 UNP P20789 NTR1_RAT 50 390 DBREF 3ZEV B 50 390 UNP P20789 NTR1_RAT 50 390 DBREF 3ZEV C 8 13 UNP P20068 NEUT_RAT 157 162 DBREF 3ZEV D 8 13 UNP P20068 NEUT_RAT 157 162 SEQADV 3ZEV GLY A 46 UNP P20789 EXPRESSION TAG SEQADV 3ZEV PRO A 47 UNP P20789 EXPRESSION TAG SEQADV 3ZEV GLY A 48 UNP P20789 EXPRESSION TAG SEQADV 3ZEV SER A 49 UNP P20789 EXPRESSION TAG SEQADV 3ZEV THR A 391 UNP P20789 EXPRESSION TAG SEQADV 3ZEV ARG A 392 UNP P20789 EXPRESSION TAG SEQADV 3ZEV GLU A 393 UNP P20789 EXPRESSION TAG SEQADV 3ZEV LEU A 394 UNP P20789 EXPRESSION TAG SEQADV 3ZEV GLU A 395 UNP P20789 EXPRESSION TAG SEQADV 3ZEV VAL A 396 UNP P20789 EXPRESSION TAG SEQADV 3ZEV LEU A 397 UNP P20789 EXPRESSION TAG SEQADV 3ZEV PHE A 398 UNP P20789 EXPRESSION TAG SEQADV 3ZEV GLN A 399 UNP P20789 EXPRESSION TAG SEQADV 3ZEV LEU A 86 UNP P20789 ALA 86 ENGINEERED MUTATION SEQADV 3ZEV ASP A 103 UNP P20789 HIS 103 ENGINEERED MUTATION SEQADV 3ZEV TYR A 105 UNP P20789 HIS 105 ENGINEERED MUTATION SEQADV 3ZEV VAL A 161 UNP P20789 ALA 161 ENGINEERED MUTATION SEQADV 3ZEV LEU A 167 UNP P20789 ARG 167 ENGINEERED MUTATION SEQADV 3ZEV LEU A 213 UNP P20789 ARG 213 ENGINEERED MUTATION SEQADV 3ZEV LEU A 234 UNP P20789 VAL 234 ENGINEERED MUTATION SEQADV 3ZEV ALA A 253 UNP P20789 ILE 253 ENGINEERED MUTATION SEQADV 3ZEV A UNP P20789 VAL 280 DELETION SEQADV 3ZEV A UNP P20789 GLY 281 DELETION SEQADV 3ZEV A UNP P20789 THR 282 DELETION SEQADV 3ZEV A UNP P20789 HIS 283 DELETION SEQADV 3ZEV A UNP P20789 ASN 284 DELETION SEQADV 3ZEV A UNP P20789 GLY 285 DELETION SEQADV 3ZEV A UNP P20789 LEU 286 DELETION SEQADV 3ZEV A UNP P20789 GLU 287 DELETION SEQADV 3ZEV A UNP P20789 HIS 288 DELETION SEQADV 3ZEV A UNP P20789 SER 289 DELETION SEQADV 3ZEV A UNP P20789 THR 290 DELETION SEQADV 3ZEV A UNP P20789 PHE 291 DELETION SEQADV 3ZEV A UNP P20789 ASN 292 DELETION SEQADV 3ZEV A UNP P20789 MET 293 DELETION SEQADV 3ZEV A UNP P20789 THR 294 DELETION SEQADV 3ZEV A UNP P20789 ILE 295 DELETION SEQADV 3ZEV A UNP P20789 THR 296 DELETION SEQADV 3ZEV ARG A 305 UNP P20789 HIS 305 ENGINEERED MUTATION SEQADV 3ZEV VAL A 358 UNP P20789 PHE 358 ENGINEERED MUTATION SEQADV 3ZEV ALA A 362 UNP P20789 SER 362 ENGINEERED MUTATION SEQADV 3ZEV GLY B 46 UNP P20789 EXPRESSION TAG SEQADV 3ZEV PRO B 47 UNP P20789 EXPRESSION TAG SEQADV 3ZEV GLY B 48 UNP P20789 EXPRESSION TAG SEQADV 3ZEV SER B 49 UNP P20789 EXPRESSION TAG SEQADV 3ZEV THR B 391 UNP P20789 EXPRESSION TAG SEQADV 3ZEV ARG B 392 UNP P20789 EXPRESSION TAG SEQADV 3ZEV GLU B 393 UNP P20789 EXPRESSION TAG SEQADV 3ZEV LEU B 394 UNP P20789 EXPRESSION TAG SEQADV 3ZEV GLU B 395 UNP P20789 EXPRESSION TAG SEQADV 3ZEV VAL B 396 UNP P20789 EXPRESSION TAG SEQADV 3ZEV LEU B 397 UNP P20789 EXPRESSION TAG SEQADV 3ZEV PHE B 398 UNP P20789 EXPRESSION TAG SEQADV 3ZEV GLN B 399 UNP P20789 EXPRESSION TAG SEQADV 3ZEV LEU B 86 UNP P20789 ALA 86 ENGINEERED MUTATION SEQADV 3ZEV ASP B 103 UNP P20789 HIS 103 ENGINEERED MUTATION SEQADV 3ZEV TYR B 105 UNP P20789 HIS 105 ENGINEERED MUTATION SEQADV 3ZEV VAL B 161 UNP P20789 ALA 161 ENGINEERED MUTATION SEQADV 3ZEV LEU B 167 UNP P20789 ARG 167 ENGINEERED MUTATION SEQADV 3ZEV LEU B 213 UNP P20789 ARG 213 ENGINEERED MUTATION SEQADV 3ZEV LEU B 234 UNP P20789 VAL 234 ENGINEERED MUTATION SEQADV 3ZEV ALA B 253 UNP P20789 ILE 253 ENGINEERED MUTATION SEQADV 3ZEV B UNP P20789 VAL 280 DELETION SEQADV 3ZEV B UNP P20789 GLY 281 DELETION SEQADV 3ZEV B UNP P20789 THR 282 DELETION SEQADV 3ZEV B UNP P20789 HIS 283 DELETION SEQADV 3ZEV B UNP P20789 ASN 284 DELETION SEQADV 3ZEV B UNP P20789 GLY 285 DELETION SEQADV 3ZEV B UNP P20789 LEU 286 DELETION SEQADV 3ZEV B UNP P20789 GLU 287 DELETION SEQADV 3ZEV B UNP P20789 HIS 288 DELETION SEQADV 3ZEV B UNP P20789 SER 289 DELETION SEQADV 3ZEV B UNP P20789 THR 290 DELETION SEQADV 3ZEV B UNP P20789 PHE 291 DELETION SEQADV 3ZEV B UNP P20789 ASN 292 DELETION SEQADV 3ZEV B UNP P20789 MET 293 DELETION SEQADV 3ZEV B UNP P20789 THR 294 DELETION SEQADV 3ZEV B UNP P20789 ILE 295 DELETION SEQADV 3ZEV B UNP P20789 THR 296 DELETION SEQADV 3ZEV ARG B 305 UNP P20789 HIS 305 ENGINEERED MUTATION SEQADV 3ZEV VAL B 358 UNP P20789 PHE 358 ENGINEERED MUTATION SEQADV 3ZEV ALA B 362 UNP P20789 SER 362 ENGINEERED MUTATION SEQADV 3ZEV GLY C 6 UNP P20068 EXPRESSION TAG SEQADV 3ZEV GLY C 7 UNP P20068 EXPRESSION TAG SEQADV 3ZEV GLY D 6 UNP P20068 EXPRESSION TAG SEQADV 3ZEV 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 SER 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 THR VAL ASP TYR TYR LEU GLY SER LEU ALA SEQRES 6 A 338 LEU SER ASP LEU LEU ILE LEU LEU LEU ALA MET PRO VAL SEQRES 7 A 338 GLU LEU TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA SEQRES 8 A 338 PHE GLY ASP ALA GLY CYS ARG GLY TYR TYR PHE LEU ARG SEQRES 9 A 338 ASP 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 CYS HIS PRO PHE SEQRES 11 A 338 LYS ALA 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 MET 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 VAL 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 ASN LYS 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 VAL VAL ILE ALA PHE VAL VAL CYS TRP SEQRES 21 A 338 LEU PRO TYR HIS VAL ARG ARG LEU MET PHE CYS TYR ILE SEQRES 22 A 338 SER ASP GLU GLN TRP THR THR PHE LEU PHE ASP PHE TYR SEQRES 23 A 338 HIS TYR PHE TYR MET LEU THR 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 SER 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 THR VAL ASP TYR TYR LEU GLY SER LEU ALA SEQRES 6 B 338 LEU SER ASP LEU LEU ILE LEU LEU LEU ALA MET PRO VAL SEQRES 7 B 338 GLU LEU TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA SEQRES 8 B 338 PHE GLY ASP ALA GLY CYS ARG GLY TYR TYR PHE LEU ARG SEQRES 9 B 338 ASP 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 CYS HIS PRO PHE SEQRES 11 B 338 LYS ALA 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 MET 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 VAL 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 ASN LYS 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 VAL VAL ILE ALA PHE VAL VAL CYS TRP SEQRES 21 B 338 LEU PRO TYR HIS VAL ARG ARG LEU MET PHE CYS TYR ILE SEQRES 22 B 338 SER ASP GLU GLN TRP THR THR PHE LEU PHE ASP PHE TYR SEQRES 23 B 338 HIS TYR PHE TYR MET LEU THR 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 8 GLY GLY ARG ARG PRO TYR ILE LEU SEQRES 1 D 8 GLY GLY ARG ARG PRO TYR ILE LEU HET GLY A1387 5 HET GLY A1388 5 HET GLY A1389 5 HET GLY A1390 5 HET GLY A1391 5 HETNAM GLY GLYCINE FORMUL 5 GLY 5(C2 H5 N O2) HELIX 1 1 ASN A 52 ASP A 56 5 5 HELIX 2 2 ASP A 60 ARG A 91 1 32 HELIX 3 3 SER A 97 LEU A 119 1 23 HELIX 4 4 LEU A 119 PHE A 128 1 10 HELIX 5 5 GLY A 138 HIS A 173 1 36 HELIX 6 6 LYS A 176 MET A 181 1 6 HELIX 7 7 SER A 182 ALA A 201 1 20 HELIX 8 8 ILE A 202 THR A 207 1 6 HELIX 9 9 HIS A 219 GLY A 221 5 3 HELIX 10 10 ASP A 230 PHE A 246 1 17 HELIX 11 11 PHE A 246 VAL A 268 1 23 HELIX 12 12 PRO A 297 ILE A 334 1 38 HELIX 13 13 THR A 340 ALA A 362 1 23 HELIX 14 14 ALA A 363 SER A 373 1 11 HELIX 15 15 SER A 373 LEU A 384 1 12 HELIX 16 16 ASP B 60 ALA B 90 1 31 HELIX 17 17 SER B 97 LEU B 119 1 23 HELIX 18 18 LEU B 119 PHE B 128 1 10 HELIX 19 19 PHE B 137 HIS B 173 1 37 HELIX 20 20 SER B 182 ALA B 201 1 20 HELIX 21 21 ILE B 202 THR B 207 1 6 HELIX 22 22 HIS B 219 GLY B 221 5 3 HELIX 23 23 ASP B 230 PHE B 246 1 17 HELIX 24 24 PHE B 246 VAL B 268 1 23 HELIX 25 25 GLY B 298 ILE B 334 1 37 HELIX 26 26 THR B 340 ALA B 362 1 23 HELIX 27 27 ALA B 363 SER B 373 1 11 HELIX 28 28 SER B 373 CYS B 386 1 14 SHEET 1 AA 2 MET 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 MET 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 2.79 CISPEP 2 HIS B 133 PRO B 134 0 2.58 SITE 1 AC1 1 TYR A 333 SITE 1 AC2 2 TYR A 104 GLY A1390 SITE 1 AC3 1 LYS A 64 SITE 1 AC4 2 TYR A 104 GLY A1388 SITE 1 AC5 2 PHE B 243 LEU B 329 CRYST1 58.550 90.180 209.360 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 0.017079 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011089 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004776 0.00000 MTRIX1 1 -0.510000 0.145600 0.847800 -3.92000 1 MTRIX2 1 0.147200 -0.956300 0.252800 28.80000 1 MTRIX3 1 0.847500 0.253700 0.466300 -2.83400 1 ATOM 1 N PRO A 51 -35.461 42.821 -51.516 1.00151.90 N ANISOU 1 N PRO A 51 21392 15391 20931 1847 -4587 2970 N ATOM 2 CA PRO A 51 -36.257 41.614 -51.758 1.00150.96 C ANISOU 2 CA PRO A 51 20868 15759 20732 1838 -4728 2880 C ATOM 3 C PRO A 51 -36.274 40.712 -50.531 1.00150.22 C ANISOU 3 C PRO A 51 20364 15922 20792 1759 -4427 2500 C ATOM 4 O PRO A 51 -37.324 40.486 -49.929 1.00150.89 O ANISOU 4 O PRO A 51 20022 16174 21136 2017 -4486 2346 O ATOM 5 CB PRO A 51 -35.500 40.921 -52.895 1.00138.85 C ANISOU 5 CB PRO A 51 19609 14409 18739 1446 -4755 3037 C ATOM 6 CG PRO A 51 -34.761 42.014 -53.582 1.00140.07 C ANISOU 6 CG PRO A 51 20304 14166 18751 1384 -4788 3333 C ATOM 7 CD PRO A 51 -34.378 42.979 -52.502 1.00140.67 C ANISOU 7 CD PRO A 51 20453 13850 19145 1504 -4558 3212 C ATOM 8 N ASN A 52 -35.099 40.213 -50.170 1.00142.83 N ANISOU 8 N ASN A 52 19559 15018 19693 1403 -4103 2359 N ATOM 9 CA ASN A 52 -34.930 39.345 -49.012 1.00141.26 C ANISOU 9 CA ASN A 52 19047 15035 19591 1290 -3804 2021 C ATOM 10 C ASN A 52 -34.081 40.025 -47.945 1.00140.64 C ANISOU 10 C ASN A 52 19114 14657 19666 1258 -3499 1863 C ATOM 11 O ASN A 52 -33.105 39.457 -47.454 1.00138.79 O ANISOU 11 O ASN A 52 18913 14504 19316 970 -3227 1702 O ATOM 12 CB ASN A 52 -34.329 37.996 -49.418 1.00140.13 C ANISOU 12 CB ASN A 52 18882 15233 19129 915 -3700 1956 C ATOM 13 CG ASN A 52 -33.181 38.135 -50.397 1.00139.96 C ANISOU 13 CG ASN A 52 19297 15105 18775 624 -3667 2154 C ATOM 14 OD1 ASN A 52 -32.492 39.155 -50.427 1.00141.04 O ANISOU 14 OD1 ASN A 52 19751 14904 18934 605 -3596 2271 O ATOM 15 ND2 ASN A 52 -32.972 37.106 -51.209 1.00138.52 N ANISOU 15 ND2 ASN A 52 19139 15210 18281 384 -3707 2185 N ATOM 16 N SER A 53 -34.462 41.250 -47.596 1.00131.25 N ANISOU 16 N SER A 53 18017 13114 18738 1563 -3563 1907 N ATOM 17 CA SER A 53 -33.695 42.059 -46.656 1.00130.74 C ANISOU 17 CA SER A 53 18146 12709 18820 1539 -3315 1769 C ATOM 18 C SER A 53 -34.038 41.725 -45.208 1.00130.05 C ANISOU 18 C SER A 53 17718 12738 18957 1658 -3087 1418 C ATOM 19 O SER A 53 -33.581 42.393 -44.282 1.00129.39 O ANISOU 19 O SER A 53 17754 12389 19018 1686 -2895 1258 O ATOM 20 CB SER A 53 -33.940 43.548 -46.916 1.00119.46 C ANISOU 20 CB SER A 53 17019 10803 17570 1815 -3479 1962 C ATOM 21 OG SER A 53 -35.304 43.882 -46.724 1.00120.81 O ANISOU 21 OG SER A 53 16917 10970 18013 2269 -3672 1948 O ATOM 22 N ASP A 54 -34.848 40.688 -45.021 1.00144.26 N ANISOU 22 N ASP A 54 19109 14934 20770 1710 -3107 1299 N ATOM 23 CA ASP A 54 -35.172 40.199 -43.688 1.00143.63 C ANISOU 23 CA ASP A 54 18702 15020 20850 1775 -2869 978 C ATOM 24 C ASP A 54 -33.993 39.390 -43.159 1.00141.74 C ANISOU 24 C ASP A 54 18535 14911 20410 1393 -2596 817 C ATOM 25 O ASP A 54 -33.958 39.005 -41.990 1.00140.68 O ANISOU 25 O ASP A 54 18225 14877 20351 1381 -2366 556 O ATOM 26 CB ASP A 54 -36.431 39.331 -43.716 1.00185.33 C ANISOU 26 CB ASP A 54 23522 20686 26208 1919 -2979 925 C ATOM 27 CG ASP A 54 -37.625 40.052 -44.308 1.00187.28 C ANISOU 27 CG ASP A 54 23643 20857 26657 2308 -3286 1094 C ATOM 28 OD1 ASP A 54 -38.050 41.074 -43.729 1.00188.22 O ANISOU 28 OD1 ASP A 54 23760 20706 27049 2643 -3263 1034 O ATOM 29 OD2 ASP A 54 -38.139 39.597 -45.351 1.00187.84 O ANISOU 29 OD2 ASP A 54 23621 21137 26614 2288 -3560 1281 O ATOM 30 N LEU A 55 -33.027 39.139 -44.038 1.00112.70 N ANISOU 30 N LEU A 55 15119 11236 16467 1092 -2624 979 N ATOM 31 CA LEU A 55 -31.882 38.295 -43.722 1.00110.73 C ANISOU 31 CA LEU A 55 14919 11139 16013 739 -2398 855 C ATOM 32 C LEU A 55 -30.607 39.117 -43.583 1.00109.80 C ANISOU 32 C LEU A 55 15149 10712 15857 561 -2266 876 C ATOM 33 O LEU A 55 -29.527 38.567 -43.366 1.00107.79 O ANISOU 33 O LEU A 55 14952 10556 15446 272 -2089 790 O ATOM 34 CB LEU A 55 -31.687 37.229 -44.806 1.00100.16 C ANISOU 34 CB LEU A 55 13579 10087 14391 508 -2490 987 C ATOM 35 CG LEU A 55 -32.622 36.018 -44.868 1.00 99.60 C ANISOU 35 CG LEU A 55 13165 10390 14289 533 -2563 913 C ATOM 36 CD1 LEU A 55 -34.043 36.431 -45.210 1.00100.67 C ANISOU 36 CD1 LEU A 55 13103 10541 14607 850 -2824 1012 C ATOM 37 CD2 LEU A 55 -32.112 35.024 -45.893 1.00 98.87 C ANISOU 37 CD2 LEU A 55 13169 10515 13880 253 -2610 1011 C ATOM 38 N ASP A 56 -30.736 40.434 -43.710 1.00111.30 N ANISOU 38 N ASP A 56 15564 10523 16199 732 -2360 989 N ATOM 39 CA ASP A 56 -29.584 41.323 -43.614 1.00110.64 C ANISOU 39 CA ASP A 56 15828 10110 16102 544 -2252 1021 C ATOM 40 C ASP A 56 -29.106 41.487 -42.176 1.00109.17 C ANISOU 40 C ASP A 56 15592 9840 16046 513 -2020 717 C ATOM 41 O ASP A 56 -29.898 41.756 -41.273 1.00109.36 O ANISOU 41 O ASP A 56 15462 9810 16280 787 -1989 538 O ATOM 42 CB ASP A 56 -29.905 42.694 -44.212 1.00142.14 C ANISOU 42 CB ASP A 56 20116 13677 20215 735 -2436 1249 C ATOM 43 CG ASP A 56 -30.140 42.637 -45.708 1.00143.56 C ANISOU 43 CG ASP A 56 20436 13905 20206 710 -2672 1584 C ATOM 44 OD1 ASP A 56 -29.639 41.693 -46.354 1.00143.05 O ANISOU 44 OD1 ASP A 56 20343 14134 19873 443 -2642 1644 O ATOM 45 OD2 ASP A 56 -30.824 43.538 -46.237 1.00145.19 O ANISOU 45 OD2 ASP A 56 20796 13848 20522 968 -2893 1786 O ATOM 46 N VAL A 57 -27.803 41.322 -41.975 1.00127.45 N ANISOU 46 N VAL A 57 18035 12163 18229 177 -1856 656 N ATOM 47 CA VAL A 57 -27.193 41.522 -40.667 1.00125.69 C ANISOU 47 CA VAL A 57 17807 11856 18094 102 -1664 381 C ATOM 48 C VAL A 57 -26.566 42.911 -40.596 1.00126.30 C ANISOU 48 C VAL A 57 18234 11474 18281 34 -1660 422 C ATOM 49 O VAL A 57 -25.631 43.217 -41.337 1.00125.82 O ANISOU 49 O VAL A 57 18401 11303 18103 -242 -1660 595 O ATOM 50 CB VAL A 57 -26.124 40.455 -40.375 1.00 93.28 C ANISOU 50 CB VAL A 57 13592 8057 13794 -217 -1501 264 C ATOM 51 CG1 VAL A 57 -25.407 40.769 -39.076 1.00 91.16 C ANISOU 51 CG1 VAL A 57 13354 7685 13598 -312 -1342 1 C ATOM 52 CG2 VAL A 57 -26.756 39.073 -40.320 1.00 93.46 C ANISOU 52 CG2 VAL A 57 13299 8489 13721 -152 -1493 199 C ATOM 53 N ASN A 58 -27.082 43.746 -39.701 1.00119.50 N ANISOU 53 N ASN A 58 17421 10341 17641 275 -1643 256 N ATOM 54 CA ASN A 58 -26.685 45.150 -39.652 1.00120.71 C ANISOU 54 CA ASN A 58 17938 9996 17931 257 -1666 295 C ATOM 55 C ASN A 58 -25.504 45.436 -38.728 1.00118.76 C ANISOU 55 C ASN A 58 17813 9635 17674 -37 -1500 74 C ATOM 56 O ASN A 58 -25.618 46.221 -37.787 1.00119.58 O ANISOU 56 O ASN A 58 18036 9457 17942 82 -1451 -135 O ATOM 57 CB ASN A 58 -27.879 46.026 -39.265 1.00216.04 C ANISOU 57 CB ASN A 58 30047 21776 30264 700 -1750 238 C ATOM 58 CG ASN A 58 -29.011 45.946 -40.271 1.00218.58 C ANISOU 58 CG ASN A 58 30271 22160 30620 995 -1963 489 C ATOM 59 OD1 ASN A 58 -30.126 45.543 -39.937 1.00219.15 O ANISOU 59 OD1 ASN A 58 30042 22428 30798 1311 -1991 393 O ATOM 60 ND2 ASN A 58 -28.729 46.328 -41.511 1.00219.86 N ANISOU 60 ND2 ASN A 58 30683 22169 30685 881 -2115 817 N ATOM 61 N THR A 59 -24.370 44.801 -39.004 1.00120.23 N ANISOU 61 N THR A 59 17967 10047 17669 -415 -1420 110 N ATOM 62 CA THR A 59 -23.131 45.107 -38.299 1.00118.22 C ANISOU 62 CA THR A 59 17820 9698 17399 -737 -1298 -59 C ATOM 63 C THR A 59 -22.305 46.120 -39.090 1.00119.33 C ANISOU 63 C THR A 59 18306 9485 17548 -1010 -1330 153 C ATOM 64 O THR A 59 -22.133 45.977 -40.301 1.00119.40 O ANISOU 64 O THR A 59 18382 9550 17433 -1128 -1380 440 O ATOM 65 CB THR A 59 -22.297 43.839 -38.028 1.00108.25 C ANISOU 65 CB THR A 59 16292 8893 15946 -986 -1184 -166 C ATOM 66 OG1 THR A 59 -22.108 43.118 -39.251 1.00107.80 O ANISOU 66 OG1 THR A 59 16165 9078 15715 -1106 -1212 83 O ATOM 67 CG2 THR A 59 -23.008 42.941 -37.029 1.00107.12 C ANISOU 67 CG2 THR A 59 15862 9040 15799 -758 -1130 -403 C ATOM 68 N ASP A 60 -21.807 47.143 -38.399 1.00121.28 N ANISOU 68 N ASP A 60 18787 9364 17930 -1124 -1296 9 N ATOM 69 CA ASP A 60 -21.105 48.253 -39.043 1.00122.61 C ANISOU 69 CA ASP A 60 19324 9121 18142 -1387 -1322 200 C ATOM 70 C ASP A 60 -19.869 47.815 -39.831 1.00121.04 C ANISOU 70 C ASP A 60 19092 9145 17754 -1835 -1241 367 C ATOM 71 O ASP A 60 -19.315 46.741 -39.595 1.00119.28 O ANISOU 71 O ASP A 60 18567 9360 17395 -1979 -1150 256 O ATOM 72 CB ASP A 60 -20.724 49.320 -38.013 1.00149.75 C ANISOU 72 CB ASP A 60 22998 12148 21752 -1470 -1290 -43 C ATOM 73 CG ASP A 60 -19.744 48.807 -36.977 1.00147.42 C ANISOU 73 CG ASP A 60 22512 12112 21391 -1749 -1175 -340 C ATOM 74 OD1 ASP A 60 -20.143 47.967 -36.144 1.00146.23 O ANISOU 74 OD1 ASP A 60 22081 12282 21196 -1561 -1134 -564 O ATOM 75 OD2 ASP A 60 -18.574 49.245 -36.996 1.00146.88 O ANISOU 75 OD2 ASP A 60 22568 11929 21311 -2163 -1130 -343 O ATOM 76 N ILE A 61 -19.450 48.661 -40.768 1.00127.20 N ANISOU 76 N ILE A 61 20190 9612 18529 -2047 -1267 638 N ATOM 77 CA ILE A 61 -18.334 48.350 -41.658 1.00127.07 C ANISOU 77 CA ILE A 61 20165 9785 18329 -2469 -1168 831 C ATOM 78 C ILE A 61 -17.011 48.249 -40.901 1.00124.99 C ANISOU 78 C ILE A 61 19770 9649 18072 -2866 -1027 605 C ATOM 79 O ILE A 61 -16.191 47.372 -41.179 1.00122.84 O ANISOU 79 O ILE A 61 19248 9781 17643 -3103 -916 612 O ATOM 80 CB ILE A 61 -18.174 49.395 -42.803 1.00147.68 C ANISOU 80 CB ILE A 61 23195 11991 20927 -2634 -1212 1188 C ATOM 81 CG1 ILE A 61 -19.504 49.684 -43.515 1.00150.15 C ANISOU 81 CG1 ILE A 61 23683 12112 21257 -2217 -1400 1423 C ATOM 82 CG2 ILE A 61 -17.121 48.937 -43.805 1.00146.50 C ANISOU 82 CG2 ILE A 61 23002 12111 20550 -3045 -1077 1395 C ATOM 83 CD1 ILE A 61 -20.399 50.715 -42.832 1.00151.35 C ANISOU 83 CD1 ILE A 61 24056 11779 21673 -1869 -1526 1322 C ATOM 84 N TYR A 62 -16.814 49.146 -39.941 1.00136.68 N ANISOU 84 N TYR A 62 21414 10784 19734 -2927 -1040 395 N ATOM 85 CA TYR A 62 -15.563 49.214 -39.191 1.00135.32 C ANISOU 85 CA TYR A 62 21144 10686 19585 -3323 -947 176 C ATOM 86 C TYR A 62 -15.314 47.959 -38.360 1.00132.36 C ANISOU 86 C TYR A 62 20341 10832 19118 -3270 -898 -85 C ATOM 87 O TYR A 62 -14.188 47.465 -38.293 1.00130.53 O ANISOU 87 O TYR A 62 19893 10895 18808 -3597 -809 -142 O ATOM 88 CB TYR A 62 -15.540 50.459 -38.301 1.00177.89 C ANISOU 88 CB TYR A 62 26839 15568 25184 -3370 -999 -18 C ATOM 89 CG TYR A 62 -15.739 51.752 -39.060 1.00181.49 C ANISOU 89 CG TYR A 62 27763 15448 25747 -3429 -1052 237 C ATOM 90 CD1 TYR A 62 -14.664 52.410 -39.643 1.00182.30 C ANISOU 90 CD1 TYR A 62 28062 15358 25847 -3925 -983 403 C ATOM 91 CD2 TYR A 62 -17.002 52.314 -39.197 1.00183.85 C ANISOU 91 CD2 TYR A 62 28304 15395 26154 -2989 -1171 321 C ATOM 92 CE1 TYR A 62 -14.839 53.591 -40.340 1.00184.69 C ANISOU 92 CE1 TYR A 62 28832 15106 26237 -3993 -1031 658 C ATOM 93 CE2 TYR A 62 -17.188 53.496 -39.892 1.00186.13 C ANISOU 93 CE2 TYR A 62 29049 15131 26542 -3018 -1238 571 C ATOM 94 CZ TYR A 62 -16.103 54.129 -40.461 1.00186.68 C ANISOU 94 CZ TYR A 62 29347 14991 26590 -3528 -1168 746 C ATOM 95 OH TYR A 62 -16.281 55.305 -41.153 1.00189.64 O ANISOU 95 OH TYR A 62 30198 14806 27051 -3563 -1228 1014 O ATOM 96 N SER A 63 -16.365 47.447 -37.727 1.00135.52 N ANISOU 96 N SER A 63 20616 11344 19531 -2857 -952 -235 N ATOM 97 CA SER A 63 -16.247 46.244 -36.912 1.00132.87 C ANISOU 97 CA SER A 63 19916 11472 19097 -2778 -912 -463 C ATOM 98 C SER A 63 -15.945 45.025 -37.779 1.00131.19 C ANISOU 98 C SER A 63 19435 11715 18697 -2836 -849 -295 C ATOM 99 O SER A 63 -15.265 44.098 -37.343 1.00128.74 O ANISOU 99 O SER A 63 18843 11781 18293 -2945 -790 -431 O ATOM 100 CB SER A 63 -17.518 46.012 -36.093 1.00166.31 C ANISOU 100 CB SER A 63 24100 15706 23384 -2334 -961 -640 C ATOM 101 OG SER A 63 -18.643 45.831 -36.935 1.00168.26 O ANISOU 101 OG SER A 63 24363 15943 23624 -2024 -1015 -424 O ATOM 102 N LYS A 64 -16.453 45.033 -39.007 1.00131.02 N ANISOU 102 N LYS A 64 19519 11649 18613 -2752 -870 -2 N ATOM 103 CA LYS A 64 -16.171 43.960 -39.955 1.00130.56 C ANISOU 103 CA LYS A 64 19264 11983 18358 -2820 -805 164 C ATOM 104 C LYS A 64 -14.697 43.954 -40.346 1.00129.75 C ANISOU 104 C LYS A 64 19102 12010 18188 -3260 -676 214 C ATOM 105 O LYS A 64 -14.062 42.901 -40.389 1.00127.54 O ANISOU 105 O LYS A 64 18538 12136 17785 -3349 -588 158 O ATOM 106 CB LYS A 64 -17.038 44.103 -41.207 1.00119.58 C ANISOU 106 CB LYS A 64 18050 10486 16899 -2653 -878 469 C ATOM 107 CG LYS A 64 -18.521 43.868 -40.978 1.00120.53 C ANISOU 107 CG LYS A 64 18133 10590 17073 -2206 -1005 438 C ATOM 108 CD LYS A 64 -19.288 43.923 -42.291 1.00122.46 C ANISOU 108 CD LYS A 64 18521 10783 17226 -2066 -1108 751 C ATOM 109 CE LYS A 64 -20.764 43.632 -42.085 1.00123.43 C ANISOU 109 CE LYS A 64 18543 10937 17417 -1631 -1244 717 C ATOM 110 NZ LYS A 64 -21.520 43.625 -43.368 1.00125.60 N ANISOU 110 NZ LYS A 64 18931 11200 17589 -1492 -1383 1018 N ATOM 111 N VAL A 65 -14.163 45.138 -40.631 1.00136.32 N ANISOU 111 N VAL A 65 20200 12486 19108 -3534 -661 320 N ATOM 112 CA VAL A 65 -12.758 45.287 -40.995 1.00135.91 C ANISOU 112 CA VAL A 65 20090 12530 19020 -3992 -525 372 C ATOM 113 C VAL A 65 -11.851 44.942 -39.816 1.00133.99 C ANISOU 113 C VAL A 65 19565 12505 18841 -4153 -497 62 C ATOM 114 O VAL A 65 -10.811 44.302 -39.986 1.00132.64 O ANISOU 114 O VAL A 65 19123 12680 18592 -4388 -384 41 O ATOM 115 CB VAL A 65 -12.456 46.719 -41.483 1.00124.38 C ANISOU 115 CB VAL A 65 19013 10589 17659 -4270 -520 553 C ATOM 116 CG1 VAL A 65 -10.973 46.883 -41.785 1.00124.37 C ANISOU 116 CG1 VAL A 65 18911 10708 17636 -4783 -360 589 C ATOM 117 CG2 VAL A 65 -13.288 47.045 -42.713 1.00126.37 C ANISOU 117 CG2 VAL A 65 19559 10638 17819 -4116 -566 892 C ATOM 118 N LEU A 66 -12.257 45.363 -38.621 1.00124.30 N ANISOU 118 N LEU A 66 18401 11080 17747 -4010 -604 -180 N ATOM 119 CA LEU A 66 -11.505 45.080 -37.402 1.00122.75 C ANISOU 119 CA LEU A 66 17976 11072 17592 -4132 -619 -486 C ATOM 120 C LEU A 66 -11.373 43.581 -37.158 1.00120.18 C ANISOU 120 C LEU A 66 17268 11269 17126 -3976 -586 -579 C ATOM 121 O LEU A 66 -10.278 43.078 -36.907 1.00118.95 O ANISOU 121 O LEU A 66 16843 11413 16940 -4197 -538 -674 O ATOM 122 CB LEU A 66 -12.170 45.747 -36.196 1.00136.97 C ANISOU 122 CB LEU A 66 19959 12566 19518 -3946 -736 -730 C ATOM 123 CG LEU A 66 -11.538 45.456 -34.832 1.00135.49 C ANISOU 123 CG LEU A 66 19576 12565 19338 -4033 -784 -1062 C ATOM 124 CD1 LEU A 66 -10.086 45.912 -34.799 1.00135.39 C ANISOU 124 CD1 LEU A 66 19488 12575 19381 -4526 -761 -1103 C ATOM 125 CD2 LEU A 66 -12.337 46.112 -33.716 1.00136.29 C ANISOU 125 CD2 LEU A 66 19902 12354 19527 -3812 -878 -1300 C ATOM 126 N VAL A 67 -12.495 42.874 -37.235 1.00115.82 N ANISOU 126 N VAL A 67 16691 10816 16499 -3593 -618 -549 N ATOM 127 CA VAL A 67 -12.505 41.429 -37.044 1.00113.53 C ANISOU 127 CA VAL A 67 16090 10972 16074 -3424 -590 -620 C ATOM 128 C VAL A 67 -11.739 40.734 -38.169 1.00113.09 C ANISOU 128 C VAL A 67 15868 11208 15894 -3596 -467 -439 C ATOM 129 O VAL A 67 -11.041 39.744 -37.940 1.00110.90 O ANISOU 129 O VAL A 67 15302 11293 15541 -3628 -417 -532 O ATOM 130 CB VAL A 67 -13.946 40.887 -36.949 1.00102.39 C ANISOU 130 CB VAL A 67 14705 9575 14621 -3009 -646 -614 C ATOM 131 CG1 VAL A 67 -13.952 39.370 -36.917 1.00100.43 C ANISOU 131 CG1 VAL A 67 14175 9757 14226 -2869 -607 -652 C ATOM 132 CG2 VAL A 67 -14.632 41.442 -35.712 1.00102.66 C ANISOU 132 CG2 VAL A 67 14854 9388 14765 -2825 -729 -836 C ATOM 133 N THR A 68 -11.861 41.268 -39.381 1.00120.88 N ANISOU 133 N THR A 68 17052 12026 16850 -3696 -415 -180 N ATOM 134 CA THR A 68 -11.139 40.731 -40.528 1.00121.24 C ANISOU 134 CA THR A 68 16986 12323 16755 -3878 -270 -2 C ATOM 135 C THR A 68 -9.635 40.850 -40.312 1.00120.84 C ANISOU 135 C THR A 68 16730 12429 16753 -4250 -165 -88 C ATOM 136 O THR A 68 -8.881 39.921 -40.601 1.00119.92 O ANISOU 136 O THR A 68 16336 12685 16543 -4312 -52 -105 O ATOM 137 CB THR A 68 -11.522 41.455 -41.833 1.00112.99 C ANISOU 137 CB THR A 68 16250 11030 15651 -3953 -240 303 C ATOM 138 OG1 THR A 68 -12.944 41.412 -42.009 1.00114.10 O ANISOU 138 OG1 THR A 68 16557 11026 15769 -3597 -370 381 O ATOM 139 CG2 THR A 68 -10.848 40.798 -43.029 1.00113.32 C ANISOU 139 CG2 THR A 68 16188 11366 15502 -4116 -68 473 C ATOM 140 N ALA A 69 -9.208 41.996 -39.792 1.00124.46 N ANISOU 140 N ALA A 69 17320 12600 17369 -4494 -207 -153 N ATOM 141 CA ALA A 69 -7.800 42.228 -39.493 1.00124.07 C ANISOU 141 CA ALA A 69 17061 12682 17396 -4880 -136 -252 C ATOM 142 C ALA A 69 -7.307 41.271 -38.413 1.00121.87 C ANISOU 142 C ALA A 69 16421 12764 17121 -4780 -194 -517 C ATOM 143 O ALA A 69 -6.189 40.761 -38.485 1.00121.72 O ANISOU 143 O ALA A 69 16083 13073 17092 -4969 -105 -562 O ATOM 144 CB ALA A 69 -7.577 43.671 -39.069 1.00 94.06 C ANISOU 144 CB ALA A 69 13515 8456 13769 -5156 -201 -289 C ATOM 145 N ILE A 70 -8.151 41.033 -37.414 1.00114.12 N ANISOU 145 N ILE A 70 15489 11722 16150 -4473 -341 -688 N ATOM 146 CA ILE A 70 -7.826 40.101 -36.340 1.00112.28 C ANISOU 146 CA ILE A 70 14970 11803 15889 -4339 -416 -921 C ATOM 147 C ILE A 70 -7.703 38.677 -36.874 1.00110.94 C ANISOU 147 C ILE A 70 14541 12036 15576 -4161 -324 -858 C ATOM 148 O ILE A 70 -6.750 37.967 -36.551 1.00109.83 O ANISOU 148 O ILE A 70 14086 12223 15423 -4223 -308 -961 O ATOM 149 CB ILE A 70 -8.878 40.146 -35.209 1.00102.10 C ANISOU 149 CB ILE A 70 13832 10353 14609 -4041 -563 -1096 C ATOM 150 CG1 ILE A 70 -8.802 41.478 -34.462 1.00103.43 C ANISOU 150 CG1 ILE A 70 14229 10151 14917 -4223 -660 -1232 C ATOM 151 CG2 ILE A 70 -8.676 38.993 -34.239 1.00 99.66 C ANISOU 151 CG2 ILE A 70 13259 10390 14216 -3861 -629 -1285 C ATOM 152 CD1 ILE A 70 -9.767 41.584 -33.302 1.00103.00 C ANISOU 152 CD1 ILE A 70 14327 9945 14863 -3941 -776 -1433 C ATOM 153 N TYR A 71 -8.664 38.272 -37.700 1.00100.58 N ANISOU 153 N TYR A 71 13366 10690 14159 -3935 -276 -692 N ATOM 154 CA TYR A 71 -8.661 36.934 -38.287 1.00 99.51 C ANISOU 154 CA TYR A 71 13045 10889 13877 -3761 -188 -635 C ATOM 155 C TYR A 71 -7.416 36.677 -39.127 1.00100.61 C ANISOU 155 C TYR A 71 12969 11277 13982 -4012 -17 -554 C ATOM 156 O TYR A 71 -6.787 35.626 -39.007 1.00 99.41 O ANISOU 156 O TYR A 71 12532 11460 13778 -3939 32 -637 O ATOM 157 CB TYR A 71 -9.905 36.708 -39.148 1.00104.70 C ANISOU 157 CB TYR A 71 13916 11437 14428 -3534 -179 -461 C ATOM 158 CG TYR A 71 -11.143 36.320 -38.373 1.00103.72 C ANISOU 158 CG TYR A 71 13863 11246 14298 -3201 -307 -559 C ATOM 159 CD1 TYR A 71 -11.270 36.622 -37.024 1.00102.69 C ANISOU 159 CD1 TYR A 71 13729 11026 14262 -3142 -418 -764 C ATOM 160 CD2 TYR A 71 -12.174 35.623 -38.988 1.00103.77 C ANISOU 160 CD2 TYR A 71 13935 11299 14194 -2961 -310 -454 C ATOM 161 CE1 TYR A 71 -12.400 36.261 -36.316 1.00102.03 C ANISOU 161 CE1 TYR A 71 13703 10902 14163 -2849 -500 -853 C ATOM 162 CE2 TYR A 71 -13.302 35.254 -38.289 1.00102.73 C ANISOU 162 CE2 TYR A 71 13835 11129 14067 -2682 -408 -542 C ATOM 163 CZ TYR A 71 -13.413 35.577 -36.955 1.00102.15 C ANISOU 163 CZ TYR A 71 13754 10971 14089 -2625 -487 -738 C ATOM 164 OH TYR A 71 -14.540 35.211 -36.257 1.00101.39 O ANISOU 164 OH TYR A 71 13683 10853 13988 -2359 -551 -824 O ATOM 165 N LEU A 72 -7.070 37.638 -39.979 1.00131.47 N ANISOU 165 N LEU A 72 17021 15014 17918 -4299 84 -389 N ATOM 166 CA LEU A 72 -5.903 37.514 -40.847 1.00132.89 C ANISOU 166 CA LEU A 72 17008 15422 18062 -4572 287 -299 C ATOM 167 C LEU A 72 -4.622 37.399 -40.029 1.00132.47 C ANISOU 167 C LEU A 72 16590 15609 18134 -4759 281 -491 C ATOM 168 O LEU A 72 -3.718 36.639 -40.379 1.00132.68 O ANISOU 168 O LEU A 72 16304 15985 18125 -4802 419 -511 O ATOM 169 CB LEU A 72 -5.810 38.704 -41.805 1.00 94.76 C ANISOU 169 CB LEU A 72 12444 10319 13240 -4880 390 -76 C ATOM 170 CG LEU A 72 -6.891 38.818 -42.883 1.00 95.92 C ANISOU 170 CG LEU A 72 12936 10277 13235 -4734 409 163 C ATOM 171 CD1 LEU A 72 -6.652 40.047 -43.746 1.00 98.39 C ANISOU 171 CD1 LEU A 72 13523 10307 13553 -5070 504 393 C ATOM 172 CD2 LEU A 72 -6.946 37.559 -43.736 1.00 95.56 C ANISOU 172 CD2 LEU A 72 12768 10562 12980 -4557 536 221 C ATOM 173 N ALA A 73 -4.551 38.158 -38.940 1.00103.95 N ANISOU 173 N ALA A 73 13018 11811 14668 -4861 115 -641 N ATOM 174 CA ALA A 73 -3.398 38.111 -38.049 1.00103.26 C ANISOU 174 CA ALA A 73 12594 11940 14699 -5041 52 -838 C ATOM 175 C ALA A 73 -3.312 36.754 -37.358 1.00101.50 C ANISOU 175 C ALA A 73 12096 12058 14412 -4719 -28 -992 C ATOM 176 O ALA A 73 -2.243 36.150 -37.287 1.00101.57 O ANISOU 176 O ALA A 73 11730 12410 14450 -4781 19 -1065 O ATOM 177 CB ALA A 73 -3.469 39.234 -37.024 1.00 89.71 C ANISOU 177 CB ALA A 73 11046 9917 13123 -5210 -131 -977 C ATOM 178 N LEU A 74 -4.447 36.278 -36.855 1.00124.49 N ANISOU 178 N LEU A 74 15190 14870 17241 -4371 -146 -1035 N ATOM 179 CA LEU A 74 -4.509 34.968 -36.217 1.00122.79 C ANISOU 179 CA LEU A 74 14782 14927 16945 -4055 -220 -1153 C ATOM 180 C LEU A 74 -4.282 33.857 -37.237 1.00123.19 C ANISOU 180 C LEU A 74 14674 15247 16886 -3920 -42 -1045 C ATOM 181 O LEU A 74 -3.822 32.769 -36.890 1.00122.55 O ANISOU 181 O LEU A 74 14343 15451 16770 -3740 -60 -1136 O ATOM 182 CB LEU A 74 -5.852 34.772 -35.512 1.00 94.55 C ANISOU 182 CB LEU A 74 11461 11163 13301 -3750 -353 -1206 C ATOM 183 CG LEU A 74 -6.135 35.695 -34.325 1.00 94.30 C ANISOU 183 CG LEU A 74 11590 10891 13350 -3812 -528 -1362 C ATOM 184 CD1 LEU A 74 -7.543 35.475 -33.794 1.00 93.26 C ANISOU 184 CD1 LEU A 74 11700 10591 13142 -3498 -602 -1395 C ATOM 185 CD2 LEU A 74 -5.103 35.491 -33.226 1.00 94.14 C ANISOU 185 CD2 LEU A 74 11308 11091 13370 -3901 -665 -1562 C ATOM 186 N PHE A 75 -4.609 34.137 -38.494 1.00111.14 N ANISOU 186 N PHE A 75 13319 13617 15294 -3999 123 -853 N ATOM 187 CA PHE A 75 -4.356 33.194 -39.577 1.00112.10 C ANISOU 187 CA PHE A 75 13327 13976 15288 -3910 317 -756 C ATOM 188 C PHE A 75 -2.861 33.031 -39.809 1.00114.05 C ANISOU 188 C PHE A 75 13196 14532 15606 -4115 459 -801 C ATOM 189 O PHE A 75 -2.341 31.918 -39.787 1.00113.87 O ANISOU 189 O PHE A 75 12911 14807 15548 -3932 510 -878 O ATOM 190 CB PHE A 75 -5.033 33.660 -40.868 1.00 97.25 C ANISOU 190 CB PHE A 75 11748 11906 13295 -3981 445 -534 C ATOM 191 CG PHE A 75 -4.775 32.766 -42.047 1.00 98.53 C ANISOU 191 CG PHE A 75 11839 12302 13295 -3916 656 -443 C ATOM 192 CD1 PHE A 75 -5.506 31.602 -42.225 1.00 97.99 C ANISOU 192 CD1 PHE A 75 11828 12318 13086 -3593 637 -460 C ATOM 193 CD2 PHE A 75 -3.809 33.094 -42.985 1.00101.11 C ANISOU 193 CD2 PHE A 75 12056 12760 13602 -4195 887 -347 C ATOM 194 CE1 PHE A 75 -5.270 30.779 -43.312 1.00 99.94 C ANISOU 194 CE1 PHE A 75 12042 12763 13170 -3535 831 -400 C ATOM 195 CE2 PHE A 75 -3.570 32.275 -44.073 1.00102.98 C ANISOU 195 CE2 PHE A 75 12246 13216 13666 -4129 1103 -282 C ATOM 196 CZ PHE A 75 -4.302 31.116 -44.237 1.00102.25 C ANISOU 196 CZ PHE A 75 12231 13191 13428 -3791 1068 -316 C ATOM 197 N VAL A 76 -2.177 34.150 -40.025 1.00120.83 N ANISOU 197 N VAL A 76 14023 15313 16575 -4494 526 -753 N ATOM 198 CA VAL A 76 -0.739 34.141 -40.269 1.00122.74 C ANISOU 198 CA VAL A 76 13873 15853 16908 -4744 677 -790 C ATOM 199 C VAL A 76 0.021 33.546 -39.087 1.00122.04 C ANISOU 199 C VAL A 76 13407 16026 16935 -4636 511 -1009 C ATOM 200 O VAL A 76 0.857 32.661 -39.260 1.00123.20 O ANISOU 200 O VAL A 76 13199 16523 17090 -4537 612 -1066 O ATOM 201 CB VAL A 76 -0.208 35.557 -40.565 1.00112.70 C ANISOU 201 CB VAL A 76 12661 14406 15753 -5218 751 -704 C ATOM 202 CG1 VAL A 76 1.309 35.547 -40.668 1.00114.53 C ANISOU 202 CG1 VAL A 76 12425 14982 16111 -5498 895 -768 C ATOM 203 CG2 VAL A 76 -0.828 36.097 -41.845 1.00114.04 C ANISOU 203 CG2 VAL A 76 13197 14345 15787 -5329 929 -457 C ATOM 204 N VAL A 77 -0.281 34.031 -37.887 1.00136.00 N ANISOU 204 N VAL A 77 15267 17624 18783 -4638 253 -1132 N ATOM 205 CA VAL A 77 0.353 33.527 -36.674 1.00135.42 C ANISOU 205 CA VAL A 77 14889 17775 18789 -4533 48 -1333 C ATOM 206 C VAL A 77 0.031 32.050 -36.464 1.00134.75 C ANISOU 206 C VAL A 77 14732 17882 18586 -4086 11 -1376 C ATOM 207 O VAL A 77 0.912 31.249 -36.145 1.00135.39 O ANISOU 207 O VAL A 77 14448 18283 18709 -3969 -18 -1470 O ATOM 208 CB VAL A 77 -0.087 34.331 -35.432 1.00104.18 C ANISOU 208 CB VAL A 77 11132 13563 14888 -4601 -221 -1460 C ATOM 209 CG1 VAL A 77 0.386 33.653 -34.155 1.00103.47 C ANISOU 209 CG1 VAL A 77 10793 13706 14815 -4427 -459 -1655 C ATOM 210 CG2 VAL A 77 0.437 35.756 -35.511 1.00105.84 C ANISOU 210 CG2 VAL A 77 11378 13593 15243 -5070 -209 -1454 C ATOM 211 N GLY A 78 -1.233 31.694 -36.663 1.00112.13 N ANISOU 211 N GLY A 78 12212 14812 15579 -3838 11 -1301 N ATOM 212 CA GLY A 78 -1.682 30.331 -36.453 1.00110.70 C ANISOU 212 CA GLY A 78 12029 14753 15280 -3440 -27 -1333 C ATOM 213 C GLY A 78 -1.157 29.349 -37.483 1.00112.25 C ANISOU 213 C GLY A 78 12033 15201 15418 -3318 195 -1277 C ATOM 214 O GLY A 78 -0.707 28.258 -37.133 1.00112.24 O ANISOU 214 O GLY A 78 11814 15426 15406 -3069 157 -1360 O ATOM 215 N THR A 79 -1.219 29.731 -38.756 1.00112.47 N ANISOU 215 N THR A 79 12162 15177 15393 -3482 426 -1135 N ATOM 216 CA THR A 79 -0.772 28.856 -39.835 1.00114.78 C ANISOU 216 CA THR A 79 12318 15695 15598 -3379 671 -1089 C ATOM 217 C THR A 79 0.732 28.618 -39.771 1.00117.47 C ANISOU 217 C THR A 79 12174 16386 16072 -3460 762 -1183 C ATOM 218 O THR A 79 1.186 27.477 -39.809 1.00118.78 O ANISOU 218 O THR A 79 12125 16787 16220 -3191 813 -1257 O ATOM 219 CB THR A 79 -1.142 29.417 -41.223 1.00129.39 C ANISOU 219 CB THR A 79 14410 17419 17332 -3571 901 -908 C ATOM 220 OG1 THR A 79 -2.557 29.631 -41.294 1.00127.74 O ANISOU 220 OG1 THR A 79 14620 16902 17014 -3473 792 -818 O ATOM 221 CG2 THR A 79 -0.725 28.451 -42.320 1.00131.91 C ANISOU 221 CG2 THR A 79 14621 17975 17523 -3446 1163 -885 C ATOM 222 N VAL A 80 1.499 29.700 -39.672 1.00119.00 N ANISOU 222 N VAL A 80 12193 16608 16413 -3830 779 -1184 N ATOM 223 CA VAL A 80 2.952 29.601 -39.571 1.00121.47 C ANISOU 223 CA VAL A 80 11995 17273 16884 -3953 852 -1278 C ATOM 224 C VAL A 80 3.380 28.906 -38.282 1.00121.10 C ANISOU 224 C VAL A 80 11677 17402 16933 -3705 580 -1449 C ATOM 225 O VAL A 80 4.262 28.046 -38.296 1.00122.84 O ANISOU 225 O VAL A 80 11517 17944 17214 -3523 634 -1528 O ATOM 226 CB VAL A 80 3.619 30.991 -39.640 1.00 94.43 C ANISOU 226 CB VAL A 80 8459 13812 13608 -4454 897 -1245 C ATOM 227 CG1 VAL A 80 5.113 30.885 -39.370 1.00 98.56 C ANISOU 227 CG1 VAL A 80 8397 14728 14325 -4589 930 -1364 C ATOM 228 CG2 VAL A 80 3.357 31.639 -40.992 1.00 95.38 C ANISOU 228 CG2 VAL A 80 8828 13789 13624 -4710 1191 -1052 C ATOM 229 N GLY A 81 2.738 29.273 -37.177 1.00111.23 N ANISOU 229 N GLY A 81 10640 15937 15686 -3680 289 -1504 N ATOM 230 CA GLY A 81 3.061 28.719 -35.874 1.00110.79 C ANISOU 230 CA GLY A 81 10396 16016 15682 -3470 -1 -1652 C ATOM 231 C GLY A 81 2.959 27.208 -35.801 1.00111.24 C ANISOU 231 C GLY A 81 10399 16218 15648 -3008 -12 -1678 C ATOM 232 O GLY A 81 3.881 26.540 -35.334 1.00112.46 O ANISOU 232 O GLY A 81 10182 16658 15890 -2846 -103 -1772 O ATOM 233 N ASN A 82 1.841 26.666 -36.271 1.00130.48 N ANISOU 233 N ASN A 82 13208 18453 17916 -2797 72 -1594 N ATOM 234 CA ASN A 82 1.608 25.229 -36.212 1.00130.81 C ANISOU 234 CA ASN A 82 13276 18567 17859 -2375 62 -1615 C ATOM 235 C ASN A 82 2.353 24.472 -37.307 1.00133.67 C ANISOU 235 C ASN A 82 13393 19165 18228 -2260 338 -1605 C ATOM 236 O ASN A 82 2.600 23.272 -37.185 1.00134.90 O ANISOU 236 O ASN A 82 13443 19449 18362 -1912 325 -1658 O ATOM 237 CB ASN A 82 0.112 24.921 -36.280 1.00100.26 C ANISOU 237 CB ASN A 82 9886 14396 13814 -2220 40 -1541 C ATOM 238 CG ASN A 82 -0.662 25.540 -35.134 1.00 97.27 C ANISOU 238 CG ASN A 82 9740 13799 13418 -2276 -211 -1570 C ATOM 239 OD1 ASN A 82 -0.696 24.999 -34.029 1.00 96.52 O ANISOU 239 OD1 ASN A 82 9637 13735 13300 -2080 -427 -1646 O ATOM 240 ND2 ASN A 82 -1.291 26.680 -35.393 1.00 95.79 N ANISOU 240 ND2 ASN A 82 9781 13383 13231 -2534 -179 -1509 N ATOM 241 N SER A 83 2.709 25.179 -38.373 1.00110.50 N ANISOU 241 N SER A 83 10390 16279 15318 -2549 598 -1538 N ATOM 242 CA SER A 83 3.411 24.568 -39.496 1.00113.73 C ANISOU 242 CA SER A 83 10582 16919 15710 -2473 909 -1535 C ATOM 243 C SER A 83 4.837 24.194 -39.117 1.00116.70 C ANISOU 243 C SER A 83 10397 17667 16277 -2395 899 -1656 C ATOM 244 O SER A 83 5.245 23.042 -39.268 1.00118.73 O ANISOU 244 O SER A 83 10485 18094 16531 -2047 967 -1722 O ATOM 245 CB SER A 83 3.418 25.503 -40.706 1.00 98.83 C ANISOU 245 CB SER A 83 8790 14988 13774 -2837 1195 -1415 C ATOM 246 OG SER A 83 2.097 25.821 -41.107 1.00 97.23 O ANISOU 246 OG SER A 83 9092 14454 13397 -2877 1185 -1295 O ATOM 247 N VAL A 84 5.594 25.170 -38.626 1.00115.47 N ANISOU 247 N VAL A 84 9948 17629 16296 -2716 805 -1689 N ATOM 248 CA VAL A 84 6.976 24.924 -38.230 1.00117.76 C ANISOU 248 CA VAL A 84 9651 18301 16793 -2678 765 -1806 C ATOM 249 C VAL A 84 7.057 24.215 -36.880 1.00117.10 C ANISOU 249 C VAL A 84 9474 18265 16755 -2350 389 -1905 C ATOM 250 O VAL A 84 8.139 23.825 -36.440 1.00119.66 O ANISOU 250 O VAL A 84 9318 18907 17241 -2226 293 -2003 O ATOM 251 CB VAL A 84 7.808 26.223 -38.198 1.00146.96 C ANISOU 251 CB VAL A 84 13042 22126 20670 -3181 791 -1813 C ATOM 252 CG1 VAL A 84 7.947 26.798 -39.599 1.00148.30 C ANISOU 252 CG1 VAL A 84 13244 22307 20794 -3491 1202 -1703 C ATOM 253 CG2 VAL A 84 7.177 27.235 -37.266 1.00144.89 C ANISOU 253 CG2 VAL A 84 13066 21579 20408 -3431 494 -1805 C ATOM 254 N THR A 85 5.910 24.052 -36.227 1.00115.66 N ANISOU 254 N THR A 85 9746 17777 16423 -2210 176 -1874 N ATOM 255 CA THR A 85 5.828 23.222 -35.033 1.00115.09 C ANISOU 255 CA THR A 85 9682 17716 16332 -1861 -148 -1941 C ATOM 256 C THR A 85 5.794 21.760 -35.458 1.00117.12 C ANISOU 256 C THR A 85 9959 18024 16517 -1401 -33 -1942 C ATOM 257 O THR A 85 6.470 20.915 -34.872 1.00118.99 O ANISOU 257 O THR A 85 9931 18452 16829 -1087 -188 -2010 O ATOM 258 CB THR A 85 4.578 23.543 -34.192 1.00108.33 C ANISOU 258 CB THR A 85 9315 16517 15327 -1882 -378 -1907 C ATOM 259 OG1 THR A 85 4.638 24.902 -33.743 1.00106.94 O ANISOU 259 OG1 THR A 85 9138 16271 15222 -2289 -494 -1930 O ATOM 260 CG2 THR A 85 4.494 22.624 -32.983 1.00108.11 C ANISOU 260 CG2 THR A 85 9327 16506 15244 -1525 -688 -1958 C ATOM 261 N LEU A 86 5.014 21.474 -36.497 1.00132.33 N ANISOU 261 N LEU A 86 12212 19771 18296 -1363 231 -1867 N ATOM 262 CA LEU A 86 4.947 20.133 -37.064 1.00134.78 C ANISOU 262 CA LEU A 86 12588 20097 18526 -966 380 -1880 C ATOM 263 C LEU A 86 6.288 19.730 -37.658 1.00138.96 C ANISOU 263 C LEU A 86 12607 20984 19209 -854 587 -1961 C ATOM 264 O LEU A 86 6.699 18.576 -37.556 1.00141.27 O ANISOU 264 O LEU A 86 12768 21377 19529 -446 573 -2024 O ATOM 265 CB LEU A 86 3.860 20.043 -38.136 1.00119.26 C ANISOU 265 CB LEU A 86 11070 17880 16362 -1013 618 -1795 C ATOM 266 CG LEU A 86 2.404 20.044 -37.671 1.00116.48 C ANISOU 266 CG LEU A 86 11231 17177 15847 -999 447 -1723 C ATOM 267 CD1 LEU A 86 1.470 20.066 -38.867 1.00116.39 C ANISOU 267 CD1 LEU A 86 11582 16977 15663 -1086 684 -1640 C ATOM 268 CD2 LEU A 86 2.128 18.830 -36.801 1.00116.86 C ANISOU 268 CD2 LEU A 86 11400 17152 15849 -603 237 -1759 C ATOM 269 N PHE A 87 6.962 20.690 -38.282 1.00140.76 N ANISOU 269 N PHE A 87 12550 21394 19539 -1216 790 -1956 N ATOM 270 CA PHE A 87 8.264 20.447 -38.885 1.00143.65 C ANISOU 270 CA PHE A 87 12382 22136 20064 -1166 1029 -2035 C ATOM 271 C PHE A 87 9.277 20.065 -37.811 1.00144.80 C ANISOU 271 C PHE A 87 12043 22553 20420 -948 745 -2138 C ATOM 272 O PHE A 87 10.141 19.217 -38.030 1.00147.84 O ANISOU 272 O PHE A 87 12059 23197 20917 -628 847 -2222 O ATOM 273 CB PHE A 87 8.738 21.693 -39.633 1.00207.93 C ANISOU 273 CB PHE A 87 20329 30404 28272 -1673 1279 -1992 C ATOM 274 CG PHE A 87 8.020 21.931 -40.930 1.00208.19 C ANISOU 274 CG PHE A 87 20750 30257 28097 -1841 1620 -1890 C ATOM 275 CD1 PHE A 87 7.515 20.872 -41.666 1.00209.83 C ANISOU 275 CD1 PHE A 87 21230 30370 28124 -1511 1801 -1897 C ATOM 276 CD2 PHE A 87 7.838 23.219 -41.405 1.00207.33 C ANISOU 276 CD2 PHE A 87 20758 30055 27962 -2332 1740 -1785 C ATOM 277 CE1 PHE A 87 6.848 21.094 -42.857 1.00209.73 C ANISOU 277 CE1 PHE A 87 21586 30205 27896 -1672 2084 -1805 C ATOM 278 CE2 PHE A 87 7.172 23.448 -42.594 1.00207.06 C ANISOU 278 CE2 PHE A 87 21099 29857 27717 -2477 2024 -1673 C ATOM 279 CZ PHE A 87 6.676 22.384 -43.321 1.00207.99 C ANISOU 279 CZ PHE A 87 21472 29912 27642 -2148 2190 -1686 C ATOM 280 N THR A 88 9.156 20.699 -36.649 1.00146.70 N ANISOU 280 N THR A 88 12298 22733 20709 -1111 381 -2135 N ATOM 281 CA THR A 88 10.025 20.416 -35.512 1.00147.88 C ANISOU 281 CA THR A 88 12038 23125 21027 -930 40 -2222 C ATOM 282 C THR A 88 9.724 19.046 -34.909 1.00148.84 C ANISOU 282 C THR A 88 12339 23149 21064 -377 -161 -2231 C ATOM 283 O THR A 88 10.632 18.302 -34.537 1.00151.34 O ANISOU 283 O THR A 88 12261 23720 21523 -43 -282 -2301 O ATOM 284 CB THR A 88 9.880 21.494 -34.420 1.00170.37 C ANISOU 284 CB THR A 88 14932 25900 23900 -1276 -304 -2225 C ATOM 285 OG1 THR A 88 10.192 22.780 -34.971 1.00170.26 O ANISOU 285 OG1 THR A 88 14768 25945 23977 -1805 -122 -2213 O ATOM 286 CG2 THR A 88 10.812 21.208 -33.256 1.00171.63 C ANISOU 286 CG2 THR A 88 14664 26335 24211 -1101 -684 -2316 C ATOM 287 N LEU A 89 8.440 18.719 -34.821 1.00155.18 N ANISOU 287 N LEU A 89 13740 23578 21644 -284 -197 -2154 N ATOM 288 CA LEU A 89 8.002 17.441 -34.269 1.00155.78 C ANISOU 288 CA LEU A 89 14077 23499 21615 192 -371 -2141 C ATOM 289 C LEU A 89 8.222 16.288 -35.245 1.00158.91 C ANISOU 289 C LEU A 89 14448 23925 22006 562 -81 -2172 C ATOM 290 O LEU A 89 8.173 15.121 -34.855 1.00160.66 O ANISOU 290 O LEU A 89 14782 24066 22194 1001 -207 -2178 O ATOM 291 CB LEU A 89 6.529 17.510 -33.858 1.00139.39 C ANISOU 291 CB LEU A 89 12630 21024 19310 126 -484 -2053 C ATOM 292 CG LEU A 89 6.175 18.543 -32.785 1.00136.49 C ANISOU 292 CG LEU A 89 12368 20578 18913 -179 -778 -2039 C ATOM 293 CD1 LEU A 89 4.676 18.559 -32.526 1.00133.72 C ANISOU 293 CD1 LEU A 89 12619 19847 18342 -219 -820 -1959 C ATOM 294 CD2 LEU A 89 6.947 18.280 -31.499 1.00137.20 C ANISOU 294 CD2 LEU A 89 12185 20861 19083 2 -1163 -2091 C ATOM 295 N ALA A 90 8.468 16.615 -36.510 1.00148.27 N ANISOU 295 N ALA A 90 12977 22680 20679 382 310 -2191 N ATOM 296 CA ALA A 90 8.672 15.591 -37.530 1.00151.11 C ANISOU 296 CA ALA A 90 13336 23069 21011 705 626 -2244 C ATOM 297 C ALA A 90 10.154 15.335 -37.771 1.00154.58 C ANISOU 297 C ALA A 90 13115 23928 21691 883 751 -2356 C ATOM 298 O ALA A 90 10.532 14.291 -38.304 1.00157.33 O ANISOU 298 O ALA A 90 13384 24334 22061 1280 935 -2431 O ATOM 299 CB ALA A 90 7.983 15.982 -38.828 1.00142.77 C ANISOU 299 CB ALA A 90 12595 21868 19785 438 996 -2200 C ATOM 300 N ARG A 91 10.994 16.286 -37.373 1.00234.44 N ANISOU 300 N ARG A 91 22749 34334 31994 590 651 -2378 N ATOM 301 CA ARG A 91 12.435 16.074 -37.409 1.00237.82 C ANISOU 301 CA ARG A 91 22476 35200 32686 756 707 -2486 C ATOM 302 C ARG A 91 12.895 15.464 -36.089 1.00238.64 C ANISOU 302 C ARG A 91 22370 35391 32911 1122 248 -2513 C ATOM 303 O ARG A 91 14.083 15.471 -35.766 1.00241.09 O ANISOU 303 O ARG A 91 22054 36083 33467 1220 148 -2591 O ATOM 304 CB ARG A 91 13.187 17.374 -37.703 1.00186.20 C ANISOU 304 CB ARG A 91 15479 28962 26306 232 844 -2501 C ATOM 305 CG ARG A 91 13.028 18.457 -36.652 1.00183.84 C ANISOU 305 CG ARG A 91 15190 28618 26041 -160 472 -2456 C ATOM 306 CD ARG A 91 13.907 19.653 -36.979 1.00184.77 C ANISOU 306 CD ARG A 91 14815 29044 26347 -670 620 -2484 C ATOM 307 NE ARG A 91 13.646 20.165 -38.321 1.00184.93 N ANISOU 307 NE ARG A 91 14995 29004 26266 -984 1097 -2431 N ATOM 308 CZ ARG A 91 14.401 21.069 -38.937 1.00185.90 C ANISOU 308 CZ ARG A 91 14726 29384 26521 -1416 1360 -2439 C ATOM 309 NH1 ARG A 91 15.474 21.563 -38.333 1.00187.28 N ANISOU 309 NH1 ARG A 91 14293 29904 26959 -1599 1189 -2513 N ATOM 310 NH2 ARG A 91 14.086 21.478 -40.158 1.00185.71 N ANISOU 310 NH2 ARG A 91 14925 29277 26360 -1681 1788 -2369 N ATOM 311 N LYS A 92 11.933 14.947 -35.331 1.00245.10 N ANISOU 311 N LYS A 92 23715 35861 33549 1315 -34 -2439 N ATOM 312 CA LYS A 92 12.214 14.206 -34.110 1.00246.08 C ANISOU 312 CA LYS A 92 23772 36004 33725 1711 -465 -2435 C ATOM 313 C LYS A 92 13.077 13.000 -34.456 1.00249.83 C ANISOU 313 C LYS A 92 23920 36656 34349 2269 -360 -2517 C ATOM 314 O LYS A 92 12.772 12.265 -35.396 1.00250.01 O ANISOU 314 O LYS A 92 24175 36527 34291 2488 -31 -2543 O ATOM 315 CB LYS A 92 10.907 13.757 -33.453 1.00180.64 C ANISOU 315 CB LYS A 92 16185 27273 25177 1815 -682 -2330 C ATOM 316 CG LYS A 92 11.085 12.999 -32.148 1.00180.85 C ANISOU 316 CG LYS A 92 16238 27274 25201 2201 -1134 -2295 C ATOM 317 CD LYS A 92 9.740 12.644 -31.530 1.00177.31 C ANISOU 317 CD LYS A 92 16496 26394 24482 2232 -1300 -2183 C ATOM 318 CE LYS A 92 8.937 11.719 -32.430 1.00176.87 C ANISOU 318 CE LYS A 92 16891 26023 24289 2443 -998 -2160 C ATOM 319 NZ LYS A 92 9.610 10.403 -32.610 1.00179.63 N ANISOU 319 NZ LYS A 92 17098 26414 24741 3007 -973 -2204 N ATOM 320 N LYS A 93 14.155 12.816 -33.699 1.00216.67 N ANISOU 320 N LYS A 93 19181 32777 30366 2500 -647 -2565 N ATOM 321 CA LYS A 93 15.144 11.771 -33.963 1.00219.79 C ANISOU 321 CA LYS A 93 19151 33399 30959 3049 -572 -2654 C ATOM 322 C LYS A 93 14.521 10.394 -34.177 1.00219.96 C ANISOU 322 C LYS A 93 19686 33054 30836 3567 -505 -2630 C ATOM 323 O LYS A 93 14.478 9.892 -35.300 1.00221.52 O ANISOU 323 O LYS A 93 19963 33193 31013 3713 -86 -2701 O ATOM 324 CB LYS A 93 16.153 11.701 -32.817 1.00183.82 C ANISOU 324 CB LYS A 93 14066 29164 26614 3263 -1036 -2671 C ATOM 325 CG LYS A 93 15.520 11.383 -31.474 1.00181.68 C ANISOU 325 CG LYS A 93 14237 28626 26168 3408 -1548 -2553 C ATOM 326 CD LYS A 93 16.568 11.101 -30.412 1.00183.41 C ANISOU 326 CD LYS A 93 13949 29164 26576 3722 -2017 -2566 C ATOM 327 CE LYS A 93 15.914 10.729 -29.093 1.00181.20 C ANISOU 327 CE LYS A 93 14167 28607 26075 3876 -2511 -2435 C ATOM 328 NZ LYS A 93 14.979 9.579 -29.246 1.00180.21 N ANISOU 328 NZ LYS A 93 14716 28014 25743 4254 -2415 -2346 N ATOM 329 N SER A 97 10.993 7.651 -25.786 1.00170.18 N ANISOU 329 N SER A 97 16113 25207 23341 4583 -3386 -1762 N ATOM 330 CA SER A 97 10.561 7.802 -24.402 1.00169.32 C ANISOU 330 CA SER A 97 16334 25007 22992 4502 -3807 -1641 C ATOM 331 C SER A 97 9.260 8.594 -24.303 1.00165.96 C ANISOU 331 C SER A 97 16398 24338 22321 3991 -3670 -1613 C ATOM 332 O SER A 97 8.538 8.752 -25.288 1.00164.92 O ANISOU 332 O SER A 97 16463 24021 22176 3784 -3272 -1648 O ATOM 333 CB SER A 97 11.654 8.472 -23.566 1.00151.76 C ANISOU 333 CB SER A 97 13554 23221 20887 4450 -4211 -1690 C ATOM 334 OG SER A 97 11.861 9.810 -23.980 1.00149.99 O ANISOU 334 OG SER A 97 12962 23249 20776 3931 -4060 -1824 O ATOM 335 N LEU A 98 8.972 9.093 -23.105 1.00218.15 N ANISOU 335 N LEU A 98 23197 30958 28732 3802 -4008 -1554 N ATOM 336 CA LEU A 98 7.726 9.806 -22.833 1.00215.62 C ANISOU 336 CA LEU A 98 23353 30405 28168 3368 -3914 -1527 C ATOM 337 C LEU A 98 7.622 11.111 -23.619 1.00212.95 C ANISOU 337 C LEU A 98 22772 30193 27948 2871 -3637 -1661 C ATOM 338 O LEU A 98 6.531 11.523 -24.011 1.00209.85 O ANISOU 338 O LEU A 98 22741 29557 27433 2578 -3381 -1652 O ATOM 339 CB LEU A 98 7.566 10.052 -21.322 1.00193.39 C ANISOU 339 CB LEU A 98 20768 27609 25105 3302 -4347 -1456 C ATOM 340 CG LEU A 98 8.365 11.079 -20.497 1.00192.72 C ANISOU 340 CG LEU A 98 20293 27885 25048 3072 -4699 -1548 C ATOM 341 CD1 LEU A 98 9.867 11.035 -20.778 1.00195.31 C ANISOU 341 CD1 LEU A 98 19900 28617 25693 3280 -4843 -1635 C ATOM 342 CD2 LEU A 98 7.824 12.502 -20.650 1.00189.26 C ANISOU 342 CD2 LEU A 98 19876 27454 24578 2496 -4536 -1663 C ATOM 343 N GLN A 99 8.764 11.750 -23.846 1.00258.81 N ANISOU 343 N GLN A 99 27959 36379 33999 2779 -3692 -1777 N ATOM 344 CA GLN A 99 8.825 12.978 -24.633 1.00256.83 C ANISOU 344 CA GLN A 99 27441 36260 33884 2311 -3429 -1894 C ATOM 345 C GLN A 99 8.470 12.694 -26.094 1.00257.17 C ANISOU 345 C GLN A 99 27535 36162 34015 2321 -2942 -1909 C ATOM 346 O GLN A 99 7.987 13.571 -26.804 1.00255.21 O ANISOU 346 O GLN A 99 27339 35856 33775 1929 -2666 -1951 O ATOM 347 CB GLN A 99 10.231 13.584 -24.546 1.00167.36 C ANISOU 347 CB GLN A 99 15396 25383 22809 2231 -3601 -2008 C ATOM 348 CG GLN A 99 10.456 14.837 -25.401 1.00165.75 C ANISOU 348 CG GLN A 99 14871 25333 22774 1739 -3321 -2121 C ATOM 349 CD GLN A 99 11.747 15.571 -25.049 1.00167.20 C ANISOU 349 CD GLN A 99 14394 25955 23179 1566 -3558 -2232 C ATOM 350 OE1 GLN A 99 12.186 16.467 -25.774 1.00167.30 O ANISOU 350 OE1 GLN A 99 14047 26145 23375 1205 -3335 -2320 O ATOM 351 NE2 GLN A 99 12.353 15.196 -23.928 1.00168.49 N ANISOU 351 NE2 GLN A 99 14404 26296 23319 1808 -4020 -2221 N ATOM 352 N SER A 100 8.734 11.476 -26.553 1.00173.17 N ANISOU 352 N SER A 100 16892 25465 23439 2775 -2843 -1879 N ATOM 353 CA SER A 100 8.421 11.117 -27.932 1.00173.38 C ANISOU 353 CA SER A 100 16996 25358 23521 2810 -2391 -1909 C ATOM 354 C SER A 100 6.920 10.941 -28.189 1.00170.80 C ANISOU 354 C SER A 100 17332 24610 22956 2670 -2204 -1830 C ATOM 355 O SER A 100 6.415 11.333 -29.245 1.00169.06 O ANISOU 355 O SER A 100 17200 24302 22733 2429 -1856 -1864 O ATOM 356 CB SER A 100 9.189 9.859 -28.348 1.00227.65 C ANISOU 356 CB SER A 100 23671 32287 30539 3356 -2336 -1928 C ATOM 357 OG SER A 100 8.906 9.495 -29.688 1.00228.44 O ANISOU 357 OG SER A 100 23869 32260 30669 3390 -1896 -1978 O ATOM 358 N THR A 101 6.216 10.341 -27.232 1.00160.91 N ANISOU 358 N THR A 101 16534 23108 21497 2818 -2437 -1719 N ATOM 359 CA THR A 101 4.768 10.174 -27.340 1.00159.07 C ANISOU 359 CA THR A 101 16901 22496 21041 2670 -2288 -1641 C ATOM 360 C THR A 101 3.993 11.491 -27.276 1.00154.83 C ANISOU 360 C THR A 101 16480 21931 20418 2161 -2224 -1659 C ATOM 361 O THR A 101 2.993 11.653 -27.978 1.00153.58 O ANISOU 361 O THR A 101 16618 21557 20179 1965 -1962 -1644 O ATOM 362 CB THR A 101 4.224 9.231 -26.248 1.00130.08 C ANISOU 362 CB THR A 101 13682 18579 17164 2925 -2548 -1507 C ATOM 363 OG1 THR A 101 4.387 9.837 -24.960 1.00128.95 O ANISOU 363 OG1 THR A 101 13505 18569 16923 2805 -2901 -1479 O ATOM 364 CG2 THR A 101 4.958 7.896 -26.273 1.00133.98 C ANISOU 364 CG2 THR A 101 14114 19049 17744 3460 -2633 -1474 C ATOM 365 N VAL A 102 4.438 12.421 -26.432 1.00139.19 N ANISOU 365 N VAL A 102 14277 20158 18453 1956 -2474 -1696 N ATOM 366 CA VAL A 102 3.743 13.701 -26.301 1.00135.33 C ANISOU 366 CA VAL A 102 13911 19620 17890 1495 -2428 -1726 C ATOM 367 C VAL A 102 3.863 14.511 -27.588 1.00134.26 C ANISOU 367 C VAL A 102 13541 19561 17912 1212 -2097 -1798 C ATOM 368 O VAL A 102 3.023 15.364 -27.870 1.00131.32 O ANISOU 368 O VAL A 102 13375 19045 17475 878 -1954 -1798 O ATOM 369 CB VAL A 102 4.249 14.540 -25.101 1.00133.44 C ANISOU 369 CB VAL A 102 13499 19576 17625 1326 -2779 -1774 C ATOM 370 CG1 VAL A 102 4.010 13.801 -23.792 1.00134.35 C ANISOU 370 CG1 VAL A 102 13921 19599 17525 1574 -3106 -1686 C ATOM 371 CG2 VAL A 102 5.713 14.904 -25.261 1.00135.69 C ANISOU 371 CG2 VAL A 102 13158 20241 18157 1329 -2882 -1870 C ATOM 372 N ASP A 103 4.912 14.243 -28.361 1.00147.34 N ANISOU 372 N ASP A 103 14768 21445 19770 1355 -1972 -1855 N ATOM 373 CA ASP A 103 5.098 14.895 -29.653 1.00147.05 C ANISOU 373 CA ASP A 103 14516 21494 19862 1108 -1628 -1910 C ATOM 374 C ASP A 103 3.969 14.517 -30.607 1.00146.31 C ANISOU 374 C ASP A 103 14849 21102 19640 1093 -1322 -1857 C ATOM 375 O ASP A 103 3.557 15.321 -31.444 1.00144.99 O ANISOU 375 O ASP A 103 14726 20889 19474 777 -1085 -1863 O ATOM 376 CB ASP A 103 6.459 14.539 -30.253 1.00152.34 C ANISOU 376 CB ASP A 103 14638 22484 20760 1308 -1533 -1986 C ATOM 377 CG ASP A 103 7.598 15.302 -29.603 1.00152.84 C ANISOU 377 CG ASP A 103 14180 22898 20994 1164 -1773 -2058 C ATOM 378 OD1 ASP A 103 7.390 15.866 -28.508 1.00150.70 O ANISOU 378 OD1 ASP A 103 14015 22606 20638 1001 -2079 -2049 O ATOM 379 OD2 ASP A 103 8.700 15.341 -30.189 1.00154.56 O ANISOU 379 OD2 ASP A 103 13878 23421 21427 1204 -1651 -2132 O ATOM 380 N TYR A 104 3.476 13.288 -30.481 1.00116.28 N ANISOU 380 N TYR A 104 11366 17092 15725 1427 -1341 -1802 N ATOM 381 CA TYR A 104 2.339 12.844 -31.281 1.00116.15 C ANISOU 381 CA TYR A 104 11778 16781 15573 1409 -1097 -1757 C ATOM 382 C TYR A 104 1.049 13.544 -30.863 1.00111.91 C ANISOU 382 C TYR A 104 11621 16023 14876 1104 -1140 -1695 C ATOM 383 O TYR A 104 0.203 13.845 -31.704 1.00110.23 O ANISOU 383 O TYR A 104 11621 15661 14603 909 -918 -1677 O ATOM 384 CB TYR A 104 2.165 11.324 -31.206 1.00148.40 C ANISOU 384 CB TYR A 104 16120 20679 19588 1828 -1119 -1719 C ATOM 385 CG TYR A 104 3.074 10.550 -32.133 1.00152.30 C ANISOU 385 CG TYR A 104 16359 21292 20216 2126 -926 -1796 C ATOM 386 CD1 TYR A 104 2.809 10.494 -33.495 1.00153.34 C ANISOU 386 CD1 TYR A 104 16558 21369 20335 2044 -577 -1845 C ATOM 387 CD2 TYR A 104 4.185 9.868 -31.654 1.00155.52 C ANISOU 387 CD2 TYR A 104 16466 21870 20753 2504 -1094 -1824 C ATOM 388 CE1 TYR A 104 3.626 9.790 -34.356 1.00156.79 C ANISOU 388 CE1 TYR A 104 16780 21916 20876 2320 -370 -1935 C ATOM 389 CE2 TYR A 104 5.010 9.158 -32.510 1.00158.94 C ANISOU 389 CE2 TYR A 104 16655 22413 21321 2806 -894 -1911 C ATOM 390 CZ TYR A 104 4.724 9.123 -33.860 1.00159.79 C ANISOU 390 CZ TYR A 104 16847 22461 21404 2709 -518 -1974 C ATOM 391 OH TYR A 104 5.536 8.420 -34.721 1.00163.11 O ANISOU 391 OH TYR A 104 17041 22993 21940 3013 -291 -2080 O ATOM 392 N TYR A 105 0.902 13.802 -29.568 1.00105.64 N ANISOU 392 N TYR A 105 10910 15219 14008 1074 -1426 -1667 N ATOM 393 CA TYR A 105 -0.263 14.527 -29.074 1.00102.01 C ANISOU 393 CA TYR A 105 10776 14575 13407 801 -1462 -1629 C ATOM 394 C TYR A 105 -0.191 15.993 -29.482 1.00 99.22 C ANISOU 394 C TYR A 105 10239 14316 13144 416 -1372 -1683 C ATOM 395 O TYR A 105 -1.183 16.574 -29.921 1.00 96.75 O ANISOU 395 O TYR A 105 10159 13831 12771 191 -1227 -1657 O ATOM 396 CB TYR A 105 -0.380 14.408 -27.553 1.00102.77 C ANISOU 396 CB TYR A 105 11021 14652 13376 878 -1779 -1598 C ATOM 397 CG TYR A 105 -0.761 13.027 -27.070 1.00105.11 C ANISOU 397 CG TYR A 105 11629 14774 13535 1204 -1861 -1507 C ATOM 398 CD1 TYR A 105 -2.073 12.582 -27.152 1.00103.79 C ANISOU 398 CD1 TYR A 105 11898 14322 13214 1169 -1738 -1434 C ATOM 399 CD2 TYR A 105 0.188 12.173 -26.525 1.00108.51 C ANISOU 399 CD2 TYR A 105 11916 15317 13997 1543 -2068 -1489 C ATOM 400 CE1 TYR A 105 -2.429 11.322 -26.712 1.00105.98 C ANISOU 400 CE1 TYR A 105 12483 14417 13367 1432 -1803 -1342 C ATOM 401 CE2 TYR A 105 -0.159 10.911 -26.081 1.00110.89 C ANISOU 401 CE2 TYR A 105 12542 15421 14170 1840 -2147 -1389 C ATOM 402 CZ TYR A 105 -1.469 10.491 -26.176 1.00109.47 C ANISOU 402 CZ TYR A 105 12817 14944 13833 1768 -2006 -1315 C ATOM 403 OH TYR A 105 -1.818 9.235 -25.734 1.00111.56 O ANISOU 403 OH TYR A 105 13427 14992 13971 2029 -2074 -1208 O ATOM 404 N LEU A 106 0.992 16.584 -29.338 1.00113.17 N ANISOU 404 N LEU A 106 11585 16351 15064 339 -1466 -1755 N ATOM 405 CA LEU A 106 1.213 17.968 -29.744 1.00111.48 C ANISOU 405 CA LEU A 106 11180 16223 14955 -43 -1380 -1805 C ATOM 406 C LEU A 106 1.088 18.106 -31.257 1.00111.66 C ANISOU 406 C LEU A 106 11173 16218 15035 -151 -1033 -1785 C ATOM 407 O LEU A 106 0.645 19.137 -31.762 1.00108.96 O ANISOU 407 O LEU A 106 10906 15794 14702 -466 -906 -1772 O ATOM 408 CB LEU A 106 2.587 18.456 -29.278 1.00 97.92 C ANISOU 408 CB LEU A 106 8986 14819 13401 -108 -1559 -1890 C ATOM 409 CG LEU A 106 2.675 19.159 -27.918 1.00 96.63 C ANISOU 409 CG LEU A 106 8833 14693 13188 -253 -1888 -1941 C ATOM 410 CD1 LEU A 106 2.167 18.276 -26.785 1.00 96.62 C ANISOU 410 CD1 LEU A 106 9140 14579 12993 27 -2126 -1894 C ATOM 411 CD2 LEU A 106 4.103 19.611 -27.647 1.00 99.06 C ANISOU 411 CD2 LEU A 106 8617 15339 13682 -341 -2053 -2033 C ATOM 412 N GLY A 107 1.486 17.060 -31.975 1.00106.92 N ANISOU 412 N GLY A 107 10485 15679 14463 121 -885 -1784 N ATOM 413 CA GLY A 107 1.372 17.043 -33.421 1.00108.19 C ANISOU 413 CA GLY A 107 10654 15820 14634 51 -552 -1773 C ATOM 414 C GLY A 107 -0.071 16.894 -33.863 1.00105.80 C ANISOU 414 C GLY A 107 10826 15213 14160 -4 -441 -1699 C ATOM 415 O GLY A 107 -0.492 17.488 -34.855 1.00104.39 O ANISOU 415 O GLY A 107 10734 14974 13956 -226 -232 -1669 O ATOM 416 N SER A 108 -0.830 16.094 -33.120 1.00112.08 N ANISOU 416 N SER A 108 11927 15823 14834 192 -588 -1663 N ATOM 417 CA SER A 108 -2.244 15.892 -33.407 1.00109.78 C ANISOU 417 CA SER A 108 12062 15257 14391 139 -511 -1597 C ATOM 418 C SER A 108 -3.024 17.176 -33.150 1.00105.29 C ANISOU 418 C SER A 108 11613 14593 13800 -186 -550 -1568 C ATOM 419 O SER A 108 -3.997 17.473 -33.843 1.00102.96 O ANISOU 419 O SER A 108 11543 14141 13438 -327 -419 -1519 O ATOM 420 CB SER A 108 -2.808 14.752 -32.558 1.00 98.42 C ANISOU 420 CB SER A 108 10901 13656 12838 397 -661 -1561 C ATOM 421 OG SER A 108 -4.183 14.542 -32.830 1.00 96.93 O ANISOU 421 OG SER A 108 11088 13221 12518 322 -583 -1503 O ATOM 422 N LEU A 109 -2.589 17.934 -32.148 1.00101.24 N ANISOU 422 N LEU A 109 10952 14172 13344 -292 -743 -1604 N ATOM 423 CA LEU A 109 -3.208 19.215 -31.832 1.00 97.49 C ANISOU 423 CA LEU A 109 10580 13598 12864 -585 -786 -1601 C ATOM 424 C LEU A 109 -2.903 20.241 -32.916 1.00 97.48 C ANISOU 424 C LEU A 109 10431 13644 12962 -855 -602 -1594 C ATOM 425 O LEU A 109 -3.777 21.006 -33.320 1.00 95.24 O ANISOU 425 O LEU A 109 10347 13193 12648 -1047 -524 -1547 O ATOM 426 CB LEU A 109 -2.728 19.732 -30.473 1.00 78.95 C ANISOU 426 CB LEU A 109 8125 11338 10536 -633 -1046 -1666 C ATOM 427 CG LEU A 109 -3.280 19.052 -29.219 1.00 78.68 C ANISOU 427 CG LEU A 109 8328 11215 10353 -445 -1243 -1657 C ATOM 428 CD1 LEU A 109 -2.601 19.598 -27.972 1.00 78.87 C ANISOU 428 CD1 LEU A 109 8214 11371 10383 -503 -1509 -1735 C ATOM 429 CD2 LEU A 109 -4.785 19.239 -29.133 1.00 76.03 C ANISOU 429 CD2 LEU A 109 8365 10628 9895 -522 -1173 -1609 C ATOM 430 N ALA A 110 -1.656 20.251 -33.379 1.00113.28 N ANISOU 430 N ALA A 110 12079 15876 15085 -866 -531 -1634 N ATOM 431 CA ALA A 110 -1.225 21.192 -34.408 1.00113.95 C ANISOU 431 CA ALA A 110 12006 16031 15260 -1142 -336 -1618 C ATOM 432 C ALA A 110 -1.921 20.925 -35.737 1.00113.88 C ANISOU 432 C ALA A 110 12212 15904 15153 -1146 -85 -1540 C ATOM 433 O ALA A 110 -2.160 21.846 -36.518 1.00112.90 O ANISOU 433 O ALA A 110 12150 15715 15031 -1403 50 -1481 O ATOM 434 CB ALA A 110 0.287 21.138 -34.578 1.00 76.92 C ANISOU 434 CB ALA A 110 6855 11649 10722 -1139 -296 -1684 C ATOM 435 N LEU A 111 -2.245 19.661 -35.988 1.00 98.64 N ANISOU 435 N LEU A 111 10416 13935 13127 -865 -36 -1537 N ATOM 436 CA LEU A 111 -2.959 19.283 -37.200 1.00 99.19 C ANISOU 436 CA LEU A 111 10721 13890 13077 -856 170 -1480 C ATOM 437 C LEU A 111 -4.403 19.756 -37.086 1.00 95.21 C ANISOU 437 C LEU A 111 10568 13132 12478 -976 102 -1405 C ATOM 438 O LEU A 111 -4.987 20.246 -38.051 1.00 94.50 O ANISOU 438 O LEU A 111 10630 12952 12326 -1134 231 -1335 O ATOM 439 CB LEU A 111 -2.893 17.767 -37.418 1.00101.09 C ANISOU 439 CB LEU A 111 11026 14136 13248 -525 222 -1520 C ATOM 440 CG LEU A 111 -3.457 17.180 -38.717 1.00102.81 C ANISOU 440 CG LEU A 111 11471 14264 13327 -489 436 -1497 C ATOM 441 CD1 LEU A 111 -2.687 15.925 -39.094 1.00107.67 C ANISOU 441 CD1 LEU A 111 11984 14984 13942 -191 550 -1581 C ATOM 442 CD2 LEU A 111 -4.941 16.865 -38.606 1.00 99.91 C ANISOU 442 CD2 LEU A 111 11496 13639 12828 -486 352 -1439 C ATOM 443 N SER A 112 -4.971 19.601 -35.894 1.00 99.24 N ANISOU 443 N SER A 112 11199 13537 12970 -892 -101 -1419 N ATOM 444 CA SER A 112 -6.343 20.019 -35.630 1.00 95.67 C ANISOU 444 CA SER A 112 11039 12865 12447 -978 -166 -1364 C ATOM 445 C SER A 112 -6.508 21.534 -35.729 1.00 94.09 C ANISOU 445 C SER A 112 10830 12604 12316 -1259 -168 -1333 C ATOM 446 O SER A 112 -7.603 22.031 -35.990 1.00 92.01 O ANISOU 446 O SER A 112 10785 12165 12008 -1347 -159 -1271 O ATOM 447 CB SER A 112 -6.783 19.539 -34.246 1.00107.02 C ANISOU 447 CB SER A 112 12584 14236 13844 -833 -358 -1395 C ATOM 448 OG SER A 112 -8.042 20.085 -33.894 1.00103.97 O ANISOU 448 OG SER A 112 12427 13667 13410 -930 -405 -1359 O ATOM 449 N ASP A 113 -5.416 22.261 -35.517 1.00125.94 N ANISOU 449 N ASP A 113 14609 16777 16468 -1396 -188 -1378 N ATOM 450 CA ASP A 113 -5.438 23.717 -35.593 1.00124.85 C ANISOU 450 CA ASP A 113 14470 16558 16408 -1682 -190 -1354 C ATOM 451 C ASP A 113 -5.297 24.218 -37.029 1.00126.35 C ANISOU 451 C ASP A 113 14663 16749 16595 -1859 21 -1262 C ATOM 452 O ASP A 113 -5.956 25.179 -37.424 1.00125.87 O ANISOU 452 O ASP A 113 14779 16514 16532 -2034 43 -1183 O ATOM 453 CB ASP A 113 -4.343 24.317 -34.709 1.00184.41 C ANISOU 453 CB ASP A 113 21751 24239 24078 -1798 -318 -1447 C ATOM 454 CG ASP A 113 -4.607 24.103 -33.230 1.00183.54 C ANISOU 454 CG ASP A 113 21705 24096 23937 -1673 -549 -1530 C ATOM 455 OD1 ASP A 113 -5.476 23.270 -32.894 1.00183.03 O ANISOU 455 OD1 ASP A 113 21845 23941 23758 -1466 -586 -1512 O ATOM 456 OD2 ASP A 113 -3.946 24.766 -32.403 1.00184.47 O ANISOU 456 OD2 ASP A 113 21678 24281 24133 -1799 -694 -1614 O ATOM 457 N LEU A 114 -4.440 23.561 -37.805 1.00116.20 N ANISOU 457 N LEU A 114 13194 15657 15301 -1801 180 -1269 N ATOM 458 CA LEU A 114 -4.217 23.941 -39.198 1.00118.20 C ANISOU 458 CA LEU A 114 13454 15944 15514 -1967 409 -1183 C ATOM 459 C LEU A 114 -5.466 23.738 -40.049 1.00117.54 C ANISOU 459 C LEU A 114 13709 15679 15270 -1929 466 -1084 C ATOM 460 O LEU A 114 -5.722 24.500 -40.981 1.00118.13 O ANISOU 460 O LEU A 114 13911 15678 15297 -2122 572 -976 O ATOM 461 CB LEU A 114 -3.051 23.151 -39.796 1.00 89.62 C ANISOU 461 CB LEU A 114 9560 12589 11903 -1872 588 -1238 C ATOM 462 CG LEU A 114 -1.641 23.637 -39.458 1.00 91.37 C ANISOU 462 CG LEU A 114 9378 13043 12296 -2010 607 -1305 C ATOM 463 CD1 LEU A 114 -0.603 22.765 -40.142 1.00 95.22 C ANISOU 463 CD1 LEU A 114 9590 13799 12791 -1868 815 -1362 C ATOM 464 CD2 LEU A 114 -1.465 25.095 -39.856 1.00 91.28 C ANISOU 464 CD2 LEU A 114 9363 12971 12348 -2396 677 -1225 C ATOM 465 N LEU A 115 -6.237 22.705 -39.725 1.00104.30 N ANISOU 465 N LEU A 115 12184 13936 13510 -1691 385 -1115 N ATOM 466 CA LEU A 115 -7.460 22.401 -40.456 1.00103.37 C ANISOU 466 CA LEU A 115 12363 13666 13248 -1651 408 -1037 C ATOM 467 C LEU A 115 -8.486 23.521 -40.311 1.00101.10 C ANISOU 467 C LEU A 115 12260 13170 12983 -1798 302 -949 C ATOM 468 O LEU A 115 -9.151 23.894 -41.277 1.00101.53 O ANISOU 468 O LEU A 115 12498 13131 12949 -1887 353 -842 O ATOM 469 CB LEU A 115 -8.056 21.074 -39.981 1.00 96.72 C ANISOU 469 CB LEU A 115 11629 12786 12336 -1395 329 -1097 C ATOM 470 CG LEU A 115 -7.276 19.808 -40.340 1.00100.24 C ANISOU 470 CG LEU A 115 11979 13376 12733 -1201 443 -1175 C ATOM 471 CD1 LEU A 115 -7.998 18.571 -39.830 1.00 99.17 C ANISOU 471 CD1 LEU A 115 12012 13138 12528 -977 349 -1216 C ATOM 472 CD2 LEU A 115 -7.050 19.721 -41.842 1.00103.34 C ANISOU 472 CD2 LEU A 115 12422 13835 13007 -1272 661 -1141 C ATOM 473 N ILE A 116 -8.608 24.056 -39.100 1.00115.18 N ANISOU 473 N ILE A 116 14003 14882 14876 -1809 147 -998 N ATOM 474 CA ILE A 116 -9.580 25.107 -38.820 1.00113.30 C ANISOU 474 CA ILE A 116 13935 14434 14680 -1907 47 -942 C ATOM 475 C ILE A 116 -9.138 26.449 -39.407 1.00114.86 C ANISOU 475 C ILE A 116 14127 14569 14945 -2163 109 -861 C ATOM 476 O ILE A 116 -9.966 27.286 -39.766 1.00115.57 O ANISOU 476 O ILE A 116 14406 14469 15036 -2242 77 -763 O ATOM 477 CB ILE A 116 -9.830 25.249 -37.299 1.00140.15 C ANISOU 477 CB ILE A 116 17318 17776 18157 -1834 -119 -1043 C ATOM 478 CG1 ILE A 116 -10.231 23.903 -36.695 1.00139.27 C ANISOU 478 CG1 ILE A 116 17234 17716 17965 -1600 -170 -1102 C ATOM 479 CG2 ILE A 116 -10.902 26.291 -37.012 1.00138.60 C ANISOU 479 CG2 ILE A 116 17301 17355 18006 -1895 -200 -1005 C ATOM 480 CD1 ILE A 116 -10.516 23.965 -35.209 1.00137.85 C ANISOU 480 CD1 ILE A 116 17070 17491 17814 -1528 -316 -1191 C ATOM 481 N LEU A 117 -7.830 26.637 -39.533 1.00108.32 N ANISOU 481 N LEU A 117 13077 13900 14178 -2292 201 -893 N ATOM 482 CA LEU A 117 -7.289 27.892 -40.042 1.00109.85 C ANISOU 482 CA LEU A 117 13256 14039 14443 -2577 276 -815 C ATOM 483 C LEU A 117 -7.300 27.963 -41.567 1.00112.19 C ANISOU 483 C LEU A 117 13663 14351 14613 -2681 462 -669 C ATOM 484 O LEU A 117 -7.572 29.016 -42.143 1.00113.52 O ANISOU 484 O LEU A 117 13997 14354 14780 -2871 486 -539 O ATOM 485 CB LEU A 117 -5.871 28.106 -39.515 1.00 92.21 C ANISOU 485 CB LEU A 117 10708 11990 12338 -2711 297 -914 C ATOM 486 CG LEU A 117 -5.781 28.370 -38.012 1.00 90.35 C ANISOU 486 CG LEU A 117 10395 11718 12217 -2683 88 -1050 C ATOM 487 CD1 LEU A 117 -4.360 28.186 -37.525 1.00 91.57 C ANISOU 487 CD1 LEU A 117 10191 12128 12474 -2748 82 -1161 C ATOM 488 CD2 LEU A 117 -6.285 29.766 -37.681 1.00 89.86 C ANISOU 488 CD2 LEU A 117 10521 11386 12237 -2875 -1 -1021 C ATOM 489 N LEU A 118 -7.008 26.840 -42.214 1.00 99.44 N ANISOU 489 N LEU A 118 11983 12922 12877 -2550 591 -690 N ATOM 490 CA LEU A 118 -6.919 26.800 -43.670 1.00102.26 C ANISOU 490 CA LEU A 118 12448 13332 13075 -2644 787 -574 C ATOM 491 C LEU A 118 -8.275 26.608 -44.343 1.00101.91 C ANISOU 491 C LEU A 118 12724 13128 12869 -2553 722 -470 C ATOM 492 O LEU A 118 -8.528 27.166 -45.410 1.00103.72 O ANISOU 492 O LEU A 118 13139 13290 12979 -2694 798 -321 O ATOM 493 CB LEU A 118 -5.960 25.694 -44.119 1.00 94.91 C ANISOU 493 CB LEU A 118 11312 12672 12077 -2539 975 -665 C ATOM 494 CG LEU A 118 -4.478 25.884 -43.795 1.00 95.95 C ANISOU 494 CG LEU A 118 11077 13024 12357 -2651 1086 -747 C ATOM 495 CD1 LEU A 118 -3.674 24.680 -44.262 1.00 98.92 C ANISOU 495 CD1 LEU A 118 11259 13658 12667 -2474 1271 -847 C ATOM 496 CD2 LEU A 118 -3.947 27.166 -44.423 1.00 96.89 C ANISOU 496 CD2 LEU A 118 11185 13122 12506 -3004 1220 -626 C ATOM 497 N LEU A 119 -9.143 25.819 -43.718 1.00114.41 N ANISOU 497 N LEU A 119 14369 14657 14444 -2328 575 -543 N ATOM 498 CA LEU A 119 -10.410 25.444 -44.336 1.00113.91 C ANISOU 498 CA LEU A 119 14558 14487 14234 -2234 504 -469 C ATOM 499 C LEU A 119 -11.608 26.220 -43.793 1.00111.89 C ANISOU 499 C LEU A 119 14446 14005 14063 -2220 307 -408 C ATOM 500 O LEU A 119 -12.467 26.659 -44.558 1.00112.96 O ANISOU 500 O LEU A 119 14783 14023 14115 -2256 255 -275 O ATOM 501 CB LEU A 119 -10.655 23.943 -44.170 1.00108.29 C ANISOU 501 CB LEU A 119 13836 13867 13443 -2009 496 -586 C ATOM 502 CG LEU A 119 -9.595 23.002 -44.745 1.00111.05 C ANISOU 502 CG LEU A 119 14069 14424 13703 -1955 693 -667 C ATOM 503 CD1 LEU A 119 -9.977 21.552 -44.495 1.00110.31 C ANISOU 503 CD1 LEU A 119 14021 14350 13544 -1723 655 -779 C ATOM 504 CD2 LEU A 119 -9.396 23.258 -46.231 1.00114.45 C ANISOU 504 CD2 LEU A 119 14628 14909 13947 -2099 867 -566 C ATOM 505 N ALA A 120 -11.663 26.386 -42.476 1.00 96.70 N ANISOU 505 N ALA A 120 12417 12029 12298 -2155 195 -507 N ATOM 506 CA ALA A 120 -12.829 26.989 -41.835 1.00 95.32 C ANISOU 506 CA ALA A 120 12356 11656 12206 -2098 29 -486 C ATOM 507 C ALA A 120 -12.830 28.516 -41.871 1.00 96.79 C ANISOU 507 C ALA A 120 12623 11654 12498 -2260 -5 -395 C ATOM 508 O ALA A 120 -13.873 29.132 -42.088 1.00 97.48 O ANISOU 508 O ALA A 120 12875 11561 12599 -2229 -103 -301 O ATOM 509 CB ALA A 120 -12.970 26.486 -40.404 1.00 65.77 C ANISOU 509 CB ALA A 120 8507 7931 8551 -1954 -61 -637 C ATOM 510 N MET A 121 -11.667 29.124 -41.658 1.00108.20 N ANISOU 510 N MET A 121 13950 13133 14028 -2433 68 -423 N ATOM 511 CA MET A 121 -11.576 30.585 -41.613 1.00109.54 C ANISOU 511 CA MET A 121 14215 13093 14312 -2616 38 -349 C ATOM 512 C MET A 121 -11.968 31.309 -42.910 1.00111.71 C ANISOU 512 C MET A 121 14717 13229 14500 -2731 75 -135 C ATOM 513 O MET A 121 -12.777 32.234 -42.864 1.00112.63 O ANISOU 513 O MET A 121 15014 13096 14684 -2719 -36 -52 O ATOM 514 CB MET A 121 -10.203 31.061 -41.119 1.00132.98 C ANISOU 514 CB MET A 121 16995 16137 17393 -2819 104 -431 C ATOM 515 CG MET A 121 -10.097 32.579 -41.036 1.00134.25 C ANISOU 515 CG MET A 121 17284 16046 17680 -3037 70 -366 C ATOM 516 SD MET A 121 -8.493 33.185 -40.485 1.00134.86 S ANISOU 516 SD MET A 121 17125 16215 17900 -3333 132 -468 S ATOM 517 CE MET A 121 -8.430 32.530 -38.821 1.00131.79 C ANISOU 517 CE MET A 121 16549 15939 17586 -3141 -26 -716 C ATOM 518 N PRO A 122 -11.404 30.904 -44.067 1.00 90.98 N ANISOU 518 N PRO A 122 12095 10758 11715 -2829 231 -44 N ATOM 519 CA PRO A 122 -11.788 31.628 -45.286 1.00 93.68 C ANISOU 519 CA PRO A 122 12690 10963 11942 -2946 253 177 C ATOM 520 C PRO A 122 -13.269 31.461 -45.617 1.00 94.15 C ANISOU 520 C PRO A 122 12942 10905 11925 -2748 86 260 C ATOM 521 O PRO A 122 -13.861 32.337 -46.246 1.00 96.68 O ANISOU 521 O PRO A 122 13487 11027 12218 -2792 10 440 O ATOM 522 CB PRO A 122 -10.924 30.975 -46.370 1.00101.98 C ANISOU 522 CB PRO A 122 13693 12254 12800 -3055 470 219 C ATOM 523 CG PRO A 122 -10.591 29.631 -45.834 1.00100.39 C ANISOU 523 CG PRO A 122 13263 12290 12592 -2881 509 23 C ATOM 524 CD PRO A 122 -10.440 29.826 -44.358 1.00 97.81 C ANISOU 524 CD PRO A 122 12764 11913 12486 -2825 395 -129 C ATOM 525 N VAL A 123 -13.855 30.350 -45.187 1.00 89.01 N ANISOU 525 N VAL A 123 12198 10372 11247 -2536 21 136 N ATOM 526 CA VAL A 123 -15.282 30.120 -45.369 1.00 89.43 C ANISOU 526 CA VAL A 123 12375 10346 11259 -2356 -147 188 C ATOM 527 C VAL A 123 -16.095 31.032 -44.453 1.00 88.98 C ANISOU 527 C VAL A 123 12347 10057 11406 -2262 -302 175 C ATOM 528 O VAL A 123 -17.018 31.714 -44.900 1.00 91.14 O ANISOU 528 O VAL A 123 12782 10158 11689 -2208 -428 314 O ATOM 529 CB VAL A 123 -15.653 28.646 -45.099 1.00 79.58 C ANISOU 529 CB VAL A 123 11018 9282 9938 -2190 -158 49 C ATOM 530 CG1 VAL A 123 -17.161 28.485 -44.965 1.00 79.71 C ANISOU 530 CG1 VAL A 123 11095 9214 9975 -2021 -343 70 C ATOM 531 CG2 VAL A 123 -15.109 27.752 -46.205 1.00 80.86 C ANISOU 531 CG2 VAL A 123 11216 9634 9874 -2246 -21 69 C ATOM 532 N GLU A 124 -15.737 31.047 -43.172 1.00111.80 N ANISOU 532 N GLU A 124 15086 12945 14450 -2232 -297 5 N ATOM 533 CA GLU A 124 -16.448 31.851 -42.184 1.00111.95 C ANISOU 533 CA GLU A 124 15130 12756 14651 -2132 -415 -50 C ATOM 534 C GLU A 124 -16.269 33.346 -42.433 1.00114.11 C ANISOU 534 C GLU A 124 15572 12762 15023 -2266 -437 68 C ATOM 535 O GLU A 124 -17.215 34.124 -42.302 1.00116.18 O ANISOU 535 O GLU A 124 15958 12799 15384 -2151 -556 122 O ATOM 536 CB GLU A 124 -15.982 31.503 -40.769 1.00125.07 C ANISOU 536 CB GLU A 124 16618 14492 16410 -2093 -396 -267 C ATOM 537 CG GLU A 124 -16.601 32.376 -39.689 1.00125.60 C ANISOU 537 CG GLU A 124 16729 14349 16646 -2005 -489 -354 C ATOM 538 CD GLU A 124 -15.962 32.173 -38.331 1.00123.79 C ANISOU 538 CD GLU A 124 16366 14192 16478 -2012 -474 -560 C ATOM 539 OE1 GLU A 124 -15.491 31.050 -38.053 1.00121.77 O ANISOU 539 OE1 GLU A 124 15966 14164 16138 -1983 -430 -641 O ATOM 540 OE2 GLU A 124 -15.930 33.140 -37.542 1.00124.63 O ANISOU 540 OE2 GLU A 124 16530 14115 16708 -2042 -516 -643 O ATOM 541 N LEU A 125 -15.051 33.741 -42.793 1.00 89.84 N ANISOU 541 N LEU A 125 12498 9707 11929 -2508 -316 109 N ATOM 542 CA LEU A 125 -14.728 35.148 -43.006 1.00 91.76 C ANISOU 542 CA LEU A 125 12915 9681 12266 -2689 -318 222 C ATOM 543 C LEU A 125 -15.544 35.745 -44.148 1.00 94.53 C ANISOU 543 C LEU A 125 13527 9850 12540 -2657 -394 469 C ATOM 544 O LEU A 125 -15.784 36.951 -44.186 1.00 95.93 O ANISOU 544 O LEU A 125 13904 9720 12825 -2699 -462 571 O ATOM 545 CB LEU A 125 -13.229 35.322 -43.272 1.00 94.61 C ANISOU 545 CB LEU A 125 13192 10148 12606 -2991 -150 227 C ATOM 546 CG LEU A 125 -12.671 36.747 -43.284 1.00 96.22 C ANISOU 546 CG LEU A 125 13548 10079 12933 -3246 -130 308 C ATOM 547 CD1 LEU A 125 -13.079 37.499 -42.027 1.00 95.61 C ANISOU 547 CD1 LEU A 125 13511 9754 13063 -3164 -262 158 C ATOM 548 CD2 LEU A 125 -11.156 36.726 -43.428 1.00 95.99 C ANISOU 548 CD2 LEU A 125 13348 10228 12897 -3553 49 277 C ATOM 549 N TYR A 126 -15.972 34.896 -45.075 1.00 95.38 N ANISOU 549 N TYR A 126 13650 10135 12455 -2579 -397 561 N ATOM 550 CA TYR A 126 -16.772 35.349 -46.206 1.00 98.64 C ANISOU 550 CA TYR A 126 14308 10414 12756 -2537 -501 801 C ATOM 551 C TYR A 126 -18.276 35.256 -45.951 1.00100.10 C ANISOU 551 C TYR A 126 14501 10520 13011 -2241 -710 797 C ATOM 552 O TYR A 126 -18.995 36.250 -46.059 1.00101.88 O ANISOU 552 O TYR A 126 14895 10478 13337 -2148 -848 921 O ATOM 553 CB TYR A 126 -16.418 34.563 -47.472 1.00 91.72 C ANISOU 553 CB TYR A 126 13478 9771 11600 -2639 -402 912 C ATOM 554 CG TYR A 126 -17.352 34.842 -48.628 1.00 95.13 C ANISOU 554 CG TYR A 126 14159 10111 11873 -2570 -549 1149 C ATOM 555 CD1 TYR A 126 -17.218 35.994 -49.392 1.00 97.37 C ANISOU 555 CD1 TYR A 126 14722 10163 12112 -2710 -565 1392 C ATOM 556 CD2 TYR A 126 -18.378 33.961 -48.945 1.00 96.43 C ANISOU 556 CD2 TYR A 126 14291 10417 11932 -2374 -687 1135 C ATOM 557 CE1 TYR A 126 -18.075 36.258 -50.444 1.00100.27 C ANISOU 557 CE1 TYR A 126 15333 10448 12318 -2632 -729 1625 C ATOM 558 CE2 TYR A 126 -19.239 34.217 -49.992 1.00 99.32 C ANISOU 558 CE2 TYR A 126 14871 10718 12148 -2310 -858 1349 C ATOM 559 CZ TYR A 126 -19.084 35.365 -50.740 1.00100.83 C ANISOU 559 CZ TYR A 126 15343 10686 12283 -2427 -886 1598 C ATOM 560 OH TYR A 126 -19.942 35.620 -51.785 1.00102.89 O ANISOU 560 OH TYR A 126 15832 10886 12377 -2349 -1083 1826 O ATOM 561 N ASN A 127 -18.742 34.059 -45.611 1.00 82.03 N ANISOU 561 N ASN A 127 12025 8463 10681 -2094 -729 655 N ATOM 562 CA ASN A 127 -20.175 33.785 -45.543 1.00 83.19 C ANISOU 562 CA ASN A 127 12140 8603 10866 -1845 -909 660 C ATOM 563 C ASN A 127 -20.848 34.009 -44.191 1.00 82.56 C ANISOU 563 C ASN A 127 11923 8426 11019 -1655 -966 489 C ATOM 564 O ASN A 127 -22.064 33.853 -44.070 1.00 83.55 O ANISOU 564 O ASN A 127 11988 8552 11206 -1448 -1100 486 O ATOM 565 CB ASN A 127 -20.469 32.369 -46.037 1.00 89.49 C ANISOU 565 CB ASN A 127 12840 9686 11477 -1809 -909 618 C ATOM 566 CG ASN A 127 -21.127 32.356 -47.399 1.00 92.87 C ANISOU 566 CG ASN A 127 13439 10131 11718 -1798 -1042 825 C ATOM 567 OD1 ASN A 127 -21.934 33.228 -47.721 1.00 95.88 O ANISOU 567 OD1 ASN A 127 13941 10328 12163 -1696 -1212 977 O ATOM 568 ND2 ASN A 127 -20.782 31.366 -48.210 1.00 92.93 N ANISOU 568 ND2 ASN A 127 13469 10356 11485 -1893 -973 828 N ATOM 569 N PHE A 128 -20.069 34.372 -43.179 1.00 92.82 N ANISOU 569 N PHE A 128 13168 9658 12443 -1732 -864 341 N ATOM 570 CA PHE A 128 -20.623 34.571 -41.843 1.00 91.85 C ANISOU 570 CA PHE A 128 12940 9454 12505 -1566 -893 158 C ATOM 571 C PHE A 128 -20.358 35.967 -41.288 1.00 92.58 C ANISOU 571 C PHE A 128 13170 9233 12772 -1599 -901 137 C ATOM 572 O PHE A 128 -21.054 36.422 -40.380 1.00 93.20 O ANISOU 572 O PHE A 128 13230 9173 13008 -1423 -946 20 O ATOM 573 CB PHE A 128 -20.102 33.504 -40.877 1.00 97.10 C ANISOU 573 CB PHE A 128 13404 10352 13138 -1586 -788 -55 C ATOM 574 CG PHE A 128 -20.680 32.139 -41.115 1.00 96.25 C ANISOU 574 CG PHE A 128 13170 10492 12908 -1495 -799 -76 C ATOM 575 CD1 PHE A 128 -21.987 31.992 -41.553 1.00 98.77 C ANISOU 575 CD1 PHE A 128 13483 10813 13234 -1335 -921 2 C ATOM 576 CD2 PHE A 128 -19.918 31.002 -40.905 1.00 93.38 C ANISOU 576 CD2 PHE A 128 12693 10354 12432 -1570 -696 -176 C ATOM 577 CE1 PHE A 128 -22.523 30.738 -41.774 1.00 98.06 C ANISOU 577 CE1 PHE A 128 13284 10939 13035 -1288 -937 -25 C ATOM 578 CE2 PHE A 128 -20.449 29.745 -41.125 1.00 92.47 C ANISOU 578 CE2 PHE A 128 12499 10428 12208 -1499 -706 -200 C ATOM 579 CZ PHE A 128 -21.753 29.613 -41.561 1.00 94.37 C ANISOU 579 CZ PHE A 128 12743 10663 12451 -1377 -824 -127 C ATOM 580 N ILE A 129 -19.355 36.645 -41.835 1.00100.87 N ANISOU 580 N ILE A 129 14366 10166 13793 -1835 -843 245 N ATOM 581 CA ILE A 129 -18.989 37.975 -41.359 1.00101.62 C ANISOU 581 CA ILE A 129 14623 9938 14051 -1920 -847 225 C ATOM 582 C ILE A 129 -19.329 39.075 -42.363 1.00104.84 C ANISOU 582 C ILE A 129 15311 10044 14480 -1932 -935 479 C ATOM 583 O ILE A 129 -19.911 40.099 -42.001 1.00106.41 O ANISOU 583 O ILE A 129 15661 9922 14847 -1800 -1022 481 O ATOM 584 CB ILE A 129 -17.497 38.041 -40.984 1.00108.79 C ANISOU 584 CB ILE A 129 15478 10909 14950 -2218 -714 127 C ATOM 585 CG1 ILE A 129 -17.261 37.318 -39.659 1.00106.05 C ANISOU 585 CG1 ILE A 129 14906 10751 14635 -2159 -678 -144 C ATOM 586 CG2 ILE A 129 -17.014 39.483 -40.906 1.00110.52 C ANISOU 586 CG2 ILE A 129 15920 10769 15303 -2394 -720 173 C ATOM 587 CD1 ILE A 129 -15.832 37.330 -39.222 1.00104.55 C ANISOU 587 CD1 ILE A 129 14620 10657 14448 -2426 -585 -253 C ATOM 588 N TRP A 130 -18.976 38.852 -43.624 1.00105.14 N ANISOU 588 N TRP A 130 15438 10177 14335 -2080 -909 693 N ATOM 589 CA TRP A 130 -19.216 39.842 -44.670 1.00107.90 C ANISOU 589 CA TRP A 130 16087 10253 14656 -2118 -993 970 C ATOM 590 C TRP A 130 -20.505 39.563 -45.443 1.00109.81 C ANISOU 590 C TRP A 130 16369 10532 14823 -1857 -1172 1128 C ATOM 591 O TRP A 130 -21.479 40.305 -45.317 1.00111.75 O ANISOU 591 O TRP A 130 16718 10527 15216 -1621 -1330 1185 O ATOM 592 CB TRP A 130 -18.012 39.936 -45.612 1.00105.28 C ANISOU 592 CB TRP A 130 15871 9977 14152 -2468 -847 1129 C ATOM 593 CG TRP A 130 -16.817 40.590 -44.975 1.00104.29 C ANISOU 593 CG TRP A 130 15752 9728 14145 -2750 -710 1026 C ATOM 594 CD1 TRP A 130 -15.819 39.974 -44.277 1.00101.66 C ANISOU 594 CD1 TRP A 130 15166 9639 13823 -2908 -569 814 C ATOM 595 CD2 TRP A 130 -16.500 41.987 -44.975 1.00105.92 C ANISOU 595 CD2 TRP A 130 16231 9532 14481 -2913 -721 1128 C ATOM 596 NE1 TRP A 130 -14.900 40.900 -43.844 1.00101.52 N ANISOU 596 NE1 TRP A 130 15219 9420 13933 -3173 -499 771 N ATOM 597 CE2 TRP A 130 -15.296 42.146 -44.260 1.00104.49 C ANISOU 597 CE2 TRP A 130 15930 9387 14385 -3196 -582 958 C ATOM 598 CE3 TRP A 130 -17.117 43.123 -45.512 1.00108.35 C ANISOU 598 CE3 TRP A 130 16882 9439 14846 -2847 -846 1352 C ATOM 599 CZ2 TRP A 130 -14.697 43.388 -44.067 1.00105.84 C ANISOU 599 CZ2 TRP A 130 16313 9207 14694 -3445 -557 992 C ATOM 600 CZ3 TRP A 130 -16.522 44.356 -45.320 1.00109.17 C ANISOU 600 CZ3 TRP A 130 17225 9167 15087 -3075 -812 1396 C ATOM 601 CH2 TRP A 130 -15.324 44.479 -44.604 1.00108.01 C ANISOU 601 CH2 TRP A 130 16952 9065 15021 -3387 -665 1211 C ATOM 602 N VAL A 131 -20.511 38.502 -46.244 1.00103.89 N ANISOU 602 N VAL A 131 15534 10093 13845 -1893 -1156 1189 N ATOM 603 CA VAL A 131 -21.699 38.148 -47.017 1.00105.86 C ANISOU 603 CA VAL A 131 15805 10418 14001 -1680 -1347 1328 C ATOM 604 C VAL A 131 -22.540 37.104 -46.285 1.00104.63 C ANISOU 604 C VAL A 131 15348 10499 13906 -1462 -1393 1120 C ATOM 605 O VAL A 131 -22.297 35.906 -46.402 1.00103.19 O ANISOU 605 O VAL A 131 15013 10619 13574 -1531 -1315 1029 O ATOM 606 CB VAL A 131 -21.330 37.620 -48.418 1.00 92.55 C ANISOU 606 CB VAL A 131 14248 8917 12000 -1852 -1323 1522 C ATOM 607 CG1 VAL A 131 -22.587 37.339 -49.230 1.00 94.50 C ANISOU 607 CG1 VAL A 131 14535 9230 12142 -1643 -1564 1668 C ATOM 608 CG2 VAL A 131 -20.438 38.617 -49.143 1.00 93.33 C ANISOU 608 CG2 VAL A 131 14647 8801 12016 -2106 -1238 1737 C ATOM 609 N HIS A 132 -23.538 37.567 -45.539 1.00 91.40 N ANISOU 609 N HIS A 132 13599 8676 12454 -1201 -1509 1046 N ATOM 610 CA HIS A 132 -24.362 36.677 -44.729 1.00 91.45 C ANISOU 610 CA HIS A 132 13316 8890 12540 -1011 -1526 846 C ATOM 611 C HIS A 132 -25.318 35.869 -45.595 1.00 93.09 C ANISOU 611 C HIS A 132 13439 9314 12615 -909 -1684 948 C ATOM 612 O HIS A 132 -25.678 34.742 -45.255 1.00 92.73 O ANISOU 612 O HIS A 132 13172 9529 12533 -878 -1657 807 O ATOM 613 CB HIS A 132 -25.141 37.470 -43.678 1.00100.41 C ANISOU 613 CB HIS A 132 14391 9809 13950 -762 -1573 727 C ATOM 614 CG HIS A 132 -24.294 38.426 -42.895 1.00 98.67 C ANISOU 614 CG HIS A 132 14307 9323 13859 -861 -1457 632 C ATOM 615 ND1 HIS A 132 -23.649 38.066 -41.734 1.00 95.57 N ANISOU 615 ND1 HIS A 132 13787 9019 13506 -949 -1298 384 N ATOM 616 CD2 HIS A 132 -23.985 39.726 -43.115 1.00 99.48 C ANISOU 616 CD2 HIS A 132 14679 9066 14053 -901 -1491 751 C ATOM 617 CE1 HIS A 132 -22.978 39.107 -41.266 1.00 95.22 C ANISOU 617 CE1 HIS A 132 13911 8695 13572 -1048 -1246 340 C ATOM 618 NE2 HIS A 132 -23.165 40.124 -42.085 1.00 97.75 N ANISOU 618 NE2 HIS A 132 14479 8729 13932 -1028 -1352 558 N ATOM 619 N HIS A 133 -25.728 36.457 -46.713 1.00 90.11 N ANISOU 619 N HIS A 133 13256 8820 12160 -868 -1860 1200 N ATOM 620 CA HIS A 133 -26.589 35.772 -47.667 1.00 92.00 C ANISOU 620 CA HIS A 133 13449 9261 12244 -798 -2048 1316 C ATOM 621 C HIS A 133 -26.334 36.289 -49.082 1.00 92.79 C ANISOU 621 C HIS A 133 13865 9267 12122 -906 -2161 1609 C ATOM 622 O HIS A 133 -26.139 37.488 -49.282 1.00 93.38 O ANISOU 622 O HIS A 133 14176 9039 12266 -891 -2201 1771 O ATOM 623 CB HIS A 133 -28.063 35.927 -47.278 1.00 83.34 C ANISOU 623 CB HIS A 133 12148 8155 11361 -482 -2244 1287 C ATOM 624 CG HIS A 133 -28.581 37.330 -47.406 1.00 85.27 C ANISOU 624 CG HIS A 133 12549 8065 11783 -271 -2404 1449 C ATOM 625 ND1 HIS A 133 -29.188 37.792 -48.559 1.00 87.19 N ANISOU 625 ND1 HIS A 133 12954 8236 11938 -171 -2665 1718 N ATOM 626 CD2 HIS A 133 -28.585 38.355 -46.536 1.00 85.60 C ANISOU 626 CD2 HIS A 133 12632 7814 12078 -130 -2349 1378 C ATOM 627 CE1 HIS A 133 -29.541 39.050 -48.380 1.00 89.50 C ANISOU 627 CE1 HIS A 133 13378 8189 12438 38 -2763 1817 C ATOM 628 NE2 HIS A 133 -29.191 39.425 -47.167 1.00 88.29 N ANISOU 628 NE2 HIS A 133 13160 7887 12498 66 -2569 1607 N ATOM 629 N PRO A 134 -26.337 35.382 -50.070 1.00 94.87 N ANISOU 629 N PRO A 134 14161 9780 12104 -1023 -2210 1677 N ATOM 630 CA PRO A 134 -26.625 33.960 -49.876 1.00 94.36 C ANISOU 630 CA PRO A 134 13852 10038 11961 -1043 -2179 1489 C ATOM 631 C PRO A 134 -25.381 33.132 -49.574 1.00 93.05 C ANISOU 631 C PRO A 134 13656 10021 11677 -1272 -1893 1323 C ATOM 632 O PRO A 134 -24.260 33.591 -49.794 1.00 92.73 O ANISOU 632 O PRO A 134 13788 9887 11557 -1450 -1730 1383 O ATOM 633 CB PRO A 134 -27.204 33.544 -51.230 1.00 80.62 C ANISOU 633 CB PRO A 134 12233 8445 9954 -1064 -2398 1663 C ATOM 634 CG PRO A 134 -26.623 34.526 -52.227 1.00 83.56 C ANISOU 634 CG PRO A 134 12970 8625 10154 -1170 -2424 1934 C ATOM 635 CD PRO A 134 -26.003 35.678 -51.472 1.00 83.89 C ANISOU 635 CD PRO A 134 13090 8361 10424 -1166 -2286 1943 C ATOM 636 N TRP A 135 -25.590 31.922 -49.064 1.00 95.55 N ANISOU 636 N TRP A 135 13749 10564 11993 -1264 -1836 1121 N ATOM 637 CA TRP A 135 -24.501 30.979 -48.854 1.00 93.39 C ANISOU 637 CA TRP A 135 13439 10449 11595 -1441 -1597 967 C ATOM 638 C TRP A 135 -23.915 30.603 -50.211 1.00 94.04 C ANISOU 638 C TRP A 135 13741 10642 11348 -1619 -1565 1089 C ATOM 639 O TRP A 135 -24.634 30.160 -51.108 1.00 95.08 O ANISOU 639 O TRP A 135 13941 10881 11304 -1603 -1737 1170 O ATOM 640 CB TRP A 135 -25.009 29.745 -48.105 1.00100.88 C ANISOU 640 CB TRP A 135 14143 11587 12600 -1378 -1577 753 C ATOM 641 CG TRP A 135 -23.991 28.663 -47.930 1.00 95.98 C ANISOU 641 CG TRP A 135 13494 11123 11851 -1517 -1363 601 C ATOM 642 CD1 TRP A 135 -23.872 27.528 -48.675 1.00 94.41 C ANISOU 642 CD1 TRP A 135 13348 11105 11421 -1608 -1343 565 C ATOM 643 CD2 TRP A 135 -22.941 28.614 -46.956 1.00 91.75 C ANISOU 643 CD2 TRP A 135 12877 10572 11413 -1566 -1152 459 C ATOM 644 NE1 TRP A 135 -22.820 26.770 -48.223 1.00 90.57 N ANISOU 644 NE1 TRP A 135 12813 10705 10896 -1685 -1123 413 N ATOM 645 CE2 TRP A 135 -22.231 27.415 -47.168 1.00 88.88 C ANISOU 645 CE2 TRP A 135 12504 10386 10882 -1661 -1014 353 C ATOM 646 CE3 TRP A 135 -22.535 29.465 -45.924 1.00 90.49 C ANISOU 646 CE3 TRP A 135 12658 10263 11462 -1534 -1079 405 C ATOM 647 CZ2 TRP A 135 -21.137 27.047 -46.388 1.00 85.27 C ANISOU 647 CZ2 TRP A 135 11955 9973 10469 -1706 -820 210 C ATOM 648 CZ3 TRP A 135 -21.449 29.097 -45.150 1.00 86.90 C ANISOU 648 CZ3 TRP A 135 12119 9865 11035 -1609 -896 257 C ATOM 649 CH2 TRP A 135 -20.762 27.899 -45.386 1.00 84.77 C ANISOU 649 CH2 TRP A 135 11817 9785 10605 -1685 -775 170 C ATOM 650 N ALA A 136 -22.604 30.770 -50.351 1.00 92.38 N ANISOU 650 N ALA A 136 13632 10419 11049 -1795 -1341 1093 N ATOM 651 CA ALA A 136 -21.955 30.672 -51.654 1.00 93.32 C ANISOU 651 CA ALA A 136 13988 10616 10854 -1972 -1268 1231 C ATOM 652 C ALA A 136 -21.325 29.311 -51.906 1.00 92.30 C ANISOU 652 C ALA A 136 13808 10734 10528 -2067 -1095 1067 C ATOM 653 O ALA A 136 -20.997 28.972 -53.044 1.00 93.25 O ANISOU 653 O ALA A 136 14117 10964 10349 -2186 -1046 1143 O ATOM 654 CB ALA A 136 -20.918 31.774 -51.812 1.00113.90 C ANISOU 654 CB ALA A 136 16748 13057 13470 -2129 -1115 1362 C ATOM 655 N PHE A 137 -21.156 28.531 -50.848 1.00130.42 N ANISOU 655 N PHE A 137 18402 15642 15511 -2006 -1000 842 N ATOM 656 CA PHE A 137 -20.513 27.234 -50.980 1.00128.44 C ANISOU 656 CA PHE A 137 18106 15590 15107 -2064 -832 677 C ATOM 657 C PHE A 137 -21.587 26.172 -51.178 1.00127.01 C ANISOU 657 C PHE A 137 17899 15516 14845 -1982 -997 598 C ATOM 658 O PHE A 137 -22.775 26.488 -51.200 1.00127.29 O ANISOU 658 O PHE A 137 17916 15496 14953 -1890 -1235 675 O ATOM 659 CB PHE A 137 -19.609 26.943 -49.783 1.00 95.15 C ANISOU 659 CB PHE A 137 13680 11396 11079 -2052 -640 493 C ATOM 660 CG PHE A 137 -18.611 28.034 -49.508 1.00 95.17 C ANISOU 660 CG PHE A 137 13679 11292 11189 -2157 -506 557 C ATOM 661 CD1 PHE A 137 -17.514 28.215 -50.337 1.00 96.57 C ANISOU 661 CD1 PHE A 137 13962 11535 11196 -2331 -314 627 C ATOM 662 CD2 PHE A 137 -18.773 28.885 -48.427 1.00 93.63 C ANISOU 662 CD2 PHE A 137 13380 10933 11263 -2096 -562 537 C ATOM 663 CE1 PHE A 137 -16.598 29.222 -50.091 1.00 96.22 C ANISOU 663 CE1 PHE A 137 13902 11395 11261 -2466 -189 687 C ATOM 664 CE2 PHE A 137 -17.859 29.894 -48.175 1.00 93.61 C ANISOU 664 CE2 PHE A 137 13390 10817 11363 -2222 -452 584 C ATOM 665 CZ PHE A 137 -16.770 30.062 -49.008 1.00 94.68 C ANISOU 665 CZ PHE A 137 13614 11020 11341 -2419 -270 664 C ATOM 666 N GLY A 138 -21.181 24.920 -51.340 1.00111.53 N ANISOU 666 N GLY A 138 15934 13702 12741 -2017 -876 443 N ATOM 667 CA GLY A 138 -22.144 23.864 -51.587 1.00108.76 C ANISOU 667 CA GLY A 138 15588 13437 12298 -1983 -1026 360 C ATOM 668 C GLY A 138 -22.940 23.465 -50.363 1.00104.39 C ANISOU 668 C GLY A 138 14805 12859 12002 -1868 -1111 240 C ATOM 669 O GLY A 138 -22.766 24.029 -49.282 1.00103.32 O ANISOU 669 O GLY A 138 14514 12638 12106 -1796 -1057 215 O ATOM 670 N ASP A 139 -23.827 22.491 -50.541 1.00108.77 N ANISOU 670 N ASP A 139 15348 13488 12492 -1869 -1240 163 N ATOM 671 CA ASP A 139 -24.566 21.915 -49.429 1.00105.62 C ANISOU 671 CA ASP A 139 14743 13087 12303 -1796 -1285 41 C ATOM 672 C ASP A 139 -23.565 21.106 -48.622 1.00102.53 C ANISOU 672 C ASP A 139 14305 12703 11947 -1787 -1051 -123 C ATOM 673 O ASP A 139 -23.648 21.021 -47.397 1.00100.58 O ANISOU 673 O ASP A 139 13894 12420 11904 -1713 -1003 -202 O ATOM 674 CB ASP A 139 -25.704 21.026 -49.929 1.00127.69 C ANISOU 674 CB ASP A 139 17549 15964 15004 -1847 -1476 1 C ATOM 675 CG ASP A 139 -26.680 20.652 -48.829 1.00125.75 C ANISOU 675 CG ASP A 139 17067 15719 14994 -1792 -1540 -83 C ATOM 676 OD1 ASP A 139 -26.567 21.203 -47.715 1.00124.75 O ANISOU 676 OD1 ASP A 139 16784 15527 15090 -1693 -1454 -97 O ATOM 677 OD2 ASP A 139 -27.561 19.803 -49.078 1.00125.58 O ANISOU 677 OD2 ASP A 139 17022 15768 14924 -1863 -1670 -140 O ATOM 678 N ALA A 140 -22.619 20.505 -49.336 1.00 84.15 N ANISOU 678 N ALA A 140 12133 10431 9410 -1850 -908 -174 N ATOM 679 CA ALA A 140 -21.538 19.755 -48.718 1.00 82.29 C ANISOU 679 CA ALA A 140 11861 10210 9196 -1815 -690 -319 C ATOM 680 C ALA A 140 -20.649 20.701 -47.926 1.00 82.87 C ANISOU 680 C ALA A 140 11804 10242 9442 -1771 -570 -287 C ATOM 681 O ALA A 140 -20.212 20.378 -46.824 1.00 80.62 O ANISOU 681 O ALA A 140 11389 9943 9300 -1700 -484 -389 O ATOM 682 CB ALA A 140 -20.728 19.024 -49.773 1.00 72.03 C ANISOU 682 CB ALA A 140 10749 8984 7634 -1872 -554 -379 C ATOM 683 N GLY A 141 -20.386 21.874 -48.494 1.00 89.75 N ANISOU 683 N GLY A 141 12728 11085 10288 -1826 -576 -142 N ATOM 684 CA GLY A 141 -19.578 22.879 -47.829 1.00 90.17 C ANISOU 684 CA GLY A 141 12678 11080 10504 -1824 -480 -108 C ATOM 685 C GLY A 141 -20.264 23.414 -46.587 1.00 88.10 C ANISOU 685 C GLY A 141 12263 10718 10494 -1733 -584 -123 C ATOM 686 O GLY A 141 -19.608 23.826 -45.633 1.00 86.60 O ANISOU 686 O GLY A 141 11958 10490 10456 -1710 -501 -177 O ATOM 687 N CYS A 142 -21.592 23.405 -46.604 1.00 84.78 N ANISOU 687 N CYS A 142 11832 10266 10113 -1684 -765 -86 N ATOM 688 CA CYS A 142 -22.382 23.819 -45.452 1.00 83.45 C ANISOU 688 CA CYS A 142 11511 10023 10173 -1582 -845 -117 C ATOM 689 C CYS A 142 -22.304 22.756 -44.364 1.00 79.68 C ANISOU 689 C CYS A 142 10923 9597 9755 -1535 -763 -282 C ATOM 690 O CYS A 142 -22.037 23.057 -43.200 1.00 77.83 O ANISOU 690 O CYS A 142 10584 9319 9668 -1478 -705 -350 O ATOM 691 CB CYS A 142 -23.839 24.049 -45.857 1.00113.69 C ANISOU 691 CB CYS A 142 15327 13839 14033 -1537 -1056 -31 C ATOM 692 SG CYS A 142 -24.964 24.339 -44.472 1.00112.63 S ANISOU 692 SG CYS A 142 14971 13654 14168 -1398 -1121 -100 S ATOM 693 N ARG A 143 -22.541 21.509 -44.759 1.00 94.52 N ANISOU 693 N ARG A 143 12855 11555 11502 -1566 -766 -344 N ATOM 694 CA ARG A 143 -22.504 20.385 -43.835 1.00 91.70 C ANISOU 694 CA ARG A 143 12443 11224 11176 -1530 -695 -480 C ATOM 695 C ARG A 143 -21.074 20.066 -43.410 1.00 90.94 C ANISOU 695 C ARG A 143 12349 11146 11059 -1504 -529 -558 C ATOM 696 O ARG A 143 -20.826 19.715 -42.258 1.00 89.59 O ANISOU 696 O ARG A 143 12099 10963 10976 -1440 -477 -641 O ATOM 697 CB ARG A 143 -23.146 19.151 -44.469 1.00 99.28 C ANISOU 697 CB ARG A 143 13493 12230 11999 -1589 -751 -523 C ATOM 698 CG ARG A 143 -24.653 19.243 -44.629 1.00100.32 C ANISOU 698 CG ARG A 143 13558 12374 12185 -1617 -929 -475 C ATOM 699 CD ARG A 143 -25.202 17.991 -45.290 1.00100.13 C ANISOU 699 CD ARG A 143 13635 12392 12016 -1717 -992 -532 C ATOM 700 NE ARG A 143 -26.499 17.605 -44.742 1.00 99.81 N ANISOU 700 NE ARG A 143 13461 12372 12092 -1750 -1092 -556 N ATOM 701 CZ ARG A 143 -27.669 17.937 -45.279 1.00101.53 C ANISOU 701 CZ ARG A 143 13594 12644 12339 -1792 -1282 -488 C ATOM 702 NH1 ARG A 143 -27.712 18.663 -46.388 1.00104.18 N ANISOU 702 NH1 ARG A 143 14002 13004 12576 -1797 -1410 -380 N ATOM 703 NH2 ARG A 143 -28.797 17.539 -44.706 1.00101.47 N ANISOU 703 NH2 ARG A 143 13422 12676 12455 -1833 -1344 -522 N ATOM 704 N GLY A 144 -20.140 20.187 -44.347 1.00 81.66 N ANISOU 704 N GLY A 144 11258 10012 9759 -1552 -447 -529 N ATOM 705 CA GLY A 144 -18.745 19.890 -44.076 1.00 81.37 C ANISOU 705 CA GLY A 144 11183 10023 9710 -1523 -288 -604 C ATOM 706 C GLY A 144 -18.092 20.899 -43.153 1.00 81.07 C ANISOU 706 C GLY A 144 11008 9959 9836 -1509 -257 -598 C ATOM 707 O GLY A 144 -17.196 20.553 -42.382 1.00 80.41 O ANISOU 707 O GLY A 144 10833 9916 9804 -1452 -179 -686 O ATOM 708 N TYR A 145 -18.533 22.151 -43.235 1.00100.36 N ANISOU 708 N TYR A 145 13445 12327 12360 -1556 -332 -498 N ATOM 709 CA TYR A 145 -18.021 23.199 -42.359 1.00100.19 C ANISOU 709 CA TYR A 145 13324 12246 12497 -1562 -319 -504 C ATOM 710 C TYR A 145 -18.302 22.857 -40.902 1.00 97.72 C ANISOU 710 C TYR A 145 12916 11917 12296 -1464 -348 -613 C ATOM 711 O TYR A 145 -17.380 22.709 -40.100 1.00 97.36 O ANISOU 711 O TYR A 145 12786 11913 12292 -1440 -292 -698 O ATOM 712 CB TYR A 145 -18.646 24.552 -42.709 1.00 96.73 C ANISOU 712 CB TYR A 145 12940 11682 12129 -1608 -411 -377 C ATOM 713 CG TYR A 145 -18.314 25.653 -41.724 1.00 96.88 C ANISOU 713 CG TYR A 145 12890 11596 12323 -1613 -415 -404 C ATOM 714 CD1 TYR A 145 -17.127 26.368 -41.825 1.00 97.63 C ANISOU 714 CD1 TYR A 145 12968 11682 12445 -1729 -331 -388 C ATOM 715 CD2 TYR A 145 -19.191 25.983 -40.697 1.00 96.12 C ANISOU 715 CD2 TYR A 145 12747 11413 12360 -1514 -495 -457 C ATOM 716 CE1 TYR A 145 -16.819 27.373 -40.927 1.00 97.34 C ANISOU 716 CE1 TYR A 145 12888 11535 12563 -1759 -349 -429 C ATOM 717 CE2 TYR A 145 -18.892 26.985 -39.796 1.00 96.75 C ANISOU 717 CE2 TYR A 145 12796 11385 12580 -1519 -498 -505 C ATOM 718 CZ TYR A 145 -17.706 27.678 -39.916 1.00 97.30 C ANISOU 718 CZ TYR A 145 12867 11428 12672 -1647 -437 -493 C ATOM 719 OH TYR A 145 -17.407 28.678 -39.020 1.00 97.07 O ANISOU 719 OH TYR A 145 12826 11277 12780 -1677 -454 -556 O ATOM 720 N TYR A 146 -19.582 22.732 -40.569 1.00 97.19 N ANISOU 720 N TYR A 146 12855 11802 12269 -1410 -439 -609 N ATOM 721 CA TYR A 146 -19.999 22.445 -39.202 1.00 95.64 C ANISOU 721 CA TYR A 146 12590 11593 12157 -1329 -448 -702 C ATOM 722 C TYR A 146 -19.518 21.081 -38.709 1.00 93.86 C ANISOU 722 C TYR A 146 12369 11442 11851 -1286 -389 -789 C ATOM 723 O TYR A 146 -19.341 20.880 -37.507 1.00 93.37 O ANISOU 723 O TYR A 146 12265 11382 11828 -1229 -375 -863 O ATOM 724 CB TYR A 146 -21.521 22.549 -39.074 1.00 88.03 C ANISOU 724 CB TYR A 146 11608 10589 11253 -1292 -532 -675 C ATOM 725 CG TYR A 146 -22.057 23.963 -39.149 1.00 89.76 C ANISOU 725 CG TYR A 146 11806 10703 11595 -1272 -600 -610 C ATOM 726 CD1 TYR A 146 -22.136 24.757 -38.011 1.00 89.86 C ANISOU 726 CD1 TYR A 146 11766 10640 11736 -1212 -586 -677 C ATOM 727 CD2 TYR A 146 -22.490 24.502 -40.354 1.00 92.06 C ANISOU 727 CD2 TYR A 146 12155 10959 11865 -1303 -685 -483 C ATOM 728 CE1 TYR A 146 -22.629 26.047 -38.070 1.00 92.31 C ANISOU 728 CE1 TYR A 146 12081 10821 12170 -1171 -644 -629 C ATOM 729 CE2 TYR A 146 -22.985 25.793 -40.423 1.00 95.06 C ANISOU 729 CE2 TYR A 146 12538 11213 12367 -1259 -760 -411 C ATOM 730 CZ TYR A 146 -23.051 26.561 -39.278 1.00 95.17 C ANISOU 730 CZ TYR A 146 12498 11132 12528 -1186 -734 -489 C ATOM 731 OH TYR A 146 -23.543 27.846 -39.342 1.00 99.07 O ANISOU 731 OH TYR A 146 13019 11470 13155 -1121 -804 -429 O ATOM 732 N PHE A 147 -19.312 20.145 -39.631 1.00 82.30 N ANISOU 732 N PHE A 147 10980 10026 10263 -1305 -358 -780 N ATOM 733 CA PHE A 147 -18.792 18.829 -39.272 1.00 81.57 C ANISOU 733 CA PHE A 147 10923 9971 10098 -1243 -301 -858 C ATOM 734 C PHE A 147 -17.330 18.906 -38.850 1.00 81.74 C ANISOU 734 C PHE A 147 10867 10051 10140 -1193 -234 -909 C ATOM 735 O PHE A 147 -16.957 18.416 -37.783 1.00 80.96 O ANISOU 735 O PHE A 147 10737 9961 10062 -1109 -237 -970 O ATOM 736 CB PHE A 147 -18.941 17.849 -40.438 1.00 86.21 C ANISOU 736 CB PHE A 147 11635 10575 10547 -1272 -281 -855 C ATOM 737 CG PHE A 147 -18.278 16.520 -40.201 1.00 86.11 C ANISOU 737 CG PHE A 147 11688 10567 10465 -1187 -213 -939 C ATOM 738 CD1 PHE A 147 -18.920 15.532 -39.473 1.00 85.07 C ANISOU 738 CD1 PHE A 147 11626 10373 10326 -1156 -240 -974 C ATOM 739 CD2 PHE A 147 -17.018 16.255 -40.715 1.00 87.79 C ANISOU 739 CD2 PHE A 147 11893 10842 10623 -1134 -115 -978 C ATOM 740 CE1 PHE A 147 -18.314 14.309 -39.253 1.00 85.77 C ANISOU 740 CE1 PHE A 147 11807 10427 10352 -1061 -188 -1037 C ATOM 741 CE2 PHE A 147 -16.408 15.034 -40.499 1.00 88.74 C ANISOU 741 CE2 PHE A 147 12074 10950 10695 -1015 -59 -1057 C ATOM 742 CZ PHE A 147 -17.057 14.060 -39.768 1.00 87.47 C ANISOU 742 CZ PHE A 147 12015 10695 10526 -973 -105 -1082 C ATOM 743 N LEU A 148 -16.506 19.513 -39.698 1.00 88.99 N ANISOU 743 N LEU A 148 11749 11018 11046 -1251 -179 -877 N ATOM 744 CA LEU A 148 -15.083 19.669 -39.417 1.00 89.92 C ANISOU 744 CA LEU A 148 11743 11221 11201 -1228 -112 -925 C ATOM 745 C LEU A 148 -14.888 20.491 -38.148 1.00 88.69 C ANISOU 745 C LEU A 148 11485 11045 11170 -1229 -177 -957 C ATOM 746 O LEU A 148 -13.989 20.222 -37.349 1.00 88.86 O ANISOU 746 O LEU A 148 11407 11134 11222 -1163 -181 -1026 O ATOM 747 CB LEU A 148 -14.369 20.334 -40.595 1.00 77.79 C ANISOU 747 CB LEU A 148 10182 9743 9632 -1336 -20 -869 C ATOM 748 CG LEU A 148 -12.861 20.542 -40.442 1.00 79.66 C ANISOU 748 CG LEU A 148 10244 10100 9922 -1343 69 -917 C ATOM 749 CD1 LEU A 148 -12.139 19.205 -40.356 1.00 80.70 C ANISOU 749 CD1 LEU A 148 10335 10325 10003 -1186 135 -1009 C ATOM 750 CD2 LEU A 148 -12.311 21.378 -41.590 1.00 82.20 C ANISOU 750 CD2 LEU A 148 10553 10469 10212 -1499 177 -840 C ATOM 751 N ARG A 149 -15.740 21.497 -37.977 1.00 86.71 N ANISOU 751 N ARG A 149 11263 10698 10985 -1293 -239 -912 N ATOM 752 CA ARG A 149 -15.675 22.382 -36.823 1.00 85.92 C ANISOU 752 CA ARG A 149 11104 10552 10991 -1302 -297 -959 C ATOM 753 C ARG A 149 -15.911 21.610 -35.529 1.00 84.69 C ANISOU 753 C ARG A 149 10955 10411 10813 -1191 -336 -1039 C ATOM 754 O ARG A 149 -15.192 21.799 -34.551 1.00 84.93 O ANISOU 754 O ARG A 149 10919 10479 10870 -1171 -371 -1110 O ATOM 755 CB ARG A 149 -16.688 23.520 -36.964 1.00139.06 C ANISOU 755 CB ARG A 149 17891 17151 17796 -1355 -345 -901 C ATOM 756 CG ARG A 149 -16.161 24.719 -37.738 1.00141.69 C ANISOU 756 CG ARG A 149 18222 17430 18184 -1483 -328 -829 C ATOM 757 CD ARG A 149 -15.063 25.441 -36.976 1.00141.88 C ANISOU 757 CD ARG A 149 18153 17462 18292 -1554 -329 -903 C ATOM 758 NE ARG A 149 -15.607 26.357 -35.978 1.00142.21 N ANISOU 758 NE ARG A 149 18230 17371 18432 -1543 -400 -959 N ATOM 759 CZ ARG A 149 -15.787 27.658 -36.183 1.00144.05 C ANISOU 759 CZ ARG A 149 18526 17446 18761 -1628 -424 -917 C ATOM 760 NH1 ARG A 149 -15.464 28.198 -37.350 1.00145.59 N ANISOU 760 NH1 ARG A 149 18761 17600 18957 -1747 -386 -797 N ATOM 761 NH2 ARG A 149 -16.289 28.420 -35.221 1.00144.59 N ANISOU 761 NH2 ARG A 149 18640 17384 18914 -1592 -477 -997 N ATOM 762 N ASP A 150 -16.915 20.738 -35.527 1.00 79.15 N ANISOU 762 N ASP A 150 10341 9681 10050 -1137 -337 -1023 N ATOM 763 CA ASP A 150 -17.205 19.917 -34.355 1.00 78.30 C ANISOU 763 CA ASP A 150 10276 9578 9897 -1051 -355 -1075 C ATOM 764 C ASP A 150 -16.141 18.850 -34.118 1.00 78.56 C ANISOU 764 C ASP A 150 10305 9682 9862 -960 -347 -1108 C ATOM 765 O ASP A 150 -15.687 18.659 -32.990 1.00 78.55 O ANISOU 765 O ASP A 150 10293 9710 9841 -893 -392 -1156 O ATOM 766 CB ASP A 150 -18.581 19.255 -34.474 1.00 89.46 C ANISOU 766 CB ASP A 150 11776 10941 11273 -1053 -344 -1041 C ATOM 767 CG ASP A 150 -19.706 20.159 -34.012 1.00 89.96 C ANISOU 767 CG ASP A 150 11815 10951 11414 -1079 -360 -1040 C ATOM 768 OD1 ASP A 150 -19.662 21.371 -34.311 1.00 90.74 O ANISOU 768 OD1 ASP A 150 11866 11012 11601 -1113 -382 -1027 O ATOM 769 OD2 ASP A 150 -20.634 19.654 -33.344 1.00 89.65 O ANISOU 769 OD2 ASP A 150 11808 10903 11352 -1063 -339 -1053 O ATOM 770 N ALA A 151 -15.741 18.170 -35.189 1.00 79.35 N ANISOU 770 N ALA A 151 10422 9809 9918 -945 -295 -1086 N ATOM 771 CA ALA A 151 -14.777 17.075 -35.107 1.00 81.02 C ANISOU 771 CA ALA A 151 10633 10072 10077 -821 -276 -1122 C ATOM 772 C ALA A 151 -13.432 17.501 -34.523 1.00 82.39 C ANISOU 772 C ALA A 151 10642 10354 10308 -774 -311 -1170 C ATOM 773 O ALA A 151 -12.837 16.778 -33.724 1.00 83.35 O ANISOU 773 O ALA A 151 10756 10511 10403 -642 -363 -1202 O ATOM 774 CB ALA A 151 -14.579 16.444 -36.477 1.00 76.78 C ANISOU 774 CB ALA A 151 10145 9545 9484 -817 -191 -1111 C ATOM 775 N CYS A 152 -12.958 18.676 -34.921 1.00 90.63 N ANISOU 775 N CYS A 152 11556 11448 11431 -889 -296 -1168 N ATOM 776 CA CYS A 152 -11.667 19.171 -34.458 1.00 92.13 C ANISOU 776 CA CYS A 152 11556 11756 11692 -890 -333 -1220 C ATOM 777 C CYS A 152 -11.666 19.494 -32.965 1.00 91.56 C ANISOU 777 C CYS A 152 11478 11680 11630 -868 -463 -1271 C ATOM 778 O CYS A 152 -10.671 19.266 -32.277 1.00 93.22 O ANISOU 778 O CYS A 152 11571 11997 11851 -791 -541 -1322 O ATOM 779 CB CYS A 152 -11.235 20.394 -35.269 1.00 89.18 C ANISOU 779 CB CYS A 152 11072 11412 11400 -1066 -274 -1196 C ATOM 780 SG CYS A 152 -10.734 20.021 -36.964 1.00 91.81 S ANISOU 780 SG CYS A 152 11375 11819 11690 -1092 -105 -1152 S ATOM 781 N THR A 153 -12.782 20.022 -32.469 1.00 97.13 N ANISOU 781 N THR A 153 12306 12274 12325 -926 -487 -1264 N ATOM 782 CA THR A 153 -12.898 20.366 -31.054 1.00 96.83 C ANISOU 782 CA THR A 153 12301 12226 12264 -912 -588 -1325 C ATOM 783 C THR A 153 -12.843 19.123 -30.177 1.00 97.95 C ANISOU 783 C THR A 153 12532 12396 12290 -755 -642 -1327 C ATOM 784 O THR A 153 -12.233 19.136 -29.108 1.00 98.43 O ANISOU 784 O THR A 153 12567 12523 12310 -706 -754 -1379 O ATOM 785 CB THR A 153 -14.203 21.121 -30.750 1.00 99.12 C ANISOU 785 CB THR A 153 12706 12390 12564 -981 -567 -1326 C ATOM 786 OG1 THR A 153 -15.326 20.278 -31.036 1.00 99.14 O ANISOU 786 OG1 THR A 153 12830 12332 12505 -932 -503 -1267 O ATOM 787 CG2 THR A 153 -14.293 22.380 -31.585 1.00 99.01 C ANISOU 787 CG2 THR A 153 12642 12312 12665 -1116 -533 -1306 C ATOM 788 N TYR A 154 -13.487 18.052 -30.633 1.00 97.39 N ANISOU 788 N TYR A 154 12582 12264 12157 -687 -575 -1268 N ATOM 789 CA TYR A 154 -13.434 16.777 -29.930 1.00 98.79 C ANISOU 789 CA TYR A 154 12882 12429 12224 -542 -615 -1248 C ATOM 790 C TYR A 154 -12.001 16.263 -29.912 1.00100.94 C ANISOU 790 C TYR A 154 13029 12810 12512 -403 -685 -1269 C ATOM 791 O TYR A 154 -11.489 15.866 -28.867 1.00102.38 O ANISOU 791 O TYR A 154 13234 13037 12629 -292 -803 -1279 O ATOM 792 CB TYR A 154 -14.344 15.744 -30.597 1.00108.60 C ANISOU 792 CB TYR A 154 14284 13563 13417 -526 -523 -1187 C ATOM 793 CG TYR A 154 -15.821 15.937 -30.336 1.00106.94 C ANISOU 793 CG TYR A 154 14189 13265 13179 -632 -472 -1162 C ATOM 794 CD1 TYR A 154 -16.355 15.759 -29.067 1.00107.76 C ANISOU 794 CD1 TYR A 154 14407 13344 13191 -621 -493 -1161 C ATOM 795 CD2 TYR A 154 -16.686 16.278 -31.367 1.00105.61 C ANISOU 795 CD2 TYR A 154 14007 13053 13067 -738 -402 -1137 C ATOM 796 CE1 TYR A 154 -17.707 15.929 -28.832 1.00107.06 C ANISOU 796 CE1 TYR A 154 14387 13201 13090 -715 -419 -1146 C ATOM 797 CE2 TYR A 154 -18.036 16.451 -31.142 1.00104.71 C ANISOU 797 CE2 TYR A 154 13949 12883 12951 -820 -361 -1118 C ATOM 798 CZ TYR A 154 -18.542 16.275 -29.874 1.00105.76 C ANISOU 798 CZ TYR A 154 14166 13004 13014 -809 -357 -1128 C ATOM 799 OH TYR A 154 -19.888 16.446 -29.651 1.00106.59 O ANISOU 799 OH TYR A 154 14292 13079 13130 -889 -290 -1117 O ATOM 800 N ALA A 155 -11.358 16.291 -31.075 1.00 91.49 N ANISOU 800 N ALA A 155 11695 11669 11397 -406 -612 -1275 N ATOM 801 CA ALA A 155 -9.976 15.843 -31.212 1.00 94.56 C ANISOU 801 CA ALA A 155 11910 12187 11830 -265 -647 -1306 C ATOM 802 C ALA A 155 -9.039 16.648 -30.319 1.00 95.11 C ANISOU 802 C ALA A 155 11786 12399 11953 -291 -788 -1362 C ATOM 803 O ALA A 155 -8.108 16.099 -29.729 1.00 97.71 O ANISOU 803 O ALA A 155 12018 12828 12278 -130 -904 -1381 O ATOM 804 CB ALA A 155 -9.531 15.928 -32.664 1.00 79.40 C ANISOU 804 CB ALA A 155 9868 10319 9980 -302 -503 -1312 C ATOM 805 N THR A 156 -9.286 17.950 -30.227 1.00101.52 N ANISOU 805 N THR A 156 12545 13210 12818 -491 -792 -1392 N ATOM 806 CA THR A 156 -8.484 18.814 -29.370 1.00101.90 C ANISOU 806 CA THR A 156 12435 13372 12912 -562 -934 -1464 C ATOM 807 C THR A 156 -8.737 18.495 -27.900 1.00102.30 C ANISOU 807 C THR A 156 12635 13405 12830 -474 -1092 -1481 C ATOM 808 O THR A 156 -7.801 18.269 -27.135 1.00104.74 O ANISOU 808 O THR A 156 12836 13842 13119 -380 -1256 -1516 O ATOM 809 CB THR A 156 -8.782 20.306 -29.624 1.00 81.44 C ANISOU 809 CB THR A 156 9809 10730 10405 -806 -895 -1496 C ATOM 810 OG1 THR A 156 -8.392 20.657 -30.957 1.00 81.97 O ANISOU 810 OG1 THR A 156 9740 10830 10577 -904 -758 -1465 O ATOM 811 CG2 THR A 156 -8.023 21.174 -28.633 1.00 81.76 C ANISOU 811 CG2 THR A 156 9727 10860 10479 -901 -1058 -1591 C ATOM 812 N ALA A 157 -10.010 18.475 -27.517 1.00 93.41 N ANISOU 812 N ALA A 157 11751 12134 11607 -506 -1042 -1454 N ATOM 813 CA ALA A 157 -10.403 18.228 -26.132 1.00 93.92 C ANISOU 813 CA ALA A 157 11996 12176 11513 -451 -1150 -1466 C ATOM 814 C ALA A 157 -9.985 16.848 -25.624 1.00 96.32 C ANISOU 814 C ALA A 157 12386 12507 11705 -234 -1240 -1402 C ATOM 815 O ALA A 157 -9.669 16.685 -24.445 1.00 97.52 O ANISOU 815 O ALA A 157 12610 12713 11730 -164 -1399 -1414 O ATOM 816 CB ALA A 157 -11.905 18.423 -25.967 1.00 69.20 C ANISOU 816 CB ALA A 157 9077 8898 8317 -530 -1029 -1446 C ATOM 817 N LEU A 158 -9.982 15.858 -26.512 1.00 85.19 N ANISOU 817 N LEU A 158 10992 11047 10330 -122 -1147 -1335 N ATOM 818 CA LEU A 158 -9.610 14.499 -26.127 1.00 88.47 C ANISOU 818 CA LEU A 158 11520 11440 10655 105 -1224 -1267 C ATOM 819 C LEU A 158 -8.098 14.337 -26.000 1.00 90.98 C ANISOU 819 C LEU A 158 11595 11929 11042 265 -1381 -1300 C ATOM 820 O LEU A 158 -7.620 13.554 -25.180 1.00 93.72 O ANISOU 820 O LEU A 158 12016 12297 11295 457 -1539 -1257 O ATOM 821 CB LEU A 158 -10.179 13.473 -27.110 1.00 88.02 C ANISOU 821 CB LEU A 158 11598 11237 10608 167 -1068 -1203 C ATOM 822 CG LEU A 158 -11.695 13.257 -27.089 1.00 86.05 C ANISOU 822 CG LEU A 158 11602 10820 10271 43 -944 -1152 C ATOM 823 CD1 LEU A 158 -12.108 12.245 -28.146 1.00 86.75 C ANISOU 823 CD1 LEU A 158 11804 10776 10379 86 -817 -1108 C ATOM 824 CD2 LEU A 158 -12.163 12.819 -25.708 1.00 87.11 C ANISOU 824 CD2 LEU A 158 11972 10900 10227 77 -1023 -1098 C ATOM 825 N ASN A 159 -7.350 15.074 -26.815 1.00 87.53 N ANISOU 825 N ASN A 159 10865 11621 10772 184 -1338 -1368 N ATOM 826 CA ASN A 159 -5.895 15.088 -26.701 1.00 90.94 C ANISOU 826 CA ASN A 159 10992 12259 11301 300 -1479 -1415 C ATOM 827 C ASN A 159 -5.459 15.698 -25.371 1.00 90.73 C ANISOU 827 C ASN A 159 10919 12349 11204 256 -1722 -1462 C ATOM 828 O ASN A 159 -4.499 15.241 -24.747 1.00 93.03 O ANISOU 828 O ASN A 159 11087 12776 11484 435 -1924 -1463 O ATOM 829 CB ASN A 159 -5.262 15.851 -27.867 1.00123.40 C ANISOU 829 CB ASN A 159 14799 16489 15599 166 -1347 -1475 C ATOM 830 CG ASN A 159 -5.255 15.050 -29.155 1.00125.42 C ANISOU 830 CG ASN A 159 15050 16695 15909 278 -1145 -1445 C ATOM 831 OD1 ASN A 159 -5.112 13.828 -29.138 1.00127.99 O ANISOU 831 OD1 ASN A 159 15473 16966 16191 529 -1159 -1408 O ATOM 832 ND2 ASN A 159 -5.407 15.737 -30.281 1.00124.30 N ANISOU 832 ND2 ASN A 159 14822 16558 15850 93 -959 -1463 N ATOM 833 N VAL A 160 -6.174 16.737 -24.950 1.00117.40 N ANISOU 833 N VAL A 160 14403 15672 14533 27 -1708 -1509 N ATOM 834 CA VAL A 160 -5.893 17.419 -23.693 1.00117.21 C ANISOU 834 CA VAL A 160 14385 15735 14413 -51 -1922 -1580 C ATOM 835 C VAL A 160 -6.042 16.474 -22.504 1.00119.37 C ANISOU 835 C VAL A 160 14906 15986 14464 141 -2086 -1512 C ATOM 836 O VAL A 160 -5.177 16.423 -21.628 1.00121.61 O ANISOU 836 O VAL A 160 15105 16419 14683 226 -2338 -1538 O ATOM 837 CB VAL A 160 -6.825 18.632 -23.497 1.00112.67 C ANISOU 837 CB VAL A 160 13944 15054 13813 -306 -1834 -1650 C ATOM 838 CG1 VAL A 160 -6.671 19.206 -22.102 1.00113.36 C ANISOU 838 CG1 VAL A 160 14119 15202 13750 -370 -2044 -1737 C ATOM 839 CG2 VAL A 160 -6.546 19.692 -24.552 1.00111.34 C ANISOU 839 CG2 VAL A 160 13547 14902 13854 -509 -1715 -1707 C ATOM 840 N VAL A 161 -7.140 15.726 -22.483 1.00117.18 N ANISOU 840 N VAL A 161 14937 15523 14063 197 -1950 -1419 N ATOM 841 CA VAL A 161 -7.388 14.761 -21.418 1.00118.91 C ANISOU 841 CA VAL A 161 15441 15685 14053 359 -2068 -1325 C ATOM 842 C VAL A 161 -6.343 13.650 -21.438 1.00122.41 C ANISOU 842 C VAL A 161 15795 16194 14523 648 -2226 -1250 C ATOM 843 O VAL A 161 -5.846 13.234 -20.392 1.00124.64 O ANISOU 843 O VAL A 161 16163 16543 14653 793 -2463 -1207 O ATOM 844 CB VAL A 161 -8.798 14.148 -21.532 1.00 90.83 C ANISOU 844 CB VAL A 161 12211 11911 10390 326 -1856 -1234 C ATOM 845 CG1 VAL A 161 -9.024 13.117 -20.436 1.00 93.07 C ANISOU 845 CG1 VAL A 161 12813 12123 10426 471 -1962 -1117 C ATOM 846 CG2 VAL A 161 -9.856 15.239 -21.470 1.00 87.98 C ANISOU 846 CG2 VAL A 161 11913 11498 10017 79 -1705 -1311 C ATOM 847 N SER A 162 -6.006 13.186 -22.638 1.00 87.52 N ANISOU 847 N SER A 162 11210 11755 10289 743 -2096 -1238 N ATOM 848 CA SER A 162 -5.012 12.132 -22.810 1.00 91.20 C ANISOU 848 CA SER A 162 11566 12270 10817 1050 -2209 -1185 C ATOM 849 C SER A 162 -3.636 12.562 -22.313 1.00 92.65 C ANISOU 849 C SER A 162 11407 12721 11074 1132 -2473 -1252 C ATOM 850 O SER A 162 -2.921 11.777 -21.691 1.00 95.76 O ANISOU 850 O SER A 162 11799 13172 11413 1399 -2696 -1190 O ATOM 851 CB SER A 162 -4.930 11.712 -24.277 1.00 91.30 C ANISOU 851 CB SER A 162 11453 12224 11014 1108 -1981 -1196 C ATOM 852 OG SER A 162 -6.189 11.264 -24.745 1.00 89.99 O ANISOU 852 OG SER A 162 11595 11819 10778 1025 -1769 -1139 O ATOM 853 N LEU A 163 -3.270 13.808 -22.594 1.00105.12 N ANISOU 853 N LEU A 163 12697 14459 12784 897 -2458 -1375 N ATOM 854 CA LEU A 163 -2.010 14.357 -22.107 1.00106.37 C ANISOU 854 CA LEU A 163 12505 14887 13022 904 -2713 -1457 C ATOM 855 C LEU A 163 -2.028 14.455 -20.587 1.00106.93 C ANISOU 855 C LEU A 163 12771 15002 12856 913 -3005 -1446 C ATOM 856 O LEU A 163 -1.016 14.219 -19.930 1.00109.46 O ANISOU 856 O LEU A 163 12917 15510 13163 1076 -3298 -1448 O ATOM 857 CB LEU A 163 -1.744 15.729 -22.726 1.00100.74 C ANISOU 857 CB LEU A 163 11498 14292 12488 591 -2612 -1587 C ATOM 858 CG LEU A 163 -1.094 15.716 -24.109 1.00101.86 C ANISOU 858 CG LEU A 163 11296 14524 12880 605 -2415 -1614 C ATOM 859 CD1 LEU A 163 -1.029 17.121 -24.685 1.00 99.40 C ANISOU 859 CD1 LEU A 163 10786 14273 12707 249 -2293 -1713 C ATOM 860 CD2 LEU A 163 0.294 15.095 -24.035 1.00105.73 C ANISOU 860 CD2 LEU A 163 11428 15253 13493 870 -2596 -1623 C ATOM 861 N SER A 164 -3.186 14.802 -20.035 1.00126.97 N ANISOU 861 N SER A 164 15666 17378 15199 742 -2923 -1438 N ATOM 862 CA SER A 164 -3.359 14.863 -18.589 1.00127.42 C ANISOU 862 CA SER A 164 15980 17457 14977 738 -3154 -1428 C ATOM 863 C SER A 164 -3.224 13.470 -17.986 1.00130.39 C ANISOU 863 C SER A 164 16584 17774 15183 1059 -3308 -1263 C ATOM 864 O SER A 164 -2.711 13.306 -16.881 1.00132.85 O ANISOU 864 O SER A 164 16967 18198 15311 1164 -3612 -1237 O ATOM 865 CB SER A 164 -4.716 15.470 -18.232 1.00110.67 C ANISOU 865 CB SER A 164 14191 15166 12693 503 -2968 -1458 C ATOM 866 OG SER A 164 -4.812 16.807 -18.691 1.00108.03 O ANISOU 866 OG SER A 164 13676 14863 12509 226 -2860 -1607 O ATOM 867 N VAL A 165 -3.686 12.468 -18.724 1.00102.33 N ANISOU 867 N VAL A 165 13166 14030 11684 1211 -3107 -1151 N ATOM 868 CA VAL A 165 -3.547 11.083 -18.299 1.00105.77 C ANISOU 868 CA VAL A 165 13837 14358 11991 1527 -3230 -985 C ATOM 869 C VAL A 165 -2.089 10.651 -18.383 1.00108.51 C ANISOU 869 C VAL A 165 13840 14898 12490 1821 -3484 -983 C ATOM 870 O VAL A 165 -1.534 10.118 -17.422 1.00110.34 O ANISOU 870 O VAL A 165 14160 15194 12570 2037 -3790 -897 O ATOM 871 CB VAL A 165 -4.404 10.135 -19.159 1.00106.60 C ANISOU 871 CB VAL A 165 14176 14188 12139 1592 -2941 -887 C ATOM 872 CG1 VAL A 165 -4.046 8.688 -18.868 1.00110.53 C ANISOU 872 CG1 VAL A 165 14881 14555 12559 1946 -3077 -725 C ATOM 873 CG2 VAL A 165 -5.884 10.386 -18.915 1.00103.99 C ANISOU 873 CG2 VAL A 165 14196 13678 11638 1334 -2721 -864 C ATOM 874 N GLU A 166 -1.473 10.892 -19.537 1.00113.88 N ANISOU 874 N GLU A 166 14122 15681 13467 1830 -3355 -1076 N ATOM 875 CA GLU A 166 -0.096 10.477 -19.779 1.00117.46 C ANISOU 875 CA GLU A 166 14182 16336 14111 2119 -3540 -1091 C ATOM 876 C GLU A 166 0.909 11.190 -18.883 1.00117.37 C ANISOU 876 C GLU A 166 13876 16634 14087 2086 -3899 -1166 C ATOM 877 O GLU A 166 1.907 10.599 -18.469 1.00119.53 O ANISOU 877 O GLU A 166 13968 17056 14392 2390 -4184 -1121 O ATOM 878 CB GLU A 166 0.281 10.673 -21.251 1.00193.33 C ANISOU 878 CB GLU A 166 23429 26005 24024 2090 -3270 -1188 C ATOM 879 CG GLU A 166 -0.423 9.721 -22.195 1.00193.68 C ANISOU 879 CG GLU A 166 23722 25772 24096 2212 -2976 -1120 C ATOM 880 CD GLU A 166 0.453 8.551 -22.590 1.00198.30 C ANISOU 880 CD GLU A 166 24177 26357 24813 2639 -3027 -1078 C ATOM 881 OE1 GLU A 166 1.490 8.775 -23.250 1.00199.80 O ANISOU 881 OE1 GLU A 166 23900 26778 25238 2728 -3007 -1177 O ATOM 882 OE2 GLU A 166 0.109 7.406 -22.229 1.00200.14 O ANISOU 882 OE2 GLU A 166 24777 26352 24914 2887 -3080 -946 O ATOM 883 N LEU A 167 0.646 12.459 -18.584 1.00134.13 N ANISOU 883 N LEU A 167 15951 18848 16166 1722 -3897 -1287 N ATOM 884 CA LEU A 167 1.541 13.221 -17.725 1.00134.68 C ANISOU 884 CA LEU A 167 15763 19200 16209 1633 -4242 -1383 C ATOM 885 C LEU A 167 1.421 12.750 -16.278 1.00136.07 C ANISOU 885 C LEU A 167 16296 19360 16046 1770 -4567 -1282 C ATOM 886 O LEU A 167 2.407 12.732 -15.544 1.00137.92 O ANISOU 886 O LEU A 167 16329 19828 16246 1899 -4945 -1293 O ATOM 887 CB LEU A 167 1.248 14.721 -17.822 1.00130.68 C ANISOU 887 CB LEU A 167 15159 18747 15745 1194 -4137 -1551 C ATOM 888 CG LEU A 167 2.278 15.634 -17.153 1.00131.16 C ANISOU 888 CG LEU A 167 14885 19109 15841 1040 -4469 -1690 C ATOM 889 CD1 LEU A 167 3.631 15.477 -17.834 1.00133.32 C ANISOU 889 CD1 LEU A 167 14574 19651 16430 1182 -4555 -1728 C ATOM 890 CD2 LEU A 167 1.825 17.085 -17.185 1.00128.29 C ANISOU 890 CD2 LEU A 167 14538 18717 15489 601 -4349 -1851 C ATOM 891 N TYR A 168 0.211 12.367 -15.874 1.00121.46 N ANISOU 891 N TYR A 168 14969 17243 13937 1734 -4420 -1180 N ATOM 892 CA TYR A 168 -0.021 11.852 -14.526 1.00122.61 C ANISOU 892 CA TYR A 168 15523 17345 13719 1851 -4678 -1059 C ATOM 893 C TYR A 168 0.723 10.540 -14.300 1.00126.05 C ANISOU 893 C TYR A 168 15969 17783 14143 2293 -4924 -886 C ATOM 894 O TYR A 168 1.362 10.346 -13.267 1.00127.70 O ANISOU 894 O TYR A 168 16213 18140 14168 2445 -5316 -831 O ATOM 895 CB TYR A 168 -1.519 11.648 -14.271 1.00139.17 C ANISOU 895 CB TYR A 168 18157 19152 15569 1709 -4403 -977 C ATOM 896 CG TYR A 168 -1.849 11.068 -12.907 1.00140.46 C ANISOU 896 CG TYR A 168 18791 19252 15324 1807 -4613 -832 C ATOM 897 CD1 TYR A 168 -2.053 11.898 -11.811 1.00139.74 C ANISOU 897 CD1 TYR A 168 18871 19272 14951 1592 -4761 -921 C ATOM 898 CD2 TYR A 168 -1.962 9.695 -12.715 1.00142.94 C ANISOU 898 CD2 TYR A 168 19410 19382 15519 2108 -4657 -607 C ATOM 899 CE1 TYR A 168 -2.357 11.379 -10.566 1.00141.20 C ANISOU 899 CE1 TYR A 168 19510 19412 14726 1670 -4939 -786 C ATOM 900 CE2 TYR A 168 -2.261 9.167 -11.470 1.00144.50 C ANISOU 900 CE2 TYR A 168 20067 19515 15320 2183 -4842 -453 C ATOM 901 CZ TYR A 168 -2.460 10.014 -10.401 1.00143.42 C ANISOU 901 CZ TYR A 168 20087 19516 14889 1960 -4978 -540 C ATOM 902 OH TYR A 168 -2.760 9.497 -9.161 1.00145.23 O ANISOU 902 OH TYR A 168 20797 19693 14689 2023 -5148 -384 O ATOM 903 N LEU A 169 0.628 9.638 -15.272 1.00131.55 N ANISOU 903 N LEU A 169 16654 18303 15027 2507 -4703 -802 N ATOM 904 CA LEU A 169 1.266 8.332 -15.171 1.00135.10 C ANISOU 904 CA LEU A 169 17144 18694 15494 2959 -4895 -639 C ATOM 905 C LEU A 169 2.784 8.447 -15.243 1.00137.50 C ANISOU 905 C LEU A 169 16883 19331 16031 3183 -5203 -714 C ATOM 906 O LEU A 169 3.504 7.629 -14.673 1.00139.89 O ANISOU 906 O LEU A 169 17190 19683 16280 3554 -5529 -590 O ATOM 907 CB LEU A 169 0.751 7.394 -16.265 1.00142.54 C ANISOU 907 CB LEU A 169 18227 19344 16589 3107 -4553 -567 C ATOM 908 CG LEU A 169 -0.755 7.125 -16.249 1.00141.30 C ANISOU 908 CG LEU A 169 18606 18854 16226 2901 -4252 -480 C ATOM 909 CD1 LEU A 169 -1.144 6.149 -17.350 1.00142.58 C ANISOU 909 CD1 LEU A 169 18885 18738 16549 3053 -3961 -424 C ATOM 910 CD2 LEU A 169 -1.193 6.607 -14.887 1.00142.12 C ANISOU 910 CD2 LEU A 169 19214 18840 15943 2956 -4462 -302 C ATOM 911 N ALA A 170 3.265 9.467 -15.946 1.00164.09 N ANISOU 911 N ALA A 170 19759 22929 19661 2955 -5100 -909 N ATOM 912 CA ALA A 170 4.700 9.683 -16.096 1.00165.61 C ANISOU 912 CA ALA A 170 19342 23472 20109 3109 -5351 -1001 C ATOM 913 C ALA A 170 5.324 10.131 -14.779 1.00166.22 C ANISOU 913 C ALA A 170 19355 23808 19993 3079 -5835 -1016 C ATOM 914 O ALA A 170 6.519 9.945 -14.551 1.00169.67 O ANISOU 914 O ALA A 170 19381 24522 20564 3322 -6169 -1026 O ATOM 915 CB ALA A 170 4.972 10.704 -17.190 1.00153.88 C ANISOU 915 CB ALA A 170 17386 22148 18932 2810 -5081 -1195 C ATOM 916 N ILE A 171 4.504 10.722 -13.916 1.00134.15 N ANISOU 916 N ILE A 171 15696 19663 15611 2784 -5872 -1026 N ATOM 917 CA ILE A 171 4.966 11.212 -12.623 1.00134.85 C ANISOU 917 CA ILE A 171 15805 19977 15455 2708 -6318 -1058 C ATOM 918 C ILE A 171 4.752 10.179 -11.521 1.00137.02 C ANISOU 918 C ILE A 171 16578 20122 15363 3009 -6596 -834 C ATOM 919 O ILE A 171 5.681 9.836 -10.789 1.00139.52 O ANISOU 919 O ILE A 171 16755 20647 15608 3263 -7050 -772 O ATOM 920 CB ILE A 171 4.247 12.515 -12.224 1.00113.61 C ANISOU 920 CB ILE A 171 13289 17282 12594 2215 -6214 -1221 C ATOM 921 CG1 ILE A 171 4.489 13.600 -13.274 1.00111.34 C ANISOU 921 CG1 ILE A 171 12538 17106 12659 1900 -5964 -1428 C ATOM 922 CG2 ILE A 171 4.718 12.986 -10.859 1.00117.65 C ANISOU 922 CG2 ILE A 171 13867 18018 12815 2134 -6684 -1271 C ATOM 923 CD1 ILE A 171 3.812 14.918 -12.965 1.00109.12 C ANISOU 923 CD1 ILE A 171 12421 16788 12252 1434 -5853 -1598 C ATOM 924 N CYS A 172 3.524 9.682 -11.414 1.00164.81 N ANISOU 924 N CYS A 172 20673 23298 18650 2972 -6325 -704 N ATOM 925 CA CYS A 172 3.150 8.777 -10.331 1.00166.39 C ANISOU 925 CA CYS A 172 21430 23336 18453 3181 -6533 -478 C ATOM 926 C CYS A 172 3.710 7.370 -10.509 1.00169.00 C ANISOU 926 C CYS A 172 21781 23555 18877 3695 -6681 -267 C ATOM 927 O CYS A 172 4.250 6.787 -9.568 1.00172.04 O ANISOU 927 O CYS A 172 22314 24006 19048 3974 -7099 -114 O ATOM 928 CB CYS A 172 1.629 8.724 -10.185 1.00170.77 C ANISOU 928 CB CYS A 172 22569 23570 18746 2939 -6160 -413 C ATOM 929 SG CYS A 172 0.881 10.309 -9.760 1.00167.88 S ANISOU 929 SG CYS A 172 22276 23300 18211 2394 -6010 -648 S ATOM 930 N HIS A 173 3.582 6.826 -11.714 1.00156.64 N ANISOU 930 N HIS A 173 20086 21809 17621 3829 -6347 -259 N ATOM 931 CA HIS A 173 4.097 5.492 -12.003 1.00159.48 C ANISOU 931 CA HIS A 173 20468 22022 18105 4331 -6442 -86 C ATOM 932 C HIS A 173 5.076 5.510 -13.173 1.00160.84 C ANISOU 932 C HIS A 173 19990 22373 18749 4520 -6361 -225 C ATOM 933 O HIS A 173 4.743 5.061 -14.269 1.00160.16 O ANISOU 933 O HIS A 173 19898 22077 18877 4582 -5990 -242 O ATOM 934 CB HIS A 173 2.949 4.524 -12.302 1.00186.62 C ANISOU 934 CB HIS A 173 24483 24999 21423 4372 -6103 83 C ATOM 935 CG HIS A 173 1.942 4.420 -11.198 1.00186.33 C ANISOU 935 CG HIS A 173 25090 24780 20926 4184 -6127 234 C ATOM 936 ND1 HIS A 173 0.969 5.369 -10.986 1.00183.76 N ANISOU 936 ND1 HIS A 173 24931 24461 20428 3717 -5893 124 N ATOM 937 CD2 HIS A 173 1.762 3.474 -10.244 1.00188.37 C ANISOU 937 CD2 HIS A 173 25872 24845 20855 4404 -6345 491 C ATOM 938 CE1 HIS A 173 0.228 5.014 -9.949 1.00184.10 C ANISOU 938 CE1 HIS A 173 25554 24343 20054 3651 -5944 294 C ATOM 939 NE2 HIS A 173 0.690 3.869 -9.482 1.00187.06 N ANISOU 939 NE2 HIS A 173 26166 24592 20316 4049 -6217 526 N ATOM 940 N PRO A 174 6.291 6.031 -12.942 1.00235.82 N ANISOU 940 N PRO A 174 28931 32270 28399 4600 -6705 -333 N ATOM 941 CA PRO A 174 7.281 6.149 -14.016 1.00236.68 C ANISOU 941 CA PRO A 174 28363 32606 28959 4747 -6615 -482 C ATOM 942 C PRO A 174 7.830 4.790 -14.434 1.00239.82 C ANISOU 942 C PRO A 174 28725 32862 29532 5326 -6655 -349 C ATOM 943 O PRO A 174 8.326 4.647 -15.551 1.00239.62 O ANISOU 943 O PRO A 174 28283 32898 29862 5467 -6419 -458 O ATOM 944 CB PRO A 174 8.384 6.997 -13.381 1.00193.59 C ANISOU 944 CB PRO A 174 22385 27615 23555 4670 -7043 -602 C ATOM 945 CG PRO A 174 8.286 6.696 -11.930 1.00194.55 C ANISOU 945 CG PRO A 174 22936 27717 23267 4773 -7485 -436 C ATOM 946 CD PRO A 174 6.822 6.500 -11.650 1.00192.85 C ANISOU 946 CD PRO A 174 23462 27102 22708 4559 -7204 -322 C ATOM 947 N PHE A 175 7.740 3.808 -13.542 1.00287.49 N ANISOU 947 N PHE A 175 35219 38702 35314 5659 -6944 -116 N ATOM 948 CA PHE A 175 8.219 2.464 -13.844 1.00290.60 C ANISOU 948 CA PHE A 175 35659 38903 35854 6241 -7008 27 C ATOM 949 C PHE A 175 7.169 1.644 -14.586 1.00290.35 C ANISOU 949 C PHE A 175 36139 38378 35803 6258 -6560 106 C ATOM 950 O PHE A 175 7.506 0.813 -15.428 1.00292.01 O ANISOU 950 O PHE A 175 36245 38436 36269 6621 -6403 103 O ATOM 951 CB PHE A 175 8.658 1.738 -12.567 1.00282.16 C ANISOU 951 CB PHE A 175 34862 37821 34525 6621 -7550 262 C ATOM 952 CG PHE A 175 7.588 1.660 -11.510 1.00281.34 C ANISOU 952 CG PHE A 175 35505 37464 33927 6385 -7615 445 C ATOM 953 CD1 PHE A 175 7.365 2.725 -10.653 1.00279.33 C ANISOU 953 CD1 PHE A 175 35285 37448 33400 5966 -7782 375 C ATOM 954 CD2 PHE A 175 6.813 0.520 -11.369 1.00282.32 C ANISOU 954 CD2 PHE A 175 36305 37110 33854 6572 -7496 681 C ATOM 955 CE1 PHE A 175 6.386 2.660 -9.681 1.00278.30 C ANISOU 955 CE1 PHE A 175 35834 37105 32802 5753 -7809 531 C ATOM 956 CE2 PHE A 175 5.833 0.449 -10.394 1.00281.21 C ANISOU 956 CE2 PHE A 175 36836 36757 33253 6335 -7527 854 C ATOM 957 CZ PHE A 175 5.619 1.521 -9.552 1.00279.15 C ANISOU 957 CZ PHE A 175 36587 36759 32716 5933 -7673 776 C ATOM 958 N LYS A 176 5.896 1.875 -14.281 1.00309.59 N ANISOU 958 N LYS A 176 39119 40569 37942 5865 -6352 164 N ATOM 959 CA LYS A 176 4.837 1.169 -14.989 1.00308.52 C ANISOU 959 CA LYS A 176 39448 39987 37789 5815 -5929 225 C ATOM 960 C LYS A 176 4.575 1.775 -16.362 1.00307.32 C ANISOU 960 C LYS A 176 38967 39879 37922 5543 -5469 -3 C ATOM 961 O LYS A 176 4.346 1.055 -17.321 1.00308.32 O ANISOU 961 O LYS A 176 39189 39749 38210 5695 -5176 -15 O ATOM 962 CB LYS A 176 3.538 1.173 -14.175 1.00201.65 C ANISOU 962 CB LYS A 176 26587 26191 23842 5486 -5856 372 C ATOM 963 CG LYS A 176 3.564 0.290 -12.935 1.00204.69 C ANISOU 963 CG LYS A 176 27477 26402 23894 5763 -6224 651 C ATOM 964 CD LYS A 176 2.418 0.612 -11.980 1.00202.39 C ANISOU 964 CD LYS A 176 27740 25990 23168 5365 -6175 758 C ATOM 965 CE LYS A 176 1.113 0.884 -12.720 1.00199.23 C ANISOU 965 CE LYS A 176 27551 25367 22782 4943 -5652 673 C ATOM 966 NZ LYS A 176 0.632 -0.292 -13.497 1.00200.08 N ANISOU 966 NZ LYS A 176 27973 25045 23003 5121 -5383 775 N ATOM 967 N ALA A 177 4.683 3.092 -16.475 1.00220.05 N ANISOU 967 N ALA A 177 27521 29155 26933 5158 -5421 -187 N ATOM 968 CA ALA A 177 4.331 3.764 -17.722 1.00217.92 C ANISOU 968 CA ALA A 177 26998 28915 26885 4850 -4988 -380 C ATOM 969 C ALA A 177 5.499 3.973 -18.682 1.00219.22 C ANISOU 969 C ALA A 177 26484 29372 27437 5027 -4931 -550 C ATOM 970 O ALA A 177 5.323 4.562 -19.749 1.00218.01 O ANISOU 970 O ALA A 177 26095 29274 27465 4778 -4581 -706 O ATOM 971 CB ALA A 177 3.667 5.102 -17.413 1.00134.16 C ANISOU 971 CB ALA A 177 16398 18442 16135 4305 -4907 -482 C ATOM 972 N LYS A 178 6.685 3.502 -18.308 1.00259.04 N ANISOU 972 N LYS A 178 31207 34612 32603 5455 -5272 -515 N ATOM 973 CA LYS A 178 7.861 3.638 -19.162 1.00259.69 C ANISOU 973 CA LYS A 178 30603 35003 33063 5656 -5220 -674 C ATOM 974 C LYS A 178 7.787 2.739 -20.392 1.00260.95 C ANISOU 974 C LYS A 178 30811 34918 33423 5927 -4848 -710 C ATOM 975 O LYS A 178 8.065 3.173 -21.512 1.00260.58 O ANISOU 975 O LYS A 178 30370 35022 33618 5809 -4528 -886 O ATOM 976 CB LYS A 178 9.135 3.309 -18.370 1.00189.03 C ANISOU 976 CB LYS A 178 21288 26339 24196 6080 -5715 -620 C ATOM 977 CG LYS A 178 10.441 3.361 -19.171 1.00190.36 C ANISOU 977 CG LYS A 178 20690 26863 24774 6341 -5682 -780 C ATOM 978 CD LYS A 178 11.130 4.716 -19.027 1.00189.88 C ANISOU 978 CD LYS A 178 20014 27295 24838 5971 -5813 -945 C ATOM 979 CE LYS A 178 12.535 4.698 -19.613 1.00192.11 C ANISOU 979 CE LYS A 178 19497 27977 25518 6260 -5850 -1079 C ATOM 980 NZ LYS A 178 12.501 4.497 -21.087 1.00189.48 N ANISOU 980 NZ LYS A 178 18998 27565 25431 6294 -5317 -1206 N ATOM 981 N THR A 179 7.419 1.481 -20.172 1.00223.99 N ANISOU 981 N THR A 179 26636 29847 28622 6281 -4890 -544 N ATOM 982 CA THR A 179 7.355 0.498 -21.247 1.00225.69 C ANISOU 982 CA THR A 179 26970 29780 29003 6580 -4573 -579 C ATOM 983 C THR A 179 5.944 0.203 -21.782 1.00224.57 C ANISOU 983 C THR A 179 27431 29203 28693 6296 -4202 -548 C ATOM 984 O THR A 179 5.791 -0.419 -22.838 1.00225.70 O ANISOU 984 O THR A 179 27660 29131 28965 6432 -3884 -625 O ATOM 985 CB THR A 179 8.052 -0.811 -20.805 1.00188.23 C ANISOU 985 CB THR A 179 22339 24872 24307 7237 -4860 -438 C ATOM 986 OG1 THR A 179 9.359 -0.494 -20.310 1.00189.35 O ANISOU 986 OG1 THR A 179 21870 25456 24617 7495 -5228 -471 O ATOM 987 CG2 THR A 179 8.204 -1.780 -21.967 1.00189.61 C ANISOU 987 CG2 THR A 179 22548 24797 24700 7595 -4539 -522 C ATOM 988 N LEU A 180 4.908 0.680 -21.099 1.00236.72 N ANISOU 988 N LEU A 180 29366 30631 29948 5887 -4227 -455 N ATOM 989 CA LEU A 180 3.541 0.352 -21.521 1.00235.50 C ANISOU 989 CA LEU A 180 29769 30076 29636 5622 -3905 -413 C ATOM 990 C LEU A 180 3.170 0.947 -22.880 1.00234.20 C ANISOU 990 C LEU A 180 29397 29959 29627 5316 -3475 -609 C ATOM 991 O LEU A 180 2.715 0.222 -23.765 1.00235.90 O ANISOU 991 O LEU A 180 29860 29884 29889 5388 -3197 -639 O ATOM 992 CB LEU A 180 2.505 0.771 -20.464 1.00164.14 C ANISOU 992 CB LEU A 180 21161 20940 20263 5251 -4009 -277 C ATOM 993 CG LEU A 180 2.345 -0.119 -19.222 1.00165.77 C ANISOU 993 CG LEU A 180 21868 20910 20206 5485 -4322 -28 C ATOM 994 CD1 LEU A 180 1.212 0.370 -18.307 1.00159.24 C ANISOU 994 CD1 LEU A 180 21462 20003 19038 5060 -4330 77 C ATOM 995 CD2 LEU A 180 2.176 -1.584 -19.590 1.00169.18 C ANISOU 995 CD2 LEU A 180 22718 20900 20664 5847 -4236 85 C ATOM 996 N MET A 181 3.303 2.260 -23.037 1.00193.98 N ANISOU 996 N MET A 181 23902 25208 24595 4956 -3423 -736 N ATOM 997 CA MET A 181 3.021 2.865 -24.338 1.00192.39 C ANISOU 997 CA MET A 181 23500 25066 24534 4676 -3032 -905 C ATOM 998 C MET A 181 4.192 2.860 -25.330 1.00193.83 C ANISOU 998 C MET A 181 23128 25500 25017 4917 -2903 -1066 C ATOM 999 O MET A 181 5.171 3.595 -25.158 1.00193.84 O ANISOU 999 O MET A 181 22592 25892 25167 4912 -3045 -1143 O ATOM 1000 CB MET A 181 2.481 4.290 -24.153 1.00218.38 C ANISOU 1000 CB MET A 181 26683 28547 27745 4148 -2987 -960 C ATOM 1001 CG MET A 181 1.225 4.341 -23.299 1.00214.15 C ANISOU 1001 CG MET A 181 26679 27772 26918 3889 -3038 -829 C ATOM 1002 SD MET A 181 -0.059 3.304 -24.009 1.00211.60 S ANISOU 1002 SD MET A 181 26933 26970 26495 3864 -2726 -764 S ATOM 1003 CE MET A 181 -0.347 4.181 -25.541 1.00204.12 C ANISOU 1003 CE MET A 181 25707 26134 25714 3537 -2334 -953 C ATOM 1004 N SER A 182 4.085 2.032 -26.365 1.00170.62 N ANISOU 1004 N SER A 182 20324 22342 22163 5114 -2624 -1125 N ATOM 1005 CA SER A 182 5.038 2.048 -27.470 1.00171.89 C ANISOU 1005 CA SER A 182 20002 22724 22583 5298 -2405 -1299 C ATOM 1006 C SER A 182 4.485 2.984 -28.551 1.00169.86 C ANISOU 1006 C SER A 182 19655 22550 22334 4834 -2041 -1424 C ATOM 1007 O SER A 182 3.267 3.113 -28.681 1.00168.37 O ANISOU 1007 O SER A 182 19895 22113 21967 4516 -1913 -1377 O ATOM 1008 CB SER A 182 5.281 0.635 -28.013 1.00153.98 C ANISOU 1008 CB SER A 182 17942 20173 20392 5792 -2297 -1316 C ATOM 1009 OG SER A 182 4.073 -0.020 -28.356 1.00154.11 O ANISOU 1009 OG SER A 182 18582 19741 20232 5674 -2114 -1267 O ATOM 1010 N ARG A 183 5.362 3.649 -29.301 1.00149.54 N ANISOU 1010 N ARG A 183 16526 20329 19962 4787 -1882 -1572 N ATOM 1011 CA ARG A 183 4.933 4.541 -30.387 1.00147.69 C ANISOU 1011 CA ARG A 183 16204 20179 19732 4365 -1535 -1676 C ATOM 1012 C ARG A 183 3.912 3.888 -31.321 1.00147.77 C ANISOU 1012 C ARG A 183 16706 19826 19616 4316 -1237 -1695 C ATOM 1013 O ARG A 183 3.082 4.571 -31.920 1.00146.09 O ANISOU 1013 O ARG A 183 16632 19567 19308 3911 -1036 -1715 O ATOM 1014 CB ARG A 183 6.131 5.040 -31.197 1.00255.86 C ANISOU 1014 CB ARG A 183 29268 34275 33671 4408 -1356 -1830 C ATOM 1015 CG ARG A 183 7.041 5.968 -30.414 1.00256.16 C ANISOU 1015 CG ARG A 183 28777 34713 33840 4303 -1620 -1833 C ATOM 1016 CD ARG A 183 7.645 7.040 -31.309 1.00256.00 C ANISOU 1016 CD ARG A 183 28247 35043 33977 3998 -1361 -1961 C ATOM 1017 NE ARG A 183 8.612 6.491 -32.254 1.00258.11 N ANISOU 1017 NE ARG A 183 28143 35487 34441 4320 -1109 -2090 N ATOM 1018 CZ ARG A 183 9.925 6.450 -32.045 1.00260.22 C ANISOU 1018 CZ ARG A 183 27815 36112 34946 4582 -1221 -2157 C ATOM 1019 NH1 ARG A 183 10.441 6.937 -30.924 1.00260.47 N ANISOU 1019 NH1 ARG A 183 27561 36366 35040 4542 -1610 -2105 N ATOM 1020 NH2 ARG A 183 10.725 5.928 -32.965 1.00262.77 N ANISOU 1020 NH2 ARG A 183 27817 36584 35440 4882 -943 -2287 N ATOM 1021 N SER A 184 3.994 2.567 -31.451 1.00166.86 N ANISOU 1021 N SER A 184 19382 21979 22037 4734 -1223 -1692 N ATOM 1022 CA SER A 184 3.034 1.803 -32.236 1.00166.80 C ANISOU 1022 CA SER A 184 19885 21590 21901 4708 -984 -1714 C ATOM 1023 C SER A 184 1.648 1.913 -31.606 1.00165.32 C ANISOU 1023 C SER A 184 20200 21125 21488 4376 -1089 -1570 C ATOM 1024 O SER A 184 0.651 2.102 -32.302 1.00164.03 O ANISOU 1024 O SER A 184 20303 20809 21212 4061 -880 -1595 O ATOM 1025 CB SER A 184 3.467 0.336 -32.317 1.00165.08 C ANISOU 1025 CB SER A 184 19867 21114 21742 5249 -997 -1735 C ATOM 1026 OG SER A 184 2.537 -0.443 -33.046 1.00164.82 O ANISOU 1026 OG SER A 184 20357 20687 21580 5206 -784 -1768 O ATOM 1027 N ARG A 185 1.596 1.796 -30.283 1.00130.82 N ANISOU 1027 N ARG A 185 15949 16708 17049 4449 -1414 -1420 N ATOM 1028 CA ARG A 185 0.336 1.893 -29.552 1.00129.41 C ANISOU 1028 CA ARG A 185 16221 16296 16653 4150 -1511 -1279 C ATOM 1029 C ARG A 185 -0.184 3.328 -29.493 1.00126.96 C ANISOU 1029 C ARG A 185 15744 16203 16293 3661 -1473 -1292 C ATOM 1030 O ARG A 185 -1.386 3.567 -29.609 1.00125.95 O ANISOU 1030 O ARG A 185 15929 15901 16025 3334 -1368 -1254 O ATOM 1031 CB ARG A 185 0.482 1.340 -28.131 1.00192.78 C ANISOU 1031 CB ARG A 185 24441 24219 24588 4381 -1861 -1110 C ATOM 1032 CG ARG A 185 0.716 -0.162 -28.042 1.00195.91 C ANISOU 1032 CG ARG A 185 25158 24287 24991 4842 -1924 -1049 C ATOM 1033 CD ARG A 185 -0.427 -0.959 -28.656 1.00196.18 C ANISOU 1033 CD ARG A 185 25737 23894 24908 4722 -1701 -1040 C ATOM 1034 NE ARG A 185 -0.128 -1.371 -30.024 1.00197.14 N ANISOU 1034 NE ARG A 185 25779 23966 25160 4862 -1415 -1220 N ATOM 1035 CZ ARG A 185 0.496 -2.500 -30.343 1.00199.18 C ANISOU 1035 CZ ARG A 185 26136 24029 25515 5322 -1394 -1266 C ATOM 1036 NH1 ARG A 185 0.885 -3.337 -29.391 1.00201.05 N ANISOU 1036 NH1 ARG A 185 26556 24089 25744 5695 -1662 -1125 N ATOM 1037 NH2 ARG A 185 0.731 -2.794 -31.615 1.00199.38 N ANISOU 1037 NH2 ARG A 185 26096 24027 25635 5420 -1105 -1453 N ATOM 1038 N THR A 186 0.730 4.278 -29.309 1.00125.92 N ANISOU 1038 N THR A 186 15112 16445 16287 3615 -1564 -1349 N ATOM 1039 CA THR A 186 0.370 5.690 -29.201 1.00122.72 C ANISOU 1039 CA THR A 186 14537 16237 15855 3173 -1549 -1368 C ATOM 1040 C THR A 186 -0.231 6.236 -30.492 1.00122.00 C ANISOU 1040 C THR A 186 14455 16127 15774 2869 -1217 -1455 C ATOM 1041 O THR A 186 -1.226 6.960 -30.461 1.00119.69 O ANISOU 1041 O THR A 186 14334 15767 15375 2511 -1166 -1423 O ATOM 1042 CB THR A 186 1.587 6.550 -28.806 1.00119.33 C ANISOU 1042 CB THR A 186 13554 16206 15580 3182 -1715 -1426 C ATOM 1043 OG1 THR A 186 2.126 6.076 -27.566 1.00120.22 O ANISOU 1043 OG1 THR A 186 13664 16353 15661 3459 -2066 -1338 O ATOM 1044 CG2 THR A 186 1.187 8.011 -28.650 1.00115.95 C ANISOU 1044 CG2 THR A 186 13006 15931 15121 2717 -1707 -1449 C ATOM 1045 N LYS A 187 0.370 5.878 -31.623 1.00120.61 N ANISOU 1045 N LYS A 187 14100 16011 15716 3028 -992 -1565 N ATOM 1046 CA LYS A 187 -0.146 6.291 -32.923 1.00119.71 C ANISOU 1046 CA LYS A 187 14026 15878 15582 2769 -678 -1642 C ATOM 1047 C LYS A 187 -1.547 5.736 -33.147 1.00118.61 C ANISOU 1047 C LYS A 187 14422 15380 15263 2639 -599 -1587 C ATOM 1048 O LYS A 187 -2.402 6.400 -33.733 1.00116.40 O ANISOU 1048 O LYS A 187 14248 15069 14910 2300 -460 -1591 O ATOM 1049 CB LYS A 187 0.784 5.844 -34.053 1.00108.61 C ANISOU 1049 CB LYS A 187 12373 14593 14302 3006 -441 -1777 C ATOM 1050 CG LYS A 187 2.076 6.637 -34.150 1.00108.59 C ANISOU 1050 CG LYS A 187 11771 14998 14489 3016 -428 -1852 C ATOM 1051 CD LYS A 187 2.881 6.229 -35.374 1.00110.47 C ANISOU 1051 CD LYS A 187 11780 15363 14831 3217 -127 -1995 C ATOM 1052 CE LYS A 187 3.269 4.760 -35.321 1.00113.27 C ANISOU 1052 CE LYS A 187 12279 15535 15223 3731 -151 -2033 C ATOM 1053 NZ LYS A 187 4.063 4.351 -36.515 1.00114.88 N ANISOU 1053 NZ LYS A 187 12261 15866 15523 3951 168 -2197 N ATOM 1054 N LYS A 188 -1.774 4.515 -32.673 1.00116.68 N ANISOU 1054 N LYS A 188 14511 14864 14957 2907 -699 -1530 N ATOM 1055 CA LYS A 188 -3.085 3.889 -32.767 1.00115.32 C ANISOU 1055 CA LYS A 188 14848 14343 14625 2775 -646 -1471 C ATOM 1056 C LYS A 188 -4.096 4.646 -31.913 1.00112.57 C ANISOU 1056 C LYS A 188 14639 13973 14162 2437 -769 -1360 C ATOM 1057 O LYS A 188 -5.268 4.754 -32.270 1.00109.07 O ANISOU 1057 O LYS A 188 14453 13373 13615 2165 -664 -1339 O ATOM 1058 CB LYS A 188 -3.019 2.425 -32.328 1.00110.72 C ANISOU 1058 CB LYS A 188 14600 13459 14009 3132 -743 -1419 C ATOM 1059 CG LYS A 188 -2.333 1.502 -33.323 1.00111.66 C ANISOU 1059 CG LYS A 188 14713 13497 14216 3462 -571 -1550 C ATOM 1060 CD LYS A 188 -2.336 0.064 -32.829 1.00113.18 C ANISOU 1060 CD LYS A 188 15291 13335 14377 3813 -683 -1487 C ATOM 1061 CE LYS A 188 -1.762 -0.885 -33.870 1.00114.45 C ANISOU 1061 CE LYS A 188 15503 13365 14616 4144 -488 -1641 C ATOM 1062 NZ LYS A 188 -0.359 -0.536 -34.229 1.00116.58 N ANISOU 1062 NZ LYS A 188 15232 13987 15074 4415 -432 -1759 N ATOM 1063 N PHE A 189 -3.633 5.169 -30.782 1.00106.78 N ANISOU 1063 N PHE A 189 13724 13406 13442 2461 -994 -1297 N ATOM 1064 CA PHE A 189 -4.495 5.933 -29.889 1.00103.12 C ANISOU 1064 CA PHE A 189 13376 12941 12863 2167 -1104 -1212 C ATOM 1065 C PHE A 189 -4.822 7.313 -30.456 1.00 98.21 C ANISOU 1065 C PHE A 189 12537 12498 12281 1810 -980 -1274 C ATOM 1066 O PHE A 189 -5.931 7.815 -30.279 1.00 93.46 O ANISOU 1066 O PHE A 189 12117 11808 11585 1533 -949 -1233 O ATOM 1067 CB PHE A 189 -3.857 6.068 -28.506 1.00132.59 C ANISOU 1067 CB PHE A 189 17007 16799 16571 2305 -1394 -1142 C ATOM 1068 CG PHE A 189 -4.769 6.672 -27.477 1.00128.82 C ANISOU 1068 CG PHE A 189 16720 16288 15937 2045 -1499 -1060 C ATOM 1069 CD1 PHE A 189 -5.860 5.964 -27.001 1.00128.57 C ANISOU 1069 CD1 PHE A 189 17133 15980 15739 1993 -1490 -951 C ATOM 1070 CD2 PHE A 189 -4.540 7.948 -26.990 1.00125.30 C ANISOU 1070 CD2 PHE A 189 16016 16081 15510 1843 -1593 -1100 C ATOM 1071 CE1 PHE A 189 -6.704 6.515 -26.056 1.00124.58 C ANISOU 1071 CE1 PHE A 189 16790 15462 15082 1760 -1553 -887 C ATOM 1072 CE2 PHE A 189 -5.380 8.505 -26.045 1.00121.84 C ANISOU 1072 CE2 PHE A 189 15766 15608 14919 1623 -1669 -1047 C ATOM 1073 CZ PHE A 189 -6.464 7.787 -25.577 1.00121.66 C ANISOU 1073 CZ PHE A 189 16167 15333 14726 1590 -1640 -942 C ATOM 1074 N ILE A 190 -3.852 7.922 -31.133 1.00126.22 N ANISOU 1074 N ILE A 190 15695 16291 15974 1822 -904 -1370 N ATOM 1075 CA ILE A 190 -4.058 9.222 -31.767 1.00122.49 C ANISOU 1075 CA ILE A 190 15028 15968 15544 1491 -777 -1418 C ATOM 1076 C ILE A 190 -5.114 9.117 -32.861 1.00120.22 C ANISOU 1076 C ILE A 190 14987 15508 15185 1313 -558 -1425 C ATOM 1077 O ILE A 190 -5.989 9.977 -32.982 1.00115.05 O ANISOU 1077 O ILE A 190 14398 14831 14486 1020 -518 -1401 O ATOM 1078 CB ILE A 190 -2.752 9.771 -32.381 1.00 95.97 C ANISOU 1078 CB ILE A 190 11211 12901 12353 1533 -704 -1512 C ATOM 1079 CG1 ILE A 190 -1.692 9.974 -31.298 1.00 95.99 C ANISOU 1079 CG1 ILE A 190 10918 13112 12441 1678 -952 -1513 C ATOM 1080 CG2 ILE A 190 -3.011 11.079 -33.116 1.00 92.37 C ANISOU 1080 CG2 ILE A 190 10614 12554 11928 1175 -556 -1540 C ATOM 1081 CD1 ILE A 190 -2.074 10.996 -30.263 1.00 91.61 C ANISOU 1081 CD1 ILE A 190 10371 12606 11831 1428 -1137 -1474 C ATOM 1082 N SER A 191 -5.029 8.051 -33.649 1.00112.74 N ANISOU 1082 N SER A 191 14180 14431 14223 1504 -429 -1466 N ATOM 1083 CA SER A 191 -5.985 7.804 -34.720 1.00110.05 C ANISOU 1083 CA SER A 191 14093 13925 13796 1352 -245 -1487 C ATOM 1084 C SER A 191 -7.369 7.511 -34.153 1.00105.71 C ANISOU 1084 C SER A 191 13907 13135 13122 1202 -319 -1397 C ATOM 1085 O SER A 191 -8.381 7.926 -34.718 1.00101.24 O ANISOU 1085 O SER A 191 13462 12508 12496 946 -235 -1387 O ATOM 1086 CB SER A 191 -5.517 6.643 -35.601 1.00 95.55 C ANISOU 1086 CB SER A 191 12354 11989 11961 1612 -102 -1574 C ATOM 1087 OG SER A 191 -4.276 6.940 -36.216 1.00 98.93 O ANISOU 1087 OG SER A 191 12420 12666 12505 1739 12 -1668 O ATOM 1088 N ALA A 192 -7.403 6.794 -33.034 1.00 93.92 N ANISOU 1088 N ALA A 192 12578 11518 11588 1363 -479 -1326 N ATOM 1089 CA ALA A 192 -8.658 6.451 -32.373 1.00 90.39 C ANISOU 1089 CA ALA A 192 12467 10856 11020 1220 -536 -1232 C ATOM 1090 C ALA A 192 -9.396 7.704 -31.913 1.00 85.75 C ANISOU 1090 C ALA A 192 11793 10376 10411 923 -569 -1195 C ATOM 1091 O ALA A 192 -10.621 7.783 -32.008 1.00 82.75 O ANISOU 1091 O ALA A 192 11601 9878 9964 707 -516 -1159 O ATOM 1092 CB ALA A 192 -8.400 5.524 -31.196 1.00 69.26 C ANISOU 1092 CB ALA A 192 9975 8048 8290 1453 -702 -1145 C ATOM 1093 N ILE A 193 -8.642 8.676 -31.412 1.00104.98 N ANISOU 1093 N ILE A 193 13938 13035 12916 916 -660 -1212 N ATOM 1094 CA ILE A 193 -9.212 9.942 -30.965 1.00100.83 C ANISOU 1094 CA ILE A 193 13325 12602 12383 658 -691 -1199 C ATOM 1095 C ILE A 193 -9.889 10.682 -32.115 1.00 97.45 C ANISOU 1095 C ILE A 193 12857 12183 11988 422 -533 -1230 C ATOM 1096 O ILE A 193 -11.024 11.143 -31.984 1.00 94.36 O ANISOU 1096 O ILE A 193 12581 11720 11551 223 -513 -1196 O ATOM 1097 CB ILE A 193 -8.137 10.845 -30.328 1.00 92.14 C ANISOU 1097 CB ILE A 193 11915 11733 11360 685 -822 -1235 C ATOM 1098 CG1 ILE A 193 -7.676 10.255 -28.993 1.00 94.79 C ANISOU 1098 CG1 ILE A 193 12324 12067 11625 885 -1029 -1185 C ATOM 1099 CG2 ILE A 193 -8.667 12.256 -30.129 1.00 87.89 C ANISOU 1099 CG2 ILE A 193 11288 11269 10837 408 -821 -1251 C ATOM 1100 CD1 ILE A 193 -6.601 11.063 -28.303 1.00 95.96 C ANISOU 1100 CD1 ILE A 193 12169 12453 11839 910 -1198 -1229 C ATOM 1101 N TRP A 194 -9.192 10.779 -33.244 1.00103.23 N ANISOU 1101 N TRP A 194 13425 13007 12791 454 -419 -1292 N ATOM 1102 CA TRP A 194 -9.726 11.449 -34.426 1.00101.13 C ANISOU 1102 CA TRP A 194 13139 12756 12532 245 -278 -1309 C ATOM 1103 C TRP A 194 -11.001 10.792 -34.948 1.00 99.28 C ANISOU 1103 C TRP A 194 13199 12324 12199 157 -215 -1282 C ATOM 1104 O TRP A 194 -11.962 11.477 -35.296 1.00 95.62 O ANISOU 1104 O TRP A 194 12774 11838 11718 -56 -189 -1253 O ATOM 1105 CB TRP A 194 -8.673 11.509 -35.535 1.00 92.30 C ANISOU 1105 CB TRP A 194 11821 11776 11473 311 -145 -1378 C ATOM 1106 CG TRP A 194 -7.791 12.715 -35.458 1.00 92.89 C ANISOU 1106 CG TRP A 194 11570 12067 11655 218 -155 -1397 C ATOM 1107 CD1 TRP A 194 -6.484 12.754 -35.067 1.00 96.75 C ANISOU 1107 CD1 TRP A 194 11781 12734 12244 361 -203 -1442 C ATOM 1108 CD2 TRP A 194 -8.151 14.060 -35.788 1.00 89.60 C ANISOU 1108 CD2 TRP A 194 11071 11704 11268 -49 -123 -1370 C ATOM 1109 NE1 TRP A 194 -6.009 14.041 -35.130 1.00 95.07 N ANISOU 1109 NE1 TRP A 194 11316 12685 12120 166 -197 -1451 N ATOM 1110 CE2 TRP A 194 -7.015 14.865 -35.571 1.00 90.96 C ANISOU 1110 CE2 TRP A 194 10932 12072 11555 -84 -145 -1404 C ATOM 1111 CE3 TRP A 194 -9.327 14.667 -36.246 1.00 86.09 C ANISOU 1111 CE3 TRP A 194 10784 11154 10773 -258 -89 -1319 C ATOM 1112 CZ2 TRP A 194 -7.016 16.239 -35.794 1.00 88.79 C ANISOU 1112 CZ2 TRP A 194 10537 11860 11340 -334 -123 -1385 C ATOM 1113 CZ3 TRP A 194 -9.327 16.032 -36.467 1.00 84.14 C ANISOU 1113 CZ3 TRP A 194 10415 10970 10586 -469 -76 -1294 C ATOM 1114 CH2 TRP A 194 -8.180 16.803 -36.241 1.00 85.33 C ANISOU 1114 CH2 TRP A 194 10292 11285 10845 -513 -87 -1326 C ATOM 1115 N LEU A 195 -11.004 9.464 -35.000 1.00 98.64 N ANISOU 1115 N LEU A 195 13323 12094 12063 321 -202 -1293 N ATOM 1116 CA LEU A 195 -12.161 8.725 -35.492 1.00 97.46 C ANISOU 1116 CA LEU A 195 13459 11747 11823 220 -153 -1280 C ATOM 1117 C LEU A 195 -13.357 8.865 -34.558 1.00 94.64 C ANISOU 1117 C LEU A 195 13232 11299 11426 64 -231 -1199 C ATOM 1118 O LEU A 195 -14.489 9.034 -35.012 1.00 91.43 O ANISOU 1118 O LEU A 195 12915 10836 10989 -136 -197 -1182 O ATOM 1119 CB LEU A 195 -11.810 7.250 -35.692 1.00 81.89 C ANISOU 1119 CB LEU A 195 11702 9604 9809 435 -124 -1319 C ATOM 1120 CG LEU A 195 -10.745 6.984 -36.757 1.00 85.31 C ANISOU 1120 CG LEU A 195 12030 10114 10270 603 -2 -1423 C ATOM 1121 CD1 LEU A 195 -10.257 5.550 -36.681 1.00 88.78 C ANISOU 1121 CD1 LEU A 195 12671 10370 10693 883 5 -1466 C ATOM 1122 CD2 LEU A 195 -11.289 7.299 -38.144 1.00 83.73 C ANISOU 1122 CD2 LEU A 195 11878 9932 10005 409 126 -1474 C ATOM 1123 N ALA A 196 -13.103 8.794 -33.255 1.00 89.50 N ANISOU 1123 N ALA A 196 12584 10651 10770 157 -336 -1151 N ATOM 1124 CA ALA A 196 -14.153 8.998 -32.266 1.00 87.57 C ANISOU 1124 CA ALA A 196 12448 10352 10474 14 -384 -1081 C ATOM 1125 C ALA A 196 -14.706 10.411 -32.389 1.00 84.39 C ANISOU 1125 C ALA A 196 11864 10077 10123 -185 -368 -1089 C ATOM 1126 O ALA A 196 -15.900 10.642 -32.205 1.00 81.72 O ANISOU 1126 O ALA A 196 11596 9691 9763 -351 -345 -1057 O ATOM 1127 CB ALA A 196 -13.619 8.754 -30.865 1.00 81.70 C ANISOU 1127 CB ALA A 196 11742 9616 9684 161 -502 -1032 C ATOM 1128 N SER A 197 -13.827 11.352 -32.714 1.00 98.82 N ANISOU 1128 N SER A 197 13454 12063 12031 -165 -375 -1133 N ATOM 1129 CA SER A 197 -14.217 12.742 -32.901 1.00 95.86 C ANISOU 1129 CA SER A 197 12925 11778 11718 -338 -364 -1140 C ATOM 1130 C SER A 197 -15.140 12.893 -34.104 1.00 94.04 C ANISOU 1130 C SER A 197 12743 11500 11489 -487 -282 -1130 C ATOM 1131 O SER A 197 -16.088 13.678 -34.078 1.00 91.87 O ANISOU 1131 O SER A 197 12446 11221 11239 -630 -285 -1105 O ATOM 1132 CB SER A 197 -12.978 13.617 -33.080 1.00 78.68 C ANISOU 1132 CB SER A 197 10504 9763 9629 -305 -382 -1184 C ATOM 1133 OG SER A 197 -12.141 13.543 -31.940 1.00 80.42 O ANISOU 1133 OG SER A 197 10657 10051 9849 -179 -494 -1199 O ATOM 1134 N ALA A 198 -14.855 12.136 -35.158 1.00 90.56 N ANISOU 1134 N ALA A 198 12370 11023 11013 -439 -217 -1154 N ATOM 1135 CA ALA A 198 -15.659 12.181 -36.371 1.00 89.14 C ANISOU 1135 CA ALA A 198 12260 10807 10802 -577 -162 -1150 C ATOM 1136 C ALA A 198 -17.038 11.576 -36.133 1.00 87.52 C ANISOU 1136 C ALA A 198 12229 10475 10551 -684 -186 -1117 C ATOM 1137 O ALA A 198 -18.036 12.060 -36.665 1.00 85.48 O ANISOU 1137 O ALA A 198 11960 10220 10300 -838 -194 -1092 O ATOM 1138 CB ALA A 198 -14.947 11.460 -37.504 1.00 75.83 C ANISOU 1138 CB ALA A 198 10630 9118 9063 -493 -78 -1207 C ATOM 1139 N LEU A 199 -17.084 10.518 -35.329 1.00 84.98 N ANISOU 1139 N LEU A 199 12061 10043 10186 -604 -201 -1109 N ATOM 1140 CA LEU A 199 -18.343 9.864 -34.991 1.00 84.06 C ANISOU 1140 CA LEU A 199 12108 9804 10028 -729 -206 -1072 C ATOM 1141 C LEU A 199 -19.248 10.785 -34.177 1.00 82.67 C ANISOU 1141 C LEU A 199 11820 9693 9897 -848 -226 -1029 C ATOM 1142 O LEU A 199 -20.466 10.791 -34.356 1.00 81.76 O ANISOU 1142 O LEU A 199 11719 9554 9791 -1007 -217 -1007 O ATOM 1143 CB LEU A 199 -18.082 8.576 -34.207 1.00 74.37 C ANISOU 1143 CB LEU A 199 11094 8427 8737 -616 -212 -1054 C ATOM 1144 CG LEU A 199 -17.340 7.454 -34.935 1.00 76.63 C ANISOU 1144 CG LEU A 199 11541 8593 8980 -474 -184 -1107 C ATOM 1145 CD1 LEU A 199 -17.113 6.276 -34.000 1.00 78.97 C ANISOU 1145 CD1 LEU A 199 12067 8715 9224 -345 -210 -1065 C ATOM 1146 CD2 LEU A 199 -18.098 7.017 -36.181 1.00 75.42 C ANISOU 1146 CD2 LEU A 199 11509 8360 8787 -628 -144 -1154 C ATOM 1147 N LEU A 200 -18.644 11.565 -33.287 1.00 88.57 N ANISOU 1147 N LEU A 200 12447 10529 10677 -767 -254 -1028 N ATOM 1148 CA LEU A 200 -19.397 12.473 -32.430 1.00 87.57 C ANISOU 1148 CA LEU A 200 12231 10456 10585 -849 -258 -1011 C ATOM 1149 C LEU A 200 -19.848 13.718 -33.189 1.00 86.00 C ANISOU 1149 C LEU A 200 11864 10331 10480 -942 -260 -1021 C ATOM 1150 O LEU A 200 -20.760 14.423 -32.757 1.00 85.39 O ANISOU 1150 O LEU A 200 11716 10277 10450 -1015 -251 -1013 O ATOM 1151 CB LEU A 200 -18.564 12.873 -31.208 1.00 71.88 C ANISOU 1151 CB LEU A 200 10205 8527 8577 -738 -304 -1024 C ATOM 1152 CG LEU A 200 -18.137 11.754 -30.253 1.00 74.13 C ANISOU 1152 CG LEU A 200 10670 8742 8754 -626 -331 -991 C ATOM 1153 CD1 LEU A 200 -17.117 12.263 -29.246 1.00 75.05 C ANISOU 1153 CD1 LEU A 200 10719 8952 8847 -505 -418 -1013 C ATOM 1154 CD2 LEU A 200 -19.339 11.142 -29.547 1.00 74.71 C ANISOU 1154 CD2 LEU A 200 10907 8730 8750 -735 -272 -937 C ATOM 1155 N ALA A 201 -19.207 13.983 -34.323 1.00 92.50 N ANISOU 1155 N ALA A 201 12632 11187 11325 -928 -266 -1033 N ATOM 1156 CA ALA A 201 -19.522 15.162 -35.123 1.00 91.96 C ANISOU 1156 CA ALA A 201 12440 11170 11329 -1009 -278 -1019 C ATOM 1157 C ALA A 201 -20.546 14.851 -36.209 1.00 91.79 C ANISOU 1157 C ALA A 201 12470 11119 11287 -1119 -287 -990 C ATOM 1158 O ALA A 201 -20.973 15.740 -36.945 1.00 91.76 O ANISOU 1158 O ALA A 201 12390 11147 11329 -1183 -320 -957 O ATOM 1159 CB ALA A 201 -18.256 15.738 -35.736 1.00 86.82 C ANISOU 1159 CB ALA A 201 11704 10586 10699 -963 -270 -1034 C ATOM 1160 N ILE A 202 -20.931 13.582 -36.302 1.00 94.74 N ANISOU 1160 N ILE A 202 12988 11422 11588 -1145 -273 -999 N ATOM 1161 CA ILE A 202 -21.931 13.133 -37.274 1.00 94.61 C ANISOU 1161 CA ILE A 202 13032 11376 11538 -1275 -303 -987 C ATOM 1162 C ILE A 202 -23.269 13.905 -37.280 1.00 94.51 C ANISOU 1162 C ILE A 202 12888 11412 11611 -1383 -355 -946 C ATOM 1163 O ILE A 202 -23.771 14.230 -38.357 1.00 94.87 O ANISOU 1163 O ILE A 202 12904 11489 11652 -1457 -421 -922 O ATOM 1164 CB ILE A 202 -22.175 11.600 -37.176 1.00 87.21 C ANISOU 1164 CB ILE A 202 12293 10324 10519 -1310 -280 -1013 C ATOM 1165 CG1 ILE A 202 -20.955 10.838 -37.698 1.00 87.92 C ANISOU 1165 CG1 ILE A 202 12520 10359 10526 -1188 -241 -1065 C ATOM 1166 CG2 ILE A 202 -23.419 11.191 -37.951 1.00 87.17 C ANISOU 1166 CG2 ILE A 202 12327 10297 10495 -1490 -331 -1010 C ATOM 1167 CD1 ILE A 202 -21.136 9.337 -37.729 1.00 89.09 C ANISOU 1167 CD1 ILE A 202 12907 10350 10596 -1207 -222 -1099 C ATOM 1168 N PRO A 203 -23.845 14.209 -36.094 1.00 86.73 N ANISOU 1168 N PRO A 203 11820 10440 10695 -1380 -326 -939 N ATOM 1169 CA PRO A 203 -25.119 14.944 -36.084 1.00 87.63 C ANISOU 1169 CA PRO A 203 11776 10609 10910 -1451 -360 -913 C ATOM 1170 C PRO A 203 -25.128 16.237 -36.902 1.00 88.65 C ANISOU 1170 C PRO A 203 11789 10782 11110 -1420 -436 -878 C ATOM 1171 O PRO A 203 -26.183 16.623 -37.406 1.00 90.05 O ANISOU 1171 O PRO A 203 11863 10998 11354 -1475 -507 -843 O ATOM 1172 CB PRO A 203 -25.314 15.272 -34.602 1.00 66.33 C ANISOU 1172 CB PRO A 203 9020 7925 8258 -1401 -282 -932 C ATOM 1173 CG PRO A 203 -24.664 14.151 -33.899 1.00 66.13 C ANISOU 1173 CG PRO A 203 9166 7836 8123 -1381 -224 -946 C ATOM 1174 CD PRO A 203 -23.461 13.794 -34.729 1.00 65.43 C ANISOU 1174 CD PRO A 203 9181 7710 7970 -1314 -261 -956 C ATOM 1175 N MET A 204 -23.977 16.888 -37.038 1.00 85.20 N ANISOU 1175 N MET A 204 11370 10338 10664 -1338 -426 -880 N ATOM 1176 CA MET A 204 -23.897 18.137 -37.791 1.00 86.11 C ANISOU 1176 CA MET A 204 11415 10464 10837 -1324 -487 -829 C ATOM 1177 C MET A 204 -24.123 17.939 -39.288 1.00 86.55 C ANISOU 1177 C MET A 204 11533 10538 10815 -1399 -565 -777 C ATOM 1178 O MET A 204 -24.497 18.874 -39.996 1.00 87.79 O ANISOU 1178 O MET A 204 11644 10702 11012 -1406 -647 -707 O ATOM 1179 CB MET A 204 -22.559 18.834 -37.537 1.00 96.30 C ANISOU 1179 CB MET A 204 12709 11744 12136 -1260 -445 -845 C ATOM 1180 CG MET A 204 -22.455 19.442 -36.153 1.00 96.41 C ANISOU 1180 CG MET A 204 12658 11742 12233 -1195 -409 -896 C ATOM 1181 SD MET A 204 -23.795 20.606 -35.835 1.00 98.47 S ANISOU 1181 SD MET A 204 12799 11974 12640 -1173 -446 -879 S ATOM 1182 CE MET A 204 -23.528 20.964 -34.103 1.00 98.26 C ANISOU 1182 CE MET A 204 12756 11935 12643 -1103 -370 -980 C ATOM 1183 N LEU A 205 -23.898 16.719 -39.764 1.00 95.03 N ANISOU 1183 N LEU A 205 12734 11607 11764 -1449 -546 -811 N ATOM 1184 CA LEU A 205 -24.140 16.390 -41.163 1.00 95.92 C ANISOU 1184 CA LEU A 205 12942 11739 11764 -1533 -619 -785 C ATOM 1185 C LEU A 205 -25.630 16.245 -41.444 1.00 96.93 C ANISOU 1185 C LEU A 205 13003 11897 11928 -1630 -741 -758 C ATOM 1186 O LEU A 205 -26.058 16.260 -42.597 1.00 97.96 O ANISOU 1186 O LEU A 205 13181 12063 11978 -1705 -853 -721 O ATOM 1187 CB LEU A 205 -23.409 15.104 -41.549 1.00 72.12 C ANISOU 1187 CB LEU A 205 10106 8691 8604 -1544 -549 -858 C ATOM 1188 CG LEU A 205 -21.882 15.172 -41.546 1.00 72.37 C ANISOU 1188 CG LEU A 205 10178 8727 8594 -1441 -436 -889 C ATOM 1189 CD1 LEU A 205 -21.282 13.810 -41.859 1.00 72.52 C ANISOU 1189 CD1 LEU A 205 10368 8697 8488 -1413 -364 -975 C ATOM 1190 CD2 LEU A 205 -21.405 16.212 -42.545 1.00 73.92 C ANISOU 1190 CD2 LEU A 205 10358 8979 8750 -1458 -443 -825 C ATOM 1191 N PHE A 206 -26.418 16.105 -40.383 1.00 91.77 N ANISOU 1191 N PHE A 206 12232 11247 11390 -1635 -719 -778 N ATOM 1192 CA PHE A 206 -27.856 15.920 -40.522 1.00 93.01 C ANISOU 1192 CA PHE A 206 12269 11458 11611 -1736 -818 -762 C ATOM 1193 C PHE A 206 -28.630 17.093 -39.927 1.00 94.64 C ANISOU 1193 C PHE A 206 12249 11713 11998 -1654 -843 -721 C ATOM 1194 O PHE A 206 -29.793 17.315 -40.264 1.00 96.16 O ANISOU 1194 O PHE A 206 12287 11977 12272 -1695 -956 -688 O ATOM 1195 CB PHE A 206 -28.290 14.609 -39.863 1.00 92.15 C ANISOU 1195 CB PHE A 206 12209 11321 11482 -1845 -749 -823 C ATOM 1196 CG PHE A 206 -27.651 13.390 -40.466 1.00 91.05 C ANISOU 1196 CG PHE A 206 12314 11101 11178 -1914 -732 -875 C ATOM 1197 CD1 PHE A 206 -26.427 12.934 -40.005 1.00 90.08 C ANISOU 1197 CD1 PHE A 206 12343 10895 10989 -1815 -612 -914 C ATOM 1198 CD2 PHE A 206 -28.271 12.703 -41.495 1.00 91.77 C ANISOU 1198 CD2 PHE A 206 12484 11200 11184 -2069 -845 -895 C ATOM 1199 CE1 PHE A 206 -25.835 11.816 -40.558 1.00 90.10 C ANISOU 1199 CE1 PHE A 206 12571 10808 10853 -1842 -586 -973 C ATOM 1200 CE2 PHE A 206 -27.684 11.583 -42.053 1.00 90.74 C ANISOU 1200 CE2 PHE A 206 12607 10973 10898 -2121 -818 -965 C ATOM 1201 CZ PHE A 206 -26.464 11.139 -41.582 1.00 90.16 C ANISOU 1201 CZ PHE A 206 12684 10803 10771 -1994 -679 -1005 C ATOM 1202 N THR A 207 -27.980 17.838 -39.040 1.00 97.74 N ANISOU 1202 N THR A 207 12617 12064 12455 -1530 -744 -735 N ATOM 1203 CA THR A 207 -28.604 18.995 -38.408 1.00 99.57 C ANISOU 1203 CA THR A 207 12668 12310 12853 -1427 -745 -721 C ATOM 1204 C THR A 207 -28.507 20.230 -39.302 1.00101.02 C ANISOU 1204 C THR A 207 12839 12465 13081 -1351 -864 -637 C ATOM 1205 O THR A 207 -29.448 21.019 -39.394 1.00103.71 O ANISOU 1205 O THR A 207 13026 12825 13555 -1283 -950 -595 O ATOM 1206 CB THR A 207 -27.969 19.299 -37.037 1.00106.21 C ANISOU 1206 CB THR A 207 13521 13106 13727 -1339 -598 -787 C ATOM 1207 OG1 THR A 207 -27.981 18.115 -36.231 1.00105.25 O ANISOU 1207 OG1 THR A 207 13459 12998 13535 -1408 -494 -841 O ATOM 1208 CG2 THR A 207 -28.737 20.399 -36.320 1.00108.20 C ANISOU 1208 CG2 THR A 207 13603 13365 14144 -1230 -577 -804 C ATOM 1209 N MET A 208 -27.365 20.388 -39.962 1.00 85.02 N ANISOU 1209 N MET A 208 10972 10389 10944 -1359 -864 -605 N ATOM 1210 CA MET A 208 -27.135 21.538 -40.828 1.00 86.92 C ANISOU 1210 CA MET A 208 11247 10581 11196 -1315 -958 -506 C ATOM 1211 C MET A 208 -27.548 21.257 -42.269 1.00 87.69 C ANISOU 1211 C MET A 208 11414 10730 11174 -1396 -1109 -421 C ATOM 1212 O MET A 208 -27.592 20.105 -42.700 1.00 86.02 O ANISOU 1212 O MET A 208 11276 10574 10831 -1502 -1115 -462 O ATOM 1213 CB MET A 208 -25.664 21.953 -40.780 1.00 86.58 C ANISOU 1213 CB MET A 208 11327 10473 11097 -1307 -860 -511 C ATOM 1214 CG MET A 208 -25.204 22.446 -39.420 1.00 85.75 C ANISOU 1214 CG MET A 208 11167 10315 11101 -1232 -751 -591 C ATOM 1215 SD MET A 208 -26.085 23.931 -38.903 1.00 89.51 S ANISOU 1215 SD MET A 208 11526 10700 11783 -1107 -806 -569 S ATOM 1216 CE MET A 208 -26.894 23.343 -37.421 1.00 88.43 C ANISOU 1216 CE MET A 208 11254 10625 11721 -1057 -705 -695 C ATOM 1217 N GLY A 209 -27.844 22.320 -43.010 1.00 87.22 N ANISOU 1217 N GLY A 209 11357 10636 11147 -1345 -1240 -303 N ATOM 1218 CA GLY A 209 -28.234 22.190 -44.402 1.00 88.77 C ANISOU 1218 CA GLY A 209 11641 10885 11203 -1415 -1411 -206 C ATOM 1219 C GLY A 209 -28.631 23.512 -45.030 1.00 92.90 C ANISOU 1219 C GLY A 209 12165 11346 11787 -1324 -1568 -53 C ATOM 1220 O GLY A 209 -28.619 24.554 -44.375 1.00 94.51 O ANISOU 1220 O GLY A 209 12303 11446 12162 -1200 -1536 -32 O ATOM 1221 N LEU A 210 -28.980 23.469 -46.310 1.00 90.27 N ANISOU 1221 N LEU A 210 11934 11065 11301 -1382 -1747 54 N ATOM 1222 CA LEU A 210 -29.368 24.670 -47.037 1.00 94.73 C ANISOU 1222 CA LEU A 210 12541 11562 11891 -1292 -1928 230 C ATOM 1223 C LEU A 210 -30.873 24.924 -46.996 1.00 96.41 C ANISOU 1223 C LEU A 210 12523 11835 12271 -1180 -2147 270 C ATOM 1224 O LEU A 210 -31.676 24.019 -47.223 1.00 95.06 O ANISOU 1224 O LEU A 210 12241 11813 12066 -1258 -2255 218 O ATOM 1225 CB LEU A 210 -28.903 24.586 -48.492 1.00 74.49 C ANISOU 1225 CB LEU A 210 10236 9026 9040 -1408 -2016 346 C ATOM 1226 CG LEU A 210 -27.398 24.644 -48.749 1.00 74.37 C ANISOU 1226 CG LEU A 210 10439 8953 8863 -1500 -1804 347 C ATOM 1227 CD1 LEU A 210 -27.118 24.634 -50.241 1.00 76.26 C ANISOU 1227 CD1 LEU A 210 10935 9237 8803 -1608 -1891 473 C ATOM 1228 CD2 LEU A 210 -26.799 25.875 -48.093 1.00 77.04 C ANISOU 1228 CD2 LEU A 210 10772 9125 9373 -1415 -1700 400 C ATOM 1229 N GLN A 211 -31.242 26.167 -46.708 1.00 86.71 N ANISOU 1229 N GLN A 211 11221 10489 11237 -996 -2213 358 N ATOM 1230 CA GLN A 211 -32.633 26.597 -46.784 1.00 89.12 C ANISOU 1230 CA GLN A 211 11297 10846 11717 -842 -2438 419 C ATOM 1231 C GLN A 211 -32.729 27.936 -47.495 1.00 93.09 C ANISOU 1231 C GLN A 211 11928 11196 12246 -691 -2619 623 C ATOM 1232 O GLN A 211 -31.807 28.750 -47.434 1.00 94.84 O ANISOU 1232 O GLN A 211 12354 11227 12453 -672 -2509 683 O ATOM 1233 CB GLN A 211 -33.264 26.705 -45.394 1.00123.61 C ANISOU 1233 CB GLN A 211 15375 15222 16369 -707 -2312 280 C ATOM 1234 CG GLN A 211 -33.697 25.380 -44.793 1.00120.24 C ANISOU 1234 CG GLN A 211 14765 14976 15946 -842 -2214 119 C ATOM 1235 CD GLN A 211 -34.566 25.562 -43.564 1.00120.58 C ANISOU 1235 CD GLN A 211 14497 15060 16258 -704 -2114 10 C ATOM 1236 OE1 GLN A 211 -35.100 24.596 -43.019 1.00119.46 O ANISOU 1236 OE1 GLN A 211 14176 15064 16148 -807 -2035 -103 O ATOM 1237 NE2 GLN A 211 -34.718 26.806 -43.125 1.00123.22 N ANISOU 1237 NE2 GLN A 211 14782 15257 16781 -474 -2106 41 N ATOM 1238 N ASN A 212 -33.849 28.161 -48.172 1.00 96.77 N ANISOU 1238 N ASN A 212 12273 11742 12752 -588 -2910 737 N ATOM 1239 CA ASN A 212 -34.091 29.433 -48.831 1.00 99.76 C ANISOU 1239 CA ASN A 212 12770 11964 13172 -408 -3120 951 C ATOM 1240 C ASN A 212 -35.025 30.281 -47.982 1.00101.36 C ANISOU 1240 C ASN A 212 12695 12089 13728 -116 -3163 928 C ATOM 1241 O ASN A 212 -36.247 30.174 -48.090 1.00102.14 O ANISOU 1241 O ASN A 212 12510 12336 13963 10 -3370 939 O ATOM 1242 CB ASN A 212 -34.687 29.220 -50.222 1.00 98.15 C ANISOU 1242 CB ASN A 212 12641 11891 12760 -454 -3453 1116 C ATOM 1243 CG ASN A 212 -34.549 30.441 -51.109 1.00100.94 C ANISOU 1243 CG ASN A 212 13260 12052 13039 -331 -3645 1377 C ATOM 1244 OD1 ASN A 212 -35.270 31.424 -50.948 1.00102.70 O ANISOU 1244 OD1 ASN A 212 13371 12157 13491 -66 -3805 1479 O ATOM 1245 ND2 ASN A 212 -33.620 30.382 -52.056 1.00101.08 N ANISOU 1245 ND2 ASN A 212 13643 12032 12732 -517 -3621 1491 N ATOM 1246 N LEU A 213 -34.445 31.121 -47.132 1.00119.82 N ANISOU 1246 N LEU A 213 15108 14200 16217 -9 -2963 884 N ATOM 1247 CA LEU A 213 -35.230 31.915 -46.194 1.00121.12 C ANISOU 1247 CA LEU A 213 15035 14270 16713 276 -2945 818 C ATOM 1248 C LEU A 213 -35.675 33.250 -46.777 1.00123.54 C ANISOU 1248 C LEU A 213 15441 14360 17137 540 -3183 1025 C ATOM 1249 O LEU A 213 -36.024 34.169 -46.040 1.00124.74 O ANISOU 1249 O LEU A 213 15508 14333 17553 796 -3136 982 O ATOM 1250 CB LEU A 213 -34.457 32.135 -44.891 1.00 90.49 C ANISOU 1250 CB LEU A 213 11192 10250 12939 268 -2618 635 C ATOM 1251 CG LEU A 213 -34.143 30.875 -44.085 1.00 88.06 C ANISOU 1251 CG LEU A 213 10759 10138 12560 67 -2384 425 C ATOM 1252 CD1 LEU A 213 -33.481 31.235 -42.767 1.00 88.87 C ANISOU 1252 CD1 LEU A 213 10896 10100 12769 97 -2106 257 C ATOM 1253 CD2 LEU A 213 -35.409 30.069 -43.850 1.00 86.04 C ANISOU 1253 CD2 LEU A 213 10136 10145 12412 102 -2450 341 C ATOM 1254 N SER A 214 -35.685 33.347 -48.102 1.00 95.55 N ANISOU 1254 N SER A 214 12093 10824 13387 487 -3442 1249 N ATOM 1255 CA SER A 214 -36.189 34.541 -48.765 1.00 97.60 C ANISOU 1255 CA SER A 214 12464 10885 13733 744 -3716 1481 C ATOM 1256 C SER A 214 -37.698 34.641 -48.568 1.00 98.26 C ANISOU 1256 C SER A 214 12134 11112 14090 1039 -3934 1461 C ATOM 1257 O SER A 214 -38.317 33.727 -48.019 1.00 96.71 O ANISOU 1257 O SER A 214 11577 11186 13982 991 -3867 1278 O ATOM 1258 CB SER A 214 -35.842 34.525 -50.255 1.00 95.07 C ANISOU 1258 CB SER A 214 12472 10572 13078 593 -3945 1734 C ATOM 1259 OG SER A 214 -36.537 33.493 -50.932 1.00 94.46 O ANISOU 1259 OG SER A 214 12220 10821 12851 488 -4154 1731 O ATOM 1260 N GLY A 215 -38.280 35.750 -49.015 1.00116.48 N ANISOU 1260 N GLY A 215 14488 13232 16535 1343 -4190 1655 N ATOM 1261 CA GLY A 215 -39.694 36.018 -48.817 1.00117.67 C ANISOU 1261 CA GLY A 215 14228 13495 16988 1683 -4402 1645 C ATOM 1262 C GLY A 215 -40.601 34.888 -49.261 1.00116.29 C ANISOU 1262 C GLY A 215 13697 13737 16752 1572 -4602 1607 C ATOM 1263 O GLY A 215 -41.444 34.419 -48.496 1.00115.61 O ANISOU 1263 O GLY A 215 13160 13870 16898 1651 -4527 1421 O ATOM 1264 N ASP A 216 -40.419 34.443 -50.499 1.00148.36 N ANISOU 1264 N ASP A 216 17971 17909 20489 1369 -4847 1778 N ATOM 1265 CA ASP A 216 -41.221 33.358 -51.049 1.00147.62 C ANISOU 1265 CA ASP A 216 17595 18195 20297 1219 -5073 1745 C ATOM 1266 C ASP A 216 -40.459 32.035 -51.046 1.00144.83 C ANISOU 1266 C ASP A 216 17356 18009 19662 792 -4850 1589 C ATOM 1267 O ASP A 216 -40.965 31.014 -51.511 1.00143.12 O ANISOU 1267 O ASP A 216 16976 18083 19322 599 -5003 1538 O ATOM 1268 CB ASP A 216 -41.689 33.709 -52.463 1.00184.19 C ANISOU 1268 CB ASP A 216 22372 22864 24747 1299 -5546 2028 C ATOM 1269 CG ASP A 216 -40.564 34.228 -53.338 1.00184.61 C ANISOU 1269 CG ASP A 216 23022 22660 24460 1176 -5557 2247 C ATOM 1270 OD1 ASP A 216 -39.400 34.223 -52.884 1.00183.80 O ANISOU 1270 OD1 ASP A 216 23188 22382 24267 1000 -5197 2165 O ATOM 1271 OD2 ASP A 216 -40.846 34.651 -54.478 1.00185.89 O ANISOU 1271 OD2 ASP A 216 23381 22805 24443 1252 -5928 2507 O ATOM 1272 N GLY A 217 -39.238 32.065 -50.521 1.00123.04 N ANISOU 1272 N GLY A 217 14880 15057 16811 649 -4497 1509 N ATOM 1273 CA GLY A 217 -38.399 30.881 -50.463 1.00120.38 C ANISOU 1273 CA GLY A 217 14676 14839 16225 287 -4264 1362 C ATOM 1274 C GLY A 217 -37.962 30.440 -51.845 1.00119.70 C ANISOU 1274 C GLY A 217 14920 14822 15737 60 -4454 1507 C ATOM 1275 O GLY A 217 -37.661 29.268 -52.070 1.00117.41 O ANISOU 1275 O GLY A 217 14672 14706 15231 -221 -4378 1389 O ATOM 1276 N THR A 218 -37.923 31.391 -52.772 1.00107.30 N ANISOU 1276 N THR A 218 13611 13103 14057 187 -4697 1765 N ATOM 1277 CA THR A 218 -37.604 31.097 -54.163 1.00107.06 C ANISOU 1277 CA THR A 218 13918 13142 13618 -4 -4905 1930 C ATOM 1278 C THR A 218 -36.413 31.915 -54.669 1.00108.24 C ANISOU 1278 C THR A 218 14557 13019 13553 -55 -4783 2113 C ATOM 1279 O THR A 218 -35.764 31.541 -55.646 1.00107.74 O ANISOU 1279 O THR A 218 14827 13003 13106 -282 -4798 2197 O ATOM 1280 CB THR A 218 -38.837 31.309 -55.070 1.00102.45 C ANISOU 1280 CB THR A 218 13199 12709 13020 151 -5397 2105 C ATOM 1281 OG1 THR A 218 -38.945 30.221 -55.995 1.00102.99 O ANISOU 1281 OG1 THR A 218 13349 13035 12749 -124 -5565 2075 O ATOM 1282 CG2 THR A 218 -38.738 32.615 -55.839 1.00105.90 C ANISOU 1282 CG2 THR A 218 13957 12900 13381 356 -5623 2422 C ATOM 1283 N HIS A 219 -36.125 33.024 -53.994 1.00100.02 N ANISOU 1283 N HIS A 219 13560 11690 12754 143 -4648 2164 N ATOM 1284 CA HIS A 219 -35.051 33.915 -54.417 1.00101.27 C ANISOU 1284 CA HIS A 219 14165 11563 12752 86 -4535 2349 C ATOM 1285 C HIS A 219 -33.689 33.340 -54.038 1.00 99.87 C ANISOU 1285 C HIS A 219 14142 11377 12426 -206 -4126 2188 C ATOM 1286 O HIS A 219 -33.453 33.007 -52.875 1.00 99.03 O ANISOU 1286 O HIS A 219 13816 11278 12532 -214 -3861 1954 O ATOM 1287 CB HIS A 219 -35.233 35.303 -53.800 1.00 99.40 C ANISOU 1287 CB HIS A 219 13933 10993 12842 389 -4541 2444 C ATOM 1288 CG HIS A 219 -34.414 36.369 -54.453 1.00101.30 C ANISOU 1288 CG HIS A 219 14648 10918 12925 354 -4536 2705 C ATOM 1289 ND1 HIS A 219 -33.077 36.551 -54.197 1.00 98.92 N ANISOU 1289 ND1 HIS A 219 14603 10451 12529 127 -4193 2667 N ATOM 1290 CD2 HIS A 219 -34.754 37.330 -55.357 1.00105.75 C ANISOU 1290 CD2 HIS A 219 15478 11294 13409 512 -4838 3021 C ATOM 1291 CE1 HIS A 219 -32.617 37.566 -54.911 1.00101.75 C ANISOU 1291 CE1 HIS A 219 15365 10536 12758 117 -4261 2943 C ATOM 1292 NE2 HIS A 219 -33.623 38.052 -55.621 1.00105.90 N ANISOU 1292 NE2 HIS A 219 15923 11031 13283 355 -4652 3168 N ATOM 1293 N PRO A 220 -32.787 33.224 -55.026 1.00 93.89 N ANISOU 1293 N PRO A 220 13763 10616 11296 -440 -4074 2316 N ATOM 1294 CA PRO A 220 -31.451 32.639 -54.858 1.00 91.81 C ANISOU 1294 CA PRO A 220 13647 10378 10859 -717 -3703 2179 C ATOM 1295 C PRO A 220 -30.627 33.344 -53.784 1.00 91.65 C ANISOU 1295 C PRO A 220 13622 10115 11085 -693 -3402 2101 C ATOM 1296 O PRO A 220 -29.766 32.722 -53.162 1.00 89.94 O ANISOU 1296 O PRO A 220 13347 9961 10865 -852 -3100 1902 O ATOM 1297 CB PRO A 220 -30.808 32.844 -56.233 1.00 92.96 C ANISOU 1297 CB PRO A 220 14225 10504 10590 -897 -3752 2410 C ATOM 1298 CG PRO A 220 -31.957 32.918 -57.175 1.00 96.73 C ANISOU 1298 CG PRO A 220 14727 11081 10943 -774 -4184 2590 C ATOM 1299 CD PRO A 220 -33.039 33.624 -56.421 1.00 97.91 C ANISOU 1299 CD PRO A 220 14577 11118 11506 -445 -4382 2605 C ATOM 1300 N GLY A 221 -30.893 34.629 -53.573 1.00 95.72 N ANISOU 1300 N GLY A 221 14207 10351 11811 -490 -3500 2252 N ATOM 1301 CA GLY A 221 -30.172 35.412 -52.586 1.00 95.88 C ANISOU 1301 CA GLY A 221 14255 10111 12064 -470 -3251 2179 C ATOM 1302 C GLY A 221 -30.544 35.051 -51.161 1.00 95.00 C ANISOU 1302 C GLY A 221 13770 10056 12270 -343 -3115 1895 C ATOM 1303 O GLY A 221 -29.859 35.436 -50.213 1.00 94.75 O ANISOU 1303 O GLY A 221 13733 9868 12399 -369 -2878 1769 O ATOM 1304 N GLY A 222 -31.637 34.309 -51.012 1.00116.06 N ANISOU 1304 N GLY A 222 16129 12954 15015 -224 -3268 1796 N ATOM 1305 CA GLY A 222 -32.111 33.894 -49.705 1.00115.51 C ANISOU 1305 CA GLY A 222 15700 12969 15220 -112 -3139 1539 C ATOM 1306 C GLY A 222 -31.569 32.538 -49.298 1.00113.17 C ANISOU 1306 C GLY A 222 15290 12911 14798 -343 -2916 1320 C ATOM 1307 O GLY A 222 -31.927 32.004 -48.248 1.00111.47 O ANISOU 1307 O GLY A 222 14796 12797 14758 -294 -2796 1111 O ATOM 1308 N LEU A 223 -30.701 31.979 -50.136 1.00103.68 N ANISOU 1308 N LEU A 223 14317 11792 13283 -589 -2853 1372 N ATOM 1309 CA LEU A 223 -30.103 30.677 -49.870 1.00101.26 C ANISOU 1309 CA LEU A 223 13947 11687 12839 -794 -2649 1178 C ATOM 1310 C LEU A 223 -29.078 30.763 -48.748 1.00101.74 C ANISOU 1310 C LEU A 223 13989 11649 13018 -849 -2339 1018 C ATOM 1311 O LEU A 223 -27.985 31.292 -48.937 1.00103.45 O ANISOU 1311 O LEU A 223 14422 11733 13150 -961 -2202 1081 O ATOM 1312 CB LEU A 223 -29.435 30.127 -51.131 1.00 84.56 C ANISOU 1312 CB LEU A 223 12100 9677 10353 -1013 -2655 1272 C ATOM 1313 CG LEU A 223 -28.858 28.717 -50.987 1.00 81.48 C ANISOU 1313 CG LEU A 223 11668 9483 9809 -1199 -2463 1071 C ATOM 1314 CD1 LEU A 223 -29.971 27.730 -50.695 1.00 78.76 C ANISOU 1314 CD1 LEU A 223 11063 9324 9539 -1163 -2591 939 C ATOM 1315 CD2 LEU A 223 -28.081 28.308 -52.227 1.00 81.43 C ANISOU 1315 CD2 LEU A 223 11955 9553 9432 -1396 -2426 1152 C ATOM 1316 N VAL A 224 -29.426 30.235 -47.580 1.00 85.92 N ANISOU 1316 N VAL A 224 11726 9721 11199 -785 -2233 813 N ATOM 1317 CA VAL A 224 -28.547 30.339 -46.422 1.00 85.56 C ANISOU 1317 CA VAL A 224 11654 9591 11266 -817 -1976 656 C ATOM 1318 C VAL A 224 -28.194 28.983 -45.826 1.00 80.05 C ANISOU 1318 C VAL A 224 10835 9083 10497 -937 -1808 459 C ATOM 1319 O VAL A 224 -28.902 27.996 -46.026 1.00 77.46 O ANISOU 1319 O VAL A 224 10387 8933 10110 -962 -1884 411 O ATOM 1320 CB VAL A 224 -29.179 31.208 -45.318 1.00 79.91 C ANISOU 1320 CB VAL A 224 10784 8727 10853 -598 -1971 586 C ATOM 1321 CG1 VAL A 224 -29.402 32.624 -45.819 1.00 82.19 C ANISOU 1321 CG1 VAL A 224 11231 8764 11232 -460 -2121 776 C ATOM 1322 CG2 VAL A 224 -30.487 30.591 -44.846 1.00 77.45 C ANISOU 1322 CG2 VAL A 224 10171 8584 10673 -468 -2051 488 C ATOM 1323 N CYS A 225 -27.085 28.950 -45.093 1.00117.02 N ANISOU 1323 N CYS A 225 15557 13718 15187 -1016 -1591 351 N ATOM 1324 CA CYS A 225 -26.677 27.758 -44.366 1.00111.10 C ANISOU 1324 CA CYS A 225 14708 13112 14393 -1095 -1431 170 C ATOM 1325 C CYS A 225 -27.182 27.869 -42.933 1.00109.85 C ANISOU 1325 C CYS A 225 14360 12928 14450 -969 -1361 24 C ATOM 1326 O CYS A 225 -26.701 28.693 -42.157 1.00110.74 O ANISOU 1326 O CYS A 225 14494 12900 14682 -921 -1274 -24 O ATOM 1327 CB CYS A 225 -25.156 27.609 -44.391 1.00 99.86 C ANISOU 1327 CB CYS A 225 13416 11680 12848 -1239 -1252 136 C ATOM 1328 SG CYS A 225 -24.536 26.118 -43.587 1.00 93.76 S ANISOU 1328 SG CYS A 225 12553 11064 12006 -1306 -1078 -63 S ATOM 1329 N THR A 226 -28.156 27.034 -42.589 1.00 85.27 N ANISOU 1329 N THR A 226 11071 9953 11376 -933 -1393 -52 N ATOM 1330 CA THR A 226 -28.852 27.151 -41.315 1.00 85.44 C ANISOU 1330 CA THR A 226 10901 9975 11588 -809 -1323 -176 C ATOM 1331 C THR A 226 -29.295 25.768 -40.843 1.00 81.74 C ANISOU 1331 C THR A 226 10303 9685 11071 -885 -1257 -287 C ATOM 1332 O THR A 226 -29.425 24.853 -41.655 1.00 79.72 O ANISOU 1332 O THR A 226 10077 9538 10674 -1002 -1328 -252 O ATOM 1333 CB THR A 226 -30.081 28.085 -41.456 1.00 74.76 C ANISOU 1333 CB THR A 226 9418 8563 10423 -618 -1476 -103 C ATOM 1334 OG1 THR A 226 -30.685 28.309 -40.176 1.00 75.56 O ANISOU 1334 OG1 THR A 226 9340 8659 10710 -483 -1367 -241 O ATOM 1335 CG2 THR A 226 -31.109 27.484 -42.405 1.00 74.45 C ANISOU 1335 CG2 THR A 226 9269 8682 10338 -638 -1668 -18 C ATOM 1336 N PRO A 227 -29.497 25.600 -39.524 1.00106.25 N ANISOU 1336 N PRO A 227 13290 12806 14273 -834 -1113 -423 N ATOM 1337 CA PRO A 227 -30.084 24.351 -39.027 1.00104.05 C ANISOU 1337 CA PRO A 227 12891 12680 13965 -913 -1048 -508 C ATOM 1338 C PRO A 227 -31.416 24.035 -39.701 1.00105.77 C ANISOU 1338 C PRO A 227 12931 13019 14237 -919 -1202 -451 C ATOM 1339 O PRO A 227 -32.329 24.859 -39.702 1.00109.04 O ANISOU 1339 O PRO A 227 13181 13427 14821 -772 -1287 -417 O ATOM 1340 CB PRO A 227 -30.289 24.624 -37.527 1.00103.24 C ANISOU 1340 CB PRO A 227 12689 12560 13978 -819 -883 -636 C ATOM 1341 CG PRO A 227 -29.983 26.091 -37.325 1.00106.35 C ANISOU 1341 CG PRO A 227 13134 12786 14489 -671 -892 -627 C ATOM 1342 CD PRO A 227 -29.037 26.454 -38.418 1.00105.90 C ANISOU 1342 CD PRO A 227 13267 12638 14332 -738 -990 -511 C ATOM 1343 N ILE A 228 -31.507 22.840 -40.275 1.00 91.91 N ANISOU 1343 N ILE A 228 11209 11369 12343 -1085 -1245 -448 N ATOM 1344 CA ILE A 228 -32.683 22.421 -41.025 1.00 92.74 C ANISOU 1344 CA ILE A 228 11160 11605 12473 -1142 -1420 -401 C ATOM 1345 C ILE A 228 -33.530 21.449 -40.219 1.00 92.41 C ANISOU 1345 C ILE A 228 10927 11688 12495 -1236 -1324 -500 C ATOM 1346 O ILE A 228 -34.479 20.858 -40.736 1.00 92.67 O ANISOU 1346 O ILE A 228 10818 11849 12543 -1341 -1451 -486 O ATOM 1347 CB ILE A 228 -32.281 21.741 -42.341 1.00 78.92 C ANISOU 1347 CB ILE A 228 9602 9881 10505 -1295 -1553 -339 C ATOM 1348 CG1 ILE A 228 -31.359 20.553 -42.050 1.00 75.51 C ANISOU 1348 CG1 ILE A 228 9352 9432 9909 -1440 -1391 -431 C ATOM 1349 CG2 ILE A 228 -31.592 22.733 -43.258 1.00 80.64 C ANISOU 1349 CG2 ILE A 228 9999 9996 10646 -1223 -1652 -216 C ATOM 1350 CD1 ILE A 228 -30.887 19.818 -43.283 1.00 74.39 C ANISOU 1350 CD1 ILE A 228 9422 9303 9538 -1579 -1480 -405 C ATOM 1351 N VAL A 229 -33.175 21.284 -38.950 1.00 92.89 N ANISOU 1351 N VAL A 229 10995 11715 12583 -1217 -1102 -596 N ATOM 1352 CA VAL A 229 -33.881 20.361 -38.074 1.00 92.22 C ANISOU 1352 CA VAL A 229 10770 11735 12535 -1324 -969 -679 C ATOM 1353 C VAL A 229 -34.725 21.124 -37.052 1.00 94.86 C ANISOU 1353 C VAL A 229 10852 12119 13071 -1172 -858 -733 C ATOM 1354 O VAL A 229 -34.564 22.334 -36.884 1.00 96.52 O ANISOU 1354 O VAL A 229 11049 12244 13380 -972 -864 -727 O ATOM 1355 CB VAL A 229 -32.896 19.401 -37.371 1.00 72.36 C ANISOU 1355 CB VAL A 229 8480 9154 9859 -1431 -796 -743 C ATOM 1356 CG1 VAL A 229 -32.394 20.000 -36.067 1.00 72.70 C ANISOU 1356 CG1 VAL A 229 8549 9135 9940 -1300 -612 -810 C ATOM 1357 CG2 VAL A 229 -33.546 18.049 -37.138 1.00 71.83 C ANISOU 1357 CG2 VAL A 229 8371 9170 9750 -1637 -741 -778 C ATOM 1358 N ASP A 230 -35.630 20.414 -36.382 1.00104.40 N ANISOU 1358 N ASP A 230 11869 13459 14338 -1275 -744 -791 N ATOM 1359 CA ASP A 230 -36.530 21.017 -35.403 1.00107.04 C ANISOU 1359 CA ASP A 230 11937 13878 14857 -1143 -601 -859 C ATOM 1360 C ASP A 230 -35.768 21.690 -34.261 1.00107.53 C ANISOU 1360 C ASP A 230 12144 13821 14893 -995 -406 -939 C ATOM 1361 O ASP A 230 -34.635 21.318 -33.955 1.00105.45 O ANISOU 1361 O ASP A 230 12155 13454 14459 -1057 -343 -952 O ATOM 1362 CB ASP A 230 -37.483 19.947 -34.856 1.00165.40 C ANISOU 1362 CB ASP A 230 19135 21437 22273 -1341 -471 -904 C ATOM 1363 CG ASP A 230 -38.416 20.478 -33.786 1.00168.77 C ANISOU 1363 CG ASP A 230 19273 21979 22872 -1219 -272 -987 C ATOM 1364 OD1 ASP A 230 -38.803 21.663 -33.862 1.00171.73 O ANISOU 1364 OD1 ASP A 230 19480 22350 23419 -970 -324 -997 O ATOM 1365 OD2 ASP A 230 -38.763 19.707 -32.866 1.00169.12 O ANISOU 1365 OD2 ASP A 230 19272 22110 22875 -1369 -52 -1043 O ATOM 1366 N THR A 231 -36.397 22.684 -33.640 1.00109.15 N ANISOU 1366 N THR A 231 12159 14044 15269 -792 -321 -1001 N ATOM 1367 CA THR A 231 -35.774 23.439 -32.556 1.00110.28 C ANISOU 1367 CA THR A 231 12439 14070 15391 -647 -150 -1099 C ATOM 1368 C THR A 231 -35.480 22.552 -31.351 1.00109.31 C ANISOU 1368 C THR A 231 12430 13995 15108 -786 85 -1179 C ATOM 1369 O THR A 231 -34.494 22.757 -30.642 1.00109.55 O ANISOU 1369 O THR A 231 12696 13916 15013 -755 169 -1235 O ATOM 1370 CB THR A 231 -36.636 24.644 -32.125 1.00107.62 C ANISOU 1370 CB THR A 231 11875 13739 15276 -388 -90 -1172 C ATOM 1371 OG1 THR A 231 -36.120 25.190 -30.904 1.00109.03 O ANISOU 1371 OG1 THR A 231 12200 13824 15402 -287 112 -1302 O ATOM 1372 CG2 THR A 231 -38.083 24.223 -31.916 1.00109.56 C ANISOU 1372 CG2 THR A 231 11746 14215 15669 -410 -5 -1200 C ATOM 1373 N ALA A 232 -36.344 21.567 -31.123 1.00113.07 N ANISOU 1373 N ALA A 232 12742 14635 15585 -950 181 -1179 N ATOM 1374 CA ALA A 232 -36.153 20.622 -30.033 1.00112.51 C ANISOU 1374 CA ALA A 232 12800 14603 15346 -1106 401 -1224 C ATOM 1375 C ALA A 232 -34.953 19.731 -30.321 1.00109.23 C ANISOU 1375 C ALA A 232 12711 14073 14720 -1250 319 -1162 C ATOM 1376 O ALA A 232 -34.154 19.440 -29.431 1.00108.68 O ANISOU 1376 O ALA A 232 12869 13939 14483 -1267 434 -1196 O ATOM 1377 CB ALA A 232 -37.402 19.784 -29.828 1.00 77.22 C ANISOU 1377 CB ALA A 232 8074 10326 10941 -1280 520 -1221 C ATOM 1378 N THR A 233 -34.832 19.306 -31.575 1.00 95.46 N ANISOU 1378 N THR A 233 10985 12306 12978 -1340 114 -1075 N ATOM 1379 CA THR A 233 -33.716 18.472 -32.001 1.00 92.10 C ANISOU 1379 CA THR A 233 10851 11773 12371 -1449 36 -1026 C ATOM 1380 C THR A 233 -32.408 19.257 -31.958 1.00 90.83 C ANISOU 1380 C THR A 233 10889 11477 12147 -1298 -11 -1039 C ATOM 1381 O THR A 233 -31.358 18.712 -31.614 1.00 88.69 O ANISOU 1381 O THR A 233 10849 11131 11718 -1333 19 -1042 O ATOM 1382 CB THR A 233 -33.931 17.931 -33.427 1.00 80.49 C ANISOU 1382 CB THR A 233 9360 10315 10908 -1571 -168 -950 C ATOM 1383 OG1 THR A 233 -35.214 17.300 -33.513 1.00 82.36 O ANISOU 1383 OG1 THR A 233 9372 10690 11230 -1730 -152 -945 O ATOM 1384 CG2 THR A 233 -32.851 16.921 -33.784 1.00 77.24 C ANISOU 1384 CG2 THR A 233 9249 9793 10305 -1680 -206 -923 C ATOM 1385 N LEU A 234 -32.475 20.539 -32.306 1.00 84.49 N ANISOU 1385 N LEU A 234 9989 10639 11474 -1131 -91 -1045 N ATOM 1386 CA LEU A 234 -31.289 21.387 -32.311 1.00 83.71 C ANISOU 1386 CA LEU A 234 10061 10407 11338 -1017 -137 -1058 C ATOM 1387 C LEU A 234 -30.722 21.567 -30.909 1.00 84.41 C ANISOU 1387 C LEU A 234 10266 10463 11343 -966 22 -1158 C ATOM 1388 O LEU A 234 -29.506 21.528 -30.718 1.00 81.75 O ANISOU 1388 O LEU A 234 10120 10050 10891 -970 1 -1168 O ATOM 1389 CB LEU A 234 -31.592 22.755 -32.920 1.00 63.65 C ANISOU 1389 CB LEU A 234 7414 7805 8965 -858 -249 -1035 C ATOM 1390 CG LEU A 234 -30.381 23.692 -32.953 1.00 62.90 C ANISOU 1390 CG LEU A 234 7500 7556 8844 -778 -292 -1044 C ATOM 1391 CD1 LEU A 234 -29.314 23.168 -33.908 1.00 59.79 C ANISOU 1391 CD1 LEU A 234 7272 7127 8321 -889 -398 -961 C ATOM 1392 CD2 LEU A 234 -30.787 25.114 -33.309 1.00 66.08 C ANISOU 1392 CD2 LEU A 234 7826 7859 9424 -609 -372 -1029 C ATOM 1393 N LYS A 235 -31.604 21.770 -29.934 1.00105.10 N ANISOU 1393 N LYS A 235 12761 13155 14016 -919 180 -1237 N ATOM 1394 CA LYS A 235 -31.180 21.915 -28.546 1.00106.34 C ANISOU 1394 CA LYS A 235 13046 13299 14060 -879 338 -1341 C ATOM 1395 C LYS A 235 -30.425 20.676 -28.095 1.00103.21 C ANISOU 1395 C LYS A 235 12855 12912 13449 -1017 372 -1308 C ATOM 1396 O LYS A 235 -29.377 20.774 -27.463 1.00101.98 O ANISOU 1396 O LYS A 235 12887 12697 13164 -987 370 -1349 O ATOM 1397 CB LYS A 235 -32.379 22.148 -27.625 1.00 76.27 C ANISOU 1397 CB LYS A 235 9065 9598 10317 -827 538 -1429 C ATOM 1398 CG LYS A 235 -33.064 23.491 -27.795 1.00 80.24 C ANISOU 1398 CG LYS A 235 9382 10070 11034 -628 531 -1493 C ATOM 1399 CD LYS A 235 -34.211 23.632 -26.808 1.00 84.22 C ANISOU 1399 CD LYS A 235 9703 10703 11594 -566 769 -1600 C ATOM 1400 CE LYS A 235 -34.941 24.949 -26.985 1.00 86.98 C ANISOU 1400 CE LYS A 235 9856 11013 12180 -326 763 -1671 C ATOM 1401 NZ LYS A 235 -36.066 25.084 -26.023 1.00 89.07 N ANISOU 1401 NZ LYS A 235 9915 11422 12506 -246 1025 -1793 N ATOM 1402 N VAL A 236 -30.960 19.511 -28.444 1.00 86.90 N ANISOU 1402 N VAL A 236 10755 10910 11352 -1167 387 -1234 N ATOM 1403 CA VAL A 236 -30.349 18.243 -28.074 1.00 84.95 C ANISOU 1403 CA VAL A 236 10722 10642 10915 -1290 416 -1188 C ATOM 1404 C VAL A 236 -28.944 18.081 -28.655 1.00 81.23 C ANISOU 1404 C VAL A 236 10431 10068 10365 -1259 262 -1152 C ATOM 1405 O VAL A 236 -28.008 17.743 -27.933 1.00 80.39 O ANISOU 1405 O VAL A 236 10511 9924 10111 -1237 276 -1165 O ATOM 1406 CB VAL A 236 -31.223 17.051 -28.510 1.00 82.24 C ANISOU 1406 CB VAL A 236 10320 10351 10577 -1477 443 -1116 C ATOM 1407 CG1 VAL A 236 -30.542 15.742 -28.168 1.00 80.98 C ANISOU 1407 CG1 VAL A 236 10424 10119 10227 -1586 462 -1062 C ATOM 1408 CG2 VAL A 236 -32.590 17.128 -27.852 1.00 85.53 C ANISOU 1408 CG2 VAL A 236 10526 10900 11072 -1531 623 -1152 C ATOM 1409 N VAL A 237 -28.792 18.340 -29.951 1.00 97.54 N ANISOU 1409 N VAL A 237 12435 12102 12524 -1253 118 -1107 N ATOM 1410 CA VAL A 237 -27.496 18.161 -30.601 1.00 94.81 C ANISOU 1410 CA VAL A 237 12233 11682 12108 -1233 2 -1076 C ATOM 1411 C VAL A 237 -26.467 19.184 -30.117 1.00 94.38 C ANISOU 1411 C VAL A 237 12226 11584 12048 -1116 -22 -1134 C ATOM 1412 O VAL A 237 -25.269 18.907 -30.104 1.00 92.66 O ANISOU 1412 O VAL A 237 12130 11335 11743 -1099 -72 -1131 O ATOM 1413 CB VAL A 237 -27.598 18.186 -32.150 1.00 82.40 C ANISOU 1413 CB VAL A 237 10605 10099 10604 -1271 -130 -1012 C ATOM 1414 CG1 VAL A 237 -28.609 17.162 -32.634 1.00 82.85 C ANISOU 1414 CG1 VAL A 237 10619 10200 10662 -1412 -131 -972 C ATOM 1415 CG2 VAL A 237 -27.964 19.569 -32.651 1.00 84.40 C ANISOU 1415 CG2 VAL A 237 10713 10348 11007 -1183 -197 -1011 C ATOM 1416 N ILE A 238 -26.941 20.357 -29.708 1.00 94.60 N ANISOU 1416 N ILE A 238 12153 11611 12180 -1038 12 -1195 N ATOM 1417 CA ILE A 238 -26.060 21.395 -29.182 1.00 94.71 C ANISOU 1417 CA ILE A 238 12224 11565 12196 -954 -11 -1269 C ATOM 1418 C ILE A 238 -25.638 21.077 -27.748 1.00 94.95 C ANISOU 1418 C ILE A 238 12381 11624 12072 -943 71 -1345 C ATOM 1419 O ILE A 238 -24.474 21.252 -27.384 1.00 93.43 O ANISOU 1419 O ILE A 238 12289 11407 11803 -923 7 -1380 O ATOM 1420 CB ILE A 238 -26.711 22.795 -29.256 1.00 95.88 C ANISOU 1420 CB ILE A 238 12259 11661 12510 -860 -8 -1318 C ATOM 1421 CG1 ILE A 238 -26.832 23.240 -30.715 1.00 95.85 C ANISOU 1421 CG1 ILE A 238 12180 11608 12630 -860 -134 -1222 C ATOM 1422 CG2 ILE A 238 -25.893 23.814 -28.484 1.00 95.91 C ANISOU 1422 CG2 ILE A 238 12354 11585 12502 -799 -13 -1424 C ATOM 1423 CD1 ILE A 238 -27.298 24.669 -30.883 1.00 98.81 C ANISOU 1423 CD1 ILE A 238 12483 11887 13173 -746 -163 -1248 C ATOM 1424 N GLN A 239 -26.589 20.607 -26.943 1.00 89.94 N ANISOU 1424 N GLN A 239 11736 11054 11384 -965 209 -1366 N ATOM 1425 CA GLN A 239 -26.309 20.206 -25.566 1.00 90.82 C ANISOU 1425 CA GLN A 239 11999 11201 11308 -968 297 -1419 C ATOM 1426 C GLN A 239 -25.230 19.133 -25.519 1.00 88.63 C ANISOU 1426 C GLN A 239 11887 10912 10877 -1003 211 -1350 C ATOM 1427 O GLN A 239 -24.233 19.274 -24.811 1.00 87.77 O ANISOU 1427 O GLN A 239 11896 10798 10653 -958 151 -1394 O ATOM 1428 CB GLN A 239 -27.571 19.666 -24.892 1.00101.72 C ANISOU 1428 CB GLN A 239 13342 12664 12645 -1025 484 -1420 C ATOM 1429 CG GLN A 239 -28.591 20.712 -24.487 1.00105.70 C ANISOU 1429 CG GLN A 239 13693 13204 13262 -949 614 -1525 C ATOM 1430 CD GLN A 239 -29.889 20.082 -24.018 1.00110.41 C ANISOU 1430 CD GLN A 239 14192 13914 13844 -1029 815 -1512 C ATOM 1431 OE1 GLN A 239 -29.952 18.877 -23.772 1.00110.55 O ANISOU 1431 OE1 GLN A 239 14311 13965 13728 -1160 867 -1428 O ATOM 1432 NE2 GLN A 239 -30.936 20.889 -23.912 1.00114.68 N ANISOU 1432 NE2 GLN A 239 14530 14509 14534 -952 932 -1592 N ATOM 1433 N VAL A 240 -25.437 18.069 -26.290 1.00 86.51 N ANISOU 1433 N VAL A 240 11622 10633 10614 -1077 195 -1248 N ATOM 1434 CA VAL A 240 -24.505 16.947 -26.347 1.00 85.00 C ANISOU 1434 CA VAL A 240 11592 10407 10298 -1084 122 -1180 C ATOM 1435 C VAL A 240 -23.108 17.407 -26.757 1.00 82.93 C ANISOU 1435 C VAL A 240 11330 10124 10057 -1001 -22 -1203 C ATOM 1436 O VAL A 240 -22.105 16.938 -26.218 1.00 82.46 O ANISOU 1436 O VAL A 240 11388 10064 9878 -947 -87 -1197 O ATOM 1437 CB VAL A 240 -25.011 15.843 -27.300 1.00 83.50 C ANISOU 1437 CB VAL A 240 11409 10180 10136 -1180 125 -1091 C ATOM 1438 CG1 VAL A 240 -23.969 14.743 -27.458 1.00 82.40 C ANISOU 1438 CG1 VAL A 240 11446 9973 9889 -1149 48 -1035 C ATOM 1439 CG2 VAL A 240 -26.323 15.266 -26.788 1.00 85.95 C ANISOU 1439 CG2 VAL A 240 11716 10522 10420 -1300 272 -1064 C ATOM 1440 N ASN A 241 -23.050 18.340 -27.701 1.00 88.72 N ANISOU 1440 N ASN A 241 11925 10844 10942 -993 -73 -1221 N ATOM 1441 CA ASN A 241 -21.778 18.917 -28.116 1.00 87.18 C ANISOU 1441 CA ASN A 241 11702 10639 10782 -949 -183 -1243 C ATOM 1442 C ASN A 241 -21.154 19.749 -27.001 1.00 87.73 C ANISOU 1442 C ASN A 241 11801 10727 10806 -906 -214 -1340 C ATOM 1443 O ASN A 241 -19.945 19.700 -26.779 1.00 87.31 O ANISOU 1443 O ASN A 241 11771 10700 10703 -874 -308 -1359 O ATOM 1444 CB ASN A 241 -21.951 19.764 -29.377 1.00119.52 C ANISOU 1444 CB ASN A 241 15674 14704 15034 -974 -217 -1222 C ATOM 1445 CG ASN A 241 -20.661 20.435 -29.807 1.00119.09 C ANISOU 1445 CG ASN A 241 15584 14643 15020 -964 -301 -1239 C ATOM 1446 OD1 ASN A 241 -20.473 21.634 -29.600 1.00119.10 O ANISOU 1446 OD1 ASN A 241 15546 14610 15098 -967 -324 -1295 O ATOM 1447 ND2 ASN A 241 -19.760 19.661 -30.401 1.00118.31 N ANISOU 1447 ND2 ASN A 241 15502 14573 14877 -957 -337 -1198 N ATOM 1448 N THR A 242 -21.988 20.514 -26.304 1.00114.01 N ANISOU 1448 N THR A 242 15120 14047 14152 -903 -137 -1412 N ATOM 1449 CA THR A 242 -21.521 21.361 -25.213 1.00114.51 C ANISOU 1449 CA THR A 242 15240 14113 14154 -873 -159 -1531 C ATOM 1450 C THR A 242 -20.974 20.522 -24.060 1.00115.07 C ANISOU 1450 C THR A 242 15465 14249 14008 -853 -184 -1537 C ATOM 1451 O THR A 242 -19.987 20.890 -23.425 1.00115.35 O ANISOU 1451 O THR A 242 15548 14310 13969 -834 -291 -1606 O ATOM 1452 CB THR A 242 -22.646 22.282 -24.695 1.00105.44 C ANISOU 1452 CB THR A 242 14067 12934 13060 -851 -40 -1623 C ATOM 1453 OG1 THR A 242 -23.171 23.057 -25.780 1.00105.59 O ANISOU 1453 OG1 THR A 242 13952 12883 13287 -844 -44 -1599 O ATOM 1454 CG2 THR A 242 -22.123 23.221 -23.617 1.00105.88 C ANISOU 1454 CG2 THR A 242 14213 12972 13044 -828 -68 -1773 C ATOM 1455 N PHE A 243 -21.614 19.386 -23.802 1.00110.38 N ANISOU 1455 N PHE A 243 14955 13676 13309 -867 -97 -1457 N ATOM 1456 CA PHE A 243 -21.184 18.496 -22.728 1.00111.66 C ANISOU 1456 CA PHE A 243 15303 13879 13246 -843 -120 -1429 C ATOM 1457 C PHE A 243 -19.927 17.709 -23.093 1.00110.41 C ANISOU 1457 C PHE A 243 15173 13721 13056 -786 -277 -1357 C ATOM 1458 O PHE A 243 -18.943 17.721 -22.356 1.00110.93 O ANISOU 1458 O PHE A 243 15308 13834 13008 -729 -404 -1388 O ATOM 1459 CB PHE A 243 -22.307 17.526 -22.347 1.00124.77 C ANISOU 1459 CB PHE A 243 17064 15539 14806 -900 40 -1352 C ATOM 1460 CG PHE A 243 -23.378 18.139 -21.488 1.00126.72 C ANISOU 1460 CG PHE A 243 17317 15827 15003 -932 212 -1437 C ATOM 1461 CD1 PHE A 243 -23.094 18.570 -20.203 1.00128.06 C ANISOU 1461 CD1 PHE A 243 17629 16043 14984 -901 220 -1529 C ATOM 1462 CD2 PHE A 243 -24.673 18.269 -21.961 1.00128.50 C ANISOU 1462 CD2 PHE A 243 17400 16058 15365 -988 367 -1432 C ATOM 1463 CE1 PHE A 243 -24.079 19.130 -19.410 1.00130.60 C ANISOU 1463 CE1 PHE A 243 17966 16409 15248 -918 409 -1626 C ATOM 1464 CE2 PHE A 243 -25.662 18.828 -21.174 1.00131.50 C ANISOU 1464 CE2 PHE A 243 17756 16493 15715 -995 549 -1521 C ATOM 1465 CZ PHE A 243 -25.365 19.258 -19.896 1.00132.30 C ANISOU 1465 CZ PHE A 243 18015 16633 15620 -957 585 -1623 C ATOM 1466 N MET A 244 -19.967 17.033 -24.237 1.00 92.14 N ANISOU 1466 N MET A 244 12802 11363 10844 -795 -273 -1272 N ATOM 1467 CA MET A 244 -18.913 16.095 -24.620 1.00 92.15 C ANISOU 1467 CA MET A 244 12841 11354 10817 -716 -383 -1205 C ATOM 1468 C MET A 244 -17.643 16.746 -25.166 1.00 91.04 C ANISOU 1468 C MET A 244 12545 11265 10782 -666 -511 -1255 C ATOM 1469 O MET A 244 -16.558 16.172 -25.069 1.00 92.10 O ANISOU 1469 O MET A 244 12688 11434 10874 -568 -622 -1233 O ATOM 1470 CB MET A 244 -19.447 15.066 -25.621 1.00114.66 C ANISOU 1470 CB MET A 244 15722 14127 13718 -748 -316 -1115 C ATOM 1471 CG MET A 244 -20.505 14.135 -25.051 1.00116.89 C ANISOU 1471 CG MET A 244 16175 14352 13884 -818 -203 -1045 C ATOM 1472 SD MET A 244 -19.922 13.223 -23.607 1.00119.91 S ANISOU 1472 SD MET A 244 16820 14721 14021 -732 -261 -983 S ATOM 1473 CE MET A 244 -20.816 14.048 -22.294 1.00120.53 C ANISOU 1473 CE MET A 244 16941 14879 13977 -813 -143 -1046 C ATOM 1474 N SER A 245 -17.773 17.937 -25.740 1.00113.33 N ANISOU 1474 N SER A 245 15220 14091 13749 -733 -492 -1318 N ATOM 1475 CA SER A 245 -16.625 18.608 -26.341 1.00112.50 C ANISOU 1475 CA SER A 245 14960 14030 13753 -730 -586 -1356 C ATOM 1476 C SER A 245 -16.053 19.701 -25.447 1.00113.15 C ANISOU 1476 C SER A 245 15009 14158 13823 -758 -675 -1466 C ATOM 1477 O SER A 245 -14.963 20.212 -25.703 1.00113.08 O ANISOU 1477 O SER A 245 14871 14204 13889 -776 -770 -1506 O ATOM 1478 CB SER A 245 -16.997 19.195 -27.704 1.00142.03 C ANISOU 1478 CB SER A 245 18586 17726 17655 -804 -521 -1333 C ATOM 1479 OG SER A 245 -15.939 19.978 -28.226 1.00141.89 O ANISOU 1479 OG SER A 245 18429 17747 17736 -838 -583 -1367 O ATOM 1480 N PHE A 246 -16.786 20.056 -24.396 1.00 97.79 N ANISOU 1480 N PHE A 246 13181 12194 11779 -774 -636 -1525 N ATOM 1481 CA PHE A 246 -16.361 21.139 -23.517 1.00 98.07 C ANISOU 1481 CA PHE A 246 13225 12251 11785 -812 -715 -1656 C ATOM 1482 C PHE A 246 -16.393 20.757 -22.040 1.00 99.97 C ANISOU 1482 C PHE A 246 13647 12547 11792 -768 -756 -1698 C ATOM 1483 O PHE A 246 -15.353 20.497 -21.440 1.00100.89 O ANISOU 1483 O PHE A 246 13778 12749 11805 -728 -919 -1714 O ATOM 1484 CB PHE A 246 -17.211 22.390 -23.756 1.00 78.62 C ANISOU 1484 CB PHE A 246 10735 9690 9448 -880 -618 -1731 C ATOM 1485 CG PHE A 246 -16.742 23.598 -22.996 1.00 79.20 C ANISOU 1485 CG PHE A 246 10834 9744 9515 -935 -697 -1885 C ATOM 1486 CD1 PHE A 246 -15.633 24.312 -23.419 1.00 78.96 C ANISOU 1486 CD1 PHE A 246 10685 9719 9599 -1014 -818 -1926 C ATOM 1487 CD2 PHE A 246 -17.411 24.021 -21.859 1.00 80.40 C ANISOU 1487 CD2 PHE A 246 11134 9874 9541 -922 -639 -1998 C ATOM 1488 CE1 PHE A 246 -15.199 25.425 -22.721 1.00 79.68 C ANISOU 1488 CE1 PHE A 246 10815 9774 9688 -1094 -902 -2078 C ATOM 1489 CE2 PHE A 246 -16.984 25.132 -21.156 1.00 81.00 C ANISOU 1489 CE2 PHE A 246 11265 9913 9598 -978 -716 -2163 C ATOM 1490 CZ PHE A 246 -15.876 25.836 -21.587 1.00 80.81 C ANISOU 1490 CZ PHE A 246 11131 9876 9697 -1072 -859 -2203 C ATOM 1491 N LEU A 247 -17.592 20.716 -21.466 1.00100.53 N ANISOU 1491 N LEU A 247 13847 12580 11771 -775 -608 -1711 N ATOM 1492 CA LEU A 247 -17.753 20.525 -20.025 1.00102.20 C ANISOU 1492 CA LEU A 247 14259 12841 11729 -755 -609 -1762 C ATOM 1493 C LEU A 247 -17.135 19.239 -19.487 1.00103.70 C ANISOU 1493 C LEU A 247 14580 13094 11728 -680 -717 -1650 C ATOM 1494 O LEU A 247 -16.334 19.280 -18.557 1.00104.86 O ANISOU 1494 O LEU A 247 14816 13317 11707 -649 -878 -1697 O ATOM 1495 CB LEU A 247 -19.231 20.598 -19.633 1.00 79.94 C ANISOU 1495 CB LEU A 247 11529 9985 8859 -780 -381 -1781 C ATOM 1496 CG LEU A 247 -19.877 21.981 -19.724 1.00 79.93 C ANISOU 1496 CG LEU A 247 11454 9921 8996 -810 -284 -1925 C ATOM 1497 CD1 LEU A 247 -21.329 21.923 -19.281 1.00 82.00 C ANISOU 1497 CD1 LEU A 247 11769 10181 9208 -808 -46 -1944 C ATOM 1498 CD2 LEU A 247 -19.098 22.988 -18.890 1.00 80.12 C ANISOU 1498 CD2 LEU A 247 11551 9952 8938 -827 -410 -2094 C ATOM 1499 N PHE A 248 -17.494 18.103 -20.076 1.00 96.29 N ANISOU 1499 N PHE A 248 13662 12113 10810 -649 -646 -1505 N ATOM 1500 CA PHE A 248 -16.992 16.816 -19.599 1.00 98.01 C ANISOU 1500 CA PHE A 248 14040 12345 10854 -559 -739 -1383 C ATOM 1501 C PHE A 248 -15.463 16.678 -19.707 1.00 98.36 C ANISOU 1501 C PHE A 248 13985 12461 10926 -454 -982 -1381 C ATOM 1502 O PHE A 248 -14.809 16.378 -18.709 1.00100.32 O ANISOU 1502 O PHE A 248 14359 12777 10982 -382 -1142 -1371 O ATOM 1503 CB PHE A 248 -17.720 15.643 -20.274 1.00 86.78 C ANISOU 1503 CB PHE A 248 12679 10827 9468 -564 -607 -1240 C ATOM 1504 CG PHE A 248 -17.536 14.324 -19.571 1.00 88.97 C ANISOU 1504 CG PHE A 248 13205 11068 9533 -490 -656 -1106 C ATOM 1505 CD1 PHE A 248 -17.142 14.276 -18.243 1.00 90.78 C ANISOU 1505 CD1 PHE A 248 13623 11360 9508 -444 -760 -1106 C ATOM 1506 CD2 PHE A 248 -17.768 13.132 -20.238 1.00 89.28 C ANISOU 1506 CD2 PHE A 248 13317 10993 9612 -469 -604 -978 C ATOM 1507 CE1 PHE A 248 -16.975 13.066 -17.596 1.00 93.10 C ANISOU 1507 CE1 PHE A 248 14177 11602 9594 -368 -817 -958 C ATOM 1508 CE2 PHE A 248 -17.605 11.919 -19.596 1.00 91.97 C ANISOU 1508 CE2 PHE A 248 13920 11259 9763 -398 -651 -842 C ATOM 1509 CZ PHE A 248 -17.208 11.885 -18.274 1.00 93.74 C ANISOU 1509 CZ PHE A 248 14336 11545 9737 -342 -759 -821 C ATOM 1510 N PRO A 249 -14.885 16.894 -20.906 1.00 99.08 N ANISOU 1510 N PRO A 249 13845 12552 11248 -445 -1013 -1388 N ATOM 1511 CA PRO A 249 -13.432 16.696 -20.977 1.00100.56 C ANISOU 1511 CA PRO A 249 13904 12835 11470 -339 -1223 -1388 C ATOM 1512 C PRO A 249 -12.634 17.735 -20.184 1.00100.87 C ANISOU 1512 C PRO A 249 13866 12991 11467 -384 -1397 -1521 C ATOM 1513 O PRO A 249 -11.593 17.392 -19.624 1.00102.67 O ANISOU 1513 O PRO A 249 14071 13325 11613 -284 -1609 -1513 O ATOM 1514 CB PRO A 249 -13.134 16.830 -22.473 1.00 94.40 C ANISOU 1514 CB PRO A 249 12894 12037 10938 -355 -1160 -1381 C ATOM 1515 CG PRO A 249 -14.230 17.680 -22.999 1.00 91.99 C ANISOU 1515 CG PRO A 249 12566 11652 10732 -500 -986 -1424 C ATOM 1516 CD PRO A 249 -15.443 17.292 -22.212 1.00 92.45 C ANISOU 1516 CD PRO A 249 12852 11646 10630 -523 -870 -1391 C ATOM 1517 N MET A 250 -13.110 18.977 -20.136 1.00 99.39 N ANISOU 1517 N MET A 250 13645 12780 11340 -527 -1323 -1644 N ATOM 1518 CA MET A 250 -12.400 20.030 -19.410 1.00 99.46 C ANISOU 1518 CA MET A 250 13606 12872 11314 -602 -1485 -1793 C ATOM 1519 C MET A 250 -12.519 19.896 -17.898 1.00101.59 C ANISOU 1519 C MET A 250 14124 13193 11283 -577 -1579 -1835 C ATOM 1520 O MET A 250 -11.569 20.187 -17.173 1.00102.65 O ANISOU 1520 O MET A 250 14239 13442 11323 -579 -1808 -1912 O ATOM 1521 CB MET A 250 -12.861 21.419 -19.854 1.00 97.07 C ANISOU 1521 CB MET A 250 13224 12485 11174 -756 -1376 -1916 C ATOM 1522 CG MET A 250 -12.313 21.838 -21.200 1.00 95.64 C ANISOU 1522 CG MET A 250 12787 12290 11262 -815 -1360 -1896 C ATOM 1523 SD MET A 250 -10.523 21.631 -21.271 1.00 97.29 S ANISOU 1523 SD MET A 250 12754 12681 11530 -789 -1606 -1904 S ATOM 1524 CE MET A 250 -10.373 20.316 -22.480 1.00 97.37 C ANISOU 1524 CE MET A 250 12656 12699 11641 -640 -1512 -1734 C ATOM 1525 N LEU A 251 -13.681 19.461 -17.423 1.00100.76 N ANISOU 1525 N LEU A 251 14250 13015 11019 -567 -1403 -1786 N ATOM 1526 CA LEU A 251 -13.873 19.246 -15.995 1.00102.88 C ANISOU 1526 CA LEU A 251 14794 13335 10961 -548 -1456 -1808 C ATOM 1527 C LEU A 251 -12.940 18.140 -15.520 1.00104.85 C ANISOU 1527 C LEU A 251 15117 13670 11053 -406 -1684 -1680 C ATOM 1528 O LEU A 251 -12.379 18.215 -14.429 1.00105.81 O ANISOU 1528 O LEU A 251 15370 13892 10939 -384 -1883 -1725 O ATOM 1529 CB LEU A 251 -15.329 18.891 -15.685 1.00 91.30 C ANISOU 1529 CB LEU A 251 13534 11785 9371 -577 -1181 -1759 C ATOM 1530 CG LEU A 251 -15.715 18.738 -14.214 1.00 93.31 C ANISOU 1530 CG LEU A 251 14103 12091 9262 -584 -1164 -1784 C ATOM 1531 CD1 LEU A 251 -15.254 19.944 -13.413 1.00 93.72 C ANISOU 1531 CD1 LEU A 251 14188 12211 9209 -647 -1293 -1999 C ATOM 1532 CD2 LEU A 251 -17.217 18.548 -14.081 1.00 93.41 C ANISOU 1532 CD2 LEU A 251 14242 12035 9214 -642 -839 -1755 C ATOM 1533 N VAL A 252 -12.769 17.121 -16.358 1.00100.19 N ANISOU 1533 N VAL A 252 14449 13032 10588 -300 -1664 -1525 N ATOM 1534 CA VAL A 252 -11.849 16.028 -16.068 1.00102.20 C ANISOU 1534 CA VAL A 252 14751 13338 10741 -121 -1880 -1395 C ATOM 1535 C VAL A 252 -10.402 16.510 -16.109 1.00102.61 C ANISOU 1535 C VAL A 252 14541 13548 10899 -73 -2162 -1480 C ATOM 1536 O VAL A 252 -9.629 16.265 -15.182 1.00104.58 O ANISOU 1536 O VAL A 252 14863 13911 10962 18 -2421 -1467 O ATOM 1537 CB VAL A 252 -12.026 14.860 -17.060 1.00 97.03 C ANISOU 1537 CB VAL A 252 14079 12566 10224 -13 -1771 -1236 C ATOM 1538 CG1 VAL A 252 -10.894 13.855 -16.910 1.00 99.43 C ANISOU 1538 CG1 VAL A 252 14377 12913 10488 212 -2012 -1124 C ATOM 1539 CG2 VAL A 252 -13.373 14.188 -16.856 1.00 97.24 C ANISOU 1539 CG2 VAL A 252 14382 12448 10114 -70 -1534 -1132 C ATOM 1540 N ALA A 253 -10.046 17.201 -17.188 1.00 93.36 N ANISOU 1540 N ALA A 253 13062 12391 10020 -147 -2114 -1560 N ATOM 1541 CA ALA A 253 -8.691 17.713 -17.368 1.00 93.86 C ANISOU 1541 CA ALA A 253 12822 12614 10226 -143 -2342 -1644 C ATOM 1542 C ALA A 253 -8.317 18.727 -16.289 1.00 94.41 C ANISOU 1542 C ALA A 253 12927 12792 10151 -269 -2534 -1804 C ATOM 1543 O ALA A 253 -7.152 18.834 -15.906 1.00 95.74 O ANISOU 1543 O ALA A 253 12932 13128 10316 -235 -2813 -1850 O ATOM 1544 CB ALA A 253 -8.534 18.325 -18.751 1.00 86.78 C ANISOU 1544 CB ALA A 253 11630 11693 9649 -243 -2200 -1691 C ATOM 1545 N SER A 254 -9.307 19.470 -15.806 1.00108.21 N ANISOU 1545 N SER A 254 14883 14449 11785 -413 -2385 -1901 N ATOM 1546 CA SER A 254 -9.080 20.440 -14.742 1.00108.90 C ANISOU 1546 CA SER A 254 15066 14607 11702 -539 -2540 -2078 C ATOM 1547 C SER A 254 -8.743 19.724 -13.442 1.00111.28 C ANISOU 1547 C SER A 254 15606 15020 11657 -422 -2770 -2024 C ATOM 1548 O SER A 254 -7.840 20.134 -12.710 1.00113.21 O ANISOU 1548 O SER A 254 15809 15413 11793 -456 -3061 -2126 O ATOM 1549 CB SER A 254 -10.309 21.328 -14.547 1.00100.82 C ANISOU 1549 CB SER A 254 14231 13442 10635 -680 -2290 -2197 C ATOM 1550 OG SER A 254 -10.649 21.994 -15.750 1.00 98.32 O ANISOU 1550 OG SER A 254 13716 13010 10630 -773 -2100 -2226 O ATOM 1551 N ILE A 255 -9.479 18.654 -13.161 1.00103.67 N ANISOU 1551 N ILE A 255 14901 13979 10509 -297 -2647 -1858 N ATOM 1552 CA ILE A 255 -9.234 17.840 -11.978 1.00105.97 C ANISOU 1552 CA ILE A 255 15468 14347 10448 -172 -2847 -1759 C ATOM 1553 C ILE A 255 -7.860 17.188 -12.047 1.00107.84 C ANISOU 1553 C ILE A 255 15504 14725 10747 8 -3184 -1670 C ATOM 1554 O ILE A 255 -7.096 17.229 -11.082 1.00109.61 O ANISOU 1554 O ILE A 255 15788 15102 10758 50 -3501 -1701 O ATOM 1555 CB ILE A 255 -10.304 16.742 -11.821 1.00112.68 C ANISOU 1555 CB ILE A 255 16630 15056 11128 -93 -2616 -1568 C ATOM 1556 CG1 ILE A 255 -11.666 17.367 -11.512 1.00111.79 C ANISOU 1556 CG1 ILE A 255 16717 14850 10907 -259 -2299 -1664 C ATOM 1557 CG2 ILE A 255 -9.915 15.766 -10.722 1.00115.31 C ANISOU 1557 CG2 ILE A 255 17254 15449 11110 59 -2845 -1418 C ATOM 1558 CD1 ILE A 255 -12.809 16.375 -11.527 1.00112.37 C ANISOU 1558 CD1 ILE A 255 17029 14791 10875 -234 -2025 -1489 C ATOM 1559 N LEU A 256 -7.545 16.601 -13.197 1.00110.10 N ANISOU 1559 N LEU A 256 15543 14969 11323 123 -3118 -1568 N ATOM 1560 CA LEU A 256 -6.260 15.940 -13.387 1.00112.09 C ANISOU 1560 CA LEU A 256 15559 15352 11678 331 -3399 -1489 C ATOM 1561 C LEU A 256 -5.090 16.913 -13.278 1.00112.52 C ANISOU 1561 C LEU A 256 15275 15624 11854 237 -3669 -1661 C ATOM 1562 O LEU A 256 -4.120 16.638 -12.575 1.00114.91 O ANISOU 1562 O LEU A 256 15517 16101 12042 360 -4017 -1644 O ATOM 1563 CB LEU A 256 -6.222 15.215 -14.735 1.00114.88 C ANISOU 1563 CB LEU A 256 15715 15606 12327 458 -3221 -1382 C ATOM 1564 CG LEU A 256 -7.151 14.005 -14.861 1.00115.67 C ANISOU 1564 CG LEU A 256 16133 15494 12321 579 -3020 -1192 C ATOM 1565 CD1 LEU A 256 -7.003 13.347 -16.225 1.00115.94 C ANISOU 1565 CD1 LEU A 256 15968 15438 12646 698 -2870 -1123 C ATOM 1566 CD2 LEU A 256 -6.883 13.005 -13.746 1.00118.35 C ANISOU 1566 CD2 LEU A 256 16773 15840 12355 780 -3253 -1036 C ATOM 1567 N ASN A 257 -5.199 18.061 -13.939 1.00120.75 N ANISOU 1567 N ASN A 257 16107 16652 13119 8 -3522 -1823 N ATOM 1568 CA ASN A 257 -4.139 19.065 -13.893 1.00121.39 C ANISOU 1568 CA ASN A 257 15868 16917 13336 -141 -3750 -1995 C ATOM 1569 C ASN A 257 -3.938 19.645 -12.498 1.00122.57 C ANISOU 1569 C ASN A 257 16214 17175 13182 -246 -4020 -2124 C ATOM 1570 O ASN A 257 -2.854 20.125 -12.165 1.00123.81 O ANISOU 1570 O ASN A 257 16134 17532 13378 -313 -4329 -2234 O ATOM 1571 CB ASN A 257 -4.397 20.185 -14.903 1.00116.31 C ANISOU 1571 CB ASN A 257 15024 16188 12982 -383 -3511 -2122 C ATOM 1572 CG ASN A 257 -3.833 19.873 -16.273 1.00115.51 C ANISOU 1572 CG ASN A 257 14553 16117 13219 -318 -3403 -2050 C ATOM 1573 OD1 ASN A 257 -2.685 20.202 -16.573 1.00116.06 O ANISOU 1573 OD1 ASN A 257 14254 16368 13477 -362 -3569 -2112 O ATOM 1574 ND2 ASN A 257 -4.638 19.233 -17.113 1.00114.08 N ANISOU 1574 ND2 ASN A 257 14465 15769 13111 -223 -3118 -1925 N ATOM 1575 N THR A 258 -4.987 19.592 -11.685 1.00121.70 N ANISOU 1575 N THR A 258 16535 16943 12762 -270 -3900 -2119 N ATOM 1576 CA THR A 258 -4.898 20.024 -10.297 1.00123.14 C ANISOU 1576 CA THR A 258 16981 17221 12587 -350 -4133 -2236 C ATOM 1577 C THR A 258 -4.136 18.980 -9.486 1.00125.84 C ANISOU 1577 C THR A 258 17402 17722 12688 -116 -4487 -2086 C ATOM 1578 O THR A 258 -3.287 19.315 -8.661 1.00128.00 O ANISOU 1578 O THR A 258 17639 18190 12806 -152 -4855 -2183 O ATOM 1579 CB THR A 258 -6.295 20.234 -9.684 1.00115.66 C ANISOU 1579 CB THR A 258 16475 16105 11366 -433 -3852 -2273 C ATOM 1580 OG1 THR A 258 -7.005 21.228 -10.435 1.00113.24 O ANISOU 1580 OG1 THR A 258 16085 15645 11298 -617 -3545 -2410 O ATOM 1581 CG2 THR A 258 -6.184 20.684 -8.234 1.00117.12 C ANISOU 1581 CG2 THR A 258 16962 16395 11144 -516 -4081 -2411 C ATOM 1582 N VAL A 259 -4.447 17.712 -9.733 1.00114.52 N ANISOU 1582 N VAL A 259 16090 16197 11225 123 -4388 -1847 N ATOM 1583 CA VAL A 259 -3.776 16.602 -9.067 1.00117.22 C ANISOU 1583 CA VAL A 259 16534 16644 11362 390 -4707 -1665 C ATOM 1584 C VAL A 259 -2.318 16.509 -9.499 1.00118.94 C ANISOU 1584 C VAL A 259 16269 17074 11848 520 -5032 -1674 C ATOM 1585 O VAL A 259 -1.425 16.293 -8.675 1.00121.56 O ANISOU 1585 O VAL A 259 16574 17603 12009 635 -5444 -1655 O ATOM 1586 CB VAL A 259 -4.483 15.262 -9.356 1.00114.45 C ANISOU 1586 CB VAL A 259 16435 16093 10960 605 -4493 -1406 C ATOM 1587 CG1 VAL A 259 -3.716 14.104 -8.735 1.00117.46 C ANISOU 1587 CG1 VAL A 259 16922 16548 11159 911 -4840 -1202 C ATOM 1588 CG2 VAL A 259 -5.910 15.297 -8.843 1.00113.57 C ANISOU 1588 CG2 VAL A 259 16776 15804 10570 467 -4178 -1388 C ATOM 1589 N ILE A 260 -2.095 16.680 -10.800 1.00136.01 N ANISOU 1589 N ILE A 260 18044 19209 14424 498 -4839 -1704 N ATOM 1590 CA ILE A 260 -0.770 16.571 -11.397 1.00137.59 C ANISOU 1590 CA ILE A 260 17735 19613 14930 618 -5061 -1715 C ATOM 1591 C ILE A 260 0.176 17.599 -10.784 1.00138.25 C ANISOU 1591 C ILE A 260 17574 19954 15002 426 -5407 -1916 C ATOM 1592 O ILE A 260 1.338 17.302 -10.503 1.00141.13 O ANISOU 1592 O ILE A 260 17655 20559 15411 577 -5778 -1897 O ATOM 1593 CB ILE A 260 -0.849 16.782 -12.929 1.00140.74 C ANISOU 1593 CB ILE A 260 17805 19928 15743 554 -4722 -1742 C ATOM 1594 CG1 ILE A 260 -1.401 15.526 -13.609 1.00141.47 C ANISOU 1594 CG1 ILE A 260 18046 19821 15885 810 -4482 -1537 C ATOM 1595 CG2 ILE A 260 0.506 17.169 -13.512 1.00141.79 C ANISOU 1595 CG2 ILE A 260 17362 20311 16199 542 -4904 -1836 C ATOM 1596 CD1 ILE A 260 -1.339 15.570 -15.116 1.00140.41 C ANISOU 1596 CD1 ILE A 260 17592 19633 16126 792 -4193 -1553 C ATOM 1597 N ALA A 261 -0.338 18.803 -10.561 1.00124.50 N ANISOU 1597 N ALA A 261 15946 18156 13202 95 -5295 -2112 N ATOM 1598 CA ALA A 261 0.448 19.882 -9.974 1.00125.28 C ANISOU 1598 CA ALA A 261 15865 18456 13280 -146 -5601 -2331 C ATOM 1599 C ALA A 261 0.816 19.577 -8.523 1.00127.87 C ANISOU 1599 C ALA A 261 16446 18943 13194 -53 -6024 -2320 C ATOM 1600 O ALA A 261 1.911 19.907 -8.067 1.00129.83 O ANISOU 1600 O ALA A 261 16427 19451 13450 -103 -6429 -2420 O ATOM 1601 CB ALA A 261 -0.307 21.199 -10.068 1.00117.89 C ANISOU 1601 CB ALA A 261 15070 17360 12363 -500 -5353 -2542 C ATOM 1602 N ASN A 262 -0.107 18.944 -7.805 1.00167.92 N ANISOU 1602 N ASN A 262 22036 23869 17897 69 -5932 -2194 N ATOM 1603 CA ASN A 262 0.122 18.570 -6.412 1.00170.58 C ANISOU 1603 CA ASN A 262 22698 24333 17781 169 -6305 -2150 C ATOM 1604 C ASN A 262 0.983 17.320 -6.260 1.00173.35 C ANISOU 1604 C ASN A 262 22925 24826 18115 543 -6636 -1916 C ATOM 1605 O ASN A 262 1.854 17.260 -5.392 1.00176.56 O ANISOU 1605 O ASN A 262 23289 25469 18328 612 -7108 -1928 O ATOM 1606 CB ASN A 262 -1.211 18.369 -5.688 1.00177.72 C ANISOU 1606 CB ASN A 262 24219 25030 18277 142 -6049 -2094 C ATOM 1607 CG ASN A 262 -1.992 19.658 -5.537 1.00176.06 C ANISOU 1607 CG ASN A 262 24174 24712 18010 -196 -5801 -2353 C ATOM 1608 OD1 ASN A 262 -1.412 20.739 -5.432 1.00175.62 O ANISOU 1608 OD1 ASN A 262 23915 24770 18044 -428 -5975 -2593 O ATOM 1609 ND2 ASN A 262 -3.315 19.551 -5.521 1.00174.75 N ANISOU 1609 ND2 ASN A 262 24375 24320 17703 -225 -5392 -2311 N ATOM 1610 N LYS A 263 0.729 16.322 -7.101 1.00193.75 N ANISOU 1610 N LYS A 263 25463 27257 20898 791 -6399 -1709 N ATOM 1611 CA LYS A 263 1.481 15.072 -7.058 1.00196.34 C ANISOU 1611 CA LYS A 263 25693 27663 21244 1188 -6669 -1479 C ATOM 1612 C LYS A 263 2.952 15.269 -7.410 1.00197.82 C ANISOU 1612 C LYS A 263 25255 28155 21753 1270 -7017 -1560 C ATOM 1613 O LYS A 263 3.818 14.573 -6.885 1.00200.85 O ANISOU 1613 O LYS A 263 25545 28713 22054 1556 -7430 -1440 O ATOM 1614 CB LYS A 263 0.850 14.029 -7.984 1.00176.36 C ANISOU 1614 CB LYS A 263 23256 24867 18887 1406 -6301 -1275 C ATOM 1615 CG LYS A 263 0.255 12.833 -7.254 1.00177.88 C ANISOU 1615 CG LYS A 263 23996 24879 18712 1646 -6323 -1013 C ATOM 1616 CD LYS A 263 -0.882 13.237 -6.331 1.00176.98 C ANISOU 1616 CD LYS A 263 24427 24648 18170 1403 -6163 -1046 C ATOM 1617 CE LYS A 263 -1.474 12.023 -5.632 1.00178.46 C ANISOU 1617 CE LYS A 263 25165 24653 17989 1612 -6157 -765 C ATOM 1618 NZ LYS A 263 -2.600 12.387 -4.729 1.00177.51 N ANISOU 1618 NZ LYS A 263 25567 24439 17440 1371 -5960 -796 N ATOM 1619 N LEU A 264 3.229 16.219 -8.297 1.00159.94 N ANISOU 1619 N LEU A 264 20024 23423 17322 1019 -6850 -1756 N ATOM 1620 CA LEU A 264 4.600 16.496 -8.713 1.00161.57 C ANISOU 1620 CA LEU A 264 19587 23934 17866 1042 -7123 -1850 C ATOM 1621 C LEU A 264 5.439 17.047 -7.561 1.00163.57 C ANISOU 1621 C LEU A 264 19758 24485 17905 931 -7657 -1977 C ATOM 1622 O LEU A 264 6.598 16.669 -7.391 1.00167.66 O ANISOU 1622 O LEU A 264 19889 25283 18531 1137 -8057 -1940 O ATOM 1623 CB LEU A 264 4.616 17.475 -9.889 1.00166.91 C ANISOU 1623 CB LEU A 264 19879 24592 18946 737 -6789 -2027 C ATOM 1624 CG LEU A 264 5.992 17.812 -10.467 1.00168.58 C ANISOU 1624 CG LEU A 264 19385 25120 19547 709 -6987 -2128 C ATOM 1625 CD1 LEU A 264 6.647 16.571 -11.055 1.00170.25 C ANISOU 1625 CD1 LEU A 264 19301 25411 19975 1158 -7024 -1942 C ATOM 1626 CD2 LEU A 264 5.886 18.913 -11.511 1.00166.47 C ANISOU 1626 CD2 LEU A 264 18842 24802 19607 337 -6641 -2299 C ATOM 1627 N THR A 265 4.846 17.940 -6.774 1.00157.07 N ANISOU 1627 N THR A 265 19297 23606 16778 610 -7666 -2137 N ATOM 1628 CA THR A 265 5.531 18.534 -5.629 1.00162.02 C ANISOU 1628 CA THR A 265 19923 24492 17146 459 -8165 -2286 C ATOM 1629 C THR A 265 5.781 17.501 -4.528 1.00165.93 C ANISOU 1629 C THR A 265 20717 25082 17246 794 -8561 -2075 C ATOM 1630 O THR A 265 6.777 17.574 -3.809 1.00171.39 O ANISOU 1630 O THR A 265 21202 26032 17887 776 -8910 -2053 O ATOM 1631 CB THR A 265 4.738 19.728 -5.059 1.00164.81 C ANISOU 1631 CB THR A 265 20659 24717 17243 44 -8030 -2523 C ATOM 1632 OG1 THR A 265 4.452 20.658 -6.111 1.00161.38 O ANISOU 1632 OG1 THR A 265 19985 24148 17183 -248 -7639 -2684 O ATOM 1633 CG2 THR A 265 5.531 20.435 -3.970 1.00170.02 C ANISOU 1633 CG2 THR A 265 21274 25624 17702 -188 -8422 -2662 C ATOM 1634 N VAL A 266 4.871 16.542 -4.391 1.00177.60 N ANISOU 1634 N VAL A 266 22685 26308 18485 1037 -8353 -1851 N ATOM 1635 CA VAL A 266 5.056 15.461 -3.431 1.00181.84 C ANISOU 1635 CA VAL A 266 23546 26880 18663 1367 -8664 -1596 C ATOM 1636 C VAL A 266 6.239 14.590 -3.851 1.00184.72 C ANISOU 1636 C VAL A 266 23414 27422 19349 1743 -8922 -1426 C ATOM 1637 O VAL A 266 7.064 14.194 -3.027 1.00189.80 O ANISOU 1637 O VAL A 266 23998 28253 19865 1886 -9275 -1294 O ATOM 1638 CB VAL A 266 3.786 14.593 -3.305 1.00217.31 C ANISOU 1638 CB VAL A 266 28671 31034 22863 1522 -8342 -1382 C ATOM 1639 CG1 VAL A 266 4.055 13.367 -2.446 1.00221.59 C ANISOU 1639 CG1 VAL A 266 29525 31580 23090 1887 -8640 -1076 C ATOM 1640 CG2 VAL A 266 2.641 15.410 -2.727 1.00215.13 C ANISOU 1640 CG2 VAL A 266 28886 30609 22245 1166 -8065 -1533 C ATOM 1641 N MET A 267 6.313 14.313 -5.148 1.00202.49 N ANISOU 1641 N MET A 267 25297 29604 22034 1887 -8688 -1426 N ATOM 1642 CA MET A 267 7.355 13.465 -5.724 1.00205.34 C ANISOU 1642 CA MET A 267 25168 30115 22736 2287 -8882 -1297 C ATOM 1643 C MET A 267 8.721 14.144 -5.854 1.00209.01 C ANISOU 1643 C MET A 267 24924 30952 23539 2149 -9122 -1444 C ATOM 1644 O MET A 267 9.744 13.465 -5.941 1.00212.32 O ANISOU 1644 O MET A 267 24957 31546 24169 2461 -9338 -1312 O ATOM 1645 CB MET A 267 6.913 12.929 -7.089 1.00252.08 C ANISOU 1645 CB MET A 267 30969 35784 29025 2420 -8362 -1217 C ATOM 1646 CG MET A 267 5.674 12.049 -7.035 1.00250.66 C ANISOU 1646 CG MET A 267 31440 35207 28594 2554 -8034 -1002 C ATOM 1647 SD MET A 267 5.913 10.565 -6.038 1.00254.77 S ANISOU 1647 SD MET A 267 32375 35664 28762 3064 -8441 -669 S ATOM 1648 CE MET A 267 4.305 9.791 -6.189 1.00251.84 C ANISOU 1648 CE MET A 267 32728 34799 28161 3059 -7922 -470 C ATOM 1649 N VAL A 268 8.743 15.474 -5.865 1.00258.48 N ANISOU 1649 N VAL A 268 31024 37323 29863 1673 -9064 -1707 N ATOM 1650 CA VAL A 268 9.981 16.207 -6.135 1.00261.82 C ANISOU 1650 CA VAL A 268 30764 38072 30644 1468 -9222 -1851 C ATOM 1651 C VAL A 268 10.937 16.161 -4.938 1.00268.84 C ANISOU 1651 C VAL A 268 31583 39226 31337 1473 -9679 -1770 C ATOM 1652 O VAL A 268 12.100 16.555 -5.038 1.00273.07 O ANISOU 1652 O VAL A 268 31542 40061 32151 1366 -9878 -1832 O ATOM 1653 CB VAL A 268 9.699 17.676 -6.549 1.00155.10 C ANISOU 1653 CB VAL A 268 17126 24543 17263 927 -9002 -2149 C ATOM 1654 CG1 VAL A 268 9.305 18.501 -5.338 1.00156.81 C ANISOU 1654 CG1 VAL A 268 17795 24731 17053 574 -9132 -2261 C ATOM 1655 CG2 VAL A 268 10.915 18.299 -7.221 1.00157.24 C ANISOU 1655 CG2 VAL A 268 16642 25101 18002 737 -9050 -2268 C ATOM 1656 N HIS A 269 10.451 15.655 -3.810 1.00232.52 N ANISOU 1656 N HIS A 269 27569 34525 26254 1595 -9841 -1619 N ATOM 1657 CA HIS A 269 11.310 15.427 -2.655 1.00239.20 C ANISOU 1657 CA HIS A 269 28394 35617 26875 1663 -10289 -1502 C ATOM 1658 C HIS A 269 11.235 13.973 -2.206 1.00241.26 C ANISOU 1658 C HIS A 269 28977 35764 26928 2177 -10429 -1175 C ATOM 1659 O HIS A 269 12.245 13.374 -1.836 1.00247.12 O ANISOU 1659 O HIS A 269 29444 36715 27737 2440 -10769 -1017 O ATOM 1660 CB HIS A 269 10.935 16.355 -1.522 1.00217.29 C ANISOU 1660 CB HIS A 269 26023 32876 23663 1251 -10393 -1649 C ATOM 1661 N GLN A 270 10.032 13.409 -2.243 1.00180.30 N ANISOU 1661 N GLN A 270 21846 27699 18960 2310 -10161 -1068 N ATOM 1662 CA GLN A 270 9.824 12.017 -1.864 1.00181.47 C ANISOU 1662 CA GLN A 270 22382 27668 18902 2768 -10238 -744 C ATOM 1663 C GLN A 270 8.595 11.437 -2.556 1.00174.94 C ANISOU 1663 C GLN A 270 21977 26449 18042 2907 -9830 -664 C ATOM 1664 O GLN A 270 7.809 10.715 -1.943 1.00174.83 O ANISOU 1664 O GLN A 270 22590 26193 17645 3038 -9771 -460 O ATOM 1665 CB GLN A 270 9.697 11.890 -0.353 1.00166.46 C ANISOU 1665 CB GLN A 270 20992 25806 16451 2712 -10500 -618 C ATOM 1666 N PRO A 297 16.767 15.733 -11.942 1.00231.05 N ANISOU 1666 N PRO A 297 22279 35701 29810 2040 -8797 -1990 N ATOM 1667 CA PRO A 297 17.728 16.579 -12.656 1.00233.50 C ANISOU 1667 CA PRO A 297 21906 36286 30525 1696 -8658 -2124 C ATOM 1668 C PRO A 297 17.104 17.280 -13.862 1.00228.08 C ANISOU 1668 C PRO A 297 21170 35468 30023 1379 -8154 -2286 C ATOM 1669 O PRO A 297 16.446 18.308 -13.698 1.00224.90 O ANISOU 1669 O PRO A 297 21054 34927 29470 909 -8083 -2418 O ATOM 1670 CB PRO A 297 18.793 15.579 -13.108 1.00223.62 C ANISOU 1670 CB PRO A 297 20118 35252 29597 2182 -8678 -2000 C ATOM 1671 CG PRO A 297 18.067 14.275 -13.246 1.00220.70 C ANISOU 1671 CG PRO A 297 20164 34612 29080 2756 -8591 -1854 C ATOM 1672 CD PRO A 297 16.857 14.318 -12.345 1.00217.05 C ANISOU 1672 CD PRO A 297 20485 33854 28130 2677 -8736 -1818 C ATOM 1673 N GLY A 298 17.303 16.728 -15.054 1.00169.65 N ANISOU 1673 N GLY A 298 13426 28101 22933 1637 -7801 -2274 N ATOM 1674 CA GLY A 298 16.704 17.281 -16.252 1.00164.11 C ANISOU 1674 CA GLY A 298 12685 27279 22389 1373 -7311 -2405 C ATOM 1675 C GLY A 298 15.313 16.726 -16.474 1.00157.46 C ANISOU 1675 C GLY A 298 12433 26091 21306 1594 -7129 -2381 C ATOM 1676 O GLY A 298 14.575 17.204 -17.336 1.00152.41 O ANISOU 1676 O GLY A 298 11964 25237 20709 1332 -6689 -2435 O ATOM 1677 N ARG A 299 14.949 15.714 -15.695 1.00172.60 N ANISOU 1677 N ARG A 299 14763 27866 22951 2035 -7393 -2230 N ATOM 1678 CA ARG A 299 13.630 15.117 -15.825 1.00167.39 C ANISOU 1678 CA ARG A 299 14814 26755 22032 2192 -7120 -2103 C ATOM 1679 C ARG A 299 12.595 15.992 -15.129 1.00164.09 C ANISOU 1679 C ARG A 299 14976 26096 21274 1759 -7128 -2152 C ATOM 1680 O ARG A 299 11.549 16.296 -15.696 1.00160.02 O ANISOU 1680 O ARG A 299 14849 25258 20695 1547 -6706 -2149 O ATOM 1681 CB ARG A 299 13.618 13.700 -15.240 1.00202.45 C ANISOU 1681 CB ARG A 299 19525 31095 26301 2800 -7374 -1900 C ATOM 1682 CG ARG A 299 12.253 13.024 -15.246 1.00198.36 C ANISOU 1682 CG ARG A 299 19789 30087 25491 2930 -7103 -1741 C ATOM 1683 CD ARG A 299 12.308 11.641 -14.608 1.00200.86 C ANISOU 1683 CD ARG A 299 20390 30293 25636 3508 -7382 -1529 C ATOM 1684 NE ARG A 299 10.988 11.020 -14.537 1.00199.81 N ANISOU 1684 NE ARG A 299 21015 29693 25210 3579 -7134 -1375 N ATOM 1685 CZ ARG A 299 10.158 11.146 -13.507 1.00198.75 C ANISOU 1685 CZ ARG A 299 21473 29377 24667 3432 -7287 -1302 C ATOM 1686 NH1 ARG A 299 10.513 11.872 -12.455 1.00199.20 N ANISOU 1686 NH1 ARG A 299 21484 29666 24537 3218 -7697 -1379 N ATOM 1687 NH2 ARG A 299 8.974 10.550 -13.527 1.00196.94 N ANISOU 1687 NH2 ARG A 299 21881 28741 24209 3487 -7023 -1163 N ATOM 1688 N VAL A 300 12.922 16.443 -13.920 1.00222.23 N ANISOU 1688 N VAL A 300 22372 33636 28429 1622 -7613 -2214 N ATOM 1689 CA VAL A 300 11.994 17.241 -13.124 1.00219.59 C ANISOU 1689 CA VAL A 300 22603 33090 27740 1249 -7656 -2279 C ATOM 1690 C VAL A 300 11.715 18.602 -13.753 1.00217.01 C ANISOU 1690 C VAL A 300 22186 32700 27566 680 -7338 -2467 C ATOM 1691 O VAL A 300 10.635 19.163 -13.575 1.00213.05 O ANISOU 1691 O VAL A 300 22208 31898 26844 418 -7139 -2501 O ATOM 1692 CB VAL A 300 12.490 17.430 -11.668 1.00164.59 C ANISOU 1692 CB VAL A 300 15722 26320 20495 1207 -8223 -2294 C ATOM 1693 CG1 VAL A 300 12.475 16.103 -10.923 1.00166.47 C ANISOU 1693 CG1 VAL A 300 16267 26503 20482 1738 -8490 -2057 C ATOM 1694 CG2 VAL A 300 13.876 18.059 -11.639 1.00170.32 C ANISOU 1694 CG2 VAL A 300 15814 27393 21507 969 -8391 -2356 C ATOM 1695 N GLN A 301 12.687 19.122 -14.494 1.00166.49 N ANISOU 1695 N GLN A 301 15124 26583 21552 497 -7281 -2582 N ATOM 1696 CA GLN A 301 12.501 20.374 -15.216 1.00164.37 C ANISOU 1696 CA GLN A 301 14749 26242 21460 -35 -6957 -2735 C ATOM 1697 C GLN A 301 11.665 20.151 -16.469 1.00158.85 C ANISOU 1697 C GLN A 301 14248 25235 20871 6 -6367 -2645 C ATOM 1698 O GLN A 301 10.860 21.002 -16.845 1.00155.60 O ANISOU 1698 O GLN A 301 14128 24568 20426 -352 -6068 -2704 O ATOM 1699 CB GLN A 301 13.847 21.005 -15.578 1.00165.29 C ANISOU 1699 CB GLN A 301 14127 26736 21939 -287 -7050 -2846 C ATOM 1700 CG GLN A 301 14.624 21.542 -14.387 1.00170.68 C ANISOU 1700 CG GLN A 301 14761 27581 22508 -508 -7483 -2859 C ATOM 1701 CD GLN A 301 14.142 22.913 -13.941 1.00169.87 C ANISOU 1701 CD GLN A 301 14988 27299 22256 -1078 -7486 -3018 C ATOM 1702 OE1 GLN A 301 12.942 23.151 -13.799 1.00165.51 O ANISOU 1702 OE1 GLN A 301 14980 26449 21459 -1153 -7357 -3080 O ATOM 1703 NE2 GLN A 301 15.081 23.823 -13.719 1.00174.70 N ANISOU 1703 NE2 GLN A 301 15279 28077 23024 -1478 -7633 -3084 N ATOM 1704 N ALA A 302 11.860 19.005 -17.114 1.00151.41 N ANISOU 1704 N ALA A 302 13156 24315 20058 454 -6214 -2507 N ATOM 1705 CA ALA A 302 11.060 18.645 -18.277 1.00148.40 C ANISOU 1705 CA ALA A 302 12994 23645 19746 535 -5685 -2418 C ATOM 1706 C ALA A 302 9.618 18.364 -17.874 1.00146.19 C ANISOU 1706 C ALA A 302 13475 22949 19120 589 -5567 -2318 C ATOM 1707 O ALA A 302 8.682 18.739 -18.581 1.00143.75 O ANISOU 1707 O ALA A 302 13455 22363 18801 393 -5174 -2312 O ATOM 1708 CB ALA A 302 11.662 17.445 -18.992 1.00124.29 C ANISOU 1708 CB ALA A 302 9614 20712 16896 1018 -5576 -2317 C ATOM 1709 N LEU A 303 9.446 17.702 -16.733 1.00143.30 N ANISOU 1709 N LEU A 303 13426 22553 18467 853 -5911 -2235 N ATOM 1710 CA LEU A 303 8.112 17.463 -16.190 1.00141.26 C ANISOU 1710 CA LEU A 303 13879 21937 17857 875 -5824 -2145 C ATOM 1711 C LEU A 303 7.448 18.769 -15.790 1.00138.98 C ANISOU 1711 C LEU A 303 13858 21524 17424 393 -5779 -2288 C ATOM 1712 O LEU A 303 6.252 18.950 -16.001 1.00137.39 O ANISOU 1712 O LEU A 303 14105 21006 17090 279 -5474 -2260 O ATOM 1713 CB LEU A 303 8.155 16.512 -14.994 1.00135.96 C ANISOU 1713 CB LEU A 303 13491 21280 16887 1237 -6217 -2017 C ATOM 1714 CG LEU A 303 8.053 15.012 -15.283 1.00138.07 C ANISOU 1714 CG LEU A 303 13893 21417 17151 1754 -6147 -1813 C ATOM 1715 CD1 LEU A 303 6.660 14.683 -15.821 1.00131.39 C ANISOU 1715 CD1 LEU A 303 13576 20161 16185 1733 -5706 -1721 C ATOM 1716 CD2 LEU A 303 9.128 14.517 -16.245 1.00140.76 C ANISOU 1716 CD2 LEU A 303 13628 21977 17876 2013 -6082 -1816 C ATOM 1717 N ARG A 304 8.224 19.674 -15.203 1.00152.80 N ANISOU 1717 N ARG A 304 15329 23521 19206 115 -6091 -2448 N ATOM 1718 CA ARG A 304 7.683 20.955 -14.767 1.00151.31 C ANISOU 1718 CA ARG A 304 15398 23208 18887 -340 -6078 -2610 C ATOM 1719 C ARG A 304 7.180 21.794 -15.945 1.00148.05 C ANISOU 1719 C ARG A 304 14953 22599 18700 -657 -5615 -2668 C ATOM 1720 O ARG A 304 6.124 22.417 -15.847 1.00145.54 O ANISOU 1720 O ARG A 304 15071 21996 18232 -866 -5420 -2711 O ATOM 1721 CB ARG A 304 8.731 21.727 -13.968 1.00274.84 C ANISOU 1721 CB ARG A 304 30714 39166 34547 -588 -6525 -2785 C ATOM 1722 CG ARG A 304 8.152 22.567 -12.842 1.00275.63 C ANISOU 1722 CG ARG A 304 31273 39142 34312 -872 -6712 -2925 C ATOM 1723 CD ARG A 304 9.251 23.230 -12.026 1.00281.61 C ANISOU 1723 CD ARG A 304 31704 40227 35070 -1105 -7201 -3104 C ATOM 1724 NE ARG A 304 8.712 24.164 -11.041 1.00282.68 N ANISOU 1724 NE ARG A 304 32283 40225 34896 -1424 -7346 -3279 N ATOM 1725 CZ ARG A 304 8.313 23.811 -9.823 1.00284.30 C ANISOU 1725 CZ ARG A 304 32945 40404 34672 -1279 -7617 -3263 C ATOM 1726 NH1 ARG A 304 8.391 22.543 -9.444 1.00285.16 N ANISOU 1726 NH1 ARG A 304 33133 40598 34616 -826 -7786 -3058 N ATOM 1727 NH2 ARG A 304 7.831 24.721 -8.987 1.00285.29 N ANISOU 1727 NH2 ARG A 304 33482 40392 34524 -1586 -7681 -3429 N ATOM 1728 N ARG A 305 7.923 21.818 -17.051 1.00149.12 N ANISOU 1728 N ARG A 305 14581 22891 19187 -685 -5435 -2665 N ATOM 1729 CA ARG A 305 7.466 22.542 -18.239 1.00147.00 C ANISOU 1729 CA ARG A 305 14300 22438 19115 -966 -4992 -2688 C ATOM 1730 C ARG A 305 6.219 21.871 -18.812 1.00144.66 C ANISOU 1730 C ARG A 305 14449 21811 18706 -750 -4630 -2540 C ATOM 1731 O ARG A 305 5.331 22.542 -19.330 1.00142.27 O ANISOU 1731 O ARG A 305 14409 21248 18401 -980 -4333 -2556 O ATOM 1732 CB ARG A 305 8.559 22.643 -19.314 1.00166.65 C ANISOU 1732 CB ARG A 305 16153 25187 21979 -1037 -4855 -2707 C ATOM 1733 CG ARG A 305 9.829 23.369 -18.877 1.00169.67 C ANISOU 1733 CG ARG A 305 16020 25922 22526 -1307 -5183 -2860 C ATOM 1734 CD ARG A 305 11.009 23.089 -19.816 1.00172.18 C ANISOU 1734 CD ARG A 305 15651 26570 23200 -1245 -5075 -2850 C ATOM 1735 NE ARG A 305 12.112 24.021 -19.583 1.00176.91 N ANISOU 1735 NE ARG A 305 15744 27477 23997 -1629 -5307 -3009 N ATOM 1736 CZ ARG A 305 13.143 24.205 -20.405 1.00180.13 C ANISOU 1736 CZ ARG A 305 15522 28180 24741 -1759 -5177 -3045 C ATOM 1737 NH1 ARG A 305 13.230 23.527 -21.542 1.00178.84 N ANISOU 1737 NH1 ARG A 305 15165 28044 24742 -1518 -4804 -2940 N ATOM 1738 NH2 ARG A 305 14.090 25.080 -20.089 1.00184.73 N ANISOU 1738 NH2 ARG A 305 15691 29013 25484 -2145 -5400 -3177 N ATOM 1739 N GLY A 306 6.154 20.546 -18.713 1.00120.59 N ANISOU 1739 N GLY A 306 11485 18766 15567 -310 -4670 -2396 N ATOM 1740 CA GLY A 306 5.002 19.803 -19.196 1.00119.14 C ANISOU 1740 CA GLY A 306 11719 18277 15270 -107 -4360 -2257 C ATOM 1741 C GLY A 306 3.750 20.174 -18.422 1.00116.94 C ANISOU 1741 C GLY A 306 12014 17726 14693 -235 -4343 -2266 C ATOM 1742 O GLY A 306 2.667 20.294 -18.994 1.00115.08 O ANISOU 1742 O GLY A 306 12075 17221 14427 -307 -4017 -2224 O ATOM 1743 N VAL A 307 3.913 20.382 -17.119 1.00129.18 N ANISOU 1743 N VAL A 307 13704 19361 16017 -268 -4697 -2329 N ATOM 1744 CA VAL A 307 2.817 20.766 -16.238 1.00127.48 C ANISOU 1744 CA VAL A 307 14019 18926 15492 -387 -4698 -2362 C ATOM 1745 C VAL A 307 2.321 22.173 -16.546 1.00125.09 C ANISOU 1745 C VAL A 307 13787 18475 15267 -799 -4505 -2514 C ATOM 1746 O VAL A 307 1.114 22.416 -16.630 1.00123.42 O ANISOU 1746 O VAL A 307 13959 17992 14943 -866 -4253 -2502 O ATOM 1747 CB VAL A 307 3.229 20.686 -14.750 1.00117.75 C ANISOU 1747 CB VAL A 307 12915 17852 13973 -333 -5145 -2409 C ATOM 1748 CG1 VAL A 307 2.182 21.339 -13.862 1.00116.07 C ANISOU 1748 CG1 VAL A 307 13213 17439 13448 -526 -5118 -2497 C ATOM 1749 CG2 VAL A 307 3.468 19.245 -14.337 1.00120.02 C ANISOU 1749 CG2 VAL A 307 13272 18207 14122 105 -5328 -2223 C ATOM 1750 N LEU A 308 3.262 23.095 -16.724 1.00104.74 N ANISOU 1750 N LEU A 308 10829 16073 12895 -1074 -4627 -2655 N ATOM 1751 CA LEU A 308 2.933 24.495 -16.955 1.00103.16 C ANISOU 1751 CA LEU A 308 10696 15721 12780 -1482 -4488 -2805 C ATOM 1752 C LEU A 308 2.266 24.708 -18.313 1.00100.62 C ANISOU 1752 C LEU A 308 10392 15181 12658 -1551 -4048 -2728 C ATOM 1753 O LEU A 308 1.309 25.474 -18.425 1.00 98.66 O ANISOU 1753 O LEU A 308 10453 14668 12366 -1730 -3851 -2775 O ATOM 1754 CB LEU A 308 4.194 25.353 -16.848 1.00127.69 C ANISOU 1754 CB LEU A 308 13368 19075 16075 -1779 -4734 -2962 C ATOM 1755 CG LEU A 308 4.721 25.567 -15.426 1.00130.01 C ANISOU 1755 CG LEU A 308 13710 19543 16145 -1839 -5193 -3098 C ATOM 1756 CD1 LEU A 308 5.980 26.417 -15.439 1.00132.97 C ANISOU 1756 CD1 LEU A 308 13608 20171 16745 -2169 -5428 -3256 C ATOM 1757 CD2 LEU A 308 3.655 26.189 -14.541 1.00128.65 C ANISOU 1757 CD2 LEU A 308 14103 19110 15669 -1968 -5185 -3206 C ATOM 1758 N VAL A 309 2.768 24.027 -19.341 1.00113.50 N ANISOU 1758 N VAL A 309 11698 16928 14499 -1393 -3899 -2613 N ATOM 1759 CA VAL A 309 2.153 24.080 -20.667 1.00111.94 C ANISOU 1759 CA VAL A 309 11534 16545 14454 -1426 -3495 -2523 C ATOM 1760 C VAL A 309 0.756 23.476 -20.674 1.00110.17 C ANISOU 1760 C VAL A 309 11774 16048 14036 -1229 -3297 -2414 C ATOM 1761 O VAL A 309 -0.189 24.105 -21.146 1.00107.73 O ANISOU 1761 O VAL A 309 11697 15497 13737 -1382 -3058 -2415 O ATOM 1762 CB VAL A 309 3.010 23.346 -21.724 1.00119.69 C ANISOU 1762 CB VAL A 309 12088 17726 15663 -1262 -3374 -2433 C ATOM 1763 CG1 VAL A 309 2.300 23.295 -23.072 1.00118.22 C ANISOU 1763 CG1 VAL A 309 11998 17345 15575 -1275 -2966 -2335 C ATOM 1764 CG2 VAL A 309 4.392 23.979 -21.833 1.00121.52 C ANISOU 1764 CG2 VAL A 309 11799 18252 16122 -1487 -3524 -2539 C ATOM 1765 N LEU A 310 0.621 22.267 -20.138 1.00123.14 N ANISOU 1765 N LEU A 310 13551 17728 15509 -895 -3406 -2316 N ATOM 1766 CA LEU A 310 -0.671 21.589 -20.125 1.00121.91 C ANISOU 1766 CA LEU A 310 13816 17330 15174 -721 -3219 -2205 C ATOM 1767 C LEU A 310 -1.706 22.382 -19.344 1.00120.14 C ANISOU 1767 C LEU A 310 13980 16912 14756 -896 -3201 -2289 C ATOM 1768 O LEU A 310 -2.858 22.485 -19.765 1.00118.65 O ANISOU 1768 O LEU A 310 14045 16496 14541 -922 -2941 -2246 O ATOM 1769 CB LEU A 310 -0.530 20.188 -19.533 1.00111.97 C ANISOU 1769 CB LEU A 310 12654 16138 13751 -359 -3377 -2086 C ATOM 1770 CG LEU A 310 -1.711 19.241 -19.753 1.00111.32 C ANISOU 1770 CG LEU A 310 12939 15822 13534 -167 -3157 -1943 C ATOM 1771 CD1 LEU A 310 -2.014 19.042 -21.230 1.00110.16 C ANISOU 1771 CD1 LEU A 310 12690 15573 13593 -162 -2830 -1881 C ATOM 1772 CD2 LEU A 310 -1.404 17.905 -19.091 1.00113.95 C ANISOU 1772 CD2 LEU A 310 13371 16213 13711 175 -3352 -1823 C ATOM 1773 N ARG A 311 -1.298 22.932 -18.206 1.00123.88 N ANISOU 1773 N ARG A 311 14493 17484 15091 -1008 -3482 -2417 N ATOM 1774 CA ARG A 311 -2.185 23.771 -17.413 1.00122.81 C ANISOU 1774 CA ARG A 311 14719 17176 14766 -1178 -3465 -2533 C ATOM 1775 C ARG A 311 -2.644 24.978 -18.224 1.00120.63 C ANISOU 1775 C ARG A 311 14436 16712 14686 -1451 -3226 -2614 C ATOM 1776 O ARG A 311 -3.823 25.331 -18.217 1.00119.46 O ANISOU 1776 O ARG A 311 14595 16334 14462 -1483 -3023 -2624 O ATOM 1777 CB ARG A 311 -1.494 24.235 -16.136 1.00138.29 C ANISOU 1777 CB ARG A 311 16694 19295 16554 -1282 -3827 -2685 C ATOM 1778 CG ARG A 311 -2.385 25.065 -15.232 1.00137.82 C ANISOU 1778 CG ARG A 311 17037 19061 16265 -1436 -3807 -2831 C ATOM 1779 CD ARG A 311 -1.576 25.709 -14.129 1.00139.73 C ANISOU 1779 CD ARG A 311 17262 19461 16367 -1602 -4171 -3018 C ATOM 1780 NE ARG A 311 -0.834 24.714 -13.362 1.00142.91 N ANISOU 1780 NE ARG A 311 17598 20113 16588 -1382 -4496 -2940 N ATOM 1781 CZ ARG A 311 0.061 25.009 -12.426 1.00145.74 C ANISOU 1781 CZ ARG A 311 17876 20680 16818 -1474 -4884 -3068 C ATOM 1782 NH1 ARG A 311 0.333 26.275 -12.142 1.00145.97 N ANISOU 1782 NH1 ARG A 311 17888 20689 16885 -1807 -4986 -3295 N ATOM 1783 NH2 ARG A 311 0.688 24.037 -11.777 1.00148.12 N ANISOU 1783 NH2 ARG A 311 18125 21201 16954 -1235 -5187 -2967 N ATOM 1784 N ALA A 312 -1.703 25.602 -18.928 1.00 96.17 N ANISOU 1784 N ALA A 312 10981 13715 11844 -1644 -3249 -2662 N ATOM 1785 CA ALA A 312 -1.995 26.783 -19.733 1.00 94.53 C ANISOU 1785 CA ALA A 312 10764 13323 11830 -1922 -3045 -2720 C ATOM 1786 C ALA A 312 -2.928 26.454 -20.892 1.00 92.74 C ANISOU 1786 C ALA A 312 10631 12914 11692 -1820 -2705 -2569 C ATOM 1787 O ALA A 312 -3.785 27.258 -21.254 1.00 91.68 O ANISOU 1787 O ALA A 312 10692 12542 11600 -1950 -2522 -2591 O ATOM 1788 CB ALA A 312 -0.709 27.404 -20.248 1.00 86.46 C ANISOU 1788 CB ALA A 312 9325 12471 11054 -2163 -3136 -2780 C ATOM 1789 N VAL A 313 -2.747 25.276 -21.480 1.00 98.47 N ANISOU 1789 N VAL A 313 11219 13749 12446 -1582 -2634 -2421 N ATOM 1790 CA VAL A 313 -3.595 24.832 -22.580 1.00 96.81 C ANISOU 1790 CA VAL A 313 11099 13388 12296 -1479 -2338 -2282 C ATOM 1791 C VAL A 313 -5.036 24.618 -22.118 1.00 95.67 C ANISOU 1791 C VAL A 313 11354 13033 11963 -1373 -2231 -2253 C ATOM 1792 O VAL A 313 -5.981 25.021 -22.800 1.00 93.22 O ANISOU 1792 O VAL A 313 11182 12528 11710 -1431 -2012 -2216 O ATOM 1793 CB VAL A 313 -3.056 23.533 -23.220 1.00 96.88 C ANISOU 1793 CB VAL A 313 10903 13552 12354 -1231 -2300 -2154 C ATOM 1794 CG1 VAL A 313 -4.041 22.985 -24.242 1.00 95.77 C ANISOU 1794 CG1 VAL A 313 10919 13244 12227 -1124 -2019 -2026 C ATOM 1795 CG2 VAL A 313 -1.701 23.779 -23.865 1.00 98.69 C ANISOU 1795 CG2 VAL A 313 10696 13999 12801 -1337 -2337 -2181 C ATOM 1796 N VAL A 314 -5.198 23.996 -20.953 1.00 93.82 N ANISOU 1796 N VAL A 314 11298 12849 11500 -1222 -2387 -2267 N ATOM 1797 CA VAL A 314 -6.525 23.728 -20.404 1.00 92.78 C ANISOU 1797 CA VAL A 314 11529 12551 11171 -1130 -2275 -2242 C ATOM 1798 C VAL A 314 -7.308 25.003 -20.100 1.00 91.51 C ANISOU 1798 C VAL A 314 11560 12209 11000 -1320 -2192 -2374 C ATOM 1799 O VAL A 314 -8.461 25.140 -20.513 1.00 90.35 O ANISOU 1799 O VAL A 314 11574 11884 10870 -1305 -1972 -2333 O ATOM 1800 CB VAL A 314 -6.447 22.870 -19.123 1.00101.09 C ANISOU 1800 CB VAL A 314 12756 13704 11949 -957 -2467 -2228 C ATOM 1801 CG1 VAL A 314 -7.819 22.758 -18.471 1.00100.69 C ANISOU 1801 CG1 VAL A 314 13077 13496 11686 -916 -2325 -2222 C ATOM 1802 CG2 VAL A 314 -5.897 21.492 -19.441 1.00102.41 C ANISOU 1802 CG2 VAL A 314 12802 13988 12123 -715 -2521 -2075 C ATOM 1803 N ILE A 315 -6.682 25.936 -19.388 1.00111.37 N ANISOU 1803 N ILE A 315 14053 14767 13496 -1493 -2377 -2539 N ATOM 1804 CA ILE A 315 -7.340 27.196 -19.050 1.00111.22 C ANISOU 1804 CA ILE A 315 14236 14553 13472 -1665 -2311 -2691 C ATOM 1805 C ILE A 315 -7.654 28.013 -20.304 1.00109.74 C ANISOU 1805 C ILE A 315 13966 14185 13546 -1800 -2108 -2657 C ATOM 1806 O ILE A 315 -8.704 28.647 -20.392 1.00108.53 O ANISOU 1806 O ILE A 315 14015 13815 13406 -1818 -1945 -2692 O ATOM 1807 CB ILE A 315 -6.520 28.046 -18.046 1.00114.24 C ANISOU 1807 CB ILE A 315 14626 15004 13777 -1850 -2571 -2895 C ATOM 1808 CG1 ILE A 315 -5.154 28.418 -18.624 1.00115.44 C ANISOU 1808 CG1 ILE A 315 14412 15298 14151 -2031 -2717 -2913 C ATOM 1809 CG2 ILE A 315 -6.356 27.302 -16.729 1.00116.00 C ANISOU 1809 CG2 ILE A 315 14997 15389 13690 -1712 -2779 -2926 C ATOM 1810 CD1 ILE A 315 -4.903 29.910 -18.672 1.00116.29 C ANISOU 1810 CD1 ILE A 315 14529 15258 14397 -2343 -2744 -3082 C ATOM 1811 N ALA A 316 -6.741 27.992 -21.270 1.00111.57 N ANISOU 1811 N ALA A 316 13900 14513 13978 -1884 -2116 -2584 N ATOM 1812 CA ALA A 316 -6.929 28.724 -22.515 1.00110.75 C ANISOU 1812 CA ALA A 316 13726 14254 14099 -2024 -1933 -2525 C ATOM 1813 C ALA A 316 -8.056 28.112 -23.339 1.00109.25 C ANISOU 1813 C ALA A 316 13641 13954 13916 -1851 -1701 -2369 C ATOM 1814 O ALA A 316 -8.764 28.816 -24.057 1.00108.28 O ANISOU 1814 O ALA A 316 13607 13632 13903 -1920 -1546 -2336 O ATOM 1815 CB ALA A 316 -5.640 28.757 -23.312 1.00 76.36 C ANISOU 1815 CB ALA A 316 9022 10064 9927 -2159 -1977 -2482 C ATOM 1816 N PHE A 317 -8.214 26.797 -23.234 1.00108.45 N ANISOU 1816 N PHE A 317 13536 13975 13695 -1631 -1693 -2270 N ATOM 1817 CA PHE A 317 -9.287 26.099 -23.930 1.00106.97 C ANISOU 1817 CA PHE A 317 13452 13698 13496 -1481 -1496 -2134 C ATOM 1818 C PHE A 317 -10.628 26.504 -23.331 1.00106.18 C ANISOU 1818 C PHE A 317 13623 13420 13299 -1447 -1406 -2188 C ATOM 1819 O PHE A 317 -11.584 26.786 -24.053 1.00105.01 O ANISOU 1819 O PHE A 317 13543 13121 13234 -1440 -1242 -2128 O ATOM 1820 CB PHE A 317 -9.096 24.583 -23.831 1.00 93.81 C ANISOU 1820 CB PHE A 317 11750 12178 11716 -1268 -1525 -2032 C ATOM 1821 CG PHE A 317 -10.062 23.791 -24.671 1.00 92.78 C ANISOU 1821 CG PHE A 317 11701 11963 11588 -1148 -1335 -1896 C ATOM 1822 CD1 PHE A 317 -11.298 23.419 -24.169 1.00 92.13 C ANISOU 1822 CD1 PHE A 317 11849 11782 11375 -1060 -1251 -1875 C ATOM 1823 CD2 PHE A 317 -9.729 23.414 -25.962 1.00 92.30 C ANISOU 1823 CD2 PHE A 317 11484 11932 11652 -1138 -1237 -1797 C ATOM 1824 CE1 PHE A 317 -12.185 22.689 -24.938 1.00 90.92 C ANISOU 1824 CE1 PHE A 317 11754 11560 11233 -980 -1095 -1759 C ATOM 1825 CE2 PHE A 317 -10.613 22.685 -26.736 1.00 91.23 C ANISOU 1825 CE2 PHE A 317 11439 11719 11504 -1046 -1085 -1688 C ATOM 1826 CZ PHE A 317 -11.842 22.322 -26.223 1.00 90.33 C ANISOU 1826 CZ PHE A 317 11540 11505 11276 -974 -1026 -1668 C ATOM 1827 N VAL A 318 -10.687 26.527 -22.003 1.00 96.53 N ANISOU 1827 N VAL A 318 12550 12232 11895 -1419 -1516 -2303 N ATOM 1828 CA VAL A 318 -11.906 26.875 -21.284 1.00 96.67 C ANISOU 1828 CA VAL A 318 12820 12114 11796 -1375 -1413 -2378 C ATOM 1829 C VAL A 318 -12.357 28.305 -21.580 1.00 96.48 C ANISOU 1829 C VAL A 318 12858 11879 11923 -1503 -1336 -2478 C ATOM 1830 O VAL A 318 -13.513 28.537 -21.935 1.00 96.58 O ANISOU 1830 O VAL A 318 12963 11745 11989 -1439 -1165 -2447 O ATOM 1831 CB VAL A 318 -11.724 26.699 -19.761 1.00 91.76 C ANISOU 1831 CB VAL A 318 12363 11586 10916 -1342 -1554 -2499 C ATOM 1832 CG1 VAL A 318 -12.892 27.313 -19.002 1.00 92.17 C ANISOU 1832 CG1 VAL A 318 12666 11497 10856 -1325 -1425 -2621 C ATOM 1833 CG2 VAL A 318 -11.566 25.226 -19.414 1.00 92.64 C ANISOU 1833 CG2 VAL A 318 12486 11856 10855 -1177 -1607 -2372 C ATOM 1834 N VAL A 319 -11.437 29.254 -21.435 1.00 91.49 N ANISOU 1834 N VAL A 319 12170 11224 11369 -1683 -1471 -2596 N ATOM 1835 CA VAL A 319 -11.742 30.670 -21.632 1.00 91.82 C ANISOU 1835 CA VAL A 319 12308 11027 11552 -1819 -1422 -2701 C ATOM 1836 C VAL A 319 -12.187 30.988 -23.061 1.00 91.19 C ANISOU 1836 C VAL A 319 12155 10803 11691 -1835 -1270 -2551 C ATOM 1837 O VAL A 319 -13.132 31.749 -23.272 1.00 91.57 O ANISOU 1837 O VAL A 319 12342 10631 11819 -1806 -1156 -2573 O ATOM 1838 CB VAL A 319 -10.537 31.563 -21.252 1.00 88.95 C ANISOU 1838 CB VAL A 319 11890 10668 11238 -2055 -1613 -2849 C ATOM 1839 CG1 VAL A 319 -10.818 33.022 -21.582 1.00 89.55 C ANISOU 1839 CG1 VAL A 319 12090 10451 11484 -2210 -1555 -2939 C ATOM 1840 CG2 VAL A 319 -10.207 31.407 -19.776 1.00 90.26 C ANISOU 1840 CG2 VAL A 319 12176 10957 11162 -2047 -1787 -3020 C ATOM 1841 N CYS A 320 -11.515 30.387 -24.037 1.00111.94 N ANISOU 1841 N CYS A 320 14571 13560 14403 -1863 -1270 -2399 N ATOM 1842 CA CYS A 320 -11.798 30.659 -25.444 1.00111.56 C ANISOU 1842 CA CYS A 320 14462 13401 14526 -1900 -1141 -2248 C ATOM 1843 C CYS A 320 -13.116 30.058 -25.929 1.00110.54 C ANISOU 1843 C CYS A 320 14408 13220 14372 -1708 -992 -2131 C ATOM 1844 O CYS A 320 -13.832 30.673 -26.719 1.00110.91 O ANISOU 1844 O CYS A 320 14513 13092 14538 -1710 -900 -2061 O ATOM 1845 CB CYS A 320 -10.649 30.164 -26.327 1.00 97.68 C ANISOU 1845 CB CYS A 320 12456 11818 12839 -1988 -1164 -2139 C ATOM 1846 SG CYS A 320 -9.135 31.142 -26.203 1.00 98.59 S ANISOU 1846 SG CYS A 320 12418 11972 13072 -2286 -1303 -2244 S ATOM 1847 N TRP A 321 -13.431 28.856 -25.458 1.00105.50 N ANISOU 1847 N TRP A 321 13771 12732 13584 -1551 -981 -2102 N ATOM 1848 CA TRP A 321 -14.585 28.124 -25.971 1.00104.80 C ANISOU 1848 CA TRP A 321 13719 12627 13475 -1404 -849 -1984 C ATOM 1849 C TRP A 321 -15.873 28.354 -25.183 1.00105.37 C ANISOU 1849 C TRP A 321 13951 12600 13484 -1297 -766 -2062 C ATOM 1850 O TRP A 321 -16.954 27.982 -25.637 1.00105.66 O ANISOU 1850 O TRP A 321 13998 12606 13543 -1200 -654 -1977 O ATOM 1851 CB TRP A 321 -14.272 26.628 -26.056 1.00 94.83 C ANISOU 1851 CB TRP A 321 12378 11553 12101 -1307 -858 -1890 C ATOM 1852 CG TRP A 321 -13.300 26.295 -27.144 1.00 94.38 C ANISOU 1852 CG TRP A 321 12148 11585 12128 -1364 -872 -1792 C ATOM 1853 CD1 TRP A 321 -11.956 26.101 -27.013 1.00 95.31 C ANISOU 1853 CD1 TRP A 321 12116 11849 12247 -1417 -978 -1820 C ATOM 1854 CD2 TRP A 321 -13.596 26.124 -28.536 1.00 93.73 C ANISOU 1854 CD2 TRP A 321 12015 11467 12132 -1371 -770 -1657 C ATOM 1855 NE1 TRP A 321 -11.396 25.817 -28.235 1.00 95.49 N ANISOU 1855 NE1 TRP A 321 11991 11932 12358 -1451 -919 -1717 N ATOM 1856 CE2 TRP A 321 -12.382 25.825 -29.186 1.00 94.27 C ANISOU 1856 CE2 TRP A 321 11915 11663 12240 -1430 -792 -1617 C ATOM 1857 CE3 TRP A 321 -14.768 26.193 -29.293 1.00 93.67 C ANISOU 1857 CE3 TRP A 321 12079 11347 12164 -1332 -670 -1571 C ATOM 1858 CZ2 TRP A 321 -12.309 25.596 -30.557 1.00 94.24 C ANISOU 1858 CZ2 TRP A 321 11848 11670 12290 -1456 -696 -1499 C ATOM 1859 CZ3 TRP A 321 -14.693 25.965 -30.653 1.00 93.58 C ANISOU 1859 CZ3 TRP A 321 12010 11345 12203 -1363 -610 -1447 C ATOM 1860 CH2 TRP A 321 -13.472 25.672 -31.271 1.00 93.97 C ANISOU 1860 CH2 TRP A 321 11925 11514 12266 -1427 -613 -1414 C ATOM 1861 N LEU A 322 -15.764 28.969 -24.010 1.00 93.51 N ANISOU 1861 N LEU A 322 12566 11061 11902 -1321 -818 -2233 N ATOM 1862 CA LEU A 322 -16.946 29.235 -23.189 1.00 95.12 C ANISOU 1862 CA LEU A 322 12922 11185 12034 -1214 -710 -2334 C ATOM 1863 C LEU A 322 -17.967 30.203 -23.819 1.00 96.21 C ANISOU 1863 C LEU A 322 13089 11112 12355 -1168 -601 -2329 C ATOM 1864 O LEU A 322 -19.149 29.866 -23.901 1.00 96.63 O ANISOU 1864 O LEU A 322 13140 11163 12413 -1040 -473 -2285 O ATOM 1865 CB LEU A 322 -16.559 29.678 -21.770 1.00 83.22 C ANISOU 1865 CB LEU A 322 11565 9690 10366 -1250 -788 -2538 C ATOM 1866 CG LEU A 322 -17.727 29.907 -20.809 1.00 84.94 C ANISOU 1866 CG LEU A 322 11951 9851 10471 -1134 -647 -2665 C ATOM 1867 CD1 LEU A 322 -18.586 28.655 -20.697 1.00 85.02 C ANISOU 1867 CD1 LEU A 322 11941 9999 10362 -1012 -518 -2548 C ATOM 1868 CD2 LEU A 322 -17.223 30.340 -19.442 1.00 86.00 C ANISOU 1868 CD2 LEU A 322 12261 10006 10409 -1187 -738 -2877 C ATOM 1869 N PRO A 323 -17.525 31.398 -24.270 1.00 98.47 N ANISOU 1869 N PRO A 323 13400 11216 12798 -1274 -657 -2368 N ATOM 1870 CA PRO A 323 -18.507 32.306 -24.879 1.00100.43 C ANISOU 1870 CA PRO A 323 13695 11242 13222 -1199 -572 -2344 C ATOM 1871 C PRO A 323 -19.106 31.719 -26.152 1.00100.26 C ANISOU 1871 C PRO A 323 13545 11260 13288 -1134 -520 -2129 C ATOM 1872 O PRO A 323 -20.249 32.019 -26.500 1.00101.57 O ANISOU 1872 O PRO A 323 13714 11327 13552 -1004 -442 -2092 O ATOM 1873 CB PRO A 323 -17.672 33.545 -25.224 1.00 83.24 C ANISOU 1873 CB PRO A 323 11581 8863 11181 -1366 -665 -2388 C ATOM 1874 CG PRO A 323 -16.485 33.471 -24.332 1.00 82.32 C ANISOU 1874 CG PRO A 323 11479 8858 10940 -1514 -784 -2522 C ATOM 1875 CD PRO A 323 -16.187 32.013 -24.212 1.00 80.90 C ANISOU 1875 CD PRO A 323 11166 8966 10605 -1468 -799 -2434 C ATOM 1876 N TYR A 324 -18.325 30.887 -26.832 1.00 81.91 N ANISOU 1876 N TYR A 324 11106 9089 10928 -1219 -570 -1999 N ATOM 1877 CA TYR A 324 -18.773 30.200 -28.035 1.00 81.21 C ANISOU 1877 CA TYR A 324 10917 9059 10881 -1179 -532 -1810 C ATOM 1878 C TYR A 324 -19.968 29.303 -27.729 1.00 81.48 C ANISOU 1878 C TYR A 324 10926 9190 10843 -1031 -440 -1791 C ATOM 1879 O TYR A 324 -20.987 29.356 -28.418 1.00 82.70 O ANISOU 1879 O TYR A 324 11040 9297 11087 -951 -395 -1705 O ATOM 1880 CB TYR A 324 -17.620 29.381 -28.619 1.00106.05 C ANISOU 1880 CB TYR A 324 13958 12366 13969 -1283 -583 -1718 C ATOM 1881 CG TYR A 324 -18.000 28.468 -29.763 1.00105.46 C ANISOU 1881 CG TYR A 324 13806 12375 13887 -1244 -542 -1551 C ATOM 1882 CD1 TYR A 324 -18.144 28.959 -31.053 1.00106.75 C ANISOU 1882 CD1 TYR A 324 13962 12447 14152 -1291 -538 -1421 C ATOM 1883 CD2 TYR A 324 -18.190 27.108 -29.555 1.00104.45 C ANISOU 1883 CD2 TYR A 324 13643 12407 13636 -1172 -513 -1523 C ATOM 1884 CE1 TYR A 324 -18.484 28.124 -32.101 1.00106.38 C ANISOU 1884 CE1 TYR A 324 13867 12482 14069 -1266 -512 -1284 C ATOM 1885 CE2 TYR A 324 -18.526 26.266 -30.595 1.00103.83 C ANISOU 1885 CE2 TYR A 324 13519 12389 13543 -1152 -482 -1392 C ATOM 1886 CZ TYR A 324 -18.673 26.778 -31.866 1.00104.82 C ANISOU 1886 CZ TYR A 324 13632 12439 13757 -1200 -484 -1282 C ATOM 1887 OH TYR A 324 -19.010 25.941 -32.906 1.00104.80 O ANISOU 1887 OH TYR A 324 13605 12501 13714 -1190 -464 -1167 O ATOM 1888 N HIS A 325 -19.840 28.489 -26.686 1.00 86.02 N ANISOU 1888 N HIS A 325 11525 9905 11255 -1006 -421 -1867 N ATOM 1889 CA HIS A 325 -20.904 27.566 -26.302 1.00 86.89 C ANISOU 1889 CA HIS A 325 11622 10114 11280 -905 -317 -1846 C ATOM 1890 C HIS A 325 -22.111 28.288 -25.711 1.00 89.68 C ANISOU 1890 C HIS A 325 12009 10377 11687 -796 -208 -1949 C ATOM 1891 O HIS A 325 -23.245 27.829 -25.853 1.00 91.33 O ANISOU 1891 O HIS A 325 12146 10636 11920 -718 -110 -1900 O ATOM 1892 CB HIS A 325 -20.380 26.499 -25.338 1.00 97.42 C ANISOU 1892 CB HIS A 325 13007 11602 12404 -915 -328 -1878 C ATOM 1893 CG HIS A 325 -19.455 25.513 -25.983 1.00 95.35 C ANISOU 1893 CG HIS A 325 12685 11444 12100 -963 -407 -1762 C ATOM 1894 ND1 HIS A 325 -19.875 24.623 -26.945 1.00 94.83 N ANISOU 1894 ND1 HIS A 325 12555 11418 12058 -950 -370 -1625 N ATOM 1895 CD2 HIS A 325 -18.134 25.276 -25.798 1.00 94.80 C ANISOU 1895 CD2 HIS A 325 12602 11448 11968 -1014 -519 -1776 C ATOM 1896 CE1 HIS A 325 -18.851 23.881 -27.333 1.00 93.51 C ANISOU 1896 CE1 HIS A 325 12356 11329 11842 -978 -439 -1565 C ATOM 1897 NE2 HIS A 325 -17.785 24.257 -26.652 1.00 93.80 N ANISOU 1897 NE2 HIS A 325 12405 11398 11837 -1008 -529 -1650 N ATOM 1898 N VAL A 326 -21.866 29.410 -25.041 1.00 92.93 N ANISOU 1898 N VAL A 326 12526 10659 12125 -793 -222 -2103 N ATOM 1899 CA VAL A 326 -22.953 30.228 -24.516 1.00 95.87 C ANISOU 1899 CA VAL A 326 12938 10920 12568 -662 -108 -2224 C ATOM 1900 C VAL A 326 -23.792 30.766 -25.673 1.00 97.53 C ANISOU 1900 C VAL A 326 13046 11010 13002 -576 -102 -2112 C ATOM 1901 O VAL A 326 -25.022 30.758 -25.620 1.00 99.99 O ANISOU 1901 O VAL A 326 13274 11337 13382 -438 7 -2119 O ATOM 1902 CB VAL A 326 -22.431 31.404 -23.655 1.00 81.97 C ANISOU 1902 CB VAL A 326 11347 9003 10796 -683 -139 -2428 C ATOM 1903 CG1 VAL A 326 -23.553 32.384 -23.344 1.00 84.83 C ANISOU 1903 CG1 VAL A 326 11752 9202 11278 -516 -16 -2552 C ATOM 1904 CG2 VAL A 326 -21.806 30.888 -22.369 1.00 80.75 C ANISOU 1904 CG2 VAL A 326 11305 8988 10391 -743 -150 -2554 C ATOM 1905 N ARG A 327 -23.113 31.214 -26.726 1.00 90.92 N ANISOU 1905 N ARG A 327 12208 10066 12271 -662 -223 -2002 N ATOM 1906 CA ARG A 327 -23.779 31.772 -27.899 1.00 93.07 C ANISOU 1906 CA ARG A 327 12420 10211 12730 -591 -254 -1870 C ATOM 1907 C ARG A 327 -24.652 30.755 -28.635 1.00 93.46 C ANISOU 1907 C ARG A 327 12307 10423 12782 -541 -231 -1721 C ATOM 1908 O ARG A 327 -25.761 31.077 -29.062 1.00 96.39 O ANISOU 1908 O ARG A 327 12590 10748 13285 -407 -214 -1676 O ATOM 1909 CB ARG A 327 -22.750 32.358 -28.868 1.00 94.79 C ANISOU 1909 CB ARG A 327 12698 10302 13015 -733 -376 -1765 C ATOM 1910 CG ARG A 327 -23.366 32.984 -30.107 1.00 97.10 C ANISOU 1910 CG ARG A 327 12975 10447 13470 -667 -429 -1606 C ATOM 1911 CD ARG A 327 -22.308 33.458 -31.088 1.00 96.27 C ANISOU 1911 CD ARG A 327 12945 10239 13393 -840 -522 -1480 C ATOM 1912 NE ARG A 327 -21.422 32.375 -31.505 1.00 93.63 N ANISOU 1912 NE ARG A 327 12533 10120 12923 -988 -534 -1402 N ATOM 1913 CZ ARG A 327 -21.734 31.462 -32.420 1.00 93.33 C ANISOU 1913 CZ ARG A 327 12403 10227 12832 -981 -541 -1256 C ATOM 1914 NH1 ARG A 327 -22.919 31.492 -33.015 1.00 96.30 N ANISOU 1914 NH1 ARG A 327 12734 10577 13277 -852 -558 -1165 N ATOM 1915 NH2 ARG A 327 -20.862 30.515 -32.737 1.00 91.25 N ANISOU 1915 NH2 ARG A 327 12088 10135 12448 -1097 -538 -1212 N ATOM 1916 N ARG A 328 -24.154 29.531 -28.784 1.00 92.42 N ANISOU 1916 N ARG A 328 12133 10473 12508 -647 -241 -1650 N ATOM 1917 CA ARG A 328 -24.912 28.488 -29.470 1.00 92.50 C ANISOU 1917 CA ARG A 328 12016 10625 12504 -636 -227 -1524 C ATOM 1918 C ARG A 328 -26.149 28.084 -28.676 1.00 95.34 C ANISOU 1918 C ARG A 328 12287 11081 12857 -535 -97 -1596 C ATOM 1919 O ARG A 328 -27.202 27.807 -29.250 1.00 97.63 O ANISOU 1919 O ARG A 328 12436 11427 13232 -482 -87 -1519 O ATOM 1920 CB ARG A 328 -24.034 27.269 -29.759 1.00120.15 C ANISOU 1920 CB ARG A 328 15529 14266 15857 -762 -260 -1451 C ATOM 1921 CG ARG A 328 -22.945 27.533 -30.783 1.00118.53 C ANISOU 1921 CG ARG A 328 15360 14009 15668 -863 -360 -1358 C ATOM 1922 CD ARG A 328 -21.955 26.386 -30.851 1.00115.76 C ANISOU 1922 CD ARG A 328 15015 13793 15173 -951 -372 -1329 C ATOM 1923 NE ARG A 328 -22.519 25.207 -31.503 1.00114.68 N ANISOU 1923 NE ARG A 328 14832 13761 14982 -953 -357 -1234 N ATOM 1924 CZ ARG A 328 -22.713 24.041 -30.898 1.00114.25 C ANISOU 1924 CZ ARG A 328 14785 13810 14814 -948 -305 -1255 C ATOM 1925 NH1 ARG A 328 -22.386 23.893 -29.621 1.00113.92 N ANISOU 1925 NH1 ARG A 328 14799 13799 14685 -927 -266 -1355 N ATOM 1926 NH2 ARG A 328 -23.230 23.020 -31.567 1.00113.96 N ANISOU 1926 NH2 ARG A 328 14725 13837 14739 -975 -299 -1174 N ATOM 1927 N LEU A 329 -26.015 28.049 -27.355 1.00 85.02 N ANISOU 1927 N LEU A 329 11057 9806 11439 -521 3 -1744 N ATOM 1928 CA LEU A 329 -27.157 27.797 -26.487 1.00 87.95 C ANISOU 1928 CA LEU A 329 11356 10269 11791 -433 167 -1830 C ATOM 1929 C LEU A 329 -28.108 28.985 -26.544 1.00 91.83 C ANISOU 1929 C LEU A 329 11771 10639 12482 -260 212 -1899 C ATOM 1930 O LEU A 329 -29.325 28.818 -26.525 1.00 95.84 O ANISOU 1930 O LEU A 329 12108 11232 13075 -166 312 -1898 O ATOM 1931 CB LEU A 329 -26.703 27.544 -25.048 1.00 82.69 C ANISOU 1931 CB LEU A 329 10836 9662 10921 -463 262 -1971 C ATOM 1932 CG LEU A 329 -25.958 26.230 -24.796 1.00 79.88 C ANISOU 1932 CG LEU A 329 10553 9439 10359 -592 233 -1901 C ATOM 1933 CD1 LEU A 329 -25.485 26.149 -23.355 1.00 79.37 C ANISOU 1933 CD1 LEU A 329 10659 9419 10079 -605 293 -2036 C ATOM 1934 CD2 LEU A 329 -26.849 25.045 -25.134 1.00 80.50 C ANISOU 1934 CD2 LEU A 329 10516 9650 10422 -630 311 -1786 C ATOM 1935 N MET A 330 -27.540 30.184 -26.619 1.00100.27 N ANISOU 1935 N MET A 330 12961 11503 13635 -218 136 -1959 N ATOM 1936 CA MET A 330 -28.327 31.406 -26.742 1.00103.84 C ANISOU 1936 CA MET A 330 13381 11782 14293 -30 155 -2019 C ATOM 1937 C MET A 330 -29.139 31.387 -28.033 1.00106.38 C ANISOU 1937 C MET A 330 13522 12109 14788 44 63 -1840 C ATOM 1938 O MET A 330 -30.260 31.892 -28.083 1.00109.45 O ANISOU 1938 O MET A 330 13773 12470 15343 235 110 -1865 O ATOM 1939 CB MET A 330 -27.407 32.629 -26.721 1.00116.24 C ANISOU 1939 CB MET A 330 15158 13093 15915 -46 63 -2089 C ATOM 1940 CG MET A 330 -28.115 33.948 -26.969 1.00119.53 C ANISOU 1940 CG MET A 330 15590 13268 16558 159 56 -2131 C ATOM 1941 SD MET A 330 -26.978 35.337 -27.130 1.00118.79 S ANISOU 1941 SD MET A 330 15772 12829 16535 82 -71 -2178 S ATOM 1942 CE MET A 330 -28.126 36.670 -27.472 1.00122.51 C ANISOU 1942 CE MET A 330 16245 13017 17285 384 -67 -2197 C ATOM 1943 N PHE A 331 -28.561 30.788 -29.070 1.00107.20 N ANISOU 1943 N PHE A 331 13625 12261 14846 -102 -72 -1666 N ATOM 1944 CA PHE A 331 -29.188 30.712 -30.385 1.00109.34 C ANISOU 1944 CA PHE A 331 13764 12546 15233 -67 -195 -1487 C ATOM 1945 C PHE A 331 -30.501 29.935 -30.358 1.00112.82 C ANISOU 1945 C PHE A 331 13960 13191 15717 -4 -125 -1470 C ATOM 1946 O PHE A 331 -31.470 30.318 -31.013 1.00117.05 O ANISOU 1946 O PHE A 331 14337 13718 16420 132 -195 -1399 O ATOM 1947 CB PHE A 331 -28.224 30.074 -31.392 1.00 88.42 C ANISOU 1947 CB PHE A 331 11188 9937 12472 -257 -319 -1333 C ATOM 1948 CG PHE A 331 -28.823 29.851 -32.756 1.00 90.27 C ANISOU 1948 CG PHE A 331 11318 10212 12767 -250 -452 -1151 C ATOM 1949 CD1 PHE A 331 -28.834 30.867 -33.697 1.00 92.97 C ANISOU 1949 CD1 PHE A 331 11723 10377 13223 -183 -588 -1037 C ATOM 1950 CD2 PHE A 331 -29.363 28.621 -33.101 1.00 89.45 C ANISOU 1950 CD2 PHE A 331 11079 10316 12593 -325 -453 -1092 C ATOM 1951 CE1 PHE A 331 -29.380 30.664 -34.952 1.00 95.34 C ANISOU 1951 CE1 PHE A 331 11950 10727 13548 -177 -734 -864 C ATOM 1952 CE2 PHE A 331 -29.911 28.414 -34.353 1.00 90.80 C ANISOU 1952 CE2 PHE A 331 11168 10534 12800 -333 -598 -939 C ATOM 1953 CZ PHE A 331 -29.919 29.436 -35.280 1.00 93.98 C ANISOU 1953 CZ PHE A 331 11631 10780 13297 -254 -744 -824 C ATOM 1954 N CYS A 332 -30.530 28.843 -29.602 1.00118.30 N ANISOU 1954 N CYS A 332 14621 14068 16262 -109 4 -1528 N ATOM 1955 CA CYS A 332 -31.672 27.935 -29.630 1.00121.54 C ANISOU 1955 CA CYS A 332 14803 14683 16694 -122 74 -1496 C ATOM 1956 C CYS A 332 -32.569 28.007 -28.395 1.00124.90 C ANISOU 1956 C CYS A 332 15111 15200 17144 -18 299 -1653 C ATOM 1957 O CYS A 332 -33.715 27.560 -28.434 1.00125.55 O ANISOU 1957 O CYS A 332 14948 15443 17311 4 371 -1639 O ATOM 1958 CB CYS A 332 -31.207 26.493 -29.860 1.00109.91 C ANISOU 1958 CB CYS A 332 13374 13347 15038 -340 59 -1413 C ATOM 1959 SG CYS A 332 -29.897 25.941 -28.743 1.00104.40 S ANISOU 1959 SG CYS A 332 12927 12644 14096 -460 150 -1501 S ATOM 1960 N TYR A 333 -32.057 28.571 -27.306 1.00112.96 N ANISOU 1960 N TYR A 333 13768 13598 15553 33 415 -1810 N ATOM 1961 CA TYR A 333 -32.829 28.622 -26.066 1.00113.83 C ANISOU 1961 CA TYR A 333 13807 13804 15640 122 660 -1975 C ATOM 1962 C TYR A 333 -33.699 29.868 -25.943 1.00115.07 C ANISOU 1962 C TYR A 333 13840 13859 16022 391 721 -2085 C ATOM 1963 O TYR A 333 -34.692 29.868 -25.217 1.00116.53 O ANISOU 1963 O TYR A 333 13857 14168 16252 498 932 -2198 O ATOM 1964 CB TYR A 333 -31.922 28.459 -24.848 1.00127.60 C ANISOU 1964 CB TYR A 333 15808 15535 17139 36 765 -2103 C ATOM 1965 CG TYR A 333 -31.722 27.013 -24.472 1.00126.79 C ANISOU 1965 CG TYR A 333 15743 15613 16819 -165 830 -2035 C ATOM 1966 CD1 TYR A 333 -32.618 26.363 -23.636 1.00129.02 C ANISOU 1966 CD1 TYR A 333 15925 16074 17022 -193 1060 -2085 C ATOM 1967 CD2 TYR A 333 -30.651 26.289 -24.979 1.00123.14 C ANISOU 1967 CD2 TYR A 333 15418 15136 16236 -325 670 -1914 C ATOM 1968 CE1 TYR A 333 -32.444 25.038 -23.300 1.00128.59 C ANISOU 1968 CE1 TYR A 333 15940 16150 16766 -386 1116 -2005 C ATOM 1969 CE2 TYR A 333 -30.469 24.963 -24.649 1.00121.73 C ANISOU 1969 CE2 TYR A 333 15298 15086 15869 -484 719 -1847 C ATOM 1970 CZ TYR A 333 -31.368 24.343 -23.809 1.00124.79 C ANISOU 1970 CZ TYR A 333 15618 15622 16175 -520 935 -1886 C ATOM 1971 OH TYR A 333 -31.192 23.023 -23.476 1.00124.33 O ANISOU 1971 OH TYR A 333 15656 15659 15927 -687 983 -1803 O ATOM 1972 N ILE A 334 -33.323 30.929 -26.647 1.00103.41 N ANISOU 1972 N ILE A 334 12453 12150 14687 503 549 -2050 N ATOM 1973 CA ILE A 334 -34.169 32.112 -26.723 1.00104.99 C ANISOU 1973 CA ILE A 334 12544 12216 15132 787 567 -2123 C ATOM 1974 C ILE A 334 -35.321 31.832 -27.681 1.00107.73 C ANISOU 1974 C ILE A 334 12555 12702 15674 875 481 -1979 C ATOM 1975 O ILE A 334 -35.100 31.495 -28.845 1.00107.55 O ANISOU 1975 O ILE A 334 12514 12685 15666 772 264 -1785 O ATOM 1976 CB ILE A 334 -33.391 33.349 -27.202 1.00 88.02 C ANISOU 1976 CB ILE A 334 10635 9738 13073 866 397 -2110 C ATOM 1977 CG1 ILE A 334 -32.263 33.683 -26.224 1.00 85.79 C ANISOU 1977 CG1 ILE A 334 10664 9324 12610 762 463 -2273 C ATOM 1978 CG2 ILE A 334 -34.327 34.539 -27.356 1.00 90.09 C ANISOU 1978 CG2 ILE A 334 10795 9830 13606 1191 398 -2165 C ATOM 1979 CD1 ILE A 334 -31.553 34.980 -26.539 1.00 85.41 C ANISOU 1979 CD1 ILE A 334 10857 8932 12662 818 328 -2293 C ATOM 1980 N SER A 335 -36.548 31.965 -27.187 1.00144.96 N ANISOU 1980 N SER A 335 16999 17547 20531 1061 652 -2082 N ATOM 1981 CA SER A 335 -37.729 31.675 -27.992 1.00145.64 C ANISOU 1981 CA SER A 335 16712 17808 20817 1144 571 -1965 C ATOM 1982 C SER A 335 -37.892 32.691 -29.119 1.00146.36 C ANISOU 1982 C SER A 335 16786 17693 21129 1357 307 -1841 C ATOM 1983 O SER A 335 -37.333 33.786 -29.061 1.00147.10 O ANISOU 1983 O SER A 335 17129 17493 21271 1497 257 -1889 O ATOM 1984 CB SER A 335 -38.983 31.647 -27.117 1.00163.17 C ANISOU 1984 CB SER A 335 18614 20230 23152 1303 843 -2122 C ATOM 1985 OG SER A 335 -40.125 31.291 -27.877 1.00164.39 O ANISOU 1985 OG SER A 335 18362 20592 23506 1355 753 -2011 O ATOM 1986 N ASP A 336 -38.658 32.322 -30.141 1.00139.72 N ANISOU 1986 N ASP A 336 15671 17000 20416 1368 128 -1678 N ATOM 1987 CA ASP A 336 -38.865 33.187 -31.299 1.00141.32 C ANISOU 1987 CA ASP A 336 15862 17029 20803 1562 -156 -1523 C ATOM 1988 C ASP A 336 -39.567 34.489 -30.927 1.00142.98 C ANISOU 1988 C ASP A 336 15987 17067 21274 1963 -102 -1637 C ATOM 1989 O ASP A 336 -39.319 35.531 -31.533 1.00144.06 O ANISOU 1989 O ASP A 336 16301 16912 21522 2143 -288 -1554 O ATOM 1990 CB ASP A 336 -39.662 32.458 -32.384 1.00207.88 C ANISOU 1990 CB ASP A 336 23988 25696 29300 1494 -365 -1343 C ATOM 1991 CG ASP A 336 -38.953 31.223 -32.897 1.00206.19 C ANISOU 1991 CG ASP A 336 23899 25607 28836 1118 -443 -1230 C ATOM 1992 OD1 ASP A 336 -37.712 31.160 -32.785 1.00205.27 O ANISOU 1992 OD1 ASP A 336 24132 25339 28524 955 -425 -1227 O ATOM 1993 OD2 ASP A 336 -39.635 30.314 -33.414 1.00204.57 O ANISOU 1993 OD2 ASP A 336 23440 25651 28638 987 -524 -1152 O ATOM 1994 N GLU A 337 -40.445 34.423 -29.932 1.00149.02 N ANISOU 1994 N GLU A 337 16488 18001 22133 2105 166 -1827 N ATOM 1995 CA GLU A 337 -41.187 35.599 -29.492 1.00150.96 C ANISOU 1995 CA GLU A 337 16622 18101 22633 2518 260 -1971 C ATOM 1996 C GLU A 337 -40.329 36.521 -28.628 1.00150.66 C ANISOU 1996 C GLU A 337 16994 17733 22516 2596 403 -2155 C ATOM 1997 O GLU A 337 -40.671 37.685 -28.422 1.00152.38 O ANISOU 1997 O GLU A 337 17254 17709 22934 2940 428 -2260 O ATOM 1998 CB GLU A 337 -42.448 35.186 -28.730 1.00180.06 C ANISOU 1998 CB GLU A 337 19856 22114 26444 2639 529 -2123 C ATOM 1999 CG GLU A 337 -42.183 34.394 -27.461 1.00179.10 C ANISOU 1999 CG GLU A 337 19800 22171 26078 2403 879 -2303 C ATOM 2000 CD GLU A 337 -42.709 32.973 -27.538 1.00178.36 C ANISOU 2000 CD GLU A 337 19399 22468 25901 2111 942 -2222 C ATOM 2001 OE1 GLU A 337 -42.925 32.477 -28.664 1.00177.59 O ANISOU 2001 OE1 GLU A 337 19141 22471 25862 1999 671 -2016 O ATOM 2002 OE2 GLU A 337 -42.907 32.354 -26.472 1.00177.54 O ANISOU 2002 OE2 GLU A 337 19235 22560 25660 1981 1263 -2365 O ATOM 2003 N GLN A 338 -39.214 35.998 -28.127 1.00127.98 N ANISOU 2003 N GLN A 338 14425 14845 19357 2282 483 -2197 N ATOM 2004 CA GLN A 338 -38.315 36.775 -27.279 1.00127.51 C ANISOU 2004 CA GLN A 338 14758 14500 19189 2296 597 -2380 C ATOM 2005 C GLN A 338 -37.277 37.547 -28.088 1.00126.84 C ANISOU 2005 C GLN A 338 15029 14059 19105 2244 333 -2245 C ATOM 2006 O GLN A 338 -36.724 38.540 -27.614 1.00126.89 O ANISOU 2006 O GLN A 338 15339 13750 19122 2332 368 -2381 O ATOM 2007 CB GLN A 338 -37.612 35.873 -26.261 1.00174.32 C ANISOU 2007 CB GLN A 338 20833 20596 24805 1995 800 -2499 C ATOM 2008 CG GLN A 338 -38.531 35.265 -25.215 1.00174.94 C ANISOU 2008 CG GLN A 338 20650 20977 24842 2035 1123 -2668 C ATOM 2009 CD GLN A 338 -37.784 34.388 -24.228 1.00173.44 C ANISOU 2009 CD GLN A 338 20659 20926 24314 1738 1297 -2756 C ATOM 2010 OE1 GLN A 338 -37.403 33.261 -24.545 1.00172.68 O ANISOU 2010 OE1 GLN A 338 20548 21005 24058 1452 1224 -2605 O ATOM 2011 NE2 GLN A 338 -37.553 34.911 -23.030 1.00173.07 N ANISOU 2011 NE2 GLN A 338 20825 20785 24148 1813 1514 -3004 N ATOM 2012 N TRP A 339 -37.014 37.087 -29.307 1.00118.66 N ANISOU 2012 N TRP A 339 13966 13073 18047 2084 80 -1982 N ATOM 2013 CA TRP A 339 -36.015 37.719 -30.163 1.00118.27 C ANISOU 2013 CA TRP A 339 14241 12721 17974 1991 -153 -1825 C ATOM 2014 C TRP A 339 -36.439 39.100 -30.651 1.00120.11 C ANISOU 2014 C TRP A 339 14558 12611 18466 2323 -290 -1781 C ATOM 2015 O TRP A 339 -37.446 39.245 -31.345 1.00121.42 O ANISOU 2015 O TRP A 339 14471 12836 18829 2556 -420 -1658 O ATOM 2016 CB TRP A 339 -35.684 36.829 -31.364 1.00 99.07 C ANISOU 2016 CB TRP A 339 11760 10454 15429 1741 -366 -1562 C ATOM 2017 CG TRP A 339 -34.690 35.751 -31.068 1.00 97.15 C ANISOU 2017 CG TRP A 339 11627 10381 14907 1381 -293 -1574 C ATOM 2018 CD1 TRP A 339 -34.955 34.436 -30.825 1.00 96.79 C ANISOU 2018 CD1 TRP A 339 11379 10668 14730 1213 -198 -1580 C ATOM 2019 CD2 TRP A 339 -33.267 35.894 -30.988 1.00 94.92 C ANISOU 2019 CD2 TRP A 339 11675 9936 14455 1153 -317 -1576 C ATOM 2020 NE1 TRP A 339 -33.787 33.750 -30.598 1.00 94.58 N ANISOU 2020 NE1 TRP A 339 11299 10428 14208 924 -168 -1583 N ATOM 2021 CE2 TRP A 339 -32.733 34.625 -30.692 1.00 93.42 C ANISOU 2021 CE2 TRP A 339 11458 10000 14039 885 -241 -1585 C ATOM 2022 CE3 TRP A 339 -32.390 36.974 -31.137 1.00 94.42 C ANISOU 2022 CE3 TRP A 339 11924 9534 14418 1140 -397 -1571 C ATOM 2023 CZ2 TRP A 339 -31.367 34.403 -30.542 1.00 90.58 C ANISOU 2023 CZ2 TRP A 339 11337 9590 13490 639 -251 -1592 C ATOM 2024 CZ3 TRP A 339 -31.033 36.753 -30.988 1.00 91.66 C ANISOU 2024 CZ3 TRP A 339 11800 9147 13879 857 -397 -1582 C ATOM 2025 CH2 TRP A 339 -30.535 35.478 -30.693 1.00 89.52 C ANISOU 2025 CH2 TRP A 339 11462 9157 13394 625 -328 -1594 C ATOM 2026 N THR A 340 -35.661 40.111 -30.279 1.00127.59 N ANISOU 2026 N THR A 340 15870 13194 19417 2340 -273 -1880 N ATOM 2027 CA THR A 340 -35.875 41.464 -30.770 1.00128.81 C ANISOU 2027 CA THR A 340 16198 12946 19800 2622 -416 -1821 C ATOM 2028 C THR A 340 -34.765 41.800 -31.757 1.00127.97 C ANISOU 2028 C THR A 340 16421 12598 19604 2380 -639 -1594 C ATOM 2029 O THR A 340 -33.847 41.005 -31.956 1.00126.14 O ANISOU 2029 O THR A 340 16256 12526 19146 2022 -655 -1520 O ATOM 2030 CB THR A 340 -35.867 42.492 -29.625 1.00131.05 C ANISOU 2030 CB THR A 340 16689 12934 20172 2828 -223 -2117 C ATOM 2031 OG1 THR A 340 -34.614 42.431 -28.932 1.00129.34 O ANISOU 2031 OG1 THR A 340 16781 12634 19727 2509 -133 -2253 O ATOM 2032 CG2 THR A 340 -36.995 42.209 -28.645 1.00132.01 C ANISOU 2032 CG2 THR A 340 16482 13302 20373 3083 35 -2351 C ATOM 2033 N THR A 341 -34.845 42.976 -32.371 1.00137.56 N ANISOU 2033 N THR A 341 17846 13423 20998 2580 -802 -1479 N ATOM 2034 CA THR A 341 -33.825 43.394 -33.325 1.00137.09 C ANISOU 2034 CA THR A 341 18118 13111 20857 2346 -994 -1250 C ATOM 2035 C THR A 341 -32.549 43.776 -32.579 1.00135.03 C ANISOU 2035 C THR A 341 18199 12637 20470 2073 -874 -1419 C ATOM 2036 O THR A 341 -31.456 43.772 -33.146 1.00133.84 O ANISOU 2036 O THR A 341 18268 12402 20183 1754 -962 -1276 O ATOM 2037 CB THR A 341 -34.314 44.571 -34.195 1.00208.29 C ANISOU 2037 CB THR A 341 27296 21746 30099 2640 -1208 -1056 C ATOM 2038 OG1 THR A 341 -35.595 44.253 -34.752 1.00209.07 O ANISOU 2038 OG1 THR A 341 27033 22066 30337 2935 -1330 -934 O ATOM 2039 CG2 THR A 341 -33.337 44.852 -35.330 1.00207.57 C ANISOU 2039 CG2 THR A 341 27523 21455 29891 2363 -1403 -769 C ATOM 2040 N PHE A 342 -32.690 44.073 -31.291 1.00134.72 N ANISOU 2040 N PHE A 342 18187 12536 20463 2189 -668 -1733 N ATOM 2041 CA PHE A 342 -31.535 44.373 -30.457 1.00133.05 C ANISOU 2041 CA PHE A 342 18273 12164 20117 1928 -564 -1930 C ATOM 2042 C PHE A 342 -30.754 43.096 -30.183 1.00130.56 C ANISOU 2042 C PHE A 342 17836 12242 19529 1566 -497 -1944 C ATOM 2043 O PHE A 342 -29.538 43.048 -30.365 1.00128.84 O ANISOU 2043 O PHE A 342 17810 11971 19173 1232 -552 -1891 O ATOM 2044 CB PHE A 342 -31.960 45.026 -29.140 1.00120.75 C ANISOU 2044 CB PHE A 342 16795 10444 18642 2165 -364 -2279 C ATOM 2045 CG PHE A 342 -30.836 45.186 -28.156 1.00118.96 C ANISOU 2045 CG PHE A 342 16839 10121 18238 1882 -263 -2514 C ATOM 2046 CD1 PHE A 342 -29.944 46.240 -28.270 1.00119.03 C ANISOU 2046 CD1 PHE A 342 17240 9695 18289 1734 -356 -2527 C ATOM 2047 CD2 PHE A 342 -30.665 44.278 -27.123 1.00117.30 C ANISOU 2047 CD2 PHE A 342 16499 10256 17812 1748 -89 -2714 C ATOM 2048 CE1 PHE A 342 -28.906 46.388 -27.369 1.00117.60 C ANISOU 2048 CE1 PHE A 342 17288 9445 17949 1454 -291 -2752 C ATOM 2049 CE2 PHE A 342 -29.628 44.419 -26.221 1.00115.45 C ANISOU 2049 CE2 PHE A 342 16511 9953 17403 1492 -32 -2925 C ATOM 2050 CZ PHE A 342 -28.748 45.476 -26.343 1.00115.85 C ANISOU 2050 CZ PHE A 342 16922 9588 17507 1343 -139 -2952 C ATOM 2051 N LEU A 343 -31.466 42.063 -29.741 1.00115.15 N ANISOU 2051 N LEU A 343 15561 10681 17509 1636 -374 -2014 N ATOM 2052 CA LEU A 343 -30.858 40.765 -29.474 1.00112.60 C ANISOU 2052 CA LEU A 343 15118 10727 16936 1335 -312 -2016 C ATOM 2053 C LEU A 343 -30.284 40.176 -30.756 1.00111.38 C ANISOU 2053 C LEU A 343 14941 10681 16699 1101 -492 -1722 C ATOM 2054 O LEU A 343 -29.286 39.457 -30.730 1.00108.95 O ANISOU 2054 O LEU A 343 14672 10529 16194 801 -489 -1699 O ATOM 2055 CB LEU A 343 -31.885 39.807 -28.869 1.00110.46 C ANISOU 2055 CB LEU A 343 14513 10823 16633 1465 -148 -2113 C ATOM 2056 CG LEU A 343 -32.352 40.122 -27.447 1.00111.09 C ANISOU 2056 CG LEU A 343 14603 10891 16715 1641 92 -2430 C ATOM 2057 CD1 LEU A 343 -33.420 39.133 -27.005 1.00112.30 C ANISOU 2057 CD1 LEU A 343 14399 11427 16842 1742 262 -2481 C ATOM 2058 CD2 LEU A 343 -31.178 40.124 -26.478 1.00108.69 C ANISOU 2058 CD2 LEU A 343 14568 10539 16191 1391 166 -2618 C ATOM 2059 N PHE A 344 -30.925 40.494 -31.877 1.00113.31 N ANISOU 2059 N PHE A 344 15123 10842 17086 1257 -652 -1500 N ATOM 2060 CA PHE A 344 -30.467 40.050 -33.186 1.00113.27 C ANISOU 2060 CA PHE A 344 15130 10915 16992 1060 -827 -1216 C ATOM 2061 C PHE A 344 -29.133 40.698 -33.536 1.00112.49 C ANISOU 2061 C PHE A 344 15361 10553 16828 803 -889 -1145 C ATOM 2062 O PHE A 344 -28.189 40.018 -33.941 1.00110.45 O ANISOU 2062 O PHE A 344 15125 10452 16391 506 -905 -1055 O ATOM 2063 CB PHE A 344 -31.511 40.385 -34.254 1.00116.22 C ANISOU 2063 CB PHE A 344 15395 11236 17527 1310 -1006 -1001 C ATOM 2064 CG PHE A 344 -31.151 39.902 -35.632 1.00116.29 C ANISOU 2064 CG PHE A 344 15427 11345 17412 1121 -1186 -713 C ATOM 2065 CD1 PHE A 344 -31.467 38.615 -36.034 1.00116.27 C ANISOU 2065 CD1 PHE A 344 15173 11724 17282 1020 -1207 -642 C ATOM 2066 CD2 PHE A 344 -30.510 40.740 -36.529 1.00116.76 C ANISOU 2066 CD2 PHE A 344 15782 11109 17472 1034 -1327 -515 C ATOM 2067 CE1 PHE A 344 -31.140 38.169 -37.301 1.00116.21 C ANISOU 2067 CE1 PHE A 344 15210 11805 17137 849 -1365 -400 C ATOM 2068 CE2 PHE A 344 -30.181 40.301 -37.797 1.00117.06 C ANISOU 2068 CE2 PHE A 344 15861 11252 17365 857 -1472 -256 C ATOM 2069 CZ PHE A 344 -30.497 39.014 -38.184 1.00116.51 C ANISOU 2069 CZ PHE A 344 15542 11569 17158 773 -1492 -208 C ATOM 2070 N ASP A 345 -29.061 42.016 -33.376 1.00116.47 N ANISOU 2070 N ASP A 345 16118 10650 17484 917 -915 -1192 N ATOM 2071 CA ASP A 345 -27.844 42.754 -33.689 1.00115.48 C ANISOU 2071 CA ASP A 345 16314 10237 17324 655 -968 -1126 C ATOM 2072 C ASP A 345 -26.729 42.438 -32.699 1.00112.35 C ANISOU 2072 C ASP A 345 15977 9933 16779 373 -843 -1343 C ATOM 2073 O ASP A 345 -25.560 42.371 -33.075 1.00110.36 O ANISOU 2073 O ASP A 345 15836 9676 16417 53 -875 -1260 O ATOM 2074 CB ASP A 345 -28.114 44.261 -33.722 1.00144.17 C ANISOU 2074 CB ASP A 345 20232 13374 21174 852 -1029 -1130 C ATOM 2075 CG ASP A 345 -29.087 44.655 -34.817 1.00147.19 C ANISOU 2075 CG ASP A 345 20591 13634 21698 1126 -1199 -872 C ATOM 2076 OD1 ASP A 345 -29.098 43.988 -35.873 1.00147.54 O ANISOU 2076 OD1 ASP A 345 20527 13897 21636 1026 -1311 -625 O ATOM 2077 OD2 ASP A 345 -29.842 45.631 -34.621 1.00148.77 O ANISOU 2077 OD2 ASP A 345 20892 13520 22114 1453 -1229 -922 O ATOM 2078 N PHE A 346 -27.093 42.242 -31.436 1.00119.81 N ANISOU 2078 N PHE A 346 16836 10975 17712 494 -702 -1618 N ATOM 2079 CA PHE A 346 -26.115 41.887 -30.415 1.00117.01 C ANISOU 2079 CA PHE A 346 16530 10736 17194 252 -607 -1829 C ATOM 2080 C PHE A 346 -25.510 40.513 -30.686 1.00114.82 C ANISOU 2080 C PHE A 346 16056 10859 16711 20 -605 -1730 C ATOM 2081 O PHE A 346 -24.321 40.294 -30.454 1.00112.87 O ANISOU 2081 O PHE A 346 15874 10673 16337 -260 -610 -1772 O ATOM 2082 CB PHE A 346 -26.745 41.910 -29.021 1.00109.29 C ANISOU 2082 CB PHE A 346 15515 9800 16210 450 -449 -2133 C ATOM 2083 CG PHE A 346 -25.848 41.365 -27.944 1.00106.57 C ANISOU 2083 CG PHE A 346 15199 9639 15655 221 -370 -2336 C ATOM 2084 CD1 PHE A 346 -24.867 42.162 -27.377 1.00105.82 C ANISOU 2084 CD1 PHE A 346 15366 9305 15535 33 -397 -2496 C ATOM 2085 CD2 PHE A 346 -25.982 40.058 -27.501 1.00104.63 C ANISOU 2085 CD2 PHE A 346 14729 9794 15232 187 -287 -2362 C ATOM 2086 CE1 PHE A 346 -24.037 41.669 -26.390 1.00103.59 C ANISOU 2086 CE1 PHE A 346 15102 9206 15051 -171 -360 -2678 C ATOM 2087 CE2 PHE A 346 -25.154 39.558 -26.514 1.00102.39 C ANISOU 2087 CE2 PHE A 346 14488 9672 14743 -4 -241 -2529 C ATOM 2088 CZ PHE A 346 -24.180 40.364 -25.958 1.00101.93 C ANISOU 2088 CZ PHE A 346 14673 9398 14658 -175 -287 -2687 C ATOM 2089 N TYR A 347 -26.339 39.594 -31.174 1.00104.09 N ANISOU 2089 N TYR A 347 14453 9767 15330 142 -605 -1606 N ATOM 2090 CA TYR A 347 -25.913 38.223 -31.444 1.00101.76 C ANISOU 2090 CA TYR A 347 13983 9833 14849 -40 -597 -1520 C ATOM 2091 C TYR A 347 -24.780 38.164 -32.459 1.00100.41 C ANISOU 2091 C TYR A 347 13902 9646 14604 -310 -693 -1331 C ATOM 2092 O TYR A 347 -23.850 37.369 -32.320 1.00 97.84 O ANISOU 2092 O TYR A 347 13527 9525 14123 -523 -667 -1348 O ATOM 2093 CB TYR A 347 -27.098 37.392 -31.945 1.00100.25 C ANISOU 2093 CB TYR A 347 13541 9873 14675 131 -603 -1408 C ATOM 2094 CG TYR A 347 -26.749 35.968 -32.322 1.00 97.90 C ANISOU 2094 CG TYR A 347 13093 9909 14197 -45 -602 -1315 C ATOM 2095 CD1 TYR A 347 -26.746 34.957 -31.370 1.00 95.98 C ANISOU 2095 CD1 TYR A 347 12735 9913 13819 -86 -482 -1455 C ATOM 2096 CD2 TYR A 347 -26.434 35.632 -33.634 1.00 97.86 C ANISOU 2096 CD2 TYR A 347 13087 9955 14141 -166 -717 -1087 C ATOM 2097 CE1 TYR A 347 -26.431 33.654 -31.712 1.00 93.87 C ANISOU 2097 CE1 TYR A 347 12360 9911 13397 -232 -483 -1371 C ATOM 2098 CE2 TYR A 347 -26.116 34.333 -33.984 1.00 95.64 C ANISOU 2098 CE2 TYR A 347 12692 9953 13696 -311 -707 -1022 C ATOM 2099 CZ TYR A 347 -26.117 33.348 -33.020 1.00 93.42 C ANISOU 2099 CZ TYR A 347 12300 9887 13306 -337 -594 -1165 C ATOM 2100 OH TYR A 347 -25.803 32.054 -33.366 1.00 91.06 O ANISOU 2100 OH TYR A 347 11916 9827 12854 -467 -588 -1102 O ATOM 2101 N HIS A 348 -24.864 39.005 -33.482 1.00104.45 N ANISOU 2101 N HIS A 348 14547 9916 15225 -290 -798 -1146 N ATOM 2102 CA HIS A 348 -23.894 38.973 -34.569 1.00103.81 C ANISOU 2102 CA HIS A 348 14552 9827 15063 -544 -866 -942 C ATOM 2103 C HIS A 348 -22.610 39.727 -34.234 1.00102.38 C ANISOU 2103 C HIS A 348 14564 9451 14883 -799 -848 -1018 C ATOM 2104 O HIS A 348 -21.559 39.464 -34.818 1.00100.52 O ANISOU 2104 O HIS A 348 14339 9305 14550 -1063 -850 -914 O ATOM 2105 CB HIS A 348 -24.526 39.483 -35.861 1.00 93.80 C ANISOU 2105 CB HIS A 348 13363 8404 13871 -436 -991 -683 C ATOM 2106 CG HIS A 348 -25.680 38.640 -36.332 1.00 95.31 C ANISOU 2106 CG HIS A 348 13334 8834 14044 -239 -1041 -594 C ATOM 2107 ND1 HIS A 348 -26.977 38.891 -35.945 1.00 97.73 N ANISOU 2107 ND1 HIS A 348 13532 9099 14503 74 -1058 -659 N ATOM 2108 CD2 HIS A 348 -25.710 37.552 -37.121 1.00 94.81 C ANISOU 2108 CD2 HIS A 348 13135 9056 13835 -323 -1074 -463 C ATOM 2109 CE1 HIS A 348 -27.769 37.985 -36.500 1.00 98.73 C ANISOU 2109 CE1 HIS A 348 13443 9489 14582 155 -1113 -560 C ATOM 2110 NE2 HIS A 348 -27.038 37.163 -37.213 1.00 97.42 N ANISOU 2110 NE2 HIS A 348 13275 9511 14230 -84 -1128 -445 N ATOM 2111 N TYR A 349 -22.700 40.664 -33.296 1.00107.76 N ANISOU 2111 N TYR A 349 15392 9875 15678 -727 -824 -1209 N ATOM 2112 CA TYR A 349 -21.506 41.291 -32.746 1.00106.59 C ANISOU 2112 CA TYR A 349 15404 9572 15525 -989 -812 -1338 C ATOM 2113 C TYR A 349 -20.865 40.324 -31.761 1.00103.80 C ANISOU 2113 C TYR A 349 14887 9539 15014 -1106 -748 -1528 C ATOM 2114 O TYR A 349 -19.641 40.233 -31.668 1.00102.35 O ANISOU 2114 O TYR A 349 14703 9427 14760 -1387 -758 -1557 O ATOM 2115 CB TYR A 349 -21.843 42.612 -32.055 1.00105.14 C ANISOU 2115 CB TYR A 349 15464 8981 15502 -871 -816 -1503 C ATOM 2116 CG TYR A 349 -22.040 43.772 -33.005 1.00108.11 C ANISOU 2116 CG TYR A 349 16084 8956 16036 -843 -899 -1307 C ATOM 2117 CD1 TYR A 349 -20.985 44.258 -33.767 1.00108.16 C ANISOU 2117 CD1 TYR A 349 16247 8816 16035 -1166 -942 -1146 C ATOM 2118 CD2 TYR A 349 -23.277 44.389 -33.131 1.00110.59 C ANISOU 2118 CD2 TYR A 349 16472 9037 16509 -491 -933 -1277 C ATOM 2119 CE1 TYR A 349 -21.160 45.320 -34.635 1.00110.48 C ANISOU 2119 CE1 TYR A 349 16802 8721 16453 -1154 -1016 -944 C ATOM 2120 CE2 TYR A 349 -23.462 45.451 -33.996 1.00112.97 C ANISOU 2120 CE2 TYR A 349 17025 8950 16951 -443 -1030 -1079 C ATOM 2121 CZ TYR A 349 -22.400 45.913 -34.745 1.00112.95 C ANISOU 2121 CZ TYR A 349 17213 8786 16916 -783 -1072 -906 C ATOM 2122 OH TYR A 349 -22.581 46.971 -35.606 1.00115.43 O ANISOU 2122 OH TYR A 349 17814 8692 17352 -748 -1166 -687 O ATOM 2123 N PHE A 350 -21.709 39.605 -31.027 1.00 96.38 N ANISOU 2123 N PHE A 350 13804 8795 14021 -889 -686 -1650 N ATOM 2124 CA PHE A 350 -21.251 38.569 -30.111 1.00 93.90 C ANISOU 2124 CA PHE A 350 13349 8792 13536 -963 -632 -1798 C ATOM 2125 C PHE A 350 -20.567 37.465 -30.906 1.00 91.70 C ANISOU 2125 C PHE A 350 12904 8800 13135 -1124 -652 -1627 C ATOM 2126 O PHE A 350 -19.553 36.915 -30.475 1.00 88.85 O ANISOU 2126 O PHE A 350 12480 8619 12659 -1299 -655 -1697 O ATOM 2127 CB PHE A 350 -22.435 37.989 -29.335 1.00102.46 C ANISOU 2127 CB PHE A 350 14322 10024 14586 -700 -541 -1915 C ATOM 2128 CG PHE A 350 -22.038 37.121 -28.173 1.00100.15 C ANISOU 2128 CG PHE A 350 13961 9985 14108 -758 -482 -2089 C ATOM 2129 CD1 PHE A 350 -20.862 37.358 -27.480 1.00 98.58 C ANISOU 2129 CD1 PHE A 350 13859 9771 13824 -965 -527 -2229 C ATOM 2130 CD2 PHE A 350 -22.841 36.063 -27.779 1.00 99.86 C ANISOU 2130 CD2 PHE A 350 13767 10202 13975 -616 -394 -2103 C ATOM 2131 CE1 PHE A 350 -20.499 36.560 -26.409 1.00 96.83 C ANISOU 2131 CE1 PHE A 350 13591 9785 13414 -1003 -501 -2373 C ATOM 2132 CE2 PHE A 350 -22.482 35.259 -26.713 1.00 98.04 C ANISOU 2132 CE2 PHE A 350 13510 10186 13553 -668 -346 -2239 C ATOM 2133 CZ PHE A 350 -21.309 35.508 -26.027 1.00 96.35 C ANISOU 2133 CZ PHE A 350 13406 9956 13244 -848 -408 -2369 C ATOM 2134 N TYR A 351 -21.137 37.151 -32.069 1.00 85.40 N ANISOU 2134 N TYR A 351 12041 8044 12362 -1050 -674 -1409 N ATOM 2135 CA TYR A 351 -20.597 36.127 -32.958 1.00 83.58 C ANISOU 2135 CA TYR A 351 11682 8063 12013 -1180 -680 -1247 C ATOM 2136 C TYR A 351 -19.161 36.454 -33.354 1.00 82.71 C ANISOU 2136 C TYR A 351 11623 7924 11880 -1466 -697 -1202 C ATOM 2137 O TYR A 351 -18.318 35.563 -33.467 1.00 80.42 O ANISOU 2137 O TYR A 351 11204 7878 11474 -1596 -674 -1189 O ATOM 2138 CB TYR A 351 -21.467 35.988 -34.211 1.00 94.96 C ANISOU 2138 CB TYR A 351 13100 9499 13483 -1068 -724 -1027 C ATOM 2139 CG TYR A 351 -21.033 34.874 -35.140 1.00 93.47 C ANISOU 2139 CG TYR A 351 12800 9565 13150 -1180 -720 -882 C ATOM 2140 CD1 TYR A 351 -20.073 35.089 -36.122 1.00 93.77 C ANISOU 2140 CD1 TYR A 351 12905 9581 13144 -1388 -728 -738 C ATOM 2141 CD2 TYR A 351 -21.585 33.605 -35.032 1.00 91.81 C ANISOU 2141 CD2 TYR A 351 12432 9610 12843 -1087 -692 -898 C ATOM 2142 CE1 TYR A 351 -19.673 34.070 -36.967 1.00 92.38 C ANISOU 2142 CE1 TYR A 351 12639 9636 12824 -1473 -702 -629 C ATOM 2143 CE2 TYR A 351 -21.194 32.581 -35.872 1.00 90.45 C ANISOU 2143 CE2 TYR A 351 12188 9643 12536 -1180 -685 -788 C ATOM 2144 CZ TYR A 351 -20.239 32.818 -36.837 1.00 90.97 C ANISOU 2144 CZ TYR A 351 12322 9688 12555 -1360 -687 -662 C ATOM 2145 OH TYR A 351 -19.849 31.797 -37.674 1.00 90.01 O ANISOU 2145 OH TYR A 351 12140 9769 12289 -1436 -660 -575 O ATOM 2146 N MET A 352 -18.894 37.737 -33.575 1.00108.68 N ANISOU 2146 N MET A 352 15097 10907 15289 -1561 -731 -1175 N ATOM 2147 CA MET A 352 -17.553 38.188 -33.919 1.00108.69 C ANISOU 2147 CA MET A 352 15145 10860 15292 -1868 -734 -1136 C ATOM 2148 C MET A 352 -16.600 37.939 -32.757 1.00106.63 C ANISOU 2148 C MET A 352 14798 10738 14980 -2005 -732 -1358 C ATOM 2149 O MET A 352 -15.463 37.519 -32.957 1.00105.49 O ANISOU 2149 O MET A 352 14528 10779 14775 -2217 -721 -1338 O ATOM 2150 CB MET A 352 -17.555 39.669 -34.300 1.00109.53 C ANISOU 2150 CB MET A 352 15505 10564 15547 -1951 -772 -1067 C ATOM 2151 CG MET A 352 -18.285 39.978 -35.596 1.00111.65 C ANISOU 2151 CG MET A 352 15881 10692 15848 -1853 -802 -804 C ATOM 2152 SD MET A 352 -18.193 41.724 -36.039 1.00115.15 S ANISOU 2152 SD MET A 352 16671 10622 16460 -1961 -854 -697 S ATOM 2153 CE MET A 352 -19.025 41.719 -37.625 1.00118.12 C ANISOU 2153 CE MET A 352 17131 10948 16802 -1825 -913 -355 C ATOM 2154 N LEU A 353 -17.072 38.202 -31.542 1.00113.12 N ANISOU 2154 N LEU A 353 15683 11480 15819 -1875 -745 -1571 N ATOM 2155 CA LEU A 353 -16.245 38.057 -30.350 1.00111.83 C ANISOU 2155 CA LEU A 353 15476 11430 15585 -1994 -774 -1793 C ATOM 2156 C LEU A 353 -15.997 36.592 -29.996 1.00109.10 C ANISOU 2156 C LEU A 353 14910 11467 15075 -1940 -759 -1813 C ATOM 2157 O LEU A 353 -14.876 36.210 -29.660 1.00108.13 O ANISOU 2157 O LEU A 353 14674 11525 14887 -2108 -801 -1874 O ATOM 2158 CB LEU A 353 -16.886 38.787 -29.165 1.00104.03 C ANISOU 2158 CB LEU A 353 14660 10234 14631 -1861 -780 -2023 C ATOM 2159 CG LEU A 353 -16.078 38.889 -27.868 1.00102.91 C ANISOU 2159 CG LEU A 353 14545 10153 14405 -1998 -837 -2276 C ATOM 2160 CD1 LEU A 353 -16.232 40.272 -27.261 1.00105.22 C ANISOU 2160 CD1 LEU A 353 15105 10072 14801 -2029 -863 -2457 C ATOM 2161 CD2 LEU A 353 -16.502 37.821 -26.868 1.00100.87 C ANISOU 2161 CD2 LEU A 353 14190 10166 13969 -1818 -807 -2396 C ATOM 2162 N THR A 354 -17.045 35.777 -30.071 1.00110.41 N ANISOU 2162 N THR A 354 15017 11749 15183 -1706 -706 -1760 N ATOM 2163 CA THR A 354 -16.943 34.362 -29.726 1.00108.03 C ANISOU 2163 CA THR A 354 14552 11767 14728 -1639 -687 -1770 C ATOM 2164 C THR A 354 -16.024 33.599 -30.673 1.00106.27 C ANISOU 2164 C THR A 354 14177 11740 14459 -1770 -687 -1621 C ATOM 2165 O THR A 354 -15.175 32.820 -30.239 1.00104.43 O ANISOU 2165 O THR A 354 13823 11725 14131 -1825 -712 -1675 O ATOM 2166 CB THR A 354 -18.322 33.673 -29.737 1.00103.00 C ANISOU 2166 CB THR A 354 13885 11194 14056 -1397 -620 -1727 C ATOM 2167 OG1 THR A 354 -18.937 33.846 -31.020 1.00103.88 O ANISOU 2167 OG1 THR A 354 13996 11220 14255 -1350 -612 -1534 O ATOM 2168 CG2 THR A 354 -19.220 34.258 -28.664 1.00104.52 C ANISOU 2168 CG2 THR A 354 14188 11252 14273 -1244 -583 -1900 C ATOM 2169 N ASN A 355 -16.198 33.832 -31.968 1.00 99.11 N ANISOU 2169 N ASN A 355 13286 10757 13613 -1805 -660 -1435 N ATOM 2170 CA ASN A 355 -15.434 33.117 -32.983 1.00 98.99 C ANISOU 2170 CA ASN A 355 13146 10925 13540 -1911 -627 -1294 C ATOM 2171 C ASN A 355 -14.013 33.644 -33.169 1.00 99.32 C ANISOU 2171 C ASN A 355 13134 10979 13626 -2173 -635 -1302 C ATOM 2172 O ASN A 355 -13.156 32.952 -33.719 1.00 98.62 O ANISOU 2172 O ASN A 355 12893 11097 13481 -2259 -593 -1242 O ATOM 2173 CB ASN A 355 -16.190 33.113 -34.312 1.00 93.47 C ANISOU 2173 CB ASN A 355 12502 10161 12850 -1855 -596 -1092 C ATOM 2174 CG ASN A 355 -17.357 32.144 -34.312 1.00 92.65 C ANISOU 2174 CG ASN A 355 12361 10165 12678 -1637 -586 -1070 C ATOM 2175 OD1 ASN A 355 -17.315 31.106 -34.972 1.00 91.89 O ANISOU 2175 OD1 ASN A 355 12184 10247 12481 -1619 -556 -987 O ATOM 2176 ND2 ASN A 355 -18.402 32.472 -33.560 1.00 92.93 N ANISOU 2176 ND2 ASN A 355 12451 10091 12769 -1477 -602 -1156 N ATOM 2177 N ALA A 356 -13.767 34.868 -32.716 1.00100.17 N ANISOU 2177 N ALA A 356 13359 10862 13839 -2304 -680 -1386 N ATOM 2178 CA ALA A 356 -12.415 35.412 -32.728 1.00100.12 C ANISOU 2178 CA ALA A 356 13283 10869 13887 -2589 -697 -1420 C ATOM 2179 C ALA A 356 -11.578 34.673 -31.695 1.00 98.46 C ANISOU 2179 C ALA A 356 12887 10918 13604 -2604 -760 -1586 C ATOM 2180 O ALA A 356 -10.398 34.404 -31.912 1.00 98.26 O ANISOU 2180 O ALA A 356 12670 11083 13583 -2772 -758 -1579 O ATOM 2181 CB ALA A 356 -12.430 36.901 -32.434 1.00100.78 C ANISOU 2181 CB ALA A 356 13574 10615 14103 -2734 -742 -1484 C ATOM 2182 N LEU A 357 -12.207 34.345 -30.570 1.00126.98 N ANISOU 2182 N LEU A 357 16555 14546 17145 -2421 -815 -1730 N ATOM 2183 CA LEU A 357 -11.551 33.598 -29.503 1.00126.09 C ANISOU 2183 CA LEU A 357 16310 14669 16930 -2398 -899 -1874 C ATOM 2184 C LEU A 357 -11.290 32.151 -29.912 1.00124.84 C ANISOU 2184 C LEU A 357 15963 14798 16673 -2277 -860 -1778 C ATOM 2185 O LEU A 357 -10.398 31.497 -29.372 1.00124.14 O ANISOU 2185 O LEU A 357 15712 14930 16524 -2289 -933 -1846 O ATOM 2186 CB LEU A 357 -12.396 33.642 -28.227 1.00 96.40 C ANISOU 2186 CB LEU A 357 12703 10836 13086 -2233 -944 -2037 C ATOM 2187 CG LEU A 357 -12.562 35.011 -27.563 1.00 98.07 C ANISOU 2187 CG LEU A 357 13119 10770 13374 -2330 -993 -2195 C ATOM 2188 CD1 LEU A 357 -13.539 34.929 -26.400 1.00 97.83 C ANISOU 2188 CD1 LEU A 357 13242 10692 13236 -2127 -988 -2350 C ATOM 2189 CD2 LEU A 357 -11.218 35.553 -27.101 1.00 98.71 C ANISOU 2189 CD2 LEU A 357 13130 10889 13487 -2603 -1116 -2318 C ATOM 2190 N VAL A 358 -12.077 31.655 -30.863 1.00116.68 N ANISOU 2190 N VAL A 358 14960 13751 15622 -2154 -759 -1625 N ATOM 2191 CA VAL A 358 -11.894 30.305 -31.387 1.00115.50 C ANISOU 2191 CA VAL A 358 14673 13830 15381 -2043 -708 -1537 C ATOM 2192 C VAL A 358 -10.588 30.199 -32.170 1.00116.58 C ANISOU 2192 C VAL A 358 14617 14119 15559 -2206 -671 -1479 C ATOM 2193 O VAL A 358 -9.843 29.228 -32.032 1.00116.30 O ANISOU 2193 O VAL A 358 14408 14312 15468 -2147 -683 -1501 O ATOM 2194 CB VAL A 358 -13.073 29.891 -32.295 1.00 90.55 C ANISOU 2194 CB VAL A 358 11607 10606 12192 -1907 -621 -1397 C ATOM 2195 CG1 VAL A 358 -12.742 28.622 -33.070 1.00 89.89 C ANISOU 2195 CG1 VAL A 358 11408 10724 12023 -1842 -558 -1307 C ATOM 2196 CG2 VAL A 358 -14.340 29.709 -31.471 1.00 90.01 C ANISOU 2196 CG2 VAL A 358 11659 10461 12079 -1726 -638 -1459 C ATOM 2197 N TYR A 359 -10.309 31.215 -32.979 1.00133.43 N ANISOU 2197 N TYR A 359 16784 16123 17792 -2406 -619 -1403 N ATOM 2198 CA TYR A 359 -9.094 31.241 -33.785 1.00134.68 C ANISOU 2198 CA TYR A 359 16755 16424 17993 -2596 -545 -1342 C ATOM 2199 C TYR A 359 -7.878 31.618 -32.946 1.00135.06 C ANISOU 2199 C TYR A 359 16622 16581 18114 -2769 -641 -1483 C ATOM 2200 O TYR A 359 -6.737 31.401 -33.355 1.00136.48 O ANISOU 2200 O TYR A 359 16562 16963 18333 -2896 -593 -1471 O ATOM 2201 CB TYR A 359 -9.263 32.181 -34.979 1.00124.82 C ANISOU 2201 CB TYR A 359 15634 14991 16801 -2769 -443 -1187 C ATOM 2202 CG TYR A 359 -10.302 31.696 -35.966 1.00124.93 C ANISOU 2202 CG TYR A 359 15785 14958 16725 -2610 -367 -1035 C ATOM 2203 CD1 TYR A 359 -10.370 30.355 -36.322 1.00123.97 C ANISOU 2203 CD1 TYR A 359 15570 15045 16487 -2440 -313 -1012 C ATOM 2204 CD2 TYR A 359 -11.210 32.574 -36.542 1.00126.40 C ANISOU 2204 CD2 TYR A 359 16201 14883 16942 -2628 -365 -919 C ATOM 2205 CE1 TYR A 359 -11.315 29.900 -37.221 1.00124.14 C ANISOU 2205 CE1 TYR A 359 15720 15029 16417 -2320 -264 -889 C ATOM 2206 CE2 TYR A 359 -12.160 32.127 -37.443 1.00126.82 C ANISOU 2206 CE2 TYR A 359 16363 14915 16907 -2488 -328 -782 C ATOM 2207 CZ TYR A 359 -12.207 30.789 -37.779 1.00125.52 C ANISOU 2207 CZ TYR A 359 16099 14975 16620 -2350 -280 -774 C ATOM 2208 OH TYR A 359 -13.148 30.339 -38.675 1.00125.97 O ANISOU 2208 OH TYR A 359 16268 15014 16581 -2236 -262 -654 O ATOM 2209 N VAL A 360 -8.130 32.186 -31.771 1.00110.21 N ANISOU 2209 N VAL A 360 13582 13311 14982 -2776 -777 -1627 N ATOM 2210 CA VAL A 360 -7.077 32.423 -30.795 1.00110.38 C ANISOU 2210 CA VAL A 360 13446 13454 15040 -2917 -917 -1787 C ATOM 2211 C VAL A 360 -6.592 31.077 -30.268 1.00109.69 C ANISOU 2211 C VAL A 360 13155 13669 14853 -2721 -984 -1833 C ATOM 2212 O VAL A 360 -5.393 30.861 -30.087 1.00111.10 O ANISOU 2212 O VAL A 360 13065 14072 15075 -2814 -1050 -1886 O ATOM 2213 CB VAL A 360 -7.580 33.291 -29.620 1.00 93.79 C ANISOU 2213 CB VAL A 360 11561 11138 12937 -2945 -1048 -1949 C ATOM 2214 CG1 VAL A 360 -6.605 33.246 -28.450 1.00 93.80 C ANISOU 2214 CG1 VAL A 360 11413 11313 12915 -3034 -1234 -2131 C ATOM 2215 CG2 VAL A 360 -7.810 34.725 -30.076 1.00 95.19 C ANISOU 2215 CG2 VAL A 360 11930 10994 13243 -3164 -1004 -1923 C ATOM 2216 N SER A 361 -7.538 30.169 -30.049 1.00101.25 N ANISOU 2216 N SER A 361 12210 12601 13660 -2448 -968 -1803 N ATOM 2217 CA SER A 361 -7.243 28.835 -29.537 1.00100.54 C ANISOU 2217 CA SER A 361 11997 12741 13461 -2233 -1031 -1825 C ATOM 2218 C SER A 361 -6.349 28.032 -30.480 1.00101.55 C ANISOU 2218 C SER A 361 11872 13090 13624 -2207 -939 -1739 C ATOM 2219 O SER A 361 -5.595 27.163 -30.041 1.00102.57 O ANISOU 2219 O SER A 361 11815 13437 13720 -2085 -1022 -1780 O ATOM 2220 CB SER A 361 -8.543 28.070 -29.277 1.00127.12 C ANISOU 2220 CB SER A 361 15577 16026 16697 -1987 -994 -1787 C ATOM 2221 OG SER A 361 -8.282 26.734 -28.886 1.00127.73 O ANISOU 2221 OG SER A 361 15575 16289 16667 -1784 -1041 -1781 O ATOM 2222 N ALA A 362 -6.433 28.327 -31.772 1.00128.13 N ANISOU 2222 N ALA A 362 15240 16397 17048 -2307 -767 -1620 N ATOM 2223 CA ALA A 362 -5.655 27.601 -32.770 1.00129.42 C ANISOU 2223 CA ALA A 362 15187 16761 17226 -2281 -636 -1547 C ATOM 2224 C ALA A 362 -4.343 28.303 -33.112 1.00131.49 C ANISOU 2224 C ALA A 362 15178 17157 17624 -2545 -603 -1569 C ATOM 2225 O ALA A 362 -3.709 27.987 -34.119 1.00133.39 O ANISOU 2225 O ALA A 362 15246 17546 17891 -2582 -441 -1501 O ATOM 2226 CB ALA A 362 -6.483 27.382 -34.029 1.00 98.04 C ANISOU 2226 CB ALA A 362 11378 12680 13194 -2234 -458 -1404 C ATOM 2227 N ALA A 363 -3.938 29.254 -32.275 1.00110.14 N ANISOU 2227 N ALA A 363 12440 14407 15001 -2742 -747 -1673 N ATOM 2228 CA ALA A 363 -2.709 30.002 -32.521 1.00111.89 C ANISOU 2228 CA ALA A 363 12396 14749 15368 -3044 -728 -1703 C ATOM 2229 C ALA A 363 -1.859 30.170 -31.264 1.00112.62 C ANISOU 2229 C ALA A 363 12290 14987 15513 -3116 -966 -1871 C ATOM 2230 O ALA A 363 -0.681 30.519 -31.347 1.00114.79 O ANISOU 2230 O ALA A 363 12252 15447 15915 -3335 -981 -1916 O ATOM 2231 CB ALA A 363 -3.034 31.360 -33.123 1.00 97.44 C ANISOU 2231 CB ALA A 363 10760 12651 13612 -3340 -636 -1634 C ATOM 2232 N ILE A 364 -2.455 29.919 -30.103 1.00140.84 N ANISOU 2232 N ILE A 364 16040 18494 18981 -2942 -1151 -1962 N ATOM 2233 CA ILE A 364 -1.775 30.140 -28.828 1.00141.37 C ANISOU 2233 CA ILE A 364 15986 18676 19053 -3011 -1409 -2127 C ATOM 2234 C ILE A 364 -0.773 29.044 -28.484 1.00142.85 C ANISOU 2234 C ILE A 364 15829 19213 19235 -2831 -1525 -2159 C ATOM 2235 O ILE A 364 0.238 29.305 -27.834 1.00144.46 O ANISOU 2235 O ILE A 364 15777 19603 19508 -2967 -1714 -2272 O ATOM 2236 CB ILE A 364 -2.774 30.294 -27.667 1.00158.14 C ANISOU 2236 CB ILE A 364 18449 20606 21031 -2894 -1556 -2220 C ATOM 2237 CG1 ILE A 364 -3.862 29.224 -27.763 1.00156.85 C ANISOU 2237 CG1 ILE A 364 18487 20391 20719 -2555 -1467 -2125 C ATOM 2238 CG2 ILE A 364 -3.385 31.685 -27.671 1.00157.82 C ANISOU 2238 CG2 ILE A 364 18677 20243 21045 -3130 -1522 -2262 C ATOM 2239 CD1 ILE A 364 -4.961 29.385 -26.746 1.00155.78 C ANISOU 2239 CD1 ILE A 364 18683 20067 20439 -2446 -1547 -2200 C ATOM 2240 N ASN A 365 -1.062 27.820 -28.914 1.00108.41 N ANISOU 2240 N ASN A 365 11464 14931 14794 -2522 -1424 -2063 N ATOM 2241 CA ASN A 365 -0.212 26.673 -28.590 1.00110.13 C ANISOU 2241 CA ASN A 365 11398 15442 15003 -2281 -1532 -2082 C ATOM 2242 C ASN A 365 1.261 26.797 -29.007 1.00112.78 C ANISOU 2242 C ASN A 365 11252 16075 15523 -2428 -1525 -2116 C ATOM 2243 O ASN A 365 2.145 26.536 -28.191 1.00114.30 O ANISOU 2243 O ASN A 365 11182 16499 15747 -2377 -1757 -2206 O ATOM 2244 CB ASN A 365 -0.827 25.362 -29.097 1.00125.04 C ANISOU 2244 CB ASN A 365 13412 17312 16785 -1937 -1398 -1973 C ATOM 2245 CG ASN A 365 -2.049 24.948 -28.303 1.00123.12 C ANISOU 2245 CG ASN A 365 13554 16872 16355 -1750 -1479 -1963 C ATOM 2246 OD1 ASN A 365 -3.161 25.403 -28.571 1.00120.84 O ANISOU 2246 OD1 ASN A 365 13557 16341 16016 -1813 -1366 -1921 O ATOM 2247 ND2 ASN A 365 -1.849 24.079 -27.320 1.00123.99 N ANISOU 2247 ND2 ASN A 365 13660 17092 16360 -1517 -1674 -1994 N ATOM 2248 N PRO A 366 1.537 27.197 -30.265 1.00122.63 N ANISOU 2248 N PRO A 366 12375 17334 16887 -2613 -1263 -2042 N ATOM 2249 CA PRO A 366 2.950 27.380 -30.623 1.00125.19 C ANISOU 2249 CA PRO A 366 12210 17961 17394 -2785 -1232 -2083 C ATOM 2250 C PRO A 366 3.612 28.494 -29.816 1.00125.67 C ANISOU 2250 C PRO A 366 12121 18065 17563 -3133 -1450 -2209 C ATOM 2251 O PRO A 366 4.815 28.436 -29.562 1.00128.06 O ANISOU 2251 O PRO A 366 11982 18675 17999 -3208 -1565 -2287 O ATOM 2252 CB PRO A 366 2.888 27.772 -32.103 1.00105.14 C ANISOU 2252 CB PRO A 366 9678 15360 14911 -2968 -883 -1968 C ATOM 2253 CG PRO A 366 1.590 27.235 -32.586 1.00103.10 C ANISOU 2253 CG PRO A 366 9831 14858 14485 -2739 -752 -1862 C ATOM 2254 CD PRO A 366 0.656 27.390 -31.431 1.00101.11 C ANISOU 2254 CD PRO A 366 9911 14388 14120 -2655 -984 -1913 C ATOM 2255 N ILE A 367 2.829 29.494 -29.420 1.00121.34 N ANISOU 2255 N ILE A 367 11931 17211 16962 -3340 -1509 -2237 N ATOM 2256 CA ILE A 367 3.338 30.580 -28.593 1.00121.90 C ANISOU 2256 CA ILE A 367 11939 17264 17112 -3677 -1728 -2379 C ATOM 2257 C ILE A 367 3.680 30.066 -27.199 1.00122.34 C ANISOU 2257 C ILE A 367 11908 17496 17081 -3499 -2082 -2512 C ATOM 2258 O ILE A 367 4.699 30.442 -26.619 1.00124.38 O ANISOU 2258 O ILE A 367 11855 17965 17440 -3700 -2298 -2633 O ATOM 2259 CB ILE A 367 2.312 31.726 -28.470 1.00115.14 C ANISOU 2259 CB ILE A 367 11547 15995 16207 -3886 -1702 -2389 C ATOM 2260 CG1 ILE A 367 1.871 32.204 -29.855 1.00114.92 C ANISOU 2260 CG1 ILE A 367 11658 15770 16237 -4027 -1375 -2228 C ATOM 2261 CG2 ILE A 367 2.887 32.879 -27.658 1.00115.89 C ANISOU 2261 CG2 ILE A 367 11598 16047 16387 -4261 -1920 -2555 C ATOM 2262 CD1 ILE A 367 0.847 33.318 -29.816 1.00113.65 C ANISOU 2262 CD1 ILE A 367 11949 15186 16048 -4189 -1348 -2220 C ATOM 2263 N LEU A 368 2.826 29.194 -26.673 1.00123.31 N ANISOU 2263 N LEU A 368 12309 17536 17007 -3134 -2147 -2482 N ATOM 2264 CA LEU A 368 3.031 28.612 -25.352 1.00123.99 C ANISOU 2264 CA LEU A 368 12385 17765 16959 -2930 -2475 -2578 C ATOM 2265 C LEU A 368 4.259 27.708 -25.326 1.00126.54 C ANISOU 2265 C LEU A 368 12219 18483 17376 -2754 -2597 -2577 C ATOM 2266 O LEU A 368 5.007 27.689 -24.348 1.00128.45 O ANISOU 2266 O LEU A 368 12263 18935 17609 -2767 -2918 -2687 O ATOM 2267 CB LEU A 368 1.793 27.826 -24.915 1.00114.34 C ANISOU 2267 CB LEU A 368 11585 16355 15503 -2589 -2462 -2515 C ATOM 2268 CG LEU A 368 0.519 28.635 -24.668 1.00112.11 C ANISOU 2268 CG LEU A 368 11777 15710 15110 -2698 -2389 -2541 C ATOM 2269 CD1 LEU A 368 -0.602 27.734 -24.169 1.00110.70 C ANISOU 2269 CD1 LEU A 368 11943 15411 14707 -2362 -2380 -2482 C ATOM 2270 CD2 LEU A 368 0.780 29.768 -23.689 1.00112.58 C ANISOU 2270 CD2 LEU A 368 11910 15709 15157 -2990 -2616 -2723 C ATOM 2271 N TYR A 369 4.455 26.957 -26.406 1.00 96.48 N ANISOU 2271 N TYR A 369 8224 14779 13654 -2577 -2347 -2460 N ATOM 2272 CA TYR A 369 5.586 26.041 -26.513 1.00 99.16 C ANISOU 2272 CA TYR A 369 8090 15482 14104 -2357 -2416 -2458 C ATOM 2273 C TYR A 369 6.904 26.812 -26.509 1.00101.68 C ANISOU 2273 C TYR A 369 7904 16084 14648 -2693 -2516 -2561 C ATOM 2274 O TYR A 369 7.885 26.380 -25.904 1.00104.52 O ANISOU 2274 O TYR A 369 7878 16758 15075 -2577 -2773 -2629 O ATOM 2275 CB TYR A 369 5.475 25.197 -27.785 1.00128.92 C ANISOU 2275 CB TYR A 369 11798 19269 17917 -2131 -2075 -2333 C ATOM 2276 CG TYR A 369 4.201 24.384 -27.883 1.00127.19 C ANISOU 2276 CG TYR A 369 12049 18783 17495 -1825 -1969 -2232 C ATOM 2277 CD1 TYR A 369 3.489 24.023 -26.745 1.00125.94 C ANISOU 2277 CD1 TYR A 369 12225 18489 17137 -1646 -2202 -2244 C ATOM 2278 CD2 TYR A 369 3.703 23.988 -29.119 1.00126.79 C ANISOU 2278 CD2 TYR A 369 12112 18623 17440 -1741 -1633 -2126 C ATOM 2279 CE1 TYR A 369 2.323 23.287 -26.835 1.00124.32 C ANISOU 2279 CE1 TYR A 369 12427 18049 16758 -1403 -2093 -2151 C ATOM 2280 CE2 TYR A 369 2.537 23.253 -29.218 1.00125.10 C ANISOU 2280 CE2 TYR A 369 12309 18173 17051 -1495 -1550 -2042 C ATOM 2281 CZ TYR A 369 1.851 22.904 -28.074 1.00123.97 C ANISOU 2281 CZ TYR A 369 12465 17901 16736 -1334 -1776 -2053 C ATOM 2282 OH TYR A 369 0.691 22.171 -28.169 1.00122.95 O ANISOU 2282 OH TYR A 369 12724 17548 16445 -1122 -1682 -1969 O ATOM 2283 N ASN A 370 6.916 27.954 -27.190 1.00137.84 N ANISOU 2283 N ASN A 370 12483 20545 19345 -3114 -2320 -2567 N ATOM 2284 CA ASN A 370 8.106 28.795 -27.260 1.00139.95 C ANISOU 2284 CA ASN A 370 12291 21047 19835 -3511 -2379 -2659 C ATOM 2285 C ASN A 370 8.427 29.465 -25.929 1.00140.88 C ANISOU 2285 C ASN A 370 12405 21197 19924 -3722 -2787 -2825 C ATOM 2286 O ASN A 370 9.587 29.532 -25.521 1.00145.34 O ANISOU 2286 O ASN A 370 12491 22098 20633 -3841 -3008 -2924 O ATOM 2287 CB ASN A 370 7.953 29.860 -28.347 1.00142.72 C ANISOU 2287 CB ASN A 370 12721 21211 20297 -3926 -2050 -2600 C ATOM 2288 CG ASN A 370 8.415 29.379 -29.706 1.00143.88 C ANISOU 2288 CG ASN A 370 12570 21536 20560 -3866 -1680 -2486 C ATOM 2289 OD1 ASN A 370 8.464 28.178 -29.970 1.00144.10 O ANISOU 2289 OD1 ASN A 370 12488 21717 20546 -3450 -1609 -2435 O ATOM 2290 ND2 ASN A 370 8.764 30.318 -30.576 1.00145.08 N ANISOU 2290 ND2 ASN A 370 12613 21661 20850 -4289 -1435 -2448 N ATOM 2291 N LEU A 371 7.391 29.964 -25.263 1.00141.22 N ANISOU 2291 N LEU A 371 12978 20898 19779 -3769 -2884 -2863 N ATOM 2292 CA LEU A 371 7.551 30.694 -24.010 1.00142.62 C ANISOU 2292 CA LEU A 371 13253 21050 19887 -3990 -3247 -3039 C ATOM 2293 C LEU A 371 8.124 29.825 -22.894 1.00145.01 C ANISOU 2293 C LEU A 371 13355 21656 20086 -3701 -3637 -3108 C ATOM 2294 O LEU A 371 9.011 30.254 -22.157 1.00150.15 O ANISOU 2294 O LEU A 371 13727 22525 20797 -3918 -3956 -3253 O ATOM 2295 CB LEU A 371 6.219 31.306 -23.567 1.00126.78 C ANISOU 2295 CB LEU A 371 11885 18605 17681 -4031 -3223 -3067 C ATOM 2296 CG LEU A 371 5.992 32.786 -23.888 1.00127.21 C ANISOU 2296 CG LEU A 371 12140 18358 17837 -4505 -3105 -3128 C ATOM 2297 CD1 LEU A 371 6.097 33.052 -25.382 1.00126.47 C ANISOU 2297 CD1 LEU A 371 11908 18211 17933 -4666 -2720 -2976 C ATOM 2298 CD2 LEU A 371 4.644 33.243 -23.352 1.00124.35 C ANISOU 2298 CD2 LEU A 371 12394 17583 17271 -4447 -3096 -3168 C ATOM 2299 N VAL A 372 7.617 28.603 -22.779 1.00139.66 N ANISOU 2299 N VAL A 372 12829 20985 19250 -3220 -3623 -2999 N ATOM 2300 CA VAL A 372 8.003 27.724 -21.681 1.00141.75 C ANISOU 2300 CA VAL A 372 13007 21479 19372 -2902 -3997 -3032 C ATOM 2301 C VAL A 372 9.260 26.913 -21.989 1.00145.08 C ANISOU 2301 C VAL A 372 12808 22326 19991 -2703 -4079 -2999 C ATOM 2302 O VAL A 372 10.270 27.032 -21.294 1.00149.40 O ANISOU 2302 O VAL A 372 12980 23178 20607 -2787 -4426 -3107 O ATOM 2303 CB VAL A 372 6.855 26.777 -21.287 1.00139.14 C ANISOU 2303 CB VAL A 372 13170 20934 18762 -2485 -3967 -2925 C ATOM 2304 CG1 VAL A 372 7.315 25.807 -20.219 1.00141.36 C ANISOU 2304 CG1 VAL A 372 13370 21450 18892 -2145 -4346 -2925 C ATOM 2305 CG2 VAL A 372 5.653 27.573 -20.807 1.00136.96 C ANISOU 2305 CG2 VAL A 372 13467 20284 18288 -2658 -3921 -2983 C ATOM 2306 N SER A 373 9.198 26.093 -23.033 1.00147.59 N ANISOU 2306 N SER A 373 13012 22666 20399 -2434 -3764 -2861 N ATOM 2307 CA SER A 373 10.324 25.237 -23.393 1.00150.32 C ANISOU 2307 CA SER A 373 12783 23396 20935 -2180 -3794 -2833 C ATOM 2308 C SER A 373 11.432 26.031 -24.077 1.00153.37 C ANISOU 2308 C SER A 373 12594 24049 21630 -2569 -3684 -2908 C ATOM 2309 O SER A 373 11.274 26.487 -25.210 1.00151.98 O ANISOU 2309 O SER A 373 12406 23767 21571 -2788 -3291 -2858 O ATOM 2310 CB SER A 373 9.863 24.089 -24.292 1.00184.66 C ANISOU 2310 CB SER A 373 17240 27657 25264 -1761 -3474 -2682 C ATOM 2311 OG SER A 373 10.948 23.244 -24.636 1.00187.94 O ANISOU 2311 OG SER A 373 17111 28428 25868 -1477 -3489 -2670 O ATOM 2312 N ALA A 374 12.554 26.188 -23.382 1.00159.34 N ANISOU 2312 N ALA A 374 12873 25161 22510 -2664 -4038 -3022 N ATOM 2313 CA ALA A 374 13.697 26.919 -23.917 1.00163.32 C ANISOU 2313 CA ALA A 374 12767 25965 23321 -3058 -3968 -3105 C ATOM 2314 C ALA A 374 14.361 26.138 -25.045 1.00164.75 C ANISOU 2314 C ALA A 374 12466 26410 23720 -2812 -3645 -3024 C ATOM 2315 O ALA A 374 14.861 26.720 -26.008 1.00166.25 O ANISOU 2315 O ALA A 374 12333 26710 24126 -3139 -3332 -3029 O ATOM 2316 CB ALA A 374 14.698 27.221 -22.814 1.00146.89 C ANISOU 2316 CB ALA A 374 10398 24126 21286 -3175 -4429 -3182 C ATOM 2317 N ASN A 375 14.362 24.815 -24.914 1.00154.93 N ANISOU 2317 N ASN A 375 11199 25257 22410 -2234 -3712 -2951 N ATOM 2318 CA ASN A 375 14.947 23.937 -25.920 1.00155.90 C ANISOU 2318 CA ASN A 375 10908 25609 22716 -1916 -3412 -2891 C ATOM 2319 C ASN A 375 14.167 23.996 -27.229 1.00151.85 C ANISOU 2319 C ASN A 375 10715 24817 22166 -1981 -2870 -2791 C ATOM 2320 O ASN A 375 14.746 23.933 -28.313 1.00153.17 O ANISOU 2320 O ASN A 375 10503 25172 22521 -2025 -2515 -2780 O ATOM 2321 CB ASN A 375 15.002 22.498 -25.403 1.00186.84 C ANISOU 2321 CB ASN A 375 14838 29607 26546 -1260 -3632 -2834 C ATOM 2322 CG ASN A 375 15.832 22.364 -24.140 1.00191.82 C ANISOU 2322 CG ASN A 375 15134 30544 27205 -1153 -4193 -2914 C ATOM 2323 OD1 ASN A 375 16.043 23.337 -23.416 1.00194.37 O ANISOU 2323 OD1 ASN A 375 15445 30897 27509 -1561 -4462 -2998 O ATOM 2324 ND2 ASN A 375 16.306 21.154 -23.869 1.00193.59 N ANISOU 2324 ND2 ASN A 375 15140 30958 27458 -593 -4373 -2868 N ATOM 2325 N PHE A 376 12.849 24.116 -27.113 1.00175.19 N ANISOU 2325 N PHE A 376 14362 27335 24866 -1985 -2812 -2721 N ATOM 2326 CA PHE A 376 11.966 24.170 -28.273 1.00173.29 C ANISOU 2326 CA PHE A 376 14490 26800 24551 -2034 -2355 -2618 C ATOM 2327 C PHE A 376 12.085 25.516 -28.977 1.00172.61 C ANISOU 2327 C PHE A 376 14336 26664 24583 -2620 -2111 -2635 C ATOM 2328 O PHE A 376 12.050 25.589 -30.205 1.00172.43 O ANISOU 2328 O PHE A 376 14279 26620 24618 -2711 -1696 -2566 O ATOM 2329 CB PHE A 376 10.515 23.899 -27.868 1.00137.72 C ANISOU 2329 CB PHE A 376 10708 21867 19754 -1862 -2397 -2542 C ATOM 2330 CG PHE A 376 9.548 23.924 -29.018 1.00135.42 C ANISOU 2330 CG PHE A 376 10800 21278 19376 -1897 -1975 -2435 C ATOM 2331 CD1 PHE A 376 9.373 22.808 -29.819 1.00136.24 C ANISOU 2331 CD1 PHE A 376 10941 21376 19448 -1515 -1727 -2359 C ATOM 2332 CD2 PHE A 376 8.803 25.060 -29.290 1.00133.08 C ANISOU 2332 CD2 PHE A 376 10845 20696 19023 -2303 -1844 -2414 C ATOM 2333 CE1 PHE A 376 8.483 22.828 -30.876 1.00134.57 C ANISOU 2333 CE1 PHE A 376 11087 20906 19137 -1559 -1368 -2267 C ATOM 2334 CE2 PHE A 376 7.911 25.085 -30.344 1.00131.36 C ANISOU 2334 CE2 PHE A 376 10975 20219 18718 -2324 -1492 -2306 C ATOM 2335 CZ PHE A 376 7.750 23.968 -31.138 1.00132.00 C ANISOU 2335 CZ PHE A 376 11078 20321 18753 -1962 -1260 -2234 C ATOM 2336 N ARG A 377 12.211 26.579 -28.187 1.00148.44 N ANISOU 2336 N ARG A 377 11293 23567 21541 -3019 -2374 -2727 N ATOM 2337 CA ARG A 377 12.263 27.941 -28.710 1.00149.30 C ANISOU 2337 CA ARG A 377 11414 23561 21751 -3605 -2189 -2742 C ATOM 2338 C ARG A 377 13.426 28.113 -29.685 1.00153.57 C ANISOU 2338 C ARG A 377 11333 24455 22560 -3821 -1911 -2746 C ATOM 2339 O ARG A 377 13.319 28.837 -30.674 1.00153.12 O ANISOU 2339 O ARG A 377 11343 24280 22555 -4172 -1557 -2679 O ATOM 2340 CB ARG A 377 12.376 28.957 -27.571 1.00173.15 C ANISOU 2340 CB ARG A 377 14505 26518 24764 -3972 -2570 -2875 C ATOM 2341 CG ARG A 377 12.161 30.400 -27.997 1.00173.51 C ANISOU 2341 CG ARG A 377 14742 26310 24872 -4560 -2402 -2883 C ATOM 2342 CD ARG A 377 12.458 31.376 -26.865 1.00176.52 C ANISOU 2342 CD ARG A 377 15142 26657 25270 -4930 -2789 -3043 C ATOM 2343 NE ARG A 377 11.774 31.028 -25.622 1.00174.13 N ANISOU 2343 NE ARG A 377 15220 26214 24726 -4657 -3152 -3116 N ATOM 2344 CZ ARG A 377 12.382 30.538 -24.546 1.00177.05 C ANISOU 2344 CZ ARG A 377 15349 26858 25064 -4474 -3567 -3215 C ATOM 2345 NH1 ARG A 377 13.693 30.337 -24.558 1.00181.93 N ANISOU 2345 NH1 ARG A 377 15415 27827 25883 -4464 -3657 -3186 N ATOM 2346 NH2 ARG A 377 11.682 30.251 -23.457 1.00175.28 N ANISOU 2346 NH2 ARG A 377 15536 26482 24581 -4243 -3861 -3265 N ATOM 2347 N GLN A 378 14.533 27.435 -29.397 1.00216.52 N ANISOU 2347 N GLN A 378 18701 32869 30698 -3602 -2069 -2818 N ATOM 2348 CA GLN A 378 15.736 27.530 -30.217 1.00221.81 C ANISOU 2348 CA GLN A 378 18727 33917 31635 -3766 -1815 -2825 C ATOM 2349 C GLN A 378 15.591 26.877 -31.586 1.00220.36 C ANISOU 2349 C GLN A 378 18511 33767 31449 -3554 -1308 -2734 C ATOM 2350 O GLN A 378 15.977 27.459 -32.600 1.00222.80 O ANISOU 2350 O GLN A 378 18631 34151 31870 -3901 -929 -2693 O ATOM 2351 CB GLN A 378 16.918 26.901 -29.472 1.00174.34 C ANISOU 2351 CB GLN A 378 12204 28268 25771 -3471 -2134 -2859 C ATOM 2352 CG GLN A 378 18.249 26.968 -30.205 1.00179.90 C ANISOU 2352 CG GLN A 378 12314 29296 26745 -3568 -1886 -2811 C ATOM 2353 CD GLN A 378 18.732 28.380 -30.453 1.00183.42 C ANISOU 2353 CD GLN A 378 12719 29653 27317 -4208 -1781 -2770 C ATOM 2354 OE1 GLN A 378 18.380 29.310 -29.729 1.00182.78 O ANISOU 2354 OE1 GLN A 378 12961 29321 27167 -4551 -2039 -2799 O ATOM 2355 NE2 GLN A 378 19.556 28.544 -31.480 1.00187.51 N ANISOU 2355 NE2 GLN A 378 12855 30367 28022 -4364 -1395 -2704 N ATOM 2356 N VAL A 379 15.034 25.673 -31.616 1.00183.06 N ANISOU 2356 N VAL A 379 14037 28945 26571 -2984 -1294 -2682 N ATOM 2357 CA VAL A 379 14.829 24.967 -32.875 1.00181.24 C ANISOU 2357 CA VAL A 379 13870 28697 26296 -2737 -833 -2599 C ATOM 2358 C VAL A 379 13.649 25.546 -33.664 1.00177.90 C ANISOU 2358 C VAL A 379 14082 27841 25670 -2977 -536 -2477 C ATOM 2359 O VAL A 379 13.648 25.529 -34.895 1.00178.09 O ANISOU 2359 O VAL A 379 14106 27876 25683 -3047 -101 -2410 O ATOM 2360 CB VAL A 379 14.653 23.444 -32.642 1.00129.49 C ANISOU 2360 CB VAL A 379 7383 22163 19655 -2047 -928 -2593 C ATOM 2361 CG1 VAL A 379 13.446 23.166 -31.761 1.00126.41 C ANISOU 2361 CG1 VAL A 379 7646 21378 19007 -1845 -1224 -2543 C ATOM 2362 CG2 VAL A 379 14.554 22.696 -33.967 1.00130.22 C ANISOU 2362 CG2 VAL A 379 7505 22261 19710 -1798 -448 -2541 C ATOM 2363 N PHE A 380 12.659 26.078 -32.950 1.00133.34 N ANISOU 2363 N PHE A 380 8972 21828 19863 -3101 -776 -2452 N ATOM 2364 CA PHE A 380 11.497 26.699 -33.582 1.00130.24 C ANISOU 2364 CA PHE A 380 9177 21016 19292 -3316 -554 -2337 C ATOM 2365 C PHE A 380 11.918 27.902 -34.419 1.00130.88 C ANISOU 2365 C PHE A 380 9117 21118 19492 -3884 -272 -2299 C ATOM 2366 O PHE A 380 11.505 28.046 -35.569 1.00130.26 O ANISOU 2366 O PHE A 380 9262 20904 19329 -3980 102 -2185 O ATOM 2367 CB PHE A 380 10.481 27.127 -32.518 1.00139.80 C ANISOU 2367 CB PHE A 380 10905 21870 20344 -3351 -888 -2346 C ATOM 2368 CG PHE A 380 9.193 27.669 -33.081 1.00137.66 C ANISOU 2368 CG PHE A 380 11248 21160 19895 -3491 -699 -2231 C ATOM 2369 CD1 PHE A 380 9.069 29.008 -33.417 1.00137.05 C ANISOU 2369 CD1 PHE A 380 11311 20898 19864 -3997 -595 -2197 C ATOM 2370 CD2 PHE A 380 8.100 26.838 -33.259 1.00135.96 C ANISOU 2370 CD2 PHE A 380 11472 20712 19475 -3116 -640 -2153 C ATOM 2371 CE1 PHE A 380 7.884 29.504 -33.927 1.00134.61 C ANISOU 2371 CE1 PHE A 380 11558 20187 19402 -4088 -446 -2082 C ATOM 2372 CE2 PHE A 380 6.911 27.328 -33.766 1.00133.49 C ANISOU 2372 CE2 PHE A 380 11685 20022 19012 -3230 -492 -2048 C ATOM 2373 CZ PHE A 380 6.803 28.663 -34.100 1.00132.70 C ANISOU 2373 CZ PHE A 380 11709 19748 18961 -3699 -401 -2009 C ATOM 2374 N LEU A 381 12.742 28.766 -33.833 1.00163.91 N ANISOU 2374 N LEU A 381 12949 25469 23862 -4275 -463 -2391 N ATOM 2375 CA LEU A 381 13.229 29.951 -34.530 1.00167.06 C ANISOU 2375 CA LEU A 381 13196 25887 24393 -4864 -218 -2356 C ATOM 2376 C LEU A 381 14.234 29.567 -35.611 1.00171.07 C ANISOU 2376 C LEU A 381 13163 26792 25045 -4878 176 -2337 C ATOM 2377 O LEU A 381 14.393 30.277 -36.604 1.00172.29 O ANISOU 2377 O LEU A 381 13318 26919 25225 -5272 535 -2247 O ATOM 2378 CB LEU A 381 13.860 30.941 -33.548 1.00157.68 C ANISOU 2378 CB LEU A 381 11771 24770 23371 -5295 -554 -2481 C ATOM 2379 CG LEU A 381 12.949 31.533 -32.469 1.00154.93 C ANISOU 2379 CG LEU A 381 11955 24028 22884 -5367 -919 -2527 C ATOM 2380 CD1 LEU A 381 13.723 32.505 -31.590 1.00159.16 C ANISOU 2380 CD1 LEU A 381 12340 24571 23561 -5728 -1228 -2601 C ATOM 2381 CD2 LEU A 381 11.739 32.214 -33.092 1.00151.13 C ANISOU 2381 CD2 LEU A 381 12141 23048 22234 -5526 -702 -2389 C ATOM 2382 N SER A 382 14.910 28.441 -35.410 1.00183.66 N ANISOU 2382 N SER A 382 14306 28749 26726 -4437 114 -2420 N ATOM 2383 CA SER A 382 15.878 27.944 -36.381 1.00187.86 C ANISOU 2383 CA SER A 382 14294 29686 27398 -4366 495 -2430 C ATOM 2384 C SER A 382 15.179 27.430 -37.638 1.00184.71 C ANISOU 2384 C SER A 382 14280 29113 26790 -4165 936 -2308 C ATOM 2385 O SER A 382 15.686 27.585 -38.749 1.00187.15 O ANISOU 2385 O SER A 382 14365 29605 27139 -4357 1373 -2265 O ATOM 2386 CB SER A 382 16.732 26.836 -35.762 1.00248.71 C ANISOU 2386 CB SER A 382 21484 37767 35249 -3865 273 -2539 C ATOM 2387 OG SER A 382 17.719 26.381 -36.672 1.00253.23 O ANISOU 2387 OG SER A 382 21607 38658 35952 -3735 639 -2517 O ATOM 2388 N THR A 383 14.013 26.817 -37.454 1.00142.75 N ANISOU 2388 N THR A 383 9546 23451 21240 -3794 821 -2256 N ATOM 2389 CA THR A 383 13.208 26.331 -38.571 1.00141.81 C ANISOU 2389 CA THR A 383 9861 23126 20894 -3609 1177 -2147 C ATOM 2390 C THR A 383 12.355 27.452 -39.155 1.00139.47 C ANISOU 2390 C THR A 383 10086 22457 20448 -4055 1329 -2001 C ATOM 2391 O THR A 383 11.774 27.312 -40.231 1.00138.60 O ANISOU 2391 O THR A 383 10313 22197 20150 -4029 1652 -1891 O ATOM 2392 CB THR A 383 12.282 25.177 -38.141 1.00165.57 C ANISOU 2392 CB THR A 383 13273 25915 23720 -3042 984 -2150 C ATOM 2393 OG1 THR A 383 11.420 25.620 -37.085 1.00163.34 O ANISOU 2393 OG1 THR A 383 13399 25309 23354 -3102 596 -2135 O ATOM 2394 CG2 THR A 383 13.098 23.990 -37.658 1.00167.73 C ANISOU 2394 CG2 THR A 383 13083 26519 24126 -2552 851 -2273 C ATOM 2395 N LEU A 384 12.290 28.564 -38.432 1.00209.53 N ANISOU 2395 N LEU A 384 19035 31176 29402 -4455 1080 -2003 N ATOM 2396 CA LEU A 384 11.484 29.717 -38.822 1.00207.96 C ANISOU 2396 CA LEU A 384 19342 30583 29090 -4869 1162 -1869 C ATOM 2397 C LEU A 384 12.114 30.498 -39.979 1.00210.95 C ANISOU 2397 C LEU A 384 19547 31080 29525 -5342 1580 -1772 C ATOM 2398 O LEU A 384 11.507 31.425 -40.516 1.00209.55 O ANISOU 2398 O LEU A 384 19797 30581 29243 -5682 1707 -1629 O ATOM 2399 CB LEU A 384 11.250 30.630 -37.614 1.00129.06 C ANISOU 2399 CB LEU A 384 9495 20372 19171 -5122 756 -1930 C ATOM 2400 CG LEU A 384 10.193 31.732 -37.736 1.00126.75 C ANISOU 2400 CG LEU A 384 9818 19587 18756 -5429 742 -1812 C ATOM 2401 CD1 LEU A 384 8.857 31.147 -38.173 1.00124.40 C ANISOU 2401 CD1 LEU A 384 10082 18982 18200 -5065 812 -1703 C ATOM 2402 CD2 LEU A 384 10.047 32.482 -36.423 1.00125.67 C ANISOU 2402 CD2 LEU A 384 9787 19267 18694 -5608 328 -1922 C ATOM 2403 N ALA A 385 13.334 30.127 -40.359 1.00202.08 N ANISOU 2403 N ALA A 385 17798 30419 28567 -5359 1798 -1844 N ATOM 2404 CA ALA A 385 14.025 30.809 -41.449 1.00206.49 C ANISOU 2404 CA ALA A 385 18139 31141 29177 -5819 2231 -1756 C ATOM 2405 C ALA A 385 13.275 30.659 -42.771 1.00204.73 C ANISOU 2405 C ALA A 385 18395 30721 28672 -5767 2622 -1587 C ATOM 2406 O ALA A 385 13.119 31.634 -43.507 1.00206.18 O ANISOU 2406 O ALA A 385 18832 30727 28782 -6220 2851 -1432 O ATOM 2407 CB ALA A 385 15.444 30.275 -41.585 1.00137.39 C ANISOU 2407 CB ALA A 385 8702 22871 20628 -5678 2367 -1835 C ATOM 2408 N CYS A 386 12.798 29.445 -43.044 1.00208.72 N ANISOU 2408 N CYS A 386 19050 31240 29012 -5222 2675 -1615 N ATOM 2409 CA CYS A 386 12.005 29.132 -44.238 1.00207.21 C ANISOU 2409 CA CYS A 386 19340 30866 28523 -5105 2993 -1481 C ATOM 2410 C CYS A 386 12.539 29.765 -45.525 1.00209.35 C ANISOU 2410 C CYS A 386 19538 31274 28731 -5533 3483 -1357 C ATOM 2411 O CYS A 386 12.048 30.805 -45.968 1.00208.03 O ANISOU 2411 O CYS A 386 19772 30815 28456 -5941 3556 -1182 O ATOM 2412 CB CYS A 386 10.543 29.535 -44.025 1.00202.70 C ANISOU 2412 CB CYS A 386 19489 29772 27755 -5090 2753 -1359 C ATOM 2413 SG CYS A 386 9.437 29.102 -45.391 1.00202.32 S ANISOU 2413 SG CYS A 386 20057 29487 27327 -4915 3047 -1199 S TER 2414 CYS A 386 ATOM 2415 N PRO B 51 -20.253 -30.055 -48.615 1.00182.30 N ANISOU 2415 N PRO B 51 28428 17288 23549 514 -1820 -5945 N ATOM 2416 CA PRO B 51 -21.296 -30.046 -47.584 1.00180.52 C ANISOU 2416 CA PRO B 51 28200 16819 23570 117 -2045 -5402 C ATOM 2417 C PRO B 51 -21.430 -28.668 -46.950 1.00177.53 C ANISOU 2417 C PRO B 51 27313 17050 23091 14 -1964 -4873 C ATOM 2418 O PRO B 51 -20.744 -27.735 -47.367 1.00177.14 O ANISOU 2418 O PRO B 51 26941 17583 22782 213 -1757 -4927 O ATOM 2419 CB PRO B 51 -20.770 -31.043 -46.549 1.00212.99 C ANISOU 2419 CB PRO B 51 32561 20237 28128 480 -2110 -5306 C ATOM 2420 CG PRO B 51 -19.870 -31.946 -47.317 1.00215.34 C ANISOU 2420 CG PRO B 51 33158 20213 28449 925 -2028 -5930 C ATOM 2421 CD PRO B 51 -19.229 -31.082 -48.359 1.00215.34 C ANISOU 2421 CD PRO B 51 32848 20938 28032 1081 -1761 -6250 C ATOM 2422 N ASN B 52 -22.308 -28.541 -45.960 1.00134.72 N ANISOU 2422 N ASN B 52 21829 11490 17868 -308 -2111 -4379 N ATOM 2423 CA ASN B 52 -22.473 -27.270 -45.267 1.00131.81 C ANISOU 2423 CA ASN B 52 21004 11644 17432 -390 -2038 -3890 C ATOM 2424 C ASN B 52 -22.064 -27.393 -43.800 1.00130.59 C ANISOU 2424 C ASN B 52 20802 11231 17584 -141 -2029 -3486 C ATOM 2425 O ASN B 52 -22.608 -26.717 -42.926 1.00128.35 O ANISOU 2425 O ASN B 52 20286 11137 17344 -346 -2044 -3023 O ATOM 2426 CB ASN B 52 -23.926 -26.799 -45.391 1.00125.17 C ANISOU 2426 CB ASN B 52 20051 11001 16505 -997 -2195 -3652 C ATOM 2427 CG ASN B 52 -24.092 -25.320 -45.112 1.00122.23 C ANISOU 2427 CG ASN B 52 19200 11273 15968 -1069 -2107 -3285 C ATOM 2428 OD1 ASN B 52 -24.644 -24.928 -44.084 1.00120.10 O ANISOU 2428 OD1 ASN B 52 18748 11028 15858 -1226 -2135 -2847 O ATOM 2429 ND2 ASN B 52 -23.617 -24.489 -46.030 1.00121.97 N ANISOU 2429 ND2 ASN B 52 18982 11757 15604 -963 -1991 -3467 N ATOM 2430 N SER B 53 -21.088 -28.260 -43.546 1.00216.46 N ANISOU 2430 N SER B 53 31908 21677 28662 323 -2010 -3678 N ATOM 2431 CA SER B 53 -20.590 -28.502 -42.196 1.00215.76 C ANISOU 2431 CA SER B 53 31838 21293 28848 614 -2046 -3322 C ATOM 2432 C SER B 53 -19.313 -27.723 -41.898 1.00215.14 C ANISOU 2432 C SER B 53 31382 21643 28719 1121 -1880 -3292 C ATOM 2433 O SER B 53 -18.707 -27.896 -40.840 1.00214.99 O ANISOU 2433 O SER B 53 31356 21427 28904 1441 -1927 -3045 O ATOM 2434 CB SER B 53 -20.347 -29.997 -41.978 1.00150.94 C ANISOU 2434 CB SER B 53 24139 12268 20942 823 -2192 -3498 C ATOM 2435 OG SER B 53 -19.360 -30.485 -42.869 1.00153.07 O ANISOU 2435 OG SER B 53 24509 12451 21198 1273 -2108 -4050 O ATOM 2436 N ASP B 54 -18.906 -26.866 -42.828 1.00132.41 N ANISOU 2436 N ASP B 54 20597 11753 17961 1171 -1698 -3532 N ATOM 2437 CA ASP B 54 -17.680 -26.093 -42.664 1.00131.91 C ANISOU 2437 CA ASP B 54 20141 12133 17844 1598 -1519 -3541 C ATOM 2438 C ASP B 54 -17.862 -24.947 -41.677 1.00129.62 C ANISOU 2438 C ASP B 54 19503 12224 17522 1468 -1513 -3027 C ATOM 2439 O ASP B 54 -16.892 -24.312 -41.263 1.00128.84 O ANISOU 2439 O ASP B 54 19084 12438 17433 1790 -1412 -2952 O ATOM 2440 CB ASP B 54 -17.226 -25.535 -44.014 1.00221.92 C ANISOU 2440 CB ASP B 54 31353 24042 28925 1629 -1298 -3949 C ATOM 2441 CG ASP B 54 -17.056 -26.615 -45.064 1.00224.49 C ANISOU 2441 CG ASP B 54 32030 24037 29226 1751 -1277 -4514 C ATOM 2442 OD1 ASP B 54 -16.201 -27.505 -44.872 1.00226.72 O ANISOU 2442 OD1 ASP B 54 32454 23933 29756 2223 -1272 -4759 O ATOM 2443 OD2 ASP B 54 -17.779 -26.574 -46.081 1.00224.99 O ANISOU 2443 OD2 ASP B 54 32237 24224 29023 1389 -1280 -4724 O ATOM 2444 N LEU B 55 -19.109 -24.689 -41.299 1.00113.72 N ANISOU 2444 N LEU B 55 17540 10187 15480 993 -1620 -2696 N ATOM 2445 CA LEU B 55 -19.421 -23.573 -40.414 1.00111.69 C ANISOU 2445 CA LEU B 55 16971 10293 15174 838 -1602 -2242 C ATOM 2446 C LEU B 55 -19.850 -24.061 -39.034 1.00110.66 C ANISOU 2446 C LEU B 55 17023 9758 15266 779 -1740 -1842 C ATOM 2447 O LEU B 55 -20.229 -23.265 -38.175 1.00109.07 O ANISOU 2447 O LEU B 55 16621 9792 15029 629 -1729 -1463 O ATOM 2448 CB LEU B 55 -20.502 -22.676 -41.027 1.00107.08 C ANISOU 2448 CB LEU B 55 16219 10105 14361 362 -1584 -2157 C ATOM 2449 CG LEU B 55 -20.092 -21.698 -42.138 1.00107.36 C ANISOU 2449 CG LEU B 55 15989 10702 14100 376 -1435 -2373 C ATOM 2450 CD1 LEU B 55 -19.593 -22.402 -43.391 1.00109.49 C ANISOU 2450 CD1 LEU B 55 16459 10891 14253 514 -1371 -2886 C ATOM 2451 CD2 LEU B 55 -21.252 -20.782 -42.483 1.00105.80 C ANISOU 2451 CD2 LEU B 55 15638 10837 13724 -75 -1485 -2181 C ATOM 2452 N ASP B 56 -19.794 -25.374 -38.830 1.00117.96 N ANISOU 2452 N ASP B 56 18353 10061 16404 893 -1866 -1931 N ATOM 2453 CA ASP B 56 -20.162 -25.968 -37.549 1.00117.26 C ANISOU 2453 CA ASP B 56 18517 9530 16506 827 -1999 -1541 C ATOM 2454 C ASP B 56 -19.089 -25.721 -36.496 1.00116.49 C ANISOU 2454 C ASP B 56 18295 9487 16478 1282 -2020 -1328 C ATOM 2455 O ASP B 56 -17.905 -25.957 -36.736 1.00116.73 O ANISOU 2455 O ASP B 56 18272 9494 16584 1773 -2018 -1586 O ATOM 2456 CB ASP B 56 -20.405 -27.472 -37.693 1.00140.51 C ANISOU 2456 CB ASP B 56 21985 11738 19666 802 -2148 -1694 C ATOM 2457 CG ASP B 56 -21.623 -27.789 -38.536 1.00141.31 C ANISOU 2457 CG ASP B 56 22239 11732 19720 267 -2178 -1847 C ATOM 2458 OD1 ASP B 56 -22.527 -26.933 -38.621 1.00140.63 O ANISOU 2458 OD1 ASP B 56 21884 12065 19482 -143 -2122 -1675 O ATOM 2459 OD2 ASP B 56 -21.674 -28.894 -39.118 1.00142.91 O ANISOU 2459 OD2 ASP B 56 22825 11426 20049 268 -2275 -2153 O ATOM 2460 N VAL B 57 -19.512 -25.245 -35.330 1.00139.76 N ANISOU 2460 N VAL B 57 21182 12526 19394 1115 -2042 -875 N ATOM 2461 CA VAL B 57 -18.600 -25.036 -34.213 1.00138.67 C ANISOU 2461 CA VAL B 57 20971 12422 19296 1496 -2110 -634 C ATOM 2462 C VAL B 57 -18.684 -26.210 -33.242 1.00138.77 C ANISOU 2462 C VAL B 57 21464 11777 19484 1563 -2301 -375 C ATOM 2463 O VAL B 57 -19.731 -26.463 -32.645 1.00138.34 O ANISOU 2463 O VAL B 57 21638 11511 19415 1145 -2317 -60 O ATOM 2464 CB VAL B 57 -18.905 -23.726 -33.473 1.00119.36 C ANISOU 2464 CB VAL B 57 18186 10502 16664 1308 -2018 -309 C ATOM 2465 CG1 VAL B 57 -18.036 -23.604 -32.234 1.00117.73 C ANISOU 2465 CG1 VAL B 57 17965 10290 16478 1661 -2130 -49 C ATOM 2466 CG2 VAL B 57 -18.696 -22.536 -34.399 1.00119.19 C ANISOU 2466 CG2 VAL B 57 17718 11091 16480 1280 -1853 -537 C ATOM 2467 N ASN B 58 -17.574 -26.922 -33.090 1.00174.98 N ANISOU 2467 N ASN B 58 26197 16043 24243 2092 -2446 -503 N ATOM 2468 CA ASN B 58 -17.557 -28.165 -32.327 1.00175.90 C ANISOU 2468 CA ASN B 58 26838 15445 24551 2214 -2667 -295 C ATOM 2469 C ASN B 58 -17.232 -28.010 -30.844 1.00174.11 C ANISOU 2469 C ASN B 58 26687 15191 24276 2364 -2812 180 C ATOM 2470 O ASN B 58 -16.238 -28.551 -30.360 1.00174.72 O ANISOU 2470 O ASN B 58 26901 14989 24497 2871 -3021 203 O ATOM 2471 CB ASN B 58 -16.601 -29.172 -32.970 1.00178.15 C ANISOU 2471 CB ASN B 58 27313 15294 25084 2734 -2787 -699 C ATOM 2472 CG ASN B 58 -17.032 -29.571 -34.367 1.00180.64 C ANISOU 2472 CG ASN B 58 27704 15504 25429 2547 -2672 -1165 C ATOM 2473 OD1 ASN B 58 -18.221 -29.563 -34.688 1.00180.42 O ANISOU 2473 OD1 ASN B 58 27788 15451 25312 1985 -2601 -1109 O ATOM 2474 ND2 ASN B 58 -16.066 -29.925 -35.206 1.00182.82 N ANISOU 2474 ND2 ASN B 58 27907 15733 25823 3020 -2653 -1644 N ATOM 2475 N THR B 59 -18.073 -27.274 -30.127 1.00124.83 N ANISOU 2475 N THR B 59 20356 9250 17824 1936 -2709 545 N ATOM 2476 CA THR B 59 -17.964 -27.209 -28.675 1.00123.46 C ANISOU 2476 CA THR B 59 20347 9016 17546 1983 -2833 1018 C ATOM 2477 C THR B 59 -18.874 -28.281 -28.084 1.00124.47 C ANISOU 2477 C THR B 59 21054 8515 17722 1630 -2908 1349 C ATOM 2478 O THR B 59 -20.028 -28.411 -28.490 1.00124.98 O ANISOU 2478 O THR B 59 21190 8517 17779 1103 -2756 1351 O ATOM 2479 CB THR B 59 -18.338 -25.818 -28.126 1.00129.83 C ANISOU 2479 CB THR B 59 20764 10488 18079 1732 -2662 1224 C ATOM 2480 OG1 THR B 59 -19.631 -25.438 -28.613 1.00129.83 O ANISOU 2480 OG1 THR B 59 20660 10671 17999 1166 -2436 1215 O ATOM 2481 CG2 THR B 59 -17.317 -24.779 -28.564 1.00128.59 C ANISOU 2481 CG2 THR B 59 20079 10898 17883 2087 -2621 948 C ATOM 2482 N ASP B 60 -18.346 -29.055 -27.138 1.00129.79 N ANISOU 2482 N ASP B 60 22140 8724 18452 1911 -3156 1636 N ATOM 2483 CA ASP B 60 -19.061 -30.213 -26.601 1.00131.42 C ANISOU 2483 CA ASP B 60 22972 8233 18728 1613 -3255 1960 C ATOM 2484 C ASP B 60 -20.404 -29.854 -25.970 1.00130.57 C ANISOU 2484 C ASP B 60 22917 8299 18396 923 -3033 2336 C ATOM 2485 O ASP B 60 -20.638 -28.707 -25.587 1.00128.59 O ANISOU 2485 O ASP B 60 22278 8675 17904 777 -2858 2439 O ATOM 2486 CB ASP B 60 -18.190 -30.974 -25.596 1.00170.52 C ANISOU 2486 CB ASP B 60 28199 12890 23699 2027 -3495 2218 C ATOM 2487 CG ASP B 60 -17.865 -30.152 -24.366 1.00168.75 C ANISOU 2487 CG ASP B 60 27837 13099 23180 2112 -3536 2584 C ATOM 2488 OD1 ASP B 60 -17.094 -29.178 -24.485 1.00165.83 O ANISOU 2488 OD1 ASP B 60 27074 13170 22762 2464 -3592 2422 O ATOM 2489 OD2 ASP B 60 -18.380 -30.484 -23.277 1.00170.88 O ANISOU 2489 OD2 ASP B 60 28388 13281 23256 1817 -3505 3020 O ATOM 2490 N ILE B 61 -21.279 -30.850 -25.866 1.00164.56 N ANISOU 2490 N ILE B 61 27674 12059 22791 498 -3023 2517 N ATOM 2491 CA ILE B 61 -22.632 -30.651 -25.358 1.00164.20 C ANISOU 2491 CA ILE B 61 27671 12137 22582 -201 -2786 2842 C ATOM 2492 C ILE B 61 -22.636 -30.228 -23.889 1.00163.74 C ANISOU 2492 C ILE B 61 27647 12364 22204 -245 -2722 3319 C ATOM 2493 O ILE B 61 -23.427 -29.376 -23.482 1.00160.73 O ANISOU 2493 O ILE B 61 27075 12387 21607 -642 -2501 3508 O ATOM 2494 CB ILE B 61 -23.499 -31.923 -25.555 1.00140.79 C ANISOU 2494 CB ILE B 61 25036 8669 19788 -642 -2725 2876 C ATOM 2495 CG1 ILE B 61 -24.858 -31.769 -24.869 1.00141.48 C ANISOU 2495 CG1 ILE B 61 25116 8932 19708 -1350 -2452 3239 C ATOM 2496 CG2 ILE B 61 -22.772 -33.161 -25.044 1.00147.22 C ANISOU 2496 CG2 ILE B 61 26241 8986 20711 -291 -2917 2990 C ATOM 2497 CD1 ILE B 61 -25.854 -30.950 -25.663 1.00138.56 C ANISOU 2497 CD1 ILE B 61 24388 8902 19355 -1825 -2267 3056 C ATOM 2498 N TYR B 62 -21.737 -30.813 -23.105 1.00187.28 N ANISOU 2498 N TYR B 62 30847 15164 25149 173 -2915 3486 N ATOM 2499 CA TYR B 62 -21.683 -30.559 -21.670 1.00188.25 C ANISOU 2499 CA TYR B 62 31066 15517 24944 144 -2889 3926 C ATOM 2500 C TYR B 62 -21.334 -29.105 -21.368 1.00182.63 C ANISOU 2500 C TYR B 62 29984 15421 23985 305 -2857 3926 C ATOM 2501 O TYR B 62 -21.929 -28.483 -20.487 1.00180.96 O ANISOU 2501 O TYR B 62 29742 15550 23464 -11 -2670 4218 O ATOM 2502 CB TYR B 62 -20.671 -31.491 -21.000 1.00175.16 C ANISOU 2502 CB TYR B 62 29699 13530 23324 608 -3164 4062 C ATOM 2503 CG TYR B 62 -20.908 -32.958 -21.280 1.00182.03 C ANISOU 2503 CG TYR B 62 30961 13748 24453 506 -3226 4061 C ATOM 2504 CD1 TYR B 62 -21.786 -33.702 -20.503 1.00186.86 C ANISOU 2504 CD1 TYR B 62 31930 14108 24960 30 -3097 4445 C ATOM 2505 CD2 TYR B 62 -20.249 -33.599 -22.321 1.00183.65 C ANISOU 2505 CD2 TYR B 62 31176 13595 25006 886 -3400 3663 C ATOM 2506 CE1 TYR B 62 -22.003 -35.044 -20.758 1.00193.15 C ANISOU 2506 CE1 TYR B 62 33095 14286 26005 -75 -3163 4448 C ATOM 2507 CE2 TYR B 62 -20.459 -34.939 -22.583 1.00189.97 C ANISOU 2507 CE2 TYR B 62 32350 13782 26046 799 -3461 3643 C ATOM 2508 CZ TYR B 62 -21.336 -35.657 -21.798 1.00194.89 C ANISOU 2508 CZ TYR B 62 33337 14138 26574 314 -3354 4045 C ATOM 2509 OH TYR B 62 -21.547 -36.992 -22.057 1.00202.35 O ANISOU 2509 OH TYR B 62 34664 14449 27770 215 -3423 4031 O ATOM 2510 N SER B 63 -20.369 -28.568 -22.107 1.00139.84 N ANISOU 2510 N SER B 63 24276 10153 18705 796 -3027 3579 N ATOM 2511 CA SER B 63 -19.937 -27.188 -21.921 1.00136.59 C ANISOU 2511 CA SER B 63 23396 10408 18094 975 -2975 3495 C ATOM 2512 C SER B 63 -21.019 -26.197 -22.342 1.00135.05 C ANISOU 2512 C SER B 63 22766 10748 17800 484 -2597 3371 C ATOM 2513 O SER B 63 -21.129 -25.112 -21.772 1.00133.33 O ANISOU 2513 O SER B 63 22263 11068 17328 415 -2459 3452 O ATOM 2514 CB SER B 63 -18.641 -26.922 -22.690 1.00124.30 C ANISOU 2514 CB SER B 63 21485 9004 16739 1584 -3161 3078 C ATOM 2515 OG SER B 63 -18.819 -27.127 -24.080 1.00124.67 O ANISOU 2515 OG SER B 63 21337 8980 17053 1544 -3053 2652 O ATOM 2516 N LYS B 64 -21.814 -26.573 -23.340 1.00124.59 N ANISOU 2516 N LYS B 64 21396 9261 16683 159 -2455 3163 N ATOM 2517 CA LYS B 64 -22.933 -25.745 -23.779 1.00123.47 C ANISOU 2517 CA LYS B 64 20855 9573 16483 -314 -2136 3059 C ATOM 2518 C LYS B 64 -23.986 -25.654 -22.681 1.00123.16 C ANISOU 2518 C LYS B 64 20976 9611 16207 -806 -1922 3477 C ATOM 2519 O LYS B 64 -24.526 -24.582 -22.412 1.00121.72 O ANISOU 2519 O LYS B 64 20427 9975 15847 -1001 -1688 3492 O ATOM 2520 CB LYS B 64 -23.564 -26.307 -25.055 1.00122.36 C ANISOU 2520 CB LYS B 64 20683 9195 16612 -569 -2087 2761 C ATOM 2521 CG LYS B 64 -22.687 -26.221 -26.293 1.00122.70 C ANISOU 2521 CG LYS B 64 20491 9288 16840 -154 -2208 2286 C ATOM 2522 CD LYS B 64 -23.446 -26.703 -27.520 1.00124.32 C ANISOU 2522 CD LYS B 64 20681 9311 17243 -472 -2149 1992 C ATOM 2523 CE LYS B 64 -22.610 -26.579 -28.782 1.00125.06 C ANISOU 2523 CE LYS B 64 20552 9504 17462 -87 -2227 1504 C ATOM 2524 NZ LYS B 64 -22.114 -25.190 -28.986 1.00123.64 N ANISOU 2524 NZ LYS B 64 19837 10010 17128 125 -2126 1364 N ATOM 2525 N VAL B 65 -24.274 -26.792 -22.057 1.00148.57 N ANISOU 2525 N VAL B 65 24756 12268 19427 -1005 -1993 3810 N ATOM 2526 CA VAL B 65 -25.236 -26.855 -20.964 1.00149.02 C ANISOU 2526 CA VAL B 65 25032 12354 19236 -1498 -1768 4239 C ATOM 2527 C VAL B 65 -24.735 -26.065 -19.758 1.00147.71 C ANISOU 2527 C VAL B 65 24857 12575 18693 -1282 -1764 4478 C ATOM 2528 O VAL B 65 -25.504 -25.369 -19.094 1.00146.83 O ANISOU 2528 O VAL B 65 24584 12876 18327 -1615 -1471 4635 O ATOM 2529 CB VAL B 65 -25.515 -28.316 -20.548 1.00126.98 C ANISOU 2529 CB VAL B 65 22796 8927 16524 -1710 -1832 4510 C ATOM 2530 CG1 VAL B 65 -26.435 -28.370 -19.337 1.00129.13 C ANISOU 2530 CG1 VAL B 65 23172 9384 16508 -2171 -1530 4902 C ATOM 2531 CG2 VAL B 65 -26.111 -29.093 -21.713 1.00128.13 C ANISOU 2531 CG2 VAL B 65 22964 8689 17032 -1987 -1829 4258 C ATOM 2532 N LEU B 66 -23.437 -26.173 -19.490 1.00139.81 N ANISOU 2532 N LEU B 66 24013 11449 17661 -714 -2096 4477 N ATOM 2533 CA LEU B 66 -22.811 -25.459 -18.382 1.00138.47 C ANISOU 2533 CA LEU B 66 23851 11626 17136 -462 -2171 4669 C ATOM 2534 C LEU B 66 -22.943 -23.945 -18.533 1.00135.73 C ANISOU 2534 C LEU B 66 22887 12017 16666 -463 -1949 4414 C ATOM 2535 O LEU B 66 -23.343 -23.253 -17.597 1.00135.09 O ANISOU 2535 O LEU B 66 22777 12302 16249 -648 -1762 4601 O ATOM 2536 CB LEU B 66 -21.336 -25.851 -18.261 1.00142.13 C ANISOU 2536 CB LEU B 66 24426 11898 17679 186 -2582 4602 C ATOM 2537 CG LEU B 66 -20.519 -25.127 -17.189 1.00141.69 C ANISOU 2537 CG LEU B 66 24303 12240 17292 500 -2722 4723 C ATOM 2538 CD1 LEU B 66 -21.115 -25.362 -15.810 1.00144.68 C ANISOU 2538 CD1 LEU B 66 24990 12690 17290 175 -2557 5126 C ATOM 2539 CD2 LEU B 66 -19.066 -25.575 -17.232 1.00143.13 C ANISOU 2539 CD2 LEU B 66 24472 12267 17645 1130 -3121 4587 C ATOM 2540 N VAL B 67 -22.602 -23.438 -19.713 1.00129.42 N ANISOU 2540 N VAL B 67 21624 11419 16130 -257 -1968 3984 N ATOM 2541 CA VAL B 67 -22.692 -22.008 -19.994 1.00127.70 C ANISOU 2541 CA VAL B 67 20838 11841 15841 -246 -1787 3730 C ATOM 2542 C VAL B 67 -24.141 -21.524 -20.000 1.00127.75 C ANISOU 2542 C VAL B 67 20634 12119 15785 -786 -1401 3767 C ATOM 2543 O VAL B 67 -24.441 -20.427 -19.523 1.00126.49 O ANISOU 2543 O VAL B 67 20201 12440 15420 -860 -1212 3757 O ATOM 2544 CB VAL B 67 -22.011 -21.659 -21.337 1.00104.22 C ANISOU 2544 CB VAL B 67 17461 8984 13155 63 -1890 3286 C ATOM 2545 CG1 VAL B 67 -22.253 -20.205 -21.708 1.00101.87 C ANISOU 2545 CG1 VAL B 67 16615 9292 12800 2 -1690 3056 C ATOM 2546 CG2 VAL B 67 -20.524 -21.943 -21.257 1.00103.95 C ANISOU 2546 CG2 VAL B 67 17515 8800 13180 629 -2237 3215 C ATOM 2547 N THR B 68 -25.038 -22.351 -20.527 1.00131.12 N ANISOU 2547 N THR B 68 21184 12229 16407 -1158 -1294 3794 N ATOM 2548 CA THR B 68 -26.457 -22.018 -20.556 1.00131.39 C ANISOU 2548 CA THR B 68 20990 12501 16433 -1687 -944 3830 C ATOM 2549 C THR B 68 -27.000 -21.873 -19.139 1.00131.98 C ANISOU 2549 C THR B 68 21273 12721 16153 -1948 -722 4199 C ATOM 2550 O THR B 68 -27.765 -20.954 -18.850 1.00131.43 O ANISOU 2550 O THR B 68 20866 13113 15958 -2162 -427 4168 O ATOM 2551 CB THR B 68 -27.277 -23.079 -21.314 1.00119.49 C ANISOU 2551 CB THR B 68 19619 10576 15206 -2070 -912 3811 C ATOM 2552 OG1 THR B 68 -26.727 -23.264 -22.625 1.00119.46 O ANISOU 2552 OG1 THR B 68 19474 10429 15485 -1814 -1120 3448 O ATOM 2553 CG2 THR B 68 -28.730 -22.644 -21.438 1.00119.44 C ANISOU 2553 CG2 THR B 68 19261 10885 15234 -2599 -570 3802 C ATOM 2554 N ALA B 69 -26.590 -22.779 -18.256 1.00122.37 N ANISOU 2554 N ALA B 69 20626 11105 14765 -1911 -867 4544 N ATOM 2555 CA ALA B 69 -27.002 -22.730 -16.857 1.00123.14 C ANISOU 2555 CA ALA B 69 21013 11319 14457 -2151 -671 4926 C ATOM 2556 C ALA B 69 -26.486 -21.457 -16.194 1.00121.50 C ANISOU 2556 C ALA B 69 20570 11652 13940 -1863 -646 4844 C ATOM 2557 O ALA B 69 -27.186 -20.831 -15.398 1.00122.32 O ANISOU 2557 O ALA B 69 20591 12127 13757 -2118 -330 4951 O ATOM 2558 CB ALA B 69 -26.508 -23.961 -16.111 1.00111.43 C ANISOU 2558 CB ALA B 69 20238 9261 12839 -2109 -909 5325 C ATOM 2559 N ILE B 70 -25.255 -21.082 -16.527 1.00121.28 N ANISOU 2559 N ILE B 70 20430 11669 13981 -1338 -973 4634 N ATOM 2560 CA ILE B 70 -24.661 -19.853 -16.017 1.00119.80 C ANISOU 2560 CA ILE B 70 20000 11967 13551 -1057 -999 4508 C ATOM 2561 C ILE B 70 -25.401 -18.624 -16.544 1.00118.63 C ANISOU 2561 C ILE B 70 19265 12320 13489 -1209 -694 4207 C ATOM 2562 O ILE B 70 -25.733 -17.717 -15.781 1.00118.28 O ANISOU 2562 O ILE B 70 19102 12674 13164 -1286 -483 4219 O ATOM 2563 CB ILE B 70 -23.162 -19.762 -16.374 1.00 98.09 C ANISOU 2563 CB ILE B 70 17200 9150 10920 -489 -1422 4327 C ATOM 2564 CG1 ILE B 70 -22.369 -20.813 -15.593 1.00101.43 C ANISOU 2564 CG1 ILE B 70 18203 9138 11199 -268 -1761 4653 C ATOM 2565 CG2 ILE B 70 -22.623 -18.370 -16.084 1.00 95.55 C ANISOU 2565 CG2 ILE B 70 16525 9355 10427 -257 -1433 4121 C ATOM 2566 CD1 ILE B 70 -20.876 -20.768 -15.841 1.00100.52 C ANISOU 2566 CD1 ILE B 70 18008 8974 11210 312 -2189 4483 C ATOM 2567 N TYR B 71 -25.666 -18.609 -17.848 1.00109.83 N ANISOU 2567 N TYR B 71 17808 11169 12753 -1242 -682 3934 N ATOM 2568 CA TYR B 71 -26.381 -17.501 -18.478 1.00108.74 C ANISOU 2568 CA TYR B 71 17123 11455 12737 -1366 -445 3660 C ATOM 2569 C TYR B 71 -27.773 -17.309 -17.883 1.00110.22 C ANISOU 2569 C TYR B 71 17231 11850 12796 -1822 -42 3800 C ATOM 2570 O TYR B 71 -28.170 -16.186 -17.572 1.00109.38 O ANISOU 2570 O TYR B 71 16814 12175 12573 -1836 168 3683 O ATOM 2571 CB TYR B 71 -26.498 -17.715 -19.990 1.00117.09 C ANISOU 2571 CB TYR B 71 17911 12388 14191 -1368 -527 3390 C ATOM 2572 CG TYR B 71 -25.276 -17.308 -20.785 1.00115.70 C ANISOU 2572 CG TYR B 71 17560 12254 14148 -924 -801 3118 C ATOM 2573 CD1 TYR B 71 -24.030 -17.194 -20.182 1.00114.91 C ANISOU 2573 CD1 TYR B 71 17622 12147 13890 -540 -1037 3159 C ATOM 2574 CD2 TYR B 71 -25.373 -17.031 -22.143 1.00115.16 C ANISOU 2574 CD2 TYR B 71 17150 12255 14349 -907 -823 2820 C ATOM 2575 CE1 TYR B 71 -22.915 -16.821 -20.912 1.00113.18 C ANISOU 2575 CE1 TYR B 71 17192 12001 13811 -163 -1256 2902 C ATOM 2576 CE2 TYR B 71 -24.266 -16.657 -22.879 1.00113.88 C ANISOU 2576 CE2 TYR B 71 16824 12160 14285 -538 -1026 2576 C ATOM 2577 CZ TYR B 71 -23.041 -16.554 -22.260 1.00112.66 C ANISOU 2577 CZ TYR B 71 16797 12008 14002 -173 -1227 2613 C ATOM 2578 OH TYR B 71 -21.938 -16.182 -22.992 1.00111.39 O ANISOU 2578 OH TYR B 71 16423 11943 13955 168 -1400 2363 O ATOM 2579 N LEU B 72 -28.508 -18.407 -17.732 1.00121.21 N ANISOU 2579 N LEU B 72 18897 12928 14229 -2197 72 4037 N ATOM 2580 CA LEU B 72 -29.858 -18.359 -17.179 1.00122.67 C ANISOU 2580 CA LEU B 72 18987 13305 14315 -2678 484 4181 C ATOM 2581 C LEU B 72 -29.851 -17.854 -15.741 1.00123.51 C ANISOU 2581 C LEU B 72 19284 13688 13957 -2684 682 4376 C ATOM 2582 O LEU B 72 -30.729 -17.092 -15.338 1.00124.06 O ANISOU 2582 O LEU B 72 19058 14161 13918 -2883 1041 4317 O ATOM 2583 CB LEU B 72 -30.520 -19.738 -17.245 1.00116.63 C ANISOU 2583 CB LEU B 72 18542 12097 13675 -3107 542 4430 C ATOM 2584 CG LEU B 72 -30.858 -20.291 -18.632 1.00116.75 C ANISOU 2584 CG LEU B 72 18363 11859 14137 -3235 417 4224 C ATOM 2585 CD1 LEU B 72 -31.508 -21.661 -18.519 1.00118.85 C ANISOU 2585 CD1 LEU B 72 19006 11655 14495 -3702 478 4494 C ATOM 2586 CD2 LEU B 72 -31.753 -19.329 -19.400 1.00115.96 C ANISOU 2586 CD2 LEU B 72 17608 12200 14251 -3362 608 3924 C ATOM 2587 N ALA B 73 -28.855 -18.284 -14.972 1.00137.84 N ANISOU 2587 N ALA B 73 21593 15288 15491 -2449 436 4595 N ATOM 2588 CA ALA B 73 -28.715 -17.855 -13.586 1.00138.82 C ANISOU 2588 CA ALA B 73 21974 15658 15112 -2431 562 4783 C ATOM 2589 C ALA B 73 -28.387 -16.368 -13.504 1.00137.16 C ANISOU 2589 C ALA B 73 21371 15936 14806 -2134 589 4466 C ATOM 2590 O ALA B 73 -28.982 -15.635 -12.715 1.00138.37 O ANISOU 2590 O ALA B 73 21432 16465 14678 -2273 914 4452 O ATOM 2591 CB ALA B 73 -27.649 -18.677 -12.880 1.00120.58 C ANISOU 2591 CB ALA B 73 20284 12984 12548 -2208 204 5086 C ATOM 2592 N LEU B 74 -27.439 -15.929 -14.326 1.00137.57 N ANISOU 2592 N LEU B 74 21202 15973 15097 -1737 259 4203 N ATOM 2593 CA LEU B 74 -27.065 -14.521 -14.382 1.00136.16 C ANISOU 2593 CA LEU B 74 20653 16199 14884 -1469 248 3894 C ATOM 2594 C LEU B 74 -28.205 -13.681 -14.947 1.00136.33 C ANISOU 2594 C LEU B 74 20151 16530 15119 -1668 590 3656 C ATOM 2595 O LEU B 74 -28.306 -12.487 -14.665 1.00136.41 O ANISOU 2595 O LEU B 74 19906 16899 15024 -1562 719 3456 O ATOM 2596 CB LEU B 74 -25.799 -14.328 -15.218 1.00 96.45 C ANISOU 2596 CB LEU B 74 15494 11065 10088 -1050 -163 3685 C ATOM 2597 CG LEU B 74 -24.519 -14.949 -14.656 1.00 96.21 C ANISOU 2597 CG LEU B 74 15884 10795 9878 -750 -554 3858 C ATOM 2598 CD1 LEU B 74 -23.375 -14.792 -15.641 1.00 94.28 C ANISOU 2598 CD1 LEU B 74 15408 10476 9938 -367 -900 3611 C ATOM 2599 CD2 LEU B 74 -24.165 -14.324 -13.317 1.00 96.91 C ANISOU 2599 CD2 LEU B 74 16185 11145 9491 -664 -564 3947 C ATOM 2600 N PHE B 75 -29.056 -14.310 -15.751 1.00118.63 N ANISOU 2600 N PHE B 75 17752 14132 13189 -1947 708 3670 N ATOM 2601 CA PHE B 75 -30.241 -13.647 -16.277 1.00118.99 C ANISOU 2601 CA PHE B 75 17294 14458 13459 -2158 1009 3477 C ATOM 2602 C PHE B 75 -31.201 -13.353 -15.132 1.00120.99 C ANISOU 2602 C PHE B 75 17552 15002 13418 -2429 1443 3589 C ATOM 2603 O PHE B 75 -31.643 -12.220 -14.958 1.00121.29 O ANISOU 2603 O PHE B 75 17244 15410 13429 -2361 1651 3376 O ATOM 2604 CB PHE B 75 -30.926 -14.514 -17.335 1.00100.88 C ANISOU 2604 CB PHE B 75 14865 11920 11543 -2431 1001 3484 C ATOM 2605 CG PHE B 75 -32.174 -13.901 -17.909 1.00100.96 C ANISOU 2605 CG PHE B 75 14331 12219 11810 -2648 1260 3297 C ATOM 2606 CD1 PHE B 75 -32.094 -12.956 -18.921 1.00 99.44 C ANISOU 2606 CD1 PHE B 75 13711 12202 11872 -2422 1128 2995 C ATOM 2607 CD2 PHE B 75 -33.425 -14.272 -17.443 1.00102.59 C ANISOU 2607 CD2 PHE B 75 14445 12526 12007 -3083 1628 3433 C ATOM 2608 CE1 PHE B 75 -33.237 -12.390 -19.453 1.00 99.76 C ANISOU 2608 CE1 PHE B 75 13249 12496 12158 -2587 1316 2836 C ATOM 2609 CE2 PHE B 75 -34.572 -13.709 -17.971 1.00103.04 C ANISOU 2609 CE2 PHE B 75 13949 12869 12334 -3256 1841 3249 C ATOM 2610 CZ PHE B 75 -34.478 -12.768 -18.978 1.00101.60 C ANISOU 2610 CZ PHE B 75 13351 12841 12409 -2988 1664 2952 C ATOM 2611 N VAL B 76 -31.520 -14.386 -14.357 1.00112.35 N ANISOU 2611 N VAL B 76 16864 13724 12099 -2736 1586 3922 N ATOM 2612 CA VAL B 76 -32.418 -14.249 -13.216 1.00115.10 C ANISOU 2612 CA VAL B 76 17271 14348 12115 -3041 2042 4062 C ATOM 2613 C VAL B 76 -31.872 -13.262 -12.188 1.00115.30 C ANISOU 2613 C VAL B 76 17421 14679 11707 -2771 2083 3980 C ATOM 2614 O VAL B 76 -32.576 -12.351 -11.758 1.00116.70 O ANISOU 2614 O VAL B 76 17307 15252 11780 -2817 2434 3804 O ATOM 2615 CB VAL B 76 -32.673 -15.609 -12.533 1.00126.33 C ANISOU 2615 CB VAL B 76 19217 15463 13318 -3425 2145 4491 C ATOM 2616 CG1 VAL B 76 -33.474 -15.422 -11.253 1.00129.30 C ANISOU 2616 CG1 VAL B 76 19703 16166 13260 -3732 2639 4647 C ATOM 2617 CG2 VAL B 76 -33.386 -16.557 -13.485 1.00126.42 C ANISOU 2617 CG2 VAL B 76 19090 15183 13761 -3770 2156 4549 C ATOM 2618 N VAL B 77 -30.613 -13.447 -11.805 1.00126.22 N ANISOU 2618 N VAL B 77 19227 15879 12853 -2479 1710 4085 N ATOM 2619 CA VAL B 77 -29.962 -12.560 -10.846 1.00126.47 C ANISOU 2619 CA VAL B 77 19418 16173 12464 -2220 1667 3998 C ATOM 2620 C VAL B 77 -29.869 -11.136 -11.388 1.00125.50 C ANISOU 2620 C VAL B 77 18789 16342 12554 -1940 1651 3572 C ATOM 2621 O VAL B 77 -30.151 -10.170 -10.678 1.00126.79 O ANISOU 2621 O VAL B 77 18863 16846 12467 -1897 1889 3404 O ATOM 2622 CB VAL B 77 -28.549 -13.066 -10.481 1.00 97.28 C ANISOU 2622 CB VAL B 77 16211 12205 8547 -1934 1182 4177 C ATOM 2623 CG1 VAL B 77 -27.798 -12.026 -9.663 1.00 96.80 C ANISOU 2623 CG1 VAL B 77 16234 12431 8114 -1645 1064 4016 C ATOM 2624 CG2 VAL B 77 -28.637 -14.383 -9.724 1.00102.91 C ANISOU 2624 CG2 VAL B 77 17513 12624 8963 -2193 1195 4635 C ATOM 2625 N GLY B 78 -29.483 -11.017 -12.654 1.00124.98 N ANISOU 2625 N GLY B 78 18418 16127 12940 -1757 1376 3396 N ATOM 2626 CA GLY B 78 -29.304 -9.721 -13.284 1.00123.72 C ANISOU 2626 CA GLY B 78 17824 16178 13006 -1497 1308 3032 C ATOM 2627 C GLY B 78 -30.588 -8.960 -13.552 1.00124.88 C ANISOU 2627 C GLY B 78 17494 16602 13351 -1644 1690 2829 C ATOM 2628 O GLY B 78 -30.672 -7.764 -13.275 1.00125.53 O ANISOU 2628 O GLY B 78 17376 16948 13371 -1480 1796 2580 O ATOM 2629 N THR B 79 -31.588 -9.647 -14.098 1.00152.02 N ANISOU 2629 N THR B 79 20740 19970 17049 -1945 1877 2920 N ATOM 2630 CA THR B 79 -32.859 -9.007 -14.427 1.00152.76 C ANISOU 2630 CA THR B 79 20320 20332 17391 -2080 2210 2731 C ATOM 2631 C THR B 79 -33.591 -8.551 -13.172 1.00155.38 C ANISOU 2631 C THR B 79 20666 20994 17378 -2203 2664 2714 C ATOM 2632 O THR B 79 -34.012 -7.400 -13.079 1.00156.48 O ANISOU 2632 O THR B 79 20474 21412 17572 -2048 2839 2436 O ATOM 2633 CB THR B 79 -33.778 -9.934 -15.246 1.00153.84 C ANISOU 2633 CB THR B 79 20243 20331 17876 -2418 2289 2839 C ATOM 2634 OG1 THR B 79 -33.101 -10.350 -16.439 1.00151.39 O ANISOU 2634 OG1 THR B 79 19939 19725 17860 -2295 1880 2817 O ATOM 2635 CG2 THR B 79 -35.062 -9.213 -15.625 1.00154.98 C ANISOU 2635 CG2 THR B 79 19791 20780 18312 -2517 2582 2625 C ATOM 2636 N VAL B 80 -33.734 -9.455 -12.208 1.00115.19 N ANISOU 2636 N VAL B 80 15984 15860 11924 -2478 2859 3010 N ATOM 2637 CA VAL B 80 -34.379 -9.126 -10.942 1.00118.27 C ANISOU 2637 CA VAL B 80 16457 16578 11902 -2628 3325 3016 C ATOM 2638 C VAL B 80 -33.568 -8.071 -10.198 1.00118.87 C ANISOU 2638 C VAL B 80 16721 16820 11623 -2276 3227 2818 C ATOM 2639 O VAL B 80 -34.125 -7.131 -9.633 1.00120.97 O ANISOU 2639 O VAL B 80 16789 17419 11755 -2217 3558 2576 O ATOM 2640 CB VAL B 80 -34.558 -10.371 -10.048 1.00103.86 C ANISOU 2640 CB VAL B 80 15131 14637 9694 -3013 3515 3429 C ATOM 2641 CG1 VAL B 80 -35.106 -9.977 -8.687 1.00109.07 C ANISOU 2641 CG1 VAL B 80 15932 15670 9839 -3155 4004 3428 C ATOM 2642 CG2 VAL B 80 -35.478 -11.378 -10.719 1.00105.63 C ANISOU 2642 CG2 VAL B 80 15154 14703 10276 -3424 3656 3605 C ATOM 2643 N GLY B 81 -32.248 -8.234 -10.210 1.00123.98 N ANISOU 2643 N GLY B 81 17736 17234 12138 -2041 2764 2899 N ATOM 2644 CA GLY B 81 -31.353 -7.306 -9.544 1.00124.37 C ANISOU 2644 CA GLY B 81 17983 17409 11864 -1730 2593 2719 C ATOM 2645 C GLY B 81 -31.493 -5.872 -10.024 1.00124.44 C ANISOU 2645 C GLY B 81 17535 17603 12142 -1466 2611 2297 C ATOM 2646 O GLY B 81 -31.626 -4.955 -9.215 1.00126.27 O ANISOU 2646 O GLY B 81 17790 18089 12097 -1364 2813 2078 O ATOM 2647 N ASN B 82 -31.463 -5.678 -11.339 1.00130.20 N ANISOU 2647 N ASN B 82 17881 18190 13398 -1356 2396 2182 N ATOM 2648 CA ASN B 82 -31.547 -4.338 -11.917 1.00129.79 C ANISOU 2648 CA ASN B 82 17426 18251 13637 -1101 2355 1823 C ATOM 2649 C ASN B 82 -32.966 -3.773 -11.989 1.00131.62 C ANISOU 2649 C ASN B 82 17202 18728 14080 -1186 2788 1635 C ATOM 2650 O ASN B 82 -33.148 -2.558 -12.065 1.00132.57 O ANISOU 2650 O ASN B 82 17067 18976 14326 -960 2838 1325 O ATOM 2651 CB ASN B 82 -30.909 -4.309 -13.309 1.00113.95 C ANISOU 2651 CB ASN B 82 15220 16008 12069 -950 1942 1787 C ATOM 2652 CG ASN B 82 -29.432 -4.651 -13.283 1.00111.81 C ANISOU 2652 CG ASN B 82 15304 15534 11642 -796 1512 1893 C ATOM 2653 OD1 ASN B 82 -28.592 -3.800 -12.991 1.00112.28 O ANISOU 2653 OD1 ASN B 82 15447 15640 11575 -574 1320 1724 O ATOM 2654 ND2 ASN B 82 -29.108 -5.900 -13.594 1.00110.08 N ANISOU 2654 ND2 ASN B 82 15283 15084 11457 -912 1349 2160 N ATOM 2655 N SER B 83 -33.966 -4.649 -11.967 1.00124.89 N ANISOU 2655 N SER B 83 16235 17930 13288 -1508 3092 1817 N ATOM 2656 CA SER B 83 -35.357 -4.212 -12.064 1.00126.68 C ANISOU 2656 CA SER B 83 15957 18416 13758 -1603 3505 1644 C ATOM 2657 C SER B 83 -35.822 -3.490 -10.804 1.00130.18 C ANISOU 2657 C SER B 83 16446 19188 13829 -1562 3940 1454 C ATOM 2658 O SER B 83 -36.277 -2.348 -10.866 1.00131.35 O ANISOU 2658 O SER B 83 16249 19505 14154 -1329 4074 1120 O ATOM 2659 CB SER B 83 -36.280 -5.398 -12.350 1.00131.01 C ANISOU 2659 CB SER B 83 16360 18947 14473 -2012 3714 1892 C ATOM 2660 OG SER B 83 -35.920 -6.044 -13.559 1.00128.50 O ANISOU 2660 OG SER B 83 15993 18325 14505 -2047 3323 2019 O ATOM 2661 N VAL B 84 -35.704 -4.158 -9.661 1.00176.80 N ANISOU 2661 N VAL B 84 22801 25169 19205 -1779 4157 1665 N ATOM 2662 CA VAL B 84 -36.118 -3.569 -8.392 1.00179.84 C ANISOU 2662 CA VAL B 84 23298 25888 19146 -1773 4601 1491 C ATOM 2663 C VAL B 84 -35.087 -2.568 -7.874 1.00179.62 C ANISOU 2663 C VAL B 84 23574 25850 18823 -1422 4352 1254 C ATOM 2664 O VAL B 84 -35.301 -1.916 -6.853 1.00182.05 O ANISOU 2664 O VAL B 84 24006 26416 18748 -1356 4664 1038 O ATOM 2665 CB VAL B 84 -36.410 -4.640 -7.321 1.00157.24 C ANISOU 2665 CB VAL B 84 20846 23136 15763 -2171 4948 1823 C ATOM 2666 CG1 VAL B 84 -37.619 -5.471 -7.723 1.00157.43 C ANISOU 2666 CG1 VAL B 84 20500 23228 16089 -2564 5294 1997 C ATOM 2667 CG2 VAL B 84 -35.201 -5.522 -7.107 1.00155.95 C ANISOU 2667 CG2 VAL B 84 21308 22663 15281 -2214 4518 2175 C ATOM 2668 N THR B 85 -33.969 -2.456 -8.583 1.00143.10 N ANISOU 2668 N THR B 85 19062 20933 14375 -1214 3798 1279 N ATOM 2669 CA THR B 85 -32.995 -1.409 -8.306 1.00143.02 C ANISOU 2669 CA THR B 85 19240 20892 14210 -892 3514 1021 C ATOM 2670 C THR B 85 -33.541 -0.099 -8.856 1.00143.76 C ANISOU 2670 C THR B 85 18853 21055 14715 -636 3599 620 C ATOM 2671 O THR B 85 -33.431 0.950 -8.221 1.00145.33 O ANISOU 2671 O THR B 85 19125 21370 14725 -433 3684 301 O ATOM 2672 CB THR B 85 -31.626 -1.709 -8.950 1.00111.31 C ANISOU 2672 CB THR B 85 15435 16562 10296 -771 2912 1172 C ATOM 2673 OG1 THR B 85 -31.094 -2.924 -8.408 1.00110.71 O ANISOU 2673 OG1 THR B 85 15822 16390 9853 -959 2797 1543 O ATOM 2674 CG2 THR B 85 -30.648 -0.576 -8.684 1.00111.77 C ANISOU 2674 CG2 THR B 85 15634 16602 10230 -480 2623 890 C ATOM 2675 N LEU B 86 -34.135 -0.171 -10.044 1.00149.27 N ANISOU 2675 N LEU B 86 19081 21663 15973 -643 3554 636 N ATOM 2676 CA LEU B 86 -34.776 0.985 -10.658 1.00149.73 C ANISOU 2676 CA LEU B 86 18659 21764 16469 -399 3614 304 C ATOM 2677 C LEU B 86 -35.989 1.437 -9.844 1.00153.29 C ANISOU 2677 C LEU B 86 18875 22546 16821 -404 4186 68 C ATOM 2678 O LEU B 86 -36.215 2.634 -9.668 1.00155.37 O ANISOU 2678 O LEU B 86 18983 22874 17177 -121 4278 -297 O ATOM 2679 CB LEU B 86 -35.187 0.663 -12.095 1.00125.22 C ANISOU 2679 CB LEU B 86 15129 18512 13938 -440 3420 418 C ATOM 2680 CG LEU B 86 -34.038 0.531 -13.098 1.00122.32 C ANISOU 2680 CG LEU B 86 14894 17832 13749 -356 2871 547 C ATOM 2681 CD1 LEU B 86 -34.553 0.093 -14.458 1.00119.45 C ANISOU 2681 CD1 LEU B 86 14148 17361 13878 -441 2726 663 C ATOM 2682 CD2 LEU B 86 -33.267 1.839 -13.210 1.00122.86 C ANISOU 2682 CD2 LEU B 86 15021 17792 13867 -38 2609 280 C ATOM 2683 N PHE B 87 -36.765 0.474 -9.352 1.00136.07 N ANISOU 2683 N PHE B 87 16671 20566 14463 -730 4582 268 N ATOM 2684 CA PHE B 87 -37.905 0.773 -8.485 1.00139.05 C ANISOU 2684 CA PHE B 87 16830 21312 14690 -784 5194 61 C ATOM 2685 C PHE B 87 -37.468 1.386 -7.161 1.00141.35 C ANISOU 2685 C PHE B 87 17564 21760 14384 -663 5380 -156 C ATOM 2686 O PHE B 87 -38.173 2.220 -6.594 1.00143.49 O ANISOU 2686 O PHE B 87 17633 22280 14608 -505 5780 -515 O ATOM 2687 CB PHE B 87 -38.745 -0.481 -8.226 1.00198.59 C ANISOU 2687 CB PHE B 87 24292 29031 22134 -1233 5580 368 C ATOM 2688 CG PHE B 87 -39.735 -0.786 -9.315 1.00197.45 C ANISOU 2688 CG PHE B 87 23517 28896 22610 -1345 5616 412 C ATOM 2689 CD1 PHE B 87 -40.301 0.239 -10.055 1.00196.88 C ANISOU 2689 CD1 PHE B 87 22889 28857 23061 -1026 5564 89 C ATOM 2690 CD2 PHE B 87 -40.113 -2.090 -9.586 1.00197.43 C ANISOU 2690 CD2 PHE B 87 23489 28857 22666 -1772 5682 773 C ATOM 2691 CE1 PHE B 87 -41.219 -0.030 -11.051 1.00195.95 C ANISOU 2691 CE1 PHE B 87 22184 28769 23500 -1123 5555 127 C ATOM 2692 CE2 PHE B 87 -41.031 -2.366 -10.583 1.00196.41 C ANISOU 2692 CE2 PHE B 87 22774 28750 23102 -1897 5688 791 C ATOM 2693 CZ PHE B 87 -41.585 -1.335 -11.316 1.00195.67 C ANISOU 2693 CZ PHE B 87 22111 28724 23511 -1569 5615 468 C ATOM 2694 N THR B 88 -36.307 0.966 -6.670 1.00173.05 N ANISOU 2694 N THR B 88 22177 25631 17942 -727 5080 46 N ATOM 2695 CA THR B 88 -35.780 1.483 -5.414 1.00175.10 C ANISOU 2695 CA THR B 88 22918 26030 17582 -637 5177 -140 C ATOM 2696 C THR B 88 -35.412 2.957 -5.562 1.00175.56 C ANISOU 2696 C THR B 88 22884 25996 17824 -229 4980 -596 C ATOM 2697 O THR B 88 -35.636 3.757 -4.653 1.00178.02 O ANISOU 2697 O THR B 88 23311 26505 17822 -91 5271 -947 O ATOM 2698 CB THR B 88 -34.546 0.687 -4.946 1.00165.93 C ANISOU 2698 CB THR B 88 22396 24713 15936 -773 4798 198 C ATOM 2699 OG1 THR B 88 -34.888 -0.699 -4.817 1.00165.87 O ANISOU 2699 OG1 THR B 88 22520 24729 15773 -1152 4962 641 O ATOM 2700 CG2 THR B 88 -34.049 1.208 -3.607 1.00167.81 C ANISOU 2700 CG2 THR B 88 23143 25128 15488 -701 4882 2 C ATOM 2701 N LEU B 89 -34.858 3.314 -6.717 1.00159.58 N ANISOU 2701 N LEU B 89 20669 23662 16303 -49 4495 -594 N ATOM 2702 CA LEU B 89 -34.483 4.698 -6.983 1.00160.16 C ANISOU 2702 CA LEU B 89 20663 23582 16607 305 4267 -982 C ATOM 2703 C LEU B 89 -35.715 5.552 -7.267 1.00161.63 C ANISOU 2703 C LEU B 89 20315 23880 17217 515 4618 -1320 C ATOM 2704 O LEU B 89 -35.666 6.778 -7.173 1.00162.97 O ANISOU 2704 O LEU B 89 20449 23969 17502 820 4580 -1710 O ATOM 2705 CB LEU B 89 -33.513 4.773 -8.165 1.00118.67 C ANISOU 2705 CB LEU B 89 15375 17971 11744 391 3664 -838 C ATOM 2706 CG LEU B 89 -32.184 4.027 -8.028 1.00116.86 C ANISOU 2706 CG LEU B 89 15602 17603 11198 256 3247 -544 C ATOM 2707 CD1 LEU B 89 -31.376 4.130 -9.313 1.00113.73 C ANISOU 2707 CD1 LEU B 89 15065 16898 11252 342 2734 -437 C ATOM 2708 CD2 LEU B 89 -31.385 4.558 -6.848 1.00118.55 C ANISOU 2708 CD2 LEU B 89 16299 17884 10860 326 3172 -742 C ATOM 2709 N ALA B 90 -36.818 4.895 -7.611 1.00205.50 N ANISOU 2709 N ALA B 90 25449 29609 23022 352 4943 -1175 N ATOM 2710 CA ALA B 90 -38.070 5.587 -7.902 1.00206.94 C ANISOU 2710 CA ALA B 90 25047 29935 23646 550 5276 -1473 C ATOM 2711 C ALA B 90 -39.040 5.514 -6.725 1.00210.23 C ANISOU 2711 C ALA B 90 25398 30774 23706 459 5963 -1662 C ATOM 2712 O ALA B 90 -38.801 6.100 -5.669 1.00212.45 O ANISOU 2712 O ALA B 90 26020 31173 23529 574 6162 -1945 O ATOM 2713 CB ALA B 90 -38.711 5.021 -9.160 1.00107.82 C ANISOU 2713 CB ALA B 90 11976 17317 11675 447 5155 -1235 C ATOM 2714 N SER B 97 -31.011 15.890 -4.878 1.00191.30 N ANISOU 2714 N SER B 97 26021 25844 20821 2375 2935 -4607 N ATOM 2715 CA SER B 97 -29.787 16.270 -4.191 1.00193.48 C ANISOU 2715 CA SER B 97 26806 26023 20685 2246 2584 -4773 C ATOM 2716 C SER B 97 -28.639 15.436 -4.731 1.00191.92 C ANISOU 2716 C SER B 97 26667 25799 20453 1956 2115 -4291 C ATOM 2717 O SER B 97 -28.798 14.751 -5.741 1.00189.51 O ANISOU 2717 O SER B 97 26022 25475 20508 1890 2050 -3884 O ATOM 2718 CB SER B 97 -29.951 16.076 -2.679 1.00132.34 C ANISOU 2718 CB SER B 97 19447 18648 12187 2199 2933 -5042 C ATOM 2719 OG SER B 97 -28.717 16.135 -1.998 1.00132.56 O ANISOU 2719 OG SER B 97 19964 18666 11736 2013 2548 -5100 O ATOM 2720 N LEU B 98 -27.504 15.474 -4.035 1.00187.38 N ANISOU 2720 N LEU B 98 26514 25242 19438 1791 1793 -4358 N ATOM 2721 CA LEU B 98 -26.300 14.750 -4.449 1.00184.94 C ANISOU 2721 CA LEU B 98 26263 24918 19088 1545 1320 -3958 C ATOM 2722 C LEU B 98 -26.515 13.235 -4.360 1.00183.61 C ANISOU 2722 C LEU B 98 26031 25082 18652 1387 1481 -3496 C ATOM 2723 O LEU B 98 -26.038 12.469 -5.196 1.00180.79 O ANISOU 2723 O LEU B 98 25491 24677 18525 1265 1233 -3084 O ATOM 2724 CB LEU B 98 -25.080 15.216 -3.617 1.00207.28 C ANISOU 2724 CB LEU B 98 29540 27714 21504 1424 929 -4192 C ATOM 2725 CG LEU B 98 -23.918 14.331 -3.096 1.00203.89 C ANISOU 2725 CG LEU B 98 29376 27494 20600 1187 561 -3926 C ATOM 2726 CD1 LEU B 98 -24.407 13.393 -2.040 1.00204.50 C ANISOU 2726 CD1 LEU B 98 29696 27972 20032 1135 889 -3817 C ATOM 2727 CD2 LEU B 98 -23.077 13.574 -4.157 1.00198.65 C ANISOU 2727 CD2 LEU B 98 28453 26747 20279 1047 175 -3452 C ATOM 2728 N GLN B 99 -27.265 12.809 -3.351 1.00245.82 N ANISOU 2728 N GLN B 99 34071 33286 26043 1384 1922 -3573 N ATOM 2729 CA GLN B 99 -27.611 11.398 -3.199 1.00245.43 C ANISOU 2729 CA GLN B 99 33994 33528 25732 1214 2132 -3139 C ATOM 2730 C GLN B 99 -28.554 11.034 -4.339 1.00244.03 C ANISOU 2730 C GLN B 99 33291 33287 26143 1265 2353 -2909 C ATOM 2731 O GLN B 99 -28.484 9.940 -4.883 1.00241.94 O ANISOU 2731 O GLN B 99 32890 33067 25970 1112 2282 -2470 O ATOM 2732 CB GLN B 99 -28.271 11.164 -1.824 1.00237.45 C ANISOU 2732 CB GLN B 99 33292 32883 24044 1178 2607 -3308 C ATOM 2733 CG GLN B 99 -28.840 9.779 -1.595 1.00235.85 C ANISOU 2733 CG GLN B 99 33073 32973 23566 980 2923 -2879 C ATOM 2734 CD GLN B 99 -27.841 8.682 -1.846 1.00228.91 C ANISOU 2734 CD GLN B 99 32346 32054 22575 783 2481 -2384 C ATOM 2735 OE1 GLN B 99 -26.639 8.870 -1.680 1.00227.26 O ANISOU 2735 OE1 GLN B 99 32398 31736 22213 764 1982 -2399 O ATOM 2736 NE2 GLN B 99 -28.333 7.521 -2.254 1.00224.81 N ANISOU 2736 NE2 GLN B 99 31648 31614 22154 637 2655 -1954 N ATOM 2737 N SER B 100 -29.407 11.991 -4.711 1.00245.56 N ANISOU 2737 N SER B 100 33199 33353 26750 1496 2582 -3225 N ATOM 2738 CA SER B 100 -30.361 11.873 -5.831 1.00243.69 C ANISOU 2738 CA SER B 100 32432 33038 27123 1591 2748 -3076 C ATOM 2739 C SER B 100 -29.749 12.041 -7.230 1.00241.09 C ANISOU 2739 C SER B 100 31876 32366 27360 1596 2280 -2857 C ATOM 2740 O SER B 100 -30.201 11.393 -8.160 1.00238.84 O ANISOU 2740 O SER B 100 31247 32081 27421 1547 2303 -2550 O ATOM 2741 CB SER B 100 -31.568 12.817 -5.635 1.00187.55 C ANISOU 2741 CB SER B 100 25086 25943 20231 1875 3174 -3506 C ATOM 2742 OG SER B 100 -31.376 14.066 -6.230 1.00187.71 O ANISOU 2742 OG SER B 100 25033 25583 20704 2109 2915 -3779 O ATOM 2743 N THR B 101 -28.767 12.929 -7.394 1.00142.57 N ANISOU 2743 N THR B 101 19587 19606 14978 1638 1876 -3026 N ATOM 2744 CA THR B 101 -28.091 13.046 -8.693 1.00140.17 C ANISOU 2744 CA THR B 101 19101 19010 15149 1593 1451 -2794 C ATOM 2745 C THR B 101 -27.381 11.740 -9.015 1.00136.91 C ANISOU 2745 C THR B 101 18701 18723 14596 1354 1246 -2343 C ATOM 2746 O THR B 101 -27.359 11.293 -10.162 1.00134.85 O ANISOU 2746 O THR B 101 18167 18364 14706 1304 1107 -2050 O ATOM 2747 CB THR B 101 -27.019 14.192 -8.752 1.00145.60 C ANISOU 2747 CB THR B 101 20015 19379 15927 1609 1042 -3035 C ATOM 2748 OG1 THR B 101 -25.904 13.854 -7.913 1.00144.85 O ANISOU 2748 OG1 THR B 101 20282 19412 15342 1428 809 -3030 O ATOM 2749 CG2 THR B 101 -27.603 15.531 -8.328 1.00148.52 C ANISOU 2749 CG2 THR B 101 20460 19562 16408 1855 1204 -3523 C ATOM 2750 N VAL B 102 -26.824 11.115 -7.987 1.00121.48 N ANISOU 2750 N VAL B 102 17083 16985 12091 1220 1226 -2296 N ATOM 2751 CA VAL B 102 -26.132 9.847 -8.149 1.00118.48 C ANISOU 2751 CA VAL B 102 16760 16708 11547 1030 1023 -1885 C ATOM 2752 C VAL B 102 -27.138 8.758 -8.549 1.00117.33 C ANISOU 2752 C VAL B 102 16366 16705 11508 967 1342 -1579 C ATOM 2753 O VAL B 102 -26.792 7.782 -9.222 1.00114.93 O ANISOU 2753 O VAL B 102 15966 16377 11324 849 1176 -1224 O ATOM 2754 CB VAL B 102 -25.360 9.482 -6.855 1.00117.68 C ANISOU 2754 CB VAL B 102 17113 16798 10802 928 906 -1910 C ATOM 2755 CG1 VAL B 102 -24.928 8.025 -6.849 1.00114.99 C ANISOU 2755 CG1 VAL B 102 16854 16583 10252 771 785 -1468 C ATOM 2756 CG2 VAL B 102 -24.160 10.414 -6.676 1.00117.96 C ANISOU 2756 CG2 VAL B 102 17339 16674 10805 935 474 -2156 C ATOM 2757 N ASP B 103 -28.396 8.970 -8.169 1.00111.76 N ANISOU 2757 N ASP B 103 15532 16141 10790 1050 1804 -1746 N ATOM 2758 CA ASP B 103 -29.483 8.053 -8.503 1.00111.62 C ANISOU 2758 CA ASP B 103 15232 16276 10903 968 2145 -1506 C ATOM 2759 C ASP B 103 -29.693 7.958 -10.010 1.00109.81 C ANISOU 2759 C ASP B 103 14592 15849 11282 992 1975 -1320 C ATOM 2760 O ASP B 103 -30.037 6.898 -10.527 1.00107.99 O ANISOU 2760 O ASP B 103 14198 15677 11157 846 2032 -1005 O ATOM 2761 CB ASP B 103 -30.795 8.489 -7.830 1.00165.07 C ANISOU 2761 CB ASP B 103 21868 23252 17598 1075 2684 -1789 C ATOM 2762 CG ASP B 103 -30.838 8.153 -6.350 1.00167.17 C ANISOU 2762 CG ASP B 103 22529 23808 17178 970 2976 -1868 C ATOM 2763 OD1 ASP B 103 -29.775 7.845 -5.776 1.00166.42 O ANISOU 2763 OD1 ASP B 103 22852 23716 16663 864 2691 -1769 O ATOM 2764 OD2 ASP B 103 -31.936 8.205 -5.754 1.00169.46 O ANISOU 2764 OD2 ASP B 103 22708 24342 17338 994 3489 -2032 O ATOM 2765 N TYR B 104 -29.483 9.068 -10.711 1.00143.14 N ANISOU 2765 N TYR B 104 18678 19823 15883 1163 1756 -1514 N ATOM 2766 CA TYR B 104 -29.651 9.099 -12.161 1.00141.49 C ANISOU 2766 CA TYR B 104 18123 19425 16213 1191 1568 -1347 C ATOM 2767 C TYR B 104 -28.558 8.300 -12.859 1.00138.65 C ANISOU 2767 C TYR B 104 17839 18975 15867 1020 1199 -1024 C ATOM 2768 O TYR B 104 -28.800 7.666 -13.885 1.00137.03 O ANISOU 2768 O TYR B 104 17394 18731 15942 950 1137 -780 O ATOM 2769 CB TYR B 104 -29.667 10.538 -12.675 1.00157.34 C ANISOU 2769 CB TYR B 104 20033 21164 18585 1409 1417 -1617 C ATOM 2770 CG TYR B 104 -30.949 11.264 -12.352 1.00159.68 C ANISOU 2770 CG TYR B 104 20119 21509 19041 1638 1772 -1911 C ATOM 2771 CD1 TYR B 104 -32.124 10.984 -13.038 1.00159.03 C ANISOU 2771 CD1 TYR B 104 19610 21502 19314 1701 1963 -1814 C ATOM 2772 CD2 TYR B 104 -30.985 12.232 -11.359 1.00162.56 C ANISOU 2772 CD2 TYR B 104 20699 21853 19211 1802 1910 -2312 C ATOM 2773 CE1 TYR B 104 -33.299 11.645 -12.736 1.00161.38 C ANISOU 2773 CE1 TYR B 104 19659 21867 19792 1941 2288 -2102 C ATOM 2774 CE2 TYR B 104 -32.151 12.900 -11.055 1.00164.52 C ANISOU 2774 CE2 TYR B 104 20737 22149 19623 2051 2254 -2617 C ATOM 2775 CZ TYR B 104 -33.305 12.605 -11.746 1.00164.16 C ANISOU 2775 CZ TYR B 104 20226 22192 19957 2131 2445 -2508 C ATOM 2776 OH TYR B 104 -34.468 13.273 -11.440 1.00166.15 O ANISOU 2776 OH TYR B 104 20212 22511 20406 2409 2786 -2831 O ATOM 2777 N TYR B 105 -27.356 8.337 -12.295 1.00107.32 N ANISOU 2777 N TYR B 105 14195 14985 11595 962 950 -1048 N ATOM 2778 CA TYR B 105 -26.234 7.578 -12.832 1.00104.36 C ANISOU 2778 CA TYR B 105 13884 14553 11216 832 608 -780 C ATOM 2779 C TYR B 105 -26.422 6.085 -12.590 1.00101.96 C ANISOU 2779 C TYR B 105 13641 14410 10691 690 726 -474 C ATOM 2780 O TYR B 105 -26.164 5.264 -13.470 1.00 99.04 O ANISOU 2780 O TYR B 105 13148 13973 10508 610 581 -217 O ATOM 2781 CB TYR B 105 -24.920 8.043 -12.209 1.00111.08 C ANISOU 2781 CB TYR B 105 15027 15366 11814 817 299 -912 C ATOM 2782 CG TYR B 105 -24.501 9.437 -12.614 1.00112.44 C ANISOU 2782 CG TYR B 105 15159 15316 12248 895 105 -1167 C ATOM 2783 CD1 TYR B 105 -23.935 9.679 -13.859 1.00111.39 C ANISOU 2783 CD1 TYR B 105 14835 14995 12495 856 -153 -1053 C ATOM 2784 CD2 TYR B 105 -24.664 10.511 -11.749 1.00115.13 C ANISOU 2784 CD2 TYR B 105 15680 15622 12441 993 186 -1525 C ATOM 2785 CE1 TYR B 105 -23.551 10.952 -14.233 1.00112.86 C ANISOU 2785 CE1 TYR B 105 15016 14949 12915 888 -327 -1252 C ATOM 2786 CE2 TYR B 105 -24.281 11.788 -12.113 1.00116.60 C ANISOU 2786 CE2 TYR B 105 15867 15550 12885 1047 -5 -1753 C ATOM 2787 CZ TYR B 105 -23.724 12.002 -13.356 1.00115.51 C ANISOU 2787 CZ TYR B 105 15544 15214 13131 982 -264 -1597 C ATOM 2788 OH TYR B 105 -23.341 13.270 -13.726 1.00117.04 O ANISOU 2788 OH TYR B 105 15769 15125 13576 997 -451 -1791 O ATOM 2789 N LEU B 106 -26.864 5.741 -11.385 1.00108.04 N ANISOU 2789 N LEU B 106 14630 15377 11045 650 994 -506 N ATOM 2790 CA LEU B 106 -27.137 4.352 -11.038 1.00107.21 C ANISOU 2790 CA LEU B 106 14636 15401 10700 489 1139 -201 C ATOM 2791 C LEU B 106 -28.305 3.820 -11.857 1.00106.24 C ANISOU 2791 C LEU B 106 14162 15285 10919 419 1392 -58 C ATOM 2792 O LEU B 106 -28.341 2.642 -12.215 1.00104.08 O ANISOU 2792 O LEU B 106 13885 14992 10669 271 1371 239 O ATOM 2793 CB LEU B 106 -27.438 4.218 -9.542 1.00131.09 C ANISOU 2793 CB LEU B 106 17992 18650 13167 438 1411 -273 C ATOM 2794 CG LEU B 106 -26.265 3.907 -8.608 1.00130.96 C ANISOU 2794 CG LEU B 106 18420 18676 12662 405 1128 -208 C ATOM 2795 CD1 LEU B 106 -25.175 4.961 -8.711 1.00130.46 C ANISOU 2795 CD1 LEU B 106 18402 18492 12675 531 744 -456 C ATOM 2796 CD2 LEU B 106 -26.752 3.777 -7.173 1.00133.88 C ANISOU 2796 CD2 LEU B 106 19129 19292 12446 335 1450 -268 C ATOM 2797 N GLY B 107 -29.256 4.699 -12.156 1.00100.59 N ANISOU 2797 N GLY B 107 13150 14585 10485 533 1607 -282 N ATOM 2798 CA GLY B 107 -30.403 4.335 -12.964 1.00 99.97 C ANISOU 2798 CA GLY B 107 12682 14533 10770 484 1810 -185 C ATOM 2799 C GLY B 107 -29.997 4.127 -14.408 1.00 97.13 C ANISOU 2799 C GLY B 107 12126 13969 10810 474 1475 -23 C ATOM 2800 O GLY B 107 -30.523 3.250 -15.093 1.00 95.47 O ANISOU 2800 O GLY B 107 11727 13760 10786 341 1518 185 O ATOM 2801 N SER B 108 -29.053 4.941 -14.868 1.00108.80 N ANISOU 2801 N SER B 108 13660 15273 12404 595 1149 -126 N ATOM 2802 CA SER B 108 -28.534 4.827 -16.224 1.00106.87 C ANISOU 2802 CA SER B 108 13268 14853 12484 578 838 12 C ATOM 2803 C SER B 108 -27.752 3.528 -16.391 1.00103.44 C ANISOU 2803 C SER B 108 12994 14402 11906 428 675 282 C ATOM 2804 O SER B 108 -27.768 2.915 -17.458 1.00101.22 O ANISOU 2804 O SER B 108 12561 14040 11857 358 561 445 O ATOM 2805 CB SER B 108 -27.642 6.025 -16.556 1.00122.94 C ANISOU 2805 CB SER B 108 15358 16720 14634 701 560 -158 C ATOM 2806 OG SER B 108 -27.127 5.932 -17.872 1.00121.36 O ANISOU 2806 OG SER B 108 15026 16377 14708 663 295 -18 O ATOM 2807 N LEU B 109 -27.071 3.114 -15.328 1.00107.32 N ANISOU 2807 N LEU B 109 13809 14962 12007 395 649 317 N ATOM 2808 CA LEU B 109 -26.309 1.870 -15.338 1.00104.36 C ANISOU 2808 CA LEU B 109 13620 14549 11484 297 479 569 C ATOM 2809 C LEU B 109 -27.222 0.648 -15.348 1.00103.75 C ANISOU 2809 C LEU B 109 13518 14509 11393 132 710 794 C ATOM 2810 O LEU B 109 -26.977 -0.313 -16.076 1.00100.85 O ANISOU 2810 O LEU B 109 13133 14027 11158 54 575 989 O ATOM 2811 CB LEU B 109 -25.371 1.810 -14.130 1.00 91.35 C ANISOU 2811 CB LEU B 109 12336 12966 9408 325 352 553 C ATOM 2812 CG LEU B 109 -24.142 2.717 -14.188 1.00 90.96 C ANISOU 2812 CG LEU B 109 12330 12858 9374 435 23 380 C ATOM 2813 CD1 LEU B 109 -23.367 2.662 -12.882 1.00 91.74 C ANISOU 2813 CD1 LEU B 109 12781 13056 9019 454 -104 346 C ATOM 2814 CD2 LEU B 109 -23.256 2.324 -15.358 1.00 87.07 C ANISOU 2814 CD2 LEU B 109 11688 12234 9159 439 -269 499 C ATOM 2815 N ALA B 110 -28.275 0.693 -14.538 1.00141.90 N ANISOU 2815 N ALA B 110 18348 19500 16068 66 1071 751 N ATOM 2816 CA ALA B 110 -29.215 -0.418 -14.440 1.00142.03 C ANISOU 2816 CA ALA B 110 18333 19570 16061 -145 1334 961 C ATOM 2817 C ALA B 110 -29.972 -0.618 -15.750 1.00140.30 C ANISOU 2817 C ALA B 110 17728 19280 16301 -208 1339 999 C ATOM 2818 O ALA B 110 -30.374 -1.734 -16.081 1.00139.04 O ANISOU 2818 O ALA B 110 17552 19068 16210 -402 1391 1208 O ATOM 2819 CB ALA B 110 -30.185 -0.195 -13.289 1.00114.03 C ANISOU 2819 CB ALA B 110 14824 16256 12248 -212 1763 872 C ATOM 2820 N LEU B 111 -30.162 0.469 -16.489 1.00 98.33 N ANISOU 2820 N LEU B 111 12124 13946 11289 -51 1263 798 N ATOM 2821 CA LEU B 111 -30.837 0.409 -17.780 1.00 96.81 C ANISOU 2821 CA LEU B 111 11574 13696 11512 -86 1208 824 C ATOM 2822 C LEU B 111 -29.962 -0.266 -18.831 1.00 94.06 C ANISOU 2822 C LEU B 111 11295 13160 11282 -127 876 974 C ATOM 2823 O LEU B 111 -30.440 -1.087 -19.614 1.00 92.19 O ANISOU 2823 O LEU B 111 10926 12872 11230 -273 860 1101 O ATOM 2824 CB LEU B 111 -31.212 1.816 -18.246 1.00126.41 C ANISOU 2824 CB LEU B 111 15052 17451 15528 120 1178 588 C ATOM 2825 CG LEU B 111 -32.016 1.904 -19.544 1.00125.00 C ANISOU 2825 CG LEU B 111 14494 17236 15765 111 1098 606 C ATOM 2826 CD1 LEU B 111 -33.370 1.228 -19.390 1.00125.15 C ANISOU 2826 CD1 LEU B 111 14249 17418 15883 -56 1396 661 C ATOM 2827 CD2 LEU B 111 -32.177 3.352 -19.980 1.00125.78 C ANISOU 2827 CD2 LEU B 111 14411 17279 16102 351 995 403 C ATOM 2828 N SER B 112 -28.678 0.078 -18.838 1.00 99.15 N ANISOU 2828 N SER B 112 12137 13714 11821 -4 618 939 N ATOM 2829 CA SER B 112 -27.733 -0.507 -19.783 1.00 95.85 C ANISOU 2829 CA SER B 112 11773 13147 11498 -13 329 1044 C ATOM 2830 C SER B 112 -27.550 -1.995 -19.511 1.00 94.69 C ANISOU 2830 C SER B 112 11845 12930 11205 -149 332 1258 C ATOM 2831 O SER B 112 -27.171 -2.757 -20.400 1.00 92.39 O ANISOU 2831 O SER B 112 11553 12506 11047 -189 168 1348 O ATOM 2832 CB SER B 112 -26.384 0.213 -19.717 1.00104.99 C ANISOU 2832 CB SER B 112 13057 14262 12573 134 82 944 C ATOM 2833 OG SER B 112 -25.776 0.045 -18.448 1.00105.58 O ANISOU 2833 OG SER B 112 13417 14390 12311 166 83 953 O ATOM 2834 N ASP B 113 -27.822 -2.399 -18.273 1.00 98.33 N ANISOU 2834 N ASP B 113 12517 13464 11378 -219 524 1336 N ATOM 2835 CA ASP B 113 -27.706 -3.796 -17.876 1.00 97.80 C ANISOU 2835 CA ASP B 113 12718 13296 11147 -359 533 1572 C ATOM 2836 C ASP B 113 -28.947 -4.585 -18.279 1.00 98.47 C ANISOU 2836 C ASP B 113 12650 13361 11404 -600 748 1686 C ATOM 2837 O ASP B 113 -28.844 -5.725 -18.726 1.00 97.49 O ANISOU 2837 O ASP B 113 12637 13056 11349 -720 656 1847 O ATOM 2838 CB ASP B 113 -27.469 -3.910 -16.368 1.00181.40 C ANISOU 2838 CB ASP B 113 23646 23971 21307 -362 637 1643 C ATOM 2839 CG ASP B 113 -26.113 -3.376 -15.948 1.00180.75 C ANISOU 2839 CG ASP B 113 23748 23887 21040 -153 353 1558 C ATOM 2840 OD1 ASP B 113 -25.469 -2.679 -16.760 1.00179.19 O ANISOU 2840 OD1 ASP B 113 23366 23657 21062 -16 142 1408 O ATOM 2841 OD2 ASP B 113 -25.692 -3.652 -14.804 1.00182.34 O ANISOU 2841 OD2 ASP B 113 24280 24130 20869 -143 333 1646 O ATOM 2842 N LEU B 114 -30.119 -3.976 -18.120 1.00114.17 N ANISOU 2842 N LEU B 114 14369 15530 13480 -669 1027 1583 N ATOM 2843 CA LEU B 114 -31.370 -4.629 -18.493 1.00114.40 C ANISOU 2843 CA LEU B 114 14174 15585 13706 -918 1236 1665 C ATOM 2844 C LEU B 114 -31.472 -4.845 -19.999 1.00112.46 C ANISOU 2844 C LEU B 114 13693 15214 13825 -942 1012 1643 C ATOM 2845 O LEU B 114 -32.022 -5.849 -20.451 1.00112.07 O ANISOU 2845 O LEU B 114 13608 15070 13904 -1173 1037 1764 O ATOM 2846 CB LEU B 114 -32.574 -3.823 -18.003 1.00 94.93 C ANISOU 2846 CB LEU B 114 11401 13379 11287 -941 1580 1520 C ATOM 2847 CG LEU B 114 -32.969 -3.980 -16.535 1.00 97.86 C ANISOU 2847 CG LEU B 114 11967 13921 11294 -1056 1940 1575 C ATOM 2848 CD1 LEU B 114 -34.193 -3.135 -16.226 1.00 99.99 C ANISOU 2848 CD1 LEU B 114 11849 14464 11678 -1043 2296 1376 C ATOM 2849 CD2 LEU B 114 -33.226 -5.442 -16.201 1.00 98.48 C ANISOU 2849 CD2 LEU B 114 12279 13900 11237 -1381 2058 1866 C ATOM 2850 N LEU B 115 -30.944 -3.900 -20.770 1.00105.52 N ANISOU 2850 N LEU B 115 12675 14328 13091 -725 792 1487 N ATOM 2851 CA LEU B 115 -30.984 -3.992 -22.226 1.00103.55 C ANISOU 2851 CA LEU B 115 12232 13984 13128 -737 572 1458 C ATOM 2852 C LEU B 115 -30.172 -5.176 -22.739 1.00102.36 C ANISOU 2852 C LEU B 115 12333 13614 12946 -804 372 1578 C ATOM 2853 O LEU B 115 -30.609 -5.896 -23.636 1.00102.11 O ANISOU 2853 O LEU B 115 12215 13489 13093 -959 304 1613 O ATOM 2854 CB LEU B 115 -30.474 -2.697 -22.864 1.00 90.14 C ANISOU 2854 CB LEU B 115 10400 12313 11536 -505 387 1297 C ATOM 2855 CG LEU B 115 -31.357 -1.456 -22.719 1.00 91.29 C ANISOU 2855 CG LEU B 115 10254 12614 11819 -398 517 1150 C ATOM 2856 CD1 LEU B 115 -30.726 -0.265 -23.424 1.00 89.89 C ANISOU 2856 CD1 LEU B 115 10024 12386 11744 -194 290 1033 C ATOM 2857 CD2 LEU B 115 -32.754 -1.724 -23.256 1.00 91.18 C ANISOU 2857 CD2 LEU B 115 9895 12688 12063 -547 620 1160 C ATOM 2858 N ILE B 116 -28.991 -5.375 -22.164 1.00118.33 N ANISOU 2858 N ILE B 116 14662 15550 14748 -674 265 1623 N ATOM 2859 CA ILE B 116 -28.101 -6.445 -22.599 1.00117.18 C ANISOU 2859 CA ILE B 116 14750 15185 14588 -666 63 1709 C ATOM 2860 C ILE B 116 -28.585 -7.816 -22.118 1.00118.56 C ANISOU 2860 C ILE B 116 15146 15201 14699 -888 172 1904 C ATOM 2861 O ILE B 116 -28.275 -8.839 -22.726 1.00118.36 O ANISOU 2861 O ILE B 116 15261 14951 14759 -939 32 1960 O ATOM 2862 CB ILE B 116 -26.639 -6.191 -22.154 1.00129.86 C ANISOU 2862 CB ILE B 116 16563 16763 16015 -428 -121 1684 C ATOM 2863 CG1 ILE B 116 -25.660 -6.899 -23.093 1.00128.11 C ANISOU 2863 CG1 ILE B 116 16418 16365 15894 -338 -361 1668 C ATOM 2864 CG2 ILE B 116 -26.421 -6.611 -20.707 1.00131.09 C ANISOU 2864 CG2 ILE B 116 17027 16910 15872 -428 -44 1826 C ATOM 2865 CD1 ILE B 116 -24.206 -6.708 -22.717 1.00126.92 C ANISOU 2865 CD1 ILE B 116 16399 16210 15614 -103 -555 1632 C ATOM 2866 N LEU B 117 -29.335 -7.837 -21.021 1.00109.00 N ANISOU 2866 N LEU B 117 13986 14097 13331 -1028 433 2002 N ATOM 2867 CA LEU B 117 -29.848 -9.091 -20.477 1.00110.51 C ANISOU 2867 CA LEU B 117 14412 14138 13439 -1290 569 2222 C ATOM 2868 C LEU B 117 -31.130 -9.534 -21.177 1.00111.48 C ANISOU 2868 C LEU B 117 14271 14260 13827 -1590 703 2225 C ATOM 2869 O LEU B 117 -31.338 -10.724 -21.413 1.00112.90 O ANISOU 2869 O LEU B 117 14619 14204 14076 -1809 675 2359 O ATOM 2870 CB LEU B 117 -30.084 -8.974 -18.969 1.00 97.73 C ANISOU 2870 CB LEU B 117 12992 12656 11487 -1352 818 2344 C ATOM 2871 CG LEU B 117 -28.846 -8.846 -18.079 1.00 97.34 C ANISOU 2871 CG LEU B 117 13296 12575 11114 -1115 657 2397 C ATOM 2872 CD1 LEU B 117 -29.239 -8.377 -16.689 1.00 99.70 C ANISOU 2872 CD1 LEU B 117 13719 13099 11064 -1169 931 2441 C ATOM 2873 CD2 LEU B 117 -28.090 -10.162 -18.007 1.00 97.04 C ANISOU 2873 CD2 LEU B 117 13658 12210 11004 -1117 442 2613 C ATOM 2874 N LEU B 118 -31.984 -8.572 -21.509 1.00117.53 N ANISOU 2874 N LEU B 118 14622 15277 14758 -1596 825 2070 N ATOM 2875 CA LEU B 118 -33.278 -8.872 -22.113 1.00118.41 C ANISOU 2875 CA LEU B 118 14407 15447 15136 -1875 941 2055 C ATOM 2876 C LEU B 118 -33.196 -9.063 -23.625 1.00117.12 C ANISOU 2876 C LEU B 118 14101 15162 15238 -1869 653 1950 C ATOM 2877 O LEU B 118 -33.903 -9.898 -24.190 1.00118.03 O ANISOU 2877 O LEU B 118 14138 15178 15530 -2146 640 1987 O ATOM 2878 CB LEU B 118 -34.291 -7.771 -21.788 1.00118.55 C ANISOU 2878 CB LEU B 118 14009 15796 15237 -1853 1186 1926 C ATOM 2879 CG LEU B 118 -34.738 -7.634 -20.332 1.00120.71 C ANISOU 2879 CG LEU B 118 14352 16253 15260 -1936 1562 1996 C ATOM 2880 CD1 LEU B 118 -35.693 -6.461 -20.179 1.00121.25 C ANISOU 2880 CD1 LEU B 118 13961 16641 15466 -1844 1783 1802 C ATOM 2881 CD2 LEU B 118 -35.384 -8.922 -19.843 1.00122.23 C ANISOU 2881 CD2 LEU B 118 14690 16357 15393 -2341 1778 2220 C ATOM 2882 N LEU B 119 -32.337 -8.287 -24.278 1.00103.05 N ANISOU 2882 N LEU B 119 12295 13392 13468 -1579 426 1816 N ATOM 2883 CA LEU B 119 -32.273 -8.289 -25.736 1.00101.61 C ANISOU 2883 CA LEU B 119 11973 13149 13485 -1563 174 1702 C ATOM 2884 C LEU B 119 -31.082 -9.071 -26.286 1.00101.60 C ANISOU 2884 C LEU B 119 12297 12890 13416 -1472 -51 1704 C ATOM 2885 O LEU B 119 -31.218 -9.814 -27.257 1.00102.60 O ANISOU 2885 O LEU B 119 12444 12871 13667 -1602 -190 1663 O ATOM 2886 CB LEU B 119 -32.247 -6.856 -26.271 1.00 91.78 C ANISOU 2886 CB LEU B 119 10451 12101 12320 -1337 84 1554 C ATOM 2887 CG LEU B 119 -33.437 -5.973 -25.891 1.00 91.99 C ANISOU 2887 CG LEU B 119 10106 12372 12473 -1356 271 1504 C ATOM 2888 CD1 LEU B 119 -33.290 -4.584 -26.495 1.00 89.81 C ANISOU 2888 CD1 LEU B 119 9629 12208 12288 -1104 125 1373 C ATOM 2889 CD2 LEU B 119 -34.746 -6.618 -26.322 1.00 92.89 C ANISOU 2889 CD2 LEU B 119 9948 12535 12811 -1654 325 1525 C ATOM 2890 N ALA B 120 -29.917 -8.903 -25.669 1.00104.98 N ANISOU 2890 N ALA B 120 12965 13271 13652 -1241 -92 1728 N ATOM 2891 CA ALA B 120 -28.691 -9.496 -26.195 1.00104.52 C ANISOU 2891 CA ALA B 120 13149 13011 13554 -1088 -304 1693 C ATOM 2892 C ALA B 120 -28.512 -10.967 -25.822 1.00105.70 C ANISOU 2892 C ALA B 120 13642 12855 13665 -1198 -319 1830 C ATOM 2893 O ALA B 120 -28.069 -11.766 -26.647 1.00106.78 O ANISOU 2893 O ALA B 120 13909 12777 13885 -1183 -477 1765 O ATOM 2894 CB ALA B 120 -27.476 -8.685 -25.766 1.00 72.15 C ANISOU 2894 CB ALA B 120 9109 9000 9304 -791 -380 1646 C ATOM 2895 N MET B 121 -28.848 -11.325 -24.586 1.00 96.86 N ANISOU 2895 N MET B 121 12694 11702 12406 -1308 -153 2015 N ATOM 2896 CA MET B 121 -28.657 -12.702 -24.122 1.00 98.20 C ANISOU 2896 CA MET B 121 13250 11541 12521 -1415 -180 2193 C ATOM 2897 C MET B 121 -29.459 -13.777 -24.875 1.00 99.83 C ANISOU 2897 C MET B 121 13487 11512 12932 -1723 -190 2203 C ATOM 2898 O MET B 121 -28.878 -14.765 -25.320 1.00100.86 O ANISOU 2898 O MET B 121 13885 11317 13121 -1678 -362 2194 O ATOM 2899 CB MET B 121 -28.870 -12.834 -22.608 1.00118.19 C ANISOU 2899 CB MET B 121 16001 14097 14807 -1499 9 2423 C ATOM 2900 CG MET B 121 -28.650 -14.256 -22.105 1.00119.85 C ANISOU 2900 CG MET B 121 16667 13925 14947 -1612 -44 2653 C ATOM 2901 SD MET B 121 -28.925 -14.477 -20.339 1.00121.69 S ANISOU 2901 SD MET B 121 17226 14186 14823 -1756 180 2968 S ATOM 2902 CE MET B 121 -27.637 -13.439 -19.660 1.00120.05 C ANISOU 2902 CE MET B 121 17062 14196 14357 -1316 29 2893 C ATOM 2903 N PRO B 122 -30.789 -13.598 -25.022 1.00101.49 N ANISOU 2903 N PRO B 122 13415 11880 13268 -2033 -18 2203 N ATOM 2904 CA PRO B 122 -31.535 -14.656 -25.717 1.00102.89 C ANISOU 2904 CA PRO B 122 13624 11825 13645 -2364 -55 2203 C ATOM 2905 C PRO B 122 -31.115 -14.810 -27.178 1.00102.93 C ANISOU 2905 C PRO B 122 13584 11726 13799 -2259 -316 1972 C ATOM 2906 O PRO B 122 -31.251 -15.894 -27.746 1.00104.39 O ANISOU 2906 O PRO B 122 13958 11604 14102 -2438 -422 1944 O ATOM 2907 CB PRO B 122 -32.989 -14.179 -25.625 1.00 91.55 C ANISOU 2907 CB PRO B 122 11780 10675 12330 -2670 163 2208 C ATOM 2908 CG PRO B 122 -32.896 -12.709 -25.434 1.00 90.16 C ANISOU 2908 CG PRO B 122 11300 10871 12085 -2405 227 2108 C ATOM 2909 CD PRO B 122 -31.675 -12.500 -24.596 1.00 89.61 C ANISOU 2909 CD PRO B 122 11541 10750 11758 -2097 202 2181 C ATOM 2910 N VAL B 123 -30.613 -13.735 -27.775 1.00113.53 N ANISOU 2910 N VAL B 123 14701 13313 15120 -1988 -409 1805 N ATOM 2911 CA VAL B 123 -30.097 -13.788 -29.137 1.00114.02 C ANISOU 2911 CA VAL B 123 14746 13322 15256 -1870 -629 1588 C ATOM 2912 C VAL B 123 -28.774 -14.551 -29.185 1.00115.43 C ANISOU 2912 C VAL B 123 15286 13209 15362 -1622 -762 1552 C ATOM 2913 O VAL B 123 -28.598 -15.460 -29.997 1.00117.42 O ANISOU 2913 O VAL B 123 15711 13204 15698 -1667 -892 1432 O ATOM 2914 CB VAL B 123 -29.901 -12.374 -29.720 1.00 79.98 C ANISOU 2914 CB VAL B 123 10119 9351 10919 -1670 -676 1456 C ATOM 2915 CG1 VAL B 123 -29.068 -12.427 -30.989 1.00 81.05 C ANISOU 2915 CG1 VAL B 123 10311 9439 11044 -1511 -871 1256 C ATOM 2916 CG2 VAL B 123 -31.249 -11.720 -29.985 1.00 79.07 C ANISOU 2916 CG2 VAL B 123 9626 9483 10936 -1883 -616 1446 C ATOM 2917 N GLU B 124 -27.852 -14.179 -28.302 1.00108.30 N ANISOU 2917 N GLU B 124 14489 12350 14310 -1351 -739 1638 N ATOM 2918 CA GLU B 124 -26.532 -14.799 -28.257 1.00108.84 C ANISOU 2918 CA GLU B 124 14839 12185 14330 -1059 -881 1603 C ATOM 2919 C GLU B 124 -26.594 -16.260 -27.826 1.00110.61 C ANISOU 2919 C GLU B 124 15459 11969 14599 -1168 -920 1740 C ATOM 2920 O GLU B 124 -25.892 -17.108 -28.378 1.00112.37 O ANISOU 2920 O GLU B 124 15898 11901 14896 -1018 -1070 1624 O ATOM 2921 CB GLU B 124 -25.611 -14.025 -27.313 1.00116.72 C ANISOU 2921 CB GLU B 124 15830 13357 15162 -772 -876 1677 C ATOM 2922 CG GLU B 124 -24.255 -14.678 -27.118 1.00116.76 C ANISOU 2922 CG GLU B 124 16086 13142 15137 -451 -1043 1660 C ATOM 2923 CD GLU B 124 -23.447 -14.030 -26.016 1.00114.90 C ANISOU 2923 CD GLU B 124 15863 13065 14728 -216 -1069 1762 C ATOM 2924 OE1 GLU B 124 -23.604 -12.810 -25.798 1.00113.24 O ANISOU 2924 OE1 GLU B 124 15405 13183 14438 -223 -981 1736 O ATOM 2925 OE2 GLU B 124 -22.661 -14.745 -25.360 1.00115.05 O ANISOU 2925 OE2 GLU B 124 16155 12865 14695 -20 -1200 1865 O ATOM 2926 N LEU B 125 -27.438 -16.549 -26.841 1.00123.00 N ANISOU 2926 N LEU B 125 17132 13481 16121 -1433 -772 1983 N ATOM 2927 CA LEU B 125 -27.550 -17.898 -26.295 1.00124.65 C ANISOU 2927 CA LEU B 125 17761 13249 16351 -1581 -796 2176 C ATOM 2928 C LEU B 125 -28.020 -18.894 -27.351 1.00126.54 C ANISOU 2928 C LEU B 125 18101 13172 16806 -1806 -887 2036 C ATOM 2929 O LEU B 125 -27.731 -20.087 -27.265 1.00128.02 O ANISOU 2929 O LEU B 125 18683 12899 17058 -1814 -995 2100 O ATOM 2930 CB LEU B 125 -28.490 -17.911 -25.086 1.00110.14 C ANISOU 2930 CB LEU B 125 15980 11474 14395 -1894 -566 2468 C ATOM 2931 CG LEU B 125 -28.534 -19.191 -24.250 1.00112.00 C ANISOU 2931 CG LEU B 125 16710 11264 14580 -2057 -569 2753 C ATOM 2932 CD1 LEU B 125 -27.130 -19.622 -23.856 1.00111.93 C ANISOU 2932 CD1 LEU B 125 17058 10998 14474 -1629 -802 2809 C ATOM 2933 CD2 LEU B 125 -29.399 -18.990 -23.016 1.00112.50 C ANISOU 2933 CD2 LEU B 125 16792 11496 14456 -2359 -289 3037 C ATOM 2934 N TYR B 126 -28.736 -18.397 -28.354 1.00117.81 N ANISOU 2934 N TYR B 126 16656 12299 15808 -1980 -869 1840 N ATOM 2935 CA TYR B 126 -29.223 -19.246 -29.434 1.00119.26 C ANISOU 2935 CA TYR B 126 16911 12231 16173 -2214 -979 1667 C ATOM 2936 C TYR B 126 -28.255 -19.300 -30.612 1.00120.19 C ANISOU 2936 C TYR B 126 17060 12296 16310 -1904 -1164 1355 C ATOM 2937 O TYR B 126 -27.837 -20.379 -31.031 1.00121.77 O ANISOU 2937 O TYR B 126 17584 12087 16596 -1854 -1292 1243 O ATOM 2938 CB TYR B 126 -30.602 -18.784 -29.913 1.00105.13 C ANISOU 2938 CB TYR B 126 14742 10715 14485 -2602 -895 1622 C ATOM 2939 CG TYR B 126 -31.074 -19.496 -31.161 1.00106.34 C ANISOU 2939 CG TYR B 126 14925 10680 14801 -2835 -1056 1394 C ATOM 2940 CD1 TYR B 126 -31.589 -20.784 -31.095 1.00107.78 C ANISOU 2940 CD1 TYR B 126 15405 10426 15121 -3174 -1087 1451 C ATOM 2941 CD2 TYR B 126 -31.007 -18.880 -32.405 1.00106.11 C ANISOU 2941 CD2 TYR B 126 14655 10895 14766 -2738 -1186 1124 C ATOM 2942 CE1 TYR B 126 -32.020 -21.441 -32.232 1.00109.02 C ANISOU 2942 CE1 TYR B 126 15608 10397 15418 -3404 -1254 1212 C ATOM 2943 CE2 TYR B 126 -31.436 -19.530 -33.548 1.00107.26 C ANISOU 2943 CE2 TYR B 126 14855 10883 15014 -2958 -1352 897 C ATOM 2944 CZ TYR B 126 -31.942 -20.809 -33.455 1.00108.83 C ANISOU 2944 CZ TYR B 126 15340 10650 15361 -3289 -1390 926 C ATOM 2945 OH TYR B 126 -32.371 -21.461 -34.589 1.00110.10 O ANISOU 2945 OH TYR B 126 15572 10643 15617 -3525 -1573 671 O ATOM 2946 N ASN B 127 -27.902 -18.134 -31.145 1.00 89.68 N ANISOU 2946 N ASN B 127 12873 8838 12363 -1702 -1165 1211 N ATOM 2947 CA ASN B 127 -27.133 -18.070 -32.384 1.00 90.97 C ANISOU 2947 CA ASN B 127 13014 9035 12515 -1479 -1292 906 C ATOM 2948 C ASN B 127 -25.614 -18.044 -32.223 1.00 91.54 C ANISOU 2948 C ASN B 127 13202 9066 12514 -1020 -1340 832 C ATOM 2949 O ASN B 127 -24.886 -18.089 -33.214 1.00 93.24 O ANISOU 2949 O ASN B 127 13410 9303 12716 -825 -1408 567 O ATOM 2950 CB ASN B 127 -27.586 -16.881 -33.236 1.00 98.15 C ANISOU 2950 CB ASN B 127 13537 10384 13372 -1548 -1285 786 C ATOM 2951 CG ASN B 127 -28.393 -17.306 -34.446 1.00 98.93 C ANISOU 2951 CG ASN B 127 13612 10436 13542 -1831 -1397 592 C ATOM 2952 OD1 ASN B 127 -28.130 -18.347 -35.049 1.00100.73 O ANISOU 2952 OD1 ASN B 127 14115 10343 13816 -1844 -1496 413 O ATOM 2953 ND2 ASN B 127 -29.384 -16.501 -34.808 1.00 97.10 N ANISOU 2953 ND2 ASN B 127 13054 10515 13323 -2045 -1401 611 N ATOM 2954 N PHE B 128 -25.135 -17.984 -30.985 1.00100.27 N ANISOU 2954 N PHE B 128 14405 10130 13564 -854 -1304 1057 N ATOM 2955 CA PHE B 128 -23.695 -17.907 -30.745 1.00 99.92 C ANISOU 2955 CA PHE B 128 14414 10083 13470 -415 -1378 996 C ATOM 2956 C PHE B 128 -23.162 -19.023 -29.846 1.00100.52 C ANISOU 2956 C PHE B 128 14879 9725 13590 -250 -1478 1154 C ATOM 2957 O PHE B 128 -21.966 -19.311 -29.852 1.00101.11 O ANISOU 2957 O PHE B 128 15033 9694 13690 135 -1592 1051 O ATOM 2958 CB PHE B 128 -23.315 -16.533 -30.185 1.00 93.80 C ANISOU 2958 CB PHE B 128 13346 9737 12557 -277 -1308 1077 C ATOM 2959 CG PHE B 128 -23.400 -15.424 -31.197 1.00 93.58 C ANISOU 2959 CG PHE B 128 12976 10090 12492 -311 -1262 894 C ATOM 2960 CD1 PHE B 128 -23.094 -15.660 -32.528 1.00 96.31 C ANISOU 2960 CD1 PHE B 128 13296 10428 12868 -269 -1309 621 C ATOM 2961 CD2 PHE B 128 -23.788 -14.148 -30.821 1.00 90.89 C ANISOU 2961 CD2 PHE B 128 12368 10098 12068 -384 -1172 993 C ATOM 2962 CE1 PHE B 128 -23.170 -14.646 -33.464 1.00 96.82 C ANISOU 2962 CE1 PHE B 128 13093 10835 12860 -319 -1276 489 C ATOM 2963 CE2 PHE B 128 -23.867 -13.129 -31.753 1.00 90.85 C ANISOU 2963 CE2 PHE B 128 12091 10397 12031 -413 -1155 856 C ATOM 2964 CZ PHE B 128 -23.557 -13.380 -33.077 1.00 93.84 C ANISOU 2964 CZ PHE B 128 12465 10772 12418 -392 -1211 623 C ATOM 2965 N ILE B 129 -24.049 -19.648 -29.078 1.00 96.79 N ANISOU 2965 N ILE B 129 14642 9003 13130 -543 -1437 1412 N ATOM 2966 CA ILE B 129 -23.644 -20.718 -28.167 1.00 97.54 C ANISOU 2966 CA ILE B 129 15168 8649 13244 -427 -1544 1624 C ATOM 2967 C ILE B 129 -24.112 -22.090 -28.649 1.00 99.92 C ANISOU 2967 C ILE B 129 15824 8415 13726 -627 -1619 1579 C ATOM 2968 O ILE B 129 -23.333 -23.045 -28.671 1.00101.34 O ANISOU 2968 O ILE B 129 16326 8171 14009 -353 -1786 1529 O ATOM 2969 CB ILE B 129 -24.127 -20.463 -26.715 1.00110.32 C ANISOU 2969 CB ILE B 129 16883 10343 14690 -594 -1441 2005 C ATOM 2970 CG1 ILE B 129 -23.169 -19.519 -25.982 1.00108.45 C ANISOU 2970 CG1 ILE B 129 16493 10435 14277 -247 -1479 2056 C ATOM 2971 CG2 ILE B 129 -24.170 -21.758 -25.927 1.00111.70 C ANISOU 2971 CG2 ILE B 129 17577 9979 14886 -660 -1532 2275 C ATOM 2972 CD1 ILE B 129 -23.193 -18.087 -26.457 1.00106.95 C ANISOU 2972 CD1 ILE B 129 15828 10778 14030 -227 -1369 1876 C ATOM 2973 N TRP B 130 -25.378 -22.185 -29.047 1.00126.62 N ANISOU 2973 N TRP B 130 19138 11807 17167 -1096 -1511 1581 N ATOM 2974 CA TRP B 130 -25.933 -23.457 -29.504 1.00128.69 C ANISOU 2974 CA TRP B 130 19731 11559 17607 -1365 -1585 1531 C ATOM 2975 C TRP B 130 -25.937 -23.601 -31.027 1.00129.96 C ANISOU 2975 C TRP B 130 19783 11717 17877 -1367 -1661 1114 C ATOM 2976 O TRP B 130 -25.146 -24.359 -31.588 1.00131.55 O ANISOU 2976 O TRP B 130 20227 11582 18175 -1088 -1801 885 O ATOM 2977 CB TRP B 130 -27.346 -23.660 -28.948 1.00121.06 C ANISOU 2977 CB TRP B 130 18787 10553 16656 -1934 -1435 1796 C ATOM 2978 CG TRP B 130 -27.381 -23.939 -27.475 1.00120.65 C ANISOU 2978 CG TRP B 130 19013 10344 16485 -1993 -1364 2215 C ATOM 2979 CD1 TRP B 130 -27.476 -23.022 -26.469 1.00118.94 C ANISOU 2979 CD1 TRP B 130 18612 10525 16056 -1979 -1204 2445 C ATOM 2980 CD2 TRP B 130 -27.322 -25.224 -26.843 1.00122.29 C ANISOU 2980 CD2 TRP B 130 19774 9941 16750 -2085 -1454 2458 C ATOM 2981 NE1 TRP B 130 -27.480 -23.656 -25.250 1.00119.50 N ANISOU 2981 NE1 TRP B 130 19086 10305 16013 -2064 -1181 2817 N ATOM 2982 CE2 TRP B 130 -27.386 -25.008 -25.452 1.00121.47 C ANISOU 2982 CE2 TRP B 130 19799 9925 16428 -2133 -1339 2854 C ATOM 2983 CE3 TRP B 130 -27.221 -26.535 -27.318 1.00124.27 C ANISOU 2983 CE3 TRP B 130 20453 9555 17208 -2131 -1627 2376 C ATOM 2984 CZ2 TRP B 130 -27.353 -26.053 -24.532 1.00122.79 C ANISOU 2984 CZ2 TRP B 130 20517 9578 16559 -2238 -1398 3205 C ATOM 2985 CZ3 TRP B 130 -27.188 -27.572 -26.402 1.00125.12 C ANISOU 2985 CZ3 TRP B 130 21105 9114 17321 -2223 -1693 2719 C ATOM 2986 CH2 TRP B 130 -27.254 -27.325 -25.026 1.00124.67 C ANISOU 2986 CH2 TRP B 130 21174 9170 17026 -2282 -1582 3147 C ATOM 2987 N VAL B 131 -26.826 -22.866 -31.690 1.00109.54 N ANISOU 2987 N VAL B 131 16838 9515 15267 -1664 -1576 1007 N ATOM 2988 CA VAL B 131 -26.945 -22.930 -33.145 1.00110.76 C ANISOU 2988 CA VAL B 131 16897 9719 15467 -1718 -1659 630 C ATOM 2989 C VAL B 131 -26.144 -21.821 -33.821 1.00109.96 C ANISOU 2989 C VAL B 131 16469 10090 15222 -1378 -1639 418 C ATOM 2990 O VAL B 131 -26.616 -20.695 -33.960 1.00108.58 O ANISOU 2990 O VAL B 131 15923 10379 14952 -1488 -1561 458 O ATOM 2991 CB VAL B 131 -28.415 -22.847 -33.597 1.00106.49 C ANISOU 2991 CB VAL B 131 16167 9304 14990 -2258 -1634 628 C ATOM 2992 CG1 VAL B 131 -28.517 -23.005 -35.106 1.00107.74 C ANISOU 2992 CG1 VAL B 131 16292 9486 15158 -2319 -1765 234 C ATOM 2993 CG2 VAL B 131 -29.243 -23.910 -32.892 1.00106.76 C ANISOU 2993 CG2 VAL B 131 16496 8894 15174 -2661 -1620 858 C ATOM 2994 N HIS B 132 -24.932 -22.154 -34.250 1.00 92.41 N ANISOU 2994 N HIS B 132 14383 7734 12995 -966 -1707 189 N ATOM 2995 CA HIS B 132 -24.012 -21.172 -34.814 1.00 92.63 C ANISOU 2995 CA HIS B 132 14120 8189 12887 -640 -1663 3 C ATOM 2996 C HIS B 132 -24.405 -20.717 -36.220 1.00 92.84 C ANISOU 2996 C HIS B 132 13960 8497 12817 -805 -1663 -281 C ATOM 2997 O HIS B 132 -24.121 -19.586 -36.614 1.00 92.35 O ANISOU 2997 O HIS B 132 13591 8888 12610 -716 -1598 -325 O ATOM 2998 CB HIS B 132 -22.593 -21.739 -34.814 1.00102.98 C ANISOU 2998 CB HIS B 132 15600 9281 14246 -150 -1717 -165 C ATOM 2999 CG HIS B 132 -22.198 -22.355 -33.507 1.00102.19 C ANISOU 2999 CG HIS B 132 15752 8835 14239 28 -1785 111 C ATOM 3000 ND1 HIS B 132 -21.612 -21.637 -32.492 1.00100.26 N ANISOU 3000 ND1 HIS B 132 15354 8828 13914 246 -1763 343 N ATOM 3001 CD2 HIS B 132 -22.325 -23.626 -33.049 1.00102.83 C ANISOU 3001 CD2 HIS B 132 16264 8334 14472 6 -1896 207 C ATOM 3002 CE1 HIS B 132 -21.384 -22.437 -31.461 1.00 99.69 C ANISOU 3002 CE1 HIS B 132 15605 8360 13915 362 -1866 576 C ATOM 3003 NE2 HIS B 132 -21.807 -23.647 -31.778 1.00101.48 N ANISOU 3003 NE2 HIS B 132 16196 8073 14288 222 -1944 513 N ATOM 3004 N HIS B 133 -25.059 -21.596 -36.972 1.00 96.57 N ANISOU 3004 N HIS B 133 14645 8689 13360 -1061 -1754 -467 N ATOM 3005 CA HIS B 133 -25.525 -21.252 -38.312 1.00 96.99 C ANISOU 3005 CA HIS B 133 14569 8992 13289 -1254 -1797 -731 C ATOM 3006 C HIS B 133 -26.790 -22.032 -38.665 1.00 97.38 C ANISOU 3006 C HIS B 133 14772 8781 13448 -1720 -1918 -771 C ATOM 3007 O HIS B 133 -26.923 -23.201 -38.303 1.00 98.82 O ANISOU 3007 O HIS B 133 15292 8455 13801 -1808 -1977 -766 O ATOM 3008 CB HIS B 133 -24.429 -21.507 -39.353 1.00104.06 C ANISOU 3008 CB HIS B 133 15575 9888 14076 -931 -1790 -1125 C ATOM 3009 CG HIS B 133 -24.131 -22.952 -39.577 1.00106.47 C ANISOU 3009 CG HIS B 133 16298 9633 14523 -840 -1871 -1366 C ATOM 3010 ND1 HIS B 133 -24.758 -23.705 -40.547 1.00107.54 N ANISOU 3010 ND1 HIS B 133 16659 9546 14655 -1107 -1984 -1650 N ATOM 3011 CD2 HIS B 133 -23.266 -23.798 -38.957 1.00107.90 C ANISOU 3011 CD2 HIS B 133 16734 9401 14863 -498 -1882 -1377 C ATOM 3012 CE1 HIS B 133 -24.299 -24.941 -40.518 1.00109.57 C ANISOU 3012 CE1 HIS B 133 17303 9259 15071 -938 -2042 -1837 C ATOM 3013 NE2 HIS B 133 -23.390 -25.020 -39.557 1.00109.22 N ANISOU 3013 NE2 HIS B 133 17280 9084 15135 -553 -1985 -1665 N ATOM 3014 N PRO B 134 -27.729 -21.385 -39.373 1.00127.95 N ANISOU 3014 N PRO B 134 18394 12987 17232 -2029 -1977 -806 N ATOM 3015 CA PRO B 134 -27.620 -20.014 -39.880 1.00126.62 C ANISOU 3015 CA PRO B 134 17874 13373 16863 -1939 -1940 -801 C ATOM 3016 C PRO B 134 -28.161 -18.966 -38.910 1.00124.19 C ANISOU 3016 C PRO B 134 17226 13363 16596 -2008 -1851 -442 C ATOM 3017 O PRO B 134 -28.892 -19.302 -37.978 1.00123.90 O ANISOU 3017 O PRO B 134 17186 13164 16725 -2220 -1819 -212 O ATOM 3018 CB PRO B 134 -28.482 -20.052 -41.144 1.00103.57 C ANISOU 3018 CB PRO B 134 14928 10574 13850 -2259 -2112 -1022 C ATOM 3019 CG PRO B 134 -29.474 -21.175 -40.916 1.00104.44 C ANISOU 3019 CG PRO B 134 15222 10282 14180 -2643 -2224 -1013 C ATOM 3020 CD PRO B 134 -29.023 -21.990 -39.729 1.00105.22 C ANISOU 3020 CD PRO B 134 15567 9943 14467 -2515 -2117 -843 C ATOM 3021 N TRP B 135 -27.795 -17.707 -39.136 1.00 86.72 N ANISOU 3021 N TRP B 135 12212 9043 11694 -1836 -1799 -403 N ATOM 3022 CA TRP B 135 -28.323 -16.596 -38.352 1.00 83.94 C ANISOU 3022 CA TRP B 135 11533 8988 11371 -1880 -1726 -117 C ATOM 3023 C TRP B 135 -29.822 -16.440 -38.595 1.00 81.78 C ANISOU 3023 C TRP B 135 11050 8829 11193 -2269 -1833 -49 C ATOM 3024 O TRP B 135 -30.270 -16.372 -39.740 1.00 81.52 O ANISOU 3024 O TRP B 135 10977 8917 11081 -2423 -1996 -222 O ATOM 3025 CB TRP B 135 -27.603 -15.296 -38.708 1.00101.26 C ANISOU 3025 CB TRP B 135 13524 11567 13384 -1634 -1678 -121 C ATOM 3026 CG TRP B 135 -28.135 -14.112 -37.968 1.00 98.22 C ANISOU 3026 CG TRP B 135 12827 11455 13036 -1656 -1618 134 C ATOM 3027 CD1 TRP B 135 -29.042 -13.199 -38.421 1.00 94.92 C ANISOU 3027 CD1 TRP B 135 12143 11316 12607 -1810 -1703 193 C ATOM 3028 CD2 TRP B 135 -27.786 -13.706 -36.641 1.00 98.28 C ANISOU 3028 CD2 TRP B 135 12771 11475 13096 -1495 -1472 345 C ATOM 3029 NE1 TRP B 135 -29.285 -12.253 -37.455 1.00 92.62 N ANISOU 3029 NE1 TRP B 135 11621 11191 12380 -1741 -1599 410 N ATOM 3030 CE2 TRP B 135 -28.523 -12.542 -36.350 1.00 94.68 C ANISOU 3030 CE2 TRP B 135 12010 11302 12661 -1562 -1449 499 C ATOM 3031 CE3 TRP B 135 -26.922 -14.215 -35.665 1.00100.45 C ANISOU 3031 CE3 TRP B 135 13228 11546 13393 -1288 -1379 414 C ATOM 3032 CZ2 TRP B 135 -28.425 -11.878 -35.131 1.00 93.89 C ANISOU 3032 CZ2 TRP B 135 11798 11290 12587 -1445 -1312 689 C ATOM 3033 CZ3 TRP B 135 -26.825 -13.555 -34.454 1.00 99.19 C ANISOU 3033 CZ3 TRP B 135 12959 11492 13237 -1188 -1268 627 C ATOM 3034 CH2 TRP B 135 -27.571 -12.399 -34.197 1.00 96.26 C ANISOU 3034 CH2 TRP B 135 12298 11406 12869 -1273 -1222 748 C ATOM 3035 N ALA B 136 -30.596 -16.397 -37.515 1.00107.56 N ANISOU 3035 N ALA B 136 14173 12075 14619 -2430 -1741 195 N ATOM 3036 CA ALA B 136 -32.053 -16.427 -37.616 1.00106.38 C ANISOU 3036 CA ALA B 136 13790 12010 14621 -2818 -1820 253 C ATOM 3037 C ALA B 136 -32.739 -15.066 -37.457 1.00103.37 C ANISOU 3037 C ALA B 136 12970 12049 14256 -2811 -1801 395 C ATOM 3038 O ALA B 136 -33.911 -14.920 -37.801 1.00102.94 O ANISOU 3038 O ALA B 136 12648 12142 14323 -3082 -1914 398 O ATOM 3039 CB ALA B 136 -32.622 -17.419 -36.609 1.00 88.76 C ANISOU 3039 CB ALA B 136 11679 9468 12578 -3077 -1713 408 C ATOM 3040 N PHE B 137 -32.019 -14.077 -36.938 1.00111.66 N ANISOU 3040 N PHE B 137 13938 13281 15205 -2497 -1676 501 N ATOM 3041 CA PHE B 137 -32.638 -12.793 -36.601 1.00108.64 C ANISOU 3041 CA PHE B 137 13176 13234 14868 -2455 -1636 640 C ATOM 3042 C PHE B 137 -32.531 -11.687 -37.654 1.00106.00 C ANISOU 3042 C PHE B 137 12688 13178 14410 -2322 -1802 567 C ATOM 3043 O PHE B 137 -32.700 -10.509 -37.337 1.00103.28 O ANISOU 3043 O PHE B 137 12099 13061 14081 -2184 -1764 679 O ATOM 3044 CB PHE B 137 -32.102 -12.301 -35.255 1.00101.28 C ANISOU 3044 CB PHE B 137 12241 12324 13916 -2238 -1402 816 C ATOM 3045 CG PHE B 137 -32.245 -13.309 -34.151 1.00103.62 C ANISOU 3045 CG PHE B 137 12715 12364 14291 -2376 -1241 939 C ATOM 3046 CD1 PHE B 137 -33.485 -13.571 -33.593 1.00103.65 C ANISOU 3046 CD1 PHE B 137 12525 12394 14462 -2685 -1147 1052 C ATOM 3047 CD2 PHE B 137 -31.144 -14.005 -33.683 1.00105.88 C ANISOU 3047 CD2 PHE B 137 13359 12385 14487 -2203 -1188 952 C ATOM 3048 CE1 PHE B 137 -33.624 -14.503 -32.583 1.00105.49 C ANISOU 3048 CE1 PHE B 137 12959 12385 14738 -2852 -983 1197 C ATOM 3049 CE2 PHE B 137 -31.275 -14.938 -32.673 1.00107.37 C ANISOU 3049 CE2 PHE B 137 13761 12307 14727 -2332 -1067 1103 C ATOM 3050 CZ PHE B 137 -32.517 -15.187 -32.123 1.00107.36 C ANISOU 3050 CZ PHE B 137 13606 12326 14859 -2675 -955 1237 C ATOM 3051 N GLY B 138 -32.259 -12.060 -38.899 1.00108.07 N ANISOU 3051 N GLY B 138 13118 13408 14537 -2368 -1985 379 N ATOM 3052 CA GLY B 138 -32.178 -11.087 -39.975 1.00106.23 C ANISOU 3052 CA GLY B 138 12795 13428 14138 -2285 -2155 332 C ATOM 3053 C GLY B 138 -30.965 -10.176 -39.950 1.00104.53 C ANISOU 3053 C GLY B 138 12652 13323 13743 -1977 -2047 367 C ATOM 3054 O GLY B 138 -30.100 -10.291 -39.083 1.00105.46 O ANISOU 3054 O GLY B 138 12871 13334 13863 -1799 -1850 408 O ATOM 3055 N ASP B 139 -30.910 -9.261 -40.915 1.00109.19 N ANISOU 3055 N ASP B 139 13190 14128 14170 -1932 -2192 361 N ATOM 3056 CA ASP B 139 -29.828 -8.287 -41.006 1.00107.71 C ANISOU 3056 CA ASP B 139 13051 14062 13811 -1700 -2100 408 C ATOM 3057 C ASP B 139 -29.909 -7.227 -39.910 1.00104.93 C ANISOU 3057 C ASP B 139 12483 13783 13604 -1549 -1985 605 C ATOM 3058 O ASP B 139 -28.886 -6.800 -39.374 1.00104.36 O ANISOU 3058 O ASP B 139 12468 13708 13474 -1362 -1826 637 O ATOM 3059 CB ASP B 139 -29.866 -7.606 -42.377 1.00130.12 C ANISOU 3059 CB ASP B 139 15928 17094 16416 -1745 -2300 383 C ATOM 3060 CG ASP B 139 -28.604 -6.820 -42.677 1.00129.16 C ANISOU 3060 CG ASP B 139 15921 17080 16075 -1572 -2180 399 C ATOM 3061 OD1 ASP B 139 -27.629 -6.928 -41.903 1.00129.85 O ANISOU 3061 OD1 ASP B 139 16049 17092 16197 -1413 -1960 385 O ATOM 3062 OD2 ASP B 139 -28.587 -6.090 -43.690 1.00128.50 O ANISOU 3062 OD2 ASP B 139 15885 17160 15779 -1612 -2317 435 O ATOM 3063 N ALA B 140 -31.126 -6.809 -39.577 1.00101.62 N ANISOU 3063 N ALA B 140 11800 13433 13377 -1628 -2068 713 N ATOM 3064 CA ALA B 140 -31.332 -5.820 -38.525 1.00 99.31 C ANISOU 3064 CA ALA B 140 11299 13204 13230 -1479 -1950 861 C ATOM 3065 C ALA B 140 -30.932 -6.383 -37.168 1.00100.84 C ANISOU 3065 C ALA B 140 11553 13262 13499 -1423 -1696 883 C ATOM 3066 O ALA B 140 -30.307 -5.698 -36.360 1.00 99.97 O ANISOU 3066 O ALA B 140 11444 13171 13371 -1241 -1558 947 O ATOM 3067 CB ALA B 140 -32.781 -5.364 -38.504 1.00 91.75 C ANISOU 3067 CB ALA B 140 10014 12361 12486 -1563 -2083 932 C ATOM 3068 N GLY B 141 -31.298 -7.638 -36.926 1.00 79.89 N ANISOU 3068 N GLY B 141 8975 10461 10918 -1595 -1656 837 N ATOM 3069 CA GLY B 141 -30.951 -8.308 -35.687 1.00 82.22 C ANISOU 3069 CA GLY B 141 9387 10598 11256 -1567 -1444 887 C ATOM 3070 C GLY B 141 -29.457 -8.530 -35.576 1.00 83.24 C ANISOU 3070 C GLY B 141 9781 10624 11224 -1366 -1376 834 C ATOM 3071 O GLY B 141 -28.908 -8.579 -34.478 1.00 84.18 O ANISOU 3071 O GLY B 141 9975 10676 11334 -1240 -1229 906 O ATOM 3072 N CYS B 142 -28.799 -8.670 -36.722 1.00108.01 N ANISOU 3072 N CYS B 142 13050 13767 14223 -1335 -1485 698 N ATOM 3073 CA CYS B 142 -27.351 -8.821 -36.761 1.00109.25 C ANISOU 3073 CA CYS B 142 13392 13873 14244 -1132 -1416 614 C ATOM 3074 C CYS B 142 -26.655 -7.497 -36.459 1.00105.52 C ANISOU 3074 C CYS B 142 12807 13579 13705 -951 -1360 688 C ATOM 3075 O CYS B 142 -25.771 -7.430 -35.604 1.00105.35 O ANISOU 3075 O CYS B 142 12832 13525 13672 -784 -1255 714 O ATOM 3076 CB CYS B 142 -26.912 -9.340 -38.132 1.00100.84 C ANISOU 3076 CB CYS B 142 12481 12797 13035 -1170 -1511 417 C ATOM 3077 SG CYS B 142 -25.123 -9.356 -38.392 1.00102.22 S ANISOU 3077 SG CYS B 142 12792 12997 13050 -911 -1402 276 S ATOM 3078 N ARG B 143 -27.063 -6.447 -37.165 1.00 99.73 N ANISOU 3078 N ARG B 143 11939 13021 12934 -993 -1455 727 N ATOM 3079 CA ARG B 143 -26.472 -5.123 -36.994 1.00 96.23 C ANISOU 3079 CA ARG B 143 11413 12711 12440 -861 -1424 800 C ATOM 3080 C ARG B 143 -26.890 -4.469 -35.683 1.00 94.72 C ANISOU 3080 C ARG B 143 11085 12521 12385 -784 -1339 921 C ATOM 3081 O ARG B 143 -26.087 -3.805 -35.030 1.00 93.47 O ANISOU 3081 O ARG B 143 10929 12388 12195 -647 -1262 945 O ATOM 3082 CB ARG B 143 -26.853 -4.216 -38.166 1.00 92.64 C ANISOU 3082 CB ARG B 143 10902 12397 11901 -935 -1577 834 C ATOM 3083 CG ARG B 143 -26.184 -4.577 -39.482 1.00 94.28 C ANISOU 3083 CG ARG B 143 11274 12661 11886 -995 -1624 712 C ATOM 3084 CD ARG B 143 -26.640 -3.648 -40.595 1.00 93.05 C ANISOU 3084 CD ARG B 143 11102 12643 11608 -1087 -1800 791 C ATOM 3085 NE ARG B 143 -25.558 -3.331 -41.524 1.00 93.83 N ANISOU 3085 NE ARG B 143 11347 12855 11451 -1096 -1751 740 N ATOM 3086 CZ ARG B 143 -25.340 -3.969 -42.668 1.00 96.51 C ANISOU 3086 CZ ARG B 143 11849 13255 11564 -1198 -1784 601 C ATOM 3087 NH1 ARG B 143 -26.131 -4.966 -43.037 1.00 98.78 N ANISOU 3087 NH1 ARG B 143 12189 13476 11866 -1303 -1902 492 N ATOM 3088 NH2 ARG B 143 -24.329 -3.609 -43.445 1.00 97.86 N ANISOU 3088 NH2 ARG B 143 12132 13561 11488 -1214 -1689 558 N ATOM 3089 N GLY B 144 -28.149 -4.661 -35.302 1.00 96.22 N ANISOU 3089 N GLY B 144 11145 12695 12720 -885 -1348 976 N ATOM 3090 CA GLY B 144 -28.682 -4.065 -34.090 1.00 95.62 C ANISOU 3090 CA GLY B 144 10928 12646 12759 -820 -1235 1062 C ATOM 3091 C GLY B 144 -28.095 -4.668 -32.831 1.00 97.97 C ANISOU 3091 C GLY B 144 11358 12848 13018 -753 -1069 1079 C ATOM 3092 O GLY B 144 -27.957 -3.988 -31.814 1.00 97.58 O ANISOU 3092 O GLY B 144 11273 12838 12964 -642 -967 1121 O ATOM 3093 N TYR B 145 -27.755 -5.951 -32.901 1.00 88.70 N ANISOU 3093 N TYR B 145 10362 11533 11807 -814 -1060 1044 N ATOM 3094 CA TYR B 145 -27.134 -6.652 -31.782 1.00 91.63 C ANISOU 3094 CA TYR B 145 10910 11779 12127 -738 -952 1085 C ATOM 3095 C TYR B 145 -25.809 -6.004 -31.400 1.00 89.02 C ANISOU 3095 C TYR B 145 10635 11501 11688 -522 -948 1059 C ATOM 3096 O TYR B 145 -25.645 -5.517 -30.281 1.00 88.02 O ANISOU 3096 O TYR B 145 10509 11413 11524 -434 -870 1119 O ATOM 3097 CB TYR B 145 -26.907 -8.120 -32.143 1.00 79.85 C ANISOU 3097 CB TYR B 145 9628 10077 10635 -812 -991 1037 C ATOM 3098 CG TYR B 145 -26.106 -8.903 -31.127 1.00 81.75 C ANISOU 3098 CG TYR B 145 10094 10148 10818 -692 -937 1091 C ATOM 3099 CD1 TYR B 145 -26.720 -9.469 -30.017 1.00 83.25 C ANISOU 3099 CD1 TYR B 145 10378 10230 11023 -794 -832 1235 C ATOM 3100 CD2 TYR B 145 -24.737 -9.089 -31.285 1.00 80.91 C ANISOU 3100 CD2 TYR B 145 10103 9997 10640 -479 -995 1005 C ATOM 3101 CE1 TYR B 145 -25.994 -10.190 -29.089 1.00 83.22 C ANISOU 3101 CE1 TYR B 145 10624 10055 10942 -681 -820 1317 C ATOM 3102 CE2 TYR B 145 -24.004 -9.807 -30.361 1.00 81.17 C ANISOU 3102 CE2 TYR B 145 10335 9870 10635 -336 -996 1063 C ATOM 3103 CZ TYR B 145 -24.637 -10.356 -29.267 1.00 82.23 C ANISOU 3103 CZ TYR B 145 10606 9874 10762 -435 -925 1232 C ATOM 3104 OH TYR B 145 -23.910 -11.074 -28.345 1.00 82.06 O ANISOU 3104 OH TYR B 145 10825 9678 10678 -289 -961 1322 O ATOM 3105 N TYR B 146 -24.868 -6.001 -32.339 1.00 95.37 N ANISOU 3105 N TYR B 146 11478 12325 12433 -454 -1028 956 N ATOM 3106 CA TYR B 146 -23.539 -5.451 -32.098 1.00 92.95 C ANISOU 3106 CA TYR B 146 11180 12089 12048 -280 -1029 913 C ATOM 3107 C TYR B 146 -23.588 -3.951 -31.825 1.00 89.57 C ANISOU 3107 C TYR B 146 10612 11803 11618 -255 -1021 953 C ATOM 3108 O TYR B 146 -22.713 -3.407 -31.151 1.00 88.21 O ANISOU 3108 O TYR B 146 10438 11677 11400 -141 -1011 944 O ATOM 3109 CB TYR B 146 -22.609 -5.752 -33.274 1.00 80.57 C ANISOU 3109 CB TYR B 146 9642 10549 10423 -242 -1074 777 C ATOM 3110 CG TYR B 146 -22.234 -7.212 -33.391 1.00 85.17 C ANISOU 3110 CG TYR B 146 10390 10955 11016 -188 -1083 694 C ATOM 3111 CD1 TYR B 146 -21.155 -7.731 -32.685 1.00 86.44 C ANISOU 3111 CD1 TYR B 146 10626 11042 11174 12 -1084 665 C ATOM 3112 CD2 TYR B 146 -22.958 -8.072 -34.206 1.00 88.06 C ANISOU 3112 CD2 TYR B 146 10845 11208 11406 -327 -1117 634 C ATOM 3113 CE1 TYR B 146 -20.809 -9.065 -32.790 1.00 90.48 C ANISOU 3113 CE1 TYR B 146 11308 11346 11723 100 -1113 587 C ATOM 3114 CE2 TYR B 146 -22.619 -9.407 -34.317 1.00 92.85 C ANISOU 3114 CE2 TYR B 146 11638 11601 12041 -271 -1134 539 C ATOM 3115 CZ TYR B 146 -21.544 -9.898 -33.607 1.00 94.44 C ANISOU 3115 CZ TYR B 146 11923 11705 12256 -43 -1129 519 C ATOM 3116 OH TYR B 146 -21.203 -11.227 -33.714 1.00 99.18 O ANISOU 3116 OH TYR B 146 12726 12049 12910 51 -1165 424 O ATOM 3117 N PHE B 147 -24.612 -3.289 -32.352 1.00102.91 N ANISOU 3117 N PHE B 147 12186 13547 13370 -357 -1049 991 N ATOM 3118 CA PHE B 147 -24.807 -1.868 -32.100 1.00100.57 C ANISOU 3118 CA PHE B 147 11778 13329 13107 -318 -1055 1028 C ATOM 3119 C PHE B 147 -25.203 -1.651 -30.647 1.00102.15 C ANISOU 3119 C PHE B 147 11967 13515 13332 -252 -950 1063 C ATOM 3120 O PHE B 147 -24.613 -0.826 -29.950 1.00101.55 O ANISOU 3120 O PHE B 147 11902 13465 13216 -157 -933 1043 O ATOM 3121 CB PHE B 147 -25.880 -1.290 -33.024 1.00 78.98 C ANISOU 3121 CB PHE B 147 8922 10632 10453 -407 -1145 1067 C ATOM 3122 CG PHE B 147 -26.236 0.139 -32.719 1.00 77.50 C ANISOU 3122 CG PHE B 147 8633 10470 10343 -335 -1166 1107 C ATOM 3123 CD1 PHE B 147 -25.468 1.178 -33.217 1.00 75.61 C ANISOU 3123 CD1 PHE B 147 8431 10242 10057 -312 -1236 1116 C ATOM 3124 CD2 PHE B 147 -27.338 0.444 -31.935 1.00 78.81 C ANISOU 3124 CD2 PHE B 147 8669 10636 10637 -296 -1103 1126 C ATOM 3125 CE1 PHE B 147 -25.789 2.493 -32.940 1.00 75.48 C ANISOU 3125 CE1 PHE B 147 8361 10188 10130 -242 -1274 1148 C ATOM 3126 CE2 PHE B 147 -27.664 1.757 -31.653 1.00 78.68 C ANISOU 3126 CE2 PHE B 147 8570 10612 10712 -192 -1124 1129 C ATOM 3127 CZ PHE B 147 -26.888 2.783 -32.157 1.00 76.92 C ANISOU 3127 CZ PHE B 147 8422 10351 10452 -160 -1225 1143 C ATOM 3128 N LEU B 148 -26.211 -2.395 -30.202 1.00 88.11 N ANISOU 3128 N LEU B 148 10171 11701 11606 -328 -872 1107 N ATOM 3129 CA LEU B 148 -26.698 -2.294 -28.832 1.00 90.97 C ANISOU 3129 CA LEU B 148 10534 12077 11953 -296 -726 1142 C ATOM 3130 C LEU B 148 -25.605 -2.629 -27.828 1.00 90.86 C ANISOU 3130 C LEU B 148 10713 12028 11783 -196 -700 1146 C ATOM 3131 O LEU B 148 -25.475 -1.967 -26.800 1.00 91.47 O ANISOU 3131 O LEU B 148 10817 12155 11784 -115 -636 1132 O ATOM 3132 CB LEU B 148 -27.891 -3.228 -28.622 1.00 74.14 C ANISOU 3132 CB LEU B 148 8355 9921 9894 -450 -624 1203 C ATOM 3133 CG LEU B 148 -28.510 -3.230 -27.221 1.00 78.52 C ANISOU 3133 CG LEU B 148 8911 10520 10402 -462 -419 1249 C ATOM 3134 CD1 LEU B 148 -29.131 -1.879 -26.901 1.00 77.43 C ANISOU 3134 CD1 LEU B 148 8574 10505 10341 -365 -350 1184 C ATOM 3135 CD2 LEU B 148 -29.531 -4.350 -27.077 1.00 80.38 C ANISOU 3135 CD2 LEU B 148 9122 10718 10701 -674 -305 1329 C ATOM 3136 N ARG B 149 -24.816 -3.655 -28.135 1.00 88.38 N ANISOU 3136 N ARG B 149 10536 11625 11420 -186 -769 1149 N ATOM 3137 CA ARG B 149 -23.741 -4.081 -27.245 1.00 88.56 C ANISOU 3137 CA ARG B 149 10730 11606 11314 -62 -797 1162 C ATOM 3138 C ARG B 149 -22.662 -3.019 -27.076 1.00 85.66 C ANISOU 3138 C ARG B 149 10313 11339 10896 62 -875 1081 C ATOM 3139 O ARG B 149 -22.225 -2.749 -25.961 1.00 86.08 O ANISOU 3139 O ARG B 149 10449 11423 10835 144 -878 1086 O ATOM 3140 CB ARG B 149 -23.115 -5.388 -27.732 1.00123.79 C ANISOU 3140 CB ARG B 149 15325 15929 15782 -36 -875 1159 C ATOM 3141 CG ARG B 149 -23.776 -6.634 -27.172 1.00127.17 C ANISOU 3141 CG ARG B 149 15932 16189 16197 -127 -814 1276 C ATOM 3142 CD ARG B 149 -22.996 -7.879 -27.550 1.00128.68 C ANISOU 3142 CD ARG B 149 16296 16191 16407 -45 -919 1255 C ATOM 3143 NE ARG B 149 -23.208 -8.969 -26.602 1.00131.07 N ANISOU 3143 NE ARG B 149 16855 16295 16651 -71 -899 1406 N ATOM 3144 CZ ARG B 149 -22.393 -9.242 -25.588 1.00131.06 C ANISOU 3144 CZ ARG B 149 17032 16238 16526 93 -973 1485 C ATOM 3145 NH1 ARG B 149 -21.307 -8.506 -25.393 1.00129.03 N ANISOU 3145 NH1 ARG B 149 16683 16128 16214 290 -1074 1401 N ATOM 3146 NH2 ARG B 149 -22.660 -10.252 -24.772 1.00133.04 N ANISOU 3146 NH2 ARG B 149 17559 16285 16705 45 -962 1658 N ATOM 3147 N ASP B 150 -22.241 -2.410 -28.179 1.00 96.54 N ANISOU 3147 N ASP B 150 11568 12771 12342 49 -941 1009 N ATOM 3148 CA ASP B 150 -21.220 -1.372 -28.116 1.00 94.73 C ANISOU 3148 CA ASP B 150 11277 12629 12088 111 -1007 937 C ATOM 3149 C ASP B 150 -21.749 -0.115 -27.438 1.00 94.98 C ANISOU 3149 C ASP B 150 11274 12691 12123 105 -970 928 C ATOM 3150 O ASP B 150 -21.065 0.481 -26.607 1.00 95.81 O ANISOU 3150 O ASP B 150 11414 12832 12158 167 -1009 875 O ATOM 3151 CB ASP B 150 -20.681 -1.045 -29.508 1.00112.66 C ANISOU 3151 CB ASP B 150 13445 14951 14409 54 -1054 884 C ATOM 3152 CG ASP B 150 -19.585 -1.996 -29.944 1.00114.05 C ANISOU 3152 CG ASP B 150 13632 15140 14561 124 -1090 818 C ATOM 3153 OD1 ASP B 150 -19.712 -3.212 -29.682 1.00115.68 O ANISOU 3153 OD1 ASP B 150 13946 15247 14760 184 -1088 835 O ATOM 3154 OD2 ASP B 150 -18.591 -1.526 -30.537 1.00113.71 O ANISOU 3154 OD2 ASP B 150 13487 15199 14516 119 -1111 744 O ATOM 3155 N ALA B 151 -22.970 0.278 -27.790 1.00 77.64 N ANISOU 3155 N ALA B 151 9003 10477 10018 43 -909 960 N ATOM 3156 CA ALA B 151 -23.581 1.483 -27.238 1.00 79.14 C ANISOU 3156 CA ALA B 151 9147 10673 10250 75 -866 925 C ATOM 3157 C ALA B 151 -23.696 1.425 -25.717 1.00 82.69 C ANISOU 3157 C ALA B 151 9701 11145 10573 142 -768 896 C ATOM 3158 O ALA B 151 -23.444 2.414 -25.030 1.00 84.25 O ANISOU 3158 O ALA B 151 9931 11350 10730 202 -773 808 O ATOM 3159 CB ALA B 151 -24.946 1.719 -27.864 1.00 68.06 C ANISOU 3159 CB ALA B 151 7610 9257 8995 31 -829 963 C ATOM 3160 N CYS B 152 -24.074 0.262 -25.196 1.00 82.98 N ANISOU 3160 N CYS B 152 9819 11181 10529 116 -679 971 N ATOM 3161 CA CYS B 152 -24.242 0.089 -23.756 1.00 86.90 C ANISOU 3161 CA CYS B 152 10457 11714 10848 152 -568 976 C ATOM 3162 C CYS B 152 -22.919 0.156 -22.994 1.00 86.12 C ANISOU 3162 C CYS B 152 10513 11634 10573 240 -697 937 C ATOM 3163 O CYS B 152 -22.860 0.702 -21.892 1.00 88.98 O ANISOU 3163 O CYS B 152 10979 12049 10779 288 -660 872 O ATOM 3164 CB CYS B 152 -24.971 -1.221 -23.450 1.00 87.37 C ANISOU 3164 CB CYS B 152 10594 11746 10858 59 -443 1105 C ATOM 3165 SG CYS B 152 -26.730 -1.201 -23.871 1.00 90.93 S ANISOU 3165 SG CYS B 152 10820 12234 11496 -67 -255 1128 S ATOM 3166 N THR B 153 -21.862 -0.401 -23.578 1.00 95.32 N ANISOU 3166 N THR B 153 11685 12772 11762 267 -853 956 N ATOM 3167 CA THR B 153 -20.546 -0.372 -22.946 1.00 94.86 C ANISOU 3167 CA THR B 153 11711 12753 11579 361 -1014 911 C ATOM 3168 C THR B 153 -20.008 1.051 -22.873 1.00 95.28 C ANISOU 3168 C THR B 153 11682 12863 11658 363 -1088 769 C ATOM 3169 O THR B 153 -19.395 1.438 -21.878 1.00 97.16 O ANISOU 3169 O THR B 153 12015 13153 11748 412 -1177 700 O ATOM 3170 CB THR B 153 -19.529 -1.251 -23.689 1.00114.10 C ANISOU 3170 CB THR B 153 14106 15161 14084 415 -1151 931 C ATOM 3171 OG1 THR B 153 -19.353 -0.758 -25.023 1.00112.08 O ANISOU 3171 OG1 THR B 153 13662 14924 13999 353 -1156 869 O ATOM 3172 CG2 THR B 153 -20.014 -2.682 -23.744 1.00115.06 C ANISOU 3172 CG2 THR B 153 14355 15168 14195 414 -1102 1059 C ATOM 3173 N TYR B 154 -20.233 1.824 -23.933 1.00 90.69 N ANISOU 3173 N TYR B 154 10947 12256 11255 295 -1071 732 N ATOM 3174 CA TYR B 154 -19.866 3.234 -23.933 1.00 90.90 C ANISOU 3174 CA TYR B 154 10925 12278 11335 265 -1133 616 C ATOM 3175 C TYR B 154 -20.659 3.975 -22.866 1.00 95.42 C ANISOU 3175 C TYR B 154 11599 12829 11826 307 -1039 536 C ATOM 3176 O TYR B 154 -20.101 4.766 -22.106 1.00 97.75 O ANISOU 3176 O TYR B 154 11970 13132 12038 321 -1117 411 O ATOM 3177 CB TYR B 154 -20.108 3.874 -25.302 1.00102.40 C ANISOU 3177 CB TYR B 154 12248 13679 12981 178 -1131 639 C ATOM 3178 CG TYR B 154 -19.055 3.553 -26.341 1.00 99.92 C ANISOU 3178 CG TYR B 154 11832 13417 12716 113 -1213 658 C ATOM 3179 CD1 TYR B 154 -17.754 4.019 -26.204 1.00 99.75 C ANISOU 3179 CD1 TYR B 154 11758 13459 12684 77 -1324 577 C ATOM 3180 CD2 TYR B 154 -19.367 2.808 -27.470 1.00 98.08 C ANISOU 3180 CD2 TYR B 154 11541 13186 12536 77 -1171 737 C ATOM 3181 CE1 TYR B 154 -16.790 3.739 -27.153 1.00 97.91 C ANISOU 3181 CE1 TYR B 154 11390 13310 12500 15 -1356 576 C ATOM 3182 CE2 TYR B 154 -18.410 2.520 -28.423 1.00 97.01 C ANISOU 3182 CE2 TYR B 154 11317 13122 12420 25 -1207 724 C ATOM 3183 CZ TYR B 154 -17.123 2.989 -28.260 1.00 96.92 C ANISOU 3183 CZ TYR B 154 11226 13193 12405 -1 -1282 644 C ATOM 3184 OH TYR B 154 -16.168 2.707 -29.208 1.00 96.40 O ANISOU 3184 OH TYR B 154 11032 13234 12363 -56 -1275 613 O ATOM 3185 N ALA B 155 -21.962 3.715 -22.817 1.00 84.71 N ANISOU 3185 N ALA B 155 10232 11457 10498 320 -866 587 N ATOM 3186 CA ALA B 155 -22.836 4.343 -21.832 1.00 89.76 C ANISOU 3186 CA ALA B 155 10935 12104 11066 377 -719 489 C ATOM 3187 C ALA B 155 -22.402 4.021 -20.407 1.00 92.45 C ANISOU 3187 C ALA B 155 11486 12529 11112 415 -710 444 C ATOM 3188 O ALA B 155 -22.412 4.890 -19.537 1.00 96.39 O ANISOU 3188 O ALA B 155 12086 13039 11500 460 -687 285 O ATOM 3189 CB ALA B 155 -24.280 3.917 -22.057 1.00 85.50 C ANISOU 3189 CB ALA B 155 10286 11578 10622 369 -520 559 C ATOM 3190 N THR B 156 -22.011 2.772 -20.176 1.00 83.75 N ANISOU 3190 N THR B 156 10475 11472 9873 401 -746 581 N ATOM 3191 CA THR B 156 -21.540 2.350 -18.863 1.00 85.40 C ANISOU 3191 CA THR B 156 10919 11757 9770 439 -785 585 C ATOM 3192 C THR B 156 -20.195 2.983 -18.529 1.00 84.91 C ANISOU 3192 C THR B 156 10901 11724 9638 475 -1040 461 C ATOM 3193 O THR B 156 -20.022 3.564 -17.458 1.00 88.19 O ANISOU 3193 O THR B 156 11476 12196 9838 500 -1069 334 O ATOM 3194 CB THR B 156 -21.419 0.818 -18.765 1.00 86.44 C ANISOU 3194 CB THR B 156 11164 11879 9801 429 -802 793 C ATOM 3195 OG1 THR B 156 -22.723 0.229 -18.857 1.00 88.30 O ANISOU 3195 OG1 THR B 156 11383 12097 10070 349 -551 901 O ATOM 3196 CG2 THR B 156 -20.787 0.416 -17.441 1.00 87.62 C ANISOU 3196 CG2 THR B 156 11589 12095 9610 482 -910 828 C ATOM 3197 N ALA B 157 -19.249 2.873 -19.457 1.00 81.23 N ANISOU 3197 N ALA B 157 10281 11234 9351 463 -1219 483 N ATOM 3198 CA ALA B 157 -17.899 3.385 -19.243 1.00 80.78 C ANISOU 3198 CA ALA B 157 10194 11228 9271 468 -1468 370 C ATOM 3199 C ALA B 157 -17.894 4.889 -18.986 1.00 83.77 C ANISOU 3199 C ALA B 157 10578 11573 9680 411 -1485 170 C ATOM 3200 O ALA B 157 -17.060 5.394 -18.236 1.00 85.44 O ANISOU 3200 O ALA B 157 10862 11837 9766 401 -1666 38 O ATOM 3201 CB ALA B 157 -17.004 3.040 -20.425 1.00 62.46 C ANISOU 3201 CB ALA B 157 7653 8911 7168 448 -1586 415 C ATOM 3202 N LEU B 158 -18.826 5.602 -19.610 1.00 82.26 N ANISOU 3202 N LEU B 158 10314 11274 9666 379 -1322 141 N ATOM 3203 CA LEU B 158 -18.925 7.045 -19.427 1.00 85.86 C ANISOU 3203 CA LEU B 158 10802 11632 10190 346 -1335 -48 C ATOM 3204 C LEU B 158 -19.624 7.403 -18.118 1.00 90.81 C ANISOU 3204 C LEU B 158 11639 12280 10586 425 -1212 -194 C ATOM 3205 O LEU B 158 -19.308 8.418 -17.499 1.00 94.23 O ANISOU 3205 O LEU B 158 12184 12661 10959 413 -1294 -402 O ATOM 3206 CB LEU B 158 -19.636 7.698 -20.614 1.00 87.87 C ANISOU 3206 CB LEU B 158 10915 11739 10733 314 -1244 -11 C ATOM 3207 CG LEU B 158 -18.860 7.710 -21.933 1.00 83.36 C ANISOU 3207 CG LEU B 158 10174 11142 10357 197 -1360 90 C ATOM 3208 CD1 LEU B 158 -19.683 8.354 -23.037 1.00 83.01 C ANISOU 3208 CD1 LEU B 158 10048 10949 10542 171 -1289 154 C ATOM 3209 CD2 LEU B 158 -17.525 8.419 -21.768 1.00 83.70 C ANISOU 3209 CD2 LEU B 158 10207 11188 10406 81 -1561 -25 C ATOM 3210 N ASN B 159 -20.571 6.568 -17.699 1.00111.64 N ANISOU 3210 N ASN B 159 14336 14994 13087 488 -1003 -96 N ATOM 3211 CA ASN B 159 -21.249 6.763 -16.420 1.00116.40 C ANISOU 3211 CA ASN B 159 15142 15668 13417 550 -831 -225 C ATOM 3212 C ASN B 159 -20.299 6.611 -15.239 1.00115.75 C ANISOU 3212 C ASN B 159 15300 15700 12981 544 -1012 -297 C ATOM 3213 O ASN B 159 -20.374 7.363 -14.267 1.00119.01 O ANISOU 3213 O ASN B 159 15898 16135 13185 570 -988 -516 O ATOM 3214 CB ASN B 159 -22.414 5.781 -16.265 1.00 96.82 C ANISOU 3214 CB ASN B 159 12653 13272 10861 565 -550 -69 C ATOM 3215 CG ASN B 159 -23.622 6.172 -17.089 1.00 98.91 C ANISOU 3215 CG ASN B 159 12690 13460 11430 595 -347 -76 C ATOM 3216 OD1 ASN B 159 -23.904 7.355 -17.279 1.00102.60 O ANISOU 3216 OD1 ASN B 159 13097 13819 12069 659 -338 -255 O ATOM 3217 ND2 ASN B 159 -24.349 5.176 -17.581 1.00 97.82 N ANISOU 3217 ND2 ASN B 159 12431 13363 11373 549 -208 118 N ATOM 3218 N VAL B 160 -19.408 5.628 -15.331 1.00 90.96 N ANISOU 3218 N VAL B 160 12161 12628 9773 526 -1209 -125 N ATOM 3219 CA VAL B 160 -18.430 5.371 -14.283 1.00 90.78 C ANISOU 3219 CA VAL B 160 12343 12721 9429 540 -1450 -157 C ATOM 3220 C VAL B 160 -17.500 6.566 -14.105 1.00 91.70 C ANISOU 3220 C VAL B 160 12445 12812 9586 488 -1694 -406 C ATOM 3221 O VAL B 160 -17.252 7.013 -12.984 1.00 93.87 O ANISOU 3221 O VAL B 160 12949 13157 9561 489 -1790 -579 O ATOM 3222 CB VAL B 160 -17.601 4.111 -14.592 1.00 81.28 C ANISOU 3222 CB VAL B 160 11087 11562 8235 572 -1652 73 C ATOM 3223 CG1 VAL B 160 -16.468 3.958 -13.588 1.00 81.43 C ANISOU 3223 CG1 VAL B 160 11272 11699 7968 609 -1980 32 C ATOM 3224 CG2 VAL B 160 -18.494 2.879 -14.590 1.00 80.84 C ANISOU 3224 CG2 VAL B 160 11120 11497 8098 594 -1433 316 C ATOM 3225 N VAL B 161 -16.994 7.083 -15.220 1.00 90.04 N ANISOU 3225 N VAL B 161 11980 12500 9732 418 -1792 -424 N ATOM 3226 CA VAL B 161 -16.123 8.252 -15.199 1.00 90.93 C ANISOU 3226 CA VAL B 161 12053 12555 9941 314 -2010 -642 C ATOM 3227 C VAL B 161 -16.878 9.474 -14.686 1.00 95.58 C ANISOU 3227 C VAL B 161 12812 13012 10491 313 -1873 -891 C ATOM 3228 O VAL B 161 -16.342 10.266 -13.910 1.00 97.46 O ANISOU 3228 O VAL B 161 13202 13240 10590 258 -2042 -1127 O ATOM 3229 CB VAL B 161 -15.540 8.546 -16.594 1.00 89.57 C ANISOU 3229 CB VAL B 161 11582 12296 10155 203 -2080 -577 C ATOM 3230 CG1 VAL B 161 -14.659 9.786 -16.556 1.00 91.02 C ANISOU 3230 CG1 VAL B 161 11732 12402 10448 41 -2289 -790 C ATOM 3231 CG2 VAL B 161 -14.751 7.348 -17.096 1.00 85.50 C ANISOU 3231 CG2 VAL B 161 10884 11917 9684 233 -2199 -383 C ATOM 3232 N SER B 162 -18.128 9.613 -15.118 1.00 95.55 N ANISOU 3232 N SER B 162 12778 12905 10623 386 -1578 -854 N ATOM 3233 CA SER B 162 -18.971 10.723 -14.688 1.00100.44 C ANISOU 3233 CA SER B 162 13529 13384 11248 445 -1416 -1099 C ATOM 3234 C SER B 162 -19.203 10.685 -13.181 1.00102.45 C ANISOU 3234 C SER B 162 14082 13779 11067 511 -1346 -1281 C ATOM 3235 O SER B 162 -19.171 11.719 -12.513 1.00105.20 O ANISOU 3235 O SER B 162 14609 14038 11323 516 -1379 -1580 O ATOM 3236 CB SER B 162 -20.309 10.693 -15.426 1.00104.98 C ANISOU 3236 CB SER B 162 13961 13870 12058 545 -1124 -1003 C ATOM 3237 OG SER B 162 -20.116 10.746 -16.827 1.00103.66 O ANISOU 3237 OG SER B 162 13560 13582 12243 476 -1202 -832 O ATOM 3238 N LEU B 163 -19.440 9.488 -12.653 1.00107.69 N ANISOU 3238 N LEU B 163 14826 14647 11445 552 -1247 -1099 N ATOM 3239 CA LEU B 163 -19.586 9.300 -11.215 1.00109.42 C ANISOU 3239 CA LEU B 163 15364 15036 11173 587 -1185 -1218 C ATOM 3240 C LEU B 163 -18.277 9.582 -10.495 1.00108.90 C ANISOU 3240 C LEU B 163 15469 15034 10874 512 -1571 -1356 C ATOM 3241 O LEU B 163 -18.270 10.138 -9.399 1.00111.67 O ANISOU 3241 O LEU B 163 16101 15442 10886 518 -1588 -1613 O ATOM 3242 CB LEU B 163 -20.058 7.880 -10.897 1.00106.84 C ANISOU 3242 CB LEU B 163 15106 14886 10602 609 -1018 -928 C ATOM 3243 CG LEU B 163 -21.567 7.646 -10.943 1.00108.77 C ANISOU 3243 CG LEU B 163 15294 15157 10877 662 -569 -882 C ATOM 3244 CD1 LEU B 163 -21.891 6.171 -10.775 1.00106.83 C ANISOU 3244 CD1 LEU B 163 15106 15045 10440 621 -447 -553 C ATOM 3245 CD2 LEU B 163 -22.249 8.471 -9.863 1.00112.44 C ANISOU 3245 CD2 LEU B 163 15975 15687 11060 724 -329 -1199 C ATOM 3246 N SER B 164 -17.171 9.197 -11.122 1.00116.29 N ANISOU 3246 N SER B 164 16219 15976 11990 442 -1881 -1205 N ATOM 3247 CA SER B 164 -15.847 9.437 -10.563 1.00115.52 C ANISOU 3247 CA SER B 164 16192 15960 11742 361 -2290 -1327 C ATOM 3248 C SER B 164 -15.541 10.930 -10.477 1.00117.83 C ANISOU 3248 C SER B 164 16520 16089 12160 256 -2405 -1675 C ATOM 3249 O SER B 164 -14.858 11.379 -9.558 1.00119.03 O ANISOU 3249 O SER B 164 16866 16310 12050 191 -2663 -1897 O ATOM 3250 CB SER B 164 -14.780 8.724 -11.395 1.00120.87 C ANISOU 3250 CB SER B 164 16575 16685 12664 325 -2554 -1106 C ATOM 3251 OG SER B 164 -14.967 7.320 -11.366 1.00118.88 O ANISOU 3251 OG SER B 164 16345 16545 12280 433 -2497 -807 O ATOM 3252 N VAL B 165 -16.044 11.695 -11.441 1.00108.93 N ANISOU 3252 N VAL B 165 15227 14729 11432 233 -2238 -1718 N ATOM 3253 CA VAL B 165 -15.877 13.143 -11.425 1.00111.49 C ANISOU 3253 CA VAL B 165 15622 14822 11916 136 -2324 -2031 C ATOM 3254 C VAL B 165 -16.727 13.778 -10.330 1.00115.47 C ANISOU 3254 C VAL B 165 16461 15288 12126 245 -2134 -2340 C ATOM 3255 O VAL B 165 -16.229 14.549 -9.511 1.00117.13 O ANISOU 3255 O VAL B 165 16897 15461 12146 169 -2326 -2650 O ATOM 3256 CB VAL B 165 -16.260 13.768 -12.779 1.00107.95 C ANISOU 3256 CB VAL B 165 14947 14105 11966 101 -2201 -1952 C ATOM 3257 CG1 VAL B 165 -16.300 15.284 -12.672 1.00110.60 C ANISOU 3257 CG1 VAL B 165 15432 14135 12458 31 -2255 -2272 C ATOM 3258 CG2 VAL B 165 -15.283 13.333 -13.856 1.00104.70 C ANISOU 3258 CG2 VAL B 165 14223 13736 11823 -46 -2388 -1711 C ATOM 3259 N GLU B 166 -18.012 13.441 -10.320 1.00125.89 N ANISOU 3259 N GLU B 166 17798 16629 13406 416 -1748 -2273 N ATOM 3260 CA GLU B 166 -18.963 14.029 -9.381 1.00128.94 C ANISOU 3260 CA GLU B 166 18448 16996 13547 549 -1482 -2577 C ATOM 3261 C GLU B 166 -18.679 13.650 -7.926 1.00129.43 C ANISOU 3261 C GLU B 166 18854 17323 13001 541 -1542 -2712 C ATOM 3262 O GLU B 166 -18.895 14.451 -7.019 1.00131.97 O ANISOU 3262 O GLU B 166 19459 17612 13072 577 -1488 -3082 O ATOM 3263 CB GLU B 166 -20.394 13.655 -9.773 1.00117.08 C ANISOU 3263 CB GLU B 166 16802 15506 12178 721 -1045 -2450 C ATOM 3264 CG GLU B 166 -20.862 14.301 -11.071 1.00117.62 C ANISOU 3264 CG GLU B 166 16600 15284 12808 768 -987 -2397 C ATOM 3265 CD GLU B 166 -22.339 14.650 -11.062 1.00120.55 C ANISOU 3265 CD GLU B 166 16913 15591 13300 986 -594 -2521 C ATOM 3266 OE1 GLU B 166 -23.007 14.403 -10.036 1.00122.28 O ANISOU 3266 OE1 GLU B 166 17288 16009 13163 1085 -319 -2668 O ATOM 3267 OE2 GLU B 166 -22.837 15.158 -12.089 1.00121.62 O ANISOU 3267 OE2 GLU B 166 16836 15492 13880 1059 -559 -2466 O ATOM 3268 N LEU B 167 -18.196 12.431 -7.704 1.00129.76 N ANISOU 3268 N LEU B 167 18896 17614 12792 500 -1666 -2417 N ATOM 3269 CA LEU B 167 -17.840 11.996 -6.356 1.00130.61 C ANISOU 3269 CA LEU B 167 19357 17976 12291 483 -1785 -2484 C ATOM 3270 C LEU B 167 -16.601 12.746 -5.886 1.00130.72 C ANISOU 3270 C LEU B 167 19500 17961 12207 350 -2248 -2747 C ATOM 3271 O LEU B 167 -16.449 13.042 -4.699 1.00132.93 O ANISOU 3271 O LEU B 167 20139 18363 12007 333 -2340 -3005 O ATOM 3272 CB LEU B 167 -17.595 10.487 -6.317 1.00139.78 C ANISOU 3272 CB LEU B 167 20495 19357 13259 488 -1850 -2064 C ATOM 3273 CG LEU B 167 -17.348 9.839 -4.951 1.00141.73 C ANISOU 3273 CG LEU B 167 21143 19872 12836 483 -1958 -2033 C ATOM 3274 CD1 LEU B 167 -18.534 10.029 -4.019 1.00145.14 C ANISOU 3274 CD1 LEU B 167 21881 20414 12851 541 -1510 -2211 C ATOM 3275 CD2 LEU B 167 -17.033 8.363 -5.124 1.00136.64 C ANISOU 3275 CD2 LEU B 167 20447 19350 12118 500 -2073 -1579 C ATOM 3276 N TYR B 168 -15.713 13.040 -6.829 1.00121.44 N ANISOU 3276 N TYR B 168 18026 16638 11476 234 -2537 -2684 N ATOM 3277 CA TYR B 168 -14.533 13.843 -6.544 1.00122.17 C ANISOU 3277 CA TYR B 168 18160 16678 11579 60 -2974 -2939 C ATOM 3278 C TYR B 168 -14.965 15.236 -6.104 1.00125.59 C ANISOU 3278 C TYR B 168 18839 16878 12002 40 -2879 -3393 C ATOM 3279 O TYR B 168 -14.426 15.793 -5.148 1.00127.14 O ANISOU 3279 O TYR B 168 19314 17114 11882 -52 -3132 -3712 O ATOM 3280 CB TYR B 168 -13.624 13.929 -7.774 1.00108.87 C ANISOU 3280 CB TYR B 168 16062 14878 10425 -84 -3209 -2774 C ATOM 3281 CG TYR B 168 -12.435 14.844 -7.591 1.00109.24 C ANISOU 3281 CG TYR B 168 16091 14854 10561 -317 -3633 -3041 C ATOM 3282 CD1 TYR B 168 -11.243 14.370 -7.061 1.00108.25 C ANISOU 3282 CD1 TYR B 168 15919 14980 10232 -408 -4070 -3017 C ATOM 3283 CD2 TYR B 168 -12.505 16.184 -7.952 1.00111.22 C ANISOU 3283 CD2 TYR B 168 16366 14773 11118 -450 -3616 -3314 C ATOM 3284 CE1 TYR B 168 -10.157 15.206 -6.893 1.00109.31 C ANISOU 3284 CE1 TYR B 168 15995 15070 10469 -652 -4470 -3274 C ATOM 3285 CE2 TYR B 168 -11.427 17.026 -7.784 1.00112.56 C ANISOU 3285 CE2 TYR B 168 16524 14860 11385 -710 -4002 -3560 C ATOM 3286 CZ TYR B 168 -10.254 16.533 -7.255 1.00111.47 C ANISOU 3286 CZ TYR B 168 16302 15008 11044 -824 -4424 -3546 C ATOM 3287 OH TYR B 168 -9.174 17.370 -7.088 1.00112.73 O ANISOU 3287 OH TYR B 168 16408 15105 11321 -1115 -4822 -3803 O ATOM 3288 N LEU B 169 -15.942 15.792 -6.815 1.00137.89 N ANISOU 3288 N LEU B 169 20299 18179 13915 139 -2534 -3430 N ATOM 3289 CA LEU B 169 -16.436 17.133 -6.530 1.00141.13 C ANISOU 3289 CA LEU B 169 20922 18298 14402 170 -2424 -3856 C ATOM 3290 C LEU B 169 -17.167 17.187 -5.193 1.00144.05 C ANISOU 3290 C LEU B 169 21686 18827 14218 317 -2188 -4154 C ATOM 3291 O LEU B 169 -17.167 18.215 -4.520 1.00146.18 O ANISOU 3291 O LEU B 169 22246 18941 14355 306 -2236 -4597 O ATOM 3292 CB LEU B 169 -17.362 17.611 -7.652 1.00121.65 C ANISOU 3292 CB LEU B 169 18235 15526 12462 290 -2127 -3778 C ATOM 3293 CG LEU B 169 -16.770 17.673 -9.062 1.00119.52 C ANISOU 3293 CG LEU B 169 17611 15076 12726 140 -2303 -3493 C ATOM 3294 CD1 LEU B 169 -17.794 18.202 -10.054 1.00120.24 C ANISOU 3294 CD1 LEU B 169 17558 14864 13265 283 -2028 -3432 C ATOM 3295 CD2 LEU B 169 -15.505 18.518 -9.085 1.00119.67 C ANISOU 3295 CD2 LEU B 169 17664 14928 12877 -140 -2723 -3675 C ATOM 3296 N ALA B 170 -17.789 16.076 -4.812 1.00171.36 N ANISOU 3296 N ALA B 170 25173 22593 17343 438 -1921 -3915 N ATOM 3297 CA ALA B 170 -18.532 16.011 -3.558 1.00173.88 C ANISOU 3297 CA ALA B 170 25860 23119 17088 555 -1632 -4152 C ATOM 3298 C ALA B 170 -17.604 16.018 -2.347 1.00174.81 C ANISOU 3298 C ALA B 170 26357 23440 16622 423 -1995 -4353 C ATOM 3299 O ALA B 170 -18.002 16.421 -1.255 1.00178.69 O ANISOU 3299 O ALA B 170 27231 24028 16633 476 -1843 -4707 O ATOM 3300 CB ALA B 170 -19.423 14.781 -3.534 1.00106.01 C ANISOU 3300 CB ALA B 170 17182 14789 8307 663 -1246 -3796 C ATOM 3301 N ILE B 171 -16.368 15.571 -2.544 1.00115.38 N ANISOU 3301 N ILE B 171 18714 15996 9130 258 -2478 -4138 N ATOM 3302 CA ILE B 171 -15.398 15.508 -1.456 1.00116.53 C ANISOU 3302 CA ILE B 171 19173 16356 8748 132 -2907 -4290 C ATOM 3303 C ILE B 171 -14.512 16.749 -1.404 1.00118.29 C ANISOU 3303 C ILE B 171 19445 16347 9153 -50 -3308 -4695 C ATOM 3304 O ILE B 171 -14.398 17.404 -0.367 1.00123.71 O ANISOU 3304 O ILE B 171 20526 17061 9416 -97 -3422 -5114 O ATOM 3305 CB ILE B 171 -14.486 14.274 -1.586 1.00124.85 C ANISOU 3305 CB ILE B 171 20062 17656 9719 76 -3263 -3844 C ATOM 3306 CG1 ILE B 171 -15.311 12.989 -1.624 1.00123.62 C ANISOU 3306 CG1 ILE B 171 19897 17689 9384 223 -2901 -3424 C ATOM 3307 CG2 ILE B 171 -13.480 14.235 -0.446 1.00126.48 C ANISOU 3307 CG2 ILE B 171 20583 18092 9382 -36 -3763 -4000 C ATOM 3308 CD1 ILE B 171 -14.471 11.738 -1.771 1.00121.06 C ANISOU 3308 CD1 ILE B 171 19438 17551 9007 210 -3243 -2984 C ATOM 3309 N CYS B 172 -13.887 17.065 -2.534 1.00121.59 N ANISOU 3309 N CYS B 172 19472 16538 10189 -175 -3512 -4572 N ATOM 3310 CA CYS B 172 -12.915 18.152 -2.600 1.00122.59 C ANISOU 3310 CA CYS B 172 19588 16443 10547 -416 -3924 -4888 C ATOM 3311 C CYS B 172 -13.560 19.535 -2.583 1.00125.23 C ANISOU 3311 C CYS B 172 20134 16377 11071 -399 -3718 -5336 C ATOM 3312 O CYS B 172 -13.105 20.430 -1.870 1.00127.67 O ANISOU 3312 O CYS B 172 20735 16572 11203 -541 -3975 -5774 O ATOM 3313 CB CYS B 172 -12.022 17.994 -3.832 1.00154.53 C ANISOU 3313 CB CYS B 172 23138 20404 15174 -584 -4171 -4584 C ATOM 3314 SG CYS B 172 -11.036 16.482 -3.817 1.00151.39 S ANISOU 3314 SG CYS B 172 22476 20439 14607 -590 -4509 -4139 S ATOM 3315 N HIS B 173 -14.618 19.708 -3.368 1.00187.29 N ANISOU 3315 N HIS B 173 27851 24010 19301 -216 -3279 -5238 N ATOM 3316 CA HIS B 173 -15.316 20.988 -3.423 1.00190.19 C ANISOU 3316 CA HIS B 173 28400 23959 19904 -134 -3073 -5638 C ATOM 3317 C HIS B 173 -16.795 20.827 -3.073 1.00191.74 C ANISOU 3317 C HIS B 173 28729 24213 19912 200 -2509 -5721 C ATOM 3318 O HIS B 173 -17.655 20.920 -3.949 1.00191.62 O ANISOU 3318 O HIS B 173 28479 24004 20326 371 -2193 -5569 O ATOM 3319 CB HIS B 173 -15.172 21.610 -4.813 1.00153.52 C ANISOU 3319 CB HIS B 173 23436 18906 15988 -232 -3120 -5480 C ATOM 3320 CG HIS B 173 -13.755 21.796 -5.250 1.00151.98 C ANISOU 3320 CG HIS B 173 23054 18667 16027 -590 -3610 -5391 C ATOM 3321 ND1 HIS B 173 -12.980 20.760 -5.735 1.00148.99 N ANISOU 3321 ND1 HIS B 173 22323 18596 15690 -702 -3797 -4972 N ATOM 3322 CD2 HIS B 173 -12.962 22.895 -5.280 1.00153.04 C ANISOU 3322 CD2 HIS B 173 23282 18486 16382 -872 -3945 -5678 C ATOM 3323 CE1 HIS B 173 -11.781 21.212 -6.042 1.00148.23 C ANISOU 3323 CE1 HIS B 173 22076 18415 15831 -1028 -4204 -5010 C ATOM 3324 NE2 HIS B 173 -11.743 22.509 -5.773 1.00150.94 N ANISOU 3324 NE2 HIS B 173 22686 18378 16284 -1161 -4305 -5427 N ATOM 3325 N PRO B 174 -17.097 20.594 -1.785 1.00153.51 N ANISOU 3325 N PRO B 174 24256 19658 14414 286 -2384 -5969 N ATOM 3326 CA PRO B 174 -18.476 20.334 -1.359 1.00155.20 C ANISOU 3326 CA PRO B 174 24569 20013 14388 576 -1808 -6043 C ATOM 3327 C PRO B 174 -19.374 21.570 -1.412 1.00158.22 C ANISOU 3327 C PRO B 174 25058 20004 15053 786 -1513 -6499 C ATOM 3328 O PRO B 174 -20.590 21.426 -1.531 1.00158.15 O ANISOU 3328 O PRO B 174 24936 20034 15122 1052 -1018 -6488 O ATOM 3329 CB PRO B 174 -18.306 19.868 0.088 1.00133.86 C ANISOU 3329 CB PRO B 174 22291 17717 10853 540 -1832 -6215 C ATOM 3330 CG PRO B 174 -17.063 20.539 0.547 1.00135.25 C ANISOU 3330 CG PRO B 174 22699 17791 10898 292 -2399 -6509 C ATOM 3331 CD PRO B 174 -16.158 20.585 -0.649 1.00132.03 C ANISOU 3331 CD PRO B 174 21880 17162 11122 100 -2778 -6201 C ATOM 3332 N PHE B 175 -18.788 22.762 -1.329 1.00192.11 N ANISOU 3332 N PHE B 175 29555 23917 19521 670 -1820 -6898 N ATOM 3333 CA PHE B 175 -19.572 23.992 -1.410 1.00195.16 C ANISOU 3333 CA PHE B 175 30071 23855 20225 889 -1592 -7344 C ATOM 3334 C PHE B 175 -19.795 24.402 -2.859 1.00193.86 C ANISOU 3334 C PHE B 175 29538 23266 20855 937 -1600 -7075 C ATOM 3335 O PHE B 175 -20.788 25.052 -3.186 1.00195.45 O ANISOU 3335 O PHE B 175 29700 23162 21400 1225 -1300 -7253 O ATOM 3336 CB PHE B 175 -18.926 25.136 -0.629 1.00214.41 C ANISOU 3336 CB PHE B 175 32959 26016 22491 747 -1906 -7931 C ATOM 3337 CG PHE B 175 -19.760 26.387 -0.601 1.00217.39 C ANISOU 3337 CG PHE B 175 33527 25906 23164 1014 -1663 -8436 C ATOM 3338 CD1 PHE B 175 -20.784 26.531 0.321 1.00219.76 C ANISOU 3338 CD1 PHE B 175 34073 26351 23075 1330 -1200 -8856 C ATOM 3339 CD2 PHE B 175 -19.531 27.412 -1.506 1.00217.18 C ANISOU 3339 CD2 PHE B 175 33437 25271 23810 956 -1886 -8486 C ATOM 3340 CE1 PHE B 175 -21.558 27.677 0.347 1.00221.55 C ANISOU 3340 CE1 PHE B 175 34451 26119 23608 1621 -972 -9342 C ATOM 3341 CE2 PHE B 175 -20.303 28.560 -1.485 1.00219.41 C ANISOU 3341 CE2 PHE B 175 33917 25057 24393 1237 -1692 -8944 C ATOM 3342 CZ PHE B 175 -21.317 28.692 -0.557 1.00221.65 C ANISOU 3342 CZ PHE B 175 34412 25487 24317 1588 -1235 -9380 C ATOM 3343 N LYS B 176 -18.863 24.018 -3.723 1.00162.92 N ANISOU 3343 N LYS B 176 25348 19338 17217 664 -1950 -6649 N ATOM 3344 CA LYS B 176 -18.976 24.321 -5.140 1.00161.29 C ANISOU 3344 CA LYS B 176 24810 18773 17700 662 -1980 -6340 C ATOM 3345 C LYS B 176 -20.082 23.429 -5.682 1.00160.16 C ANISOU 3345 C LYS B 176 24339 18858 17657 931 -1557 -5980 C ATOM 3346 O LYS B 176 -20.790 23.787 -6.624 1.00159.68 O ANISOU 3346 O LYS B 176 24067 18507 18095 1103 -1404 -5855 O ATOM 3347 CB LYS B 176 -17.661 24.042 -5.868 1.00162.72 C ANISOU 3347 CB LYS B 176 24775 18969 18084 282 -2420 -5989 C ATOM 3348 CG LYS B 176 -16.495 24.930 -5.444 1.00163.69 C ANISOU 3348 CG LYS B 176 25150 18865 18180 -48 -2875 -6316 C ATOM 3349 CD LYS B 176 -16.896 26.383 -5.261 1.00166.37 C ANISOU 3349 CD LYS B 176 25822 18641 18750 35 -2858 -6809 C ATOM 3350 CE LYS B 176 -15.740 27.184 -4.677 1.00167.16 C ANISOU 3350 CE LYS B 176 26210 18555 18748 -328 -3318 -7176 C ATOM 3351 NZ LYS B 176 -16.116 28.592 -4.374 1.00169.91 N ANISOU 3351 NZ LYS B 176 26953 18322 19281 -247 -3315 -7712 N ATOM 3352 N ALA B 177 -20.216 22.258 -5.064 1.00155.07 N ANISOU 3352 N ALA B 177 23667 18727 16524 952 -1392 -5808 N ATOM 3353 CA ALA B 177 -21.242 21.293 -5.430 1.00154.25 C ANISOU 3353 CA ALA B 177 23273 18889 16446 1157 -987 -5477 C ATOM 3354 C ALA B 177 -22.481 21.454 -4.551 1.00156.90 C ANISOU 3354 C ALA B 177 23763 19349 16504 1460 -500 -5827 C ATOM 3355 O ALA B 177 -23.447 20.710 -4.693 1.00156.31 O ANISOU 3355 O ALA B 177 23457 19519 16416 1626 -113 -5619 O ATOM 3356 CB ALA B 177 -20.700 19.878 -5.338 1.00136.22 C ANISOU 3356 CB ALA B 177 20870 17056 13832 989 -1077 -5048 C ATOM 3357 N LYS B 178 -22.441 22.418 -3.634 1.00209.35 N ANISOU 3357 N LYS B 178 30791 25835 22920 1519 -512 -6377 N ATOM 3358 CA LYS B 178 -23.601 22.720 -2.801 1.00212.43 C ANISOU 3358 CA LYS B 178 31331 26319 23065 1828 -24 -6789 C ATOM 3359 C LYS B 178 -24.671 23.342 -3.687 1.00212.98 C ANISOU 3359 C LYS B 178 31104 26043 23776 2146 230 -6827 C ATOM 3360 O LYS B 178 -25.853 23.011 -3.583 1.00213.74 O ANISOU 3360 O LYS B 178 31000 26345 23868 2411 706 -6844 O ATOM 3361 CB LYS B 178 -23.244 23.663 -1.654 1.00205.24 C ANISOU 3361 CB LYS B 178 30930 25286 21768 1818 -124 -7413 C ATOM 3362 CG LYS B 178 -24.446 24.068 -0.819 1.00208.16 C ANISOU 3362 CG LYS B 178 31452 25737 21902 2163 415 -7900 C ATOM 3363 CD LYS B 178 -24.103 25.164 0.168 1.00211.26 C ANISOU 3363 CD LYS B 178 32363 25906 21999 2175 293 -8575 C ATOM 3364 CE LYS B 178 -25.364 25.717 0.811 1.00214.72 C ANISOU 3364 CE LYS B 178 32899 26347 22339 2580 858 -9104 C ATOM 3365 NZ LYS B 178 -25.083 26.844 1.740 1.00218.10 N ANISOU 3365 NZ LYS B 178 33806 26511 22552 2564 779 -9728 N ATOM 3366 N THR B 179 -24.238 24.243 -4.564 1.00187.69 N ANISOU 3366 N THR B 179 27870 22318 21127 2106 -106 -6826 N ATOM 3367 CA THR B 179 -25.118 24.852 -5.553 1.00187.64 C ANISOU 3367 CA THR B 179 27595 21928 21773 2391 21 -6786 C ATOM 3368 C THR B 179 -24.941 23.992 -6.787 1.00184.54 C ANISOU 3368 C THR B 179 26790 21635 21689 2239 -108 -6140 C ATOM 3369 O THR B 179 -24.470 24.436 -7.834 1.00182.59 O ANISOU 3369 O THR B 179 26450 21019 21906 2123 -422 -5917 O ATOM 3370 CB THR B 179 -24.770 26.319 -5.841 1.00184.41 C ANISOU 3370 CB THR B 179 27433 20851 21782 2422 -279 -7113 C ATOM 3371 OG1 THR B 179 -23.408 26.411 -6.276 1.00183.08 O ANISOU 3371 OG1 THR B 179 27360 20522 21681 2001 -780 -6892 O ATOM 3372 CG2 THR B 179 -24.955 27.164 -4.593 1.00187.33 C ANISOU 3372 CG2 THR B 179 28241 21107 21831 2585 -148 -7805 C ATOM 3373 N LEU B 180 -25.345 22.739 -6.623 1.00166.23 N ANISOU 3373 N LEU B 180 24254 19827 19080 2229 158 -5850 N ATOM 3374 CA LEU B 180 -25.108 21.674 -7.581 1.00163.35 C ANISOU 3374 CA LEU B 180 23547 19658 18862 2053 59 -5260 C ATOM 3375 C LEU B 180 -25.839 21.843 -8.904 1.00162.06 C ANISOU 3375 C LEU B 180 23009 19248 19318 2223 98 -4999 C ATOM 3376 O LEU B 180 -26.702 22.712 -9.055 1.00162.84 O ANISOU 3376 O LEU B 180 23066 19057 19749 2530 246 -5254 O ATOM 3377 CB LEU B 180 -25.483 20.336 -6.932 1.00191.67 C ANISOU 3377 CB LEU B 180 27056 23810 21959 2019 368 -5072 C ATOM 3378 CG LEU B 180 -25.003 18.994 -7.484 1.00188.51 C ANISOU 3378 CG LEU B 180 26439 23701 21486 1785 250 -4518 C ATOM 3379 CD1 LEU B 180 -23.488 18.957 -7.616 1.00186.95 C ANISOU 3379 CD1 LEU B 180 26389 23434 21208 1479 -245 -4388 C ATOM 3380 CD2 LEU B 180 -25.514 17.865 -6.600 1.00188.15 C ANISOU 3380 CD2 LEU B 180 26425 24147 20918 1780 599 -4428 C ATOM 3381 N MET B 181 -25.497 20.972 -9.846 1.00178.56 N ANISOU 3381 N MET B 181 24831 21468 21544 2036 -42 -4494 N ATOM 3382 CA MET B 181 -26.108 20.964 -11.157 1.00177.80 C ANISOU 3382 CA MET B 181 24388 21201 21968 2147 -45 -4188 C ATOM 3383 C MET B 181 -27.517 20.451 -10.954 1.00178.30 C ANISOU 3383 C MET B 181 24181 21536 22030 2425 401 -4211 C ATOM 3384 O MET B 181 -27.726 19.412 -10.323 1.00177.76 O ANISOU 3384 O MET B 181 24065 21908 21569 2355 649 -4125 O ATOM 3385 CB MET B 181 -25.357 20.031 -12.112 1.00210.37 C ANISOU 3385 CB MET B 181 28319 25464 26148 1859 -274 -3676 C ATOM 3386 CG MET B 181 -23.883 20.346 -12.305 1.00209.70 C ANISOU 3386 CG MET B 181 28424 25215 26037 1539 -687 -3619 C ATOM 3387 SD MET B 181 -23.039 19.081 -13.278 1.00206.44 S ANISOU 3387 SD MET B 181 27752 25060 25626 1245 -873 -3070 S ATOM 3388 CE MET B 181 -24.053 19.041 -14.755 1.00206.02 C ANISOU 3388 CE MET B 181 27355 24852 26072 1404 -780 -2758 C ATOM 3389 N SER B 182 -28.474 21.245 -11.421 1.00168.37 N ANISOU 3389 N SER B 182 22762 19999 21211 2741 499 -4354 N ATOM 3390 CA SER B 182 -29.896 20.949 -11.307 1.00168.74 C ANISOU 3390 CA SER B 182 22480 20268 21364 3043 915 -4425 C ATOM 3391 C SER B 182 -30.265 19.541 -11.743 1.00166.58 C ANISOU 3391 C SER B 182 21861 20417 21014 2897 1066 -3993 C ATOM 3392 O SER B 182 -29.601 18.944 -12.597 1.00164.87 O ANISOU 3392 O SER B 182 21576 20202 20864 2648 797 -3585 O ATOM 3393 CB SER B 182 -30.707 21.942 -12.139 1.00181.74 C ANISOU 3393 CB SER B 182 23934 21503 23618 3386 850 -4508 C ATOM 3394 OG SER B 182 -30.496 23.266 -11.691 1.00183.93 O ANISOU 3394 OG SER B 182 24545 21343 23997 3559 740 -4943 O ATOM 3395 N ARG B 183 -31.316 19.014 -11.117 1.00165.65 N ANISOU 3395 N ARG B 183 21537 20659 20744 3040 1516 -4106 N ATOM 3396 CA ARG B 183 -31.872 17.712 -11.457 1.00163.76 C ANISOU 3396 CA ARG B 183 20955 20804 20461 2912 1713 -3741 C ATOM 3397 C ARG B 183 -32.065 17.631 -12.969 1.00161.19 C ANISOU 3397 C ARG B 183 20305 20286 20653 2921 1444 -3381 C ATOM 3398 O ARG B 183 -31.899 16.576 -13.575 1.00158.57 O ANISOU 3398 O ARG B 183 19819 20138 20292 2690 1372 -2986 O ATOM 3399 CB ARG B 183 -33.220 17.514 -10.760 1.00215.06 C ANISOU 3399 CB ARG B 183 27187 27624 26901 3128 2250 -3973 C ATOM 3400 CG ARG B 183 -33.162 17.508 -9.241 1.00217.27 C ANISOU 3400 CG ARG B 183 27787 28163 26604 3111 2587 -4324 C ATOM 3401 CD ARG B 183 -32.333 16.358 -8.715 1.00216.37 C ANISOU 3401 CD ARG B 183 27934 28347 25930 2730 2551 -4040 C ATOM 3402 NE ARG B 183 -32.973 15.069 -8.949 1.00215.17 N ANISOU 3402 NE ARG B 183 27469 28547 25738 2569 2797 -3678 N ATOM 3403 CZ ARG B 183 -33.758 14.457 -8.070 1.00216.21 C ANISOU 3403 CZ ARG B 183 27537 29081 25533 2531 3292 -3749 C ATOM 3404 NH1 ARG B 183 -34.005 15.020 -6.895 1.00219.08 N ANISOU 3404 NH1 ARG B 183 28128 29571 25541 2666 3611 -4184 N ATOM 3405 NH2 ARG B 183 -34.297 13.281 -8.363 1.00214.59 N ANISOU 3405 NH2 ARG B 183 27054 29147 25332 2339 3479 -3393 N ATOM 3406 N SER B 184 -32.407 18.772 -13.563 1.00175.89 N ANISOU 3406 N SER B 184 22102 21755 22973 3194 1283 -3530 N ATOM 3407 CA SER B 184 -32.589 18.899 -15.003 1.00173.59 C ANISOU 3407 CA SER B 184 21565 21231 23159 3229 986 -3213 C ATOM 3408 C SER B 184 -31.288 18.727 -15.784 1.00171.52 C ANISOU 3408 C SER B 184 21519 20796 22855 2899 571 -2880 C ATOM 3409 O SER B 184 -31.264 18.054 -16.814 1.00168.90 O ANISOU 3409 O SER B 184 20983 20532 22659 2753 423 -2498 O ATOM 3410 CB SER B 184 -33.209 20.257 -15.337 1.00161.16 C ANISOU 3410 CB SER B 184 19947 19230 22057 3622 886 -3465 C ATOM 3411 OG SER B 184 -33.373 20.412 -16.736 1.00158.83 O ANISOU 3411 OG SER B 184 19460 18701 22187 3653 563 -3133 O ATOM 3412 N ARG B 185 -30.212 19.337 -15.295 1.00136.31 N ANISOU 3412 N ARG B 185 17458 16127 18206 2773 390 -3044 N ATOM 3413 CA ARG B 185 -28.924 19.273 -15.983 1.00134.43 C ANISOU 3413 CA ARG B 185 17397 15735 17944 2454 17 -2770 C ATOM 3414 C ARG B 185 -28.301 17.887 -15.901 1.00132.55 C ANISOU 3414 C ARG B 185 17118 15892 17353 2150 42 -2487 C ATOM 3415 O ARG B 185 -27.688 17.419 -16.861 1.00130.88 O ANISOU 3415 O ARG B 185 16836 15671 17223 1940 -181 -2149 O ATOM 3416 CB ARG B 185 -27.953 20.323 -15.437 1.00125.62 C ANISOU 3416 CB ARG B 185 16687 14298 16745 2378 -189 -3049 C ATOM 3417 CG ARG B 185 -28.348 21.754 -15.758 1.00127.51 C ANISOU 3417 CG ARG B 185 17030 14021 17396 2634 -317 -3265 C ATOM 3418 CD ARG B 185 -27.126 22.649 -15.887 1.00127.93 C ANISOU 3418 CD ARG B 185 17441 13678 17487 2402 -668 -3317 C ATOM 3419 NE ARG B 185 -26.431 22.832 -14.617 1.00129.02 N ANISOU 3419 NE ARG B 185 17892 13888 17242 2287 -636 -3671 N ATOM 3420 CZ ARG B 185 -26.675 23.828 -13.773 1.00132.10 C ANISOU 3420 CZ ARG B 185 18542 14020 17632 2491 -573 -4141 C ATOM 3421 NH1 ARG B 185 -27.601 24.732 -14.064 1.00133.53 N ANISOU 3421 NH1 ARG B 185 18690 13835 18211 2848 -528 -4310 N ATOM 3422 NH2 ARG B 185 -25.995 23.924 -12.639 1.00133.97 N ANISOU 3422 NH2 ARG B 185 19077 14356 17468 2352 -573 -4453 N ATOM 3423 N THR B 186 -28.451 17.236 -14.753 1.00135.40 N ANISOU 3423 N THR B 186 17543 16589 17313 2134 316 -2628 N ATOM 3424 CA THR B 186 -27.924 15.889 -14.579 1.00134.21 C ANISOU 3424 CA THR B 186 17387 16784 16824 1880 340 -2359 C ATOM 3425 C THR B 186 -28.647 14.936 -15.526 1.00132.32 C ANISOU 3425 C THR B 186 16787 16701 16786 1859 423 -2018 C ATOM 3426 O THR B 186 -28.024 14.076 -16.147 1.00130.83 O ANISOU 3426 O THR B 186 16555 16600 16554 1645 264 -1704 O ATOM 3427 CB THR B 186 -28.060 15.398 -13.127 1.00122.64 C ANISOU 3427 CB THR B 186 16100 15635 14863 1872 628 -2556 C ATOM 3428 OG1 THR B 186 -27.383 16.306 -12.249 1.00124.64 O ANISOU 3428 OG1 THR B 186 16709 15744 14906 1884 521 -2904 O ATOM 3429 CG2 THR B 186 -27.452 14.011 -12.975 1.00120.99 C ANISOU 3429 CG2 THR B 186 15928 15722 14320 1619 597 -2243 C ATOM 3430 N LYS B 187 -29.962 15.102 -15.637 1.00132.52 N ANISOU 3430 N LYS B 187 16541 16764 17046 2088 666 -2104 N ATOM 3431 CA LYS B 187 -30.764 14.307 -16.562 1.00130.10 C ANISOU 3431 CA LYS B 187 15864 16594 16975 2073 722 -1818 C ATOM 3432 C LYS B 187 -30.341 14.541 -18.008 1.00127.46 C ANISOU 3432 C LYS B 187 15458 16006 16964 2007 354 -1556 C ATOM 3433 O LYS B 187 -30.331 13.614 -18.817 1.00124.84 O ANISOU 3433 O LYS B 187 14964 15797 16671 1848 281 -1250 O ATOM 3434 CB LYS B 187 -32.255 14.616 -16.396 1.00163.78 C ANISOU 3434 CB LYS B 187 19808 20941 21481 2356 1023 -2006 C ATOM 3435 CG LYS B 187 -32.870 14.032 -15.139 1.00166.01 C ANISOU 3435 CG LYS B 187 20065 21585 21427 2356 1473 -2178 C ATOM 3436 CD LYS B 187 -34.372 14.267 -15.079 1.00167.11 C ANISOU 3436 CD LYS B 187 19792 21852 21850 2622 1795 -2355 C ATOM 3437 CE LYS B 187 -34.704 15.750 -15.057 1.00169.19 C ANISOU 3437 CE LYS B 187 20062 21798 22425 2995 1737 -2707 C ATOM 3438 NZ LYS B 187 -36.172 15.989 -14.985 1.00170.40 N ANISOU 3438 NZ LYS B 187 19762 22093 22890 3301 2048 -2907 N ATOM 3439 N LYS B 188 -29.997 15.786 -18.326 1.00113.14 N ANISOU 3439 N LYS B 188 13793 13828 15366 2118 128 -1680 N ATOM 3440 CA LYS B 188 -29.513 16.127 -19.660 1.00111.06 C ANISOU 3440 CA LYS B 188 13528 13307 15363 2026 -217 -1427 C ATOM 3441 C LYS B 188 -28.158 15.485 -19.932 1.00109.75 C ANISOU 3441 C LYS B 188 13524 13214 14960 1693 -398 -1212 C ATOM 3442 O LYS B 188 -27.862 15.091 -21.060 1.00106.12 O ANISOU 3442 O LYS B 188 12974 12741 14606 1548 -574 -923 O ATOM 3443 CB LYS B 188 -29.415 17.644 -19.833 1.00 92.30 C ANISOU 3443 CB LYS B 188 11331 10485 13253 2195 -409 -1606 C ATOM 3444 CG LYS B 188 -30.754 18.342 -19.994 1.00 92.47 C ANISOU 3444 CG LYS B 188 11139 10360 13636 2570 -329 -1750 C ATOM 3445 CD LYS B 188 -30.572 19.836 -20.196 1.00 94.04 C ANISOU 3445 CD LYS B 188 11575 10047 14109 2736 -561 -1904 C ATOM 3446 CE LYS B 188 -31.897 20.518 -20.491 1.00 94.54 C ANISOU 3446 CE LYS B 188 11402 9933 14586 3155 -537 -2016 C ATOM 3447 NZ LYS B 188 -32.878 20.321 -19.390 1.00 96.84 N ANISOU 3447 NZ LYS B 188 11483 10495 14815 3418 -135 -2358 N ATOM 3448 N PHE B 189 -27.340 15.378 -18.891 1.00100.65 N ANISOU 3448 N PHE B 189 12607 12155 13483 1584 -359 -1369 N ATOM 3449 CA PHE B 189 -26.021 14.776 -19.024 1.00100.25 C ANISOU 3449 CA PHE B 189 12676 12195 13219 1303 -537 -1203 C ATOM 3450 C PHE B 189 -26.148 13.270 -19.220 1.00 97.98 C ANISOU 3450 C PHE B 189 12224 12227 12778 1195 -428 -953 C ATOM 3451 O PHE B 189 -25.371 12.665 -19.956 1.00 95.52 O ANISOU 3451 O PHE B 189 11881 11958 12453 1013 -589 -725 O ATOM 3452 CB PHE B 189 -25.153 15.097 -17.807 1.00135.33 C ANISOU 3452 CB PHE B 189 17404 16656 17359 1236 -568 -1454 C ATOM 3453 CG PHE B 189 -23.717 14.689 -17.962 1.00134.99 C ANISOU 3453 CG PHE B 189 17450 16676 17162 972 -804 -1319 C ATOM 3454 CD1 PHE B 189 -22.888 15.355 -18.851 1.00134.30 C ANISOU 3454 CD1 PHE B 189 17384 16358 17286 818 -1061 -1233 C ATOM 3455 CD2 PHE B 189 -23.192 13.649 -17.215 1.00133.90 C ANISOU 3455 CD2 PHE B 189 17370 16830 16675 880 -771 -1274 C ATOM 3456 CE1 PHE B 189 -21.565 14.986 -18.996 1.00132.56 C ANISOU 3456 CE1 PHE B 189 17184 16232 16950 578 -1254 -1132 C ATOM 3457 CE2 PHE B 189 -21.869 13.276 -17.356 1.00131.44 C ANISOU 3457 CE2 PHE B 189 17095 16586 16260 678 -1006 -1168 C ATOM 3458 CZ PHE B 189 -21.055 13.945 -18.248 1.00130.41 C ANISOU 3458 CZ PHE B 189 16929 16260 16363 528 -1235 -1111 C ATOM 3459 N ILE B 190 -27.133 12.671 -18.557 1.00135.52 N ANISOU 3459 N ILE B 190 16876 17196 17421 1301 -141 -1007 N ATOM 3460 CA ILE B 190 -27.416 11.250 -18.724 1.00133.23 C ANISOU 3460 CA ILE B 190 16441 17164 17015 1190 -20 -771 C ATOM 3461 C ILE B 190 -27.857 10.975 -20.157 1.00128.96 C ANISOU 3461 C ILE B 190 15649 16565 16784 1164 -128 -534 C ATOM 3462 O ILE B 190 -27.432 9.997 -20.774 1.00125.40 O ANISOU 3462 O ILE B 190 15157 16205 16284 1001 -212 -305 O ATOM 3463 CB ILE B 190 -28.511 10.770 -17.750 1.00113.39 C ANISOU 3463 CB ILE B 190 13853 14882 14349 1278 343 -875 C ATOM 3464 CG1 ILE B 190 -28.044 10.923 -16.302 1.00116.36 C ANISOU 3464 CG1 ILE B 190 14528 15356 14329 1279 453 -1094 C ATOM 3465 CG2 ILE B 190 -28.871 9.318 -18.021 1.00111.07 C ANISOU 3465 CG2 ILE B 190 13415 14802 13984 1128 455 -610 C ATOM 3466 CD1 ILE B 190 -26.839 10.077 -15.958 1.00115.89 C ANISOU 3466 CD1 ILE B 190 14689 15397 13945 1084 290 -942 C ATOM 3467 N SER B 191 -28.707 11.852 -20.684 1.00105.51 N ANISOU 3467 N SER B 191 12527 13435 14128 1340 -143 -601 N ATOM 3468 CA SER B 191 -29.190 11.726 -22.053 1.00101.02 C ANISOU 3468 CA SER B 191 11739 12804 13841 1332 -287 -386 C ATOM 3469 C SER B 191 -28.067 11.945 -23.060 1.00 97.65 C ANISOU 3469 C SER B 191 11446 12214 13443 1168 -584 -215 C ATOM 3470 O SER B 191 -27.994 11.259 -24.078 1.00 92.83 O ANISOU 3470 O SER B 191 10735 11665 12873 1041 -685 10 O ATOM 3471 CB SER B 191 -30.323 12.720 -22.315 1.00113.94 C ANISOU 3471 CB SER B 191 13196 14285 15811 1598 -279 -505 C ATOM 3472 OG SER B 191 -31.427 12.472 -21.462 1.00116.22 O ANISOU 3472 OG SER B 191 13289 14772 16097 1746 35 -672 O ATOM 3473 N ALA B 192 -27.193 12.903 -22.766 1.00 99.37 N ANISOU 3473 N ALA B 192 11892 12232 13633 1151 -710 -337 N ATOM 3474 CA ALA B 192 -26.067 13.212 -23.641 1.00 96.67 C ANISOU 3474 CA ALA B 192 11669 11748 13315 961 -957 -192 C ATOM 3475 C ALA B 192 -25.115 12.029 -23.755 1.00 93.26 C ANISOU 3475 C ALA B 192 11241 11541 12654 747 -969 -52 C ATOM 3476 O ALA B 192 -24.602 11.737 -24.834 1.00 88.18 O ANISOU 3476 O ALA B 192 10558 10900 12047 600 -1097 140 O ATOM 3477 CB ALA B 192 -25.327 14.443 -23.139 1.00 86.26 C ANISOU 3477 CB ALA B 192 10588 10178 12010 951 -1071 -380 C ATOM 3478 N ILE B 193 -24.884 11.352 -22.635 1.00105.15 N ANISOU 3478 N ILE B 193 12806 13233 13913 744 -836 -152 N ATOM 3479 CA ILE B 193 -24.020 10.177 -22.611 1.00101.83 C ANISOU 3479 CA ILE B 193 12397 13007 13286 595 -860 -30 C ATOM 3480 C ILE B 193 -24.581 9.070 -23.499 1.00 96.14 C ANISOU 3480 C ILE B 193 11504 12402 12624 556 -810 180 C ATOM 3481 O ILE B 193 -23.852 8.470 -24.290 1.00 90.59 O ANISOU 3481 O ILE B 193 10776 11743 11902 428 -915 319 O ATOM 3482 CB ILE B 193 -23.825 9.648 -21.175 1.00 82.84 C ANISOU 3482 CB ILE B 193 10124 10763 10588 624 -742 -152 C ATOM 3483 CG1 ILE B 193 -22.973 10.625 -20.363 1.00 87.17 C ANISOU 3483 CG1 ILE B 193 10868 11219 11035 612 -857 -366 C ATOM 3484 CG2 ILE B 193 -23.169 8.276 -21.190 1.00 77.80 C ANISOU 3484 CG2 ILE B 193 9485 10302 9773 522 -770 9 C ATOM 3485 CD1 ILE B 193 -22.751 10.195 -18.933 1.00 90.23 C ANISOU 3485 CD1 ILE B 193 11428 11771 11084 639 -779 -493 C ATOM 3486 N TRP B 194 -25.879 8.812 -23.368 1.00102.53 N ANISOU 3486 N TRP B 194 12182 13265 13509 659 -645 179 N ATOM 3487 CA TRP B 194 -26.541 7.780 -24.159 1.00 98.21 C ANISOU 3487 CA TRP B 194 11464 12820 13031 602 -606 352 C ATOM 3488 C TRP B 194 -26.456 8.054 -25.657 1.00 93.09 C ANISOU 3488 C TRP B 194 10738 12070 12563 541 -799 491 C ATOM 3489 O TRP B 194 -26.180 7.152 -26.447 1.00 88.44 O ANISOU 3489 O TRP B 194 10115 11554 11936 420 -854 630 O ATOM 3490 CB TRP B 194 -28.004 7.631 -23.739 1.00106.18 C ANISOU 3490 CB TRP B 194 12297 13914 14133 708 -397 302 C ATOM 3491 CG TRP B 194 -28.195 6.689 -22.597 1.00109.70 C ANISOU 3491 CG TRP B 194 12799 14535 14346 667 -169 280 C ATOM 3492 CD1 TRP B 194 -28.529 7.010 -21.314 1.00114.94 C ANISOU 3492 CD1 TRP B 194 13537 15269 14864 757 38 111 C ATOM 3493 CD2 TRP B 194 -28.040 5.265 -22.629 1.00108.16 C ANISOU 3493 CD2 TRP B 194 12632 14450 14013 516 -125 440 C ATOM 3494 NE1 TRP B 194 -28.605 5.872 -20.547 1.00116.36 N ANISOU 3494 NE1 TRP B 194 13797 15612 14802 652 211 186 N ATOM 3495 CE2 TRP B 194 -28.308 4.789 -21.330 1.00112.77 C ANISOU 3495 CE2 TRP B 194 13320 15161 14366 507 103 394 C ATOM 3496 CE3 TRP B 194 -27.706 4.349 -23.630 1.00103.59 C ANISOU 3496 CE3 TRP B 194 12026 13860 13474 388 -255 608 C ATOM 3497 CZ2 TRP B 194 -28.251 3.434 -21.008 1.00112.53 C ANISOU 3497 CZ2 TRP B 194 13380 15214 14161 368 186 545 C ATOM 3498 CZ3 TRP B 194 -27.651 3.006 -23.307 1.00104.69 C ANISOU 3498 CZ3 TRP B 194 12242 14071 13465 273 -173 720 C ATOM 3499 CH2 TRP B 194 -27.922 2.561 -22.007 1.00109.30 C ANISOU 3499 CH2 TRP B 194 12943 14750 13838 260 36 705 C ATOM 3500 N LEU B 195 -26.697 9.302 -26.041 1.00 95.67 N ANISOU 3500 N LEU B 195 11065 12216 13070 629 -905 452 N ATOM 3501 CA LEU B 195 -26.643 9.693 -27.444 1.00 92.59 C ANISOU 3501 CA LEU B 195 10649 11714 12815 566 -1103 607 C ATOM 3502 C LEU B 195 -25.216 9.634 -27.979 1.00 90.34 C ANISOU 3502 C LEU B 195 10504 11420 12401 375 -1215 683 C ATOM 3503 O LEU B 195 -24.982 9.177 -29.097 1.00 87.09 O ANISOU 3503 O LEU B 195 10065 11057 11968 252 -1297 832 O ATOM 3504 CB LEU B 195 -27.236 11.087 -27.630 1.00 84.24 C ANISOU 3504 CB LEU B 195 9602 10421 11985 724 -1207 562 C ATOM 3505 CG LEU B 195 -28.719 11.167 -27.262 1.00 86.51 C ANISOU 3505 CG LEU B 195 9677 10741 12454 945 -1100 477 C ATOM 3506 CD1 LEU B 195 -29.178 12.609 -27.179 1.00 89.78 C ANISOU 3506 CD1 LEU B 195 10128 10886 13100 1163 -1193 374 C ATOM 3507 CD2 LEU B 195 -29.563 10.384 -28.259 1.00 82.97 C ANISOU 3507 CD2 LEU B 195 9009 10421 12095 907 -1162 643 C ATOM 3508 N ALA B 196 -24.266 10.099 -27.174 1.00 79.73 N ANISOU 3508 N ALA B 196 9295 10033 10967 343 -1213 561 N ATOM 3509 CA ALA B 196 -22.855 10.018 -27.530 1.00 77.81 C ANISOU 3509 CA ALA B 196 9123 9824 10616 158 -1298 601 C ATOM 3510 C ALA B 196 -22.433 8.560 -27.658 1.00 73.54 C ANISOU 3510 C ALA B 196 8512 9505 9926 96 -1236 662 C ATOM 3511 O ALA B 196 -21.602 8.215 -28.496 1.00 71.04 O ANISOU 3511 O ALA B 196 8175 9253 9564 -39 -1288 742 O ATOM 3512 CB ALA B 196 -22.000 10.729 -26.492 1.00 65.57 C ANISOU 3512 CB ALA B 196 7699 8209 9007 138 -1325 431 C ATOM 3513 N SER B 197 -23.016 7.710 -26.820 1.00100.03 N ANISOU 3513 N SER B 197 11839 12963 13203 194 -1112 619 N ATOM 3514 CA SER B 197 -22.729 6.282 -26.844 1.00 97.45 C ANISOU 3514 CA SER B 197 11484 12788 12753 157 -1062 680 C ATOM 3515 C SER B 197 -23.205 5.651 -28.147 1.00 94.70 C ANISOU 3515 C SER B 197 11045 12465 12473 91 -1083 811 C ATOM 3516 O SER B 197 -22.547 4.769 -28.699 1.00 92.89 O ANISOU 3516 O SER B 197 10811 12312 12171 20 -1102 855 O ATOM 3517 CB SER B 197 -23.397 5.592 -25.657 1.00 84.76 C ANISOU 3517 CB SER B 197 9908 11253 11045 246 -916 637 C ATOM 3518 OG SER B 197 -22.933 6.137 -24.435 1.00 88.69 O ANISOU 3518 OG SER B 197 10525 11749 11423 302 -906 503 O ATOM 3519 N ALA B 198 -24.356 6.107 -28.630 1.00 92.69 N ANISOU 3519 N ALA B 198 10712 12147 12360 129 -1092 855 N ATOM 3520 CA ALA B 198 -24.925 5.598 -29.871 1.00 90.28 C ANISOU 3520 CA ALA B 198 10326 11870 12108 61 -1152 969 C ATOM 3521 C ALA B 198 -24.094 6.036 -31.073 1.00 88.63 C ANISOU 3521 C ALA B 198 10175 11634 11865 -59 -1278 1045 C ATOM 3522 O ALA B 198 -23.930 5.283 -32.033 1.00 86.80 O ANISOU 3522 O ALA B 198 9937 11479 11563 -155 -1306 1105 O ATOM 3523 CB ALA B 198 -26.364 6.060 -30.021 1.00 48.15 C ANISOU 3523 CB ALA B 198 4860 6488 6948 151 -1168 991 C ATOM 3524 N LEU B 199 -23.574 7.259 -31.013 1.00 76.00 N ANISOU 3524 N LEU B 199 8651 9921 10305 -71 -1343 1034 N ATOM 3525 CA LEU B 199 -22.730 7.789 -32.078 1.00 75.96 C ANISOU 3525 CA LEU B 199 8718 9891 10253 -228 -1432 1122 C ATOM 3526 C LEU B 199 -21.434 6.994 -32.188 1.00 74.74 C ANISOU 3526 C LEU B 199 8553 9893 9952 -336 -1365 1078 C ATOM 3527 O LEU B 199 -20.917 6.780 -33.284 1.00 74.16 O ANISOU 3527 O LEU B 199 8489 9898 9791 -470 -1374 1144 O ATOM 3528 CB LEU B 199 -22.415 9.266 -31.830 1.00 80.02 C ANISOU 3528 CB LEU B 199 9332 10214 10859 -245 -1508 1115 C ATOM 3529 CG LEU B 199 -23.594 10.238 -31.862 1.00 82.05 C ANISOU 3529 CG LEU B 199 9612 10267 11296 -106 -1605 1156 C ATOM 3530 CD1 LEU B 199 -23.129 11.651 -31.547 1.00 86.06 C ANISOU 3530 CD1 LEU B 199 10267 10535 11898 -130 -1682 1125 C ATOM 3531 CD2 LEU B 199 -24.297 10.186 -33.211 1.00 80.82 C ANISOU 3531 CD2 LEU B 199 9447 10105 11155 -141 -1732 1339 C ATOM 3532 N LEU B 200 -20.914 6.561 -31.044 1.00 73.43 N ANISOU 3532 N LEU B 200 8368 9783 9751 -264 -1300 959 N ATOM 3533 CA LEU B 200 -19.673 5.798 -31.006 1.00 73.23 C ANISOU 3533 CA LEU B 200 8299 9901 9623 -311 -1264 900 C ATOM 3534 C LEU B 200 -19.899 4.355 -31.450 1.00 71.41 C ANISOU 3534 C LEU B 200 8037 9766 9329 -272 -1209 912 C ATOM 3535 O LEU B 200 -18.953 3.651 -31.808 1.00 71.10 O ANISOU 3535 O LEU B 200 7953 9837 9223 -296 -1181 867 O ATOM 3536 CB LEU B 200 -19.065 5.836 -29.601 1.00 66.22 C ANISOU 3536 CB LEU B 200 7421 9030 8711 -230 -1268 780 C ATOM 3537 CG LEU B 200 -18.650 7.215 -29.084 1.00 68.51 C ANISOU 3537 CG LEU B 200 7759 9218 9055 -289 -1336 719 C ATOM 3538 CD1 LEU B 200 -18.328 7.163 -27.604 1.00 70.08 C ANISOU 3538 CD1 LEU B 200 7998 9438 9189 -190 -1357 586 C ATOM 3539 CD2 LEU B 200 -17.462 7.749 -29.868 1.00 68.95 C ANISOU 3539 CD2 LEU B 200 7757 9320 9122 -487 -1373 733 C ATOM 3540 N ALA B 201 -21.155 3.922 -31.427 1.00 88.40 N ANISOU 3540 N ALA B 201 10199 11870 11520 -214 -1195 958 N ATOM 3541 CA ALA B 201 -21.506 2.557 -31.807 1.00 88.12 C ANISOU 3541 CA ALA B 201 10159 11878 11443 -205 -1157 965 C ATOM 3542 C ALA B 201 -21.911 2.455 -33.274 1.00 87.63 C ANISOU 3542 C ALA B 201 10096 11840 11360 -313 -1205 1025 C ATOM 3543 O ALA B 201 -22.191 1.365 -33.769 1.00 88.32 O ANISOU 3543 O ALA B 201 10197 11951 11408 -334 -1193 1009 O ATOM 3544 CB ALA B 201 -22.617 2.032 -30.919 1.00 60.48 C ANISOU 3544 CB ALA B 201 6659 8330 7991 -130 -1104 977 C ATOM 3545 N ILE B 202 -21.950 3.596 -33.958 1.00 85.27 N ANISOU 3545 N ILE B 202 9811 11515 11072 -391 -1276 1098 N ATOM 3546 CA ILE B 202 -22.304 3.644 -35.380 1.00 85.78 C ANISOU 3546 CA ILE B 202 9915 11612 11066 -506 -1352 1181 C ATOM 3547 C ILE B 202 -21.508 2.704 -36.310 1.00 86.44 C ANISOU 3547 C ILE B 202 10031 11825 10985 -592 -1291 1117 C ATOM 3548 O ILE B 202 -22.108 2.054 -37.169 1.00 87.06 O ANISOU 3548 O ILE B 202 10148 11934 10995 -644 -1337 1124 O ATOM 3549 CB ILE B 202 -22.298 5.101 -35.926 1.00 77.79 C ANISOU 3549 CB ILE B 202 8964 10524 10069 -584 -1451 1303 C ATOM 3550 CG1 ILE B 202 -23.483 5.883 -35.356 1.00 77.99 C ANISOU 3550 CG1 ILE B 202 8955 10400 10276 -462 -1546 1355 C ATOM 3551 CG2 ILE B 202 -22.346 5.119 -37.446 1.00 78.77 C ANISOU 3551 CG2 ILE B 202 9178 10713 10037 -733 -1525 1404 C ATOM 3552 CD1 ILE B 202 -23.611 7.289 -35.905 1.00 80.16 C ANISOU 3552 CD1 ILE B 202 9324 10534 10598 -503 -1683 1490 C ATOM 3553 N PRO B 203 -20.168 2.620 -36.147 1.00 85.03 N ANISOU 3553 N PRO B 203 9825 11732 10751 -603 -1191 1033 N ATOM 3554 CA PRO B 203 -19.400 1.715 -37.016 1.00 86.73 C ANISOU 3554 CA PRO B 203 10045 12082 10826 -648 -1103 933 C ATOM 3555 C PRO B 203 -19.914 0.275 -37.046 1.00 87.29 C ANISOU 3555 C PRO B 203 10149 12121 10894 -563 -1097 843 C ATOM 3556 O PRO B 203 -19.748 -0.403 -38.058 1.00 89.65 O ANISOU 3556 O PRO B 203 10505 12493 11066 -617 -1062 765 O ATOM 3557 CB PRO B 203 -18.000 1.755 -36.401 1.00 70.08 C ANISOU 3557 CB PRO B 203 7826 10060 8742 -602 -1009 831 C ATOM 3558 CG PRO B 203 -17.901 3.113 -35.832 1.00 69.54 C ANISOU 3558 CG PRO B 203 7742 9928 8752 -661 -1061 919 C ATOM 3559 CD PRO B 203 -19.272 3.431 -35.300 1.00 67.76 C ANISOU 3559 CD PRO B 203 7584 9538 8624 -591 -1164 1009 C ATOM 3560 N MET B 204 -20.531 -0.177 -35.960 1.00 78.41 N ANISOU 3560 N MET B 204 9013 10882 9896 -450 -1122 848 N ATOM 3561 CA MET B 204 -21.055 -1.537 -35.894 1.00 80.12 C ANISOU 3561 CA MET B 204 9286 11024 10132 -405 -1120 786 C ATOM 3562 C MET B 204 -22.238 -1.748 -36.838 1.00 80.26 C ANISOU 3562 C MET B 204 9350 11022 10122 -527 -1209 826 C ATOM 3563 O MET B 204 -22.544 -2.878 -37.217 1.00 82.38 O ANISOU 3563 O MET B 204 9688 11241 10370 -552 -1217 745 O ATOM 3564 CB MET B 204 -21.436 -1.904 -34.459 1.00 89.09 C ANISOU 3564 CB MET B 204 10418 12049 11383 -296 -1107 817 C ATOM 3565 CG MET B 204 -20.238 -2.134 -33.555 1.00 89.63 C ANISOU 3565 CG MET B 204 10476 12129 11451 -155 -1066 755 C ATOM 3566 SD MET B 204 -19.148 -3.412 -34.213 1.00 93.25 S ANISOU 3566 SD MET B 204 10966 12604 11860 -66 -1027 595 S ATOM 3567 CE MET B 204 -17.766 -3.313 -33.078 1.00 93.83 C ANISOU 3567 CE MET B 204 10952 12728 11970 117 -1037 547 C ATOM 3568 N LEU B 205 -22.899 -0.658 -37.214 1.00 91.50 N ANISOU 3568 N LEU B 205 10741 12470 11555 -601 -1300 946 N ATOM 3569 CA LEU B 205 -24.003 -0.729 -38.164 1.00 92.18 C ANISOU 3569 CA LEU B 205 10848 12564 11613 -711 -1438 995 C ATOM 3570 C LEU B 205 -23.484 -0.931 -39.584 1.00 94.34 C ANISOU 3570 C LEU B 205 11242 12947 11656 -826 -1457 939 C ATOM 3571 O LEU B 205 -24.234 -1.317 -40.480 1.00 96.02 O ANISOU 3571 O LEU B 205 11513 13182 11787 -928 -1581 931 O ATOM 3572 CB LEU B 205 -24.856 0.539 -38.098 1.00 72.07 C ANISOU 3572 CB LEU B 205 8225 9992 9166 -707 -1563 1147 C ATOM 3573 CG LEU B 205 -25.632 0.793 -36.804 1.00 71.14 C ANISOU 3573 CG LEU B 205 7973 9791 9265 -596 -1535 1178 C ATOM 3574 CD1 LEU B 205 -26.352 2.132 -36.866 1.00 70.46 C ANISOU 3574 CD1 LEU B 205 7815 9667 9290 -550 -1660 1296 C ATOM 3575 CD2 LEU B 205 -26.616 -0.334 -36.538 1.00 72.44 C ANISOU 3575 CD2 LEU B 205 8069 9932 9522 -630 -1531 1135 C ATOM 3576 N PHE B 206 -22.196 -0.665 -39.784 1.00 91.63 N ANISOU 3576 N PHE B 206 10926 12692 11196 -823 -1329 890 N ATOM 3577 CA PHE B 206 -21.585 -0.789 -41.103 1.00 94.43 C ANISOU 3577 CA PHE B 206 11391 13191 11296 -941 -1284 824 C ATOM 3578 C PHE B 206 -20.516 -1.875 -41.143 1.00 97.65 C ANISOU 3578 C PHE B 206 11803 13653 11647 -862 -1108 602 C ATOM 3579 O PHE B 206 -20.165 -2.370 -42.213 1.00101.37 O ANISOU 3579 O PHE B 206 12373 14233 11908 -933 -1047 475 O ATOM 3580 CB PHE B 206 -20.987 0.548 -41.549 1.00 94.18 C ANISOU 3580 CB PHE B 206 11380 13251 11154 -1048 -1262 962 C ATOM 3581 CG PHE B 206 -22.001 1.646 -41.695 1.00 92.67 C ANISOU 3581 CG PHE B 206 11223 12976 11010 -1101 -1464 1182 C ATOM 3582 CD1 PHE B 206 -22.688 1.813 -42.886 1.00 93.72 C ANISOU 3582 CD1 PHE B 206 11494 13158 10959 -1227 -1628 1276 C ATOM 3583 CD2 PHE B 206 -22.267 2.509 -40.645 1.00 91.02 C ANISOU 3583 CD2 PHE B 206 10919 12635 11028 -1008 -1507 1282 C ATOM 3584 CE1 PHE B 206 -23.623 2.820 -43.028 1.00 92.69 C ANISOU 3584 CE1 PHE B 206 11386 12935 10898 -1236 -1852 1485 C ATOM 3585 CE2 PHE B 206 -23.201 3.519 -40.781 1.00 90.40 C ANISOU 3585 CE2 PHE B 206 10866 12456 11028 -1011 -1699 1462 C ATOM 3586 CZ PHE B 206 -23.880 3.675 -41.974 1.00 91.04 C ANISOU 3586 CZ PHE B 206 11064 12574 10953 -1114 -1882 1574 C ATOM 3587 N THR B 207 -20.000 -2.244 -39.976 1.00 92.54 N ANISOU 3587 N THR B 207 11055 12928 11177 -700 -1035 546 N ATOM 3588 CA THR B 207 -18.969 -3.271 -39.899 1.00 96.15 C ANISOU 3588 CA THR B 207 11493 13407 11630 -567 -901 339 C ATOM 3589 C THR B 207 -19.590 -4.665 -39.946 1.00 98.96 C ANISOU 3589 C THR B 207 11970 13602 12027 -511 -951 219 C ATOM 3590 O THR B 207 -19.060 -5.570 -40.591 1.00103.12 O ANISOU 3590 O THR B 207 12569 14144 12468 -461 -872 15 O ATOM 3591 CB THR B 207 -18.122 -3.127 -38.619 1.00 82.32 C ANISOU 3591 CB THR B 207 9599 11633 10046 -403 -853 339 C ATOM 3592 OG1 THR B 207 -17.626 -1.786 -38.518 1.00 80.34 O ANISOU 3592 OG1 THR B 207 9245 11499 9781 -492 -829 447 O ATOM 3593 CG2 THR B 207 -16.952 -4.094 -38.641 1.00 86.44 C ANISOU 3593 CG2 THR B 207 10065 12199 10579 -233 -739 125 C ATOM 3594 N MET B 208 -20.722 -4.826 -39.267 1.00108.22 N ANISOU 3594 N MET B 208 13165 14615 13339 -531 -1070 334 N ATOM 3595 CA MET B 208 -21.414 -6.110 -39.205 1.00110.80 C ANISOU 3595 CA MET B 208 13609 14756 13734 -532 -1125 253 C ATOM 3596 C MET B 208 -22.461 -6.247 -40.308 1.00111.32 C ANISOU 3596 C MET B 208 13764 14840 13693 -729 -1249 238 C ATOM 3597 O MET B 208 -22.940 -5.251 -40.851 1.00108.77 O ANISOU 3597 O MET B 208 13397 14646 13285 -846 -1333 359 O ATOM 3598 CB MET B 208 -22.073 -6.291 -37.838 1.00 95.05 C ANISOU 3598 CB MET B 208 11579 12597 11937 -485 -1159 386 C ATOM 3599 CG MET B 208 -21.093 -6.349 -36.676 1.00 94.99 C ANISOU 3599 CG MET B 208 11531 12553 12010 -286 -1084 396 C ATOM 3600 SD MET B 208 -19.960 -7.749 -36.778 1.00100.94 S ANISOU 3600 SD MET B 208 12395 13185 12774 -88 -1031 182 S ATOM 3601 CE MET B 208 -18.392 -6.900 -36.904 1.00100.61 C ANISOU 3601 CE MET B 208 12165 13392 12671 43 -932 105 C ATOM 3602 N GLY B 209 -22.809 -7.488 -40.638 1.00103.24 N ANISOU 3602 N GLY B 209 12880 13670 12678 -765 -1287 89 N ATOM 3603 CA GLY B 209 -23.821 -7.759 -41.644 1.00103.50 C ANISOU 3603 CA GLY B 209 13001 13711 12614 -968 -1440 44 C ATOM 3604 C GLY B 209 -23.982 -9.241 -41.932 1.00107.94 C ANISOU 3604 C GLY B 209 13749 14067 13197 -1000 -1465 -169 C ATOM 3605 O GLY B 209 -23.268 -10.072 -41.373 1.00111.59 O ANISOU 3605 O GLY B 209 14286 14359 13755 -837 -1360 -276 O ATOM 3606 N LEU B 210 -24.921 -9.574 -42.812 1.00100.84 N ANISOU 3606 N LEU B 210 12935 13164 12215 -1208 -1631 -236 N ATOM 3607 CA LEU B 210 -25.177 -10.966 -43.166 1.00104.41 C ANISOU 3607 CA LEU B 210 13590 13391 12689 -1284 -1684 -459 C ATOM 3608 C LEU B 210 -24.355 -11.415 -44.368 1.00107.87 C ANISOU 3608 C LEU B 210 14232 13898 12855 -1245 -1621 -752 C ATOM 3609 O LEU B 210 -24.259 -10.706 -45.370 1.00107.00 O ANISOU 3609 O LEU B 210 14138 14047 12472 -1325 -1648 -768 O ATOM 3610 CB LEU B 210 -26.664 -11.197 -43.444 1.00 85.97 C ANISOU 3610 CB LEU B 210 11229 11008 10427 -1560 -1914 -412 C ATOM 3611 CG LEU B 210 -27.613 -11.112 -42.250 1.00 84.09 C ANISOU 3611 CG LEU B 210 10797 10668 10487 -1631 -1941 -186 C ATOM 3612 CD1 LEU B 210 -29.029 -11.464 -42.676 1.00 84.19 C ANISOU 3612 CD1 LEU B 210 10748 10657 10581 -1925 -2167 -191 C ATOM 3613 CD2 LEU B 210 -27.143 -12.024 -41.128 1.00 86.76 C ANISOU 3613 CD2 LEU B 210 11234 10722 11010 -1511 -1790 -188 C ATOM 3614 N GLN B 211 -23.758 -12.596 -44.254 1.00107.89 N ANISOU 3614 N GLN B 211 14406 13661 12925 -1113 -1532 -984 N ATOM 3615 CA GLN B 211 -23.040 -13.204 -45.365 1.00111.12 C ANISOU 3615 CA GLN B 211 15022 14102 13099 -1056 -1452 -1327 C ATOM 3616 C GLN B 211 -23.410 -14.677 -45.501 1.00113.37 C ANISOU 3616 C GLN B 211 15565 14021 13490 -1103 -1540 -1576 C ATOM 3617 O GLN B 211 -23.722 -15.341 -44.513 1.00112.88 O ANISOU 3617 O GLN B 211 15528 13644 13719 -1078 -1580 -1484 O ATOM 3618 CB GLN B 211 -21.531 -13.059 -45.171 1.00125.19 C ANISOU 3618 CB GLN B 211 16727 15984 14854 -752 -1197 -1428 C ATOM 3619 CG GLN B 211 -20.993 -11.677 -45.493 1.00123.42 C ANISOU 3619 CG GLN B 211 16315 16147 14430 -763 -1086 -1281 C ATOM 3620 CD GLN B 211 -19.480 -11.640 -45.535 1.00125.53 C ANISOU 3620 CD GLN B 211 16489 16556 14650 -511 -821 -1448 C ATOM 3621 OE1 GLN B 211 -18.882 -10.626 -45.893 1.00124.54 O ANISOU 3621 OE1 GLN B 211 16227 16742 14350 -542 -691 -1371 O ATOM 3622 NE2 GLN B 211 -18.851 -12.751 -45.170 1.00128.33 N ANISOU 3622 NE2 GLN B 211 16909 16675 15177 -262 -746 -1676 N ATOM 3623 N ASN B 212 -23.375 -15.181 -46.729 1.00101.57 N ANISOU 3623 N ASN B 212 14292 12558 11741 -1188 -1570 -1890 N ATOM 3624 CA ASN B 212 -23.642 -16.591 -46.984 1.00104.18 C ANISOU 3624 CA ASN B 212 14913 12517 12154 -1234 -1655 -2185 C ATOM 3625 C ASN B 212 -22.340 -17.348 -47.213 1.00107.11 C ANISOU 3625 C ASN B 212 15437 12765 12495 -904 -1438 -2531 C ATOM 3626 O ASN B 212 -21.837 -17.414 -48.335 1.00108.40 O ANISOU 3626 O ASN B 212 15728 13111 12348 -875 -1338 -2840 O ATOM 3627 CB ASN B 212 -24.569 -16.754 -48.188 1.00 95.75 C ANISOU 3627 CB ASN B 212 14018 11531 10832 -1559 -1872 -2353 C ATOM 3628 CG ASN B 212 -25.221 -18.120 -48.240 1.00 97.41 C ANISOU 3628 CG ASN B 212 14495 11308 11207 -1714 -2036 -2579 C ATOM 3629 OD1 ASN B 212 -24.587 -19.109 -48.607 1.00 99.96 O ANISOU 3629 OD1 ASN B 212 15088 11389 11504 -1564 -1950 -2938 O ATOM 3630 ND2 ASN B 212 -26.494 -18.183 -47.870 1.00 95.81 N ANISOU 3630 ND2 ASN B 212 14212 10999 11194 -2020 -2269 -2380 N ATOM 3631 N LEU B 213 -21.800 -17.919 -46.142 1.00109.32 N ANISOU 3631 N LEU B 213 15703 12745 13091 -646 -1366 -2482 N ATOM 3632 CA LEU B 213 -20.498 -18.573 -46.195 1.00111.72 C ANISOU 3632 CA LEU B 213 16081 12932 13436 -260 -1172 -2781 C ATOM 3633 C LEU B 213 -20.568 -20.049 -46.584 1.00113.99 C ANISOU 3633 C LEU B 213 16739 12762 13811 -207 -1241 -3155 C ATOM 3634 O LEU B 213 -19.653 -20.817 -46.287 1.00115.42 O ANISOU 3634 O LEU B 213 17003 12685 14166 152 -1140 -3357 O ATOM 3635 CB LEU B 213 -19.764 -18.409 -44.862 1.00 97.25 C ANISOU 3635 CB LEU B 213 14046 11017 11889 40 -1095 -2543 C ATOM 3636 CG LEU B 213 -19.435 -16.965 -44.478 1.00 95.27 C ANISOU 3636 CG LEU B 213 13439 11202 11558 42 -998 -2243 C ATOM 3637 CD1 LEU B 213 -18.608 -16.918 -43.203 1.00 95.57 C ANISOU 3637 CD1 LEU B 213 13306 11150 11856 355 -945 -2073 C ATOM 3638 CD2 LEU B 213 -18.719 -16.253 -45.619 1.00 95.22 C ANISOU 3638 CD2 LEU B 213 13326 11636 11217 55 -806 -2437 C ATOM 3639 N SER B 214 -21.650 -20.444 -47.247 1.00 97.22 N ANISOU 3639 N SER B 214 14834 10523 11584 -559 -1433 -3256 N ATOM 3640 CA SER B 214 -21.758 -21.803 -47.764 1.00100.36 C ANISOU 3640 CA SER B 214 15620 10483 12029 -558 -1512 -3656 C ATOM 3641 C SER B 214 -20.776 -21.995 -48.916 1.00103.27 C ANISOU 3641 C SER B 214 16104 11036 12099 -328 -1306 -4137 C ATOM 3642 O SER B 214 -20.115 -21.045 -49.339 1.00102.38 O ANISOU 3642 O SER B 214 15762 11411 11726 -235 -1107 -4122 O ATOM 3643 CB SER B 214 -23.185 -22.104 -48.224 1.00122.66 C ANISOU 3643 CB SER B 214 18619 13183 14803 -1038 -1791 -3655 C ATOM 3644 OG SER B 214 -23.532 -21.342 -49.366 1.00122.03 O ANISOU 3644 OG SER B 214 18492 13561 14314 -1265 -1832 -3739 O ATOM 3645 N GLY B 215 -20.680 -23.225 -49.413 1.00121.34 N ANISOU 3645 N GLY B 215 18756 12924 14425 -248 -1339 -4571 N ATOM 3646 CA GLY B 215 -19.725 -23.564 -50.454 1.00123.81 C ANISOU 3646 CA GLY B 215 19202 13363 14477 11 -1112 -5091 C ATOM 3647 C GLY B 215 -19.786 -22.659 -51.669 1.00123.70 C ANISOU 3647 C GLY B 215 19130 13943 13929 -210 -1014 -5193 C ATOM 3648 O GLY B 215 -18.775 -22.090 -52.082 1.00124.60 O ANISOU 3648 O GLY B 215 19060 14462 13819 11 -715 -5311 O ATOM 3649 N ASP B 216 -20.978 -22.517 -52.237 1.00155.20 N ANISOU 3649 N ASP B 216 23269 17990 17711 -660 -1276 -5133 N ATOM 3650 CA ASP B 216 -21.172 -21.669 -53.408 1.00155.15 C ANISOU 3650 CA ASP B 216 23265 18520 17166 -905 -1255 -5186 C ATOM 3651 C ASP B 216 -21.813 -20.337 -53.032 1.00152.26 C ANISOU 3651 C ASP B 216 22577 18513 16761 -1151 -1381 -4629 C ATOM 3652 O ASP B 216 -22.103 -19.511 -53.898 1.00152.12 O ANISOU 3652 O ASP B 216 22556 18922 16323 -1379 -1425 -4565 O ATOM 3653 CB ASP B 216 -22.017 -22.389 -54.462 1.00148.34 C ANISOU 3653 CB ASP B 216 22807 17520 16035 -1223 -1496 -5548 C ATOM 3654 CG ASP B 216 -23.278 -23.000 -53.884 1.00147.10 C ANISOU 3654 CG ASP B 216 22748 16916 16226 -1528 -1874 -5385 C ATOM 3655 OD1 ASP B 216 -23.548 -22.791 -52.683 1.00144.57 O ANISOU 3655 OD1 ASP B 216 22181 16434 16315 -1510 -1929 -4963 O ATOM 3656 OD2 ASP B 216 -24.001 -23.689 -54.634 1.00149.03 O ANISOU 3656 OD2 ASP B 216 23316 16985 16324 -1808 -2110 -5687 O ATOM 3657 N GLY B 217 -22.029 -20.134 -51.736 1.00123.01 N ANISOU 3657 N GLY B 217 18627 14623 13487 -1094 -1444 -4230 N ATOM 3658 CA GLY B 217 -22.663 -18.922 -51.254 1.00120.34 C ANISOU 3658 CA GLY B 217 17982 14566 13174 -1288 -1561 -3725 C ATOM 3659 C GLY B 217 -24.130 -18.879 -51.630 1.00119.17 C ANISOU 3659 C GLY B 217 17911 14405 12962 -1718 -1924 -3614 C ATOM 3660 O GLY B 217 -24.709 -17.805 -51.790 1.00117.01 O ANISOU 3660 O GLY B 217 17448 14466 12544 -1909 -2051 -3308 O ATOM 3661 N THR B 218 -24.734 -20.056 -51.772 1.00118.56 N ANISOU 3661 N THR B 218 18106 13926 13013 -1868 -2110 -3869 N ATOM 3662 CA THR B 218 -26.118 -20.151 -52.220 1.00117.36 C ANISOU 3662 CA THR B 218 18021 13760 12809 -2300 -2478 -3833 C ATOM 3663 C THR B 218 -27.006 -20.881 -51.211 1.00116.71 C ANISOU 3663 C THR B 218 17905 13229 13213 -2474 -2657 -3672 C ATOM 3664 O THR B 218 -28.223 -20.691 -51.193 1.00115.35 O ANISOU 3664 O THR B 218 17606 13101 13121 -2827 -2940 -3490 O ATOM 3665 CB THR B 218 -26.204 -20.840 -53.607 1.00109.76 C ANISOU 3665 CB THR B 218 17454 12795 11453 -2453 -2589 -4334 C ATOM 3666 OG1 THR B 218 -27.079 -20.100 -54.463 1.00109.07 O ANISOU 3666 OG1 THR B 218 17331 13088 11023 -2782 -2869 -4229 O ATOM 3667 CG2 THR B 218 -26.702 -22.279 -53.491 1.00112.05 C ANISOU 3667 CG2 THR B 218 18044 12519 12012 -2593 -2759 -4632 C ATOM 3668 N HIS B 219 -26.392 -21.700 -50.362 1.00127.14 N ANISOU 3668 N HIS B 219 19324 14126 14857 -2228 -2494 -3726 N ATOM 3669 CA HIS B 219 -27.139 -22.499 -49.395 1.00126.82 C ANISOU 3669 CA HIS B 219 19320 13615 15253 -2404 -2629 -3573 C ATOM 3670 C HIS B 219 -27.558 -21.671 -48.181 1.00124.16 C ANISOU 3670 C HIS B 219 18592 13411 15170 -2432 -2600 -3044 C ATOM 3671 O HIS B 219 -26.726 -21.013 -47.557 1.00123.56 O ANISOU 3671 O HIS B 219 18330 13500 15119 -2113 -2380 -2848 O ATOM 3672 CB HIS B 219 -26.318 -23.713 -48.959 1.00119.24 C ANISOU 3672 CB HIS B 219 18669 12111 14525 -2117 -2494 -3813 C ATOM 3673 CG HIS B 219 -27.126 -24.776 -48.285 1.00119.65 C ANISOU 3673 CG HIS B 219 18908 11600 14953 -2377 -2666 -3751 C ATOM 3674 ND1 HIS B 219 -27.494 -24.705 -46.959 1.00118.31 N ANISOU 3674 ND1 HIS B 219 18562 11269 15124 -2430 -2647 -3315 N ATOM 3675 CD2 HIS B 219 -27.648 -25.934 -48.758 1.00121.43 C ANISOU 3675 CD2 HIS B 219 19500 11382 15255 -2631 -2856 -4068 C ATOM 3676 CE1 HIS B 219 -28.202 -25.774 -46.642 1.00119.25 C ANISOU 3676 CE1 HIS B 219 18925 10873 15511 -2718 -2800 -3342 C ATOM 3677 NE2 HIS B 219 -28.310 -26.535 -47.717 1.00121.21 N ANISOU 3677 NE2 HIS B 219 19504 10927 15625 -2849 -2940 -3798 N ATOM 3678 N PRO B 220 -28.859 -21.704 -47.847 1.00 98.81 N ANISOU 3678 N PRO B 220 15246 10143 12152 -2823 -2818 -2835 N ATOM 3679 CA PRO B 220 -29.461 -20.924 -46.757 1.00 95.51 C ANISOU 3679 CA PRO B 220 14447 9879 11964 -2899 -2795 -2368 C ATOM 3680 C PRO B 220 -28.816 -21.186 -45.400 1.00 94.49 C ANISOU 3680 C PRO B 220 14318 9475 12110 -2636 -2573 -2148 C ATOM 3681 O PRO B 220 -28.817 -20.302 -44.542 1.00 91.89 O ANISOU 3681 O PRO B 220 13690 9366 11860 -2539 -2463 -1805 O ATOM 3682 CB PRO B 220 -30.912 -21.413 -46.740 1.00 96.33 C ANISOU 3682 CB PRO B 220 14497 9837 12268 -3387 -3055 -2322 C ATOM 3683 CG PRO B 220 -31.159 -21.908 -48.114 1.00100.69 C ANISOU 3683 CG PRO B 220 15302 10386 12568 -3586 -3282 -2725 C ATOM 3684 CD PRO B 220 -29.863 -22.518 -48.553 1.00102.14 C ANISOU 3684 CD PRO B 220 15864 10365 12580 -3238 -3104 -3075 C ATOM 3685 N GLY B 221 -28.274 -22.384 -45.211 1.00102.00 N ANISOU 3685 N GLY B 221 15623 9938 13196 -2513 -2527 -2351 N ATOM 3686 CA GLY B 221 -27.664 -22.753 -43.947 1.00102.63 C ANISOU 3686 CA GLY B 221 15760 9710 13523 -2260 -2369 -2141 C ATOM 3687 C GLY B 221 -26.347 -22.050 -43.687 1.00102.51 C ANISOU 3687 C GLY B 221 15615 9939 13394 -1779 -2155 -2101 C ATOM 3688 O GLY B 221 -25.841 -22.063 -42.565 1.00102.25 O ANISOU 3688 O GLY B 221 15548 9772 13531 -1554 -2045 -1867 O ATOM 3689 N GLY B 222 -25.788 -21.437 -44.725 1.00107.07 N ANISOU 3689 N GLY B 222 16126 10887 13670 -1643 -2102 -2326 N ATOM 3690 CA GLY B 222 -24.526 -20.734 -44.598 1.00107.43 C ANISOU 3690 CA GLY B 222 16014 11204 13601 -1235 -1889 -2315 C ATOM 3691 C GLY B 222 -24.693 -19.257 -44.298 1.00104.81 C ANISOU 3691 C GLY B 222 15299 11356 13169 -1273 -1838 -1985 C ATOM 3692 O GLY B 222 -23.709 -18.525 -44.196 1.00104.87 O ANISOU 3692 O GLY B 222 15140 11628 13078 -994 -1671 -1948 O ATOM 3693 N LEU B 223 -25.938 -18.816 -44.152 1.00120.81 N ANISOU 3693 N LEU B 223 17170 13489 15241 -1616 -1986 -1755 N ATOM 3694 CA LEU B 223 -26.217 -17.415 -43.858 1.00117.78 C ANISOU 3694 CA LEU B 223 16437 13519 14796 -1648 -1963 -1449 C ATOM 3695 C LEU B 223 -25.868 -17.088 -42.410 1.00117.23 C ANISOU 3695 C LEU B 223 16213 13394 14935 -1459 -1828 -1146 C ATOM 3696 O LEU B 223 -26.593 -17.461 -41.490 1.00117.30 O ANISOU 3696 O LEU B 223 16211 13192 15168 -1608 -1863 -947 O ATOM 3697 CB LEU B 223 -27.686 -17.092 -44.132 1.00100.96 C ANISOU 3697 CB LEU B 223 14161 11512 12689 -2036 -2176 -1323 C ATOM 3698 CG LEU B 223 -28.089 -15.627 -43.959 1.00 97.51 C ANISOU 3698 CG LEU B 223 13373 11477 12198 -2057 -2190 -1036 C ATOM 3699 CD1 LEU B 223 -27.330 -14.747 -44.938 1.00 97.24 C ANISOU 3699 CD1 LEU B 223 13330 11783 11832 -1915 -2149 -1127 C ATOM 3700 CD2 LEU B 223 -29.588 -15.458 -44.138 1.00 96.12 C ANISOU 3700 CD2 LEU B 223 13019 11384 12119 -2408 -2420 -927 C ATOM 3701 N VAL B 224 -24.761 -16.380 -42.212 1.00 92.74 N ANISOU 3701 N VAL B 224 12992 10502 11743 -1156 -1671 -1114 N ATOM 3702 CA VAL B 224 -24.274 -16.087 -40.868 1.00 92.68 C ANISOU 3702 CA VAL B 224 12865 10452 11897 -951 -1563 -866 C ATOM 3703 C VAL B 224 -24.077 -14.595 -40.617 1.00 89.58 C ANISOU 3703 C VAL B 224 12170 10456 11411 -892 -1493 -660 C ATOM 3704 O VAL B 224 -23.964 -13.806 -41.553 1.00 87.73 O ANISOU 3704 O VAL B 224 11842 10520 10971 -933 -1493 -727 O ATOM 3705 CB VAL B 224 -22.947 -16.814 -40.583 1.00 98.51 C ANISOU 3705 CB VAL B 224 13756 10983 12693 -587 -1463 -1028 C ATOM 3706 CG1 VAL B 224 -23.145 -18.318 -40.651 1.00100.71 C ANISOU 3706 CG1 VAL B 224 14373 10778 13112 -617 -1546 -1205 C ATOM 3707 CG2 VAL B 224 -21.877 -16.366 -41.567 1.00 99.31 C ANISOU 3707 CG2 VAL B 224 13785 11369 12578 -390 -1346 -1276 C ATOM 3708 N CYS B 225 -24.039 -14.222 -39.341 1.00 97.76 N ANISOU 3708 N CYS B 225 13086 11473 12584 -806 -1438 -407 N ATOM 3709 CA CYS B 225 -23.766 -12.845 -38.946 1.00 94.47 C ANISOU 3709 CA CYS B 225 12414 11372 12110 -727 -1371 -227 C ATOM 3710 C CYS B 225 -22.276 -12.667 -38.678 1.00 95.32 C ANISOU 3710 C CYS B 225 12488 11549 12181 -408 -1255 -299 C ATOM 3711 O CYS B 225 -21.740 -13.205 -37.711 1.00 98.10 O ANISOU 3711 O CYS B 225 12907 11710 12657 -221 -1233 -249 O ATOM 3712 CB CYS B 225 -24.570 -12.478 -37.701 1.00112.16 C ANISOU 3712 CB CYS B 225 14537 13584 14494 -816 -1368 54 C ATOM 3713 SG CYS B 225 -24.350 -10.772 -37.158 1.00107.11 S ANISOU 3713 SG CYS B 225 13615 13278 13803 -726 -1303 246 S ATOM 3714 N THR B 226 -21.616 -11.906 -39.543 1.00 93.21 N ANISOU 3714 N THR B 226 12112 11564 11740 -362 -1191 -406 N ATOM 3715 CA THR B 226 -20.164 -11.791 -39.521 1.00 95.00 C ANISOU 3715 CA THR B 226 12264 11899 11934 -92 -1066 -529 C ATOM 3716 C THR B 226 -19.746 -10.401 -40.002 1.00 91.47 C ANISOU 3716 C THR B 226 11611 11819 11326 -144 -989 -472 C ATOM 3717 O THR B 226 -20.506 -9.737 -40.707 1.00 88.87 O ANISOU 3717 O THR B 226 11271 11631 10864 -365 -1043 -402 O ATOM 3718 CB THR B 226 -19.528 -12.884 -40.422 1.00 92.54 C ANISOU 3718 CB THR B 226 12120 11470 11569 35 -1015 -865 C ATOM 3719 OG1 THR B 226 -18.101 -12.867 -40.298 1.00 94.87 O ANISOU 3719 OG1 THR B 226 12289 11872 11885 332 -885 -1000 O ATOM 3720 CG2 THR B 226 -19.912 -12.670 -41.880 1.00 91.99 C ANISOU 3720 CG2 THR B 226 12116 11584 11250 -174 -1007 -1024 C ATOM 3721 N PRO B 227 -18.549 -9.940 -39.597 1.00 98.54 N ANISOU 3721 N PRO B 227 12342 12857 12242 49 -883 -485 N ATOM 3722 CA PRO B 227 -17.992 -8.701 -40.153 1.00 96.39 C ANISOU 3722 CA PRO B 227 11895 12913 11815 -26 -785 -455 C ATOM 3723 C PRO B 227 -17.910 -8.739 -41.679 1.00 98.15 C ANISOU 3723 C PRO B 227 12204 13303 11787 -154 -704 -640 C ATOM 3724 O PRO B 227 -17.340 -9.673 -42.242 1.00102.47 O ANISOU 3724 O PRO B 227 12834 13812 12289 -30 -614 -910 O ATOM 3725 CB PRO B 227 -16.585 -8.633 -39.535 1.00 86.06 C ANISOU 3725 CB PRO B 227 10401 11693 10606 220 -684 -527 C ATOM 3726 CG PRO B 227 -16.376 -9.957 -38.831 1.00 89.79 C ANISOU 3726 CG PRO B 227 10983 11874 11259 465 -745 -623 C ATOM 3727 CD PRO B 227 -17.740 -10.438 -38.475 1.00 88.58 C ANISOU 3727 CD PRO B 227 11037 11457 11160 319 -882 -482 C ATOM 3728 N ILE B 228 -18.478 -7.731 -42.333 1.00 93.82 N ANISOU 3728 N ILE B 228 11654 12930 11063 -388 -743 -497 N ATOM 3729 CA ILE B 228 -18.548 -7.706 -43.791 1.00 95.50 C ANISOU 3729 CA ILE B 228 11999 13312 10976 -549 -699 -630 C ATOM 3730 C ILE B 228 -17.526 -6.760 -44.413 1.00 95.95 C ANISOU 3730 C ILE B 228 11941 13685 10830 -604 -507 -632 C ATOM 3731 O ILE B 228 -17.567 -6.499 -45.614 1.00 96.59 O ANISOU 3731 O ILE B 228 12144 13952 10604 -776 -456 -684 O ATOM 3732 CB ILE B 228 -19.945 -7.280 -44.275 1.00 68.37 C ANISOU 3732 CB ILE B 228 8677 9860 7441 -792 -914 -459 C ATOM 3733 CG1 ILE B 228 -20.284 -5.882 -43.753 1.00 64.22 C ANISOU 3733 CG1 ILE B 228 8007 9411 6981 -870 -989 -146 C ATOM 3734 CG2 ILE B 228 -20.989 -8.298 -43.843 1.00 68.78 C ANISOU 3734 CG2 ILE B 228 8829 9630 7673 -802 -1081 -488 C ATOM 3735 CD1 ILE B 228 -21.648 -5.389 -44.173 1.00 62.01 C ANISOU 3735 CD1 ILE B 228 7790 9119 6651 -1059 -1224 30 C ATOM 3736 N VAL B 229 -16.615 -6.245 -43.595 1.00 88.21 N ANISOU 3736 N VAL B 229 10737 12773 10007 -483 -405 -571 N ATOM 3737 CA VAL B 229 -15.596 -5.328 -44.090 1.00 89.09 C ANISOU 3737 CA VAL B 229 10703 13180 9965 -572 -207 -563 C ATOM 3738 C VAL B 229 -14.238 -6.019 -44.146 1.00 93.52 C ANISOU 3738 C VAL B 229 11097 13866 10571 -361 26 -856 C ATOM 3739 O VAL B 229 -14.053 -7.082 -43.554 1.00 95.43 O ANISOU 3739 O VAL B 229 11325 13920 11016 -101 -8 -1018 O ATOM 3740 CB VAL B 229 -15.497 -4.060 -43.217 1.00 95.56 C ANISOU 3740 CB VAL B 229 11360 14020 10928 -637 -266 -291 C ATOM 3741 CG1 VAL B 229 -16.863 -3.403 -43.078 1.00 90.83 C ANISOU 3741 CG1 VAL B 229 10897 13279 10337 -784 -499 -27 C ATOM 3742 CG2 VAL B 229 -14.916 -4.396 -41.852 1.00 94.93 C ANISOU 3742 CG2 VAL B 229 11091 13827 11152 -390 -287 -325 C ATOM 3743 N ASP B 230 -13.297 -5.416 -44.867 1.00 87.70 N ANISOU 3743 N ASP B 230 10229 13443 9649 -473 264 -920 N ATOM 3744 CA ASP B 230 -11.954 -5.975 -44.995 1.00 91.19 C ANISOU 3744 CA ASP B 230 10440 14066 10142 -274 520 -1219 C ATOM 3745 C ASP B 230 -11.271 -6.065 -43.634 1.00 91.45 C ANISOU 3745 C ASP B 230 10192 14010 10544 -20 449 -1205 C ATOM 3746 O ASP B 230 -11.644 -5.361 -42.694 1.00 88.73 O ANISOU 3746 O ASP B 230 9812 13553 10347 -75 268 -945 O ATOM 3747 CB ASP B 230 -11.105 -5.158 -45.973 1.00137.96 C ANISOU 3747 CB ASP B 230 16240 20383 15795 -506 816 -1251 C ATOM 3748 CG ASP B 230 -11.070 -3.685 -45.627 1.00136.02 C ANISOU 3748 CG ASP B 230 15896 20224 15561 -767 771 -916 C ATOM 3749 OD1 ASP B 230 -12.149 -3.104 -45.387 1.00133.35 O ANISOU 3749 OD1 ASP B 230 15757 19694 15216 -902 526 -638 O ATOM 3750 OD2 ASP B 230 -9.962 -3.108 -45.593 1.00136.74 O ANISOU 3750 OD2 ASP B 230 15700 20567 15687 -837 979 -944 O ATOM 3751 N THR B 231 -10.273 -6.938 -43.537 1.00110.62 N ANISOU 3751 N THR B 231 12428 16490 13112 275 581 -1499 N ATOM 3752 CA THR B 231 -9.583 -7.194 -42.276 1.00109.09 C ANISOU 3752 CA THR B 231 11982 16207 13261 564 470 -1508 C ATOM 3753 C THR B 231 -8.901 -5.956 -41.693 1.00105.52 C ANISOU 3753 C THR B 231 11224 15974 12894 421 485 -1334 C ATOM 3754 O THR B 231 -8.825 -5.802 -40.475 1.00102.25 O ANISOU 3754 O THR B 231 10712 15430 12706 543 281 -1203 O ATOM 3755 CB THR B 231 -8.545 -8.328 -42.427 1.00134.50 C ANISOU 3755 CB THR B 231 15017 19467 16621 935 608 -1880 C ATOM 3756 OG1 THR B 231 -7.708 -8.371 -41.265 1.00132.26 O ANISOU 3756 OG1 THR B 231 14428 19174 16651 1197 489 -1869 O ATOM 3757 CG2 THR B 231 -7.681 -8.104 -43.660 1.00136.26 C ANISOU 3757 CG2 THR B 231 15051 20092 16630 831 979 -2128 C ATOM 3758 N ALA B 232 -8.416 -5.074 -42.561 1.00109.01 N ANISOU 3758 N ALA B 232 11542 16741 13138 141 722 -1329 N ATOM 3759 CA ALA B 232 -7.760 -3.848 -42.117 1.00106.15 C ANISOU 3759 CA ALA B 232 10907 16574 12851 -58 749 -1170 C ATOM 3760 C ALA B 232 -8.748 -2.886 -41.460 1.00103.18 C ANISOU 3760 C ALA B 232 10737 15983 12483 -261 500 -822 C ATOM 3761 O ALA B 232 -8.436 -2.265 -40.445 1.00100.09 O ANISOU 3761 O ALA B 232 10181 15565 12282 -261 365 -707 O ATOM 3762 CB ALA B 232 -7.060 -3.173 -43.283 1.00 82.86 C ANISOU 3762 CB ALA B 232 7819 14003 9663 -357 1088 -1230 C ATOM 3763 N THR B 233 -9.936 -2.768 -42.044 1.00 94.48 N ANISOU 3763 N THR B 233 9986 14736 11177 -421 431 -676 N ATOM 3764 CA THR B 233 -10.975 -1.902 -41.497 1.00 91.05 C ANISOU 3764 CA THR B 233 9740 14091 10762 -574 203 -372 C ATOM 3765 C THR B 233 -11.479 -2.444 -40.166 1.00 87.38 C ANISOU 3765 C THR B 233 9309 13349 10541 -320 -39 -332 C ATOM 3766 O THR B 233 -11.773 -1.681 -39.245 1.00 82.95 O ANISOU 3766 O THR B 233 8742 12681 10095 -366 -192 -152 O ATOM 3767 CB THR B 233 -12.169 -1.775 -42.461 1.00 78.44 C ANISOU 3767 CB THR B 233 8479 12413 8912 -762 153 -246 C ATOM 3768 OG1 THR B 233 -11.700 -1.376 -43.755 1.00 81.30 O ANISOU 3768 OG1 THR B 233 8865 13042 8983 -1001 383 -280 O ATOM 3769 CG2 THR B 233 -13.167 -0.746 -41.952 1.00 73.11 C ANISOU 3769 CG2 THR B 233 7943 11549 8285 -903 -67 56 C ATOM 3770 N LEU B 234 -11.567 -3.767 -40.071 1.00102.91 N ANISOU 3770 N LEU B 234 11338 15192 12572 -61 -64 -506 N ATOM 3771 CA LEU B 234 -12.055 -4.419 -38.862 1.00 99.66 C ANISOU 3771 CA LEU B 234 11007 14506 12355 163 -275 -453 C ATOM 3772 C LEU B 234 -11.117 -4.171 -37.688 1.00 96.72 C ANISOU 3772 C LEU B 234 10383 14182 12183 317 -351 -451 C ATOM 3773 O LEU B 234 -11.566 -3.928 -36.571 1.00 93.05 O ANISOU 3773 O LEU B 234 9983 13560 11813 356 -531 -295 O ATOM 3774 CB LEU B 234 -12.231 -5.921 -39.086 1.00 77.96 C ANISOU 3774 CB LEU B 234 8400 11584 9637 392 -282 -642 C ATOM 3775 CG LEU B 234 -12.775 -6.694 -37.883 1.00 75.67 C ANISOU 3775 CG LEU B 234 8246 10981 9524 591 -490 -557 C ATOM 3776 CD1 LEU B 234 -14.205 -6.271 -37.587 1.00 71.79 C ANISOU 3776 CD1 LEU B 234 7966 10326 8987 393 -615 -318 C ATOM 3777 CD2 LEU B 234 -12.689 -8.195 -38.112 1.00 80.64 C ANISOU 3777 CD2 LEU B 234 9008 11414 10217 831 -492 -765 C ATOM 3778 N LYS B 235 -9.814 -4.240 -37.943 1.00105.71 N ANISOU 3778 N LYS B 235 11227 15561 13378 404 -213 -640 N ATOM 3779 CA LYS B 235 -8.824 -3.970 -36.909 1.00103.47 C ANISOU 3779 CA LYS B 235 10656 15371 13287 537 -311 -660 C ATOM 3780 C LYS B 235 -9.010 -2.560 -36.366 1.00 99.45 C ANISOU 3780 C LYS B 235 10125 14894 12765 272 -393 -450 C ATOM 3781 O LYS B 235 -8.981 -2.339 -35.156 1.00 96.25 O ANISOU 3781 O LYS B 235 9701 14394 12474 358 -593 -367 O ATOM 3782 CB LYS B 235 -7.407 -4.136 -37.459 1.00 88.24 C ANISOU 3782 CB LYS B 235 8346 13756 11426 622 -116 -911 C ATOM 3783 CG LYS B 235 -7.033 -5.567 -37.800 1.00 92.05 C ANISOU 3783 CG LYS B 235 8806 14187 11983 974 -58 -1171 C ATOM 3784 CD LYS B 235 -5.608 -5.648 -38.323 1.00 94.76 C ANISOU 3784 CD LYS B 235 8707 14884 12416 1073 163 -1444 C ATOM 3785 CE LYS B 235 -5.239 -7.069 -38.716 1.00 98.01 C ANISOU 3785 CE LYS B 235 9101 15221 12916 1463 233 -1741 C ATOM 3786 NZ LYS B 235 -3.848 -7.154 -39.244 1.00 99.34 N ANISOU 3786 NZ LYS B 235 8787 15767 13190 1589 480 -2042 N ATOM 3787 N VAL B 236 -9.214 -1.611 -37.273 1.00 88.90 N ANISOU 3787 N VAL B 236 8828 13674 11275 -51 -247 -366 N ATOM 3788 CA VAL B 236 -9.419 -0.217 -36.900 1.00 86.34 C ANISOU 3788 CA VAL B 236 8524 13336 10946 -316 -319 -171 C ATOM 3789 C VAL B 236 -10.673 -0.019 -36.047 1.00 83.05 C ANISOU 3789 C VAL B 236 8383 12627 10545 -281 -530 12 C ATOM 3790 O VAL B 236 -10.622 0.642 -35.012 1.00 80.48 O ANISOU 3790 O VAL B 236 8029 12236 10313 -293 -673 84 O ATOM 3791 CB VAL B 236 -9.483 0.694 -38.142 1.00 84.33 C ANISOU 3791 CB VAL B 236 8325 13214 10503 -665 -134 -83 C ATOM 3792 CG1 VAL B 236 -9.752 2.131 -37.734 1.00 82.00 C ANISOU 3792 CG1 VAL B 236 8099 12826 10231 -920 -237 126 C ATOM 3793 CG2 VAL B 236 -8.188 0.599 -38.931 1.00 87.37 C ANISOU 3793 CG2 VAL B 236 8405 13934 10856 -741 125 -266 C ATOM 3794 N VAL B 237 -11.794 -0.594 -36.476 1.00 99.56 N ANISOU 3794 N VAL B 237 10728 14557 12544 -247 -542 67 N ATOM 3795 CA VAL B 237 -13.052 -0.420 -35.749 1.00 96.30 C ANISOU 3795 CA VAL B 237 10535 13903 12153 -231 -702 229 C ATOM 3796 C VAL B 237 -13.047 -1.123 -34.389 1.00 94.62 C ANISOU 3796 C VAL B 237 10330 13560 12060 17 -842 208 C ATOM 3797 O VAL B 237 -13.747 -0.704 -33.468 1.00 92.32 O ANISOU 3797 O VAL B 237 10148 13133 11797 17 -953 326 O ATOM 3798 CB VAL B 237 -14.285 -0.864 -36.577 1.00 77.29 C ANISOU 3798 CB VAL B 237 8355 11379 9633 -285 -695 290 C ATOM 3799 CG1 VAL B 237 -14.314 -0.143 -37.916 1.00 79.42 C ANISOU 3799 CG1 VAL B 237 8663 11779 9734 -533 -591 339 C ATOM 3800 CG2 VAL B 237 -14.296 -2.366 -36.775 1.00 80.26 C ANISOU 3800 CG2 VAL B 237 8786 11695 10013 -94 -670 141 C ATOM 3801 N ILE B 238 -12.263 -2.190 -34.265 1.00114.65 N ANISOU 3801 N ILE B 238 12767 16137 14659 237 -835 58 N ATOM 3802 CA ILE B 238 -12.145 -2.898 -32.995 1.00114.14 C ANISOU 3802 CA ILE B 238 12737 15944 14686 480 -994 63 C ATOM 3803 C ILE B 238 -11.249 -2.120 -32.034 1.00113.11 C ANISOU 3803 C ILE B 238 12417 15935 14623 492 -1105 58 C ATOM 3804 O ILE B 238 -11.563 -1.981 -30.851 1.00111.25 O ANISOU 3804 O ILE B 238 12290 15593 14387 553 -1255 148 O ATOM 3805 CB ILE B 238 -11.599 -4.333 -33.179 1.00 93.69 C ANISOU 3805 CB ILE B 238 10128 13308 12163 750 -991 -89 C ATOM 3806 CG1 ILE B 238 -12.602 -5.200 -33.944 1.00 96.03 C ANISOU 3806 CG1 ILE B 238 10668 13424 12394 731 -925 -92 C ATOM 3807 CG2 ILE B 238 -11.269 -4.966 -31.834 1.00 92.97 C ANISOU 3807 CG2 ILE B 238 10070 13094 12159 1007 -1192 -56 C ATOM 3808 CD1 ILE B 238 -13.974 -5.247 -33.324 1.00 93.96 C ANISOU 3808 CD1 ILE B 238 10662 12940 12100 649 -1011 98 C ATOM 3809 N GLN B 239 -10.138 -1.607 -32.558 1.00102.80 N ANISOU 3809 N GLN B 239 10829 14868 13363 410 -1024 -57 N ATOM 3810 CA GLN B 239 -9.207 -0.800 -31.774 1.00101.74 C ANISOU 3810 CA GLN B 239 10473 14875 13310 367 -1136 -88 C ATOM 3811 C GLN B 239 -9.891 0.412 -31.153 1.00 99.48 C ANISOU 3811 C GLN B 239 10342 14484 12971 162 -1215 54 C ATOM 3812 O GLN B 239 -9.739 0.670 -29.960 1.00 98.44 O ANISOU 3812 O GLN B 239 10228 14317 12859 228 -1396 66 O ATOM 3813 CB GLN B 239 -8.030 -0.340 -32.636 1.00143.98 C ANISOU 3813 CB GLN B 239 15477 20513 18716 223 -981 -223 C ATOM 3814 CG GLN B 239 -7.000 -1.420 -32.915 1.00146.47 C ANISOU 3814 CG GLN B 239 15523 20987 19141 487 -935 -428 C ATOM 3815 CD GLN B 239 -5.960 -0.980 -33.925 1.00148.96 C ANISOU 3815 CD GLN B 239 15486 21623 19488 311 -702 -572 C ATOM 3816 OE1 GLN B 239 -5.868 0.200 -34.265 1.00149.06 O ANISOU 3816 OE1 GLN B 239 15447 21737 19452 -34 -611 -496 O ATOM 3817 NE2 GLN B 239 -5.170 -1.928 -34.412 1.00150.95 N ANISOU 3817 NE2 GLN B 239 15500 22029 19826 543 -592 -783 N ATOM 3818 N VAL B 240 -10.634 1.154 -31.969 1.00 94.59 N ANISOU 3818 N VAL B 240 9848 13812 12279 -71 -1093 150 N ATOM 3819 CA VAL B 240 -11.333 2.348 -31.504 1.00 93.17 C ANISOU 3819 CA VAL B 240 9822 13501 12078 -241 -1158 269 C ATOM 3820 C VAL B 240 -12.270 2.033 -30.338 1.00 91.48 C ANISOU 3820 C VAL B 240 9826 13100 11834 -76 -1283 333 C ATOM 3821 O VAL B 240 -12.344 2.790 -29.371 1.00 91.25 O ANISOU 3821 O VAL B 240 9852 13013 11806 -106 -1392 341 O ATOM 3822 CB VAL B 240 -12.125 3.024 -32.649 1.00 85.04 C ANISOU 3822 CB VAL B 240 8926 12408 10979 -460 -1037 386 C ATOM 3823 CG1 VAL B 240 -12.969 4.176 -32.120 1.00 83.82 C ANISOU 3823 CG1 VAL B 240 8946 12065 10838 -564 -1125 498 C ATOM 3824 CG2 VAL B 240 -11.177 3.510 -33.735 1.00 87.41 C ANISOU 3824 CG2 VAL B 240 9045 12904 11261 -683 -893 351 C ATOM 3825 N ASN B 241 -12.966 0.904 -30.422 1.00 90.04 N ANISOU 3825 N ASN B 241 9775 12823 11614 81 -1256 366 N ATOM 3826 CA ASN B 241 -13.842 0.477 -29.336 1.00 89.46 C ANISOU 3826 CA ASN B 241 9903 12592 11495 210 -1334 439 C ATOM 3827 C ASN B 241 -13.066 0.066 -28.088 1.00 89.87 C ANISOU 3827 C ASN B 241 9931 12680 11537 386 -1494 392 C ATOM 3828 O ASN B 241 -13.451 0.404 -26.970 1.00 89.61 O ANISOU 3828 O ASN B 241 10034 12584 11430 409 -1578 433 O ATOM 3829 CB ASN B 241 -14.750 -0.667 -29.788 1.00103.25 C ANISOU 3829 CB ASN B 241 11794 14218 13219 284 -1265 494 C ATOM 3830 CG ASN B 241 -15.650 -1.168 -28.674 1.00103.12 C ANISOU 3830 CG ASN B 241 11978 14054 13150 376 -1309 587 C ATOM 3831 OD1 ASN B 241 -15.400 -2.219 -28.082 1.00103.86 O ANISOU 3831 OD1 ASN B 241 12151 14087 13224 539 -1374 596 O ATOM 3832 ND2 ASN B 241 -16.703 -0.414 -28.380 1.00102.23 N ANISOU 3832 ND2 ASN B 241 11952 13878 13013 275 -1268 661 N ATOM 3833 N THR B 242 -11.971 -0.661 -28.286 1.00101.85 N ANISOU 3833 N THR B 242 11274 14306 13117 524 -1542 296 N ATOM 3834 CA THR B 242 -11.149 -1.127 -27.176 1.00102.79 C ANISOU 3834 CA THR B 242 11351 14467 13237 725 -1744 258 C ATOM 3835 C THR B 242 -10.526 0.054 -26.437 1.00102.57 C ANISOU 3835 C THR B 242 11211 14560 13202 610 -1874 202 C ATOM 3836 O THR B 242 -10.400 0.038 -25.213 1.00102.97 O ANISOU 3836 O THR B 242 11364 14596 13165 706 -2060 217 O ATOM 3837 CB THR B 242 -10.043 -2.089 -27.657 1.00102.74 C ANISOU 3837 CB THR B 242 11121 14564 13350 927 -1777 139 C ATOM 3838 OG1 THR B 242 -10.637 -3.184 -28.364 1.00104.13 O ANISOU 3838 OG1 THR B 242 11440 14592 13533 1025 -1662 161 O ATOM 3839 CG2 THR B 242 -9.247 -2.629 -26.479 1.00103.26 C ANISOU 3839 CG2 THR B 242 11156 14652 13425 1175 -2042 124 C ATOM 3840 N PHE B 243 -10.145 1.082 -27.187 1.00 99.68 N ANISOU 3840 N PHE B 243 10661 14303 12910 382 -1782 141 N ATOM 3841 CA PHE B 243 -9.571 2.281 -26.590 1.00100.82 C ANISOU 3841 CA PHE B 243 10708 14527 13071 218 -1901 76 C ATOM 3842 C PHE B 243 -10.631 3.147 -25.913 1.00100.36 C ANISOU 3842 C PHE B 243 10933 14294 12907 117 -1909 142 C ATOM 3843 O PHE B 243 -10.496 3.501 -24.743 1.00101.59 O ANISOU 3843 O PHE B 243 11176 14442 12982 148 -2077 97 O ATOM 3844 CB PHE B 243 -8.818 3.111 -27.635 1.00121.14 C ANISOU 3844 CB PHE B 243 13016 17249 15764 -35 -1784 8 C ATOM 3845 CG PHE B 243 -7.445 2.589 -27.958 1.00122.50 C ANISOU 3845 CG PHE B 243 12812 17671 16062 39 -1808 -125 C ATOM 3846 CD1 PHE B 243 -6.448 2.589 -26.996 1.00123.77 C ANISOU 3846 CD1 PHE B 243 12774 17970 16284 129 -2051 -232 C ATOM 3847 CD2 PHE B 243 -7.144 2.124 -29.227 1.00122.84 C ANISOU 3847 CD2 PHE B 243 12684 17830 16158 22 -1592 -163 C ATOM 3848 CE1 PHE B 243 -5.181 2.120 -27.290 1.00125.48 C ANISOU 3848 CE1 PHE B 243 12584 18438 16654 222 -2082 -371 C ATOM 3849 CE2 PHE B 243 -5.879 1.653 -29.527 1.00124.96 C ANISOU 3849 CE2 PHE B 243 12567 18353 16561 113 -1581 -318 C ATOM 3850 CZ PHE B 243 -4.896 1.651 -28.558 1.00126.11 C ANISOU 3850 CZ PHE B 243 12471 18637 16809 222 -1829 -422 C ATOM 3851 N MET B 244 -11.691 3.472 -26.646 1.00 97.80 N ANISOU 3851 N MET B 244 10747 13836 12578 14 -1736 233 N ATOM 3852 CA MET B 244 -12.669 4.455 -26.183 1.00 97.95 C ANISOU 3852 CA MET B 244 10976 13693 12549 -77 -1720 268 C ATOM 3853 C MET B 244 -13.666 3.939 -25.143 1.00 98.13 C ANISOU 3853 C MET B 244 11238 13611 12435 89 -1729 317 C ATOM 3854 O MET B 244 -14.172 4.716 -24.334 1.00100.34 O ANISOU 3854 O MET B 244 11665 13809 12650 64 -1752 279 O ATOM 3855 CB MET B 244 -13.424 5.060 -27.371 1.00 94.84 C ANISOU 3855 CB MET B 244 10617 13198 12219 -232 -1567 355 C ATOM 3856 CG MET B 244 -12.554 5.873 -28.320 1.00 96.09 C ANISOU 3856 CG MET B 244 10605 13433 12470 -468 -1536 336 C ATOM 3857 SD MET B 244 -11.676 7.222 -27.506 1.00 98.79 S ANISOU 3857 SD MET B 244 10898 13766 12873 -652 -1691 217 S ATOM 3858 CE MET B 244 -10.000 6.589 -27.502 1.00 99.52 C ANISOU 3858 CE MET B 244 10634 14157 13022 -652 -1763 96 C ATOM 3859 N SER B 245 -13.953 2.641 -25.163 1.00106.29 N ANISOU 3859 N SER B 245 12322 14641 13422 246 -1694 391 N ATOM 3860 CA SER B 245 -14.936 2.080 -24.238 1.00106.98 C ANISOU 3860 CA SER B 245 12641 14635 13370 357 -1664 468 C ATOM 3861 C SER B 245 -14.291 1.338 -23.073 1.00108.39 C ANISOU 3861 C SER B 245 12906 14868 13409 516 -1833 466 C ATOM 3862 O SER B 245 -14.966 0.988 -22.105 1.00109.89 O ANISOU 3862 O SER B 245 13321 15004 13430 580 -1818 533 O ATOM 3863 CB SER B 245 -15.901 1.144 -24.968 1.00 92.97 C ANISOU 3863 CB SER B 245 10924 12772 11629 381 -1514 581 C ATOM 3864 OG SER B 245 -15.295 -0.112 -25.222 1.00 93.07 O ANISOU 3864 OG SER B 245 10904 12800 11658 506 -1565 602 O ATOM 3865 N PHE B 246 -12.988 1.099 -23.165 1.00114.37 N ANISOU 3865 N PHE B 246 13479 15746 14231 579 -1996 395 N ATOM 3866 CA PHE B 246 -12.300 0.322 -22.141 1.00115.50 C ANISOU 3866 CA PHE B 246 13689 15938 14259 767 -2213 409 C ATOM 3867 C PHE B 246 -11.045 1.009 -21.612 1.00116.16 C ANISOU 3867 C PHE B 246 13593 16188 14356 750 -2452 268 C ATOM 3868 O PHE B 246 -11.045 1.533 -20.500 1.00117.56 O ANISOU 3868 O PHE B 246 13921 16387 14359 731 -2587 229 O ATOM 3869 CB PHE B 246 -11.961 -1.075 -22.666 1.00 91.46 C ANISOU 3869 CB PHE B 246 10594 12855 11300 952 -2232 472 C ATOM 3870 CG PHE B 246 -11.390 -1.991 -21.623 1.00 92.75 C ANISOU 3870 CG PHE B 246 10881 13011 11350 1181 -2477 534 C ATOM 3871 CD1 PHE B 246 -12.209 -2.566 -20.666 1.00 93.77 C ANISOU 3871 CD1 PHE B 246 11365 13007 11257 1233 -2481 693 C ATOM 3872 CD2 PHE B 246 -10.037 -2.287 -21.606 1.00 93.23 C ANISOU 3872 CD2 PHE B 246 10697 13203 11523 1344 -2707 442 C ATOM 3873 CE1 PHE B 246 -11.688 -3.413 -19.705 1.00 95.42 C ANISOU 3873 CE1 PHE B 246 11738 13187 11329 1438 -2732 788 C ATOM 3874 CE2 PHE B 246 -9.510 -3.134 -20.648 1.00 94.10 C ANISOU 3874 CE2 PHE B 246 10930 13290 11532 1586 -2982 517 C ATOM 3875 CZ PHE B 246 -10.337 -3.698 -19.697 1.00 95.45 C ANISOU 3875 CZ PHE B 246 11512 13300 11453 1632 -3005 704 C ATOM 3876 N LEU B 247 -9.981 1.000 -22.409 1.00 94.75 N ANISOU 3876 N LEU B 247 10550 13608 11842 743 -2497 177 N ATOM 3877 CA LEU B 247 -8.679 1.493 -21.964 1.00 95.89 C ANISOU 3877 CA LEU B 247 10448 13942 12043 725 -2743 36 C ATOM 3878 C LEU B 247 -8.706 2.947 -21.497 1.00 96.91 C ANISOU 3878 C LEU B 247 10615 14084 12124 480 -2787 -67 C ATOM 3879 O LEU B 247 -8.243 3.255 -20.400 1.00 98.73 O ANISOU 3879 O LEU B 247 10900 14382 12229 496 -3035 -143 O ATOM 3880 CB LEU B 247 -7.624 1.302 -23.056 1.00102.32 C ANISOU 3880 CB LEU B 247 10851 14922 13106 720 -2703 -58 C ATOM 3881 CG LEU B 247 -7.218 -0.146 -23.340 1.00102.65 C ANISOU 3881 CG LEU B 247 10803 14974 13225 1024 -2743 -30 C ATOM 3882 CD1 LEU B 247 -6.139 -0.208 -24.411 1.00103.85 C ANISOU 3882 CD1 LEU B 247 10509 15332 13618 1014 -2664 -174 C ATOM 3883 CD2 LEU B 247 -6.755 -0.834 -22.064 1.00103.49 C ANISOU 3883 CD2 LEU B 247 11010 15089 13224 1285 -3081 5 C ATOM 3884 N PHE B 248 -9.242 3.836 -22.327 1.00 92.49 N ANISOU 3884 N PHE B 248 10048 13439 11656 257 -2569 -72 N ATOM 3885 CA PHE B 248 -9.290 5.261 -21.991 1.00 94.23 C ANISOU 3885 CA PHE B 248 10327 13607 11869 23 -2604 -176 C ATOM 3886 C PHE B 248 -10.147 5.605 -20.757 1.00 96.08 C ANISOU 3886 C PHE B 248 10919 13718 11869 73 -2654 -195 C ATOM 3887 O PHE B 248 -9.639 6.217 -19.817 1.00 98.00 O ANISOU 3887 O PHE B 248 11209 14010 12017 16 -2865 -331 O ATOM 3888 CB PHE B 248 -9.716 6.104 -23.204 1.00101.45 C ANISOU 3888 CB PHE B 248 11194 14416 12938 -205 -2375 -143 C ATOM 3889 CG PHE B 248 -9.454 7.576 -23.049 1.00103.97 C ANISOU 3889 CG PHE B 248 11522 14661 13320 -470 -2439 -255 C ATOM 3890 CD1 PHE B 248 -8.511 8.041 -22.147 1.00106.06 C ANISOU 3890 CD1 PHE B 248 11705 15027 13566 -547 -2692 -415 C ATOM 3891 CD2 PHE B 248 -10.168 8.498 -23.797 1.00104.85 C ANISOU 3891 CD2 PHE B 248 11744 14579 13515 -644 -2274 -200 C ATOM 3892 CE1 PHE B 248 -8.277 9.396 -22.003 1.00109.06 C ANISOU 3892 CE1 PHE B 248 12120 15301 14018 -817 -2761 -534 C ATOM 3893 CE2 PHE B 248 -9.939 9.853 -23.658 1.00107.58 C ANISOU 3893 CE2 PHE B 248 12142 14797 13939 -888 -2345 -297 C ATOM 3894 CZ PHE B 248 -8.993 10.303 -22.760 1.00109.61 C ANISOU 3894 CZ PHE B 248 12325 15139 14184 -987 -2579 -472 C ATOM 3895 N PRO B 249 -11.439 5.214 -20.745 1.00 86.27 N ANISOU 3895 N PRO B 249 9918 12335 10525 169 -2456 -76 N ATOM 3896 CA PRO B 249 -12.261 5.637 -19.603 1.00 88.30 C ANISOU 3896 CA PRO B 249 10487 12507 10557 199 -2448 -123 C ATOM 3897 C PRO B 249 -11.871 4.978 -18.283 1.00 89.72 C ANISOU 3897 C PRO B 249 10826 12796 10466 349 -2662 -130 C ATOM 3898 O PRO B 249 -11.977 5.614 -17.235 1.00 92.46 O ANISOU 3898 O PRO B 249 11377 13145 10609 319 -2752 -253 O ATOM 3899 CB PRO B 249 -13.672 5.201 -20.008 1.00 82.70 C ANISOU 3899 CB PRO B 249 9916 11670 9837 264 -2170 18 C ATOM 3900 CG PRO B 249 -13.458 4.065 -20.933 1.00 79.78 C ANISOU 3900 CG PRO B 249 9390 11338 9585 339 -2123 156 C ATOM 3901 CD PRO B 249 -12.216 4.400 -21.700 1.00 78.65 C ANISOU 3901 CD PRO B 249 8950 11299 9633 239 -2233 80 C ATOM 3902 N MET B 250 -11.427 3.727 -18.330 1.00 92.48 N ANISOU 3902 N MET B 250 11114 13224 10802 516 -2753 -4 N ATOM 3903 CA MET B 250 -11.063 3.014 -17.110 1.00 93.47 C ANISOU 3903 CA MET B 250 11426 13430 10657 676 -2990 38 C ATOM 3904 C MET B 250 -9.759 3.533 -16.522 1.00 94.62 C ANISOU 3904 C MET B 250 11423 13740 10787 644 -3344 -126 C ATOM 3905 O MET B 250 -9.605 3.594 -15.305 1.00 97.08 O ANISOU 3905 O MET B 250 11960 14117 10809 688 -3557 -169 O ATOM 3906 CB MET B 250 -10.984 1.507 -17.352 1.00102.92 C ANISOU 3906 CB MET B 250 12626 14605 11873 885 -3010 234 C ATOM 3907 CG MET B 250 -12.343 0.850 -17.500 1.00102.85 C ANISOU 3907 CG MET B 250 12857 14436 11783 905 -2717 407 C ATOM 3908 SD MET B 250 -13.455 1.307 -16.156 1.00106.15 S ANISOU 3908 SD MET B 250 13683 14832 11819 844 -2596 412 S ATOM 3909 CE MET B 250 -14.680 2.278 -17.032 1.00105.73 C ANISOU 3909 CE MET B 250 13545 14670 11957 677 -2227 336 C ATOM 3910 N LEU B 251 -8.823 3.902 -17.390 1.00108.40 N ANISOU 3910 N LEU B 251 12785 15571 12829 547 -3407 -221 N ATOM 3911 CA LEU B 251 -7.566 4.485 -16.942 1.00110.04 C ANISOU 3911 CA LEU B 251 12776 15953 13080 463 -3736 -398 C ATOM 3912 C LEU B 251 -7.826 5.822 -16.257 1.00112.55 C ANISOU 3912 C LEU B 251 13287 16213 13264 247 -3774 -579 C ATOM 3913 O LEU B 251 -7.178 6.160 -15.268 1.00114.41 O ANISOU 3913 O LEU B 251 13571 16560 13338 220 -4088 -716 O ATOM 3914 CB LEU B 251 -6.600 4.658 -18.114 1.00113.55 C ANISOU 3914 CB LEU B 251 12742 16512 13888 354 -3716 -462 C ATOM 3915 CG LEU B 251 -5.199 5.175 -17.786 1.00115.27 C ANISOU 3915 CG LEU B 251 12627 16950 14221 242 -4048 -647 C ATOM 3916 CD1 LEU B 251 -4.584 4.374 -16.651 1.00116.12 C ANISOU 3916 CD1 LEU B 251 12782 17199 14139 497 -4441 -636 C ATOM 3917 CD2 LEU B 251 -4.319 5.104 -19.021 1.00114.90 C ANISOU 3917 CD2 LEU B 251 12082 17048 14527 160 -3949 -683 C ATOM 3918 N VAL B 252 -8.783 6.576 -16.788 1.00115.34 N ANISOU 3918 N VAL B 252 13757 16379 13686 107 -3472 -590 N ATOM 3919 CA VAL B 252 -9.182 7.845 -16.191 1.00118.08 C ANISOU 3919 CA VAL B 252 14328 16608 13930 -61 -3470 -776 C ATOM 3920 C VAL B 252 -9.879 7.620 -14.853 1.00119.90 C ANISOU 3920 C VAL B 252 14967 16834 13756 79 -3500 -797 C ATOM 3921 O VAL B 252 -9.531 8.243 -13.849 1.00122.46 O ANISOU 3921 O VAL B 252 15451 17204 13875 12 -3720 -990 O ATOM 3922 CB VAL B 252 -10.114 8.644 -17.125 1.00 96.02 C ANISOU 3922 CB VAL B 252 11567 13587 11331 -189 -3148 -761 C ATOM 3923 CG1 VAL B 252 -10.733 9.822 -16.387 1.00 99.34 C ANISOU 3923 CG1 VAL B 252 12282 13836 11626 -278 -3123 -957 C ATOM 3924 CG2 VAL B 252 -9.354 9.115 -18.356 1.00 94.83 C ANISOU 3924 CG2 VAL B 252 11069 13440 11522 -399 -3131 -757 C ATOM 3925 N ALA B 253 -10.859 6.722 -14.846 1.00 96.06 N ANISOU 3925 N ALA B 253 12121 13768 10607 250 -3271 -605 N ATOM 3926 CA ALA B 253 -11.617 6.422 -13.635 1.00 98.14 C ANISOU 3926 CA ALA B 253 12779 14046 10465 359 -3226 -591 C ATOM 3927 C ALA B 253 -10.729 5.840 -12.537 1.00 98.50 C ANISOU 3927 C ALA B 253 12940 14275 10209 457 -3601 -585 C ATOM 3928 O ALA B 253 -10.970 6.067 -11.353 1.00100.60 O ANISOU 3928 O ALA B 253 13539 14592 10091 465 -3676 -679 O ATOM 3929 CB ALA B 253 -12.768 5.476 -13.948 1.00 73.02 C ANISOU 3929 CB ALA B 253 9707 10789 7247 480 -2906 -357 C ATOM 3930 N SER B 254 -9.701 5.097 -12.937 1.00 93.64 N ANISOU 3930 N SER B 254 12050 13766 9762 542 -3843 -483 N ATOM 3931 CA SER B 254 -8.760 4.514 -11.987 1.00 94.25 C ANISOU 3931 CA SER B 254 12186 14019 9607 669 -4264 -462 C ATOM 3932 C SER B 254 -7.926 5.599 -11.317 1.00 96.52 C ANISOU 3932 C SER B 254 12436 14422 9817 507 -4587 -744 C ATOM 3933 O SER B 254 -7.688 5.555 -10.109 1.00 98.53 O ANISOU 3933 O SER B 254 12963 14788 9686 551 -4867 -799 O ATOM 3934 CB SER B 254 -7.845 3.507 -12.683 1.00100.47 C ANISOU 3934 CB SER B 254 12625 14881 10669 833 -4439 -318 C ATOM 3935 OG SER B 254 -8.601 2.486 -13.310 1.00 98.82 O ANISOU 3935 OG SER B 254 12478 14536 10533 969 -4159 -81 O ATOM 3936 N ILE B 255 -7.479 6.567 -12.112 1.00122.47 N ANISOU 3936 N ILE B 255 15402 17675 13455 296 -4558 -919 N ATOM 3937 CA ILE B 255 -6.723 7.699 -11.589 1.00124.98 C ANISOU 3937 CA ILE B 255 15670 18058 13756 80 -4844 -1208 C ATOM 3938 C ILE B 255 -7.591 8.499 -10.627 1.00127.87 C ANISOU 3938 C ILE B 255 16505 18314 13766 8 -4745 -1383 C ATOM 3939 O ILE B 255 -7.152 8.864 -9.537 1.00130.17 O ANISOU 3939 O ILE B 255 16992 18712 13754 -39 -5060 -1566 O ATOM 3940 CB ILE B 255 -6.219 8.618 -12.719 1.00102.44 C ANISOU 3940 CB ILE B 255 12423 15138 11361 -180 -4760 -1328 C ATOM 3941 CG1 ILE B 255 -5.167 7.895 -13.563 1.00100.48 C ANISOU 3941 CG1 ILE B 255 11672 15068 11439 -124 -4880 -1219 C ATOM 3942 CG2 ILE B 255 -5.634 9.897 -12.145 1.00105.05 C ANISOU 3942 CG2 ILE B 255 12777 15465 11671 -454 -5014 -1639 C ATOM 3943 CD1 ILE B 255 -4.740 8.660 -14.797 1.00100.13 C ANISOU 3943 CD1 ILE B 255 11246 14980 11818 -394 -4718 -1285 C ATOM 3944 N LEU B 256 -8.830 8.759 -11.035 1.00118.58 N ANISOU 3944 N LEU B 256 15498 16935 12622 12 -4312 -1342 N ATOM 3945 CA LEU B 256 -9.779 9.484 -10.198 1.00121.45 C ANISOU 3945 CA LEU B 256 16278 17191 12678 -14 -4143 -1524 C ATOM 3946 C LEU B 256 -10.071 8.714 -8.912 1.00122.55 C ANISOU 3946 C LEU B 256 16805 17485 12273 150 -4227 -1454 C ATOM 3947 O LEU B 256 -10.107 9.294 -7.827 1.00124.95 O ANISOU 3947 O LEU B 256 17428 17836 12210 100 -4349 -1684 O ATOM 3948 CB LEU B 256 -11.075 9.764 -10.963 1.00 97.77 C ANISOU 3948 CB LEU B 256 13315 13969 9866 7 -3664 -1463 C ATOM 3949 CG LEU B 256 -10.966 10.750 -12.129 1.00 97.82 C ANISOU 3949 CG LEU B 256 13057 13773 10339 -174 -3568 -1544 C ATOM 3950 CD1 LEU B 256 -12.322 10.973 -12.779 1.00 98.22 C ANISOU 3950 CD1 LEU B 256 13173 13614 10532 -109 -3143 -1471 C ATOM 3951 CD2 LEU B 256 -10.367 12.071 -11.665 1.00100.23 C ANISOU 3951 CD2 LEU B 256 13435 13988 10658 -391 -3798 -1877 C ATOM 3952 N ASN B 257 -10.279 7.407 -9.040 1.00113.81 N ANISOU 3952 N ASN B 257 15698 16446 11097 333 -4159 -1136 N ATOM 3953 CA ASN B 257 -10.526 6.554 -7.881 1.00115.23 C ANISOU 3953 CA ASN B 257 16268 16758 10756 473 -4242 -998 C ATOM 3954 C ASN B 257 -9.319 6.457 -6.950 1.00116.29 C ANISOU 3954 C ASN B 257 16467 17096 10623 487 -4796 -1074 C ATOM 3955 O ASN B 257 -9.463 6.172 -5.761 1.00118.04 O ANISOU 3955 O ASN B 257 17101 17435 10314 542 -4924 -1057 O ATOM 3956 CB ASN B 257 -10.983 5.159 -8.313 1.00124.60 C ANISOU 3956 CB ASN B 257 17444 17916 11983 642 -4065 -621 C ATOM 3957 CG ASN B 257 -12.486 5.070 -8.502 1.00125.60 C ANISOU 3957 CG ASN B 257 17743 17917 12062 638 -3535 -537 C ATOM 3958 OD1 ASN B 257 -13.220 4.748 -7.567 1.00128.00 O ANISOU 3958 OD1 ASN B 257 18431 18277 11928 667 -3379 -474 O ATOM 3959 ND2 ASN B 257 -12.952 5.362 -9.711 1.00123.65 N ANISOU 3959 ND2 ASN B 257 17204 17519 12258 593 -3258 -534 N ATOM 3960 N THR B 258 -8.131 6.687 -7.498 1.00152.90 N ANISOU 3960 N THR B 258 20686 21791 15617 428 -5126 -1155 N ATOM 3961 CA THR B 258 -6.917 6.730 -6.693 1.00154.32 C ANISOU 3961 CA THR B 258 20837 22181 15617 421 -5695 -1270 C ATOM 3962 C THR B 258 -6.860 8.031 -5.904 1.00157.44 C ANISOU 3962 C THR B 258 21455 22587 15780 203 -5819 -1651 C ATOM 3963 O THR B 258 -6.521 8.036 -4.720 1.00159.80 O ANISOU 3963 O THR B 258 22060 23045 15612 214 -6164 -1749 O ATOM 3964 CB THR B 258 -5.654 6.619 -7.567 1.00131.79 C ANISOU 3964 CB THR B 258 17392 19416 13267 405 -5980 -1270 C ATOM 3965 OG1 THR B 258 -5.678 5.385 -8.293 1.00129.47 O ANISOU 3965 OG1 THR B 258 16909 19100 13185 635 -5870 -953 O ATOM 3966 CG2 THR B 258 -4.400 6.671 -6.707 1.00133.63 C ANISOU 3966 CG2 THR B 258 17516 19874 13382 371 -6485 -1365 C ATOM 3967 N VAL B 259 -7.210 9.131 -6.566 1.00138.72 N ANISOU 3967 N VAL B 259 18960 20025 13722 8 -5550 -1866 N ATOM 3968 CA VAL B 259 -7.208 10.445 -5.930 1.00141.77 C ANISOU 3968 CA VAL B 259 19566 20346 13956 -205 -5636 -2259 C ATOM 3969 C VAL B 259 -8.264 10.538 -4.830 1.00144.39 C ANISOU 3969 C VAL B 259 20478 20669 13715 -126 -5420 -2355 C ATOM 3970 O VAL B 259 -7.988 11.024 -3.733 1.00147.03 O ANISOU 3970 O VAL B 259 21127 21104 13633 -201 -5690 -2615 O ATOM 3971 CB VAL B 259 -7.448 11.573 -6.960 1.00128.18 C ANISOU 3971 CB VAL B 259 17621 18355 12727 -411 -5367 -2427 C ATOM 3972 CG1 VAL B 259 -7.544 12.916 -6.260 1.00131.74 C ANISOU 3972 CG1 VAL B 259 18365 18673 13018 -609 -5442 -2846 C ATOM 3973 CG2 VAL B 259 -6.343 11.591 -8.009 1.00126.37 C ANISOU 3973 CG2 VAL B 259 16826 18165 13023 -549 -5561 -2361 C ATOM 3974 N ILE B 260 -9.469 10.064 -5.132 1.00164.63 N ANISOU 3974 N ILE B 260 23170 23131 16251 13 -4926 -2157 N ATOM 3975 CA ILE B 260 -10.573 10.082 -4.178 1.00167.11 C ANISOU 3975 CA ILE B 260 23982 23463 16048 87 -4624 -2229 C ATOM 3976 C ILE B 260 -10.255 9.237 -2.938 1.00168.35 C ANISOU 3976 C ILE B 260 24505 23884 15576 181 -4918 -2104 C ATOM 3977 O ILE B 260 -10.543 9.641 -1.807 1.00172.18 O ANISOU 3977 O ILE B 260 25433 24462 15524 147 -4929 -2328 O ATOM 3978 CB ILE B 260 -11.869 9.549 -4.832 1.00114.70 C ANISOU 3978 CB ILE B 260 17319 16706 9556 210 -4056 -1986 C ATOM 3979 CG1 ILE B 260 -12.561 10.641 -5.656 1.00112.83 C ANISOU 3979 CG1 ILE B 260 16924 16204 9743 138 -3712 -2195 C ATOM 3980 CG2 ILE B 260 -12.820 9.042 -3.782 1.00120.02 C ANISOU 3980 CG2 ILE B 260 18456 17506 9641 304 -3790 -1923 C ATOM 3981 CD1 ILE B 260 -13.924 10.236 -6.197 1.00108.90 C ANISOU 3981 CD1 ILE B 260 16403 15610 9364 256 -3172 -2009 C ATOM 3982 N ALA B 261 -9.628 8.083 -3.151 1.00175.62 N ANISOU 3982 N ALA B 261 25257 24916 16555 304 -5174 -1756 N ATOM 3983 CA ALA B 261 -9.294 7.183 -2.051 1.00176.72 C ANISOU 3983 CA ALA B 261 25750 25272 16124 416 -5497 -1567 C ATOM 3984 C ALA B 261 -8.283 7.831 -1.114 1.00178.87 C ANISOU 3984 C ALA B 261 26049 25703 16210 273 -5915 -1819 C ATOM 3985 O ALA B 261 -8.332 7.637 0.102 1.00180.88 O ANISOU 3985 O ALA B 261 26670 26120 15937 261 -5965 -1799 O ATOM 3986 CB ALA B 261 -8.760 5.862 -2.581 1.00116.95 C ANISOU 3986 CB ALA B 261 17929 17726 8780 597 -5687 -1148 C ATOM 3987 N ASN B 262 -7.366 8.602 -1.688 1.00141.61 N ANISOU 3987 N ASN B 262 20908 20946 11953 131 -6171 -2040 N ATOM 3988 CA ASN B 262 -6.377 9.320 -0.897 1.00144.27 C ANISOU 3988 CA ASN B 262 21197 21421 12199 -56 -6532 -2296 C ATOM 3989 C ASN B 262 -6.982 10.563 -0.258 1.00146.76 C ANISOU 3989 C ASN B 262 21894 21651 12216 -223 -6374 -2733 C ATOM 3990 O ASN B 262 -6.718 10.862 0.904 1.00151.02 O ANISOU 3990 O ASN B 262 22702 22346 12331 -314 -6534 -2895 O ATOM 3991 CB ASN B 262 -5.168 9.697 -1.754 1.00199.43 C ANISOU 3991 CB ASN B 262 27573 28403 19797 -187 -6822 -2367 C ATOM 3992 CG ASN B 262 -4.384 8.487 -2.221 1.00198.38 C ANISOU 3992 CG ASN B 262 27043 28393 19940 -5 -7008 -1988 C ATOM 3993 OD1 ASN B 262 -4.346 7.459 -1.544 1.00201.02 O ANISOU 3993 OD1 ASN B 262 27566 28854 19959 179 -7102 -1707 O ATOM 3994 ND2 ASN B 262 -3.752 8.603 -3.383 1.00195.42 N ANISOU 3994 ND2 ASN B 262 26123 27970 20158 -56 -7047 -1983 N ATOM 3995 N LYS B 263 -7.808 11.274 -1.021 1.00154.83 N ANISOU 3995 N LYS B 263 22945 22421 13462 -249 -6059 -2932 N ATOM 3996 CA LYS B 263 -8.449 12.490 -0.535 1.00157.84 C ANISOU 3996 CA LYS B 263 23677 22657 13637 -368 -5866 -3378 C ATOM 3997 C LYS B 263 -9.399 12.191 0.621 1.00159.91 C ANISOU 3997 C LYS B 263 24498 23051 13210 -259 -5577 -3391 C ATOM 3998 O LYS B 263 -9.542 12.997 1.538 1.00162.63 O ANISOU 3998 O LYS B 263 25157 23417 13219 -366 -5543 -3744 O ATOM 3999 CB LYS B 263 -9.206 13.192 -1.665 1.00184.02 C ANISOU 3999 CB LYS B 263 26825 25645 17448 -384 -5472 -3491 C ATOM 4000 CG LYS B 263 -8.591 14.509 -2.115 1.00184.93 C ANISOU 4000 CG LYS B 263 26737 25534 17994 -638 -5663 -3848 C ATOM 4001 CD LYS B 263 -7.211 14.299 -2.718 1.00183.54 C ANISOU 4001 CD LYS B 263 26063 25460 18216 -781 -6134 -3724 C ATOM 4002 CE LYS B 263 -6.615 15.610 -3.206 1.00184.32 C ANISOU 4002 CE LYS B 263 25949 25322 18764 -1094 -6278 -4043 C ATOM 4003 NZ LYS B 263 -5.274 15.417 -3.824 1.00183.12 N ANISOU 4003 NZ LYS B 263 25213 25309 19056 -1269 -6587 -3880 N ATOM 4004 N LEU B 264 -10.040 11.027 0.571 1.00194.42 N ANISOU 4004 N LEU B 264 28984 27513 17374 -64 -5349 -3006 N ATOM 4005 CA LEU B 264 -10.973 10.616 1.615 1.00196.44 C ANISOU 4005 CA LEU B 264 29739 27919 16979 10 -5015 -2952 C ATOM 4006 C LEU B 264 -10.245 10.396 2.936 1.00199.42 C ANISOU 4006 C LEU B 264 30312 28571 16889 -75 -5330 -2930 C ATOM 4007 O LEU B 264 -10.738 10.772 4.000 1.00204.35 O ANISOU 4007 O LEU B 264 31341 29315 16986 -127 -5146 -3151 O ATOM 4008 CB LEU B 264 -11.717 9.343 1.206 1.00153.96 C ANISOU 4008 CB LEU B 264 24402 22559 11535 190 -4725 -2489 C ATOM 4009 CG LEU B 264 -12.768 8.826 2.191 1.00155.94 C ANISOU 4009 CG LEU B 264 25135 22969 11144 229 -4301 -2374 C ATOM 4010 CD1 LEU B 264 -13.899 9.831 2.347 1.00158.09 C ANISOU 4010 CD1 LEU B 264 25627 23156 11286 216 -3787 -2790 C ATOM 4011 CD2 LEU B 264 -13.304 7.472 1.749 1.00153.58 C ANISOU 4011 CD2 LEU B 264 24835 22671 10849 355 -4086 -1858 C ATOM 4012 N THR B 265 -9.069 9.781 2.859 1.00143.69 N ANISOU 4012 N THR B 265 22945 21624 10027 -74 -5797 -2675 N ATOM 4013 CA THR B 265 -8.248 9.540 4.040 1.00150.42 C ANISOU 4013 CA THR B 265 23927 22743 10482 -132 -6172 -2637 C ATOM 4014 C THR B 265 -7.728 10.862 4.602 1.00154.62 C ANISOU 4014 C THR B 265 24500 23298 10951 -351 -6381 -3143 C ATOM 4015 O THR B 265 -7.565 11.017 5.812 1.00160.28 O ANISOU 4015 O THR B 265 25526 24227 11146 -425 -6507 -3276 O ATOM 4016 CB THR B 265 -7.067 8.599 3.724 1.00173.88 C ANISOU 4016 CB THR B 265 26495 25809 13761 -45 -6625 -2268 C ATOM 4017 OG1 THR B 265 -7.559 7.401 3.110 1.00169.26 O ANISOU 4017 OG1 THR B 265 25869 25145 13296 157 -6422 -1823 O ATOM 4018 CG2 THR B 265 -6.307 8.237 4.992 1.00180.76 C ANISOU 4018 CG2 THR B 265 27539 26966 14178 -64 -7012 -2190 C ATOM 4019 N VAL B 266 -7.477 11.815 3.710 1.00196.62 N ANISOU 4019 N VAL B 266 29516 28388 16804 -468 -6415 -3422 N ATOM 4020 CA VAL B 266 -7.046 13.150 4.107 1.00200.60 C ANISOU 4020 CA VAL B 266 30056 28834 17328 -704 -6577 -3919 C ATOM 4021 C VAL B 266 -8.144 13.883 4.878 1.00203.81 C ANISOU 4021 C VAL B 266 30987 29186 17267 -719 -6178 -4288 C ATOM 4022 O VAL B 266 -7.867 14.567 5.865 1.00210.18 O ANISOU 4022 O VAL B 266 32026 30099 17734 -865 -6319 -4622 O ATOM 4023 CB VAL B 266 -6.615 13.991 2.882 1.00178.78 C ANISOU 4023 CB VAL B 266 26860 25788 15281 -843 -6653 -4098 C ATOM 4024 CG1 VAL B 266 -6.363 15.438 3.279 1.00182.79 C ANISOU 4024 CG1 VAL B 266 27480 26158 15814 -1102 -6746 -4627 C ATOM 4025 CG2 VAL B 266 -5.373 13.393 2.241 1.00177.22 C ANISOU 4025 CG2 VAL B 266 26101 25703 15530 -866 -7052 -3807 C ATOM 4026 N MET B 267 -9.391 13.723 4.443 1.00183.19 N ANISOU 4026 N MET B 267 28546 26427 14631 -559 -5669 -4239 N ATOM 4027 CA MET B 267 -10.497 14.436 5.073 1.00185.69 C ANISOU 4027 CA MET B 267 29300 26685 14570 -541 -5218 -4613 C ATOM 4028 C MET B 267 -10.807 13.877 6.459 1.00191.46 C ANISOU 4028 C MET B 267 30447 27764 14537 -515 -5113 -4541 C ATOM 4029 O MET B 267 -11.250 14.608 7.344 1.00196.31 O ANISOU 4029 O MET B 267 31400 28432 14755 -573 -4916 -4938 O ATOM 4030 CB MET B 267 -11.757 14.363 4.202 1.00189.63 C ANISOU 4030 CB MET B 267 29818 26963 15271 -356 -4681 -4569 C ATOM 4031 CG MET B 267 -11.629 14.973 2.813 1.00187.01 C ANISOU 4031 CG MET B 267 29119 26271 15664 -365 -4732 -4659 C ATOM 4032 SD MET B 267 -11.282 16.741 2.801 1.00189.17 S ANISOU 4032 SD MET B 267 29403 26218 16256 -572 -4862 -5277 S ATOM 4033 CE MET B 267 -11.217 17.057 1.039 1.00185.90 C ANISOU 4033 CE MET B 267 28537 25419 16679 -564 -4892 -5191 C ATOM 4034 N VAL B 268 -10.569 12.581 6.646 1.00202.32 N ANISOU 4034 N VAL B 268 31795 29365 15713 -426 -5242 -4037 N ATOM 4035 CA VAL B 268 -10.863 11.932 7.922 1.00207.75 C ANISOU 4035 CA VAL B 268 32878 30381 15677 -405 -5150 -3892 C ATOM 4036 C VAL B 268 -9.737 12.114 8.941 1.00214.99 C ANISOU 4036 C VAL B 268 33855 31542 16291 -541 -5685 -4004 C ATOM 4037 O VAL B 268 -8.556 12.134 8.585 1.00215.00 O ANISOU 4037 O VAL B 268 33504 31525 16664 -605 -6199 -3941 O ATOM 4038 CB VAL B 268 -11.211 10.432 7.751 1.00198.50 C ANISOU 4038 CB VAL B 268 31717 29310 14393 -252 -5019 -3283 C ATOM 4039 CG1 VAL B 268 -9.991 9.628 7.337 1.00196.66 C ANISOU 4039 CG1 VAL B 268 31127 29100 14496 -211 -5576 -2896 C ATOM 4040 CG2 VAL B 268 -11.818 9.881 9.034 1.00204.44 C ANISOU 4040 CG2 VAL B 268 32932 30365 14382 -248 -4775 -3162 C ATOM 4041 N THR B 279 -19.553 18.188 10.288 1.00274.29 N ANISOU 4041 N THR B 279 42832 38360 23026 172 -736 -7423 N ATOM 4042 CA THR B 279 -19.624 17.633 11.634 1.00280.99 C ANISOU 4042 CA THR B 279 43960 39729 23076 87 -644 -7370 C ATOM 4043 C THR B 279 -21.078 17.517 12.091 1.00284.93 C ANISOU 4043 C THR B 279 44498 40485 23276 262 151 -7521 C ATOM 4044 O THR B 279 -21.353 17.157 13.236 1.00291.73 O ANISOU 4044 O THR B 279 45591 41794 23459 238 338 -7536 O ATOM 4045 CB THR B 279 -18.828 18.493 12.642 1.00270.60 C ANISOU 4045 CB THR B 279 42904 38480 21431 -72 -1027 -7837 C ATOM 4046 OG1 THR B 279 -17.718 19.110 11.979 1.00267.58 O ANISOU 4046 OG1 THR B 279 42387 37711 21570 -200 -1629 -7911 O ATOM 4047 CG2 THR B 279 -18.316 17.642 13.798 1.00275.87 C ANISOU 4047 CG2 THR B 279 43819 39654 21345 -198 -1280 -7557 C ATOM 4048 N GLU B 296 -22.008 17.821 11.191 1.00279.79 N ANISOU 4048 N GLU B 296 43597 39566 23145 456 612 -7627 N ATOM 4049 CA GLU B 296 -23.431 17.731 11.516 1.00282.38 C ANISOU 4049 CA GLU B 296 43852 40144 23296 648 1390 -7776 C ATOM 4050 C GLU B 296 -24.094 16.417 11.067 1.00277.90 C ANISOU 4050 C GLU B 296 43097 39790 22703 687 1728 -7153 C ATOM 4051 O GLU B 296 -24.702 15.730 11.888 1.00282.33 O ANISOU 4051 O GLU B 296 43759 40797 22717 693 2092 -6978 O ATOM 4052 CB GLU B 296 -24.211 18.952 10.998 1.00249.43 C ANISOU 4052 CB GLU B 296 39502 35590 19680 867 1775 -8354 C ATOM 4053 CG GLU B 296 -23.803 20.279 11.616 1.00255.12 C ANISOU 4053 CG GLU B 296 40451 36110 20374 825 1589 -9024 C ATOM 4054 CD GLU B 296 -24.588 21.447 11.049 1.00255.52 C ANISOU 4054 CD GLU B 296 40355 35688 21043 1047 1974 -9536 C ATOM 4055 OE1 GLU B 296 -25.271 21.264 10.019 1.00250.35 O ANISOU 4055 OE1 GLU B 296 39398 34807 20919 1240 2264 -9334 O ATOM 4056 OE2 GLU B 296 -24.526 22.549 11.635 1.00261.21 O ANISOU 4056 OE2 GLU B 296 41279 36237 21731 1037 1982 -10129 O ATOM 4057 N PRO B 297 -23.986 16.056 9.772 1.00254.59 N ANISOU 4057 N PRO B 297 39886 36513 20334 715 1609 -6804 N ATOM 4058 CA PRO B 297 -24.703 14.836 9.392 1.00251.30 C ANISOU 4058 CA PRO B 297 39297 36295 19890 725 1984 -6251 C ATOM 4059 C PRO B 297 -23.780 13.629 9.276 1.00247.98 C ANISOU 4059 C PRO B 297 38973 35953 19293 523 1486 -5591 C ATOM 4060 O PRO B 297 -22.573 13.740 9.494 1.00248.76 O ANISOU 4060 O PRO B 297 39231 35985 19302 402 840 -5566 O ATOM 4061 CB PRO B 297 -25.242 15.184 8.007 1.00187.04 C ANISOU 4061 CB PRO B 297 30798 27754 12515 919 2193 -6296 C ATOM 4062 CG PRO B 297 -24.197 16.102 7.434 1.00184.33 C ANISOU 4062 CG PRO B 297 30485 26960 12593 936 1578 -6543 C ATOM 4063 CD PRO B 297 -23.480 16.772 8.586 1.00190.65 C ANISOU 4063 CD PRO B 297 31611 27869 12957 790 1262 -6928 C ATOM 4064 N GLY B 298 -24.358 12.482 8.935 1.00239.95 N ANISOU 4064 N GLY B 298 37832 35072 18265 489 1787 -5063 N ATOM 4065 CA GLY B 298 -23.589 11.282 8.667 1.00236.51 C ANISOU 4065 CA GLY B 298 37444 34645 17774 335 1351 -4417 C ATOM 4066 C GLY B 298 -23.216 11.246 7.197 1.00229.02 C ANISOU 4066 C GLY B 298 36220 33291 17506 409 1082 -4246 C ATOM 4067 O GLY B 298 -23.513 10.284 6.489 1.00226.72 O ANISOU 4067 O GLY B 298 35773 32962 17407 384 1208 -3772 O ATOM 4068 N ARG B 299 -22.560 12.308 6.742 1.00219.67 N ANISOU 4068 N ARG B 299 34977 31798 16689 498 702 -4636 N ATOM 4069 CA ARG B 299 -22.179 12.446 5.342 1.00216.42 C ANISOU 4069 CA ARG B 299 34161 31010 17059 585 417 -4502 C ATOM 4070 C ARG B 299 -20.966 11.587 5.001 1.00213.30 C ANISOU 4070 C ARG B 299 33731 30586 16730 464 -233 -4018 C ATOM 4071 O ARG B 299 -20.927 10.946 3.952 1.00210.80 O ANISOU 4071 O ARG B 299 32997 30125 16974 473 -291 -3605 O ATOM 4072 CB ARG B 299 -21.897 13.916 5.015 1.00208.71 C ANISOU 4072 CB ARG B 299 33077 29705 16519 691 233 -5064 C ATOM 4073 CG ARG B 299 -21.396 14.160 3.603 1.00205.78 C ANISOU 4073 CG ARG B 299 32186 28952 17047 718 -101 -4896 C ATOM 4074 CD ARG B 299 -21.085 15.630 3.365 1.00206.93 C ANISOU 4074 CD ARG B 299 32304 28746 17572 781 -298 -5434 C ATOM 4075 NE ARG B 299 -20.514 15.862 2.040 1.00203.97 N ANISOU 4075 NE ARG B 299 31479 28023 17999 760 -637 -5244 N ATOM 4076 CZ ARG B 299 -21.232 16.096 0.946 1.00203.52 C ANISOU 4076 CZ ARG B 299 30991 27720 18616 892 -362 -5161 C ATOM 4077 NH1 ARG B 299 -22.556 16.131 1.012 1.00205.50 N ANISOU 4077 NH1 ARG B 299 31157 28038 18887 1073 241 -5264 N ATOM 4078 NH2 ARG B 299 -20.625 16.297 -0.217 1.00201.13 N ANISOU 4078 NH2 ARG B 299 30336 27125 18959 840 -693 -4977 N ATOM 4079 N VAL B 300 -19.995 11.551 5.907 1.00227.08 N ANISOU 4079 N VAL B 300 35815 32485 17981 344 -709 -4054 N ATOM 4080 CA VAL B 300 -18.757 10.813 5.678 1.00224.22 C ANISOU 4080 CA VAL B 300 35374 32110 17711 258 -1368 -3643 C ATOM 4081 C VAL B 300 -18.995 9.313 5.531 1.00222.25 C ANISOU 4081 C VAL B 300 35117 31987 17339 234 -1263 -3003 C ATOM 4082 O VAL B 300 -18.208 8.612 4.894 1.00218.89 O ANISOU 4082 O VAL B 300 34515 31458 17195 241 -1699 -2628 O ATOM 4083 CB VAL B 300 -17.726 11.066 6.797 1.00204.70 C ANISOU 4083 CB VAL B 300 33102 29823 14853 120 -1856 -3778 C ATOM 4084 CG1 VAL B 300 -17.254 12.511 6.768 1.00206.06 C ANISOU 4084 CG1 VAL B 300 33236 29795 15265 99 -2083 -4366 C ATOM 4085 CG2 VAL B 300 -18.315 10.715 8.155 1.00211.36 C ANISOU 4085 CG2 VAL B 300 34293 31038 14975 53 -1515 -3765 C ATOM 4086 N GLN B 301 -20.081 8.821 6.116 1.00202.79 N ANISOU 4086 N GLN B 301 32821 29742 14488 199 -677 -2885 N ATOM 4087 CA GLN B 301 -20.428 7.415 5.980 1.00201.58 C ANISOU 4087 CA GLN B 301 32673 29672 14247 141 -521 -2281 C ATOM 4088 C GLN B 301 -20.985 7.157 4.587 1.00198.69 C ANISOU 4088 C GLN B 301 31890 29055 14547 219 -275 -2100 C ATOM 4089 O GLN B 301 -20.691 6.135 3.975 1.00196.84 O ANISOU 4089 O GLN B 301 31488 28722 14579 200 -467 -1616 O ATOM 4090 CB GLN B 301 -21.453 7.005 7.041 1.00237.75 C ANISOU 4090 CB GLN B 301 37490 34577 18268 42 58 -2211 C ATOM 4091 CG GLN B 301 -20.922 7.021 8.468 1.00244.66 C ANISOU 4091 CG GLN B 301 38700 35742 18516 -37 -186 -2270 C ATOM 4092 CD GLN B 301 -21.960 6.574 9.482 1.00250.64 C ANISOU 4092 CD GLN B 301 39682 36836 18714 -122 399 -2174 C ATOM 4093 OE1 GLN B 301 -22.638 5.565 9.287 1.00249.48 O ANISOU 4093 OE1 GLN B 301 39501 36721 18569 -193 736 -1731 O ATOM 4094 NE2 GLN B 301 -22.085 7.321 10.575 1.00257.22 N ANISOU 4094 NE2 GLN B 301 40740 37922 19070 -122 520 -2590 N ATOM 4095 N ALA B 302 -21.757 8.112 4.079 1.00146.22 N ANISOU 4095 N ALA B 302 24920 22293 8343 310 126 -2484 N ATOM 4096 CA ALA B 302 -22.326 8.015 2.740 1.00143.49 C ANISOU 4096 CA ALA B 302 23989 21717 8812 379 351 -2337 C ATOM 4097 C ALA B 302 -21.249 8.073 1.664 1.00140.54 C ANISOU 4097 C ALA B 302 23268 21064 9066 422 -224 -2210 C ATOM 4098 O ALA B 302 -21.332 7.377 0.650 1.00138.88 O ANISOU 4098 O ALA B 302 22701 20716 9352 427 -226 -1854 O ATOM 4099 CB ALA B 302 -23.357 9.111 2.522 1.00127.89 C ANISOU 4099 CB ALA B 302 21777 19680 7136 499 854 -2801 C ATOM 4100 N LEU B 303 -20.245 8.912 1.896 1.00173.01 N ANISOU 4100 N LEU B 303 27488 25107 13142 435 -697 -2522 N ATOM 4101 CA LEU B 303 -19.108 9.041 0.993 1.00170.23 C ANISOU 4101 CA LEU B 303 26819 24536 13325 442 -1252 -2441 C ATOM 4102 C LEU B 303 -18.288 7.757 0.930 1.00167.56 C ANISOU 4102 C LEU B 303 26514 24266 12884 407 -1653 -1940 C ATOM 4103 O LEU B 303 -17.846 7.345 -0.142 1.00164.77 O ANISOU 4103 O LEU B 303 25771 23746 13088 436 -1851 -1691 O ATOM 4104 CB LEU B 303 -18.216 10.215 1.417 1.00150.14 C ANISOU 4104 CB LEU B 303 24417 21932 10696 414 -1667 -2903 C ATOM 4105 CG LEU B 303 -18.569 11.590 0.842 1.00152.00 C ANISOU 4105 CG LEU B 303 24423 21901 11430 468 -1501 -3352 C ATOM 4106 CD1 LEU B 303 -18.396 11.535 -0.660 1.00143.47 C ANISOU 4106 CD1 LEU B 303 22800 20557 11155 490 -1580 -3125 C ATOM 4107 CD2 LEU B 303 -19.981 12.025 1.183 1.00155.78 C ANISOU 4107 CD2 LEU B 303 24992 22418 11779 569 -843 -3610 C ATOM 4108 N ARG B 304 -18.089 7.129 2.084 1.00183.07 N ANISOU 4108 N ARG B 304 28964 26471 14125 356 -1773 -1796 N ATOM 4109 CA ARG B 304 -17.325 5.889 2.163 1.00181.45 C ANISOU 4109 CA ARG B 304 28861 26314 13769 356 -2183 -1315 C ATOM 4110 C ARG B 304 -18.003 4.816 1.333 1.00178.93 C ANISOU 4110 C ARG B 304 28298 25883 13805 369 -1862 -871 C ATOM 4111 O ARG B 304 -17.356 3.985 0.704 1.00176.31 O ANISOU 4111 O ARG B 304 27777 25434 13777 421 -2186 -530 O ATOM 4112 CB ARG B 304 -17.194 5.413 3.607 1.00195.44 C ANISOU 4112 CB ARG B 304 31227 28356 14673 289 -2295 -1211 C ATOM 4113 CG ARG B 304 -15.915 4.660 3.865 1.00195.30 C ANISOU 4113 CG ARG B 304 31147 28370 14687 305 -2927 -894 C ATOM 4114 CD ARG B 304 -15.850 4.223 5.308 1.00201.91 C ANISOU 4114 CD ARG B 304 32353 29473 14889 220 -2956 -761 C ATOM 4115 NE ARG B 304 -14.739 3.310 5.538 1.00204.11 N ANISOU 4115 NE ARG B 304 32582 29765 15204 277 -3516 -388 N ATOM 4116 CZ ARG B 304 -14.807 1.997 5.350 1.00204.16 C ANISOU 4116 CZ ARG B 304 32614 29688 15270 327 -3522 131 C ATOM 4117 NH1 ARG B 304 -15.938 1.443 4.929 1.00202.34 N ANISOU 4117 NH1 ARG B 304 32454 29367 15060 286 -2997 351 N ATOM 4118 NH2 ARG B 304 -13.747 1.238 5.585 1.00206.57 N ANISOU 4118 NH2 ARG B 304 32865 29988 15635 418 -4048 422 N ATOM 4119 N ARG B 305 -19.327 4.820 1.368 1.00174.08 N ANISOU 4119 N ARG B 305 27691 25313 13138 320 -1219 -895 N ATOM 4120 CA ARG B 305 -20.100 3.878 0.587 1.00172.17 C ANISOU 4120 CA ARG B 305 27206 24969 13241 295 -877 -519 C ATOM 4121 C ARG B 305 -19.849 4.186 -0.858 1.00169.22 C ANISOU 4121 C ARG B 305 26262 24340 13695 379 -997 -559 C ATOM 4122 O ARG B 305 -19.550 3.298 -1.656 1.00166.65 O ANISOU 4122 O ARG B 305 25726 23873 13720 401 -1159 -214 O ATOM 4123 CB ARG B 305 -21.574 4.067 0.862 1.00180.78 C ANISOU 4123 CB ARG B 305 28318 26182 14187 221 -160 -636 C ATOM 4124 CG ARG B 305 -21.931 3.943 2.309 1.00190.39 C ANISOU 4124 CG ARG B 305 30101 27692 14547 116 63 -670 C ATOM 4125 CD ARG B 305 -23.249 4.638 2.561 1.00191.67 C ANISOU 4125 CD ARG B 305 30186 27996 14645 96 756 -1007 C ATOM 4126 NE ARG B 305 -24.335 3.762 2.992 1.00190.67 N ANISOU 4126 NE ARG B 305 30206 28054 14187 -70 1317 -721 N ATOM 4127 CZ ARG B 305 -24.782 3.696 4.241 1.00195.02 C ANISOU 4127 CZ ARG B 305 31232 28908 13959 -191 1644 -778 C ATOM 4128 NH1 ARG B 305 -24.213 4.434 5.184 1.00195.16 N ANISOU 4128 NH1 ARG B 305 31624 29070 13458 -145 1425 -1119 N ATOM 4129 NH2 ARG B 305 -25.790 2.891 4.553 1.00199.06 N ANISOU 4129 NH2 ARG B 305 31832 29586 14216 -382 2189 -499 N ATOM 4130 N GLY B 306 -19.862 5.479 -1.162 1.00123.73 N ANISOU 4130 N GLY B 306 20289 18506 8218 428 -966 -994 N ATOM 4131 CA GLY B 306 -19.729 5.935 -2.528 1.00121.77 C ANISOU 4131 CA GLY B 306 19529 18017 8721 487 -1029 -1056 C ATOM 4132 C GLY B 306 -18.402 5.590 -3.134 1.00118.93 C ANISOU 4132 C GLY B 306 18990 17552 8645 513 -1593 -889 C ATOM 4133 O GLY B 306 -18.324 5.212 -4.297 1.00116.35 O ANISOU 4133 O GLY B 306 18293 17068 8846 540 -1616 -701 O ATOM 4134 N VAL B 307 -17.359 5.670 -2.323 1.00141.83 N ANISOU 4134 N VAL B 307 22151 20564 11172 507 -2049 -959 N ATOM 4135 CA VAL B 307 -16.019 5.369 -2.802 1.00139.02 C ANISOU 4135 CA VAL B 307 21591 20153 11078 545 -2609 -835 C ATOM 4136 C VAL B 307 -15.781 3.875 -3.049 1.00136.48 C ANISOU 4136 C VAL B 307 21270 19817 10771 609 -2739 -352 C ATOM 4137 O VAL B 307 -15.310 3.487 -4.117 1.00133.37 O ANISOU 4137 O VAL B 307 20501 19285 10888 666 -2885 -202 O ATOM 4138 CB VAL B 307 -14.956 5.906 -1.829 1.00153.84 C ANISOU 4138 CB VAL B 307 23718 22172 12563 519 -3106 -1069 C ATOM 4139 CG1 VAL B 307 -13.568 5.511 -2.299 1.00150.91 C ANISOU 4139 CG1 VAL B 307 23076 21783 12479 570 -3684 -929 C ATOM 4140 CG2 VAL B 307 -15.058 7.412 -1.730 1.00155.74 C ANISOU 4140 CG2 VAL B 307 23932 22357 12885 449 -3033 -1570 C ATOM 4141 N LEU B 308 -16.136 3.042 -2.072 1.00148.17 N ANISOU 4141 N LEU B 308 23192 21423 11683 595 -2666 -111 N ATOM 4142 CA LEU B 308 -15.910 1.594 -2.174 1.00146.40 C ANISOU 4142 CA LEU B 308 23060 21140 11427 658 -2819 361 C ATOM 4143 C LEU B 308 -16.790 0.893 -3.209 1.00144.76 C ANISOU 4143 C LEU B 308 22597 20753 11653 640 -2415 603 C ATOM 4144 O LEU B 308 -16.318 -0.014 -3.897 1.00142.06 O ANISOU 4144 O LEU B 308 22090 20264 11621 728 -2622 875 O ATOM 4145 CB LEU B 308 -16.054 0.899 -0.812 1.00163.20 C ANISOU 4145 CB LEU B 308 25792 23428 12789 619 -2865 589 C ATOM 4146 CG LEU B 308 -14.871 0.942 0.169 1.00165.44 C ANISOU 4146 CG LEU B 308 26380 23864 12615 685 -3484 560 C ATOM 4147 CD1 LEU B 308 -13.641 0.269 -0.442 1.00162.48 C ANISOU 4147 CD1 LEU B 308 25694 23372 12671 853 -4032 764 C ATOM 4148 CD2 LEU B 308 -14.531 2.345 0.654 1.00163.53 C ANISOU 4148 CD2 LEU B 308 26148 23769 12216 630 -3610 55 C ATOM 4149 N VAL B 309 -18.050 1.305 -3.332 1.00148.24 N ANISOU 4149 N VAL B 309 22989 21205 12131 537 -1856 484 N ATOM 4150 CA VAL B 309 -18.899 0.750 -4.382 1.00146.62 C ANISOU 4150 CA VAL B 309 22490 20842 12378 503 -1501 669 C ATOM 4151 C VAL B 309 -18.259 1.065 -5.720 1.00143.44 C ANISOU 4151 C VAL B 309 21596 20272 12632 591 -1721 578 C ATOM 4152 O VAL B 309 -18.116 0.190 -6.571 1.00140.64 O ANISOU 4152 O VAL B 309 21058 19767 12612 630 -1786 826 O ATOM 4153 CB VAL B 309 -20.311 1.359 -4.410 1.00 94.33 C ANISOU 4153 CB VAL B 309 15776 14279 5786 403 -903 483 C ATOM 4154 CG1 VAL B 309 -21.148 0.685 -5.466 1.00 90.85 C ANISOU 4154 CG1 VAL B 309 15033 13692 5793 352 -601 697 C ATOM 4155 CG2 VAL B 309 -20.982 1.219 -3.101 1.00 99.62 C ANISOU 4155 CG2 VAL B 309 16893 15158 5799 298 -609 504 C ATOM 4156 N LEU B 310 -17.894 2.331 -5.905 1.00123.04 N ANISOU 4156 N LEU B 310 18821 17707 10221 608 -1818 214 N ATOM 4157 CA LEU B 310 -17.328 2.793 -7.168 1.00120.45 C ANISOU 4157 CA LEU B 310 18041 17237 10487 648 -1979 110 C ATOM 4158 C LEU B 310 -16.011 2.068 -7.442 1.00118.16 C ANISOU 4158 C LEU B 310 17657 16922 10316 743 -2466 285 C ATOM 4159 O LEU B 310 -15.717 1.707 -8.581 1.00115.77 O ANISOU 4159 O LEU B 310 17020 16497 10469 785 -2515 384 O ATOM 4160 CB LEU B 310 -17.098 4.309 -7.139 1.00111.00 C ANISOU 4160 CB LEU B 310 16740 16046 9391 617 -2031 -302 C ATOM 4161 CG LEU B 310 -17.054 4.959 -8.523 1.00108.82 C ANISOU 4161 CG LEU B 310 16022 15599 9727 605 -1989 -405 C ATOM 4162 CD1 LEU B 310 -18.421 4.812 -9.174 1.00109.12 C ANISOU 4162 CD1 LEU B 310 15927 15551 9984 596 -1519 -322 C ATOM 4163 CD2 LEU B 310 -16.600 6.414 -8.502 1.00110.92 C ANISOU 4163 CD2 LEU B 310 16216 15817 10110 554 -2129 -778 C ATOM 4164 N ARG B 311 -15.223 1.878 -6.386 1.00138.91 N ANISOU 4164 N ARG B 311 20576 19682 12523 786 -2828 305 N ATOM 4165 CA ARG B 311 -13.950 1.165 -6.464 1.00136.81 C ANISOU 4165 CA ARG B 311 20230 19419 12331 917 -3331 463 C ATOM 4166 C ARG B 311 -14.157 -0.252 -6.985 1.00135.18 C ANISOU 4166 C ARG B 311 20023 19064 12273 1008 -3272 843 C ATOM 4167 O ARG B 311 -13.406 -0.735 -7.836 1.00132.80 O ANISOU 4167 O ARG B 311 19419 18674 12364 1126 -3493 921 O ATOM 4168 CB ARG B 311 -13.286 1.115 -5.084 1.00184.19 C ANISOU 4168 CB ARG B 311 26623 25596 17766 952 -3719 458 C ATOM 4169 CG ARG B 311 -11.912 0.461 -5.054 1.00183.36 C ANISOU 4169 CG ARG B 311 26413 25520 17734 1121 -4305 593 C ATOM 4170 CD ARG B 311 -11.460 0.171 -3.623 1.00185.66 C ANISOU 4170 CD ARG B 311 27178 25975 17388 1168 -4684 681 C ATOM 4171 NE ARG B 311 -11.489 1.358 -2.771 1.00188.28 N ANISOU 4171 NE ARG B 311 27702 26483 17354 1028 -4710 331 N ATOM 4172 CZ ARG B 311 -10.451 2.162 -2.557 1.00188.79 C ANISOU 4172 CZ ARG B 311 27602 26670 17457 1012 -5145 45 C ATOM 4173 NH1 ARG B 311 -9.282 1.918 -3.134 1.00186.79 N ANISOU 4173 NH1 ARG B 311 26889 26414 17669 1103 -5506 78 N ATOM 4174 NH2 ARG B 311 -10.585 3.216 -1.763 1.00191.71 N ANISOU 4174 NH2 ARG B 311 28190 27163 17486 866 -5126 -287 N ATOM 4175 N ALA B 312 -15.172 -0.919 -6.447 1.00139.30 N ANISOU 4175 N ALA B 312 20896 19560 12472 943 -2964 1066 N ATOM 4176 CA ALA B 312 -15.497 -2.281 -6.847 1.00137.98 C ANISOU 4176 CA ALA B 312 20802 19213 12413 986 -2882 1433 C ATOM 4177 C ALA B 312 -16.018 -2.335 -8.277 1.00135.62 C ANISOU 4177 C ALA B 312 20092 18754 12683 952 -2595 1409 C ATOM 4178 O ALA B 312 -15.696 -3.255 -9.026 1.00133.43 O ANISOU 4178 O ALA B 312 19686 18309 12702 1051 -2708 1591 O ATOM 4179 CB ALA B 312 -16.510 -2.891 -5.885 1.00123.13 C ANISOU 4179 CB ALA B 312 19402 17354 10029 856 -2584 1672 C ATOM 4180 N VAL B 313 -16.811 -1.336 -8.656 1.00107.89 N ANISOU 4180 N VAL B 313 16387 15288 9319 829 -2244 1171 N ATOM 4181 CA VAL B 313 -17.384 -1.282 -9.998 1.00106.15 C ANISOU 4181 CA VAL B 313 15795 14936 9600 786 -1985 1142 C ATOM 4182 C VAL B 313 -16.304 -1.135 -11.065 1.00103.08 C ANISOU 4182 C VAL B 313 15027 14487 9650 894 -2277 1049 C ATOM 4183 O VAL B 313 -16.346 -1.809 -12.093 1.00100.93 O ANISOU 4183 O VAL B 313 14559 14076 9714 926 -2232 1166 O ATOM 4184 CB VAL B 313 -18.408 -0.133 -10.134 1.00 89.81 C ANISOU 4184 CB VAL B 313 13597 12928 7600 668 -1604 894 C ATOM 4185 CG1 VAL B 313 -18.866 0.011 -11.575 1.00 88.06 C ANISOU 4185 CG1 VAL B 313 12982 12578 7898 641 -1426 863 C ATOM 4186 CG2 VAL B 313 -19.598 -0.376 -9.222 1.00 92.73 C ANISOU 4186 CG2 VAL B 313 14266 13379 7588 555 -1228 981 C ATOM 4187 N VAL B 314 -15.333 -0.264 -10.812 1.00119.54 N ANISOU 4187 N VAL B 314 17012 16687 11720 931 -2566 827 N ATOM 4188 CA VAL B 314 -14.221 -0.070 -11.737 1.00116.96 C ANISOU 4188 CA VAL B 314 16306 16351 11785 1004 -2831 727 C ATOM 4189 C VAL B 314 -13.432 -1.368 -11.868 1.00115.53 C ANISOU 4189 C VAL B 314 16124 16107 11663 1186 -3112 952 C ATOM 4190 O VAL B 314 -13.110 -1.804 -12.973 1.00112.87 O ANISOU 4190 O VAL B 314 15499 15681 11704 1252 -3114 981 O ATOM 4191 CB VAL B 314 -13.288 1.074 -11.294 1.00116.21 C ANISOU 4191 CB VAL B 314 16117 16400 11636 972 -3115 452 C ATOM 4192 CG1 VAL B 314 -12.052 1.131 -12.180 1.00113.71 C ANISOU 4192 CG1 VAL B 314 15388 16110 11708 1028 -3389 377 C ATOM 4193 CG2 VAL B 314 -14.027 2.400 -11.329 1.00118.08 C ANISOU 4193 CG2 VAL B 314 16338 16632 11896 815 -2845 204 C ATOM 4194 N ILE B 315 -13.129 -1.983 -10.728 1.00123.53 N ANISOU 4194 N ILE B 315 17484 17161 12290 1279 -3354 1106 N ATOM 4195 CA ILE B 315 -12.401 -3.245 -10.712 1.00123.16 C ANISOU 4195 CA ILE B 315 17497 17019 12280 1493 -3662 1338 C ATOM 4196 C ILE B 315 -13.192 -4.356 -11.399 1.00122.20 C ANISOU 4196 C ILE B 315 17446 16657 12328 1500 -3396 1575 C ATOM 4197 O ILE B 315 -12.639 -5.133 -12.176 1.00120.67 O ANISOU 4197 O ILE B 315 17068 16333 12447 1662 -3529 1641 O ATOM 4198 CB ILE B 315 -12.042 -3.678 -9.272 1.00103.18 C ANISOU 4198 CB ILE B 315 15404 14558 9241 1582 -3986 1499 C ATOM 4199 CG1 ILE B 315 -11.033 -2.708 -8.654 1.00104.43 C ANISOU 4199 CG1 ILE B 315 15456 14952 9269 1599 -4360 1250 C ATOM 4200 CG2 ILE B 315 -11.482 -5.090 -9.255 1.00102.95 C ANISOU 4200 CG2 ILE B 315 15502 14358 9257 1824 -4282 1791 C ATOM 4201 CD1 ILE B 315 -10.706 -3.011 -7.206 1.00107.15 C ANISOU 4201 CD1 ILE B 315 16256 15401 9056 1668 -4705 1384 C ATOM 4202 N ALA B 316 -14.494 -4.409 -11.135 1.00113.32 N ANISOU 4202 N ALA B 316 16566 15480 11010 1316 -3009 1676 N ATOM 4203 CA ALA B 316 -15.344 -5.433 -11.731 1.00112.60 C ANISOU 4203 CA ALA B 316 16552 15164 11068 1264 -2748 1894 C ATOM 4204 C ALA B 316 -15.507 -5.221 -13.233 1.00110.29 C ANISOU 4204 C ALA B 316 15832 14801 11270 1234 -2569 1746 C ATOM 4205 O ALA B 316 -15.613 -6.181 -13.993 1.00109.07 O ANISOU 4205 O ALA B 316 15642 14447 11352 1283 -2535 1870 O ATOM 4206 CB ALA B 316 -16.702 -5.466 -11.047 1.00 78.17 C ANISOU 4206 CB ALA B 316 12502 10813 6385 1040 -2362 2018 C ATOM 4207 N PHE B 317 -15.520 -3.961 -13.655 1.00 96.77 N ANISOU 4207 N PHE B 317 13830 13239 9698 1149 -2466 1481 N ATOM 4208 CA PHE B 317 -15.644 -3.631 -15.070 1.00 94.48 C ANISOU 4208 CA PHE B 317 13162 12906 9829 1104 -2314 1348 C ATOM 4209 C PHE B 317 -14.396 -4.047 -15.843 1.00 92.49 C ANISOU 4209 C PHE B 317 12651 12630 9862 1285 -2590 1299 C ATOM 4210 O PHE B 317 -14.490 -4.659 -16.908 1.00 90.91 O ANISOU 4210 O PHE B 317 12303 12302 9935 1313 -2499 1327 O ATOM 4211 CB PHE B 317 -15.893 -2.131 -15.247 1.00 88.88 C ANISOU 4211 CB PHE B 317 12257 12334 9179 974 -2176 1099 C ATOM 4212 CG PHE B 317 -16.201 -1.728 -16.663 1.00 87.38 C ANISOU 4212 CG PHE B 317 11740 12094 9365 898 -2000 1002 C ATOM 4213 CD1 PHE B 317 -17.502 -1.755 -17.138 1.00 88.09 C ANISOU 4213 CD1 PHE B 317 11826 12109 9536 774 -1678 1052 C ATOM 4214 CD2 PHE B 317 -15.190 -1.318 -17.517 1.00 85.39 C ANISOU 4214 CD2 PHE B 317 11180 11891 9374 938 -2159 866 C ATOM 4215 CE1 PHE B 317 -17.788 -1.384 -18.439 1.00 85.68 C ANISOU 4215 CE1 PHE B 317 11249 11763 9543 708 -1558 978 C ATOM 4216 CE2 PHE B 317 -15.470 -0.945 -18.818 1.00 83.48 C ANISOU 4216 CE2 PHE B 317 10684 11611 9422 851 -1997 799 C ATOM 4217 CZ PHE B 317 -16.770 -0.978 -19.279 1.00 83.35 C ANISOU 4217 CZ PHE B 317 10701 11506 9461 744 -1716 860 C ATOM 4218 N VAL B 318 -13.230 -3.713 -15.300 1.00103.28 N ANISOU 4218 N VAL B 318 13948 14134 11158 1407 -2924 1206 N ATOM 4219 CA VAL B 318 -11.960 -4.030 -15.945 1.00101.82 C ANISOU 4219 CA VAL B 318 13455 13982 11251 1593 -3187 1127 C ATOM 4220 C VAL B 318 -11.755 -5.535 -16.077 1.00101.83 C ANISOU 4220 C VAL B 318 13591 13780 11321 1811 -3307 1325 C ATOM 4221 O VAL B 318 -11.453 -6.034 -17.161 1.00100.64 O ANISOU 4221 O VAL B 318 13208 13547 11484 1903 -3264 1275 O ATOM 4222 CB VAL B 318 -10.769 -3.414 -15.183 1.00104.20 C ANISOU 4222 CB VAL B 318 13648 14492 11453 1673 -3560 994 C ATOM 4223 CG1 VAL B 318 -9.452 -3.963 -15.715 1.00103.45 C ANISOU 4223 CG1 VAL B 318 13221 14443 11643 1907 -3846 936 C ATOM 4224 CG2 VAL B 318 -10.801 -1.897 -15.288 1.00104.13 C ANISOU 4224 CG2 VAL B 318 13455 14639 11472 1451 -3459 755 C ATOM 4225 N VAL B 319 -11.929 -6.253 -14.972 1.00108.55 N ANISOU 4225 N VAL B 319 14848 14535 11861 1889 -3455 1549 N ATOM 4226 CA VAL B 319 -11.718 -7.697 -14.944 1.00109.59 C ANISOU 4226 CA VAL B 319 15186 14417 12036 2108 -3617 1769 C ATOM 4227 C VAL B 319 -12.662 -8.433 -15.898 1.00109.39 C ANISOU 4227 C VAL B 319 15210 14144 12211 2012 -3294 1850 C ATOM 4228 O VAL B 319 -12.254 -9.369 -16.585 1.00109.31 O ANISOU 4228 O VAL B 319 15135 13941 12454 2200 -3380 1868 O ATOM 4229 CB VAL B 319 -11.861 -8.264 -13.512 1.00 97.45 C ANISOU 4229 CB VAL B 319 14155 12806 10065 2156 -3818 2042 C ATOM 4230 CG1 VAL B 319 -11.769 -9.782 -13.518 1.00 98.29 C ANISOU 4230 CG1 VAL B 319 14535 12578 10230 2361 -3971 2305 C ATOM 4231 CG2 VAL B 319 -10.798 -7.673 -12.598 1.00 98.57 C ANISOU 4231 CG2 VAL B 319 14253 13190 10011 2285 -4224 1955 C ATOM 4232 N CYS B 320 -13.917 -7.998 -15.945 1.00113.66 N ANISOU 4232 N CYS B 320 15848 14691 12647 1727 -2932 1874 N ATOM 4233 CA CYS B 320 -14.918 -8.650 -16.786 1.00113.51 C ANISOU 4233 CA CYS B 320 15873 14459 12798 1590 -2639 1948 C ATOM 4234 C CYS B 320 -14.732 -8.377 -18.278 1.00112.00 C ANISOU 4234 C CYS B 320 15277 14294 12984 1590 -2525 1725 C ATOM 4235 O CYS B 320 -14.923 -9.269 -19.105 1.00111.99 O ANISOU 4235 O CYS B 320 15283 14081 13187 1624 -2462 1751 O ATOM 4236 CB CYS B 320 -16.329 -8.241 -16.359 1.00108.17 C ANISOU 4236 CB CYS B 320 15366 13821 11912 1290 -2293 2030 C ATOM 4237 SG CYS B 320 -16.868 -8.949 -14.789 1.00111.40 S ANISOU 4237 SG CYS B 320 16335 14137 11856 1216 -2302 2358 S ATOM 4238 N TRP B 321 -14.359 -7.148 -18.622 1.00 92.36 N ANISOU 4238 N TRP B 321 12467 12056 10571 1537 -2500 1505 N ATOM 4239 CA TRP B 321 -14.292 -6.746 -20.025 1.00 90.64 C ANISOU 4239 CA TRP B 321 11901 11891 10649 1481 -2353 1317 C ATOM 4240 C TRP B 321 -12.921 -6.944 -20.665 1.00 90.16 C ANISOU 4240 C TRP B 321 11548 11896 10813 1704 -2556 1163 C ATOM 4241 O TRP B 321 -12.785 -6.850 -21.884 1.00 89.21 O ANISOU 4241 O TRP B 321 11177 11805 10915 1676 -2428 1022 O ATOM 4242 CB TRP B 321 -14.755 -5.296 -20.199 1.00 97.23 C ANISOU 4242 CB TRP B 321 12560 12917 11466 1267 -2177 1183 C ATOM 4243 CG TRP B 321 -16.229 -5.129 -20.023 1.00 98.22 C ANISOU 4243 CG TRP B 321 12853 12981 11484 1058 -1904 1277 C ATOM 4244 CD1 TRP B 321 -16.881 -4.696 -18.905 1.00100.01 C ANISOU 4244 CD1 TRP B 321 13286 13264 11449 966 -1825 1342 C ATOM 4245 CD2 TRP B 321 -17.242 -5.417 -20.989 1.00 97.65 C ANISOU 4245 CD2 TRP B 321 12733 12802 11565 918 -1672 1300 C ATOM 4246 NE1 TRP B 321 -18.237 -4.685 -19.121 1.00100.89 N ANISOU 4246 NE1 TRP B 321 13441 13322 11571 786 -1537 1399 N ATOM 4247 CE2 TRP B 321 -18.486 -5.127 -20.401 1.00 99.60 C ANISOU 4247 CE2 TRP B 321 13118 13056 11670 748 -1461 1382 C ATOM 4248 CE3 TRP B 321 -17.219 -5.890 -22.307 1.00 96.63 C ANISOU 4248 CE3 TRP B 321 12453 12590 11672 916 -1625 1243 C ATOM 4249 CZ2 TRP B 321 -19.693 -5.291 -21.071 1.00100.19 C ANISOU 4249 CZ2 TRP B 321 13145 13062 11860 580 -1232 1416 C ATOM 4250 CZ3 TRP B 321 -18.416 -6.054 -22.975 1.00 97.22 C ANISOU 4250 CZ3 TRP B 321 12528 12584 11827 738 -1417 1279 C ATOM 4251 CH2 TRP B 321 -19.636 -5.758 -22.357 1.00 98.83 C ANISOU 4251 CH2 TRP B 321 12834 12801 11918 572 -1236 1370 C ATOM 4252 N LEU B 322 -11.910 -7.222 -19.850 1.00 98.18 N ANISOU 4252 N LEU B 322 12587 12954 11762 1928 -2870 1187 N ATOM 4253 CA LEU B 322 -10.562 -7.439 -20.373 1.00 98.08 C ANISOU 4253 CA LEU B 322 12243 13036 11987 2170 -3070 1027 C ATOM 4254 C LEU B 322 -10.443 -8.660 -21.303 1.00 98.83 C ANISOU 4254 C LEU B 322 12326 12911 12314 2356 -3028 1011 C ATOM 4255 O LEU B 322 -9.919 -8.529 -22.409 1.00 98.52 O ANISOU 4255 O LEU B 322 11952 12976 12505 2389 -2928 807 O ATOM 4256 CB LEU B 322 -9.517 -7.483 -19.250 1.00113.11 C ANISOU 4256 CB LEU B 322 14151 15044 13782 2389 -3465 1055 C ATOM 4257 CG LEU B 322 -8.064 -7.624 -19.705 1.00113.77 C ANISOU 4257 CG LEU B 322 13808 15280 14140 2650 -3690 865 C ATOM 4258 CD1 LEU B 322 -7.695 -6.496 -20.657 1.00112.55 C ANISOU 4258 CD1 LEU B 322 13208 15391 14165 2450 -3498 619 C ATOM 4259 CD2 LEU B 322 -7.128 -7.646 -18.509 1.00115.14 C ANISOU 4259 CD2 LEU B 322 13991 15566 14190 2858 -4128 908 C ATOM 4260 N PRO B 323 -10.918 -9.846 -20.867 1.00116.62 N ANISOU 4260 N PRO B 323 14964 14851 14497 2464 -3094 1218 N ATOM 4261 CA PRO B 323 -10.827 -10.996 -21.777 1.00118.18 C ANISOU 4261 CA PRO B 323 15180 14796 14928 2637 -3056 1169 C ATOM 4262 C PRO B 323 -11.673 -10.805 -23.033 1.00117.94 C ANISOU 4262 C PRO B 323 15060 14750 15001 2387 -2707 1055 C ATOM 4263 O PRO B 323 -11.349 -11.351 -24.087 1.00119.10 O ANISOU 4263 O PRO B 323 15069 14824 15360 2504 -2641 889 O ATOM 4264 CB PRO B 323 -11.396 -12.150 -20.943 1.00110.24 C ANISOU 4264 CB PRO B 323 14680 13423 13784 2703 -3173 1458 C ATOM 4265 CG PRO B 323 -11.252 -11.714 -19.531 1.00109.93 C ANISOU 4265 CG PRO B 323 14816 13503 13450 2700 -3382 1633 C ATOM 4266 CD PRO B 323 -11.478 -10.239 -19.561 1.00107.74 C ANISOU 4266 CD PRO B 323 14286 13573 13075 2437 -3209 1496 C ATOM 4267 N TYR B 324 -12.750 -10.037 -22.903 1.00 95.07 N ANISOU 4267 N TYR B 324 12246 11929 11947 2062 -2499 1132 N ATOM 4268 CA TYR B 324 -13.645 -9.736 -24.015 1.00 94.48 C ANISOU 4268 CA TYR B 324 12087 11863 11946 1811 -2210 1049 C ATOM 4269 C TYR B 324 -12.924 -8.999 -25.142 1.00 93.59 C ANISOU 4269 C TYR B 324 11573 11998 11988 1810 -2129 798 C ATOM 4270 O TYR B 324 -13.028 -9.376 -26.308 1.00 94.78 O ANISOU 4270 O TYR B 324 11648 12098 12266 1791 -1996 672 O ATOM 4271 CB TYR B 324 -14.828 -8.907 -23.508 1.00111.49 C ANISOU 4271 CB TYR B 324 14351 14091 13918 1513 -2043 1170 C ATOM 4272 CG TYR B 324 -15.765 -8.398 -24.581 1.00110.97 C ANISOU 4272 CG TYR B 324 14161 14074 13927 1263 -1793 1093 C ATOM 4273 CD1 TYR B 324 -16.740 -9.222 -25.127 1.00112.46 C ANISOU 4273 CD1 TYR B 324 14510 14049 14171 1140 -1669 1153 C ATOM 4274 CD2 TYR B 324 -15.691 -7.085 -25.029 1.00109.23 C ANISOU 4274 CD2 TYR B 324 13681 14099 13722 1140 -1708 972 C ATOM 4275 CE1 TYR B 324 -17.606 -8.758 -26.099 1.00112.40 C ANISOU 4275 CE1 TYR B 324 14381 14103 14224 920 -1488 1087 C ATOM 4276 CE2 TYR B 324 -16.556 -6.610 -25.996 1.00108.71 C ANISOU 4276 CE2 TYR B 324 13526 14067 13714 932 -1523 930 C ATOM 4277 CZ TYR B 324 -17.508 -7.452 -26.530 1.00110.18 C ANISOU 4277 CZ TYR B 324 13850 14069 13946 832 -1424 984 C ATOM 4278 OH TYR B 324 -18.368 -6.985 -27.498 1.00110.04 O ANISOU 4278 OH TYR B 324 13732 14100 13979 635 -1287 943 O ATOM 4279 N HIS B 325 -12.191 -7.948 -24.788 1.00 91.26 N ANISOU 4279 N HIS B 325 11039 11971 11663 1806 -2208 723 N ATOM 4280 CA HIS B 325 -11.474 -7.148 -25.775 1.00 90.69 C ANISOU 4280 CA HIS B 325 10588 12150 11718 1751 -2116 513 C ATOM 4281 C HIS B 325 -10.289 -7.903 -26.371 1.00 92.50 C ANISOU 4281 C HIS B 325 10593 12413 12141 2029 -2192 338 C ATOM 4282 O HIS B 325 -9.949 -7.715 -27.539 1.00 93.23 O ANISOU 4282 O HIS B 325 10445 12639 12339 1981 -2024 162 O ATOM 4283 CB HIS B 325 -11.006 -5.824 -25.165 1.00106.47 C ANISOU 4283 CB HIS B 325 12408 14398 13649 1638 -2192 482 C ATOM 4284 CG HIS B 325 -12.122 -4.877 -24.844 1.00105.10 C ANISOU 4284 CG HIS B 325 12386 14220 13327 1369 -2064 579 C ATOM 4285 ND1 HIS B 325 -12.894 -4.280 -25.819 1.00104.13 N ANISOU 4285 ND1 HIS B 325 12217 14111 13236 1145 -1840 556 N ATOM 4286 CD2 HIS B 325 -12.595 -4.427 -23.661 1.00105.17 C ANISOU 4286 CD2 HIS B 325 12590 14216 13154 1310 -2132 686 C ATOM 4287 CE1 HIS B 325 -13.794 -3.503 -25.246 1.00103.73 C ANISOU 4287 CE1 HIS B 325 12301 14044 13068 984 -1782 639 C ATOM 4288 NE2 HIS B 325 -13.638 -3.573 -23.938 1.00104.38 N ANISOU 4288 NE2 HIS B 325 12532 14117 13012 1075 -1934 706 N ATOM 4289 N VAL B 326 -9.665 -8.756 -25.564 1.00108.61 N ANISOU 4289 N VAL B 326 12715 14335 14216 2331 -2445 388 N ATOM 4290 CA VAL B 326 -8.552 -9.580 -26.027 1.00110.47 C ANISOU 4290 CA VAL B 326 12736 14570 14669 2668 -2543 213 C ATOM 4291 C VAL B 326 -9.004 -10.561 -27.106 1.00112.77 C ANISOU 4291 C VAL B 326 13159 14632 15059 2717 -2362 124 C ATOM 4292 O VAL B 326 -8.327 -10.739 -28.120 1.00113.94 O ANISOU 4292 O VAL B 326 13035 14896 15360 2830 -2243 -119 O ATOM 4293 CB VAL B 326 -7.903 -10.353 -24.859 1.00 79.90 C ANISOU 4293 CB VAL B 326 8984 10562 10813 3013 -2906 323 C ATOM 4294 CG1 VAL B 326 -6.937 -11.408 -25.378 1.00 82.33 C ANISOU 4294 CG1 VAL B 326 9119 10780 11381 3417 -3006 144 C ATOM 4295 CG2 VAL B 326 -7.193 -9.392 -23.921 1.00 78.88 C ANISOU 4295 CG2 VAL B 326 8649 10716 10604 2993 -3123 336 C ATOM 4296 N ARG B 327 -10.160 -11.180 -26.885 1.00 93.45 N ANISOU 4296 N ARG B 327 11125 11870 12511 2610 -2328 307 N ATOM 4297 CA ARG B 327 -10.715 -12.142 -27.830 1.00 95.51 C ANISOU 4297 CA ARG B 327 11568 11870 12852 2613 -2186 228 C ATOM 4298 C ARG B 327 -11.033 -11.486 -29.170 1.00 95.75 C ANISOU 4298 C ARG B 327 11404 12106 12870 2360 -1902 51 C ATOM 4299 O ARG B 327 -10.804 -12.070 -30.229 1.00 98.26 O ANISOU 4299 O ARG B 327 11671 12380 13285 2450 -1787 -161 O ATOM 4300 CB ARG B 327 -11.968 -12.799 -27.252 1.00 98.02 C ANISOU 4300 CB ARG B 327 12345 11838 13059 2464 -2202 482 C ATOM 4301 CG ARG B 327 -12.600 -13.823 -28.173 1.00101.27 C ANISOU 4301 CG ARG B 327 12971 11946 13560 2426 -2088 400 C ATOM 4302 CD ARG B 327 -13.883 -14.384 -27.592 1.00102.03 C ANISOU 4302 CD ARG B 327 13482 11727 13558 2204 -2083 661 C ATOM 4303 NE ARG B 327 -14.859 -13.339 -27.301 1.00 99.75 N ANISOU 4303 NE ARG B 327 13159 11644 13098 1849 -1941 802 N ATOM 4304 CZ ARG B 327 -15.633 -12.762 -28.213 1.00100.06 C ANISOU 4304 CZ ARG B 327 13081 11819 13119 1573 -1742 718 C ATOM 4305 NH1 ARG B 327 -15.544 -13.123 -29.486 1.00102.98 N ANISOU 4305 NH1 ARG B 327 13380 12161 13586 1579 -1655 497 N ATOM 4306 NH2 ARG B 327 -16.494 -11.821 -27.853 1.00 97.58 N ANISOU 4306 NH2 ARG B 327 12727 11670 12679 1307 -1639 847 N ATOM 4307 N ARG B 328 -11.564 -10.270 -29.113 1.00 83.97 N ANISOU 4307 N ARG B 328 9832 10830 11244 2054 -1799 137 N ATOM 4308 CA ARG B 328 -11.902 -9.516 -30.314 1.00 84.16 C ANISOU 4308 CA ARG B 328 9703 11047 11225 1796 -1566 23 C ATOM 4309 C ARG B 328 -10.650 -9.124 -31.091 1.00 84.82 C ANISOU 4309 C ARG B 328 9405 11427 11394 1891 -1483 -217 C ATOM 4310 O ARG B 328 -10.644 -9.142 -32.322 1.00 86.63 O ANISOU 4310 O ARG B 328 9557 11747 11610 1806 -1290 -381 O ATOM 4311 CB ARG B 328 -12.731 -8.284 -29.947 1.00107.69 C ANISOU 4311 CB ARG B 328 12701 14147 14069 1490 -1515 187 C ATOM 4312 CG ARG B 328 -14.108 -8.643 -29.421 1.00107.92 C ANISOU 4312 CG ARG B 328 13053 13934 14017 1349 -1515 388 C ATOM 4313 CD ARG B 328 -14.809 -7.472 -28.755 1.00105.43 C ANISOU 4313 CD ARG B 328 12739 13730 13589 1136 -1489 533 C ATOM 4314 NE ARG B 328 -15.294 -6.455 -29.682 1.00104.48 N ANISOU 4314 NE ARG B 328 12485 13766 13445 901 -1345 491 N ATOM 4315 CZ ARG B 328 -14.866 -5.196 -29.698 1.00102.46 C ANISOU 4315 CZ ARG B 328 12039 13723 13170 810 -1330 463 C ATOM 4316 NH1 ARG B 328 -13.939 -4.798 -28.838 1.00100.99 N ANISOU 4316 NH1 ARG B 328 11743 13641 12986 919 -1449 445 N ATOM 4317 NH2 ARG B 328 -15.369 -4.334 -30.570 1.00101.57 N ANISOU 4317 NH2 ARG B 328 11857 13700 13034 602 -1221 458 N ATOM 4318 N LEU B 329 -9.590 -8.774 -30.369 1.00 85.83 N ANISOU 4318 N LEU B 329 9291 11724 11596 2052 -1626 -242 N ATOM 4319 CA LEU B 329 -8.305 -8.495 -30.998 1.00 86.91 C ANISOU 4319 CA LEU B 329 9010 12162 11851 2155 -1548 -478 C ATOM 4320 C LEU B 329 -7.715 -9.788 -31.548 1.00 90.46 C ANISOU 4320 C LEU B 329 9424 12491 12454 2499 -1533 -691 C ATOM 4321 O LEU B 329 -7.119 -9.806 -32.625 1.00 92.41 O ANISOU 4321 O LEU B 329 9427 12935 12750 2521 -1325 -934 O ATOM 4322 CB LEU B 329 -7.338 -7.860 -29.997 1.00 90.70 C ANISOU 4322 CB LEU B 329 9220 12845 12396 2240 -1752 -457 C ATOM 4323 CG LEU B 329 -7.666 -6.447 -29.514 1.00 87.92 C ANISOU 4323 CG LEU B 329 8844 12643 11917 1911 -1759 -319 C ATOM 4324 CD1 LEU B 329 -6.654 -5.993 -28.475 1.00 86.98 C ANISOU 4324 CD1 LEU B 329 8482 12699 11866 2018 -2008 -332 C ATOM 4325 CD2 LEU B 329 -7.717 -5.474 -30.679 1.00 88.10 C ANISOU 4325 CD2 LEU B 329 8696 12884 11894 1591 -1486 -398 C ATOM 4326 N MET B 330 -7.895 -10.868 -30.795 1.00131.72 N ANISOU 4326 N MET B 330 14920 17381 17747 2766 -1748 -600 N ATOM 4327 CA MET B 330 -7.440 -12.194 -31.197 1.00135.52 C ANISOU 4327 CA MET B 330 15448 17644 18398 3132 -1777 -788 C ATOM 4328 C MET B 330 -8.130 -12.638 -32.482 1.00138.48 C ANISOU 4328 C MET B 330 15998 17905 18711 2991 -1522 -939 C ATOM 4329 O MET B 330 -7.541 -13.329 -33.314 1.00141.81 O ANISOU 4329 O MET B 330 16313 18321 19246 3217 -1411 -1224 O ATOM 4330 CB MET B 330 -7.721 -13.198 -30.076 1.00132.66 C ANISOU 4330 CB MET B 330 15451 16871 18084 3374 -2076 -583 C ATOM 4331 CG MET B 330 -7.411 -14.640 -30.422 1.00135.95 C ANISOU 4331 CG MET B 330 16019 16946 18692 3754 -2141 -745 C ATOM 4332 SD MET B 330 -7.938 -15.787 -29.138 1.00136.52 S ANISOU 4332 SD MET B 330 16628 16466 18778 3947 -2484 -428 S ATOM 4333 CE MET B 330 -7.495 -17.354 -29.885 1.00140.31 C ANISOU 4333 CE MET B 330 17245 16543 19525 4382 -2509 -703 C ATOM 4334 N PHE B 331 -9.384 -12.226 -32.636 1.00108.84 N ANISOU 4334 N PHE B 331 12505 14074 14774 2622 -1437 -763 N ATOM 4335 CA PHE B 331 -10.194 -12.598 -33.789 1.00111.83 C ANISOU 4335 CA PHE B 331 13083 14344 15063 2441 -1248 -875 C ATOM 4336 C PHE B 331 -9.618 -12.092 -35.110 1.00114.00 C ANISOU 4336 C PHE B 331 13074 14968 15273 2355 -982 -1142 C ATOM 4337 O PHE B 331 -9.615 -12.812 -36.108 1.00117.50 O ANISOU 4337 O PHE B 331 13602 15337 15705 2423 -846 -1384 O ATOM 4338 CB PHE B 331 -11.622 -12.073 -33.607 1.00 92.06 C ANISOU 4338 CB PHE B 331 10829 11756 12393 2057 -1239 -617 C ATOM 4339 CG PHE B 331 -12.517 -12.309 -34.792 1.00 95.40 C ANISOU 4339 CG PHE B 331 11427 12113 12708 1826 -1088 -715 C ATOM 4340 CD1 PHE B 331 -13.177 -13.516 -34.947 1.00 98.73 C ANISOU 4340 CD1 PHE B 331 12180 12155 13178 1864 -1144 -750 C ATOM 4341 CD2 PHE B 331 -12.712 -11.317 -35.741 1.00 95.59 C ANISOU 4341 CD2 PHE B 331 11307 12440 12573 1553 -914 -760 C ATOM 4342 CE1 PHE B 331 -14.005 -13.734 -36.029 1.00102.64 C ANISOU 4342 CE1 PHE B 331 12832 12599 13566 1634 -1040 -857 C ATOM 4343 CE2 PHE B 331 -13.539 -11.531 -36.827 1.00 99.69 C ANISOU 4343 CE2 PHE B 331 12001 12914 12964 1343 -819 -844 C ATOM 4344 CZ PHE B 331 -14.186 -12.741 -36.971 1.00103.55 C ANISOU 4344 CZ PHE B 331 12794 13048 13503 1382 -887 -906 C ATOM 4345 N CYS B 332 -9.127 -10.856 -35.112 1.00113.45 N ANISOU 4345 N CYS B 332 12690 15271 15144 2189 -901 -1103 N ATOM 4346 CA CYS B 332 -8.703 -10.214 -36.354 1.00115.42 C ANISOU 4346 CA CYS B 332 12708 15868 15277 2011 -622 -1291 C ATOM 4347 C CYS B 332 -7.188 -10.075 -36.527 1.00115.92 C ANISOU 4347 C CYS B 332 12310 16257 15476 2219 -517 -1526 C ATOM 4348 O CYS B 332 -6.709 -9.870 -37.641 1.00118.21 O ANISOU 4348 O CYS B 332 12416 16820 15677 2134 -242 -1742 O ATOM 4349 CB CYS B 332 -9.383 -8.850 -36.510 1.00113.58 C ANISOU 4349 CB CYS B 332 12489 15809 14855 1587 -560 -1073 C ATOM 4350 SG CYS B 332 -9.248 -7.770 -35.067 1.00107.82 S ANISOU 4350 SG CYS B 332 11629 15146 14192 1511 -764 -808 S ATOM 4351 N TYR B 333 -6.436 -10.185 -35.435 1.00109.02 N ANISOU 4351 N TYR B 333 11241 15377 14805 2482 -733 -1487 N ATOM 4352 CA TYR B 333 -4.982 -10.036 -35.509 1.00109.14 C ANISOU 4352 CA TYR B 333 10750 15727 14993 2685 -666 -1711 C ATOM 4353 C TYR B 333 -4.226 -11.332 -35.794 1.00111.93 C ANISOU 4353 C TYR B 333 10995 15979 15554 3162 -656 -2019 C ATOM 4354 O TYR B 333 -3.096 -11.298 -36.280 1.00113.30 O ANISOU 4354 O TYR B 333 10722 16475 15852 3316 -487 -2292 O ATOM 4355 CB TYR B 333 -4.421 -9.346 -34.262 1.00116.25 C ANISOU 4355 CB TYR B 333 11414 16746 16008 2708 -922 -1546 C ATOM 4356 CG TYR B 333 -4.295 -7.846 -34.409 1.00114.35 C ANISOU 4356 CG TYR B 333 10956 16839 15653 2284 -797 -1450 C ATOM 4357 CD1 TYR B 333 -3.160 -7.286 -34.982 1.00115.66 C ANISOU 4357 CD1 TYR B 333 10630 17422 15896 2212 -595 -1648 C ATOM 4358 CD2 TYR B 333 -5.302 -6.992 -33.979 1.00111.11 C ANISOU 4358 CD2 TYR B 333 10828 16318 15072 1954 -873 -1169 C ATOM 4359 CE1 TYR B 333 -3.029 -5.921 -35.124 1.00114.07 C ANISOU 4359 CE1 TYR B 333 10261 17482 15599 1794 -486 -1545 C ATOM 4360 CE2 TYR B 333 -5.180 -5.620 -34.117 1.00109.73 C ANISOU 4360 CE2 TYR B 333 10490 16389 14813 1582 -778 -1084 C ATOM 4361 CZ TYR B 333 -4.040 -5.092 -34.691 1.00111.18 C ANISOU 4361 CZ TYR B 333 10222 16950 15071 1489 -592 -1262 C ATOM 4362 OH TYR B 333 -3.904 -3.731 -34.835 1.00110.03 O ANISOU 4362 OH TYR B 333 9944 17010 14852 1087 -502 -1162 O ATOM 4363 N ILE B 334 -4.842 -12.471 -35.497 1.00116.36 N ANISOU 4363 N ILE B 334 11956 16087 16169 3394 -828 -1985 N ATOM 4364 CA ILE B 334 -4.245 -13.751 -35.858 1.00119.09 C ANISOU 4364 CA ILE B 334 12277 16255 16715 3856 -819 -2293 C ATOM 4365 C ILE B 334 -4.396 -13.976 -37.357 1.00122.45 C ANISOU 4365 C ILE B 334 12749 16786 16990 3742 -450 -2595 C ATOM 4366 O ILE B 334 -5.508 -13.974 -37.882 1.00123.08 O ANISOU 4366 O ILE B 334 13217 16705 16844 3440 -374 -2507 O ATOM 4367 CB ILE B 334 -4.894 -14.923 -35.102 1.00115.05 C ANISOU 4367 CB ILE B 334 12243 15168 16305 4105 -1122 -2147 C ATOM 4368 CG1 ILE B 334 -4.675 -14.775 -33.597 1.00112.43 C ANISOU 4368 CG1 ILE B 334 11896 14743 16079 4244 -1496 -1851 C ATOM 4369 CG2 ILE B 334 -4.321 -16.247 -35.582 1.00118.00 C ANISOU 4369 CG2 ILE B 334 12638 15299 16897 4585 -1107 -2489 C ATOM 4370 CD1 ILE B 334 -5.137 -15.974 -32.799 1.00113.04 C ANISOU 4370 CD1 ILE B 334 12434 14260 16258 4516 -1800 -1689 C ATOM 4371 N SER B 335 -3.272 -14.166 -38.041 1.00129.12 N ANISOU 4371 N SER B 335 13184 17924 17952 3985 -223 -2963 N ATOM 4372 CA SER B 335 -3.266 -14.329 -39.492 1.00132.52 C ANISOU 4372 CA SER B 335 13627 18529 18197 3882 168 -3290 C ATOM 4373 C SER B 335 -3.913 -15.639 -39.931 1.00135.11 C ANISOU 4373 C SER B 335 14429 18382 18525 4089 133 -3471 C ATOM 4374 O SER B 335 -4.039 -16.574 -39.141 1.00134.64 O ANISOU 4374 O SER B 335 14594 17870 18694 4423 -169 -3411 O ATOM 4375 CB SER B 335 -1.836 -14.244 -40.032 1.00162.82 C ANISOU 4375 CB SER B 335 16865 22823 22175 4115 447 -3662 C ATOM 4376 OG SER B 335 -1.821 -14.324 -41.446 1.00166.06 O ANISOU 4376 OG SER B 335 17299 23454 22344 3979 866 -3979 O ATOM 4377 N ASP B 336 -4.318 -15.696 -41.198 1.00148.70 N ANISOU 4377 N ASP B 336 16327 20200 19974 3870 431 -3687 N ATOM 4378 CA ASP B 336 -4.982 -16.874 -41.751 1.00150.49 C ANISOU 4378 CA ASP B 336 17024 19992 20162 3994 414 -3897 C ATOM 4379 C ASP B 336 -4.083 -18.105 -41.738 1.00152.07 C ANISOU 4379 C ASP B 336 17124 19970 20684 4607 399 -4290 C ATOM 4380 O ASP B 336 -4.555 -19.227 -41.559 1.00153.00 O ANISOU 4380 O ASP B 336 17655 19543 20935 4832 200 -4352 O ATOM 4381 CB ASP B 336 -5.460 -16.601 -43.180 1.00148.81 C ANISOU 4381 CB ASP B 336 16979 20010 19553 3634 742 -4091 C ATOM 4382 CG ASP B 336 -6.473 -15.478 -43.252 1.00147.84 C ANISOU 4382 CG ASP B 336 17017 20030 19125 3062 709 -3700 C ATOM 4383 OD1 ASP B 336 -7.155 -15.228 -42.237 1.00146.20 O ANISOU 4383 OD1 ASP B 336 16952 19587 19011 2949 412 -3314 O ATOM 4384 OD2 ASP B 336 -6.588 -14.846 -44.322 1.00149.37 O ANISOU 4384 OD2 ASP B 336 17204 20571 18979 2737 982 -3780 O ATOM 4385 N GLU B 337 -2.785 -17.889 -41.927 1.00200.42 N ANISOU 4385 N GLU B 337 22688 26508 26953 4876 607 -4557 N ATOM 4386 CA GLU B 337 -1.829 -18.987 -41.938 1.00202.32 C ANISOU 4386 CA GLU B 337 22747 26589 27537 5512 606 -4963 C ATOM 4387 C GLU B 337 -1.538 -19.449 -40.515 1.00200.89 C ANISOU 4387 C GLU B 337 22534 26049 27745 5910 142 -4722 C ATOM 4388 O GLU B 337 -1.009 -20.539 -40.299 1.00202.60 O ANISOU 4388 O GLU B 337 22763 25929 28285 6474 -3 -4960 O ATOM 4389 CB GLU B 337 -0.530 -18.575 -42.636 1.00175.63 C ANISOU 4389 CB GLU B 337 18712 23827 24193 5659 1010 -5347 C ATOM 4390 CG GLU B 337 -0.728 -17.873 -43.972 1.00176.64 C ANISOU 4390 CG GLU B 337 18833 24413 23870 5187 1486 -5507 C ATOM 4391 CD GLU B 337 -0.692 -16.361 -43.849 1.00174.38 C ANISOU 4391 CD GLU B 337 18256 24622 23379 4662 1585 -5158 C ATOM 4392 OE1 GLU B 337 -0.144 -15.859 -42.845 1.00171.59 O ANISOU 4392 OE1 GLU B 337 17531 24386 23279 4739 1374 -4932 O ATOM 4393 OE2 GLU B 337 -1.210 -15.675 -44.755 1.00174.87 O ANISOU 4393 OE2 GLU B 337 18482 24938 23022 4172 1852 -5110 O ATOM 4394 N GLN B 338 -1.889 -18.607 -39.548 1.00154.62 N ANISOU 4394 N GLN B 338 16657 20253 21838 5621 -98 -4249 N ATOM 4395 CA GLN B 338 -1.647 -18.905 -38.143 1.00152.63 C ANISOU 4395 CA GLN B 338 16400 19718 21876 5933 -550 -3970 C ATOM 4396 C GLN B 338 -2.805 -19.675 -37.512 1.00151.96 C ANISOU 4396 C GLN B 338 16998 18969 21771 5889 -871 -3673 C ATOM 4397 O GLN B 338 -2.622 -20.375 -36.516 1.00150.82 O ANISOU 4397 O GLN B 338 16995 18436 21876 6256 -1241 -3520 O ATOM 4398 CB GLN B 338 -1.388 -17.613 -37.365 1.00172.49 C ANISOU 4398 CB GLN B 338 18557 22647 24336 5649 -647 -3639 C ATOM 4399 CG GLN B 338 -0.123 -16.882 -37.787 1.00173.07 C ANISOU 4399 CG GLN B 338 17905 23357 24498 5699 -384 -3899 C ATOM 4400 CD GLN B 338 0.104 -15.606 -37.001 1.00170.69 C ANISOU 4400 CD GLN B 338 17289 23415 24152 5383 -508 -3580 C ATOM 4401 OE1 GLN B 338 -0.830 -15.037 -36.434 1.00168.68 O ANISOU 4401 OE1 GLN B 338 17376 23019 23696 5010 -669 -3193 O ATOM 4402 NE2 GLN B 338 1.348 -15.141 -36.973 1.00171.02 N ANISOU 4402 NE2 GLN B 338 16662 23929 24388 5523 -425 -3764 N ATOM 4403 N TRP B 339 -3.995 -19.542 -38.091 1.00159.13 N ANISOU 4403 N TRP B 339 18326 19756 22380 5428 -738 -3580 N ATOM 4404 CA TRP B 339 -5.178 -20.214 -37.559 1.00158.69 C ANISOU 4404 CA TRP B 339 18889 19111 22294 5298 -999 -3298 C ATOM 4405 C TRP B 339 -5.128 -21.724 -37.769 1.00160.90 C ANISOU 4405 C TRP B 339 19520 18812 22801 5723 -1106 -3563 C ATOM 4406 O TRP B 339 -5.109 -22.206 -38.901 1.00162.89 O ANISOU 4406 O TRP B 339 19851 19038 23003 5773 -859 -3970 O ATOM 4407 CB TRP B 339 -6.460 -19.644 -38.173 1.00113.20 C ANISOU 4407 CB TRP B 339 13420 13413 16179 4689 -838 -3153 C ATOM 4408 CG TRP B 339 -6.938 -18.382 -37.521 1.00110.34 C ANISOU 4408 CG TRP B 339 12945 13339 15639 4273 -891 -2738 C ATOM 4409 CD1 TRP B 339 -6.774 -17.108 -37.980 1.00109.39 C ANISOU 4409 CD1 TRP B 339 12488 13759 15316 3954 -665 -2717 C ATOM 4410 CD2 TRP B 339 -7.659 -18.273 -36.287 1.00107.92 C ANISOU 4410 CD2 TRP B 339 12888 12777 15338 4133 -1181 -2293 C ATOM 4411 NE1 TRP B 339 -7.349 -16.213 -37.111 1.00106.98 N ANISOU 4411 NE1 TRP B 339 12207 13525 14914 3650 -811 -2309 N ATOM 4412 CE2 TRP B 339 -7.900 -16.903 -36.062 1.00105.56 C ANISOU 4412 CE2 TRP B 339 12374 12887 14848 3756 -1113 -2056 C ATOM 4413 CE3 TRP B 339 -8.126 -19.202 -35.351 1.00107.68 C ANISOU 4413 CE3 TRP B 339 13263 12208 15444 4280 -1479 -2071 C ATOM 4414 CZ2 TRP B 339 -8.585 -16.438 -34.942 1.00102.72 C ANISOU 4414 CZ2 TRP B 339 12169 12433 14426 3549 -1315 -1646 C ATOM 4415 CZ3 TRP B 339 -8.806 -18.739 -34.239 1.00105.17 C ANISOU 4415 CZ3 TRP B 339 13100 11823 15036 4041 -1665 -1636 C ATOM 4416 CH2 TRP B 339 -9.029 -17.369 -34.044 1.00103.04 C ANISOU 4416 CH2 TRP B 339 12588 11989 14573 3692 -1575 -1447 C ATOM 4417 N THR B 340 -5.109 -22.462 -36.664 1.00155.39 N ANISOU 4417 N THR B 340 19067 17635 22340 6021 -1485 -3327 N ATOM 4418 CA THR B 340 -5.164 -23.918 -36.701 1.00157.76 C ANISOU 4418 CA THR B 340 19792 17271 22879 6405 -1653 -3499 C ATOM 4419 C THR B 340 -6.520 -24.391 -36.193 1.00156.93 C ANISOU 4419 C THR B 340 20334 16619 22671 6049 -1855 -3128 C ATOM 4420 O THR B 340 -7.359 -23.581 -35.800 1.00155.31 O ANISOU 4420 O THR B 340 20193 16593 22224 5552 -1853 -2762 O ATOM 4421 CB THR B 340 -4.055 -24.547 -35.841 1.00155.62 C ANISOU 4421 CB THR B 340 19347 16793 22988 7070 -1966 -3510 C ATOM 4422 OG1 THR B 340 -4.184 -24.098 -34.486 1.00153.44 O ANISOU 4422 OG1 THR B 340 19099 16512 22689 6978 -2292 -2994 O ATOM 4423 CG2 THR B 340 -2.684 -24.156 -36.371 1.00156.14 C ANISOU 4423 CG2 THR B 340 18711 17412 23205 7441 -1753 -3920 C ATOM 4424 N THR B 341 -6.735 -25.702 -36.203 1.00156.09 N ANISOU 4424 N THR B 341 20701 15841 22764 6299 -2021 -3232 N ATOM 4425 CA THR B 341 -7.994 -26.261 -35.727 1.00155.88 C ANISOU 4425 CA THR B 341 21294 15260 22673 5946 -2205 -2890 C ATOM 4426 C THR B 341 -8.086 -26.173 -34.206 1.00153.65 C ANISOU 4426 C THR B 341 21140 14806 22433 5964 -2543 -2342 C ATOM 4427 O THR B 341 -9.177 -26.233 -33.639 1.00153.27 O ANISOU 4427 O THR B 341 21487 14499 22248 5547 -2640 -1958 O ATOM 4428 CB THR B 341 -8.166 -27.727 -36.170 1.00170.77 C ANISOU 4428 CB THR B 341 23688 16420 24778 6190 -2299 -3162 C ATOM 4429 OG1 THR B 341 -7.052 -28.502 -35.712 1.00171.36 O ANISOU 4429 OG1 THR B 341 23708 16188 25211 6893 -2529 -3288 O ATOM 4430 CG2 THR B 341 -8.251 -27.818 -37.687 1.00172.65 C ANISOU 4430 CG2 THR B 341 23883 16817 24899 6092 -1962 -3705 C ATOM 4431 N PHE B 342 -6.938 -26.030 -33.550 1.00161.17 N ANISOU 4431 N PHE B 342 21746 15929 23562 6441 -2719 -2317 N ATOM 4432 CA PHE B 342 -6.904 -25.845 -32.103 1.00159.19 C ANISOU 4432 CA PHE B 342 21583 15600 23300 6476 -3052 -1816 C ATOM 4433 C PHE B 342 -7.332 -24.435 -31.709 1.00156.23 C ANISOU 4433 C PHE B 342 20940 15810 22612 5984 -2930 -1531 C ATOM 4434 O PHE B 342 -8.193 -24.258 -30.847 1.00154.74 O ANISOU 4434 O PHE B 342 21064 15486 22246 5638 -3046 -1097 O ATOM 4435 CB PHE B 342 -5.510 -26.141 -31.546 1.00156.52 C ANISOU 4435 CB PHE B 342 20930 15307 23232 7105 -3299 -1882 C ATOM 4436 CG PHE B 342 -5.350 -25.774 -30.097 1.00154.96 C ANISOU 4436 CG PHE B 342 20737 15211 22931 7054 -3597 -1378 C ATOM 4437 CD1 PHE B 342 -5.832 -26.606 -29.100 1.00157.01 C ANISOU 4437 CD1 PHE B 342 21555 14946 23156 6981 -3862 -953 C ATOM 4438 CD2 PHE B 342 -4.714 -24.597 -29.731 1.00152.21 C ANISOU 4438 CD2 PHE B 342 19844 15493 22496 7045 -3600 -1337 C ATOM 4439 CE1 PHE B 342 -5.688 -26.270 -27.766 1.00156.37 C ANISOU 4439 CE1 PHE B 342 21504 14985 22925 6917 -4115 -509 C ATOM 4440 CE2 PHE B 342 -4.567 -24.256 -28.400 1.00151.14 C ANISOU 4440 CE2 PHE B 342 19740 15458 22230 6976 -3875 -907 C ATOM 4441 CZ PHE B 342 -5.054 -25.094 -27.417 1.00153.53 C ANISOU 4441 CZ PHE B 342 20615 15252 22468 6922 -4129 -499 C ATOM 4442 N LEU B 343 -6.723 -23.435 -32.342 1.00115.06 N ANISOU 4442 N LEU B 343 15151 11234 17331 5951 -2682 -1783 N ATOM 4443 CA LEU B 343 -7.053 -22.038 -32.075 1.00112.47 C ANISOU 4443 CA LEU B 343 14551 11450 16731 5504 -2555 -1562 C ATOM 4444 C LEU B 343 -8.506 -21.733 -32.418 1.00112.24 C ANISOU 4444 C LEU B 343 14842 11367 16439 4898 -2371 -1399 C ATOM 4445 O LEU B 343 -9.125 -20.864 -31.807 1.00110.02 O ANISOU 4445 O LEU B 343 14555 11298 15949 4527 -2370 -1079 O ATOM 4446 CB LEU B 343 -6.127 -21.103 -32.856 1.00135.13 C ANISOU 4446 CB LEU B 343 16782 14965 19597 5556 -2296 -1891 C ATOM 4447 CG LEU B 343 -4.674 -21.021 -32.390 1.00134.98 C ANISOU 4447 CG LEU B 343 16278 15188 19820 6062 -2467 -2012 C ATOM 4448 CD1 LEU B 343 -3.868 -20.119 -33.312 1.00135.27 C ANISOU 4448 CD1 LEU B 343 15690 15865 19840 6018 -2135 -2355 C ATOM 4449 CD2 LEU B 343 -4.607 -20.518 -30.956 1.00132.47 C ANISOU 4449 CD2 LEU B 343 15962 14929 19441 6032 -2797 -1587 C ATOM 4450 N PHE B 344 -9.041 -22.449 -33.402 1.00134.14 N ANISOU 4450 N PHE B 344 17877 13859 19230 4810 -2225 -1642 N ATOM 4451 CA PHE B 344 -10.434 -22.282 -33.792 1.00134.59 C ANISOU 4451 CA PHE B 344 18225 13841 19073 4253 -2088 -1517 C ATOM 4452 C PHE B 344 -11.351 -22.739 -32.663 1.00133.34 C ANISOU 4452 C PHE B 344 18522 13246 18893 4055 -2310 -1070 C ATOM 4453 O PHE B 344 -12.265 -22.020 -32.260 1.00131.69 O ANISOU 4453 O PHE B 344 18346 13209 18483 3617 -2255 -779 O ATOM 4454 CB PHE B 344 -10.729 -23.077 -35.065 1.00109.27 C ANISOU 4454 CB PHE B 344 15225 10390 15901 4233 -1934 -1907 C ATOM 4455 CG PHE B 344 -12.120 -22.880 -35.595 1.00109.88 C ANISOU 4455 CG PHE B 344 15541 10443 15766 3659 -1814 -1824 C ATOM 4456 CD1 PHE B 344 -12.403 -21.833 -36.455 1.00109.94 C ANISOU 4456 CD1 PHE B 344 15271 10968 15535 3334 -1571 -1932 C ATOM 4457 CD2 PHE B 344 -13.145 -23.740 -35.234 1.00110.70 C ANISOU 4457 CD2 PHE B 344 16139 10004 15917 3437 -1957 -1629 C ATOM 4458 CE1 PHE B 344 -13.680 -21.646 -36.946 1.00110.70 C ANISOU 4458 CE1 PHE B 344 15557 11053 15452 2836 -1504 -1855 C ATOM 4459 CE2 PHE B 344 -14.425 -23.557 -35.720 1.00111.31 C ANISOU 4459 CE2 PHE B 344 16376 10089 15829 2906 -1864 -1567 C ATOM 4460 CZ PHE B 344 -14.692 -22.508 -36.578 1.00111.33 C ANISOU 4460 CZ PHE B 344 16076 10622 15603 2625 -1653 -1686 C ATOM 4461 N ASP B 345 -11.096 -23.941 -32.156 1.00128.66 N ANISOU 4461 N ASP B 345 18285 12087 18512 4385 -2552 -1018 N ATOM 4462 CA ASP B 345 -11.895 -24.506 -31.074 1.00128.35 C ANISOU 4462 CA ASP B 345 18731 11588 18448 4203 -2759 -579 C ATOM 4463 C ASP B 345 -11.646 -23.784 -29.753 1.00125.64 C ANISOU 4463 C ASP B 345 18266 11494 17976 4221 -2916 -188 C ATOM 4464 O ASP B 345 -12.564 -23.612 -28.952 1.00124.93 O ANISOU 4464 O ASP B 345 18427 11329 17710 3855 -2939 194 O ATOM 4465 CB ASP B 345 -11.621 -26.004 -30.927 1.00124.62 C ANISOU 4465 CB ASP B 345 18712 10397 18242 4568 -2996 -623 C ATOM 4466 CG ASP B 345 -12.025 -26.793 -32.158 1.00127.56 C ANISOU 4466 CG ASP B 345 19301 10446 18722 4493 -2857 -1005 C ATOM 4467 OD1 ASP B 345 -13.000 -26.392 -32.829 1.00127.62 O ANISOU 4467 OD1 ASP B 345 19308 10629 18554 3993 -2640 -1059 O ATOM 4468 OD2 ASP B 345 -11.366 -27.811 -32.456 1.00129.05 O ANISOU 4468 OD2 ASP B 345 19662 10202 19170 4946 -2981 -1267 O ATOM 4469 N PHE B 346 -10.404 -23.364 -29.533 1.00114.56 N ANISOU 4469 N PHE B 346 16467 10405 16656 4638 -3018 -302 N ATOM 4470 CA PHE B 346 -10.052 -22.611 -28.334 1.00111.94 C ANISOU 4470 CA PHE B 346 15985 10357 16190 4669 -3190 12 C ATOM 4471 C PHE B 346 -10.781 -21.276 -28.300 1.00109.37 C ANISOU 4471 C PHE B 346 15443 10529 15585 4163 -2958 135 C ATOM 4472 O PHE B 346 -11.211 -20.821 -27.242 1.00107.32 O ANISOU 4472 O PHE B 346 15307 10340 15130 3962 -3043 486 O ATOM 4473 CB PHE B 346 -8.539 -22.381 -28.263 1.00140.05 C ANISOU 4473 CB PHE B 346 19081 14204 19926 5195 -3340 -200 C ATOM 4474 CG PHE B 346 -8.123 -21.392 -27.208 1.00137.48 C ANISOU 4474 CG PHE B 346 18508 14285 19443 5175 -3494 42 C ATOM 4475 CD1 PHE B 346 -8.003 -21.778 -25.883 1.00137.21 C ANISOU 4475 CD1 PHE B 346 18777 14002 19352 5338 -3852 409 C ATOM 4476 CD2 PHE B 346 -7.844 -20.076 -27.545 1.00135.48 C ANISOU 4476 CD2 PHE B 346 17747 14648 19081 4980 -3293 -97 C ATOM 4477 CE1 PHE B 346 -7.619 -20.868 -24.914 1.00135.31 C ANISOU 4477 CE1 PHE B 346 18332 14144 18935 5310 -4009 603 C ATOM 4478 CE2 PHE B 346 -7.462 -19.163 -26.582 1.00133.32 C ANISOU 4478 CE2 PHE B 346 17265 14723 18668 4944 -3447 94 C ATOM 4479 CZ PHE B 346 -7.348 -19.559 -25.265 1.00133.17 C ANISOU 4479 CZ PHE B 346 17544 14474 18580 5112 -3807 429 C ATOM 4480 N TYR B 347 -10.911 -20.655 -29.468 1.00100.80 N ANISOU 4480 N TYR B 347 14053 9778 14470 3971 -2667 -160 N ATOM 4481 CA TYR B 347 -11.563 -19.358 -29.587 1.00 98.92 C ANISOU 4481 CA TYR B 347 13594 9991 14000 3527 -2454 -78 C ATOM 4482 C TYR B 347 -13.020 -19.425 -29.140 1.00 98.53 C ANISOU 4482 C TYR B 347 13916 9734 13788 3077 -2405 232 C ATOM 4483 O TYR B 347 -13.519 -18.514 -28.478 1.00 96.02 O ANISOU 4483 O TYR B 347 13530 9671 13281 2812 -2361 461 O ATOM 4484 CB TYR B 347 -11.482 -18.856 -31.032 1.00101.91 C ANISOU 4484 CB TYR B 347 13664 10687 14372 3410 -2173 -438 C ATOM 4485 CG TYR B 347 -12.159 -17.524 -31.268 1.00100.39 C ANISOU 4485 CG TYR B 347 13265 10918 13960 2973 -1974 -355 C ATOM 4486 CD1 TYR B 347 -11.469 -16.334 -31.081 1.00 97.55 C ANISOU 4486 CD1 TYR B 347 12500 11027 13537 2982 -1937 -366 C ATOM 4487 CD2 TYR B 347 -13.485 -17.456 -31.677 1.00101.15 C ANISOU 4487 CD2 TYR B 347 13567 10930 13936 2555 -1845 -270 C ATOM 4488 CE1 TYR B 347 -12.079 -15.115 -31.298 1.00 95.72 C ANISOU 4488 CE1 TYR B 347 12115 11128 13128 2605 -1775 -287 C ATOM 4489 CE2 TYR B 347 -14.105 -16.241 -31.892 1.00 99.23 C ANISOU 4489 CE2 TYR B 347 13133 11048 13520 2203 -1694 -193 C ATOM 4490 CZ TYR B 347 -13.397 -15.074 -31.700 1.00 96.71 C ANISOU 4490 CZ TYR B 347 12454 11151 13142 2239 -1659 -198 C ATOM 4491 OH TYR B 347 -14.009 -13.859 -31.913 1.00 94.44 O ANISOU 4491 OH TYR B 347 12011 11170 12703 1909 -1527 -118 O ATOM 4492 N HIS B 348 -13.696 -20.513 -29.497 1.00107.71 N ANISOU 4492 N HIS B 348 15459 10431 15037 2989 -2406 220 N ATOM 4493 CA HIS B 348 -15.124 -20.644 -29.227 1.00107.46 C ANISOU 4493 CA HIS B 348 15732 10214 14885 2520 -2326 473 C ATOM 4494 C HIS B 348 -15.423 -21.073 -27.794 1.00106.36 C ANISOU 4494 C HIS B 348 15951 9793 14670 2490 -2500 891 C ATOM 4495 O HIS B 348 -16.506 -20.805 -27.275 1.00105.59 O ANISOU 4495 O HIS B 348 15989 9716 14416 2089 -2399 1151 O ATOM 4496 CB HIS B 348 -15.776 -21.593 -30.234 1.00105.16 C ANISOU 4496 CB HIS B 348 15692 9553 14710 2367 -2256 278 C ATOM 4497 CG HIS B 348 -15.708 -21.108 -31.643 1.00106.89 C ANISOU 4497 CG HIS B 348 15614 10083 14917 2300 -2064 -99 C ATOM 4498 ND1 HIS B 348 -14.654 -21.406 -32.489 1.00108.73 N ANISOU 4498 ND1 HIS B 348 15693 10348 15273 2673 -2049 -476 N ATOM 4499 CD2 HIS B 348 -16.553 -20.337 -32.370 1.00107.12 C ANISOU 4499 CD2 HIS B 348 15475 10418 14806 1910 -1879 -156 C ATOM 4500 CE1 HIS B 348 -14.857 -20.845 -33.661 1.00110.12 C ANISOU 4500 CE1 HIS B 348 15652 10841 15348 2487 -1847 -735 C ATOM 4501 NE2 HIS B 348 -16.009 -20.187 -33.617 1.00109.31 N ANISOU 4501 NE2 HIS B 348 15546 10898 15087 2028 -1765 -535 N ATOM 4502 N TYR B 349 -14.463 -21.736 -27.158 1.00105.21 N ANISOU 4502 N TYR B 349 15952 9395 14627 2920 -2760 956 N ATOM 4503 CA TYR B 349 -14.562 -22.006 -25.730 1.00104.28 C ANISOU 4503 CA TYR B 349 16164 9081 14378 2931 -2956 1373 C ATOM 4504 C TYR B 349 -14.219 -20.736 -24.963 1.00101.45 C ANISOU 4504 C TYR B 349 15493 9251 13802 2921 -2961 1487 C ATOM 4505 O TYR B 349 -14.814 -20.444 -23.926 1.00100.46 O ANISOU 4505 O TYR B 349 15559 9171 13441 2684 -2959 1813 O ATOM 4506 CB TYR B 349 -13.633 -23.147 -25.314 1.00 97.16 C ANISOU 4506 CB TYR B 349 15545 7711 13660 3424 -3288 1420 C ATOM 4507 CG TYR B 349 -14.171 -24.526 -25.628 1.00100.50 C ANISOU 4507 CG TYR B 349 16467 7464 14253 3371 -3336 1449 C ATOM 4508 CD1 TYR B 349 -15.316 -25.003 -25.003 1.00101.42 C ANISOU 4508 CD1 TYR B 349 17043 7252 14238 2944 -3295 1813 C ATOM 4509 CD2 TYR B 349 -13.525 -25.357 -26.532 1.00103.58 C ANISOU 4509 CD2 TYR B 349 16873 7543 14940 3739 -3412 1102 C ATOM 4510 CE1 TYR B 349 -15.811 -26.265 -25.281 1.00105.55 C ANISOU 4510 CE1 TYR B 349 18039 7133 14933 2851 -3347 1845 C ATOM 4511 CE2 TYR B 349 -14.011 -26.620 -26.817 1.00107.71 C ANISOU 4511 CE2 TYR B 349 17885 7408 15632 3685 -3472 1107 C ATOM 4512 CZ TYR B 349 -15.153 -27.069 -26.189 1.00108.66 C ANISOU 4512 CZ TYR B 349 18469 7188 15628 3226 -3451 1489 C ATOM 4513 OH TYR B 349 -15.639 -28.325 -26.471 1.00113.14 O ANISOU 4513 OH TYR B 349 19538 7073 16379 3129 -3518 1497 O ATOM 4514 N PHE B 350 -13.256 -19.984 -25.487 1.00111.25 N ANISOU 4514 N PHE B 350 16259 10893 15118 3161 -2952 1200 N ATOM 4515 CA PHE B 350 -12.881 -18.697 -24.917 1.00108.56 C ANISOU 4515 CA PHE B 350 15585 11061 14603 3127 -2951 1244 C ATOM 4516 C PHE B 350 -14.067 -17.745 -25.001 1.00107.15 C ANISOU 4516 C PHE B 350 15340 11145 14226 2627 -2667 1322 C ATOM 4517 O PHE B 350 -14.313 -16.964 -24.083 1.00104.99 O ANISOU 4517 O PHE B 350 15058 11101 13734 2477 -2665 1515 O ATOM 4518 CB PHE B 350 -11.688 -18.108 -25.672 1.00121.43 C ANISOU 4518 CB PHE B 350 16695 13054 16387 3409 -2947 891 C ATOM 4519 CG PHE B 350 -11.054 -16.930 -24.987 1.00118.59 C ANISOU 4519 CG PHE B 350 16011 13150 15897 3437 -3028 928 C ATOM 4520 CD1 PHE B 350 -11.071 -16.821 -23.606 1.00117.38 C ANISOU 4520 CD1 PHE B 350 16078 12976 15546 3447 -3245 1235 C ATOM 4521 CD2 PHE B 350 -10.443 -15.930 -25.725 1.00117.20 C ANISOU 4521 CD2 PHE B 350 15335 13418 15779 3426 -2889 655 C ATOM 4522 CE1 PHE B 350 -10.486 -15.739 -22.974 1.00115.28 C ANISOU 4522 CE1 PHE B 350 15533 13117 15152 3458 -3341 1238 C ATOM 4523 CE2 PHE B 350 -9.858 -14.845 -25.100 1.00114.99 C ANISOU 4523 CE2 PHE B 350 14769 13526 15398 3417 -2977 677 C ATOM 4524 CZ PHE B 350 -9.880 -14.749 -23.723 1.00114.00 C ANISOU 4524 CZ PHE B 350 14862 13369 15086 3438 -3213 953 C ATOM 4525 N TYR B 351 -14.799 -17.824 -26.110 1.00104.26 N ANISOU 4525 N TYR B 351 14931 10743 13939 2387 -2442 1155 N ATOM 4526 CA TYR B 351 -15.984 -17.000 -26.328 1.00103.03 C ANISOU 4526 CA TYR B 351 14691 10810 13645 1940 -2193 1209 C ATOM 4527 C TYR B 351 -17.009 -17.186 -25.219 1.00102.90 C ANISOU 4527 C TYR B 351 15004 10641 13454 1665 -2168 1561 C ATOM 4528 O TYR B 351 -17.663 -16.230 -24.800 1.00101.32 O ANISOU 4528 O TYR B 351 14686 10725 13085 1412 -2023 1661 O ATOM 4529 CB TYR B 351 -16.627 -17.335 -27.678 1.00102.61 C ANISOU 4529 CB TYR B 351 14614 10661 13711 1749 -2027 992 C ATOM 4530 CG TYR B 351 -17.845 -16.496 -28.011 1.00102.06 C ANISOU 4530 CG TYR B 351 14416 10826 13535 1321 -1811 1031 C ATOM 4531 CD1 TYR B 351 -19.116 -16.880 -27.593 1.00102.53 C ANISOU 4531 CD1 TYR B 351 14717 10694 13546 983 -1733 1248 C ATOM 4532 CD2 TYR B 351 -17.726 -15.324 -28.743 1.00100.67 C ANISOU 4532 CD2 TYR B 351 13870 11059 13320 1255 -1689 857 C ATOM 4533 CE1 TYR B 351 -20.228 -16.117 -27.893 1.00101.96 C ANISOU 4533 CE1 TYR B 351 14476 10852 13412 629 -1552 1268 C ATOM 4534 CE2 TYR B 351 -18.833 -14.556 -29.048 1.00100.24 C ANISOU 4534 CE2 TYR B 351 13698 11196 13191 909 -1531 899 C ATOM 4535 CZ TYR B 351 -20.081 -14.957 -28.621 1.00100.81 C ANISOU 4535 CZ TYR B 351 13972 11091 13240 616 -1469 1093 C ATOM 4536 OH TYR B 351 -21.186 -14.195 -28.924 1.00100.62 O ANISOU 4536 OH TYR B 351 13781 11272 13176 306 -1327 1118 O ATOM 4537 N MET B 352 -17.147 -18.420 -24.751 1.00105.00 N ANISOU 4537 N MET B 352 15691 10446 13759 1714 -2296 1745 N ATOM 4538 CA MET B 352 -18.094 -18.727 -23.691 1.00104.97 C ANISOU 4538 CA MET B 352 16039 10273 13572 1427 -2249 2103 C ATOM 4539 C MET B 352 -17.719 -18.021 -22.396 1.00103.36 C ANISOU 4539 C MET B 352 15845 10323 13106 1509 -2336 2309 C ATOM 4540 O MET B 352 -18.575 -17.452 -21.722 1.00102.43 O ANISOU 4540 O MET B 352 15761 10386 12770 1206 -2162 2481 O ATOM 4541 CB MET B 352 -18.163 -20.238 -23.464 1.00117.84 C ANISOU 4541 CB MET B 352 18161 11309 15304 1480 -2401 2274 C ATOM 4542 CG MET B 352 -18.761 -21.012 -24.627 1.00119.95 C ANISOU 4542 CG MET B 352 18503 11273 15800 1308 -2306 2089 C ATOM 4543 SD MET B 352 -18.880 -22.780 -24.296 1.00122.90 S ANISOU 4543 SD MET B 352 19513 10875 16309 1338 -2496 2302 S ATOM 4544 CE MET B 352 -19.713 -23.342 -25.778 1.00125.35 C ANISOU 4544 CE MET B 352 19806 10965 16857 1044 -2342 2001 C ATOM 4545 N LEU B 353 -16.432 -18.040 -22.066 1.00 98.81 N ANISOU 4545 N LEU B 353 15215 9778 12552 1926 -2607 2263 N ATOM 4546 CA LEU B 353 -15.952 -17.458 -20.817 1.00 97.92 C ANISOU 4546 CA LEU B 353 15141 9884 12178 2033 -2760 2442 C ATOM 4547 C LEU B 353 -15.967 -15.931 -20.855 1.00 95.30 C ANISOU 4547 C LEU B 353 14396 10081 11734 1910 -2607 2282 C ATOM 4548 O LEU B 353 -16.344 -15.285 -19.877 1.00 94.10 O ANISOU 4548 O LEU B 353 14325 10127 11303 1751 -2555 2442 O ATOM 4549 CB LEU B 353 -14.549 -17.976 -20.484 1.00107.89 C ANISOU 4549 CB LEU B 353 16439 11021 13533 2530 -3146 2430 C ATOM 4550 CG LEU B 353 -13.983 -17.601 -19.112 1.00107.53 C ANISOU 4550 CG LEU B 353 16516 11138 13202 2671 -3399 2645 C ATOM 4551 CD1 LEU B 353 -13.276 -18.793 -18.489 1.00110.09 C ANISOU 4551 CD1 LEU B 353 17223 11049 13558 3030 -3785 2859 C ATOM 4552 CD2 LEU B 353 -13.031 -16.419 -19.216 1.00105.73 C ANISOU 4552 CD2 LEU B 353 15788 11390 12993 2840 -3480 2388 C ATOM 4553 N THR B 354 -15.551 -15.362 -21.983 1.00103.71 N ANISOU 4553 N THR B 354 15045 11359 13003 1980 -2531 1965 N ATOM 4554 CA THR B 354 -15.490 -13.911 -22.135 1.00101.59 C ANISOU 4554 CA THR B 354 14395 11541 12665 1868 -2405 1807 C ATOM 4555 C THR B 354 -16.873 -13.282 -22.036 1.00101.06 C ANISOU 4555 C THR B 354 14352 11588 12459 1465 -2115 1893 C ATOM 4556 O THR B 354 -17.058 -12.269 -21.362 1.00 99.91 O ANISOU 4556 O THR B 354 14125 11710 12124 1361 -2055 1924 O ATOM 4557 CB THR B 354 -14.862 -13.504 -23.480 1.00 94.69 C ANISOU 4557 CB THR B 354 13111 10840 12027 1970 -2347 1478 C ATOM 4558 OG1 THR B 354 -15.588 -14.117 -24.553 1.00 96.66 O ANISOU 4558 OG1 THR B 354 13416 10890 12422 1822 -2178 1394 O ATOM 4559 CG2 THR B 354 -13.410 -13.939 -23.545 1.00 95.20 C ANISOU 4559 CG2 THR B 354 13041 10885 12245 2388 -2606 1347 C ATOM 4560 N ASN B 355 -17.842 -13.885 -22.716 1.00115.47 N ANISOU 4560 N ASN B 355 16275 13209 14391 1248 -1944 1908 N ATOM 4561 CA ASN B 355 -19.202 -13.363 -22.723 1.00115.63 C ANISOU 4561 CA ASN B 355 16259 13343 14334 877 -1674 1969 C ATOM 4562 C ASN B 355 -19.965 -13.703 -21.446 1.00116.67 C ANISOU 4562 C ASN B 355 16724 13374 14229 694 -1602 2269 C ATOM 4563 O ASN B 355 -20.972 -13.070 -21.129 1.00116.60 O ANISOU 4563 O ASN B 355 16648 13545 14108 429 -1371 2320 O ATOM 4564 CB ASN B 355 -19.963 -13.851 -23.956 1.00107.85 C ANISOU 4564 CB ASN B 355 15213 12210 13554 689 -1543 1858 C ATOM 4565 CG ASN B 355 -19.547 -13.128 -25.222 1.00106.93 C ANISOU 4565 CG ASN B 355 14733 12314 13581 756 -1518 1569 C ATOM 4566 OD1 ASN B 355 -20.303 -12.324 -25.767 1.00105.93 O ANISOU 4566 OD1 ASN B 355 14392 12388 13467 545 -1361 1498 O ATOM 4567 ND2 ASN B 355 -18.337 -13.407 -25.694 1.00106.90 N ANISOU 4567 ND2 ASN B 355 14655 12279 13682 1055 -1673 1408 N ATOM 4568 N ALA B 356 -19.483 -14.706 -20.718 1.00108.12 N ANISOU 4568 N ALA B 356 16007 12007 13067 842 -1794 2469 N ATOM 4569 CA ALA B 356 -20.055 -15.038 -19.419 1.00109.20 C ANISOU 4569 CA ALA B 356 16513 12061 12917 675 -1741 2786 C ATOM 4570 C ALA B 356 -19.712 -13.940 -18.423 1.00108.31 C ANISOU 4570 C ALA B 356 16331 12305 12516 742 -1763 2794 C ATOM 4571 O ALA B 356 -20.531 -13.571 -17.583 1.00109.78 O ANISOU 4571 O ALA B 356 16634 12630 12446 506 -1557 2933 O ATOM 4572 CB ALA B 356 -19.534 -16.377 -18.930 1.00 79.38 C ANISOU 4572 CB ALA B 356 13182 7857 9122 843 -1991 3017 C ATOM 4573 N LEU B 357 -18.494 -13.418 -18.529 1.00102.32 N ANISOU 4573 N LEU B 357 15369 11702 11804 1056 -2003 2623 N ATOM 4574 CA LEU B 357 -18.045 -12.325 -17.676 1.00101.40 C ANISOU 4574 CA LEU B 357 15165 11919 11444 1123 -2069 2578 C ATOM 4575 C LEU B 357 -18.757 -11.024 -18.031 1.00100.31 C ANISOU 4575 C LEU B 357 14699 12094 11319 913 -1789 2387 C ATOM 4576 O LEU B 357 -18.871 -10.121 -17.202 1.00100.15 O ANISOU 4576 O LEU B 357 14681 12315 11055 858 -1734 2372 O ATOM 4577 CB LEU B 357 -16.528 -12.149 -17.782 1.00111.17 C ANISOU 4577 CB LEU B 357 16223 13238 12781 1489 -2416 2429 C ATOM 4578 CG LEU B 357 -15.680 -13.298 -17.232 1.00112.56 C ANISOU 4578 CG LEU B 357 16707 13134 12926 1780 -2767 2616 C ATOM 4579 CD1 LEU B 357 -14.206 -13.076 -17.530 1.00112.01 C ANISOU 4579 CD1 LEU B 357 16331 13190 13038 2148 -3085 2410 C ATOM 4580 CD2 LEU B 357 -15.908 -13.456 -15.736 1.00113.99 C ANISOU 4580 CD2 LEU B 357 17324 13303 12684 1714 -2854 2916 C ATOM 4581 N VAL B 358 -19.236 -10.936 -19.268 1.00113.94 N ANISOU 4581 N VAL B 358 16166 13801 13324 807 -1630 2235 N ATOM 4582 CA VAL B 358 -19.991 -9.773 -19.718 1.00113.22 C ANISOU 4582 CA VAL B 358 15776 13957 13285 623 -1391 2075 C ATOM 4583 C VAL B 358 -21.325 -9.691 -18.984 1.00115.03 C ANISOU 4583 C VAL B 358 16144 14230 13332 348 -1110 2221 C ATOM 4584 O VAL B 358 -21.747 -8.616 -18.556 1.00115.76 O ANISOU 4584 O VAL B 358 16112 14564 13305 274 -961 2138 O ATOM 4585 CB VAL B 358 -20.239 -9.820 -21.239 1.00 94.79 C ANISOU 4585 CB VAL B 358 13175 11576 11263 567 -1318 1911 C ATOM 4586 CG1 VAL B 358 -21.265 -8.775 -21.652 1.00 94.24 C ANISOU 4586 CG1 VAL B 358 12854 11707 11244 358 -1082 1811 C ATOM 4587 CG2 VAL B 358 -18.933 -9.626 -21.995 1.00 93.11 C ANISOU 4587 CG2 VAL B 358 12754 11415 11207 816 -1522 1720 C ATOM 4588 N TYR B 359 -21.979 -10.838 -18.833 1.00125.11 N ANISOU 4588 N TYR B 359 17677 15264 14596 192 -1028 2428 N ATOM 4589 CA TYR B 359 -23.264 -10.899 -18.147 1.00127.20 C ANISOU 4589 CA TYR B 359 18057 15575 14698 -107 -727 2581 C ATOM 4590 C TYR B 359 -23.102 -10.861 -16.628 1.00128.63 C ANISOU 4590 C TYR B 359 18569 15836 14468 -97 -724 2763 C ATOM 4591 O TYR B 359 -24.050 -10.559 -15.903 1.00130.67 O ANISOU 4591 O TYR B 359 18878 16248 14522 -315 -436 2833 O ATOM 4592 CB TYR B 359 -24.042 -12.138 -18.591 1.00120.85 C ANISOU 4592 CB TYR B 359 17397 14477 14045 -337 -632 2737 C ATOM 4593 CG TYR B 359 -24.429 -12.094 -20.050 1.00119.81 C ANISOU 4593 CG TYR B 359 16942 14313 14266 -404 -603 2542 C ATOM 4594 CD1 TYR B 359 -24.909 -10.924 -20.623 1.00118.89 C ANISOU 4594 CD1 TYR B 359 16432 14479 14261 -443 -474 2335 C ATOM 4595 CD2 TYR B 359 -24.312 -13.218 -20.857 1.00120.42 C ANISOU 4595 CD2 TYR B 359 17135 14065 14552 -421 -723 2559 C ATOM 4596 CE1 TYR B 359 -25.263 -10.872 -21.956 1.00118.17 C ANISOU 4596 CE1 TYR B 359 16078 14372 14450 -507 -479 2177 C ATOM 4597 CE2 TYR B 359 -24.663 -13.176 -22.194 1.00120.32 C ANISOU 4597 CE2 TYR B 359 16858 14045 14815 -493 -710 2366 C ATOM 4598 CZ TYR B 359 -25.138 -12.000 -22.737 1.00119.05 C ANISOU 4598 CZ TYR B 359 16312 14192 14728 -541 -594 2189 C ATOM 4599 OH TYR B 359 -25.490 -11.951 -24.066 1.00119.60 O ANISOU 4599 OH TYR B 359 16149 14264 15031 -616 -611 2018 O ATOM 4600 N VAL B 360 -21.898 -11.168 -16.153 1.00131.48 N ANISOU 4600 N VAL B 360 19147 16110 14699 162 -1048 2829 N ATOM 4601 CA VAL B 360 -21.567 -10.983 -14.747 1.00132.84 C ANISOU 4601 CA VAL B 360 19629 16400 14446 211 -1120 2968 C ATOM 4602 C VAL B 360 -21.494 -9.488 -14.461 1.00132.43 C ANISOU 4602 C VAL B 360 19326 16710 14283 253 -1045 2717 C ATOM 4603 O VAL B 360 -21.972 -9.010 -13.431 1.00134.01 O ANISOU 4603 O VAL B 360 19681 17098 14140 138 -869 2754 O ATOM 4604 CB VAL B 360 -20.219 -11.645 -14.385 1.00112.80 C ANISOU 4604 CB VAL B 360 17338 13686 11834 518 -1557 3082 C ATOM 4605 CG1 VAL B 360 -19.732 -11.169 -13.024 1.00113.56 C ANISOU 4605 CG1 VAL B 360 17683 13980 11483 600 -1699 3156 C ATOM 4606 CG2 VAL B 360 -20.347 -13.158 -14.406 1.00113.88 C ANISOU 4606 CG2 VAL B 360 17837 13411 12021 481 -1637 3371 C ATOM 4607 N SER B 361 -20.902 -8.755 -15.400 1.00121.04 N ANISOU 4607 N SER B 361 17511 15351 13128 404 -1166 2456 N ATOM 4608 CA SER B 361 -20.747 -7.309 -15.285 1.00120.64 C ANISOU 4608 CA SER B 361 17218 15582 13039 445 -1132 2203 C ATOM 4609 C SER B 361 -22.093 -6.591 -15.237 1.00122.09 C ANISOU 4609 C SER B 361 17264 15917 13208 225 -739 2121 C ATOM 4610 O SER B 361 -22.215 -5.523 -14.636 1.00123.31 O ANISOU 4610 O SER B 361 17377 16281 13193 229 -650 1968 O ATOM 4611 CB SER B 361 -19.909 -6.775 -16.450 1.00125.68 C ANISOU 4611 CB SER B 361 17492 16241 14018 600 -1311 1976 C ATOM 4612 OG SER B 361 -19.836 -5.360 -16.423 1.00125.35 O ANISOU 4612 OG SER B 361 17231 16422 13975 600 -1268 1745 O ATOM 4613 N ALA B 362 -23.100 -7.182 -15.873 1.00108.07 N ANISOU 4613 N ALA B 362 15405 14030 11626 41 -517 2205 N ATOM 4614 CA ALA B 362 -24.433 -6.588 -15.918 1.00109.65 C ANISOU 4614 CA ALA B 362 15407 14381 11875 -155 -153 2126 C ATOM 4615 C ALA B 362 -25.343 -7.148 -14.828 1.00112.31 C ANISOU 4615 C ALA B 362 16012 14756 11906 -373 132 2329 C ATOM 4616 O ALA B 362 -26.562 -6.983 -14.880 1.00113.80 O ANISOU 4616 O ALA B 362 16026 15049 12164 -571 467 2305 O ATOM 4617 CB ALA B 362 -25.058 -6.789 -17.289 1.00 70.36 C ANISOU 4617 CB ALA B 362 10123 9311 7301 -251 -86 2071 C ATOM 4618 N ALA B 363 -24.748 -7.812 -13.844 1.00109.42 N ANISOU 4618 N ALA B 363 16064 14316 11197 -341 -4 2535 N ATOM 4619 CA ALA B 363 -25.515 -8.411 -12.759 1.00112.03 C ANISOU 4619 CA ALA B 363 16719 14674 11172 -573 263 2772 C ATOM 4620 C ALA B 363 -24.874 -8.145 -11.403 1.00113.45 C ANISOU 4620 C ALA B 363 17272 14988 10844 -475 157 2828 C ATOM 4621 O ALA B 363 -25.503 -8.333 -10.360 1.00115.78 O ANISOU 4621 O ALA B 363 17842 15399 10752 -663 422 2975 O ATOM 4622 CB ALA B 363 -25.674 -9.907 -12.986 1.00111.01 C ANISOU 4622 CB ALA B 363 16836 14224 11120 -728 219 3080 C ATOM 4623 N ILE B 364 -23.620 -7.703 -11.424 1.00111.77 N ANISOU 4623 N ILE B 364 17064 14782 10623 -196 -230 2705 N ATOM 4624 CA ILE B 364 -22.851 -7.525 -10.197 1.00112.83 C ANISOU 4624 CA ILE B 364 17559 15026 10284 -82 -437 2756 C ATOM 4625 C ILE B 364 -23.219 -6.249 -9.432 1.00114.65 C ANISOU 4625 C ILE B 364 17748 15580 10234 -109 -216 2503 C ATOM 4626 O ILE B 364 -23.171 -6.226 -8.201 1.00116.46 O ANISOU 4626 O ILE B 364 18352 15946 9951 -150 -188 2584 O ATOM 4627 CB ILE B 364 -21.326 -7.559 -10.481 1.00144.21 C ANISOU 4627 CB ILE B 364 21515 18902 14376 222 -964 2707 C ATOM 4628 CG1 ILE B 364 -20.531 -7.618 -9.175 1.00145.67 C ANISOU 4628 CG1 ILE B 364 22119 19174 14057 330 -1246 2821 C ATOM 4629 CG2 ILE B 364 -20.899 -6.375 -11.341 1.00142.69 C ANISOU 4629 CG2 ILE B 364 20861 18832 14524 355 -1042 2347 C ATOM 4630 CD1 ILE B 364 -20.863 -8.818 -8.316 1.00147.76 C ANISOU 4630 CD1 ILE B 364 22904 19289 13950 198 -1210 3225 C ATOM 4631 N ASN B 365 -23.601 -5.201 -10.157 1.00106.12 N ANISOU 4631 N ASN B 365 16241 14606 9474 -82 -64 2195 N ATOM 4632 CA ASN B 365 -23.899 -3.906 -9.541 1.00108.33 C ANISOU 4632 CA ASN B 365 16459 15142 9558 -62 119 1901 C ATOM 4633 C ASN B 365 -24.993 -3.899 -8.461 1.00111.84 C ANISOU 4633 C ASN B 365 17120 15787 9588 -258 569 1941 C ATOM 4634 O ASN B 365 -24.779 -3.340 -7.385 1.00114.06 O ANISOU 4634 O ASN B 365 17661 16254 9425 -225 582 1826 O ATOM 4635 CB ASN B 365 -24.160 -2.833 -10.604 1.00150.06 C ANISOU 4635 CB ASN B 365 21262 20446 15309 13 185 1595 C ATOM 4636 CG ASN B 365 -22.902 -2.433 -11.345 1.00147.45 C ANISOU 4636 CG ASN B 365 20768 20015 15241 204 -242 1475 C ATOM 4637 OD1 ASN B 365 -22.504 -3.083 -12.311 1.00144.56 O ANISOU 4637 OD1 ASN B 365 20261 19477 15187 241 -418 1589 O ATOM 4638 ND2 ASN B 365 -22.266 -1.361 -10.891 1.00148.13 N ANISOU 4638 ND2 ASN B 365 20871 20215 15198 312 -398 1229 N ATOM 4639 N PRO B 366 -26.163 -4.508 -8.736 1.00119.33 N ANISOU 4639 N PRO B 366 17954 16717 10667 -478 946 2088 N ATOM 4640 CA PRO B 366 -27.163 -4.560 -7.661 1.00122.47 C ANISOU 4640 CA PRO B 366 18549 17338 10646 -689 1408 2137 C ATOM 4641 C PRO B 366 -26.680 -5.389 -6.472 1.00123.36 C ANISOU 4641 C PRO B 366 19260 17447 10163 -776 1301 2446 C ATOM 4642 O PRO B 366 -27.066 -5.116 -5.335 1.00125.79 O ANISOU 4642 O PRO B 366 19837 17996 9961 -876 1574 2415 O ATOM 4643 CB PRO B 366 -28.361 -5.243 -8.329 1.00135.93 C ANISOU 4643 CB PRO B 366 19984 18985 12677 -935 1756 2281 C ATOM 4644 CG PRO B 366 -28.176 -4.992 -9.785 1.00133.54 C ANISOU 4644 CG PRO B 366 19244 18513 12983 -798 1533 2146 C ATOM 4645 CD PRO B 366 -26.699 -5.043 -10.000 1.00131.36 C ANISOU 4645 CD PRO B 366 19135 18063 12711 -563 1004 2165 C ATOM 4646 N ILE B 367 -25.844 -6.388 -6.739 1.00145.62 N ANISOU 4646 N ILE B 367 22297 19991 13039 -724 904 2735 N ATOM 4647 CA ILE B 367 -25.260 -7.198 -5.677 1.00146.25 C ANISOU 4647 CA ILE B 367 22968 20017 12584 -758 700 3059 C ATOM 4648 C ILE B 367 -24.282 -6.352 -4.869 1.00146.86 C ANISOU 4648 C ILE B 367 23247 20273 12280 -538 389 2861 C ATOM 4649 O ILE B 367 -24.224 -6.454 -3.644 1.00149.07 O ANISOU 4649 O ILE B 367 23993 20704 11943 -613 421 2981 O ATOM 4650 CB ILE B 367 -24.531 -8.437 -6.237 1.00130.37 C ANISOU 4650 CB ILE B 367 21111 17626 10798 -687 294 3385 C ATOM 4651 CG1 ILE B 367 -25.473 -9.261 -7.116 1.00129.93 C ANISOU 4651 CG1 ILE B 367 20854 17364 11149 -920 567 3543 C ATOM 4652 CG2 ILE B 367 -23.978 -9.292 -5.106 1.00131.49 C ANISOU 4652 CG2 ILE B 367 21895 17683 10381 -707 59 3756 C ATOM 4653 CD1 ILE B 367 -24.826 -10.491 -7.721 1.00128.05 C ANISOU 4653 CD1 ILE B 367 20777 16713 11163 -846 196 3821 C ATOM 4654 N LEU B 368 -23.519 -5.513 -5.564 1.00130.42 N ANISOU 4654 N LEU B 368 20823 18179 10554 -293 88 2557 N ATOM 4655 CA LEU B 368 -22.563 -4.627 -4.908 1.00130.75 C ANISOU 4655 CA LEU B 368 20990 18378 10309 -107 -235 2322 C ATOM 4656 C LEU B 368 -23.260 -3.571 -4.056 1.00133.60 C ANISOU 4656 C LEU B 368 21416 19046 10300 -190 142 2027 C ATOM 4657 O LEU B 368 -22.790 -3.240 -2.971 1.00135.03 O ANISOU 4657 O LEU B 368 21965 19396 9945 -157 -3 1963 O ATOM 4658 CB LEU B 368 -21.650 -3.947 -5.932 1.00120.68 C ANISOU 4658 CB LEU B 368 19292 17013 9547 121 -595 2063 C ATOM 4659 CG LEU B 368 -20.662 -4.837 -6.686 1.00117.94 C ANISOU 4659 CG LEU B 368 18878 16408 9526 275 -1039 2269 C ATOM 4660 CD1 LEU B 368 -19.779 -3.998 -7.595 1.00115.39 C ANISOU 4660 CD1 LEU B 368 18127 16073 9644 461 -1326 1972 C ATOM 4661 CD2 LEU B 368 -19.819 -5.648 -5.715 1.00118.35 C ANISOU 4661 CD2 LEU B 368 19415 16420 9133 358 -1428 2552 C ATOM 4662 N TYR B 369 -24.378 -3.047 -4.550 1.00129.70 N ANISOU 4662 N TYR B 369 20562 18627 10092 -282 612 1832 N ATOM 4663 CA TYR B 369 -25.125 -2.025 -3.823 1.00132.69 C ANISOU 4663 CA TYR B 369 20946 19282 10186 -324 1015 1508 C ATOM 4664 C TYR B 369 -25.658 -2.563 -2.499 1.00135.47 C ANISOU 4664 C TYR B 369 21793 19840 9839 -532 1328 1703 C ATOM 4665 O TYR B 369 -25.660 -1.861 -1.488 1.00137.62 O ANISOU 4665 O TYR B 369 22322 20352 9614 -518 1438 1474 O ATOM 4666 CB TYR B 369 -26.291 -1.494 -4.661 1.00112.70 C ANISOU 4666 CB TYR B 369 17898 16776 8147 -361 1452 1299 C ATOM 4667 CG TYR B 369 -25.904 -0.857 -5.978 1.00110.53 C ANISOU 4667 CG TYR B 369 17154 16317 8525 -180 1196 1103 C ATOM 4668 CD1 TYR B 369 -24.632 -0.337 -6.179 1.00108.73 C ANISOU 4668 CD1 TYR B 369 16944 15994 8376 6 700 971 C ATOM 4669 CD2 TYR B 369 -26.823 -0.761 -7.016 1.00110.05 C ANISOU 4669 CD2 TYR B 369 16631 16197 8988 -215 1452 1054 C ATOM 4670 CE1 TYR B 369 -24.283 0.251 -7.382 1.00106.98 C ANISOU 4670 CE1 TYR B 369 16313 15615 8717 133 501 812 C ATOM 4671 CE2 TYR B 369 -26.483 -0.175 -8.219 1.00108.32 C ANISOU 4671 CE2 TYR B 369 16029 15816 9314 -67 1220 900 C ATOM 4672 CZ TYR B 369 -25.213 0.329 -8.397 1.00106.94 C ANISOU 4672 CZ TYR B 369 15903 15543 9185 97 763 787 C ATOM 4673 OH TYR B 369 -24.872 0.913 -9.596 1.00105.57 O ANISOU 4673 OH TYR B 369 15370 15218 9522 208 562 656 O ATOM 4674 N ASN B 370 -26.108 -3.813 -2.514 1.00144.86 N ANISOU 4674 N ASN B 370 23138 20926 10977 -743 1474 2125 N ATOM 4675 CA ASN B 370 -26.668 -4.442 -1.323 1.00147.46 C ANISOU 4675 CA ASN B 370 23956 21430 10644 -998 1806 2382 C ATOM 4676 C ASN B 370 -25.635 -4.713 -0.234 1.00148.15 C ANISOU 4676 C ASN B 370 24666 21551 10074 -938 1389 2556 C ATOM 4677 O ASN B 370 -25.898 -4.490 0.944 1.00151.21 O ANISOU 4677 O ASN B 370 25450 22210 9793 -1052 1623 2519 O ATOM 4678 CB ASN B 370 -27.380 -5.746 -1.690 1.00183.19 C ANISOU 4678 CB ASN B 370 28495 25778 15329 -1274 2036 2816 C ATOM 4679 CG ASN B 370 -28.829 -5.531 -2.078 1.00184.51 C ANISOU 4679 CG ASN B 370 28219 26101 15787 -1479 2676 2676 C ATOM 4680 OD1 ASN B 370 -29.221 -4.435 -2.478 1.00184.54 O ANISOU 4680 OD1 ASN B 370 27775 26248 16092 -1336 2853 2254 O ATOM 4681 ND2 ASN B 370 -29.634 -6.579 -1.956 1.00185.72 N ANISOU 4681 ND2 ASN B 370 28486 26213 15864 -1820 3011 3034 N ATOM 4682 N LEU B 371 -24.457 -5.182 -0.631 1.00149.97 N ANISOU 4682 N LEU B 371 24971 21523 10489 -749 767 2731 N ATOM 4683 CA LEU B 371 -23.430 -5.584 0.329 1.00150.82 C ANISOU 4683 CA LEU B 371 25648 21632 10027 -669 287 2950 C ATOM 4684 C LEU B 371 -22.942 -4.444 1.224 1.00152.66 C ANISOU 4684 C LEU B 371 26038 22157 9808 -550 150 2570 C ATOM 4685 O LEU B 371 -22.791 -4.614 2.433 1.00156.39 O ANISOU 4685 O LEU B 371 26808 22809 9803 -591 104 2649 O ATOM 4686 CB LEU B 371 -22.243 -6.221 -0.399 1.00169.44 C ANISOU 4686 CB LEU B 371 27928 23662 12789 -433 -363 3143 C ATOM 4687 CG LEU B 371 -22.197 -7.751 -0.432 1.00169.62 C ANISOU 4687 CG LEU B 371 28152 23387 12908 -503 -489 3655 C ATOM 4688 CD1 LEU B 371 -23.449 -8.327 -1.075 1.00169.60 C ANISOU 4688 CD1 LEU B 371 28039 23259 13144 -790 47 3832 C ATOM 4689 CD2 LEU B 371 -20.949 -8.230 -1.159 1.00166.91 C ANISOU 4689 CD2 LEU B 371 27679 22749 12990 -204 -1128 3747 C ATOM 4690 N VAL B 372 -22.699 -3.286 0.629 1.00201.74 N ANISOU 4690 N VAL B 372 31823 28411 16416 -378 78 2111 N ATOM 4691 CA VAL B 372 -22.132 -2.155 1.355 1.00203.36 C ANISOU 4691 CA VAL B 372 32167 28835 16266 -263 -119 1711 C ATOM 4692 C VAL B 372 -23.163 -1.241 2.034 1.00206.59 C ANISOU 4692 C VAL B 372 32627 29541 16327 -379 477 1348 C ATOM 4693 O VAL B 372 -23.112 -1.040 3.246 1.00210.06 O ANISOU 4693 O VAL B 372 33485 30224 16106 -437 511 1274 O ATOM 4694 CB VAL B 372 -21.219 -1.344 0.435 1.00161.56 C ANISOU 4694 CB VAL B 372 26415 23404 11568 -30 -548 1399 C ATOM 4695 CG1 VAL B 372 -21.917 -1.102 -0.873 1.00160.16 C ANISOU 4695 CG1 VAL B 372 25648 23074 12133 -23 -232 1285 C ATOM 4696 CG2 VAL B 372 -20.771 -0.049 1.107 1.00163.29 C ANISOU 4696 CG2 VAL B 372 26730 23820 11492 47 -695 926 C ATOM 4697 N SER B 373 -24.088 -0.686 1.255 1.00164.69 N ANISOU 4697 N SER B 373 26821 24220 11534 -385 928 1102 N ATOM 4698 CA SER B 373 -25.068 0.260 1.780 1.00167.28 C ANISOU 4698 CA SER B 373 27105 24810 11645 -432 1493 697 C ATOM 4699 C SER B 373 -26.147 -0.435 2.603 1.00170.08 C ANISOU 4699 C SER B 373 27756 25395 11471 -701 2086 929 C ATOM 4700 O SER B 373 -26.958 -1.191 2.070 1.00169.55 O ANISOU 4700 O SER B 373 27463 25257 11699 -862 2422 1203 O ATOM 4701 CB SER B 373 -25.710 1.062 0.645 1.00174.34 C ANISOU 4701 CB SER B 373 27346 25597 13298 -320 1743 379 C ATOM 4702 OG SER B 373 -26.650 1.995 1.150 1.00177.29 O ANISOU 4702 OG SER B 373 27654 26204 13504 -313 2274 -37 O ATOM 4703 N ALA B 374 -26.147 -0.171 3.907 1.00169.77 N ANISOU 4703 N ALA B 374 28168 25638 10698 -759 2201 809 N ATOM 4704 CA ALA B 374 -27.116 -0.773 4.814 1.00173.99 C ANISOU 4704 CA ALA B 374 28810 26422 10875 -973 2720 1008 C ATOM 4705 C ALA B 374 -28.525 -0.233 4.575 1.00175.17 C ANISOU 4705 C ALA B 374 28589 26758 11209 -1050 3492 710 C ATOM 4706 O ALA B 374 -29.503 -0.974 4.678 1.00177.58 O ANISOU 4706 O ALA B 374 28775 27158 11538 -1268 3961 975 O ATOM 4707 CB ALA B 374 -26.698 -0.546 6.258 1.00149.04 C ANISOU 4707 CB ALA B 374 26046 23523 7058 -943 2575 915 C ATOM 4708 N ASN B 375 -28.629 1.054 4.251 1.00222.43 N ANISOU 4708 N ASN B 375 34365 32781 17366 -865 3611 151 N ATOM 4709 CA ASN B 375 -29.928 1.650 3.949 1.00223.81 C ANISOU 4709 CA ASN B 375 34090 33115 17834 -867 4301 -182 C ATOM 4710 C ASN B 375 -30.545 1.100 2.669 1.00221.72 C ANISOU 4710 C ASN B 375 33231 32645 18369 -918 4412 56 C ATOM 4711 O ASN B 375 -31.759 0.919 2.588 1.00222.73 O ANISOU 4711 O ASN B 375 33047 32947 18632 -1065 5019 51 O ATOM 4712 CB ASN B 375 -29.836 3.180 3.849 1.00192.53 C ANISOU 4712 CB ASN B 375 29901 29148 14104 -557 4266 -834 C ATOM 4713 CG ASN B 375 -29.477 3.840 5.167 1.00195.40 C ANISOU 4713 CG ASN B 375 30751 29752 13741 -498 4245 -1166 C ATOM 4714 OD1 ASN B 375 -30.356 4.158 5.966 1.00199.32 O ANISOU 4714 OD1 ASN B 375 31196 30546 13991 -492 4759 -1394 O ATOM 4715 ND2 ASN B 375 -28.192 4.068 5.394 1.00194.13 N ANISOU 4715 ND2 ASN B 375 30929 29458 13374 -406 3583 -1193 N ATOM 4716 N PHE B 376 -29.709 0.835 1.671 1.00226.53 N ANISOU 4716 N PHE B 376 33671 32902 19499 -805 3828 248 N ATOM 4717 CA PHE B 376 -30.201 0.383 0.374 1.00224.38 C ANISOU 4717 CA PHE B 376 32850 32417 19989 -833 3865 431 C ATOM 4718 C PHE B 376 -30.676 -1.070 0.368 1.00223.50 C ANISOU 4718 C PHE B 376 32855 32283 19784 -1164 4059 974 C ATOM 4719 O PHE B 376 -31.742 -1.369 -0.168 1.00223.63 O ANISOU 4719 O PHE B 376 32454 32340 20176 -1311 4476 1031 O ATOM 4720 CB PHE B 376 -29.117 0.571 -0.693 1.00176.09 C ANISOU 4720 CB PHE B 376 26540 25948 14420 -613 3199 443 C ATOM 4721 CG PHE B 376 -29.546 0.169 -2.079 1.00173.95 C ANISOU 4721 CG PHE B 376 25733 25455 14906 -625 3192 598 C ATOM 4722 CD1 PHE B 376 -30.234 1.056 -2.890 1.00174.14 C ANISOU 4722 CD1 PHE B 376 25204 25463 15498 -476 3386 267 C ATOM 4723 CD2 PHE B 376 -29.259 -1.095 -2.573 1.00171.65 C ANISOU 4723 CD2 PHE B 376 25514 24956 14748 -776 2968 1068 C ATOM 4724 CE1 PHE B 376 -30.627 0.691 -4.166 1.00172.03 C ANISOU 4724 CE1 PHE B 376 24469 25010 15884 -495 3347 409 C ATOM 4725 CE2 PHE B 376 -29.654 -1.466 -3.845 1.00169.30 C ANISOU 4725 CE2 PHE B 376 24754 24462 15112 -799 2953 1180 C ATOM 4726 CZ PHE B 376 -30.337 -0.571 -4.642 1.00169.61 C ANISOU 4726 CZ PHE B 376 24247 24521 15678 -668 3137 854 C ATOM 4727 N ARG B 377 -29.894 -1.965 0.969 1.00226.94 N ANISOU 4727 N ARG B 377 33857 32640 19728 -1285 3738 1370 N ATOM 4728 CA ARG B 377 -30.180 -3.399 0.896 1.00226.33 C ANISOU 4728 CA ARG B 377 33956 32438 19602 -1590 3816 1925 C ATOM 4729 C ARG B 377 -31.507 -3.821 1.523 1.00229.53 C ANISOU 4729 C ARG B 377 34364 33130 19719 -1936 4553 2038 C ATOM 4730 O ARG B 377 -32.196 -4.694 0.995 1.00229.23 O ANISOU 4730 O ARG B 377 34104 32983 20010 -2181 4766 2335 O ATOM 4731 CB ARG B 377 -29.040 -4.218 1.515 1.00193.68 C ANISOU 4731 CB ARG B 377 30479 28146 14965 -1607 3288 2324 C ATOM 4732 CG ARG B 377 -28.844 -4.043 3.016 1.00198.02 C ANISOU 4732 CG ARG B 377 31425 28967 14845 -1585 3295 2279 C ATOM 4733 CD ARG B 377 -27.625 -4.816 3.490 1.00199.24 C ANISOU 4733 CD ARG B 377 32013 28926 14763 -1494 2630 2639 C ATOM 4734 NE ARG B 377 -27.424 -4.729 4.932 1.00206.04 N ANISOU 4734 NE ARG B 377 33255 30052 14979 -1492 2608 2633 N ATOM 4735 CZ ARG B 377 -26.498 -5.416 5.594 1.00209.22 C ANISOU 4735 CZ ARG B 377 34043 30357 15094 -1433 2101 2949 C ATOM 4736 NH1 ARG B 377 -25.690 -6.240 4.940 1.00205.87 N ANISOU 4736 NH1 ARG B 377 33650 29566 15004 -1346 1584 3276 N ATOM 4737 NH2 ARG B 377 -26.380 -5.280 6.907 1.00216.12 N ANISOU 4737 NH2 ARG B 377 35259 31502 15356 -1447 2112 2925 N ATOM 4738 N GLN B 378 -31.862 -3.213 2.649 1.00195.64 N ANISOU 4738 N GLN B 378 30183 29177 14974 -1891 4859 1780 N ATOM 4739 CA GLN B 378 -33.077 -3.597 3.352 1.00201.39 C ANISOU 4739 CA GLN B 378 30789 30181 15551 -2125 5476 1871 C ATOM 4740 C GLN B 378 -34.297 -3.089 2.588 1.00199.76 C ANISOU 4740 C GLN B 378 29908 30116 15874 -2167 6033 1572 C ATOM 4741 O GLN B 378 -35.308 -3.782 2.475 1.00202.24 O ANISOU 4741 O GLN B 378 29943 30495 16405 -2430 6434 1788 O ATOM 4742 CB GLN B 378 -33.072 -3.082 4.791 1.00204.01 C ANISOU 4742 CB GLN B 378 31449 30846 15219 -2044 5633 1670 C ATOM 4743 CG GLN B 378 -34.178 -3.676 5.643 1.00211.77 C ANISOU 4743 CG GLN B 378 32418 32098 15949 -2308 6211 1867 C ATOM 4744 CD GLN B 378 -34.022 -5.181 5.812 1.00213.88 C ANISOU 4744 CD GLN B 378 33002 32141 16121 -2593 6028 2519 C ATOM 4745 OE1 GLN B 378 -32.913 -5.714 5.740 1.00212.09 O ANISOU 4745 OE1 GLN B 378 33156 31624 15804 -2529 5419 2803 O ATOM 4746 NE2 GLN B 378 -35.134 -5.872 6.031 1.00218.54 N ANISOU 4746 NE2 GLN B 378 33419 32851 16764 -2897 6543 2748 N ATOM 4747 N VAL B 379 -34.188 -1.871 2.067 1.00209.23 N ANISOU 4747 N VAL B 379 30833 31355 17308 -1900 6032 1065 N ATOM 4748 CA VAL B 379 -35.253 -1.271 1.271 1.00209.48 C ANISOU 4748 CA VAL B 379 30172 31508 17914 -1863 6483 733 C ATOM 4749 C VAL B 379 -35.344 -1.994 -0.072 1.00206.57 C ANISOU 4749 C VAL B 379 29389 30809 18288 -1937 6210 1031 C ATOM 4750 O VAL B 379 -36.417 -2.097 -0.671 1.00206.78 O ANISOU 4750 O VAL B 379 28851 30924 18794 -2052 6581 991 O ATOM 4751 CB VAL B 379 -35.024 0.246 1.070 1.00175.84 C ANISOU 4751 CB VAL B 379 25653 27251 13907 -1415 6347 129 C ATOM 4752 CG1 VAL B 379 -36.096 0.850 0.174 1.00175.86 C ANISOU 4752 CG1 VAL B 379 24865 27300 14653 -1274 6663 -176 C ATOM 4753 CG2 VAL B 379 -34.992 0.957 2.415 1.00179.01 C ANISOU 4753 CG2 VAL B 379 26461 27968 13587 -1337 6619 -208 C ATOM 4754 N PHE B 380 -34.206 -2.510 -0.526 1.00201.16 N ANISOU 4754 N PHE B 380 28987 29759 17686 -1869 5556 1317 N ATOM 4755 CA PHE B 380 -34.137 -3.309 -1.744 1.00198.19 C ANISOU 4755 CA PHE B 380 28334 29045 17925 -1944 5253 1616 C ATOM 4756 C PHE B 380 -34.989 -4.565 -1.601 1.00198.90 C ANISOU 4756 C PHE B 380 28465 29175 17932 -2407 5642 2038 C ATOM 4757 O PHE B 380 -35.778 -4.898 -2.486 1.00198.12 O ANISOU 4757 O PHE B 380 27863 29018 18394 -2545 5799 2086 O ATOM 4758 CB PHE B 380 -32.683 -3.692 -2.032 1.00177.34 C ANISOU 4758 CB PHE B 380 26074 26044 15261 -1785 4520 1840 C ATOM 4759 CG PHE B 380 -32.489 -4.469 -3.304 1.00174.24 C ANISOU 4759 CG PHE B 380 25433 25291 15481 -1816 4180 2097 C ATOM 4760 CD1 PHE B 380 -32.301 -3.816 -4.510 1.00171.92 C ANISOU 4760 CD1 PHE B 380 24648 24837 15835 -1554 3905 1847 C ATOM 4761 CD2 PHE B 380 -32.471 -5.854 -3.287 1.00173.82 C ANISOU 4761 CD2 PHE B 380 25676 25039 15329 -2111 4126 2587 C ATOM 4762 CE1 PHE B 380 -32.112 -4.532 -5.677 1.00169.37 C ANISOU 4762 CE1 PHE B 380 24125 24203 16025 -1586 3603 2059 C ATOM 4763 CE2 PHE B 380 -32.284 -6.575 -4.450 1.00170.85 C ANISOU 4763 CE2 PHE B 380 25098 24317 15500 -2130 3815 2783 C ATOM 4764 CZ PHE B 380 -32.102 -5.913 -5.646 1.00168.72 C ANISOU 4764 CZ PHE B 380 24330 23929 15846 -1867 3561 2507 C ATOM 4765 N LEU B 381 -34.824 -5.255 -0.477 1.00177.73 N ANISOU 4765 N LEU B 381 26405 26589 14536 -2664 5781 2351 N ATOM 4766 CA LEU B 381 -35.570 -6.479 -0.207 1.00180.23 C ANISOU 4766 CA LEU B 381 26736 26863 14879 -3021 6019 2774 C ATOM 4767 C LEU B 381 -37.038 -6.196 0.101 1.00184.59 C ANISOU 4767 C LEU B 381 26783 27791 15562 -3172 6712 2571 C ATOM 4768 O LEU B 381 -37.904 -7.035 -0.145 1.00186.50 O ANISOU 4768 O LEU B 381 26772 27999 16090 -3484 6962 2819 O ATOM 4769 CB LEU B 381 -34.927 -7.249 0.948 1.00174.62 C ANISOU 4769 CB LEU B 381 26702 26073 13572 -3076 5784 3147 C ATOM 4770 CG LEU B 381 -33.492 -7.726 0.713 1.00171.26 C ANISOU 4770 CG LEU B 381 26754 25256 13060 -2913 5055 3405 C ATOM 4771 CD1 LEU B 381 -32.970 -8.486 1.923 1.00176.86 C ANISOU 4771 CD1 LEU B 381 28066 25924 13208 -2956 4848 3763 C ATOM 4772 CD2 LEU B 381 -33.404 -8.579 -0.545 1.00166.94 C ANISOU 4772 CD2 LEU B 381 26046 24303 13082 -3034 4805 3671 C ATOM 4773 N SER B 382 -37.313 -5.013 0.642 1.00260.94 N ANISOU 4773 N SER B 382 36298 37805 25043 -2937 7004 2104 N ATOM 4774 CA SER B 382 -38.683 -4.611 0.936 1.00266.00 C ANISOU 4774 CA SER B 382 36413 38817 25838 -2995 7648 1851 C ATOM 4775 C SER B 382 -39.426 -4.335 -0.363 1.00262.25 C ANISOU 4775 C SER B 382 35185 38321 26135 -2992 7777 1653 C ATOM 4776 O SER B 382 -40.624 -4.596 -0.476 1.00265.34 O ANISOU 4776 O SER B 382 35077 38888 26852 -3176 8195 1661 O ATOM 4777 CB SER B 382 -38.710 -3.373 1.834 1.00169.82 C ANISOU 4777 CB SER B 382 24286 26964 13272 -2684 7880 1365 C ATOM 4778 OG SER B 382 -38.307 -2.217 1.120 1.00164.63 O ANISOU 4778 OG SER B 382 23389 26258 12905 -2340 7699 905 O ATOM 4779 N THR B 383 -38.702 -3.805 -1.342 1.00216.39 N ANISOU 4779 N THR B 383 29288 32310 20622 -2781 7395 1476 N ATOM 4780 CA THR B 383 -39.269 -3.535 -2.654 1.00214.60 C ANISOU 4780 CA THR B 383 28343 32004 21191 -2698 7353 1308 C ATOM 4781 C THR B 383 -39.275 -4.820 -3.478 1.00212.22 C ANISOU 4781 C THR B 383 28021 31389 21225 -3025 7105 1773 C ATOM 4782 O THR B 383 -39.950 -4.912 -4.505 1.00210.99 O ANISOU 4782 O THR B 383 27273 31181 21715 -3068 7103 1729 O ATOM 4783 CB THR B 383 -38.470 -2.443 -3.396 1.00206.69 C ANISOU 4783 CB THR B 383 27196 30773 20564 -2174 6807 969 C ATOM 4784 OG1 THR B 383 -38.106 -1.405 -2.476 1.00208.76 O ANISOU 4784 OG1 THR B 383 27724 31220 20376 -1897 6902 605 O ATOM 4785 CG2 THR B 383 -39.290 -1.844 -4.531 1.00206.02 C ANISOU 4785 CG2 THR B 383 26316 30696 21266 -1992 6841 694 C ATOM 4786 N LEU B 384 -38.528 -5.819 -3.015 1.00217.97 N ANISOU 4786 N LEU B 384 29415 31896 21506 -3249 6881 2214 N ATOM 4787 CA LEU B 384 -38.462 -7.100 -3.708 1.00215.88 C ANISOU 4787 CA LEU B 384 29231 31280 21514 -3557 6634 2658 C ATOM 4788 C LEU B 384 -39.724 -7.914 -3.453 1.00219.56 C ANISOU 4788 C LEU B 384 29424 31870 22130 -3945 7079 2860 C ATOM 4789 O LEU B 384 -40.249 -8.564 -4.357 1.00219.13 O ANISOU 4789 O LEU B 384 29021 31652 22585 -4180 7044 2999 O ATOM 4790 CB LEU B 384 -37.223 -7.882 -3.258 1.00168.33 C ANISOU 4790 CB LEU B 384 24005 24925 15027 -3573 6171 3052 C ATOM 4791 CG LEU B 384 -36.830 -9.147 -4.025 1.00166.03 C ANISOU 4791 CG LEU B 384 23899 24159 15027 -3764 5764 3477 C ATOM 4792 CD1 LEU B 384 -35.319 -9.283 -4.070 1.00163.98 C ANISOU 4792 CD1 LEU B 384 24151 23549 14606 -3442 5084 3603 C ATOM 4793 CD2 LEU B 384 -37.450 -10.384 -3.388 1.00170.26 C ANISOU 4793 CD2 LEU B 384 24642 24609 15438 -4139 5975 3882 C ATOM 4794 N ALA B 385 -40.211 -7.863 -2.217 1.00198.77 N ANISOU 4794 N ALA B 385 26938 29521 19064 -3998 7470 2861 N ATOM 4795 CA ALA B 385 -41.447 -8.540 -1.847 1.00204.97 C ANISOU 4795 CA ALA B 385 27446 30470 19962 -4346 7927 3028 C ATOM 4796 C ALA B 385 -42.624 -7.844 -2.514 1.00205.46 C ANISOU 4796 C ALA B 385 26638 30820 20609 -4299 8279 2651 C ATOM 4797 O ALA B 385 -43.545 -8.488 -3.016 1.00207.11 O ANISOU 4797 O ALA B 385 26419 31013 21260 -4593 8435 2782 O ATOM 4798 CB ALA B 385 -41.616 -8.560 -0.339 1.00160.29 C ANISOU 4798 CB ALA B 385 22172 25080 13650 -4390 8264 3101 C ATOM 4799 N CYS B 386 -42.577 -6.516 -2.505 1.00236.74 N ANISOU 4799 N CYS B 386 30339 35029 24582 -3906 8374 2172 N ATOM 4800 CA CYS B 386 -43.600 -5.692 -3.135 1.00236.96 C ANISOU 4800 CA CYS B 386 29533 35315 25184 -3745 8641 1766 C ATOM 4801 C CYS B 386 -43.595 -5.851 -4.652 1.00230.75 C ANISOU 4801 C CYS B 386 28313 34290 25072 -3777 8295 1768 C ATOM 4802 O CYS B 386 -42.623 -6.336 -5.231 1.00225.47 O ANISOU 4802 O CYS B 386 28018 33266 24383 -3836 7840 1993 O ATOM 4803 CB CYS B 386 -43.410 -4.222 -2.753 1.00235.60 C ANISOU 4803 CB CYS B 386 29273 35387 24858 -3268 8756 1245 C ATOM 4804 SG CYS B 386 -44.666 -3.104 -3.411 1.00236.73 S ANISOU 4804 SG CYS B 386 28407 35827 25714 -2961 9054 719 S TER 4805 CYS B 386 ATOM 4806 N GLY C 7 -38.693 42.615 -35.574 1.00131.65 N ATOM 4807 CA GLY C 7 -38.225 41.459 -34.832 1.00135.62 C ATOM 4808 C GLY C 7 -37.938 40.273 -35.732 1.00143.84 C ATOM 4809 O GLY C 7 -38.728 39.950 -36.618 1.00163.61 O ATOM 4810 N ARG C 8 -36.801 39.624 -35.500 1.00202.09 N ATOM 4811 CA ARG C 8 -36.370 38.497 -36.321 1.00185.68 C ATOM 4812 C ARG C 8 -35.357 37.630 -35.577 1.00169.85 C ATOM 4813 O ARG C 8 -34.678 38.096 -34.661 1.00153.24 O ATOM 4814 CB ARG C 8 -35.798 38.982 -37.655 1.00147.88 C ATOM 4815 CG ARG C 8 -34.881 40.186 -37.562 1.00159.02 C ATOM 4816 CD ARG C 8 -34.254 40.481 -38.915 1.00151.37 C ATOM 4817 NE ARG C 8 -33.547 41.758 -38.931 1.00151.87 N ATOM 4818 CZ ARG C 8 -32.920 42.249 -39.995 1.00162.79 C ATOM 4819 NH1 ARG C 8 -32.914 41.571 -41.134 1.00166.86 N ATOM 4820 NH2 ARG C 8 -32.301 43.419 -39.922 1.00175.50 N ATOM 4821 N ARG C 9 -35.261 36.368 -35.983 1.00141.76 N ATOM 4822 CA ARG C 9 -34.341 35.421 -35.364 1.00137.67 C ATOM 4823 C ARG C 9 -33.162 35.108 -36.278 1.00127.34 C ATOM 4824 O ARG C 9 -33.338 34.927 -37.483 1.00130.66 O ATOM 4825 CB ARG C 9 -35.083 34.125 -35.027 1.00115.62 C ATOM 4826 CG ARG C 9 -34.191 32.975 -34.591 1.00121.60 C ATOM 4827 CD ARG C 9 -35.015 31.752 -34.237 1.00134.05 C ATOM 4828 NE ARG C 9 -34.283 30.810 -33.396 1.00138.79 N ATOM 4829 CZ ARG C 9 -34.509 30.640 -32.098 1.00137.55 C ATOM 4830 NH1 ARG C 9 -35.453 31.345 -31.489 1.00151.67 N ATOM 4831 NH2 ARG C 9 -33.797 29.760 -31.408 1.00135.94 N ATOM 4832 N PRO C 10 -31.949 35.056 -35.702 1.00149.32 N ATOM 4833 CA PRO C 10 -30.734 34.697 -36.440 1.00144.66 C ATOM 4834 C PRO C 10 -30.849 33.330 -37.104 1.00128.90 C ATOM 4835 O PRO C 10 -31.429 32.408 -36.531 1.00122.09 O ATOM 4836 CB PRO C 10 -29.664 34.652 -35.345 1.00104.32 C ATOM 4837 CG PRO C 10 -30.162 35.579 -34.298 1.00 98.98 C ATOM 4838 CD PRO C 10 -31.655 35.422 -34.305 1.00122.81 C ATOM 4839 N TYR C 11 -30.308 33.214 -38.311 1.00 98.87 N ATOM 4840 CA TYR C 11 -30.275 31.943 -39.023 1.00100.44 C ATOM 4841 C TYR C 11 -28.865 31.360 -39.021 1.00 98.28 C ATOM 4842 O TYR C 11 -28.658 30.201 -39.381 1.00 91.00 O ATOM 4843 CB TYR C 11 -30.791 32.114 -40.456 1.00 87.88 C ATOM 4844 CG TYR C 11 -30.124 33.229 -41.237 1.00 98.32 C ATOM 4845 CD1 TYR C 11 -28.969 32.998 -41.973 1.00 97.06 C ATOM 4846 CD2 TYR C 11 -30.658 34.513 -41.244 1.00 90.81 C ATOM 4847 CE1 TYR C 11 -28.361 34.015 -42.689 1.00 89.43 C ATOM 4848 CE2 TYR C 11 -30.058 35.535 -41.955 1.00 75.87 C ATOM 4849 CZ TYR C 11 -28.909 35.281 -42.677 1.00 79.75 C ATOM 4850 OH TYR C 11 -28.308 36.296 -43.388 1.00 83.00 O ATOM 4851 N ILE C 12 -27.901 32.175 -38.605 1.00102.31 N ATOM 4852 CA ILE C 12 -26.503 31.765 -38.567 1.00 88.67 C ATOM 4853 C ILE C 12 -26.139 31.192 -37.200 1.00 86.12 C ATOM 4854 O ILE C 12 -26.538 31.727 -36.166 1.00 79.47 O ATOM 4855 CB ILE C 12 -25.573 32.952 -38.898 1.00 85.31 C ATOM 4856 CG1 ILE C 12 -25.797 33.421 -40.337 1.00 90.54 C ATOM 4857 CG2 ILE C 12 -24.113 32.582 -38.679 1.00 94.50 C ATOM 4858 CD1 ILE C 12 -25.113 34.729 -40.666 1.00 86.17 C ATOM 4859 N LEU C 13 -25.371 30.106 -37.203 1.00107.55 N ATOM 4860 CA LEU C 13 -24.969 29.444 -35.970 1.00113.56 C ATOM 4861 C LEU C 13 -23.450 29.339 -35.898 1.00135.05 C ATOM 4862 O LEU C 13 -22.763 29.384 -36.920 1.00102.08 O ATOM 4863 CB LEU C 13 -25.595 28.050 -35.892 1.00 86.21 C ATOM 4864 CG LEU C 13 -25.361 27.227 -34.623 1.00 98.36 C ATOM 4865 CD1 LEU C 13 -25.899 27.947 -33.399 1.00107.99 C ATOM 4866 CD2 LEU C 13 -25.987 25.846 -34.754 1.00 90.02 C ATOM 4867 OXT LEU C 13 -22.870 29.214 -34.818 1.00105.86 O TER 4868 LEU C 13 ATOM 4869 N GLY D 6 -2.328 -23.561 -41.110 1.00124.62 N ATOM 4870 CA GLY D 6 -3.487 -23.144 -41.876 1.00143.31 C ATOM 4871 C GLY D 6 -4.732 -23.924 -41.505 1.00150.67 C ATOM 4872 O GLY D 6 -4.648 -25.072 -41.068 1.00174.61 O ATOM 4873 N GLY D 7 -5.893 -23.301 -41.678 1.00176.20 N ATOM 4874 CA GLY D 7 -7.151 -23.944 -41.351 1.00165.27 C ATOM 4875 C GLY D 7 -8.329 -22.991 -41.307 1.00168.67 C ATOM 4876 O GLY D 7 -8.355 -21.981 -42.011 1.00151.48 O ATOM 4877 N ARG D 8 -9.307 -23.315 -40.468 1.00158.36 N ATOM 4878 CA ARG D 8 -10.532 -22.532 -40.372 1.00139.28 C ATOM 4879 C ARG D 8 -10.346 -21.265 -39.545 1.00145.84 C ATOM 4880 O ARG D 8 -9.547 -21.234 -38.609 1.00147.73 O ATOM 4881 CB ARG D 8 -11.635 -23.381 -39.734 1.00153.35 C ATOM 4882 CG ARG D 8 -11.895 -24.709 -40.422 1.00149.90 C ATOM 4883 CD ARG D 8 -12.814 -25.592 -39.585 1.00146.20 C ATOM 4884 NE ARG D 8 -14.073 -24.941 -39.232 1.00135.68 N ATOM 4885 CZ ARG D 8 -15.022 -25.509 -38.494 1.00145.91 C ATOM 4886 NH1 ARG D 8 -14.852 -26.737 -38.025 1.00156.05 N ATOM 4887 NH2 ARG D 8 -16.139 -24.849 -38.220 1.00150.48 N ATOM 4888 N ARG D 9 -11.086 -20.221 -39.903 1.00121.15 N ATOM 4889 CA ARG D 9 -11.138 -19.004 -39.102 1.00120.67 C ATOM 4890 C ARG D 9 -12.562 -18.793 -38.600 1.00102.22 C ATOM 4891 O ARG D 9 -13.517 -18.985 -39.354 1.00111.88 O ATOM 4892 CB ARG D 9 -10.662 -17.787 -39.900 1.00127.48 C ATOM 4893 CG ARG D 9 -10.946 -16.462 -39.202 1.00132.90 C ATOM 4894 CD ARG D 9 -10.365 -15.274 -39.941 1.00133.67 C ATOM 4895 NE ARG D 9 -8.959 -15.074 -39.606 1.00132.07 N ATOM 4896 CZ ARG D 9 -8.291 -13.948 -39.831 1.00136.64 C ATOM 4897 NH1 ARG D 9 -8.900 -12.914 -40.394 1.00129.68 N ATOM 4898 NH2 ARG D 9 -7.013 -13.856 -39.497 1.00145.42 N ATOM 4899 N PRO D 10 -12.713 -18.413 -37.322 1.00 90.61 N ATOM 4900 CA PRO D 10 -14.033 -18.093 -36.770 1.00 99.83 C ATOM 4901 C PRO D 10 -14.706 -16.973 -37.558 1.00108.25 C ATOM 4902 O PRO D 10 -14.027 -16.052 -38.010 1.00107.18 O ATOM 4903 CB PRO D 10 -13.709 -17.616 -35.351 1.00 89.27 C ATOM 4904 CG PRO D 10 -12.432 -18.300 -35.012 1.00 76.34 C ATOM 4905 CD PRO D 10 -11.657 -18.355 -36.296 1.00 87.47 C ATOM 4906 N TYR D 11 -16.020 -17.066 -37.740 1.00117.63 N ATOM 4907 CA TYR D 11 -16.770 -16.009 -38.408 1.00111.81 C ATOM 4908 C TYR D 11 -17.570 -15.214 -37.382 1.00119.87 C ATOM 4909 O TYR D 11 -18.124 -14.159 -37.688 1.00121.70 O ATOM 4910 CB TYR D 11 -17.697 -16.584 -39.486 1.00 87.30 C ATOM 4911 CG TYR D 11 -18.635 -17.667 -38.996 1.00 91.95 C ATOM 4912 CD1 TYR D 11 -19.882 -17.347 -38.471 1.00 90.05 C ATOM 4913 CD2 TYR D 11 -18.280 -19.008 -39.066 1.00 85.69 C ATOM 4914 CE1 TYR D 11 -20.745 -18.329 -38.022 1.00 90.86 C ATOM 4915 CE2 TYR D 11 -19.137 -20.000 -38.619 1.00 85.89 C ATOM 4916 CZ TYR D 11 -20.368 -19.654 -38.098 1.00103.14 C ATOM 4917 OH TYR D 11 -21.225 -20.636 -37.652 1.00 79.30 O ATOM 4918 N ILE D 12 -17.620 -15.735 -36.159 1.00103.51 N ATOM 4919 CA ILE D 12 -18.370 -15.109 -35.077 1.00100.95 C ATOM 4920 C ILE D 12 -17.493 -14.150 -34.274 1.00 98.96 C ATOM 4921 O ILE D 12 -16.336 -14.449 -33.980 1.00 94.21 O ATOM 4922 CB ILE D 12 -18.972 -16.180 -34.136 1.00 64.43 C ATOM 4923 CG1 ILE D 12 -20.033 -16.996 -34.875 1.00 86.38 C ATOM 4924 CG2 ILE D 12 -19.574 -15.545 -32.890 1.00 46.15 C ATOM 4925 CD1 ILE D 12 -20.506 -18.219 -34.120 1.00 97.14 C ATOM 4926 N LEU D 13 -18.058 -12.999 -33.920 1.00121.85 N ATOM 4927 CA LEU D 13 -17.338 -11.981 -33.168 1.00118.79 C ATOM 4928 C LEU D 13 -18.096 -11.639 -31.890 1.00129.94 C ATOM 4929 O LEU D 13 -17.504 -11.278 -30.872 1.00125.67 O ATOM 4930 CB LEU D 13 -17.157 -10.722 -34.018 1.00 89.49 C ATOM 4931 CG LEU D 13 -16.328 -9.591 -33.404 1.00 88.09 C ATOM 4932 CD1 LEU D 13 -14.912 -10.057 -33.105 1.00 93.56 C ATOM 4933 CD2 LEU D 13 -16.315 -8.373 -34.311 1.00 89.53 C ATOM 4934 OXT LEU D 13 -19.324 -11.725 -31.841 1.00113.26 O TER 4935 LEU D 13 HETATM 4936 N GLY A1387 -34.991 26.777 -19.594 1.00125.23 N HETATM 4937 CA GLY A1387 -33.811 27.521 -19.196 1.00132.03 C HETATM 4938 C GLY A1387 -32.547 27.009 -19.860 1.00139.70 C HETATM 4939 O GLY A1387 -31.590 27.756 -20.060 1.00125.56 O HETATM 4940 OXT GLY A1387 -32.448 25.834 -20.216 1.00120.36 O HETATM 4941 N GLY A1388 0.787 10.169 -38.717 1.00139.84 N HETATM 4942 CA GLY A1388 1.745 10.355 -37.643 1.00139.84 C HETATM 4943 C GLY A1388 3.180 10.217 -38.114 1.00139.84 C HETATM 4944 O GLY A1388 4.112 10.672 -37.451 1.00139.84 O HETATM 4945 OXT GLY A1388 3.448 9.647 -39.172 1.00215.64 O HETATM 4946 N GLY A1389 -22.491 43.097 -48.847 1.00130.00 N HETATM 4947 CA GLY A1389 -22.347 43.244 -47.410 1.00130.00 C HETATM 4948 C GLY A1389 -23.608 43.767 -46.751 1.00130.00 C HETATM 4949 O GLY A1389 -23.799 43.622 -45.543 1.00130.00 O HETATM 4950 OXT GLY A1389 -24.471 44.350 -47.407 1.00129.71 O HETATM 4951 N GLY A1390 3.410 13.940 -35.867 1.00121.15 N HETATM 4952 CA GLY A1390 2.156 13.475 -35.305 1.00123.64 C HETATM 4953 C GLY A1390 0.989 13.641 -36.259 1.00131.20 C HETATM 4954 O GLY A1390 -0.062 13.023 -36.089 1.00121.95 O HETATM 4955 OXT GLY A1390 1.063 14.399 -37.227 1.00138.32 O HETATM 4956 N GLY A1391 -2.618 -4.405 -31.013 1.00146.86 N HETATM 4957 CA GLY A1391 -3.315 -3.135 -31.112 1.00146.86 C HETATM 4958 C GLY A1391 -3.874 -2.673 -29.781 1.00146.86 C HETATM 4959 O GLY A1391 -4.027 -3.462 -28.850 1.00146.86 O HETATM 4960 OXT GLY A1391 -4.188 -1.497 -29.597 1.00118.69 O CONECT 692 1328 CONECT 1328 692 CONECT 3077 3713 CONECT 3713 3077 CONECT 4936 4937 CONECT 4937 4936 4938 CONECT 4938 4937 4939 4940 CONECT 4939 4938 CONECT 4940 4938 CONECT 4941 4942 CONECT 4942 4941 4943 CONECT 4943 4942 4944 4945 CONECT 4944 4943 CONECT 4945 4943 CONECT 4946 4947 CONECT 4947 4946 4948 CONECT 4948 4947 4949 4950 CONECT 4949 4948 CONECT 4950 4948 CONECT 4951 4952 CONECT 4952 4951 4953 CONECT 4953 4952 4954 4955 CONECT 4954 4953 CONECT 4955 4953 CONECT 4956 4957 CONECT 4957 4956 4958 CONECT 4958 4957 4959 4960 CONECT 4959 4958 CONECT 4960 4958 MASTER 390 0 5 28 4 0 5 9 4956 4 29 54 END