HEADER MEMBRANE PROTEIN/AGONIST 03-OCT-17 6B73 TITLE CRYSTAL STRUCTURE OF A NANOBODY-STABILIZED ACTIVE STATE OF THE KAPPA- TITLE 2 OPIOID RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOLUBLE CYTOCHROME B562, KAPPA-TYPE OPIOID RECEPTOR; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: UNP RESIDUES 23-128; UNP RESIDUES 54-358; COMPND 5 SYNONYM: CYTOCHROME B-562,KOR-1; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: NANOBODY; COMPND 10 CHAIN: C, D; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 562, 9606; SOURCE 5 GENE: CYBC, OPRK1, OPRK; SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: LAMA GLAMA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9844 KEYWDS GPCR, OPIOID RECEPTOR, ADDICTION, ACTIVE STATE, NANOBODY, STRUCTURE- KEYWDS 2 FUNCTION, MORPHINAN, LCP, MEMBRANE PROTEIN, MEMBRANE PROTEIN-AGONIST KEYWDS 3 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.CHE,S.MAJUMDAR,S.A.ZAIDI,C.KORMOS,J.D.MCCORVY,S.WANG,P.D.MOSIER, AUTHOR 2 R.UPRETY,E.VARDY,B.E.KRUMM,G.W.HAN,M.Y.LEE,E.PARDON,J.STEYAERT, AUTHOR 3 X.P.HUANG,R.T.STRACHAN,A.R.TRIBO,G.W.PASTERNAK,I.F.CARROLL, AUTHOR 4 R.C.STEVENS,V.CHEREZOV,V.KATRITCH,D.WACKER,B.L.ROTH REVDAT 3 27-NOV-19 6B73 1 REMARK REVDAT 2 24-JAN-18 6B73 1 JRNL REVDAT 1 17-JAN-18 6B73 0 JRNL AUTH T.CHE,S.MAJUMDAR,S.A.ZAIDI,P.ONDACHI,J.D.MCCORVY,S.WANG, JRNL AUTH 2 P.D.MOSIER,R.UPRETY,E.VARDY,B.E.KRUMM,G.W.HAN,M.Y.LEE, JRNL AUTH 3 E.PARDON,J.STEYAERT,X.P.HUANG,R.T.STRACHAN,A.R.TRIBO, JRNL AUTH 4 G.W.PASTERNAK,F.I.CARROLL,R.C.STEVENS,V.CHEREZOV,V.KATRITCH, JRNL AUTH 5 D.WACKER,B.L.ROTH JRNL TITL STRUCTURE OF THE NANOBODY-STABILIZED ACTIVE STATE OF THE JRNL TITL 2 KAPPA OPIOID RECEPTOR. JRNL REF CELL V. 172 55 2018 JRNL REFN ISSN 1097-4172 JRNL PMID 29307491 JRNL DOI 10.1016/J.CELL.2017.12.011 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.2 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.94 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5 REMARK 3 NUMBER OF REFLECTIONS : 30255 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.255 REMARK 3 R VALUE (WORKING SET) : 0.254 REMARK 3 FREE R VALUE : 0.275 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970 REMARK 3 FREE R VALUE TEST SET COUNT : 1505 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 15 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.21 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.61 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2708 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2470 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2570 REMARK 3 BIN R VALUE (WORKING SET) : 0.2450 REMARK 3 BIN FREE R VALUE : 0.2830 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 138 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6006 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 136 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 78.82 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 85.74 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -29.65480 REMARK 3 B22 (A**2) : 21.50320 REMARK 3 B33 (A**2) : 8.15160 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -3.23570 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.600 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.714 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.374 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.834 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.391 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.867 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.832 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 6307 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 8661 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 2728 ; 15.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 81 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 931 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 6307 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 901 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 7781 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 0.95 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.54 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 1.57 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|51 - A|339 } REMARK 3 ORIGIN FOR THE GROUP (A): 61.2141 -21.9866 5.1559 REMARK 3 T TENSOR REMARK 3 T11: 0.0608 T22: -0.1567 REMARK 3 T33: -0.1908 T12: -0.0397 REMARK 3 T13: -0.0984 T23: 0.0077 REMARK 3 L TENSOR REMARK 3 L11: 0.6808 L22: 2.5682 REMARK 3 L33: 1.6936 L12: -0.1949 REMARK 3 L13: -0.3377 L23: 0.9759 REMARK 3 S TENSOR REMARK 3 S11: 0.0929 S12: -0.1566 S13: -0.0532 REMARK 3 S21: -0.1717 S22: 0.0023 S23: 0.0208 REMARK 3 S31: 0.0122 S32: -0.0852 S33: -0.0952 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|54 - B|334 } REMARK 3 ORIGIN FOR THE GROUP (A): 56.7465 13.9345 -5.7761 REMARK 3 T TENSOR REMARK 3 T11: 0.1822 T22: -0.1697 REMARK 3 T33: -0.2378 T12: -0.0208 REMARK 3 T13: -0.0436 T23: 0.0206 REMARK 3 L TENSOR REMARK 3 L11: 0.7626 L22: 2.1248 REMARK 3 L33: 1.0044 L12: -0.3708 REMARK 3 L13: 0.1139 L23: 0.6449 REMARK 3 S TENSOR REMARK 3 S11: 0.0418 S12: 0.1213 S13: -0.0641 REMARK 3 S21: 0.2860 S22: -0.0921 S23: -0.0290 REMARK 3 S31: -0.0033 S32: -0.1052 S33: 0.0503 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { C|4 - C|129 } REMARK 3 ORIGIN FOR THE GROUP (A): 49.9534 3.0159 -40.5571 REMARK 3 T TENSOR REMARK 3 T11: 0.0541 T22: -0.1786 REMARK 3 T33: -0.2251 T12: 0.0600 REMARK 3 T13: -0.0929 T23: 0.0343 REMARK 3 L TENSOR REMARK 3 L11: 4.8117 L22: 2.9340 REMARK 3 L33: 4.7865 L12: 1.6414 REMARK 3 L13: 1.1000 L23: 1.0974 REMARK 3 S TENSOR REMARK 3 S11: -0.0681 S12: -0.0728 S13: 0.3412 REMARK 3 S21: -0.0963 S22: 0.0442 S23: 0.1442 REMARK 3 S31: -0.2113 S32: -0.0197 S33: 0.0239 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { D|4 - D|129 } REMARK 3 ORIGIN FOR THE GROUP (A): 53.6609 -9.7035 39.7407 REMARK 3 T TENSOR REMARK 3 T11: 0.1137 T22: -0.2278 REMARK 3 T33: -0.2442 T12: -0.0409 REMARK 3 T13: -0.0531 T23: 0.0609 REMARK 3 L TENSOR REMARK 3 L11: 2.7839 L22: 3.4103 REMARK 3 L33: 6.1550 L12: -2.0803 REMARK 3 L13: -2.0908 L23: 1.8807 REMARK 3 S TENSOR REMARK 3 S11: -0.0191 S12: 0.0475 S13: -0.2738 REMARK 3 S21: 0.2529 S22: 0.1427 S23: 0.0658 REMARK 3 S31: -0.0334 S32: -0.0208 S33: -0.1237 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THERE ARE SOME UNKNOWN DENSITIES REMARK 3 LOCATED ABOVE THE LIGAND BINDING SITE AND NEAR THE TRP222 ON REMARK 3 BOTH A AND B CHAINS. THEY HAVE NOT BEEN MODELLED. REMARK 4 REMARK 4 6B73 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-17. REMARK 100 THE DEPOSITION ID IS D_1000230329. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-DEC-16 REMARK 200 TEMPERATURE (KELVIN) : 123 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0330 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30278 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 46.940 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : 0.18700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.27 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.2 REMARK 200 DATA REDUNDANCY IN SHELL : 2.50 REMARK 200 R MERGE FOR SHELL (I) : 0.96100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB 4DJH, 5C1M, 1M6T REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.40 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.66 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS PH 6.5-7.0, 140-200 MM REMARK 280 MAGNESIUM SULFATE HYDRATE, 100 MM SODIUM CITRATE TRIBASIC REMARK 280 DEHYDRATE, 10 MM MANGANESE(II) CHLORIDE TETRAHYDRATE, 28-30% REMARK 280 PEG400, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 75.37500 REMARK 290 SMTRY3 2 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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2590 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19360 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18940 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 -59 REMARK 465 GLY A -58 REMARK 465 THR A -57 REMARK 465 THR A -56 REMARK 465 MET A -55 REMARK 465 ALA A -54 REMARK 465 ASP A -53 REMARK 465 LEU A -52 REMARK 465 GLU A -51 REMARK 465 ASP A -50 REMARK 465 ASN A -49 REMARK 465 TRP A -48 REMARK 465 GLU A -47 REMARK 465 THR A -46 REMARK 465 LEU A -45 REMARK 465 ASN A -44 REMARK 465 ASP A -43 REMARK 465 ASN A -42 REMARK 465 LEU A -41 REMARK 465 LYS A -40 REMARK 465 VAL A -39 REMARK 465 ILE A -38 REMARK 465 GLU A -37 REMARK 465 LYS A -36 REMARK 465 ALA A -35 REMARK 465 ASP A -34 REMARK 465 ASN A -33 REMARK 465 ALA A -32 REMARK 465 ALA A -31 REMARK 465 GLN A -30 REMARK 465 VAL A -29 REMARK 465 LYS A -28 REMARK 465 ASP A -27 REMARK 465 ALA A -26 REMARK 465 LEU A -25 REMARK 465 THR A -24 REMARK 465 LYS A -23 REMARK 465 MET A -22 REMARK 465 ARG A -21 REMARK 465 ALA A -20 REMARK 465 ALA A -19 REMARK 465 ALA A -18 REMARK 465 LEU A -17 REMARK 465 ASP A -16 REMARK 465 ALA A -15 REMARK 465 GLN A -14 REMARK 465 LYS A -13 REMARK 465 ALA A -12 REMARK 465 THR A -11 REMARK 465 PRO A -10 REMARK 465 PRO A -9 REMARK 465 LYS A -8 REMARK 465 LEU A -7 REMARK 465 GLU A -6 REMARK 465 ASP A -5 REMARK 465 LYS A -4 REMARK 465 SER A -3 REMARK 465 PRO A -2 REMARK 465 ASP A -1 REMARK 465 SER A 0 REMARK 465 PRO A 1 REMARK 465 GLU A 2 REMARK 465 MET A 3 REMARK 465 LYS A 4 REMARK 465 ASP A 5 REMARK 465 PHE A 6 REMARK 465 ARG A 7 REMARK 465 HIS A 8 REMARK 465 GLY A 9 REMARK 465 PHE A 10 REMARK 465 ASP A 11 REMARK 465 ILE A 12 REMARK 465 LEU A 13 REMARK 465 VAL A 14 REMARK 465 GLY A 15 REMARK 465 GLN A 16 REMARK 465 ILE A 17 REMARK 465 ASP A 18 REMARK 465 ASP A 19 REMARK 465 ALA A 20 REMARK 465 LEU A 21 REMARK 465 LYS A 22 REMARK 465 LEU A 23 REMARK 465 ALA A 24 REMARK 465 ASN A 25 REMARK 465 GLU A 26 REMARK 465 GLY A 27 REMARK 465 LYS A 28 REMARK 465 VAL A 29 REMARK 465 LYS A 30 REMARK 465 GLU A 31 REMARK 465 ALA A 32 REMARK 465 GLN A 33 REMARK 465 ALA A 34 REMARK 465 ALA A 35 REMARK 465 ALA A 36 REMARK 465 GLU A 37 REMARK 465 GLN A 38 REMARK 465 LEU A 39 REMARK 465 LYS A 40 REMARK 465 THR A 41 REMARK 465 THR A 42 REMARK 465 ARG A 43 REMARK 465 ASN A 44 REMARK 465 ALA A 45 REMARK 465 TYR A 46 REMARK 465 ILE A 47 REMARK 465 GLN A 48 REMARK 465 LYS A 49 REMARK 465 TYR A 50 REMARK 465 GLU A 203 REMARK 465 ASP A 204 REMARK 465 VAL A 205 REMARK 465 LEU A 258 REMARK 465 LEU A 259 REMARK 465 SER A 260 REMARK 465 GLY A 261 REMARK 465 SER A 301 REMARK 465 CYS A 340 REMARK 465 PHE A 341 REMARK 465 ARG A 342 REMARK 465 ASP A 343 REMARK 465 PHE A 344 REMARK 465 CYS A 345 REMARK 465 PHE A 346 REMARK 465 PRO A 347 REMARK 465 LEU A 348 REMARK 465 LYS A 349 REMARK 465 MET A 350 REMARK 465 ARG A 351 REMARK 465 MET A 352 REMARK 465 GLU A 353 REMARK 465 ARG A 354 REMARK 465 GLN A 355 REMARK 465 SER A 356 REMARK 465 THR A 357 REMARK 465 SER A 358 REMARK 465 GLY B -59 REMARK 465 GLY B -58 REMARK 465 THR B -57 REMARK 465 THR B -56 REMARK 465 MET B -55 REMARK 465 ALA B -54 REMARK 465 ASP B -53 REMARK 465 LEU B -52 REMARK 465 GLU B -51 REMARK 465 ASP B -50 REMARK 465 ASN B -49 REMARK 465 TRP B -48 REMARK 465 GLU B -47 REMARK 465 THR B -46 REMARK 465 LEU B -45 REMARK 465 ASN B -44 REMARK 465 ASP B -43 REMARK 465 ASN B -42 REMARK 465 LEU B -41 REMARK 465 LYS B -40 REMARK 465 VAL B -39 REMARK 465 ILE B -38 REMARK 465 GLU B -37 REMARK 465 LYS B -36 REMARK 465 ALA B -35 REMARK 465 ASP B -34 REMARK 465 ASN B -33 REMARK 465 ALA B -32 REMARK 465 ALA B -31 REMARK 465 GLN B -30 REMARK 465 VAL B -29 REMARK 465 LYS B -28 REMARK 465 ASP B -27 REMARK 465 ALA B -26 REMARK 465 LEU B -25 REMARK 465 THR B -24 REMARK 465 LYS B -23 REMARK 465 MET B -22 REMARK 465 ARG B -21 REMARK 465 ALA B -20 REMARK 465 ALA B -19 REMARK 465 ALA B -18 REMARK 465 LEU B -17 REMARK 465 ASP B -16 REMARK 465 ALA B -15 REMARK 465 GLN B -14 REMARK 465 LYS B -13 REMARK 465 ALA B -12 REMARK 465 THR B -11 REMARK 465 PRO B -10 REMARK 465 PRO B -9 REMARK 465 LYS B -8 REMARK 465 LEU B -7 REMARK 465 GLU B -6 REMARK 465 ASP B -5 REMARK 465 LYS B -4 REMARK 465 SER B -3 REMARK 465 PRO B -2 REMARK 465 ASP B -1 REMARK 465 SER B 0 REMARK 465 PRO B 1 REMARK 465 GLU B 2 REMARK 465 MET B 3 REMARK 465 LYS B 4 REMARK 465 ASP B 5 REMARK 465 PHE B 6 REMARK 465 ARG B 7 REMARK 465 HIS B 8 REMARK 465 GLY B 9 REMARK 465 PHE B 10 REMARK 465 ASP B 11 REMARK 465 ILE B 12 REMARK 465 LEU B 13 REMARK 465 VAL B 14 REMARK 465 GLY B 15 REMARK 465 GLN B 16 REMARK 465 ILE B 17 REMARK 465 ASP B 18 REMARK 465 ASP B 19 REMARK 465 ALA B 20 REMARK 465 LEU B 21 REMARK 465 LYS B 22 REMARK 465 LEU B 23 REMARK 465 ALA B 24 REMARK 465 ASN B 25 REMARK 465 GLU B 26 REMARK 465 GLY B 27 REMARK 465 LYS B 28 REMARK 465 VAL B 29 REMARK 465 LYS B 30 REMARK 465 GLU B 31 REMARK 465 ALA B 32 REMARK 465 GLN B 33 REMARK 465 ALA B 34 REMARK 465 ALA B 35 REMARK 465 ALA B 36 REMARK 465 GLU B 37 REMARK 465 GLN B 38 REMARK 465 LEU B 39 REMARK 465 LYS B 40 REMARK 465 THR B 41 REMARK 465 THR B 42 REMARK 465 ARG B 43 REMARK 465 ASN B 44 REMARK 465 ALA B 45 REMARK 465 TYR B 46 REMARK 465 ILE B 47 REMARK 465 GLN B 48 REMARK 465 LYS B 49 REMARK 465 TYR B 50 REMARK 465 LEU B 51 REMARK 465 GLY B 52 REMARK 465 SER B 53 REMARK 465 ARG B 202 REMARK 465 GLU B 203 REMARK 465 ASP B 204 REMARK 465 VAL B 205 REMARK 465 ASP B 206 REMARK 465 LEU B 259 REMARK 465 SER B 260 REMARK 465 GLY B 261 REMARK 465 SER B 301 REMARK 465 THR B 302 REMARK 465 SER B 303 REMARK 465 HIS B 304 REMARK 465 GLU B 335 REMARK 465 ASN B 336 REMARK 465 PHE B 337 REMARK 465 LYS B 338 REMARK 465 ARG B 339 REMARK 465 CYS B 340 REMARK 465 PHE B 341 REMARK 465 ARG B 342 REMARK 465 ASP B 343 REMARK 465 PHE B 344 REMARK 465 CYS B 345 REMARK 465 PHE B 346 REMARK 465 PRO B 347 REMARK 465 LEU B 348 REMARK 465 LYS B 349 REMARK 465 MET B 350 REMARK 465 ARG B 351 REMARK 465 MET B 352 REMARK 465 GLU B 353 REMARK 465 ARG B 354 REMARK 465 GLN B 355 REMARK 465 SER B 356 REMARK 465 THR B 357 REMARK 465 SER B 358 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 GLN C 3 REMARK 465 HIS C 130 REMARK 465 GLU C 131 REMARK 465 PRO C 132 REMARK 465 GLU C 133 REMARK 465 ALA C 134 REMARK 465 MET D 1 REMARK 465 ALA D 2 REMARK 465 GLN D 3 REMARK 465 GLY D 103 REMARK 465 GLN D 104 REMARK 465 SER D 105 REMARK 465 SER D 106 REMARK 465 HIS D 130 REMARK 465 GLU D 131 REMARK 465 PRO D 132 REMARK 465 GLU D 133 REMARK 465 ALA D 134 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 LEU A 51 CG CD1 CD2 REMARK 470 ILE A 54 CG1 CG2 CD1 REMARK 470 ARG A 86 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 89 CG CD CE NZ REMARK 470 SER A 188 OG REMARK 470 SER A 192 OG REMARK 470 LYS A 200 CG CD CE NZ REMARK 470 VAL A 201 CG1 CG2 REMARK 470 ARG A 202 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 206 CG OD1 OD2 REMARK 470 VAL A 207 CG1 CG2 REMARK 470 ASP A 216 CG OD1 OD2 REMARK 470 ASP A 217 CG OD1 OD2 REMARK 470 MET A 226 CG SD CE REMARK 470 LEU A 251 CG CD1 CD2 REMARK 470 LYS A 254 CG CD CE NZ REMARK 470 ARG A 257 CG CD NE CZ NH1 NH2 REMARK 470 SER A 262 OG REMARK 470 ARG A 263 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 264 CG CD OE1 OE2 REMARK 470 LYS A 265 CG CD CE NZ REMARK 470 ARG A 267 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 269 CG CD1 CD2 REMARK 470 ARG A 270 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 271 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 297 CG CD OE1 OE2 REMARK 470 THR A 302 OG1 CG2 REMARK 470 SER A 305 OG REMARK 470 ILE A 328 CG1 CG2 CD1 REMARK 470 LEU A 329 CG CD1 CD2 REMARK 470 ASN A 336 CG OD1 ND2 REMARK 470 ARG A 339 CG CD NE CZ NH1 NH2 REMARK 470 ILE B 54 CG1 CG2 CD1 REMARK 470 SER B 55 OG REMARK 470 PHE B 82 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG B 86 CG CD NE CZ NH1 NH2 REMARK 470 THR B 88 OG1 CG2 REMARK 470 LYS B 89 CG CD CE NZ REMARK 470 LYS B 91 CG CD CE NZ REMARK 470 SER B 136 OG REMARK 470 SER B 145 OG REMARK 470 LYS B 174 CG CD CE NZ REMARK 470 LYS B 176 CG CD CE NZ REMARK 470 ILE B 180 CG1 CG2 CD1 REMARK 470 SER B 186 OG REMARK 470 ILE B 191 CG1 CG2 CD1 REMARK 470 LYS B 200 CG CD CE NZ REMARK 470 VAL B 201 CG1 CG2 REMARK 470 VAL B 207 CG1 CG2 REMARK 470 GLU B 209 CG CD OE1 OE2 REMARK 470 ASP B 216 CG OD1 OD2 REMARK 470 ASP B 217 CG OD1 OD2 REMARK 470 SER B 255 OG REMARK 470 ARG B 257 CG CD NE CZ NH1 NH2 REMARK 470 LEU B 258 CG CD1 CD2 REMARK 470 SER B 262 OG REMARK 470 ARG B 263 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 265 CG CD CE NZ REMARK 470 ARG B 267 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 270 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 271 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 274 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 297 CG CD OE1 OE2 REMARK 470 SER B 305 OG REMARK 470 THR B 306 OG1 CG2 REMARK 470 LEU B 333 CG CD1 CD2 REMARK 470 ASP B 334 CG OD1 OD2 REMARK 470 VAL C 4 CG1 CG2 REMARK 470 ARG C 29 CG CD NE CZ NH1 NH2 REMARK 470 TRP C 114 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP C 114 CZ3 CH2 REMARK 470 SER C 124 OG REMARK 470 HIS C 127 CG ND1 CD2 CE1 NE2 REMARK 470 HIS C 129 CG ND1 CD2 CE1 NE2 REMARK 470 VAL D 4 CG1 CG2 REMARK 470 LYS D 43 CG CD CE NZ REMARK 470 GLU D 44 CG CD OE1 OE2 REMARK 470 ASP D 57 CG OD1 OD2 REMARK 470 LYS D 87 CG CD CE NZ REMARK 470 VAL D 93 CG1 CG2 REMARK 470 ARG D 99 CG CD NE CZ NH1 NH2 REMARK 470 TRP D 114 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP D 114 CZ3 CH2 REMARK 470 SER D 124 OG REMARK 470 HIS D 127 CG ND1 CD2 CE1 NE2 REMARK 470 HIS D 129 CG ND1 CD2 CE1 NE2 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 ALA A 57 32.82 -73.39 REMARK 500 TYR A 87 -46.84 -130.71 REMARK 500 PHE A 169 -30.67 -135.37 REMARK 500 ARG A 170 40.23 -98.55 REMARK 500 PHE A 235 -62.73 -153.51 REMARK 500 SER A 255 53.57 -94.80 REMARK 500 ALA B 57 30.38 -72.60 REMARK 500 TYR B 87 -46.37 -130.80 REMARK 500 ARG B 170 39.94 -98.66 REMARK 500 PHE B 235 -67.27 -128.59 REMARK 500 ARG B 257 78.90 -150.21 REMARK 500 VAL C 48 -66.09 -100.34 REMARK 500 HIS C 127 -43.57 -138.84 REMARK 500 HIS C 128 -84.14 -145.42 REMARK 500 VAL D 48 -66.03 -100.16 REMARK 500 HIS D 88 7.48 -67.05 REMARK 500 HIS D 127 -41.91 -142.57 REMARK 500 HIS D 128 -84.06 -145.91 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLA A 2003 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CVV A 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CVV B 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR B 2002 DBREF 6B73 A -54 51 UNP P0ABE7 C562_ECOLX 23 128 DBREF 6B73 A 54 358 UNP P41145 OPRK_HUMAN 54 358 DBREF 6B73 B -54 51 UNP P0ABE7 C562_ECOLX 23 128 DBREF 6B73 B 54 358 UNP P41145 OPRK_HUMAN 54 358 DBREF 6B73 C 1 134 PDB 6B73 6B73 1 134 DBREF 6B73 D 1 134 PDB 6B73 6B73 1 134 SEQADV 6B73 GLY A -59 UNP P0ABE7 EXPRESSION TAG SEQADV 6B73 GLY A -58 UNP P0ABE7 EXPRESSION TAG SEQADV 6B73 THR A -57 UNP P0ABE7 EXPRESSION TAG SEQADV 6B73 THR A -56 UNP P0ABE7 EXPRESSION TAG SEQADV 6B73 MET A -55 UNP P0ABE7 EXPRESSION TAG SEQADV 6B73 TRP A -48 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6B73 ILE A 47 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 6B73 LEU A 51 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 6B73 GLY A 52 UNP P0ABE7 LINKER SEQADV 6B73 SER A 53 UNP P0ABE7 LINKER SEQADV 6B73 LEU A 135 UNP P41145 ILE 135 ENGINEERED MUTATION SEQADV 6B73 GLY B -59 UNP P0ABE7 EXPRESSION TAG SEQADV 6B73 GLY B -58 UNP P0ABE7 EXPRESSION TAG SEQADV 6B73 THR B -57 UNP P0ABE7 EXPRESSION TAG SEQADV 6B73 THR B -56 UNP P0ABE7 EXPRESSION TAG SEQADV 6B73 MET B -55 UNP P0ABE7 EXPRESSION TAG SEQADV 6B73 TRP B -48 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6B73 ILE B 47 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 6B73 LEU B 51 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 6B73 GLY B 52 UNP P0ABE7 LINKER SEQADV 6B73 SER B 53 UNP P0ABE7 LINKER SEQADV 6B73 LEU B 135 UNP P41145 ILE 135 ENGINEERED MUTATION SEQRES 1 A 418 GLY GLY THR THR MET ALA ASP LEU GLU ASP ASN TRP GLU SEQRES 2 A 418 THR LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP SEQRES 3 A 418 ASN ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG SEQRES 4 A 418 ALA ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS SEQRES 5 A 418 LEU GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP SEQRES 6 A 418 PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP SEQRES 7 A 418 ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU SEQRES 8 A 418 ALA GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN SEQRES 9 A 418 ALA TYR ILE GLN LYS TYR LEU GLY SER ILE SER PRO ALA SEQRES 10 A 418 ILE PRO VAL ILE ILE THR ALA VAL TYR SER VAL VAL PHE SEQRES 11 A 418 VAL VAL GLY LEU VAL GLY ASN SER LEU VAL MET PHE VAL SEQRES 12 A 418 ILE ILE ARG TYR THR LYS MET LYS THR ALA THR ASN ILE SEQRES 13 A 418 TYR ILE PHE ASN LEU ALA LEU ALA ASP ALA LEU VAL THR SEQRES 14 A 418 THR THR MET PRO PHE GLN SER THR VAL TYR LEU MET ASN SEQRES 15 A 418 SER TRP PRO PHE GLY ASP VAL LEU CYS LYS ILE VAL LEU SEQRES 16 A 418 SER ILE ASP TYR TYR ASN MET PHE THR SER ILE PHE THR SEQRES 17 A 418 LEU THR MET MET SER VAL ASP ARG TYR ILE ALA VAL CYS SEQRES 18 A 418 HIS PRO VAL LYS ALA LEU ASP PHE ARG THR PRO LEU LYS SEQRES 19 A 418 ALA LYS ILE ILE ASN ILE CYS ILE TRP LEU LEU SER SER SEQRES 20 A 418 SER VAL GLY ILE SER ALA ILE VAL LEU GLY GLY THR LYS SEQRES 21 A 418 VAL ARG GLU ASP VAL ASP VAL ILE GLU CYS SER LEU GLN SEQRES 22 A 418 PHE PRO ASP ASP ASP TYR SER TRP TRP ASP LEU PHE MET SEQRES 23 A 418 LYS ILE CYS VAL PHE ILE PHE ALA PHE VAL ILE PRO VAL SEQRES 24 A 418 LEU ILE ILE ILE VAL CYS TYR THR LEU MET ILE LEU ARG SEQRES 25 A 418 LEU LYS SER VAL ARG LEU LEU SER GLY SER ARG GLU LYS SEQRES 26 A 418 ASP ARG ASN LEU ARG ARG ILE THR ARG LEU VAL LEU VAL SEQRES 27 A 418 VAL VAL ALA VAL PHE VAL VAL CYS TRP THR PRO ILE HIS SEQRES 28 A 418 ILE PHE ILE LEU VAL GLU ALA LEU GLY SER THR SER HIS SEQRES 29 A 418 SER THR ALA ALA LEU SER SER TYR TYR PHE CYS ILE ALA SEQRES 30 A 418 LEU GLY TYR THR ASN SER SER LEU ASN PRO ILE LEU TYR SEQRES 31 A 418 ALA PHE LEU ASP GLU ASN PHE LYS ARG CYS PHE ARG ASP SEQRES 32 A 418 PHE CYS PHE PRO LEU LYS MET ARG MET GLU ARG GLN SER SEQRES 33 A 418 THR SER SEQRES 1 B 418 GLY GLY THR THR MET ALA ASP LEU GLU ASP ASN TRP GLU SEQRES 2 B 418 THR LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP SEQRES 3 B 418 ASN ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG SEQRES 4 B 418 ALA ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS SEQRES 5 B 418 LEU GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP SEQRES 6 B 418 PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP SEQRES 7 B 418 ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU SEQRES 8 B 418 ALA GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN SEQRES 9 B 418 ALA TYR ILE GLN LYS TYR LEU GLY SER ILE SER PRO ALA SEQRES 10 B 418 ILE PRO VAL ILE ILE THR ALA VAL TYR SER VAL VAL PHE SEQRES 11 B 418 VAL VAL GLY LEU VAL GLY ASN SER LEU VAL MET PHE VAL SEQRES 12 B 418 ILE ILE ARG TYR THR LYS MET LYS THR ALA THR ASN ILE SEQRES 13 B 418 TYR ILE PHE ASN LEU ALA LEU ALA ASP ALA LEU VAL THR SEQRES 14 B 418 THR THR MET PRO PHE GLN SER THR VAL TYR LEU MET ASN SEQRES 15 B 418 SER TRP PRO PHE GLY ASP VAL LEU CYS LYS ILE VAL LEU SEQRES 16 B 418 SER ILE ASP TYR TYR ASN MET PHE THR SER ILE PHE THR SEQRES 17 B 418 LEU THR MET MET SER VAL ASP ARG TYR ILE ALA VAL CYS SEQRES 18 B 418 HIS PRO VAL LYS ALA LEU ASP PHE ARG THR PRO LEU LYS SEQRES 19 B 418 ALA LYS ILE ILE ASN ILE CYS ILE TRP LEU LEU SER SER SEQRES 20 B 418 SER VAL GLY ILE SER ALA ILE VAL LEU GLY GLY THR LYS SEQRES 21 B 418 VAL ARG GLU ASP VAL ASP VAL ILE GLU CYS SER LEU GLN SEQRES 22 B 418 PHE PRO ASP ASP ASP TYR SER TRP TRP ASP LEU PHE MET SEQRES 23 B 418 LYS ILE CYS VAL PHE ILE PHE ALA PHE VAL ILE PRO VAL SEQRES 24 B 418 LEU ILE ILE ILE VAL CYS TYR THR LEU MET ILE LEU ARG SEQRES 25 B 418 LEU LYS SER VAL ARG LEU LEU SER GLY SER ARG GLU LYS SEQRES 26 B 418 ASP ARG ASN LEU ARG ARG ILE THR ARG LEU VAL LEU VAL SEQRES 27 B 418 VAL VAL ALA VAL PHE VAL VAL CYS TRP THR PRO ILE HIS SEQRES 28 B 418 ILE PHE ILE LEU VAL GLU ALA LEU GLY SER THR SER HIS SEQRES 29 B 418 SER THR ALA ALA LEU SER SER TYR TYR PHE CYS ILE ALA SEQRES 30 B 418 LEU GLY TYR THR ASN SER SER LEU ASN PRO ILE LEU TYR SEQRES 31 B 418 ALA PHE LEU ASP GLU ASN PHE LYS ARG CYS PHE ARG ASP SEQRES 32 B 418 PHE CYS PHE PRO LEU LYS MET ARG MET GLU ARG GLN SER SEQRES 33 B 418 THR SER SEQRES 1 C 134 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 C 134 VAL ARG PRO GLY GLY SER LEU ARG LEU SER CYS VAL ASP SEQRES 3 C 134 SER GLU ARG THR SER TYR PRO MET GLY TRP PHE ARG ARG SEQRES 4 C 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA SER ILE THR SEQRES 5 C 134 TRP SER GLY ILE ASP PRO THR TYR ALA ASP SER VAL ALA SEQRES 6 C 134 ASP ARG PHE THR THR SER ARG ASP VAL ALA ASN ASN THR SEQRES 7 C 134 LEU TYR LEU GLN MET ASN SER LEU LYS HIS GLU ASP THR SEQRES 8 C 134 ALA VAL TYR TYR CYS ALA ALA ARG ALA PRO VAL GLY GLN SEQRES 9 C 134 SER SER SER PRO TYR ASP TYR ASP TYR TRP GLY GLN GLY SEQRES 10 C 134 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 11 C 134 GLU PRO GLU ALA SEQRES 1 D 134 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 D 134 VAL ARG PRO GLY GLY SER LEU ARG LEU SER CYS VAL ASP SEQRES 3 D 134 SER GLU ARG THR SER TYR PRO MET GLY TRP PHE ARG ARG SEQRES 4 D 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA SER ILE THR SEQRES 5 D 134 TRP SER GLY ILE ASP PRO THR TYR ALA ASP SER VAL ALA SEQRES 6 D 134 ASP ARG PHE THR THR SER ARG ASP VAL ALA ASN ASN THR SEQRES 7 D 134 LEU TYR LEU GLN MET ASN SER LEU LYS HIS GLU ASP THR SEQRES 8 D 134 ALA VAL TYR TYR CYS ALA ALA ARG ALA PRO VAL GLY GLN SEQRES 9 D 134 SER SER SER PRO TYR ASP TYR ASP TYR TRP GLY GLN GLY SEQRES 10 D 134 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 11 D 134 GLU PRO GLU ALA HET CVV A2001 33 HET CLR A2002 28 HET OLA A2003 14 HET CVV B2001 33 HET CLR B2002 28 HETNAM CVV N-[(5ALPHA,6BETA)-17-(CYCLOPROPYLMETHYL)-3-HYDROXY-7,8- HETNAM 2 CVV DIDEHYDRO-4,5-EPOXYMORPHINAN-6-YL]-3-IODOBENZAMIDE HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID FORMUL 5 CVV 2(C27 H27 I N2 O3) FORMUL 6 CLR 2(C27 H46 O) FORMUL 7 OLA C18 H34 O2 HELIX 1 AA1 ALA A 57 TYR A 87 1 31 HELIX 2 AA2 THR A 92 THR A 109 1 18 HELIX 3 AA3 THR A 111 ASN A 122 1 12 HELIX 4 AA4 PHE A 126 HIS A 162 1 37 HELIX 5 AA5 HIS A 162 ASP A 168 1 7 HELIX 6 AA6 THR A 171 LEU A 196 1 26 HELIX 7 AA7 TRP A 221 ALA A 234 1 14 HELIX 8 AA8 PHE A 235 SER A 255 1 21 HELIX 9 AA9 ARG A 263 GLY A 300 1 38 HELIX 10 AB1 SER A 305 ALA A 331 1 27 HELIX 11 AB2 ASP A 334 ARG A 339 1 6 HELIX 12 AB3 ALA B 57 TYR B 87 1 31 HELIX 13 AB4 THR B 92 ASN B 122 1 31 HELIX 14 AB5 PHE B 126 HIS B 162 1 37 HELIX 15 AB6 HIS B 162 ASP B 168 1 7 HELIX 16 AB7 THR B 171 LEU B 196 1 26 HELIX 17 AB8 TRP B 221 PHE B 235 1 15 HELIX 18 AB9 PHE B 235 VAL B 256 1 22 HELIX 19 AC1 ARG B 263 GLY B 300 1 38 HELIX 20 AC2 THR B 306 ASP B 334 1 29 HELIX 21 AC3 LYS C 87 THR C 91 5 5 SHEET 1 AA1 2 GLY A 197 LYS A 200 0 SHEET 2 AA1 2 GLU A 209 LEU A 212 -1 O GLU A 209 N LYS A 200 SHEET 1 AA2 2 GLY B 197 LYS B 200 0 SHEET 2 AA2 2 GLU B 209 LEU B 212 -1 O GLU B 209 N LYS B 200 SHEET 1 AA3 4 VAL C 7 SER C 9 0 SHEET 2 AA3 4 LEU C 20 VAL C 25 -1 O VAL C 25 N VAL C 7 SHEET 3 AA3 4 THR C 78 MET C 83 -1 O LEU C 79 N CYS C 24 SHEET 4 AA3 4 PHE C 68 ASP C 73 -1 N ASP C 73 O THR C 78 SHEET 1 AA4 6 GLY C 12 VAL C 14 0 SHEET 2 AA4 6 THR C 118 VAL C 122 1 O GLN C 119 N GLY C 12 SHEET 3 AA4 6 ALA C 92 ARG C 99 -1 N TYR C 94 O THR C 118 SHEET 4 AA4 6 TYR C 32 ARG C 39 -1 N PHE C 37 O TYR C 95 SHEET 5 AA4 6 ARG C 45 ILE C 51 -1 O VAL C 48 N TRP C 36 SHEET 6 AA4 6 PRO C 58 TYR C 60 -1 O THR C 59 N SER C 50 SHEET 1 AA5 4 VAL D 7 SER D 9 0 SHEET 2 AA5 4 LEU D 20 VAL D 25 -1 O VAL D 25 N VAL D 7 SHEET 3 AA5 4 THR D 78 MET D 83 -1 O LEU D 79 N CYS D 24 SHEET 4 AA5 4 PHE D 68 ASP D 73 -1 N ASP D 73 O THR D 78 SHEET 1 AA6 6 GLY D 12 VAL D 14 0 SHEET 2 AA6 6 THR D 118 VAL D 122 1 O THR D 121 N GLY D 12 SHEET 3 AA6 6 ALA D 92 ARG D 99 -1 N ALA D 92 O VAL D 120 SHEET 4 AA6 6 TYR D 32 ARG D 39 -1 N GLY D 35 O ALA D 97 SHEET 5 AA6 6 ARG D 45 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AA6 6 PRO D 58 TYR D 60 -1 O THR D 59 N SER D 50 SSBOND 1 CYS A 131 CYS A 210 1555 1555 2.04 SSBOND 2 CYS B 131 CYS B 210 1555 1555 2.04 SSBOND 3 CYS C 24 CYS C 96 1555 1555 2.04 SSBOND 4 CYS D 24 CYS D 96 1555 1555 2.04 SITE 1 AC1 13 GLN A 115 VAL A 134 LEU A 135 ASP A 138 SITE 2 AC1 13 TYR A 139 MET A 142 CYS A 210 TRP A 287 SITE 3 AC1 13 ILE A 294 TYR A 312 ILE A 316 GLY A 319 SITE 4 AC1 13 TYR A 320 SITE 1 AC2 4 VAL A 284 VAL A 285 PHE A 293 THR A 302 SITE 1 AC3 2 ALA A 57 ILE A 61 SITE 1 AC4 12 GLN B 115 VAL B 134 LEU B 135 ASP B 138 SITE 2 AC4 12 TYR B 139 MET B 142 CYS B 210 ILE B 294 SITE 3 AC4 12 TYR B 312 ILE B 316 GLY B 319 TYR B 320 SITE 1 AC5 3 VAL B 284 VAL B 285 PHE B 293 CRYST1 62.310 150.750 100.280 90.00 105.66 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.016049 0.000000 0.004499 0.00000 SCALE2 0.000000 0.006633 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010357 0.00000 ATOM 1 N LEU A 51 83.769 -36.095 -17.227 1.00127.37 N ANISOU 1 N LEU A 51 19061 13146 16188 -91 2168 -1669 N ATOM 2 CA LEU A 51 84.754 -36.186 -18.302 1.00129.42 C ANISOU 2 CA LEU A 51 19399 13274 16500 -120 2506 -1819 C ATOM 3 C LEU A 51 84.428 -37.335 -19.272 1.00133.66 C ANISOU 3 C LEU A 51 20207 13673 16904 -68 2516 -1801 C ATOM 4 O LEU A 51 84.644 -37.190 -20.478 1.00134.66 O ANISOU 4 O LEU A 51 20589 13658 16919 -126 2772 -1861 O ATOM 5 CB LEU A 51 86.159 -36.381 -17.721 1.00131.00 C ANISOU 5 CB LEU A 51 19219 13535 17022 -68 2622 -1991 C ATOM 6 N GLY A 52 83.926 -38.454 -18.734 1.00129.00 N ANISOU 6 N GLY A 52 19572 13117 16323 35 2247 -1723 N ATOM 7 CA GLY A 52 83.574 -39.647 -19.506 1.00129.07 C ANISOU 7 CA GLY A 52 19816 13003 16223 89 2219 -1705 C ATOM 8 C GLY A 52 82.106 -40.036 -19.451 1.00130.23 C ANISOU 8 C GLY A 52 20174 13154 16155 88 1932 -1539 C ATOM 9 O GLY A 52 81.280 -39.296 -18.900 1.00128.26 O ANISOU 9 O GLY A 52 19915 12999 15820 41 1766 -1431 O ATOM 10 N SER A 53 81.773 -41.219 -20.022 1.00126.13 N ANISOU 10 N SER A 53 19839 12527 15556 139 1876 -1527 N ATOM 11 CA SER A 53 80.401 -41.745 -20.092 1.00124.06 C ANISOU 11 CA SER A 53 19784 12250 15102 131 1619 -1395 C ATOM 12 C SER A 53 79.914 -42.258 -18.716 1.00124.30 C ANISOU 12 C SER A 53 19590 12403 15234 188 1325 -1297 C ATOM 13 O SER A 53 78.797 -41.912 -18.311 1.00122.50 O ANISOU 13 O SER A 53 19407 12247 14891 142 1121 -1179 O ATOM 14 CB SER A 53 80.307 -42.867 -21.124 1.00128.95 C ANISOU 14 CB SER A 53 20662 12709 15623 160 1670 -1435 C ATOM 15 OG SER A 53 78.984 -43.366 -21.244 1.00136.69 O ANISOU 15 OG SER A 53 21837 13672 16428 139 1426 -1326 O ATOM 16 N ILE A 54 80.738 -43.084 -18.010 1.00119.19 N ANISOU 16 N ILE A 54 18715 11775 14798 294 1306 -1348 N ATOM 17 CA ILE A 54 80.400 -43.636 -16.689 1.00116.63 C ANISOU 17 CA ILE A 54 18202 11547 14566 361 1046 -1259 C ATOM 18 C ILE A 54 80.144 -42.484 -15.714 1.00115.86 C ANISOU 18 C ILE A 54 17919 11610 14490 315 950 -1197 C ATOM 19 O ILE A 54 81.016 -41.636 -15.511 1.00116.04 O ANISOU 19 O ILE A 54 17763 11694 14632 307 1090 -1279 O ATOM 20 CB ILE A 54 81.505 -44.583 -16.167 1.00120.98 C ANISOU 20 CB ILE A 54 18549 12081 15339 501 1065 -1343 C ATOM 21 N SER A 55 78.919 -42.423 -15.171 1.00108.27 N ANISOU 21 N SER A 55 17013 10712 13414 273 724 -1062 N ATOM 22 CA SER A 55 78.477 -41.362 -14.268 1.00105.56 C ANISOU 22 CA SER A 55 16531 10514 13065 225 618 -991 C ATOM 23 C SER A 55 78.810 -41.687 -12.799 1.00106.88 C ANISOU 23 C SER A 55 16433 10788 13389 308 461 -960 C ATOM 24 O SER A 55 78.666 -42.842 -12.390 1.00106.87 O ANISOU 24 O SER A 55 16439 10748 13418 382 334 -921 O ATOM 25 CB SER A 55 76.974 -41.145 -14.415 1.00107.61 C ANISOU 25 CB SER A 55 16973 10786 13129 144 458 -871 C ATOM 26 OG SER A 55 76.615 -40.868 -15.759 1.00116.92 O ANISOU 26 OG SER A 55 18418 11863 14143 82 569 -897 O ATOM 27 N PRO A 56 79.238 -40.697 -11.972 1.00101.22 N ANISOU 27 N PRO A 56 15498 10198 12763 301 462 -977 N ATOM 28 CA PRO A 56 79.496 -40.999 -10.549 1.00 99.90 C ANISOU 28 CA PRO A 56 15105 10132 12719 387 290 -945 C ATOM 29 C PRO A 56 78.184 -41.233 -9.793 1.00 99.25 C ANISOU 29 C PRO A 56 15094 10098 12519 357 62 -790 C ATOM 30 O PRO A 56 77.134 -40.732 -10.210 1.00 98.29 O ANISOU 30 O PRO A 56 15121 9978 12246 258 39 -723 O ATOM 31 CB PRO A 56 80.238 -39.753 -10.035 1.00101.68 C ANISOU 31 CB PRO A 56 15108 10473 13053 364 368 -1018 C ATOM 32 CG PRO A 56 80.486 -38.888 -11.247 1.00106.95 C ANISOU 32 CG PRO A 56 15886 11080 13670 268 613 -1097 C ATOM 33 CD PRO A 56 79.461 -39.268 -12.262 1.00102.38 C ANISOU 33 CD PRO A 56 15613 10395 12893 213 609 -1024 C ATOM 34 N ALA A 57 78.238 -42.011 -8.692 1.00 92.44 N ANISOU 34 N ALA A 57 14133 9267 11723 447 -103 -740 N ATOM 35 CA ALA A 57 77.059 -42.379 -7.898 1.00 89.53 C ANISOU 35 CA ALA A 57 13832 8930 11257 420 -299 -599 C ATOM 36 C ALA A 57 76.520 -41.187 -7.047 1.00 88.19 C ANISOU 36 C ALA A 57 13556 8905 11047 352 -373 -541 C ATOM 37 O ALA A 57 75.915 -41.410 -5.995 1.00 87.30 O ANISOU 37 O ALA A 57 13416 8848 10906 359 -529 -446 O ATOM 38 CB ALA A 57 77.392 -43.549 -6.993 1.00 90.91 C ANISOU 38 CB ALA A 57 13959 9076 11508 543 -428 -567 C ATOM 39 N ILE A 58 76.650 -39.948 -7.561 1.00 80.88 N ANISOU 39 N ILE A 58 12604 8025 10103 278 -250 -593 N ATOM 40 CA ILE A 58 76.149 -38.732 -6.915 1.00 78.12 C ANISOU 40 CA ILE A 58 12175 7798 9711 210 -295 -549 C ATOM 41 C ILE A 58 74.597 -38.822 -6.752 1.00 77.95 C ANISOU 41 C ILE A 58 12287 7788 9542 136 -430 -423 C ATOM 42 O ILE A 58 74.121 -38.490 -5.663 1.00 76.99 O ANISOU 42 O ILE A 58 12077 7764 9411 126 -545 -355 O ATOM 43 CB ILE A 58 76.560 -37.440 -7.698 1.00 81.22 C ANISOU 43 CB ILE A 58 12562 8200 10098 140 -112 -632 C ATOM 44 CG1 ILE A 58 78.075 -37.414 -8.032 1.00 83.49 C ANISOU 44 CG1 ILE A 58 12721 8459 10543 193 57 -778 C ATOM 45 CG2 ILE A 58 76.103 -36.158 -6.958 1.00 79.79 C ANISOU 45 CG2 ILE A 58 12293 8140 9882 79 -159 -592 C ATOM 46 CD1 ILE A 58 78.533 -36.296 -9.054 1.00 94.21 C ANISOU 46 CD1 ILE A 58 14127 9780 11887 110 292 -871 C ATOM 47 N PRO A 59 73.788 -39.288 -7.759 1.00 71.96 N ANISOU 47 N PRO A 59 11731 6935 8675 86 -423 -397 N ATOM 48 CA PRO A 59 72.326 -39.333 -7.557 1.00 70.29 C ANISOU 48 CA PRO A 59 11607 6747 8352 14 -556 -298 C ATOM 49 C PRO A 59 71.919 -40.241 -6.397 1.00 73.58 C ANISOU 49 C PRO A 59 11976 7185 8797 40 -700 -217 C ATOM 50 O PRO A 59 70.936 -39.937 -5.717 1.00 72.40 O ANISOU 50 O PRO A 59 11804 7106 8596 -15 -798 -142 O ATOM 51 CB PRO A 59 71.804 -39.887 -8.883 1.00 72.39 C ANISOU 51 CB PRO A 59 12087 6893 8525 -24 -526 -315 C ATOM 52 CG PRO A 59 72.850 -39.558 -9.863 1.00 77.73 C ANISOU 52 CG PRO A 59 12805 7506 9224 2 -347 -416 C ATOM 53 CD PRO A 59 74.130 -39.725 -9.128 1.00 73.94 C ANISOU 53 CD PRO A 59 12138 7058 8898 87 -296 -467 C ATOM 54 N VAL A 60 72.691 -41.322 -6.146 1.00 70.69 N ANISOU 54 N VAL A 60 11596 6752 8510 129 -706 -234 N ATOM 55 CA VAL A 60 72.439 -42.250 -5.036 1.00 70.77 C ANISOU 55 CA VAL A 60 11593 6757 8538 170 -831 -156 C ATOM 56 C VAL A 60 72.674 -41.504 -3.704 1.00 73.83 C ANISOU 56 C VAL A 60 11813 7279 8962 198 -895 -125 C ATOM 57 O VAL A 60 71.847 -41.615 -2.802 1.00 73.31 O ANISOU 57 O VAL A 60 11754 7254 8846 162 -994 -36 O ATOM 58 CB VAL A 60 73.295 -43.539 -5.136 1.00 76.29 C ANISOU 58 CB VAL A 60 12334 7340 9312 280 -822 -187 C ATOM 59 CG1 VAL A 60 73.020 -44.475 -3.962 1.00 76.57 C ANISOU 59 CG1 VAL A 60 12392 7355 9349 326 -950 -96 C ATOM 60 CG2 VAL A 60 73.040 -44.264 -6.454 1.00 76.76 C ANISOU 60 CG2 VAL A 60 12574 7264 9329 246 -755 -223 C ATOM 61 N ILE A 61 73.770 -40.713 -3.608 1.00 69.77 N ANISOU 61 N ILE A 61 11149 6828 8531 253 -829 -208 N ATOM 62 CA ILE A 61 74.123 -39.911 -2.422 1.00 68.64 C ANISOU 62 CA ILE A 61 10838 6813 8427 281 -886 -204 C ATOM 63 C ILE A 61 73.012 -38.880 -2.153 1.00 71.48 C ANISOU 63 C ILE A 61 11204 7264 8693 169 -909 -143 C ATOM 64 O ILE A 61 72.617 -38.681 -1.005 1.00 70.73 O ANISOU 64 O ILE A 61 11056 7246 8572 167 -1004 -80 O ATOM 65 CB ILE A 61 75.512 -39.209 -2.594 1.00 71.76 C ANISOU 65 CB ILE A 61 11068 7252 8946 340 -789 -333 C ATOM 66 CG1 ILE A 61 76.619 -40.188 -3.047 1.00 72.96 C ANISOU 66 CG1 ILE A 61 11204 7309 9207 452 -743 -415 C ATOM 67 CG2 ILE A 61 75.914 -38.448 -1.319 1.00 72.03 C ANISOU 67 CG2 ILE A 61 10927 7416 9024 373 -867 -341 C ATOM 68 CD1 ILE A 61 77.942 -39.521 -3.468 1.00 77.84 C ANISOU 68 CD1 ILE A 61 11657 7954 9963 488 -607 -566 C ATOM 69 N ILE A 62 72.517 -38.237 -3.223 1.00 67.90 N ANISOU 69 N ILE A 62 10824 6791 8183 86 -824 -166 N ATOM 70 CA ILE A 62 71.458 -37.228 -3.158 1.00 66.77 C ANISOU 70 CA ILE A 62 10694 6721 7955 -7 -842 -121 C ATOM 71 C ILE A 62 70.163 -37.884 -2.625 1.00 70.04 C ANISOU 71 C ILE A 62 11180 7133 8299 -55 -958 -20 C ATOM 72 O ILE A 62 69.563 -37.347 -1.690 1.00 69.59 O ANISOU 72 O ILE A 62 11059 7167 8216 -88 -1017 32 O ATOM 73 CB ILE A 62 71.252 -36.563 -4.551 1.00 69.52 C ANISOU 73 CB ILE A 62 11146 7021 8247 -63 -735 -170 C ATOM 74 CG1 ILE A 62 72.500 -35.723 -4.926 1.00 70.08 C ANISOU 74 CG1 ILE A 62 11137 7101 8389 -38 -592 -272 C ATOM 75 CG2 ILE A 62 70.002 -35.687 -4.565 1.00 69.22 C ANISOU 75 CG2 ILE A 62 11146 7040 8114 -142 -781 -119 C ATOM 76 CD1 ILE A 62 72.493 -35.112 -6.311 1.00 76.45 C ANISOU 76 CD1 ILE A 62 12077 7837 9134 -84 -459 -324 C ATOM 77 N THR A 63 69.790 -39.074 -3.159 1.00 65.33 N ANISOU 77 N THR A 63 10711 6429 7683 -62 -980 1 N ATOM 78 CA THR A 63 68.584 -39.807 -2.745 1.00 64.30 C ANISOU 78 CA THR A 63 10652 6277 7502 -124 -1069 82 C ATOM 79 C THR A 63 68.708 -40.206 -1.267 1.00 65.95 C ANISOU 79 C THR A 63 10801 6526 7732 -85 -1138 147 C ATOM 80 O THR A 63 67.695 -40.237 -0.566 1.00 64.68 O ANISOU 80 O THR A 63 10647 6401 7527 -152 -1191 215 O ATOM 81 CB THR A 63 68.368 -41.030 -3.650 1.00 75.17 C ANISOU 81 CB THR A 63 12179 7516 8866 -136 -1066 72 C ATOM 82 OG1 THR A 63 68.388 -40.594 -5.006 1.00 75.32 O ANISOU 82 OG1 THR A 63 12270 7497 8851 -159 -1000 5 O ATOM 83 CG2 THR A 63 67.049 -41.754 -3.375 1.00 74.74 C ANISOU 83 CG2 THR A 63 12199 7430 8769 -226 -1141 136 C ATOM 84 N ALA A 64 69.954 -40.457 -0.794 1.00 62.34 N ANISOU 84 N ALA A 64 10282 6064 7340 28 -1138 120 N ATOM 85 CA ALA A 64 70.251 -40.817 0.595 1.00 62.26 C ANISOU 85 CA ALA A 64 10233 6085 7338 94 -1218 174 C ATOM 86 C ALA A 64 70.127 -39.590 1.529 1.00 66.48 C ANISOU 86 C ALA A 64 10643 6762 7853 73 -1241 185 C ATOM 87 O ALA A 64 69.576 -39.732 2.627 1.00 65.97 O ANISOU 87 O ALA A 64 10597 6731 7738 58 -1304 261 O ATOM 88 CB ALA A 64 71.642 -41.416 0.696 1.00 63.79 C ANISOU 88 CB ALA A 64 10392 6232 7616 237 -1227 122 C ATOM 89 N VAL A 65 70.626 -38.387 1.099 1.00 62.61 N ANISOU 89 N VAL A 65 10044 6346 7398 68 -1178 108 N ATOM 90 CA VAL A 65 70.512 -37.164 1.911 1.00 61.83 C ANISOU 90 CA VAL A 65 9835 6375 7283 43 -1191 107 C ATOM 91 C VAL A 65 69.020 -36.845 2.051 1.00 65.51 C ANISOU 91 C VAL A 65 10355 6873 7665 -67 -1205 178 C ATOM 92 O VAL A 65 68.536 -36.705 3.176 1.00 65.45 O ANISOU 92 O VAL A 65 10327 6925 7615 -83 -1257 236 O ATOM 93 CB VAL A 65 71.327 -35.956 1.349 1.00 65.33 C ANISOU 93 CB VAL A 65 10168 6871 7783 46 -1103 5 C ATOM 94 CG1 VAL A 65 71.112 -34.694 2.189 1.00 64.18 C ANISOU 94 CG1 VAL A 65 9925 6847 7615 10 -1116 6 C ATOM 95 CG2 VAL A 65 72.817 -36.285 1.254 1.00 66.22 C ANISOU 95 CG2 VAL A 65 10196 6959 8004 150 -1082 -84 C ATOM 96 N TYR A 66 68.279 -36.844 0.916 1.00 61.64 N ANISOU 96 N TYR A 66 9939 6333 7148 -137 -1164 170 N ATOM 97 CA TYR A 66 66.834 -36.617 0.882 1.00 61.37 C ANISOU 97 CA TYR A 66 9941 6323 7055 -235 -1185 217 C ATOM 98 C TYR A 66 66.109 -37.528 1.876 1.00 65.95 C ANISOU 98 C TYR A 66 10564 6887 7609 -267 -1242 299 C ATOM 99 O TYR A 66 65.257 -37.040 2.617 1.00 65.76 O ANISOU 99 O TYR A 66 10500 6934 7551 -324 -1257 337 O ATOM 100 CB TYR A 66 66.275 -36.827 -0.530 1.00 63.17 C ANISOU 100 CB TYR A 66 10263 6475 7262 -282 -1162 187 C ATOM 101 CG TYR A 66 66.287 -35.576 -1.386 1.00 65.73 C ANISOU 101 CG TYR A 66 10573 6834 7566 -293 -1110 131 C ATOM 102 CD1 TYR A 66 67.468 -35.101 -1.948 1.00 68.04 C ANISOU 102 CD1 TYR A 66 10853 7109 7891 -241 -1028 64 C ATOM 103 CD2 TYR A 66 65.103 -34.917 -1.708 1.00 66.65 C ANISOU 103 CD2 TYR A 66 10703 6988 7634 -355 -1138 139 C ATOM 104 CE1 TYR A 66 67.484 -33.953 -2.736 1.00 69.38 C ANISOU 104 CE1 TYR A 66 11042 7291 8029 -257 -962 18 C ATOM 105 CE2 TYR A 66 65.101 -33.787 -2.524 1.00 67.57 C ANISOU 105 CE2 TYR A 66 10840 7117 7716 -353 -1096 94 C ATOM 106 CZ TYR A 66 66.295 -33.309 -3.038 1.00 76.94 C ANISOU 106 CZ TYR A 66 12037 8276 8920 -307 -1002 39 C ATOM 107 OH TYR A 66 66.308 -32.198 -3.846 1.00 80.13 O ANISOU 107 OH TYR A 66 12493 8674 9279 -310 -943 -1 O ATOM 108 N SER A 67 66.492 -38.820 1.945 1.00 62.63 N ANISOU 108 N SER A 67 10229 6367 7202 -226 -1262 324 N ATOM 109 CA SER A 67 65.890 -39.774 2.872 1.00 62.62 C ANISOU 109 CA SER A 67 10303 6322 7168 -256 -1299 405 C ATOM 110 C SER A 67 66.080 -39.317 4.323 1.00 67.40 C ANISOU 110 C SER A 67 10855 7012 7740 -222 -1329 449 C ATOM 111 O SER A 67 65.119 -39.334 5.091 1.00 67.38 O ANISOU 111 O SER A 67 10874 7034 7691 -298 -1327 506 O ATOM 112 CB SER A 67 66.483 -41.165 2.676 1.00 65.66 C ANISOU 112 CB SER A 67 10803 6572 7572 -194 -1313 419 C ATOM 113 OG SER A 67 66.251 -41.653 1.368 1.00 72.75 O ANISOU 113 OG SER A 67 11769 7384 8489 -232 -1284 377 O ATOM 114 N VAL A 68 67.299 -38.862 4.678 1.00 64.35 N ANISOU 114 N VAL A 68 10394 6674 7382 -114 -1352 411 N ATOM 115 CA VAL A 68 67.624 -38.417 6.034 1.00 64.90 C ANISOU 115 CA VAL A 68 10418 6824 7415 -66 -1399 438 C ATOM 116 C VAL A 68 66.788 -37.165 6.360 1.00 68.42 C ANISOU 116 C VAL A 68 10784 7385 7828 -153 -1367 437 C ATOM 117 O VAL A 68 65.955 -37.219 7.263 1.00 67.92 O ANISOU 117 O VAL A 68 10759 7344 7702 -208 -1370 500 O ATOM 118 CB VAL A 68 69.153 -38.162 6.218 1.00 69.34 C ANISOU 118 CB VAL A 68 10892 7418 8036 69 -1442 369 C ATOM 119 CG1 VAL A 68 69.463 -37.527 7.580 1.00 69.29 C ANISOU 119 CG1 VAL A 68 10830 7510 7986 114 -1505 380 C ATOM 120 CG2 VAL A 68 69.954 -39.450 6.027 1.00 70.21 C ANISOU 120 CG2 VAL A 68 11081 7414 8183 175 -1483 371 C ATOM 121 N VAL A 69 66.959 -36.085 5.571 1.00 64.80 N ANISOU 121 N VAL A 69 10228 6984 7410 -170 -1325 364 N ATOM 122 CA VAL A 69 66.283 -34.787 5.734 1.00 63.83 C ANISOU 122 CA VAL A 69 10028 6961 7264 -234 -1293 350 C ATOM 123 C VAL A 69 64.737 -34.986 5.795 1.00 67.98 C ANISOU 123 C VAL A 69 10599 7482 7750 -341 -1278 404 C ATOM 124 O VAL A 69 64.080 -34.340 6.617 1.00 67.97 O ANISOU 124 O VAL A 69 10557 7556 7712 -382 -1269 426 O ATOM 125 CB VAL A 69 66.671 -33.789 4.597 1.00 66.66 C ANISOU 125 CB VAL A 69 10323 7338 7666 -235 -1238 267 C ATOM 126 CG1 VAL A 69 66.026 -32.422 4.815 1.00 65.67 C ANISOU 126 CG1 VAL A 69 10131 7305 7515 -286 -1210 254 C ATOM 127 CG2 VAL A 69 68.185 -33.636 4.478 1.00 66.77 C ANISOU 127 CG2 VAL A 69 10275 7351 7743 -147 -1230 196 C ATOM 128 N PHE A 70 64.177 -35.889 4.952 1.00 63.81 N ANISOU 128 N PHE A 70 10146 6864 7235 -386 -1273 415 N ATOM 129 CA PHE A 70 62.734 -36.153 4.912 1.00 62.82 C ANISOU 129 CA PHE A 70 10042 6730 7096 -494 -1261 444 C ATOM 130 C PHE A 70 62.251 -36.790 6.226 1.00 67.71 C ANISOU 130 C PHE A 70 10711 7342 7675 -532 -1255 519 C ATOM 131 O PHE A 70 61.348 -36.237 6.854 1.00 67.53 O ANISOU 131 O PHE A 70 10639 7387 7633 -598 -1226 532 O ATOM 132 CB PHE A 70 62.362 -37.053 3.718 1.00 64.01 C ANISOU 132 CB PHE A 70 10267 6778 7274 -532 -1267 426 C ATOM 133 CG PHE A 70 60.938 -37.548 3.709 1.00 64.83 C ANISOU 133 CG PHE A 70 10386 6861 7384 -649 -1263 442 C ATOM 134 CD1 PHE A 70 59.891 -36.693 3.406 1.00 66.54 C ANISOU 134 CD1 PHE A 70 10517 7152 7615 -709 -1266 405 C ATOM 135 CD2 PHE A 70 60.652 -38.888 3.917 1.00 67.48 C ANISOU 135 CD2 PHE A 70 10822 7095 7723 -697 -1256 483 C ATOM 136 CE1 PHE A 70 58.572 -37.150 3.403 1.00 67.87 C ANISOU 136 CE1 PHE A 70 10669 7307 7811 -818 -1264 400 C ATOM 137 CE2 PHE A 70 59.334 -39.352 3.883 1.00 70.77 C ANISOU 137 CE2 PHE A 70 11237 7488 8162 -822 -1240 480 C ATOM 138 CZ PHE A 70 58.303 -38.480 3.622 1.00 68.22 C ANISOU 138 CZ PHE A 70 10801 7253 7866 -883 -1246 433 C ATOM 139 N VAL A 71 62.850 -37.922 6.643 1.00 64.64 N ANISOU 139 N VAL A 71 10429 6864 7267 -486 -1274 565 N ATOM 140 CA VAL A 71 62.444 -38.637 7.854 1.00 65.44 C ANISOU 140 CA VAL A 71 10626 6929 7309 -518 -1259 644 C ATOM 141 C VAL A 71 62.735 -37.754 9.103 1.00 70.64 C ANISOU 141 C VAL A 71 11242 7690 7908 -475 -1267 662 C ATOM 142 O VAL A 71 61.818 -37.532 9.893 1.00 70.83 O ANISOU 142 O VAL A 71 11271 7750 7890 -555 -1217 695 O ATOM 143 CB VAL A 71 63.115 -40.029 7.970 1.00 70.01 C ANISOU 143 CB VAL A 71 11355 7372 7871 -456 -1288 691 C ATOM 144 CG1 VAL A 71 62.746 -40.715 9.281 1.00 70.73 C ANISOU 144 CG1 VAL A 71 11581 7413 7879 -481 -1266 780 C ATOM 145 CG2 VAL A 71 62.722 -40.915 6.794 1.00 70.24 C ANISOU 145 CG2 VAL A 71 11439 7295 7954 -513 -1272 669 C ATOM 146 N VAL A 72 63.970 -37.225 9.254 1.00 67.17 N ANISOU 146 N VAL A 72 10753 7298 7471 -358 -1324 628 N ATOM 147 CA VAL A 72 64.351 -36.374 10.395 1.00 67.16 C ANISOU 147 CA VAL A 72 10711 7393 7414 -311 -1348 629 C ATOM 148 C VAL A 72 63.320 -35.229 10.543 1.00 72.35 C ANISOU 148 C VAL A 72 11276 8150 8066 -406 -1285 610 C ATOM 149 O VAL A 72 62.801 -35.015 11.639 1.00 72.63 O ANISOU 149 O VAL A 72 11343 8223 8031 -440 -1258 649 O ATOM 150 CB VAL A 72 65.805 -35.827 10.246 1.00 70.52 C ANISOU 150 CB VAL A 72 11050 7864 7881 -188 -1415 559 C ATOM 151 CG1 VAL A 72 66.109 -34.706 11.240 1.00 70.00 C ANISOU 151 CG1 VAL A 72 10913 7913 7772 -160 -1439 533 C ATOM 152 CG2 VAL A 72 66.832 -36.953 10.360 1.00 71.26 C ANISOU 152 CG2 VAL A 72 11228 7868 7978 -73 -1490 576 C ATOM 153 N GLY A 73 62.994 -34.575 9.429 1.00 69.31 N ANISOU 153 N GLY A 73 10794 7792 7748 -443 -1260 551 N ATOM 154 CA GLY A 73 62.046 -33.466 9.388 1.00 68.72 C ANISOU 154 CA GLY A 73 10627 7803 7681 -512 -1212 522 C ATOM 155 C GLY A 73 60.603 -33.842 9.648 1.00 72.85 C ANISOU 155 C GLY A 73 11167 8313 8198 -624 -1156 557 C ATOM 156 O GLY A 73 59.900 -33.129 10.371 1.00 72.63 O ANISOU 156 O GLY A 73 11091 8358 8146 -668 -1111 557 O ATOM 157 N LEU A 74 60.150 -34.961 9.070 1.00 69.33 N ANISOU 157 N LEU A 74 10785 7774 7781 -676 -1151 576 N ATOM 158 CA LEU A 74 58.768 -35.390 9.223 1.00 69.80 C ANISOU 158 CA LEU A 74 10844 7816 7860 -798 -1090 590 C ATOM 159 C LEU A 74 58.533 -35.940 10.656 1.00 74.99 C ANISOU 159 C LEU A 74 11602 8450 8442 -837 -1030 663 C ATOM 160 O LEU A 74 57.535 -35.584 11.272 1.00 74.55 O ANISOU 160 O LEU A 74 11503 8441 8382 -921 -954 662 O ATOM 161 CB LEU A 74 58.418 -36.438 8.157 1.00 70.19 C ANISOU 161 CB LEU A 74 10938 7765 7965 -848 -1105 578 C ATOM 162 CG LEU A 74 56.943 -36.682 7.886 1.00 75.71 C ANISOU 162 CG LEU A 74 11583 8460 8726 -980 -1061 548 C ATOM 163 CD1 LEU A 74 56.287 -35.441 7.270 1.00 75.19 C ANISOU 163 CD1 LEU A 74 11363 8495 8708 -982 -1084 473 C ATOM 164 CD2 LEU A 74 56.768 -37.840 6.926 1.00 79.28 C ANISOU 164 CD2 LEU A 74 12101 8798 9222 -1026 -1085 534 C ATOM 165 N VAL A 75 59.478 -36.745 11.199 1.00 72.14 N ANISOU 165 N VAL A 75 11380 8016 8016 -765 -1063 722 N ATOM 166 CA VAL A 75 59.392 -37.307 12.560 1.00 72.91 C ANISOU 166 CA VAL A 75 11620 8072 8012 -780 -1017 800 C ATOM 167 C VAL A 75 59.550 -36.171 13.595 1.00 76.81 C ANISOU 167 C VAL A 75 12071 8678 8435 -743 -1011 795 C ATOM 168 O VAL A 75 58.724 -36.057 14.497 1.00 77.33 O ANISOU 168 O VAL A 75 12172 8761 8450 -822 -919 823 O ATOM 169 CB VAL A 75 60.436 -38.443 12.805 1.00 77.14 C ANISOU 169 CB VAL A 75 12327 8491 8489 -683 -1082 861 C ATOM 170 CG1 VAL A 75 60.461 -38.887 14.266 1.00 78.14 C ANISOU 170 CG1 VAL A 75 12632 8574 8483 -672 -1052 945 C ATOM 171 CG2 VAL A 75 60.178 -39.632 11.892 1.00 77.34 C ANISOU 171 CG2 VAL A 75 12420 8390 8575 -734 -1070 868 C ATOM 172 N GLY A 76 60.593 -35.352 13.432 1.00 72.40 N ANISOU 172 N GLY A 76 11437 8191 7881 -631 -1097 752 N ATOM 173 CA GLY A 76 60.914 -34.238 14.317 1.00 71.84 C ANISOU 173 CA GLY A 76 11322 8224 7750 -586 -1109 732 C ATOM 174 C GLY A 76 59.760 -33.293 14.558 1.00 75.20 C ANISOU 174 C GLY A 76 11651 8732 8189 -680 -1014 703 C ATOM 175 O GLY A 76 59.336 -33.118 15.702 1.00 74.88 O ANISOU 175 O GLY A 76 11672 8716 8063 -713 -953 734 O ATOM 176 N ASN A 77 59.206 -32.726 13.470 1.00 71.48 N ANISOU 176 N ASN A 77 11042 8297 7822 -720 -1000 643 N ATOM 177 CA ASN A 77 58.096 -31.769 13.525 1.00 71.01 C ANISOU 177 CA ASN A 77 10867 8316 7798 -790 -926 600 C ATOM 178 C ASN A 77 56.791 -32.445 13.969 1.00 76.36 C ANISOU 178 C ASN A 77 11573 8957 8482 -915 -818 628 C ATOM 179 O ASN A 77 55.976 -31.793 14.621 1.00 75.96 O ANISOU 179 O ASN A 77 11469 8969 8424 -967 -734 609 O ATOM 180 CB ASN A 77 57.900 -31.090 12.179 1.00 68.23 C ANISOU 180 CB ASN A 77 10386 7994 7545 -780 -962 530 C ATOM 181 CG ASN A 77 58.995 -30.099 11.868 1.00 81.27 C ANISOU 181 CG ASN A 77 11993 9692 9192 -683 -1022 487 C ATOM 182 OD1 ASN A 77 59.116 -29.043 12.506 1.00 70.98 O ANISOU 182 OD1 ASN A 77 10649 8464 7857 -659 -1005 462 O ATOM 183 ND2 ASN A 77 59.787 -30.388 10.851 1.00 72.72 N ANISOU 183 ND2 ASN A 77 10918 8562 8149 -632 -1082 469 N ATOM 184 N SER A 78 56.605 -33.738 13.668 1.00 74.50 N ANISOU 184 N SER A 78 11425 8618 8264 -966 -808 667 N ATOM 185 CA SER A 78 55.411 -34.439 14.132 1.00 76.11 C ANISOU 185 CA SER A 78 11662 8774 8480 -1101 -686 688 C ATOM 186 C SER A 78 55.508 -34.708 15.630 1.00 82.08 C ANISOU 186 C SER A 78 12577 9506 9104 -1114 -606 759 C ATOM 187 O SER A 78 54.482 -34.733 16.312 1.00 82.74 O ANISOU 187 O SER A 78 12662 9592 9182 -1223 -470 760 O ATOM 188 CB SER A 78 55.203 -35.739 13.367 1.00 80.14 C ANISOU 188 CB SER A 78 12232 9169 9047 -1161 -692 702 C ATOM 189 OG SER A 78 54.961 -35.482 11.992 1.00 86.28 O ANISOU 189 OG SER A 78 12875 9970 9938 -1158 -762 629 O ATOM 190 N LEU A 79 56.748 -34.867 16.144 1.00 79.28 N ANISOU 190 N LEU A 79 12354 9127 8640 -997 -691 811 N ATOM 191 CA LEU A 79 57.011 -35.114 17.556 1.00 80.67 C ANISOU 191 CA LEU A 79 12715 9274 8662 -978 -650 882 C ATOM 192 C LEU A 79 56.715 -33.856 18.366 1.00 85.02 C ANISOU 192 C LEU A 79 13198 9940 9166 -979 -599 846 C ATOM 193 O LEU A 79 56.069 -33.951 19.408 1.00 86.02 O ANISOU 193 O LEU A 79 13425 10052 9208 -1050 -474 879 O ATOM 194 CB LEU A 79 58.469 -35.561 17.751 1.00 80.94 C ANISOU 194 CB LEU A 79 12880 9262 8611 -828 -794 926 C ATOM 195 CG LEU A 79 58.804 -36.283 19.044 1.00 87.65 C ANISOU 195 CG LEU A 79 13984 10029 9289 -792 -783 1017 C ATOM 196 CD1 LEU A 79 58.381 -37.747 18.945 1.00 89.30 C ANISOU 196 CD1 LEU A 79 14362 10079 9488 -865 -713 1088 C ATOM 197 CD2 LEU A 79 60.276 -36.325 19.234 1.00 90.72 C ANISOU 197 CD2 LEU A 79 14436 10419 9614 -618 -957 1025 C ATOM 198 N VAL A 80 57.152 -32.675 17.860 1.00 80.75 N ANISOU 198 N VAL A 80 12494 9505 8681 -907 -680 775 N ATOM 199 CA VAL A 80 56.963 -31.359 18.495 1.00 80.79 C ANISOU 199 CA VAL A 80 12422 9620 8653 -896 -644 727 C ATOM 200 C VAL A 80 55.463 -31.078 18.674 1.00 86.38 C ANISOU 200 C VAL A 80 13046 10356 9417 -1024 -484 698 C ATOM 201 O VAL A 80 55.035 -30.779 19.792 1.00 87.30 O ANISOU 201 O VAL A 80 13230 10495 9446 -1062 -380 709 O ATOM 202 CB VAL A 80 57.650 -30.209 17.695 1.00 82.95 C ANISOU 202 CB VAL A 80 12539 9980 9000 -809 -748 651 C ATOM 203 CG1 VAL A 80 57.316 -28.841 18.283 1.00 82.30 C ANISOU 203 CG1 VAL A 80 12376 9998 8896 -810 -697 597 C ATOM 204 CG2 VAL A 80 59.158 -30.403 17.638 1.00 82.51 C ANISOU 204 CG2 VAL A 80 12542 9906 8901 -689 -889 661 C ATOM 205 N MET A 81 54.675 -31.194 17.583 1.00 82.88 N ANISOU 205 N MET A 81 12459 9911 9123 -1087 -467 652 N ATOM 206 CA MET A 81 53.229 -30.959 17.603 1.00 83.61 C ANISOU 206 CA MET A 81 12429 10034 9304 -1202 -333 601 C ATOM 207 C MET A 81 52.543 -31.880 18.610 1.00 89.35 C ANISOU 207 C MET A 81 13293 10686 9968 -1320 -172 653 C ATOM 208 O MET A 81 51.737 -31.399 19.405 1.00 89.94 O ANISOU 208 O MET A 81 13339 10803 10030 -1385 -33 627 O ATOM 209 CB MET A 81 52.610 -31.147 16.213 1.00 85.67 C ANISOU 209 CB MET A 81 12533 10290 9728 -1239 -377 542 C ATOM 210 CG MET A 81 53.103 -30.142 15.199 1.00 88.24 C ANISOU 210 CG MET A 81 12736 10681 10110 -1133 -507 486 C ATOM 211 SD MET A 81 52.330 -30.283 13.572 1.00 92.60 S ANISOU 211 SD MET A 81 13132 11226 10827 -1161 -576 412 S ATOM 212 CE MET A 81 52.878 -31.913 13.071 1.00 89.82 C ANISOU 212 CE MET A 81 12920 10745 10462 -1192 -621 474 C ATOM 213 N PHE A 82 52.909 -33.185 18.619 1.00 86.26 N ANISOU 213 N PHE A 82 13068 10176 9529 -1343 -182 728 N ATOM 214 CA PHE A 82 52.357 -34.179 19.537 1.00 87.76 C ANISOU 214 CA PHE A 82 13436 10266 9644 -1457 -23 789 C ATOM 215 C PHE A 82 52.509 -33.724 20.996 1.00 92.72 C ANISOU 215 C PHE A 82 14215 10913 10101 -1437 62 830 C ATOM 216 O PHE A 82 51.533 -33.769 21.751 1.00 94.51 O ANISOU 216 O PHE A 82 14471 11126 10312 -1556 254 823 O ATOM 217 CB PHE A 82 53.030 -35.551 19.340 1.00 90.08 C ANISOU 217 CB PHE A 82 13925 10418 9883 -1440 -82 873 C ATOM 218 CG PHE A 82 52.641 -36.570 20.391 1.00 94.09 C ANISOU 218 CG PHE A 82 14676 10798 10275 -1540 80 954 C ATOM 219 CD1 PHE A 82 51.460 -37.296 20.278 1.00 98.72 C ANISOU 219 CD1 PHE A 82 15241 11312 10955 -1719 252 933 C ATOM 220 CD2 PHE A 82 53.454 -36.799 21.499 1.00 97.22 C ANISOU 220 CD2 PHE A 82 15333 11142 10466 -1454 60 1046 C ATOM 221 CE1 PHE A 82 51.091 -38.221 21.262 1.00101.81 C ANISOU 221 CE1 PHE A 82 15879 11570 11235 -1824 428 1008 C ATOM 222 CE2 PHE A 82 53.082 -37.721 22.484 1.00102.17 C ANISOU 222 CE2 PHE A 82 16221 11634 10963 -1542 218 1127 C ATOM 223 CZ PHE A 82 51.907 -38.429 22.356 1.00101.63 C ANISOU 223 CZ PHE A 82 16141 11485 10988 -1732 413 1111 C ATOM 224 N VAL A 83 53.723 -33.282 21.381 1.00 87.51 N ANISOU 224 N VAL A 83 13647 10285 9317 -1290 -78 862 N ATOM 225 CA VAL A 83 54.038 -32.839 22.740 1.00 87.67 C ANISOU 225 CA VAL A 83 13831 10325 9155 -1248 -38 896 C ATOM 226 C VAL A 83 53.142 -31.633 23.110 1.00 90.82 C ANISOU 226 C VAL A 83 14076 10833 9597 -1304 86 816 C ATOM 227 O VAL A 83 52.531 -31.648 24.175 1.00 92.08 O ANISOU 227 O VAL A 83 14355 10973 9660 -1379 254 834 O ATOM 228 CB VAL A 83 55.551 -32.503 22.886 1.00 90.46 C ANISOU 228 CB VAL A 83 14256 10709 9407 -1073 -248 915 C ATOM 229 CG1 VAL A 83 55.864 -31.898 24.251 1.00 91.07 C ANISOU 229 CG1 VAL A 83 14483 10823 9298 -1023 -230 930 C ATOM 230 CG2 VAL A 83 56.412 -33.740 22.643 1.00 90.62 C ANISOU 230 CG2 VAL A 83 14438 10614 9380 -1006 -361 992 C ATOM 231 N ILE A 84 53.021 -30.640 22.209 1.00 85.10 N ANISOU 231 N ILE A 84 13104 10213 9019 -1269 17 728 N ATOM 232 CA ILE A 84 52.237 -29.420 22.431 1.00 84.70 C ANISOU 232 CA ILE A 84 12892 10265 9024 -1295 110 643 C ATOM 233 C ILE A 84 50.723 -29.761 22.550 1.00 90.96 C ANISOU 233 C ILE A 84 13604 11039 9919 -1454 322 607 C ATOM 234 O ILE A 84 50.064 -29.237 23.449 1.00 91.55 O ANISOU 234 O ILE A 84 13687 11147 9952 -1506 479 578 O ATOM 235 CB ILE A 84 52.500 -28.385 21.295 1.00 85.62 C ANISOU 235 CB ILE A 84 12786 10472 9274 -1210 -27 564 C ATOM 236 CG1 ILE A 84 53.976 -27.912 21.331 1.00 84.66 C ANISOU 236 CG1 ILE A 84 12733 10376 9059 -1071 -200 581 C ATOM 237 CG2 ILE A 84 51.550 -27.181 21.392 1.00 86.08 C ANISOU 237 CG2 ILE A 84 12669 10623 9414 -1233 69 473 C ATOM 238 CD1 ILE A 84 54.400 -26.992 20.210 1.00 88.38 C ANISOU 238 CD1 ILE A 84 13028 10909 9641 -992 -323 513 C ATOM 239 N ILE A 85 50.191 -30.634 21.677 1.00 88.67 N ANISOU 239 N ILE A 85 13236 10693 9762 -1534 332 599 N ATOM 240 CA ILE A 85 48.766 -30.992 21.689 1.00 90.37 C ANISOU 240 CA ILE A 85 13339 10892 10105 -1693 522 543 C ATOM 241 C ILE A 85 48.421 -31.805 22.968 1.00 98.22 C ANISOU 241 C ILE A 85 14568 11788 10964 -1809 734 611 C ATOM 242 O ILE A 85 47.423 -31.496 23.628 1.00 99.60 O ANISOU 242 O ILE A 85 14689 11986 11168 -1910 938 558 O ATOM 243 CB ILE A 85 48.364 -31.786 20.399 1.00 92.96 C ANISOU 243 CB ILE A 85 13536 11179 10607 -1751 459 511 C ATOM 244 CG1 ILE A 85 48.584 -30.925 19.131 1.00 91.47 C ANISOU 244 CG1 ILE A 85 13134 11081 10541 -1640 268 439 C ATOM 245 CG2 ILE A 85 46.898 -32.271 20.469 1.00 95.28 C ANISOU 245 CG2 ILE A 85 13710 11448 11044 -1932 660 440 C ATOM 246 CD1 ILE A 85 48.370 -31.644 17.786 1.00 98.38 C ANISOU 246 CD1 ILE A 85 13908 11916 11558 -1669 166 408 C ATOM 247 N ARG A 86 49.243 -32.815 23.318 1.00 95.94 N ANISOU 247 N ARG A 86 14545 11383 10523 -1787 691 723 N ATOM 248 CA ARG A 86 48.945 -33.724 24.426 1.00 98.28 C ANISOU 248 CA ARG A 86 15108 11557 10678 -1895 887 799 C ATOM 249 C ARG A 86 49.466 -33.245 25.807 1.00103.67 C ANISOU 249 C ARG A 86 16026 12244 11121 -1827 929 856 C ATOM 250 O ARG A 86 49.013 -33.804 26.812 1.00105.59 O ANISOU 250 O ARG A 86 16487 12393 11241 -1928 1132 905 O ATOM 251 CB ARG A 86 49.560 -35.106 24.150 1.00 98.55 C ANISOU 251 CB ARG A 86 15349 11443 10653 -1893 816 897 C ATOM 252 N TYR A 87 50.401 -32.265 25.886 1.00 98.79 N ANISOU 252 N TYR A 87 15385 11723 10429 -1666 749 847 N ATOM 253 CA TYR A 87 50.948 -31.922 27.204 1.00 99.63 C ANISOU 253 CA TYR A 87 15737 11823 10295 -1600 768 898 C ATOM 254 C TYR A 87 50.941 -30.408 27.504 1.00103.33 C ANISOU 254 C TYR A 87 16062 12434 10764 -1536 751 813 C ATOM 255 O TYR A 87 50.568 -30.042 28.623 1.00104.85 O ANISOU 255 O TYR A 87 16385 12628 10825 -1574 906 811 O ATOM 256 CB TYR A 87 52.398 -32.431 27.337 1.00100.54 C ANISOU 256 CB TYR A 87 16068 11882 10249 -1447 543 989 C ATOM 257 CG TYR A 87 52.532 -33.933 27.182 1.00103.91 C ANISOU 257 CG TYR A 87 16689 12152 10640 -1486 551 1084 C ATOM 258 CD1 TYR A 87 52.425 -34.781 28.280 1.00108.29 C ANISOU 258 CD1 TYR A 87 17584 12569 10992 -1534 685 1180 C ATOM 259 CD2 TYR A 87 52.750 -34.509 25.933 1.00103.60 C ANISOU 259 CD2 TYR A 87 16513 12088 10762 -1475 433 1078 C ATOM 260 CE1 TYR A 87 52.522 -36.165 28.139 1.00110.08 C ANISOU 260 CE1 TYR A 87 18009 12634 11184 -1570 703 1269 C ATOM 261 CE2 TYR A 87 52.839 -35.892 25.779 1.00105.44 C ANISOU 261 CE2 TYR A 87 16929 12166 10967 -1514 450 1160 C ATOM 262 CZ TYR A 87 52.732 -36.715 26.885 1.00115.19 C ANISOU 262 CZ TYR A 87 18501 13262 12005 -1560 584 1256 C ATOM 263 OH TYR A 87 52.835 -38.076 26.733 1.00118.43 O ANISOU 263 OH TYR A 87 19111 13504 12384 -1594 603 1339 O ATOM 264 N THR A 88 51.391 -29.544 26.571 1.00 97.49 N ANISOU 264 N THR A 88 15089 11800 10153 -1438 572 747 N ATOM 265 CA THR A 88 51.500 -28.111 26.873 1.00 96.46 C ANISOU 265 CA THR A 88 14853 11787 10010 -1369 547 671 C ATOM 266 C THR A 88 50.149 -27.385 26.685 1.00101.60 C ANISOU 266 C THR A 88 15272 12506 10826 -1462 726 570 C ATOM 267 O THR A 88 49.930 -26.364 27.340 1.00101.76 O ANISOU 267 O THR A 88 15272 12593 10798 -1443 797 515 O ATOM 268 CB THR A 88 52.577 -27.433 26.012 1.00100.37 C ANISOU 268 CB THR A 88 15219 12354 10564 -1229 301 639 C ATOM 269 OG1 THR A 88 52.109 -27.237 24.682 1.00 99.00 O ANISOU 269 OG1 THR A 88 14788 12217 10612 -1246 264 579 O ATOM 270 CG2 THR A 88 53.923 -28.168 26.042 1.00 97.29 C ANISOU 270 CG2 THR A 88 15007 11904 10055 -1128 112 718 C ATOM 271 N LYS A 89 49.273 -27.885 25.774 1.00 98.93 N ANISOU 271 N LYS A 89 14751 12152 10685 -1554 783 535 N ATOM 272 CA LYS A 89 47.929 -27.347 25.448 1.00 99.58 C ANISOU 272 CA LYS A 89 14579 12296 10961 -1638 930 426 C ATOM 273 C LYS A 89 48.000 -25.920 24.784 1.00102.42 C ANISOU 273 C LYS A 89 14711 12775 11430 -1525 807 333 C ATOM 274 O LYS A 89 46.951 -25.312 24.534 1.00102.22 O ANISOU 274 O LYS A 89 14470 12808 11560 -1560 903 235 O ATOM 275 CB LYS A 89 47.034 -27.281 26.705 1.00104.14 C ANISOU 275 CB LYS A 89 15247 12857 11466 -1749 1206 406 C ATOM 276 N MET A 90 49.213 -25.464 24.491 1.00 97.73 N ANISOU 276 N MET A 90 14167 12204 10761 -1394 604 362 N ATOM 277 CA MET A 90 49.444 -24.178 23.840 1.00 96.30 C ANISOU 277 CA MET A 90 13816 12111 10662 -1287 486 288 C ATOM 278 C MET A 90 48.563 -23.036 24.337 1.00 99.89 C ANISOU 278 C MET A 90 14155 12636 11162 -1293 623 195 C ATOM 279 O MET A 90 47.877 -22.386 23.548 1.00 99.07 O ANISOU 279 O MET A 90 13831 12583 11228 -1270 609 112 O ATOM 280 CB MET A 90 49.297 -24.321 22.322 1.00 97.75 C ANISOU 280 CB MET A 90 13812 12300 11029 -1264 357 257 C ATOM 281 CG MET A 90 47.862 -24.492 21.851 1.00102.81 C ANISOU 281 CG MET A 90 14252 12955 11856 -1353 469 182 C ATOM 282 SD MET A 90 47.699 -24.369 20.059 1.00106.10 S ANISOU 282 SD MET A 90 14456 13392 12467 -1293 285 127 S ATOM 283 CE MET A 90 46.017 -24.940 19.832 1.00104.79 C ANISOU 283 CE MET A 90 14091 13229 12498 -1427 430 42 C ATOM 284 N LYS A 91 48.583 -22.792 25.642 1.00 96.49 N ANISOU 284 N LYS A 91 13883 12204 10575 -1315 750 207 N ATOM 285 CA LYS A 91 47.805 -21.688 26.219 1.00 96.14 C ANISOU 285 CA LYS A 91 13750 12222 10558 -1316 894 117 C ATOM 286 C LYS A 91 48.626 -20.385 26.176 1.00 96.62 C ANISOU 286 C LYS A 91 13804 12339 10568 -1187 760 79 C ATOM 287 O LYS A 91 48.046 -19.300 26.179 1.00 96.30 O ANISOU 287 O LYS A 91 13632 12352 10604 -1153 820 -9 O ATOM 288 CB LYS A 91 47.359 -22.006 27.657 1.00100.43 C ANISOU 288 CB LYS A 91 14479 12730 10951 -1409 1122 137 C ATOM 289 CG LYS A 91 46.354 -23.153 27.740 1.00113.29 C ANISOU 289 CG LYS A 91 16094 14297 12653 -1560 1308 151 C ATOM 290 CD LYS A 91 45.918 -23.461 29.171 1.00123.40 C ANISOU 290 CD LYS A 91 17587 15527 13771 -1660 1560 173 C ATOM 291 CE LYS A 91 47.028 -23.982 30.057 1.00131.90 C ANISOU 291 CE LYS A 91 19012 16535 14570 -1627 1497 289 C ATOM 292 NZ LYS A 91 47.571 -25.288 29.592 1.00139.57 N ANISOU 292 NZ LYS A 91 20095 17418 15515 -1647 1389 392 N ATOM 293 N THR A 92 49.972 -20.504 26.110 1.00 90.43 N ANISOU 293 N THR A 92 13154 11538 9666 -1115 581 139 N ATOM 294 CA THR A 92 50.917 -19.382 26.028 1.00 88.13 C ANISOU 294 CA THR A 92 12867 11289 9331 -1008 445 102 C ATOM 295 C THR A 92 51.183 -19.020 24.562 1.00 88.52 C ANISOU 295 C THR A 92 12741 11351 9539 -942 293 74 C ATOM 296 O THR A 92 51.047 -19.873 23.684 1.00 87.59 O ANISOU 296 O THR A 92 12561 11203 9516 -965 239 110 O ATOM 297 CB THR A 92 52.242 -19.725 26.750 1.00 94.19 C ANISOU 297 CB THR A 92 13856 12032 9899 -968 331 163 C ATOM 298 OG1 THR A 92 52.881 -20.826 26.098 1.00 91.86 O ANISOU 298 OG1 THR A 92 13595 11688 9619 -962 204 238 O ATOM 299 CG2 THR A 92 52.053 -20.029 28.232 1.00 94.66 C ANISOU 299 CG2 THR A 92 14133 12069 9765 -1018 467 194 C ATOM 300 N ALA A 93 51.595 -17.764 24.310 1.00 82.76 N ANISOU 300 N ALA A 93 11957 10659 8830 -861 227 11 N ATOM 301 CA ALA A 93 51.918 -17.251 22.976 1.00 80.29 C ANISOU 301 CA ALA A 93 11518 10347 8641 -791 96 -17 C ATOM 302 C ALA A 93 53.155 -17.943 22.396 1.00 82.14 C ANISOU 302 C ALA A 93 11818 10546 8844 -766 -65 42 C ATOM 303 O ALA A 93 53.222 -18.158 21.184 1.00 81.14 O ANISOU 303 O ALA A 93 11605 10399 8826 -744 -150 47 O ATOM 304 CB ALA A 93 52.148 -15.750 23.041 1.00 80.54 C ANISOU 304 CB ALA A 93 11522 10407 8671 -721 88 -95 C ATOM 305 N THR A 94 54.121 -18.304 23.268 1.00 77.99 N ANISOU 305 N THR A 94 11450 10013 8169 -764 -108 80 N ATOM 306 CA THR A 94 55.380 -18.970 22.919 1.00 76.74 C ANISOU 306 CA THR A 94 11358 9825 7973 -730 -259 126 C ATOM 307 C THR A 94 55.086 -20.288 22.177 1.00 78.64 C ANISOU 307 C THR A 94 11580 10016 8283 -768 -279 194 C ATOM 308 O THR A 94 55.500 -20.437 21.026 1.00 77.23 O ANISOU 308 O THR A 94 11329 9817 8197 -736 -376 194 O ATOM 309 CB THR A 94 56.208 -19.208 24.197 1.00 89.80 C ANISOU 309 CB THR A 94 13191 11483 9447 -718 -293 150 C ATOM 310 OG1 THR A 94 56.378 -17.968 24.894 1.00 91.87 O ANISOU 310 OG1 THR A 94 13469 11790 9648 -693 -267 75 O ATOM 311 CG2 THR A 94 57.566 -19.845 23.911 1.00 89.04 C ANISOU 311 CG2 THR A 94 13148 11361 9320 -665 -462 180 C ATOM 312 N ASN A 95 54.322 -21.202 22.818 1.00 74.76 N ANISOU 312 N ASN A 95 11160 9498 7746 -842 -172 245 N ATOM 313 CA ASN A 95 53.936 -22.512 22.280 1.00 74.00 C ANISOU 313 CA ASN A 95 11066 9344 7707 -898 -165 305 C ATOM 314 C ASN A 95 53.110 -22.397 20.997 1.00 74.74 C ANISOU 314 C ASN A 95 10971 9443 7984 -914 -165 264 C ATOM 315 O ASN A 95 53.200 -23.282 20.146 1.00 73.30 O ANISOU 315 O ASN A 95 10770 9214 7865 -927 -228 298 O ATOM 316 CB ASN A 95 53.135 -23.297 23.311 1.00 78.09 C ANISOU 316 CB ASN A 95 11698 9828 8146 -991 -8 350 C ATOM 317 CG ASN A 95 53.903 -23.708 24.539 1.00108.32 C ANISOU 317 CG ASN A 95 15759 13627 11769 -973 -20 410 C ATOM 318 OD1 ASN A 95 55.139 -23.809 24.541 1.00104.99 O ANISOU 318 OD1 ASN A 95 15417 13198 11275 -891 -177 432 O ATOM 319 ND2 ASN A 95 53.169 -24.063 25.581 1.00102.46 N ANISOU 319 ND2 ASN A 95 15139 12859 10933 -1051 146 436 N ATOM 320 N ILE A 96 52.302 -21.324 20.865 1.00 70.44 N ANISOU 320 N ILE A 96 10294 8950 7519 -904 -100 188 N ATOM 321 CA ILE A 96 51.488 -21.066 19.674 1.00 69.20 C ANISOU 321 CA ILE A 96 9961 8804 7530 -895 -122 136 C ATOM 322 C ILE A 96 52.444 -20.924 18.467 1.00 71.68 C ANISOU 322 C ILE A 96 10263 9095 7878 -818 -285 142 C ATOM 323 O ILE A 96 52.245 -21.606 17.462 1.00 71.08 O ANISOU 323 O ILE A 96 10137 8985 7886 -830 -345 154 O ATOM 324 CB ILE A 96 50.566 -19.832 19.872 1.00 72.18 C ANISOU 324 CB ILE A 96 10218 9237 7970 -871 -35 50 C ATOM 325 CG1 ILE A 96 49.489 -20.151 20.939 1.00 73.60 C ANISOU 325 CG1 ILE A 96 10390 9432 8142 -965 152 36 C ATOM 326 CG2 ILE A 96 49.901 -19.429 18.547 1.00 72.91 C ANISOU 326 CG2 ILE A 96 10143 9338 8223 -824 -105 -8 C ATOM 327 CD1 ILE A 96 48.613 -18.999 21.382 1.00 78.94 C ANISOU 327 CD1 ILE A 96 10963 10162 8867 -943 263 -52 C ATOM 328 N TYR A 97 53.527 -20.132 18.611 1.00 67.52 N ANISOU 328 N TYR A 97 9795 8580 7281 -750 -349 131 N ATOM 329 CA TYR A 97 54.530 -19.993 17.558 1.00 66.35 C ANISOU 329 CA TYR A 97 9648 8403 7160 -689 -475 130 C ATOM 330 C TYR A 97 55.199 -21.329 17.245 1.00 69.25 C ANISOU 330 C TYR A 97 10084 8718 7508 -708 -546 197 C ATOM 331 O TYR A 97 55.280 -21.705 16.072 1.00 68.00 O ANISOU 331 O TYR A 97 9888 8523 7424 -694 -613 201 O ATOM 332 CB TYR A 97 55.604 -18.967 17.934 1.00 67.69 C ANISOU 332 CB TYR A 97 9864 8592 7262 -634 -510 95 C ATOM 333 CG TYR A 97 55.201 -17.521 17.761 1.00 70.12 C ANISOU 333 CG TYR A 97 10108 8924 7608 -593 -472 23 C ATOM 334 CD1 TYR A 97 55.188 -16.927 16.500 1.00 71.37 C ANISOU 334 CD1 TYR A 97 10213 9054 7851 -542 -521 -9 C ATOM 335 CD2 TYR A 97 54.995 -16.701 18.867 1.00 71.86 C ANISOU 335 CD2 TYR A 97 10352 9186 7764 -595 -392 -15 C ATOM 336 CE1 TYR A 97 54.879 -15.578 16.338 1.00 72.64 C ANISOU 336 CE1 TYR A 97 10342 9220 8037 -492 -490 -71 C ATOM 337 CE2 TYR A 97 54.690 -15.348 18.718 1.00 73.12 C ANISOU 337 CE2 TYR A 97 10467 9357 7959 -549 -357 -84 C ATOM 338 CZ TYR A 97 54.639 -14.788 17.452 1.00 81.06 C ANISOU 338 CZ TYR A 97 11421 10327 9052 -496 -407 -109 C ATOM 339 OH TYR A 97 54.349 -13.451 17.304 1.00 82.46 O ANISOU 339 OH TYR A 97 11578 10500 9254 -441 -374 -172 O ATOM 340 N ILE A 98 55.654 -22.051 18.304 1.00 65.99 N ANISOU 340 N ILE A 98 9789 8296 6987 -733 -531 248 N ATOM 341 CA ILE A 98 56.365 -23.340 18.225 1.00 65.32 C ANISOU 341 CA ILE A 98 9799 8155 6866 -736 -599 315 C ATOM 342 C ILE A 98 55.518 -24.358 17.450 1.00 68.17 C ANISOU 342 C ILE A 98 10121 8467 7314 -797 -577 344 C ATOM 343 O ILE A 98 56.068 -25.075 16.613 1.00 67.58 O ANISOU 343 O ILE A 98 10062 8341 7274 -778 -659 369 O ATOM 344 CB ILE A 98 56.726 -23.879 19.641 1.00 69.31 C ANISOU 344 CB ILE A 98 10459 8652 7223 -748 -574 366 C ATOM 345 CG1 ILE A 98 57.503 -22.818 20.455 1.00 70.18 C ANISOU 345 CG1 ILE A 98 10603 8817 7245 -692 -605 321 C ATOM 346 CG2 ILE A 98 57.533 -25.176 19.542 1.00 69.61 C ANISOU 346 CG2 ILE A 98 10606 8621 7221 -727 -660 434 C ATOM 347 CD1 ILE A 98 57.745 -23.161 21.966 1.00 83.40 C ANISOU 347 CD1 ILE A 98 12449 10491 8749 -694 -584 360 C ATOM 348 N PHE A 99 54.192 -24.391 17.698 1.00 64.49 N ANISOU 348 N PHE A 99 9594 8015 6894 -870 -465 329 N ATOM 349 CA PHE A 99 53.278 -25.309 17.022 1.00 64.52 C ANISOU 349 CA PHE A 99 9541 7978 6995 -942 -438 336 C ATOM 350 C PHE A 99 53.154 -24.966 15.538 1.00 66.99 C ANISOU 350 C PHE A 99 9735 8291 7425 -899 -532 288 C ATOM 351 O PHE A 99 53.312 -25.855 14.700 1.00 65.65 O ANISOU 351 O PHE A 99 9582 8066 7297 -912 -595 310 O ATOM 352 CB PHE A 99 51.886 -25.287 17.684 1.00 67.83 C ANISOU 352 CB PHE A 99 9895 8423 7455 -1034 -285 307 C ATOM 353 CG PHE A 99 50.882 -26.225 17.049 1.00 70.61 C ANISOU 353 CG PHE A 99 10167 8736 7925 -1125 -250 294 C ATOM 354 CD1 PHE A 99 50.840 -27.569 17.405 1.00 74.96 C ANISOU 354 CD1 PHE A 99 10832 9210 8440 -1212 -195 357 C ATOM 355 CD2 PHE A 99 49.965 -25.761 16.114 1.00 73.00 C ANISOU 355 CD2 PHE A 99 10286 9075 8374 -1122 -275 212 C ATOM 356 CE1 PHE A 99 49.923 -28.440 16.806 1.00 76.44 C ANISOU 356 CE1 PHE A 99 10943 9356 8746 -1310 -159 334 C ATOM 357 CE2 PHE A 99 49.051 -26.636 15.511 1.00 76.68 C ANISOU 357 CE2 PHE A 99 10667 9510 8959 -1208 -259 184 C ATOM 358 CZ PHE A 99 49.030 -27.966 15.870 1.00 75.52 C ANISOU 358 CZ PHE A 99 10625 9287 8784 -1311 -194 241 C ATOM 359 N ASN A 100 52.853 -23.687 15.217 1.00 63.35 N ANISOU 359 N ASN A 100 9176 7885 7009 -845 -540 222 N ATOM 360 CA ASN A 100 52.638 -23.221 13.845 1.00 62.56 C ANISOU 360 CA ASN A 100 8989 7780 7002 -791 -628 174 C ATOM 361 C ASN A 100 53.921 -23.353 13.005 1.00 66.57 C ANISOU 361 C ASN A 100 9575 8239 7478 -731 -733 199 C ATOM 362 O ASN A 100 53.820 -23.648 11.808 1.00 65.57 O ANISOU 362 O ASN A 100 9428 8075 7410 -714 -805 187 O ATOM 363 CB ASN A 100 52.140 -21.792 13.838 1.00 61.61 C ANISOU 363 CB ASN A 100 8783 7713 6913 -732 -608 107 C ATOM 364 CG ASN A 100 50.769 -21.645 14.474 1.00 87.12 C ANISOU 364 CG ASN A 100 11904 10991 10206 -784 -503 62 C ATOM 365 OD1 ASN A 100 49.792 -22.323 14.113 1.00 81.49 O ANISOU 365 OD1 ASN A 100 11101 10274 9589 -841 -491 39 O ATOM 366 ND2 ASN A 100 50.652 -20.738 15.419 1.00 79.47 N ANISOU 366 ND2 ASN A 100 10933 10068 9195 -768 -419 38 N ATOM 367 N LEU A 101 55.112 -23.200 13.629 1.00 63.83 N ANISOU 367 N LEU A 101 9317 7894 7043 -700 -742 226 N ATOM 368 CA LEU A 101 56.388 -23.414 12.938 1.00 63.40 C ANISOU 368 CA LEU A 101 9322 7794 6972 -651 -824 239 C ATOM 369 C LEU A 101 56.555 -24.900 12.629 1.00 69.96 C ANISOU 369 C LEU A 101 10210 8563 7810 -686 -858 293 C ATOM 370 O LEU A 101 56.882 -25.252 11.493 1.00 70.60 O ANISOU 370 O LEU A 101 10297 8595 7933 -664 -918 288 O ATOM 371 CB LEU A 101 57.585 -22.891 13.767 1.00 63.13 C ANISOU 371 CB LEU A 101 9343 7786 6860 -612 -831 235 C ATOM 372 CG LEU A 101 58.996 -23.061 13.145 1.00 66.87 C ANISOU 372 CG LEU A 101 9853 8220 7335 -562 -905 229 C ATOM 373 CD1 LEU A 101 59.189 -22.155 11.936 1.00 66.58 C ANISOU 373 CD1 LEU A 101 9781 8164 7354 -525 -916 177 C ATOM 374 CD2 LEU A 101 60.084 -22.761 14.155 1.00 67.81 C ANISOU 374 CD2 LEU A 101 10009 8371 7386 -532 -924 217 C ATOM 375 N ALA A 102 56.304 -25.772 13.641 1.00 67.14 N ANISOU 375 N ALA A 102 9910 8197 7404 -742 -810 343 N ATOM 376 CA ALA A 102 56.396 -27.228 13.518 1.00 67.29 C ANISOU 376 CA ALA A 102 10005 8142 7419 -781 -826 400 C ATOM 377 C ALA A 102 55.427 -27.755 12.454 1.00 70.83 C ANISOU 377 C ALA A 102 10389 8556 7967 -833 -831 379 C ATOM 378 O ALA A 102 55.817 -28.602 11.660 1.00 70.33 O ANISOU 378 O ALA A 102 10370 8426 7926 -828 -888 397 O ATOM 379 CB ALA A 102 56.109 -27.885 14.855 1.00 69.16 C ANISOU 379 CB ALA A 102 10333 8368 7576 -836 -749 455 C ATOM 380 N LEU A 103 54.190 -27.211 12.410 1.00 67.34 N ANISOU 380 N LEU A 103 9836 8161 7589 -875 -781 331 N ATOM 381 CA LEU A 103 53.148 -27.582 11.446 1.00 66.97 C ANISOU 381 CA LEU A 103 9701 8096 7648 -920 -802 289 C ATOM 382 C LEU A 103 53.558 -27.183 10.023 1.00 68.42 C ANISOU 382 C LEU A 103 9872 8261 7865 -843 -914 254 C ATOM 383 O LEU A 103 53.361 -27.971 9.100 1.00 67.97 O ANISOU 383 O LEU A 103 9824 8149 7853 -866 -969 246 O ATOM 384 CB LEU A 103 51.809 -26.913 11.833 1.00 67.75 C ANISOU 384 CB LEU A 103 9664 8263 7815 -961 -730 229 C ATOM 385 CG LEU A 103 50.565 -27.206 10.973 1.00 72.81 C ANISOU 385 CG LEU A 103 10175 8904 8584 -1008 -758 160 C ATOM 386 CD1 LEU A 103 50.204 -28.684 10.985 1.00 73.58 C ANISOU 386 CD1 LEU A 103 10307 8934 8716 -1123 -722 184 C ATOM 387 CD2 LEU A 103 49.379 -26.410 11.469 1.00 76.34 C ANISOU 387 CD2 LEU A 103 10473 9427 9104 -1027 -684 90 C ATOM 388 N ALA A 104 54.145 -25.979 9.853 1.00 63.64 N ANISOU 388 N ALA A 104 9263 7689 7229 -757 -939 231 N ATOM 389 CA ALA A 104 54.608 -25.482 8.551 1.00 62.55 C ANISOU 389 CA ALA A 104 9146 7521 7102 -683 -1021 201 C ATOM 390 C ALA A 104 55.789 -26.305 8.040 1.00 65.01 C ANISOU 390 C ALA A 104 9561 7761 7380 -668 -1059 238 C ATOM 391 O ALA A 104 55.819 -26.658 6.862 1.00 65.03 O ANISOU 391 O ALA A 104 9593 7709 7406 -652 -1119 222 O ATOM 392 CB ALA A 104 54.999 -24.014 8.651 1.00 62.73 C ANISOU 392 CB ALA A 104 9160 7583 7094 -610 -1008 170 C ATOM 393 N ASP A 105 56.739 -26.641 8.929 1.00 60.45 N ANISOU 393 N ASP A 105 9040 7181 6748 -666 -1031 281 N ATOM 394 CA ASP A 105 57.913 -27.437 8.582 1.00 60.17 C ANISOU 394 CA ASP A 105 9089 7083 6692 -639 -1066 308 C ATOM 395 C ASP A 105 57.543 -28.910 8.347 1.00 64.06 C ANISOU 395 C ASP A 105 9628 7507 7205 -695 -1080 345 C ATOM 396 O ASP A 105 58.257 -29.616 7.632 1.00 63.19 O ANISOU 396 O ASP A 105 9581 7328 7099 -671 -1119 353 O ATOM 397 CB ASP A 105 58.972 -27.335 9.678 1.00 62.61 C ANISOU 397 CB ASP A 105 9432 7415 6941 -607 -1052 332 C ATOM 398 CG ASP A 105 59.558 -25.952 9.895 1.00 77.16 C ANISOU 398 CG ASP A 105 11236 9313 8766 -559 -1038 286 C ATOM 399 OD1 ASP A 105 59.748 -25.222 8.895 1.00 78.48 O ANISOU 399 OD1 ASP A 105 11389 9466 8963 -527 -1046 242 O ATOM 400 OD2 ASP A 105 59.937 -25.646 11.046 1.00 82.42 O ANISOU 400 OD2 ASP A 105 11907 10026 9384 -551 -1022 293 O ATOM 401 N ALA A 106 56.439 -29.372 8.948 1.00 61.34 N ANISOU 401 N ALA A 106 9253 7174 6878 -775 -1037 360 N ATOM 402 CA ALA A 106 55.965 -30.738 8.767 1.00 61.91 C ANISOU 402 CA ALA A 106 9371 7174 6978 -848 -1033 387 C ATOM 403 C ALA A 106 55.341 -30.922 7.384 1.00 66.92 C ANISOU 403 C ALA A 106 9967 7776 7684 -863 -1093 334 C ATOM 404 O ALA A 106 55.423 -32.010 6.811 1.00 67.35 O ANISOU 404 O ALA A 106 10085 7750 7754 -893 -1120 346 O ATOM 405 CB ALA A 106 54.954 -31.090 9.844 1.00 63.51 C ANISOU 405 CB ALA A 106 9551 7395 7185 -944 -944 407 C ATOM 406 N LEU A 107 54.711 -29.859 6.854 1.00 63.12 N ANISOU 406 N LEU A 107 9393 7352 7237 -836 -1121 274 N ATOM 407 CA LEU A 107 54.022 -29.891 5.569 1.00 62.94 C ANISOU 407 CA LEU A 107 9337 7308 7270 -835 -1199 216 C ATOM 408 C LEU A 107 54.961 -29.550 4.422 1.00 66.93 C ANISOU 408 C LEU A 107 9927 7767 7735 -746 -1262 204 C ATOM 409 O LEU A 107 54.628 -29.862 3.278 1.00 67.28 O ANISOU 409 O LEU A 107 9998 7767 7800 -742 -1334 167 O ATOM 410 CB LEU A 107 52.833 -28.920 5.570 1.00 63.10 C ANISOU 410 CB LEU A 107 9225 7406 7345 -831 -1210 152 C ATOM 411 CG LEU A 107 51.682 -29.279 6.516 1.00 68.37 C ANISOU 411 CG LEU A 107 9783 8115 8078 -933 -1136 138 C ATOM 412 CD1 LEU A 107 50.769 -28.110 6.740 1.00 68.62 C ANISOU 412 CD1 LEU A 107 9680 8234 8159 -903 -1128 77 C ATOM 413 CD2 LEU A 107 50.928 -30.509 6.043 1.00 71.87 C ANISOU 413 CD2 LEU A 107 10206 8506 8597 -1030 -1158 110 C ATOM 414 N VAL A 108 56.127 -28.924 4.700 1.00 62.91 N ANISOU 414 N VAL A 108 9465 7268 7171 -682 -1232 228 N ATOM 415 CA VAL A 108 57.070 -28.615 3.618 1.00 62.67 C ANISOU 415 CA VAL A 108 9519 7185 7109 -611 -1261 210 C ATOM 416 C VAL A 108 57.863 -29.866 3.273 1.00 67.17 C ANISOU 416 C VAL A 108 10177 7671 7674 -622 -1266 237 C ATOM 417 O VAL A 108 58.165 -30.064 2.100 1.00 66.57 O ANISOU 417 O VAL A 108 10175 7530 7588 -594 -1299 212 O ATOM 418 CB VAL A 108 58.028 -27.429 3.870 1.00 66.16 C ANISOU 418 CB VAL A 108 9968 7657 7513 -547 -1217 203 C ATOM 419 CG1 VAL A 108 57.304 -26.100 3.807 1.00 66.17 C ANISOU 419 CG1 VAL A 108 9917 7711 7512 -517 -1221 167 C ATOM 420 CG2 VAL A 108 58.795 -27.574 5.165 1.00 65.73 C ANISOU 420 CG2 VAL A 108 9895 7638 7443 -555 -1167 240 C ATOM 421 N THR A 109 58.166 -30.732 4.277 1.00 64.36 N ANISOU 421 N THR A 109 9829 7307 7316 -656 -1233 287 N ATOM 422 CA THR A 109 58.921 -31.973 4.045 1.00 64.36 C ANISOU 422 CA THR A 109 9920 7220 7314 -654 -1241 315 C ATOM 423 C THR A 109 58.052 -32.977 3.279 1.00 67.56 C ANISOU 423 C THR A 109 10358 7558 7752 -718 -1278 302 C ATOM 424 O THR A 109 58.591 -33.845 2.610 1.00 67.62 O ANISOU 424 O THR A 109 10453 7480 7759 -706 -1294 303 O ATOM 425 CB THR A 109 59.431 -32.579 5.359 1.00 75.63 C ANISOU 425 CB THR A 109 11369 8649 8718 -657 -1209 375 C ATOM 426 OG1 THR A 109 58.320 -32.904 6.188 1.00 78.92 O ANISOU 426 OG1 THR A 109 11757 9089 9140 -741 -1179 402 O ATOM 427 CG2 THR A 109 60.405 -31.654 6.103 1.00 74.25 C ANISOU 427 CG2 THR A 109 11162 8539 8512 -590 -1191 373 C ATOM 428 N THR A 110 56.715 -32.822 3.340 1.00 63.37 N ANISOU 428 N THR A 110 9750 7069 7258 -784 -1291 277 N ATOM 429 CA THR A 110 55.730 -33.658 2.650 1.00 63.36 C ANISOU 429 CA THR A 110 9749 7019 7305 -858 -1335 242 C ATOM 430 C THR A 110 55.962 -33.597 1.122 1.00 66.34 C ANISOU 430 C THR A 110 10198 7343 7668 -807 -1411 192 C ATOM 431 O THR A 110 55.803 -34.606 0.434 1.00 66.38 O ANISOU 431 O THR A 110 10267 7266 7687 -845 -1446 174 O ATOM 432 CB THR A 110 54.316 -33.177 3.035 1.00 72.41 C ANISOU 432 CB THR A 110 10759 8244 8510 -921 -1336 202 C ATOM 433 OG1 THR A 110 54.167 -33.266 4.452 1.00 71.94 O ANISOU 433 OG1 THR A 110 10662 8223 8450 -971 -1245 250 O ATOM 434 CG2 THR A 110 53.206 -33.968 2.357 1.00 73.55 C ANISOU 434 CG2 THR A 110 10869 8352 8726 -1006 -1390 143 C ATOM 435 N THR A 111 56.358 -32.422 0.611 1.00 62.04 N ANISOU 435 N THR A 111 9657 6830 7083 -723 -1427 169 N ATOM 436 CA THR A 111 56.598 -32.193 -0.820 1.00 61.35 C ANISOU 436 CA THR A 111 9666 6687 6956 -666 -1484 124 C ATOM 437 C THR A 111 57.942 -32.785 -1.276 1.00 64.07 C ANISOU 437 C THR A 111 10133 6944 7265 -629 -1441 143 C ATOM 438 O THR A 111 58.108 -33.083 -2.453 1.00 62.95 O ANISOU 438 O THR A 111 10097 6728 7092 -608 -1475 109 O ATOM 439 CB THR A 111 56.574 -30.665 -1.138 1.00 65.48 C ANISOU 439 CB THR A 111 10177 7261 7440 -590 -1495 99 C ATOM 440 OG1 THR A 111 57.693 -29.998 -0.539 1.00 59.99 O ANISOU 440 OG1 THR A 111 9486 6588 6719 -547 -1407 131 O ATOM 441 CG2 THR A 111 55.266 -29.989 -0.740 1.00 63.38 C ANISOU 441 CG2 THR A 111 9783 7080 7216 -604 -1541 69 C ATOM 442 N MET A 112 58.888 -32.945 -0.338 1.00 61.13 N ANISOU 442 N MET A 112 9745 6582 6898 -615 -1370 190 N ATOM 443 CA MET A 112 60.274 -33.349 -0.569 1.00 61.22 C ANISOU 443 CA MET A 112 9834 6530 6895 -564 -1322 199 C ATOM 444 C MET A 112 60.381 -34.645 -1.466 1.00 66.05 C ANISOU 444 C MET A 112 10557 7029 7510 -580 -1345 186 C ATOM 445 O MET A 112 61.117 -34.572 -2.464 1.00 65.22 O ANISOU 445 O MET A 112 10541 6863 7377 -532 -1324 151 O ATOM 446 CB MET A 112 60.988 -33.569 0.772 1.00 63.45 C ANISOU 446 CB MET A 112 10066 6848 7196 -551 -1279 248 C ATOM 447 CG MET A 112 62.470 -33.595 0.656 1.00 67.09 C ANISOU 447 CG MET A 112 10557 7275 7660 -479 -1235 236 C ATOM 448 SD MET A 112 63.309 -33.586 2.250 1.00 71.43 S ANISOU 448 SD MET A 112 11036 7884 8221 -441 -1219 277 S ATOM 449 CE MET A 112 64.946 -33.440 1.670 1.00 68.38 C ANISOU 449 CE MET A 112 10657 7459 7865 -356 -1175 222 C ATOM 450 N PRO A 113 59.664 -35.791 -1.204 1.00 63.20 N ANISOU 450 N PRO A 113 10205 6628 7179 -652 -1377 205 N ATOM 451 CA PRO A 113 59.815 -36.966 -2.091 1.00 63.67 C ANISOU 451 CA PRO A 113 10382 6572 7239 -666 -1395 185 C ATOM 452 C PRO A 113 59.539 -36.661 -3.567 1.00 68.02 C ANISOU 452 C PRO A 113 11013 7083 7749 -650 -1444 118 C ATOM 453 O PRO A 113 60.117 -37.329 -4.423 1.00 68.71 O ANISOU 453 O PRO A 113 11218 7073 7815 -628 -1433 94 O ATOM 454 CB PRO A 113 58.767 -37.948 -1.564 1.00 66.01 C ANISOU 454 CB PRO A 113 10658 6846 7577 -769 -1420 202 C ATOM 455 CG PRO A 113 58.583 -37.582 -0.171 1.00 69.95 C ANISOU 455 CG PRO A 113 11060 7427 8092 -788 -1381 255 C ATOM 456 CD PRO A 113 58.742 -36.096 -0.091 1.00 64.72 C ANISOU 456 CD PRO A 113 10317 6867 7406 -730 -1377 241 C ATOM 457 N PHE A 114 58.668 -35.659 -3.865 1.00 63.23 N ANISOU 457 N PHE A 114 10354 6545 7124 -652 -1499 86 N ATOM 458 CA PHE A 114 58.343 -35.270 -5.239 1.00 62.65 C ANISOU 458 CA PHE A 114 10378 6434 6991 -622 -1565 25 C ATOM 459 C PHE A 114 59.576 -34.686 -5.922 1.00 65.97 C ANISOU 459 C PHE A 114 10909 6810 7348 -539 -1488 17 C ATOM 460 O PHE A 114 59.838 -35.040 -7.064 1.00 65.52 O ANISOU 460 O PHE A 114 10997 6663 7236 -518 -1496 -21 O ATOM 461 CB PHE A 114 57.172 -34.275 -5.290 1.00 64.28 C ANISOU 461 CB PHE A 114 10502 6726 7195 -621 -1650 -6 C ATOM 462 CG PHE A 114 55.854 -34.834 -4.799 1.00 66.31 C ANISOU 462 CG PHE A 114 10639 7025 7532 -711 -1722 -26 C ATOM 463 CD1 PHE A 114 55.510 -34.774 -3.451 1.00 68.98 C ANISOU 463 CD1 PHE A 114 10833 7441 7937 -762 -1671 15 C ATOM 464 CD2 PHE A 114 54.942 -35.388 -5.688 1.00 69.10 C ANISOU 464 CD2 PHE A 114 11023 7339 7892 -749 -1835 -96 C ATOM 465 CE1 PHE A 114 54.287 -35.283 -2.999 1.00 70.48 C ANISOU 465 CE1 PHE A 114 10908 7662 8208 -859 -1709 -13 C ATOM 466 CE2 PHE A 114 53.726 -35.909 -5.234 1.00 72.55 C ANISOU 466 CE2 PHE A 114 11328 7815 8423 -846 -1889 -132 C ATOM 467 CZ PHE A 114 53.403 -35.844 -3.894 1.00 70.30 C ANISOU 467 CZ PHE A 114 10897 7602 8212 -905 -1814 -90 C ATOM 468 N GLN A 115 60.362 -33.843 -5.212 1.00 62.84 N ANISOU 468 N GLN A 115 10448 6469 6960 -499 -1404 47 N ATOM 469 CA GLN A 115 61.617 -33.263 -5.737 1.00 62.53 C ANISOU 469 CA GLN A 115 10488 6389 6883 -437 -1303 29 C ATOM 470 C GLN A 115 62.620 -34.373 -6.067 1.00 67.76 C ANISOU 470 C GLN A 115 11224 6957 7565 -426 -1242 21 C ATOM 471 O GLN A 115 63.217 -34.378 -7.147 1.00 67.60 O ANISOU 471 O GLN A 115 11336 6853 7496 -394 -1189 -20 O ATOM 472 CB GLN A 115 62.240 -32.274 -4.727 1.00 62.49 C ANISOU 472 CB GLN A 115 10368 6468 6909 -413 -1231 52 C ATOM 473 CG GLN A 115 61.412 -31.037 -4.368 1.00 61.83 C ANISOU 473 CG GLN A 115 10217 6471 6806 -411 -1267 57 C ATOM 474 CD GLN A 115 61.406 -29.921 -5.382 1.00 68.78 C ANISOU 474 CD GLN A 115 11209 7317 7606 -366 -1251 22 C ATOM 475 OE1 GLN A 115 61.538 -30.128 -6.594 1.00 64.39 O ANISOU 475 OE1 GLN A 115 10810 6670 6986 -345 -1251 -9 O ATOM 476 NE2 GLN A 115 61.219 -28.692 -4.888 1.00 52.71 N ANISOU 476 NE2 GLN A 115 9115 5348 5565 -347 -1234 27 N ATOM 477 N SER A 116 62.772 -35.327 -5.124 1.00 64.87 N ANISOU 477 N SER A 116 10784 6597 7265 -448 -1248 59 N ATOM 478 CA SER A 116 63.663 -36.481 -5.227 1.00 65.45 C ANISOU 478 CA SER A 116 10913 6583 7372 -426 -1204 57 C ATOM 479 C SER A 116 63.371 -37.286 -6.513 1.00 70.78 C ANISOU 479 C SER A 116 11744 7146 8003 -442 -1231 15 C ATOM 480 O SER A 116 64.278 -37.509 -7.319 1.00 71.03 O ANISOU 480 O SER A 116 11874 7096 8018 -399 -1157 -24 O ATOM 481 CB SER A 116 63.510 -37.368 -3.989 1.00 68.30 C ANISOU 481 CB SER A 116 11199 6962 7790 -451 -1234 115 C ATOM 482 OG SER A 116 64.378 -38.489 -4.013 1.00 75.75 O ANISOU 482 OG SER A 116 12201 7815 8767 -413 -1202 117 O ATOM 483 N THR A 117 62.082 -37.645 -6.717 1.00 67.42 N ANISOU 483 N THR A 117 11335 6720 7561 -508 -1333 12 N ATOM 484 CA THR A 117 61.540 -38.424 -7.835 1.00 67.62 C ANISOU 484 CA THR A 117 11497 6651 7545 -539 -1393 -35 C ATOM 485 C THR A 117 61.783 -37.696 -9.183 1.00 71.21 C ANISOU 485 C THR A 117 12095 7062 7901 -490 -1378 -90 C ATOM 486 O THR A 117 62.287 -38.320 -10.119 1.00 71.21 O ANISOU 486 O THR A 117 12243 6954 7861 -472 -1341 -130 O ATOM 487 CB THR A 117 60.029 -38.657 -7.586 1.00 72.09 C ANISOU 487 CB THR A 117 11996 7260 8134 -625 -1513 -39 C ATOM 488 OG1 THR A 117 59.864 -39.343 -6.346 1.00 69.22 O ANISOU 488 OG1 THR A 117 11532 6919 7849 -677 -1497 15 O ATOM 489 CG2 THR A 117 59.357 -39.450 -8.689 1.00 71.60 C ANISOU 489 CG2 THR A 117 12057 7109 8037 -667 -1598 -103 C ATOM 490 N VAL A 118 61.441 -36.387 -9.261 1.00 67.19 N ANISOU 490 N VAL A 118 11557 6625 7346 -465 -1397 -92 N ATOM 491 CA VAL A 118 61.556 -35.546 -10.461 1.00 67.44 C ANISOU 491 CA VAL A 118 11746 6612 7265 -415 -1384 -135 C ATOM 492 C VAL A 118 63.032 -35.452 -10.892 1.00 72.81 C ANISOU 492 C VAL A 118 12518 7219 7927 -369 -1216 -150 C ATOM 493 O VAL A 118 63.302 -35.511 -12.089 1.00 73.83 O ANISOU 493 O VAL A 118 12838 7249 7963 -345 -1181 -195 O ATOM 494 CB VAL A 118 60.940 -34.136 -10.238 1.00 70.38 C ANISOU 494 CB VAL A 118 12061 7076 7605 -391 -1429 -123 C ATOM 495 CG1 VAL A 118 61.270 -33.182 -11.382 1.00 70.61 C ANISOU 495 CG1 VAL A 118 12280 7041 7507 -329 -1386 -154 C ATOM 496 CG2 VAL A 118 59.432 -34.224 -10.050 1.00 70.44 C ANISOU 496 CG2 VAL A 118 11986 7146 7633 -428 -1598 -133 C ATOM 497 N TYR A 119 63.973 -35.332 -9.933 1.00 68.98 N ANISOU 497 N TYR A 119 11898 6778 7531 -356 -1115 -123 N ATOM 498 CA TYR A 119 65.403 -35.264 -10.241 1.00 69.32 C ANISOU 498 CA TYR A 119 11983 6763 7592 -316 -951 -155 C ATOM 499 C TYR A 119 65.871 -36.510 -10.982 1.00 74.68 C ANISOU 499 C TYR A 119 12783 7324 8268 -308 -915 -191 C ATOM 500 O TYR A 119 66.545 -36.395 -12.009 1.00 75.27 O ANISOU 500 O TYR A 119 13006 7308 8284 -283 -806 -243 O ATOM 501 CB TYR A 119 66.235 -35.083 -8.957 1.00 70.41 C ANISOU 501 CB TYR A 119 11926 6981 7845 -301 -889 -130 C ATOM 502 CG TYR A 119 67.718 -35.376 -9.115 1.00 73.62 C ANISOU 502 CG TYR A 119 12325 7332 8315 -258 -742 -177 C ATOM 503 CD1 TYR A 119 68.518 -34.597 -9.947 1.00 76.21 C ANISOU 503 CD1 TYR A 119 12738 7610 8610 -243 -594 -236 C ATOM 504 CD2 TYR A 119 68.343 -36.348 -8.338 1.00 74.83 C ANISOU 504 CD2 TYR A 119 12375 7486 8571 -231 -746 -167 C ATOM 505 CE1 TYR A 119 69.884 -34.837 -10.070 1.00 77.99 C ANISOU 505 CE1 TYR A 119 12927 7790 8915 -210 -446 -297 C ATOM 506 CE2 TYR A 119 69.713 -36.589 -8.442 1.00 76.44 C ANISOU 506 CE2 TYR A 119 12543 7647 8853 -178 -622 -225 C ATOM 507 CZ TYR A 119 70.481 -35.825 -9.306 1.00 85.22 C ANISOU 507 CZ TYR A 119 13717 8717 9947 -172 -468 -295 C ATOM 508 OH TYR A 119 71.833 -36.041 -9.422 1.00 88.39 O ANISOU 508 OH TYR A 119 14060 9079 10445 -127 -331 -369 O ATOM 509 N LEU A 120 65.509 -37.691 -10.461 1.00 71.60 N ANISOU 509 N LEU A 120 12343 6925 7938 -333 -995 -166 N ATOM 510 CA LEU A 120 65.948 -38.978 -10.977 1.00 71.88 C ANISOU 510 CA LEU A 120 12479 6844 7987 -324 -966 -196 C ATOM 511 C LEU A 120 65.182 -39.356 -12.255 1.00 77.61 C ANISOU 511 C LEU A 120 13405 7481 8603 -352 -1032 -239 C ATOM 512 O LEU A 120 65.829 -39.739 -13.227 1.00 78.14 O ANISOU 512 O LEU A 120 13627 7440 8624 -325 -945 -292 O ATOM 513 CB LEU A 120 65.772 -40.055 -9.897 1.00 71.33 C ANISOU 513 CB LEU A 120 12304 6787 8013 -342 -1029 -147 C ATOM 514 CG LEU A 120 66.601 -39.839 -8.612 1.00 74.52 C ANISOU 514 CG LEU A 120 12531 7267 8515 -297 -983 -107 C ATOM 515 CD1 LEU A 120 66.172 -40.766 -7.529 1.00 75.00 C ANISOU 515 CD1 LEU A 120 12525 7338 8632 -321 -1062 -46 C ATOM 516 CD2 LEU A 120 68.097 -39.969 -8.866 1.00 75.48 C ANISOU 516 CD2 LEU A 120 12652 7336 8690 -219 -849 -158 C ATOM 517 N MET A 121 63.837 -39.219 -12.281 1.00 74.97 N ANISOU 517 N MET A 121 13068 7191 8226 -403 -1184 -228 N ATOM 518 CA MET A 121 63.050 -39.546 -13.480 1.00 76.31 C ANISOU 518 CA MET A 121 13419 7284 8290 -425 -1279 -282 C ATOM 519 C MET A 121 63.293 -38.550 -14.606 1.00 82.52 C ANISOU 519 C MET A 121 14381 8032 8940 -375 -1231 -321 C ATOM 520 O MET A 121 63.299 -38.945 -15.774 1.00 82.84 O ANISOU 520 O MET A 121 14633 7966 8878 -366 -1233 -376 O ATOM 521 CB MET A 121 61.547 -39.594 -13.192 1.00 78.62 C ANISOU 521 CB MET A 121 13634 7646 8592 -488 -1461 -278 C ATOM 522 CG MET A 121 61.153 -40.619 -12.180 1.00 82.29 C ANISOU 522 CG MET A 121 13964 8128 9175 -556 -1500 -245 C ATOM 523 SD MET A 121 59.364 -40.807 -12.112 1.00 87.41 S ANISOU 523 SD MET A 121 14536 8831 9843 -649 -1695 -276 S ATOM 524 CE MET A 121 59.077 -41.669 -13.650 1.00 85.83 C ANISOU 524 CE MET A 121 14569 8494 9548 -665 -1773 -371 C ATOM 525 N ASN A 122 63.462 -37.256 -14.248 1.00 80.02 N ANISOU 525 N ASN A 122 13995 7795 8613 -346 -1185 -292 N ATOM 526 CA ASN A 122 63.685 -36.113 -15.144 1.00 81.00 C ANISOU 526 CA ASN A 122 14284 7884 8607 -300 -1124 -314 C ATOM 527 C ASN A 122 62.402 -35.888 -16.005 1.00 86.61 C ANISOU 527 C ASN A 122 15141 8579 9188 -292 -1310 -342 C ATOM 528 O ASN A 122 62.484 -35.718 -17.226 1.00 87.74 O ANISOU 528 O ASN A 122 15534 8622 9182 -257 -1296 -384 O ATOM 529 CB ASN A 122 64.947 -36.322 -16.013 1.00 84.93 C ANISOU 529 CB ASN A 122 14954 8258 9057 -272 -930 -360 C ATOM 530 CG ASN A 122 65.417 -35.104 -16.772 1.00115.52 C ANISOU 530 CG ASN A 122 18994 12085 12812 -236 -805 -377 C ATOM 531 OD1 ASN A 122 65.196 -33.957 -16.366 1.00111.30 O ANISOU 531 OD1 ASN A 122 18398 11622 12268 -225 -813 -345 O ATOM 532 ND2 ASN A 122 66.169 -35.333 -17.841 1.00109.23 N ANISOU 532 ND2 ASN A 122 18416 11159 11928 -220 -662 -430 N ATOM 533 N SER A 123 61.217 -35.889 -15.332 1.00 82.82 N ANISOU 533 N SER A 123 14500 8201 8768 -323 -1485 -324 N ATOM 534 CA SER A 123 59.871 -35.678 -15.908 1.00 83.48 C ANISOU 534 CA SER A 123 14645 8301 8773 -314 -1695 -360 C ATOM 535 C SER A 123 58.776 -35.698 -14.824 1.00 85.87 C ANISOU 535 C SER A 123 14690 8734 9202 -362 -1831 -341 C ATOM 536 O SER A 123 58.924 -36.376 -13.804 1.00 84.68 O ANISOU 536 O SER A 123 14364 8626 9185 -424 -1785 -308 O ATOM 537 CB SER A 123 59.536 -36.721 -16.981 1.00 89.26 C ANISOU 537 CB SER A 123 15560 8928 9427 -331 -1786 -429 C ATOM 538 OG SER A 123 59.849 -38.060 -16.617 1.00101.39 O ANISOU 538 OG SER A 123 17031 10427 11066 -397 -1741 -434 O ATOM 539 N TRP A 124 57.674 -34.949 -15.062 1.00 82.10 N ANISOU 539 N TRP A 124 14201 8312 8679 -328 -1996 -366 N ATOM 540 CA TRP A 124 56.499 -34.936 -14.190 1.00 81.36 C ANISOU 540 CA TRP A 124 13870 8338 8705 -372 -2129 -371 C ATOM 541 C TRP A 124 55.334 -35.616 -14.933 1.00 87.08 C ANISOU 541 C TRP A 124 14631 9042 9412 -398 -2338 -460 C ATOM 542 O TRP A 124 54.618 -34.959 -15.693 1.00 87.48 O ANISOU 542 O TRP A 124 14771 9096 9370 -326 -2492 -509 O ATOM 543 CB TRP A 124 56.132 -33.513 -13.726 1.00 79.22 C ANISOU 543 CB TRP A 124 13509 8162 8430 -309 -2153 -342 C ATOM 544 CG TRP A 124 54.941 -33.476 -12.809 1.00 80.10 C ANISOU 544 CG TRP A 124 13366 8396 8672 -354 -2269 -355 C ATOM 545 CD1 TRP A 124 53.627 -33.449 -13.173 1.00 84.15 C ANISOU 545 CD1 TRP A 124 13825 8949 9199 -345 -2473 -429 C ATOM 546 CD2 TRP A 124 54.962 -33.431 -11.376 1.00 79.04 C ANISOU 546 CD2 TRP A 124 12999 8359 8675 -413 -2181 -301 C ATOM 547 NE1 TRP A 124 52.828 -33.442 -12.056 1.00 83.44 N ANISOU 547 NE1 TRP A 124 13469 8974 9260 -406 -2500 -429 N ATOM 548 CE2 TRP A 124 53.619 -33.408 -10.939 1.00 83.58 C ANISOU 548 CE2 TRP A 124 13387 9025 9343 -447 -2319 -345 C ATOM 549 CE3 TRP A 124 55.987 -33.389 -10.414 1.00 79.27 C ANISOU 549 CE3 TRP A 124 12959 8406 8754 -435 -2003 -226 C ATOM 550 CZ2 TRP A 124 53.273 -33.368 -9.580 1.00 82.40 C ANISOU 550 CZ2 TRP A 124 13006 8977 9327 -512 -2262 -311 C ATOM 551 CZ3 TRP A 124 55.644 -33.345 -9.069 1.00 80.24 C ANISOU 551 CZ3 TRP A 124 12863 8630 8995 -489 -1971 -189 C ATOM 552 CH2 TRP A 124 54.302 -33.329 -8.664 1.00 81.50 C ANISOU 552 CH2 TRP A 124 12860 8871 9236 -530 -2089 -228 C ATOM 553 N PRO A 125 55.128 -36.937 -14.744 1.00 84.35 N ANISOU 553 N PRO A 125 14227 8668 9155 -497 -2353 -488 N ATOM 554 CA PRO A 125 54.052 -37.614 -15.488 1.00 86.29 C ANISOU 554 CA PRO A 125 14506 8888 9393 -534 -2551 -590 C ATOM 555 C PRO A 125 52.747 -37.736 -14.692 1.00 91.80 C ANISOU 555 C PRO A 125 14934 9699 10246 -611 -2676 -631 C ATOM 556 O PRO A 125 51.862 -38.503 -15.086 1.00 93.42 O ANISOU 556 O PRO A 125 15112 9890 10495 -677 -2820 -725 O ATOM 557 CB PRO A 125 54.647 -39.001 -15.736 1.00 88.20 C ANISOU 557 CB PRO A 125 14848 9017 9647 -608 -2470 -602 C ATOM 558 CG PRO A 125 55.605 -39.227 -14.561 1.00 90.64 C ANISOU 558 CG PRO A 125 15041 9343 10055 -642 -2264 -503 C ATOM 559 CD PRO A 125 55.894 -37.893 -13.916 1.00 84.74 C ANISOU 559 CD PRO A 125 14200 8692 9307 -574 -2197 -435 C ATOM 560 N PHE A 126 52.616 -36.977 -13.595 1.00 87.18 N ANISOU 560 N PHE A 126 14153 9224 9749 -607 -2616 -572 N ATOM 561 CA PHE A 126 51.493 -37.113 -12.679 1.00 87.23 C ANISOU 561 CA PHE A 126 13891 9336 9917 -692 -2681 -604 C ATOM 562 C PHE A 126 50.383 -36.050 -12.923 1.00 91.11 C ANISOU 562 C PHE A 126 14286 9922 10410 -614 -2863 -671 C ATOM 563 O PHE A 126 49.537 -35.836 -12.049 1.00 90.67 O ANISOU 563 O PHE A 126 13987 9971 10491 -662 -2886 -690 O ATOM 564 CB PHE A 126 52.012 -36.999 -11.244 1.00 87.79 C ANISOU 564 CB PHE A 126 13808 9466 10082 -738 -2497 -502 C ATOM 565 CG PHE A 126 53.261 -37.812 -10.963 1.00 88.71 C ANISOU 565 CG PHE A 126 14026 9494 10184 -770 -2323 -427 C ATOM 566 CD1 PHE A 126 53.237 -39.202 -11.023 1.00 92.35 C ANISOU 566 CD1 PHE A 126 14522 9873 10695 -870 -2309 -451 C ATOM 567 CD2 PHE A 126 54.434 -37.192 -10.550 1.00 89.42 C ANISOU 567 CD2 PHE A 126 14159 9587 10228 -703 -2174 -339 C ATOM 568 CE1 PHE A 126 54.389 -39.950 -10.756 1.00 92.41 C ANISOU 568 CE1 PHE A 126 14624 9795 10694 -880 -2159 -385 C ATOM 569 CE2 PHE A 126 55.578 -37.944 -10.261 1.00 91.43 C ANISOU 569 CE2 PHE A 126 14484 9767 10486 -720 -2029 -283 C ATOM 570 CZ PHE A 126 55.547 -39.316 -10.366 1.00 90.01 C ANISOU 570 CZ PHE A 126 14350 9502 10349 -800 -2026 -303 C ATOM 571 N GLY A 127 50.361 -35.457 -14.117 1.00 88.05 N ANISOU 571 N GLY A 127 14097 9488 9870 -494 -2991 -712 N ATOM 572 CA GLY A 127 49.335 -34.491 -14.512 1.00 88.80 C ANISOU 572 CA GLY A 127 14141 9653 9946 -392 -3193 -783 C ATOM 573 C GLY A 127 49.418 -33.117 -13.872 1.00 90.34 C ANISOU 573 C GLY A 127 14261 9927 10138 -299 -3136 -716 C ATOM 574 O GLY A 127 50.271 -32.874 -13.014 1.00 88.20 O ANISOU 574 O GLY A 127 13954 9669 9890 -325 -2932 -615 O ATOM 575 N ASP A 128 48.523 -32.199 -14.298 1.00 86.89 N ANISOU 575 N ASP A 128 13804 9539 9673 -182 -3327 -779 N ATOM 576 CA ASP A 128 48.493 -30.822 -13.800 1.00 85.60 C ANISOU 576 CA ASP A 128 13588 9439 9498 -77 -3296 -728 C ATOM 577 C ASP A 128 47.810 -30.736 -12.441 1.00 88.29 C ANISOU 577 C ASP A 128 13590 9912 10043 -155 -3246 -733 C ATOM 578 O ASP A 128 48.178 -29.872 -11.638 1.00 86.46 O ANISOU 578 O ASP A 128 13300 9726 9825 -124 -3116 -657 O ATOM 579 CB ASP A 128 47.779 -29.880 -14.791 1.00 88.85 C ANISOU 579 CB ASP A 128 14126 9840 9794 97 -3529 -795 C ATOM 580 CG ASP A 128 48.418 -29.780 -16.164 1.00 98.03 C ANISOU 580 CG ASP A 128 15665 10862 10720 193 -3575 -786 C ATOM 581 OD1 ASP A 128 48.756 -30.838 -16.740 1.00 99.29 O ANISOU 581 OD1 ASP A 128 15944 10946 10837 119 -3568 -811 O ATOM 582 OD2 ASP A 128 48.442 -28.663 -16.724 1.00102.93 O ANISOU 582 OD2 ASP A 128 16471 11443 11196 348 -3639 -768 O ATOM 583 N VAL A 129 46.815 -31.622 -12.185 1.00 85.45 N ANISOU 583 N VAL A 129 13014 9608 9843 -263 -3340 -829 N ATOM 584 CA VAL A 129 46.028 -31.646 -10.947 1.00 84.87 C ANISOU 584 CA VAL A 129 12619 9655 9973 -354 -3288 -854 C ATOM 585 C VAL A 129 46.959 -31.851 -9.740 1.00 84.88 C ANISOU 585 C VAL A 129 12580 9661 10010 -452 -3020 -728 C ATOM 586 O VAL A 129 46.876 -31.060 -8.807 1.00 83.73 O ANISOU 586 O VAL A 129 12300 9593 9918 -432 -2932 -687 O ATOM 587 CB VAL A 129 44.886 -32.692 -10.949 1.00 91.13 C ANISOU 587 CB VAL A 129 13207 10485 10933 -479 -3405 -988 C ATOM 588 CG1 VAL A 129 43.792 -32.266 -11.908 1.00 93.38 C ANISOU 588 CG1 VAL A 129 13458 10803 11219 -364 -3694 -1131 C ATOM 589 CG2 VAL A 129 45.377 -34.111 -11.271 1.00 91.08 C ANISOU 589 CG2 VAL A 129 13314 10379 10912 -613 -3348 -985 C ATOM 590 N LEU A 130 47.874 -32.839 -9.777 1.00 79.57 N ANISOU 590 N LEU A 130 12035 8901 9296 -539 -2898 -670 N ATOM 591 CA LEU A 130 48.814 -33.065 -8.679 1.00 77.26 C ANISOU 591 CA LEU A 130 11722 8607 9027 -612 -2668 -556 C ATOM 592 C LEU A 130 49.841 -31.936 -8.635 1.00 79.31 C ANISOU 592 C LEU A 130 12113 8855 9164 -496 -2572 -464 C ATOM 593 O LEU A 130 50.164 -31.454 -7.556 1.00 77.21 O ANISOU 593 O LEU A 130 11748 8648 8940 -510 -2439 -398 O ATOM 594 CB LEU A 130 49.512 -34.435 -8.817 1.00 76.99 C ANISOU 594 CB LEU A 130 11798 8472 8981 -714 -2584 -528 C ATOM 595 CG LEU A 130 50.424 -34.855 -7.650 1.00 79.88 C ANISOU 595 CG LEU A 130 12139 8831 9380 -786 -2372 -419 C ATOM 596 CD1 LEU A 130 49.625 -35.062 -6.356 1.00 80.22 C ANISOU 596 CD1 LEU A 130 11946 8959 9573 -895 -2309 -422 C ATOM 597 CD2 LEU A 130 51.170 -36.111 -7.969 1.00 80.93 C ANISOU 597 CD2 LEU A 130 12416 8850 9485 -849 -2311 -396 C ATOM 598 N CYS A 131 50.305 -31.487 -9.817 1.00 77.11 N ANISOU 598 N CYS A 131 12065 8500 8735 -387 -2639 -469 N ATOM 599 CA CYS A 131 51.273 -30.402 -10.002 1.00 76.32 C ANISOU 599 CA CYS A 131 12126 8365 8509 -281 -2546 -398 C ATOM 600 C CYS A 131 50.814 -29.149 -9.216 1.00 78.70 C ANISOU 600 C CYS A 131 12282 8765 8856 -221 -2539 -384 C ATOM 601 O CYS A 131 51.543 -28.681 -8.335 1.00 76.37 O ANISOU 601 O CYS A 131 11948 8496 8573 -234 -2378 -310 O ATOM 602 CB CYS A 131 51.444 -30.105 -11.492 1.00 77.91 C ANISOU 602 CB CYS A 131 12596 8466 8542 -175 -2653 -431 C ATOM 603 SG CYS A 131 52.639 -28.798 -11.871 1.00 81.34 S ANISOU 603 SG CYS A 131 13265 8828 8812 -61 -2516 -355 S ATOM 604 N LYS A 132 49.569 -28.687 -9.466 1.00 76.03 N ANISOU 604 N LYS A 132 11845 8484 8558 -160 -2718 -465 N ATOM 605 CA LYS A 132 48.957 -27.536 -8.794 1.00 75.39 C ANISOU 605 CA LYS A 132 11618 8495 8533 -91 -2734 -471 C ATOM 606 C LYS A 132 48.919 -27.730 -7.275 1.00 77.99 C ANISOU 606 C LYS A 132 11714 8915 9004 -203 -2580 -433 C ATOM 607 O LYS A 132 49.171 -26.771 -6.546 1.00 77.35 O ANISOU 607 O LYS A 132 11589 8877 8922 -163 -2485 -386 O ATOM 608 CB LYS A 132 47.529 -27.287 -9.317 1.00 79.37 C ANISOU 608 CB LYS A 132 12018 9049 9092 -15 -2971 -588 C ATOM 609 CG LYS A 132 47.461 -26.791 -10.759 1.00 88.19 C ANISOU 609 CG LYS A 132 13385 10080 10044 136 -3149 -624 C ATOM 610 CD LYS A 132 46.024 -26.689 -11.254 1.00 94.35 C ANISOU 610 CD LYS A 132 14040 10916 10892 214 -3414 -756 C ATOM 611 CE LYS A 132 45.888 -26.090 -12.638 1.00 99.31 C ANISOU 611 CE LYS A 132 14934 11458 11339 390 -3615 -791 C ATOM 612 NZ LYS A 132 46.288 -24.652 -12.691 1.00101.72 N ANISOU 612 NZ LYS A 132 15402 11726 11522 541 -3570 -722 N ATOM 613 N ILE A 133 48.624 -28.962 -6.801 1.00 73.63 N ANISOU 613 N ILE A 133 11032 8382 8562 -344 -2550 -453 N ATOM 614 CA ILE A 133 48.533 -29.276 -5.371 1.00 72.24 C ANISOU 614 CA ILE A 133 10664 8278 8507 -459 -2402 -417 C ATOM 615 C ILE A 133 49.932 -29.229 -4.734 1.00 73.67 C ANISOU 615 C ILE A 133 10949 8425 8618 -477 -2214 -302 C ATOM 616 O ILE A 133 50.127 -28.494 -3.774 1.00 72.11 O ANISOU 616 O ILE A 133 10675 8285 8436 -466 -2113 -258 O ATOM 617 CB ILE A 133 47.852 -30.659 -5.131 1.00 76.17 C ANISOU 617 CB ILE A 133 11034 8778 9127 -609 -2413 -471 C ATOM 618 CG1 ILE A 133 46.379 -30.644 -5.625 1.00 78.22 C ANISOU 618 CG1 ILE A 133 11134 9093 9492 -600 -2600 -609 C ATOM 619 CG2 ILE A 133 47.923 -31.055 -3.644 1.00 76.32 C ANISOU 619 CG2 ILE A 133 10915 8846 9238 -731 -2232 -415 C ATOM 620 CD1 ILE A 133 45.611 -31.991 -5.527 1.00 84.80 C ANISOU 620 CD1 ILE A 133 11837 9921 10461 -761 -2619 -688 C ATOM 621 N VAL A 134 50.890 -30.002 -5.275 1.00 70.14 N ANISOU 621 N VAL A 134 10669 7883 8097 -501 -2175 -264 N ATOM 622 CA VAL A 134 52.262 -30.135 -4.769 1.00 68.65 C ANISOU 622 CA VAL A 134 10569 7657 7859 -517 -2014 -174 C ATOM 623 C VAL A 134 52.975 -28.762 -4.785 1.00 73.05 C ANISOU 623 C VAL A 134 11204 8220 8332 -413 -1957 -137 C ATOM 624 O VAL A 134 53.634 -28.432 -3.794 1.00 72.46 O ANISOU 624 O VAL A 134 11080 8181 8270 -429 -1832 -82 O ATOM 625 CB VAL A 134 53.054 -31.189 -5.575 1.00 72.24 C ANISOU 625 CB VAL A 134 11190 8001 8257 -541 -2003 -164 C ATOM 626 CG1 VAL A 134 54.509 -31.235 -5.156 1.00 70.60 C ANISOU 626 CG1 VAL A 134 11063 7755 8006 -535 -1851 -88 C ATOM 627 CG2 VAL A 134 52.428 -32.567 -5.414 1.00 72.92 C ANISOU 627 CG2 VAL A 134 11205 8069 8430 -658 -2035 -195 C ATOM 628 N LEU A 135 52.815 -27.955 -5.858 1.00 70.22 N ANISOU 628 N LEU A 135 10972 7823 7885 -308 -2049 -172 N ATOM 629 CA LEU A 135 53.444 -26.627 -5.909 1.00 69.80 C ANISOU 629 CA LEU A 135 11011 7758 7751 -218 -1983 -141 C ATOM 630 C LEU A 135 52.886 -25.702 -4.820 1.00 74.35 C ANISOU 630 C LEU A 135 11417 8436 8395 -203 -1958 -137 C ATOM 631 O LEU A 135 53.672 -25.060 -4.127 1.00 73.52 O ANISOU 631 O LEU A 135 11311 8347 8277 -201 -1831 -90 O ATOM 632 CB LEU A 135 53.279 -25.943 -7.285 1.00 70.75 C ANISOU 632 CB LEU A 135 11333 7801 7749 -103 -2089 -175 C ATOM 633 CG LEU A 135 54.043 -26.530 -8.484 1.00 75.46 C ANISOU 633 CG LEU A 135 12160 8275 8234 -94 -2082 -176 C ATOM 634 CD1 LEU A 135 53.616 -25.857 -9.770 1.00 76.27 C ANISOU 634 CD1 LEU A 135 12466 8306 8207 24 -2212 -215 C ATOM 635 CD2 LEU A 135 55.570 -26.420 -8.301 1.00 76.84 C ANISOU 635 CD2 LEU A 135 12431 8395 8369 -119 -1883 -120 C ATOM 636 N SER A 136 51.545 -25.649 -4.654 1.00 72.09 N ANISOU 636 N SER A 136 10979 8221 8191 -197 -2074 -195 N ATOM 637 CA SER A 136 50.893 -24.759 -3.684 1.00 71.82 C ANISOU 637 CA SER A 136 10780 8281 8227 -175 -2052 -205 C ATOM 638 C SER A 136 51.322 -25.080 -2.247 1.00 73.86 C ANISOU 638 C SER A 136 10914 8599 8550 -278 -1895 -152 C ATOM 639 O SER A 136 51.574 -24.151 -1.483 1.00 71.90 O ANISOU 639 O SER A 136 10631 8391 8296 -250 -1810 -127 O ATOM 640 CB SER A 136 49.375 -24.837 -3.802 1.00 76.93 C ANISOU 640 CB SER A 136 11265 8993 8974 -160 -2201 -294 C ATOM 641 OG SER A 136 48.881 -26.146 -3.587 1.00 86.22 O ANISOU 641 OG SER A 136 12323 10189 10248 -282 -2217 -325 O ATOM 642 N ILE A 137 51.455 -26.378 -1.902 1.00 70.84 N ANISOU 642 N ILE A 137 10490 8209 8216 -390 -1856 -135 N ATOM 643 CA ILE A 137 51.904 -26.821 -0.578 1.00 70.18 C ANISOU 643 CA ILE A 137 10329 8165 8173 -480 -1719 -79 C ATOM 644 C ILE A 137 53.371 -26.385 -0.373 1.00 74.20 C ANISOU 644 C ILE A 137 10957 8638 8597 -447 -1615 -15 C ATOM 645 O ILE A 137 53.711 -25.868 0.698 1.00 73.53 O ANISOU 645 O ILE A 137 10815 8606 8518 -457 -1522 16 O ATOM 646 CB ILE A 137 51.724 -28.365 -0.414 1.00 73.42 C ANISOU 646 CB ILE A 137 10709 8547 8639 -597 -1711 -74 C ATOM 647 CG1 ILE A 137 50.235 -28.760 -0.581 1.00 74.76 C ANISOU 647 CG1 ILE A 137 10734 8756 8914 -647 -1804 -157 C ATOM 648 CG2 ILE A 137 52.270 -28.851 0.954 1.00 74.18 C ANISOU 648 CG2 ILE A 137 10769 8666 8751 -675 -1573 -5 C ATOM 649 CD1 ILE A 137 49.934 -30.251 -0.562 1.00 81.68 C ANISOU 649 CD1 ILE A 137 11591 9591 9853 -771 -1799 -169 C ATOM 650 N ASP A 138 54.213 -26.554 -1.422 1.00 70.97 N ANISOU 650 N ASP A 138 10711 8140 8114 -409 -1629 -8 N ATOM 651 CA ASP A 138 55.641 -26.231 -1.397 1.00 70.22 C ANISOU 651 CA ASP A 138 10720 8003 7957 -384 -1528 31 C ATOM 652 C ASP A 138 55.851 -24.723 -1.128 1.00 73.87 C ANISOU 652 C ASP A 138 11188 8495 8386 -319 -1480 28 C ATOM 653 O ASP A 138 56.634 -24.389 -0.239 1.00 73.30 O ANISOU 653 O ASP A 138 11081 8453 8318 -336 -1382 55 O ATOM 654 CB ASP A 138 56.315 -26.650 -2.720 1.00 72.60 C ANISOU 654 CB ASP A 138 11196 8197 8191 -356 -1546 21 C ATOM 655 CG ASP A 138 57.836 -26.744 -2.678 1.00 86.19 C ANISOU 655 CG ASP A 138 12996 9868 9883 -357 -1428 48 C ATOM 656 OD1 ASP A 138 58.392 -26.942 -1.571 1.00 86.35 O ANISOU 656 OD1 ASP A 138 12927 9935 9946 -393 -1357 80 O ATOM 657 OD2 ASP A 138 58.462 -26.747 -3.762 1.00 94.00 O ANISOU 657 OD2 ASP A 138 14137 10769 10810 -323 -1410 33 O ATOM 658 N TYR A 139 55.109 -23.829 -1.845 1.00 70.44 N ANISOU 658 N TYR A 139 10796 8050 7919 -241 -1558 -8 N ATOM 659 CA TYR A 139 55.160 -22.363 -1.695 1.00 69.71 C ANISOU 659 CA TYR A 139 10729 7967 7789 -170 -1522 -15 C ATOM 660 C TYR A 139 54.501 -21.869 -0.404 1.00 72.80 C ANISOU 660 C TYR A 139 10947 8463 8251 -187 -1495 -18 C ATOM 661 O TYR A 139 55.146 -21.145 0.354 1.00 71.69 O ANISOU 661 O TYR A 139 10796 8344 8100 -190 -1396 0 O ATOM 662 CB TYR A 139 54.476 -21.645 -2.871 1.00 71.61 C ANISOU 662 CB TYR A 139 11088 8153 7967 -65 -1632 -51 C ATOM 663 CG TYR A 139 55.321 -21.497 -4.115 1.00 73.74 C ANISOU 663 CG TYR A 139 11592 8301 8125 -22 -1611 -45 C ATOM 664 CD1 TYR A 139 56.222 -20.447 -4.245 1.00 75.71 C ANISOU 664 CD1 TYR A 139 11970 8491 8306 11 -1496 -31 C ATOM 665 CD2 TYR A 139 55.112 -22.312 -5.222 1.00 75.12 C ANISOU 665 CD2 TYR A 139 11874 8413 8256 -12 -1707 -64 C ATOM 666 CE1 TYR A 139 56.967 -20.270 -5.410 1.00 77.35 C ANISOU 666 CE1 TYR A 139 12408 8576 8407 43 -1452 -31 C ATOM 667 CE2 TYR A 139 55.845 -22.141 -6.397 1.00 76.24 C ANISOU 667 CE2 TYR A 139 12255 8434 8280 30 -1676 -62 C ATOM 668 CZ TYR A 139 56.765 -21.112 -6.490 1.00 83.70 C ANISOU 668 CZ TYR A 139 13327 9318 9159 56 -1541 -44 C ATOM 669 OH TYR A 139 57.483 -20.932 -7.649 1.00 84.79 O ANISOU 669 OH TYR A 139 13711 9326 9178 87 -1484 -45 O ATOM 670 N TYR A 140 53.196 -22.180 -0.201 1.00 69.29 N ANISOU 670 N TYR A 140 10369 8079 7879 -196 -1582 -51 N ATOM 671 CA TYR A 140 52.400 -21.723 0.945 1.00 68.55 C ANISOU 671 CA TYR A 140 10107 8081 7858 -211 -1551 -68 C ATOM 672 C TYR A 140 53.169 -21.896 2.259 1.00 70.94 C ANISOU 672 C TYR A 140 10362 8426 8167 -288 -1417 -20 C ATOM 673 O TYR A 140 53.386 -20.910 2.965 1.00 70.92 O ANISOU 673 O TYR A 140 10341 8456 8149 -263 -1348 -18 O ATOM 674 CB TYR A 140 51.054 -22.477 1.021 1.00 70.20 C ANISOU 674 CB TYR A 140 10161 8344 8169 -253 -1634 -116 C ATOM 675 CG TYR A 140 50.227 -22.153 2.248 1.00 71.37 C ANISOU 675 CG TYR A 140 10127 8588 8402 -286 -1574 -139 C ATOM 676 CD1 TYR A 140 49.323 -21.095 2.246 1.00 73.84 C ANISOU 676 CD1 TYR A 140 10361 8942 8753 -197 -1621 -197 C ATOM 677 CD2 TYR A 140 50.330 -22.919 3.405 1.00 71.74 C ANISOU 677 CD2 TYR A 140 10095 8677 8488 -401 -1466 -106 C ATOM 678 CE1 TYR A 140 48.569 -20.787 3.378 1.00 74.51 C ANISOU 678 CE1 TYR A 140 10278 9113 8921 -228 -1548 -226 C ATOM 679 CE2 TYR A 140 49.586 -22.618 4.542 1.00 73.00 C ANISOU 679 CE2 TYR A 140 10108 8916 8713 -438 -1389 -128 C ATOM 680 CZ TYR A 140 48.699 -21.559 4.519 1.00 80.34 C ANISOU 680 CZ TYR A 140 10945 9891 9689 -355 -1425 -192 C ATOM 681 OH TYR A 140 47.963 -21.280 5.637 1.00 83.31 O ANISOU 681 OH TYR A 140 11175 10343 10135 -393 -1334 -222 O ATOM 682 N ASN A 141 53.593 -23.132 2.572 1.00 66.03 N ANISOU 682 N ASN A 141 9733 7796 7560 -375 -1388 15 N ATOM 683 CA ASN A 141 54.273 -23.423 3.824 1.00 64.83 C ANISOU 683 CA ASN A 141 9549 7680 7404 -437 -1286 59 C ATOM 684 C ASN A 141 55.736 -22.916 3.817 1.00 68.08 C ANISOU 684 C ASN A 141 10062 8055 7751 -406 -1226 82 C ATOM 685 O ASN A 141 56.313 -22.817 4.898 1.00 67.61 O ANISOU 685 O ASN A 141 9973 8034 7680 -433 -1156 104 O ATOM 686 CB ASN A 141 54.231 -24.900 4.134 1.00 64.72 C ANISOU 686 CB ASN A 141 9516 7653 7420 -525 -1281 90 C ATOM 687 CG ASN A 141 52.862 -25.360 4.558 1.00 92.35 C ANISOU 687 CG ASN A 141 12889 11201 10999 -587 -1292 62 C ATOM 688 OD1 ASN A 141 52.051 -25.816 3.747 1.00 91.96 O ANISOU 688 OD1 ASN A 141 12808 11133 10999 -598 -1374 20 O ATOM 689 ND2 ASN A 141 52.554 -25.192 5.839 1.00 81.49 N ANISOU 689 ND2 ASN A 141 11435 9888 9640 -632 -1206 75 N ATOM 690 N MET A 142 56.312 -22.523 2.656 1.00 64.34 N ANISOU 690 N MET A 142 9705 7507 7232 -350 -1246 68 N ATOM 691 CA MET A 142 57.656 -21.927 2.664 1.00 63.37 C ANISOU 691 CA MET A 142 9659 7352 7068 -333 -1168 70 C ATOM 692 C MET A 142 57.597 -20.589 3.382 1.00 67.64 C ANISOU 692 C MET A 142 10164 7937 7598 -306 -1115 51 C ATOM 693 O MET A 142 58.391 -20.349 4.288 1.00 67.64 O ANISOU 693 O MET A 142 10133 7969 7596 -331 -1047 55 O ATOM 694 CB MET A 142 58.231 -21.766 1.251 1.00 65.68 C ANISOU 694 CB MET A 142 10099 7543 7312 -290 -1173 55 C ATOM 695 CG MET A 142 59.595 -21.098 1.235 1.00 68.80 C ANISOU 695 CG MET A 142 10559 7900 7682 -286 -1069 41 C ATOM 696 SD MET A 142 60.034 -20.506 -0.410 1.00 73.35 S ANISOU 696 SD MET A 142 11337 8347 8185 -234 -1040 16 S ATOM 697 CE MET A 142 61.550 -19.793 -0.075 1.00 69.94 C ANISOU 697 CE MET A 142 10920 7892 7762 -262 -893 -14 C ATOM 698 N PHE A 143 56.618 -19.733 3.000 1.00 63.85 N ANISOU 698 N PHE A 143 9687 7459 7115 -248 -1156 26 N ATOM 699 CA PHE A 143 56.384 -18.430 3.625 1.00 63.17 C ANISOU 699 CA PHE A 143 9573 7406 7022 -212 -1110 3 C ATOM 700 C PHE A 143 55.858 -18.601 5.054 1.00 65.94 C ANISOU 700 C PHE A 143 9782 7857 7416 -261 -1080 8 C ATOM 701 O PHE A 143 56.270 -17.849 5.928 1.00 63.70 O ANISOU 701 O PHE A 143 9481 7605 7117 -267 -1009 -1 O ATOM 702 CB PHE A 143 55.406 -17.575 2.803 1.00 65.35 C ANISOU 702 CB PHE A 143 9895 7650 7285 -119 -1179 -27 C ATOM 703 CG PHE A 143 55.937 -17.164 1.455 1.00 67.15 C ANISOU 703 CG PHE A 143 10307 7765 7441 -62 -1191 -31 C ATOM 704 CD1 PHE A 143 56.699 -16.010 1.310 1.00 70.52 C ANISOU 704 CD1 PHE A 143 10850 8129 7816 -33 -1103 -41 C ATOM 705 CD2 PHE A 143 55.652 -17.910 0.321 1.00 69.54 C ANISOU 705 CD2 PHE A 143 10684 8015 7724 -40 -1283 -28 C ATOM 706 CE1 PHE A 143 57.171 -15.617 0.054 1.00 71.47 C ANISOU 706 CE1 PHE A 143 11167 8129 7859 13 -1091 -43 C ATOM 707 CE2 PHE A 143 56.142 -17.528 -0.929 1.00 72.50 C ANISOU 707 CE2 PHE A 143 11259 8276 8013 13 -1284 -30 C ATOM 708 CZ PHE A 143 56.902 -16.388 -1.053 1.00 70.65 C ANISOU 708 CZ PHE A 143 11148 7974 7723 38 -1180 -35 C ATOM 709 N THR A 144 54.977 -19.603 5.297 1.00 63.56 N ANISOU 709 N THR A 144 9389 7597 7163 -303 -1124 19 N ATOM 710 CA THR A 144 54.419 -19.867 6.628 1.00 64.12 C ANISOU 710 CA THR A 144 9345 7751 7268 -360 -1074 25 C ATOM 711 C THR A 144 55.570 -20.282 7.570 1.00 68.41 C ANISOU 711 C THR A 144 9916 8306 7769 -413 -1010 64 C ATOM 712 O THR A 144 55.601 -19.830 8.718 1.00 68.53 O ANISOU 712 O THR A 144 9895 8375 7767 -430 -948 61 O ATOM 713 CB THR A 144 53.297 -20.916 6.563 1.00 73.16 C ANISOU 713 CB THR A 144 10399 8917 8480 -410 -1119 21 C ATOM 714 OG1 THR A 144 52.290 -20.440 5.676 1.00 73.50 O ANISOU 714 OG1 THR A 144 10407 8955 8566 -344 -1201 -30 O ATOM 715 CG2 THR A 144 52.652 -21.179 7.921 1.00 73.05 C ANISOU 715 CG2 THR A 144 10281 8976 8498 -479 -1040 25 C ATOM 716 N SER A 145 56.549 -21.065 7.064 1.00 63.92 N ANISOU 716 N SER A 145 9419 7684 7182 -427 -1030 90 N ATOM 717 CA SER A 145 57.730 -21.458 7.843 1.00 62.88 C ANISOU 717 CA SER A 145 9312 7560 7018 -454 -994 115 C ATOM 718 C SER A 145 58.623 -20.227 8.170 1.00 65.16 C ANISOU 718 C SER A 145 9622 7859 7278 -423 -945 79 C ATOM 719 O SER A 145 58.929 -19.979 9.337 1.00 63.74 O ANISOU 719 O SER A 145 9414 7731 7073 -441 -911 77 O ATOM 720 CB SER A 145 58.542 -22.513 7.090 1.00 65.30 C ANISOU 720 CB SER A 145 9681 7802 7329 -460 -1029 137 C ATOM 721 OG SER A 145 59.779 -22.815 7.718 1.00 72.20 O ANISOU 721 OG SER A 145 10571 8678 8182 -464 -1011 147 O ATOM 722 N ILE A 146 58.989 -19.451 7.135 1.00 61.42 N ANISOU 722 N ILE A 146 9208 7328 6802 -382 -939 47 N ATOM 723 CA ILE A 146 59.910 -18.322 7.223 1.00 60.93 C ANISOU 723 CA ILE A 146 9179 7250 6721 -366 -879 4 C ATOM 724 C ILE A 146 59.246 -17.120 7.969 1.00 65.38 C ANISOU 724 C ILE A 146 9709 7858 7272 -349 -842 -23 C ATOM 725 O ILE A 146 59.924 -16.511 8.798 1.00 64.70 O ANISOU 725 O ILE A 146 9610 7801 7170 -366 -795 -53 O ATOM 726 CB ILE A 146 60.377 -17.931 5.793 1.00 63.59 C ANISOU 726 CB ILE A 146 9619 7490 7052 -335 -864 -17 C ATOM 727 CG1 ILE A 146 61.211 -19.104 5.176 1.00 63.38 C ANISOU 727 CG1 ILE A 146 9622 7419 7041 -354 -881 -2 C ATOM 728 CG2 ILE A 146 61.203 -16.639 5.814 1.00 64.38 C ANISOU 728 CG2 ILE A 146 9764 7558 7140 -331 -779 -70 C ATOM 729 CD1 ILE A 146 61.600 -18.989 3.691 1.00 69.70 C ANISOU 729 CD1 ILE A 146 10542 8116 7825 -330 -860 -17 C ATOM 730 N PHE A 147 57.956 -16.797 7.717 1.00 62.25 N ANISOU 730 N PHE A 147 9294 7471 6888 -314 -867 -22 N ATOM 731 CA PHE A 147 57.319 -15.655 8.395 1.00 62.14 C ANISOU 731 CA PHE A 147 9247 7493 6869 -287 -827 -55 C ATOM 732 C PHE A 147 57.046 -15.949 9.890 1.00 65.11 C ANISOU 732 C PHE A 147 9540 7959 7239 -336 -793 -47 C ATOM 733 O PHE A 147 57.122 -15.017 10.687 1.00 64.45 O ANISOU 733 O PHE A 147 9451 7904 7134 -331 -738 -80 O ATOM 734 CB PHE A 147 56.014 -15.211 7.723 1.00 64.39 C ANISOU 734 CB PHE A 147 9521 7764 7179 -219 -871 -68 C ATOM 735 CG PHE A 147 56.159 -14.670 6.314 1.00 66.00 C ANISOU 735 CG PHE A 147 9845 7871 7361 -151 -905 -78 C ATOM 736 CD1 PHE A 147 57.302 -13.969 5.932 1.00 68.56 C ANISOU 736 CD1 PHE A 147 10283 8122 7643 -151 -842 -93 C ATOM 737 CD2 PHE A 147 55.082 -14.684 5.436 1.00 68.60 C ANISOU 737 CD2 PHE A 147 10180 8178 7709 -82 -993 -85 C ATOM 738 CE1 PHE A 147 57.420 -13.436 4.645 1.00 69.52 C ANISOU 738 CE1 PHE A 147 10549 8138 7728 -92 -853 -98 C ATOM 739 CE2 PHE A 147 55.189 -14.117 4.158 1.00 71.32 C ANISOU 739 CE2 PHE A 147 10670 8421 8008 -5 -1029 -91 C ATOM 740 CZ PHE A 147 56.358 -13.503 3.769 1.00 68.90 C ANISOU 740 CZ PHE A 147 10502 8032 7645 -13 -950 -93 C ATOM 741 N THR A 148 56.755 -17.212 10.274 1.00 61.80 N ANISOU 741 N THR A 148 9077 7574 6832 -384 -818 -5 N ATOM 742 CA THR A 148 56.561 -17.563 11.692 1.00 62.20 C ANISOU 742 CA THR A 148 9086 7692 6854 -433 -775 11 C ATOM 743 C THR A 148 57.916 -17.415 12.404 1.00 67.21 C ANISOU 743 C THR A 148 9768 8336 7434 -446 -762 4 C ATOM 744 O THR A 148 57.993 -16.793 13.463 1.00 67.13 O ANISOU 744 O THR A 148 9755 8369 7381 -454 -718 -20 O ATOM 745 CB THR A 148 55.957 -18.978 11.839 1.00 67.31 C ANISOU 745 CB THR A 148 9703 8350 7523 -486 -793 59 C ATOM 746 OG1 THR A 148 54.706 -19.016 11.153 1.00 64.28 O ANISOU 746 OG1 THR A 148 9253 7963 7207 -474 -813 42 O ATOM 747 CG2 THR A 148 55.748 -19.389 13.302 1.00 65.93 C ANISOU 747 CG2 THR A 148 9523 8227 7300 -540 -732 83 C ATOM 748 N LEU A 149 58.984 -17.923 11.758 1.00 64.15 N ANISOU 748 N LEU A 149 9419 7903 7052 -444 -804 13 N ATOM 749 CA LEU A 149 60.379 -17.892 12.192 1.00 64.06 C ANISOU 749 CA LEU A 149 9429 7894 7015 -449 -813 -10 C ATOM 750 C LEU A 149 60.871 -16.458 12.429 1.00 69.60 C ANISOU 750 C LEU A 149 10136 8601 7709 -438 -765 -81 C ATOM 751 O LEU A 149 61.670 -16.221 13.338 1.00 70.48 O ANISOU 751 O LEU A 149 10241 8748 7789 -451 -766 -116 O ATOM 752 CB LEU A 149 61.224 -18.555 11.091 1.00 63.69 C ANISOU 752 CB LEU A 149 9407 7785 7007 -440 -850 -4 C ATOM 753 CG LEU A 149 62.661 -18.891 11.407 1.00 68.66 C ANISOU 753 CG LEU A 149 10034 8416 7639 -439 -875 -31 C ATOM 754 CD1 LEU A 149 62.727 -20.040 12.369 1.00 69.74 C ANISOU 754 CD1 LEU A 149 10174 8588 7737 -445 -930 19 C ATOM 755 CD2 LEU A 149 63.369 -19.333 10.176 1.00 70.36 C ANISOU 755 CD2 LEU A 149 10270 8561 7904 -428 -882 -39 C ATOM 756 N THR A 150 60.396 -15.513 11.592 1.00 65.88 N ANISOU 756 N THR A 150 9685 8085 7261 -411 -729 -106 N ATOM 757 CA THR A 150 60.753 -14.094 11.627 1.00 65.58 C ANISOU 757 CA THR A 150 9675 8025 7218 -400 -669 -172 C ATOM 758 C THR A 150 59.965 -13.373 12.737 1.00 70.30 C ANISOU 758 C THR A 150 10249 8681 7783 -397 -631 -190 C ATOM 759 O THR A 150 60.538 -12.523 13.414 1.00 69.78 O ANISOU 759 O THR A 150 10193 8626 7692 -411 -593 -247 O ATOM 760 CB THR A 150 60.489 -13.469 10.249 1.00 70.66 C ANISOU 760 CB THR A 150 10384 8580 7885 -360 -648 -179 C ATOM 761 OG1 THR A 150 61.219 -14.209 9.271 1.00 68.23 O ANISOU 761 OG1 THR A 150 10107 8218 7598 -369 -670 -164 O ATOM 762 CG2 THR A 150 60.892 -12.006 10.169 1.00 69.26 C ANISOU 762 CG2 THR A 150 10265 8352 7699 -353 -572 -244 C ATOM 763 N MET A 151 58.678 -13.721 12.946 1.00 68.20 N ANISOU 763 N MET A 151 9946 8448 7519 -383 -636 -153 N ATOM 764 CA MET A 151 57.867 -13.096 13.998 1.00 68.96 C ANISOU 764 CA MET A 151 10014 8597 7589 -380 -582 -175 C ATOM 765 C MET A 151 58.328 -13.556 15.376 1.00 73.45 C ANISOU 765 C MET A 151 10585 9230 8094 -428 -576 -170 C ATOM 766 O MET A 151 58.101 -12.848 16.352 1.00 73.42 O ANISOU 766 O MET A 151 10588 9262 8047 -432 -523 -207 O ATOM 767 CB MET A 151 56.379 -13.371 13.818 1.00 71.88 C ANISOU 767 CB MET A 151 10324 8986 8000 -358 -579 -152 C ATOM 768 CG MET A 151 55.800 -12.697 12.600 1.00 76.28 C ANISOU 768 CG MET A 151 10891 9485 8608 -286 -601 -171 C ATOM 769 SD MET A 151 56.128 -10.907 12.542 1.00 81.57 S ANISOU 769 SD MET A 151 11636 10101 9257 -232 -542 -237 S ATOM 770 CE MET A 151 57.385 -10.854 11.263 1.00 77.90 C ANISOU 770 CE MET A 151 11274 9538 8787 -233 -568 -232 C ATOM 771 N MET A 152 59.025 -14.699 15.447 1.00 70.39 N ANISOU 771 N MET A 152 10207 8848 7691 -455 -634 -130 N ATOM 772 CA MET A 152 59.655 -15.168 16.678 1.00 71.06 C ANISOU 772 CA MET A 152 10320 8980 7700 -481 -655 -125 C ATOM 773 C MET A 152 60.799 -14.244 17.027 1.00 74.73 C ANISOU 773 C MET A 152 10800 9448 8144 -479 -663 -202 C ATOM 774 O MET A 152 60.991 -13.914 18.196 1.00 75.82 O ANISOU 774 O MET A 152 10965 9632 8210 -490 -656 -234 O ATOM 775 CB MET A 152 60.138 -16.615 16.536 1.00 73.55 C ANISOU 775 CB MET A 152 10649 9284 8010 -492 -726 -63 C ATOM 776 CG MET A 152 59.031 -17.601 16.378 1.00 77.85 C ANISOU 776 CG MET A 152 11185 9824 8569 -513 -711 6 C ATOM 777 SD MET A 152 59.704 -19.237 16.105 1.00 82.75 S ANISOU 777 SD MET A 152 11845 10410 9187 -520 -792 74 S ATOM 778 CE MET A 152 58.270 -20.136 16.002 1.00 79.87 C ANISOU 778 CE MET A 152 11467 10035 8846 -565 -747 134 C ATOM 779 N SER A 153 61.531 -13.788 15.987 1.00 69.22 N ANISOU 779 N SER A 153 10092 8698 7512 -470 -669 -241 N ATOM 780 CA SER A 153 62.640 -12.850 16.090 1.00 68.52 C ANISOU 780 CA SER A 153 10004 8597 7435 -483 -658 -332 C ATOM 781 C SER A 153 62.121 -11.485 16.575 1.00 72.05 C ANISOU 781 C SER A 153 10475 9046 7856 -484 -581 -387 C ATOM 782 O SER A 153 62.696 -10.904 17.500 1.00 72.23 O ANISOU 782 O SER A 153 10505 9101 7839 -505 -580 -455 O ATOM 783 CB SER A 153 63.347 -12.733 14.739 1.00 70.87 C ANISOU 783 CB SER A 153 10298 8820 7812 -484 -647 -353 C ATOM 784 OG SER A 153 64.462 -11.864 14.771 1.00 78.29 O ANISOU 784 OG SER A 153 11228 9739 8781 -513 -618 -451 O ATOM 785 N VAL A 154 60.985 -11.021 15.993 1.00 67.49 N ANISOU 785 N VAL A 154 9908 8434 7300 -452 -526 -361 N ATOM 786 CA VAL A 154 60.320 -9.749 16.318 1.00 66.92 C ANISOU 786 CA VAL A 154 9862 8352 7215 -433 -450 -407 C ATOM 787 C VAL A 154 59.758 -9.822 17.752 1.00 70.50 C ANISOU 787 C VAL A 154 10311 8883 7595 -445 -430 -409 C ATOM 788 O VAL A 154 59.870 -8.845 18.499 1.00 71.24 O ANISOU 788 O VAL A 154 10434 8984 7649 -452 -383 -476 O ATOM 789 CB VAL A 154 59.205 -9.409 15.282 1.00 69.99 C ANISOU 789 CB VAL A 154 10256 8686 7650 -374 -423 -377 C ATOM 790 CG1 VAL A 154 58.452 -8.132 15.661 1.00 69.98 C ANISOU 790 CG1 VAL A 154 10280 8670 7639 -336 -349 -425 C ATOM 791 CG2 VAL A 154 59.781 -9.290 13.871 1.00 69.27 C ANISOU 791 CG2 VAL A 154 10210 8505 7606 -361 -435 -374 C ATOM 792 N ASP A 155 59.181 -10.982 18.133 1.00 65.77 N ANISOU 792 N ASP A 155 9688 8330 6970 -453 -457 -339 N ATOM 793 CA ASP A 155 58.614 -11.212 19.464 1.00 66.04 C ANISOU 793 CA ASP A 155 9741 8428 6924 -471 -420 -330 C ATOM 794 C ASP A 155 59.715 -11.124 20.524 1.00 67.97 C ANISOU 794 C ASP A 155 10040 8707 7079 -497 -462 -374 C ATOM 795 O ASP A 155 59.547 -10.399 21.506 1.00 67.86 O ANISOU 795 O ASP A 155 10067 8720 6997 -504 -413 -425 O ATOM 796 CB ASP A 155 57.910 -12.574 19.519 1.00 68.58 C ANISOU 796 CB ASP A 155 10043 8772 7242 -488 -432 -244 C ATOM 797 CG ASP A 155 57.132 -12.820 20.790 1.00 83.08 C ANISOU 797 CG ASP A 155 11912 10657 8998 -515 -359 -229 C ATOM 798 OD1 ASP A 155 55.992 -12.303 20.898 1.00 85.09 O ANISOU 798 OD1 ASP A 155 12125 10920 9283 -506 -267 -249 O ATOM 799 OD2 ASP A 155 57.615 -13.611 21.637 1.00 88.07 O ANISOU 799 OD2 ASP A 155 12613 11312 9536 -542 -392 -196 O ATOM 800 N ARG A 156 60.867 -11.814 20.285 1.00 62.83 N ANISOU 800 N ARG A 156 9386 8053 6435 -505 -560 -368 N ATOM 801 CA ARG A 156 62.051 -11.801 21.166 1.00 62.26 C ANISOU 801 CA ARG A 156 9345 8015 6297 -516 -636 -424 C ATOM 802 C ARG A 156 62.694 -10.406 21.198 1.00 64.89 C ANISOU 802 C ARG A 156 9670 8332 6654 -531 -608 -540 C ATOM 803 O ARG A 156 63.256 -10.021 22.224 1.00 64.88 O ANISOU 803 O ARG A 156 9704 8369 6580 -544 -642 -608 O ATOM 804 CB ARG A 156 63.105 -12.846 20.741 1.00 60.13 C ANISOU 804 CB ARG A 156 9047 7740 6058 -507 -748 -402 C ATOM 805 CG ARG A 156 62.689 -14.312 20.875 1.00 65.32 C ANISOU 805 CG ARG A 156 9737 8404 6676 -495 -789 -294 C ATOM 806 CD ARG A 156 63.835 -15.203 20.441 1.00 78.88 C ANISOU 806 CD ARG A 156 11428 10109 8433 -473 -902 -289 C ATOM 807 NE ARG A 156 63.486 -16.626 20.387 1.00 93.39 N ANISOU 807 NE ARG A 156 13306 11933 10246 -459 -938 -185 N ATOM 808 CZ ARG A 156 64.334 -17.585 20.020 1.00111.92 C ANISOU 808 CZ ARG A 156 15641 14260 12623 -429 -1033 -165 C ATOM 809 NH1 ARG A 156 65.585 -17.286 19.683 1.00 98.84 N ANISOU 809 NH1 ARG A 156 13917 12605 11033 -409 -1099 -248 N ATOM 810 NH2 ARG A 156 63.940 -18.852 19.995 1.00101.13 N ANISOU 810 NH2 ARG A 156 14329 12868 11229 -420 -1054 -69 N ATOM 811 N TYR A 157 62.610 -9.655 20.080 1.00 60.54 N ANISOU 811 N TYR A 157 9088 7716 6198 -530 -548 -563 N ATOM 812 CA TYR A 157 63.134 -8.290 19.981 1.00 60.61 C ANISOU 812 CA TYR A 157 9106 7685 6238 -553 -495 -669 C ATOM 813 C TYR A 157 62.329 -7.327 20.865 1.00 65.14 C ANISOU 813 C TYR A 157 9734 8272 6746 -547 -416 -706 C ATOM 814 O TYR A 157 62.918 -6.575 21.645 1.00 65.15 O ANISOU 814 O TYR A 157 9762 8286 6706 -577 -415 -800 O ATOM 815 CB TYR A 157 63.122 -7.806 18.526 1.00 61.02 C ANISOU 815 CB TYR A 157 9151 7645 6389 -546 -437 -666 C ATOM 816 CG TYR A 157 63.280 -6.309 18.402 1.00 63.80 C ANISOU 816 CG TYR A 157 9548 7933 6762 -564 -347 -757 C ATOM 817 CD1 TYR A 157 64.528 -5.706 18.531 1.00 66.69 C ANISOU 817 CD1 TYR A 157 9903 8278 7159 -624 -344 -867 C ATOM 818 CD2 TYR A 157 62.179 -5.491 18.159 1.00 64.61 C ANISOU 818 CD2 TYR A 157 9701 7988 6860 -520 -264 -741 C ATOM 819 CE1 TYR A 157 64.676 -4.323 18.436 1.00 67.92 C ANISOU 819 CE1 TYR A 157 10113 8359 7334 -652 -248 -954 C ATOM 820 CE2 TYR A 157 62.314 -4.107 18.067 1.00 66.09 C ANISOU 820 CE2 TYR A 157 9952 8100 7061 -530 -178 -822 C ATOM 821 CZ TYR A 157 63.565 -3.527 18.210 1.00 74.97 C ANISOU 821 CZ TYR A 157 11080 9196 8208 -603 -163 -926 C ATOM 822 OH TYR A 157 63.709 -2.164 18.129 1.00 78.99 O ANISOU 822 OH TYR A 157 11663 9618 8730 -625 -66 -1009 O ATOM 823 N ILE A 158 60.992 -7.329 20.707 1.00 62.06 N ANISOU 823 N ILE A 158 9350 7876 6355 -510 -350 -643 N ATOM 824 CA ILE A 158 60.077 -6.481 21.472 1.00 62.91 C ANISOU 824 CA ILE A 158 9496 7993 6413 -493 -260 -676 C ATOM 825 C ILE A 158 60.196 -6.841 22.961 1.00 68.66 C ANISOU 825 C ILE A 158 10272 8797 7019 -519 -281 -690 C ATOM 826 O ILE A 158 60.237 -5.942 23.796 1.00 69.75 O ANISOU 826 O ILE A 158 10464 8942 7097 -530 -235 -768 O ATOM 827 CB ILE A 158 58.622 -6.631 20.932 1.00 65.52 C ANISOU 827 CB ILE A 158 9792 8311 6792 -441 -200 -609 C ATOM 828 CG1 ILE A 158 58.531 -5.965 19.534 1.00 65.13 C ANISOU 828 CG1 ILE A 158 9737 8172 6838 -399 -185 -614 C ATOM 829 CG2 ILE A 158 57.579 -6.020 21.899 1.00 66.87 C ANISOU 829 CG2 ILE A 158 9984 8509 6913 -422 -101 -640 C ATOM 830 CD1 ILE A 158 57.195 -6.029 18.844 1.00 72.89 C ANISOU 830 CD1 ILE A 158 10678 9137 7881 -331 -159 -566 C ATOM 831 N ALA A 159 60.356 -8.138 23.273 1.00 64.73 N ANISOU 831 N ALA A 159 9773 8346 6474 -527 -354 -620 N ATOM 832 CA ALA A 159 60.504 -8.645 24.636 1.00 65.27 C ANISOU 832 CA ALA A 159 9920 8475 6406 -542 -387 -617 C ATOM 833 C ALA A 159 61.622 -7.925 25.426 1.00 70.01 C ANISOU 833 C ALA A 159 10567 9093 6940 -562 -450 -729 C ATOM 834 O ALA A 159 61.457 -7.664 26.615 1.00 70.89 O ANISOU 834 O ALA A 159 10769 9239 6929 -568 -430 -764 O ATOM 835 CB ALA A 159 60.807 -10.130 24.592 1.00 65.68 C ANISOU 835 CB ALA A 159 9975 8548 6434 -540 -481 -529 C ATOM 836 N VAL A 160 62.727 -7.590 24.767 1.00 66.30 N ANISOU 836 N VAL A 160 10038 8598 6554 -576 -516 -793 N ATOM 837 CA VAL A 160 63.887 -7.006 25.421 1.00 67.30 C ANISOU 837 CA VAL A 160 10179 8745 6647 -603 -592 -914 C ATOM 838 C VAL A 160 63.927 -5.479 25.225 1.00 72.38 C ANISOU 838 C VAL A 160 10822 9335 7342 -634 -497 -1022 C ATOM 839 O VAL A 160 64.187 -4.749 26.188 1.00 74.16 O ANISOU 839 O VAL A 160 11107 9581 7491 -656 -499 -1118 O ATOM 840 CB VAL A 160 65.174 -7.667 24.849 1.00 71.35 C ANISOU 840 CB VAL A 160 10608 9264 7239 -607 -721 -935 C ATOM 841 CG1 VAL A 160 66.426 -7.137 25.531 1.00 72.50 C ANISOU 841 CG1 VAL A 160 10738 9439 7368 -636 -820 -1080 C ATOM 842 CG2 VAL A 160 65.113 -9.182 24.978 1.00 71.07 C ANISOU 842 CG2 VAL A 160 10586 9263 7154 -567 -813 -824 C ATOM 843 N CYS A 161 63.694 -5.005 23.990 1.00 67.53 N ANISOU 843 N CYS A 161 10162 8647 6849 -634 -417 -1007 N ATOM 844 CA CYS A 161 63.852 -3.603 23.631 1.00 67.35 C ANISOU 844 CA CYS A 161 10157 8549 6884 -662 -325 -1103 C ATOM 845 C CYS A 161 62.579 -2.784 23.922 1.00 72.25 C ANISOU 845 C CYS A 161 10846 9141 7466 -626 -201 -1092 C ATOM 846 O CYS A 161 62.702 -1.593 24.219 1.00 72.56 O ANISOU 846 O CYS A 161 10936 9134 7498 -648 -135 -1190 O ATOM 847 CB CYS A 161 64.237 -3.486 22.165 1.00 66.58 C ANISOU 847 CB CYS A 161 10011 8368 6917 -672 -295 -1090 C ATOM 848 SG CYS A 161 65.805 -4.290 21.760 1.00 70.34 S ANISOU 848 SG CYS A 161 10390 8869 7468 -718 -412 -1132 S ATOM 849 N HIS A 162 61.384 -3.381 23.839 1.00 69.11 N ANISOU 849 N HIS A 162 10443 8764 7051 -572 -166 -987 N ATOM 850 CA HIS A 162 60.144 -2.641 24.121 1.00 69.66 C ANISOU 850 CA HIS A 162 10553 8813 7102 -529 -47 -989 C ATOM 851 C HIS A 162 59.347 -3.397 25.214 1.00 74.48 C ANISOU 851 C HIS A 162 11185 9505 7608 -519 -33 -939 C ATOM 852 O HIS A 162 58.334 -4.030 24.903 1.00 74.09 O ANISOU 852 O HIS A 162 11092 9471 7590 -484 4 -855 O ATOM 853 CB HIS A 162 59.335 -2.465 22.823 1.00 69.74 C ANISOU 853 CB HIS A 162 10526 8754 7220 -469 3 -929 C ATOM 854 CG HIS A 162 60.103 -1.796 21.721 1.00 72.68 C ANISOU 854 CG HIS A 162 10911 9030 7674 -481 4 -966 C ATOM 855 ND1 HIS A 162 60.110 -0.421 21.576 1.00 74.97 N ANISOU 855 ND1 HIS A 162 11273 9229 7983 -473 90 -1044 N ATOM 856 CD2 HIS A 162 60.882 -2.341 20.757 1.00 73.54 C ANISOU 856 CD2 HIS A 162 10984 9112 7845 -505 -56 -936 C ATOM 857 CE1 HIS A 162 60.882 -0.175 20.528 1.00 73.95 C ANISOU 857 CE1 HIS A 162 11158 9018 7922 -499 87 -1056 C ATOM 858 NE2 HIS A 162 61.369 -1.299 20.003 1.00 73.41 N ANISOU 858 NE2 HIS A 162 11022 8987 7883 -518 3 -995 N ATOM 859 N PRO A 163 59.830 -3.403 26.488 1.00 71.87 N ANISOU 859 N PRO A 163 10929 9227 7151 -553 -63 -993 N ATOM 860 CA PRO A 163 59.187 -4.234 27.520 1.00 72.29 C ANISOU 860 CA PRO A 163 11036 9347 7086 -551 -44 -938 C ATOM 861 C PRO A 163 57.746 -3.832 27.841 1.00 76.17 C ANISOU 861 C PRO A 163 11538 9833 7572 -520 114 -928 C ATOM 862 O PRO A 163 56.963 -4.703 28.218 1.00 76.20 O ANISOU 862 O PRO A 163 11544 9875 7535 -520 159 -856 O ATOM 863 CB PRO A 163 60.071 -4.006 28.750 1.00 75.25 C ANISOU 863 CB PRO A 163 11514 9759 7319 -585 -111 -1023 C ATOM 864 CG PRO A 163 61.395 -3.620 28.187 1.00 79.27 C ANISOU 864 CG PRO A 163 11973 10244 7902 -613 -219 -1098 C ATOM 865 CD PRO A 163 61.042 -2.754 27.028 1.00 74.13 C ANISOU 865 CD PRO A 163 11260 9513 7394 -600 -128 -1110 C ATOM 866 N VAL A 164 57.389 -2.546 27.701 1.00 72.28 N ANISOU 866 N VAL A 164 11051 9288 7125 -494 204 -1005 N ATOM 867 CA VAL A 164 56.021 -2.104 28.001 1.00 72.36 C ANISOU 867 CA VAL A 164 11054 9292 7147 -451 355 -1012 C ATOM 868 C VAL A 164 55.100 -2.546 26.830 1.00 74.98 C ANISOU 868 C VAL A 164 11259 9607 7624 -399 372 -933 C ATOM 869 O VAL A 164 53.940 -2.912 27.063 1.00 75.00 O ANISOU 869 O VAL A 164 11212 9638 7646 -378 464 -904 O ATOM 870 CB VAL A 164 55.953 -0.584 28.274 1.00 76.77 C ANISOU 870 CB VAL A 164 11672 9792 7704 -428 439 -1124 C ATOM 871 CG1 VAL A 164 54.530 -0.147 28.598 1.00 77.27 C ANISOU 871 CG1 VAL A 164 11717 9852 7791 -370 597 -1140 C ATOM 872 CG2 VAL A 164 56.892 -0.197 29.417 1.00 77.53 C ANISOU 872 CG2 VAL A 164 11892 9909 7658 -486 405 -1213 C ATOM 873 N LYS A 165 55.651 -2.578 25.594 1.00 69.61 N ANISOU 873 N LYS A 165 10527 8881 7040 -384 281 -905 N ATOM 874 CA LYS A 165 54.945 -3.049 24.401 1.00 67.89 C ANISOU 874 CA LYS A 165 10205 8645 6947 -334 263 -834 C ATOM 875 C LYS A 165 54.789 -4.552 24.439 1.00 69.95 C ANISOU 875 C LYS A 165 10417 8968 7195 -372 215 -743 C ATOM 876 O LYS A 165 53.789 -5.062 23.954 1.00 70.35 O ANISOU 876 O LYS A 165 10376 9028 7324 -342 242 -696 O ATOM 877 CB LYS A 165 55.665 -2.632 23.110 1.00 69.46 C ANISOU 877 CB LYS A 165 10400 8764 7226 -313 190 -834 C ATOM 878 CG LYS A 165 55.624 -1.130 22.849 1.00 88.93 C ANISOU 878 CG LYS A 165 12926 11141 9722 -265 253 -913 C ATOM 879 CD LYS A 165 56.235 -0.749 21.493 1.00 95.77 C ANISOU 879 CD LYS A 165 13814 11912 10661 -245 204 -903 C ATOM 880 CE LYS A 165 56.019 0.707 21.154 1.00103.32 C ANISOU 880 CE LYS A 165 14852 12760 11646 -184 278 -969 C ATOM 881 NZ LYS A 165 56.688 1.622 22.118 1.00113.74 N ANISOU 881 NZ LYS A 165 16258 14061 12897 -242 336 -1070 N ATOM 882 N ALA A 166 55.765 -5.259 25.042 1.00 64.48 N ANISOU 882 N ALA A 166 9784 8312 6405 -433 141 -723 N ATOM 883 CA ALA A 166 55.795 -6.716 25.173 1.00 63.19 C ANISOU 883 CA ALA A 166 9609 8193 6208 -470 89 -634 C ATOM 884 C ALA A 166 54.551 -7.228 25.914 1.00 66.79 C ANISOU 884 C ALA A 166 10058 8688 6632 -483 208 -605 C ATOM 885 O ALA A 166 54.026 -8.276 25.563 1.00 66.15 O ANISOU 885 O ALA A 166 9920 8620 6596 -499 207 -532 O ATOM 886 CB ALA A 166 57.058 -7.140 25.902 1.00 64.00 C ANISOU 886 CB ALA A 166 9801 8322 6192 -512 -11 -641 C ATOM 887 N LEU A 167 54.062 -6.463 26.897 1.00 64.14 N ANISOU 887 N LEU A 167 9779 8364 6229 -481 324 -669 N ATOM 888 CA LEU A 167 52.847 -6.762 27.662 1.00 65.15 C ANISOU 888 CA LEU A 167 9900 8521 6332 -498 477 -664 C ATOM 889 C LEU A 167 51.609 -6.749 26.761 1.00 71.32 C ANISOU 889 C LEU A 167 10518 9294 7286 -456 539 -659 C ATOM 890 O LEU A 167 50.679 -7.534 26.955 1.00 71.49 O ANISOU 890 O LEU A 167 10481 9343 7340 -488 626 -627 O ATOM 891 CB LEU A 167 52.675 -5.716 28.794 1.00 66.01 C ANISOU 891 CB LEU A 167 10107 8633 6341 -494 590 -755 C ATOM 892 CG LEU A 167 53.784 -5.608 29.834 1.00 70.39 C ANISOU 892 CG LEU A 167 10831 9200 6712 -531 530 -784 C ATOM 893 CD1 LEU A 167 53.676 -4.334 30.601 1.00 71.31 C ANISOU 893 CD1 LEU A 167 11025 9304 6766 -514 621 -891 C ATOM 894 CD2 LEU A 167 53.800 -6.798 30.760 1.00 73.24 C ANISOU 894 CD2 LEU A 167 11305 9595 6928 -586 542 -716 C ATOM 895 N ASP A 168 51.626 -5.857 25.779 1.00 69.18 N ANISOU 895 N ASP A 168 10182 8982 7124 -383 491 -696 N ATOM 896 CA ASP A 168 50.524 -5.668 24.848 1.00 69.84 C ANISOU 896 CA ASP A 168 10117 9050 7368 -314 515 -706 C ATOM 897 C ASP A 168 50.734 -6.339 23.500 1.00 73.97 C ANISOU 897 C ASP A 168 10567 9552 7985 -297 380 -641 C ATOM 898 O ASP A 168 50.008 -6.049 22.572 1.00 73.99 O ANISOU 898 O ASP A 168 10468 9533 8114 -223 359 -656 O ATOM 899 CB ASP A 168 50.265 -4.169 24.572 1.00 72.12 C ANISOU 899 CB ASP A 168 10404 9288 7710 -220 548 -791 C ATOM 900 CG ASP A 168 50.408 -3.263 25.807 1.00 78.71 C ANISOU 900 CG ASP A 168 11349 10123 8435 -232 658 -868 C ATOM 901 OD1 ASP A 168 49.689 -3.416 26.799 1.00 79.36 O ANISOU 901 OD1 ASP A 168 11430 10246 8475 -260 790 -894 O ATOM 902 OD2 ASP A 168 51.214 -2.332 25.754 1.00 80.27 O ANISOU 902 OD2 ASP A 168 11636 10270 8591 -214 621 -911 O ATOM 903 N PHE A 169 51.741 -7.197 23.395 1.00 70.16 N ANISOU 903 N PHE A 169 10144 9074 7440 -356 284 -576 N ATOM 904 CA PHE A 169 52.128 -7.865 22.140 1.00 69.26 C ANISOU 904 CA PHE A 169 9985 8934 7398 -347 158 -516 C ATOM 905 C PHE A 169 52.414 -9.372 22.316 1.00 73.57 C ANISOU 905 C PHE A 169 10541 9510 7903 -423 115 -434 C ATOM 906 O PHE A 169 52.265 -10.132 21.354 1.00 72.76 O ANISOU 906 O PHE A 169 10373 9394 7879 -421 45 -386 O ATOM 907 CB PHE A 169 53.396 -7.193 21.559 1.00 70.38 C ANISOU 907 CB PHE A 169 10203 9021 7518 -327 68 -532 C ATOM 908 CG PHE A 169 53.922 -7.763 20.258 1.00 71.23 C ANISOU 908 CG PHE A 169 10287 9090 7687 -317 -47 -479 C ATOM 909 CD1 PHE A 169 53.430 -7.319 19.036 1.00 74.36 C ANISOU 909 CD1 PHE A 169 10640 9433 8180 -242 -79 -483 C ATOM 910 CD2 PHE A 169 54.941 -8.713 20.254 1.00 73.06 C ANISOU 910 CD2 PHE A 169 10554 9332 7872 -374 -126 -430 C ATOM 911 CE1 PHE A 169 53.921 -7.843 17.832 1.00 74.46 C ANISOU 911 CE1 PHE A 169 10654 9403 8233 -234 -176 -437 C ATOM 912 CE2 PHE A 169 55.418 -9.249 19.051 1.00 75.11 C ANISOU 912 CE2 PHE A 169 10796 9552 8189 -365 -216 -387 C ATOM 913 CZ PHE A 169 54.916 -8.799 17.847 1.00 72.76 C ANISOU 913 CZ PHE A 169 10466 9201 7978 -300 -236 -391 C ATOM 914 N ARG A 170 52.901 -9.800 23.490 1.00 70.96 N ANISOU 914 N ARG A 170 10312 9209 7441 -484 145 -419 N ATOM 915 CA ARG A 170 53.276 -11.209 23.669 1.00 70.63 C ANISOU 915 CA ARG A 170 10311 9178 7346 -543 96 -337 C ATOM 916 C ARG A 170 52.141 -12.004 24.387 1.00 76.02 C ANISOU 916 C ARG A 170 10979 9887 8016 -601 226 -309 C ATOM 917 O ARG A 170 52.418 -12.890 25.205 1.00 76.48 O ANISOU 917 O ARG A 170 11147 9953 7961 -658 243 -257 O ATOM 918 CB ARG A 170 54.601 -11.328 24.448 1.00 69.99 C ANISOU 918 CB ARG A 170 10367 9105 7122 -564 21 -331 C ATOM 919 CG ARG A 170 55.793 -10.590 23.806 1.00 75.01 C ANISOU 919 CG ARG A 170 11005 9714 7781 -528 -90 -374 C ATOM 920 CD ARG A 170 57.087 -10.923 24.521 1.00 81.94 C ANISOU 920 CD ARG A 170 11984 10607 8541 -547 -186 -376 C ATOM 921 NE ARG A 170 57.484 -12.313 24.282 1.00 90.17 N ANISOU 921 NE ARG A 170 13039 11647 9573 -562 -271 -292 N ATOM 922 CZ ARG A 170 58.385 -12.974 24.999 1.00103.88 C ANISOU 922 CZ ARG A 170 14871 13399 11200 -568 -360 -272 C ATOM 923 NH1 ARG A 170 58.924 -12.418 26.077 1.00 90.55 N ANISOU 923 NH1 ARG A 170 13276 11738 9393 -566 -377 -331 N ATOM 924 NH2 ARG A 170 58.685 -14.231 24.701 1.00 92.33 N ANISOU 924 NH2 ARG A 170 13422 11921 9739 -571 -434 -195 N ATOM 925 N THR A 171 50.872 -11.718 24.017 1.00 72.98 N ANISOU 925 N THR A 171 10461 9511 7757 -584 316 -347 N ATOM 926 CA THR A 171 49.680 -12.383 24.558 1.00 74.08 C ANISOU 926 CA THR A 171 10547 9673 7927 -647 462 -344 C ATOM 927 C THR A 171 49.285 -13.564 23.656 1.00 78.29 C ANISOU 927 C THR A 171 10985 10194 8568 -684 411 -290 C ATOM 928 O THR A 171 49.609 -13.535 22.460 1.00 77.36 O ANISOU 928 O THR A 171 10805 10055 8533 -633 275 -280 O ATOM 929 CB THR A 171 48.514 -11.381 24.696 1.00 85.46 C ANISOU 929 CB THR A 171 11870 11135 9465 -604 588 -439 C ATOM 930 OG1 THR A 171 48.072 -10.956 23.408 1.00 86.60 O ANISOU 930 OG1 THR A 171 11863 11269 9773 -524 502 -471 O ATOM 931 CG2 THR A 171 48.865 -10.182 25.562 1.00 86.40 C ANISOU 931 CG2 THR A 171 12089 11257 9481 -568 646 -500 C ATOM 932 N PRO A 172 48.552 -14.593 24.170 1.00 75.75 N ANISOU 932 N PRO A 172 10657 9876 8249 -777 526 -262 N ATOM 933 CA PRO A 172 48.144 -15.710 23.292 1.00 75.10 C ANISOU 933 CA PRO A 172 10481 9776 8278 -821 480 -223 C ATOM 934 C PRO A 172 47.306 -15.226 22.100 1.00 78.32 C ANISOU 934 C PRO A 172 10681 10198 8880 -757 426 -290 C ATOM 935 O PRO A 172 47.490 -15.730 20.999 1.00 77.30 O ANISOU 935 O PRO A 172 10502 10046 8822 -740 295 -262 O ATOM 936 CB PRO A 172 47.321 -16.615 24.216 1.00 78.50 C ANISOU 936 CB PRO A 172 10936 10204 8685 -940 664 -209 C ATOM 937 CG PRO A 172 46.966 -15.775 25.394 1.00 84.21 C ANISOU 937 CG PRO A 172 11712 10954 9331 -941 824 -265 C ATOM 938 CD PRO A 172 48.090 -14.810 25.558 1.00 78.87 C ANISOU 938 CD PRO A 172 11148 10281 8538 -854 713 -266 C ATOM 939 N LEU A 173 46.441 -14.206 22.309 1.00 75.36 N ANISOU 939 N LEU A 173 10197 9854 8581 -707 515 -382 N ATOM 940 CA LEU A 173 45.612 -13.590 21.267 1.00 75.03 C ANISOU 940 CA LEU A 173 9967 9825 8715 -616 452 -458 C ATOM 941 C LEU A 173 46.475 -13.018 20.140 1.00 76.03 C ANISOU 941 C LEU A 173 10137 9915 8835 -511 261 -436 C ATOM 942 O LEU A 173 46.247 -13.358 18.981 1.00 75.21 O ANISOU 942 O LEU A 173 9950 9797 8831 -477 142 -434 O ATOM 943 CB LEU A 173 44.733 -12.469 21.871 1.00 76.59 C ANISOU 943 CB LEU A 173 10078 10056 8967 -562 583 -560 C ATOM 944 CG LEU A 173 43.826 -11.682 20.896 1.00 82.08 C ANISOU 944 CG LEU A 173 10583 10762 9841 -438 512 -651 C ATOM 945 CD1 LEU A 173 42.676 -12.547 20.372 1.00 83.56 C ANISOU 945 CD1 LEU A 173 10563 10979 10207 -482 519 -696 C ATOM 946 CD2 LEU A 173 43.248 -10.460 21.566 1.00 85.49 C ANISOU 946 CD2 LEU A 173 10974 11213 10295 -366 631 -744 C ATOM 947 N LYS A 174 47.463 -12.157 20.490 1.00 71.24 N ANISOU 947 N LYS A 174 9670 9290 8109 -467 240 -426 N ATOM 948 CA LYS A 174 48.363 -11.477 19.553 1.00 69.87 C ANISOU 948 CA LYS A 174 9559 9070 7917 -381 98 -414 C ATOM 949 C LYS A 174 49.134 -12.487 18.695 1.00 72.88 C ANISOU 949 C LYS A 174 9983 9420 8287 -413 -30 -337 C ATOM 950 O LYS A 174 49.212 -12.306 17.478 1.00 72.02 O ANISOU 950 O LYS A 174 9848 9275 8240 -346 -144 -337 O ATOM 951 CB LYS A 174 49.348 -10.579 20.312 1.00 72.46 C ANISOU 951 CB LYS A 174 10031 9386 8116 -370 126 -423 C ATOM 952 CG LYS A 174 49.910 -9.389 19.514 1.00 89.62 C ANISOU 952 CG LYS A 174 12248 11505 10298 -272 45 -454 C ATOM 953 CD LYS A 174 48.931 -8.207 19.453 1.00 99.15 C ANISOU 953 CD LYS A 174 13385 12706 11583 -174 101 -537 C ATOM 954 CE LYS A 174 49.546 -6.981 18.828 1.00105.55 C ANISOU 954 CE LYS A 174 14284 13444 12377 -86 46 -563 C ATOM 955 NZ LYS A 174 48.594 -5.841 18.824 1.00114.42 N ANISOU 955 NZ LYS A 174 15355 14550 13569 23 99 -642 N ATOM 956 N ALA A 175 49.665 -13.569 19.319 1.00 68.89 N ANISOU 956 N ALA A 175 9554 8923 7699 -508 -9 -272 N ATOM 957 CA ALA A 175 50.378 -14.641 18.607 1.00 67.23 C ANISOU 957 CA ALA A 175 9385 8680 7479 -540 -118 -200 C ATOM 958 C ALA A 175 49.482 -15.277 17.537 1.00 69.91 C ANISOU 958 C ALA A 175 9598 9011 7953 -538 -171 -206 C ATOM 959 O ALA A 175 49.914 -15.426 16.388 1.00 69.03 O ANISOU 959 O ALA A 175 9496 8861 7871 -496 -293 -187 O ATOM 960 CB ALA A 175 50.850 -15.699 19.588 1.00 68.07 C ANISOU 960 CB ALA A 175 9593 8791 7478 -632 -72 -136 C ATOM 961 N LYS A 176 48.214 -15.598 17.917 1.00 65.55 N ANISOU 961 N LYS A 176 8925 8495 7485 -583 -73 -246 N ATOM 962 CA LYS A 176 47.186 -16.182 17.055 1.00 64.81 C ANISOU 962 CA LYS A 176 8680 8405 7538 -591 -113 -278 C ATOM 963 C LYS A 176 46.876 -15.249 15.875 1.00 67.30 C ANISOU 963 C LYS A 176 8922 8710 7941 -461 -234 -334 C ATOM 964 O LYS A 176 46.878 -15.710 14.731 1.00 66.30 O ANISOU 964 O LYS A 176 8773 8553 7865 -436 -361 -323 O ATOM 965 CB LYS A 176 45.903 -16.478 17.856 1.00 68.14 C ANISOU 965 CB LYS A 176 8973 8873 8045 -667 44 -335 C ATOM 966 CG LYS A 176 46.054 -17.579 18.907 1.00 75.88 C ANISOU 966 CG LYS A 176 10046 9846 8941 -806 173 -274 C ATOM 967 CD LYS A 176 44.770 -17.791 19.707 1.00 85.46 C ANISOU 967 CD LYS A 176 11138 11095 10239 -892 363 -340 C ATOM 968 CE LYS A 176 44.893 -18.888 20.738 1.00 94.59 C ANISOU 968 CE LYS A 176 12421 12223 11295 -1032 506 -274 C ATOM 969 NZ LYS A 176 43.622 -19.094 21.485 1.00103.37 N ANISOU 969 NZ LYS A 176 13419 13361 12497 -1131 720 -346 N ATOM 970 N ILE A 177 46.667 -13.938 16.149 1.00 63.31 N ANISOU 970 N ILE A 177 8404 8216 7435 -372 -199 -391 N ATOM 971 CA ILE A 177 46.388 -12.912 15.130 1.00 62.90 C ANISOU 971 CA ILE A 177 8318 8136 7443 -230 -306 -441 C ATOM 972 C ILE A 177 47.564 -12.839 14.131 1.00 66.21 C ANISOU 972 C ILE A 177 8886 8487 7785 -188 -435 -380 C ATOM 973 O ILE A 177 47.333 -12.838 12.919 1.00 65.08 O ANISOU 973 O ILE A 177 8726 8309 7694 -115 -562 -390 O ATOM 974 CB ILE A 177 46.110 -11.528 15.784 1.00 66.14 C ANISOU 974 CB ILE A 177 8727 8557 7845 -151 -222 -504 C ATOM 975 CG1 ILE A 177 44.785 -11.575 16.585 1.00 68.26 C ANISOU 975 CG1 ILE A 177 8822 8893 8221 -178 -92 -584 C ATOM 976 CG2 ILE A 177 46.065 -10.408 14.724 1.00 66.17 C ANISOU 976 CG2 ILE A 177 8759 8506 7876 6 -338 -538 C ATOM 977 CD1 ILE A 177 44.423 -10.308 17.380 1.00 77.03 C ANISOU 977 CD1 ILE A 177 9924 10018 9328 -109 19 -654 C ATOM 978 N ILE A 178 48.812 -12.819 14.644 1.00 62.99 N ANISOU 978 N ILE A 178 8621 8058 7254 -236 -403 -325 N ATOM 979 CA ILE A 178 50.031 -12.766 13.833 1.00 62.03 C ANISOU 979 CA ILE A 178 8632 7873 7065 -215 -492 -278 C ATOM 980 C ILE A 178 50.051 -13.983 12.868 1.00 67.92 C ANISOU 980 C ILE A 178 9361 8597 7847 -246 -591 -236 C ATOM 981 O ILE A 178 50.286 -13.785 11.680 1.00 67.66 O ANISOU 981 O ILE A 178 9379 8507 7821 -180 -690 -232 O ATOM 982 CB ILE A 178 51.283 -12.701 14.743 1.00 64.07 C ANISOU 982 CB ILE A 178 9004 8132 7208 -276 -435 -245 C ATOM 983 CG1 ILE A 178 51.338 -11.306 15.431 1.00 64.45 C ANISOU 983 CG1 ILE A 178 9088 8181 7219 -229 -359 -300 C ATOM 984 CG2 ILE A 178 52.560 -12.944 13.939 1.00 63.35 C ANISOU 984 CG2 ILE A 178 9017 7981 7070 -278 -515 -203 C ATOM 985 CD1 ILE A 178 52.391 -11.095 16.506 1.00 68.03 C ANISOU 985 CD1 ILE A 178 9635 8648 7564 -286 -303 -295 C ATOM 986 N ASN A 179 49.710 -15.197 13.349 1.00 66.12 N ANISOU 986 N ASN A 179 9075 8406 7643 -344 -556 -209 N ATOM 987 CA ASN A 179 49.643 -16.387 12.492 1.00 66.41 C ANISOU 987 CA ASN A 179 9096 8419 7720 -382 -641 -177 C ATOM 988 C ASN A 179 48.455 -16.306 11.520 1.00 71.72 C ANISOU 988 C ASN A 179 9647 9094 8510 -321 -725 -238 C ATOM 989 O ASN A 179 48.574 -16.813 10.407 1.00 70.85 O ANISOU 989 O ASN A 179 9564 8941 8416 -301 -838 -225 O ATOM 990 CB ASN A 179 49.555 -17.671 13.311 1.00 70.10 C ANISOU 990 CB ASN A 179 9547 8908 8178 -506 -570 -136 C ATOM 991 CG ASN A 179 50.853 -18.025 13.998 1.00102.26 C ANISOU 991 CG ASN A 179 13759 12965 12131 -550 -542 -68 C ATOM 992 OD1 ASN A 179 50.979 -17.960 15.234 1.00 97.62 O ANISOU 992 OD1 ASN A 179 13205 12408 11477 -593 -445 -57 O ATOM 993 ND2 ASN A 179 51.858 -18.404 13.205 1.00 94.08 N ANISOU 993 ND2 ASN A 179 12808 11878 11061 -533 -632 -28 N ATOM 994 N ILE A 180 47.336 -15.645 11.910 1.00 70.30 N ANISOU 994 N ILE A 180 9338 8962 8412 -280 -679 -313 N ATOM 995 CA ILE A 180 46.187 -15.452 11.006 1.00 71.63 C ANISOU 995 CA ILE A 180 9375 9139 8703 -198 -781 -389 C ATOM 996 C ILE A 180 46.633 -14.556 9.829 1.00 76.80 C ANISOU 996 C ILE A 180 10147 9725 9310 -57 -913 -387 C ATOM 997 O ILE A 180 46.197 -14.773 8.700 1.00 77.03 O ANISOU 997 O ILE A 180 10155 9728 9386 5 -1052 -412 O ATOM 998 CB ILE A 180 44.933 -14.871 11.725 1.00 75.99 C ANISOU 998 CB ILE A 180 9749 9758 9364 -172 -698 -482 C ATOM 999 CG1 ILE A 180 44.440 -15.805 12.846 1.00 77.31 C ANISOU 999 CG1 ILE A 180 9818 9981 9576 -324 -544 -487 C ATOM 1000 CG2 ILE A 180 43.796 -14.609 10.712 1.00 77.38 C ANISOU 1000 CG2 ILE A 180 9782 9945 9675 -60 -837 -574 C ATOM 1001 CD1 ILE A 180 43.289 -15.215 13.757 1.00 89.18 C ANISOU 1001 CD1 ILE A 180 11153 11551 11182 -318 -410 -583 C ATOM 1002 N CYS A 181 47.526 -13.575 10.102 1.00 73.22 N ANISOU 1002 N CYS A 181 9830 9234 8756 -14 -865 -359 N ATOM 1003 CA CYS A 181 48.087 -12.675 9.091 1.00 72.94 C ANISOU 1003 CA CYS A 181 9943 9113 8657 100 -949 -350 C ATOM 1004 C CYS A 181 49.063 -13.447 8.192 1.00 76.46 C ANISOU 1004 C CYS A 181 10517 9498 9037 61 -1017 -286 C ATOM 1005 O CYS A 181 49.051 -13.245 6.976 1.00 76.17 O ANISOU 1005 O CYS A 181 10563 9394 8983 147 -1129 -288 O ATOM 1006 CB CYS A 181 48.769 -11.474 9.744 1.00 72.89 C ANISOU 1006 CB CYS A 181 10038 9081 8575 129 -852 -348 C ATOM 1007 SG CYS A 181 47.656 -10.409 10.703 1.00 77.96 S ANISOU 1007 SG CYS A 181 10558 9778 9286 197 -768 -431 S ATOM 1008 N ILE A 182 49.889 -14.349 8.797 1.00 72.88 N ANISOU 1008 N ILE A 182 10086 9062 8543 -62 -950 -231 N ATOM 1009 CA ILE A 182 50.877 -15.206 8.111 1.00 72.25 C ANISOU 1009 CA ILE A 182 10110 8930 8411 -109 -994 -174 C ATOM 1010 C ILE A 182 50.120 -16.224 7.202 1.00 79.19 C ANISOU 1010 C ILE A 182 10928 9805 9354 -114 -1105 -184 C ATOM 1011 O ILE A 182 50.609 -16.575 6.127 1.00 78.31 O ANISOU 1011 O ILE A 182 10920 9629 9207 -93 -1184 -162 O ATOM 1012 CB ILE A 182 51.810 -15.908 9.145 1.00 74.02 C ANISOU 1012 CB ILE A 182 10353 9182 8587 -221 -905 -124 C ATOM 1013 CG1 ILE A 182 52.648 -14.858 9.913 1.00 73.33 C ANISOU 1013 CG1 ILE A 182 10334 9094 8433 -212 -820 -129 C ATOM 1014 CG2 ILE A 182 52.739 -16.920 8.455 1.00 74.26 C ANISOU 1014 CG2 ILE A 182 10469 9163 8585 -264 -952 -74 C ATOM 1015 CD1 ILE A 182 53.441 -15.374 11.105 1.00 77.92 C ANISOU 1015 CD1 ILE A 182 10927 9714 8963 -301 -748 -97 C ATOM 1016 N TRP A 183 48.924 -16.650 7.632 1.00 78.66 N ANISOU 1016 N TRP A 183 10696 9806 9387 -145 -1104 -228 N ATOM 1017 CA TRP A 183 48.015 -17.518 6.886 1.00 80.20 C ANISOU 1017 CA TRP A 183 10795 10008 9669 -155 -1207 -264 C ATOM 1018 C TRP A 183 47.546 -16.789 5.613 1.00 83.30 C ANISOU 1018 C TRP A 183 11225 10356 10068 -10 -1357 -312 C ATOM 1019 O TRP A 183 47.637 -17.352 4.521 1.00 83.12 O ANISOU 1019 O TRP A 183 11270 10284 10028 7 -1472 -307 O ATOM 1020 CB TRP A 183 46.831 -17.918 7.799 1.00 81.03 C ANISOU 1020 CB TRP A 183 10697 10198 9893 -226 -1138 -319 C ATOM 1021 CG TRP A 183 45.653 -18.566 7.122 1.00 84.11 C ANISOU 1021 CG TRP A 183 10938 10609 10409 -231 -1242 -394 C ATOM 1022 CD1 TRP A 183 45.565 -19.856 6.692 1.00 87.37 C ANISOU 1022 CD1 TRP A 183 11334 11006 10857 -324 -1286 -387 C ATOM 1023 CD2 TRP A 183 44.330 -18.013 6.996 1.00 85.84 C ANISOU 1023 CD2 TRP A 183 10978 10882 10757 -154 -1297 -502 C ATOM 1024 NE1 TRP A 183 44.307 -20.105 6.191 1.00 88.56 N ANISOU 1024 NE1 TRP A 183 11313 11193 11145 -310 -1380 -488 N ATOM 1025 CE2 TRP A 183 43.521 -18.997 6.387 1.00 90.97 C ANISOU 1025 CE2 TRP A 183 11504 11546 11516 -204 -1391 -563 C ATOM 1026 CE3 TRP A 183 43.759 -16.763 7.301 1.00 87.96 C ANISOU 1026 CE3 TRP A 183 11177 11183 11063 -40 -1284 -562 C ATOM 1027 CZ2 TRP A 183 42.170 -18.773 6.080 1.00 92.17 C ANISOU 1027 CZ2 TRP A 183 11446 11752 11822 -143 -1481 -689 C ATOM 1028 CZ3 TRP A 183 42.420 -16.547 7.004 1.00 91.27 C ANISOU 1028 CZ3 TRP A 183 11395 11652 11632 31 -1370 -680 C ATOM 1029 CH2 TRP A 183 41.644 -17.540 6.393 1.00 92.94 C ANISOU 1029 CH2 TRP A 183 11469 11885 11958 -19 -1472 -746 C ATOM 1030 N LEU A 184 47.120 -15.515 5.757 1.00 78.95 N ANISOU 1030 N LEU A 184 10659 9812 9526 102 -1356 -354 N ATOM 1031 CA LEU A 184 46.637 -14.663 4.669 1.00 79.24 C ANISOU 1031 CA LEU A 184 10753 9798 9556 265 -1498 -398 C ATOM 1032 C LEU A 184 47.732 -14.356 3.636 1.00 82.28 C ANISOU 1032 C LEU A 184 11389 10071 9804 317 -1542 -339 C ATOM 1033 O LEU A 184 47.489 -14.517 2.434 1.00 82.70 O ANISOU 1033 O LEU A 184 11519 10070 9834 394 -1687 -353 O ATOM 1034 CB LEU A 184 46.091 -13.341 5.228 1.00 79.88 C ANISOU 1034 CB LEU A 184 10784 9900 9666 369 -1457 -447 C ATOM 1035 CG LEU A 184 44.808 -13.403 6.046 1.00 85.46 C ANISOU 1035 CG LEU A 184 11238 10709 10522 358 -1424 -533 C ATOM 1036 CD1 LEU A 184 44.600 -12.125 6.809 1.00 85.93 C ANISOU 1036 CD1 LEU A 184 11283 10780 10586 437 -1334 -564 C ATOM 1037 CD2 LEU A 184 43.602 -13.724 5.175 1.00 89.17 C ANISOU 1037 CD2 LEU A 184 11570 11204 11109 438 -1600 -622 C ATOM 1038 N LEU A 185 48.922 -13.895 4.098 1.00 77.27 N ANISOU 1038 N LEU A 185 10882 9397 9078 276 -1415 -282 N ATOM 1039 CA LEU A 185 50.045 -13.545 3.219 1.00 76.62 C ANISOU 1039 CA LEU A 185 11031 9203 8876 306 -1415 -234 C ATOM 1040 C LEU A 185 50.528 -14.753 2.400 1.00 81.24 C ANISOU 1040 C LEU A 185 11679 9754 9434 243 -1471 -201 C ATOM 1041 O LEU A 185 50.913 -14.592 1.236 1.00 81.35 O ANISOU 1041 O LEU A 185 11871 9672 9367 305 -1533 -187 O ATOM 1042 CB LEU A 185 51.229 -12.973 4.019 1.00 75.55 C ANISOU 1042 CB LEU A 185 10972 9052 8683 244 -1258 -199 C ATOM 1043 CG LEU A 185 51.021 -11.648 4.753 1.00 80.77 C ANISOU 1043 CG LEU A 185 11625 9719 9343 302 -1184 -230 C ATOM 1044 CD1 LEU A 185 52.245 -11.298 5.567 1.00 80.35 C ANISOU 1044 CD1 LEU A 185 11632 9659 9240 216 -1041 -206 C ATOM 1045 CD2 LEU A 185 50.693 -10.503 3.790 1.00 83.54 C ANISOU 1045 CD2 LEU A 185 12125 9971 9646 457 -1254 -251 C ATOM 1046 N SER A 186 50.516 -15.952 3.010 1.00 77.27 N ANISOU 1046 N SER A 186 11050 9320 8990 122 -1441 -186 N ATOM 1047 CA SER A 186 50.944 -17.179 2.354 1.00 76.44 C ANISOU 1047 CA SER A 186 10993 9182 8869 56 -1484 -158 C ATOM 1048 C SER A 186 49.861 -17.676 1.392 1.00 81.09 C ANISOU 1048 C SER A 186 11540 9768 9504 108 -1647 -207 C ATOM 1049 O SER A 186 50.185 -18.039 0.254 1.00 80.80 O ANISOU 1049 O SER A 186 11642 9655 9404 136 -1728 -198 O ATOM 1050 CB SER A 186 51.281 -18.250 3.385 1.00 78.93 C ANISOU 1050 CB SER A 186 11208 9557 9225 -82 -1395 -124 C ATOM 1051 OG SER A 186 52.334 -17.835 4.241 1.00 84.32 O ANISOU 1051 OG SER A 186 11935 10244 9860 -121 -1270 -87 O ATOM 1052 N SER A 187 48.569 -17.645 1.823 1.00 78.13 N ANISOU 1052 N SER A 187 10972 9474 9240 124 -1697 -271 N ATOM 1053 CA SER A 187 47.435 -18.089 0.994 1.00 78.97 C ANISOU 1053 CA SER A 187 10995 9593 9417 172 -1867 -343 C ATOM 1054 C SER A 187 47.379 -17.308 -0.328 1.00 82.92 C ANISOU 1054 C SER A 187 11673 10006 9827 334 -2013 -361 C ATOM 1055 O SER A 187 46.904 -17.852 -1.323 1.00 82.81 O ANISOU 1055 O SER A 187 11683 9967 9815 370 -2168 -400 O ATOM 1056 CB SER A 187 46.108 -17.959 1.738 1.00 83.46 C ANISOU 1056 CB SER A 187 11313 10264 10134 174 -1877 -426 C ATOM 1057 OG SER A 187 45.892 -16.684 2.319 1.00 92.54 O ANISOU 1057 OG SER A 187 12438 11436 11288 263 -1823 -442 O ATOM 1058 N SER A 188 47.922 -16.072 -0.355 1.00 79.60 N ANISOU 1058 N SER A 188 11400 9527 9315 425 -1960 -330 N ATOM 1059 CA SER A 188 47.999 -15.282 -1.585 1.00 80.26 C ANISOU 1059 CA SER A 188 11707 9504 9286 577 -2072 -331 C ATOM 1060 C SER A 188 48.887 -16.007 -2.613 1.00 83.80 C ANISOU 1060 C SER A 188 12359 9859 9624 538 -2089 -285 C ATOM 1061 O SER A 188 48.486 -16.161 -3.770 1.00 84.78 O ANISOU 1061 O SER A 188 12593 9925 9693 625 -2250 -313 O ATOM 1062 CB SER A 188 48.521 -13.875 -1.302 1.00 83.06 C ANISOU 1062 CB SER A 188 12195 9801 9565 653 -1970 -302 C ATOM 1063 N VAL A 189 50.050 -16.527 -2.161 1.00 78.12 N ANISOU 1063 N VAL A 189 11675 9129 8878 407 -1932 -224 N ATOM 1064 CA VAL A 189 50.992 -17.272 -3.004 1.00 77.05 C ANISOU 1064 CA VAL A 189 11711 8909 8655 357 -1915 -184 C ATOM 1065 C VAL A 189 50.412 -18.673 -3.284 1.00 80.68 C ANISOU 1065 C VAL A 189 12061 9412 9184 290 -2021 -214 C ATOM 1066 O VAL A 189 50.612 -19.219 -4.373 1.00 80.56 O ANISOU 1066 O VAL A 189 12192 9322 9096 306 -2099 -216 O ATOM 1067 CB VAL A 189 52.396 -17.351 -2.356 1.00 79.51 C ANISOU 1067 CB VAL A 189 12064 9205 8940 250 -1720 -126 C ATOM 1068 CG1 VAL A 189 53.411 -17.987 -3.313 1.00 79.02 C ANISOU 1068 CG1 VAL A 189 12187 9045 8791 215 -1690 -96 C ATOM 1069 CG2 VAL A 189 52.871 -15.965 -1.928 1.00 79.16 C ANISOU 1069 CG2 VAL A 189 12092 9131 8853 296 -1611 -113 C ATOM 1070 N GLY A 190 49.682 -19.214 -2.301 1.00 76.63 N ANISOU 1070 N GLY A 190 11303 9009 8805 213 -2013 -242 N ATOM 1071 CA GLY A 190 49.020 -20.514 -2.386 1.00 76.34 C ANISOU 1071 CA GLY A 190 11134 9016 8858 130 -2093 -281 C ATOM 1072 C GLY A 190 47.971 -20.582 -3.480 1.00 79.71 C ANISOU 1072 C GLY A 190 11564 9428 9295 225 -2307 -361 C ATOM 1073 O GLY A 190 47.973 -21.522 -4.273 1.00 78.99 O ANISOU 1073 O GLY A 190 11534 9297 9184 192 -2392 -378 O ATOM 1074 N ILE A 191 47.081 -19.567 -3.541 1.00 76.90 N ANISOU 1074 N ILE A 191 11149 9101 8967 355 -2404 -417 N ATOM 1075 CA ILE A 191 46.032 -19.443 -4.563 1.00 78.47 C ANISOU 1075 CA ILE A 191 11349 9292 9176 482 -2639 -506 C ATOM 1076 C ILE A 191 46.697 -19.189 -5.928 1.00 82.24 C ANISOU 1076 C ILE A 191 12149 9635 9465 582 -2721 -471 C ATOM 1077 O ILE A 191 46.232 -19.717 -6.940 1.00 83.12 O ANISOU 1077 O ILE A 191 12320 9713 9547 626 -2900 -525 O ATOM 1078 CB ILE A 191 45.014 -18.323 -4.191 1.00 82.87 C ANISOU 1078 CB ILE A 191 11767 9909 9810 615 -2710 -572 C ATOM 1079 CG1 ILE A 191 44.294 -18.642 -2.856 1.00 83.51 C ANISOU 1079 CG1 ILE A 191 11528 10121 10083 505 -2612 -619 C ATOM 1080 CG2 ILE A 191 43.986 -18.104 -5.315 1.00 85.81 C ANISOU 1080 CG2 ILE A 191 12158 10265 10181 778 -2981 -669 C ATOM 1081 CD1 ILE A 191 43.386 -17.485 -2.278 1.00 93.13 C ANISOU 1081 CD1 ILE A 191 12590 11404 11391 625 -2632 -683 C ATOM 1082 N SER A 192 47.808 -18.414 -5.937 1.00 77.09 N ANISOU 1082 N SER A 192 11708 8899 8684 607 -2578 -387 N ATOM 1083 CA SER A 192 48.592 -18.105 -7.139 1.00 76.52 C ANISOU 1083 CA SER A 192 11966 8684 8424 682 -2595 -345 C ATOM 1084 C SER A 192 49.224 -19.373 -7.723 1.00 79.32 C ANISOU 1084 C SER A 192 12407 8994 8737 574 -2578 -327 C ATOM 1085 O SER A 192 49.317 -19.509 -8.942 1.00 79.09 O ANISOU 1085 O SER A 192 12601 8868 8582 643 -2683 -337 O ATOM 1086 CB SER A 192 49.675 -17.080 -6.821 1.00 78.44 C ANISOU 1086 CB SER A 192 12369 8858 8577 690 -2402 -270 C ATOM 1087 N ALA A 193 49.633 -20.307 -6.850 1.00 75.10 N ANISOU 1087 N ALA A 193 11709 8524 8303 414 -2450 -303 N ATOM 1088 CA ALA A 193 50.235 -21.568 -7.265 1.00 74.82 C ANISOU 1088 CA ALA A 193 11735 8448 8247 309 -2422 -287 C ATOM 1089 C ALA A 193 49.177 -22.543 -7.786 1.00 80.51 C ANISOU 1089 C ALA A 193 12357 9201 9034 295 -2613 -368 C ATOM 1090 O ALA A 193 49.491 -23.358 -8.654 1.00 80.58 O ANISOU 1090 O ALA A 193 12505 9138 8975 269 -2659 -375 O ATOM 1091 CB ALA A 193 50.995 -22.191 -6.114 1.00 74.09 C ANISOU 1091 CB ALA A 193 11510 8405 8235 162 -2234 -234 C ATOM 1092 N ILE A 194 47.927 -22.459 -7.268 1.00 77.72 N ANISOU 1092 N ILE A 194 11760 8951 8818 309 -2719 -441 N ATOM 1093 CA ILE A 194 46.815 -23.321 -7.703 1.00 78.55 C ANISOU 1093 CA ILE A 194 11732 9098 9017 288 -2906 -542 C ATOM 1094 C ILE A 194 46.332 -22.867 -9.089 1.00 82.13 C ANISOU 1094 C ILE A 194 12369 9483 9353 454 -3137 -602 C ATOM 1095 O ILE A 194 46.028 -23.707 -9.934 1.00 82.12 O ANISOU 1095 O ILE A 194 12419 9450 9332 439 -3278 -660 O ATOM 1096 CB ILE A 194 45.642 -23.332 -6.669 1.00 82.33 C ANISOU 1096 CB ILE A 194 11873 9711 9697 243 -2924 -616 C ATOM 1097 CG1 ILE A 194 46.100 -23.927 -5.323 1.00 81.51 C ANISOU 1097 CG1 ILE A 194 11621 9661 9687 72 -2699 -555 C ATOM 1098 CG2 ILE A 194 44.428 -24.118 -7.205 1.00 85.00 C ANISOU 1098 CG2 ILE A 194 12057 10091 10147 227 -3130 -746 C ATOM 1099 CD1 ILE A 194 45.060 -23.857 -4.162 1.00 91.37 C ANISOU 1099 CD1 ILE A 194 12561 11033 11122 14 -2658 -616 C ATOM 1100 N VAL A 195 46.276 -21.554 -9.325 1.00 78.58 N ANISOU 1100 N VAL A 195 12038 9002 8817 615 -3178 -587 N ATOM 1101 CA VAL A 195 45.760 -21.035 -10.584 1.00 80.32 C ANISOU 1101 CA VAL A 195 12453 9152 8913 795 -3410 -640 C ATOM 1102 C VAL A 195 46.860 -21.079 -11.685 1.00 83.49 C ANISOU 1102 C VAL A 195 13238 9398 9088 823 -3365 -571 C ATOM 1103 O VAL A 195 46.542 -21.455 -12.816 1.00 84.39 O ANISOU 1103 O VAL A 195 13508 9450 9105 890 -3552 -623 O ATOM 1104 CB VAL A 195 45.168 -19.596 -10.446 1.00 85.40 C ANISOU 1104 CB VAL A 195 13091 9808 9547 977 -3488 -657 C ATOM 1105 CG1 VAL A 195 43.959 -19.586 -9.511 1.00 85.92 C ANISOU 1105 CG1 VAL A 195 12777 10025 9843 964 -3552 -751 C ATOM 1106 CG2 VAL A 195 46.209 -18.572 -9.990 1.00 83.81 C ANISOU 1106 CG2 VAL A 195 13051 9543 9249 991 -3264 -546 C ATOM 1107 N LEU A 196 48.128 -20.723 -11.358 1.00 78.37 N ANISOU 1107 N LEU A 196 12731 8686 8360 767 -3120 -465 N ATOM 1108 CA LEU A 196 49.215 -20.631 -12.344 1.00 78.16 C ANISOU 1108 CA LEU A 196 13062 8507 8129 789 -3038 -405 C ATOM 1109 C LEU A 196 49.985 -21.942 -12.526 1.00 81.97 C ANISOU 1109 C LEU A 196 13572 8961 8612 639 -2938 -388 C ATOM 1110 O LEU A 196 50.571 -22.132 -13.591 1.00 82.32 O ANISOU 1110 O LEU A 196 13900 8883 8495 666 -2934 -374 O ATOM 1111 CB LEU A 196 50.219 -19.541 -11.956 1.00 77.11 C ANISOU 1111 CB LEU A 196 13064 8313 7923 802 -2816 -318 C ATOM 1112 CG LEU A 196 49.716 -18.097 -12.000 1.00 82.97 C ANISOU 1112 CG LEU A 196 13889 9027 8607 969 -2884 -319 C ATOM 1113 CD1 LEU A 196 50.640 -17.177 -11.246 1.00 82.01 C ANISOU 1113 CD1 LEU A 196 13800 8879 8479 931 -2640 -246 C ATOM 1114 CD2 LEU A 196 49.504 -17.619 -13.436 1.00 87.18 C ANISOU 1114 CD2 LEU A 196 14772 9420 8931 1137 -3046 -332 C ATOM 1115 N GLY A 197 50.005 -22.805 -11.510 1.00 77.85 N ANISOU 1115 N GLY A 197 12781 8539 8259 490 -2849 -387 N ATOM 1116 CA GLY A 197 50.708 -24.086 -11.571 1.00 77.14 C ANISOU 1116 CA GLY A 197 12702 8422 8186 353 -2754 -370 C ATOM 1117 C GLY A 197 50.230 -24.983 -12.696 1.00 83.08 C ANISOU 1117 C GLY A 197 13563 9122 8880 365 -2935 -440 C ATOM 1118 O GLY A 197 49.039 -25.007 -13.010 1.00 84.25 O ANISOU 1118 O GLY A 197 13623 9317 9070 427 -3158 -525 O ATOM 1119 N GLY A 198 51.162 -25.682 -13.330 1.00 80.03 N ANISOU 1119 N GLY A 198 13372 8636 8399 313 -2844 -413 N ATOM 1120 CA GLY A 198 50.842 -26.566 -14.439 1.00 81.97 C ANISOU 1120 CA GLY A 198 13757 8817 8571 318 -2997 -479 C ATOM 1121 C GLY A 198 52.025 -27.277 -15.052 1.00 87.76 C ANISOU 1121 C GLY A 198 14712 9433 9201 259 -2849 -442 C ATOM 1122 O GLY A 198 53.165 -27.121 -14.604 1.00 85.43 O ANISOU 1122 O GLY A 198 14447 9109 8902 210 -2620 -369 O ATOM 1123 N THR A 199 51.739 -28.036 -16.121 1.00 88.40 N ANISOU 1123 N THR A 199 14950 9444 9195 270 -2989 -506 N ATOM 1124 CA THR A 199 52.672 -28.888 -16.856 1.00 89.31 C ANISOU 1124 CA THR A 199 15280 9442 9212 217 -2884 -497 C ATOM 1125 C THR A 199 53.022 -28.260 -18.246 1.00 97.07 C ANISOU 1125 C THR A 199 16659 10280 9942 342 -2914 -500 C ATOM 1126 O THR A 199 52.138 -27.724 -18.928 1.00 98.30 O ANISOU 1126 O THR A 199 16923 10425 10000 463 -3135 -550 O ATOM 1127 CB THR A 199 52.019 -30.272 -17.001 1.00 96.07 C ANISOU 1127 CB THR A 199 16025 10319 10157 126 -3018 -577 C ATOM 1128 OG1 THR A 199 51.775 -30.808 -15.700 1.00 93.63 O ANISOU 1128 OG1 THR A 199 15388 10123 10064 7 -2954 -564 O ATOM 1129 CG2 THR A 199 52.850 -31.237 -17.776 1.00 94.59 C ANISOU 1129 CG2 THR A 199 16052 10011 9877 76 -2930 -582 C ATOM 1130 N LYS A 200 54.325 -28.346 -18.643 1.00 94.60 N ANISOU 1130 N LYS A 200 16562 9854 9528 313 -2686 -450 N ATOM 1131 CA LYS A 200 54.857 -27.832 -19.915 1.00 96.17 C ANISOU 1131 CA LYS A 200 17162 9896 9482 404 -2646 -445 C ATOM 1132 C LYS A 200 55.730 -28.901 -20.601 1.00101.38 C ANISOU 1132 C LYS A 200 17997 10447 10077 331 -2518 -461 C ATOM 1133 O LYS A 200 56.575 -29.519 -19.949 1.00 99.30 O ANISOU 1133 O LYS A 200 17590 10202 9939 224 -2323 -432 O ATOM 1134 CB LYS A 200 55.661 -26.542 -19.686 1.00 97.80 C ANISOU 1134 CB LYS A 200 17474 10059 9627 446 -2440 -369 C ATOM 1135 N VAL A 201 55.518 -29.109 -21.921 1.00101.05 N ANISOU 1135 N VAL A 201 18272 10288 9833 400 -2635 -512 N ATOM 1136 CA VAL A 201 56.215 -30.114 -22.736 1.00102.05 C ANISOU 1136 CA VAL A 201 18605 10298 9872 347 -2539 -544 C ATOM 1137 C VAL A 201 57.639 -29.637 -23.158 1.00106.88 C ANISOU 1137 C VAL A 201 19472 10776 10362 343 -2224 -491 C ATOM 1138 O VAL A 201 58.406 -30.439 -23.705 1.00107.57 O ANISOU 1138 O VAL A 201 19703 10768 10402 290 -2085 -514 O ATOM 1139 CB VAL A 201 55.383 -30.452 -23.992 1.00108.13 C ANISOU 1139 CB VAL A 201 19634 10994 10458 427 -2798 -627 C ATOM 1140 N ARG A 202 57.985 -28.355 -22.899 1.00102.47 N ANISOU 1140 N ARG A 202 18961 10208 9764 392 -2104 -431 N ATOM 1141 CA ARG A 202 59.288 -27.771 -23.236 1.00122.04 C ANISOU 1141 CA ARG A 202 21659 12564 12147 377 -1793 -391 C ATOM 1142 C ARG A 202 60.420 -28.402 -22.409 1.00141.17 C ANISOU 1142 C ARG A 202 23846 15027 14767 250 -1537 -377 C ATOM 1143 O ARG A 202 60.202 -28.857 -21.286 1.00 97.35 O ANISOU 1143 O ARG A 202 17943 9616 9429 189 -1584 -366 O ATOM 1144 CB ARG A 202 59.265 -26.253 -23.009 1.00121.94 C ANISOU 1144 CB ARG A 202 21713 12543 12077 449 -1742 -336 C ATOM 1145 N ASP A 206 61.324 -32.839 -24.623 1.00 89.12 N ANISOU 1145 N ASP A 206 17606 8177 8079 104 -1494 -572 N ATOM 1146 CA ASP A 206 60.641 -34.131 -24.531 1.00 89.10 C ANISOU 1146 CA ASP A 206 17475 8216 8163 58 -1683 -623 C ATOM 1147 C ASP A 206 60.572 -34.615 -23.052 1.00 91.92 C ANISOU 1147 C ASP A 206 17405 8722 8798 -22 -1686 -588 C ATOM 1148 O ASP A 206 60.181 -35.761 -22.789 1.00 92.00 O ANISOU 1148 O ASP A 206 17281 8760 8914 -81 -1786 -621 O ATOM 1149 CB ASP A 206 61.341 -35.178 -25.413 1.00 91.63 C ANISOU 1149 CB ASP A 206 18016 8397 8404 28 -1560 -680 C ATOM 1150 N VAL A 207 60.939 -33.725 -22.097 1.00 86.38 N ANISOU 1150 N VAL A 207 16510 8107 8202 -23 -1574 -522 N ATOM 1151 CA VAL A 207 60.884 -33.966 -20.651 1.00 83.97 C ANISOU 1151 CA VAL A 207 15830 7943 8132 -85 -1572 -480 C ATOM 1152 C VAL A 207 59.807 -33.054 -20.072 1.00 87.60 C ANISOU 1152 C VAL A 207 16142 8523 8620 -49 -1752 -453 C ATOM 1153 O VAL A 207 59.888 -31.831 -20.211 1.00 87.74 O ANISOU 1153 O VAL A 207 16255 8534 8550 13 -1712 -423 O ATOM 1154 CB VAL A 207 62.254 -33.768 -19.967 1.00 86.29 C ANISOU 1154 CB VAL A 207 16010 8241 8537 -116 -1296 -441 C ATOM 1155 N ILE A 208 58.767 -33.649 -19.487 1.00 83.35 N ANISOU 1155 N ILE A 208 15388 8083 8199 -88 -1948 -470 N ATOM 1156 CA ILE A 208 57.606 -32.934 -18.960 1.00 82.55 C ANISOU 1156 CA ILE A 208 15123 8099 8143 -57 -2136 -465 C ATOM 1157 C ILE A 208 58.007 -32.204 -17.651 1.00 84.63 C ANISOU 1157 C ILE A 208 15145 8468 8545 -77 -2004 -392 C ATOM 1158 O ILE A 208 58.621 -32.810 -16.770 1.00 83.11 O ANISOU 1158 O ILE A 208 14774 8311 8492 -151 -1879 -361 O ATOM 1159 CB ILE A 208 56.405 -33.909 -18.745 1.00 85.92 C ANISOU 1159 CB ILE A 208 15381 8591 8674 -114 -2358 -524 C ATOM 1160 CG1 ILE A 208 56.116 -34.826 -19.970 1.00 87.85 C ANISOU 1160 CG1 ILE A 208 15850 8728 8800 -115 -2479 -608 C ATOM 1161 CG2 ILE A 208 55.169 -33.172 -18.343 1.00 86.46 C ANISOU 1161 CG2 ILE A 208 15287 8775 8790 -73 -2556 -540 C ATOM 1162 CD1 ILE A 208 57.091 -36.056 -20.198 1.00 94.94 C ANISOU 1162 CD1 ILE A 208 16835 9524 9714 -187 -2315 -615 C ATOM 1163 N GLU A 209 57.674 -30.895 -17.548 1.00 81.03 N ANISOU 1163 N GLU A 209 14700 8050 8037 -3 -2039 -367 N ATOM 1164 CA GLU A 209 58.026 -30.053 -16.397 1.00 79.13 C ANISOU 1164 CA GLU A 209 14263 7900 7903 -14 -1920 -306 C ATOM 1165 C GLU A 209 56.787 -29.536 -15.652 1.00 81.30 C ANISOU 1165 C GLU A 209 14322 8304 8263 8 -2096 -307 C ATOM 1166 O GLU A 209 55.835 -29.081 -16.278 1.00 81.39 O ANISOU 1166 O GLU A 209 14424 8312 8190 88 -2283 -345 O ATOM 1167 CB GLU A 209 58.859 -28.851 -16.885 1.00 80.93 C ANISOU 1167 CB GLU A 209 14706 8045 8000 49 -1760 -278 C ATOM 1168 CG GLU A 209 59.316 -27.884 -15.798 1.00 95.54 C ANISOU 1168 CG GLU A 209 16385 9972 9946 37 -1626 -226 C ATOM 1169 CD GLU A 209 59.790 -26.522 -16.279 1.00128.24 C ANISOU 1169 CD GLU A 209 20738 14033 13956 102 -1510 -206 C ATOM 1170 OE1 GLU A 209 59.369 -26.095 -17.381 1.00129.14 O ANISOU 1170 OE1 GLU A 209 21125 14051 13891 186 -1597 -223 O ATOM 1171 OE2 GLU A 209 60.472 -25.826 -15.491 1.00124.77 O ANISOU 1171 OE2 GLU A 209 20186 13629 13591 74 -1351 -175 O ATOM 1172 N CYS A 210 56.847 -29.555 -14.307 1.00 76.79 N ANISOU 1172 N CYS A 210 13476 7843 7857 -55 -2029 -269 N ATOM 1173 CA CYS A 210 55.838 -28.996 -13.394 1.00 76.54 C ANISOU 1173 CA CYS A 210 13215 7939 7927 -46 -2138 -266 C ATOM 1174 C CYS A 210 56.382 -27.689 -12.817 1.00 79.47 C ANISOU 1174 C CYS A 210 13568 8336 8289 -5 -2006 -214 C ATOM 1175 O CYS A 210 57.450 -27.701 -12.205 1.00 77.29 O ANISOU 1175 O CYS A 210 13243 8062 8063 -55 -1820 -173 O ATOM 1176 CB CYS A 210 55.471 -30.000 -12.299 1.00 76.18 C ANISOU 1176 CB CYS A 210 12901 7988 8058 -154 -2147 -263 C ATOM 1177 SG CYS A 210 54.394 -29.343 -10.985 1.00 79.45 S ANISOU 1177 SG CYS A 210 13017 8559 8613 -164 -2215 -257 S ATOM 1178 N SER A 211 55.700 -26.551 -13.096 1.00 77.13 N ANISOU 1178 N SER A 211 13335 8049 7923 94 -2106 -223 N ATOM 1179 CA SER A 211 56.096 -25.198 -12.658 1.00 76.66 C ANISOU 1179 CA SER A 211 13290 7997 7839 142 -1995 -181 C ATOM 1180 C SER A 211 54.947 -24.210 -12.760 1.00 79.39 C ANISOU 1180 C SER A 211 13631 8380 8153 252 -2165 -202 C ATOM 1181 O SER A 211 53.907 -24.542 -13.330 1.00 80.29 O ANISOU 1181 O SER A 211 13755 8504 8248 302 -2377 -256 O ATOM 1182 CB SER A 211 57.264 -24.674 -13.502 1.00 81.87 C ANISOU 1182 CB SER A 211 14234 8519 8354 170 -1826 -161 C ATOM 1183 OG SER A 211 58.444 -25.449 -13.376 1.00 93.51 O ANISOU 1183 OG SER A 211 15700 9959 9872 80 -1647 -149 O ATOM 1184 N LEU A 212 55.148 -22.977 -12.250 1.00 73.74 N ANISOU 1184 N LEU A 212 12909 7678 7432 296 -2079 -168 N ATOM 1185 CA LEU A 212 54.183 -21.893 -12.423 1.00 74.11 C ANISOU 1185 CA LEU A 212 12992 7735 7431 424 -2223 -185 C ATOM 1186 C LEU A 212 54.217 -21.460 -13.877 1.00 79.79 C ANISOU 1186 C LEU A 212 14070 8307 7941 538 -2292 -195 C ATOM 1187 O LEU A 212 55.265 -21.035 -14.361 1.00 79.12 O ANISOU 1187 O LEU A 212 14219 8105 7740 533 -2115 -159 O ATOM 1188 CB LEU A 212 54.457 -20.709 -11.468 1.00 73.03 C ANISOU 1188 CB LEU A 212 12769 7638 7341 435 -2095 -147 C ATOM 1189 CG LEU A 212 54.220 -20.943 -9.986 1.00 75.65 C ANISOU 1189 CG LEU A 212 12764 8119 7859 348 -2054 -141 C ATOM 1190 CD1 LEU A 212 54.691 -19.774 -9.186 1.00 75.03 C ANISOU 1190 CD1 LEU A 212 12655 8055 7798 357 -1910 -107 C ATOM 1191 CD2 LEU A 212 52.765 -21.192 -9.700 1.00 77.93 C ANISOU 1191 CD2 LEU A 212 12851 8512 8246 383 -2259 -194 C ATOM 1192 N GLN A 213 53.115 -21.675 -14.601 1.00 78.57 N ANISOU 1192 N GLN A 213 13963 8152 7737 630 -2544 -252 N ATOM 1193 CA GLN A 213 53.046 -21.391 -16.030 1.00 80.44 C ANISOU 1193 CA GLN A 213 14561 8247 7755 749 -2647 -267 C ATOM 1194 C GLN A 213 52.527 -19.973 -16.268 1.00 88.01 C ANISOU 1194 C GLN A 213 15668 9160 8612 914 -2734 -256 C ATOM 1195 O GLN A 213 51.489 -19.580 -15.726 1.00 88.33 O ANISOU 1195 O GLN A 213 15502 9303 8755 984 -2895 -290 O ATOM 1196 CB GLN A 213 52.162 -22.424 -16.754 1.00 82.66 C ANISOU 1196 CB GLN A 213 14836 8544 8025 769 -2895 -346 C ATOM 1197 CG GLN A 213 52.604 -23.891 -16.545 1.00 93.57 C ANISOU 1197 CG GLN A 213 16086 9958 9508 608 -2817 -360 C ATOM 1198 CD GLN A 213 54.021 -24.219 -17.000 1.00109.79 C ANISOU 1198 CD GLN A 213 18360 11891 11463 537 -2577 -313 C ATOM 1199 OE1 GLN A 213 54.640 -23.510 -17.801 1.00107.33 O ANISOU 1199 OE1 GLN A 213 18364 11447 10970 604 -2484 -283 O ATOM 1200 NE2 GLN A 213 54.566 -25.323 -16.502 1.00 95.79 N ANISOU 1200 NE2 GLN A 213 16430 10156 9809 400 -2463 -309 N ATOM 1201 N PHE A 214 53.289 -19.200 -17.056 1.00 86.68 N ANISOU 1201 N PHE A 214 15861 8829 8245 973 -2609 -211 N ATOM 1202 CA PHE A 214 52.980 -17.822 -17.423 1.00 88.52 C ANISOU 1202 CA PHE A 214 16320 8973 8340 1134 -2659 -188 C ATOM 1203 C PHE A 214 52.916 -17.661 -18.946 1.00 97.00 C ANISOU 1203 C PHE A 214 17835 9874 9147 1263 -2768 -194 C ATOM 1204 O PHE A 214 53.640 -18.377 -19.646 1.00 96.95 O ANISOU 1204 O PHE A 214 18011 9781 9044 1190 -2667 -191 O ATOM 1205 CB PHE A 214 54.037 -16.866 -16.849 1.00 89.08 C ANISOU 1205 CB PHE A 214 16447 8987 8412 1075 -2362 -120 C ATOM 1206 CG PHE A 214 54.243 -16.917 -15.360 1.00 88.35 C ANISOU 1206 CG PHE A 214 15971 9048 8551 953 -2237 -111 C ATOM 1207 CD1 PHE A 214 53.457 -16.156 -14.509 1.00 91.06 C ANISOU 1207 CD1 PHE A 214 16114 9485 8998 1019 -2321 -118 C ATOM 1208 CD2 PHE A 214 55.268 -17.676 -14.811 1.00 88.59 C ANISOU 1208 CD2 PHE A 214 15858 9117 8685 781 -2028 -96 C ATOM 1209 CE1 PHE A 214 53.665 -16.188 -13.130 1.00 90.05 C ANISOU 1209 CE1 PHE A 214 15660 9490 9063 907 -2199 -109 C ATOM 1210 CE2 PHE A 214 55.473 -17.709 -13.433 1.00 89.64 C ANISOU 1210 CE2 PHE A 214 15664 9384 9011 680 -1925 -86 C ATOM 1211 CZ PHE A 214 54.666 -16.970 -12.601 1.00 87.46 C ANISOU 1211 CZ PHE A 214 15206 9200 8824 739 -2009 -91 C ATOM 1212 N PRO A 215 52.128 -16.695 -19.492 1.00 96.82 N ANISOU 1212 N PRO A 215 18017 9783 8988 1461 -2961 -200 N ATOM 1213 CA PRO A 215 52.129 -16.501 -20.967 1.00 99.35 C ANISOU 1213 CA PRO A 215 18811 9919 9020 1594 -3060 -199 C ATOM 1214 C PRO A 215 53.458 -15.887 -21.455 1.00103.52 C ANISOU 1214 C PRO A 215 19714 10253 9367 1544 -2733 -121 C ATOM 1215 O PRO A 215 53.957 -14.930 -20.854 1.00102.30 O ANISOU 1215 O PRO A 215 19556 10068 9247 1520 -2533 -69 O ATOM 1216 CB PRO A 215 50.946 -15.559 -21.211 1.00102.99 C ANISOU 1216 CB PRO A 215 19351 10370 9410 1827 -3348 -223 C ATOM 1217 CG PRO A 215 50.733 -14.861 -19.907 1.00105.79 C ANISOU 1217 CG PRO A 215 19379 10845 9973 1806 -3274 -207 C ATOM 1218 CD PRO A 215 51.202 -15.763 -18.810 1.00 98.69 C ANISOU 1218 CD PRO A 215 18077 10101 9319 1583 -3101 -212 C ATOM 1219 N ASP A 216 54.048 -16.466 -22.521 1.00100.95 N ANISOU 1219 N ASP A 216 19702 9795 8860 1514 -2665 -122 N ATOM 1220 CA ASP A 216 55.344 -16.033 -23.049 1.00100.84 C ANISOU 1220 CA ASP A 216 20037 9593 8685 1443 -2330 -64 C ATOM 1221 C ASP A 216 55.205 -14.843 -24.015 1.00106.81 C ANISOU 1221 C ASP A 216 21295 10139 9151 1620 -2358 -22 C ATOM 1222 O ASP A 216 56.210 -14.202 -24.317 1.00107.00 O ANISOU 1222 O ASP A 216 21607 9998 9052 1566 -2056 30 O ATOM 1223 CB ASP A 216 56.039 -17.198 -23.772 1.00102.63 C ANISOU 1223 CB ASP A 216 20386 9763 8844 1333 -2226 -90 C ATOM 1224 N ASP A 217 53.970 -14.541 -24.471 1.00104.16 N ANISOU 1224 N ASP A 217 21060 9805 8711 1832 -2716 -49 N ATOM 1225 CA ASP A 217 53.639 -13.490 -25.444 1.00105.96 C ANISOU 1225 CA ASP A 217 21783 9833 8645 2042 -2819 -13 C ATOM 1226 C ASP A 217 54.208 -12.112 -25.078 1.00109.41 C ANISOU 1226 C ASP A 217 22382 10148 9039 2050 -2565 64 C ATOM 1227 O ASP A 217 54.351 -11.792 -23.905 1.00107.23 O ANISOU 1227 O ASP A 217 21753 9995 8996 1960 -2446 73 O ATOM 1228 CB ASP A 217 52.115 -13.354 -25.566 1.00109.03 C ANISOU 1228 CB ASP A 217 22084 10310 9033 2268 -3271 -71 C ATOM 1229 N ASP A 218 54.467 -11.292 -26.089 1.00107.95 N ANISOU 1229 N ASP A 218 22748 9717 8549 2165 -2496 116 N ATOM 1230 CA ASP A 218 54.950 -9.926 -25.890 1.00108.00 C ANISOU 1230 CA ASP A 218 22983 9571 8481 2186 -2263 188 C ATOM 1231 C ASP A 218 56.141 -9.737 -24.948 1.00109.49 C ANISOU 1231 C ASP A 218 22943 9791 8867 1943 -1849 211 C ATOM 1232 O ASP A 218 56.044 -9.032 -23.944 1.00107.94 O ANISOU 1232 O ASP A 218 22501 9671 8839 1929 -1799 223 O ATOM 1233 CB ASP A 218 53.796 -9.023 -25.441 1.00110.26 C ANISOU 1233 CB ASP A 218 23174 9911 8808 2399 -2545 188 C ATOM 1234 CG ASP A 218 54.000 -7.574 -25.840 1.00118.79 C ANISOU 1234 CG ASP A 218 24722 10747 9665 2524 -2419 264 C ATOM 1235 OD1 ASP A 218 54.899 -7.305 -26.664 1.00119.98 O ANISOU 1235 OD1 ASP A 218 25333 10670 9584 2469 -2155 314 O ATOM 1236 OD2 ASP A 218 53.263 -6.706 -25.329 1.00124.82 O ANISOU 1236 OD2 ASP A 218 25400 11540 10486 2674 -2572 271 O ATOM 1237 N TYR A 219 57.259 -10.369 -25.281 1.00105.03 N ANISOU 1237 N TYR A 219 22459 9166 8283 1758 -1561 207 N ATOM 1238 CA TYR A 219 58.506 -10.226 -24.511 1.00102.56 C ANISOU 1238 CA TYR A 219 21956 8866 8146 1526 -1160 213 C ATOM 1239 C TYR A 219 58.265 -10.246 -22.966 1.00104.12 C ANISOU 1239 C TYR A 219 21574 9308 8678 1451 -1203 190 C ATOM 1240 O TYR A 219 59.032 -9.618 -22.223 1.00102.59 O ANISOU 1240 O TYR A 219 21268 9108 8606 1326 -932 202 O ATOM 1241 CB TYR A 219 59.214 -8.905 -24.898 1.00104.54 C ANISOU 1241 CB TYR A 219 22639 8866 8218 1524 -862 269 C ATOM 1242 CG TYR A 219 59.503 -8.753 -26.377 1.00108.27 C ANISOU 1242 CG TYR A 219 23727 9070 8340 1592 -777 300 C ATOM 1243 CD1 TYR A 219 60.682 -9.241 -26.931 1.00110.21 C ANISOU 1243 CD1 TYR A 219 24140 9205 8529 1417 -442 284 C ATOM 1244 CD2 TYR A 219 58.624 -8.068 -27.212 1.00111.43 C ANISOU 1244 CD2 TYR A 219 24560 9318 8461 1838 -1018 342 C ATOM 1245 CE1 TYR A 219 60.963 -9.086 -28.288 1.00113.23 C ANISOU 1245 CE1 TYR A 219 25113 9331 8578 1473 -337 311 C ATOM 1246 CE2 TYR A 219 58.891 -7.912 -28.572 1.00114.91 C ANISOU 1246 CE2 TYR A 219 25606 9499 8555 1907 -938 374 C ATOM 1247 CZ TYR A 219 60.063 -8.422 -29.106 1.00121.77 C ANISOU 1247 CZ TYR A 219 26643 10260 9366 1718 -587 360 C ATOM 1248 OH TYR A 219 60.331 -8.267 -30.443 1.00125.50 O ANISOU 1248 OH TYR A 219 27731 10468 9484 1780 -488 391 O ATOM 1249 N SER A 220 57.234 -10.991 -22.491 1.00 99.88 N ANISOU 1249 N SER A 220 20678 8982 8289 1515 -1529 151 N ATOM 1250 CA SER A 220 56.897 -11.082 -21.063 1.00 97.67 C ANISOU 1250 CA SER A 220 19873 8931 8306 1453 -1584 128 C ATOM 1251 C SER A 220 58.055 -11.669 -20.252 1.00 99.51 C ANISOU 1251 C SER A 220 19807 9256 8746 1212 -1292 113 C ATOM 1252 O SER A 220 58.831 -12.478 -20.768 1.00 99.52 O ANISOU 1252 O SER A 220 19887 9213 8714 1103 -1149 98 O ATOM 1253 CB SER A 220 55.642 -11.917 -20.845 1.00101.01 C ANISOU 1253 CB SER A 220 19998 9543 8838 1544 -1955 78 C ATOM 1254 OG SER A 220 54.495 -11.232 -21.322 1.00111.01 O ANISOU 1254 OG SER A 220 21446 10760 9971 1779 -2247 77 O ATOM 1255 N TRP A 221 58.186 -11.220 -18.992 1.00 93.79 N ANISOU 1255 N TRP A 221 18756 8651 8228 1138 -1204 112 N ATOM 1256 CA TRP A 221 59.260 -11.628 -18.089 1.00 91.27 C ANISOU 1256 CA TRP A 221 18141 8425 8114 929 -949 93 C ATOM 1257 C TRP A 221 58.701 -11.885 -16.673 1.00 94.56 C ANISOU 1257 C TRP A 221 18068 9077 8783 897 -1076 73 C ATOM 1258 O TRP A 221 59.455 -11.871 -15.694 1.00 92.93 O ANISOU 1258 O TRP A 221 17611 8952 8746 756 -890 62 O ATOM 1259 CB TRP A 221 60.348 -10.534 -18.072 1.00 89.99 C ANISOU 1259 CB TRP A 221 18182 8105 7904 844 -612 111 C ATOM 1260 CG TRP A 221 59.861 -9.200 -17.582 1.00 91.22 C ANISOU 1260 CG TRP A 221 18385 8227 8049 937 -639 136 C ATOM 1261 CD1 TRP A 221 59.085 -8.309 -18.263 1.00 95.81 C ANISOU 1261 CD1 TRP A 221 19303 8669 8432 1126 -778 173 C ATOM 1262 CD2 TRP A 221 60.202 -8.568 -16.341 1.00 89.72 C ANISOU 1262 CD2 TRP A 221 17926 8123 8043 847 -506 124 C ATOM 1263 NE1 TRP A 221 58.834 -7.208 -17.483 1.00 95.01 N ANISOU 1263 NE1 TRP A 221 19132 8573 8395 1166 -755 185 N ATOM 1264 CE2 TRP A 221 59.540 -7.319 -16.314 1.00 94.49 C ANISOU 1264 CE2 TRP A 221 18706 8639 8556 989 -576 154 C ATOM 1265 CE3 TRP A 221 60.968 -8.957 -15.221 1.00 88.93 C ANISOU 1265 CE3 TRP A 221 17449 8170 8173 670 -354 87 C ATOM 1266 CZ2 TRP A 221 59.636 -6.444 -15.222 1.00 92.82 C ANISOU 1266 CZ2 TRP A 221 18313 8477 8478 948 -483 145 C ATOM 1267 CZ3 TRP A 221 61.063 -8.090 -14.143 1.00 89.51 C ANISOU 1267 CZ3 TRP A 221 17345 8296 8368 632 -273 77 C ATOM 1268 CH2 TRP A 221 60.414 -6.845 -14.156 1.00 91.11 C ANISOU 1268 CH2 TRP A 221 17736 8405 8478 763 -328 105 C ATOM 1269 N TRP A 222 57.375 -12.155 -16.579 1.00 92.15 N ANISOU 1269 N TRP A 222 17628 8881 8503 1028 -1394 60 N ATOM 1270 CA TRP A 222 56.650 -12.371 -15.323 1.00 91.03 C ANISOU 1270 CA TRP A 222 17056 8951 8582 1016 -1529 38 C ATOM 1271 C TRP A 222 57.124 -13.661 -14.615 1.00 93.47 C ANISOU 1271 C TRP A 222 17027 9412 9076 849 -1470 14 C ATOM 1272 O TRP A 222 56.909 -13.782 -13.405 1.00 92.11 O ANISOU 1272 O TRP A 222 16510 9397 9090 791 -1481 3 O ATOM 1273 CB TRP A 222 55.132 -12.410 -15.554 1.00 91.14 C ANISOU 1273 CB TRP A 222 17023 9028 8576 1194 -1873 13 C ATOM 1274 CG TRP A 222 54.519 -11.034 -15.539 1.00 93.62 C ANISOU 1274 CG TRP A 222 17484 9271 8815 1357 -1944 29 C ATOM 1275 CD1 TRP A 222 53.913 -10.434 -14.474 1.00 96.05 C ANISOU 1275 CD1 TRP A 222 17532 9691 9270 1393 -1995 17 C ATOM 1276 CD2 TRP A 222 54.646 -10.014 -16.555 1.00 95.59 C ANISOU 1276 CD2 TRP A 222 18196 9299 8824 1488 -1914 67 C ATOM 1277 NE1 TRP A 222 53.575 -9.134 -14.789 1.00 97.04 N ANISOU 1277 NE1 TRP A 222 17914 9686 9269 1553 -2025 39 N ATOM 1278 CE2 TRP A 222 54.023 -8.847 -16.055 1.00100.10 C ANISOU 1278 CE2 TRP A 222 18754 9864 9414 1614 -1976 74 C ATOM 1279 CE3 TRP A 222 55.207 -9.978 -17.848 1.00 98.24 C ANISOU 1279 CE3 TRP A 222 18973 9433 8919 1514 -1836 95 C ATOM 1280 CZ2 TRP A 222 53.932 -7.661 -16.809 1.00101.36 C ANISOU 1280 CZ2 TRP A 222 19334 9818 9362 1772 -1975 113 C ATOM 1281 CZ3 TRP A 222 55.119 -8.804 -18.592 1.00101.60 C ANISOU 1281 CZ3 TRP A 222 19823 9653 9125 1664 -1827 135 C ATOM 1282 CH2 TRP A 222 54.482 -7.667 -18.077 1.00102.69 C ANISOU 1282 CH2 TRP A 222 19945 9785 9288 1795 -1902 146 C ATOM 1283 N ASP A 223 57.845 -14.563 -15.324 1.00 89.53 N ANISOU 1283 N ASP A 223 16643 8854 8522 770 -1383 8 N ATOM 1284 CA ASP A 223 58.445 -15.729 -14.674 1.00 87.42 C ANISOU 1284 CA ASP A 223 16091 8704 8421 618 -1301 -11 C ATOM 1285 C ASP A 223 59.610 -15.253 -13.819 1.00 88.43 C ANISOU 1285 C ASP A 223 16102 8841 8655 492 -1028 -6 C ATOM 1286 O ASP A 223 59.680 -15.610 -12.648 1.00 86.58 O ANISOU 1286 O ASP A 223 15538 8757 8602 413 -1019 -14 O ATOM 1287 CB ASP A 223 58.883 -16.800 -15.685 1.00 90.08 C ANISOU 1287 CB ASP A 223 16590 8967 8672 581 -1283 -27 C ATOM 1288 CG ASP A 223 59.489 -18.049 -15.056 1.00102.03 C ANISOU 1288 CG ASP A 223 17826 10588 10353 441 -1210 -46 C ATOM 1289 OD1 ASP A 223 59.130 -18.373 -13.898 1.00101.59 O ANISOU 1289 OD1 ASP A 223 17433 10692 10473 397 -1276 -49 O ATOM 1290 OD2 ASP A 223 60.240 -18.756 -15.755 1.00110.74 O ANISOU 1290 OD2 ASP A 223 19063 11611 11404 386 -1101 -60 O ATOM 1291 N LEU A 224 60.487 -14.396 -14.389 1.00 84.19 N ANISOU 1291 N LEU A 224 15844 8140 8003 474 -808 4 N ATOM 1292 CA LEU A 224 61.612 -13.799 -13.668 1.00 82.41 C ANISOU 1292 CA LEU A 224 15530 7906 7875 354 -543 -8 C ATOM 1293 C LEU A 224 61.110 -12.886 -12.562 1.00 84.40 C ANISOU 1293 C LEU A 224 15600 8249 8221 381 -589 0 C ATOM 1294 O LEU A 224 61.589 -12.970 -11.431 1.00 82.32 O ANISOU 1294 O LEU A 224 15053 8102 8124 282 -506 -20 O ATOM 1295 CB LEU A 224 62.521 -13.011 -14.632 1.00 83.69 C ANISOU 1295 CB LEU A 224 16063 7852 7882 330 -296 -8 C ATOM 1296 CG LEU A 224 63.732 -12.297 -14.011 1.00 87.61 C ANISOU 1296 CG LEU A 224 16491 8318 8480 196 -3 -39 C ATOM 1297 CD1 LEU A 224 64.788 -13.289 -13.555 1.00 86.39 C ANISOU 1297 CD1 LEU A 224 16083 8252 8492 52 131 -88 C ATOM 1298 CD2 LEU A 224 64.357 -11.349 -14.998 1.00 92.08 C ANISOU 1298 CD2 LEU A 224 17459 8653 8876 188 225 -36 C ATOM 1299 N PHE A 225 60.132 -12.026 -12.895 1.00 81.76 N ANISOU 1299 N PHE A 225 15434 7857 7774 527 -731 24 N ATOM 1300 CA PHE A 225 59.539 -11.073 -11.974 1.00 81.12 C ANISOU 1300 CA PHE A 225 15222 7840 7761 579 -783 29 C ATOM 1301 C PHE A 225 59.042 -11.789 -10.714 1.00 82.79 C ANISOU 1301 C PHE A 225 15012 8275 8172 534 -904 12 C ATOM 1302 O PHE A 225 59.403 -11.375 -9.615 1.00 81.53 O ANISOU 1302 O PHE A 225 14655 8191 8132 460 -801 0 O ATOM 1303 CB PHE A 225 58.396 -10.308 -12.655 1.00 84.53 C ANISOU 1303 CB PHE A 225 15889 8186 8043 774 -976 52 C ATOM 1304 CG PHE A 225 57.732 -9.300 -11.752 1.00 86.21 C ANISOU 1304 CG PHE A 225 15976 8455 8325 845 -1032 52 C ATOM 1305 CD1 PHE A 225 58.253 -8.023 -11.609 1.00 89.94 C ANISOU 1305 CD1 PHE A 225 16620 8804 8748 839 -847 63 C ATOM 1306 CD2 PHE A 225 56.585 -9.629 -11.041 1.00 88.17 C ANISOU 1306 CD2 PHE A 225 15935 8873 8691 913 -1256 33 C ATOM 1307 CE1 PHE A 225 57.646 -7.095 -10.763 1.00 90.89 C ANISOU 1307 CE1 PHE A 225 16630 8972 8933 906 -893 58 C ATOM 1308 CE2 PHE A 225 55.983 -8.703 -10.187 1.00 91.02 C ANISOU 1308 CE2 PHE A 225 16176 9285 9122 979 -1292 26 C ATOM 1309 CZ PHE A 225 56.512 -7.441 -10.060 1.00 89.62 C ANISOU 1309 CZ PHE A 225 16178 8984 8888 981 -1116 39 C ATOM 1310 N MET A 226 58.260 -12.880 -10.869 1.00 78.53 N ANISOU 1310 N MET A 226 14345 7831 7664 568 -1110 6 N ATOM 1311 CA MET A 226 57.736 -13.654 -9.740 1.00 76.97 C ANISOU 1311 CA MET A 226 13775 7828 7644 518 -1215 -9 C ATOM 1312 C MET A 226 58.870 -14.165 -8.842 1.00 79.30 C ANISOU 1312 C MET A 226 13868 8194 8067 357 -1032 -17 C ATOM 1313 O MET A 226 58.757 -14.089 -7.620 1.00 77.54 O ANISOU 1313 O MET A 226 13393 8096 7971 312 -1024 -23 O ATOM 1314 CB MET A 226 56.892 -14.837 -10.235 1.00 79.57 C ANISOU 1314 CB MET A 226 14042 8215 7977 555 -1429 -23 C ATOM 1315 N LYS A 227 59.957 -14.614 -9.461 1.00 76.45 N ANISOU 1315 N LYS A 227 13633 7748 7666 282 -884 -21 N ATOM 1316 CA LYS A 227 61.111 -15.118 -8.731 1.00 75.34 C ANISOU 1316 CA LYS A 227 13315 7664 7647 146 -720 -40 C ATOM 1317 C LYS A 227 61.815 -14.026 -7.926 1.00 79.24 C ANISOU 1317 C LYS A 227 13758 8156 8195 91 -549 -58 C ATOM 1318 O LYS A 227 62.365 -14.301 -6.860 1.00 78.50 O ANISOU 1318 O LYS A 227 13426 8167 8232 4 -491 -78 O ATOM 1319 CB LYS A 227 62.101 -15.781 -9.691 1.00 78.15 C ANISOU 1319 CB LYS A 227 13829 7915 7949 91 -594 -55 C ATOM 1320 CG LYS A 227 61.611 -17.094 -10.280 1.00 92.20 C ANISOU 1320 CG LYS A 227 15606 9716 9708 112 -744 -49 C ATOM 1321 CD LYS A 227 62.581 -17.629 -11.320 1.00103.50 C ANISOU 1321 CD LYS A 227 17233 11025 11069 69 -604 -68 C ATOM 1322 CE LYS A 227 62.158 -19.003 -11.814 1.00112.27 C ANISOU 1322 CE LYS A 227 18326 12160 12172 79 -747 -69 C ATOM 1323 NZ LYS A 227 61.827 -18.994 -13.266 1.00121.53 N ANISOU 1323 NZ LYS A 227 19829 13191 13156 156 -799 -68 N ATOM 1324 N ILE A 228 61.804 -12.791 -8.426 1.00 75.92 N ANISOU 1324 N ILE A 228 13572 7607 7668 142 -474 -53 N ATOM 1325 CA ILE A 228 62.470 -11.705 -7.704 1.00 75.19 C ANISOU 1325 CA ILE A 228 13446 7496 7625 82 -303 -79 C ATOM 1326 C ILE A 228 61.621 -11.364 -6.456 1.00 78.93 C ANISOU 1326 C ILE A 228 13686 8114 8189 116 -426 -74 C ATOM 1327 O ILE A 228 62.188 -11.139 -5.383 1.00 77.82 O ANISOU 1327 O ILE A 228 13359 8051 8157 32 -336 -104 O ATOM 1328 CB ILE A 228 62.724 -10.469 -8.612 1.00 79.18 C ANISOU 1328 CB ILE A 228 14298 7801 7984 120 -166 -75 C ATOM 1329 CG1 ILE A 228 63.507 -10.891 -9.895 1.00 80.27 C ANISOU 1329 CG1 ILE A 228 14687 7792 8020 84 -34 -80 C ATOM 1330 CG2 ILE A 228 63.472 -9.367 -7.829 1.00 78.92 C ANISOU 1330 CG2 ILE A 228 14222 7746 8020 36 26 -114 C ATOM 1331 CD1 ILE A 228 63.651 -9.837 -11.003 1.00 87.21 C ANISOU 1331 CD1 ILE A 228 15975 8447 8715 132 94 -64 C ATOM 1332 N CYS A 229 60.272 -11.391 -6.583 1.00 76.34 N ANISOU 1332 N CYS A 229 13357 7826 7824 239 -634 -47 N ATOM 1333 CA CYS A 229 59.360 -11.116 -5.468 1.00 76.22 C ANISOU 1333 CA CYS A 229 13122 7944 7896 277 -745 -49 C ATOM 1334 C CYS A 229 59.544 -12.166 -4.374 1.00 78.36 C ANISOU 1334 C CYS A 229 13085 8380 8307 179 -765 -58 C ATOM 1335 O CYS A 229 59.650 -11.808 -3.198 1.00 77.56 O ANISOU 1335 O CYS A 229 12812 8367 8290 133 -719 -75 O ATOM 1336 CB CYS A 229 57.915 -11.066 -5.945 1.00 77.98 C ANISOU 1336 CB CYS A 229 13389 8173 8065 427 -964 -34 C ATOM 1337 SG CYS A 229 57.559 -9.687 -7.061 1.00 84.15 S ANISOU 1337 SG CYS A 229 14544 8759 8670 580 -972 -19 S ATOM 1338 N VAL A 230 59.624 -13.449 -4.766 1.00 73.77 N ANISOU 1338 N VAL A 230 12458 7829 7741 146 -826 -49 N ATOM 1339 CA VAL A 230 59.856 -14.541 -3.826 1.00 72.30 C ANISOU 1339 CA VAL A 230 12022 7776 7673 58 -842 -50 C ATOM 1340 C VAL A 230 61.212 -14.304 -3.130 1.00 74.79 C ANISOU 1340 C VAL A 230 12269 8100 8049 -45 -664 -78 C ATOM 1341 O VAL A 230 61.275 -14.384 -1.914 1.00 74.16 O ANISOU 1341 O VAL A 230 11992 8131 8054 -90 -662 -86 O ATOM 1342 CB VAL A 230 59.784 -15.942 -4.507 1.00 76.34 C ANISOU 1342 CB VAL A 230 12536 8288 8180 44 -925 -38 C ATOM 1343 CG1 VAL A 230 60.128 -17.063 -3.524 1.00 75.09 C ANISOU 1343 CG1 VAL A 230 12149 8246 8135 -44 -926 -35 C ATOM 1344 CG2 VAL A 230 58.410 -16.185 -5.119 1.00 76.92 C ANISOU 1344 CG2 VAL A 230 12647 8368 8211 140 -1119 -29 C ATOM 1345 N PHE A 231 62.259 -13.931 -3.886 1.00 70.59 N ANISOU 1345 N PHE A 231 11905 7445 7470 -80 -512 -100 N ATOM 1346 CA PHE A 231 63.593 -13.705 -3.334 1.00 69.65 C ANISOU 1346 CA PHE A 231 11711 7329 7424 -181 -343 -148 C ATOM 1347 C PHE A 231 63.618 -12.561 -2.294 1.00 73.55 C ANISOU 1347 C PHE A 231 12126 7864 7957 -198 -289 -175 C ATOM 1348 O PHE A 231 64.326 -12.682 -1.295 1.00 72.43 O ANISOU 1348 O PHE A 231 11806 7804 7908 -272 -241 -212 O ATOM 1349 CB PHE A 231 64.596 -13.387 -4.455 1.00 71.92 C ANISOU 1349 CB PHE A 231 12212 7460 7654 -216 -169 -178 C ATOM 1350 CG PHE A 231 65.984 -13.027 -3.977 1.00 73.00 C ANISOU 1350 CG PHE A 231 12267 7589 7882 -325 19 -250 C ATOM 1351 CD1 PHE A 231 66.804 -13.980 -3.386 1.00 75.29 C ANISOU 1351 CD1 PHE A 231 12350 7969 8289 -390 29 -285 C ATOM 1352 CD2 PHE A 231 66.500 -11.758 -4.189 1.00 75.42 C ANISOU 1352 CD2 PHE A 231 12712 7785 8160 -361 188 -290 C ATOM 1353 CE1 PHE A 231 68.088 -13.647 -2.950 1.00 76.23 C ANISOU 1353 CE1 PHE A 231 12370 8088 8506 -483 184 -369 C ATOM 1354 CE2 PHE A 231 67.798 -11.437 -3.787 1.00 78.31 C ANISOU 1354 CE2 PHE A 231 12986 8142 8626 -473 365 -376 C ATOM 1355 CZ PHE A 231 68.579 -12.381 -3.161 1.00 75.87 C ANISOU 1355 CZ PHE A 231 12442 7941 8444 -530 354 -420 C ATOM 1356 N ILE A 232 62.870 -11.477 -2.507 1.00 70.97 N ANISOU 1356 N ILE A 232 11933 7477 7558 -125 -305 -161 N ATOM 1357 CA ILE A 232 62.959 -10.373 -1.564 1.00 71.32 C ANISOU 1357 CA ILE A 232 11920 7544 7636 -146 -238 -194 C ATOM 1358 C ILE A 232 62.000 -10.615 -0.354 1.00 75.43 C ANISOU 1358 C ILE A 232 12223 8222 8215 -115 -376 -177 C ATOM 1359 O ILE A 232 62.389 -10.280 0.768 1.00 74.70 O ANISOU 1359 O ILE A 232 11993 8204 8187 -173 -328 -212 O ATOM 1360 CB ILE A 232 62.706 -8.976 -2.211 1.00 75.70 C ANISOU 1360 CB ILE A 232 12723 7948 8092 -85 -164 -194 C ATOM 1361 CG1 ILE A 232 61.274 -8.818 -2.769 1.00 76.97 C ANISOU 1361 CG1 ILE A 232 12993 8086 8167 64 -332 -142 C ATOM 1362 CG2 ILE A 232 63.778 -8.676 -3.287 1.00 77.07 C ANISOU 1362 CG2 ILE A 232 13120 7955 8208 -142 19 -218 C ATOM 1363 CD1 ILE A 232 60.922 -7.396 -3.269 1.00 88.00 C ANISOU 1363 CD1 ILE A 232 14638 9337 9463 151 -284 -138 C ATOM 1364 N PHE A 233 60.793 -11.206 -0.559 1.00 72.14 N ANISOU 1364 N PHE A 233 11774 7854 7780 -33 -540 -133 N ATOM 1365 CA PHE A 233 59.841 -11.404 0.548 1.00 71.39 C ANISOU 1365 CA PHE A 233 11482 7898 7745 -13 -643 -125 C ATOM 1366 C PHE A 233 60.007 -12.783 1.241 1.00 73.99 C ANISOU 1366 C PHE A 233 11618 8347 8147 -83 -694 -111 C ATOM 1367 O PHE A 233 59.373 -13.010 2.271 1.00 74.38 O ANISOU 1367 O PHE A 233 11510 8508 8245 -89 -747 -106 O ATOM 1368 CB PHE A 233 58.387 -11.258 0.072 1.00 73.87 C ANISOU 1368 CB PHE A 233 11834 8210 8025 108 -787 -103 C ATOM 1369 CG PHE A 233 58.051 -9.879 -0.439 1.00 76.70 C ANISOU 1369 CG PHE A 233 12378 8456 8309 204 -763 -113 C ATOM 1370 CD1 PHE A 233 57.823 -8.829 0.446 1.00 80.35 C ANISOU 1370 CD1 PHE A 233 12795 8940 8794 221 -713 -138 C ATOM 1371 CD2 PHE A 233 57.888 -9.644 -1.798 1.00 80.21 C ANISOU 1371 CD2 PHE A 233 13057 8767 8651 287 -799 -95 C ATOM 1372 CE1 PHE A 233 57.518 -7.548 -0.026 1.00 82.34 C ANISOU 1372 CE1 PHE A 233 13237 9074 8976 317 -689 -145 C ATOM 1373 CE2 PHE A 233 57.567 -8.366 -2.269 1.00 84.51 C ANISOU 1373 CE2 PHE A 233 13803 9193 9114 389 -782 -97 C ATOM 1374 CZ PHE A 233 57.388 -7.325 -1.380 1.00 82.67 C ANISOU 1374 CZ PHE A 233 13521 8976 8912 404 -725 -121 C ATOM 1375 N ALA A 234 60.858 -13.679 0.723 1.00 68.54 N ANISOU 1375 N ALA A 234 10950 7628 7463 -134 -666 -107 N ATOM 1376 CA ALA A 234 61.058 -14.976 1.371 1.00 67.40 C ANISOU 1376 CA ALA A 234 10647 7580 7382 -190 -714 -91 C ATOM 1377 C ALA A 234 62.543 -15.205 1.724 1.00 70.33 C ANISOU 1377 C ALA A 234 10974 7951 7797 -268 -610 -126 C ATOM 1378 O ALA A 234 62.930 -16.324 2.100 1.00 69.95 O ANISOU 1378 O ALA A 234 10827 7957 7794 -303 -645 -115 O ATOM 1379 CB ALA A 234 60.556 -16.095 0.474 1.00 68.31 C ANISOU 1379 CB ALA A 234 10801 7673 7481 -166 -811 -58 C ATOM 1380 N PHE A 235 63.369 -14.148 1.616 1.00 65.63 N ANISOU 1380 N PHE A 235 10449 7292 7196 -293 -485 -176 N ATOM 1381 CA PHE A 235 64.780 -14.246 1.955 1.00 64.77 C ANISOU 1381 CA PHE A 235 10275 7186 7150 -368 -387 -233 C ATOM 1382 C PHE A 235 65.333 -12.876 2.381 1.00 69.16 C ANISOU 1382 C PHE A 235 10849 7713 7717 -406 -270 -298 C ATOM 1383 O PHE A 235 65.722 -12.737 3.533 1.00 68.46 O ANISOU 1383 O PHE A 235 10622 7711 7678 -444 -273 -336 O ATOM 1384 CB PHE A 235 65.597 -14.819 0.778 1.00 66.44 C ANISOU 1384 CB PHE A 235 10581 7302 7360 -387 -318 -247 C ATOM 1385 CG PHE A 235 67.078 -14.916 1.045 1.00 67.92 C ANISOU 1385 CG PHE A 235 10681 7491 7634 -460 -210 -325 C ATOM 1386 CD1 PHE A 235 67.611 -16.018 1.696 1.00 70.80 C ANISOU 1386 CD1 PHE A 235 10888 7942 8072 -474 -273 -332 C ATOM 1387 CD2 PHE A 235 67.945 -13.921 0.614 1.00 70.51 C ANISOU 1387 CD2 PHE A 235 11089 7727 7976 -512 -45 -397 C ATOM 1388 CE1 PHE A 235 68.981 -16.101 1.952 1.00 72.16 C ANISOU 1388 CE1 PHE A 235 10959 8121 8337 -526 -192 -418 C ATOM 1389 CE2 PHE A 235 69.314 -14.005 0.870 1.00 73.65 C ANISOU 1389 CE2 PHE A 235 11376 8133 8477 -584 55 -489 C ATOM 1390 CZ PHE A 235 69.825 -15.095 1.532 1.00 71.54 C ANISOU 1390 CZ PHE A 235 10930 7962 8288 -584 -29 -503 C ATOM 1391 N VAL A 236 65.331 -11.868 1.479 1.00 66.15 N ANISOU 1391 N VAL A 236 10650 7204 7278 -393 -172 -311 N ATOM 1392 CA VAL A 236 65.935 -10.553 1.715 1.00 66.14 C ANISOU 1392 CA VAL A 236 10699 7143 7287 -441 -34 -378 C ATOM 1393 C VAL A 236 65.292 -9.848 2.946 1.00 70.31 C ANISOU 1393 C VAL A 236 11136 7757 7820 -424 -86 -384 C ATOM 1394 O VAL A 236 66.034 -9.567 3.890 1.00 70.02 O ANISOU 1394 O VAL A 236 10980 7778 7846 -492 -43 -451 O ATOM 1395 CB VAL A 236 65.849 -9.648 0.467 1.00 70.20 C ANISOU 1395 CB VAL A 236 11473 7485 7716 -416 74 -373 C ATOM 1396 CG1 VAL A 236 66.364 -8.239 0.754 1.00 70.54 C ANISOU 1396 CG1 VAL A 236 11584 7453 7767 -471 224 -440 C ATOM 1397 CG2 VAL A 236 66.621 -10.267 -0.682 1.00 70.38 C ANISOU 1397 CG2 VAL A 236 11597 7416 7730 -449 159 -381 C ATOM 1398 N ILE A 237 63.964 -9.544 2.942 1.00 66.83 N ANISOU 1398 N ILE A 237 10747 7325 7320 -334 -176 -328 N ATOM 1399 CA ILE A 237 63.374 -8.815 4.076 1.00 66.63 C ANISOU 1399 CA ILE A 237 10645 7371 7301 -318 -201 -342 C ATOM 1400 C ILE A 237 63.387 -9.779 5.330 1.00 69.20 C ANISOU 1400 C ILE A 237 10755 7856 7680 -351 -289 -338 C ATOM 1401 O ILE A 237 63.815 -9.284 6.369 1.00 68.34 O ANISOU 1401 O ILE A 237 10567 7800 7598 -397 -254 -391 O ATOM 1402 CB ILE A 237 61.962 -8.157 3.820 1.00 70.13 C ANISOU 1402 CB ILE A 237 11180 7783 7684 -205 -266 -300 C ATOM 1403 CG1 ILE A 237 60.800 -9.153 3.563 1.00 70.80 C ANISOU 1403 CG1 ILE A 237 11208 7933 7761 -130 -420 -235 C ATOM 1404 CG2 ILE A 237 62.028 -7.129 2.692 1.00 70.93 C ANISOU 1404 CG2 ILE A 237 11524 7713 7715 -162 -180 -303 C ATOM 1405 CD1 ILE A 237 59.984 -9.600 4.841 1.00 80.05 C ANISOU 1405 CD1 ILE A 237 12183 9255 8976 -126 -503 -225 C ATOM 1406 N PRO A 238 63.160 -11.087 5.175 1.00 65.45 N ANISOU 1406 N PRO A 238 10213 7436 7217 -340 -383 -288 N ATOM 1407 CA PRO A 238 63.291 -11.920 6.380 1.00 64.83 C ANISOU 1407 CA PRO A 238 9971 7487 7176 -374 -448 -284 C ATOM 1408 C PRO A 238 64.704 -11.829 7.014 1.00 69.79 C ANISOU 1408 C PRO A 238 10525 8139 7854 -449 -389 -359 C ATOM 1409 O PRO A 238 64.837 -11.346 8.139 1.00 70.32 O ANISOU 1409 O PRO A 238 10523 8270 7925 -472 -387 -399 O ATOM 1410 CB PRO A 238 63.043 -13.337 5.852 1.00 66.12 C ANISOU 1410 CB PRO A 238 10111 7665 7346 -359 -532 -224 C ATOM 1411 CG PRO A 238 62.256 -13.148 4.596 1.00 70.95 C ANISOU 1411 CG PRO A 238 10853 8190 7916 -298 -549 -190 C ATOM 1412 CD PRO A 238 62.742 -11.862 3.995 1.00 67.23 C ANISOU 1412 CD PRO A 238 10518 7610 7416 -297 -438 -234 C ATOM 1413 N VAL A 239 65.727 -12.290 6.291 1.00 66.54 N ANISOU 1413 N VAL A 239 10124 7675 7481 -482 -346 -386 N ATOM 1414 CA VAL A 239 67.145 -12.297 6.727 1.00 66.80 C ANISOU 1414 CA VAL A 239 10066 7728 7587 -548 -297 -475 C ATOM 1415 C VAL A 239 67.480 -10.963 7.394 1.00 72.64 C ANISOU 1415 C VAL A 239 10799 8464 8336 -592 -220 -558 C ATOM 1416 O VAL A 239 68.049 -10.964 8.481 1.00 73.24 O ANISOU 1416 O VAL A 239 10759 8624 8446 -623 -256 -616 O ATOM 1417 CB VAL A 239 68.156 -12.598 5.572 1.00 71.00 C ANISOU 1417 CB VAL A 239 10641 8169 8169 -580 -207 -514 C ATOM 1418 CG1 VAL A 239 69.596 -12.308 5.981 1.00 71.42 C ANISOU 1418 CG1 VAL A 239 10585 8233 8318 -654 -133 -636 C ATOM 1419 CG2 VAL A 239 68.033 -14.030 5.074 1.00 70.48 C ANISOU 1419 CG2 VAL A 239 10560 8114 8104 -543 -287 -450 C ATOM 1420 N LEU A 240 67.099 -9.837 6.771 1.00 69.40 N ANISOU 1420 N LEU A 240 10527 7952 7888 -588 -124 -563 N ATOM 1421 CA LEU A 240 67.401 -8.535 7.334 1.00 69.82 C ANISOU 1421 CA LEU A 240 10596 7982 7950 -635 -38 -644 C ATOM 1422 C LEU A 240 66.571 -8.279 8.589 1.00 72.70 C ANISOU 1422 C LEU A 240 10900 8446 8274 -601 -121 -626 C ATOM 1423 O LEU A 240 67.160 -7.829 9.563 1.00 73.46 O ANISOU 1423 O LEU A 240 10919 8594 8399 -652 -110 -707 O ATOM 1424 CB LEU A 240 67.190 -7.409 6.319 1.00 70.80 C ANISOU 1424 CB LEU A 240 10915 7953 8034 -631 91 -648 C ATOM 1425 CG LEU A 240 68.168 -7.414 5.130 1.00 76.85 C ANISOU 1425 CG LEU A 240 11769 8597 8834 -688 224 -687 C ATOM 1426 CD1 LEU A 240 67.792 -6.367 4.110 1.00 77.87 C ANISOU 1426 CD1 LEU A 240 12138 8560 8890 -667 342 -668 C ATOM 1427 CD2 LEU A 240 69.618 -7.220 5.588 1.00 80.62 C ANISOU 1427 CD2 LEU A 240 12119 9090 9420 -802 315 -819 C ATOM 1428 N ILE A 241 65.261 -8.634 8.623 1.00 67.51 N ANISOU 1428 N ILE A 241 10266 7824 7561 -522 -205 -533 N ATOM 1429 CA ILE A 241 64.445 -8.437 9.838 1.00 67.11 C ANISOU 1429 CA ILE A 241 10156 7868 7476 -496 -262 -522 C ATOM 1430 C ILE A 241 65.039 -9.262 11.002 1.00 70.41 C ANISOU 1430 C ILE A 241 10437 8405 7909 -533 -338 -543 C ATOM 1431 O ILE A 241 65.298 -8.701 12.072 1.00 69.59 O ANISOU 1431 O ILE A 241 10294 8351 7795 -562 -333 -604 O ATOM 1432 CB ILE A 241 62.939 -8.774 9.638 1.00 69.93 C ANISOU 1432 CB ILE A 241 10535 8245 7792 -411 -330 -432 C ATOM 1433 CG1 ILE A 241 62.300 -7.850 8.581 1.00 70.65 C ANISOU 1433 CG1 ILE A 241 10770 8219 7856 -349 -281 -418 C ATOM 1434 CG2 ILE A 241 62.167 -8.666 10.981 1.00 70.71 C ANISOU 1434 CG2 ILE A 241 10557 8445 7863 -397 -366 -429 C ATOM 1435 CD1 ILE A 241 60.844 -8.195 8.197 1.00 78.66 C ANISOU 1435 CD1 ILE A 241 11792 9248 8849 -255 -367 -347 C ATOM 1436 N ILE A 242 65.301 -10.568 10.772 1.00 67.12 N ANISOU 1436 N ILE A 242 9967 8023 7513 -527 -411 -497 N ATOM 1437 CA ILE A 242 65.828 -11.458 11.804 1.00 67.70 C ANISOU 1437 CA ILE A 242 9938 8196 7589 -541 -499 -504 C ATOM 1438 C ILE A 242 67.283 -11.037 12.183 1.00 70.86 C ANISOU 1438 C ILE A 242 10273 8603 8046 -598 -475 -623 C ATOM 1439 O ILE A 242 67.649 -11.203 13.347 1.00 71.54 O ANISOU 1439 O ILE A 242 10294 8773 8115 -605 -546 -660 O ATOM 1440 CB ILE A 242 65.766 -12.969 11.428 1.00 71.28 C ANISOU 1440 CB ILE A 242 10364 8667 8051 -514 -580 -427 C ATOM 1441 CG1 ILE A 242 66.776 -13.369 10.327 1.00 72.52 C ANISOU 1441 CG1 ILE A 242 10521 8756 8276 -530 -548 -456 C ATOM 1442 CG2 ILE A 242 64.335 -13.395 11.067 1.00 71.96 C ANISOU 1442 CG2 ILE A 242 10495 8749 8096 -471 -606 -329 C ATOM 1443 CD1 ILE A 242 66.764 -14.899 9.909 1.00 83.42 C ANISOU 1443 CD1 ILE A 242 11884 10143 9667 -500 -625 -385 C ATOM 1444 N ILE A 243 68.075 -10.448 11.253 1.00 65.31 N ANISOU 1444 N ILE A 243 9596 7811 7409 -641 -374 -691 N ATOM 1445 CA ILE A 243 69.421 -10.001 11.625 1.00 65.04 C ANISOU 1445 CA ILE A 243 9476 7785 7450 -708 -342 -824 C ATOM 1446 C ILE A 243 69.293 -8.727 12.499 1.00 68.35 C ANISOU 1446 C ILE A 243 9913 8216 7840 -743 -302 -896 C ATOM 1447 O ILE A 243 69.845 -8.709 13.592 1.00 68.51 O ANISOU 1447 O ILE A 243 9846 8319 7867 -762 -373 -970 O ATOM 1448 CB ILE A 243 70.376 -9.787 10.407 1.00 68.09 C ANISOU 1448 CB ILE A 243 9875 8067 7927 -762 -219 -890 C ATOM 1449 CG1 ILE A 243 70.803 -11.166 9.847 1.00 68.13 C ANISOU 1449 CG1 ILE A 243 9824 8086 7976 -730 -277 -851 C ATOM 1450 CG2 ILE A 243 71.630 -8.982 10.808 1.00 69.42 C ANISOU 1450 CG2 ILE A 243 9953 8233 8189 -851 -152 -1053 C ATOM 1451 CD1 ILE A 243 71.811 -11.151 8.690 1.00 76.82 C ANISOU 1451 CD1 ILE A 243 10925 9093 9171 -782 -151 -920 C ATOM 1452 N VAL A 244 68.534 -7.718 12.053 1.00 64.01 N ANISOU 1452 N VAL A 244 9485 7585 7253 -740 -204 -875 N ATOM 1453 CA VAL A 244 68.352 -6.448 12.771 1.00 64.18 C ANISOU 1453 CA VAL A 244 9544 7595 7245 -769 -150 -942 C ATOM 1454 C VAL A 244 67.734 -6.714 14.173 1.00 68.95 C ANISOU 1454 C VAL A 244 10103 8320 7775 -731 -260 -917 C ATOM 1455 O VAL A 244 68.264 -6.206 15.160 1.00 68.76 O ANISOU 1455 O VAL A 244 10034 8343 7749 -773 -277 -1013 O ATOM 1456 CB VAL A 244 67.484 -5.450 11.946 1.00 67.29 C ANISOU 1456 CB VAL A 244 10099 7868 7601 -741 -39 -901 C ATOM 1457 CG1 VAL A 244 67.056 -4.239 12.766 1.00 67.03 C ANISOU 1457 CG1 VAL A 244 10115 7827 7527 -748 6 -952 C ATOM 1458 CG2 VAL A 244 68.219 -5.006 10.685 1.00 67.65 C ANISOU 1458 CG2 VAL A 244 10226 7776 7701 -794 95 -941 C ATOM 1459 N CYS A 245 66.669 -7.534 14.263 1.00 65.98 N ANISOU 1459 N CYS A 245 9740 7992 7339 -659 -330 -799 N ATOM 1460 CA CYS A 245 65.988 -7.792 15.534 1.00 66.49 C ANISOU 1460 CA CYS A 245 9785 8155 7324 -630 -403 -768 C ATOM 1461 C CYS A 245 66.934 -8.429 16.557 1.00 69.64 C ANISOU 1461 C CYS A 245 10100 8645 7714 -651 -508 -822 C ATOM 1462 O CYS A 245 67.024 -7.909 17.668 1.00 70.01 O ANISOU 1462 O CYS A 245 10147 8742 7710 -667 -528 -884 O ATOM 1463 CB CYS A 245 64.758 -8.666 15.336 1.00 66.82 C ANISOU 1463 CB CYS A 245 9844 8221 7324 -566 -443 -642 C ATOM 1464 SG CYS A 245 63.349 -7.795 14.615 1.00 70.94 S ANISOU 1464 SG CYS A 245 10453 8669 7834 -512 -360 -595 S ATOM 1465 N TYR A 246 67.614 -9.535 16.211 1.00 65.00 N ANISOU 1465 N TYR A 246 9450 8077 7171 -643 -582 -801 N ATOM 1466 CA TYR A 246 68.477 -10.204 17.176 1.00 65.15 C ANISOU 1466 CA TYR A 246 9396 8180 7177 -638 -706 -848 C ATOM 1467 C TYR A 246 69.751 -9.372 17.490 1.00 68.97 C ANISOU 1467 C TYR A 246 9808 8669 7731 -698 -701 -1011 C ATOM 1468 O TYR A 246 70.198 -9.398 18.640 1.00 69.08 O ANISOU 1468 O TYR A 246 9789 8758 7700 -694 -802 -1075 O ATOM 1469 CB TYR A 246 68.880 -11.611 16.715 1.00 66.29 C ANISOU 1469 CB TYR A 246 9495 8335 7357 -600 -789 -788 C ATOM 1470 CG TYR A 246 67.736 -12.605 16.702 1.00 67.89 C ANISOU 1470 CG TYR A 246 9758 8550 7487 -550 -819 -642 C ATOM 1471 CD1 TYR A 246 66.963 -12.821 17.842 1.00 70.32 C ANISOU 1471 CD1 TYR A 246 10118 8918 7684 -528 -861 -591 C ATOM 1472 CD2 TYR A 246 67.556 -13.474 15.630 1.00 68.14 C ANISOU 1472 CD2 TYR A 246 9792 8535 7563 -530 -814 -566 C ATOM 1473 CE1 TYR A 246 65.931 -13.760 17.852 1.00 70.91 C ANISOU 1473 CE1 TYR A 246 10241 8999 7705 -499 -872 -469 C ATOM 1474 CE2 TYR A 246 66.541 -14.434 15.635 1.00 68.71 C ANISOU 1474 CE2 TYR A 246 9910 8616 7580 -497 -844 -446 C ATOM 1475 CZ TYR A 246 65.737 -14.582 16.755 1.00 76.02 C ANISOU 1475 CZ TYR A 246 10878 9597 8407 -486 -869 -399 C ATOM 1476 OH TYR A 246 64.728 -15.522 16.768 1.00 75.10 O ANISOU 1476 OH TYR A 246 10802 9484 8249 -470 -877 -292 O ATOM 1477 N THR A 247 70.306 -8.618 16.513 1.00 65.30 N ANISOU 1477 N THR A 247 9326 8117 7367 -758 -584 -1085 N ATOM 1478 CA THR A 247 71.501 -7.797 16.779 1.00 66.01 C ANISOU 1478 CA THR A 247 9336 8204 7542 -835 -560 -1256 C ATOM 1479 C THR A 247 71.143 -6.709 17.801 1.00 70.11 C ANISOU 1479 C THR A 247 9908 8744 7988 -862 -545 -1317 C ATOM 1480 O THR A 247 71.824 -6.617 18.822 1.00 70.57 O ANISOU 1480 O THR A 247 9899 8876 8038 -877 -643 -1421 O ATOM 1481 CB THR A 247 72.113 -7.194 15.501 1.00 72.50 C ANISOU 1481 CB THR A 247 10152 8912 8483 -908 -403 -1320 C ATOM 1482 OG1 THR A 247 71.085 -6.557 14.750 1.00 73.29 O ANISOU 1482 OG1 THR A 247 10398 8915 8533 -900 -278 -1233 O ATOM 1483 CG2 THR A 247 72.801 -8.235 14.628 1.00 68.85 C ANISOU 1483 CG2 THR A 247 9612 8438 8111 -894 -418 -1307 C ATOM 1484 N LEU A 248 70.023 -5.965 17.581 1.00 66.22 N ANISOU 1484 N LEU A 248 9538 8190 7432 -852 -440 -1249 N ATOM 1485 CA LEU A 248 69.540 -4.916 18.501 1.00 66.59 C ANISOU 1485 CA LEU A 248 9653 8245 7405 -868 -408 -1298 C ATOM 1486 C LEU A 248 69.187 -5.494 19.878 1.00 73.43 C ANISOU 1486 C LEU A 248 10519 9228 8153 -818 -542 -1271 C ATOM 1487 O LEU A 248 69.335 -4.800 20.889 1.00 75.02 O ANISOU 1487 O LEU A 248 10739 9462 8302 -844 -560 -1361 O ATOM 1488 CB LEU A 248 68.308 -4.171 17.937 1.00 65.40 C ANISOU 1488 CB LEU A 248 9629 8007 7213 -839 -282 -1218 C ATOM 1489 CG LEU A 248 68.479 -3.323 16.668 1.00 69.09 C ANISOU 1489 CG LEU A 248 10162 8332 7756 -879 -132 -1242 C ATOM 1490 CD1 LEU A 248 67.155 -2.741 16.234 1.00 68.19 C ANISOU 1490 CD1 LEU A 248 10178 8147 7584 -814 -54 -1151 C ATOM 1491 CD2 LEU A 248 69.489 -2.202 16.863 1.00 72.26 C ANISOU 1491 CD2 LEU A 248 10553 8680 8222 -984 -50 -1406 C ATOM 1492 N MET A 249 68.720 -6.758 19.911 1.00 69.70 N ANISOU 1492 N MET A 249 10043 8807 7632 -750 -627 -1147 N ATOM 1493 CA MET A 249 68.358 -7.469 21.132 1.00 69.93 C ANISOU 1493 CA MET A 249 10102 8929 7538 -701 -741 -1100 C ATOM 1494 C MET A 249 69.596 -7.696 22.005 1.00 74.58 C ANISOU 1494 C MET A 249 10623 9590 8124 -710 -884 -1215 C ATOM 1495 O MET A 249 69.553 -7.407 23.203 1.00 74.81 O ANISOU 1495 O MET A 249 10703 9674 8048 -705 -943 -1263 O ATOM 1496 CB MET A 249 67.697 -8.802 20.772 1.00 71.48 C ANISOU 1496 CB MET A 249 10312 9140 7706 -641 -781 -949 C ATOM 1497 CG MET A 249 67.178 -9.567 21.956 1.00 75.70 C ANISOU 1497 CG MET A 249 10911 9748 8103 -596 -865 -882 C ATOM 1498 SD MET A 249 66.673 -11.241 21.504 1.00 79.31 S ANISOU 1498 SD MET A 249 11378 10209 8548 -543 -917 -724 S ATOM 1499 CE MET A 249 68.254 -11.966 21.151 1.00 76.52 C ANISOU 1499 CE MET A 249 10923 9866 8284 -528 -1049 -788 C ATOM 1500 N ILE A 250 70.696 -8.201 21.396 1.00 71.34 N ANISOU 1500 N ILE A 250 10099 9177 7830 -719 -942 -1268 N ATOM 1501 CA ILE A 250 71.967 -8.460 22.083 1.00 72.84 C ANISOU 1501 CA ILE A 250 10190 9434 8050 -715 -1095 -1395 C ATOM 1502 C ILE A 250 72.596 -7.124 22.518 1.00 78.06 C ANISOU 1502 C ILE A 250 10816 10092 8754 -798 -1061 -1574 C ATOM 1503 O ILE A 250 73.049 -7.014 23.659 1.00 78.94 O ANISOU 1503 O ILE A 250 10922 10274 8798 -787 -1191 -1665 O ATOM 1504 CB ILE A 250 72.943 -9.284 21.199 1.00 76.09 C ANISOU 1504 CB ILE A 250 10471 9836 8603 -703 -1141 -1418 C ATOM 1505 CG1 ILE A 250 72.332 -10.659 20.833 1.00 75.35 C ANISOU 1505 CG1 ILE A 250 10426 9743 8460 -621 -1184 -1245 C ATOM 1506 CG2 ILE A 250 74.313 -9.455 21.896 1.00 78.86 C ANISOU 1506 CG2 ILE A 250 10691 10260 9011 -692 -1310 -1577 C ATOM 1507 CD1 ILE A 250 73.179 -11.523 19.881 1.00 80.43 C ANISOU 1507 CD1 ILE A 250 10957 10364 9237 -601 -1213 -1255 C ATOM 1508 N LEU A 251 72.596 -6.112 21.620 1.00 74.31 N ANISOU 1508 N LEU A 251 10333 9523 8378 -880 -887 -1622 N ATOM 1509 CA LEU A 251 73.139 -4.775 21.885 1.00 75.07 C ANISOU 1509 CA LEU A 251 10408 9588 8527 -976 -817 -1791 C ATOM 1510 C LEU A 251 72.500 -4.168 23.149 1.00 79.78 C ANISOU 1510 C LEU A 251 11117 10226 8971 -964 -850 -1806 C ATOM 1511 O LEU A 251 73.210 -3.553 23.945 1.00 80.69 O ANISOU 1511 O LEU A 251 11194 10376 9090 -1012 -913 -1964 O ATOM 1512 CB LEU A 251 72.917 -3.852 20.677 1.00 74.39 C ANISOU 1512 CB LEU A 251 10364 9369 8531 -1049 -600 -1791 C ATOM 1513 N ARG A 252 71.176 -4.393 23.348 1.00 75.68 N ANISOU 1513 N ARG A 252 10728 9705 8321 -900 -810 -1651 N ATOM 1514 CA ARG A 252 70.422 -3.935 24.516 1.00 76.07 C ANISOU 1514 CA ARG A 252 10897 9790 8217 -880 -818 -1647 C ATOM 1515 C ARG A 252 70.940 -4.612 25.794 1.00 80.56 C ANISOU 1515 C ARG A 252 11465 10467 8676 -835 -1017 -1690 C ATOM 1516 O ARG A 252 71.144 -3.938 26.809 1.00 81.30 O ANISOU 1516 O ARG A 252 11606 10592 8692 -859 -1061 -1800 O ATOM 1517 CB ARG A 252 68.909 -4.213 24.335 1.00 75.78 C ANISOU 1517 CB ARG A 252 10970 9731 8093 -819 -725 -1473 C ATOM 1518 CG ARG A 252 68.047 -3.962 25.596 1.00 88.32 C ANISOU 1518 CG ARG A 252 12682 11363 9514 -789 -724 -1455 C ATOM 1519 CD ARG A 252 68.064 -2.534 26.116 1.00 99.73 C ANISOU 1519 CD ARG A 252 14182 12772 10939 -844 -644 -1584 C ATOM 1520 NE ARG A 252 67.389 -1.613 25.208 1.00110.51 N ANISOU 1520 NE ARG A 252 15578 14032 12378 -860 -467 -1563 N ATOM 1521 CZ ARG A 252 66.103 -1.290 25.298 1.00127.58 C ANISOU 1521 CZ ARG A 252 17828 16166 14478 -814 -361 -1483 C ATOM 1522 NH1 ARG A 252 65.348 -1.802 26.266 1.00115.20 N ANISOU 1522 NH1 ARG A 252 16325 14669 12778 -767 -389 -1421 N ATOM 1523 NH2 ARG A 252 65.562 -0.446 24.429 1.00115.81 N ANISOU 1523 NH2 ARG A 252 16369 14574 13058 -813 -223 -1470 N ATOM 1524 N LEU A 253 71.135 -5.936 25.738 1.00 76.47 N ANISOU 1524 N LEU A 253 10914 9998 8144 -765 -1140 -1602 N ATOM 1525 CA LEU A 253 71.598 -6.727 26.871 1.00 77.60 C ANISOU 1525 CA LEU A 253 11084 10232 8170 -699 -1343 -1620 C ATOM 1526 C LEU A 253 73.062 -6.408 27.188 1.00 85.21 C ANISOU 1526 C LEU A 253 11916 11239 9223 -730 -1485 -1820 C ATOM 1527 O LEU A 253 73.428 -6.386 28.366 1.00 86.52 O ANISOU 1527 O LEU A 253 12130 11471 9273 -699 -1637 -1901 O ATOM 1528 CB LEU A 253 71.420 -8.230 26.592 1.00 76.70 C ANISOU 1528 CB LEU A 253 10976 10135 8030 -614 -1423 -1469 C ATOM 1529 CG LEU A 253 69.975 -8.727 26.380 1.00 79.43 C ANISOU 1529 CG LEU A 253 11442 10450 8289 -585 -1304 -1279 C ATOM 1530 CD1 LEU A 253 69.957 -10.129 25.847 1.00 78.60 C ANISOU 1530 CD1 LEU A 253 11317 10342 8204 -524 -1365 -1154 C ATOM 1531 CD2 LEU A 253 69.146 -8.628 27.655 1.00 81.98 C ANISOU 1531 CD2 LEU A 253 11933 10806 8411 -562 -1302 -1240 C ATOM 1532 N LYS A 254 73.885 -6.104 26.154 1.00 83.05 N ANISOU 1532 N LYS A 254 11479 10924 9152 -794 -1428 -1912 N ATOM 1533 CA LYS A 254 75.295 -5.736 26.350 1.00 85.21 C ANISOU 1533 CA LYS A 254 11591 11235 9551 -841 -1539 -2127 C ATOM 1534 C LYS A 254 75.385 -4.382 27.062 1.00 91.89 C ANISOU 1534 C LYS A 254 12474 12073 10366 -927 -1499 -2280 C ATOM 1535 O LYS A 254 76.338 -4.137 27.802 1.00 93.21 O ANISOU 1535 O LYS A 254 12560 12302 10554 -943 -1651 -2458 O ATOM 1536 CB LYS A 254 76.063 -5.704 25.019 1.00 87.14 C ANISOU 1536 CB LYS A 254 11662 11422 10026 -906 -1440 -2187 C ATOM 1537 N SER A 255 74.341 -3.549 26.898 1.00 88.78 N ANISOU 1537 N SER A 255 12214 11606 9913 -971 -1308 -2211 N ATOM 1538 CA SER A 255 74.226 -2.240 27.526 1.00 90.21 C ANISOU 1538 CA SER A 255 12465 11760 10050 -1047 -1239 -2333 C ATOM 1539 C SER A 255 73.413 -2.342 28.846 1.00 95.31 C ANISOU 1539 C SER A 255 13291 12463 10459 -976 -1315 -2274 C ATOM 1540 O SER A 255 72.423 -1.625 29.030 1.00 94.84 O ANISOU 1540 O SER A 255 13366 12354 10314 -991 -1170 -2224 O ATOM 1541 CB SER A 255 73.584 -1.250 26.558 1.00 93.21 C ANISOU 1541 CB SER A 255 12896 12015 10506 -1122 -984 -2298 C ATOM 1542 OG SER A 255 74.368 -1.117 25.382 1.00102.60 O ANISOU 1542 OG SER A 255 13948 13140 11895 -1195 -899 -2360 O ATOM 1543 N VAL A 256 73.839 -3.254 29.753 1.00 92.87 N ANISOU 1543 N VAL A 256 12992 12252 10042 -892 -1540 -2279 N ATOM 1544 CA VAL A 256 73.234 -3.470 31.078 1.00 93.54 C ANISOU 1544 CA VAL A 256 13266 12391 9885 -823 -1630 -2232 C ATOM 1545 C VAL A 256 74.372 -3.510 32.119 1.00101.20 C ANISOU 1545 C VAL A 256 14201 13447 10805 -801 -1882 -2411 C ATOM 1546 O VAL A 256 75.311 -4.303 31.976 1.00101.68 O ANISOU 1546 O VAL A 256 14130 13559 10945 -751 -2060 -2453 O ATOM 1547 CB VAL A 256 72.326 -4.737 31.153 1.00 95.93 C ANISOU 1547 CB VAL A 256 13686 12710 10054 -718 -1640 -2008 C ATOM 1548 CG1 VAL A 256 71.857 -5.006 32.584 1.00 96.95 C ANISOU 1548 CG1 VAL A 256 14023 12888 9925 -653 -1734 -1976 C ATOM 1549 CG2 VAL A 256 71.126 -4.621 30.217 1.00 93.60 C ANISOU 1549 CG2 VAL A 256 13423 12338 9805 -738 -1405 -1853 C ATOM 1550 N ARG A 257 74.288 -2.631 33.148 1.00 99.36 N ANISOU 1550 N ARG A 257 14082 13227 10445 -834 -1902 -2524 N ATOM 1551 CA ARG A 257 75.277 -2.512 34.219 1.00121.69 C ANISOU 1551 CA ARG A 257 16900 16133 13204 -816 -2147 -2711 C ATOM 1552 C ARG A 257 74.590 -2.427 35.580 1.00144.96 C ANISOU 1552 C ARG A 257 20107 19107 15864 -761 -2196 -2680 C ATOM 1553 O ARG A 257 74.506 -3.424 36.296 1.00105.92 O ANISOU 1553 O ARG A 257 15290 14214 10741 -646 -2356 -2591 O ATOM 1554 CB ARG A 257 76.163 -1.279 33.992 1.00122.46 C ANISOU 1554 CB ARG A 257 16837 16208 13482 -949 -2117 -2953 C ATOM 1555 N SER A 262 77.845 -9.155 37.713 1.00129.06 N ANISOU 1555 N SER A 262 18202 17400 13434 23 -3626 -2484 N ATOM 1556 CA SER A 262 78.562 -8.904 36.465 1.00127.81 C ANISOU 1556 CA SER A 262 17704 17243 13613 -56 -3562 -2586 C ATOM 1557 C SER A 262 78.759 -10.198 35.656 1.00130.22 C ANISOU 1557 C SER A 262 17922 17533 14023 39 -3602 -2452 C ATOM 1558 O SER A 262 78.785 -10.145 34.425 1.00127.88 O ANISOU 1558 O SER A 262 17430 17200 13959 -39 -3428 -2430 O ATOM 1559 CB SER A 262 79.918 -8.265 36.750 1.00133.75 C ANISOU 1559 CB SER A 262 18236 18072 14511 -73 -3782 -2877 C ATOM 1560 N ARG A 263 78.904 -11.351 36.351 1.00127.88 N ANISOU 1560 N ARG A 263 17790 17253 13545 212 -3830 -2365 N ATOM 1561 CA ARG A 263 79.116 -12.668 35.735 1.00127.03 C ANISOU 1561 CA ARG A 263 17637 17123 13506 325 -3897 -2239 C ATOM 1562 C ARG A 263 77.817 -13.233 35.135 1.00128.22 C ANISOU 1562 C ARG A 263 17938 17187 13595 288 -3629 -1976 C ATOM 1563 O ARG A 263 77.881 -13.953 34.136 1.00126.49 O ANISOU 1563 O ARG A 263 17598 16932 13529 304 -3568 -1891 O ATOM 1564 CB ARG A 263 79.679 -13.662 36.761 1.00129.59 C ANISOU 1564 CB ARG A 263 18124 17481 13634 531 -4236 -2236 C ATOM 1565 N GLU A 264 76.649 -12.923 35.755 1.00123.84 N ANISOU 1565 N GLU A 264 17641 16596 12818 240 -3472 -1857 N ATOM 1566 CA GLU A 264 75.321 -13.376 35.314 1.00121.08 C ANISOU 1566 CA GLU A 264 17435 16168 12402 195 -3214 -1626 C ATOM 1567 C GLU A 264 74.980 -12.792 33.935 1.00121.24 C ANISOU 1567 C GLU A 264 17234 16156 12677 58 -2958 -1619 C ATOM 1568 O GLU A 264 74.446 -13.509 33.084 1.00119.24 O ANISOU 1568 O GLU A 264 16965 15849 12492 55 -2832 -1467 O ATOM 1569 CB GLU A 264 74.242 -12.983 36.343 1.00122.80 C ANISOU 1569 CB GLU A 264 17943 16364 12350 163 -3098 -1550 C ATOM 1570 N LYS A 265 75.308 -11.499 33.715 1.00116.65 N ANISOU 1570 N LYS A 265 16496 15597 12230 -52 -2888 -1787 N ATOM 1571 CA LYS A 265 75.069 -10.805 32.448 1.00114.03 C ANISOU 1571 CA LYS A 265 15979 15223 12126 -180 -2653 -1799 C ATOM 1572 C LYS A 265 75.873 -11.463 31.329 1.00116.63 C ANISOU 1572 C LYS A 265 16086 15546 12683 -155 -2696 -1814 C ATOM 1573 O LYS A 265 75.307 -11.789 30.284 1.00114.44 O ANISOU 1573 O LYS A 265 15771 15210 12500 -190 -2524 -1688 O ATOM 1574 CB LYS A 265 75.426 -9.312 32.567 1.00116.89 C ANISOU 1574 CB LYS A 265 16242 15601 12570 -294 -2595 -1995 C ATOM 1575 N ASP A 266 77.173 -11.724 31.588 1.00114.19 N ANISOU 1575 N ASP A 266 15638 15296 12453 -84 -2938 -1969 N ATOM 1576 CA ASP A 266 78.116 -12.343 30.652 1.00113.60 C ANISOU 1576 CA ASP A 266 15334 15224 12603 -48 -3005 -2020 C ATOM 1577 C ASP A 266 77.738 -13.804 30.350 1.00115.85 C ANISOU 1577 C ASP A 266 15719 15471 12826 66 -3037 -1820 C ATOM 1578 O ASP A 266 77.974 -14.271 29.232 1.00114.33 O ANISOU 1578 O ASP A 266 15382 15245 12813 58 -2962 -1789 O ATOM 1579 CB ASP A 266 79.546 -12.285 31.220 1.00117.87 C ANISOU 1579 CB ASP A 266 15712 15849 13225 20 -3284 -2249 C ATOM 1580 CG ASP A 266 80.074 -10.886 31.513 1.00127.22 C ANISOU 1580 CG ASP A 266 16772 17072 14495 -99 -3272 -2478 C ATOM 1581 OD1 ASP A 266 79.292 -9.912 31.397 1.00125.46 O ANISOU 1581 OD1 ASP A 266 16625 16806 14240 -227 -3051 -2452 O ATOM 1582 OD2 ASP A 266 81.259 -10.768 31.888 1.00136.18 O ANISOU 1582 OD2 ASP A 266 17736 18277 15730 -62 -3490 -2689 O ATOM 1583 N ARG A 267 77.159 -14.518 31.344 1.00112.14 N ANISOU 1583 N ARG A 267 15511 14998 12098 167 -3137 -1687 N ATOM 1584 CA ARG A 267 76.718 -15.911 31.201 1.00110.74 C ANISOU 1584 CA ARG A 267 15474 14771 11832 269 -3160 -1491 C ATOM 1585 C ARG A 267 75.530 -15.993 30.242 1.00109.49 C ANISOU 1585 C ARG A 267 15351 14537 11713 170 -2874 -1320 C ATOM 1586 O ARG A 267 75.518 -16.856 29.365 1.00107.40 O ANISOU 1586 O ARG A 267 15030 14228 11548 198 -2836 -1229 O ATOM 1587 CB ARG A 267 76.352 -16.516 32.567 1.00113.03 C ANISOU 1587 CB ARG A 267 16067 15060 11818 381 -3309 -1400 C ATOM 1588 N ASN A 268 74.546 -15.077 30.392 1.00104.03 N ANISOU 1588 N ASN A 268 14743 13831 10951 59 -2678 -1289 N ATOM 1589 CA ASN A 268 73.388 -15.019 29.505 1.00101.21 C ANISOU 1589 CA ASN A 268 14404 13411 10640 -31 -2419 -1151 C ATOM 1590 C ASN A 268 73.798 -14.504 28.128 1.00102.60 C ANISOU 1590 C ASN A 268 14341 13567 11074 -112 -2304 -1224 C ATOM 1591 O ASN A 268 73.432 -15.122 27.132 1.00101.14 O ANISOU 1591 O ASN A 268 14122 13331 10977 -119 -2205 -1117 O ATOM 1592 CB ASN A 268 72.260 -14.150 30.079 1.00101.29 C ANISOU 1592 CB ASN A 268 14559 13414 10514 -111 -2254 -1114 C ATOM 1593 CG ASN A 268 71.587 -14.704 31.314 1.00118.34 C ANISOU 1593 CG ASN A 268 16987 15571 12407 -53 -2296 -1010 C ATOM 1594 OD1 ASN A 268 72.234 -15.150 32.266 1.00108.81 O ANISOU 1594 OD1 ASN A 268 15885 14395 11063 45 -2506 -1046 O ATOM 1595 ND2 ASN A 268 70.260 -14.624 31.350 1.00109.44 N ANISOU 1595 ND2 ASN A 268 15982 14404 11196 -113 -2090 -888 N ATOM 1596 N LEU A 269 74.591 -13.401 28.069 1.00 98.19 N ANISOU 1596 N LEU A 269 13628 13042 10636 -175 -2315 -1413 N ATOM 1597 CA LEU A 269 75.055 -12.805 26.806 1.00 96.08 C ANISOU 1597 CA LEU A 269 13154 12745 10608 -264 -2187 -1499 C ATOM 1598 C LEU A 269 75.771 -13.845 25.934 1.00 97.04 C ANISOU 1598 C LEU A 269 13146 12851 10875 -203 -2251 -1483 C ATOM 1599 O LEU A 269 75.459 -13.932 24.751 1.00 94.64 O ANISOU 1599 O LEU A 269 12787 12486 10685 -253 -2091 -1418 O ATOM 1600 CB LEU A 269 75.985 -11.609 27.055 1.00 97.38 C ANISOU 1600 CB LEU A 269 13178 12947 10874 -336 -2220 -1725 C ATOM 1601 N ARG A 270 76.676 -14.665 26.525 1.00 93.70 N ANISOU 1601 N ARG A 270 12690 12477 10435 -85 -2489 -1536 N ATOM 1602 CA ARG A 270 77.404 -15.712 25.800 1.00 92.90 C ANISOU 1602 CA ARG A 270 12469 12362 10468 -6 -2567 -1529 C ATOM 1603 C ARG A 270 76.434 -16.781 25.255 1.00 93.50 C ANISOU 1603 C ARG A 270 12685 12368 10473 28 -2476 -1307 C ATOM 1604 O ARG A 270 76.495 -17.095 24.066 1.00 91.98 O ANISOU 1604 O ARG A 270 12397 12125 10427 0 -2365 -1276 O ATOM 1605 CB ARG A 270 78.463 -16.367 26.696 1.00 95.18 C ANISOU 1605 CB ARG A 270 12722 12715 10726 138 -2862 -1626 C ATOM 1606 N ARG A 271 75.513 -17.286 26.109 1.00 88.63 N ANISOU 1606 N ARG A 271 12302 11742 9633 75 -2505 -1160 N ATOM 1607 CA ARG A 271 74.518 -18.310 25.761 1.00 86.58 C ANISOU 1607 CA ARG A 271 12192 11415 9291 97 -2420 -955 C ATOM 1608 C ARG A 271 73.555 -17.830 24.663 1.00 87.32 C ANISOU 1608 C ARG A 271 12258 11455 9466 -24 -2168 -882 C ATOM 1609 O ARG A 271 73.253 -18.591 23.741 1.00 86.33 O ANISOU 1609 O ARG A 271 12123 11273 9405 -20 -2099 -785 O ATOM 1610 CB ARG A 271 73.709 -18.718 27.000 1.00 86.98 C ANISOU 1610 CB ARG A 271 12500 11464 9084 143 -2468 -839 C ATOM 1611 N ILE A 272 73.081 -16.576 24.762 1.00 82.18 N ANISOU 1611 N ILE A 272 11601 10818 8807 -122 -2042 -934 N ATOM 1612 CA ILE A 272 72.138 -15.991 23.807 1.00 80.03 C ANISOU 1612 CA ILE A 272 11316 10493 8596 -220 -1821 -875 C ATOM 1613 C ILE A 272 72.863 -15.709 22.476 1.00 82.81 C ANISOU 1613 C ILE A 272 11488 10812 9162 -264 -1751 -956 C ATOM 1614 O ILE A 272 72.333 -16.086 21.435 1.00 80.81 O ANISOU 1614 O ILE A 272 11237 10500 8967 -285 -1640 -864 O ATOM 1615 CB ILE A 272 71.475 -14.711 24.386 1.00 83.15 C ANISOU 1615 CB ILE A 272 11771 10907 8916 -294 -1718 -915 C ATOM 1616 CG1 ILE A 272 70.658 -15.066 25.660 1.00 84.20 C ANISOU 1616 CG1 ILE A 272 12101 11063 8829 -256 -1755 -824 C ATOM 1617 CG2 ILE A 272 70.575 -14.024 23.332 1.00 82.33 C ANISOU 1617 CG2 ILE A 272 11645 10745 8891 -377 -1506 -870 C ATOM 1618 CD1 ILE A 272 70.169 -13.905 26.484 1.00 90.89 C ANISOU 1618 CD1 ILE A 272 13020 11936 9579 -308 -1687 -882 C ATOM 1619 N THR A 273 74.067 -15.083 22.507 1.00 80.32 N ANISOU 1619 N THR A 273 11024 10531 8963 -281 -1812 -1133 N ATOM 1620 CA THR A 273 74.831 -14.769 21.288 1.00 79.72 C ANISOU 1620 CA THR A 273 10781 10416 9092 -335 -1722 -1227 C ATOM 1621 C THR A 273 75.106 -16.066 20.510 1.00 82.97 C ANISOU 1621 C THR A 273 11159 10795 9573 -266 -1759 -1152 C ATOM 1622 O THR A 273 74.848 -16.096 19.308 1.00 80.79 O ANISOU 1622 O THR A 273 10863 10450 9383 -312 -1615 -1107 O ATOM 1623 CB THR A 273 76.129 -14.020 21.621 1.00 89.74 C ANISOU 1623 CB THR A 273 11885 11734 10478 -364 -1796 -1443 C ATOM 1624 OG1 THR A 273 75.791 -12.820 22.315 1.00 89.75 O ANISOU 1624 OG1 THR A 273 11938 11755 10407 -434 -1750 -1506 O ATOM 1625 CG2 THR A 273 76.942 -13.661 20.378 1.00 89.06 C ANISOU 1625 CG2 THR A 273 11629 11599 10609 -437 -1672 -1552 C ATOM 1626 N ARG A 274 75.558 -17.141 21.202 1.00 81.50 N ANISOU 1626 N ARG A 274 10991 10645 9331 -149 -1953 -1132 N ATOM 1627 CA ARG A 274 75.797 -18.448 20.578 1.00 81.68 C ANISOU 1627 CA ARG A 274 11003 10629 9404 -70 -2000 -1057 C ATOM 1628 C ARG A 274 74.521 -18.958 19.903 1.00 84.39 C ANISOU 1628 C ARG A 274 11483 10901 9680 -98 -1865 -873 C ATOM 1629 O ARG A 274 74.571 -19.351 18.739 1.00 82.99 O ANISOU 1629 O ARG A 274 11259 10665 9608 -114 -1777 -845 O ATOM 1630 CB ARG A 274 76.308 -19.492 21.600 1.00 84.18 C ANISOU 1630 CB ARG A 274 11370 10985 9631 74 -2238 -1044 C ATOM 1631 CG ARG A 274 77.745 -19.335 22.149 1.00100.63 C ANISOU 1631 CG ARG A 274 13287 13139 11809 143 -2427 -1237 C ATOM 1632 CD ARG A 274 78.887 -19.547 21.150 1.00115.55 C ANISOU 1632 CD ARG A 274 14950 15016 13936 154 -2416 -1364 C ATOM 1633 NE ARG A 274 79.168 -18.364 20.333 1.00129.03 N ANISOU 1633 NE ARG A 274 16508 16713 15803 10 -2229 -1488 N ATOM 1634 CZ ARG A 274 80.058 -17.426 20.655 1.00147.11 C ANISOU 1634 CZ ARG A 274 18634 19059 18202 -39 -2263 -1689 C ATOM 1635 NH1 ARG A 274 80.258 -16.387 19.857 1.00133.86 N ANISOU 1635 NH1 ARG A 274 16850 17349 16662 -180 -2066 -1789 N ATOM 1636 NH2 ARG A 274 80.760 -17.527 21.779 1.00136.67 N ANISOU 1636 NH2 ARG A 274 17263 17819 16847 52 -2498 -1795 N ATOM 1637 N LEU A 275 73.372 -18.877 20.612 1.00 81.14 N ANISOU 1637 N LEU A 275 11235 10494 9100 -113 -1838 -761 N ATOM 1638 CA LEU A 275 72.053 -19.310 20.132 1.00 79.90 C ANISOU 1638 CA LEU A 275 11198 10281 8878 -146 -1717 -600 C ATOM 1639 C LEU A 275 71.646 -18.499 18.879 1.00 81.71 C ANISOU 1639 C LEU A 275 11367 10464 9216 -239 -1535 -614 C ATOM 1640 O LEU A 275 71.258 -19.096 17.870 1.00 80.20 O ANISOU 1640 O LEU A 275 11188 10213 9071 -245 -1468 -537 O ATOM 1641 CB LEU A 275 71.021 -19.141 21.273 1.00 80.36 C ANISOU 1641 CB LEU A 275 11415 10366 8754 -156 -1711 -522 C ATOM 1642 CG LEU A 275 69.598 -19.715 21.106 1.00 84.84 C ANISOU 1642 CG LEU A 275 12109 10887 9238 -184 -1606 -363 C ATOM 1643 CD1 LEU A 275 68.926 -19.864 22.460 1.00 86.23 C ANISOU 1643 CD1 LEU A 275 12446 11089 9228 -170 -1633 -301 C ATOM 1644 CD2 LEU A 275 68.718 -18.882 20.131 1.00 85.69 C ANISOU 1644 CD2 LEU A 275 12175 10965 9418 -272 -1430 -351 C ATOM 1645 N VAL A 276 71.754 -17.147 18.955 1.00 77.40 N ANISOU 1645 N VAL A 276 10770 9938 8700 -307 -1461 -714 N ATOM 1646 CA VAL A 276 71.437 -16.196 17.882 1.00 75.67 C ANISOU 1646 CA VAL A 276 10520 9665 8565 -388 -1292 -739 C ATOM 1647 C VAL A 276 72.274 -16.526 16.644 1.00 79.46 C ANISOU 1647 C VAL A 276 10903 10092 9194 -394 -1252 -785 C ATOM 1648 O VAL A 276 71.707 -16.693 15.564 1.00 77.98 O ANISOU 1648 O VAL A 276 10757 9839 9034 -415 -1151 -713 O ATOM 1649 CB VAL A 276 71.654 -14.725 18.335 1.00 79.47 C ANISOU 1649 CB VAL A 276 10970 10169 9054 -452 -1238 -859 C ATOM 1650 CG1 VAL A 276 71.641 -13.757 17.156 1.00 78.35 C ANISOU 1650 CG1 VAL A 276 10801 9954 9014 -529 -1070 -905 C ATOM 1651 CG2 VAL A 276 70.627 -14.313 19.380 1.00 79.31 C ANISOU 1651 CG2 VAL A 276 11063 10186 8885 -454 -1235 -805 C ATOM 1652 N LEU A 277 73.610 -16.642 16.803 1.00 77.27 N ANISOU 1652 N LEU A 277 10498 9845 9015 -371 -1335 -912 N ATOM 1653 CA LEU A 277 74.517 -16.948 15.696 1.00 77.25 C ANISOU 1653 CA LEU A 277 10389 9796 9168 -378 -1285 -978 C ATOM 1654 C LEU A 277 74.078 -18.220 14.970 1.00 80.20 C ANISOU 1654 C LEU A 277 10827 10117 9527 -324 -1290 -847 C ATOM 1655 O LEU A 277 73.962 -18.200 13.747 1.00 79.32 O ANISOU 1655 O LEU A 277 10727 9932 9479 -362 -1164 -829 O ATOM 1656 CB LEU A 277 75.975 -17.093 16.173 1.00 79.00 C ANISOU 1656 CB LEU A 277 10445 10073 9499 -339 -1406 -1136 C ATOM 1657 CG LEU A 277 76.647 -15.844 16.775 1.00 85.08 C ANISOU 1657 CG LEU A 277 11115 10890 10323 -406 -1402 -1306 C ATOM 1658 CD1 LEU A 277 78.016 -16.176 17.316 1.00 87.43 C ANISOU 1658 CD1 LEU A 277 11237 11254 10728 -348 -1561 -1463 C ATOM 1659 CD2 LEU A 277 76.734 -14.699 15.775 1.00 86.53 C ANISOU 1659 CD2 LEU A 277 11270 11002 10606 -530 -1185 -1379 C ATOM 1660 N VAL A 278 73.750 -19.284 15.727 1.00 76.38 N ANISOU 1660 N VAL A 278 10414 9662 8944 -241 -1427 -752 N ATOM 1661 CA VAL A 278 73.333 -20.581 15.195 1.00 75.35 C ANISOU 1661 CA VAL A 278 10357 9480 8793 -190 -1446 -630 C ATOM 1662 C VAL A 278 72.003 -20.450 14.408 1.00 77.14 C ANISOU 1662 C VAL A 278 10692 9649 8968 -250 -1314 -515 C ATOM 1663 O VAL A 278 71.984 -20.837 13.240 1.00 75.90 O ANISOU 1663 O VAL A 278 10539 9425 8874 -260 -1243 -491 O ATOM 1664 CB VAL A 278 73.205 -21.639 16.326 1.00 80.04 C ANISOU 1664 CB VAL A 278 11034 10106 9271 -96 -1610 -552 C ATOM 1665 CG1 VAL A 278 72.498 -22.904 15.849 1.00 79.24 C ANISOU 1665 CG1 VAL A 278 11043 9939 9127 -65 -1605 -410 C ATOM 1666 CG2 VAL A 278 74.572 -21.980 16.909 1.00 81.53 C ANISOU 1666 CG2 VAL A 278 11116 10340 9523 -6 -1769 -665 C ATOM 1667 N VAL A 279 70.918 -19.907 15.023 1.00 73.20 N ANISOU 1667 N VAL A 279 10277 9176 8360 -284 -1286 -454 N ATOM 1668 CA VAL A 279 69.585 -19.846 14.389 1.00 71.68 C ANISOU 1668 CA VAL A 279 10172 8939 8123 -326 -1188 -352 C ATOM 1669 C VAL A 279 69.666 -19.103 13.025 1.00 74.81 C ANISOU 1669 C VAL A 279 10543 9272 8608 -375 -1060 -397 C ATOM 1670 O VAL A 279 69.089 -19.592 12.048 1.00 73.26 O ANISOU 1670 O VAL A 279 10399 9017 8420 -378 -1017 -329 O ATOM 1671 CB VAL A 279 68.457 -19.223 15.273 1.00 75.12 C ANISOU 1671 CB VAL A 279 10675 9416 8450 -354 -1162 -306 C ATOM 1672 CG1 VAL A 279 68.141 -20.112 16.469 1.00 75.53 C ANISOU 1672 CG1 VAL A 279 10801 9505 8390 -313 -1257 -234 C ATOM 1673 CG2 VAL A 279 68.766 -17.796 15.717 1.00 75.12 C ANISOU 1673 CG2 VAL A 279 10634 9452 8456 -391 -1120 -409 C ATOM 1674 N VAL A 280 70.405 -17.981 12.942 1.00 72.31 N ANISOU 1674 N VAL A 280 10161 8959 8354 -414 -1001 -513 N ATOM 1675 CA VAL A 280 70.495 -17.252 11.674 1.00 71.80 C ANISOU 1675 CA VAL A 280 10108 8817 8355 -463 -865 -551 C ATOM 1676 C VAL A 280 71.462 -18.007 10.746 1.00 75.13 C ANISOU 1676 C VAL A 280 10480 9189 8877 -449 -850 -589 C ATOM 1677 O VAL A 280 71.164 -18.115 9.559 1.00 74.90 O ANISOU 1677 O VAL A 280 10517 9080 8861 -462 -766 -553 O ATOM 1678 CB VAL A 280 70.881 -15.746 11.802 1.00 76.00 C ANISOU 1678 CB VAL A 280 10613 9345 8919 -525 -773 -661 C ATOM 1679 CG1 VAL A 280 69.826 -14.971 12.601 1.00 75.29 C ANISOU 1679 CG1 VAL A 280 10586 9290 8730 -534 -771 -621 C ATOM 1680 CG2 VAL A 280 72.273 -15.551 12.401 1.00 77.03 C ANISOU 1680 CG2 VAL A 280 10610 9522 9136 -538 -815 -801 C ATOM 1681 N ALA A 281 72.566 -18.584 11.291 1.00 71.13 N ANISOU 1681 N ALA A 281 9865 8727 8434 -410 -940 -660 N ATOM 1682 CA ALA A 281 73.537 -19.342 10.493 1.00 71.02 C ANISOU 1682 CA ALA A 281 9786 8670 8528 -386 -927 -709 C ATOM 1683 C ALA A 281 72.850 -20.464 9.732 1.00 72.59 C ANISOU 1683 C ALA A 281 10084 8811 8687 -350 -934 -587 C ATOM 1684 O ALA A 281 73.104 -20.622 8.549 1.00 72.09 O ANISOU 1684 O ALA A 281 10041 8671 8679 -367 -839 -602 O ATOM 1685 CB ALA A 281 74.635 -19.907 11.374 1.00 73.02 C ANISOU 1685 CB ALA A 281 9910 8990 8842 -322 -1064 -791 C ATOM 1686 N VAL A 282 71.915 -21.176 10.388 1.00 67.40 N ANISOU 1686 N VAL A 282 9501 8182 7925 -311 -1032 -470 N ATOM 1687 CA VAL A 282 71.131 -22.255 9.782 1.00 65.69 C ANISOU 1687 CA VAL A 282 9381 7911 7665 -289 -1045 -356 C ATOM 1688 C VAL A 282 70.231 -21.669 8.655 1.00 67.08 C ANISOU 1688 C VAL A 282 9645 8025 7819 -343 -930 -318 C ATOM 1689 O VAL A 282 70.184 -22.242 7.567 1.00 66.14 O ANISOU 1689 O VAL A 282 9577 7833 7722 -339 -890 -295 O ATOM 1690 CB VAL A 282 70.297 -23.011 10.854 1.00 69.17 C ANISOU 1690 CB VAL A 282 9885 8394 8001 -256 -1153 -251 C ATOM 1691 CG1 VAL A 282 69.327 -24.007 10.218 1.00 68.50 C ANISOU 1691 CG1 VAL A 282 9899 8249 7878 -257 -1149 -141 C ATOM 1692 CG2 VAL A 282 71.206 -23.710 11.864 1.00 69.78 C ANISOU 1692 CG2 VAL A 282 9915 8514 8083 -180 -1282 -279 C ATOM 1693 N PHE A 283 69.578 -20.510 8.895 1.00 61.97 N ANISOU 1693 N PHE A 283 9022 7399 7126 -384 -880 -322 N ATOM 1694 CA PHE A 283 68.701 -19.892 7.897 1.00 60.35 C ANISOU 1694 CA PHE A 283 8908 7133 6890 -414 -794 -289 C ATOM 1695 C PHE A 283 69.508 -19.408 6.676 1.00 63.55 C ANISOU 1695 C PHE A 283 9333 7453 7359 -440 -676 -363 C ATOM 1696 O PHE A 283 69.035 -19.536 5.547 1.00 62.66 O ANISOU 1696 O PHE A 283 9321 7264 7223 -440 -629 -325 O ATOM 1697 CB PHE A 283 67.919 -18.723 8.512 1.00 61.68 C ANISOU 1697 CB PHE A 283 9092 7340 7003 -438 -770 -287 C ATOM 1698 CG PHE A 283 66.817 -18.177 7.633 1.00 62.56 C ANISOU 1698 CG PHE A 283 9301 7396 7072 -442 -718 -243 C ATOM 1699 CD1 PHE A 283 65.549 -18.740 7.650 1.00 65.13 C ANISOU 1699 CD1 PHE A 283 9662 7735 7349 -424 -775 -156 C ATOM 1700 CD2 PHE A 283 67.035 -17.075 6.819 1.00 64.41 C ANISOU 1700 CD2 PHE A 283 9595 7561 7317 -463 -613 -294 C ATOM 1701 CE1 PHE A 283 64.522 -18.218 6.860 1.00 65.38 C ANISOU 1701 CE1 PHE A 283 9769 7724 7349 -413 -751 -129 C ATOM 1702 CE2 PHE A 283 66.010 -16.567 6.016 1.00 66.67 C ANISOU 1702 CE2 PHE A 283 9987 7790 7552 -446 -587 -252 C ATOM 1703 CZ PHE A 283 64.764 -17.142 6.042 1.00 64.25 C ANISOU 1703 CZ PHE A 283 9697 7510 7205 -414 -667 -174 C ATOM 1704 N VAL A 284 70.720 -18.873 6.902 1.00 60.69 N ANISOU 1704 N VAL A 284 8881 7102 7076 -465 -626 -474 N ATOM 1705 CA VAL A 284 71.588 -18.366 5.836 1.00 60.99 C ANISOU 1705 CA VAL A 284 8932 7056 7187 -507 -483 -560 C ATOM 1706 C VAL A 284 72.208 -19.555 5.066 1.00 66.05 C ANISOU 1706 C VAL A 284 9562 7650 7883 -476 -482 -563 C ATOM 1707 O VAL A 284 72.095 -19.597 3.846 1.00 65.87 O ANISOU 1707 O VAL A 284 9648 7533 7848 -490 -388 -549 O ATOM 1708 CB VAL A 284 72.684 -17.406 6.384 1.00 65.11 C ANISOU 1708 CB VAL A 284 9337 7606 7795 -558 -421 -697 C ATOM 1709 CG1 VAL A 284 73.726 -17.068 5.316 1.00 65.66 C ANISOU 1709 CG1 VAL A 284 9402 7585 7961 -612 -255 -801 C ATOM 1710 CG2 VAL A 284 72.060 -16.133 6.947 1.00 64.39 C ANISOU 1710 CG2 VAL A 284 9288 7535 7644 -594 -394 -699 C ATOM 1711 N VAL A 285 72.823 -20.520 5.772 1.00 63.44 N ANISOU 1711 N VAL A 285 9120 7378 7605 -427 -589 -579 N ATOM 1712 CA VAL A 285 73.481 -21.682 5.163 1.00 64.02 C ANISOU 1712 CA VAL A 285 9172 7410 7744 -385 -596 -591 C ATOM 1713 C VAL A 285 72.469 -22.478 4.286 1.00 68.90 C ANISOU 1713 C VAL A 285 9941 7960 8279 -367 -606 -475 C ATOM 1714 O VAL A 285 72.855 -22.951 3.222 1.00 68.88 O ANISOU 1714 O VAL A 285 9986 7877 8309 -364 -531 -495 O ATOM 1715 CB VAL A 285 74.144 -22.611 6.237 1.00 68.16 C ANISOU 1715 CB VAL A 285 9571 8011 8318 -311 -746 -612 C ATOM 1716 CG1 VAL A 285 74.649 -23.916 5.634 1.00 68.36 C ANISOU 1716 CG1 VAL A 285 9592 7983 8397 -250 -766 -606 C ATOM 1717 CG2 VAL A 285 75.284 -21.898 6.960 1.00 68.95 C ANISOU 1717 CG2 VAL A 285 9505 8175 8519 -323 -748 -753 C ATOM 1718 N CYS A 286 71.193 -22.570 4.700 1.00 66.09 N ANISOU 1718 N CYS A 286 9657 7633 7820 -361 -687 -369 N ATOM 1719 CA CYS A 286 70.199 -23.395 4.018 1.00 66.39 C ANISOU 1719 CA CYS A 286 9811 7620 7792 -347 -722 -272 C ATOM 1720 C CYS A 286 69.473 -22.644 2.864 1.00 69.73 C ANISOU 1720 C CYS A 286 10367 7970 8156 -379 -635 -256 C ATOM 1721 O CYS A 286 69.184 -23.291 1.852 1.00 70.27 O ANISOU 1721 O CYS A 286 10534 7965 8200 -369 -626 -225 O ATOM 1722 CB CYS A 286 69.177 -23.911 5.022 1.00 67.01 C ANISOU 1722 CB CYS A 286 9892 7764 7805 -331 -843 -180 C ATOM 1723 SG CYS A 286 69.854 -25.074 6.239 1.00 71.90 S ANISOU 1723 SG CYS A 286 10429 8437 8453 -272 -963 -169 S ATOM 1724 N TRP A 287 69.110 -21.351 3.019 1.00 64.58 N ANISOU 1724 N TRP A 287 9734 7333 7472 -409 -586 -272 N ATOM 1725 CA TRP A 287 68.322 -20.684 1.977 1.00 63.71 C ANISOU 1725 CA TRP A 287 9769 7147 7290 -417 -531 -247 C ATOM 1726 C TRP A 287 69.167 -19.932 0.939 1.00 68.56 C ANISOU 1726 C TRP A 287 10466 7662 7921 -447 -373 -321 C ATOM 1727 O TRP A 287 68.759 -19.898 -0.222 1.00 68.45 O ANISOU 1727 O TRP A 287 10609 7557 7844 -438 -333 -297 O ATOM 1728 CB TRP A 287 67.334 -19.694 2.575 1.00 61.94 C ANISOU 1728 CB TRP A 287 9553 6970 7011 -418 -561 -218 C ATOM 1729 CG TRP A 287 66.224 -20.358 3.325 1.00 62.53 C ANISOU 1729 CG TRP A 287 9585 7118 7054 -397 -687 -141 C ATOM 1730 CD1 TRP A 287 66.084 -20.444 4.677 1.00 65.24 C ANISOU 1730 CD1 TRP A 287 9827 7558 7405 -401 -746 -128 C ATOM 1731 CD2 TRP A 287 65.172 -21.153 2.763 1.00 62.22 C ANISOU 1731 CD2 TRP A 287 9608 7058 6976 -378 -761 -76 C ATOM 1732 NE1 TRP A 287 64.953 -21.158 4.992 1.00 64.52 N ANISOU 1732 NE1 TRP A 287 9735 7500 7280 -391 -831 -55 N ATOM 1733 CE2 TRP A 287 64.382 -21.621 3.836 1.00 66.00 C ANISOU 1733 CE2 TRP A 287 10009 7620 7448 -380 -845 -27 C ATOM 1734 CE3 TRP A 287 64.786 -21.474 1.447 1.00 63.61 C ANISOU 1734 CE3 TRP A 287 9905 7148 7115 -361 -763 -60 C ATOM 1735 CZ2 TRP A 287 63.236 -22.402 3.639 1.00 65.35 C ANISOU 1735 CZ2 TRP A 287 9946 7539 7346 -379 -921 29 C ATOM 1736 CZ3 TRP A 287 63.651 -22.244 1.252 1.00 65.08 C ANISOU 1736 CZ3 TRP A 287 10108 7341 7276 -351 -862 -7 C ATOM 1737 CH2 TRP A 287 62.880 -22.686 2.338 1.00 65.62 C ANISOU 1737 CH2 TRP A 287 10078 7496 7360 -364 -935 33 C ATOM 1738 N THR A 288 70.314 -19.333 1.329 1.00 65.85 N ANISOU 1738 N THR A 288 10029 7331 7660 -486 -281 -415 N ATOM 1739 CA THR A 288 71.186 -18.574 0.413 1.00 66.51 C ANISOU 1739 CA THR A 288 10184 7313 7772 -536 -98 -499 C ATOM 1740 C THR A 288 71.592 -19.413 -0.836 1.00 73.12 C ANISOU 1740 C THR A 288 11118 8054 8612 -527 -28 -504 C ATOM 1741 O THR A 288 71.579 -18.836 -1.924 1.00 73.16 O ANISOU 1741 O THR A 288 11294 7944 8557 -550 99 -514 O ATOM 1742 CB THR A 288 72.456 -18.080 1.132 1.00 69.13 C ANISOU 1742 CB THR A 288 10349 7689 8228 -586 -24 -620 C ATOM 1743 OG1 THR A 288 72.083 -17.347 2.298 1.00 66.31 O ANISOU 1743 OG1 THR A 288 9917 7420 7859 -593 -93 -619 O ATOM 1744 CG2 THR A 288 73.355 -17.223 0.246 1.00 66.46 C ANISOU 1744 CG2 THR A 288 10077 7242 7934 -660 194 -719 C ATOM 1745 N PRO A 289 71.936 -20.736 -0.755 1.00 71.34 N ANISOU 1745 N PRO A 289 10812 7856 8439 -491 -101 -497 N ATOM 1746 CA PRO A 289 72.372 -21.440 -1.975 1.00 72.01 C ANISOU 1746 CA PRO A 289 10998 7838 8525 -486 -14 -515 C ATOM 1747 C PRO A 289 71.279 -21.569 -3.031 1.00 76.36 C ANISOU 1747 C PRO A 289 11770 8306 8936 -463 -39 -431 C ATOM 1748 O PRO A 289 71.538 -21.277 -4.200 1.00 76.37 O ANISOU 1748 O PRO A 289 11936 8191 8891 -482 97 -458 O ATOM 1749 CB PRO A 289 72.763 -22.837 -1.468 1.00 73.61 C ANISOU 1749 CB PRO A 289 11069 8096 8804 -436 -123 -510 C ATOM 1750 CG PRO A 289 72.977 -22.688 -0.036 1.00 77.76 C ANISOU 1750 CG PRO A 289 11413 8742 9392 -427 -222 -526 C ATOM 1751 CD PRO A 289 72.041 -21.625 0.422 1.00 72.71 C ANISOU 1751 CD PRO A 289 10818 8140 8670 -451 -251 -480 C ATOM 1752 N ILE A 290 70.073 -22.001 -2.627 1.00 73.09 N ANISOU 1752 N ILE A 290 11364 7949 8457 -423 -208 -338 N ATOM 1753 CA ILE A 290 68.996 -22.289 -3.559 1.00 73.25 C ANISOU 1753 CA ILE A 290 11562 7907 8363 -394 -270 -271 C ATOM 1754 C ILE A 290 68.347 -20.971 -4.070 1.00 76.78 C ANISOU 1754 C ILE A 290 12163 8300 8709 -393 -227 -258 C ATOM 1755 O ILE A 290 68.009 -20.925 -5.252 1.00 76.77 O ANISOU 1755 O ILE A 290 12362 8195 8611 -374 -201 -244 O ATOM 1756 CB ILE A 290 67.934 -23.247 -2.944 1.00 76.18 C ANISOU 1756 CB ILE A 290 11869 8356 8722 -363 -457 -193 C ATOM 1757 CG1 ILE A 290 66.918 -23.712 -4.008 1.00 77.32 C ANISOU 1757 CG1 ILE A 290 12178 8432 8767 -336 -530 -146 C ATOM 1758 CG2 ILE A 290 67.248 -22.697 -1.682 1.00 76.17 C ANISOU 1758 CG2 ILE A 290 11746 8466 8728 -364 -544 -159 C ATOM 1759 CD1 ILE A 290 67.568 -24.406 -5.245 1.00 87.76 C ANISOU 1759 CD1 ILE A 290 13637 9640 10069 -333 -448 -179 C ATOM 1760 N HIS A 291 68.211 -19.913 -3.229 1.00 72.90 N ANISOU 1760 N HIS A 291 11599 7866 8234 -408 -220 -266 N ATOM 1761 CA HIS A 291 67.646 -18.632 -3.696 1.00 72.50 C ANISOU 1761 CA HIS A 291 11707 7751 8090 -397 -175 -256 C ATOM 1762 C HIS A 291 68.510 -18.038 -4.810 1.00 76.31 C ANISOU 1762 C HIS A 291 12367 8090 8536 -430 22 -311 C ATOM 1763 O HIS A 291 67.971 -17.651 -5.846 1.00 75.83 O ANISOU 1763 O HIS A 291 12536 7923 8352 -395 37 -281 O ATOM 1764 CB HIS A 291 67.478 -17.610 -2.561 1.00 72.60 C ANISOU 1764 CB HIS A 291 11608 7842 8135 -411 -181 -267 C ATOM 1765 CG HIS A 291 66.219 -17.797 -1.777 1.00 75.31 C ANISOU 1765 CG HIS A 291 11869 8287 8459 -367 -353 -202 C ATOM 1766 ND1 HIS A 291 65.020 -17.260 -2.209 1.00 77.15 N ANISOU 1766 ND1 HIS A 291 12220 8491 8602 -310 -425 -158 N ATOM 1767 CD2 HIS A 291 66.014 -18.425 -0.596 1.00 76.51 C ANISOU 1767 CD2 HIS A 291 11838 8561 8672 -372 -452 -183 C ATOM 1768 CE1 HIS A 291 64.126 -17.592 -1.293 1.00 75.98 C ANISOU 1768 CE1 HIS A 291 11937 8453 8479 -291 -554 -121 C ATOM 1769 NE2 HIS A 291 64.677 -18.289 -0.302 1.00 75.90 N ANISOU 1769 NE2 HIS A 291 11757 8531 8550 -332 -567 -129 N ATOM 1770 N ILE A 292 69.846 -18.047 -4.623 1.00 73.03 N ANISOU 1770 N ILE A 292 11852 7668 8228 -495 169 -395 N ATOM 1771 CA ILE A 292 70.819 -17.540 -5.593 1.00 73.67 C ANISOU 1771 CA ILE A 292 12074 7614 8304 -550 394 -466 C ATOM 1772 C ILE A 292 70.815 -18.438 -6.836 1.00 76.92 C ANISOU 1772 C ILE A 292 12654 7928 8644 -523 417 -447 C ATOM 1773 O ILE A 292 70.808 -17.911 -7.947 1.00 76.93 O ANISOU 1773 O ILE A 292 12908 7789 8533 -527 538 -448 O ATOM 1774 CB ILE A 292 72.246 -17.438 -4.962 1.00 77.25 C ANISOU 1774 CB ILE A 292 12320 8106 8926 -628 530 -581 C ATOM 1775 CG1 ILE A 292 72.286 -16.409 -3.791 1.00 77.35 C ANISOU 1775 CG1 ILE A 292 12195 8200 8995 -663 519 -613 C ATOM 1776 CG2 ILE A 292 73.334 -17.119 -6.006 1.00 79.37 C ANISOU 1776 CG2 ILE A 292 12709 8233 9214 -699 789 -670 C ATOM 1777 CD1 ILE A 292 71.901 -14.882 -4.132 1.00 86.24 C ANISOU 1777 CD1 ILE A 292 13516 9225 10024 -689 629 -607 C ATOM 1778 N PHE A 293 70.778 -19.774 -6.655 1.00 73.00 N ANISOU 1778 N PHE A 293 12043 7496 8197 -492 299 -428 N ATOM 1779 CA PHE A 293 70.796 -20.718 -7.776 1.00 73.27 C ANISOU 1779 CA PHE A 293 12227 7442 8170 -468 315 -419 C ATOM 1780 C PHE A 293 69.596 -20.472 -8.706 1.00 75.87 C ANISOU 1780 C PHE A 293 12817 7693 8317 -412 228 -345 C ATOM 1781 O PHE A 293 69.793 -20.312 -9.911 1.00 76.06 O ANISOU 1781 O PHE A 293 13084 7578 8237 -413 345 -359 O ATOM 1782 CB PHE A 293 70.798 -22.169 -7.280 1.00 74.75 C ANISOU 1782 CB PHE A 293 12248 7715 8439 -438 178 -402 C ATOM 1783 CG PHE A 293 71.309 -23.153 -8.306 1.00 77.66 C ANISOU 1783 CG PHE A 293 12721 7989 8796 -431 251 -431 C ATOM 1784 CD1 PHE A 293 70.496 -23.584 -9.349 1.00 81.57 C ANISOU 1784 CD1 PHE A 293 13440 8403 9151 -394 187 -381 C ATOM 1785 CD2 PHE A 293 72.589 -23.682 -8.206 1.00 80.80 C ANISOU 1785 CD2 PHE A 293 12987 8383 9330 -456 374 -516 C ATOM 1786 CE1 PHE A 293 70.975 -24.484 -10.306 1.00 83.30 C ANISOU 1786 CE1 PHE A 293 13772 8528 9351 -389 262 -413 C ATOM 1787 CE2 PHE A 293 73.056 -24.607 -9.147 1.00 84.53 C ANISOU 1787 CE2 PHE A 293 13557 8766 9796 -445 450 -548 C ATOM 1788 CZ PHE A 293 72.246 -25.000 -10.191 1.00 82.87 C ANISOU 1788 CZ PHE A 293 13588 8467 9432 -415 399 -494 C ATOM 1789 N ILE A 294 68.372 -20.389 -8.133 1.00 70.79 N ANISOU 1789 N ILE A 294 12126 7135 7637 -363 28 -275 N ATOM 1790 CA ILE A 294 67.125 -20.137 -8.862 1.00 70.67 C ANISOU 1790 CA ILE A 294 12311 7070 7470 -294 -97 -216 C ATOM 1791 C ILE A 294 67.217 -18.785 -9.604 1.00 76.72 C ANISOU 1791 C ILE A 294 13322 7708 8120 -287 36 -226 C ATOM 1792 O ILE A 294 66.925 -18.728 -10.803 1.00 77.03 O ANISOU 1792 O ILE A 294 13631 7624 8013 -246 46 -212 O ATOM 1793 CB ILE A 294 65.901 -20.173 -7.887 1.00 72.52 C ANISOU 1793 CB ILE A 294 12387 7437 7729 -254 -310 -162 C ATOM 1794 CG1 ILE A 294 65.714 -21.592 -7.309 1.00 72.14 C ANISOU 1794 CG1 ILE A 294 12156 7486 7770 -263 -434 -145 C ATOM 1795 CG2 ILE A 294 64.607 -19.703 -8.581 1.00 73.70 C ANISOU 1795 CG2 ILE A 294 12718 7542 7741 -172 -446 -120 C ATOM 1796 CD1 ILE A 294 64.629 -21.756 -6.291 1.00 76.59 C ANISOU 1796 CD1 ILE A 294 12553 8176 8374 -245 -606 -100 C ATOM 1797 N LEU A 295 67.660 -17.722 -8.893 1.00 74.11 N ANISOU 1797 N LEU A 295 12913 7397 7848 -329 143 -253 N ATOM 1798 CA LEU A 295 67.757 -16.349 -9.390 1.00 75.01 C ANISOU 1798 CA LEU A 295 13245 7389 7866 -332 280 -262 C ATOM 1799 C LEU A 295 68.761 -16.248 -10.549 1.00 82.11 C ANISOU 1799 C LEU A 295 14370 8121 8706 -383 517 -311 C ATOM 1800 O LEU A 295 68.445 -15.611 -11.551 1.00 82.43 O ANISOU 1800 O LEU A 295 14721 8017 8581 -344 569 -286 O ATOM 1801 CB LEU A 295 68.169 -15.422 -8.240 1.00 74.56 C ANISOU 1801 CB LEU A 295 13009 7401 7919 -388 352 -298 C ATOM 1802 CG LEU A 295 67.867 -13.934 -8.383 1.00 80.31 C ANISOU 1802 CG LEU A 295 13920 8036 8557 -372 426 -289 C ATOM 1803 CD1 LEU A 295 66.360 -13.679 -8.432 1.00 80.27 C ANISOU 1803 CD1 LEU A 295 14000 8054 8443 -250 206 -211 C ATOM 1804 CD2 LEU A 295 68.429 -13.161 -7.200 1.00 82.94 C ANISOU 1804 CD2 LEU A 295 14053 8442 9018 -445 509 -343 C ATOM 1805 N VAL A 296 69.939 -16.914 -10.438 1.00 80.84 N ANISOU 1805 N VAL A 296 14065 7977 8674 -463 657 -382 N ATOM 1806 CA VAL A 296 70.980 -16.913 -11.481 1.00 82.81 C ANISOU 1806 CA VAL A 296 14494 8076 8896 -525 910 -445 C ATOM 1807 C VAL A 296 70.499 -17.752 -12.695 1.00 88.10 C ANISOU 1807 C VAL A 296 15404 8655 9414 -460 845 -404 C ATOM 1808 O VAL A 296 70.646 -17.291 -13.829 1.00 89.51 O ANISOU 1808 O VAL A 296 15901 8664 9442 -462 992 -407 O ATOM 1809 CB VAL A 296 72.351 -17.414 -10.951 1.00 87.03 C ANISOU 1809 CB VAL A 296 14766 8667 9637 -616 1061 -549 C ATOM 1810 CG1 VAL A 296 73.355 -17.606 -12.082 1.00 88.49 C ANISOU 1810 CG1 VAL A 296 15119 8699 9802 -675 1321 -621 C ATOM 1811 CG2 VAL A 296 72.914 -16.453 -9.906 1.00 86.79 C ANISOU 1811 CG2 VAL A 296 14539 8699 9739 -689 1146 -609 C ATOM 1812 N GLU A 297 69.891 -18.935 -12.467 1.00 83.92 N ANISOU 1812 N GLU A 297 14748 8228 8911 -405 629 -366 N ATOM 1813 CA GLU A 297 69.379 -19.759 -13.578 1.00 84.33 C ANISOU 1813 CA GLU A 297 15018 8201 8822 -347 546 -336 C ATOM 1814 C GLU A 297 68.320 -18.972 -14.384 1.00 88.83 C ANISOU 1814 C GLU A 297 15903 8673 9177 -264 451 -275 C ATOM 1815 O GLU A 297 68.303 -19.050 -15.614 1.00 89.52 O ANISOU 1815 O GLU A 297 16299 8615 9099 -236 508 -274 O ATOM 1816 CB GLU A 297 68.796 -21.092 -13.071 1.00 84.49 C ANISOU 1816 CB GLU A 297 14835 8350 8918 -311 318 -308 C ATOM 1817 N ALA A 298 67.501 -18.156 -13.686 1.00 84.76 N ANISOU 1817 N ALA A 298 15319 8228 8659 -220 318 -232 N ATOM 1818 CA ALA A 298 66.452 -17.338 -14.285 1.00 85.41 C ANISOU 1818 CA ALA A 298 15661 8232 8558 -120 200 -178 C ATOM 1819 C ALA A 298 67.044 -16.147 -15.069 1.00 91.12 C ANISOU 1819 C ALA A 298 16705 8766 9150 -139 438 -191 C ATOM 1820 O ALA A 298 66.461 -15.751 -16.080 1.00 91.78 O ANISOU 1820 O ALA A 298 17126 8719 9029 -53 388 -155 O ATOM 1821 CB ALA A 298 65.507 -16.839 -13.207 1.00 85.08 C ANISOU 1821 CB ALA A 298 15416 8326 8583 -71 13 -142 C ATOM 1822 N LEU A 299 68.187 -15.579 -14.608 1.00 87.87 N ANISOU 1822 N LEU A 299 16198 8335 8853 -252 692 -246 N ATOM 1823 CA LEU A 299 68.861 -14.458 -15.283 1.00 89.11 C ANISOU 1823 CA LEU A 299 16645 8303 8908 -300 962 -270 C ATOM 1824 C LEU A 299 69.724 -14.940 -16.465 1.00 95.67 C ANISOU 1824 C LEU A 299 17712 8981 9659 -354 1183 -313 C ATOM 1825 O LEU A 299 69.941 -14.174 -17.406 1.00 97.82 O ANISOU 1825 O LEU A 299 18348 9059 9762 -358 1363 -309 O ATOM 1826 CB LEU A 299 69.743 -13.658 -14.304 1.00 88.49 C ANISOU 1826 CB LEU A 299 16354 8266 9004 -415 1152 -331 C ATOM 1827 CG LEU A 299 69.037 -12.896 -13.183 1.00 91.54 C ANISOU 1827 CG LEU A 299 16566 8764 9449 -377 1000 -299 C ATOM 1828 CD1 LEU A 299 70.023 -12.393 -12.167 1.00 91.31 C ANISOU 1828 CD1 LEU A 299 16282 8799 9614 -502 1170 -378 C ATOM 1829 CD2 LEU A 299 68.217 -11.756 -13.715 1.00 93.97 C ANISOU 1829 CD2 LEU A 299 17198 8941 9565 -284 962 -238 C ATOM 1830 N GLY A 300 70.218 -16.177 -16.399 1.00 91.62 N ANISOU 1830 N GLY A 300 17004 8545 9261 -392 1181 -355 N ATOM 1831 CA GLY A 300 71.060 -16.759 -17.439 1.00121.53 C ANISOU 1831 CA GLY A 300 20975 12204 12997 -443 1392 -407 C ATOM 1832 C GLY A 300 70.268 -17.456 -18.523 1.00156.39 C ANISOU 1832 C GLY A 300 25669 16545 17206 -341 1234 -357 C ATOM 1833 O GLY A 300 69.818 -18.587 -18.339 1.00122.46 O ANISOU 1833 O GLY A 300 21211 12360 12960 -298 1028 -345 O ATOM 1834 N THR A 302 71.125 -20.560 -17.009 1.00127.26 N ANISOU 1834 N THR A 302 21172 13199 13982 -405 1061 -447 N ATOM 1835 CA THR A 302 72.542 -20.812 -16.824 1.00127.42 C ANISOU 1835 CA THR A 302 21026 13212 14176 -503 1318 -546 C ATOM 1836 C THR A 302 72.957 -22.016 -17.643 1.00131.79 C ANISOU 1836 C THR A 302 21662 13701 14710 -498 1377 -586 C ATOM 1837 O THR A 302 73.057 -21.944 -18.861 1.00132.95 O ANISOU 1837 O THR A 302 22148 13684 14685 -496 1512 -595 O ATOM 1838 CB THR A 302 72.881 -21.069 -15.350 1.00133.42 C ANISOU 1838 CB THR A 302 21352 14160 15183 -531 1237 -572 C ATOM 1839 N SER A 303 73.170 -23.134 -16.968 1.00126.91 N ANISOU 1839 N SER A 303 20754 13206 14261 -489 1271 -607 N ATOM 1840 CA SER A 303 73.581 -24.357 -17.631 1.00127.09 C ANISOU 1840 CA SER A 303 20824 13175 14289 -479 1317 -649 C ATOM 1841 C SER A 303 72.673 -25.485 -17.212 1.00129.22 C ANISOU 1841 C SER A 303 20971 13552 14574 -409 1015 -589 C ATOM 1842 O SER A 303 72.006 -25.400 -16.197 1.00127.28 O ANISOU 1842 O SER A 303 20522 13443 14395 -386 812 -534 O ATOM 1843 CB SER A 303 75.018 -24.703 -17.254 1.00130.69 C ANISOU 1843 CB SER A 303 21035 13652 14970 -544 1539 -762 C ATOM 1844 OG SER A 303 75.238 -26.096 -17.322 1.00137.20 O ANISOU 1844 OG SER A 303 21761 14499 15869 -507 1477 -788 O ATOM 1845 N HIS A 304 72.610 -26.528 -18.021 1.00126.19 N ANISOU 1845 N HIS A 304 20729 13097 14120 -381 995 -602 N ATOM 1846 CA HIS A 304 71.804 -27.682 -17.672 1.00124.85 C ANISOU 1846 CA HIS A 304 20452 13012 13974 -330 731 -557 C ATOM 1847 C HIS A 304 72.700 -28.900 -17.845 1.00126.70 C ANISOU 1847 C HIS A 304 20603 13215 14321 -336 835 -626 C ATOM 1848 O HIS A 304 72.487 -29.717 -18.730 1.00127.01 O ANISOU 1848 O HIS A 304 20836 13166 14258 -312 812 -636 O ATOM 1849 CB HIS A 304 70.555 -27.780 -18.558 1.00126.37 C ANISOU 1849 CB HIS A 304 20932 13142 13942 -275 544 -501 C ATOM 1850 CG HIS A 304 69.285 -27.343 -17.882 1.00128.84 C ANISOU 1850 CG HIS A 304 21158 13567 14230 -236 281 -422 C ATOM 1851 ND1 HIS A 304 68.886 -26.026 -17.823 1.00130.66 N ANISOU 1851 ND1 HIS A 304 21474 13793 14377 -223 278 -387 N ATOM 1852 CD2 HIS A 304 68.321 -28.053 -17.249 1.00129.55 C ANISOU 1852 CD2 HIS A 304 21083 13768 14371 -210 23 -379 C ATOM 1853 CE1 HIS A 304 67.737 -25.942 -17.179 1.00129.04 C ANISOU 1853 CE1 HIS A 304 21149 13700 14180 -183 27 -330 C ATOM 1854 NE2 HIS A 304 67.372 -27.157 -16.821 1.00128.72 N ANISOU 1854 NE2 HIS A 304 20953 13732 14222 -181 -125 -326 N ATOM 1855 N SER A 305 73.689 -29.022 -16.960 1.00120.54 N ANISOU 1855 N SER A 305 19530 12513 13758 -362 934 -679 N ATOM 1856 CA SER A 305 74.648 -30.113 -16.985 1.00119.64 C ANISOU 1856 CA SER A 305 19295 12378 13784 -354 1035 -756 C ATOM 1857 C SER A 305 74.185 -31.222 -16.083 1.00119.97 C ANISOU 1857 C SER A 305 19129 12528 13925 -305 795 -708 C ATOM 1858 O SER A 305 73.028 -31.269 -15.705 1.00118.60 O ANISOU 1858 O SER A 305 18960 12421 13683 -287 565 -621 O ATOM 1859 CB SER A 305 76.012 -29.637 -16.523 1.00123.10 C ANISOU 1859 CB SER A 305 19520 12839 14413 -397 1264 -855 C ATOM 1860 N THR A 306 75.082 -32.123 -15.713 1.00114.77 N ANISOU 1860 N THR A 306 18287 11885 13436 -282 849 -770 N ATOM 1861 CA THR A 306 74.640 -33.218 -14.863 1.00112.44 C ANISOU 1861 CA THR A 306 17830 11672 13221 -233 627 -718 C ATOM 1862 C THR A 306 74.994 -32.750 -13.471 1.00112.23 C ANISOU 1862 C THR A 306 17502 11788 13353 -231 575 -711 C ATOM 1863 O THR A 306 74.211 -32.867 -12.527 1.00110.62 O ANISOU 1863 O THR A 306 17187 11687 13158 -217 369 -630 O ATOM 1864 CB THR A 306 75.386 -34.525 -15.176 1.00121.02 C ANISOU 1864 CB THR A 306 18897 12688 14395 -188 691 -782 C ATOM 1865 OG1 THR A 306 76.754 -34.408 -14.764 1.00122.15 O ANISOU 1865 OG1 THR A 306 18825 12855 14731 -177 861 -881 O ATOM 1866 CG2 THR A 306 75.335 -34.822 -16.667 1.00120.62 C ANISOU 1866 CG2 THR A 306 19159 12480 14192 -199 813 -819 C ATOM 1867 N ALA A 307 76.202 -32.213 -13.368 1.00107.10 N ANISOU 1867 N ALA A 307 16725 11139 12830 -250 773 -809 N ATOM 1868 CA ALA A 307 76.710 -31.635 -12.120 1.00105.23 C ANISOU 1868 CA ALA A 307 16204 11030 12748 -253 747 -830 C ATOM 1869 C ALA A 307 75.871 -30.427 -11.695 1.00105.43 C ANISOU 1869 C ALA A 307 16255 11123 12682 -298 670 -758 C ATOM 1870 O ALA A 307 75.597 -30.270 -10.506 1.00104.14 O ANISOU 1870 O ALA A 307 15904 11082 12581 -284 520 -714 O ATOM 1871 CB ALA A 307 78.167 -31.230 -12.282 1.00107.26 C ANISOU 1871 CB ALA A 307 16334 11261 13160 -278 996 -973 C ATOM 1872 N ALA A 308 75.435 -29.599 -12.675 1.00100.23 N ANISOU 1872 N ALA A 308 15847 10375 11862 -344 768 -743 N ATOM 1873 CA ALA A 308 74.584 -28.424 -12.451 1.00 98.03 C ANISOU 1873 CA ALA A 308 15637 10134 11477 -374 702 -676 C ATOM 1874 C ALA A 308 73.189 -28.842 -11.955 1.00 97.53 C ANISOU 1874 C ALA A 308 15578 10146 11333 -335 425 -562 C ATOM 1875 O ALA A 308 72.597 -28.144 -11.128 1.00 96.55 O ANISOU 1875 O ALA A 308 15360 10117 11208 -342 317 -510 O ATOM 1876 CB ALA A 308 74.464 -27.610 -13.729 1.00 99.76 C ANISOU 1876 CB ALA A 308 16162 10214 11527 -410 865 -687 C ATOM 1877 N LEU A 309 72.680 -29.992 -12.436 1.00 91.34 N ANISOU 1877 N LEU A 309 14893 9318 10492 -300 320 -531 N ATOM 1878 CA LEU A 309 71.383 -30.512 -12.015 1.00 88.86 C ANISOU 1878 CA LEU A 309 14574 9067 10123 -278 74 -440 C ATOM 1879 C LEU A 309 71.506 -31.130 -10.616 1.00 88.86 C ANISOU 1879 C LEU A 309 14305 9186 10270 -259 -43 -415 C ATOM 1880 O LEU A 309 70.608 -30.959 -9.792 1.00 87.63 O ANISOU 1880 O LEU A 309 14067 9125 10106 -262 -200 -347 O ATOM 1881 CB LEU A 309 70.849 -31.539 -13.033 1.00 89.51 C ANISOU 1881 CB LEU A 309 14859 9050 10099 -259 13 -432 C ATOM 1882 CG LEU A 309 69.404 -32.018 -12.830 1.00 93.71 C ANISOU 1882 CG LEU A 309 15415 9629 10563 -251 -229 -357 C ATOM 1883 CD1 LEU A 309 68.400 -30.878 -13.046 1.00 93.37 C ANISOU 1883 CD1 LEU A 309 15473 9608 10396 -255 -308 -317 C ATOM 1884 CD2 LEU A 309 69.072 -33.149 -13.779 1.00 97.60 C ANISOU 1884 CD2 LEU A 309 16082 10021 10980 -241 -278 -371 C ATOM 1885 N SER A 310 72.645 -31.820 -10.353 1.00 83.25 N ANISOU 1885 N SER A 310 13467 8467 9695 -234 41 -476 N ATOM 1886 CA SER A 310 72.970 -32.453 -9.073 1.00 81.25 C ANISOU 1886 CA SER A 310 12984 8309 9578 -198 -60 -463 C ATOM 1887 C SER A 310 73.131 -31.411 -7.985 1.00 81.83 C ANISOU 1887 C SER A 310 12879 8499 9712 -215 -75 -461 C ATOM 1888 O SER A 310 72.569 -31.567 -6.899 1.00 80.72 O ANISOU 1888 O SER A 310 12627 8453 9589 -203 -229 -396 O ATOM 1889 CB SER A 310 74.246 -33.285 -9.188 1.00 85.79 C ANISOU 1889 CB SER A 310 13477 8836 10282 -151 43 -548 C ATOM 1890 OG SER A 310 74.096 -34.370 -10.090 1.00 96.12 O ANISOU 1890 OG SER A 310 14946 10035 11539 -129 48 -549 O ATOM 1891 N SER A 311 73.866 -30.327 -8.287 1.00 76.77 N ANISOU 1891 N SER A 311 12227 7844 9098 -250 94 -534 N ATOM 1892 CA SER A 311 74.105 -29.231 -7.356 1.00 75.11 C ANISOU 1892 CA SER A 311 11861 7731 8946 -277 103 -551 C ATOM 1893 C SER A 311 72.794 -28.519 -7.013 1.00 76.66 C ANISOU 1893 C SER A 311 12120 7981 9026 -299 -22 -456 C ATOM 1894 O SER A 311 72.593 -28.194 -5.843 1.00 76.79 O ANISOU 1894 O SER A 311 11984 8106 9085 -297 -119 -429 O ATOM 1895 CB SER A 311 75.114 -28.244 -7.925 1.00 78.26 C ANISOU 1895 CB SER A 311 12268 8077 9391 -328 335 -657 C ATOM 1896 OG SER A 311 74.637 -27.698 -9.138 1.00 86.65 O ANISOU 1896 OG SER A 311 13589 9030 10305 -364 437 -640 O ATOM 1897 N TYR A 312 71.879 -28.338 -8.005 1.00 70.72 N ANISOU 1897 N TYR A 312 11591 7155 8126 -311 -32 -411 N ATOM 1898 CA TYR A 312 70.562 -27.710 -7.794 1.00 68.72 C ANISOU 1898 CA TYR A 312 11397 6945 7767 -318 -161 -332 C ATOM 1899 C TYR A 312 69.730 -28.485 -6.753 1.00 69.67 C ANISOU 1899 C TYR A 312 11392 7163 7915 -298 -359 -260 C ATOM 1900 O TYR A 312 69.214 -27.876 -5.812 1.00 67.69 O ANISOU 1900 O TYR A 312 11039 7007 7672 -307 -434 -224 O ATOM 1901 CB TYR A 312 69.770 -27.602 -9.115 1.00 69.73 C ANISOU 1901 CB TYR A 312 11788 6969 7736 -313 -167 -309 C ATOM 1902 CG TYR A 312 68.309 -27.222 -8.937 1.00 70.12 C ANISOU 1902 CG TYR A 312 11881 7067 7694 -300 -338 -237 C ATOM 1903 CD1 TYR A 312 67.930 -25.900 -8.720 1.00 71.78 C ANISOU 1903 CD1 TYR A 312 12109 7305 7859 -304 -327 -223 C ATOM 1904 CD2 TYR A 312 67.303 -28.176 -9.048 1.00 70.41 C ANISOU 1904 CD2 TYR A 312 11945 7113 7694 -284 -505 -192 C ATOM 1905 CE1 TYR A 312 66.586 -25.546 -8.570 1.00 72.37 C ANISOU 1905 CE1 TYR A 312 12209 7425 7862 -280 -486 -168 C ATOM 1906 CE2 TYR A 312 65.958 -27.837 -8.896 1.00 70.82 C ANISOU 1906 CE2 TYR A 312 12010 7215 7683 -274 -660 -143 C ATOM 1907 CZ TYR A 312 65.601 -26.520 -8.661 1.00 78.70 C ANISOU 1907 CZ TYR A 312 13012 8247 8643 -265 -653 -133 C ATOM 1908 OH TYR A 312 64.268 -26.193 -8.524 1.00 79.05 O ANISOU 1908 OH TYR A 312 13056 8341 8639 -242 -808 -96 O ATOM 1909 N TYR A 313 69.598 -29.811 -6.924 1.00 65.71 N ANISOU 1909 N TYR A 313 10910 6630 7425 -277 -429 -241 N ATOM 1910 CA TYR A 313 68.796 -30.615 -6.017 1.00 64.89 C ANISOU 1910 CA TYR A 313 10719 6595 7340 -271 -593 -173 C ATOM 1911 C TYR A 313 69.525 -30.796 -4.681 1.00 70.19 C ANISOU 1911 C TYR A 313 11193 7353 8125 -251 -610 -176 C ATOM 1912 O TYR A 313 68.858 -31.043 -3.675 1.00 69.33 O ANISOU 1912 O TYR A 313 11005 7318 8021 -255 -725 -116 O ATOM 1913 CB TYR A 313 68.421 -31.962 -6.636 1.00 65.89 C ANISOU 1913 CB TYR A 313 10948 6645 7441 -263 -655 -156 C ATOM 1914 CG TYR A 313 67.306 -31.802 -7.649 1.00 66.67 C ANISOU 1914 CG TYR A 313 11220 6693 7419 -282 -713 -140 C ATOM 1915 CD1 TYR A 313 65.973 -31.751 -7.246 1.00 68.25 C ANISOU 1915 CD1 TYR A 313 11394 6954 7585 -305 -857 -88 C ATOM 1916 CD2 TYR A 313 67.584 -31.620 -8.998 1.00 67.64 C ANISOU 1916 CD2 TYR A 313 11532 6708 7460 -275 -624 -186 C ATOM 1917 CE1 TYR A 313 64.945 -31.558 -8.165 1.00 69.12 C ANISOU 1917 CE1 TYR A 313 11643 7025 7593 -310 -934 -88 C ATOM 1918 CE2 TYR A 313 66.562 -31.449 -9.930 1.00 68.92 C ANISOU 1918 CE2 TYR A 313 11866 6823 7498 -278 -701 -176 C ATOM 1919 CZ TYR A 313 65.243 -31.406 -9.508 1.00 76.76 C ANISOU 1919 CZ TYR A 313 12811 7885 8469 -290 -867 -131 C ATOM 1920 OH TYR A 313 64.232 -31.220 -10.424 1.00 79.83 O ANISOU 1920 OH TYR A 313 13353 8234 8745 -281 -966 -135 O ATOM 1921 N PHE A 314 70.850 -30.561 -4.634 1.00 68.55 N ANISOU 1921 N PHE A 314 10904 7138 8004 -232 -494 -253 N ATOM 1922 CA PHE A 314 71.549 -30.552 -3.354 1.00 69.07 C ANISOU 1922 CA PHE A 314 10779 7294 8171 -204 -529 -269 C ATOM 1923 C PHE A 314 71.144 -29.268 -2.597 1.00 72.95 C ANISOU 1923 C PHE A 314 11201 7878 8639 -239 -545 -255 C ATOM 1924 O PHE A 314 70.886 -29.322 -1.393 1.00 72.27 O ANISOU 1924 O PHE A 314 11011 7881 8569 -228 -647 -215 O ATOM 1925 CB PHE A 314 73.075 -30.677 -3.525 1.00 72.43 C ANISOU 1925 CB PHE A 314 11111 7691 8717 -171 -414 -375 C ATOM 1926 CG PHE A 314 73.825 -30.619 -2.208 1.00 75.34 C ANISOU 1926 CG PHE A 314 11277 8158 9190 -129 -475 -407 C ATOM 1927 CD1 PHE A 314 73.937 -31.750 -1.400 1.00 79.42 C ANISOU 1927 CD1 PHE A 314 11737 8696 9744 -59 -604 -370 C ATOM 1928 CD2 PHE A 314 74.420 -29.433 -1.775 1.00 77.96 C ANISOU 1928 CD2 PHE A 314 11490 8553 9577 -159 -408 -479 C ATOM 1929 CE1 PHE A 314 74.606 -31.685 -0.166 1.00 80.79 C ANISOU 1929 CE1 PHE A 314 11745 8958 9995 -6 -683 -399 C ATOM 1930 CE2 PHE A 314 75.098 -29.374 -0.549 1.00 81.05 C ANISOU 1930 CE2 PHE A 314 11698 9039 10059 -117 -485 -518 C ATOM 1931 CZ PHE A 314 75.189 -30.500 0.245 1.00 79.59 C ANISOU 1931 CZ PHE A 314 11464 8877 9897 -35 -630 -478 C ATOM 1932 N CYS A 315 71.022 -28.129 -3.333 1.00 69.78 N ANISOU 1932 N CYS A 315 10883 7444 8186 -280 -443 -284 N ATOM 1933 CA CYS A 315 70.603 -26.827 -2.800 1.00 69.21 C ANISOU 1933 CA CYS A 315 10777 7436 8082 -312 -440 -275 C ATOM 1934 C CYS A 315 69.136 -26.885 -2.377 1.00 73.16 C ANISOU 1934 C CYS A 315 11310 7985 8501 -315 -581 -182 C ATOM 1935 O CYS A 315 68.769 -26.235 -1.393 1.00 72.98 O ANISOU 1935 O CYS A 315 11199 8050 8479 -325 -627 -161 O ATOM 1936 CB CYS A 315 70.839 -25.719 -3.817 1.00 69.69 C ANISOU 1936 CB CYS A 315 10960 7419 8098 -348 -287 -325 C ATOM 1937 SG CYS A 315 72.578 -25.480 -4.251 1.00 74.64 S ANISOU 1937 SG CYS A 315 11527 7991 8843 -370 -81 -456 S ATOM 1938 N ILE A 316 68.304 -27.657 -3.121 1.00 69.36 N ANISOU 1938 N ILE A 316 10949 7449 7956 -310 -643 -136 N ATOM 1939 CA ILE A 316 66.895 -27.913 -2.802 1.00 68.83 C ANISOU 1939 CA ILE A 316 10895 7423 7835 -318 -776 -64 C ATOM 1940 C ILE A 316 66.831 -28.612 -1.437 1.00 72.23 C ANISOU 1940 C ILE A 316 11190 7934 8319 -316 -859 -23 C ATOM 1941 O ILE A 316 66.072 -28.179 -0.567 1.00 71.44 O ANISOU 1941 O ILE A 316 11026 7913 8205 -332 -916 14 O ATOM 1942 CB ILE A 316 66.201 -28.752 -3.935 1.00 72.66 C ANISOU 1942 CB ILE A 316 11527 7822 8259 -318 -825 -47 C ATOM 1943 CG1 ILE A 316 65.972 -27.918 -5.209 1.00 73.77 C ANISOU 1943 CG1 ILE A 316 11835 7887 8308 -311 -772 -75 C ATOM 1944 CG2 ILE A 316 64.862 -29.359 -3.478 1.00 73.43 C ANISOU 1944 CG2 ILE A 316 11595 7964 8340 -338 -964 11 C ATOM 1945 CD1 ILE A 316 64.912 -26.777 -5.097 1.00 82.98 C ANISOU 1945 CD1 ILE A 316 13016 9098 9412 -307 -829 -52 C ATOM 1946 N ALA A 317 67.672 -29.658 -1.242 1.00 68.99 N ANISOU 1946 N ALA A 317 10747 7498 7968 -289 -858 -33 N ATOM 1947 CA ALA A 317 67.751 -30.436 -0.007 1.00 68.91 C ANISOU 1947 CA ALA A 317 10648 7540 7996 -271 -937 8 C ATOM 1948 C ALA A 317 68.115 -29.543 1.185 1.00 73.83 C ANISOU 1948 C ALA A 317 11148 8263 8642 -265 -939 -5 C ATOM 1949 O ALA A 317 67.546 -29.726 2.260 1.00 73.09 O ANISOU 1949 O ALA A 317 11014 8231 8527 -272 -1013 50 O ATOM 1950 CB ALA A 317 68.767 -31.549 -0.155 1.00 70.18 C ANISOU 1950 CB ALA A 317 10808 7639 8216 -221 -928 -16 C ATOM 1951 N LEU A 318 69.021 -28.550 0.980 1.00 71.60 N ANISOU 1951 N LEU A 318 10817 7991 8397 -262 -850 -81 N ATOM 1952 CA LEU A 318 69.439 -27.580 2.009 1.00 71.49 C ANISOU 1952 CA LEU A 318 10688 8066 8409 -264 -845 -114 C ATOM 1953 C LEU A 318 68.252 -26.723 2.479 1.00 73.94 C ANISOU 1953 C LEU A 318 11011 8435 8649 -303 -875 -66 C ATOM 1954 O LEU A 318 68.128 -26.480 3.675 1.00 73.40 O ANISOU 1954 O LEU A 318 10867 8446 8574 -301 -925 -50 O ATOM 1955 CB LEU A 318 70.573 -26.668 1.509 1.00 71.91 C ANISOU 1955 CB LEU A 318 10698 8100 8525 -274 -721 -219 C ATOM 1956 CG LEU A 318 71.950 -27.319 1.379 1.00 77.21 C ANISOU 1956 CG LEU A 318 11291 8744 9301 -231 -687 -296 C ATOM 1957 CD1 LEU A 318 72.890 -26.435 0.618 1.00 78.05 C ANISOU 1957 CD1 LEU A 318 11377 8809 9470 -264 -528 -405 C ATOM 1958 CD2 LEU A 318 72.536 -27.676 2.747 1.00 78.98 C ANISOU 1958 CD2 LEU A 318 11377 9052 9578 -179 -793 -310 C ATOM 1959 N GLY A 319 67.379 -26.318 1.555 1.00 69.34 N ANISOU 1959 N GLY A 319 10526 7809 8011 -328 -850 -48 N ATOM 1960 CA GLY A 319 66.170 -25.569 1.887 1.00 68.21 C ANISOU 1960 CA GLY A 319 10391 7714 7811 -350 -885 -9 C ATOM 1961 C GLY A 319 65.247 -26.366 2.797 1.00 70.41 C ANISOU 1961 C GLY A 319 10634 8045 8075 -360 -980 60 C ATOM 1962 O GLY A 319 64.680 -25.823 3.751 1.00 69.90 O ANISOU 1962 O GLY A 319 10513 8055 7992 -374 -1001 79 O ATOM 1963 N TYR A 320 65.111 -27.676 2.518 1.00 65.55 N ANISOU 1963 N TYR A 320 10059 7381 7465 -359 -1025 94 N ATOM 1964 CA TYR A 320 64.313 -28.590 3.325 1.00 64.90 C ANISOU 1964 CA TYR A 320 9963 7324 7371 -381 -1093 159 C ATOM 1965 C TYR A 320 64.990 -28.882 4.672 1.00 69.76 C ANISOU 1965 C TYR A 320 10519 7990 7997 -358 -1115 175 C ATOM 1966 O TYR A 320 64.294 -29.225 5.632 1.00 69.75 O ANISOU 1966 O TYR A 320 10509 8026 7966 -382 -1149 228 O ATOM 1967 CB TYR A 320 64.060 -29.907 2.576 1.00 65.76 C ANISOU 1967 CB TYR A 320 10151 7349 7486 -390 -1125 182 C ATOM 1968 CG TYR A 320 63.042 -29.811 1.459 1.00 66.42 C ANISOU 1968 CG TYR A 320 10299 7394 7545 -419 -1143 174 C ATOM 1969 CD1 TYR A 320 61.676 -29.830 1.732 1.00 68.11 C ANISOU 1969 CD1 TYR A 320 10485 7644 7748 -465 -1191 200 C ATOM 1970 CD2 TYR A 320 63.435 -29.865 0.124 1.00 66.94 C ANISOU 1970 CD2 TYR A 320 10456 7377 7599 -398 -1119 136 C ATOM 1971 CE1 TYR A 320 60.731 -29.800 0.709 1.00 68.10 C ANISOU 1971 CE1 TYR A 320 10531 7611 7733 -481 -1235 180 C ATOM 1972 CE2 TYR A 320 62.495 -29.844 -0.910 1.00 67.57 C ANISOU 1972 CE2 TYR A 320 10613 7418 7643 -413 -1160 125 C ATOM 1973 CZ TYR A 320 61.143 -29.812 -0.610 1.00 72.32 C ANISOU 1973 CZ TYR A 320 11171 8066 8242 -450 -1229 144 C ATOM 1974 OH TYR A 320 60.197 -29.772 -1.601 1.00 70.52 O ANISOU 1974 OH TYR A 320 11001 7806 7985 -455 -1294 120 O ATOM 1975 N THR A 321 66.344 -28.751 4.739 1.00 66.66 N ANISOU 1975 N THR A 321 10088 7595 7645 -310 -1095 124 N ATOM 1976 CA THR A 321 67.159 -28.990 5.942 1.00 66.87 C ANISOU 1976 CA THR A 321 10057 7668 7683 -266 -1140 121 C ATOM 1977 C THR A 321 66.799 -27.960 7.025 1.00 71.31 C ANISOU 1977 C THR A 321 10565 8324 8206 -286 -1144 121 C ATOM 1978 O THR A 321 66.708 -28.332 8.195 1.00 71.15 O ANISOU 1978 O THR A 321 10545 8342 8145 -273 -1198 161 O ATOM 1979 CB THR A 321 68.652 -28.943 5.591 1.00 72.40 C ANISOU 1979 CB THR A 321 10701 8348 8459 -211 -1116 38 C ATOM 1980 OG1 THR A 321 68.911 -29.913 4.581 1.00 73.38 O ANISOU 1980 OG1 THR A 321 10886 8380 8615 -192 -1101 37 O ATOM 1981 CG2 THR A 321 69.553 -29.203 6.785 1.00 69.46 C ANISOU 1981 CG2 THR A 321 10260 8026 8105 -148 -1190 19 C ATOM 1982 N ASN A 322 66.564 -26.682 6.632 1.00 68.07 N ANISOU 1982 N ASN A 322 10128 7940 7797 -317 -1082 78 N ATOM 1983 CA ASN A 322 66.154 -25.606 7.546 1.00 68.22 C ANISOU 1983 CA ASN A 322 10103 8038 7779 -338 -1073 71 C ATOM 1984 C ASN A 322 64.921 -26.052 8.338 1.00 73.26 C ANISOU 1984 C ASN A 322 10770 8707 8358 -367 -1107 149 C ATOM 1985 O ASN A 322 64.920 -25.994 9.568 1.00 73.35 O ANISOU 1985 O ASN A 322 10767 8775 8329 -363 -1134 166 O ATOM 1986 CB ASN A 322 65.878 -24.301 6.764 1.00 69.07 C ANISOU 1986 CB ASN A 322 10214 8138 7892 -363 -997 25 C ATOM 1987 CG ASN A 322 65.337 -23.149 7.594 1.00 97.41 C ANISOU 1987 CG ASN A 322 13770 11797 11446 -383 -980 15 C ATOM 1988 OD1 ASN A 322 66.059 -22.470 8.333 1.00 91.60 O ANISOU 1988 OD1 ASN A 322 12979 11107 10717 -378 -969 -36 O ATOM 1989 ND2 ASN A 322 64.051 -22.877 7.451 1.00 91.38 N ANISOU 1989 ND2 ASN A 322 13032 11040 10649 -403 -976 53 N ATOM 1990 N SER A 323 63.923 -26.595 7.617 1.00 70.35 N ANISOU 1990 N SER A 323 10447 8294 7987 -399 -1106 190 N ATOM 1991 CA SER A 323 62.653 -27.104 8.132 1.00 70.67 C ANISOU 1991 CA SER A 323 10506 8350 7997 -445 -1118 250 C ATOM 1992 C SER A 323 62.849 -28.301 9.062 1.00 75.46 C ANISOU 1992 C SER A 323 11157 8941 8573 -442 -1153 308 C ATOM 1993 O SER A 323 62.077 -28.484 10.000 1.00 75.36 O ANISOU 1993 O SER A 323 11159 8958 8518 -480 -1141 351 O ATOM 1994 CB SER A 323 61.765 -27.517 6.965 1.00 74.43 C ANISOU 1994 CB SER A 323 11011 8771 8498 -475 -1122 258 C ATOM 1995 OG SER A 323 61.643 -26.457 6.029 1.00 83.42 O ANISOU 1995 OG SER A 323 12142 9906 9647 -461 -1101 209 O ATOM 1996 N SER A 324 63.869 -29.122 8.787 1.00 72.71 N ANISOU 1996 N SER A 324 10843 8539 8246 -394 -1190 307 N ATOM 1997 CA SER A 324 64.178 -30.322 9.558 1.00 73.55 C ANISOU 1997 CA SER A 324 11018 8608 8319 -368 -1235 363 C ATOM 1998 C SER A 324 64.992 -29.984 10.819 1.00 78.94 C ANISOU 1998 C SER A 324 11688 9350 8957 -312 -1277 354 C ATOM 1999 O SER A 324 64.917 -30.715 11.802 1.00 79.10 O ANISOU 1999 O SER A 324 11787 9356 8910 -298 -1311 412 O ATOM 2000 CB SER A 324 64.946 -31.315 8.689 1.00 76.98 C ANISOU 2000 CB SER A 324 11493 8955 8801 -323 -1263 356 C ATOM 2001 OG SER A 324 64.198 -31.658 7.533 1.00 83.17 O ANISOU 2001 OG SER A 324 12305 9682 9614 -375 -1235 359 O ATOM 2002 N LEU A 325 65.764 -28.885 10.788 1.00 76.23 N ANISOU 2002 N LEU A 325 11257 9064 8643 -282 -1275 276 N ATOM 2003 CA LEU A 325 66.587 -28.474 11.923 1.00 76.71 C ANISOU 2003 CA LEU A 325 11291 9187 8670 -228 -1330 245 C ATOM 2004 C LEU A 325 65.797 -27.596 12.889 1.00 81.66 C ANISOU 2004 C LEU A 325 11918 9886 9223 -275 -1298 257 C ATOM 2005 O LEU A 325 66.103 -27.620 14.077 1.00 81.93 O ANISOU 2005 O LEU A 325 11987 9958 9185 -240 -1351 266 O ATOM 2006 CB LEU A 325 67.849 -27.727 11.453 1.00 76.48 C ANISOU 2006 CB LEU A 325 11156 9181 8723 -186 -1336 138 C ATOM 2007 CG LEU A 325 68.866 -28.544 10.640 1.00 81.00 C ANISOU 2007 CG LEU A 325 11710 9688 9378 -126 -1362 104 C ATOM 2008 CD1 LEU A 325 69.970 -27.665 10.124 1.00 80.97 C ANISOU 2008 CD1 LEU A 325 11589 9708 9469 -112 -1328 -15 C ATOM 2009 CD2 LEU A 325 69.442 -29.696 11.449 1.00 84.03 C ANISOU 2009 CD2 LEU A 325 12147 10049 9731 -39 -1471 140 C ATOM 2010 N ASN A 326 64.771 -26.851 12.400 1.00 78.96 N ANISOU 2010 N ASN A 326 11547 9561 8894 -343 -1219 255 N ATOM 2011 CA ASN A 326 63.930 -25.973 13.232 1.00 79.74 C ANISOU 2011 CA ASN A 326 11637 9724 8936 -385 -1172 258 C ATOM 2012 C ASN A 326 63.387 -26.695 14.481 1.00 85.66 C ANISOU 2012 C ASN A 326 12479 10479 9589 -400 -1180 331 C ATOM 2013 O ASN A 326 63.516 -26.110 15.556 1.00 86.12 O ANISOU 2013 O ASN A 326 12551 10594 9577 -389 -1185 316 O ATOM 2014 CB ASN A 326 62.752 -25.385 12.456 1.00 81.88 C ANISOU 2014 CB ASN A 326 11872 9995 9243 -442 -1100 255 C ATOM 2015 CG ASN A 326 63.086 -24.237 11.533 1.00107.92 C ANISOU 2015 CG ASN A 326 15110 13298 12598 -431 -1071 182 C ATOM 2016 OD1 ASN A 326 63.979 -23.423 11.793 1.00102.47 O ANISOU 2016 OD1 ASN A 326 14383 12638 11913 -406 -1072 121 O ATOM 2017 ND2 ASN A 326 62.246 -24.037 10.532 1.00100.23 N ANISOU 2017 ND2 ASN A 326 14130 12295 11659 -454 -1040 184 N ATOM 2018 N PRO A 327 62.817 -27.936 14.418 1.00 83.18 N ANISOU 2018 N PRO A 327 12246 10100 9259 -427 -1173 406 N ATOM 2019 CA PRO A 327 62.348 -28.577 15.664 1.00 84.55 C ANISOU 2019 CA PRO A 327 12535 10263 9326 -448 -1158 476 C ATOM 2020 C PRO A 327 63.467 -28.706 16.715 1.00 90.23 C ANISOU 2020 C PRO A 327 13327 10998 9959 -360 -1251 476 C ATOM 2021 O PRO A 327 63.211 -28.456 17.890 1.00 90.81 O ANISOU 2021 O PRO A 327 13472 11105 9926 -367 -1236 495 O ATOM 2022 CB PRO A 327 61.865 -29.961 15.204 1.00 86.55 C ANISOU 2022 CB PRO A 327 12867 10421 9598 -484 -1143 543 C ATOM 2023 CG PRO A 327 62.413 -30.150 13.852 1.00 89.98 C ANISOU 2023 CG PRO A 327 13238 10818 10132 -454 -1185 507 C ATOM 2024 CD PRO A 327 62.534 -28.795 13.252 1.00 84.37 C ANISOU 2024 CD PRO A 327 12403 10175 9480 -449 -1169 428 C ATOM 2025 N ILE A 328 64.709 -29.029 16.291 1.00 87.01 N ANISOU 2025 N ILE A 328 12894 10569 9598 -273 -1350 442 N ATOM 2026 CA ILE A 328 65.850 -29.159 17.197 1.00 87.72 C ANISOU 2026 CA ILE A 328 13028 10678 9625 -172 -1468 422 C ATOM 2027 C ILE A 328 66.360 -27.768 17.636 1.00 92.25 C ANISOU 2027 C ILE A 328 13501 11351 10200 -158 -1488 327 C ATOM 2028 O ILE A 328 66.637 -27.574 18.818 1.00 92.01 O ANISOU 2028 O ILE A 328 13537 11359 10064 -118 -1548 322 O ATOM 2029 CB ILE A 328 66.984 -29.970 16.531 1.00 90.80 C ANISOU 2029 CB ILE A 328 13396 11013 10091 -80 -1563 400 C ATOM 2030 N LEU A 329 66.472 -26.817 16.691 1.00 89.58 N ANISOU 2030 N LEU A 329 13023 11044 9971 -192 -1436 250 N ATOM 2031 CA LEU A 329 67.011 -25.473 16.910 1.00 90.49 C ANISOU 2031 CA LEU A 329 13037 11234 10110 -191 -1438 148 C ATOM 2032 C LEU A 329 66.097 -24.574 17.780 1.00 97.93 C ANISOU 2032 C LEU A 329 14012 12233 10964 -248 -1370 155 C ATOM 2033 O LEU A 329 66.624 -23.740 18.518 1.00 97.98 O ANISOU 2033 O LEU A 329 13993 12300 10936 -229 -1408 85 O ATOM 2034 CB LEU A 329 67.234 -24.772 15.566 1.00 89.46 C ANISOU 2034 CB LEU A 329 12787 11094 10110 -223 -1372 80 C ATOM 2035 N TYR A 330 64.757 -24.715 17.687 1.00 96.63 N ANISOU 2035 N TYR A 330 13894 12049 10774 -318 -1270 225 N ATOM 2036 CA TYR A 330 63.841 -23.843 18.431 1.00 97.58 C ANISOU 2036 CA TYR A 330 14028 12219 10828 -370 -1187 221 C ATOM 2037 C TYR A 330 63.050 -24.562 19.540 1.00105.18 C ANISOU 2037 C TYR A 330 15132 13168 11663 -395 -1153 306 C ATOM 2038 O TYR A 330 62.803 -23.930 20.570 1.00105.78 O ANISOU 2038 O TYR A 330 15255 13291 11647 -405 -1123 289 O ATOM 2039 CB TYR A 330 62.833 -23.191 17.484 1.00 97.94 C ANISOU 2039 CB TYR A 330 13993 12263 10958 -431 -1082 210 C ATOM 2040 CG TYR A 330 63.398 -22.003 16.737 1.00 99.51 C ANISOU 2040 CG TYR A 330 14090 12482 11239 -420 -1075 119 C ATOM 2041 CD1 TYR A 330 64.136 -22.173 15.569 1.00101.19 C ANISOU 2041 CD1 TYR A 330 14250 12652 11546 -398 -1103 90 C ATOM 2042 CD2 TYR A 330 63.169 -20.703 17.182 1.00100.15 C ANISOU 2042 CD2 TYR A 330 14140 12611 11301 -437 -1023 60 C ATOM 2043 CE1 TYR A 330 64.679 -21.082 14.893 1.00101.64 C ANISOU 2043 CE1 TYR A 330 14236 12712 11671 -399 -1074 6 C ATOM 2044 CE2 TYR A 330 63.681 -19.603 16.498 1.00100.61 C ANISOU 2044 CE2 TYR A 330 14127 12669 11430 -434 -1002 -22 C ATOM 2045 CZ TYR A 330 64.435 -19.796 15.351 1.00108.60 C ANISOU 2045 CZ TYR A 330 15097 13636 12532 -419 -1023 -47 C ATOM 2046 OH TYR A 330 64.925 -18.710 14.665 1.00110.36 O ANISOU 2046 OH TYR A 330 15271 13843 12818 -427 -978 -127 O ATOM 2047 N ALA A 331 62.613 -25.827 19.339 1.00103.42 N ANISOU 2047 N ALA A 331 14988 12875 11433 -413 -1140 391 N ATOM 2048 CA ALA A 331 61.806 -26.517 20.353 1.00105.02 C ANISOU 2048 CA ALA A 331 15340 13048 11516 -455 -1076 471 C ATOM 2049 C ALA A 331 62.671 -27.411 21.258 1.00112.46 C ANISOU 2049 C ALA A 331 16448 13950 12333 -375 -1185 519 C ATOM 2050 O ALA A 331 62.560 -27.295 22.477 1.00113.06 O ANISOU 2050 O ALA A 331 16652 14040 12265 -368 -1175 539 O ATOM 2051 CB ALA A 331 60.721 -27.349 19.695 1.00105.63 C ANISOU 2051 CB ALA A 331 15419 13061 11653 -537 -982 529 C ATOM 2052 N PHE A 332 63.548 -28.272 20.683 1.00111.02 N ANISOU 2052 N PHE A 332 16272 13713 12197 -304 -1293 533 N ATOM 2053 CA PHE A 332 64.399 -29.169 21.484 1.00113.00 C ANISOU 2053 CA PHE A 332 16682 13917 12334 -203 -1417 576 C ATOM 2054 C PHE A 332 65.650 -28.417 22.023 1.00118.34 C ANISOU 2054 C PHE A 332 17308 14669 12985 -100 -1564 485 C ATOM 2055 O PHE A 332 66.634 -29.046 22.435 1.00118.52 O ANISOU 2055 O PHE A 332 17408 14667 12959 15 -1713 487 O ATOM 2056 CB PHE A 332 64.824 -30.414 20.686 1.00115.01 C ANISOU 2056 CB PHE A 332 16965 14078 12655 -159 -1474 621 C ATOM 2057 CG PHE A 332 63.683 -31.350 20.352 1.00116.72 C ANISOU 2057 CG PHE A 332 17267 14204 12875 -257 -1350 710 C ATOM 2058 CD1 PHE A 332 63.174 -32.223 21.309 1.00121.21 C ANISOU 2058 CD1 PHE A 332 18059 14695 13302 -278 -1304 807 C ATOM 2059 CD2 PHE A 332 63.172 -31.418 19.062 1.00117.73 C ANISOU 2059 CD2 PHE A 332 17269 14315 13149 -327 -1283 694 C ATOM 2060 CE1 PHE A 332 62.129 -33.095 20.997 1.00122.35 C ANISOU 2060 CE1 PHE A 332 18274 14749 13464 -385 -1176 876 C ATOM 2061 CE2 PHE A 332 62.137 -32.303 18.747 1.00120.73 C ANISOU 2061 CE2 PHE A 332 17716 14613 13544 -423 -1179 760 C ATOM 2062 CZ PHE A 332 61.620 -33.129 19.717 1.00120.19 C ANISOU 2062 CZ PHE A 332 17847 14470 13349 -458 -1120 847 C ATOM 2063 N LEU A 333 65.568 -27.073 22.058 1.00115.40 N ANISOU 2063 N LEU A 333 16813 14386 12647 -139 -1523 400 N ATOM 2064 CA LEU A 333 66.547 -26.161 22.644 1.00115.97 C ANISOU 2064 CA LEU A 333 16829 14538 12697 -75 -1632 297 C ATOM 2065 C LEU A 333 65.807 -25.113 23.493 1.00120.93 C ANISOU 2065 C LEU A 333 17491 15226 13232 -140 -1540 275 C ATOM 2066 O LEU A 333 66.455 -24.364 24.231 1.00121.59 O ANISOU 2066 O LEU A 333 17570 15372 13259 -98 -1622 196 O ATOM 2067 CB LEU A 333 67.466 -25.495 21.601 1.00115.02 C ANISOU 2067 CB LEU A 333 16494 14455 12752 -57 -1675 184 C ATOM 2068 CG LEU A 333 68.567 -26.381 20.988 1.00119.89 C ANISOU 2068 CG LEU A 333 17065 15032 13458 36 -1796 166 C ATOM 2069 CD1 LEU A 333 69.318 -25.640 19.903 1.00118.97 C ANISOU 2069 CD1 LEU A 333 16741 14945 13518 25 -1785 52 C ATOM 2070 CD2 LEU A 333 69.554 -26.890 22.053 1.00124.11 C ANISOU 2070 CD2 LEU A 333 17691 15574 13892 165 -1984 149 C ATOM 2071 N ASP A 334 64.445 -25.109 23.439 1.00117.38 N ANISOU 2071 N ASP A 334 17079 14755 12766 -241 -1371 340 N ATOM 2072 CA ASP A 334 63.605 -24.237 24.272 1.00117.84 C ANISOU 2072 CA ASP A 334 17181 14858 12734 -303 -1260 326 C ATOM 2073 C ASP A 334 63.694 -24.703 25.726 1.00123.73 C ANISOU 2073 C ASP A 334 18156 15587 13268 -262 -1302 374 C ATOM 2074 O ASP A 334 63.464 -25.882 26.009 1.00124.10 O ANISOU 2074 O ASP A 334 18363 15556 13233 -253 -1298 473 O ATOM 2075 CB ASP A 334 62.139 -24.218 23.776 1.00119.06 C ANISOU 2075 CB ASP A 334 17295 14991 12950 -412 -1073 370 C ATOM 2076 CG ASP A 334 61.170 -23.359 24.590 1.00129.49 C ANISOU 2076 CG ASP A 334 18648 16354 14197 -476 -935 351 C ATOM 2077 OD1 ASP A 334 61.622 -22.353 25.194 1.00130.47 O ANISOU 2077 OD1 ASP A 334 18766 16538 14269 -447 -971 276 O ATOM 2078 OD2 ASP A 334 59.951 -23.635 24.544 1.00134.25 O ANISOU 2078 OD2 ASP A 334 19261 16931 14816 -558 -786 397 O ATOM 2079 N GLU A 335 64.041 -23.780 26.640 1.00120.90 N ANISOU 2079 N GLU A 335 17830 15293 12814 -237 -1344 302 N ATOM 2080 CA GLU A 335 64.228 -24.074 28.062 1.00122.50 C ANISOU 2080 CA GLU A 335 18268 15485 12793 -185 -1405 333 C ATOM 2081 C GLU A 335 62.877 -24.437 28.739 1.00126.64 C ANISOU 2081 C GLU A 335 18967 15958 13191 -275 -1207 427 C ATOM 2082 O GLU A 335 62.877 -25.090 29.787 1.00127.74 O ANISOU 2082 O GLU A 335 19355 16047 13132 -242 -1227 493 O ATOM 2083 CB GLU A 335 64.874 -22.860 28.756 1.00124.34 C ANISOU 2083 CB GLU A 335 18468 15804 12972 -150 -1489 212 C ATOM 2084 CG GLU A 335 65.682 -23.175 30.011 1.00135.83 C ANISOU 2084 CG GLU A 335 20128 17260 14223 -43 -1664 205 C ATOM 2085 CD GLU A 335 67.012 -23.898 29.842 1.00153.52 C ANISOU 2085 CD GLU A 335 22351 19489 16490 90 -1904 184 C ATOM 2086 OE1 GLU A 335 67.850 -23.788 30.766 1.00147.46 O ANISOU 2086 OE1 GLU A 335 21683 18753 15594 189 -2086 127 O ATOM 2087 OE2 GLU A 335 67.254 -24.500 28.770 1.00143.78 O ANISOU 2087 OE2 GLU A 335 20991 18223 15415 100 -1919 207 O ATOM 2088 N ASN A 336 61.738 -24.049 28.109 1.00121.60 N ANISOU 2088 N ASN A 336 18202 15327 12672 -386 -1017 429 N ATOM 2089 CA ASN A 336 60.382 -24.314 28.603 1.00121.69 C ANISOU 2089 CA ASN A 336 18321 15299 12615 -489 -804 493 C ATOM 2090 C ASN A 336 59.759 -25.586 27.959 1.00124.20 C ANISOU 2090 C ASN A 336 18662 15527 13002 -546 -726 590 C ATOM 2091 O ASN A 336 58.953 -26.251 28.617 1.00124.95 O ANISOU 2091 O ASN A 336 18929 15556 12991 -614 -585 664 O ATOM 2092 CB ASN A 336 59.476 -23.112 28.332 1.00121.37 C ANISOU 2092 CB ASN A 336 18113 15324 12679 -568 -651 419 C ATOM 2093 N PHE A 337 60.119 -25.913 26.685 1.00118.28 N ANISOU 2093 N PHE A 337 17749 14768 12426 -528 -804 584 N ATOM 2094 CA PHE A 337 59.584 -27.082 25.962 1.00117.38 C ANISOU 2094 CA PHE A 337 17641 14568 12390 -583 -745 661 C ATOM 2095 C PHE A 337 60.197 -28.403 26.511 1.00122.03 C ANISOU 2095 C PHE A 337 18470 15057 12839 -519 -835 755 C ATOM 2096 O PHE A 337 59.491 -29.415 26.561 1.00121.97 O ANISOU 2096 O PHE A 337 18582 14955 12806 -589 -724 838 O ATOM 2097 CB PHE A 337 59.846 -26.954 24.447 1.00117.13 C ANISOU 2097 CB PHE A 337 17381 14556 12568 -573 -809 617 C ATOM 2098 CG PHE A 337 59.247 -28.029 23.564 1.00118.15 C ANISOU 2098 CG PHE A 337 17489 14604 12797 -635 -752 675 C ATOM 2099 CD1 PHE A 337 57.918 -27.959 23.160 1.00120.84 C ANISOU 2099 CD1 PHE A 337 17737 14945 13233 -752 -590 669 C ATOM 2100 CD2 PHE A 337 60.034 -29.059 23.062 1.00119.98 C ANISOU 2100 CD2 PHE A 337 17774 14766 13046 -573 -870 719 C ATOM 2101 CE1 PHE A 337 57.369 -28.943 22.330 1.00121.53 C ANISOU 2101 CE1 PHE A 337 17797 14960 13418 -816 -548 707 C ATOM 2102 CE2 PHE A 337 59.488 -30.033 22.220 1.00122.48 C ANISOU 2102 CE2 PHE A 337 18076 15004 13456 -635 -818 764 C ATOM 2103 CZ PHE A 337 58.160 -29.970 21.860 1.00120.40 C ANISOU 2103 CZ PHE A 337 17728 14742 13279 -761 -661 756 C ATOM 2104 N LYS A 338 61.495 -28.384 26.926 1.00118.82 N ANISOU 2104 N LYS A 338 18132 14666 12347 -383 -1035 736 N ATOM 2105 CA LYS A 338 62.206 -29.542 27.506 1.00119.91 C ANISOU 2105 CA LYS A 338 18507 14712 12342 -286 -1158 816 C ATOM 2106 C LYS A 338 61.524 -30.026 28.800 1.00126.20 C ANISOU 2106 C LYS A 338 19603 15433 12912 -327 -1038 903 C ATOM 2107 O LYS A 338 61.254 -31.222 28.943 1.00126.91 O ANISOU 2107 O LYS A 338 19887 15400 12932 -343 -990 1005 O ATOM 2108 CB LYS A 338 63.682 -29.201 27.802 1.00122.11 C ANISOU 2108 CB LYS A 338 18771 15045 12580 -126 -1404 748 C ATOM 2109 CG LYS A 338 64.542 -28.889 26.588 1.00128.27 C ANISOU 2109 CG LYS A 338 19288 15879 13570 -76 -1522 663 C ATOM 2110 CD LYS A 338 65.928 -28.438 27.030 1.00136.94 C ANISOU 2110 CD LYS A 338 20355 17042 14635 64 -1746 573 C ATOM 2111 CE LYS A 338 66.819 -28.070 25.873 1.00145.08 C ANISOU 2111 CE LYS A 338 21123 18123 15879 103 -1837 474 C ATOM 2112 NZ LYS A 338 68.143 -27.570 26.328 1.00153.33 N ANISOU 2112 NZ LYS A 338 22108 19238 16914 224 -2043 363 N ATOM 2113 N ARG A 339 61.249 -29.084 29.736 1.00123.30 N ANISOU 2113 N ARG A 339 19289 15131 12428 -349 -979 860 N ATOM 2114 CA ARG A 339 60.598 -29.356 31.020 1.00151.10 C ANISOU 2114 CA ARG A 339 23102 18588 15720 -394 -843 928 C ATOM 2115 C ARG A 339 59.103 -29.625 30.828 1.00174.15 C ANISOU 2115 C ARG A 339 26006 21459 18705 -572 -556 969 C ATOM 2116 O ARG A 339 58.433 -28.924 30.068 1.00131.66 O ANISOU 2116 O ARG A 339 20364 16151 13512 -659 -453 902 O ATOM 2117 CB ARG A 339 60.804 -28.180 31.987 1.00151.76 C ANISOU 2117 CB ARG A 339 23225 18764 15674 -361 -870 850 C TER 2118 ARG A 339 ATOM 2119 N ILE B 54 76.118 35.315 18.147 1.00103.08 N ANISOU 2119 N ILE B 54 17774 9180 12211 82 -4478 -897 N ATOM 2120 CA ILE B 54 75.778 35.793 16.809 1.00101.44 C ANISOU 2120 CA ILE B 54 17345 9061 12138 -26 -4221 -805 C ATOM 2121 C ILE B 54 75.504 34.594 15.890 1.00103.58 C ANISOU 2121 C ILE B 54 17490 9477 12389 -47 -4036 -703 C ATOM 2122 O ILE B 54 76.373 33.733 15.723 1.00104.02 O ANISOU 2122 O ILE B 54 17418 9539 12567 -48 -4139 -734 O ATOM 2123 CB ILE B 54 76.904 36.694 16.246 1.00105.50 C ANISOU 2123 CB ILE B 54 17603 9493 12988 -126 -4305 -869 C ATOM 2124 N SER B 55 74.285 34.523 15.326 1.00 97.73 N ANISOU 2124 N SER B 55 16789 8849 11495 -57 -3773 -592 N ATOM 2125 CA SER B 55 73.866 33.428 14.445 1.00 95.81 C ANISOU 2125 CA SER B 55 16445 8745 11214 -75 -3584 -496 C ATOM 2126 C SER B 55 74.196 33.730 12.971 1.00 98.51 C ANISOU 2126 C SER B 55 16496 9153 11781 -181 -3425 -441 C ATOM 2127 O SER B 55 74.036 34.879 12.545 1.00 98.26 O ANISOU 2127 O SER B 55 16411 9095 11829 -235 -3347 -426 O ATOM 2128 CB SER B 55 72.368 33.173 14.594 1.00 98.01 C ANISOU 2128 CB SER B 55 16910 9110 11221 -29 -3388 -415 C ATOM 2129 N PRO B 56 74.643 32.725 12.165 1.00 93.87 N ANISOU 2129 N PRO B 56 15729 8646 11291 -210 -3369 -409 N ATOM 2130 CA PRO B 56 74.924 32.998 10.741 1.00 92.68 C ANISOU 2130 CA PRO B 56 15322 8560 11334 -307 -3200 -353 C ATOM 2131 C PRO B 56 73.632 33.252 9.971 1.00 93.98 C ANISOU 2131 C PRO B 56 15518 8830 11360 -321 -2941 -243 C ATOM 2132 O PRO B 56 72.578 32.742 10.362 1.00 92.58 O ANISOU 2132 O PRO B 56 15508 8710 10956 -258 -2870 -204 O ATOM 2133 CB PRO B 56 75.637 31.726 10.254 1.00 94.27 C ANISOU 2133 CB PRO B 56 15365 8820 11631 -311 -3218 -357 C ATOM 2134 CG PRO B 56 75.908 30.914 11.480 1.00 99.85 C ANISOU 2134 CG PRO B 56 16237 9469 12232 -218 -3437 -428 C ATOM 2135 CD PRO B 56 74.885 31.307 12.487 1.00 95.40 C ANISOU 2135 CD PRO B 56 15958 8872 11417 -153 -3448 -419 C ATOM 2136 N ALA B 57 73.716 34.020 8.860 1.00 89.28 N ANISOU 2136 N ALA B 57 14761 8255 10904 -402 -2797 -194 N ATOM 2137 CA ALA B 57 72.568 34.417 8.033 1.00 87.04 C ANISOU 2137 CA ALA B 57 14496 8060 10516 -412 -2569 -96 C ATOM 2138 C ALA B 57 72.001 33.239 7.194 1.00 87.61 C ANISOU 2138 C ALA B 57 14506 8280 10503 -401 -2406 -21 C ATOM 2139 O ALA B 57 71.399 33.476 6.143 1.00 86.22 O ANISOU 2139 O ALA B 57 14264 8182 10313 -428 -2220 57 O ATOM 2140 CB ALA B 57 72.973 35.551 7.105 1.00 88.10 C ANISOU 2140 CB ALA B 57 14490 8154 10832 -500 -2484 -67 C ATOM 2141 N ILE B 58 72.113 31.996 7.704 1.00 82.70 N ANISOU 2141 N ILE B 58 13927 7689 9808 -353 -2482 -46 N ATOM 2142 CA ILE B 58 71.599 30.795 7.042 1.00 81.11 C ANISOU 2142 CA ILE B 58 13680 7613 9524 -338 -2350 12 C ATOM 2143 C ILE B 58 70.049 30.902 6.869 1.00 82.01 C ANISOU 2143 C ILE B 58 13913 7811 9437 -305 -2177 80 C ATOM 2144 O ILE B 58 69.582 30.590 5.770 1.00 80.64 O ANISOU 2144 O ILE B 58 13638 7741 9261 -325 -2013 143 O ATOM 2145 CB ILE B 58 71.994 29.490 7.819 1.00 84.84 C ANISOU 2145 CB ILE B 58 14216 8076 9944 -285 -2488 -33 C ATOM 2146 CG1 ILE B 58 73.516 29.446 8.197 1.00 87.17 C ANISOU 2146 CG1 ILE B 58 14409 8272 10437 -299 -2701 -123 C ATOM 2147 CG2 ILE B 58 71.547 28.212 7.096 1.00 83.37 C ANISOU 2147 CG2 ILE B 58 13972 8011 9695 -276 -2358 21 C ATOM 2148 CD1 ILE B 58 74.570 29.543 7.037 1.00 95.74 C ANISOU 2148 CD1 ILE B 58 15218 9377 11780 -379 -2656 -127 C ATOM 2149 N PRO B 59 69.240 31.372 7.876 1.00 76.78 N ANISOU 2149 N PRO B 59 13454 7105 8614 -252 -2205 62 N ATOM 2150 CA PRO B 59 67.781 31.436 7.666 1.00 75.20 C ANISOU 2150 CA PRO B 59 13336 6987 8248 -221 -2034 115 C ATOM 2151 C PRO B 59 67.393 32.366 6.510 1.00 77.03 C ANISOU 2151 C PRO B 59 13460 7262 8547 -257 -1892 170 C ATOM 2152 O PRO B 59 66.417 32.085 5.814 1.00 75.36 O ANISOU 2152 O PRO B 59 13226 7152 8256 -243 -1737 222 O ATOM 2153 CB PRO B 59 67.254 31.980 8.999 1.00 77.46 C ANISOU 2153 CB PRO B 59 13846 7195 8390 -164 -2109 69 C ATOM 2154 CG PRO B 59 68.292 31.638 9.980 1.00 82.69 C ANISOU 2154 CG PRO B 59 14574 7759 9084 -148 -2318 0 C ATOM 2155 CD PRO B 59 69.581 31.796 9.250 1.00 78.71 C ANISOU 2155 CD PRO B 59 13864 7228 8816 -213 -2391 -14 C ATOM 2156 N VAL B 60 68.175 33.445 6.286 1.00 73.05 N ANISOU 2156 N VAL B 60 12890 6673 8194 -303 -1949 157 N ATOM 2157 CA VAL B 60 67.938 34.389 5.192 1.00 72.45 C ANISOU 2157 CA VAL B 60 12727 6614 8187 -341 -1824 214 C ATOM 2158 C VAL B 60 68.169 33.666 3.861 1.00 75.51 C ANISOU 2158 C VAL B 60 12942 7104 8644 -380 -1704 272 C ATOM 2159 O VAL B 60 67.340 33.787 2.954 1.00 75.12 O ANISOU 2159 O VAL B 60 12869 7135 8537 -369 -1556 333 O ATOM 2160 CB VAL B 60 68.812 35.665 5.311 1.00 77.53 C ANISOU 2160 CB VAL B 60 13345 7126 8987 -392 -1913 184 C ATOM 2161 CG1 VAL B 60 68.561 36.620 4.140 1.00 77.19 C ANISOU 2161 CG1 VAL B 60 13232 7090 9005 -431 -1774 255 C ATOM 2162 CG2 VAL B 60 68.567 36.375 6.637 1.00 78.06 C ANISOU 2162 CG2 VAL B 60 13593 7089 8975 -345 -2040 119 C ATOM 2163 N ILE B 61 69.265 32.877 3.767 1.00 71.35 N ANISOU 2163 N ILE B 61 12300 6574 8235 -415 -1773 245 N ATOM 2164 CA ILE B 61 69.614 32.110 2.564 1.00 70.12 C ANISOU 2164 CA ILE B 61 11981 6510 8153 -450 -1669 287 C ATOM 2165 C ILE B 61 68.491 31.096 2.279 1.00 72.39 C ANISOU 2165 C ILE B 61 12308 6922 8274 -397 -1563 323 C ATOM 2166 O ILE B 61 68.075 30.953 1.130 1.00 70.47 O ANISOU 2166 O ILE B 61 11988 6768 8019 -405 -1423 379 O ATOM 2167 CB ILE B 61 71.002 31.411 2.696 1.00 73.68 C ANISOU 2167 CB ILE B 61 12306 6925 8763 -486 -1782 232 C ATOM 2168 CG1 ILE B 61 72.109 32.416 3.107 1.00 75.09 C ANISOU 2168 CG1 ILE B 61 12438 6970 9123 -539 -1905 178 C ATOM 2169 CG2 ILE B 61 71.364 30.682 1.391 1.00 74.37 C ANISOU 2169 CG2 ILE B 61 12221 7107 8928 -520 -1657 272 C ATOM 2170 CD1 ILE B 61 73.492 31.811 3.428 1.00 81.36 C ANISOU 2170 CD1 ILE B 61 13108 7713 10092 -565 -2051 101 C ATOM 2171 N ILE B 62 67.975 30.434 3.342 1.00 69.77 N ANISOU 2171 N ILE B 62 12109 6590 7811 -344 -1630 288 N ATOM 2172 CA ILE B 62 66.887 29.449 3.246 1.00 68.91 C ANISOU 2172 CA ILE B 62 12048 6582 7551 -301 -1536 312 C ATOM 2173 C ILE B 62 65.612 30.168 2.726 1.00 73.37 C ANISOU 2173 C ILE B 62 12651 7203 8024 -276 -1398 355 C ATOM 2174 O ILE B 62 64.937 29.635 1.850 1.00 72.28 O ANISOU 2174 O ILE B 62 12453 7167 7842 -266 -1279 392 O ATOM 2175 CB ILE B 62 66.648 28.717 4.622 1.00 71.81 C ANISOU 2175 CB ILE B 62 12575 6911 7797 -255 -1633 267 C ATOM 2176 CG1 ILE B 62 67.899 27.908 5.084 1.00 72.51 C ANISOU 2176 CG1 ILE B 62 12629 6946 7975 -264 -1786 221 C ATOM 2177 CG2 ILE B 62 65.406 27.832 4.624 1.00 71.00 C ANISOU 2177 CG2 ILE B 62 12537 6899 7542 -220 -1518 289 C ATOM 2178 CD1 ILE B 62 68.489 26.833 4.074 1.00 77.70 C ANISOU 2178 CD1 ILE B 62 13115 7678 8730 -290 -1744 237 C ATOM 2179 N THR B 63 65.345 31.405 3.184 1.00 70.77 N ANISOU 2179 N THR B 63 12410 6801 7680 -265 -1423 346 N ATOM 2180 CA THR B 63 64.173 32.154 2.726 1.00 70.63 C ANISOU 2180 CA THR B 63 12427 6823 7584 -231 -1310 379 C ATOM 2181 C THR B 63 64.360 32.544 1.247 1.00 75.09 C ANISOU 2181 C THR B 63 12862 7433 8235 -262 -1215 439 C ATOM 2182 O THR B 63 63.369 32.642 0.520 1.00 74.75 O ANISOU 2182 O THR B 63 12812 7466 8123 -227 -1107 474 O ATOM 2183 CB THR B 63 63.945 33.371 3.617 1.00 81.97 C ANISOU 2183 CB THR B 63 13995 8160 8992 -207 -1372 348 C ATOM 2184 OG1 THR B 63 63.885 32.933 4.976 1.00 87.68 O ANISOU 2184 OG1 THR B 63 14849 8838 9625 -177 -1461 292 O ATOM 2185 CG2 THR B 63 62.667 34.123 3.273 1.00 79.29 C ANISOU 2185 CG2 THR B 63 13702 7856 8568 -157 -1267 370 C ATOM 2186 N ALA B 64 65.626 32.711 0.796 1.00 71.70 N ANISOU 2186 N ALA B 64 12331 6957 7956 -326 -1252 448 N ATOM 2187 CA ALA B 64 65.938 33.065 -0.588 1.00 71.22 C ANISOU 2187 CA ALA B 64 12159 6927 7974 -363 -1152 508 C ATOM 2188 C ALA B 64 65.750 31.864 -1.526 1.00 74.75 C ANISOU 2188 C ALA B 64 12511 7499 8391 -355 -1062 534 C ATOM 2189 O ALA B 64 65.198 32.040 -2.614 1.00 74.71 O ANISOU 2189 O ALA B 64 12479 7559 8350 -339 -952 585 O ATOM 2190 CB ALA B 64 67.357 33.590 -0.697 1.00 72.76 C ANISOU 2190 CB ALA B 64 12270 7026 8348 -440 -1206 501 C ATOM 2191 N VAL B 65 66.189 30.649 -1.119 1.00 70.12 N ANISOU 2191 N VAL B 65 11885 6941 7816 -360 -1115 496 N ATOM 2192 CA VAL B 65 66.047 29.478 -1.989 1.00 69.02 C ANISOU 2192 CA VAL B 65 11657 6912 7654 -353 -1037 513 C ATOM 2193 C VAL B 65 64.558 29.171 -2.124 1.00 71.33 C ANISOU 2193 C VAL B 65 12015 7291 7796 -292 -961 524 C ATOM 2194 O VAL B 65 64.076 29.080 -3.250 1.00 70.42 O ANISOU 2194 O VAL B 65 11847 7256 7652 -276 -862 561 O ATOM 2195 CB VAL B 65 66.857 28.219 -1.574 1.00 73.33 C ANISOU 2195 CB VAL B 65 12147 7464 8253 -367 -1113 469 C ATOM 2196 CG1 VAL B 65 68.356 28.480 -1.661 1.00 74.26 C ANISOU 2196 CG1 VAL B 65 12159 7508 8547 -426 -1177 450 C ATOM 2197 CG2 VAL B 65 66.469 27.695 -0.198 1.00 73.27 C ANISOU 2197 CG2 VAL B 65 12262 7421 8155 -332 -1211 423 C ATOM 2198 N TYR B 66 63.817 29.139 -0.993 1.00 67.84 N ANISOU 2198 N TYR B 66 11690 6826 7260 -256 -1006 489 N ATOM 2199 CA TYR B 66 62.372 28.923 -0.963 1.00 67.38 C ANISOU 2199 CA TYR B 66 11687 6838 7074 -202 -933 486 C ATOM 2200 C TYR B 66 61.649 29.865 -1.938 1.00 70.49 C ANISOU 2200 C TYR B 66 12068 7267 7449 -172 -849 525 C ATOM 2201 O TYR B 66 60.792 29.405 -2.689 1.00 68.72 O ANISOU 2201 O TYR B 66 11804 7136 7169 -138 -771 533 O ATOM 2202 CB TYR B 66 61.819 29.112 0.459 1.00 69.60 C ANISOU 2202 CB TYR B 66 12110 7063 7273 -174 -984 444 C ATOM 2203 CG TYR B 66 61.817 27.846 1.292 1.00 72.69 C ANISOU 2203 CG TYR B 66 12547 7461 7612 -175 -1017 411 C ATOM 2204 CD1 TYR B 66 62.991 27.352 1.850 1.00 75.18 C ANISOU 2204 CD1 TYR B 66 12866 7714 7987 -205 -1128 392 C ATOM 2205 CD2 TYR B 66 60.626 27.189 1.595 1.00 73.37 C ANISOU 2205 CD2 TYR B 66 12682 7604 7590 -145 -942 395 C ATOM 2206 CE1 TYR B 66 62.992 26.197 2.632 1.00 75.95 C ANISOU 2206 CE1 TYR B 66 13028 7804 8025 -198 -1167 366 C ATOM 2207 CE2 TYR B 66 60.611 26.044 2.392 1.00 74.25 C ANISOU 2207 CE2 TYR B 66 12857 7708 7647 -150 -963 372 C ATOM 2208 CZ TYR B 66 61.797 25.552 2.912 1.00 81.29 C ANISOU 2208 CZ TYR B 66 13768 8533 8585 -174 -1079 361 C ATOM 2209 OH TYR B 66 61.792 24.423 3.704 1.00 79.68 O ANISOU 2209 OH TYR B 66 13648 8310 8318 -172 -1108 343 O ATOM 2210 N SER B 67 62.038 31.155 -1.975 1.00 67.80 N ANISOU 2210 N SER B 67 11757 6845 7158 -184 -873 547 N ATOM 2211 CA SER B 67 61.440 32.137 -2.872 1.00 67.70 C ANISOU 2211 CA SER B 67 11752 6844 7126 -151 -807 589 C ATOM 2212 C SER B 67 61.632 31.725 -4.340 1.00 70.99 C ANISOU 2212 C SER B 67 12070 7339 7563 -158 -727 636 C ATOM 2213 O SER B 67 60.673 31.763 -5.116 1.00 70.79 O ANISOU 2213 O SER B 67 12045 7385 7467 -103 -665 652 O ATOM 2214 CB SER B 67 62.039 33.519 -2.626 1.00 72.74 C ANISOU 2214 CB SER B 67 12443 7361 7832 -177 -852 607 C ATOM 2215 OG SER B 67 61.819 33.970 -1.298 1.00 82.69 O ANISOU 2215 OG SER B 67 13808 8547 9064 -160 -930 557 O ATOM 2216 N VAL B 68 62.852 31.280 -4.701 1.00 66.78 N ANISOU 2216 N VAL B 68 11454 6795 7125 -221 -732 650 N ATOM 2217 CA VAL B 68 63.182 30.866 -6.070 1.00 66.00 C ANISOU 2217 CA VAL B 68 11266 6764 7045 -232 -648 692 C ATOM 2218 C VAL B 68 62.350 29.621 -6.426 1.00 67.83 C ANISOU 2218 C VAL B 68 11463 7116 7193 -187 -613 667 C ATOM 2219 O VAL B 68 61.523 29.697 -7.331 1.00 67.11 O ANISOU 2219 O VAL B 68 11376 7092 7031 -135 -553 688 O ATOM 2220 CB VAL B 68 64.711 30.617 -6.253 1.00 70.00 C ANISOU 2220 CB VAL B 68 11680 7230 7689 -311 -658 696 C ATOM 2221 CG1 VAL B 68 65.028 30.023 -7.625 1.00 69.43 C ANISOU 2221 CG1 VAL B 68 11519 7237 7624 -318 -559 730 C ATOM 2222 CG2 VAL B 68 65.509 31.901 -6.025 1.00 70.68 C ANISOU 2222 CG2 VAL B 68 11788 7193 7876 -365 -682 718 C ATOM 2223 N VAL B 69 62.516 28.520 -5.661 1.00 63.37 N ANISOU 2223 N VAL B 69 10875 6567 6634 -202 -661 619 N ATOM 2224 CA VAL B 69 61.838 27.227 -5.851 1.00 62.47 C ANISOU 2224 CA VAL B 69 10726 6550 6459 -173 -634 589 C ATOM 2225 C VAL B 69 60.293 27.425 -5.907 1.00 65.85 C ANISOU 2225 C VAL B 69 11203 7032 6783 -107 -597 575 C ATOM 2226 O VAL B 69 59.639 26.797 -6.740 1.00 65.43 O ANISOU 2226 O VAL B 69 11104 7069 6688 -73 -547 568 O ATOM 2227 CB VAL B 69 62.226 26.212 -4.732 1.00 66.34 C ANISOU 2227 CB VAL B 69 11226 7015 6966 -199 -705 542 C ATOM 2228 CG1 VAL B 69 61.576 24.850 -4.955 1.00 65.65 C ANISOU 2228 CG1 VAL B 69 11103 7014 6826 -179 -671 514 C ATOM 2229 CG2 VAL B 69 63.737 26.051 -4.627 1.00 66.67 C ANISOU 2229 CG2 VAL B 69 11208 6999 7125 -253 -761 541 C ATOM 2230 N PHE B 70 59.729 28.310 -5.052 1.00 62.21 N ANISOU 2230 N PHE B 70 10832 6516 6291 -85 -623 564 N ATOM 2231 CA PHE B 70 58.287 28.575 -5.015 1.00 61.41 C ANISOU 2231 CA PHE B 70 10766 6457 6109 -20 -589 539 C ATOM 2232 C PHE B 70 57.811 29.234 -6.325 1.00 65.67 C ANISOU 2232 C PHE B 70 11284 7040 6627 32 -545 574 C ATOM 2233 O PHE B 70 56.912 28.694 -6.971 1.00 64.40 O ANISOU 2233 O PHE B 70 11081 6967 6421 79 -510 552 O ATOM 2234 CB PHE B 70 57.909 29.457 -3.806 1.00 62.85 C ANISOU 2234 CB PHE B 70 11052 6561 6268 -5 -625 516 C ATOM 2235 CG PHE B 70 56.482 29.950 -3.798 1.00 63.83 C ANISOU 2235 CG PHE B 70 11205 6719 6329 68 -586 486 C ATOM 2236 CD1 PHE B 70 55.430 29.084 -3.526 1.00 66.12 C ANISOU 2236 CD1 PHE B 70 11469 7079 6573 91 -542 433 C ATOM 2237 CD2 PHE B 70 56.193 31.295 -3.994 1.00 65.94 C ANISOU 2237 CD2 PHE B 70 11524 6940 6591 111 -595 505 C ATOM 2238 CE1 PHE B 70 54.108 29.539 -3.534 1.00 67.17 C ANISOU 2238 CE1 PHE B 70 11608 7246 6668 160 -505 394 C ATOM 2239 CE2 PHE B 70 54.871 31.755 -3.974 1.00 68.69 C ANISOU 2239 CE2 PHE B 70 11891 7318 6891 189 -568 468 C ATOM 2240 CZ PHE B 70 53.838 30.876 -3.735 1.00 66.51 C ANISOU 2240 CZ PHE B 70 11571 7120 6580 213 -523 408 C ATOM 2241 N VAL B 71 58.413 30.373 -6.715 1.00 63.53 N ANISOU 2241 N VAL B 71 11050 6702 6388 24 -551 627 N ATOM 2242 CA VAL B 71 58.013 31.108 -7.918 1.00 64.45 C ANISOU 2242 CA VAL B 71 11179 6839 6470 77 -514 670 C ATOM 2243 C VAL B 71 58.311 30.248 -9.180 1.00 69.23 C ANISOU 2243 C VAL B 71 11710 7529 7066 76 -466 692 C ATOM 2244 O VAL B 71 57.398 30.044 -9.983 1.00 69.10 O ANISOU 2244 O VAL B 71 11682 7588 6984 145 -446 680 O ATOM 2245 CB VAL B 71 58.689 32.503 -8.006 1.00 69.06 C ANISOU 2245 CB VAL B 71 11832 7313 7094 57 -523 729 C ATOM 2246 CG1 VAL B 71 58.338 33.207 -9.318 1.00 69.31 C ANISOU 2246 CG1 VAL B 71 11899 7358 7078 114 -481 785 C ATOM 2247 CG2 VAL B 71 58.293 33.374 -6.813 1.00 69.00 C ANISOU 2247 CG2 VAL B 71 11906 7224 7087 72 -576 699 C ATOM 2248 N VAL B 72 59.550 29.720 -9.330 1.00 65.51 N ANISOU 2248 N VAL B 72 11184 7045 6661 3 -453 712 N ATOM 2249 CA VAL B 72 59.941 28.892 -10.483 1.00 65.16 C ANISOU 2249 CA VAL B 72 11071 7075 6611 0 -401 727 C ATOM 2250 C VAL B 72 58.909 27.747 -10.660 1.00 69.80 C ANISOU 2250 C VAL B 72 11616 7769 7138 50 -403 668 C ATOM 2251 O VAL B 72 58.399 27.550 -11.764 1.00 69.43 O ANISOU 2251 O VAL B 72 11557 7792 7031 105 -372 672 O ATOM 2252 CB VAL B 72 61.396 28.348 -10.334 1.00 68.53 C ANISOU 2252 CB VAL B 72 11429 7471 7138 -85 -396 733 C ATOM 2253 CG1 VAL B 72 61.710 27.257 -11.353 1.00 68.18 C ANISOU 2253 CG1 VAL B 72 11307 7514 7086 -83 -344 728 C ATOM 2254 CG2 VAL B 72 62.419 29.473 -10.420 1.00 68.91 C ANISOU 2254 CG2 VAL B 72 11500 7419 7262 -139 -377 789 C ATOM 2255 N GLY B 73 58.576 27.066 -9.562 1.00 67.18 N ANISOU 2255 N GLY B 73 11269 7438 6817 33 -439 613 N ATOM 2256 CA GLY B 73 57.632 25.949 -9.548 1.00 66.97 C ANISOU 2256 CA GLY B 73 11198 7495 6754 62 -435 552 C ATOM 2257 C GLY B 73 56.175 26.307 -9.760 1.00 71.57 C ANISOU 2257 C GLY B 73 11797 8123 7275 140 -432 518 C ATOM 2258 O GLY B 73 55.438 25.542 -10.383 1.00 70.96 O ANISOU 2258 O GLY B 73 11666 8127 7169 178 -420 477 O ATOM 2259 N LEU B 74 55.736 27.453 -9.229 1.00 68.81 N ANISOU 2259 N LEU B 74 11516 7717 6913 168 -448 527 N ATOM 2260 CA LEU B 74 54.350 27.877 -9.382 1.00 68.73 C ANISOU 2260 CA LEU B 74 11513 7743 6857 250 -451 486 C ATOM 2261 C LEU B 74 54.128 28.447 -10.803 1.00 71.59 C ANISOU 2261 C LEU B 74 11888 8139 7175 323 -452 520 C ATOM 2262 O LEU B 74 53.137 28.098 -11.432 1.00 71.07 O ANISOU 2262 O LEU B 74 11782 8147 7076 391 -460 473 O ATOM 2263 CB LEU B 74 53.989 28.908 -8.299 1.00 69.26 C ANISOU 2263 CB LEU B 74 11654 7735 6927 262 -469 477 C ATOM 2264 CG LEU B 74 52.509 29.139 -8.034 1.00 74.54 C ANISOU 2264 CG LEU B 74 12313 8438 7571 336 -466 409 C ATOM 2265 CD1 LEU B 74 51.855 27.885 -7.447 1.00 74.29 C ANISOU 2265 CD1 LEU B 74 12214 8464 7550 310 -432 336 C ATOM 2266 CD2 LEU B 74 52.324 30.267 -7.048 1.00 78.11 C ANISOU 2266 CD2 LEU B 74 12850 8807 8023 351 -480 406 C ATOM 2267 N VAL B 75 55.077 29.261 -11.324 1.00 67.97 N ANISOU 2267 N VAL B 75 11486 7621 6717 306 -443 600 N ATOM 2268 CA VAL B 75 54.998 29.845 -12.678 1.00 68.64 C ANISOU 2268 CA VAL B 75 11616 7722 6744 371 -434 648 C ATOM 2269 C VAL B 75 55.163 28.726 -13.731 1.00 73.41 C ANISOU 2269 C VAL B 75 12159 8416 7319 378 -409 637 C ATOM 2270 O VAL B 75 54.351 28.636 -14.657 1.00 73.47 O ANISOU 2270 O VAL B 75 12169 8485 7261 464 -428 614 O ATOM 2271 CB VAL B 75 56.045 30.985 -12.895 1.00 72.76 C ANISOU 2271 CB VAL B 75 12221 8142 7281 334 -410 741 C ATOM 2272 CG1 VAL B 75 56.088 31.452 -14.347 1.00 72.93 C ANISOU 2272 CG1 VAL B 75 12307 8174 7229 392 -382 802 C ATOM 2273 CG2 VAL B 75 55.779 32.161 -11.964 1.00 73.02 C ANISOU 2273 CG2 VAL B 75 12326 8081 7336 342 -445 746 C ATOM 2274 N GLY B 76 56.204 27.904 -13.570 1.00 69.93 N ANISOU 2274 N GLY B 76 11664 7978 6928 294 -377 646 N ATOM 2275 CA GLY B 76 56.533 26.806 -14.472 1.00 69.69 C ANISOU 2275 CA GLY B 76 11575 8023 6881 291 -349 633 C ATOM 2276 C GLY B 76 55.381 25.866 -14.740 1.00 73.98 C ANISOU 2276 C GLY B 76 12060 8659 7390 349 -380 550 C ATOM 2277 O GLY B 76 54.968 25.702 -15.888 1.00 73.62 O ANISOU 2277 O GLY B 76 12022 8673 7278 419 -385 541 O ATOM 2278 N ASN B 77 54.822 25.285 -13.671 1.00 71.60 N ANISOU 2278 N ASN B 77 11708 8364 7134 322 -402 487 N ATOM 2279 CA ASN B 77 53.713 24.328 -13.750 1.00 71.93 C ANISOU 2279 CA ASN B 77 11677 8482 7170 358 -422 398 C ATOM 2280 C ASN B 77 52.408 25.010 -14.194 1.00 77.47 C ANISOU 2280 C ASN B 77 12393 9214 7827 461 -461 361 C ATOM 2281 O ASN B 77 51.598 24.367 -14.865 1.00 77.59 O ANISOU 2281 O ASN B 77 12353 9303 7825 516 -488 294 O ATOM 2282 CB ASN B 77 53.507 23.623 -12.415 1.00 70.66 C ANISOU 2282 CB ASN B 77 11477 8303 7069 293 -416 350 C ATOM 2283 CG ASN B 77 54.603 22.633 -12.113 1.00 87.47 C ANISOU 2283 CG ASN B 77 13578 10418 9240 211 -398 364 C ATOM 2284 OD1 ASN B 77 54.734 21.592 -12.771 1.00 83.14 O ANISOU 2284 OD1 ASN B 77 12974 9924 8693 209 -393 335 O ATOM 2285 ND2 ASN B 77 55.391 22.903 -11.089 1.00 77.19 N ANISOU 2285 ND2 ASN B 77 12314 9040 7975 149 -399 398 N ATOM 2286 N SER B 78 52.219 26.298 -13.873 1.00 74.82 N ANISOU 2286 N SER B 78 12131 8819 7478 494 -475 396 N ATOM 2287 CA SER B 78 51.031 27.007 -14.341 1.00 75.80 C ANISOU 2287 CA SER B 78 12272 8964 7564 605 -523 360 C ATOM 2288 C SER B 78 51.144 27.295 -15.839 1.00 81.59 C ANISOU 2288 C SER B 78 13062 9726 8214 683 -547 398 C ATOM 2289 O SER B 78 50.127 27.325 -16.535 1.00 82.25 O ANISOU 2289 O SER B 78 13132 9860 8260 785 -605 342 O ATOM 2290 CB SER B 78 50.818 28.299 -13.561 1.00 79.13 C ANISOU 2290 CB SER B 78 12765 9307 7995 622 -533 385 C ATOM 2291 OG SER B 78 50.567 28.021 -12.195 1.00 87.00 O ANISOU 2291 OG SER B 78 13722 10282 9051 564 -510 339 O ATOM 2292 N LEU B 79 52.384 27.468 -16.335 1.00 78.39 N ANISOU 2292 N LEU B 79 12717 9285 7780 638 -501 488 N ATOM 2293 CA LEU B 79 52.657 27.736 -17.742 1.00 79.25 C ANISOU 2293 CA LEU B 79 12903 9411 7796 701 -499 539 C ATOM 2294 C LEU B 79 52.367 26.484 -18.571 1.00 83.56 C ANISOU 2294 C LEU B 79 13381 10055 8313 732 -515 473 C ATOM 2295 O LEU B 79 51.728 26.595 -19.619 1.00 83.63 O ANISOU 2295 O LEU B 79 13432 10106 8238 838 -566 452 O ATOM 2296 CB LEU B 79 54.120 28.200 -17.913 1.00 79.58 C ANISOU 2296 CB LEU B 79 13013 9384 7839 623 -420 647 C ATOM 2297 CG LEU B 79 54.558 28.789 -19.274 1.00 85.78 C ANISOU 2297 CG LEU B 79 13917 10155 8521 676 -386 727 C ATOM 2298 CD1 LEU B 79 55.805 29.593 -19.137 1.00 86.30 C ANISOU 2298 CD1 LEU B 79 14047 10125 8617 592 -304 830 C ATOM 2299 CD2 LEU B 79 54.778 27.708 -20.353 1.00 88.92 C ANISOU 2299 CD2 LEU B 79 14288 10639 8860 697 -362 703 C ATOM 2300 N VAL B 80 52.803 25.293 -18.076 1.00 79.89 N ANISOU 2300 N VAL B 80 12818 9622 7916 645 -483 435 N ATOM 2301 CA VAL B 80 52.624 23.984 -18.734 1.00 79.68 C ANISOU 2301 CA VAL B 80 12718 9678 7877 658 -495 366 C ATOM 2302 C VAL B 80 51.127 23.701 -18.928 1.00 84.02 C ANISOU 2302 C VAL B 80 13211 10288 8423 746 -578 260 C ATOM 2303 O VAL B 80 50.710 23.409 -20.052 1.00 83.63 O ANISOU 2303 O VAL B 80 13174 10295 8306 831 -625 223 O ATOM 2304 CB VAL B 80 53.309 22.831 -17.947 1.00 82.57 C ANISOU 2304 CB VAL B 80 12995 10047 8331 548 -452 344 C ATOM 2305 CG1 VAL B 80 52.984 21.470 -18.558 1.00 82.30 C ANISOU 2305 CG1 VAL B 80 12884 10092 8295 564 -473 261 C ATOM 2306 CG2 VAL B 80 54.816 23.037 -17.878 1.00 82.29 C ANISOU 2306 CG2 VAL B 80 12995 9958 8312 470 -382 432 C ATOM 2307 N MET B 81 50.327 23.805 -17.841 1.00 80.93 N ANISOU 2307 N MET B 81 12759 9882 8108 728 -594 207 N ATOM 2308 CA MET B 81 48.882 23.565 -17.878 1.00 81.43 C ANISOU 2308 CA MET B 81 12743 9996 8201 800 -662 95 C ATOM 2309 C MET B 81 48.204 24.497 -18.881 1.00 87.02 C ANISOU 2309 C MET B 81 13522 10715 8826 939 -743 92 C ATOM 2310 O MET B 81 47.408 24.021 -19.692 1.00 88.00 O ANISOU 2310 O MET B 81 13602 10903 8931 1022 -817 7 O ATOM 2311 CB MET B 81 48.250 23.733 -16.494 1.00 83.39 C ANISOU 2311 CB MET B 81 12933 10213 8539 754 -640 53 C ATOM 2312 CG MET B 81 48.736 22.710 -15.490 1.00 86.35 C ANISOU 2312 CG MET B 81 13249 10575 8986 630 -572 44 C ATOM 2313 SD MET B 81 47.945 22.829 -13.866 1.00 90.63 S ANISOU 2313 SD MET B 81 13744 11079 9613 578 -530 -7 S ATOM 2314 CE MET B 81 48.495 24.451 -13.334 1.00 87.28 C ANISOU 2314 CE MET B 81 13445 10569 9150 592 -524 90 C ATOM 2315 N PHE B 82 48.567 25.803 -18.873 1.00 83.08 N ANISOU 2315 N PHE B 82 13142 10148 8276 968 -736 183 N ATOM 2316 CA PHE B 82 48.019 26.809 -19.787 1.00 83.76 C ANISOU 2316 CA PHE B 82 13327 10224 8273 1104 -814 198 C ATOM 2317 C PHE B 82 48.192 26.379 -21.257 1.00 88.62 C ANISOU 2317 C PHE B 82 14002 10891 8779 1177 -851 201 C ATOM 2318 O PHE B 82 47.227 26.421 -22.024 1.00 89.32 O ANISOU 2318 O PHE B 82 14094 11020 8823 1302 -957 130 O ATOM 2319 CB PHE B 82 48.687 28.174 -19.558 1.00 85.51 C ANISOU 2319 CB PHE B 82 13685 10347 8456 1096 -778 316 C ATOM 2320 N VAL B 83 49.409 25.936 -21.631 1.00 84.31 N ANISOU 2320 N VAL B 83 13498 10341 8193 1103 -768 275 N ATOM 2321 CA VAL B 83 49.743 25.506 -22.991 1.00 84.35 C ANISOU 2321 CA VAL B 83 13574 10391 8084 1162 -777 287 C ATOM 2322 C VAL B 83 48.857 24.298 -23.381 1.00 88.22 C ANISOU 2322 C VAL B 83 13948 10973 8599 1208 -859 149 C ATOM 2323 O VAL B 83 48.265 24.314 -24.453 1.00 88.34 O ANISOU 2323 O VAL B 83 14019 11026 8522 1332 -950 106 O ATOM 2324 CB VAL B 83 51.260 25.178 -23.120 1.00 87.47 C ANISOU 2324 CB VAL B 83 14004 10764 8465 1055 -652 379 C ATOM 2325 CG1 VAL B 83 51.597 24.579 -24.482 1.00 87.94 C ANISOU 2325 CG1 VAL B 83 14127 10877 8409 1111 -646 377 C ATOM 2326 CG2 VAL B 83 52.113 26.416 -22.861 1.00 87.36 C ANISOU 2326 CG2 VAL B 83 14104 10655 8436 1012 -576 508 C ATOM 2327 N ILE B 84 48.726 23.299 -22.492 1.00 84.86 N ANISOU 2327 N ILE B 84 13372 10574 8298 1114 -834 78 N ATOM 2328 CA ILE B 84 47.946 22.078 -22.736 1.00 85.14 C ANISOU 2328 CA ILE B 84 13283 10683 8382 1133 -897 -54 C ATOM 2329 C ILE B 84 46.435 22.418 -22.863 1.00 90.50 C ANISOU 2329 C ILE B 84 13908 11389 9088 1247 -1021 -163 C ATOM 2330 O ILE B 84 45.787 21.897 -23.770 1.00 91.07 O ANISOU 2330 O ILE B 84 13956 11519 9129 1336 -1118 -255 O ATOM 2331 CB ILE B 84 48.199 21.031 -21.610 1.00 87.09 C ANISOU 2331 CB ILE B 84 13399 10931 8761 993 -825 -89 C ATOM 2332 CG1 ILE B 84 49.678 20.564 -21.640 1.00 86.85 C ANISOU 2332 CG1 ILE B 84 13410 10881 8709 900 -727 -3 C ATOM 2333 CG2 ILE B 84 47.255 19.825 -21.737 1.00 87.72 C ANISOU 2333 CG2 ILE B 84 13343 11072 8914 1003 -886 -232 C ATOM 2334 CD1 ILE B 84 50.092 19.634 -20.531 1.00 93.59 C ANISOU 2334 CD1 ILE B 84 14167 11717 9676 771 -664 -19 C ATOM 2335 N ILE B 85 45.892 23.287 -21.990 1.00 87.26 N ANISOU 2335 N ILE B 85 13478 10936 8739 1250 -1024 -160 N ATOM 2336 CA ILE B 85 44.467 23.645 -22.015 1.00 88.12 C ANISOU 2336 CA ILE B 85 13518 11068 8897 1357 -1135 -271 C ATOM 2337 C ILE B 85 44.137 24.473 -23.289 1.00 95.30 C ANISOU 2337 C ILE B 85 14561 11979 9671 1525 -1254 -259 C ATOM 2338 O ILE B 85 43.144 24.174 -23.956 1.00 96.35 O ANISOU 2338 O ILE B 85 14638 12163 9810 1634 -1380 -377 O ATOM 2339 CB ILE B 85 44.049 24.420 -20.722 1.00 90.32 C ANISOU 2339 CB ILE B 85 13753 11296 9270 1320 -1093 -268 C ATOM 2340 CG1 ILE B 85 44.255 23.536 -19.462 1.00 89.33 C ANISOU 2340 CG1 ILE B 85 13509 11167 9265 1164 -983 -290 C ATOM 2341 CG2 ILE B 85 42.583 24.901 -20.806 1.00 91.62 C ANISOU 2341 CG2 ILE B 85 13842 11480 9490 1444 -1208 -387 C ATOM 2342 CD1 ILE B 85 44.023 24.224 -18.113 1.00 96.66 C ANISOU 2342 CD1 ILE B 85 14417 12040 10268 1114 -920 -276 C ATOM 2343 N ARG B 86 44.966 25.474 -23.633 1.00 93.10 N ANISOU 2343 N ARG B 86 14462 11639 9273 1546 -1217 -121 N ATOM 2344 CA ARG B 86 44.682 26.384 -24.747 1.00 94.93 C ANISOU 2344 CA ARG B 86 14853 11851 9364 1705 -1320 -90 C ATOM 2345 C ARG B 86 45.219 25.907 -26.124 1.00100.80 C ANISOU 2345 C ARG B 86 15716 12630 9955 1761 -1339 -62 C ATOM 2346 O ARG B 86 44.778 26.461 -27.134 1.00101.81 O ANISOU 2346 O ARG B 86 15973 12753 9959 1912 -1450 -66 O ATOM 2347 CB ARG B 86 45.296 27.765 -24.465 1.00 95.08 C ANISOU 2347 CB ARG B 86 15027 11773 9326 1699 -1261 52 C ATOM 2348 N TYR B 87 46.154 24.932 -26.193 1.00 97.77 N ANISOU 2348 N TYR B 87 15303 12275 9569 1652 -1237 -36 N ATOM 2349 CA TYR B 87 46.722 24.581 -27.503 1.00 99.19 C ANISOU 2349 CA TYR B 87 15613 12481 9592 1709 -1239 -4 C ATOM 2350 C TYR B 87 46.724 23.065 -27.794 1.00104.90 C ANISOU 2350 C TYR B 87 16219 13285 10355 1672 -1248 -107 C ATOM 2351 O TYR B 87 46.386 22.682 -28.916 1.00106.07 O ANISOU 2351 O TYR B 87 16425 13478 10398 1783 -1342 -168 O ATOM 2352 CB TYR B 87 48.174 25.091 -27.615 1.00100.15 C ANISOU 2352 CB TYR B 87 15878 12543 9632 1627 -1082 162 C ATOM 2353 CG TYR B 87 48.304 26.592 -27.462 1.00102.82 C ANISOU 2353 CG TYR B 87 16358 12788 9919 1659 -1064 276 C ATOM 2354 CD1 TYR B 87 48.214 27.435 -28.565 1.00106.51 C ANISOU 2354 CD1 TYR B 87 17035 13220 10213 1792 -1115 337 C ATOM 2355 CD2 TYR B 87 48.503 27.172 -26.211 1.00102.64 C ANISOU 2355 CD2 TYR B 87 16274 12707 10018 1560 -1001 320 C ATOM 2356 CE1 TYR B 87 48.306 28.819 -28.428 1.00107.93 C ANISOU 2356 CE1 TYR B 87 17355 13303 10349 1823 -1102 442 C ATOM 2357 CE2 TYR B 87 48.589 28.555 -26.060 1.00104.02 C ANISOU 2357 CE2 TYR B 87 16579 12789 10153 1591 -992 416 C ATOM 2358 CZ TYR B 87 48.498 29.375 -27.174 1.00113.02 C ANISOU 2358 CZ TYR B 87 17923 13890 11129 1720 -1041 479 C ATOM 2359 OH TYR B 87 48.592 30.738 -27.041 1.00114.88 O ANISOU 2359 OH TYR B 87 18300 14023 11327 1749 -1032 578 O ATOM 2360 N THR B 88 47.158 22.221 -26.833 1.00101.13 N ANISOU 2360 N THR B 88 15594 12817 10014 1522 -1153 -123 N ATOM 2361 CA THR B 88 47.280 20.771 -27.038 1.00100.98 C ANISOU 2361 CA THR B 88 15470 12858 10039 1474 -1148 -210 C ATOM 2362 C THR B 88 45.929 20.034 -26.921 1.00106.29 C ANISOU 2362 C THR B 88 15982 13583 10820 1516 -1275 -381 C ATOM 2363 O THR B 88 45.766 18.979 -27.540 1.00106.36 O ANISOU 2363 O THR B 88 15943 13644 10826 1536 -1326 -474 O ATOM 2364 CB THR B 88 48.254 20.182 -26.024 1.00106.89 C ANISOU 2364 CB THR B 88 16137 13585 10893 1304 -1007 -159 C ATOM 2365 N LYS B 89 44.988 20.568 -26.096 1.00103.43 N ANISOU 2365 N LYS B 89 15528 13202 10566 1523 -1319 -428 N ATOM 2366 CA LYS B 89 43.642 20.033 -25.797 1.00103.87 C ANISOU 2366 CA LYS B 89 15409 13297 10761 1550 -1420 -592 C ATOM 2367 C LYS B 89 43.711 18.601 -25.137 1.00107.33 C ANISOU 2367 C LYS B 89 15683 13758 11339 1412 -1353 -666 C ATOM 2368 O LYS B 89 42.664 17.992 -24.890 1.00107.68 O ANISOU 2368 O LYS B 89 15570 13829 11513 1411 -1415 -805 O ATOM 2369 CB LYS B 89 42.770 19.983 -27.066 1.00107.79 C ANISOU 2369 CB LYS B 89 15933 13840 11182 1720 -1599 -701 C ATOM 2370 N MET B 90 44.924 18.137 -24.856 1.00102.25 N ANISOU 2370 N MET B 90 15081 13095 10675 1301 -1229 -572 N ATOM 2371 CA MET B 90 45.149 16.846 -24.214 1.00100.92 C ANISOU 2371 CA MET B 90 14791 12931 10622 1172 -1161 -619 C ATOM 2372 C MET B 90 44.274 15.706 -24.730 1.00102.55 C ANISOU 2372 C MET B 90 14877 13188 10899 1201 -1257 -780 C ATOM 2373 O MET B 90 43.584 15.046 -23.953 1.00101.86 O ANISOU 2373 O MET B 90 14640 13097 10964 1126 -1244 -869 O ATOM 2374 CB MET B 90 44.986 16.975 -22.696 1.00102.70 C ANISOU 2374 CB MET B 90 14930 13111 10981 1056 -1071 -600 C ATOM 2375 CG MET B 90 43.547 17.146 -22.239 1.00107.48 C ANISOU 2375 CG MET B 90 15407 13728 11703 1088 -1132 -717 C ATOM 2376 SD MET B 90 43.393 17.240 -20.445 1.00111.07 S ANISOU 2376 SD MET B 90 15781 14126 12295 950 -1004 -694 S ATOM 2377 CE MET B 90 41.685 17.754 -20.278 1.00109.15 C ANISOU 2377 CE MET B 90 15407 13906 12161 1033 -1086 -833 C ATOM 2378 N LYS B 91 44.303 15.476 -26.038 1.00 97.61 N ANISOU 2378 N LYS B 91 14322 12604 10160 1308 -1350 -820 N ATOM 2379 CA LYS B 91 43.530 14.377 -26.632 1.00 96.93 C ANISOU 2379 CA LYS B 91 14131 12563 10135 1343 -1457 -981 C ATOM 2380 C LYS B 91 44.363 13.072 -26.607 1.00 96.91 C ANISOU 2380 C LYS B 91 14104 12560 10157 1241 -1380 -983 C ATOM 2381 O LYS B 91 43.795 11.976 -26.629 1.00 96.36 O ANISOU 2381 O LYS B 91 13912 12506 10195 1209 -1427 -1111 O ATOM 2382 CB LYS B 91 43.094 14.727 -28.067 1.00100.65 C ANISOU 2382 CB LYS B 91 14701 13077 10465 1522 -1614 -1038 C ATOM 2383 N THR B 92 45.709 13.205 -26.546 1.00 90.37 N ANISOU 2383 N THR B 92 13388 11709 9241 1189 -1264 -846 N ATOM 2384 CA THR B 92 46.668 12.096 -26.489 1.00 88.37 C ANISOU 2384 CA THR B 92 13125 11448 9004 1100 -1184 -832 C ATOM 2385 C THR B 92 46.944 11.705 -25.034 1.00 88.60 C ANISOU 2385 C THR B 92 13064 11423 9176 945 -1075 -794 C ATOM 2386 O THR B 92 46.797 12.537 -24.141 1.00 87.15 O ANISOU 2386 O THR B 92 12876 11206 9030 908 -1029 -732 O ATOM 2387 CB THR B 92 47.988 12.468 -27.205 1.00 95.88 C ANISOU 2387 CB THR B 92 14234 12401 9794 1130 -1114 -713 C ATOM 2388 OG1 THR B 92 48.617 13.561 -26.533 1.00 94.23 O ANISOU 2388 OG1 THR B 92 14089 12148 9565 1087 -1020 -573 O ATOM 2389 CG2 THR B 92 47.792 12.795 -28.684 1.00 95.69 C ANISOU 2389 CG2 THR B 92 14331 12424 9602 1286 -1209 -743 C ATOM 2390 N ALA B 93 47.374 10.449 -24.806 1.00 83.61 N ANISOU 2390 N ALA B 93 12377 10778 8614 861 -1036 -830 N ATOM 2391 CA ALA B 93 47.702 9.911 -23.484 1.00 81.61 C ANISOU 2391 CA ALA B 93 12061 10464 8482 720 -940 -796 C ATOM 2392 C ALA B 93 48.924 10.613 -22.887 1.00 83.24 C ANISOU 2392 C ALA B 93 12357 10631 8640 670 -837 -644 C ATOM 2393 O ALA B 93 48.984 10.806 -21.672 1.00 82.57 O ANISOU 2393 O ALA B 93 12249 10494 8629 582 -774 -595 O ATOM 2394 CB ALA B 93 47.962 8.413 -23.583 1.00 82.32 C ANISOU 2394 CB ALA B 93 12097 10544 8637 663 -938 -868 C ATOM 2395 N THR B 94 49.886 11.004 -23.749 1.00 78.67 N ANISOU 2395 N THR B 94 11882 10072 7936 726 -819 -574 N ATOM 2396 CA THR B 94 51.139 11.678 -23.387 1.00 76.92 C ANISOU 2396 CA THR B 94 11740 9815 7672 685 -725 -439 C ATOM 2397 C THR B 94 50.828 12.975 -22.619 1.00 76.78 C ANISOU 2397 C THR B 94 11749 9764 7659 676 -707 -366 C ATOM 2398 O THR B 94 51.236 13.105 -21.465 1.00 75.12 O ANISOU 2398 O THR B 94 11524 9500 7519 585 -646 -310 O ATOM 2399 CB THR B 94 51.968 11.951 -24.664 1.00 88.10 C ANISOU 2399 CB THR B 94 13260 11266 8948 764 -708 -396 C ATOM 2400 OG1 THR B 94 52.156 10.725 -25.384 1.00 89.47 O ANISOU 2400 OG1 THR B 94 13407 11471 9115 782 -731 -479 O ATOM 2401 CG2 THR B 94 53.316 12.602 -24.367 1.00 85.84 C ANISOU 2401 CG2 THR B 94 13039 10940 8637 715 -601 -266 C ATOM 2402 N ASN B 95 50.055 13.888 -23.244 1.00 72.09 N ANISOU 2402 N ASN B 95 11197 9200 6993 777 -770 -378 N ATOM 2403 CA ASN B 95 49.653 15.183 -22.684 1.00 71.15 C ANISOU 2403 CA ASN B 95 11112 9052 6870 793 -769 -321 C ATOM 2404 C ASN B 95 48.823 15.037 -21.407 1.00 72.98 C ANISOU 2404 C ASN B 95 11242 9256 7233 722 -763 -368 C ATOM 2405 O ASN B 95 48.905 15.907 -20.539 1.00 72.18 O ANISOU 2405 O ASN B 95 11166 9109 7150 689 -721 -301 O ATOM 2406 CB ASN B 95 48.850 15.980 -23.705 1.00 72.18 C ANISOU 2406 CB ASN B 95 11301 9221 6903 931 -862 -350 C ATOM 2407 CG ASN B 95 49.621 16.420 -24.923 1.00 92.09 C ANISOU 2407 CG ASN B 95 13963 11759 9269 1009 -853 -282 C ATOM 2408 OD1 ASN B 95 50.857 16.537 -24.916 1.00 81.90 O ANISOU 2408 OD1 ASN B 95 12734 10441 7942 956 -755 -184 O ATOM 2409 ND2 ASN B 95 48.892 16.782 -25.965 1.00 87.43 N ANISOU 2409 ND2 ASN B 95 13433 11206 8581 1141 -954 -329 N ATOM 2410 N ILE B 96 48.023 13.954 -21.297 1.00 68.66 N ANISOU 2410 N ILE B 96 10582 8728 6775 699 -798 -485 N ATOM 2411 CA ILE B 96 47.207 13.664 -20.115 1.00 67.84 C ANISOU 2411 CA ILE B 96 10381 8596 6801 622 -772 -538 C ATOM 2412 C ILE B 96 48.158 13.518 -18.907 1.00 70.99 C ANISOU 2412 C ILE B 96 10811 8927 7235 504 -669 -447 C ATOM 2413 O ILE B 96 47.943 14.185 -17.890 1.00 69.70 O ANISOU 2413 O ILE B 96 10656 8724 7105 466 -627 -409 O ATOM 2414 CB ILE B 96 46.307 12.417 -20.337 1.00 71.26 C ANISOU 2414 CB ILE B 96 10691 9055 7329 608 -818 -680 C ATOM 2415 CG1 ILE B 96 45.228 12.737 -21.397 1.00 72.64 C ANISOU 2415 CG1 ILE B 96 10827 9291 7481 735 -939 -783 C ATOM 2416 CG2 ILE B 96 45.643 11.976 -19.027 1.00 72.30 C ANISOU 2416 CG2 ILE B 96 10731 9143 7598 502 -752 -720 C ATOM 2417 CD1 ILE B 96 44.363 11.565 -21.867 1.00 80.75 C ANISOU 2417 CD1 ILE B 96 11733 10348 8599 739 -1010 -936 C ATOM 2418 N TYR B 97 49.253 12.738 -19.059 1.00 67.63 N ANISOU 2418 N TYR B 97 10413 8488 6795 458 -638 -410 N ATOM 2419 CA TYR B 97 50.257 12.591 -18.005 1.00 66.54 C ANISOU 2419 CA TYR B 97 10312 8284 6687 361 -564 -328 C ATOM 2420 C TYR B 97 50.905 13.928 -17.664 1.00 69.10 C ANISOU 2420 C TYR B 97 10721 8577 6956 369 -534 -218 C ATOM 2421 O TYR B 97 50.971 14.286 -16.484 1.00 67.56 O ANISOU 2421 O TYR B 97 10543 8326 6800 308 -494 -177 O ATOM 2422 CB TYR B 97 51.347 11.585 -18.401 1.00 67.69 C ANISOU 2422 CB TYR B 97 10468 8424 6827 333 -551 -318 C ATOM 2423 CG TYR B 97 50.962 10.131 -18.258 1.00 69.85 C ANISOU 2423 CG TYR B 97 10670 8690 7180 284 -561 -407 C ATOM 2424 CD1 TYR B 97 50.963 9.511 -17.011 1.00 71.54 C ANISOU 2424 CD1 TYR B 97 10871 8835 7476 186 -517 -402 C ATOM 2425 CD2 TYR B 97 50.769 9.330 -19.380 1.00 71.10 C ANISOU 2425 CD2 TYR B 97 10793 8899 7325 335 -612 -490 C ATOM 2426 CE1 TYR B 97 50.675 8.155 -16.875 1.00 73.48 C ANISOU 2426 CE1 TYR B 97 11066 9059 7796 135 -520 -476 C ATOM 2427 CE2 TYR B 97 50.488 7.969 -19.259 1.00 72.29 C ANISOU 2427 CE2 TYR B 97 10881 9030 7555 286 -623 -572 C ATOM 2428 CZ TYR B 97 50.444 7.385 -18.004 1.00 80.58 C ANISOU 2428 CZ TYR B 97 11917 10006 8693 183 -573 -563 C ATOM 2429 OH TYR B 97 50.176 6.044 -17.877 1.00 81.38 O ANISOU 2429 OH TYR B 97 11969 10075 8875 130 -578 -638 O ATOM 2430 N ILE B 98 51.357 14.673 -18.708 1.00 65.96 N ANISOU 2430 N ILE B 98 10387 8210 6465 446 -551 -172 N ATOM 2431 CA ILE B 98 52.056 15.962 -18.603 1.00 65.58 C ANISOU 2431 CA ILE B 98 10426 8128 6362 456 -520 -65 C ATOM 2432 C ILE B 98 51.196 16.961 -17.814 1.00 70.10 C ANISOU 2432 C ILE B 98 11006 8674 6954 466 -530 -59 C ATOM 2433 O ILE B 98 51.731 17.671 -16.962 1.00 69.46 O ANISOU 2433 O ILE B 98 10972 8535 6886 420 -492 13 O ATOM 2434 CB ILE B 98 52.424 16.527 -20.005 1.00 69.20 C ANISOU 2434 CB ILE B 98 10958 8627 6710 546 -533 -30 C ATOM 2435 CG1 ILE B 98 53.214 15.493 -20.835 1.00 70.19 C ANISOU 2435 CG1 ILE B 98 11074 8784 6812 544 -515 -49 C ATOM 2436 CG2 ILE B 98 53.226 17.824 -19.871 1.00 69.84 C ANISOU 2436 CG2 ILE B 98 11130 8657 6747 540 -486 86 C ATOM 2437 CD1 ILE B 98 53.458 15.871 -22.346 1.00 82.38 C ANISOU 2437 CD1 ILE B 98 12701 10375 8226 643 -521 -30 C ATOM 2438 N PHE B 99 49.872 16.986 -18.071 1.00 67.37 N ANISOU 2438 N PHE B 99 10608 8369 6620 528 -584 -146 N ATOM 2439 CA PHE B 99 48.946 17.885 -17.385 1.00 67.51 C ANISOU 2439 CA PHE B 99 10618 8368 6666 549 -594 -160 C ATOM 2440 C PHE B 99 48.812 17.518 -15.908 1.00 70.19 C ANISOU 2440 C PHE B 99 10919 8657 7093 448 -534 -168 C ATOM 2441 O PHE B 99 48.958 18.394 -15.054 1.00 69.07 O ANISOU 2441 O PHE B 99 10829 8464 6951 427 -503 -113 O ATOM 2442 CB PHE B 99 47.558 17.867 -18.055 1.00 70.50 C ANISOU 2442 CB PHE B 99 10927 8804 7055 642 -673 -270 C ATOM 2443 CG PHE B 99 46.550 18.796 -17.411 1.00 72.64 C ANISOU 2443 CG PHE B 99 11176 9059 7365 677 -685 -298 C ATOM 2444 CD1 PHE B 99 46.505 20.148 -17.750 1.00 76.03 C ANISOU 2444 CD1 PHE B 99 11691 9473 7722 764 -721 -244 C ATOM 2445 CD2 PHE B 99 45.627 18.316 -16.485 1.00 74.69 C ANISOU 2445 CD2 PHE B 99 11331 9315 7734 626 -653 -382 C ATOM 2446 CE1 PHE B 99 45.578 21.006 -17.152 1.00 77.04 C ANISOU 2446 CE1 PHE B 99 11797 9585 7892 804 -735 -278 C ATOM 2447 CE2 PHE B 99 44.703 19.178 -15.883 1.00 77.59 C ANISOU 2447 CE2 PHE B 99 11671 9668 8142 661 -653 -416 C ATOM 2448 CZ PHE B 99 44.679 20.513 -16.229 1.00 75.92 C ANISOU 2448 CZ PHE B 99 11541 9445 7861 755 -700 -368 C ATOM 2449 N ASN B 100 48.518 16.235 -15.611 1.00 66.93 N ANISOU 2449 N ASN B 100 10428 8252 6749 387 -516 -238 N ATOM 2450 CA ASN B 100 48.300 15.744 -14.248 1.00 66.46 C ANISOU 2450 CA ASN B 100 10346 8140 6764 291 -451 -251 C ATOM 2451 C ASN B 100 49.577 15.876 -13.399 1.00 69.42 C ANISOU 2451 C ASN B 100 10811 8445 7118 221 -408 -149 C ATOM 2452 O ASN B 100 49.468 16.153 -12.201 1.00 67.95 O ANISOU 2452 O ASN B 100 10659 8205 6954 170 -364 -129 O ATOM 2453 CB ASN B 100 47.819 14.305 -14.267 1.00 67.62 C ANISOU 2453 CB ASN B 100 10407 8302 6985 242 -442 -339 C ATOM 2454 CG ASN B 100 46.457 14.141 -14.913 1.00 90.32 C ANISOU 2454 CG ASN B 100 13173 11235 9908 300 -487 -458 C ATOM 2455 OD1 ASN B 100 46.310 13.446 -15.917 1.00 82.29 O ANISOU 2455 OD1 ASN B 100 12107 10265 8896 336 -544 -520 O ATOM 2456 ND2 ASN B 100 45.428 14.787 -14.363 1.00 81.96 N ANISOU 2456 ND2 ASN B 100 12071 10175 8894 316 -469 -501 N ATOM 2457 N LEU B 101 50.774 15.743 -14.019 1.00 66.53 N ANISOU 2457 N LEU B 101 10486 8081 6712 223 -423 -91 N ATOM 2458 CA LEU B 101 52.047 15.959 -13.319 1.00 66.24 C ANISOU 2458 CA LEU B 101 10521 7979 6669 166 -399 -3 C ATOM 2459 C LEU B 101 52.198 17.446 -12.983 1.00 72.09 C ANISOU 2459 C LEU B 101 11331 8687 7375 191 -397 63 C ATOM 2460 O LEU B 101 52.517 17.783 -11.844 1.00 72.17 O ANISOU 2460 O LEU B 101 11390 8632 7401 141 -377 99 O ATOM 2461 CB LEU B 101 53.255 15.461 -14.154 1.00 66.00 C ANISOU 2461 CB LEU B 101 10495 7962 6621 167 -408 29 C ATOM 2462 CG LEU B 101 54.661 15.645 -13.526 1.00 70.06 C ANISOU 2462 CG LEU B 101 11061 8410 7150 112 -393 107 C ATOM 2463 CD1 LEU B 101 54.861 14.723 -12.336 1.00 70.07 C ANISOU 2463 CD1 LEU B 101 11067 8350 7205 37 -387 93 C ATOM 2464 CD2 LEU B 101 55.762 15.392 -14.539 1.00 71.93 C ANISOU 2464 CD2 LEU B 101 11287 8670 7372 128 -390 132 C ATOM 2465 N ALA B 102 51.943 18.332 -13.982 1.00 69.04 N ANISOU 2465 N ALA B 102 10958 8340 6935 273 -424 75 N ATOM 2466 CA ALA B 102 52.026 19.782 -13.835 1.00 68.79 C ANISOU 2466 CA ALA B 102 10997 8272 6867 307 -427 136 C ATOM 2467 C ALA B 102 51.047 20.283 -12.771 1.00 73.16 C ANISOU 2467 C ALA B 102 11550 8798 7449 304 -419 103 C ATOM 2468 O ALA B 102 51.427 21.120 -11.956 1.00 72.76 O ANISOU 2468 O ALA B 102 11565 8685 7396 281 -406 154 O ATOM 2469 CB ALA B 102 51.746 20.458 -15.164 1.00 69.95 C ANISOU 2469 CB ALA B 102 11166 8465 6945 405 -462 144 C ATOM 2470 N LEU B 103 49.810 19.732 -12.749 1.00 70.11 N ANISOU 2470 N LEU B 103 11085 8456 7097 325 -421 10 N ATOM 2471 CA LEU B 103 48.761 20.080 -11.786 1.00 70.47 C ANISOU 2471 CA LEU B 103 11111 8484 7181 323 -395 -40 C ATOM 2472 C LEU B 103 49.164 19.659 -10.358 1.00 74.33 C ANISOU 2472 C LEU B 103 11640 8905 7697 224 -335 -18 C ATOM 2473 O LEU B 103 48.955 20.431 -9.420 1.00 73.56 O ANISOU 2473 O LEU B 103 11594 8760 7595 219 -309 -4 O ATOM 2474 CB LEU B 103 47.432 19.411 -12.192 1.00 71.13 C ANISOU 2474 CB LEU B 103 11079 8631 7316 356 -404 -155 C ATOM 2475 CG LEU B 103 46.182 19.682 -11.329 1.00 76.42 C ANISOU 2475 CG LEU B 103 11697 9295 8045 358 -364 -229 C ATOM 2476 CD1 LEU B 103 45.813 21.162 -11.316 1.00 76.96 C ANISOU 2476 CD1 LEU B 103 11809 9350 8082 442 -393 -212 C ATOM 2477 CD2 LEU B 103 45.000 18.890 -11.843 1.00 79.56 C ANISOU 2477 CD2 LEU B 103 11958 9754 8515 381 -377 -350 C ATOM 2478 N ALA B 104 49.758 18.453 -10.207 1.00 70.94 N ANISOU 2478 N ALA B 104 11200 8467 7289 155 -318 -17 N ATOM 2479 CA ALA B 104 50.221 17.935 -8.916 1.00 70.42 C ANISOU 2479 CA ALA B 104 11190 8329 7235 70 -276 7 C ATOM 2480 C ALA B 104 51.394 18.759 -8.385 1.00 72.70 C ANISOU 2480 C ALA B 104 11580 8552 7489 55 -298 95 C ATOM 2481 O ALA B 104 51.414 19.089 -7.202 1.00 72.48 O ANISOU 2481 O ALA B 104 11626 8462 7453 22 -274 110 O ATOM 2482 CB ALA B 104 50.627 16.470 -9.044 1.00 71.07 C ANISOU 2482 CB ALA B 104 11242 8413 7347 15 -271 -11 C ATOM 2483 N ASP B 105 52.347 19.113 -9.258 1.00 68.43 N ANISOU 2483 N ASP B 105 11046 8023 6932 78 -339 146 N ATOM 2484 CA ASP B 105 53.514 19.905 -8.887 1.00 68.32 C ANISOU 2484 CA ASP B 105 11108 7945 6907 60 -362 222 C ATOM 2485 C ASP B 105 53.133 21.369 -8.627 1.00 72.36 C ANISOU 2485 C ASP B 105 11672 8429 7392 102 -367 245 C ATOM 2486 O ASP B 105 53.840 22.062 -7.893 1.00 72.16 O ANISOU 2486 O ASP B 105 11719 8331 7366 76 -382 291 O ATOM 2487 CB ASP B 105 54.585 19.832 -9.975 1.00 70.61 C ANISOU 2487 CB ASP B 105 11374 8256 7197 68 -384 264 C ATOM 2488 CG ASP B 105 55.183 18.463 -10.218 1.00 84.17 C ANISOU 2488 CG ASP B 105 13046 9989 8945 31 -386 245 C ATOM 2489 OD1 ASP B 105 55.374 17.712 -9.232 1.00 83.68 O ANISOU 2489 OD1 ASP B 105 13005 9881 8908 -23 -387 233 O ATOM 2490 OD2 ASP B 105 55.573 18.188 -11.375 1.00 93.71 O ANISOU 2490 OD2 ASP B 105 14212 11248 10147 57 -387 248 O ATOM 2491 N ALA B 106 52.028 21.839 -9.231 1.00 68.57 N ANISOU 2491 N ALA B 106 11157 8002 6897 171 -364 206 N ATOM 2492 CA ALA B 106 51.552 23.201 -9.032 1.00 68.43 C ANISOU 2492 CA ALA B 106 11187 7956 6857 223 -374 218 C ATOM 2493 C ALA B 106 50.926 23.362 -7.652 1.00 72.57 C ANISOU 2493 C ALA B 106 11747 8437 7391 200 -339 183 C ATOM 2494 O ALA B 106 51.006 24.440 -7.067 1.00 73.56 O ANISOU 2494 O ALA B 106 11944 8505 7499 215 -348 209 O ATOM 2495 CB ALA B 106 50.546 23.569 -10.108 1.00 69.58 C ANISOU 2495 CB ALA B 106 11283 8170 6986 316 -395 178 C ATOM 2496 N LEU B 107 50.302 22.303 -7.130 1.00 67.56 N ANISOU 2496 N LEU B 107 11068 7822 6780 161 -294 124 N ATOM 2497 CA LEU B 107 49.645 22.380 -5.836 1.00 67.18 C ANISOU 2497 CA LEU B 107 11059 7733 6731 137 -239 89 C ATOM 2498 C LEU B 107 50.611 22.039 -4.708 1.00 71.25 C ANISOU 2498 C LEU B 107 11676 8169 7226 63 -235 134 C ATOM 2499 O LEU B 107 50.355 22.430 -3.568 1.00 71.70 O ANISOU 2499 O LEU B 107 11813 8172 7258 51 -202 125 O ATOM 2500 CB LEU B 107 48.420 21.447 -5.778 1.00 67.48 C ANISOU 2500 CB LEU B 107 11006 7823 6810 126 -174 1 C ATOM 2501 CG LEU B 107 47.262 21.751 -6.739 1.00 72.36 C ANISOU 2501 CG LEU B 107 11513 8518 7463 207 -187 -70 C ATOM 2502 CD1 LEU B 107 46.207 20.682 -6.663 1.00 72.65 C ANISOU 2502 CD1 LEU B 107 11443 8597 7562 178 -125 -162 C ATOM 2503 CD2 LEU B 107 46.643 23.118 -6.467 1.00 75.76 C ANISOU 2503 CD2 LEU B 107 11970 8932 7882 279 -191 -84 C ATOM 2504 N VAL B 108 51.708 21.312 -4.994 1.00 67.08 N ANISOU 2504 N VAL B 108 11151 7631 6707 21 -272 174 N ATOM 2505 CA VAL B 108 52.646 20.987 -3.915 1.00 66.79 C ANISOU 2505 CA VAL B 108 11212 7512 6655 -38 -291 210 C ATOM 2506 C VAL B 108 53.433 22.236 -3.550 1.00 70.78 C ANISOU 2506 C VAL B 108 11796 7952 7144 -24 -345 259 C ATOM 2507 O VAL B 108 53.719 22.417 -2.375 1.00 71.26 O ANISOU 2507 O VAL B 108 11960 7939 7177 -48 -356 266 O ATOM 2508 CB VAL B 108 53.606 19.805 -4.176 1.00 70.61 C ANISOU 2508 CB VAL B 108 11675 7992 7163 -83 -322 229 C ATOM 2509 CG1 VAL B 108 52.882 18.476 -4.146 1.00 70.25 C ANISOU 2509 CG1 VAL B 108 11585 7976 7130 -113 -267 179 C ATOM 2510 CG2 VAL B 108 54.380 19.981 -5.463 1.00 70.50 C ANISOU 2510 CG2 VAL B 108 11590 8019 7176 -60 -367 260 C ATOM 2511 N THR B 109 53.738 23.120 -4.532 1.00 66.68 N ANISOU 2511 N THR B 109 11241 7455 6639 16 -378 290 N ATOM 2512 CA THR B 109 54.481 24.362 -4.273 1.00 66.30 C ANISOU 2512 CA THR B 109 11262 7338 6591 23 -426 337 C ATOM 2513 C THR B 109 53.599 25.351 -3.497 1.00 68.96 C ANISOU 2513 C THR B 109 11666 7642 6893 61 -406 311 C ATOM 2514 O THR B 109 54.127 26.214 -2.810 1.00 68.85 O ANISOU 2514 O THR B 109 11737 7550 6872 56 -445 334 O ATOM 2515 CB THR B 109 54.998 24.995 -5.570 1.00 76.29 C ANISOU 2515 CB THR B 109 12481 8628 7877 51 -447 382 C ATOM 2516 OG1 THR B 109 53.894 25.334 -6.404 1.00 76.99 O ANISOU 2516 OG1 THR B 109 12525 8783 7943 119 -420 357 O ATOM 2517 CG2 THR B 109 55.976 24.090 -6.318 1.00 75.12 C ANISOU 2517 CG2 THR B 109 12270 8507 7764 15 -458 405 C ATOM 2518 N THR B 110 52.265 25.187 -3.572 1.00 64.85 N ANISOU 2518 N THR B 110 11102 7179 6360 99 -347 254 N ATOM 2519 CA THR B 110 51.270 26.006 -2.874 1.00 65.02 C ANISOU 2519 CA THR B 110 11167 7182 6358 142 -312 213 C ATOM 2520 C THR B 110 51.492 25.918 -1.352 1.00 68.77 C ANISOU 2520 C THR B 110 11758 7577 6794 99 -297 206 C ATOM 2521 O THR B 110 51.332 26.917 -0.655 1.00 68.63 O ANISOU 2521 O THR B 110 11823 7505 6750 127 -303 199 O ATOM 2522 CB THR B 110 49.862 25.530 -3.275 1.00 75.17 C ANISOU 2522 CB THR B 110 12352 8550 7660 178 -247 140 C ATOM 2523 OG1 THR B 110 49.722 25.645 -4.689 1.00 77.24 O ANISOU 2523 OG1 THR B 110 12525 8877 7945 228 -282 145 O ATOM 2524 CG2 THR B 110 48.746 26.304 -2.594 1.00 75.84 C ANISOU 2524 CG2 THR B 110 12458 8624 7735 227 -198 82 C ATOM 2525 N THR B 111 51.887 24.736 -0.857 1.00 65.64 N ANISOU 2525 N THR B 111 11383 7170 6388 38 -283 208 N ATOM 2526 CA THR B 111 52.121 24.478 0.568 1.00 65.95 C ANISOU 2526 CA THR B 111 11553 7131 6373 0 -273 204 C ATOM 2527 C THR B 111 53.467 25.059 1.046 1.00 71.86 C ANISOU 2527 C THR B 111 12398 7792 7115 -15 -379 252 C ATOM 2528 O THR B 111 53.622 25.329 2.237 1.00 71.61 O ANISOU 2528 O THR B 111 12498 7683 7028 -20 -394 244 O ATOM 2529 CB THR B 111 52.098 22.948 0.857 1.00 66.68 C ANISOU 2529 CB THR B 111 11644 7233 6458 -57 -229 195 C ATOM 2530 OG1 THR B 111 53.227 22.301 0.264 1.00 58.97 O ANISOU 2530 OG1 THR B 111 10630 6257 5518 -86 -305 236 O ATOM 2531 CG2 THR B 111 50.801 22.270 0.427 1.00 64.59 C ANISOU 2531 CG2 THR B 111 11275 7047 6219 -56 -124 139 C ATOM 2532 N MET B 112 54.438 25.220 0.119 1.00 69.75 N ANISOU 2532 N MET B 112 12064 7531 6905 -22 -450 295 N ATOM 2533 CA MET B 112 55.824 25.636 0.377 1.00 70.47 C ANISOU 2533 CA MET B 112 12206 7545 7025 -47 -552 334 C ATOM 2534 C MET B 112 55.921 26.948 1.243 1.00 75.89 C ANISOU 2534 C MET B 112 13005 8146 7685 -24 -595 329 C ATOM 2535 O MET B 112 56.713 26.924 2.191 1.00 76.73 O ANISOU 2535 O MET B 112 13208 8170 7777 -47 -669 329 O ATOM 2536 CB MET B 112 56.576 25.838 -0.943 1.00 72.59 C ANISOU 2536 CB MET B 112 12365 7847 7367 -51 -583 375 C ATOM 2537 CG MET B 112 58.052 25.958 -0.773 1.00 76.41 C ANISOU 2537 CG MET B 112 12863 8261 7908 -91 -674 404 C ATOM 2538 SD MET B 112 58.921 25.937 -2.344 1.00 80.45 S ANISOU 2538 SD MET B 112 13240 8820 8506 -106 -673 449 S ATOM 2539 CE MET B 112 60.548 25.854 -1.736 1.00 77.63 C ANISOU 2539 CE MET B 112 12898 8371 8227 -159 -778 456 C ATOM 2540 N PRO B 113 55.089 27.969 1.002 1.00 72.04 N ANISOU 2540 N PRO B 113 12513 7671 7186 26 -557 316 N ATOM 2541 CA PRO B 113 55.178 29.176 1.840 1.00 72.29 C ANISOU 2541 CA PRO B 113 12657 7615 7194 50 -600 306 C ATOM 2542 C PRO B 113 54.950 28.916 3.344 1.00 76.24 C ANISOU 2542 C PRO B 113 13299 8058 7611 47 -594 266 C ATOM 2543 O PRO B 113 55.467 29.656 4.181 1.00 77.10 O ANISOU 2543 O PRO B 113 13520 8075 7699 52 -666 259 O ATOM 2544 CB PRO B 113 54.059 30.066 1.289 1.00 74.28 C ANISOU 2544 CB PRO B 113 12873 7909 7443 116 -543 288 C ATOM 2545 CG PRO B 113 53.824 29.576 -0.102 1.00 78.26 C ANISOU 2545 CG PRO B 113 13240 8507 7988 123 -510 308 C ATOM 2546 CD PRO B 113 54.075 28.097 -0.058 1.00 73.45 C ANISOU 2546 CD PRO B 113 12590 7940 7378 71 -489 306 C ATOM 2547 N PHE B 114 54.185 27.875 3.664 1.00 71.26 N ANISOU 2547 N PHE B 114 12669 7475 6932 37 -506 240 N ATOM 2548 CA PHE B 114 53.842 27.482 5.035 1.00 71.04 C ANISOU 2548 CA PHE B 114 12787 7398 6808 31 -469 207 C ATOM 2549 C PHE B 114 55.063 26.878 5.728 1.00 74.91 C ANISOU 2549 C PHE B 114 13374 7811 7277 -8 -573 230 C ATOM 2550 O PHE B 114 55.305 27.200 6.884 1.00 75.14 O ANISOU 2550 O PHE B 114 13561 7755 7233 3 -618 213 O ATOM 2551 CB PHE B 114 52.662 26.501 5.065 1.00 72.64 C ANISOU 2551 CB PHE B 114 12950 7671 6980 22 -329 175 C ATOM 2552 CG PHE B 114 51.358 27.082 4.567 1.00 74.28 C ANISOU 2552 CG PHE B 114 13066 7948 7211 70 -231 132 C ATOM 2553 CD1 PHE B 114 51.033 27.049 3.217 1.00 76.95 C ANISOU 2553 CD1 PHE B 114 13238 8371 7628 87 -223 137 C ATOM 2554 CD2 PHE B 114 50.441 27.632 5.452 1.00 76.99 C ANISOU 2554 CD2 PHE B 114 13490 8268 7495 106 -149 80 C ATOM 2555 CE1 PHE B 114 49.826 27.584 2.760 1.00 78.06 C ANISOU 2555 CE1 PHE B 114 13294 8572 7795 143 -154 88 C ATOM 2556 CE2 PHE B 114 49.238 28.173 4.992 1.00 79.91 C ANISOU 2556 CE2 PHE B 114 13762 8700 7901 159 -67 29 C ATOM 2557 CZ PHE B 114 48.936 28.140 3.651 1.00 77.56 C ANISOU 2557 CZ PHE B 114 13296 8484 7688 179 -78 32 C ATOM 2558 N GLN B 115 55.865 26.057 5.007 1.00 71.28 N ANISOU 2558 N GLN B 115 12822 7378 6884 -46 -623 264 N ATOM 2559 CA GLN B 115 57.105 25.456 5.533 1.00 71.50 C ANISOU 2559 CA GLN B 115 12916 7335 6916 -76 -740 280 C ATOM 2560 C GLN B 115 58.126 26.536 5.877 1.00 76.57 C ANISOU 2560 C GLN B 115 13608 7889 7595 -67 -874 281 C ATOM 2561 O GLN B 115 58.774 26.468 6.927 1.00 76.58 O ANISOU 2561 O GLN B 115 13745 7800 7551 -65 -971 266 O ATOM 2562 CB GLN B 115 57.716 24.469 4.521 1.00 72.13 C ANISOU 2562 CB GLN B 115 12858 7470 7079 -110 -758 307 C ATOM 2563 CG GLN B 115 56.911 23.197 4.231 1.00 83.21 C ANISOU 2563 CG GLN B 115 14216 8942 8457 -128 -651 302 C ATOM 2564 CD GLN B 115 56.979 22.118 5.292 1.00 96.10 C ANISOU 2564 CD GLN B 115 15987 10517 10010 -147 -654 296 C ATOM 2565 OE1 GLN B 115 56.983 22.370 6.505 1.00 87.25 O ANISOU 2565 OE1 GLN B 115 15038 9315 8798 -134 -679 285 O ATOM 2566 NE2 GLN B 115 56.949 20.870 4.837 1.00 90.08 N ANISOU 2566 NE2 GLN B 115 15163 9793 9271 -176 -621 304 N ATOM 2567 N SER B 116 58.252 27.537 4.984 1.00 73.87 N ANISOU 2567 N SER B 116 13164 7568 7335 -60 -880 296 N ATOM 2568 CA SER B 116 59.145 28.680 5.120 1.00 75.13 C ANISOU 2568 CA SER B 116 13346 7646 7556 -60 -989 298 C ATOM 2569 C SER B 116 58.845 29.457 6.420 1.00 81.16 C ANISOU 2569 C SER B 116 14286 8323 8230 -25 -1025 258 C ATOM 2570 O SER B 116 59.753 29.643 7.237 1.00 81.95 O ANISOU 2570 O SER B 116 14480 8327 8332 -31 -1152 239 O ATOM 2571 CB SER B 116 59.009 29.593 3.900 1.00 79.77 C ANISOU 2571 CB SER B 116 13813 8274 8223 -55 -950 328 C ATOM 2572 OG SER B 116 59.865 30.723 3.956 1.00 92.80 O ANISOU 2572 OG SER B 116 15478 9836 9945 -66 -1042 333 O ATOM 2573 N THR B 117 57.565 29.853 6.633 1.00 78.05 N ANISOU 2573 N THR B 117 13937 7962 7758 16 -915 235 N ATOM 2574 CA THR B 117 57.128 30.626 7.810 1.00 78.89 C ANISOU 2574 CA THR B 117 14210 7995 7771 59 -923 191 C ATOM 2575 C THR B 117 57.277 29.828 9.117 1.00 83.16 C ANISOU 2575 C THR B 117 14922 8479 8195 58 -951 166 C ATOM 2576 O THR B 117 57.741 30.395 10.103 1.00 83.80 O ANISOU 2576 O THR B 117 15151 8463 8227 79 -1050 136 O ATOM 2577 CB THR B 117 55.672 31.084 7.671 1.00 86.54 C ANISOU 2577 CB THR B 117 15165 9023 8693 106 -781 165 C ATOM 2578 OG1 THR B 117 54.850 29.950 7.427 1.00 87.55 O ANISOU 2578 OG1 THR B 117 15236 9241 8790 93 -657 165 O ATOM 2579 CG2 THR B 117 55.482 32.072 6.562 1.00 84.81 C ANISOU 2579 CG2 THR B 117 14826 8835 8564 127 -773 184 C ATOM 2580 N VAL B 118 56.877 28.537 9.129 1.00 78.68 N ANISOU 2580 N VAL B 118 14348 7967 7582 36 -868 178 N ATOM 2581 CA VAL B 118 56.959 27.679 10.320 1.00 79.16 C ANISOU 2581 CA VAL B 118 14587 7970 7519 35 -880 166 C ATOM 2582 C VAL B 118 58.427 27.568 10.776 1.00 82.16 C ANISOU 2582 C VAL B 118 15035 8256 7925 27 -1078 169 C ATOM 2583 O VAL B 118 58.682 27.614 11.978 1.00 82.08 O ANISOU 2583 O VAL B 118 15224 8155 7809 54 -1153 142 O ATOM 2584 CB VAL B 118 56.337 26.278 10.070 1.00 83.06 C ANISOU 2584 CB VAL B 118 15041 8535 7985 3 -756 186 C ATOM 2585 CG1 VAL B 118 56.645 25.305 11.206 1.00 83.73 C ANISOU 2585 CG1 VAL B 118 15319 8544 7950 -3 -788 188 C ATOM 2586 CG2 VAL B 118 54.834 26.386 9.863 1.00 83.05 C ANISOU 2586 CG2 VAL B 118 14990 8611 7954 14 -565 163 C ATOM 2587 N TYR B 119 59.379 27.451 9.826 1.00 77.44 N ANISOU 2587 N TYR B 119 14276 7678 7471 -6 -1164 195 N ATOM 2588 CA TYR B 119 60.803 27.370 10.151 1.00 77.23 C ANISOU 2588 CA TYR B 119 14273 7566 7504 -15 -1355 186 C ATOM 2589 C TYR B 119 61.264 28.605 10.922 1.00 81.31 C ANISOU 2589 C TYR B 119 14899 7980 8014 14 -1477 145 C ATOM 2590 O TYR B 119 61.918 28.469 11.962 1.00 82.00 O ANISOU 2590 O TYR B 119 15141 7972 8044 37 -1616 112 O ATOM 2591 CB TYR B 119 61.655 27.206 8.870 1.00 77.39 C ANISOU 2591 CB TYR B 119 14073 7635 7697 -58 -1393 216 C ATOM 2592 CG TYR B 119 63.137 27.480 9.064 1.00 79.24 C ANISOU 2592 CG TYR B 119 14287 7781 8040 -70 -1585 194 C ATOM 2593 CD1 TYR B 119 63.914 26.673 9.895 1.00 82.22 C ANISOU 2593 CD1 TYR B 119 14765 8087 8387 -56 -1722 170 C ATOM 2594 CD2 TYR B 119 63.784 28.470 8.330 1.00 79.36 C ANISOU 2594 CD2 TYR B 119 14168 7784 8202 -97 -1627 197 C ATOM 2595 CE1 TYR B 119 65.280 26.899 10.055 1.00 84.12 C ANISOU 2595 CE1 TYR B 119 14965 8248 8748 -64 -1909 136 C ATOM 2596 CE2 TYR B 119 65.152 28.704 8.479 1.00 80.85 C ANISOU 2596 CE2 TYR B 119 14313 7890 8516 -117 -1795 167 C ATOM 2597 CZ TYR B 119 65.897 27.913 9.340 1.00 91.11 C ANISOU 2597 CZ TYR B 119 15700 9124 9793 -98 -1941 132 C ATOM 2598 OH TYR B 119 67.246 28.123 9.499 1.00 95.10 O ANISOU 2598 OH TYR B 119 16148 9548 10438 -112 -2119 89 O ATOM 2599 N LEU B 120 60.920 29.799 10.407 1.00 76.42 N ANISOU 2599 N LEU B 120 14208 7375 7452 18 -1434 143 N ATOM 2600 CA LEU B 120 61.354 31.078 10.944 1.00 76.12 C ANISOU 2600 CA LEU B 120 14247 7240 7437 38 -1545 104 C ATOM 2601 C LEU B 120 60.571 31.447 12.213 1.00 81.17 C ANISOU 2601 C LEU B 120 15110 7826 7904 96 -1520 58 C ATOM 2602 O LEU B 120 61.205 31.817 13.201 1.00 81.98 O ANISOU 2602 O LEU B 120 15361 7822 7966 121 -1667 13 O ATOM 2603 CB LEU B 120 61.196 32.166 9.876 1.00 75.20 C ANISOU 2603 CB LEU B 120 13982 7153 7438 23 -1494 126 C ATOM 2604 CG LEU B 120 62.045 31.968 8.607 1.00 78.33 C ANISOU 2604 CG LEU B 120 14171 7590 8002 -35 -1512 170 C ATOM 2605 CD1 LEU B 120 61.635 32.912 7.528 1.00 78.13 C ANISOU 2605 CD1 LEU B 120 14031 7603 8051 -42 -1424 204 C ATOM 2606 CD2 LEU B 120 63.537 32.088 8.892 1.00 79.85 C ANISOU 2606 CD2 LEU B 120 14345 7687 8310 -67 -1694 145 C ATOM 2607 N MET B 121 59.227 31.321 12.214 1.00 77.91 N ANISOU 2607 N MET B 121 14724 7485 7393 119 -1339 63 N ATOM 2608 CA MET B 121 58.422 31.638 13.403 1.00 79.34 C ANISOU 2608 CA MET B 121 15115 7622 7408 174 -1285 17 C ATOM 2609 C MET B 121 58.643 30.633 14.524 1.00 85.73 C ANISOU 2609 C MET B 121 16120 8378 8073 185 -1325 7 C ATOM 2610 O MET B 121 58.634 31.015 15.691 1.00 86.06 O ANISOU 2610 O MET B 121 16376 8334 7989 232 -1379 -38 O ATOM 2611 CB MET B 121 56.930 31.695 13.098 1.00 81.38 C ANISOU 2611 CB MET B 121 15331 7972 7617 192 -1071 17 C ATOM 2612 CG MET B 121 56.540 32.744 12.109 1.00 84.75 C ANISOU 2612 CG MET B 121 15603 8441 8155 202 -1031 21 C ATOM 2613 SD MET B 121 54.741 32.949 12.062 1.00 89.50 S ANISOU 2613 SD MET B 121 16190 9129 8688 249 -806 -10 S ATOM 2614 CE MET B 121 54.212 31.280 11.597 1.00 85.79 C ANISOU 2614 CE MET B 121 15622 8767 8205 199 -669 27 C ATOM 2615 N ASN B 122 58.810 29.344 14.159 1.00 83.97 N ANISOU 2615 N ASN B 122 15836 8205 7863 147 -1296 50 N ATOM 2616 CA ASN B 122 59.017 28.192 15.048 1.00 85.38 C ANISOU 2616 CA ASN B 122 16190 8338 7914 153 -1324 56 C ATOM 2617 C ASN B 122 57.729 27.962 15.890 1.00 90.99 C ANISOU 2617 C ASN B 122 17075 9055 8440 178 -1138 43 C ATOM 2618 O ASN B 122 57.799 27.787 17.109 1.00 91.89 O ANISOU 2618 O ASN B 122 17439 9083 8393 215 -1177 21 O ATOM 2619 CB ASN B 122 60.272 28.387 15.937 1.00 88.38 C ANISOU 2619 CB ASN B 122 16720 8589 8270 184 -1566 21 C ATOM 2620 CG ASN B 122 60.728 27.158 16.683 1.00114.98 C ANISOU 2620 CG ASN B 122 20251 11902 11533 195 -1640 33 C ATOM 2621 OD1 ASN B 122 60.505 26.016 16.260 1.00107.30 O ANISOU 2621 OD1 ASN B 122 19220 10986 10563 161 -1552 78 O ATOM 2622 ND2 ASN B 122 61.477 27.375 17.755 1.00110.68 N ANISOU 2622 ND2 ASN B 122 19909 11239 10906 246 -1827 -11 N ATOM 2623 N SER B 123 56.547 27.977 15.204 1.00 87.37 N ANISOU 2623 N SER B 123 16483 8702 8013 159 -933 53 N ATOM 2624 CA SER B 123 55.188 27.760 15.743 1.00 87.75 C ANISOU 2624 CA SER B 123 16625 8781 7933 170 -715 36 C ATOM 2625 C SER B 123 54.117 27.784 14.648 1.00 90.42 C ANISOU 2625 C SER B 123 16735 9244 8375 146 -539 40 C ATOM 2626 O SER B 123 54.278 28.479 13.641 1.00 88.86 O ANISOU 2626 O SER B 123 16351 9095 8317 146 -585 44 O ATOM 2627 CB SER B 123 54.824 28.807 16.795 1.00 92.41 C ANISOU 2627 CB SER B 123 17408 9302 8403 233 -708 -22 C ATOM 2628 OG SER B 123 55.385 28.525 18.060 1.00102.20 O ANISOU 2628 OG SER B 123 18919 10430 9482 263 -806 -34 O ATOM 2629 N TRP B 124 53.011 27.039 14.867 1.00 87.59 N ANISOU 2629 N TRP B 124 16399 8932 7950 126 -336 36 N ATOM 2630 CA TRP B 124 51.847 27.037 13.976 1.00 87.23 C ANISOU 2630 CA TRP B 124 16149 8999 7994 111 -163 22 C ATOM 2631 C TRP B 124 50.668 27.708 14.708 1.00 92.24 C ANISOU 2631 C TRP B 124 16871 9632 8542 153 0 -40 C ATOM 2632 O TRP B 124 49.939 27.035 15.440 1.00 92.59 O ANISOU 2632 O TRP B 124 17028 9668 8483 135 163 -53 O ATOM 2633 CB TRP B 124 51.480 25.621 13.480 1.00 85.77 C ANISOU 2633 CB TRP B 124 15870 8876 7843 46 -54 54 C ATOM 2634 CG TRP B 124 50.303 25.609 12.540 1.00 86.42 C ANISOU 2634 CG TRP B 124 15733 9073 8031 33 103 27 C ATOM 2635 CD1 TRP B 124 48.982 25.584 12.879 1.00 90.23 C ANISOU 2635 CD1 TRP B 124 16210 9590 8482 35 307 -22 C ATOM 2636 CD2 TRP B 124 50.347 25.592 11.106 1.00 85.18 C ANISOU 2636 CD2 TRP B 124 15330 9007 8030 21 64 42 C ATOM 2637 NE1 TRP B 124 48.201 25.600 11.749 1.00 89.16 N ANISOU 2637 NE1 TRP B 124 15832 9561 8484 30 380 -47 N ATOM 2638 CE2 TRP B 124 49.012 25.582 10.645 1.00 89.29 C ANISOU 2638 CE2 TRP B 124 15708 9613 8606 24 232 -5 C ATOM 2639 CE3 TRP B 124 51.387 25.563 10.161 1.00 85.37 C ANISOU 2639 CE3 TRP B 124 15240 9046 8151 10 -92 86 C ATOM 2640 CZ2 TRP B 124 48.688 25.565 9.281 1.00 87.70 C ANISOU 2640 CZ2 TRP B 124 15271 9509 8541 24 229 -9 C ATOM 2641 CZ3 TRP B 124 51.067 25.541 8.811 1.00 86.02 C ANISOU 2641 CZ3 TRP B 124 15098 9226 8359 6 -75 88 C ATOM 2642 CH2 TRP B 124 49.732 25.536 8.382 1.00 86.79 C ANISOU 2642 CH2 TRP B 124 15073 9406 8499 16 76 42 C ATOM 2643 N PRO B 125 50.465 29.033 14.540 1.00 89.06 N ANISOU 2643 N PRO B 125 16423 9233 8183 210 -34 -82 N ATOM 2644 CA PRO B 125 49.381 29.700 15.277 1.00 90.07 C ANISOU 2644 CA PRO B 125 16637 9354 8230 260 116 -150 C ATOM 2645 C PRO B 125 48.086 29.833 14.466 1.00 93.32 C ANISOU 2645 C PRO B 125 16832 9876 8749 267 283 -190 C ATOM 2646 O PRO B 125 47.196 30.590 14.860 1.00 94.12 O ANISOU 2646 O PRO B 125 16954 9982 8825 321 390 -258 O ATOM 2647 CB PRO B 125 49.977 31.087 15.549 1.00 92.07 C ANISOU 2647 CB PRO B 125 16969 9536 8478 325 -41 -177 C ATOM 2648 CG PRO B 125 50.942 31.327 14.401 1.00 94.82 C ANISOU 2648 CG PRO B 125 17148 9901 8976 304 -216 -128 C ATOM 2649 CD PRO B 125 51.246 30.005 13.742 1.00 89.51 C ANISOU 2649 CD PRO B 125 16368 9286 8358 233 -207 -69 C ATOM 2650 N PHE B 126 47.971 29.099 13.354 1.00 88.40 N ANISOU 2650 N PHE B 126 16003 9338 8247 220 300 -158 N ATOM 2651 CA PHE B 126 46.864 29.258 12.422 1.00 87.90 C ANISOU 2651 CA PHE B 126 15714 9379 8306 235 412 -200 C ATOM 2652 C PHE B 126 45.746 28.196 12.626 1.00 92.27 C ANISOU 2652 C PHE B 126 16220 9986 8853 186 634 -232 C ATOM 2653 O PHE B 126 44.910 28.003 11.732 1.00 91.33 O ANISOU 2653 O PHE B 126 15886 9959 8856 182 713 -265 O ATOM 2654 CB PHE B 126 47.405 29.170 10.991 1.00 88.41 C ANISOU 2654 CB PHE B 126 15579 9504 8508 219 288 -153 C ATOM 2655 CG PHE B 126 48.660 29.983 10.746 1.00 89.55 C ANISOU 2655 CG PHE B 126 15765 9589 8671 240 81 -108 C ATOM 2656 CD1 PHE B 126 48.638 31.372 10.833 1.00 92.98 C ANISOU 2656 CD1 PHE B 126 16230 9985 9114 309 20 -139 C ATOM 2657 CD2 PHE B 126 49.838 29.368 10.337 1.00 90.92 C ANISOU 2657 CD2 PHE B 126 15926 9746 8873 190 -48 -41 C ATOM 2658 CE1 PHE B 126 49.794 32.123 10.597 1.00 93.34 C ANISOU 2658 CE1 PHE B 126 16306 9966 9192 317 -162 -100 C ATOM 2659 CE2 PHE B 126 50.988 30.123 10.079 1.00 93.19 C ANISOU 2659 CE2 PHE B 126 16231 9978 9201 201 -226 -7 C ATOM 2660 CZ PHE B 126 50.955 31.496 10.208 1.00 91.60 C ANISOU 2660 CZ PHE B 126 16065 9732 9007 260 -279 -36 C ATOM 2661 N GLY B 127 45.705 27.579 13.810 1.00 89.62 N ANISOU 2661 N GLY B 127 16088 9585 8378 153 733 -228 N ATOM 2662 CA GLY B 127 44.673 26.608 14.174 1.00 90.09 C ANISOU 2662 CA GLY B 127 16136 9672 8420 98 964 -257 C ATOM 2663 C GLY B 127 44.763 25.249 13.507 1.00 92.36 C ANISOU 2663 C GLY B 127 16313 10001 8779 13 986 -211 C ATOM 2664 O GLY B 127 45.628 25.020 12.660 1.00 90.54 O ANISOU 2664 O GLY B 127 15997 9789 8617 0 820 -158 O ATOM 2665 N ASP B 128 43.863 24.326 13.900 1.00 89.34 N ANISOU 2665 N ASP B 128 15934 9628 8384 -50 1201 -235 N ATOM 2666 CA ASP B 128 43.826 22.960 13.372 1.00 88.30 C ANISOU 2666 CA ASP B 128 15710 9523 8318 -137 1247 -200 C ATOM 2667 C ASP B 128 43.162 22.911 12.001 1.00 91.07 C ANISOU 2667 C ASP B 128 15748 9991 8865 -140 1254 -245 C ATOM 2668 O ASP B 128 43.529 22.071 11.183 1.00 89.72 O ANISOU 2668 O ASP B 128 15469 9851 8770 -186 1186 -208 O ATOM 2669 CB ASP B 128 43.083 22.014 14.333 1.00 91.70 C ANISOU 2669 CB ASP B 128 16270 9907 8666 -211 1487 -209 C ATOM 2670 CG ASP B 128 43.695 21.882 15.719 1.00103.83 C ANISOU 2670 CG ASP B 128 18148 11319 9984 -210 1492 -160 C ATOM 2671 OD1 ASP B 128 44.024 22.923 16.325 1.00105.47 O ANISOU 2671 OD1 ASP B 128 18493 11485 10095 -134 1417 -174 O ATOM 2672 OD2 ASP B 128 43.700 20.756 16.257 1.00110.09 O ANISOU 2672 OD2 ASP B 128 19078 12051 10700 -282 1593 -117 O ATOM 2673 N VAL B 129 42.178 23.803 11.752 1.00 88.13 N ANISOU 2673 N VAL B 129 15234 9679 8572 -83 1329 -331 N ATOM 2674 CA VAL B 129 41.406 23.872 10.501 1.00 87.41 C ANISOU 2674 CA VAL B 129 14851 9697 8663 -66 1332 -391 C ATOM 2675 C VAL B 129 42.372 24.076 9.306 1.00 88.29 C ANISOU 2675 C VAL B 129 14866 9844 8837 -36 1098 -334 C ATOM 2676 O VAL B 129 42.295 23.303 8.352 1.00 86.98 O ANISOU 2676 O VAL B 129 14540 9736 8772 -73 1075 -330 O ATOM 2677 CB VAL B 129 40.281 24.963 10.518 1.00 92.80 C ANISOU 2677 CB VAL B 129 15422 10426 9411 14 1422 -497 C ATOM 2678 CG1 VAL B 129 40.762 26.339 11.033 1.00 92.76 C ANISOU 2678 CG1 VAL B 129 15563 10370 9313 106 1319 -492 C ATOM 2679 CG2 VAL B 129 39.591 25.078 9.161 1.00 92.21 C ANISOU 2679 CG2 VAL B 129 15057 10458 9521 49 1380 -559 C ATOM 2680 N LEU B 130 43.282 25.063 9.375 1.00 84.00 N ANISOU 2680 N LEU B 130 14424 9259 8233 26 935 -292 N ATOM 2681 CA LEU B 130 44.241 25.303 8.300 1.00 82.40 C ANISOU 2681 CA LEU B 130 14143 9080 8085 48 735 -236 C ATOM 2682 C LEU B 130 45.268 24.166 8.251 1.00 85.75 C ANISOU 2682 C LEU B 130 14633 9471 8476 -26 664 -156 C ATOM 2683 O LEU B 130 45.611 23.699 7.166 1.00 84.34 O ANISOU 2683 O LEU B 130 14319 9346 8383 -42 583 -131 O ATOM 2684 CB LEU B 130 44.942 26.664 8.470 1.00 82.22 C ANISOU 2684 CB LEU B 130 14216 9008 8017 121 594 -215 C ATOM 2685 CG LEU B 130 45.881 27.093 7.324 1.00 85.71 C ANISOU 2685 CG LEU B 130 14572 9469 8524 145 406 -160 C ATOM 2686 CD1 LEU B 130 45.115 27.328 6.019 1.00 85.13 C ANISOU 2686 CD1 LEU B 130 14275 9494 8576 188 406 -199 C ATOM 2687 CD2 LEU B 130 46.626 28.339 7.680 1.00 88.80 C ANISOU 2687 CD2 LEU B 130 15083 9788 8868 198 284 -138 C ATOM 2688 N CYS B 131 45.708 23.695 9.434 1.00 83.07 N ANISOU 2688 N CYS B 131 14509 9042 8010 -65 698 -123 N ATOM 2689 CA CYS B 131 46.665 22.602 9.613 1.00 82.76 C ANISOU 2689 CA CYS B 131 14569 8952 7923 -126 632 -53 C ATOM 2690 C CYS B 131 46.213 21.368 8.794 1.00 84.49 C ANISOU 2690 C CYS B 131 14626 9234 8241 -190 703 -58 C ATOM 2691 O CYS B 131 46.953 20.910 7.917 1.00 82.48 O ANISOU 2691 O CYS B 131 14286 9006 8047 -204 582 -19 O ATOM 2692 CB CYS B 131 46.807 22.277 11.100 1.00 84.93 C ANISOU 2692 CB CYS B 131 15109 9123 8038 -149 702 -36 C ATOM 2693 SG CYS B 131 47.985 20.956 11.481 1.00 89.17 S ANISOU 2693 SG CYS B 131 15806 9576 8499 -208 607 48 S ATOM 2694 N LYS B 132 44.960 20.913 9.014 1.00 80.80 N ANISOU 2694 N LYS B 132 14098 8796 7805 -227 900 -118 N ATOM 2695 CA LYS B 132 44.353 19.777 8.310 1.00 79.57 C ANISOU 2695 CA LYS B 132 13781 8694 7756 -291 985 -141 C ATOM 2696 C LYS B 132 44.345 19.999 6.799 1.00 80.85 C ANISOU 2696 C LYS B 132 13707 8957 8057 -255 873 -162 C ATOM 2697 O LYS B 132 44.605 19.053 6.060 1.00 80.20 O ANISOU 2697 O LYS B 132 13535 8900 8035 -297 833 -144 O ATOM 2698 CB LYS B 132 42.911 19.529 8.800 1.00 82.81 C ANISOU 2698 CB LYS B 132 14142 9120 8201 -329 1223 -220 C ATOM 2699 CG LYS B 132 42.809 19.010 10.233 1.00 86.80 C ANISOU 2699 CG LYS B 132 14888 9524 8567 -385 1376 -196 C ATOM 2700 CD LYS B 132 41.359 18.914 10.690 1.00 91.43 C ANISOU 2700 CD LYS B 132 15409 10129 9200 -421 1629 -282 C ATOM 2701 CE LYS B 132 41.193 18.299 12.063 1.00103.22 C ANISOU 2701 CE LYS B 132 17148 11518 10551 -487 1811 -254 C ATOM 2702 NZ LYS B 132 41.584 16.861 12.102 1.00111.97 N ANISOU 2702 NZ LYS B 132 18332 12569 11642 -581 1831 -191 N ATOM 2703 N ILE B 133 44.066 21.243 6.340 1.00 75.76 N ANISOU 2703 N ILE B 133 12972 8361 7451 -171 819 -199 N ATOM 2704 CA ILE B 133 44.000 21.583 4.911 1.00 73.82 C ANISOU 2704 CA ILE B 133 12525 8205 7319 -122 712 -218 C ATOM 2705 C ILE B 133 45.410 21.527 4.293 1.00 75.67 C ANISOU 2705 C ILE B 133 12792 8425 7532 -117 531 -133 C ATOM 2706 O ILE B 133 45.616 20.788 3.332 1.00 73.57 O ANISOU 2706 O ILE B 133 12414 8207 7334 -139 483 -124 O ATOM 2707 CB ILE B 133 43.340 22.976 4.683 1.00 76.69 C ANISOU 2707 CB ILE B 133 12816 8606 7716 -27 701 -275 C ATOM 2708 CG1 ILE B 133 41.859 22.965 5.146 1.00 77.93 C ANISOU 2708 CG1 ILE B 133 12893 8791 7925 -28 887 -378 C ATOM 2709 CG2 ILE B 133 43.440 23.392 3.210 1.00 76.68 C ANISOU 2709 CG2 ILE B 133 12651 8681 7803 34 568 -277 C ATOM 2710 CD1 ILE B 133 41.106 24.325 5.068 1.00 79.78 C ANISOU 2710 CD1 ILE B 133 13063 9055 8196 74 888 -448 C ATOM 2711 N VAL B 134 46.363 22.287 4.862 1.00 72.74 N ANISOU 2711 N VAL B 134 12574 7986 7077 -90 436 -79 N ATOM 2712 CA VAL B 134 47.745 22.413 4.386 1.00 71.83 C ANISOU 2712 CA VAL B 134 12490 7848 6954 -84 269 -7 C ATOM 2713 C VAL B 134 48.446 21.027 4.387 1.00 76.31 C ANISOU 2713 C VAL B 134 13089 8391 7514 -154 248 36 C ATOM 2714 O VAL B 134 49.115 20.707 3.403 1.00 74.62 O ANISOU 2714 O VAL B 134 12783 8213 7355 -156 154 65 O ATOM 2715 CB VAL B 134 48.528 23.442 5.238 1.00 75.72 C ANISOU 2715 CB VAL B 134 13150 8256 7364 -51 187 26 C ATOM 2716 CG1 VAL B 134 49.991 23.483 4.856 1.00 74.49 C ANISOU 2716 CG1 VAL B 134 13021 8067 7216 -58 25 93 C ATOM 2717 CG2 VAL B 134 47.920 24.830 5.094 1.00 75.96 C ANISOU 2717 CG2 VAL B 134 13143 8306 7412 23 190 -14 C ATOM 2718 N LEU B 135 48.265 20.204 5.445 1.00 74.65 N ANISOU 2718 N LEU B 135 13010 8119 7234 -208 340 38 N ATOM 2719 CA LEU B 135 48.886 18.867 5.487 1.00 74.54 C ANISOU 2719 CA LEU B 135 13040 8071 7212 -269 318 78 C ATOM 2720 C LEU B 135 48.338 17.958 4.372 1.00 78.27 C ANISOU 2720 C LEU B 135 13323 8624 7792 -300 360 47 C ATOM 2721 O LEU B 135 49.130 17.315 3.678 1.00 76.79 O ANISOU 2721 O LEU B 135 13088 8447 7643 -313 267 79 O ATOM 2722 CB LEU B 135 48.690 18.168 6.851 1.00 75.56 C ANISOU 2722 CB LEU B 135 13368 8107 7234 -318 421 89 C ATOM 2723 CG LEU B 135 49.429 18.732 8.065 1.00 80.50 C ANISOU 2723 CG LEU B 135 14226 8632 7728 -291 355 124 C ATOM 2724 CD1 LEU B 135 48.968 18.043 9.331 1.00 82.01 C ANISOU 2724 CD1 LEU B 135 14615 8740 7804 -335 491 128 C ATOM 2725 CD2 LEU B 135 50.946 18.607 7.911 1.00 81.51 C ANISOU 2725 CD2 LEU B 135 14406 8713 7849 -278 158 180 C ATOM 2726 N SER B 136 46.987 17.924 4.200 1.00 75.56 N ANISOU 2726 N SER B 136 12866 8336 7506 -308 498 -23 N ATOM 2727 CA SER B 136 46.277 17.107 3.209 1.00 74.96 C ANISOU 2727 CA SER B 136 12605 8335 7543 -336 544 -73 C ATOM 2728 C SER B 136 46.778 17.380 1.808 1.00 77.35 C ANISOU 2728 C SER B 136 12765 8713 7912 -286 406 -66 C ATOM 2729 O SER B 136 47.041 16.432 1.073 1.00 76.90 O ANISOU 2729 O SER B 136 12632 8680 7905 -314 371 -63 O ATOM 2730 CB SER B 136 44.776 17.368 3.271 1.00 79.03 C ANISOU 2730 CB SER B 136 13009 8899 8122 -333 692 -163 C ATOM 2731 N ILE B 137 46.946 18.670 1.453 1.00 72.45 N ANISOU 2731 N ILE B 137 12122 8121 7286 -211 330 -60 N ATOM 2732 CA ILE B 137 47.423 19.119 0.141 1.00 70.92 C ANISOU 2732 CA ILE B 137 11818 7991 7138 -156 210 -46 C ATOM 2733 C ILE B 137 48.896 18.679 -0.049 1.00 74.29 C ANISOU 2733 C ILE B 137 12308 8379 7538 -178 99 30 C ATOM 2734 O ILE B 137 49.242 18.169 -1.115 1.00 72.66 O ANISOU 2734 O ILE B 137 12005 8222 7380 -175 44 34 O ATOM 2735 CB ILE B 137 47.255 20.673 -0.008 1.00 73.45 C ANISOU 2735 CB ILE B 137 12135 8326 7447 -74 168 -50 C ATOM 2736 CG1 ILE B 137 45.766 21.081 0.148 1.00 73.99 C ANISOU 2736 CG1 ILE B 137 12122 8434 7556 -42 273 -138 C ATOM 2737 CG2 ILE B 137 47.819 21.167 -1.351 1.00 73.16 C ANISOU 2737 CG2 ILE B 137 12014 8341 7442 -20 51 -22 C ATOM 2738 CD1 ILE B 137 45.474 22.565 0.132 1.00 76.04 C ANISOU 2738 CD1 ILE B 137 12390 8697 7805 43 240 -151 C ATOM 2739 N ASP B 138 49.737 18.849 0.995 1.00 71.81 N ANISOU 2739 N ASP B 138 12157 7977 7151 -196 66 80 N ATOM 2740 CA ASP B 138 51.161 18.508 0.971 1.00 71.58 C ANISOU 2740 CA ASP B 138 12189 7900 7106 -212 -47 141 C ATOM 2741 C ASP B 138 51.353 17.008 0.656 1.00 76.12 C ANISOU 2741 C ASP B 138 12729 8480 7713 -263 -38 140 C ATOM 2742 O ASP B 138 52.096 16.678 -0.273 1.00 74.64 O ANISOU 2742 O ASP B 138 12464 8324 7572 -255 -115 157 O ATOM 2743 CB ASP B 138 51.818 18.872 2.324 1.00 74.03 C ANISOU 2743 CB ASP B 138 12690 8106 7332 -220 -82 175 C ATOM 2744 CG ASP B 138 53.341 18.823 2.350 1.00 84.15 C ANISOU 2744 CG ASP B 138 14026 9335 8614 -221 -221 227 C ATOM 2745 OD1 ASP B 138 53.966 19.184 1.326 1.00 84.70 O ANISOU 2745 OD1 ASP B 138 13989 9446 8745 -200 -294 243 O ATOM 2746 OD2 ASP B 138 53.909 18.550 3.435 1.00 87.54 O ANISOU 2746 OD2 ASP B 138 14610 9673 8978 -237 -260 247 O ATOM 2747 N TYR B 139 50.638 16.111 1.407 1.00 73.75 N ANISOU 2747 N TYR B 139 12486 8144 7391 -314 68 116 N ATOM 2748 CA TYR B 139 50.687 14.644 1.241 1.00 72.98 C ANISOU 2748 CA TYR B 139 12373 8033 7322 -368 91 112 C ATOM 2749 C TYR B 139 50.046 14.156 -0.065 1.00 74.93 C ANISOU 2749 C TYR B 139 12428 8376 7666 -367 112 60 C ATOM 2750 O TYR B 139 50.702 13.438 -0.821 1.00 73.77 O ANISOU 2750 O TYR B 139 12227 8246 7557 -370 44 70 O ATOM 2751 CB TYR B 139 49.981 13.919 2.397 1.00 74.90 C ANISOU 2751 CB TYR B 139 12737 8204 7516 -429 218 102 C ATOM 2752 CG TYR B 139 50.798 13.752 3.651 1.00 77.28 C ANISOU 2752 CG TYR B 139 13261 8391 7713 -442 180 158 C ATOM 2753 CD1 TYR B 139 51.697 12.697 3.781 1.00 79.19 C ANISOU 2753 CD1 TYR B 139 13579 8569 7943 -466 107 196 C ATOM 2754 CD2 TYR B 139 50.567 14.550 4.767 1.00 79.12 C ANISOU 2754 CD2 TYR B 139 13638 8571 7852 -428 225 166 C ATOM 2755 CE1 TYR B 139 52.407 12.492 4.962 1.00 80.99 C ANISOU 2755 CE1 TYR B 139 14023 8682 8068 -469 59 242 C ATOM 2756 CE2 TYR B 139 51.271 14.356 5.955 1.00 80.67 C ANISOU 2756 CE2 TYR B 139 14058 8655 7939 -433 183 212 C ATOM 2757 CZ TYR B 139 52.179 13.314 6.053 1.00 87.71 C ANISOU 2757 CZ TYR B 139 15025 9483 8819 -452 96 250 C ATOM 2758 OH TYR B 139 52.870 13.098 7.222 1.00 88.39 O ANISOU 2758 OH TYR B 139 15342 9452 8792 -447 37 292 O ATOM 2759 N TYR B 140 48.743 14.474 -0.283 1.00 70.87 N ANISOU 2759 N TYR B 140 11814 7919 7193 -360 207 -4 N ATOM 2760 CA TYR B 140 47.961 14.029 -1.441 1.00 70.28 C ANISOU 2760 CA TYR B 140 11559 7932 7213 -353 225 -71 C ATOM 2761 C TYR B 140 48.749 14.216 -2.742 1.00 72.54 C ANISOU 2761 C TYR B 140 11760 8280 7522 -299 99 -53 C ATOM 2762 O TYR B 140 48.981 13.239 -3.462 1.00 71.91 O ANISOU 2762 O TYR B 140 11617 8222 7485 -317 69 -68 O ATOM 2763 CB TYR B 140 46.613 14.789 -1.524 1.00 71.97 C ANISOU 2763 CB TYR B 140 11674 8203 7469 -322 304 -144 C ATOM 2764 CG TYR B 140 45.800 14.480 -2.765 1.00 74.17 C ANISOU 2764 CG TYR B 140 11761 8572 7846 -298 294 -224 C ATOM 2765 CD1 TYR B 140 44.894 13.427 -2.785 1.00 76.79 C ANISOU 2765 CD1 TYR B 140 12008 8909 8259 -359 384 -296 C ATOM 2766 CD2 TYR B 140 45.921 15.257 -3.912 1.00 74.83 C ANISOU 2766 CD2 TYR B 140 11758 8732 7943 -212 192 -232 C ATOM 2767 CE1 TYR B 140 44.156 13.128 -3.929 1.00 77.62 C ANISOU 2767 CE1 TYR B 140 11934 9095 8462 -332 356 -381 C ATOM 2768 CE2 TYR B 140 45.195 14.964 -5.064 1.00 76.22 C ANISOU 2768 CE2 TYR B 140 11774 8988 8198 -178 164 -310 C ATOM 2769 CZ TYR B 140 44.306 13.905 -5.064 1.00 84.72 C ANISOU 2769 CZ TYR B 140 12757 10071 9360 -236 239 -389 C ATOM 2770 OH TYR B 140 43.586 13.631 -6.198 1.00 88.20 O ANISOU 2770 OH TYR B 140 13039 10589 9884 -197 195 -477 O ATOM 2771 N ASN B 141 49.174 15.459 -3.026 1.00 67.58 N ANISOU 2771 N ASN B 141 11140 7674 6864 -235 32 -22 N ATOM 2772 CA ASN B 141 49.868 15.776 -4.258 1.00 66.10 C ANISOU 2772 CA ASN B 141 10883 7541 6690 -184 -65 -1 C ATOM 2773 C ASN B 141 51.336 15.275 -4.239 1.00 68.13 C ANISOU 2773 C ASN B 141 11204 7752 6929 -207 -139 62 C ATOM 2774 O ASN B 141 51.928 15.205 -5.312 1.00 68.15 O ANISOU 2774 O ASN B 141 11142 7801 6953 -178 -199 72 O ATOM 2775 CB ASN B 141 49.820 17.264 -4.543 1.00 66.27 C ANISOU 2775 CB ASN B 141 10903 7588 6688 -115 -100 16 C ATOM 2776 CG ASN B 141 48.447 17.721 -4.971 1.00 89.61 C ANISOU 2776 CG ASN B 141 13761 10609 9680 -68 -58 -56 C ATOM 2777 OD1 ASN B 141 48.082 17.644 -6.152 1.00 81.79 O ANISOU 2777 OD1 ASN B 141 12663 9691 8722 -22 -95 -94 O ATOM 2778 ND2 ASN B 141 47.637 18.166 -4.019 1.00 82.77 N ANISOU 2778 ND2 ASN B 141 12928 9715 8807 -73 17 -86 N ATOM 2779 N MET B 142 51.899 14.864 -3.081 1.00 63.10 N ANISOU 2779 N MET B 142 10692 7025 6256 -254 -137 97 N ATOM 2780 CA MET B 142 53.246 14.281 -3.083 1.00 62.38 C ANISOU 2780 CA MET B 142 10646 6890 6167 -269 -218 141 C ATOM 2781 C MET B 142 53.209 12.959 -3.822 1.00 66.99 C ANISOU 2781 C MET B 142 11152 7502 6800 -290 -215 109 C ATOM 2782 O MET B 142 54.016 12.745 -4.723 1.00 67.50 O ANISOU 2782 O MET B 142 11155 7598 6893 -268 -278 118 O ATOM 2783 CB MET B 142 53.805 14.101 -1.670 1.00 65.25 C ANISOU 2783 CB MET B 142 11172 7144 6477 -302 -234 178 C ATOM 2784 CG MET B 142 55.176 13.447 -1.649 1.00 69.04 C ANISOU 2784 CG MET B 142 11688 7572 6970 -309 -332 211 C ATOM 2785 SD MET B 142 55.599 12.807 -0.009 1.00 74.35 S ANISOU 2785 SD MET B 142 12565 8110 7574 -344 -354 239 S ATOM 2786 CE MET B 142 57.135 12.146 -0.342 1.00 70.94 C ANISOU 2786 CE MET B 142 12119 7643 7190 -332 -486 259 C ATOM 2787 N PHE B 143 52.233 12.086 -3.468 1.00 63.00 N ANISOU 2787 N PHE B 143 10644 6985 6308 -335 -132 65 N ATOM 2788 CA PHE B 143 52.022 10.793 -4.122 1.00 61.97 C ANISOU 2788 CA PHE B 143 10439 6874 6233 -361 -122 23 C ATOM 2789 C PHE B 143 51.514 10.989 -5.551 1.00 65.59 C ANISOU 2789 C PHE B 143 10742 7441 6738 -314 -136 -29 C ATOM 2790 O PHE B 143 51.951 10.261 -6.434 1.00 64.92 O ANISOU 2790 O PHE B 143 10596 7385 6685 -304 -181 -46 O ATOM 2791 CB PHE B 143 51.039 9.914 -3.333 1.00 63.82 C ANISOU 2791 CB PHE B 143 10713 7057 6480 -430 -17 -11 C ATOM 2792 CG PHE B 143 51.537 9.480 -1.981 1.00 65.12 C ANISOU 2792 CG PHE B 143 11056 7103 6583 -475 -3 41 C ATOM 2793 CD1 PHE B 143 52.294 8.324 -1.843 1.00 68.05 C ANISOU 2793 CD1 PHE B 143 11490 7407 6959 -501 -49 62 C ATOM 2794 CD2 PHE B 143 51.228 10.210 -0.839 1.00 67.02 C ANISOU 2794 CD2 PHE B 143 11414 7296 6756 -484 52 66 C ATOM 2795 CE1 PHE B 143 52.757 7.919 -0.590 1.00 69.27 C ANISOU 2795 CE1 PHE B 143 11829 7444 7046 -532 -51 111 C ATOM 2796 CE2 PHE B 143 51.694 9.809 0.413 1.00 69.99 C ANISOU 2796 CE2 PHE B 143 11978 7557 7057 -516 57 115 C ATOM 2797 CZ PHE B 143 52.461 8.670 0.530 1.00 68.22 C ANISOU 2797 CZ PHE B 143 11823 7265 6835 -538 1 138 C ATOM 2798 N THR B 144 50.616 11.982 -5.785 1.00 62.07 N ANISOU 2798 N THR B 144 10240 7052 6292 -276 -105 -57 N ATOM 2799 CA THR B 144 50.075 12.266 -7.118 1.00 62.27 C ANISOU 2799 CA THR B 144 10135 7177 6349 -217 -133 -109 C ATOM 2800 C THR B 144 51.234 12.714 -8.037 1.00 66.19 C ANISOU 2800 C THR B 144 10629 7704 6816 -164 -219 -60 C ATOM 2801 O THR B 144 51.281 12.282 -9.192 1.00 66.38 O ANISOU 2801 O THR B 144 10575 7788 6858 -131 -254 -92 O ATOM 2802 CB THR B 144 48.940 13.304 -7.046 1.00 73.33 C ANISOU 2802 CB THR B 144 11493 8617 7754 -179 -95 -146 C ATOM 2803 OG1 THR B 144 47.928 12.804 -6.176 1.00 74.70 O ANISOU 2803 OG1 THR B 144 11662 8757 7965 -237 4 -195 O ATOM 2804 CG2 THR B 144 48.308 13.591 -8.406 1.00 72.56 C ANISOU 2804 CG2 THR B 144 11272 8614 7683 -105 -140 -206 C ATOM 2805 N SER B 145 52.201 13.500 -7.506 1.00 61.53 N ANISOU 2805 N SER B 145 10127 7068 6185 -160 -248 14 N ATOM 2806 CA SER B 145 53.381 13.922 -8.265 1.00 60.60 C ANISOU 2806 CA SER B 145 10006 6967 6054 -125 -310 63 C ATOM 2807 C SER B 145 54.296 12.712 -8.606 1.00 64.56 C ANISOU 2807 C SER B 145 10491 7455 6584 -148 -341 61 C ATOM 2808 O SER B 145 54.619 12.491 -9.775 1.00 63.08 O ANISOU 2808 O SER B 145 10239 7325 6404 -112 -364 47 O ATOM 2809 CB SER B 145 54.173 14.971 -7.490 1.00 62.46 C ANISOU 2809 CB SER B 145 10330 7142 6260 -128 -333 130 C ATOM 2810 N ILE B 146 54.659 11.919 -7.585 1.00 61.86 N ANISOU 2810 N ILE B 146 10217 7033 6252 -202 -342 72 N ATOM 2811 CA ILE B 146 55.593 10.802 -7.687 1.00 61.98 C ANISOU 2811 CA ILE B 146 10236 7015 6298 -221 -382 72 C ATOM 2812 C ILE B 146 54.955 9.608 -8.465 1.00 68.64 C ANISOU 2812 C ILE B 146 11002 7900 7177 -225 -362 4 C ATOM 2813 O ILE B 146 55.649 9.027 -9.302 1.00 68.76 O ANISOU 2813 O ILE B 146 10969 7940 7215 -204 -399 -9 O ATOM 2814 CB ILE B 146 56.049 10.380 -6.263 1.00 64.76 C ANISOU 2814 CB ILE B 146 10710 7257 6639 -267 -397 104 C ATOM 2815 CG1 ILE B 146 56.861 11.537 -5.614 1.00 64.82 C ANISOU 2815 CG1 ILE B 146 10786 7223 6621 -255 -441 161 C ATOM 2816 CG2 ILE B 146 56.895 9.102 -6.308 1.00 65.15 C ANISOU 2816 CG2 ILE B 146 10768 7262 6726 -281 -446 96 C ATOM 2817 CD1 ILE B 146 57.228 11.394 -4.133 1.00 71.60 C ANISOU 2817 CD1 ILE B 146 11786 7971 7447 -286 -470 191 C ATOM 2818 N PHE B 147 53.672 9.260 -8.231 1.00 66.32 N ANISOU 2818 N PHE B 147 10689 7614 6896 -253 -305 -45 N ATOM 2819 CA PHE B 147 53.060 8.129 -8.944 1.00 66.68 C ANISOU 2819 CA PHE B 147 10656 7690 6990 -263 -294 -119 C ATOM 2820 C PHE B 147 52.802 8.450 -10.437 1.00 69.18 C ANISOU 2820 C PHE B 147 10866 8113 7307 -194 -323 -163 C ATOM 2821 O PHE B 147 52.907 7.536 -11.257 1.00 69.02 O ANISOU 2821 O PHE B 147 10791 8118 7314 -183 -349 -211 O ATOM 2822 CB PHE B 147 51.747 7.661 -8.302 1.00 69.41 C ANISOU 2822 CB PHE B 147 10995 8008 7369 -320 -216 -168 C ATOM 2823 CG PHE B 147 51.874 7.097 -6.905 1.00 71.79 C ANISOU 2823 CG PHE B 147 11420 8198 7660 -391 -172 -131 C ATOM 2824 CD1 PHE B 147 53.013 6.395 -6.524 1.00 75.15 C ANISOU 2824 CD1 PHE B 147 11929 8549 8074 -405 -224 -88 C ATOM 2825 CD2 PHE B 147 50.781 7.085 -6.042 1.00 75.10 C ANISOU 2825 CD2 PHE B 147 11866 8582 8088 -445 -75 -152 C ATOM 2826 CE1 PHE B 147 53.113 5.827 -5.254 1.00 76.43 C ANISOU 2826 CE1 PHE B 147 12228 8600 8215 -462 -193 -53 C ATOM 2827 CE2 PHE B 147 50.873 6.494 -4.775 1.00 78.52 C ANISOU 2827 CE2 PHE B 147 12435 8904 8495 -511 -24 -115 C ATOM 2828 CZ PHE B 147 52.041 5.872 -4.390 1.00 76.28 C ANISOU 2828 CZ PHE B 147 12255 8542 8184 -516 -90 -63 C ATOM 2829 N THR B 148 52.488 9.717 -10.793 1.00 64.45 N ANISOU 2829 N THR B 148 10248 7568 6670 -143 -325 -148 N ATOM 2830 CA THR B 148 52.299 10.095 -12.202 1.00 64.02 C ANISOU 2830 CA THR B 148 10122 7606 6595 -66 -360 -180 C ATOM 2831 C THR B 148 53.662 9.985 -12.908 1.00 67.23 C ANISOU 2831 C THR B 148 10544 8022 6977 -39 -396 -138 C ATOM 2832 O THR B 148 53.759 9.385 -13.974 1.00 66.63 O ANISOU 2832 O THR B 148 10420 7996 6900 -3 -420 -183 O ATOM 2833 CB THR B 148 51.672 11.504 -12.319 1.00 68.36 C ANISOU 2833 CB THR B 148 10672 8195 7107 -15 -357 -165 C ATOM 2834 OG1 THR B 148 50.417 11.512 -11.643 1.00 65.22 O ANISOU 2834 OG1 THR B 148 10246 7788 6748 -42 -315 -216 O ATOM 2835 CG2 THR B 148 51.457 11.939 -13.767 1.00 66.60 C ANISOU 2835 CG2 THR B 148 10403 8058 6846 74 -401 -193 C ATOM 2836 N LEU B 149 54.713 10.494 -12.245 1.00 63.78 N ANISOU 2836 N LEU B 149 10173 7533 6529 -59 -398 -62 N ATOM 2837 CA LEU B 149 56.112 10.499 -12.668 1.00 63.30 C ANISOU 2837 CA LEU B 149 10120 7466 6467 -46 -419 -19 C ATOM 2838 C LEU B 149 56.634 9.083 -12.934 1.00 67.92 C ANISOU 2838 C LEU B 149 10677 8036 7093 -60 -439 -61 C ATOM 2839 O LEU B 149 57.447 8.883 -13.848 1.00 67.61 O ANISOU 2839 O LEU B 149 10606 8031 7052 -25 -448 -64 O ATOM 2840 CB LEU B 149 56.938 11.154 -11.546 1.00 62.91 C ANISOU 2840 CB LEU B 149 10140 7340 6425 -81 -427 51 C ATOM 2841 CG LEU B 149 58.371 11.505 -11.847 1.00 67.48 C ANISOU 2841 CG LEU B 149 10716 7905 7019 -72 -446 98 C ATOM 2842 CD1 LEU B 149 58.430 12.671 -12.781 1.00 68.06 C ANISOU 2842 CD1 LEU B 149 10775 8035 7051 -26 -421 130 C ATOM 2843 CD2 LEU B 149 59.066 11.915 -10.603 1.00 69.56 C ANISOU 2843 CD2 LEU B 149 11044 8081 7306 -111 -474 145 C ATOM 2844 N THR B 150 56.178 8.112 -12.110 1.00 64.78 N ANISOU 2844 N THR B 150 10299 7581 6732 -111 -437 -91 N ATOM 2845 CA THR B 150 56.566 6.706 -12.170 1.00 64.89 C ANISOU 2845 CA THR B 150 10303 7559 6792 -131 -459 -131 C ATOM 2846 C THR B 150 55.802 5.999 -13.299 1.00 69.77 C ANISOU 2846 C THR B 150 10846 8245 7419 -101 -460 -215 C ATOM 2847 O THR B 150 56.394 5.189 -14.006 1.00 69.61 O ANISOU 2847 O THR B 150 10796 8236 7416 -78 -485 -249 O ATOM 2848 CB THR B 150 56.307 6.049 -10.811 1.00 70.89 C ANISOU 2848 CB THR B 150 11139 8220 7578 -199 -451 -122 C ATOM 2849 OG1 THR B 150 57.009 6.786 -9.813 1.00 65.11 O ANISOU 2849 OG1 THR B 150 10485 7428 6825 -213 -466 -50 O ATOM 2850 CG2 THR B 150 56.751 4.592 -10.762 1.00 70.88 C ANISOU 2850 CG2 THR B 150 11148 8161 7624 -219 -480 -155 C ATOM 2851 N MET B 151 54.501 6.312 -13.478 1.00 66.96 N ANISOU 2851 N MET B 151 10455 7932 7055 -97 -439 -257 N ATOM 2852 CA MET B 151 53.703 5.703 -14.541 1.00 67.60 C ANISOU 2852 CA MET B 151 10459 8074 7150 -65 -456 -349 C ATOM 2853 C MET B 151 54.179 6.195 -15.903 1.00 72.16 C ANISOU 2853 C MET B 151 11012 8737 7667 22 -484 -352 C ATOM 2854 O MET B 151 53.982 5.502 -16.898 1.00 72.54 O ANISOU 2854 O MET B 151 11017 8829 7715 60 -513 -425 O ATOM 2855 CB MET B 151 52.208 5.971 -14.362 1.00 70.38 C ANISOU 2855 CB MET B 151 10767 8448 7525 -78 -435 -402 C ATOM 2856 CG MET B 151 51.605 5.306 -13.132 1.00 74.47 C ANISOU 2856 CG MET B 151 11305 8882 8106 -170 -385 -413 C ATOM 2857 SD MET B 151 51.887 3.515 -12.991 1.00 79.14 S ANISOU 2857 SD MET B 151 11905 9397 8767 -229 -392 -459 S ATOM 2858 CE MET B 151 53.334 3.502 -11.946 1.00 75.27 C ANISOU 2858 CE MET B 151 11538 8816 8247 -255 -396 -352 C ATOM 2859 N MET B 152 54.850 7.364 -15.937 1.00 68.02 N ANISOU 2859 N MET B 152 10527 8228 7090 50 -471 -273 N ATOM 2860 CA MET B 152 55.488 7.901 -17.139 1.00 67.69 C ANISOU 2860 CA MET B 152 10485 8251 6983 122 -475 -256 C ATOM 2861 C MET B 152 56.647 7.015 -17.540 1.00 71.44 C ANISOU 2861 C MET B 152 10951 8714 7478 125 -476 -264 C ATOM 2862 O MET B 152 56.880 6.788 -18.721 1.00 71.89 O ANISOU 2862 O MET B 152 10992 8830 7494 184 -480 -300 O ATOM 2863 CB MET B 152 55.963 9.336 -16.908 1.00 69.65 C ANISOU 2863 CB MET B 152 10780 8496 7188 132 -448 -164 C ATOM 2864 CG MET B 152 54.852 10.320 -16.792 1.00 73.27 C ANISOU 2864 CG MET B 152 11248 8978 7614 155 -452 -161 C ATOM 2865 SD MET B 152 55.499 11.959 -16.457 1.00 77.13 S ANISOU 2865 SD MET B 152 11803 9443 8060 161 -424 -52 S ATOM 2866 CE MET B 152 54.064 12.852 -16.540 1.00 74.09 C ANISOU 2866 CE MET B 152 11419 9093 7640 208 -441 -76 C ATOM 2867 N SER B 153 57.366 6.503 -16.531 1.00 66.77 N ANISOU 2867 N SER B 153 10377 8044 6949 66 -477 -236 N ATOM 2868 CA SER B 153 58.492 5.595 -16.662 1.00 66.02 C ANISOU 2868 CA SER B 153 10270 7918 6896 65 -488 -249 C ATOM 2869 C SER B 153 57.998 4.231 -17.171 1.00 69.44 C ANISOU 2869 C SER B 153 10670 8358 7356 74 -516 -343 C ATOM 2870 O SER B 153 58.584 3.675 -18.103 1.00 69.35 O ANISOU 2870 O SER B 153 10632 8380 7338 120 -520 -384 O ATOM 2871 CB SER B 153 59.200 5.474 -15.313 1.00 68.54 C ANISOU 2871 CB SER B 153 10629 8141 7273 7 -503 -199 C ATOM 2872 OG SER B 153 60.335 4.631 -15.359 1.00 78.77 O ANISOU 2872 OG SER B 153 11909 9398 8621 13 -527 -214 O ATOM 2873 N VAL B 154 56.874 3.734 -16.595 1.00 64.97 N ANISOU 2873 N VAL B 154 10103 7760 6821 29 -527 -383 N ATOM 2874 CA VAL B 154 56.234 2.455 -16.936 1.00 64.59 C ANISOU 2874 CA VAL B 154 10023 7703 6817 21 -553 -477 C ATOM 2875 C VAL B 154 55.669 2.536 -18.366 1.00 67.25 C ANISOU 2875 C VAL B 154 10311 8137 7103 96 -573 -549 C ATOM 2876 O VAL B 154 55.797 1.572 -19.122 1.00 67.44 O ANISOU 2876 O VAL B 154 10311 8174 7140 125 -601 -624 O ATOM 2877 CB VAL B 154 55.125 2.082 -15.902 1.00 68.59 C ANISOU 2877 CB VAL B 154 10539 8145 7377 -57 -539 -494 C ATOM 2878 CG1 VAL B 154 54.389 0.800 -16.295 1.00 68.95 C ANISOU 2878 CG1 VAL B 154 10541 8175 7482 -75 -562 -597 C ATOM 2879 CG2 VAL B 154 55.711 1.942 -14.503 1.00 68.16 C ANISOU 2879 CG2 VAL B 154 10560 7986 7351 -121 -525 -422 C ATOM 2880 N ASP B 155 55.068 3.690 -18.731 1.00 62.34 N ANISOU 2880 N ASP B 155 9687 7581 6420 134 -565 -530 N ATOM 2881 CA ASP B 155 54.495 3.925 -20.059 1.00 62.07 C ANISOU 2881 CA ASP B 155 9629 7636 6319 218 -597 -592 C ATOM 2882 C ASP B 155 55.600 3.871 -21.124 1.00 63.52 C ANISOU 2882 C ASP B 155 9836 7864 6436 286 -587 -584 C ATOM 2883 O ASP B 155 55.448 3.151 -22.111 1.00 62.73 O ANISOU 2883 O ASP B 155 9719 7802 6312 338 -622 -669 O ATOM 2884 CB ASP B 155 53.764 5.274 -20.094 1.00 64.18 C ANISOU 2884 CB ASP B 155 9907 7947 6531 249 -594 -556 C ATOM 2885 CG ASP B 155 52.984 5.524 -21.363 1.00 76.41 C ANISOU 2885 CG ASP B 155 11441 9579 8011 343 -647 -627 C ATOM 2886 OD1 ASP B 155 51.858 4.989 -21.480 1.00 77.35 O ANISOU 2886 OD1 ASP B 155 11502 9708 8181 342 -697 -725 O ATOM 2887 OD2 ASP B 155 53.451 6.335 -22.196 1.00 82.78 O ANISOU 2887 OD2 ASP B 155 12301 10436 8715 416 -639 -584 O ATOM 2888 N ARG B 156 56.738 4.582 -20.880 1.00 59.00 N ANISOU 2888 N ARG B 156 9299 7279 5841 280 -536 -489 N ATOM 2889 CA ARG B 156 57.918 4.605 -21.761 1.00 58.49 C ANISOU 2889 CA ARG B 156 9249 7247 5729 331 -499 -473 C ATOM 2890 C ARG B 156 58.584 3.223 -21.815 1.00 60.96 C ANISOU 2890 C ARG B 156 9531 7525 6106 322 -513 -533 C ATOM 2891 O ARG B 156 59.148 2.866 -22.848 1.00 60.53 O ANISOU 2891 O ARG B 156 9477 7514 6009 382 -496 -573 O ATOM 2892 CB ARG B 156 58.952 5.665 -21.315 1.00 57.82 C ANISOU 2892 CB ARG B 156 9189 7140 5639 308 -438 -363 C ATOM 2893 CG ARG B 156 58.512 7.131 -21.429 1.00 69.92 C ANISOU 2893 CG ARG B 156 10766 8704 7098 328 -416 -295 C ATOM 2894 CD ARG B 156 59.654 8.031 -20.983 1.00 88.50 C ANISOU 2894 CD ARG B 156 13136 11022 9469 296 -357 -198 C ATOM 2895 NE ARG B 156 59.299 9.450 -20.918 1.00105.05 N ANISOU 2895 NE ARG B 156 15280 13126 11508 304 -336 -125 N ATOM 2896 CZ ARG B 156 60.136 10.414 -20.533 1.00122.34 C ANISOU 2896 CZ ARG B 156 17489 15280 13713 273 -288 -40 C ATOM 2897 NH1 ARG B 156 61.388 10.124 -20.192 1.00106.15 N ANISOU 2897 NH1 ARG B 156 15403 13189 11739 233 -258 -21 N ATOM 2898 NH2 ARG B 156 59.730 11.677 -20.498 1.00112.77 N ANISOU 2898 NH2 ARG B 156 16329 14069 12449 284 -276 21 N ATOM 2899 N TYR B 157 58.521 2.456 -20.703 1.00 56.79 N ANISOU 2899 N TYR B 157 8989 6914 5676 251 -540 -541 N ATOM 2900 CA TYR B 157 59.072 1.103 -20.617 1.00 56.55 C ANISOU 2900 CA TYR B 157 8940 6831 5716 241 -566 -598 C ATOM 2901 C TYR B 157 58.283 0.131 -21.510 1.00 62.14 C ANISOU 2901 C TYR B 157 9625 7569 6414 278 -610 -713 C ATOM 2902 O TYR B 157 58.887 -0.606 -22.294 1.00 62.29 O ANISOU 2902 O TYR B 157 9634 7604 6428 327 -615 -771 O ATOM 2903 CB TYR B 157 59.074 0.605 -19.166 1.00 56.65 C ANISOU 2903 CB TYR B 157 8970 6736 5819 157 -587 -569 C ATOM 2904 CG TYR B 157 59.261 -0.890 -19.059 1.00 58.57 C ANISOU 2904 CG TYR B 157 9208 6913 6135 145 -628 -639 C ATOM 2905 CD1 TYR B 157 60.520 -1.468 -19.199 1.00 60.69 C ANISOU 2905 CD1 TYR B 157 9467 7153 6440 175 -636 -647 C ATOM 2906 CD2 TYR B 157 58.177 -1.734 -18.818 1.00 59.45 C ANISOU 2906 CD2 TYR B 157 9318 6984 6287 103 -658 -701 C ATOM 2907 CE1 TYR B 157 60.695 -2.847 -19.118 1.00 61.19 C ANISOU 2907 CE1 TYR B 157 9532 7148 6571 172 -681 -714 C ATOM 2908 CE2 TYR B 157 58.341 -3.115 -18.739 1.00 60.63 C ANISOU 2908 CE2 TYR B 157 9472 7061 6505 90 -695 -764 C ATOM 2909 CZ TYR B 157 59.602 -3.665 -18.892 1.00 67.41 C ANISOU 2909 CZ TYR B 157 10333 7890 7390 129 -711 -769 C ATOM 2910 OH TYR B 157 59.770 -5.019 -18.822 1.00 69.62 O ANISOU 2910 OH TYR B 157 10623 8091 7737 123 -754 -833 O ATOM 2911 N ILE B 158 56.945 0.106 -21.354 1.00 59.26 N ANISOU 2911 N ILE B 158 9248 7209 6060 253 -642 -754 N ATOM 2912 CA ILE B 158 56.045 -0.752 -22.121 1.00 60.18 C ANISOU 2912 CA ILE B 158 9333 7349 6185 281 -697 -873 C ATOM 2913 C ILE B 158 56.155 -0.380 -23.606 1.00 67.05 C ANISOU 2913 C ILE B 158 10215 8320 6942 389 -706 -913 C ATOM 2914 O ILE B 158 56.209 -1.271 -24.450 1.00 67.54 O ANISOU 2914 O ILE B 158 10269 8397 6994 437 -742 -1007 O ATOM 2915 CB ILE B 158 54.593 -0.635 -21.579 1.00 63.06 C ANISOU 2915 CB ILE B 158 9665 7698 6597 228 -720 -904 C ATOM 2916 CG1 ILE B 158 54.516 -1.323 -20.189 1.00 63.16 C ANISOU 2916 CG1 ILE B 158 9685 7597 6718 120 -700 -878 C ATOM 2917 CG2 ILE B 158 53.559 -1.252 -22.554 1.00 64.35 C ANISOU 2917 CG2 ILE B 158 9781 7903 6766 271 -789 -1038 C ATOM 2918 CD1 ILE B 158 53.175 -1.295 -19.493 1.00 72.30 C ANISOU 2918 CD1 ILE B 158 10808 8723 7938 50 -693 -905 C ATOM 2919 N ALA B 159 56.292 0.922 -23.908 1.00 64.56 N ANISOU 2919 N ALA B 159 9933 8063 6534 429 -670 -839 N ATOM 2920 CA ALA B 159 56.430 1.442 -25.270 1.00 65.12 C ANISOU 2920 CA ALA B 159 10045 8222 6474 532 -665 -856 C ATOM 2921 C ALA B 159 57.557 0.746 -26.063 1.00 69.68 C ANISOU 2921 C ALA B 159 10639 8814 7023 582 -632 -888 C ATOM 2922 O ALA B 159 57.395 0.477 -27.256 1.00 70.85 O ANISOU 2922 O ALA B 159 10816 9021 7083 668 -656 -962 O ATOM 2923 CB ALA B 159 56.714 2.932 -25.213 1.00 65.52 C ANISOU 2923 CB ALA B 159 10143 8302 6449 546 -607 -742 C ATOM 2924 N VAL B 160 58.680 0.457 -25.394 1.00 65.61 N ANISOU 2924 N VAL B 160 10105 8243 6580 534 -581 -838 N ATOM 2925 CA VAL B 160 59.883 -0.076 -26.016 1.00 66.37 C ANISOU 2925 CA VAL B 160 10202 8349 6667 577 -534 -860 C ATOM 2926 C VAL B 160 59.977 -1.606 -25.858 1.00 72.27 C ANISOU 2926 C VAL B 160 10913 9039 7508 564 -588 -957 C ATOM 2927 O VAL B 160 60.344 -2.290 -26.825 1.00 73.35 O ANISOU 2927 O VAL B 160 11056 9206 7608 633 -587 -1037 O ATOM 2928 CB VAL B 160 61.121 0.614 -25.376 1.00 69.75 C ANISOU 2928 CB VAL B 160 10619 8748 7134 538 -452 -754 C ATOM 2929 CG1 VAL B 160 62.426 0.073 -25.938 1.00 70.30 C ANISOU 2929 CG1 VAL B 160 10668 8824 7221 578 -393 -782 C ATOM 2930 CG2 VAL B 160 61.059 2.118 -25.578 1.00 69.49 C ANISOU 2930 CG2 VAL B 160 10629 8762 7012 548 -394 -660 C ATOM 2931 N CYS B 161 59.667 -2.132 -24.653 1.00 68.22 N ANISOU 2931 N CYS B 161 10373 8437 7110 480 -630 -948 N ATOM 2932 CA CYS B 161 59.862 -3.536 -24.311 1.00 68.09 C ANISOU 2932 CA CYS B 161 10337 8341 7194 456 -677 -1018 C ATOM 2933 C CYS B 161 58.610 -4.384 -24.599 1.00 73.29 C ANISOU 2933 C CYS B 161 10985 8988 7874 450 -753 -1126 C ATOM 2934 O CYS B 161 58.763 -5.569 -24.903 1.00 73.84 O ANISOU 2934 O CYS B 161 11047 9018 7991 467 -792 -1215 O ATOM 2935 CB CYS B 161 60.261 -3.653 -22.851 1.00 67.40 C ANISOU 2935 CB CYS B 161 10249 8151 7208 371 -679 -945 C ATOM 2936 SG CYS B 161 61.802 -2.788 -22.457 1.00 70.72 S ANISOU 2936 SG CYS B 161 10663 8571 7636 376 -612 -841 S ATOM 2937 N HIS B 162 57.399 -3.813 -24.510 1.00 69.91 N ANISOU 2937 N HIS B 162 10550 8587 7424 427 -776 -1126 N ATOM 2938 CA HIS B 162 56.172 -4.574 -24.787 1.00 70.46 C ANISOU 2938 CA HIS B 162 10591 8645 7536 416 -850 -1239 C ATOM 2939 C HIS B 162 55.360 -3.831 -25.869 1.00 74.33 C ANISOU 2939 C HIS B 162 11083 9240 7919 496 -884 -1285 C ATOM 2940 O HIS B 162 54.338 -3.215 -25.550 1.00 74.09 O ANISOU 2940 O HIS B 162 11029 9224 7899 467 -903 -1276 O ATOM 2941 CB HIS B 162 55.370 -4.774 -23.488 1.00 71.08 C ANISOU 2941 CB HIS B 162 10647 8636 7725 302 -853 -1214 C ATOM 2942 CG HIS B 162 56.159 -5.435 -22.396 1.00 74.36 C ANISOU 2942 CG HIS B 162 11088 8940 8225 233 -829 -1160 C ATOM 2943 ND1 HIS B 162 56.188 -6.811 -22.256 1.00 76.81 N ANISOU 2943 ND1 HIS B 162 11400 9162 8624 205 -867 -1232 N ATOM 2944 CD2 HIS B 162 56.937 -4.882 -21.436 1.00 75.33 C ANISOU 2944 CD2 HIS B 162 11244 9025 8354 197 -782 -1045 C ATOM 2945 CE1 HIS B 162 56.973 -7.049 -21.218 1.00 75.83 C ANISOU 2945 CE1 HIS B 162 11316 8948 8549 157 -844 -1156 C ATOM 2946 NE2 HIS B 162 57.448 -5.918 -20.694 1.00 75.27 N ANISOU 2946 NE2 HIS B 162 11263 8905 8432 152 -797 -1045 N ATOM 2947 N PRO B 163 55.837 -3.818 -27.149 1.00 70.73 N ANISOU 2947 N PRO B 163 10665 8858 7351 603 -888 -1331 N ATOM 2948 CA PRO B 163 55.176 -3.001 -28.179 1.00 70.86 C ANISOU 2948 CA PRO B 163 10713 8970 7239 692 -923 -1359 C ATOM 2949 C PRO B 163 53.739 -3.430 -28.492 1.00 75.03 C ANISOU 2949 C PRO B 163 11197 9504 7808 700 -1035 -1483 C ATOM 2950 O PRO B 163 52.939 -2.576 -28.870 1.00 75.31 O ANISOU 2950 O PRO B 163 11240 9598 7777 746 -1076 -1488 O ATOM 2951 CB PRO B 163 56.059 -3.218 -29.408 1.00 73.25 C ANISOU 2951 CB PRO B 163 11078 9329 7425 797 -899 -1395 C ATOM 2952 CG PRO B 163 57.385 -3.568 -28.851 1.00 76.98 C ANISOU 2952 CG PRO B 163 11542 9752 7956 757 -815 -1333 C ATOM 2953 CD PRO B 163 57.058 -4.442 -27.697 1.00 72.21 C ANISOU 2953 CD PRO B 163 10878 9045 7513 654 -853 -1350 C ATOM 2954 N VAL B 164 53.404 -4.718 -28.337 1.00 70.81 N ANISOU 2954 N VAL B 164 10613 8905 7387 657 -1089 -1587 N ATOM 2955 CA VAL B 164 52.045 -5.184 -28.623 1.00 71.14 C ANISOU 2955 CA VAL B 164 10594 8943 7492 655 -1197 -1719 C ATOM 2956 C VAL B 164 51.112 -4.731 -27.459 1.00 73.68 C ANISOU 2956 C VAL B 164 10846 9224 7927 549 -1180 -1675 C ATOM 2957 O VAL B 164 49.954 -4.379 -27.710 1.00 73.58 O ANISOU 2957 O VAL B 164 10781 9245 7930 567 -1249 -1744 O ATOM 2958 CB VAL B 164 52.000 -6.714 -28.863 1.00 75.88 C ANISOU 2958 CB VAL B 164 11166 9477 8186 638 -1255 -1848 C ATOM 2959 CG1 VAL B 164 50.585 -7.179 -29.177 1.00 76.78 C ANISOU 2959 CG1 VAL B 164 11204 9584 8383 630 -1369 -1996 C ATOM 2960 CG2 VAL B 164 52.948 -7.117 -29.992 1.00 76.27 C ANISOU 2960 CG2 VAL B 164 11289 9570 8119 749 -1261 -1893 C ATOM 2961 N LYS B 165 51.641 -4.673 -26.212 1.00 68.82 N ANISOU 2961 N LYS B 165 10233 8538 7379 449 -1089 -1563 N ATOM 2962 CA LYS B 165 50.877 -4.202 -25.054 1.00 68.00 C ANISOU 2962 CA LYS B 165 10082 8392 7364 351 -1051 -1510 C ATOM 2963 C LYS B 165 50.746 -2.697 -25.097 1.00 72.93 C ANISOU 2963 C LYS B 165 10728 9092 7889 397 -1028 -1425 C ATOM 2964 O LYS B 165 49.751 -2.162 -24.609 1.00 73.36 O ANISOU 2964 O LYS B 165 10730 9149 7994 361 -1032 -1429 O ATOM 2965 CB LYS B 165 51.519 -4.636 -23.721 1.00 69.32 C ANISOU 2965 CB LYS B 165 10272 8453 7615 240 -970 -1418 C ATOM 2966 CG LYS B 165 50.653 -4.363 -22.475 1.00 80.46 C ANISOU 2966 CG LYS B 165 11644 9806 9122 130 -921 -1378 C ATOM 2967 CD LYS B 165 49.343 -5.170 -22.501 1.00 92.31 C ANISOU 2967 CD LYS B 165 13056 11268 10751 74 -965 -1510 C ATOM 2968 CE LYS B 165 48.462 -4.944 -21.303 1.00103.54 C ANISOU 2968 CE LYS B 165 14435 12631 12272 -39 -896 -1480 C ATOM 2969 NZ LYS B 165 47.243 -5.796 -21.360 1.00113.01 N ANISOU 2969 NZ LYS B 165 15536 13787 13617 -102 -926 -1616 N ATOM 2970 N ALA B 166 51.750 -2.006 -25.691 1.00 69.18 N ANISOU 2970 N ALA B 166 10331 8676 7278 478 -997 -1349 N ATOM 2971 CA ALA B 166 51.770 -0.547 -25.827 1.00 68.20 C ANISOU 2971 CA ALA B 166 10248 8617 7048 528 -970 -1259 C ATOM 2972 C ALA B 166 50.520 -0.048 -26.565 1.00 73.58 C ANISOU 2972 C ALA B 166 10902 9363 7692 602 -1062 -1344 C ATOM 2973 O ALA B 166 49.976 0.993 -26.206 1.00 72.59 O ANISOU 2973 O ALA B 166 10769 9257 7553 603 -1056 -1295 O ATOM 2974 CB ALA B 166 53.025 -0.111 -26.556 1.00 68.59 C ANISOU 2974 CB ALA B 166 10383 8712 6965 603 -920 -1190 C ATOM 2975 N LEU B 167 50.037 -0.827 -27.548 1.00 72.64 N ANISOU 2975 N LEU B 167 10765 9270 7567 665 -1159 -1482 N ATOM 2976 CA LEU B 167 48.819 -0.543 -28.315 1.00 74.14 C ANISOU 2976 CA LEU B 167 10919 9513 7736 745 -1277 -1593 C ATOM 2977 C LEU B 167 47.577 -0.557 -27.419 1.00 80.37 C ANISOU 2977 C LEU B 167 11587 10264 8686 659 -1298 -1642 C ATOM 2978 O LEU B 167 46.650 0.228 -27.619 1.00 80.51 O ANISOU 2978 O LEU B 167 11571 10325 8695 710 -1360 -1676 O ATOM 2979 CB LEU B 167 48.655 -1.595 -29.438 1.00 75.10 C ANISOU 2979 CB LEU B 167 11043 9653 7839 816 -1381 -1743 C ATOM 2980 CG LEU B 167 49.763 -1.690 -30.478 1.00 79.60 C ANISOU 2980 CG LEU B 167 11733 10267 8245 915 -1362 -1724 C ATOM 2981 CD1 LEU B 167 49.678 -2.985 -31.237 1.00 80.94 C ANISOU 2981 CD1 LEU B 167 11890 10425 8439 950 -1445 -1873 C ATOM 2982 CD2 LEU B 167 49.762 -0.493 -31.405 1.00 82.05 C ANISOU 2982 CD2 LEU B 167 12147 10660 8366 1044 -1387 -1681 C ATOM 2983 N ASP B 168 47.580 -1.449 -26.439 1.00 78.04 N ANISOU 2983 N ASP B 168 11232 9884 8537 531 -1241 -1647 N ATOM 2984 CA ASP B 168 46.472 -1.626 -25.512 1.00 78.63 C ANISOU 2984 CA ASP B 168 11193 9907 8777 429 -1230 -1694 C ATOM 2985 C ASP B 168 46.659 -0.918 -24.180 1.00 81.27 C ANISOU 2985 C ASP B 168 11539 10200 9140 339 -1110 -1557 C ATOM 2986 O ASP B 168 45.840 -1.054 -23.295 1.00 81.44 O ANISOU 2986 O ASP B 168 11480 10172 9291 246 -1071 -1581 O ATOM 2987 CB ASP B 168 46.255 -3.122 -25.215 1.00 81.63 C ANISOU 2987 CB ASP B 168 11510 10200 9306 334 -1233 -1788 C ATOM 2988 CG ASP B 168 46.390 -4.022 -26.448 1.00 95.92 C ANISOU 2988 CG ASP B 168 13332 12031 11083 415 -1340 -1913 C ATOM 2989 OD1 ASP B 168 45.567 -3.924 -27.368 1.00 97.87 O ANISOU 2989 OD1 ASP B 168 13533 12335 11319 499 -1459 -2036 O ATOM 2990 OD2 ASP B 168 47.297 -4.869 -26.480 1.00101.05 O ANISOU 2990 OD2 ASP B 168 14036 12635 11724 396 -1312 -1897 O ATOM 2991 N PHE B 169 47.731 -0.162 -24.043 1.00 76.51 N ANISOU 2991 N PHE B 169 11036 9615 8419 366 -1049 -1420 N ATOM 2992 CA PHE B 169 48.086 0.501 -22.785 1.00 75.48 C ANISOU 2992 CA PHE B 169 10936 9441 8303 288 -944 -1288 C ATOM 2993 C PHE B 169 48.344 2.015 -22.941 1.00 79.80 C ANISOU 2993 C PHE B 169 11543 10049 8728 360 -929 -1189 C ATOM 2994 O PHE B 169 48.174 2.758 -21.966 1.00 78.55 O ANISOU 2994 O PHE B 169 11387 9867 8594 309 -868 -1113 O ATOM 2995 CB PHE B 169 49.364 -0.157 -22.211 1.00 76.63 C ANISOU 2995 CB PHE B 169 11149 9518 8450 227 -875 -1205 C ATOM 2996 CG PHE B 169 49.880 0.397 -20.900 1.00 77.75 C ANISOU 2996 CG PHE B 169 11338 9603 8601 150 -781 -1073 C ATOM 2997 CD1 PHE B 169 49.397 -0.079 -19.686 1.00 80.79 C ANISOU 2997 CD1 PHE B 169 11701 9901 9096 36 -726 -1067 C ATOM 2998 CD2 PHE B 169 50.875 1.370 -20.879 1.00 79.93 C ANISOU 2998 CD2 PHE B 169 11689 9907 8775 190 -746 -958 C ATOM 2999 CE1 PHE B 169 49.872 0.437 -18.471 1.00 80.85 C ANISOU 2999 CE1 PHE B 169 11769 9854 9096 -26 -648 -950 C ATOM 3000 CE2 PHE B 169 51.338 1.897 -19.664 1.00 81.86 C ANISOU 3000 CE2 PHE B 169 11977 10095 9030 123 -676 -846 C ATOM 3001 CZ PHE B 169 50.844 1.417 -18.469 1.00 79.50 C ANISOU 3001 CZ PHE B 169 11666 9713 8826 21 -632 -844 C ATOM 3002 N ARG B 170 48.824 2.467 -24.111 1.00 77.18 N ANISOU 3002 N ARG B 170 11276 9787 8261 475 -976 -1183 N ATOM 3003 CA ARG B 170 49.175 3.885 -24.270 1.00 76.55 C ANISOU 3003 CA ARG B 170 11271 9751 8062 537 -952 -1078 C ATOM 3004 C ARG B 170 48.029 4.676 -24.980 1.00 82.13 C ANISOU 3004 C ARG B 170 11957 10521 8726 636 -1046 -1145 C ATOM 3005 O ARG B 170 48.292 5.583 -25.782 1.00 82.51 O ANISOU 3005 O ARG B 170 12092 10621 8638 738 -1069 -1099 O ATOM 3006 CB ARG B 170 50.499 4.036 -25.046 1.00 74.96 C ANISOU 3006 CB ARG B 170 11172 9578 7732 597 -919 -1008 C ATOM 3007 CG ARG B 170 51.699 3.312 -24.411 1.00 76.99 C ANISOU 3007 CG ARG B 170 11443 9775 8035 517 -840 -950 C ATOM 3008 CD ARG B 170 52.987 3.675 -25.120 1.00 79.16 C ANISOU 3008 CD ARG B 170 11802 10081 8196 575 -791 -878 C ATOM 3009 NE ARG B 170 53.359 5.068 -24.867 1.00 85.20 N ANISOU 3009 NE ARG B 170 12623 10855 8894 583 -735 -758 N ATOM 3010 CZ ARG B 170 54.249 5.750 -25.578 1.00102.80 C ANISOU 3010 CZ ARG B 170 14931 13118 11011 640 -685 -688 C ATOM 3011 NH1 ARG B 170 54.802 5.210 -26.656 1.00 93.21 N ANISOU 3011 NH1 ARG B 170 13752 11940 9723 705 -682 -731 N ATOM 3012 NH2 ARG B 170 54.527 7.008 -25.268 1.00 92.30 N ANISOU 3012 NH2 ARG B 170 13648 11782 9638 636 -635 -580 N ATOM 3013 N THR B 171 46.767 4.362 -24.622 1.00 78.93 N ANISOU 3013 N THR B 171 11438 10105 8447 604 -1094 -1249 N ATOM 3014 CA THR B 171 45.568 5.014 -25.159 1.00 79.37 C ANISOU 3014 CA THR B 171 11445 10211 8500 693 -1196 -1334 C ATOM 3015 C THR B 171 45.149 6.178 -24.242 1.00 83.04 C ANISOU 3015 C THR B 171 11897 10665 8991 668 -1144 -1260 C ATOM 3016 O THR B 171 45.466 6.129 -23.045 1.00 82.05 O ANISOU 3016 O THR B 171 11761 10481 8932 556 -1035 -1185 O ATOM 3017 CB THR B 171 44.418 3.994 -25.317 1.00 86.11 C ANISOU 3017 CB THR B 171 12160 11057 9500 671 -1279 -1509 C ATOM 3018 OG1 THR B 171 43.981 3.543 -24.037 1.00 83.14 O ANISOU 3018 OG1 THR B 171 11687 10613 9288 530 -1191 -1513 O ATOM 3019 CG2 THR B 171 44.793 2.815 -26.188 1.00 86.71 C ANISOU 3019 CG2 THR B 171 12251 11138 9558 694 -1337 -1592 C ATOM 3020 N PRO B 172 44.402 7.208 -24.746 1.00 79.86 N ANISOU 3020 N PRO B 172 11496 10309 8536 776 -1226 -1287 N ATOM 3021 CA PRO B 172 43.969 8.302 -23.850 1.00 78.92 C ANISOU 3021 CA PRO B 172 11361 10174 8450 756 -1178 -1226 C ATOM 3022 C PRO B 172 43.132 7.780 -22.670 1.00 81.66 C ANISOU 3022 C PRO B 172 11568 10474 8984 636 -1117 -1288 C ATOM 3023 O PRO B 172 43.296 8.273 -21.559 1.00 80.63 O ANISOU 3023 O PRO B 172 11452 10302 8883 561 -1013 -1201 O ATOM 3024 CB PRO B 172 43.136 9.210 -24.763 1.00 81.89 C ANISOU 3024 CB PRO B 172 11746 10607 8762 906 -1309 -1286 C ATOM 3025 CG PRO B 172 42.811 8.384 -25.960 1.00 87.57 C ANISOU 3025 CG PRO B 172 12444 11367 9461 985 -1436 -1416 C ATOM 3026 CD PRO B 172 43.946 7.442 -26.133 1.00 82.54 C ANISOU 3026 CD PRO B 172 11869 10713 8779 928 -1372 -1371 C ATOM 3027 N LEU B 173 42.290 6.749 -22.902 1.00 78.48 N ANISOU 3027 N LEU B 173 11040 10071 8707 611 -1172 -1437 N ATOM 3028 CA LEU B 173 41.465 6.096 -21.879 1.00 78.10 C ANISOU 3028 CA LEU B 173 10855 9971 8847 487 -1101 -1508 C ATOM 3029 C LEU B 173 42.332 5.521 -20.758 1.00 79.81 C ANISOU 3029 C LEU B 173 11128 10111 9085 347 -955 -1400 C ATOM 3030 O LEU B 173 42.092 5.836 -19.595 1.00 78.96 O ANISOU 3030 O LEU B 173 11003 9959 9038 264 -849 -1353 O ATOM 3031 CB LEU B 173 40.612 4.966 -22.510 1.00 79.37 C ANISOU 3031 CB LEU B 173 10885 10139 9133 484 -1193 -1686 C ATOM 3032 CG LEU B 173 39.713 4.149 -21.560 1.00 84.31 C ANISOU 3032 CG LEU B 173 11359 10702 9971 344 -1112 -1775 C ATOM 3033 CD1 LEU B 173 38.545 4.982 -21.035 1.00 85.07 C ANISOU 3033 CD1 LEU B 173 11339 10814 10171 352 -1097 -1832 C ATOM 3034 CD2 LEU B 173 39.165 2.929 -22.255 1.00 87.76 C ANISOU 3034 CD2 LEU B 173 11691 11133 10521 332 -1201 -1937 C ATOM 3035 N LYS B 174 43.334 4.679 -21.118 1.00 75.50 N ANISOU 3035 N LYS B 174 10655 9547 8485 328 -953 -1367 N ATOM 3036 CA LYS B 174 44.246 4.004 -20.183 1.00 74.31 C ANISOU 3036 CA LYS B 174 10566 9318 8349 212 -842 -1275 C ATOM 3037 C LYS B 174 44.995 5.016 -19.304 1.00 77.63 C ANISOU 3037 C LYS B 174 11088 9717 8691 192 -755 -1121 C ATOM 3038 O LYS B 174 45.068 4.815 -18.089 1.00 76.99 O ANISOU 3038 O LYS B 174 11020 9566 8667 86 -655 -1069 O ATOM 3039 CB LYS B 174 45.249 3.130 -20.937 1.00 76.00 C ANISOU 3039 CB LYS B 174 10844 9531 8502 234 -879 -1272 C ATOM 3040 N ALA B 175 45.505 6.119 -19.906 1.00 73.30 N ANISOU 3040 N ALA B 175 10616 9223 8010 292 -793 -1050 N ATOM 3041 CA ALA B 175 46.195 7.187 -19.175 1.00 72.00 C ANISOU 3041 CA ALA B 175 10544 9039 7775 282 -725 -912 C ATOM 3042 C ALA B 175 45.282 7.789 -18.097 1.00 75.53 C ANISOU 3042 C ALA B 175 10942 9458 8297 234 -667 -916 C ATOM 3043 O ALA B 175 45.705 7.929 -16.942 1.00 74.81 O ANISOU 3043 O ALA B 175 10902 9306 8215 153 -576 -832 O ATOM 3044 CB ALA B 175 46.654 8.270 -20.138 1.00 72.65 C ANISOU 3044 CB ALA B 175 10704 9181 7718 401 -780 -858 C ATOM 3045 N LYS B 176 44.009 8.094 -18.480 1.00 71.14 N ANISOU 3045 N LYS B 176 10283 8946 7800 288 -724 -1024 N ATOM 3046 CA LYS B 176 42.968 8.646 -17.613 1.00 69.88 C ANISOU 3046 CA LYS B 176 10051 8773 7729 257 -673 -1058 C ATOM 3047 C LYS B 176 42.668 7.689 -16.459 1.00 71.01 C ANISOU 3047 C LYS B 176 10146 8841 7993 114 -560 -1079 C ATOM 3048 O LYS B 176 42.649 8.131 -15.313 1.00 70.20 O ANISOU 3048 O LYS B 176 10080 8693 7901 52 -459 -1016 O ATOM 3049 CB LYS B 176 41.690 8.934 -18.417 1.00 73.41 C ANISOU 3049 CB LYS B 176 10376 9283 8236 350 -777 -1196 C ATOM 3050 N ILE B 177 42.485 6.378 -16.755 1.00 66.46 N ANISOU 3050 N ILE B 177 9507 8246 7500 61 -573 -1163 N ATOM 3051 CA ILE B 177 42.217 5.327 -15.756 1.00 65.98 C ANISOU 3051 CA ILE B 177 9415 8101 7554 -80 -463 -1183 C ATOM 3052 C ILE B 177 43.384 5.260 -14.749 1.00 68.76 C ANISOU 3052 C ILE B 177 9917 8379 7828 -151 -373 -1037 C ATOM 3053 O ILE B 177 43.138 5.239 -13.541 1.00 67.82 O ANISOU 3053 O ILE B 177 9823 8194 7750 -241 -259 -1002 O ATOM 3054 CB ILE B 177 41.972 3.946 -16.436 1.00 69.20 C ANISOU 3054 CB ILE B 177 9745 8496 8051 -110 -514 -1294 C ATOM 3055 CG1 ILE B 177 40.652 3.983 -17.248 1.00 70.57 C ANISOU 3055 CG1 ILE B 177 9753 8731 8331 -52 -604 -1460 C ATOM 3056 CG2 ILE B 177 41.939 2.811 -15.393 1.00 69.75 C ANISOU 3056 CG2 ILE B 177 9825 8460 8219 -261 -394 -1288 C ATOM 3057 CD1 ILE B 177 40.310 2.735 -18.060 1.00 76.90 C ANISOU 3057 CD1 ILE B 177 10466 9526 9225 -65 -681 -1591 C ATOM 3058 N ILE B 178 44.637 5.269 -15.249 1.00 64.82 N ANISOU 3058 N ILE B 178 9519 7890 7218 -104 -426 -956 N ATOM 3059 CA ILE B 178 45.848 5.226 -14.428 1.00 63.82 C ANISOU 3059 CA ILE B 178 9527 7699 7024 -154 -371 -828 C ATOM 3060 C ILE B 178 45.836 6.427 -13.444 1.00 69.73 C ANISOU 3060 C ILE B 178 10335 8431 7727 -160 -307 -743 C ATOM 3061 O ILE B 178 46.062 6.214 -12.252 1.00 69.22 O ANISOU 3061 O ILE B 178 10344 8287 7670 -244 -222 -685 O ATOM 3062 CB ILE B 178 47.109 5.202 -15.333 1.00 65.69 C ANISOU 3062 CB ILE B 178 9829 7968 7162 -84 -445 -776 C ATOM 3063 CG1 ILE B 178 47.196 3.817 -16.042 1.00 65.68 C ANISOU 3063 CG1 ILE B 178 9786 7957 7212 -96 -490 -858 C ATOM 3064 CG2 ILE B 178 48.379 5.463 -14.514 1.00 65.37 C ANISOU 3064 CG2 ILE B 178 9911 7869 7055 -116 -404 -646 C ATOM 3065 CD1 ILE B 178 48.255 3.640 -17.107 1.00 66.20 C ANISOU 3065 CD1 ILE B 178 9894 8065 7195 -20 -559 -840 C ATOM 3066 N ASN B 179 45.485 7.643 -13.914 1.00 68.12 N ANISOU 3066 N ASN B 179 10108 8296 7479 -71 -349 -745 N ATOM 3067 CA ASN B 179 45.395 8.820 -13.041 1.00 68.66 C ANISOU 3067 CA ASN B 179 10228 8349 7509 -69 -296 -678 C ATOM 3068 C ASN B 179 44.202 8.707 -12.088 1.00 75.56 C ANISOU 3068 C ASN B 179 11038 9190 8483 -138 -201 -739 C ATOM 3069 O ASN B 179 44.307 9.200 -10.969 1.00 75.34 O ANISOU 3069 O ASN B 179 11085 9111 8429 -181 -120 -675 O ATOM 3070 CB ASN B 179 45.299 10.115 -13.841 1.00 71.17 C ANISOU 3070 CB ASN B 179 10544 8739 7759 49 -370 -667 C ATOM 3071 CG ASN B 179 46.592 10.507 -14.518 1.00 94.17 C ANISOU 3071 CG ASN B 179 13550 11669 10561 104 -424 -577 C ATOM 3072 OD1 ASN B 179 46.726 10.457 -15.750 1.00 80.24 O ANISOU 3072 OD1 ASN B 179 11768 9964 8757 181 -502 -606 O ATOM 3073 ND2 ASN B 179 47.590 10.883 -13.716 1.00 88.14 N ANISOU 3073 ND2 ASN B 179 12890 10850 9748 64 -381 -468 N ATOM 3074 N ILE B 180 43.091 8.035 -12.499 1.00 74.60 N ANISOU 3074 N ILE B 180 10777 9091 8475 -152 -205 -867 N ATOM 3075 CA ILE B 180 41.931 7.822 -11.616 1.00 75.95 C ANISOU 3075 CA ILE B 180 10869 9227 8763 -231 -93 -937 C ATOM 3076 C ILE B 180 42.362 6.918 -10.447 1.00 81.58 C ANISOU 3076 C ILE B 180 11679 9834 9484 -360 25 -875 C ATOM 3077 O ILE B 180 41.908 7.122 -9.326 1.00 81.33 O ANISOU 3077 O ILE B 180 11676 9752 9473 -425 147 -859 O ATOM 3078 CB ILE B 180 40.706 7.241 -12.364 1.00 80.09 C ANISOU 3078 CB ILE B 180 11209 9793 9428 -224 -131 -1098 C ATOM 3079 N CYS B 181 43.281 5.957 -10.711 1.00 79.49 N ANISOU 3079 N CYS B 181 11479 9532 9189 -388 -13 -838 N ATOM 3080 CA CYS B 181 43.840 5.051 -9.703 1.00 80.07 C ANISOU 3080 CA CYS B 181 11669 9498 9255 -493 71 -772 C ATOM 3081 C CYS B 181 44.788 5.824 -8.785 1.00 84.28 C ANISOU 3081 C CYS B 181 12364 9991 9668 -487 95 -641 C ATOM 3082 O CYS B 181 44.760 5.608 -7.571 1.00 84.48 O ANISOU 3082 O CYS B 181 12486 9930 9682 -566 199 -594 O ATOM 3083 CB CYS B 181 44.549 3.867 -10.358 1.00 80.44 C ANISOU 3083 CB CYS B 181 11730 9522 9312 -505 3 -781 C ATOM 3084 SG CYS B 181 43.465 2.794 -11.338 1.00 85.66 S ANISOU 3084 SG CYS B 181 12214 10210 10124 -526 -29 -944 S ATOM 3085 N ILE B 182 45.615 6.737 -9.360 1.00 80.23 N ANISOU 3085 N ILE B 182 11886 9534 9063 -393 0 -583 N ATOM 3086 CA ILE B 182 46.568 7.565 -8.605 1.00 79.42 C ANISOU 3086 CA ILE B 182 11923 9397 8858 -379 2 -468 C ATOM 3087 C ILE B 182 45.768 8.519 -7.692 1.00 85.43 C ANISOU 3087 C ILE B 182 12697 10149 9614 -389 88 -466 C ATOM 3088 O ILE B 182 46.152 8.731 -6.538 1.00 84.38 O ANISOU 3088 O ILE B 182 12692 9944 9426 -430 146 -395 O ATOM 3089 CB ILE B 182 47.537 8.320 -9.560 1.00 81.22 C ANISOU 3089 CB ILE B 182 12161 9687 9011 -283 -108 -421 C ATOM 3090 CG1 ILE B 182 48.419 7.307 -10.345 1.00 80.86 C ANISOU 3090 CG1 ILE B 182 12115 9642 8967 -278 -175 -422 C ATOM 3091 CG2 ILE B 182 48.420 9.302 -8.778 1.00 81.38 C ANISOU 3091 CG2 ILE B 182 12305 9670 8945 -272 -108 -316 C ATOM 3092 CD1 ILE B 182 49.307 7.883 -11.455 1.00 85.18 C ANISOU 3092 CD1 ILE B 182 12658 10255 9451 -188 -264 -391 C ATOM 3093 N TRP B 183 44.625 9.022 -8.197 1.00 84.82 N ANISOU 3093 N TRP B 183 12487 10141 9598 -348 94 -555 N ATOM 3094 CA TRP B 183 43.688 9.873 -7.465 1.00 86.42 C ANISOU 3094 CA TRP B 183 12670 10346 9821 -349 178 -580 C ATOM 3095 C TRP B 183 43.204 9.134 -6.208 1.00 88.91 C ANISOU 3095 C TRP B 183 13034 10573 10177 -465 329 -586 C ATOM 3096 O TRP B 183 43.285 9.692 -5.120 1.00 88.47 O ANISOU 3096 O TRP B 183 13087 10466 10060 -486 405 -530 O ATOM 3097 CB TRP B 183 42.511 10.268 -8.392 1.00 87.16 C ANISOU 3097 CB TRP B 183 12586 10528 10002 -281 139 -699 C ATOM 3098 CG TRP B 183 41.320 10.903 -7.727 1.00 89.99 C ANISOU 3098 CG TRP B 183 12876 10891 10424 -287 235 -762 C ATOM 3099 CD1 TRP B 183 41.216 12.192 -7.296 1.00 93.00 C ANISOU 3099 CD1 TRP B 183 13301 11283 10752 -228 246 -731 C ATOM 3100 CD2 TRP B 183 39.999 10.338 -7.618 1.00 91.49 C ANISOU 3100 CD2 TRP B 183 12916 11086 10760 -339 321 -887 C ATOM 3101 NE1 TRP B 183 39.948 12.430 -6.812 1.00 93.99 N ANISOU 3101 NE1 TRP B 183 13324 11416 10973 -243 344 -823 N ATOM 3102 CE2 TRP B 183 39.174 11.314 -7.017 1.00 96.40 C ANISOU 3102 CE2 TRP B 183 13500 11721 11408 -312 394 -922 C ATOM 3103 CE3 TRP B 183 39.440 9.084 -7.937 1.00 93.62 C ANISOU 3103 CE3 TRP B 183 13076 11345 11152 -411 349 -976 C ATOM 3104 CZ2 TRP B 183 37.823 11.075 -6.715 1.00 97.13 C ANISOU 3104 CZ2 TRP B 183 13440 11817 11648 -356 503 -1046 C ATOM 3105 CZ3 TRP B 183 38.100 8.854 -7.648 1.00 96.52 C ANISOU 3105 CZ3 TRP B 183 13292 11713 11670 -461 452 -1097 C ATOM 3106 CH2 TRP B 183 37.310 9.838 -7.038 1.00 97.82 C ANISOU 3106 CH2 TRP B 183 13413 11892 11861 -434 533 -1132 C ATOM 3107 N LEU B 184 42.796 7.854 -6.362 1.00 84.53 N ANISOU 3107 N LEU B 184 12416 9988 9712 -540 369 -646 N ATOM 3108 CA LEU B 184 42.308 6.989 -5.287 1.00 84.85 C ANISOU 3108 CA LEU B 184 12506 9936 9799 -660 522 -653 C ATOM 3109 C LEU B 184 43.394 6.686 -4.244 1.00 89.17 C ANISOU 3109 C LEU B 184 13272 10379 10230 -707 550 -529 C ATOM 3110 O LEU B 184 43.135 6.840 -3.046 1.00 88.82 O ANISOU 3110 O LEU B 184 13335 10267 10147 -761 675 -495 O ATOM 3111 CB LEU B 184 41.783 5.667 -5.859 1.00 85.38 C ANISOU 3111 CB LEU B 184 12460 9989 9992 -725 534 -741 C ATOM 3112 CG LEU B 184 40.508 5.724 -6.687 1.00 90.60 C ANISOU 3112 CG LEU B 184 12897 10729 10799 -703 526 -887 C ATOM 3113 CD1 LEU B 184 40.321 4.449 -7.477 1.00 91.24 C ANISOU 3113 CD1 LEU B 184 12881 10800 10984 -746 482 -967 C ATOM 3114 CD2 LEU B 184 39.289 6.034 -5.822 1.00 93.66 C ANISOU 3114 CD2 LEU B 184 13217 11097 11271 -762 691 -948 C ATOM 3115 N LEU B 185 44.597 6.247 -4.690 1.00 86.04 N ANISOU 3115 N LEU B 185 12945 9969 9777 -681 434 -469 N ATOM 3116 CA LEU B 185 45.721 5.913 -3.800 1.00 86.10 C ANISOU 3116 CA LEU B 185 13153 9878 9684 -710 426 -362 C ATOM 3117 C LEU B 185 46.173 7.126 -2.984 1.00 90.82 C ANISOU 3117 C LEU B 185 13870 10464 10172 -668 425 -286 C ATOM 3118 O LEU B 185 46.550 6.975 -1.823 1.00 90.91 O ANISOU 3118 O LEU B 185 14054 10380 10108 -710 478 -220 O ATOM 3119 CB LEU B 185 46.922 5.363 -4.592 1.00 85.49 C ANISOU 3119 CB LEU B 185 13091 9806 9586 -670 288 -330 C ATOM 3120 CG LEU B 185 46.730 4.035 -5.339 1.00 91.33 C ANISOU 3120 CG LEU B 185 13747 10537 10418 -707 270 -395 C ATOM 3121 CD1 LEU B 185 47.955 3.702 -6.159 1.00 91.01 C ANISOU 3121 CD1 LEU B 185 13716 10515 10347 -649 134 -366 C ATOM 3122 CD2 LEU B 185 46.408 2.877 -4.382 1.00 95.15 C ANISOU 3122 CD2 LEU B 185 14327 10896 10930 -819 382 -387 C ATOM 3123 N SER B 186 46.137 8.324 -3.595 1.00 86.99 N ANISOU 3123 N SER B 186 13307 10070 9675 -582 360 -297 N ATOM 3124 CA SER B 186 46.534 9.558 -2.937 1.00 86.13 C ANISOU 3124 CA SER B 186 13298 9954 9475 -538 349 -236 C ATOM 3125 C SER B 186 45.435 10.038 -1.984 1.00 90.82 C ANISOU 3125 C SER B 186 13908 10526 10072 -570 491 -268 C ATOM 3126 O SER B 186 45.750 10.423 -0.856 1.00 90.73 O ANISOU 3126 O SER B 186 14056 10447 9972 -584 534 -209 O ATOM 3127 CB SER B 186 46.858 10.630 -3.968 1.00 88.52 C ANISOU 3127 CB SER B 186 13517 10348 9768 -439 236 -236 C ATOM 3128 N SER B 187 44.143 9.975 -2.414 1.00 87.79 N ANISOU 3128 N SER B 187 13361 10199 9795 -580 564 -369 N ATOM 3129 CA SER B 187 42.999 10.398 -1.597 1.00 88.48 C ANISOU 3129 CA SER B 187 13432 10277 9911 -610 714 -418 C ATOM 3130 C SER B 187 42.933 9.618 -0.293 1.00 93.70 C ANISOU 3130 C SER B 187 14248 10823 10531 -713 860 -380 C ATOM 3131 O SER B 187 42.421 10.151 0.691 1.00 93.68 O ANISOU 3131 O SER B 187 14317 10787 10488 -729 981 -380 O ATOM 3132 CB SER B 187 41.685 10.241 -2.351 1.00 92.47 C ANISOU 3132 CB SER B 187 13714 10855 10565 -610 757 -546 C ATOM 3133 OG SER B 187 41.619 11.135 -3.446 1.00100.57 O ANISOU 3133 OG SER B 187 14621 11981 11611 -500 627 -583 O ATOM 3134 N SER B 188 43.489 8.381 -0.262 1.00 91.02 N ANISOU 3134 N SER B 188 13979 10417 10189 -776 848 -345 N ATOM 3135 CA SER B 188 43.533 7.584 0.965 1.00 92.02 C ANISOU 3135 CA SER B 188 14288 10418 10258 -870 974 -295 C ATOM 3136 C SER B 188 44.391 8.308 2.013 1.00 95.35 C ANISOU 3136 C SER B 188 14932 10779 10519 -835 947 -198 C ATOM 3137 O SER B 188 43.959 8.458 3.156 1.00 96.09 O ANISOU 3137 O SER B 188 15155 10806 10548 -875 1087 -182 O ATOM 3138 CB SER B 188 44.063 6.174 0.698 1.00 95.70 C ANISOU 3138 CB SER B 188 14791 10820 10750 -927 936 -273 C ATOM 3139 OG SER B 188 45.452 6.148 0.419 1.00103.37 O ANISOU 3139 OG SER B 188 15852 11780 11643 -869 767 -199 O ATOM 3140 N VAL B 189 45.564 8.830 1.587 1.00 89.78 N ANISOU 3140 N VAL B 189 14261 10098 9753 -756 771 -143 N ATOM 3141 CA VAL B 189 46.494 9.569 2.449 1.00 88.67 C ANISOU 3141 CA VAL B 189 14311 9903 9477 -713 708 -61 C ATOM 3142 C VAL B 189 45.904 10.971 2.722 1.00 90.66 C ANISOU 3142 C VAL B 189 14534 10206 9706 -661 751 -88 C ATOM 3143 O VAL B 189 46.075 11.511 3.816 1.00 90.40 O ANISOU 3143 O VAL B 189 14671 10110 9566 -655 789 -48 O ATOM 3144 CB VAL B 189 47.916 9.644 1.816 1.00 91.55 C ANISOU 3144 CB VAL B 189 14688 10280 9817 -653 511 -8 C ATOM 3145 CG1 VAL B 189 48.913 10.264 2.783 1.00 91.21 C ANISOU 3145 CG1 VAL B 189 14842 10163 9649 -619 438 68 C ATOM 3146 CG2 VAL B 189 48.406 8.262 1.389 1.00 91.40 C ANISOU 3146 CG2 VAL B 189 14666 10223 9841 -693 467 1 C ATOM 3147 N GLY B 190 45.195 11.514 1.730 1.00 85.69 N ANISOU 3147 N GLY B 190 13698 9684 9175 -620 741 -160 N ATOM 3148 CA GLY B 190 44.536 12.817 1.808 1.00 85.03 C ANISOU 3148 CA GLY B 190 13559 9656 9094 -560 772 -200 C ATOM 3149 C GLY B 190 43.456 12.888 2.868 1.00 88.23 C ANISOU 3149 C GLY B 190 14010 10022 9491 -609 966 -241 C ATOM 3150 O GLY B 190 43.438 13.826 3.664 1.00 87.50 O ANISOU 3150 O GLY B 190 14023 9905 9317 -574 998 -224 O ATOM 3151 N ILE B 191 42.558 11.877 2.898 1.00 85.00 N ANISOU 3151 N ILE B 191 13525 9601 9172 -693 1104 -298 N ATOM 3152 CA ILE B 191 41.485 11.759 3.887 1.00 85.85 C ANISOU 3152 CA ILE B 191 13666 9666 9289 -758 1322 -341 C ATOM 3153 C ILE B 191 42.103 11.487 5.265 1.00 89.62 C ANISOU 3153 C ILE B 191 14428 10018 9604 -801 1388 -249 C ATOM 3154 O ILE B 191 41.611 12.008 6.267 1.00 89.86 O ANISOU 3154 O ILE B 191 14562 10012 9568 -808 1523 -256 O ATOM 3155 CB ILE B 191 40.476 10.657 3.484 1.00 89.80 C ANISOU 3155 CB ILE B 191 14004 10175 9943 -848 1444 -425 C ATOM 3156 N SER B 192 43.215 10.708 5.299 1.00 85.60 N ANISOU 3156 N SER B 192 14053 9443 9028 -820 1280 -166 N ATOM 3157 CA SER B 192 43.970 10.383 6.514 1.00 85.88 C ANISOU 3157 CA SER B 192 14374 9352 8902 -845 1295 -75 C ATOM 3158 C SER B 192 44.584 11.637 7.122 1.00 89.07 C ANISOU 3158 C SER B 192 14913 9748 9180 -761 1211 -35 C ATOM 3159 O SER B 192 44.644 11.754 8.343 1.00 89.27 O ANISOU 3159 O SER B 192 15161 9685 9073 -773 1291 3 O ATOM 3160 CB SER B 192 45.065 9.362 6.218 1.00 88.69 C ANISOU 3160 CB SER B 192 14805 9653 9239 -861 1159 -10 C ATOM 3161 OG SER B 192 44.521 8.132 5.771 1.00 98.91 O ANISOU 3161 OG SER B 192 16005 10935 10641 -944 1241 -45 O ATOM 3162 N ALA B 193 45.023 12.579 6.271 1.00 84.18 N ANISOU 3162 N ALA B 193 14169 9216 8600 -675 1053 -46 N ATOM 3163 CA ALA B 193 45.624 13.831 6.715 1.00 83.38 C ANISOU 3163 CA ALA B 193 14171 9106 8402 -596 959 -15 C ATOM 3164 C ALA B 193 44.561 14.804 7.220 1.00 87.62 C ANISOU 3164 C ALA B 193 14687 9671 8933 -573 1096 -75 C ATOM 3165 O ALA B 193 44.857 15.600 8.108 1.00 87.80 O ANISOU 3165 O ALA B 193 14874 9645 8840 -533 1087 -50 O ATOM 3166 CB ALA B 193 46.417 14.462 5.590 1.00 82.71 C ANISOU 3166 CB ALA B 193 13959 9096 8372 -524 763 -5 C ATOM 3167 N ILE B 194 43.326 14.738 6.671 1.00 84.29 N ANISOU 3167 N ILE B 194 14061 9325 8641 -593 1218 -163 N ATOM 3168 CA ILE B 194 42.211 15.603 7.092 1.00 84.94 C ANISOU 3168 CA ILE B 194 14091 9439 8742 -568 1360 -238 C ATOM 3169 C ILE B 194 41.688 15.133 8.461 1.00 90.40 C ANISOU 3169 C ILE B 194 14966 10038 9344 -641 1574 -232 C ATOM 3170 O ILE B 194 41.373 15.965 9.312 1.00 90.88 O ANISOU 3170 O ILE B 194 15131 10076 9324 -607 1656 -248 O ATOM 3171 CB ILE B 194 41.064 15.637 6.029 1.00 88.07 C ANISOU 3171 CB ILE B 194 14195 9944 9324 -561 1407 -345 C ATOM 3172 CG1 ILE B 194 41.568 16.244 4.700 1.00 87.29 C ANISOU 3172 CG1 ILE B 194 13947 9932 9286 -474 1196 -346 C ATOM 3173 CG2 ILE B 194 39.840 16.425 6.549 1.00 89.67 C ANISOU 3173 CG2 ILE B 194 14335 10172 9562 -539 1571 -435 C ATOM 3174 CD1 ILE B 194 40.581 16.209 3.509 1.00 97.77 C ANISOU 3174 CD1 ILE B 194 14999 11364 10784 -452 1194 -449 C ATOM 3175 N VAL B 195 41.613 13.816 8.676 1.00 87.33 N ANISOU 3175 N VAL B 195 14629 9590 8963 -739 1667 -209 N ATOM 3176 CA VAL B 195 41.061 13.289 9.916 1.00 88.99 C ANISOU 3176 CA VAL B 195 15018 9705 9089 -817 1893 -200 C ATOM 3177 C VAL B 195 42.137 13.309 11.048 1.00 92.82 C ANISOU 3177 C VAL B 195 15840 10072 9355 -799 1829 -96 C ATOM 3178 O VAL B 195 41.798 13.668 12.178 1.00 93.13 O ANISOU 3178 O VAL B 195 16061 10052 9273 -801 1970 -93 O ATOM 3179 CB VAL B 195 40.460 11.861 9.744 1.00 93.84 C ANISOU 3179 CB VAL B 195 15565 10287 9804 -938 2039 -218 C ATOM 3180 CG1 VAL B 195 39.274 11.876 8.783 1.00 93.87 C ANISOU 3180 CG1 VAL B 195 15243 10398 10025 -957 2115 -339 C ATOM 3181 CG2 VAL B 195 41.501 10.834 9.300 1.00 92.67 C ANISOU 3181 CG2 VAL B 195 15478 10093 9641 -964 1883 -141 C ATOM 3182 N LEU B 196 43.409 12.947 10.744 1.00 88.46 N ANISOU 3182 N LEU B 196 15368 9488 8756 -775 1617 -19 N ATOM 3183 CA LEU B 196 44.474 12.827 11.752 1.00 88.38 C ANISOU 3183 CA LEU B 196 15665 9361 8556 -755 1530 71 C ATOM 3184 C LEU B 196 45.258 14.121 11.966 1.00 90.65 C ANISOU 3184 C LEU B 196 16026 9658 8759 -650 1358 86 C ATOM 3185 O LEU B 196 45.834 14.282 13.041 1.00 91.48 O ANISOU 3185 O LEU B 196 16397 9665 8695 -625 1327 135 O ATOM 3186 CB LEU B 196 45.472 11.728 11.365 1.00 87.81 C ANISOU 3186 CB LEU B 196 15638 9238 8489 -780 1384 136 C ATOM 3187 CG LEU B 196 44.947 10.288 11.377 1.00 93.40 C ANISOU 3187 CG LEU B 196 16353 9891 9245 -888 1532 143 C ATOM 3188 CD1 LEU B 196 45.874 9.374 10.630 1.00 92.76 C ANISOU 3188 CD1 LEU B 196 16232 9796 9217 -893 1359 184 C ATOM 3189 CD2 LEU B 196 44.690 9.786 12.797 1.00 97.19 C ANISOU 3189 CD2 LEU B 196 17134 10234 9560 -941 1706 191 C ATOM 3190 N GLY B 197 45.304 15.001 10.966 1.00 84.68 N ANISOU 3190 N GLY B 197 15053 9009 8115 -589 1244 45 N ATOM 3191 CA GLY B 197 46.020 16.272 11.061 1.00 83.41 C ANISOU 3191 CA GLY B 197 14939 8856 7898 -497 1084 56 C ATOM 3192 C GLY B 197 45.527 17.152 12.195 1.00 87.82 C ANISOU 3192 C GLY B 197 15659 9373 8337 -463 1193 30 C ATOM 3193 O GLY B 197 44.329 17.185 12.485 1.00 88.20 O ANISOU 3193 O GLY B 197 15661 9444 8409 -493 1404 -28 O ATOM 3194 N GLY B 198 46.454 17.828 12.862 1.00 83.89 N ANISOU 3194 N GLY B 198 15351 8809 7715 -403 1053 68 N ATOM 3195 CA GLY B 198 46.125 18.699 13.981 1.00 84.59 C ANISOU 3195 CA GLY B 198 15621 8848 7671 -360 1132 44 C ATOM 3196 C GLY B 198 47.312 19.381 14.626 1.00 88.15 C ANISOU 3196 C GLY B 198 16276 9220 7995 -292 932 82 C ATOM 3197 O GLY B 198 48.453 19.215 14.184 1.00 86.61 O ANISOU 3197 O GLY B 198 16069 9011 7829 -277 726 127 O ATOM 3198 N THR B 199 47.047 20.157 15.686 1.00 85.75 N ANISOU 3198 N THR B 199 16159 8864 7558 -247 995 56 N ATOM 3199 CA THR B 199 48.098 20.868 16.407 1.00 85.44 C ANISOU 3199 CA THR B 199 16327 8741 7394 -178 806 78 C ATOM 3200 C THR B 199 48.370 20.182 17.766 1.00 90.01 C ANISOU 3200 C THR B 199 17246 9190 7761 -189 847 119 C ATOM 3201 O THR B 199 47.504 19.491 18.314 1.00 90.43 O ANISOU 3201 O THR B 199 17392 9220 7746 -242 1073 119 O ATOM 3202 CB THR B 199 47.747 22.352 16.592 1.00 94.80 C ANISOU 3202 CB THR B 199 17495 9950 8574 -104 804 16 C ATOM 3203 OG1 THR B 199 46.511 22.466 17.296 1.00 96.33 O ANISOU 3203 OG1 THR B 199 17754 10146 8701 -112 1055 -36 O ATOM 3204 CG2 THR B 199 47.663 23.103 15.268 1.00 92.54 C ANISOU 3204 CG2 THR B 199 16911 9771 8478 -80 724 -13 C ATOM 3205 N LYS B 200 49.602 20.362 18.274 1.00 86.31 N ANISOU 3205 N LYS B 200 16962 8634 7197 -138 622 153 N ATOM 3206 CA LYS B 200 50.102 19.822 19.541 1.00 87.27 C ANISOU 3206 CA LYS B 200 17432 8622 7107 -123 590 193 C ATOM 3207 C LYS B 200 51.004 20.848 20.257 1.00 91.65 C ANISOU 3207 C LYS B 200 18166 9101 7555 -30 378 174 C ATOM 3208 O LYS B 200 51.848 21.473 19.615 1.00 90.29 O ANISOU 3208 O LYS B 200 17851 8956 7498 3 165 164 O ATOM 3209 CB LYS B 200 50.873 18.523 19.287 1.00 89.07 C ANISOU 3209 CB LYS B 200 17687 8803 7350 -163 486 260 C ATOM 3210 N VAL B 201 50.833 21.015 21.581 1.00 89.79 N ANISOU 3210 N VAL B 201 18247 8769 7101 9 439 165 N ATOM 3211 CA VAL B 201 51.651 21.945 22.362 1.00109.63 C ANISOU 3211 CA VAL B 201 20958 11198 9497 100 235 137 C ATOM 3212 C VAL B 201 52.650 21.159 23.222 1.00129.66 C ANISOU 3212 C VAL B 201 23794 13601 11870 129 67 186 C ATOM 3213 O VAL B 201 53.508 20.449 22.692 1.00 86.20 O ANISOU 3213 O VAL B 201 18211 8087 6454 111 -97 228 O ATOM 3214 CB VAL B 201 50.780 22.873 23.231 1.00114.74 C ANISOU 3214 CB VAL B 201 21755 11832 10011 145 396 77 C ATOM 3215 N VAL B 207 56.287 26.327 21.463 1.00 89.83 N ANISOU 3215 N VAL B 207 18183 8580 7366 331 -934 -10 N ATOM 3216 CA VAL B 207 56.420 26.004 20.046 1.00 87.87 C ANISOU 3216 CA VAL B 207 17611 8436 7338 267 -924 27 C ATOM 3217 C VAL B 207 55.301 25.025 19.637 1.00 91.79 C ANISOU 3217 C VAL B 207 18028 9019 7829 207 -664 67 C ATOM 3218 O VAL B 207 55.490 23.807 19.683 1.00 91.29 O ANISOU 3218 O VAL B 207 18016 8938 7731 173 -652 114 O ATOM 3219 CB VAL B 207 57.822 25.433 19.720 1.00 91.12 C ANISOU 3219 CB VAL B 207 17968 8806 7845 259 -1166 52 C ATOM 3220 N ILE B 208 54.129 25.575 19.248 1.00 88.59 N ANISOU 3220 N ILE B 208 17496 8699 7464 195 -461 41 N ATOM 3221 CA ILE B 208 52.949 24.806 18.821 1.00 88.12 C ANISOU 3221 CA ILE B 208 17329 8727 7426 138 -207 59 C ATOM 3222 C ILE B 208 53.258 24.202 17.414 1.00 89.95 C ANISOU 3222 C ILE B 208 17273 9048 7856 81 -247 98 C ATOM 3223 O ILE B 208 53.777 24.888 16.531 1.00 88.65 O ANISOU 3223 O ILE B 208 16919 8926 7838 90 -370 93 O ATOM 3224 CB ILE B 208 51.647 25.678 18.861 1.00 91.54 C ANISOU 3224 CB ILE B 208 17706 9220 7857 157 -3 2 C ATOM 3225 CG1 ILE B 208 50.393 24.864 18.423 1.00 91.77 C ANISOU 3225 CG1 ILE B 208 17602 9336 7929 94 261 7 C ATOM 3226 CG2 ILE B 208 51.796 26.995 18.085 1.00 91.49 C ANISOU 3226 CG2 ILE B 208 17508 9259 7994 194 -103 -34 C ATOM 3227 CD1 ILE B 208 49.016 25.556 18.638 1.00 99.07 C ANISOU 3227 CD1 ILE B 208 18489 10311 8841 115 487 -61 C ATOM 3228 N GLU B 209 52.988 22.891 17.263 1.00 85.92 N ANISOU 3228 N GLU B 209 16755 8553 7337 24 -145 139 N ATOM 3229 CA GLU B 209 53.322 22.088 16.090 1.00 84.37 C ANISOU 3229 CA GLU B 209 16336 8425 7296 -27 -183 176 C ATOM 3230 C GLU B 209 52.091 21.577 15.327 1.00 88.38 C ANISOU 3230 C GLU B 209 16655 9038 7889 -83 42 170 C ATOM 3231 O GLU B 209 51.136 21.106 15.933 1.00 88.04 O ANISOU 3231 O GLU B 209 16712 8984 7755 -110 239 162 O ATOM 3232 CB GLU B 209 54.152 20.869 16.536 1.00 86.10 C ANISOU 3232 CB GLU B 209 16709 8560 7445 -43 -282 225 C ATOM 3233 N CYS B 210 52.159 21.632 13.984 1.00 85.31 N ANISOU 3233 N CYS B 210 15993 8747 7675 -102 6 172 N ATOM 3234 CA CYS B 210 51.156 21.101 13.052 1.00 85.33 C ANISOU 3234 CA CYS B 210 15783 8854 7787 -150 169 160 C ATOM 3235 C CYS B 210 51.693 19.798 12.454 1.00 90.18 C ANISOU 3235 C CYS B 210 16329 9475 8462 -201 120 204 C ATOM 3236 O CYS B 210 52.765 19.817 11.850 1.00 89.29 O ANISOU 3236 O CYS B 210 16141 9364 8422 -189 -56 228 O ATOM 3237 CB CYS B 210 50.814 22.132 11.974 1.00 84.72 C ANISOU 3237 CB CYS B 210 15470 8875 7846 -121 156 126 C ATOM 3238 SG CYS B 210 49.756 21.510 10.630 1.00 87.80 S ANISOU 3238 SG CYS B 210 15575 9396 8388 -164 296 103 S ATOM 3239 N SER B 211 51.001 18.659 12.698 1.00 88.19 N ANISOU 3239 N SER B 211 16120 9212 8175 -259 277 213 N ATOM 3240 CA SER B 211 51.391 17.314 12.230 1.00 88.33 C ANISOU 3240 CA SER B 211 16096 9223 8241 -310 251 251 C ATOM 3241 C SER B 211 50.236 16.332 12.309 1.00 93.47 C ANISOU 3241 C SER B 211 16734 9887 8894 -382 474 241 C ATOM 3242 O SER B 211 49.194 16.660 12.879 1.00 94.28 O ANISOU 3242 O SER B 211 16884 9992 8945 -393 654 207 O ATOM 3243 CB SER B 211 52.554 16.766 13.063 1.00 93.62 C ANISOU 3243 CB SER B 211 16998 9772 8801 -293 98 300 C ATOM 3244 OG SER B 211 53.739 17.534 12.936 1.00104.62 O ANISOU 3244 OG SER B 211 18382 11147 10221 -236 -124 303 O ATOM 3245 N LEU B 212 50.432 15.103 11.777 1.00 89.48 N ANISOU 3245 N LEU B 212 16168 9380 8451 -433 468 267 N ATOM 3246 CA LEU B 212 49.459 14.022 11.924 1.00 89.77 C ANISOU 3246 CA LEU B 212 16213 9403 8491 -513 670 263 C ATOM 3247 C LEU B 212 49.474 13.561 13.368 1.00 94.79 C ANISOU 3247 C LEU B 212 17170 9905 8942 -528 745 303 C ATOM 3248 O LEU B 212 50.516 13.112 13.856 1.00 94.58 O ANISOU 3248 O LEU B 212 17326 9783 8826 -505 596 355 O ATOM 3249 CB LEU B 212 49.738 12.856 10.956 1.00 88.98 C ANISOU 3249 CB LEU B 212 15972 9328 8507 -558 624 277 C ATOM 3250 CG LEU B 212 49.534 13.117 9.473 1.00 92.01 C ANISOU 3250 CG LEU B 212 16048 9845 9066 -551 585 234 C ATOM 3251 CD1 LEU B 212 50.011 11.948 8.653 1.00 91.46 C ANISOU 3251 CD1 LEU B 212 15885 9781 9084 -584 516 250 C ATOM 3252 CD2 LEU B 212 48.088 13.387 9.168 1.00 94.68 C ANISOU 3252 CD2 LEU B 212 16230 10264 9481 -582 777 166 C ATOM 3253 N GLN B 213 48.362 13.774 14.080 1.00 92.41 N ANISOU 3253 N GLN B 213 16945 9593 8575 -557 966 275 N ATOM 3254 CA GLN B 213 48.263 13.461 15.503 1.00 93.77 C ANISOU 3254 CA GLN B 213 17444 9637 8549 -568 1068 311 C ATOM 3255 C GLN B 213 47.719 12.047 15.697 1.00 99.35 C ANISOU 3255 C GLN B 213 18220 10282 9248 -666 1241 341 C ATOM 3256 O GLN B 213 46.682 11.694 15.129 1.00 98.32 O ANISOU 3256 O GLN B 213 17894 10217 9247 -737 1421 298 O ATOM 3257 CB GLN B 213 47.378 14.495 16.230 1.00 95.77 C ANISOU 3257 CB GLN B 213 17759 9904 8724 -544 1229 262 C ATOM 3258 CG GLN B 213 47.838 15.959 16.051 1.00103.67 C ANISOU 3258 CG GLN B 213 18694 10958 9737 -449 1067 227 C ATOM 3259 CD GLN B 213 49.244 16.263 16.540 1.00120.61 C ANISOU 3259 CD GLN B 213 21031 13021 11773 -377 811 271 C ATOM 3260 OE1 GLN B 213 50.025 16.945 15.870 1.00112.13 O ANISOU 3260 OE1 GLN B 213 19824 11994 10787 -327 610 263 O ATOM 3261 NE2 GLN B 213 49.612 15.733 17.698 1.00117.72 N ANISOU 3261 NE2 GLN B 213 20981 12525 11220 -372 808 317 N ATOM 3262 N PHE B 214 48.454 11.231 16.474 1.00 98.32 N ANISOU 3262 N PHE B 214 18366 10016 8974 -666 1173 413 N ATOM 3263 CA PHE B 214 48.111 9.832 16.782 1.00100.02 C ANISOU 3263 CA PHE B 214 18707 10139 9156 -754 1316 458 C ATOM 3264 C PHE B 214 47.937 9.644 18.295 1.00108.44 C ANISOU 3264 C PHE B 214 20157 11061 9983 -758 1445 506 C ATOM 3265 O PHE B 214 48.590 10.368 19.054 1.00108.69 O ANISOU 3265 O PHE B 214 20391 11044 9862 -670 1314 520 O ATOM 3266 CB PHE B 214 49.188 8.868 16.242 1.00100.72 C ANISOU 3266 CB PHE B 214 18790 10185 9295 -746 1107 506 C ATOM 3267 CG PHE B 214 49.419 8.966 14.752 1.00100.12 C ANISOU 3267 CG PHE B 214 18361 10241 9437 -741 985 463 C ATOM 3268 CD1 PHE B 214 48.621 8.260 13.860 1.00102.69 C ANISOU 3268 CD1 PHE B 214 18461 10631 9926 -824 1116 429 C ATOM 3269 CD2 PHE B 214 50.466 9.723 14.244 1.00101.03 C ANISOU 3269 CD2 PHE B 214 18382 10411 9595 -654 737 455 C ATOM 3270 CE1 PHE B 214 48.843 8.341 12.482 1.00102.06 C ANISOU 3270 CE1 PHE B 214 18078 10670 10029 -810 999 389 C ATOM 3271 CE2 PHE B 214 50.689 9.803 12.866 1.00102.31 C ANISOU 3271 CE2 PHE B 214 18240 10691 9943 -649 639 420 C ATOM 3272 CZ PHE B 214 49.873 9.114 11.994 1.00100.03 C ANISOU 3272 CZ PHE B 214 17743 10467 9796 -722 768 388 C ATOM 3273 N PRO B 215 47.083 8.689 18.766 1.00107.83 N ANISOU 3273 N PRO B 215 20197 10910 9866 -858 1700 531 N ATOM 3274 CA PRO B 215 46.890 8.534 20.222 1.00110.45 C ANISOU 3274 CA PRO B 215 20918 11100 9950 -861 1844 581 C ATOM 3275 C PRO B 215 48.166 8.038 20.927 1.00115.62 C ANISOU 3275 C PRO B 215 21902 11608 10419 -790 1614 665 C ATOM 3276 O PRO B 215 48.823 7.106 20.450 1.00114.74 O ANISOU 3276 O PRO B 215 21770 11457 10371 -801 1474 705 O ATOM 3277 CB PRO B 215 45.759 7.500 20.327 1.00113.76 C ANISOU 3277 CB PRO B 215 21338 11473 10413 -998 2160 591 C ATOM 3278 CG PRO B 215 45.781 6.761 19.034 1.00116.46 C ANISOU 3278 CG PRO B 215 21375 11884 10990 -1055 2095 572 C ATOM 3279 CD PRO B 215 46.215 7.763 18.007 1.00109.44 C ANISOU 3279 CD PRO B 215 20185 11151 10248 -974 1880 509 C ATOM 3280 N ASP B 216 48.522 8.690 22.055 1.00113.73 N ANISOU 3280 N ASP B 216 21966 11292 9955 -707 1563 682 N ATOM 3281 CA ASP B 216 49.730 8.387 22.834 1.00114.46 C ANISOU 3281 CA ASP B 216 22391 11243 9856 -618 1322 747 C ATOM 3282 C ASP B 216 49.487 7.175 23.808 1.00120.82 C ANISOU 3282 C ASP B 216 23568 11870 10468 -672 1483 835 C ATOM 3283 O ASP B 216 49.533 7.324 25.039 1.00122.52 O ANISOU 3283 O ASP B 216 24156 11967 10428 -626 1525 871 O ATOM 3284 CB ASP B 216 50.185 9.639 23.614 1.00116.54 C ANISOU 3284 CB ASP B 216 22821 11497 9962 -503 1188 718 C ATOM 3285 N ASP B 217 49.272 5.973 23.231 1.00116.61 N ANISOU 3285 N ASP B 217 22942 11310 10053 -766 1561 869 N ATOM 3286 CA ASP B 217 49.071 4.741 23.994 1.00118.32 C ANISOU 3286 CA ASP B 217 23485 11352 10117 -827 1707 957 C ATOM 3287 C ASP B 217 50.424 4.061 24.255 1.00123.84 C ANISOU 3287 C ASP B 217 24419 11921 10714 -736 1394 1023 C ATOM 3288 O ASP B 217 51.433 4.472 23.679 1.00121.23 O ANISOU 3288 O ASP B 217 23930 11654 10477 -645 1089 990 O ATOM 3289 CB ASP B 217 48.111 3.798 23.257 1.00119.77 C ANISOU 3289 CB ASP B 217 23450 11565 10494 -978 1954 953 C ATOM 3290 N ASP B 218 50.442 3.036 25.143 1.00124.67 N ANISOU 3290 N ASP B 218 24906 11837 10625 -757 1474 1114 N ATOM 3291 CA ASP B 218 51.630 2.268 25.552 1.00125.96 C ANISOU 3291 CA ASP B 218 25352 11846 10662 -667 1198 1182 C ATOM 3292 C ASP B 218 52.237 1.519 24.344 1.00130.86 C ANISOU 3292 C ASP B 218 25683 12512 11525 -681 1013 1170 C ATOM 3293 O ASP B 218 53.384 1.809 23.999 1.00129.35 O ANISOU 3293 O ASP B 218 25409 12350 11387 -570 684 1143 O ATOM 3294 CB ASP B 218 51.269 1.294 26.677 1.00130.42 C ANISOU 3294 CB ASP B 218 26374 12200 10979 -709 1386 1285 C ATOM 3295 CG ASP B 218 50.797 1.987 27.943 1.00139.62 C ANISOU 3295 CG ASP B 218 27875 13304 11872 -679 1551 1301 C ATOM 3296 OD1 ASP B 218 51.456 2.964 28.368 1.00139.22 O ANISOU 3296 OD1 ASP B 218 27909 13276 11711 -550 1336 1264 O ATOM 3297 OD2 ASP B 218 49.830 1.497 28.557 1.00147.24 O ANISOU 3297 OD2 ASP B 218 29043 14179 12720 -781 1888 1352 O ATOM 3298 N TYR B 219 51.486 0.585 23.694 1.00129.28 N ANISOU 3298 N TYR B 219 25322 12319 11480 -814 1221 1182 N ATOM 3299 CA TYR B 219 51.950 -0.042 22.449 1.00128.25 C ANISOU 3299 CA TYR B 219 24882 12253 11594 -830 1067 1155 C ATOM 3300 C TYR B 219 51.208 0.618 21.294 1.00129.81 C ANISOU 3300 C TYR B 219 24615 12664 12044 -900 1184 1062 C ATOM 3301 O TYR B 219 50.089 0.228 20.946 1.00130.45 O ANISOU 3301 O TYR B 219 24553 12777 12234 -1030 1460 1046 O ATOM 3302 CB TYR B 219 51.822 -1.587 22.413 1.00131.74 C ANISOU 3302 CB TYR B 219 25458 12547 12049 -910 1149 1223 C ATOM 3303 CG TYR B 219 52.025 -2.199 21.029 1.00133.17 C ANISOU 3303 CG TYR B 219 25277 12817 12507 -948 1054 1178 C ATOM 3304 CD1 TYR B 219 53.277 -2.197 20.417 1.00133.78 C ANISOU 3304 CD1 TYR B 219 25230 12929 12671 -836 713 1152 C ATOM 3305 CD2 TYR B 219 50.979 -2.835 20.364 1.00134.46 C ANISOU 3305 CD2 TYR B 219 25233 13016 12841 -1096 1307 1157 C ATOM 3306 CE1 TYR B 219 53.466 -2.744 19.146 1.00133.19 C ANISOU 3306 CE1 TYR B 219 24831 12936 12837 -866 635 1107 C ATOM 3307 CE2 TYR B 219 51.157 -3.392 19.094 1.00133.98 C ANISOU 3307 CE2 TYR B 219 24851 13034 13022 -1124 1215 1109 C ATOM 3308 CZ TYR B 219 52.404 -3.347 18.489 1.00139.20 C ANISOU 3308 CZ TYR B 219 25400 13736 13753 -1007 883 1086 C ATOM 3309 OH TYR B 219 52.587 -3.908 17.244 1.00136.53 O ANISOU 3309 OH TYR B 219 24761 13474 13641 -1030 800 1037 O ATOM 3310 N SER B 220 51.808 1.694 20.777 1.00123.20 N ANISOU 3310 N SER B 220 23558 11963 11288 -809 976 998 N ATOM 3311 CA SER B 220 51.324 2.484 19.656 1.00120.38 C ANISOU 3311 CA SER B 220 22776 11809 11155 -841 1020 910 C ATOM 3312 C SER B 220 52.490 3.253 19.065 1.00121.29 C ANISOU 3312 C SER B 220 22721 12014 11348 -724 700 869 C ATOM 3313 O SER B 220 52.976 4.233 19.641 1.00121.14 O ANISOU 3313 O SER B 220 22811 12000 11218 -634 576 858 O ATOM 3314 CB SER B 220 50.178 3.410 20.059 1.00124.44 C ANISOU 3314 CB SER B 220 23260 12393 11627 -887 1279 872 C ATOM 3315 OG SER B 220 49.012 2.664 20.363 1.00134.18 O ANISOU 3315 OG SER B 220 24565 13568 12852 -1016 1603 894 O ATOM 3316 N TRP B 221 52.974 2.739 17.937 1.00115.07 N ANISOU 3316 N TRP B 221 21682 11288 10752 -728 567 846 N ATOM 3317 CA TRP B 221 54.107 3.223 17.145 1.00112.40 C ANISOU 3317 CA TRP B 221 21137 11036 10533 -636 280 805 C ATOM 3318 C TRP B 221 53.632 3.652 15.748 1.00113.54 C ANISOU 3318 C TRP B 221 20861 11368 10912 -681 335 734 C ATOM 3319 O TRP B 221 54.434 3.705 14.811 1.00111.97 O ANISOU 3319 O TRP B 221 20450 11243 10852 -636 146 704 O ATOM 3320 CB TRP B 221 55.159 2.094 17.055 1.00111.18 C ANISOU 3320 CB TRP B 221 21085 10770 10387 -592 73 842 C ATOM 3321 CG TRP B 221 54.645 0.836 16.406 1.00111.91 C ANISOU 3321 CG TRP B 221 21085 10841 10595 -687 200 854 C ATOM 3322 CD1 TRP B 221 53.808 -0.090 16.958 1.00116.46 C ANISOU 3322 CD1 TRP B 221 21856 11302 11092 -779 421 904 C ATOM 3323 CD2 TRP B 221 55.020 0.321 15.125 1.00110.26 C ANISOU 3323 CD2 TRP B 221 20588 10712 10594 -694 101 813 C ATOM 3324 NE1 TRP B 221 53.562 -1.099 16.061 1.00115.31 N ANISOU 3324 NE1 TRP B 221 21537 11166 11109 -851 471 891 N ATOM 3325 CE2 TRP B 221 54.314 -0.887 14.936 1.00114.92 C ANISOU 3325 CE2 TRP B 221 21199 11236 11230 -794 270 835 C ATOM 3326 CE3 TRP B 221 55.871 0.772 14.104 1.00109.70 C ANISOU 3326 CE3 TRP B 221 20244 10761 10677 -628 -103 759 C ATOM 3327 CZ2 TRP B 221 54.422 -1.642 13.763 1.00113.28 C ANISOU 3327 CZ2 TRP B 221 20749 11081 11212 -824 228 798 C ATOM 3328 CZ3 TRP B 221 55.985 0.018 12.947 1.00110.12 C ANISOU 3328 CZ3 TRP B 221 20065 10868 10908 -656 -132 726 C ATOM 3329 CH2 TRP B 221 55.264 -1.171 12.782 1.00111.63 C ANISOU 3329 CH2 TRP B 221 20284 10995 11137 -749 26 743 C ATOM 3330 N TRP B 222 52.322 3.983 15.627 1.00109.39 N ANISOU 3330 N TRP B 222 20222 10918 10425 -766 596 704 N ATOM 3331 CA TRP B 222 51.650 4.337 14.377 1.00107.25 C ANISOU 3331 CA TRP B 222 19577 10814 10360 -812 678 633 C ATOM 3332 C TRP B 222 52.198 5.661 13.801 1.00106.83 C ANISOU 3332 C TRP B 222 19328 10890 10373 -728 513 587 C ATOM 3333 O TRP B 222 52.030 5.884 12.601 1.00104.58 O ANISOU 3333 O TRP B 222 18739 10736 10260 -739 498 536 O ATOM 3334 CB TRP B 222 50.126 4.412 14.564 1.00107.17 C ANISOU 3334 CB TRP B 222 19519 10834 10366 -912 988 606 C ATOM 3335 CG TRP B 222 49.467 3.072 14.361 1.00109.56 C ANISOU 3335 CG TRP B 222 19816 11074 10738 -1022 1151 618 C ATOM 3336 CD1 TRP B 222 48.893 2.618 13.209 1.00111.66 C ANISOU 3336 CD1 TRP B 222 19788 11431 11207 -1087 1214 561 C ATOM 3337 CD2 TRP B 222 49.517 1.942 15.255 1.00111.16 C ANISOU 3337 CD2 TRP B 222 20327 11096 10811 -1067 1225 693 C ATOM 3338 NE1 TRP B 222 48.512 1.301 13.355 1.00112.52 N ANISOU 3338 NE1 TRP B 222 19991 11429 11333 -1181 1338 591 N ATOM 3339 CE2 TRP B 222 48.887 0.860 14.600 1.00115.48 C ANISOU 3339 CE2 TRP B 222 20739 11634 11504 -1172 1352 676 C ATOM 3340 CE3 TRP B 222 50.011 1.745 16.557 1.00114.00 C ANISOU 3340 CE3 TRP B 222 21080 11296 10940 -1028 1196 773 C ATOM 3341 CZ2 TRP B 222 48.717 -0.392 15.211 1.00116.43 C ANISOU 3341 CZ2 TRP B 222 21100 11585 11554 -1247 1464 741 C ATOM 3342 CZ3 TRP B 222 49.847 0.504 17.158 1.00117.12 C ANISOU 3342 CZ3 TRP B 222 21725 11524 11251 -1094 1303 840 C ATOM 3343 CH2 TRP B 222 49.202 -0.545 16.491 1.00118.00 C ANISOU 3343 CH2 TRP B 222 21692 11625 11517 -1206 1442 826 C ATOM 3344 N ASP B 223 52.958 6.415 14.589 1.00102.05 N ANISOU 3344 N ASP B 223 18901 10236 9636 -643 369 606 N ATOM 3345 CA ASP B 223 53.596 7.625 14.085 1.00 99.34 C ANISOU 3345 CA ASP B 223 18392 9994 9360 -568 201 566 C ATOM 3346 C ASP B 223 54.753 7.167 13.185 1.00 98.92 C ANISOU 3346 C ASP B 223 18194 9962 9431 -528 -23 563 C ATOM 3347 O ASP B 223 54.881 7.606 12.042 1.00 97.59 O ANISOU 3347 O ASP B 223 17745 9919 9417 -521 -72 522 O ATOM 3348 CB ASP B 223 54.120 8.483 15.235 1.00102.33 C ANISOU 3348 CB ASP B 223 19016 10298 9567 -491 101 581 C ATOM 3349 CG ASP B 223 54.658 9.821 14.766 1.00113.60 C ANISOU 3349 CG ASP B 223 20272 11822 11068 -426 -46 536 C ATOM 3350 OD1 ASP B 223 54.324 10.234 13.636 1.00112.70 O ANISOU 3350 OD1 ASP B 223 19864 11841 11115 -447 -10 497 O ATOM 3351 OD2 ASP B 223 55.415 10.458 15.528 1.00121.98 O ANISOU 3351 OD2 ASP B 223 21502 12820 12027 -352 -200 540 O ATOM 3352 N LEU B 224 55.589 6.279 13.724 1.00 93.68 N ANISOU 3352 N LEU B 224 17733 9169 8692 -497 -154 607 N ATOM 3353 CA LEU B 224 56.721 5.688 13.016 1.00 91.67 C ANISOU 3353 CA LEU B 224 17373 8910 8546 -455 -363 602 C ATOM 3354 C LEU B 224 56.229 4.856 11.841 1.00 94.38 C ANISOU 3354 C LEU B 224 17484 9328 9047 -523 -266 581 C ATOM 3355 O LEU B 224 56.762 4.997 10.745 1.00 92.99 O ANISOU 3355 O LEU B 224 17064 9248 9019 -500 -370 545 O ATOM 3356 CB LEU B 224 57.585 4.822 13.960 1.00 92.64 C ANISOU 3356 CB LEU B 224 17793 8861 8544 -404 -512 650 C ATOM 3357 CG LEU B 224 58.802 4.109 13.322 1.00 96.14 C ANISOU 3357 CG LEU B 224 18144 9285 9102 -350 -736 639 C ATOM 3358 CD1 LEU B 224 59.888 5.093 12.948 1.00 95.15 C ANISOU 3358 CD1 LEU B 224 17866 9224 9060 -271 -950 596 C ATOM 3359 CD2 LEU B 224 59.384 3.090 14.257 1.00 99.60 C ANISOU 3359 CD2 LEU B 224 18889 9542 9413 -308 -847 688 C ATOM 3360 N PHE B 225 55.199 4.007 12.064 1.00 91.47 N ANISOU 3360 N PHE B 225 17192 8912 8650 -609 -60 601 N ATOM 3361 CA PHE B 225 54.626 3.116 11.050 1.00 90.90 C ANISOU 3361 CA PHE B 225 16923 8892 8723 -682 41 575 C ATOM 3362 C PHE B 225 54.193 3.887 9.787 1.00 93.63 C ANISOU 3362 C PHE B 225 16928 9420 9228 -692 76 509 C ATOM 3363 O PHE B 225 54.491 3.423 8.685 1.00 92.16 O ANISOU 3363 O PHE B 225 16543 9297 9178 -691 10 478 O ATOM 3364 CB PHE B 225 53.425 2.332 11.610 1.00 93.99 C ANISOU 3364 CB PHE B 225 17447 9205 9060 -785 289 598 C ATOM 3365 CG PHE B 225 52.667 1.543 10.565 1.00 95.15 C ANISOU 3365 CG PHE B 225 17368 9413 9372 -869 409 556 C ATOM 3366 CD1 PHE B 225 53.161 0.337 10.085 1.00 98.01 C ANISOU 3366 CD1 PHE B 225 17722 9716 9803 -878 326 564 C ATOM 3367 CD2 PHE B 225 51.447 2.000 10.075 1.00 97.04 C ANISOU 3367 CD2 PHE B 225 17406 9764 9700 -935 598 501 C ATOM 3368 CE1 PHE B 225 52.464 -0.385 9.111 1.00 98.45 C ANISOU 3368 CE1 PHE B 225 17571 9824 10012 -953 426 516 C ATOM 3369 CE2 PHE B 225 50.750 1.275 9.101 1.00 99.32 C ANISOU 3369 CE2 PHE B 225 17482 10106 10148 -1008 690 450 C ATOM 3370 CZ PHE B 225 51.254 0.079 8.640 1.00 97.18 C ANISOU 3370 CZ PHE B 225 17212 9773 9938 -1019 606 459 C ATOM 3371 N MET B 226 53.490 5.040 9.937 1.00 90.16 N ANISOU 3371 N MET B 226 16431 9059 8767 -695 178 485 N ATOM 3372 CA MET B 226 53.049 5.834 8.782 1.00 88.81 C ANISOU 3372 CA MET B 226 15960 9052 8732 -694 204 424 C ATOM 3373 C MET B 226 54.252 6.376 8.034 1.00 88.19 C ANISOU 3373 C MET B 226 15752 9036 8722 -614 -12 415 C ATOM 3374 O MET B 226 54.233 6.414 6.808 1.00 86.55 O ANISOU 3374 O MET B 226 15305 8936 8645 -613 -34 375 O ATOM 3375 CB MET B 226 52.109 6.988 9.185 1.00 92.19 C ANISOU 3375 CB MET B 226 16375 9535 9116 -701 343 400 C ATOM 3376 CG MET B 226 50.757 6.531 9.729 1.00 98.55 C ANISOU 3376 CG MET B 226 17245 10307 9895 -789 594 391 C ATOM 3377 SD MET B 226 49.659 5.675 8.555 1.00104.09 S ANISOU 3377 SD MET B 226 17678 11088 10782 -878 740 327 S ATOM 3378 CE MET B 226 48.301 5.178 9.684 1.00102.85 C ANISOU 3378 CE MET B 226 17685 10838 10555 -985 1037 332 C ATOM 3379 N LYS B 227 55.314 6.699 8.764 1.00 83.03 N ANISOU 3379 N LYS B 227 15261 8305 7981 -550 -172 448 N ATOM 3380 CA LYS B 227 56.539 7.201 8.156 1.00 81.26 C ANISOU 3380 CA LYS B 227 14920 8124 7830 -480 -375 436 C ATOM 3381 C LYS B 227 57.267 6.107 7.369 1.00 83.52 C ANISOU 3381 C LYS B 227 15114 8403 8216 -474 -475 430 C ATOM 3382 O LYS B 227 57.866 6.382 6.329 1.00 82.36 O ANISOU 3382 O LYS B 227 14765 8344 8184 -444 -563 401 O ATOM 3383 CB LYS B 227 57.466 7.785 9.224 1.00 84.36 C ANISOU 3383 CB LYS B 227 15514 8425 8115 -415 -527 462 C ATOM 3384 CG LYS B 227 56.935 9.049 9.882 1.00 97.52 C ANISOU 3384 CG LYS B 227 17249 10109 9696 -405 -461 457 C ATOM 3385 CD LYS B 227 57.841 9.506 11.013 1.00108.01 C ANISOU 3385 CD LYS B 227 18802 11330 10907 -339 -621 476 C ATOM 3386 CE LYS B 227 57.391 10.845 11.574 1.00118.46 C ANISOU 3386 CE LYS B 227 20177 12675 12156 -321 -571 462 C ATOM 3387 NZ LYS B 227 56.036 10.763 12.186 1.00128.60 N ANISOU 3387 NZ LYS B 227 21576 13949 13339 -373 -339 469 N ATOM 3388 N ILE B 228 57.216 4.870 7.862 1.00 80.00 N ANISOU 3388 N ILE B 228 14826 7848 7724 -501 -454 457 N ATOM 3389 CA ILE B 228 57.886 3.750 7.178 1.00 79.06 C ANISOU 3389 CA ILE B 228 14636 7706 7695 -490 -549 447 C ATOM 3390 C ILE B 228 57.168 3.491 5.839 1.00 81.06 C ANISOU 3390 C ILE B 228 14632 8084 8083 -538 -442 400 C ATOM 3391 O ILE B 228 57.830 3.308 4.813 1.00 79.68 O ANISOU 3391 O ILE B 228 14284 7974 8018 -506 -537 369 O ATOM 3392 CB ILE B 228 57.957 2.446 8.045 1.00 83.35 C ANISOU 3392 CB ILE B 228 15430 8087 8153 -507 -552 490 C ATOM 3393 CG1 ILE B 228 58.453 2.698 9.495 1.00 84.86 C ANISOU 3393 CG1 ILE B 228 15921 8143 8177 -458 -639 539 C ATOM 3394 CG2 ILE B 228 58.782 1.342 7.354 1.00 83.94 C ANISOU 3394 CG2 ILE B 228 15435 8132 8327 -479 -677 474 C ATOM 3395 CD1 ILE B 228 59.866 3.283 9.669 1.00 94.40 C ANISOU 3395 CD1 ILE B 228 17140 9335 9394 -358 -885 528 C ATOM 3396 N CYS B 229 55.811 3.478 5.870 1.00 77.33 N ANISOU 3396 N CYS B 229 14137 7643 7602 -612 -244 389 N ATOM 3397 CA CYS B 229 54.940 3.261 4.713 1.00 76.62 C ANISOU 3397 CA CYS B 229 13817 7663 7631 -659 -136 335 C ATOM 3398 C CYS B 229 55.178 4.344 3.664 1.00 78.41 C ANISOU 3398 C CYS B 229 13819 8037 7936 -610 -196 297 C ATOM 3399 O CYS B 229 55.296 4.017 2.485 1.00 77.63 O ANISOU 3399 O CYS B 229 13538 8017 7942 -601 -227 258 O ATOM 3400 CB CYS B 229 53.475 3.222 5.132 1.00 78.06 C ANISOU 3400 CB CYS B 229 14027 7842 7791 -741 80 323 C ATOM 3401 SG CYS B 229 53.035 1.803 6.160 1.00 84.08 S ANISOU 3401 SG CYS B 229 15034 8430 8482 -822 194 366 S ATOM 3402 N VAL B 230 55.277 5.622 4.081 1.00 73.24 N ANISOU 3402 N VAL B 230 13189 7412 7226 -575 -214 311 N ATOM 3403 CA VAL B 230 55.551 6.714 3.150 1.00 71.47 C ANISOU 3403 CA VAL B 230 12779 7311 7067 -528 -270 286 C ATOM 3404 C VAL B 230 56.950 6.492 2.546 1.00 73.76 C ANISOU 3404 C VAL B 230 13006 7603 7416 -474 -441 288 C ATOM 3405 O VAL B 230 57.107 6.630 1.341 1.00 72.14 O ANISOU 3405 O VAL B 230 12612 7497 7300 -456 -461 257 O ATOM 3406 CB VAL B 230 55.409 8.123 3.810 1.00 75.70 C ANISOU 3406 CB VAL B 230 13374 7858 7531 -502 -260 301 C ATOM 3407 CG1 VAL B 230 55.883 9.241 2.877 1.00 74.61 C ANISOU 3407 CG1 VAL B 230 13066 7823 7457 -452 -336 285 C ATOM 3408 CG2 VAL B 230 53.971 8.382 4.248 1.00 76.07 C ANISOU 3408 CG2 VAL B 230 13444 7920 7538 -550 -78 283 C ATOM 3409 N PHE B 231 57.935 6.071 3.357 1.00 71.00 N ANISOU 3409 N PHE B 231 12815 7142 7021 -447 -559 320 N ATOM 3410 CA PHE B 231 59.291 5.871 2.850 1.00 70.82 C ANISOU 3410 CA PHE B 231 12722 7116 7069 -393 -721 312 C ATOM 3411 C PHE B 231 59.347 4.770 1.764 1.00 75.40 C ANISOU 3411 C PHE B 231 13168 7734 7745 -402 -716 278 C ATOM 3412 O PHE B 231 60.126 4.915 0.824 1.00 75.28 O ANISOU 3412 O PHE B 231 13001 7785 7818 -364 -790 253 O ATOM 3413 CB PHE B 231 60.277 5.525 3.978 1.00 73.48 C ANISOU 3413 CB PHE B 231 13261 7315 7344 -355 -863 342 C ATOM 3414 CG PHE B 231 61.691 5.278 3.494 1.00 74.95 C ANISOU 3414 CG PHE B 231 13361 7494 7624 -296 -1033 322 C ATOM 3415 CD1 PHE B 231 62.475 6.323 3.019 1.00 77.58 C ANISOU 3415 CD1 PHE B 231 13559 7892 8026 -260 -1112 305 C ATOM 3416 CD2 PHE B 231 62.253 4.009 3.557 1.00 77.66 C ANISOU 3416 CD2 PHE B 231 13762 7755 7992 -277 -1113 316 C ATOM 3417 CE1 PHE B 231 63.773 6.090 2.555 1.00 78.56 C ANISOU 3417 CE1 PHE B 231 13586 8010 8253 -211 -1252 278 C ATOM 3418 CE2 PHE B 231 63.566 3.786 3.129 1.00 80.48 C ANISOU 3418 CE2 PHE B 231 14027 8104 8446 -217 -1270 287 C ATOM 3419 CZ PHE B 231 64.312 4.825 2.619 1.00 78.05 C ANISOU 3419 CZ PHE B 231 13567 7871 8217 -187 -1332 265 C ATOM 3420 N ILE B 232 58.527 3.713 1.852 1.00 71.80 N ANISOU 3420 N ILE B 232 12764 7239 7280 -454 -621 273 N ATOM 3421 CA ILE B 232 58.634 2.656 0.849 1.00 71.40 C ANISOU 3421 CA ILE B 232 12594 7213 7320 -458 -630 234 C ATOM 3422 C ILE B 232 57.685 2.946 -0.365 1.00 73.20 C ANISOU 3422 C ILE B 232 12617 7581 7615 -483 -522 185 C ATOM 3423 O ILE B 232 58.089 2.675 -1.492 1.00 71.84 O ANISOU 3423 O ILE B 232 12296 7479 7523 -454 -565 146 O ATOM 3424 CB ILE B 232 58.372 1.230 1.433 1.00 76.07 C ANISOU 3424 CB ILE B 232 13337 7678 7887 -497 -604 246 C ATOM 3425 CG1 ILE B 232 56.926 1.045 1.968 1.00 77.46 C ANISOU 3425 CG1 ILE B 232 13589 7827 8013 -583 -424 254 C ATOM 3426 CG2 ILE B 232 59.422 0.895 2.517 1.00 77.92 C ANISOU 3426 CG2 ILE B 232 13778 7772 8056 -452 -742 290 C ATOM 3427 CD1 ILE B 232 56.567 -0.385 2.418 1.00 87.34 C ANISOU 3427 CD1 ILE B 232 14978 8951 9255 -638 -372 266 C ATOM 3428 N PHE B 233 56.474 3.513 -0.150 1.00 69.06 N ANISOU 3428 N PHE B 233 12086 7096 7058 -527 -392 181 N ATOM 3429 CA PHE B 233 55.531 3.760 -1.248 1.00 67.86 C ANISOU 3429 CA PHE B 233 11748 7067 6971 -541 -307 126 C ATOM 3430 C PHE B 233 55.684 5.171 -1.864 1.00 71.10 C ANISOU 3430 C PHE B 233 12041 7588 7384 -491 -333 124 C ATOM 3431 O PHE B 233 55.066 5.442 -2.893 1.00 70.90 O ANISOU 3431 O PHE B 233 11865 7667 7407 -483 -292 79 O ATOM 3432 CB PHE B 233 54.075 3.580 -0.790 1.00 70.02 C ANISOU 3432 CB PHE B 233 12047 7326 7232 -614 -151 107 C ATOM 3433 CG PHE B 233 53.740 2.179 -0.354 1.00 72.34 C ANISOU 3433 CG PHE B 233 12436 7513 7536 -678 -97 105 C ATOM 3434 CD1 PHE B 233 53.515 1.178 -1.290 1.00 75.78 C ANISOU 3434 CD1 PHE B 233 12759 7970 8064 -697 -96 49 C ATOM 3435 CD2 PHE B 233 53.568 1.875 0.988 1.00 75.05 C ANISOU 3435 CD2 PHE B 233 12990 7730 7794 -722 -38 155 C ATOM 3436 CE1 PHE B 233 53.200 -0.121 -0.883 1.00 77.64 C ANISOU 3436 CE1 PHE B 233 13087 8095 8317 -762 -44 47 C ATOM 3437 CE2 PHE B 233 53.242 0.580 1.395 1.00 78.83 C ANISOU 3437 CE2 PHE B 233 13573 8098 8280 -786 23 160 C ATOM 3438 CZ PHE B 233 53.062 -0.411 0.458 1.00 77.17 C ANISOU 3438 CZ PHE B 233 13243 7904 8173 -809 19 106 C ATOM 3439 N ALA B 234 56.497 6.046 -1.275 1.00 66.56 N ANISOU 3439 N ALA B 234 11541 6987 6763 -455 -405 168 N ATOM 3440 CA ALA B 234 56.706 7.366 -1.858 1.00 65.33 C ANISOU 3440 CA ALA B 234 11286 6921 6617 -413 -429 170 C ATOM 3441 C ALA B 234 58.152 7.506 -2.336 1.00 68.95 C ANISOU 3441 C ALA B 234 11696 7384 7117 -364 -553 183 C ATOM 3442 O ALA B 234 58.428 8.363 -3.176 1.00 68.66 O ANISOU 3442 O ALA B 234 11548 7429 7110 -332 -566 179 O ATOM 3443 CB ALA B 234 56.336 8.453 -0.870 1.00 66.20 C ANISOU 3443 CB ALA B 234 11495 7004 6653 -416 -395 200 C ATOM 3444 N PHE B 235 59.040 6.621 -1.889 1.00 65.00 N ANISOU 3444 N PHE B 235 11273 6796 6627 -358 -637 192 N ATOM 3445 CA PHE B 235 60.441 6.689 -2.304 1.00 64.26 C ANISOU 3445 CA PHE B 235 11120 6703 6594 -312 -753 192 C ATOM 3446 C PHE B 235 61.035 5.382 -2.850 1.00 68.57 C ANISOU 3446 C PHE B 235 11621 7228 7202 -298 -803 160 C ATOM 3447 O PHE B 235 61.359 5.284 -4.033 1.00 68.50 O ANISOU 3447 O PHE B 235 11469 7301 7258 -274 -802 128 O ATOM 3448 CB PHE B 235 61.307 7.209 -1.153 1.00 66.19 C ANISOU 3448 CB PHE B 235 11490 6853 6804 -293 -855 226 C ATOM 3449 CG PHE B 235 62.771 7.288 -1.483 1.00 67.27 C ANISOU 3449 CG PHE B 235 11555 6981 7024 -249 -978 215 C ATOM 3450 CD1 PHE B 235 63.269 8.338 -2.235 1.00 69.52 C ANISOU 3450 CD1 PHE B 235 11709 7341 7364 -233 -981 213 C ATOM 3451 CD2 PHE B 235 63.647 6.311 -1.041 1.00 69.13 C ANISOU 3451 CD2 PHE B 235 11852 7125 7288 -225 -1088 205 C ATOM 3452 CE1 PHE B 235 64.615 8.414 -2.540 1.00 70.12 C ANISOU 3452 CE1 PHE B 235 11704 7407 7533 -201 -1078 197 C ATOM 3453 CE2 PHE B 235 64.994 6.381 -1.342 1.00 71.67 C ANISOU 3453 CE2 PHE B 235 12088 7438 7705 -182 -1200 182 C ATOM 3454 CZ PHE B 235 65.479 7.434 -2.093 1.00 69.22 C ANISOU 3454 CZ PHE B 235 11634 7209 7460 -174 -1189 177 C ATOM 3455 N VAL B 236 61.173 4.389 -1.977 1.00 65.25 N ANISOU 3455 N VAL B 236 11339 6695 6758 -308 -845 169 N ATOM 3456 CA VAL B 236 61.773 3.089 -2.317 1.00 65.42 C ANISOU 3456 CA VAL B 236 11347 6672 6837 -289 -907 139 C ATOM 3457 C VAL B 236 61.179 2.292 -3.529 1.00 70.01 C ANISOU 3457 C VAL B 236 11801 7328 7471 -303 -835 88 C ATOM 3458 O VAL B 236 61.937 2.010 -4.463 1.00 69.71 O ANISOU 3458 O VAL B 236 11646 7336 7505 -261 -882 52 O ATOM 3459 CB VAL B 236 61.717 2.074 -1.140 1.00 69.81 C ANISOU 3459 CB VAL B 236 12104 7081 7339 -306 -942 163 C ATOM 3460 CG1 VAL B 236 62.295 0.716 -1.547 1.00 70.00 C ANISOU 3460 CG1 VAL B 236 12114 7055 7429 -281 -1009 129 C ATOM 3461 CG2 VAL B 236 62.465 2.610 0.068 1.00 69.97 C ANISOU 3461 CG2 VAL B 236 12273 7008 7303 -276 -1048 203 C ATOM 3462 N ILE B 237 59.868 1.921 -3.501 1.00 66.70 N ANISOU 3462 N ILE B 237 11405 6916 7023 -358 -725 78 N ATOM 3463 CA ILE B 237 59.178 1.261 -4.628 1.00 66.21 C ANISOU 3463 CA ILE B 237 11219 6924 7012 -373 -663 20 C ATOM 3464 C ILE B 237 59.224 2.192 -5.886 1.00 68.88 C ANISOU 3464 C ILE B 237 11387 7407 7376 -333 -647 -7 C ATOM 3465 O ILE B 237 59.779 1.734 -6.883 1.00 69.12 O ANISOU 3465 O ILE B 237 11320 7483 7460 -295 -682 -47 O ATOM 3466 CB ILE B 237 57.714 0.835 -4.276 1.00 69.54 C ANISOU 3466 CB ILE B 237 11686 7323 7414 -447 -545 8 C ATOM 3467 CG1 ILE B 237 57.655 -0.156 -3.057 1.00 70.52 C ANISOU 3467 CG1 ILE B 237 12001 7290 7502 -492 -541 41 C ATOM 3468 CG2 ILE B 237 56.966 0.276 -5.495 1.00 69.87 C ANISOU 3468 CG2 ILE B 237 11583 7445 7519 -457 -495 -66 C ATOM 3469 CD1 ILE B 237 58.408 -1.568 -3.191 1.00 75.09 C ANISOU 3469 CD1 ILE B 237 12624 7779 8129 -473 -626 22 C ATOM 3470 N PRO B 238 58.783 3.489 -5.857 1.00 63.94 N ANISOU 3470 N PRO B 238 10735 6847 6711 -334 -602 18 N ATOM 3471 CA PRO B 238 58.878 4.325 -7.070 1.00 63.03 C ANISOU 3471 CA PRO B 238 10482 6855 6612 -292 -590 0 C ATOM 3472 C PRO B 238 60.305 4.401 -7.651 1.00 66.65 C ANISOU 3472 C PRO B 238 10881 7330 7115 -240 -666 1 C ATOM 3473 O PRO B 238 60.452 4.098 -8.839 1.00 65.42 O ANISOU 3473 O PRO B 238 10622 7247 6990 -209 -657 -41 O ATOM 3474 CB PRO B 238 58.428 5.697 -6.576 1.00 64.48 C ANISOU 3474 CB PRO B 238 10695 7062 6744 -299 -554 41 C ATOM 3475 CG PRO B 238 57.480 5.397 -5.491 1.00 69.31 C ANISOU 3475 CG PRO B 238 11412 7604 7318 -353 -498 49 C ATOM 3476 CD PRO B 238 58.085 4.221 -4.778 1.00 65.55 C ANISOU 3476 CD PRO B 238 11040 7014 6851 -370 -550 58 C ATOM 3477 N VAL B 239 61.349 4.760 -6.828 1.00 63.84 N ANISOU 3477 N VAL B 239 10587 6903 6765 -230 -739 42 N ATOM 3478 CA VAL B 239 62.770 4.843 -7.260 1.00 63.79 C ANISOU 3478 CA VAL B 239 10512 6901 6824 -186 -810 35 C ATOM 3479 C VAL B 239 63.162 3.547 -7.994 1.00 69.20 C ANISOU 3479 C VAL B 239 11139 7587 7565 -161 -832 -20 C ATOM 3480 O VAL B 239 63.674 3.607 -9.112 1.00 68.72 O ANISOU 3480 O VAL B 239 10964 7602 7544 -125 -817 -50 O ATOM 3481 CB VAL B 239 63.758 5.126 -6.085 1.00 67.67 C ANISOU 3481 CB VAL B 239 11090 7292 7330 -181 -909 69 C ATOM 3482 CG1 VAL B 239 65.211 4.962 -6.514 1.00 67.60 C ANISOU 3482 CG1 VAL B 239 10992 7277 7417 -137 -986 43 C ATOM 3483 CG2 VAL B 239 63.545 6.508 -5.501 1.00 67.32 C ANISOU 3483 CG2 VAL B 239 11088 7251 7240 -197 -894 116 C ATOM 3484 N LEU B 240 62.892 2.386 -7.375 1.00 66.69 N ANISOU 3484 N LEU B 240 10910 7182 7246 -179 -861 -34 N ATOM 3485 CA LEU B 240 63.199 1.095 -7.975 1.00 67.11 C ANISOU 3485 CA LEU B 240 10926 7220 7353 -155 -888 -90 C ATOM 3486 C LEU B 240 62.505 0.956 -9.327 1.00 70.32 C ANISOU 3486 C LEU B 240 11221 7739 7760 -148 -812 -140 C ATOM 3487 O LEU B 240 63.175 0.619 -10.296 1.00 70.79 O ANISOU 3487 O LEU B 240 11187 7845 7864 -102 -824 -184 O ATOM 3488 CB LEU B 240 62.800 -0.064 -7.046 1.00 67.96 C ANISOU 3488 CB LEU B 240 11169 7205 7447 -187 -916 -88 C ATOM 3489 CG LEU B 240 63.515 -0.113 -5.690 1.00 73.94 C ANISOU 3489 CG LEU B 240 12068 7835 8190 -180 -1012 -43 C ATOM 3490 CD1 LEU B 240 62.921 -1.178 -4.801 1.00 75.17 C ANISOU 3490 CD1 LEU B 240 12384 7868 8308 -218 -1012 -29 C ATOM 3491 CD2 LEU B 240 65.025 -0.313 -5.847 1.00 77.40 C ANISOU 3491 CD2 LEU B 240 12451 8247 8709 -112 -1128 -68 C ATOM 3492 N ILE B 241 61.205 1.309 -9.421 1.00 65.26 N ANISOU 3492 N ILE B 241 10584 7143 7069 -186 -735 -138 N ATOM 3493 CA ILE B 241 60.459 1.194 -10.674 1.00 64.41 C ANISOU 3493 CA ILE B 241 10378 7137 6957 -172 -680 -194 C ATOM 3494 C ILE B 241 61.050 2.152 -11.742 1.00 67.94 C ANISOU 3494 C ILE B 241 10728 7691 7394 -118 -665 -191 C ATOM 3495 O ILE B 241 61.334 1.679 -12.842 1.00 67.79 O ANISOU 3495 O ILE B 241 10637 7728 7393 -76 -662 -244 O ATOM 3496 CB ILE B 241 58.946 1.447 -10.485 1.00 67.11 C ANISOU 3496 CB ILE B 241 10734 7501 7262 -219 -611 -200 C ATOM 3497 CG1 ILE B 241 58.346 0.432 -9.494 1.00 67.82 C ANISOU 3497 CG1 ILE B 241 10920 7480 7367 -282 -601 -204 C ATOM 3498 CG2 ILE B 241 58.220 1.366 -11.835 1.00 67.77 C ANISOU 3498 CG2 ILE B 241 10713 7691 7346 -191 -580 -268 C ATOM 3499 CD1 ILE B 241 56.858 0.638 -9.156 1.00 76.87 C ANISOU 3499 CD1 ILE B 241 12076 8636 8496 -341 -518 -215 C ATOM 3500 N ILE B 242 61.285 3.456 -11.421 1.00 63.59 N ANISOU 3500 N ILE B 242 10187 7160 6814 -119 -651 -131 N ATOM 3501 CA ILE B 242 61.807 4.404 -12.423 1.00 63.11 C ANISOU 3501 CA ILE B 242 10049 7189 6741 -77 -621 -120 C ATOM 3502 C ILE B 242 63.246 3.975 -12.846 1.00 66.51 C ANISOU 3502 C ILE B 242 10424 7609 7237 -41 -654 -139 C ATOM 3503 O ILE B 242 63.602 4.201 -13.999 1.00 66.74 O ANISOU 3503 O ILE B 242 10381 7717 7261 -1 -612 -159 O ATOM 3504 CB ILE B 242 61.779 5.909 -12.004 1.00 66.14 C ANISOU 3504 CB ILE B 242 10456 7584 7088 -89 -599 -53 C ATOM 3505 CG1 ILE B 242 62.806 6.253 -10.905 1.00 67.04 C ANISOU 3505 CG1 ILE B 242 10617 7612 7245 -108 -657 -8 C ATOM 3506 CG2 ILE B 242 60.357 6.357 -11.614 1.00 66.82 C ANISOU 3506 CG2 ILE B 242 10586 7684 7118 -116 -563 -44 C ATOM 3507 CD1 ILE B 242 62.896 7.776 -10.536 1.00 76.38 C ANISOU 3507 CD1 ILE B 242 11820 8800 8402 -119 -641 53 C ATOM 3508 N ILE B 243 64.022 3.297 -11.961 1.00 61.95 N ANISOU 3508 N ILE B 243 9883 6935 6720 -48 -727 -140 N ATOM 3509 CA ILE B 243 65.368 2.820 -12.308 1.00 61.55 C ANISOU 3509 CA ILE B 243 9767 6869 6751 -8 -766 -172 C ATOM 3510 C ILE B 243 65.234 1.569 -13.202 1.00 64.40 C ANISOU 3510 C ILE B 243 10088 7255 7127 25 -759 -248 C ATOM 3511 O ILE B 243 65.753 1.584 -14.316 1.00 64.00 O ANISOU 3511 O ILE B 243 9951 7276 7089 68 -717 -283 O ATOM 3512 CB ILE B 243 66.269 2.550 -11.057 1.00 64.92 C ANISOU 3512 CB ILE B 243 10247 7178 7241 -14 -869 -156 C ATOM 3513 CG1 ILE B 243 66.670 3.900 -10.386 1.00 64.98 C ANISOU 3513 CG1 ILE B 243 10269 7171 7248 -35 -880 -95 C ATOM 3514 CG2 ILE B 243 67.540 1.758 -11.447 1.00 66.25 C ANISOU 3514 CG2 ILE B 243 10337 7324 7510 37 -920 -212 C ATOM 3515 CD1 ILE B 243 67.556 3.813 -9.112 1.00 68.38 C ANISOU 3515 CD1 ILE B 243 10761 7486 7736 -34 -999 -82 C ATOM 3516 N VAL B 244 64.526 0.517 -12.731 1.00 60.48 N ANISOU 3516 N VAL B 244 9659 6695 6624 4 -792 -273 N ATOM 3517 CA VAL B 244 64.344 -0.750 -13.458 1.00 60.48 C ANISOU 3517 CA VAL B 244 9633 6700 6647 30 -799 -350 C ATOM 3518 C VAL B 244 63.720 -0.477 -14.853 1.00 66.01 C ANISOU 3518 C VAL B 244 10263 7524 7295 57 -725 -390 C ATOM 3519 O VAL B 244 64.258 -0.958 -15.848 1.00 65.32 O ANISOU 3519 O VAL B 244 10112 7480 7226 110 -715 -448 O ATOM 3520 CB VAL B 244 63.485 -1.764 -12.644 1.00 63.88 C ANISOU 3520 CB VAL B 244 10161 7034 7076 -16 -830 -359 C ATOM 3521 CG1 VAL B 244 63.071 -2.969 -13.484 1.00 64.06 C ANISOU 3521 CG1 VAL B 244 10154 7065 7120 2 -829 -444 C ATOM 3522 CG2 VAL B 244 64.219 -2.216 -11.388 1.00 63.87 C ANISOU 3522 CG2 VAL B 244 10251 6901 7116 -24 -916 -327 C ATOM 3523 N CYS B 245 62.641 0.329 -14.927 1.00 64.53 N ANISOU 3523 N CYS B 245 10090 7389 7038 30 -677 -362 N ATOM 3524 CA CYS B 245 61.947 0.599 -16.186 1.00 65.53 C ANISOU 3524 CA CYS B 245 10168 7625 7105 64 -628 -402 C ATOM 3525 C CYS B 245 62.877 1.266 -17.200 1.00 70.67 C ANISOU 3525 C CYS B 245 10761 8355 7736 121 -584 -395 C ATOM 3526 O CYS B 245 62.972 0.764 -18.323 1.00 71.16 O ANISOU 3526 O CYS B 245 10785 8475 7779 173 -566 -458 O ATOM 3527 CB CYS B 245 60.703 1.451 -15.967 1.00 65.86 C ANISOU 3527 CB CYS B 245 10235 7701 7088 32 -598 -371 C ATOM 3528 SG CYS B 245 59.305 0.549 -15.259 1.00 70.19 S ANISOU 3528 SG CYS B 245 10822 8187 7659 -31 -612 -412 S ATOM 3529 N TYR B 246 63.539 2.378 -16.834 1.00 66.99 N ANISOU 3529 N TYR B 246 10293 7889 7271 110 -561 -323 N ATOM 3530 CA TYR B 246 64.383 3.079 -17.793 1.00 67.39 C ANISOU 3530 CA TYR B 246 10292 8008 7306 151 -498 -311 C ATOM 3531 C TYR B 246 65.672 2.278 -18.131 1.00 70.84 C ANISOU 3531 C TYR B 246 10666 8426 7823 186 -503 -359 C ATOM 3532 O TYR B 246 66.113 2.335 -19.285 1.00 71.07 O ANISOU 3532 O TYR B 246 10651 8525 7826 234 -437 -389 O ATOM 3533 CB TYR B 246 64.759 4.482 -17.306 1.00 69.02 C ANISOU 3533 CB TYR B 246 10507 8208 7509 122 -469 -225 C ATOM 3534 CG TYR B 246 63.593 5.455 -17.277 1.00 71.41 C ANISOU 3534 CG TYR B 246 10861 8547 7724 108 -447 -182 C ATOM 3535 CD1 TYR B 246 62.815 5.676 -18.413 1.00 73.69 C ANISOU 3535 CD1 TYR B 246 11154 8922 7922 152 -407 -205 C ATOM 3536 CD2 TYR B 246 63.394 6.300 -16.188 1.00 71.82 C ANISOU 3536 CD2 TYR B 246 10957 8550 7783 61 -466 -117 C ATOM 3537 CE1 TYR B 246 61.764 6.591 -18.407 1.00 73.84 C ANISOU 3537 CE1 TYR B 246 11214 8973 7870 150 -398 -172 C ATOM 3538 CE2 TYR B 246 62.362 7.241 -16.180 1.00 72.52 C ANISOU 3538 CE2 TYR B 246 11085 8671 7797 56 -444 -83 C ATOM 3539 CZ TYR B 246 61.557 7.395 -17.300 1.00 78.65 C ANISOU 3539 CZ TYR B 246 11858 9531 8494 102 -411 -110 C ATOM 3540 OH TYR B 246 60.534 8.317 -17.304 1.00 76.79 O ANISOU 3540 OH TYR B 246 11657 9324 8194 108 -402 -84 O ATOM 3541 N THR B 247 66.246 1.516 -17.171 1.00 66.28 N ANISOU 3541 N THR B 247 10091 7754 7337 169 -579 -373 N ATOM 3542 CA THR B 247 67.455 0.729 -17.460 1.00 66.14 C ANISOU 3542 CA THR B 247 10007 7714 7410 211 -595 -429 C ATOM 3543 C THR B 247 67.114 -0.349 -18.506 1.00 69.07 C ANISOU 3543 C THR B 247 10364 8128 7752 261 -581 -517 C ATOM 3544 O THR B 247 67.783 -0.402 -19.536 1.00 69.18 O ANISOU 3544 O THR B 247 10316 8203 7768 312 -519 -558 O ATOM 3545 CB THR B 247 68.081 0.121 -16.190 1.00 71.55 C ANISOU 3545 CB THR B 247 10713 8280 8193 195 -701 -428 C ATOM 3546 OG1 THR B 247 67.071 -0.558 -15.450 1.00 73.53 O ANISOU 3546 OG1 THR B 247 11059 8467 8412 162 -760 -426 O ATOM 3547 CG2 THR B 247 68.744 1.170 -15.298 1.00 65.62 C ANISOU 3547 CG2 THR B 247 9958 7489 7487 162 -723 -361 C ATOM 3548 N LEU B 248 66.014 -1.118 -18.295 1.00 64.39 N ANISOU 3548 N LEU B 248 9830 7507 7128 244 -628 -546 N ATOM 3549 CA LEU B 248 65.546 -2.157 -19.230 1.00 64.01 C ANISOU 3549 CA LEU B 248 9775 7490 7056 286 -630 -637 C ATOM 3550 C LEU B 248 65.167 -1.558 -20.592 1.00 68.64 C ANISOU 3550 C LEU B 248 10342 8198 7540 331 -550 -655 C ATOM 3551 O LEU B 248 65.316 -2.228 -21.617 1.00 68.84 O ANISOU 3551 O LEU B 248 10345 8266 7546 390 -533 -734 O ATOM 3552 CB LEU B 248 64.336 -2.939 -18.667 1.00 63.26 C ANISOU 3552 CB LEU B 248 9743 7335 6957 242 -688 -659 C ATOM 3553 CG LEU B 248 64.537 -3.808 -17.410 1.00 66.54 C ANISOU 3553 CG LEU B 248 10212 7616 7454 203 -767 -650 C ATOM 3554 CD1 LEU B 248 63.233 -4.426 -16.971 1.00 65.96 C ANISOU 3554 CD1 LEU B 248 10201 7492 7368 148 -789 -666 C ATOM 3555 CD2 LEU B 248 65.559 -4.902 -17.639 1.00 68.59 C ANISOU 3555 CD2 LEU B 248 10442 7826 7793 258 -813 -717 C ATOM 3556 N MET B 249 64.682 -0.306 -20.595 1.00 65.66 N ANISOU 3556 N MET B 249 9986 7870 7092 309 -506 -584 N ATOM 3557 CA MET B 249 64.296 0.425 -21.801 1.00 66.53 C ANISOU 3557 CA MET B 249 10103 8085 7090 354 -437 -585 C ATOM 3558 C MET B 249 65.522 0.695 -22.682 1.00 71.29 C ANISOU 3558 C MET B 249 10663 8736 7687 404 -351 -589 C ATOM 3559 O MET B 249 65.473 0.436 -23.888 1.00 70.87 O ANISOU 3559 O MET B 249 10615 8751 7560 468 -308 -645 O ATOM 3560 CB MET B 249 63.614 1.739 -21.413 1.00 68.50 C ANISOU 3560 CB MET B 249 10390 8354 7281 317 -418 -500 C ATOM 3561 CG MET B 249 63.076 2.512 -22.577 1.00 72.96 C ANISOU 3561 CG MET B 249 10984 9014 7722 369 -366 -496 C ATOM 3562 SD MET B 249 62.545 4.172 -22.091 1.00 77.25 S ANISOU 3562 SD MET B 249 11572 9569 8212 334 -341 -388 S ATOM 3563 CE MET B 249 64.123 4.922 -21.732 1.00 74.05 C ANISOU 3563 CE MET B 249 11133 9130 7872 305 -270 -311 C ATOM 3564 N ILE B 250 66.620 1.201 -22.071 1.00 68.50 N ANISOU 3564 N ILE B 250 10267 8344 7418 374 -324 -536 N ATOM 3565 CA ILE B 250 67.880 1.498 -22.765 1.00 69.45 C ANISOU 3565 CA ILE B 250 10326 8497 7565 406 -228 -539 C ATOM 3566 C ILE B 250 68.522 0.186 -23.238 1.00 75.49 C ANISOU 3566 C ILE B 250 11040 9253 8388 460 -239 -641 C ATOM 3567 O ILE B 250 68.961 0.109 -24.388 1.00 76.10 O ANISOU 3567 O ILE B 250 11099 9396 8418 517 -149 -684 O ATOM 3568 CB ILE B 250 68.852 2.313 -21.867 1.00 72.27 C ANISOU 3568 CB ILE B 250 10633 8801 8026 353 -216 -470 C ATOM 3569 CG1 ILE B 250 68.220 3.671 -21.461 1.00 71.98 C ANISOU 3569 CG1 ILE B 250 10653 8771 7926 304 -199 -371 C ATOM 3570 CG2 ILE B 250 70.215 2.520 -22.572 1.00 73.91 C ANISOU 3570 CG2 ILE B 250 10753 9036 8293 379 -106 -488 C ATOM 3571 CD1 ILE B 250 69.049 4.522 -20.494 1.00 80.51 C ANISOU 3571 CD1 ILE B 250 11695 9790 9105 248 -205 -307 C ATOM 3572 N LEU B 251 68.545 -0.849 -22.360 1.00 72.51 N ANISOU 3572 N LEU B 251 10653 8791 8106 447 -349 -681 N ATOM 3573 CA LEU B 251 69.102 -2.174 -22.663 1.00 73.12 C ANISOU 3573 CA LEU B 251 10690 8840 8251 500 -382 -782 C ATOM 3574 C LEU B 251 68.466 -2.760 -23.924 1.00 78.69 C ANISOU 3574 C LEU B 251 11429 9618 8853 561 -352 -860 C ATOM 3575 O LEU B 251 69.178 -3.346 -24.743 1.00 79.74 O ANISOU 3575 O LEU B 251 11520 9778 9000 625 -305 -936 O ATOM 3576 CB LEU B 251 68.908 -3.136 -21.484 1.00 72.76 C ANISOU 3576 CB LEU B 251 10671 8681 8295 471 -514 -798 C ATOM 3577 CG LEU B 251 69.638 -2.783 -20.186 1.00 77.71 C ANISOU 3577 CG LEU B 251 11278 9220 9026 427 -572 -739 C ATOM 3578 CD1 LEU B 251 69.176 -3.664 -19.039 1.00 77.72 C ANISOU 3578 CD1 LEU B 251 11351 9108 9071 397 -698 -741 C ATOM 3579 CD2 LEU B 251 71.156 -2.821 -20.355 1.00 81.90 C ANISOU 3579 CD2 LEU B 251 11701 9744 9673 468 -545 -775 C ATOM 3580 N ARG B 252 67.136 -2.551 -24.104 1.00 75.01 N ANISOU 3580 N ARG B 252 11035 9183 8283 546 -377 -848 N ATOM 3581 CA ARG B 252 66.378 -2.996 -25.276 1.00 75.29 C ANISOU 3581 CA ARG B 252 11110 9285 8210 606 -371 -925 C ATOM 3582 C ARG B 252 66.866 -2.286 -26.546 1.00 80.26 C ANISOU 3582 C ARG B 252 11747 10015 8735 668 -246 -921 C ATOM 3583 O ARG B 252 67.060 -2.933 -27.582 1.00 80.53 O ANISOU 3583 O ARG B 252 11787 10092 8719 741 -216 -1008 O ATOM 3584 CB ARG B 252 64.864 -2.746 -25.076 1.00 73.58 C ANISOU 3584 CB ARG B 252 10954 9078 7925 571 -431 -908 C ATOM 3585 CG ARG B 252 63.997 -3.011 -26.327 1.00 82.67 C ANISOU 3585 CG ARG B 252 12148 10305 8958 638 -439 -989 C ATOM 3586 CD ARG B 252 64.051 -4.438 -26.861 1.00 90.79 C ANISOU 3586 CD ARG B 252 13167 11313 10017 688 -489 -1114 C ATOM 3587 NE ARG B 252 63.430 -5.390 -25.945 1.00 96.02 N ANISOU 3587 NE ARG B 252 13824 11880 10781 630 -590 -1148 N ATOM 3588 CZ ARG B 252 62.157 -5.761 -26.012 1.00111.88 C ANISOU 3588 CZ ARG B 252 15855 13882 12772 612 -660 -1199 C ATOM 3589 NH1 ARG B 252 61.370 -5.281 -26.971 1.00101.97 N ANISOU 3589 NH1 ARG B 252 14628 12714 11401 660 -660 -1231 N ATOM 3590 NH2 ARG B 252 61.663 -6.620 -25.135 1.00 98.07 N ANISOU 3590 NH2 ARG B 252 14103 12035 11124 548 -732 -1223 N ATOM 3591 N LEU B 253 67.043 -0.962 -26.463 1.00 76.77 N ANISOU 3591 N LEU B 253 11315 9604 8252 637 -171 -821 N ATOM 3592 CA LEU B 253 67.478 -0.149 -27.590 1.00 77.71 C ANISOU 3592 CA LEU B 253 11460 9804 8263 684 -38 -797 C ATOM 3593 C LEU B 253 68.947 -0.442 -27.930 1.00 84.25 C ANISOU 3593 C LEU B 253 12208 10632 9171 710 61 -831 C ATOM 3594 O LEU B 253 69.308 -0.427 -29.110 1.00 85.02 O ANISOU 3594 O LEU B 253 12329 10795 9179 774 169 -867 O ATOM 3595 CB LEU B 253 67.274 1.344 -27.286 1.00 77.06 C ANISOU 3595 CB LEU B 253 11412 9735 8134 635 10 -676 C ATOM 3596 CG LEU B 253 65.830 1.819 -27.041 1.00 80.58 C ANISOU 3596 CG LEU B 253 11931 10189 8495 619 -72 -643 C ATOM 3597 CD1 LEU B 253 65.804 3.223 -26.480 1.00 80.26 C ANISOU 3597 CD1 LEU B 253 11911 10138 8447 564 -35 -525 C ATOM 3598 CD2 LEU B 253 64.983 1.723 -28.297 1.00 82.66 C ANISOU 3598 CD2 LEU B 253 12279 10530 8599 701 -75 -697 C ATOM 3599 N LYS B 254 69.779 -0.759 -26.913 1.00 81.81 N ANISOU 3599 N LYS B 254 11807 10248 9031 666 23 -828 N ATOM 3600 CA LYS B 254 71.185 -1.108 -27.138 1.00 83.45 C ANISOU 3600 CA LYS B 254 11913 10447 9347 693 101 -875 C ATOM 3601 C LYS B 254 71.302 -2.464 -27.844 1.00 89.84 C ANISOU 3601 C LYS B 254 12714 11266 10155 774 81 -1003 C ATOM 3602 O LYS B 254 72.222 -2.662 -28.642 1.00 90.48 O ANISOU 3602 O LYS B 254 12745 11385 10249 826 193 -1058 O ATOM 3603 CB LYS B 254 71.993 -1.131 -25.825 1.00 85.54 C ANISOU 3603 CB LYS B 254 12084 10620 9798 637 34 -851 C ATOM 3604 CG LYS B 254 72.232 0.251 -25.204 1.00 95.29 C ANISOU 3604 CG LYS B 254 13304 11842 11060 562 75 -738 C ATOM 3605 CD LYS B 254 73.276 0.249 -24.074 1.00102.09 C ANISOU 3605 CD LYS B 254 14059 12618 12112 522 17 -733 C ATOM 3606 CE LYS B 254 74.680 -0.063 -24.559 1.00113.14 C ANISOU 3606 CE LYS B 254 15329 14025 13635 560 106 -804 C ATOM 3607 NZ LYS B 254 75.666 -0.037 -23.450 1.00123.88 N ANISOU 3607 NZ LYS B 254 16580 15299 15189 528 28 -808 N ATOM 3608 N SER B 255 70.364 -3.386 -27.549 1.00 87.37 N ANISOU 3608 N SER B 255 12450 10916 9830 781 -55 -1053 N ATOM 3609 CA SER B 255 70.322 -4.747 -28.085 1.00 88.62 C ANISOU 3609 CA SER B 255 12611 11065 9995 851 -103 -1178 C ATOM 3610 C SER B 255 70.133 -4.776 -29.615 1.00 95.15 C ANISOU 3610 C SER B 255 13498 11991 10665 934 -8 -1238 C ATOM 3611 O SER B 255 70.726 -5.634 -30.276 1.00 96.04 O ANISOU 3611 O SER B 255 13583 12113 10794 1006 24 -1340 O ATOM 3612 CB SER B 255 69.194 -5.535 -27.431 1.00 91.34 C ANISOU 3612 CB SER B 255 13009 11346 10353 822 -259 -1202 C ATOM 3613 N VAL B 256 69.315 -3.863 -30.173 1.00 92.56 N ANISOU 3613 N VAL B 256 13260 11731 10179 933 31 -1181 N ATOM 3614 CA VAL B 256 69.062 -3.837 -31.619 1.00 93.90 C ANISOU 3614 CA VAL B 256 13515 11990 10174 1021 108 -1234 C ATOM 3615 C VAL B 256 70.234 -3.085 -32.323 1.00 99.82 C ANISOU 3615 C VAL B 256 14243 12792 10890 1044 306 -1198 C ATOM 3616 O VAL B 256 70.778 -2.111 -31.787 1.00 98.68 O ANISOU 3616 O VAL B 256 14053 12636 10807 978 378 -1098 O ATOM 3617 CB VAL B 256 67.669 -3.228 -31.982 1.00 97.30 C ANISOU 3617 CB VAL B 256 14060 12465 10445 1026 51 -1200 C ATOM 3618 CG1 VAL B 256 67.485 -1.813 -31.429 1.00 96.21 C ANISOU 3618 CG1 VAL B 256 13937 12331 10287 956 89 -1060 C ATOM 3619 CG2 VAL B 256 67.403 -3.275 -33.488 1.00 98.43 C ANISOU 3619 CG2 VAL B 256 14310 12693 10396 1132 107 -1264 C ATOM 3620 N ARG B 257 70.634 -3.600 -33.505 1.00 99.04 N ANISOU 3620 N ARG B 257 14177 12747 10705 1136 395 -1288 N ATOM 3621 CA ARG B 257 71.702 -3.065 -34.351 1.00100.85 C ANISOU 3621 CA ARG B 257 14399 13030 10888 1169 604 -1275 C ATOM 3622 C ARG B 257 71.403 -3.382 -35.842 1.00106.67 C ANISOU 3622 C ARG B 257 15268 13845 11417 1281 671 -1354 C ATOM 3623 O ARG B 257 71.961 -4.332 -36.407 1.00107.49 O ANISOU 3623 O ARG B 257 15344 13958 11537 1353 709 -1470 O ATOM 3624 CB ARG B 257 73.070 -3.633 -33.918 1.00102.31 C ANISOU 3624 CB ARG B 257 14423 13172 11278 1159 662 -1327 C ATOM 3625 N LEU B 258 70.496 -2.587 -36.461 1.00102.94 N ANISOU 3625 N LEU B 258 14945 13423 10744 1304 674 -1296 N ATOM 3626 CA LEU B 258 70.081 -2.752 -37.857 1.00121.92 C ANISOU 3626 CA LEU B 258 17505 15898 12921 1417 715 -1361 C ATOM 3627 C LEU B 258 70.830 -1.782 -38.766 1.00147.11 C ANISOU 3627 C LEU B 258 20775 19142 15976 1440 952 -1292 C ATOM 3628 O LEU B 258 71.027 -2.069 -39.946 1.00109.39 O ANISOU 3628 O LEU B 258 16103 14418 11042 1538 1050 -1359 O ATOM 3629 CB LEU B 258 68.568 -2.536 -37.994 1.00121.24 C ANISOU 3629 CB LEU B 258 17541 15827 12697 1440 550 -1354 C ATOM 3630 N SER B 262 73.851 2.674 -38.287 1.00120.32 N ANISOU 3630 N SER B 262 17279 15713 12726 1153 1654 -835 N ATOM 3631 CA SER B 262 74.571 2.408 -37.045 1.00119.23 C ANISOU 3631 CA SER B 262 16917 15513 12873 1064 1600 -848 C ATOM 3632 C SER B 262 74.762 3.690 -36.214 1.00122.85 C ANISOU 3632 C SER B 262 17329 15921 13427 947 1632 -710 C ATOM 3633 O SER B 262 74.784 3.614 -34.984 1.00120.85 O ANISOU 3633 O SER B 262 16948 15610 13359 878 1493 -700 O ATOM 3634 CB SER B 262 75.929 1.781 -37.340 1.00124.05 C ANISOU 3634 CB SER B 262 17384 16129 13621 1078 1760 -938 C ATOM 3635 N ARG B 263 74.900 4.857 -36.884 1.00120.91 N ANISOU 3635 N ARG B 263 17200 15689 13049 928 1812 -606 N ATOM 3636 CA ARG B 263 75.099 6.163 -36.237 1.00120.33 C ANISOU 3636 CA ARG B 263 17104 15565 13053 819 1863 -473 C ATOM 3637 C ARG B 263 73.787 6.711 -35.634 1.00122.66 C ANISOU 3637 C ARG B 263 17501 15839 13265 807 1664 -397 C ATOM 3638 O ARG B 263 73.836 7.412 -34.619 1.00121.01 O ANISOU 3638 O ARG B 263 17219 15573 13187 715 1610 -323 O ATOM 3639 CB ARG B 263 75.666 7.180 -37.237 1.00122.08 C ANISOU 3639 CB ARG B 263 17435 15798 13150 806 2134 -387 C ATOM 3640 N GLU B 264 72.627 6.405 -36.271 1.00119.03 N ANISOU 3640 N GLU B 264 17206 15426 12593 902 1557 -423 N ATOM 3641 CA GLU B 264 71.289 6.835 -35.830 1.00117.03 C ANISOU 3641 CA GLU B 264 17048 15163 12254 908 1368 -372 C ATOM 3642 C GLU B 264 70.945 6.209 -34.469 1.00117.41 C ANISOU 3642 C GLU B 264 16948 15168 12494 855 1162 -414 C ATOM 3643 O GLU B 264 70.392 6.895 -33.609 1.00115.58 O ANISOU 3643 O GLU B 264 16714 14896 12305 797 1065 -340 O ATOM 3644 CB GLU B 264 70.223 6.459 -36.886 1.00118.98 C ANISOU 3644 CB GLU B 264 17480 15471 12255 1033 1293 -424 C ATOM 3645 CG GLU B 264 68.798 6.892 -36.546 1.00128.22 C ANISOU 3645 CG GLU B 264 18742 16636 13338 1051 1100 -387 C ATOM 3646 CD GLU B 264 67.719 6.555 -37.562 1.00149.41 C ANISOU 3646 CD GLU B 264 21598 19377 15795 1179 1002 -448 C ATOM 3647 OE1 GLU B 264 66.531 6.522 -37.166 1.00141.44 O ANISOU 3647 OE1 GLU B 264 20609 18365 14768 1197 809 -466 O ATOM 3648 OE2 GLU B 264 68.055 6.297 -38.741 1.00145.37 O ANISOU 3648 OE2 GLU B 264 21197 18910 15128 1263 1116 -488 O ATOM 3649 N LYS B 265 71.287 4.915 -34.277 1.00112.86 N ANISOU 3649 N LYS B 265 16260 14594 12030 878 1102 -532 N ATOM 3650 CA LYS B 265 71.047 4.188 -33.029 1.00110.73 C ANISOU 3650 CA LYS B 265 15864 14273 11935 834 918 -577 C ATOM 3651 C LYS B 265 71.835 4.826 -31.891 1.00112.96 C ANISOU 3651 C LYS B 265 16017 14488 12414 726 939 -506 C ATOM 3652 O LYS B 265 71.258 5.116 -30.848 1.00110.92 O ANISOU 3652 O LYS B 265 15743 14184 12217 672 806 -461 O ATOM 3653 CB LYS B 265 71.416 2.701 -33.174 1.00113.55 C ANISOU 3653 CB LYS B 265 16140 14636 12367 887 873 -714 C ATOM 3654 N ASP B 266 73.131 5.115 -32.133 1.00110.37 N ANISOU 3654 N ASP B 266 15603 14153 12179 696 1114 -498 N ATOM 3655 CA ASP B 266 74.058 5.725 -31.175 1.00109.91 C ANISOU 3655 CA ASP B 266 15407 14031 12324 597 1148 -447 C ATOM 3656 C ASP B 266 73.657 7.174 -30.842 1.00112.23 C ANISOU 3656 C ASP B 266 15777 14296 12568 530 1168 -313 C ATOM 3657 O ASP B 266 73.875 7.616 -29.713 1.00110.64 O ANISOU 3657 O ASP B 266 15492 14031 12515 451 1096 -272 O ATOM 3658 CB ASP B 266 75.492 5.698 -31.730 1.00113.80 C ANISOU 3658 CB ASP B 266 15788 14530 12919 589 1352 -484 C ATOM 3659 CG ASP B 266 76.042 4.309 -32.048 1.00126.55 C ANISOU 3659 CG ASP B 266 17311 16166 14604 658 1346 -623 C ATOM 3660 OD1 ASP B 266 75.270 3.322 -31.956 1.00125.99 O ANISOU 3660 OD1 ASP B 266 17282 16106 14483 718 1187 -691 O ATOM 3661 OD2 ASP B 266 77.233 4.214 -32.413 1.00135.26 O ANISOU 3661 OD2 ASP B 266 18300 17274 15818 653 1506 -667 O ATOM 3662 N ARG B 267 73.072 7.904 -31.821 1.00108.88 N ANISOU 3662 N ARG B 267 15523 13915 11933 568 1258 -249 N ATOM 3663 CA ARG B 267 72.604 9.286 -31.648 1.00107.74 C ANISOU 3663 CA ARG B 267 15477 13742 11716 520 1277 -123 C ATOM 3664 C ARG B 267 71.407 9.322 -30.696 1.00108.28 C ANISOU 3664 C ARG B 267 15577 13788 11777 512 1059 -106 C ATOM 3665 O ARG B 267 71.376 10.160 -29.795 1.00107.09 O ANISOU 3665 O ARG B 267 15400 13580 11707 438 1019 -32 O ATOM 3666 CB ARG B 267 72.237 9.916 -33.002 1.00109.12 C ANISOU 3666 CB ARG B 267 15846 13965 11649 583 1412 -69 C ATOM 3667 N ASN B 268 70.439 8.393 -30.877 1.00103.23 N ANISOU 3667 N ASN B 268 14986 13189 11049 586 923 -181 N ATOM 3668 CA ASN B 268 69.274 8.287 -29.998 1.00101.02 C ANISOU 3668 CA ASN B 268 14722 12889 10773 578 729 -181 C ATOM 3669 C ASN B 268 69.688 7.742 -28.632 1.00102.45 C ANISOU 3669 C ASN B 268 14756 13007 11164 509 626 -210 C ATOM 3670 O ASN B 268 69.302 8.326 -27.623 1.00101.10 O ANISOU 3670 O ASN B 268 14578 12788 11049 451 544 -154 O ATOM 3671 CB ASN B 268 68.168 7.411 -30.602 1.00102.11 C ANISOU 3671 CB ASN B 268 14938 13082 10778 670 620 -264 C ATOM 3672 CG ASN B 268 67.493 7.972 -31.828 1.00125.74 C ANISOU 3672 CG ASN B 268 18101 16131 13545 752 666 -238 C ATOM 3673 OD1 ASN B 268 68.134 8.468 -32.761 1.00122.74 O ANISOU 3673 OD1 ASN B 268 17790 15772 13072 777 830 -200 O ATOM 3674 ND2 ASN B 268 66.181 7.784 -31.904 1.00116.05 N ANISOU 3674 ND2 ASN B 268 16944 14927 12223 805 521 -272 N ATOM 3675 N LEU B 269 70.499 6.654 -28.597 1.00 98.17 N ANISOU 3675 N LEU B 269 14105 12460 10735 520 632 -299 N ATOM 3676 CA LEU B 269 70.971 6.038 -27.351 1.00 96.82 C ANISOU 3676 CA LEU B 269 13808 12222 10759 469 526 -334 C ATOM 3677 C LEU B 269 71.661 7.061 -26.446 1.00100.37 C ANISOU 3677 C LEU B 269 14192 12607 11335 381 551 -254 C ATOM 3678 O LEU B 269 71.342 7.104 -25.260 1.00 99.00 O ANISOU 3678 O LEU B 269 14000 12376 11239 335 422 -235 O ATOM 3679 CB LEU B 269 71.926 4.864 -27.613 1.00 97.48 C ANISOU 3679 CB LEU B 269 13786 12307 10945 505 553 -439 C ATOM 3680 CG LEU B 269 71.291 3.554 -28.074 1.00101.81 C ANISOU 3680 CG LEU B 269 14370 12887 11428 581 469 -541 C ATOM 3681 CD1 LEU B 269 72.348 2.559 -28.486 1.00103.18 C ANISOU 3681 CD1 LEU B 269 14446 13065 11695 624 524 -641 C ATOM 3682 CD2 LEU B 269 70.416 2.960 -26.996 1.00102.16 C ANISOU 3682 CD2 LEU B 269 14420 12880 11518 557 283 -556 C ATOM 3683 N ARG B 270 72.552 7.915 -27.008 1.00 97.32 N ANISOU 3683 N ARG B 270 13783 12227 10965 354 719 -208 N ATOM 3684 CA ARG B 270 73.256 8.953 -26.247 1.00 96.76 C ANISOU 3684 CA ARG B 270 13647 12092 11024 266 753 -137 C ATOM 3685 C ARG B 270 72.262 9.983 -25.677 1.00 98.82 C ANISOU 3685 C ARG B 270 14014 12328 11205 232 680 -43 C ATOM 3686 O ARG B 270 72.310 10.265 -24.479 1.00 97.43 O ANISOU 3686 O ARG B 270 13794 12086 11139 175 577 -20 O ATOM 3687 CB ARG B 270 74.308 9.657 -27.117 1.00 98.23 C ANISOU 3687 CB ARG B 270 13799 12290 11232 242 970 -107 C ATOM 3688 N ARG B 271 71.335 10.494 -26.525 1.00 94.89 N ANISOU 3688 N ARG B 271 13661 11879 10511 276 721 4 N ATOM 3689 CA ARG B 271 70.320 11.491 -26.154 1.00 93.51 C ANISOU 3689 CA ARG B 271 13596 11688 10246 260 660 87 C ATOM 3690 C ARG B 271 69.362 10.962 -25.075 1.00 94.66 C ANISOU 3690 C ARG B 271 13738 11811 10416 259 470 57 C ATOM 3691 O ARG B 271 69.048 11.690 -24.132 1.00 93.26 O ANISOU 3691 O ARG B 271 13574 11583 10278 209 405 112 O ATOM 3692 CB ARG B 271 69.509 11.917 -27.389 1.00 94.17 C ANISOU 3692 CB ARG B 271 13836 11833 10111 333 723 120 C ATOM 3693 N ILE B 272 68.908 9.704 -25.214 1.00 90.23 N ANISOU 3693 N ILE B 272 13165 11284 9834 310 391 -31 N ATOM 3694 CA ILE B 272 67.969 9.076 -24.282 1.00 88.68 C ANISOU 3694 CA ILE B 272 12971 11066 9658 306 232 -65 C ATOM 3695 C ILE B 272 68.690 8.768 -22.955 1.00 91.29 C ANISOU 3695 C ILE B 272 13205 11317 10166 242 159 -75 C ATOM 3696 O ILE B 272 68.149 9.109 -21.906 1.00 89.93 O ANISOU 3696 O ILE B 272 13055 11096 10017 202 70 -41 O ATOM 3697 CB ILE B 272 67.331 7.799 -24.903 1.00 91.83 C ANISOU 3697 CB ILE B 272 13386 11515 9991 376 178 -161 C ATOM 3698 CG1 ILE B 272 66.521 8.172 -26.175 1.00 92.70 C ANISOU 3698 CG1 ILE B 272 13608 11701 9915 449 223 -156 C ATOM 3699 CG2 ILE B 272 66.431 7.070 -23.875 1.00 91.47 C ANISOU 3699 CG2 ILE B 272 13332 11432 9989 356 29 -199 C ATOM 3700 CD1 ILE B 272 66.059 7.012 -27.034 1.00 99.99 C ANISOU 3700 CD1 ILE B 272 14550 12678 10763 527 189 -258 C ATOM 3701 N THR B 273 69.903 8.159 -22.998 1.00 87.65 N ANISOU 3701 N THR B 273 12641 10838 9825 238 196 -123 N ATOM 3702 CA THR B 273 70.665 7.820 -21.784 1.00 86.58 C ANISOU 3702 CA THR B 273 12416 10623 9859 192 110 -142 C ATOM 3703 C THR B 273 70.921 9.098 -20.966 1.00 88.53 C ANISOU 3703 C THR B 273 12664 10813 10162 123 108 -60 C ATOM 3704 O THR B 273 70.659 9.088 -19.765 1.00 87.22 O ANISOU 3704 O THR B 273 12510 10584 10045 91 -10 -48 O ATOM 3705 CB THR B 273 71.975 7.098 -22.129 1.00 95.01 C ANISOU 3705 CB THR B 273 13362 11686 11050 210 161 -213 C ATOM 3706 OG1 THR B 273 71.661 5.917 -22.871 1.00 94.20 O ANISOU 3706 OG1 THR B 273 13272 11631 10888 279 156 -293 O ATOM 3707 CG2 THR B 273 72.780 6.712 -20.887 1.00 93.17 C ANISOU 3707 CG2 THR B 273 13039 11364 10995 178 50 -242 C ATOM 3708 N ARG B 274 71.355 10.204 -21.624 1.00 84.57 N ANISOU 3708 N ARG B 274 12165 10328 9638 102 240 -1 N ATOM 3709 CA ARG B 274 71.583 11.491 -20.960 1.00 83.58 C ANISOU 3709 CA ARG B 274 12048 10146 9563 35 246 77 C ATOM 3710 C ARG B 274 70.299 11.969 -20.281 1.00 85.36 C ANISOU 3710 C ARG B 274 12384 10357 9692 30 150 125 C ATOM 3711 O ARG B 274 70.339 12.331 -19.107 1.00 84.62 O ANISOU 3711 O ARG B 274 12286 10194 9671 -15 60 146 O ATOM 3712 CB ARG B 274 72.095 12.552 -21.952 1.00 84.59 C ANISOU 3712 CB ARG B 274 12187 10295 9660 17 421 136 C ATOM 3713 N LEU B 275 69.154 11.888 -20.995 1.00 81.03 N ANISOU 3713 N LEU B 275 11932 9873 8984 82 160 131 N ATOM 3714 CA LEU B 275 67.831 12.292 -20.508 1.00 80.00 C ANISOU 3714 CA LEU B 275 11896 9741 8760 89 80 163 C ATOM 3715 C LEU B 275 67.428 11.440 -19.282 1.00 80.91 C ANISOU 3715 C LEU B 275 11995 9812 8936 72 -56 119 C ATOM 3716 O LEU B 275 67.029 12.002 -18.258 1.00 79.98 O ANISOU 3716 O LEU B 275 11913 9643 8832 36 -120 156 O ATOM 3717 CB LEU B 275 66.805 12.147 -21.659 1.00 80.76 C ANISOU 3717 CB LEU B 275 12073 9919 8693 161 110 150 C ATOM 3718 CG LEU B 275 65.371 12.702 -21.478 1.00 85.87 C ANISOU 3718 CG LEU B 275 12812 10580 9233 183 48 177 C ATOM 3719 CD1 LEU B 275 64.703 12.894 -22.825 1.00 87.00 C ANISOU 3719 CD1 LEU B 275 13036 10798 9222 260 96 176 C ATOM 3720 CD2 LEU B 275 64.495 11.825 -20.541 1.00 87.70 C ANISOU 3720 CD2 LEU B 275 13032 10797 9494 176 -74 122 C ATOM 3721 N VAL B 276 67.552 10.096 -19.396 1.00 75.69 N ANISOU 3721 N VAL B 276 11290 9165 8305 99 -94 42 N ATOM 3722 CA VAL B 276 67.242 9.111 -18.354 1.00 74.07 C ANISOU 3722 CA VAL B 276 11081 8910 8153 87 -211 -1 C ATOM 3723 C VAL B 276 68.072 9.408 -17.102 1.00 76.79 C ANISOU 3723 C VAL B 276 11396 9164 8618 35 -273 21 C ATOM 3724 O VAL B 276 67.499 9.530 -16.020 1.00 76.09 O ANISOU 3724 O VAL B 276 11363 9023 8524 7 -353 42 O ATOM 3725 CB VAL B 276 67.478 7.658 -18.851 1.00 78.19 C ANISOU 3725 CB VAL B 276 11557 9452 8699 128 -227 -88 C ATOM 3726 CG1 VAL B 276 67.481 6.658 -17.700 1.00 77.54 C ANISOU 3726 CG1 VAL B 276 11473 9293 8694 109 -342 -125 C ATOM 3727 CG2 VAL B 276 66.456 7.264 -19.910 1.00 78.02 C ANISOU 3727 CG2 VAL B 276 11580 9510 8555 181 -201 -123 C ATOM 3728 N LEU B 277 69.408 9.544 -17.250 1.00 73.04 N ANISOU 3728 N LEU B 277 10831 8667 8252 23 -236 13 N ATOM 3729 CA LEU B 277 70.307 9.831 -16.128 1.00 72.42 C ANISOU 3729 CA LEU B 277 10711 8501 8304 -19 -309 20 C ATOM 3730 C LEU B 277 69.848 11.074 -15.365 1.00 75.24 C ANISOU 3730 C LEU B 277 11139 8819 8630 -62 -332 92 C ATOM 3731 O LEU B 277 69.726 11.016 -14.147 1.00 74.07 O ANISOU 3731 O LEU B 277 11033 8600 8510 -83 -439 95 O ATOM 3732 CB LEU B 277 71.765 10.015 -16.595 1.00 73.42 C ANISOU 3732 CB LEU B 277 10713 8621 8562 -28 -243 -3 C ATOM 3733 CG LEU B 277 72.461 8.801 -17.231 1.00 78.83 C ANISOU 3733 CG LEU B 277 11309 9333 9311 18 -224 -86 C ATOM 3734 CD1 LEU B 277 73.831 9.179 -17.767 1.00 80.40 C ANISOU 3734 CD1 LEU B 277 11376 9533 9640 4 -127 -107 C ATOM 3735 CD2 LEU B 277 72.570 7.630 -16.261 1.00 80.48 C ANISOU 3735 CD2 LEU B 277 11516 9476 9585 39 -374 -144 C ATOM 3736 N VAL B 278 69.510 12.155 -16.090 1.00 72.05 N ANISOU 3736 N VAL B 278 10766 8457 8152 -69 -233 149 N ATOM 3737 CA VAL B 278 69.074 13.428 -15.523 1.00 71.70 C ANISOU 3737 CA VAL B 278 10790 8377 8074 -104 -242 216 C ATOM 3738 C VAL B 278 67.743 13.256 -14.747 1.00 75.56 C ANISOU 3738 C VAL B 278 11379 8859 8470 -95 -322 222 C ATOM 3739 O VAL B 278 67.712 13.603 -13.567 1.00 75.38 O ANISOU 3739 O VAL B 278 11396 8767 8480 -125 -401 238 O ATOM 3740 CB VAL B 278 68.934 14.518 -16.625 1.00 75.89 C ANISOU 3740 CB VAL B 278 11348 8955 8531 -101 -114 275 C ATOM 3741 CG1 VAL B 278 68.214 15.760 -16.108 1.00 75.29 C ANISOU 3741 CG1 VAL B 278 11362 8846 8398 -122 -131 341 C ATOM 3742 CG2 VAL B 278 70.295 14.894 -17.200 1.00 76.76 C ANISOU 3742 CG2 VAL B 278 11365 9053 8749 -131 -17 280 C ATOM 3743 N VAL B 279 66.667 12.722 -15.387 1.00 71.99 N ANISOU 3743 N VAL B 279 10966 8475 7911 -53 -301 203 N ATOM 3744 CA VAL B 279 65.330 12.626 -14.767 1.00 71.13 C ANISOU 3744 CA VAL B 279 10936 8366 7725 -48 -354 203 C ATOM 3745 C VAL B 279 65.412 11.840 -13.425 1.00 75.83 C ANISOU 3745 C VAL B 279 11551 8885 8378 -75 -453 176 C ATOM 3746 O VAL B 279 64.823 12.293 -12.436 1.00 75.32 O ANISOU 3746 O VAL B 279 11556 8776 8287 -98 -494 200 O ATOM 3747 CB VAL B 279 64.211 12.022 -15.675 1.00 74.06 C ANISOU 3747 CB VAL B 279 11323 8817 7998 0 -328 166 C ATOM 3748 CG1 VAL B 279 63.892 12.944 -16.845 1.00 74.14 C ANISOU 3748 CG1 VAL B 279 11357 8893 7921 37 -250 200 C ATOM 3749 CG2 VAL B 279 64.538 10.618 -16.164 1.00 73.85 C ANISOU 3749 CG2 VAL B 279 11244 8815 8001 24 -337 97 C ATOM 3750 N VAL B 280 66.161 10.724 -13.373 1.00 72.82 N ANISOU 3750 N VAL B 280 11118 8483 8068 -69 -491 127 N ATOM 3751 CA VAL B 280 66.247 9.958 -12.129 1.00 72.51 C ANISOU 3751 CA VAL B 280 11120 8361 8070 -86 -590 106 C ATOM 3752 C VAL B 280 67.197 10.694 -11.166 1.00 75.60 C ANISOU 3752 C VAL B 280 11515 8671 8539 -115 -651 134 C ATOM 3753 O VAL B 280 66.887 10.759 -9.977 1.00 75.79 O ANISOU 3753 O VAL B 280 11625 8627 8546 -134 -723 148 O ATOM 3754 CB VAL B 280 66.652 8.465 -12.299 1.00 76.88 C ANISOU 3754 CB VAL B 280 11636 8903 8671 -62 -629 42 C ATOM 3755 CG1 VAL B 280 65.616 7.711 -13.125 1.00 76.39 C ANISOU 3755 CG1 VAL B 280 11579 8909 8535 -38 -584 6 C ATOM 3756 CG2 VAL B 280 68.049 8.302 -12.893 1.00 77.58 C ANISOU 3756 CG2 VAL B 280 11616 8997 8863 -43 -617 13 C ATOM 3757 N ALA B 281 68.300 11.301 -11.680 1.00 70.78 N ANISOU 3757 N ALA B 281 10816 8066 8010 -121 -618 140 N ATOM 3758 CA ALA B 281 69.257 12.037 -10.851 1.00 70.30 C ANISOU 3758 CA ALA B 281 10740 7927 8045 -151 -680 154 C ATOM 3759 C ALA B 281 68.552 13.123 -10.057 1.00 72.11 C ANISOU 3759 C ALA B 281 11068 8122 8209 -177 -699 207 C ATOM 3760 O ALA B 281 68.790 13.249 -8.862 1.00 71.54 O ANISOU 3760 O ALA B 281 11051 7966 8164 -191 -799 206 O ATOM 3761 CB ALA B 281 70.356 12.644 -11.707 1.00 71.82 C ANISOU 3761 CB ALA B 281 10813 8140 8334 -163 -605 154 C ATOM 3762 N VAL B 282 67.618 13.841 -10.701 1.00 67.15 N ANISOU 3762 N VAL B 282 10473 7555 7485 -175 -610 246 N ATOM 3763 CA VAL B 282 66.819 14.894 -10.069 1.00 65.72 C ANISOU 3763 CA VAL B 282 10385 7350 7236 -191 -616 291 C ATOM 3764 C VAL B 282 65.910 14.262 -8.970 1.00 67.10 C ANISOU 3764 C VAL B 282 10660 7489 7344 -188 -682 277 C ATOM 3765 O VAL B 282 65.850 14.797 -7.867 1.00 65.36 O ANISOU 3765 O VAL B 282 10518 7199 7116 -205 -741 293 O ATOM 3766 CB VAL B 282 65.993 15.680 -11.130 1.00 68.74 C ANISOU 3766 CB VAL B 282 10778 7810 7531 -173 -512 328 C ATOM 3767 CG1 VAL B 282 65.016 16.650 -10.476 1.00 68.19 C ANISOU 3767 CG1 VAL B 282 10804 7718 7388 -177 -522 364 C ATOM 3768 CG2 VAL B 282 66.907 16.417 -12.102 1.00 68.91 C ANISOU 3768 CG2 VAL B 282 10729 7847 7605 -184 -434 356 C ATOM 3769 N PHE B 283 65.265 13.109 -9.256 1.00 62.94 N ANISOU 3769 N PHE B 283 10137 7002 6776 -169 -668 243 N ATOM 3770 CA PHE B 283 64.384 12.452 -8.289 1.00 62.52 C ANISOU 3770 CA PHE B 283 10178 6910 6665 -175 -706 231 C ATOM 3771 C PHE B 283 65.181 11.935 -7.072 1.00 67.08 C ANISOU 3771 C PHE B 283 10811 7385 7292 -186 -815 220 C ATOM 3772 O PHE B 283 64.692 12.024 -5.942 1.00 66.08 O ANISOU 3772 O PHE B 283 10798 7196 7112 -200 -852 233 O ATOM 3773 CB PHE B 283 63.617 11.296 -8.947 1.00 64.15 C ANISOU 3773 CB PHE B 283 10362 7174 6838 -159 -666 192 C ATOM 3774 CG PHE B 283 62.510 10.711 -8.092 1.00 65.40 C ANISOU 3774 CG PHE B 283 10612 7300 6937 -177 -670 181 C ATOM 3775 CD1 PHE B 283 61.235 11.264 -8.102 1.00 68.10 C ANISOU 3775 CD1 PHE B 283 10983 7682 7211 -181 -610 189 C ATOM 3776 CD2 PHE B 283 62.734 9.590 -7.305 1.00 67.36 C ANISOU 3776 CD2 PHE B 283 10917 7475 7203 -189 -727 162 C ATOM 3777 CE1 PHE B 283 60.206 10.712 -7.328 1.00 68.74 C ANISOU 3777 CE1 PHE B 283 11136 7732 7250 -205 -593 174 C ATOM 3778 CE2 PHE B 283 61.704 9.048 -6.524 1.00 70.10 C ANISOU 3778 CE2 PHE B 283 11356 7783 7494 -214 -709 157 C ATOM 3779 CZ PHE B 283 60.451 9.614 -6.541 1.00 67.89 C ANISOU 3779 CZ PHE B 283 11093 7548 7156 -226 -634 161 C ATOM 3780 N VAL B 284 66.402 11.415 -7.303 1.00 64.85 N ANISOU 3780 N VAL B 284 10453 7080 7106 -175 -866 192 N ATOM 3781 CA VAL B 284 67.263 10.883 -6.243 1.00 65.47 C ANISOU 3781 CA VAL B 284 10576 7058 7241 -170 -991 172 C ATOM 3782 C VAL B 284 67.856 12.053 -5.423 1.00 70.95 C ANISOU 3782 C VAL B 284 11301 7687 7969 -185 -1057 194 C ATOM 3783 O VAL B 284 67.720 12.057 -4.203 1.00 70.63 O ANISOU 3783 O VAL B 284 11385 7565 7886 -187 -1139 201 O ATOM 3784 CB VAL B 284 68.381 9.961 -6.808 1.00 69.43 C ANISOU 3784 CB VAL B 284 10968 7559 7852 -143 -1029 122 C ATOM 3785 CG1 VAL B 284 69.405 9.596 -5.733 1.00 69.94 C ANISOU 3785 CG1 VAL B 284 11068 7514 7992 -127 -1180 96 C ATOM 3786 CG2 VAL B 284 67.785 8.701 -7.425 1.00 68.86 C ANISOU 3786 CG2 VAL B 284 10890 7529 7743 -125 -986 93 C ATOM 3787 N VAL B 285 68.478 13.045 -6.092 1.00 68.31 N ANISOU 3787 N VAL B 285 10866 7384 7704 -199 -1016 205 N ATOM 3788 CA VAL B 285 69.119 14.190 -5.436 1.00 68.71 C ANISOU 3788 CA VAL B 285 10927 7370 7810 -219 -1077 218 C ATOM 3789 C VAL B 285 68.088 14.951 -4.550 1.00 73.44 C ANISOU 3789 C VAL B 285 11672 7940 8293 -230 -1079 256 C ATOM 3790 O VAL B 285 68.456 15.392 -3.466 1.00 73.52 O ANISOU 3790 O VAL B 285 11757 7862 8314 -234 -1181 252 O ATOM 3791 CB VAL B 285 69.789 15.155 -6.472 1.00 72.59 C ANISOU 3791 CB VAL B 285 11288 7904 8390 -243 -995 232 C ATOM 3792 CG1 VAL B 285 70.270 16.453 -5.825 1.00 72.70 C ANISOU 3792 CG1 VAL B 285 11319 7847 8457 -274 -1046 249 C ATOM 3793 CG2 VAL B 285 70.946 14.471 -7.199 1.00 72.94 C ANISOU 3793 CG2 VAL B 285 11185 7964 8564 -234 -992 186 C ATOM 3794 N CYS B 286 66.815 15.052 -4.980 1.00 70.18 N ANISOU 3794 N CYS B 286 11298 7596 7774 -229 -976 283 N ATOM 3795 CA CYS B 286 65.799 15.851 -4.293 1.00 69.89 C ANISOU 3795 CA CYS B 286 11375 7542 7637 -236 -956 312 C ATOM 3796 C CYS B 286 65.064 15.061 -3.178 1.00 75.51 C ANISOU 3796 C CYS B 286 12226 8206 8260 -230 -992 302 C ATOM 3797 O CYS B 286 64.756 15.676 -2.152 1.00 76.56 O ANISOU 3797 O CYS B 286 12474 8280 8336 -234 -1026 314 O ATOM 3798 CB CYS B 286 64.787 16.387 -5.297 1.00 69.50 C ANISOU 3798 CB CYS B 286 11292 7587 7530 -231 -833 336 C ATOM 3799 SG CYS B 286 65.472 17.583 -6.477 1.00 73.62 S ANISOU 3799 SG CYS B 286 11706 8146 8120 -239 -773 367 S ATOM 3800 N TRP B 287 64.713 13.771 -3.376 1.00 71.40 N ANISOU 3800 N TRP B 287 11704 7706 7717 -224 -972 282 N ATOM 3801 CA TRP B 287 63.914 13.075 -2.360 1.00 71.27 C ANISOU 3801 CA TRP B 287 11829 7640 7612 -228 -978 281 C ATOM 3802 C TRP B 287 64.744 12.296 -1.333 1.00 74.64 C ANISOU 3802 C TRP B 287 12350 7959 8052 -217 -1104 267 C ATOM 3803 O TRP B 287 64.312 12.220 -0.183 1.00 74.38 O ANISOU 3803 O TRP B 287 12475 7853 7932 -220 -1129 278 O ATOM 3804 CB TRP B 287 62.939 12.097 -2.992 1.00 70.15 C ANISOU 3804 CB TRP B 287 11658 7560 7435 -235 -886 266 C ATOM 3805 CG TRP B 287 61.835 12.773 -3.734 1.00 71.04 C ANISOU 3805 CG TRP B 287 11718 7764 7510 -237 -776 272 C ATOM 3806 CD1 TRP B 287 61.712 12.894 -5.084 1.00 73.67 C ANISOU 3806 CD1 TRP B 287 11926 8191 7872 -223 -718 263 C ATOM 3807 CD2 TRP B 287 60.767 13.545 -3.161 1.00 70.92 C ANISOU 3807 CD2 TRP B 287 11777 7748 7419 -246 -720 286 C ATOM 3808 NE1 TRP B 287 60.577 13.610 -5.394 1.00 73.06 N ANISOU 3808 NE1 TRP B 287 11845 8173 7743 -218 -641 268 N ATOM 3809 CE2 TRP B 287 59.988 14.038 -4.231 1.00 74.78 C ANISOU 3809 CE2 TRP B 287 12175 8336 7904 -232 -638 280 C ATOM 3810 CE3 TRP B 287 60.369 13.838 -1.842 1.00 72.42 C ANISOU 3810 CE3 TRP B 287 12111 7864 7540 -257 -729 297 C ATOM 3811 CZ2 TRP B 287 58.835 14.810 -4.025 1.00 74.11 C ANISOU 3811 CZ2 TRP B 287 12120 8276 7764 -228 -573 281 C ATOM 3812 CZ3 TRP B 287 59.230 14.599 -1.639 1.00 73.85 C ANISOU 3812 CZ3 TRP B 287 12323 8074 7663 -258 -649 299 C ATOM 3813 CH2 TRP B 287 58.466 15.062 -2.718 1.00 74.24 C ANISOU 3813 CH2 TRP B 287 12264 8221 7725 -243 -574 288 C ATOM 3814 N THR B 288 65.899 11.714 -1.723 1.00 71.09 N ANISOU 3814 N THR B 288 11812 7494 7703 -198 -1182 240 N ATOM 3815 CA THR B 288 66.755 10.929 -0.817 1.00 71.32 C ANISOU 3815 CA THR B 288 11923 7418 7756 -173 -1323 218 C ATOM 3816 C THR B 288 67.134 11.732 0.461 1.00 75.78 C ANISOU 3816 C THR B 288 12617 7887 8289 -164 -1434 226 C ATOM 3817 O THR B 288 67.097 11.123 1.531 1.00 75.79 O ANISOU 3817 O THR B 288 12782 7796 8219 -145 -1512 228 O ATOM 3818 CB THR B 288 68.039 10.458 -1.529 1.00 78.92 C ANISOU 3818 CB THR B 288 12736 8389 8861 -148 -1391 177 C ATOM 3819 OG1 THR B 288 67.699 9.761 -2.727 1.00 79.76 O ANISOU 3819 OG1 THR B 288 12733 8585 8988 -150 -1290 165 O ATOM 3820 CG2 THR B 288 68.922 9.578 -0.650 1.00 77.07 C ANISOU 3820 CG2 THR B 288 12579 8044 8661 -108 -1553 146 C ATOM 3821 N PRO B 289 67.473 13.061 0.424 1.00 72.15 N ANISOU 3821 N PRO B 289 12107 7436 7870 -174 -1445 232 N ATOM 3822 CA PRO B 289 67.882 13.730 1.671 1.00 72.44 C ANISOU 3822 CA PRO B 289 12273 7372 7879 -160 -1569 228 C ATOM 3823 C PRO B 289 66.767 13.826 2.712 1.00 76.04 C ANISOU 3823 C PRO B 289 12935 7786 8169 -163 -1531 257 C ATOM 3824 O PRO B 289 67.004 13.503 3.878 1.00 76.06 O ANISOU 3824 O PRO B 289 13106 7687 8107 -135 -1642 250 O ATOM 3825 CB PRO B 289 68.277 15.141 1.210 1.00 73.91 C ANISOU 3825 CB PRO B 289 12348 7587 8147 -182 -1553 230 C ATOM 3826 CG PRO B 289 68.523 15.029 -0.222 1.00 77.48 C ANISOU 3826 CG PRO B 289 12607 8135 8696 -198 -1459 228 C ATOM 3827 CD PRO B 289 67.596 13.985 -0.724 1.00 72.55 C ANISOU 3827 CD PRO B 289 11994 7575 7997 -196 -1358 240 C ATOM 3828 N ILE B 290 65.567 14.265 2.298 1.00 72.28 N ANISOU 3828 N ILE B 290 12450 7387 7624 -190 -1376 284 N ATOM 3829 CA ILE B 290 64.474 14.527 3.218 1.00 72.47 C ANISOU 3829 CA ILE B 290 12646 7382 7506 -196 -1315 305 C ATOM 3830 C ILE B 290 63.814 13.193 3.679 1.00 77.28 C ANISOU 3830 C ILE B 290 13377 7961 8027 -201 -1271 313 C ATOM 3831 O ILE B 290 63.450 13.116 4.856 1.00 77.51 O ANISOU 3831 O ILE B 290 13603 7909 7940 -194 -1286 324 O ATOM 3832 CB ILE B 290 63.423 15.503 2.615 1.00 74.87 C ANISOU 3832 CB ILE B 290 12886 7776 7785 -217 -1172 322 C ATOM 3833 CG1 ILE B 290 62.388 15.940 3.675 1.00 75.55 C ANISOU 3833 CG1 ILE B 290 13146 7825 7737 -218 -1114 332 C ATOM 3834 CG2 ILE B 290 62.763 14.986 1.331 1.00 74.85 C ANISOU 3834 CG2 ILE B 290 12740 7885 7816 -234 -1047 323 C ATOM 3835 CD1 ILE B 290 63.011 16.604 4.939 1.00 81.73 C ANISOU 3835 CD1 ILE B 290 14085 8497 8471 -193 -1244 325 C ATOM 3836 N HIS B 291 63.693 12.156 2.809 1.00 74.00 N ANISOU 3836 N HIS B 291 12860 7597 7660 -212 -1218 306 N ATOM 3837 CA HIS B 291 63.099 10.880 3.240 1.00 74.31 C ANISOU 3837 CA HIS B 291 13015 7594 7627 -224 -1176 314 C ATOM 3838 C HIS B 291 63.948 10.225 4.321 1.00 78.55 C ANISOU 3838 C HIS B 291 13718 7998 8128 -189 -1327 314 C ATOM 3839 O HIS B 291 63.385 9.730 5.292 1.00 78.23 O ANISOU 3839 O HIS B 291 13874 7881 7969 -196 -1302 335 O ATOM 3840 CB HIS B 291 62.894 9.899 2.086 1.00 74.91 C ANISOU 3840 CB HIS B 291 12948 7741 7772 -240 -1108 298 C ATOM 3841 CG HIS B 291 61.639 10.130 1.301 1.00 77.98 C ANISOU 3841 CG HIS B 291 13245 8235 8149 -274 -946 297 C ATOM 3842 ND1 HIS B 291 61.652 10.789 0.087 1.00 79.18 N ANISOU 3842 ND1 HIS B 291 13217 8495 8373 -269 -905 285 N ATOM 3843 CD2 HIS B 291 60.368 9.759 1.583 1.00 79.95 C ANISOU 3843 CD2 HIS B 291 13561 8490 8328 -309 -822 301 C ATOM 3844 CE1 HIS B 291 60.400 10.776 -0.339 1.00 78.25 C ANISOU 3844 CE1 HIS B 291 13062 8446 8225 -293 -777 278 C ATOM 3845 NE2 HIS B 291 59.591 10.175 0.533 1.00 79.00 N ANISOU 3845 NE2 HIS B 291 13290 8484 8244 -321 -720 283 N ATOM 3846 N ILE B 292 65.295 10.265 4.173 1.00 75.75 N ANISOU 3846 N ILE B 292 13289 7614 7876 -151 -1484 287 N ATOM 3847 CA ILE B 292 66.258 9.726 5.141 1.00 76.69 C ANISOU 3847 CA ILE B 292 13549 7608 7984 -101 -1665 274 C ATOM 3848 C ILE B 292 66.229 10.584 6.413 1.00 82.25 C ANISOU 3848 C ILE B 292 14442 8229 8580 -82 -1735 284 C ATOM 3849 O ILE B 292 66.201 10.027 7.505 1.00 83.09 O ANISOU 3849 O ILE B 292 14772 8226 8572 -55 -1802 298 O ATOM 3850 CB ILE B 292 67.696 9.642 4.535 1.00 79.78 C ANISOU 3850 CB ILE B 292 13767 8002 8544 -64 -1808 226 C ATOM 3851 CG1 ILE B 292 67.759 8.652 3.342 1.00 80.07 C ANISOU 3851 CG1 ILE B 292 13642 8109 8673 -72 -1744 210 C ATOM 3852 CG2 ILE B 292 68.760 9.292 5.584 1.00 81.41 C ANISOU 3852 CG2 ILE B 292 14106 8074 8752 1 -2028 199 C ATOM 3853 CD1 ILE B 292 67.346 7.110 3.628 1.00 91.77 C ANISOU 3853 CD1 ILE B 292 15253 9528 10087 -64 -1734 221 C ATOM 3854 N PHE B 293 66.192 11.918 6.275 1.00 79.27 N ANISOU 3854 N PHE B 293 13992 7898 8228 -94 -1714 279 N ATOM 3855 CA PHE B 293 66.187 12.822 7.427 1.00 80.31 C ANISOU 3855 CA PHE B 293 14295 7954 8264 -74 -1784 280 C ATOM 3856 C PHE B 293 64.975 12.547 8.335 1.00 84.00 C ANISOU 3856 C PHE B 293 14991 8382 8544 -87 -1669 317 C ATOM 3857 O PHE B 293 65.151 12.337 9.537 1.00 84.75 O ANISOU 3857 O PHE B 293 15316 8363 8521 -50 -1764 321 O ATOM 3858 CB PHE B 293 66.186 14.292 6.975 1.00 81.92 C ANISOU 3858 CB PHE B 293 14369 8222 8533 -93 -1750 271 C ATOM 3859 CG PHE B 293 66.679 15.247 8.035 1.00 84.86 C ANISOU 3859 CG PHE B 293 14872 8504 8866 -61 -1887 249 C ATOM 3860 CD1 PHE B 293 65.847 15.649 9.075 1.00 88.62 C ANISOU 3860 CD1 PHE B 293 15564 8932 9175 -53 -1842 266 C ATOM 3861 CD2 PHE B 293 67.962 15.778 7.971 1.00 87.95 C ANISOU 3861 CD2 PHE B 293 15163 8858 9395 -40 -2056 205 C ATOM 3862 CE1 PHE B 293 66.306 16.527 10.057 1.00 90.54 C ANISOU 3862 CE1 PHE B 293 15938 9088 9374 -17 -1977 239 C ATOM 3863 CE2 PHE B 293 68.412 16.675 8.940 1.00 91.85 C ANISOU 3863 CE2 PHE B 293 15773 9264 9862 -10 -2194 175 C ATOM 3864 CZ PHE B 293 67.581 17.043 9.976 1.00 90.34 C ANISOU 3864 CZ PHE B 293 15810 9024 9489 4 -2159 192 C ATOM 3865 N ILE B 294 63.761 12.524 7.749 1.00 78.99 N ANISOU 3865 N ILE B 294 14293 7839 7882 -137 -1466 339 N ATOM 3866 CA ILE B 294 62.498 12.270 8.453 1.00 78.63 C ANISOU 3866 CA ILE B 294 14421 7772 7685 -164 -1316 368 C ATOM 3867 C ILE B 294 62.531 10.851 9.079 1.00 83.50 C ANISOU 3867 C ILE B 294 15213 8291 8222 -158 -1339 389 C ATOM 3868 O ILE B 294 62.131 10.690 10.237 1.00 83.90 O ANISOU 3868 O ILE B 294 15511 8249 8120 -150 -1319 411 O ATOM 3869 CB ILE B 294 61.297 12.455 7.473 1.00 80.35 C ANISOU 3869 CB ILE B 294 14476 8116 7938 -217 -1110 371 C ATOM 3870 CG1 ILE B 294 61.214 13.934 7.026 1.00 80.02 C ANISOU 3870 CG1 ILE B 294 14310 8148 7945 -212 -1094 357 C ATOM 3871 CG2 ILE B 294 59.963 12.002 8.106 1.00 81.37 C ANISOU 3871 CG2 ILE B 294 14751 8226 7940 -255 -937 390 C ATOM 3872 CD1 ILE B 294 60.150 14.276 6.053 1.00 86.67 C ANISOU 3872 CD1 ILE B 294 14994 9109 8827 -245 -929 353 C ATOM 3873 N LEU B 295 63.055 9.854 8.332 1.00 79.89 N ANISOU 3873 N LEU B 295 14642 7846 7866 -158 -1384 381 N ATOM 3874 CA LEU B 295 63.151 8.456 8.765 1.00 80.39 C ANISOU 3874 CA LEU B 295 14853 7816 7877 -151 -1414 399 C ATOM 3875 C LEU B 295 64.064 8.315 9.979 1.00 86.65 C ANISOU 3875 C LEU B 295 15875 8463 8584 -82 -1611 402 C ATOM 3876 O LEU B 295 63.669 7.692 10.965 1.00 87.88 O ANISOU 3876 O LEU B 295 16286 8512 8590 -78 -1588 436 O ATOM 3877 CB LEU B 295 63.680 7.580 7.613 1.00 79.60 C ANISOU 3877 CB LEU B 295 14555 7765 7925 -151 -1446 377 C ATOM 3878 CG LEU B 295 63.582 6.071 7.782 1.00 84.62 C ANISOU 3878 CG LEU B 295 15302 8321 8529 -156 -1441 394 C ATOM 3879 CD1 LEU B 295 62.127 5.614 7.705 1.00 84.43 C ANISOU 3879 CD1 LEU B 295 15316 8323 8438 -233 -1216 421 C ATOM 3880 CD2 LEU B 295 64.364 5.363 6.694 1.00 86.92 C ANISOU 3880 CD2 LEU B 295 15395 8654 8976 -136 -1515 358 C ATOM 3881 N VAL B 296 65.272 8.911 9.913 1.00 83.47 N ANISOU 3881 N VAL B 296 15387 8050 8277 -27 -1804 362 N ATOM 3882 CA VAL B 296 66.275 8.841 10.977 1.00 84.91 C ANISOU 3882 CA VAL B 296 15757 8099 8407 51 -2031 346 C ATOM 3883 C VAL B 296 65.744 9.588 12.219 1.00 90.64 C ANISOU 3883 C VAL B 296 16734 8757 8949 63 -2013 366 C ATOM 3884 O VAL B 296 65.858 9.050 13.323 1.00 91.28 O ANISOU 3884 O VAL B 296 17092 8708 8884 108 -2097 385 O ATOM 3885 CB VAL B 296 67.657 9.388 10.512 1.00 88.66 C ANISOU 3885 CB VAL B 296 16035 8590 9061 97 -2228 284 C ATOM 3886 CG1 VAL B 296 68.627 9.563 11.682 1.00 90.05 C ANISOU 3886 CG1 VAL B 296 16398 8630 9187 181 -2476 252 C ATOM 3887 CG2 VAL B 296 68.266 8.479 9.446 1.00 87.93 C ANISOU 3887 CG2 VAL B 296 15736 8541 9130 99 -2255 260 C ATOM 3888 N GLU B 297 65.122 10.783 12.035 1.00 87.67 N ANISOU 3888 N GLU B 297 16277 8464 8570 26 -1897 362 N ATOM 3889 CA GLU B 297 64.548 11.586 13.133 1.00 88.68 C ANISOU 3889 CA GLU B 297 16624 8541 8530 37 -1861 373 C ATOM 3890 C GLU B 297 63.462 10.801 13.889 1.00 94.61 C ANISOU 3890 C GLU B 297 17622 9233 9092 10 -1696 425 C ATOM 3891 O GLU B 297 63.299 10.988 15.098 1.00 95.91 O ANISOU 3891 O GLU B 297 18062 9298 9080 45 -1722 438 O ATOM 3892 CB GLU B 297 63.960 12.903 12.605 1.00 88.89 C ANISOU 3892 CB GLU B 297 16488 8679 8608 -2 -1740 359 C ATOM 3893 N ALA B 298 62.742 9.913 13.176 1.00 90.50 N ANISOU 3893 N ALA B 298 17007 8769 8612 -52 -1528 452 N ATOM 3894 CA ALA B 298 61.686 9.074 13.740 1.00 90.88 C ANISOU 3894 CA ALA B 298 17252 8764 8516 -96 -1347 500 C ATOM 3895 C ALA B 298 62.259 7.825 14.435 1.00 95.45 C ANISOU 3895 C ALA B 298 18063 9196 9009 -55 -1466 530 C ATOM 3896 O ALA B 298 61.688 7.378 15.433 1.00 97.09 O ANISOU 3896 O ALA B 298 18553 9301 9034 -62 -1381 573 O ATOM 3897 CB ALA B 298 60.721 8.656 12.652 1.00 90.57 C ANISOU 3897 CB ALA B 298 16998 8839 8576 -180 -1135 505 C ATOM 3898 N LEU B 299 63.382 7.268 13.915 1.00 90.10 N ANISOU 3898 N LEU B 299 17274 8502 8458 -10 -1657 506 N ATOM 3899 CA LEU B 299 64.039 6.083 14.496 1.00 90.17 C ANISOU 3899 CA LEU B 299 17487 8367 8405 44 -1802 527 C ATOM 3900 C LEU B 299 64.924 6.464 15.702 1.00 95.86 C ANISOU 3900 C LEU B 299 18456 8959 9008 146 -2037 514 C ATOM 3901 O LEU B 299 65.183 5.619 16.562 1.00 96.88 O ANISOU 3901 O LEU B 299 18863 8942 9005 196 -2130 544 O ATOM 3902 CB LEU B 299 64.887 5.352 13.442 1.00 88.88 C ANISOU 3902 CB LEU B 299 17093 8240 8436 62 -1916 494 C ATOM 3903 CG LEU B 299 64.132 4.708 12.280 1.00 91.37 C ANISOU 3903 CG LEU B 299 17199 8658 8859 -23 -1721 502 C ATOM 3904 CD1 LEU B 299 65.078 4.312 11.178 1.00 90.38 C ANISOU 3904 CD1 LEU B 299 16817 8589 8934 5 -1844 455 C ATOM 3905 CD2 LEU B 299 63.274 3.536 12.743 1.00 94.03 C ANISOU 3905 CD2 LEU B 299 17748 8904 9076 -70 -1576 559 C ATOM 3906 N GLY B 300 65.356 7.728 15.747 1.00 92.13 N ANISOU 3906 N GLY B 300 17890 8535 8582 175 -2133 467 N ATOM 3907 CA GLY B 300 66.196 8.267 16.809 1.00118.01 C ANISOU 3907 CA GLY B 300 21366 11702 11769 270 -2367 436 C ATOM 3908 C GLY B 300 66.001 9.745 17.071 1.00132.05 C ANISOU 3908 C GLY B 300 23115 13532 13525 266 -2351 405 C ATOM 3909 O GLY B 300 66.339 10.237 18.148 1.00 94.29 O ANISOU 3909 O GLY B 300 18563 8651 8611 335 -2491 387 O ATOM 3910 N SER B 305 68.955 21.061 17.420 1.00 97.91 N ANISOU 3910 N SER B 305 18075 9321 9805 329 -3040 -46 N ATOM 3911 CA SER B 305 70.064 21.916 17.027 1.00 98.06 C ANISOU 3911 CA SER B 305 17888 9322 10049 320 -3213 -116 C ATOM 3912 C SER B 305 69.553 22.991 16.095 1.00101.40 C ANISOU 3912 C SER B 305 18104 9844 10582 244 -3037 -97 C ATOM 3913 O SER B 305 68.467 22.863 15.557 1.00100.34 O ANISOU 3913 O SER B 305 17936 9806 10384 202 -2798 -33 O ATOM 3914 CB SER B 305 71.148 21.094 16.334 1.00101.26 C ANISOU 3914 CB SER B 305 18086 9736 10651 316 -3333 -136 C ATOM 3915 N THR B 306 70.309 24.069 15.932 1.00 98.01 N ANISOU 3915 N THR B 306 17543 9381 10314 229 -3158 -156 N ATOM 3916 CA THR B 306 69.908 25.143 15.015 1.00 96.34 C ANISOU 3916 CA THR B 306 17141 9247 10215 160 -3003 -136 C ATOM 3917 C THR B 306 70.288 24.683 13.604 1.00 98.84 C ANISOU 3917 C THR B 306 17162 9663 10729 95 -2914 -103 C ATOM 3918 O THR B 306 69.467 24.781 12.688 1.00 97.36 O ANISOU 3918 O THR B 306 16863 9583 10546 46 -2697 -42 O ATOM 3919 CB THR B 306 70.586 26.466 15.393 1.00101.23 C ANISOU 3919 CB THR B 306 17746 9779 10936 163 -3163 -211 C ATOM 3920 N ALA B 307 71.510 24.115 13.455 1.00 95.35 N ANISOU 3920 N ALA B 307 16603 9183 10443 105 -3085 -148 N ATOM 3921 CA ALA B 307 72.034 23.585 12.194 1.00 93.97 C ANISOU 3921 CA ALA B 307 16156 9090 10458 54 -3021 -129 C ATOM 3922 C ALA B 307 71.196 22.399 11.710 1.00 96.05 C ANISOU 3922 C ALA B 307 16435 9446 10614 49 -2846 -57 C ATOM 3923 O ALA B 307 70.945 22.284 10.507 1.00 94.75 O ANISOU 3923 O ALA B 307 16077 9388 10537 -5 -2681 -14 O ATOM 3924 CB ALA B 307 73.485 23.168 12.363 1.00 95.87 C ANISOU 3924 CB ALA B 307 16301 9256 10870 81 -3258 -208 C ATOM 3925 N ALA B 308 70.735 21.537 12.654 1.00 91.83 N ANISOU 3925 N ALA B 308 16144 8866 9883 106 -2877 -43 N ATOM 3926 CA ALA B 308 69.879 20.381 12.368 1.00 89.99 C ANISOU 3926 CA ALA B 308 15959 8699 9534 100 -2716 22 C ATOM 3927 C ALA B 308 68.499 20.828 11.857 1.00 91.49 C ANISOU 3927 C ALA B 308 16134 8989 9638 52 -2458 82 C ATOM 3928 O ALA B 308 67.919 20.159 11.000 1.00 89.93 O ANISOU 3928 O ALA B 308 15833 8886 9450 17 -2296 128 O ATOM 3929 CB ALA B 308 69.725 19.525 13.612 1.00 91.62 C ANISOU 3929 CB ALA B 308 16457 8809 9545 169 -2810 22 C ATOM 3930 N LEU B 309 67.991 21.974 12.363 1.00 87.12 N ANISOU 3930 N LEU B 309 15679 8413 9011 56 -2431 73 N ATOM 3931 CA LEU B 309 66.708 22.519 11.933 1.00 85.13 C ANISOU 3931 CA LEU B 309 15409 8248 8688 22 -2207 116 C ATOM 3932 C LEU B 309 66.858 23.171 10.548 1.00 87.04 C ANISOU 3932 C LEU B 309 15379 8581 9112 -34 -2122 131 C ATOM 3933 O LEU B 309 65.971 23.013 9.712 1.00 85.65 O ANISOU 3933 O LEU B 309 15112 8507 8924 -64 -1936 175 O ATOM 3934 CB LEU B 309 66.165 23.525 12.967 1.00 85.62 C ANISOU 3934 CB LEU B 309 15672 8247 8613 54 -2216 93 C ATOM 3935 CG LEU B 309 64.722 24.022 12.744 1.00 89.35 C ANISOU 3935 CG LEU B 309 16162 8797 8989 36 -1987 127 C ATOM 3936 CD1 LEU B 309 63.708 22.888 12.912 1.00 88.90 C ANISOU 3936 CD1 LEU B 309 16205 8783 8791 33 -1828 169 C ATOM 3937 CD2 LEU B 309 64.374 25.126 13.713 1.00 93.00 C ANISOU 3937 CD2 LEU B 309 16801 9190 9344 73 -2017 92 C ATOM 3938 N SER B 310 67.982 23.882 10.299 1.00 83.04 N ANISOU 3938 N SER B 310 14747 8032 8774 -47 -2258 91 N ATOM 3939 CA SER B 310 68.249 24.538 9.013 1.00 81.46 C ANISOU 3939 CA SER B 310 14306 7901 8746 -103 -2179 108 C ATOM 3940 C SER B 310 68.495 23.506 7.920 1.00 82.87 C ANISOU 3940 C SER B 310 14308 8166 9015 -130 -2107 136 C ATOM 3941 O SER B 310 68.007 23.676 6.800 1.00 81.66 O ANISOU 3941 O SER B 310 14017 8109 8902 -166 -1949 178 O ATOM 3942 CB SER B 310 69.446 25.471 9.121 1.00 86.32 C ANISOU 3942 CB SER B 310 14840 8432 9525 -118 -2340 54 C ATOM 3943 OG SER B 310 70.629 24.718 9.333 1.00 96.90 O ANISOU 3943 OG SER B 310 16129 9720 10970 -103 -2510 7 O ATOM 3944 N SER B 311 69.246 22.428 8.245 1.00 78.68 N ANISOU 3944 N SER B 311 13789 7595 8510 -104 -2229 109 N ATOM 3945 CA SER B 311 69.513 21.349 7.290 1.00 77.25 C ANISOU 3945 CA SER B 311 13455 7488 8410 -120 -2173 126 C ATOM 3946 C SER B 311 68.206 20.645 6.899 1.00 79.56 C ANISOU 3946 C SER B 311 13790 7870 8567 -126 -1983 182 C ATOM 3947 O SER B 311 68.025 20.355 5.719 1.00 79.34 O ANISOU 3947 O SER B 311 13600 7939 8606 -157 -1862 209 O ATOM 3948 CB SER B 311 70.509 20.347 7.855 1.00 80.52 C ANISOU 3948 CB SER B 311 13902 7827 8865 -78 -2356 80 C ATOM 3949 OG SER B 311 70.002 19.766 9.041 1.00 89.56 O ANISOU 3949 OG SER B 311 15299 8905 9822 -27 -2410 84 O ATOM 3950 N TYR B 312 67.270 20.437 7.867 1.00 74.24 N ANISOU 3950 N TYR B 312 13333 7166 7708 -100 -1950 196 N ATOM 3951 CA TYR B 312 65.954 19.823 7.617 1.00 72.00 C ANISOU 3951 CA TYR B 312 13093 6958 7305 -112 -1765 239 C ATOM 3952 C TYR B 312 65.145 20.632 6.589 1.00 74.74 C ANISOU 3952 C TYR B 312 13305 7409 7684 -145 -1599 266 C ATOM 3953 O TYR B 312 64.646 20.052 5.625 1.00 73.16 O ANISOU 3953 O TYR B 312 12990 7301 7506 -166 -1477 290 O ATOM 3954 CB TYR B 312 65.140 19.688 8.925 1.00 72.47 C ANISOU 3954 CB TYR B 312 13413 6953 7169 -83 -1749 244 C ATOM 3955 CG TYR B 312 63.682 19.322 8.718 1.00 71.29 C ANISOU 3955 CG TYR B 312 13296 6878 6913 -104 -1539 278 C ATOM 3956 CD1 TYR B 312 63.299 18.008 8.469 1.00 72.38 C ANISOU 3956 CD1 TYR B 312 13433 7045 7022 -119 -1465 300 C ATOM 3957 CD2 TYR B 312 62.680 20.281 8.838 1.00 71.40 C ANISOU 3957 CD2 TYR B 312 13344 6924 6861 -108 -1422 282 C ATOM 3958 CE1 TYR B 312 61.958 17.665 8.292 1.00 71.97 C ANISOU 3958 CE1 TYR B 312 13397 7056 6892 -145 -1274 321 C ATOM 3959 CE2 TYR B 312 61.337 19.952 8.666 1.00 71.78 C ANISOU 3959 CE2 TYR B 312 13404 7040 6831 -126 -1233 301 C ATOM 3960 CZ TYR B 312 60.978 18.641 8.396 1.00 78.22 C ANISOU 3960 CZ TYR B 312 14206 7884 7629 -148 -1158 319 C ATOM 3961 OH TYR B 312 59.650 18.311 8.235 1.00 77.01 O ANISOU 3961 OH TYR B 312 14051 7793 7418 -173 -973 327 O ATOM 3962 N TYR B 313 65.012 21.953 6.794 1.00 71.97 N ANISOU 3962 N TYR B 313 12976 7037 7333 -144 -1603 259 N ATOM 3963 CA TYR B 313 64.231 22.787 5.892 1.00 71.61 C ANISOU 3963 CA TYR B 313 12827 7075 7308 -164 -1461 285 C ATOM 3964 C TYR B 313 64.981 23.001 4.572 1.00 76.18 C ANISOU 3964 C TYR B 313 13190 7707 8049 -195 -1452 297 C ATOM 3965 O TYR B 313 64.329 23.276 3.558 1.00 75.05 O ANISOU 3965 O TYR B 313 12946 7652 7918 -208 -1324 326 O ATOM 3966 CB TYR B 313 63.853 24.119 6.532 1.00 73.17 C ANISOU 3966 CB TYR B 313 13125 7223 7454 -148 -1470 272 C ATOM 3967 CG TYR B 313 62.720 23.942 7.521 1.00 75.41 C ANISOU 3967 CG TYR B 313 13597 7492 7565 -119 -1398 267 C ATOM 3968 CD1 TYR B 313 61.396 23.908 7.094 1.00 77.35 C ANISOU 3968 CD1 TYR B 313 13818 7824 7749 -121 -1224 285 C ATOM 3969 CD2 TYR B 313 62.973 23.727 8.871 1.00 76.80 C ANISOU 3969 CD2 TYR B 313 13974 7567 7637 -89 -1501 241 C ATOM 3970 CE1 TYR B 313 60.350 23.699 7.991 1.00 78.96 C ANISOU 3970 CE1 TYR B 313 14179 8014 7806 -102 -1137 275 C ATOM 3971 CE2 TYR B 313 61.933 23.545 9.781 1.00 77.95 C ANISOU 3971 CE2 TYR B 313 14304 7698 7616 -67 -1413 239 C ATOM 3972 CZ TYR B 313 60.623 23.518 9.334 1.00 84.30 C ANISOU 3972 CZ TYR B 313 15066 8590 8375 -78 -1222 255 C ATOM 3973 OH TYR B 313 59.587 23.321 10.211 1.00 85.44 O ANISOU 3973 OH TYR B 313 15375 8720 8369 -62 -1114 248 O ATOM 3974 N PHE B 314 66.308 22.766 4.545 1.00 73.64 N ANISOU 3974 N PHE B 314 12796 7336 7848 -205 -1582 273 N ATOM 3975 CA PHE B 314 67.028 22.792 3.280 1.00 73.47 C ANISOU 3975 CA PHE B 314 12569 7368 7977 -238 -1550 283 C ATOM 3976 C PHE B 314 66.632 21.526 2.477 1.00 75.87 C ANISOU 3976 C PHE B 314 12800 7765 8262 -238 -1454 301 C ATOM 3977 O PHE B 314 66.390 21.613 1.269 1.00 74.42 O ANISOU 3977 O PHE B 314 12489 7668 8120 -255 -1341 328 O ATOM 3978 CB PHE B 314 68.552 22.911 3.482 1.00 76.66 C ANISOU 3978 CB PHE B 314 12898 7693 8536 -250 -1707 240 C ATOM 3979 CG PHE B 314 69.320 22.901 2.173 1.00 79.09 C ANISOU 3979 CG PHE B 314 12991 8056 9004 -289 -1651 248 C ATOM 3980 CD1 PHE B 314 69.432 24.056 1.400 1.00 82.27 C ANISOU 3980 CD1 PHE B 314 13302 8472 9484 -328 -1575 273 C ATOM 3981 CD2 PHE B 314 69.924 21.733 1.708 1.00 81.72 C ANISOU 3981 CD2 PHE B 314 13224 8421 9404 -284 -1667 230 C ATOM 3982 CE1 PHE B 314 70.109 24.035 0.171 1.00 82.96 C ANISOU 3982 CE1 PHE B 314 13208 8609 9704 -365 -1501 286 C ATOM 3983 CE2 PHE B 314 70.613 21.721 0.484 1.00 84.17 C ANISOU 3983 CE2 PHE B 314 13341 8785 9855 -318 -1598 234 C ATOM 3984 CZ PHE B 314 70.703 22.872 -0.272 1.00 81.91 C ANISOU 3984 CZ PHE B 314 12973 8514 9635 -360 -1509 264 C ATOM 3985 N CYS B 315 66.500 20.371 3.180 1.00 72.09 N ANISOU 3985 N CYS B 315 12422 7261 7710 -214 -1500 288 N ATOM 3986 CA CYS B 315 66.091 19.083 2.605 1.00 71.27 C ANISOU 3986 CA CYS B 315 12274 7224 7580 -214 -1423 298 C ATOM 3987 C CYS B 315 64.629 19.153 2.159 1.00 72.83 C ANISOU 3987 C CYS B 315 12486 7507 7681 -220 -1258 327 C ATOM 3988 O CYS B 315 64.278 18.530 1.153 1.00 71.85 O ANISOU 3988 O CYS B 315 12255 7467 7576 -228 -1167 336 O ATOM 3989 CB CYS B 315 66.310 17.946 3.598 1.00 72.29 C ANISOU 3989 CB CYS B 315 12537 7280 7649 -188 -1520 279 C ATOM 3990 SG CYS B 315 68.042 17.690 4.060 1.00 77.30 S ANISOU 3990 SG CYS B 315 13140 7817 8414 -165 -1738 229 S ATOM 3991 N ILE B 316 63.785 19.905 2.910 1.00 67.99 N ANISOU 3991 N ILE B 316 11997 6868 6966 -211 -1225 333 N ATOM 3992 CA ILE B 316 62.381 20.168 2.576 1.00 66.69 C ANISOU 3992 CA ILE B 316 11838 6778 6724 -210 -1077 348 C ATOM 3993 C ILE B 316 62.338 20.900 1.230 1.00 69.75 C ANISOU 3993 C ILE B 316 12067 7246 7189 -217 -1010 366 C ATOM 3994 O ILE B 316 61.592 20.493 0.340 1.00 69.09 O ANISOU 3994 O ILE B 316 11905 7252 7096 -216 -908 372 O ATOM 3995 CB ILE B 316 61.670 20.978 3.720 1.00 70.01 C ANISOU 3995 CB ILE B 316 12423 7143 7037 -192 -1068 340 C ATOM 3996 CG1 ILE B 316 61.416 20.110 4.971 1.00 70.42 C ANISOU 3996 CG1 ILE B 316 12655 7126 6975 -184 -1089 330 C ATOM 3997 CG2 ILE B 316 60.345 21.596 3.258 1.00 70.69 C ANISOU 3997 CG2 ILE B 316 12477 7303 7078 -185 -928 346 C ATOM 3998 CD1 ILE B 316 60.358 18.975 4.815 1.00 73.84 C ANISOU 3998 CD1 ILE B 316 13097 7613 7348 -200 -959 335 C ATOM 3999 N ALA B 317 63.185 21.944 1.071 1.00 66.06 N ANISOU 3999 N ALA B 317 11559 6741 6801 -224 -1072 372 N ATOM 4000 CA ALA B 317 63.282 22.752 -0.148 1.00 65.46 C ANISOU 4000 CA ALA B 317 11358 6719 6794 -232 -1012 398 C ATOM 4001 C ALA B 317 63.654 21.900 -1.352 1.00 68.12 C ANISOU 4001 C ALA B 317 11555 7132 7194 -243 -967 405 C ATOM 4002 O ALA B 317 63.095 22.110 -2.429 1.00 67.58 O ANISOU 4002 O ALA B 317 11417 7144 7118 -234 -872 426 O ATOM 4003 CB ALA B 317 64.305 23.859 0.035 1.00 66.94 C ANISOU 4003 CB ALA B 317 11534 6829 7071 -251 -1094 400 C ATOM 4004 N LEU B 318 64.565 20.910 -1.159 1.00 64.24 N ANISOU 4004 N LEU B 318 11034 6614 6759 -253 -1040 383 N ATOM 4005 CA LEU B 318 65.001 19.971 -2.205 1.00 63.20 C ANISOU 4005 CA LEU B 318 10776 6547 6690 -258 -1005 379 C ATOM 4006 C LEU B 318 63.822 19.122 -2.714 1.00 66.89 C ANISOU 4006 C LEU B 318 11241 7100 7074 -242 -908 379 C ATOM 4007 O LEU B 318 63.711 18.912 -3.917 1.00 66.55 O ANISOU 4007 O LEU B 318 11096 7137 7052 -237 -835 386 O ATOM 4008 CB LEU B 318 66.133 19.050 -1.712 1.00 63.08 C ANISOU 4008 CB LEU B 318 10745 6474 6748 -260 -1118 346 C ATOM 4009 CG LEU B 318 67.504 19.699 -1.544 1.00 67.42 C ANISOU 4009 CG LEU B 318 11234 6953 7429 -279 -1215 329 C ATOM 4010 CD1 LEU B 318 68.437 18.799 -0.784 1.00 68.05 C ANISOU 4010 CD1 LEU B 318 11329 6962 7564 -265 -1354 285 C ATOM 4011 CD2 LEU B 318 68.103 20.115 -2.895 1.00 67.83 C ANISOU 4011 CD2 LEU B 318 11124 7062 7588 -303 -1134 344 C ATOM 4012 N GLY B 319 62.939 18.694 -1.814 1.00 62.97 N ANISOU 4012 N GLY B 319 10858 6582 6484 -234 -903 369 N ATOM 4013 CA GLY B 319 61.743 17.951 -2.193 1.00 62.13 C ANISOU 4013 CA GLY B 319 10746 6547 6313 -227 -808 360 C ATOM 4014 C GLY B 319 60.861 18.773 -3.115 1.00 65.43 C ANISOU 4014 C GLY B 319 11105 7045 6710 -210 -717 372 C ATOM 4015 O GLY B 319 60.409 18.282 -4.154 1.00 65.50 O ANISOU 4015 O GLY B 319 11030 7136 6722 -200 -655 364 O ATOM 4016 N TYR B 320 60.666 20.059 -2.767 1.00 61.05 N ANISOU 4016 N TYR B 320 10600 6461 6135 -202 -719 389 N ATOM 4017 CA TYR B 320 59.879 20.993 -3.560 1.00 60.40 C ANISOU 4017 CA TYR B 320 10481 6437 6032 -175 -651 403 C ATOM 4018 C TYR B 320 60.565 21.313 -4.890 1.00 66.51 C ANISOU 4018 C TYR B 320 11151 7255 6866 -172 -635 430 C ATOM 4019 O TYR B 320 59.873 21.668 -5.851 1.00 66.58 O ANISOU 4019 O TYR B 320 11119 7331 6848 -140 -574 438 O ATOM 4020 CB TYR B 320 59.619 22.295 -2.786 1.00 60.98 C ANISOU 4020 CB TYR B 320 10645 6452 6075 -164 -668 413 C ATOM 4021 CG TYR B 320 58.588 22.179 -1.682 1.00 61.54 C ANISOU 4021 CG TYR B 320 10818 6500 6064 -154 -642 384 C ATOM 4022 CD1 TYR B 320 57.227 22.209 -1.968 1.00 63.06 C ANISOU 4022 CD1 TYR B 320 10992 6757 6211 -126 -555 362 C ATOM 4023 CD2 TYR B 320 58.966 22.189 -0.343 1.00 62.12 C ANISOU 4023 CD2 TYR B 320 11013 6482 6107 -168 -703 376 C ATOM 4024 CE1 TYR B 320 56.272 22.145 -0.957 1.00 62.59 C ANISOU 4024 CE1 TYR B 320 11017 6676 6086 -122 -510 331 C ATOM 4025 CE2 TYR B 320 58.016 22.140 0.679 1.00 62.89 C ANISOU 4025 CE2 TYR B 320 11220 6556 6118 -159 -660 352 C ATOM 4026 CZ TYR B 320 56.669 22.118 0.365 1.00 67.35 C ANISOU 4026 CZ TYR B 320 11752 7189 6648 -140 -554 330 C ATOM 4027 OH TYR B 320 55.716 22.060 1.350 1.00 66.11 O ANISOU 4027 OH TYR B 320 11692 7011 6417 -136 -490 301 O ATOM 4028 N THR B 321 61.918 21.187 -4.945 1.00 64.52 N ANISOU 4028 N THR B 321 10858 6961 6695 -200 -688 439 N ATOM 4029 CA THR B 321 62.742 21.458 -6.136 1.00 65.18 C ANISOU 4029 CA THR B 321 10845 7075 6846 -208 -659 464 C ATOM 4030 C THR B 321 62.398 20.455 -7.253 1.00 70.21 C ANISOU 4030 C THR B 321 11406 7808 7464 -187 -598 450 C ATOM 4031 O THR B 321 62.312 20.855 -8.415 1.00 68.98 O ANISOU 4031 O THR B 321 11205 7707 7298 -167 -536 473 O ATOM 4032 CB THR B 321 64.234 21.405 -5.772 1.00 72.32 C ANISOU 4032 CB THR B 321 11711 7908 7859 -246 -731 460 C ATOM 4033 OG1 THR B 321 64.484 22.348 -4.735 1.00 70.76 O ANISOU 4033 OG1 THR B 321 11590 7619 7676 -261 -799 464 O ATOM 4034 CG2 THR B 321 65.146 21.698 -6.955 1.00 72.18 C ANISOU 4034 CG2 THR B 321 11587 7915 7922 -263 -679 483 C ATOM 4035 N ASN B 322 62.166 19.173 -6.890 1.00 68.68 N ANISOU 4035 N ASN B 322 11212 7628 7258 -188 -617 412 N ATOM 4036 CA ASN B 322 61.775 18.116 -7.830 1.00 69.38 C ANISOU 4036 CA ASN B 322 11234 7797 7329 -169 -571 386 C ATOM 4037 C ASN B 322 60.543 18.571 -8.623 1.00 75.09 C ANISOU 4037 C ASN B 322 11954 8595 7981 -129 -506 388 C ATOM 4038 O ASN B 322 60.552 18.536 -9.857 1.00 75.43 O ANISOU 4038 O ASN B 322 11941 8704 8014 -102 -464 391 O ATOM 4039 CB ASN B 322 61.505 16.792 -7.077 1.00 70.28 C ANISOU 4039 CB ASN B 322 11378 7892 7434 -181 -603 346 C ATOM 4040 CG ASN B 322 60.977 15.658 -7.931 1.00 98.63 C ANISOU 4040 CG ASN B 322 14908 11556 11011 -164 -563 310 C ATOM 4041 OD1 ASN B 322 59.784 15.354 -7.904 1.00 97.74 O ANISOU 4041 OD1 ASN B 322 14812 11478 10849 -156 -526 286 O ATOM 4042 ND2 ASN B 322 61.849 14.965 -8.659 1.00 88.68 N ANISOU 4042 ND2 ASN B 322 13574 10317 9804 -161 -569 297 N ATOM 4043 N SER B 323 59.533 19.089 -7.897 1.00 72.05 N ANISOU 4043 N SER B 323 11636 8195 7546 -119 -503 383 N ATOM 4044 CA SER B 323 58.262 19.599 -8.412 1.00 72.16 C ANISOU 4044 CA SER B 323 11649 8267 7502 -74 -458 372 C ATOM 4045 C SER B 323 58.455 20.812 -9.318 1.00 76.90 C ANISOU 4045 C SER B 323 12247 8881 8090 -42 -440 417 C ATOM 4046 O SER B 323 57.690 21.007 -10.264 1.00 76.18 O ANISOU 4046 O SER B 323 12135 8855 7955 9 -412 408 O ATOM 4047 CB SER B 323 57.364 19.984 -7.245 1.00 76.01 C ANISOU 4047 CB SER B 323 12209 8715 7955 -77 -458 356 C ATOM 4048 OG SER B 323 57.244 18.903 -6.334 1.00 87.29 O ANISOU 4048 OG SER B 323 13665 10114 9385 -113 -464 325 O ATOM 4049 N SER B 324 59.471 21.634 -9.015 1.00 74.43 N ANISOU 4049 N SER B 324 11962 8500 7817 -71 -461 461 N ATOM 4050 CA SER B 324 59.778 22.852 -9.759 1.00 74.68 C ANISOU 4050 CA SER B 324 12008 8521 7846 -54 -437 513 C ATOM 4051 C SER B 324 60.605 22.548 -11.024 1.00 79.57 C ANISOU 4051 C SER B 324 12565 9181 8486 -55 -393 536 C ATOM 4052 O SER B 324 60.524 23.292 -12.003 1.00 79.72 O ANISOU 4052 O SER B 324 12601 9219 8468 -23 -350 575 O ATOM 4053 CB SER B 324 60.533 23.827 -8.864 1.00 77.40 C ANISOU 4053 CB SER B 324 12403 8765 8240 -94 -474 544 C ATOM 4054 OG SER B 324 59.770 24.137 -7.708 1.00 80.94 O ANISOU 4054 OG SER B 324 12922 9175 8656 -86 -508 521 O ATOM 4055 N LEU B 325 61.388 21.461 -11.006 1.00 76.39 N ANISOU 4055 N LEU B 325 12100 8786 8137 -87 -402 511 N ATOM 4056 CA LEU B 325 62.222 21.084 -12.141 1.00 76.60 C ANISOU 4056 CA LEU B 325 12063 8852 8189 -89 -352 522 C ATOM 4057 C LEU B 325 61.453 20.212 -13.130 1.00 81.25 C ANISOU 4057 C LEU B 325 12625 9537 8709 -37 -323 487 C ATOM 4058 O LEU B 325 61.778 20.253 -14.311 1.00 81.11 O ANISOU 4058 O LEU B 325 12589 9562 8667 -13 -266 505 O ATOM 4059 CB LEU B 325 63.489 20.352 -11.679 1.00 76.67 C ANISOU 4059 CB LEU B 325 12008 8820 8302 -140 -381 502 C ATOM 4060 CG LEU B 325 64.484 21.171 -10.844 1.00 81.64 C ANISOU 4060 CG LEU B 325 12644 9352 9023 -193 -420 526 C ATOM 4061 CD1 LEU B 325 65.597 20.300 -10.323 1.00 82.08 C ANISOU 4061 CD1 LEU B 325 12632 9371 9183 -228 -475 489 C ATOM 4062 CD2 LEU B 325 65.054 22.337 -11.636 1.00 84.04 C ANISOU 4062 CD2 LEU B 325 12944 9636 9352 -209 -350 583 C ATOM 4063 N ASN B 326 60.420 19.456 -12.670 1.00 78.62 N ANISOU 4063 N ASN B 326 12295 9234 8344 -19 -357 435 N ATOM 4064 CA ASN B 326 59.595 18.590 -13.530 1.00 79.31 C ANISOU 4064 CA ASN B 326 12350 9406 8379 29 -344 386 C ATOM 4065 C ASN B 326 59.078 19.338 -14.784 1.00 85.97 C ANISOU 4065 C ASN B 326 13221 10304 9142 96 -309 408 C ATOM 4066 O ASN B 326 59.217 18.756 -15.864 1.00 85.95 O ANISOU 4066 O ASN B 326 13189 10359 9107 128 -284 390 O ATOM 4067 CB ASN B 326 58.408 17.990 -12.783 1.00 79.74 C ANISOU 4067 CB ASN B 326 12408 9470 8421 32 -375 331 C ATOM 4068 CG ASN B 326 58.742 16.827 -11.878 1.00 98.11 C ANISOU 4068 CG ASN B 326 14717 11760 10801 -19 -402 298 C ATOM 4069 OD1 ASN B 326 59.647 16.029 -12.142 1.00 88.25 O ANISOU 4069 OD1 ASN B 326 13428 10509 9593 -36 -407 289 O ATOM 4070 ND2 ASN B 326 57.901 16.601 -10.886 1.00 90.97 N ANISOU 4070 ND2 ASN B 326 13844 10830 9891 -36 -415 271 N ATOM 4071 N PRO B 327 58.566 20.616 -14.723 1.00 84.29 N ANISOU 4071 N PRO B 327 13071 10067 8888 123 -310 448 N ATOM 4072 CA PRO B 327 58.144 21.294 -15.976 1.00 85.15 C ANISOU 4072 CA PRO B 327 13224 10219 8911 197 -287 473 C ATOM 4073 C PRO B 327 59.271 21.387 -17.015 1.00 90.95 C ANISOU 4073 C PRO B 327 13965 10959 9634 191 -220 522 C ATOM 4074 O PRO B 327 59.027 21.193 -18.200 1.00 91.19 O ANISOU 4074 O PRO B 327 14014 11048 9585 251 -198 515 O ATOM 4075 CB PRO B 327 57.738 22.701 -15.518 1.00 86.98 C ANISOU 4075 CB PRO B 327 13529 10393 9125 212 -300 518 C ATOM 4076 CG PRO B 327 57.519 22.605 -14.088 1.00 90.83 C ANISOU 4076 CG PRO B 327 14005 10836 9672 165 -335 492 C ATOM 4077 CD PRO B 327 58.314 21.471 -13.543 1.00 85.82 C ANISOU 4077 CD PRO B 327 13310 10191 9105 99 -338 467 C ATOM 4078 N ILE B 328 60.504 21.655 -16.563 1.00 88.55 N ANISOU 4078 N ILE B 328 13644 10590 9410 118 -188 564 N ATOM 4079 CA ILE B 328 61.678 21.755 -17.428 1.00 89.52 C ANISOU 4079 CA ILE B 328 13757 10710 9549 96 -106 606 C ATOM 4080 C ILE B 328 62.091 20.328 -17.892 1.00 95.31 C ANISOU 4080 C ILE B 328 14409 11503 10300 97 -92 548 C ATOM 4081 O ILE B 328 62.530 20.158 -19.025 1.00 95.07 O ANISOU 4081 O ILE B 328 14383 11512 10227 122 -21 558 O ATOM 4082 CB ILE B 328 62.856 22.506 -16.705 1.00 92.78 C ANISOU 4082 CB ILE B 328 14154 11026 10070 13 -83 655 C ATOM 4083 CG1 ILE B 328 62.502 23.982 -16.329 1.00 93.50 C ANISOU 4083 CG1 ILE B 328 14334 11048 10143 13 -93 714 C ATOM 4084 CG2 ILE B 328 64.148 22.484 -17.527 1.00 94.20 C ANISOU 4084 CG2 ILE B 328 14294 11200 10296 -24 17 686 C ATOM 4085 CD1 ILE B 328 61.487 24.230 -15.152 1.00100.25 C ANISOU 4085 CD1 ILE B 328 15220 11879 10991 27 -185 684 C ATOM 4086 N LEU B 329 61.898 19.309 -17.041 1.00 93.71 N ANISOU 4086 N LEU B 329 14148 11304 10153 75 -156 486 N ATOM 4087 CA LEU B 329 62.320 17.943 -17.361 1.00 94.61 C ANISOU 4087 CA LEU B 329 14190 11460 10298 74 -153 428 C ATOM 4088 C LEU B 329 61.334 17.215 -18.313 1.00101.21 C ANISOU 4088 C LEU B 329 15034 12382 11038 147 -162 374 C ATOM 4089 O LEU B 329 61.714 16.925 -19.447 1.00101.64 O ANISOU 4089 O LEU B 329 15087 12484 11048 182 -108 368 O ATOM 4090 CB LEU B 329 62.489 17.097 -16.082 1.00 94.00 C ANISOU 4090 CB LEU B 329 14066 11340 10310 25 -223 385 C ATOM 4091 CG LEU B 329 63.536 17.550 -15.054 1.00 98.53 C ANISOU 4091 CG LEU B 329 14623 11825 10988 -42 -244 415 C ATOM 4092 CD1 LEU B 329 63.464 16.694 -13.820 1.00 98.25 C ANISOU 4092 CD1 LEU B 329 14578 11749 11006 -70 -326 372 C ATOM 4093 CD2 LEU B 329 64.950 17.536 -15.629 1.00100.81 C ANISOU 4093 CD2 LEU B 329 14846 12102 11353 -68 -184 428 C ATOM 4094 N TYR B 330 60.110 16.882 -17.847 1.00 98.75 N ANISOU 4094 N TYR B 330 14728 12089 10704 169 -228 327 N ATOM 4095 CA TYR B 330 59.156 16.075 -18.612 1.00 99.38 C ANISOU 4095 CA TYR B 330 14795 12243 10722 230 -255 257 C ATOM 4096 C TYR B 330 58.248 16.898 -19.552 1.00105.60 C ANISOU 4096 C TYR B 330 15649 13076 11399 314 -260 268 C ATOM 4097 O TYR B 330 57.808 16.347 -20.566 1.00106.12 O ANISOU 4097 O TYR B 330 15715 13206 11399 378 -273 218 O ATOM 4098 CB TYR B 330 58.257 15.276 -17.662 1.00100.17 C ANISOU 4098 CB TYR B 330 14856 12335 10868 206 -316 193 C ATOM 4099 CG TYR B 330 58.973 14.131 -16.973 1.00101.85 C ANISOU 4099 CG TYR B 330 15018 12512 11167 147 -326 164 C ATOM 4100 CD1 TYR B 330 59.710 14.340 -15.810 1.00103.67 C ANISOU 4100 CD1 TYR B 330 15255 12666 11469 83 -335 203 C ATOM 4101 CD2 TYR B 330 58.888 12.832 -17.466 1.00102.46 C ANISOU 4101 CD2 TYR B 330 15049 12626 11254 161 -340 94 C ATOM 4102 CE1 TYR B 330 60.403 13.299 -15.196 1.00104.00 C ANISOU 4102 CE1 TYR B 330 15262 12667 11585 40 -359 176 C ATOM 4103 CE2 TYR B 330 59.541 11.774 -16.834 1.00103.12 C ANISOU 4103 CE2 TYR B 330 15097 12667 11416 114 -357 68 C ATOM 4104 CZ TYR B 330 60.293 12.012 -15.694 1.00110.46 C ANISOU 4104 CZ TYR B 330 16038 13519 12411 56 -369 111 C ATOM 4105 OH TYR B 330 60.937 10.978 -15.059 1.00112.12 O ANISOU 4105 OH TYR B 330 16226 13681 12694 21 -401 85 O ATOM 4106 N ALA B 331 57.951 18.173 -19.236 1.00102.84 N ANISOU 4106 N ALA B 331 15360 12690 11027 321 -261 325 N ATOM 4107 CA ALA B 331 57.050 18.971 -20.076 1.00103.64 C ANISOU 4107 CA ALA B 331 15533 12824 11024 412 -283 333 C ATOM 4108 C ALA B 331 57.805 19.749 -21.176 1.00110.18 C ANISOU 4108 C ALA B 331 16447 13647 11768 444 -213 410 C ATOM 4109 O ALA B 331 57.299 19.862 -22.297 1.00110.25 O ANISOU 4109 O ALA B 331 16519 13705 11667 533 -225 399 O ATOM 4110 CB ALA B 331 56.270 19.940 -19.218 1.00104.07 C ANISOU 4110 CB ALA B 331 15615 12836 11092 414 -322 350 C ATOM 4111 N PHE B 332 58.987 20.261 -20.850 1.00108.49 N ANISOU 4111 N PHE B 332 16240 13373 11609 373 -141 482 N ATOM 4112 CA PHE B 332 59.785 21.020 -21.807 1.00109.96 C ANISOU 4112 CA PHE B 332 16506 13542 11733 385 -49 561 C ATOM 4113 C PHE B 332 60.387 20.129 -22.890 1.00114.49 C ANISOU 4113 C PHE B 332 17066 14174 12262 407 14 535 C ATOM 4114 O PHE B 332 60.346 20.464 -24.074 1.00115.25 O ANISOU 4114 O PHE B 332 17257 14296 12236 473 60 564 O ATOM 4115 CB PHE B 332 60.894 21.790 -21.086 1.00112.12 C ANISOU 4115 CB PHE B 332 16768 13727 12104 291 12 633 C ATOM 4116 CG PHE B 332 61.926 22.372 -22.008 1.00115.14 C ANISOU 4116 CG PHE B 332 17206 14086 12457 275 135 708 C ATOM 4117 CD1 PHE B 332 63.014 21.618 -22.417 1.00118.83 C ANISOU 4117 CD1 PHE B 332 17604 14572 12973 235 217 693 C ATOM 4118 CD2 PHE B 332 61.809 23.673 -22.467 1.00118.51 C ANISOU 4118 CD2 PHE B 332 17755 14464 12809 300 176 791 C ATOM 4119 CE1 PHE B 332 63.965 22.151 -23.265 1.00121.04 C ANISOU 4119 CE1 PHE B 332 17929 14828 13232 214 352 759 C ATOM 4120 CE2 PHE B 332 62.757 24.212 -23.316 1.00122.68 C ANISOU 4120 CE2 PHE B 332 18343 14961 13310 276 308 865 C ATOM 4121 CZ PHE B 332 63.837 23.450 -23.716 1.00121.12 C ANISOU 4121 CZ PHE B 332 18068 14787 13165 230 404 848 C ATOM 4122 N LEU B 333 60.946 18.995 -22.480 1.00110.51 N ANISOU 4122 N LEU B 333 16454 13684 11851 356 14 479 N ATOM 4123 CA LEU B 333 61.566 18.061 -23.423 1.00111.15 C ANISOU 4123 CA LEU B 333 16510 13818 11905 376 72 443 C ATOM 4124 C LEU B 333 60.546 17.508 -24.454 1.00116.42 C ANISOU 4124 C LEU B 333 17228 14565 12442 482 20 379 C ATOM 4125 O LEU B 333 60.913 17.304 -25.615 1.00117.15 O ANISOU 4125 O LEU B 333 17372 14696 12441 532 85 379 O ATOM 4126 CB LEU B 333 62.213 16.898 -22.673 1.00110.51 C ANISOU 4126 CB LEU B 333 16304 13730 11956 313 55 383 C ATOM 4127 N ASP B 334 59.281 17.279 -24.037 1.00112.57 N ANISOU 4127 N ASP B 334 16724 14098 11949 518 -94 320 N ATOM 4128 CA ASP B 334 58.234 16.750 -24.919 1.00141.70 C ANISOU 4128 CA ASP B 334 20443 17858 15538 617 -167 243 C ATOM 4129 C ASP B 334 57.351 17.877 -25.453 1.00160.99 C ANISOU 4129 C ASP B 334 23002 20304 17865 704 -209 278 C ATOM 4130 O ASP B 334 56.789 17.757 -26.539 1.00121.39 O ANISOU 4130 O ASP B 334 18056 15338 12727 805 -248 241 O ATOM 4131 CB ASP B 334 57.375 15.714 -24.178 1.00142.77 C ANISOU 4131 CB ASP B 334 20474 18012 15759 600 -264 142 C TER 4132 ASP B 334 ATOM 4133 N VAL C 4 58.889 -7.872 -51.386 1.00 67.67 N ANISOU 4133 N VAL C 4 9686 9005 7022 925 -145 -1710 N ATOM 4134 CA VAL C 4 58.453 -6.547 -50.939 1.00 64.80 C ANISOU 4134 CA VAL C 4 9387 8685 6549 734 -187 -1357 C ATOM 4135 C VAL C 4 59.271 -6.100 -49.715 1.00 69.47 C ANISOU 4135 C VAL C 4 9845 9249 7302 859 -239 -1253 C ATOM 4136 O VAL C 4 59.573 -6.918 -48.844 1.00 68.91 O ANISOU 4136 O VAL C 4 9741 8979 7462 1108 -343 -1306 O ATOM 4137 CB VAL C 4 56.944 -6.539 -50.622 1.00 65.87 C ANISOU 4137 CB VAL C 4 9761 8572 6694 667 -331 -1109 C ATOM 4138 N GLN C 5 59.634 -4.805 -49.656 1.00 67.46 N ANISOU 4138 N GLN C 5 9526 9186 6921 672 -185 -1100 N ATOM 4139 CA GLN C 5 60.406 -4.239 -48.542 1.00 67.87 C ANISOU 4139 CA GLN C 5 9449 9251 7089 735 -232 -1012 C ATOM 4140 C GLN C 5 59.505 -4.074 -47.315 1.00 72.30 C ANISOU 4140 C GLN C 5 10181 9524 7767 795 -403 -755 C ATOM 4141 O GLN C 5 59.706 -4.767 -46.314 1.00 72.77 O ANISOU 4141 O GLN C 5 10218 9427 8005 1004 -516 -759 O ATOM 4142 CB GLN C 5 61.035 -2.895 -48.942 1.00 69.48 C ANISOU 4142 CB GLN C 5 9555 9731 7113 466 -117 -942 C ATOM 4143 CG GLN C 5 61.900 -2.244 -47.864 1.00 75.85 C ANISOU 4143 CG GLN C 5 10213 10585 8021 485 -158 -884 C ATOM 4144 CD GLN C 5 62.307 -0.821 -48.205 1.00 88.81 C ANISOU 4144 CD GLN C 5 11828 12422 9495 163 -69 -767 C ATOM 4145 OE1 GLN C 5 61.574 -0.055 -48.845 1.00 76.07 O ANISOU 4145 OE1 GLN C 5 10403 10773 7728 -61 -56 -591 O ATOM 4146 NE2 GLN C 5 63.434 -0.394 -47.671 1.00 87.39 N ANISOU 4146 NE2 GLN C 5 11430 12416 9359 130 -41 -834 N ATOM 4147 N LEU C 6 58.510 -3.166 -47.401 1.00 68.27 N ANISOU 4147 N LEU C 6 9835 8954 7151 612 -428 -536 N ATOM 4148 CA LEU C 6 57.531 -2.903 -46.340 1.00 66.71 C ANISOU 4148 CA LEU C 6 9778 8534 7035 642 -557 -327 C ATOM 4149 C LEU C 6 56.368 -3.910 -46.437 1.00 72.25 C ANISOU 4149 C LEU C 6 10628 9044 7780 710 -627 -313 C ATOM 4150 O LEU C 6 55.509 -3.793 -47.317 1.00 71.82 O ANISOU 4150 O LEU C 6 10669 9002 7617 591 -613 -279 O ATOM 4151 CB LEU C 6 57.010 -1.451 -46.411 1.00 65.64 C ANISOU 4151 CB LEU C 6 9722 8413 6805 448 -559 -138 C ATOM 4152 CG LEU C 6 57.930 -0.289 -45.980 1.00 70.27 C ANISOU 4152 CG LEU C 6 10215 9103 7379 341 -527 -100 C ATOM 4153 CD1 LEU C 6 59.197 -0.181 -46.771 1.00 72.47 C ANISOU 4153 CD1 LEU C 6 10329 9643 7565 239 -399 -242 C ATOM 4154 CD2 LEU C 6 57.230 0.997 -46.162 1.00 72.15 C ANISOU 4154 CD2 LEU C 6 10585 9267 7561 174 -557 81 C ATOM 4155 N VAL C 7 56.374 -4.918 -45.544 1.00 70.51 N ANISOU 4155 N VAL C 7 10428 8652 7710 882 -717 -330 N ATOM 4156 CA VAL C 7 55.382 -5.995 -45.526 1.00 70.82 C ANISOU 4156 CA VAL C 7 10613 8488 7809 921 -789 -319 C ATOM 4157 C VAL C 7 54.186 -5.535 -44.675 1.00 73.97 C ANISOU 4157 C VAL C 7 11117 8793 8196 837 -859 -102 C ATOM 4158 O VAL C 7 54.193 -5.646 -43.441 1.00 73.52 O ANISOU 4158 O VAL C 7 11075 8652 8206 894 -931 0 O ATOM 4159 CB VAL C 7 55.983 -7.340 -45.023 1.00 76.41 C ANISOU 4159 CB VAL C 7 11320 9022 8692 1130 -870 -424 C ATOM 4160 CG1 VAL C 7 54.958 -8.468 -45.115 1.00 76.74 C ANISOU 4160 CG1 VAL C 7 11541 8822 8796 1120 -944 -414 C ATOM 4161 CG2 VAL C 7 57.248 -7.706 -45.799 1.00 78.40 C ANISOU 4161 CG2 VAL C 7 11407 9400 8982 1255 -790 -689 C ATOM 4162 N GLU C 8 53.177 -4.993 -45.360 1.00 70.26 N ANISOU 4162 N GLU C 8 10700 8367 7628 698 -838 -43 N ATOM 4163 CA GLU C 8 51.954 -4.466 -44.770 1.00 69.03 C ANISOU 4163 CA GLU C 8 10596 8169 7464 625 -886 115 C ATOM 4164 C GLU C 8 50.924 -5.580 -44.577 1.00 73.84 C ANISOU 4164 C GLU C 8 11297 8646 8114 600 -944 132 C ATOM 4165 O GLU C 8 50.460 -6.186 -45.544 1.00 74.15 O ANISOU 4165 O GLU C 8 11382 8671 8119 541 -946 54 O ATOM 4166 CB GLU C 8 51.381 -3.348 -45.654 1.00 70.02 C ANISOU 4166 CB GLU C 8 10716 8401 7488 513 -870 174 C ATOM 4167 CG GLU C 8 52.264 -2.113 -45.727 1.00 77.69 C ANISOU 4167 CG GLU C 8 11632 9466 8423 484 -827 202 C ATOM 4168 CD GLU C 8 51.823 -1.116 -46.775 1.00 89.06 C ANISOU 4168 CD GLU C 8 13106 10976 9758 362 -839 287 C ATOM 4169 OE1 GLU C 8 51.845 -1.476 -47.973 1.00 91.40 O ANISOU 4169 OE1 GLU C 8 13425 11368 9934 283 -816 237 O ATOM 4170 OE2 GLU C 8 51.561 0.052 -46.413 1.00 75.12 O ANISOU 4170 OE2 GLU C 8 11349 9169 8025 341 -876 398 O ATOM 4171 N SER C 9 50.595 -5.860 -43.316 1.00 71.06 N ANISOU 4171 N SER C 9 10974 8210 7816 613 -990 230 N ATOM 4172 CA SER C 9 49.613 -6.871 -42.943 1.00 71.95 C ANISOU 4172 CA SER C 9 11178 8203 7956 536 -1042 282 C ATOM 4173 C SER C 9 48.465 -6.212 -42.179 1.00 75.33 C ANISOU 4173 C SER C 9 11563 8721 8338 437 -1033 394 C ATOM 4174 O SER C 9 48.586 -5.061 -41.753 1.00 73.55 O ANISOU 4174 O SER C 9 11256 8601 8089 469 -1001 419 O ATOM 4175 CB SER C 9 50.265 -7.975 -42.119 1.00 77.55 C ANISOU 4175 CB SER C 9 11975 8736 8753 614 -1113 309 C ATOM 4176 OG SER C 9 49.323 -8.990 -41.812 1.00 89.81 O ANISOU 4176 OG SER C 9 13649 10146 10327 493 -1168 380 O ATOM 4177 N GLY C 10 47.361 -6.937 -42.034 1.00 73.16 N ANISOU 4177 N GLY C 10 11332 8409 8057 308 -1057 435 N ATOM 4178 CA GLY C 10 46.150 -6.417 -41.408 1.00 72.85 C ANISOU 4178 CA GLY C 10 11206 8500 7973 202 -1030 498 C ATOM 4179 C GLY C 10 45.292 -5.722 -42.446 1.00 76.31 C ANISOU 4179 C GLY C 10 11542 9055 8395 178 -1031 449 C ATOM 4180 O GLY C 10 45.676 -5.643 -43.620 1.00 75.13 O ANISOU 4180 O GLY C 10 11417 8894 8236 214 -1051 391 O ATOM 4181 N GLY C 11 44.122 -5.254 -42.033 1.00 73.52 N ANISOU 4181 N GLY C 11 11066 8837 8031 114 -1016 469 N ATOM 4182 CA GLY C 11 43.213 -4.562 -42.941 1.00 73.81 C ANISOU 4182 CA GLY C 11 10981 8989 8073 117 -1056 440 C ATOM 4183 C GLY C 11 42.012 -5.358 -43.413 1.00 78.69 C ANISOU 4183 C GLY C 11 11549 9677 8671 -46 -1096 423 C ATOM 4184 O GLY C 11 41.573 -6.301 -42.743 1.00 79.18 O ANISOU 4184 O GLY C 11 11639 9727 8719 -198 -1067 442 O ATOM 4185 N GLY C 12 41.473 -4.952 -44.566 1.00 75.18 N ANISOU 4185 N GLY C 12 11035 9317 8214 -38 -1176 401 N ATOM 4186 CA GLY C 12 40.265 -5.542 -45.135 1.00 76.31 C ANISOU 4186 CA GLY C 12 11089 9574 8331 -196 -1239 371 C ATOM 4187 C GLY C 12 38.984 -4.967 -44.552 1.00 80.12 C ANISOU 4187 C GLY C 12 11322 10260 8860 -204 -1239 364 C ATOM 4188 O GLY C 12 38.956 -3.813 -44.117 1.00 79.34 O ANISOU 4188 O GLY C 12 11111 10209 8825 -33 -1228 368 O ATOM 4189 N LEU C 13 37.909 -5.767 -44.557 1.00 77.74 N ANISOU 4189 N LEU C 13 10920 10081 8537 -408 -1251 331 N ATOM 4190 CA LEU C 13 36.602 -5.379 -44.030 1.00 79.06 C ANISOU 4190 CA LEU C 13 10797 10501 8743 -446 -1236 288 C ATOM 4191 C LEU C 13 36.548 -5.466 -42.518 1.00 84.37 C ANISOU 4191 C LEU C 13 11423 11226 9406 -506 -1081 283 C ATOM 4192 O LEU C 13 37.094 -6.400 -41.919 1.00 83.96 O ANISOU 4192 O LEU C 13 11567 11040 9292 -658 -1013 342 O ATOM 4193 CB LEU C 13 35.494 -6.260 -44.614 1.00 81.03 C ANISOU 4193 CB LEU C 13 10935 10899 8952 -693 -1302 246 C ATOM 4194 CG LEU C 13 35.041 -5.950 -46.023 1.00 86.21 C ANISOU 4194 CG LEU C 13 11511 11648 9596 -650 -1479 229 C ATOM 4195 CD1 LEU C 13 34.220 -7.072 -46.573 1.00 88.52 C ANISOU 4195 CD1 LEU C 13 11768 12042 9823 -947 -1536 174 C ATOM 4196 CD2 LEU C 13 34.259 -4.650 -46.074 1.00 89.15 C ANISOU 4196 CD2 LEU C 13 11588 12219 10065 -431 -1566 218 C ATOM 4197 N VAL C 14 35.829 -4.512 -41.907 1.00 82.41 N ANISOU 4197 N VAL C 14 10909 11188 9216 -393 -1034 205 N ATOM 4198 CA VAL C 14 35.617 -4.434 -40.461 1.00 83.11 C ANISOU 4198 CA VAL C 14 10899 11417 9261 -459 -868 157 C ATOM 4199 C VAL C 14 34.229 -3.768 -40.215 1.00 89.58 C ANISOU 4199 C VAL C 14 11315 12572 10148 -418 -837 3 C ATOM 4200 O VAL C 14 33.839 -2.867 -40.966 1.00 89.66 O ANISOU 4200 O VAL C 14 11163 12611 10291 -187 -962 -53 O ATOM 4201 CB VAL C 14 36.794 -3.683 -39.759 1.00 84.90 C ANISOU 4201 CB VAL C 14 11275 11488 9496 -263 -811 170 C ATOM 4202 CG1 VAL C 14 36.947 -2.249 -40.267 1.00 84.05 C ANISOU 4202 CG1 VAL C 14 11080 11325 9531 51 -894 106 C ATOM 4203 CG2 VAL C 14 36.666 -3.722 -38.241 1.00 85.75 C ANISOU 4203 CG2 VAL C 14 11319 11762 9501 -375 -642 123 C ATOM 4204 N ARG C 15 33.509 -4.202 -39.188 1.00 87.93 N ANISOU 4204 N ARG C 15 10942 12620 9846 -639 -681 -62 N ATOM 4205 CA ARG C 15 32.211 -3.630 -38.851 1.00 90.67 C ANISOU 4205 CA ARG C 15 10861 13336 10253 -608 -618 -253 C ATOM 4206 C ARG C 15 32.349 -2.253 -38.223 1.00 93.80 C ANISOU 4206 C ARG C 15 11112 13771 10758 -281 -559 -417 C ATOM 4207 O ARG C 15 33.259 -2.035 -37.462 1.00 92.21 O ANISOU 4207 O ARG C 15 11108 13439 10490 -243 -471 -396 O ATOM 4208 CB ARG C 15 31.479 -4.554 -37.884 1.00 94.73 C ANISOU 4208 CB ARG C 15 11253 14146 10593 -1000 -435 -277 C ATOM 4209 CG ARG C 15 31.620 -6.031 -38.205 1.00107.64 C ANISOU 4209 CG ARG C 15 13150 15641 12109 -1370 -474 -88 C ATOM 4210 CD ARG C 15 30.336 -6.785 -37.900 1.00123.77 C ANISOU 4210 CD ARG C 15 14929 18043 14056 -1758 -378 -142 C ATOM 4211 NE ARG C 15 30.268 -8.089 -38.559 1.00134.75 N ANISOU 4211 NE ARG C 15 16533 19268 15397 -2086 -473 1 N ATOM 4212 CZ ARG C 15 29.221 -8.513 -39.262 1.00149.38 C ANISOU 4212 CZ ARG C 15 18160 21321 17278 -2282 -541 -65 C ATOM 4213 NH1 ARG C 15 28.158 -7.736 -39.401 1.00139.01 N ANISOU 4213 NH1 ARG C 15 16376 20394 16047 -2159 -535 -258 N ATOM 4214 NH2 ARG C 15 29.230 -9.712 -39.825 1.00132.79 N ANISOU 4214 NH2 ARG C 15 16290 19029 15134 -2595 -627 44 N ATOM 4215 N PRO C 16 31.418 -1.327 -38.489 1.00 91.58 N ANISOU 4215 N PRO C 16 10472 13670 10653 -44 -616 -598 N ATOM 4216 CA PRO C 16 31.601 -0.002 -37.866 1.00 91.43 C ANISOU 4216 CA PRO C 16 10347 13624 10770 284 -566 -782 C ATOM 4217 C PRO C 16 31.584 -0.115 -36.342 1.00 94.91 C ANISOU 4217 C PRO C 16 10715 14303 11041 119 -296 -932 C ATOM 4218 O PRO C 16 30.667 -0.704 -35.765 1.00 96.89 O ANISOU 4218 O PRO C 16 10714 14930 11168 -137 -143 -1030 O ATOM 4219 CB PRO C 16 30.421 0.815 -38.403 1.00 96.30 C ANISOU 4219 CB PRO C 16 10552 14417 11622 549 -688 -960 C ATOM 4220 CG PRO C 16 29.972 0.084 -39.628 1.00100.91 C ANISOU 4220 CG PRO C 16 11129 15017 12197 416 -875 -795 C ATOM 4221 CD PRO C 16 30.185 -1.361 -39.297 1.00 95.49 C ANISOU 4221 CD PRO C 16 10632 14396 11256 -32 -740 -666 C ATOM 4222 N GLY C 17 32.654 0.378 -35.727 1.00 88.72 N ANISOU 4222 N GLY C 17 10174 13315 10219 220 -244 -928 N ATOM 4223 CA GLY C 17 32.885 0.284 -34.292 1.00 89.12 C ANISOU 4223 CA GLY C 17 10236 13563 10062 52 -14 -1036 C ATOM 4224 C GLY C 17 33.831 -0.858 -33.978 1.00 90.45 C ANISOU 4224 C GLY C 17 10782 13599 9988 -256 6 -759 C ATOM 4225 O GLY C 17 34.153 -1.110 -32.811 1.00 91.16 O ANISOU 4225 O GLY C 17 10948 13832 9854 -446 161 -769 O ATOM 4226 N GLY C 18 34.267 -1.544 -35.035 1.00 83.76 N ANISOU 4226 N GLY C 18 10164 12478 9184 -298 -163 -519 N ATOM 4227 CA GLY C 18 35.188 -2.670 -34.965 1.00 81.29 C ANISOU 4227 CA GLY C 18 10212 11963 8712 -528 -194 -259 C ATOM 4228 C GLY C 18 36.633 -2.231 -34.942 1.00 81.62 C ANISOU 4228 C GLY C 18 10540 11693 8778 -342 -265 -178 C ATOM 4229 O GLY C 18 36.933 -1.046 -35.126 1.00 79.70 O ANISOU 4229 O GLY C 18 10245 11354 8682 -56 -303 -302 O ATOM 4230 N SER C 19 37.542 -3.190 -34.732 1.00 77.73 N ANISOU 4230 N SER C 19 10348 11029 8159 -505 -298 31 N ATOM 4231 CA SER C 19 38.968 -2.904 -34.622 1.00 75.82 C ANISOU 4231 CA SER C 19 10349 10537 7922 -359 -363 107 C ATOM 4232 C SER C 19 39.805 -3.639 -35.679 1.00 78.63 C ANISOU 4232 C SER C 19 10949 10577 8348 -331 -513 284 C ATOM 4233 O SER C 19 39.386 -4.675 -36.203 1.00 79.17 O ANISOU 4233 O SER C 19 11073 10602 8406 -497 -557 379 O ATOM 4234 CB SER C 19 39.468 -3.296 -33.236 1.00 80.13 C ANISOU 4234 CB SER C 19 11013 11190 8244 -536 -277 172 C ATOM 4235 OG SER C 19 38.754 -2.594 -32.232 1.00 91.04 O ANISOU 4235 OG SER C 19 12166 12900 9525 -573 -114 -32 O ATOM 4236 N LEU C 20 40.993 -3.080 -35.984 1.00 73.04 N ANISOU 4236 N LEU C 20 10374 9665 7711 -132 -582 299 N ATOM 4237 CA LEU C 20 42.012 -3.632 -36.885 1.00 71.04 C ANISOU 4237 CA LEU C 20 10329 9148 7513 -74 -697 415 C ATOM 4238 C LEU C 20 43.394 -3.243 -36.410 1.00 73.46 C ANISOU 4238 C LEU C 20 10760 9347 7802 40 -715 437 C ATOM 4239 O LEU C 20 43.625 -2.078 -36.089 1.00 72.95 O ANISOU 4239 O LEU C 20 10617 9330 7769 163 -682 331 O ATOM 4240 CB LEU C 20 41.826 -3.186 -38.351 1.00 70.25 C ANISOU 4240 CB LEU C 20 10184 8959 7547 57 -779 379 C ATOM 4241 CG LEU C 20 40.650 -3.740 -39.154 1.00 76.28 C ANISOU 4241 CG LEU C 20 10850 9799 8333 -54 -815 374 C ATOM 4242 CD1 LEU C 20 40.590 -3.106 -40.512 1.00 75.57 C ANISOU 4242 CD1 LEU C 20 10726 9650 8339 87 -919 353 C ATOM 4243 CD2 LEU C 20 40.754 -5.253 -39.323 1.00 81.18 C ANISOU 4243 CD2 LEU C 20 11639 10312 8895 -253 -844 472 C ATOM 4244 N ARG C 21 44.316 -4.202 -36.369 1.00 69.19 N ANISOU 4244 N ARG C 21 10403 8654 7230 4 -781 561 N ATOM 4245 CA ARG C 21 45.694 -3.921 -35.980 1.00 68.11 C ANISOU 4245 CA ARG C 21 10354 8439 7085 116 -821 580 C ATOM 4246 C ARG C 21 46.579 -4.015 -37.213 1.00 71.25 C ANISOU 4246 C ARG C 21 10817 8657 7599 248 -892 575 C ATOM 4247 O ARG C 21 46.898 -5.119 -37.667 1.00 71.37 O ANISOU 4247 O ARG C 21 10944 8530 7642 229 -955 638 O ATOM 4248 CB ARG C 21 46.164 -4.871 -34.867 1.00 68.24 C ANISOU 4248 CB ARG C 21 10501 8450 6978 4 -863 720 C ATOM 4249 CG ARG C 21 47.613 -4.651 -34.414 1.00 74.50 C ANISOU 4249 CG ARG C 21 11355 9192 7760 124 -935 744 C ATOM 4250 CD ARG C 21 48.024 -5.687 -33.384 1.00 81.86 C ANISOU 4250 CD ARG C 21 12429 10100 8574 25 -1028 923 C ATOM 4251 NE ARG C 21 47.264 -5.550 -32.140 1.00 88.45 N ANISOU 4251 NE ARG C 21 13238 11168 9200 -172 -952 957 N ATOM 4252 CZ ARG C 21 47.314 -6.415 -31.135 1.00105.39 C ANISOU 4252 CZ ARG C 21 15518 13346 11180 -338 -1022 1150 C ATOM 4253 NH1 ARG C 21 48.035 -7.522 -31.239 1.00 96.70 N ANISOU 4253 NH1 ARG C 21 14596 12003 10142 -300 -1194 1334 N ATOM 4254 NH2 ARG C 21 46.596 -6.207 -30.038 1.00 93.66 N ANISOU 4254 NH2 ARG C 21 13991 12133 9463 -549 -924 1157 N ATOM 4255 N LEU C 22 46.938 -2.858 -37.782 1.00 66.92 N ANISOU 4255 N LEU C 22 10200 8112 7115 366 -879 489 N ATOM 4256 CA LEU C 22 47.795 -2.825 -38.960 1.00 66.14 C ANISOU 4256 CA LEU C 22 10144 7903 7082 452 -920 476 C ATOM 4257 C LEU C 22 49.245 -3.073 -38.561 1.00 70.94 C ANISOU 4257 C LEU C 22 10804 8466 7685 516 -951 488 C ATOM 4258 O LEU C 22 49.669 -2.678 -37.475 1.00 70.14 O ANISOU 4258 O LEU C 22 10683 8431 7535 519 -948 491 O ATOM 4259 CB LEU C 22 47.669 -1.500 -39.726 1.00 65.48 C ANISOU 4259 CB LEU C 22 9993 7834 7052 513 -910 422 C ATOM 4260 CG LEU C 22 46.306 -1.172 -40.351 1.00 70.04 C ANISOU 4260 CG LEU C 22 10495 8452 7665 496 -924 413 C ATOM 4261 CD1 LEU C 22 46.339 0.189 -40.996 1.00 70.12 C ANISOU 4261 CD1 LEU C 22 10473 8426 7741 575 -956 399 C ATOM 4262 CD2 LEU C 22 45.882 -2.217 -41.387 1.00 71.86 C ANISOU 4262 CD2 LEU C 22 10769 8660 7876 428 -964 443 C ATOM 4263 N SER C 23 49.984 -3.746 -39.446 1.00 69.22 N ANISOU 4263 N SER C 23 10630 8157 7511 569 -984 473 N ATOM 4264 CA SER C 23 51.378 -4.114 -39.250 1.00 70.36 C ANISOU 4264 CA SER C 23 10780 8270 7682 663 -1025 456 C ATOM 4265 C SER C 23 52.203 -3.799 -40.483 1.00 75.40 C ANISOU 4265 C SER C 23 11369 8925 8355 718 -991 358 C ATOM 4266 O SER C 23 51.719 -3.918 -41.607 1.00 74.95 O ANISOU 4266 O SER C 23 11331 8853 8293 682 -964 320 O ATOM 4267 CB SER C 23 51.489 -5.602 -38.921 1.00 75.93 C ANISOU 4267 CB SER C 23 11589 8839 8424 687 -1110 517 C ATOM 4268 OG SER C 23 50.735 -5.954 -37.770 1.00 87.13 O ANISOU 4268 OG SER C 23 13071 10263 9771 582 -1139 640 O ATOM 4269 N CYS C 24 53.450 -3.409 -40.272 1.00 73.17 N ANISOU 4269 N CYS C 24 11011 8708 8084 779 -992 311 N ATOM 4270 CA CYS C 24 54.397 -3.132 -41.345 1.00 73.94 C ANISOU 4270 CA CYS C 24 11030 8876 8188 800 -938 207 C ATOM 4271 C CYS C 24 55.785 -3.545 -40.889 1.00 78.45 C ANISOU 4271 C CYS C 24 11502 9496 8811 914 -978 142 C ATOM 4272 O CYS C 24 56.254 -3.061 -39.856 1.00 78.51 O ANISOU 4272 O CYS C 24 11460 9565 8806 917 -1021 180 O ATOM 4273 CB CYS C 24 54.342 -1.664 -41.743 1.00 74.31 C ANISOU 4273 CB CYS C 24 11045 9005 8183 693 -878 217 C ATOM 4274 SG CYS C 24 55.504 -1.198 -43.052 1.00 79.55 S ANISOU 4274 SG CYS C 24 11620 9808 8799 631 -792 121 S ATOM 4275 N VAL C 25 56.435 -4.462 -41.623 1.00 75.15 N ANISOU 4275 N VAL C 25 11039 9060 8453 1019 -975 25 N ATOM 4276 CA VAL C 25 57.741 -4.958 -41.198 1.00 76.01 C ANISOU 4276 CA VAL C 25 11017 9214 8648 1177 -1037 -55 C ATOM 4277 C VAL C 25 58.714 -5.018 -42.395 1.00 79.04 C ANISOU 4277 C VAL C 25 11243 9743 9046 1218 -933 -265 C ATOM 4278 O VAL C 25 58.350 -5.444 -43.490 1.00 78.46 O ANISOU 4278 O VAL C 25 11214 9645 8952 1198 -859 -365 O ATOM 4279 CB VAL C 25 57.607 -6.357 -40.512 1.00 81.45 C ANISOU 4279 CB VAL C 25 11807 9690 9451 1332 -1188 4 C ATOM 4280 CG1 VAL C 25 56.876 -7.375 -41.392 1.00 81.55 C ANISOU 4280 CG1 VAL C 25 11949 9517 9517 1348 -1174 -57 C ATOM 4281 CG2 VAL C 25 58.958 -6.897 -40.038 1.00 83.63 C ANISOU 4281 CG2 VAL C 25 11936 9994 9846 1543 -1301 -65 C ATOM 4282 N ASP C 26 59.957 -4.582 -42.152 1.00 75.97 N ANISOU 4282 N ASP C 26 10650 9540 8673 1257 -924 -347 N ATOM 4283 CA ASP C 26 61.049 -4.661 -43.111 1.00 77.61 C ANISOU 4283 CA ASP C 26 10646 9952 8890 1295 -815 -572 C ATOM 4284 C ASP C 26 62.087 -5.632 -42.553 1.00 83.88 C ANISOU 4284 C ASP C 26 11272 10738 9860 1571 -935 -689 C ATOM 4285 O ASP C 26 62.974 -5.239 -41.793 1.00 84.35 O ANISOU 4285 O ASP C 26 11160 10943 9946 1607 -1002 -681 O ATOM 4286 CB ASP C 26 61.643 -3.271 -43.417 1.00 79.03 C ANISOU 4286 CB ASP C 26 10697 10391 8941 1071 -693 -581 C ATOM 4287 CG ASP C 26 62.736 -3.253 -44.478 1.00 88.22 C ANISOU 4287 CG ASP C 26 11622 11835 10061 1037 -541 -814 C ATOM 4288 OD1 ASP C 26 62.940 -4.291 -45.147 1.00 90.14 O ANISOU 4288 OD1 ASP C 26 11803 12079 10367 1198 -505 -1008 O ATOM 4289 OD2 ASP C 26 63.326 -2.184 -44.693 1.00 92.79 O ANISOU 4289 OD2 ASP C 26 12088 12634 10534 824 -446 -814 O ATOM 4290 N SER C 27 61.930 -6.916 -42.897 1.00 81.53 N ANISOU 4290 N SER C 27 11035 10247 9696 1770 -989 -792 N ATOM 4291 CA SER C 27 62.778 -8.015 -42.441 1.00 83.78 C ANISOU 4291 CA SER C 27 11200 10432 10199 2086 -1145 -899 C ATOM 4292 C SER C 27 64.226 -7.870 -42.940 1.00 88.69 C ANISOU 4292 C SER C 27 11455 11368 10876 2200 -1057 -1179 C ATOM 4293 O SER C 27 65.150 -8.228 -42.207 1.00 89.53 O ANISOU 4293 O SER C 27 11375 11507 11135 2425 -1213 -1211 O ATOM 4294 CB SER C 27 62.204 -9.344 -42.916 1.00 89.15 C ANISOU 4294 CB SER C 27 12056 10799 11020 2241 -1198 -983 C ATOM 4295 OG SER C 27 60.881 -9.520 -42.434 1.00 96.52 O ANISOU 4295 OG SER C 27 13298 11475 11899 2107 -1275 -730 O ATOM 4296 N GLU C 28 64.423 -7.318 -44.169 1.00 85.33 N ANISOU 4296 N GLU C 28 10911 11204 10308 2026 -815 -1371 N ATOM 4297 CA GLU C 28 65.754 -7.113 -44.771 1.00 87.56 C ANISOU 4297 CA GLU C 28 10817 11857 10594 2065 -677 -1662 C ATOM 4298 C GLU C 28 66.533 -5.998 -44.034 1.00 89.99 C ANISOU 4298 C GLU C 28 10927 12434 10833 1920 -693 -1561 C ATOM 4299 O GLU C 28 67.745 -5.862 -44.235 1.00 91.99 O ANISOU 4299 O GLU C 28 10822 13010 11119 1967 -624 -1781 O ATOM 4300 CB GLU C 28 65.674 -6.772 -46.280 1.00 89.34 C ANISOU 4300 CB GLU C 28 11003 12323 10619 1841 -403 -1860 C ATOM 4301 CG GLU C 28 64.915 -7.761 -47.156 1.00100.59 C ANISOU 4301 CG GLU C 28 12611 13544 12063 1924 -361 -2004 C ATOM 4302 CD GLU C 28 63.409 -7.585 -47.266 1.00120.25 C ANISOU 4302 CD GLU C 28 15478 15784 14428 1727 -393 -1747 C ATOM 4303 OE1 GLU C 28 62.919 -6.450 -47.064 1.00107.82 O ANISOU 4303 OE1 GLU C 28 14010 14272 12686 1464 -372 -1492 O ATOM 4304 OE2 GLU C 28 62.742 -8.546 -47.712 1.00117.64 O ANISOU 4304 OE2 GLU C 28 15315 15225 14160 1820 -419 -1841 O ATOM 4305 N ARG C 29 65.826 -5.208 -43.187 1.00 82.93 N ANISOU 4305 N ARG C 29 10251 11417 9843 1737 -778 -1257 N ATOM 4306 CA ARG C 29 66.362 -4.106 -42.381 1.00 82.35 C ANISOU 4306 CA ARG C 29 10062 11532 9695 1566 -813 -1147 C ATOM 4307 C ARG C 29 67.029 -3.051 -43.293 1.00 87.51 C ANISOU 4307 C ARG C 29 10519 12542 10189 1268 -583 -1276 C ATOM 4308 O ARG C 29 68.130 -2.575 -42.997 1.00 89.28 O ANISOU 4308 O ARG C 29 10452 13052 10418 1212 -575 -1371 O ATOM 4309 CB ARG C 29 67.353 -4.622 -41.318 1.00 84.88 C ANISOU 4309 CB ARG C 29 10150 11917 10183 1827 -1026 -1184 C ATOM 4310 N THR C 30 66.352 -2.698 -44.409 1.00 82.84 N ANISOU 4310 N THR C 30 10090 11944 9441 1055 -407 -1264 N ATOM 4311 CA THR C 30 66.837 -1.701 -45.379 1.00 83.40 C ANISOU 4311 CA THR C 30 10044 12327 9316 716 -190 -1329 C ATOM 4312 C THR C 30 66.205 -0.316 -45.064 1.00 84.75 C ANISOU 4312 C THR C 30 10451 12389 9360 394 -204 -1054 C ATOM 4313 O THR C 30 66.626 0.696 -45.634 1.00 85.23 O ANISOU 4313 O THR C 30 10458 12656 9270 69 -71 -1038 O ATOM 4314 CB THR C 30 66.549 -2.146 -46.840 1.00 87.91 C ANISOU 4314 CB THR C 30 10652 12989 9763 659 -7 -1480 C ATOM 4315 OG1 THR C 30 65.167 -2.480 -46.986 1.00 81.67 O ANISOU 4315 OG1 THR C 30 10208 11864 8958 698 -77 -1318 O ATOM 4316 CG2 THR C 30 67.392 -3.342 -47.266 1.00 88.87 C ANISOU 4316 CG2 THR C 30 10481 13278 10009 947 50 -1836 C ATOM 4317 N SER C 31 65.228 -0.284 -44.126 1.00 78.70 N ANISOU 4317 N SER C 31 9939 11300 8663 484 -368 -850 N ATOM 4318 CA SER C 31 64.509 0.915 -43.672 1.00 76.73 C ANISOU 4318 CA SER C 31 9916 10888 8348 263 -408 -629 C ATOM 4319 C SER C 31 63.819 0.675 -42.323 1.00 80.80 C ANISOU 4319 C SER C 31 10578 11157 8965 436 -590 -505 C ATOM 4320 O SER C 31 63.681 -0.475 -41.894 1.00 80.07 O ANISOU 4320 O SER C 31 10479 10971 8972 700 -690 -532 O ATOM 4321 CB SER C 31 63.470 1.348 -44.705 1.00 77.71 C ANISOU 4321 CB SER C 31 10287 10889 8350 93 -329 -504 C ATOM 4322 OG SER C 31 62.434 0.391 -44.859 1.00 80.92 O ANISOU 4322 OG SER C 31 10854 11093 8800 290 -382 -476 O ATOM 4323 N TYR C 32 63.368 1.761 -41.667 1.00 78.16 N ANISOU 4323 N TYR C 32 10386 10711 8599 274 -633 -375 N ATOM 4324 CA TYR C 32 62.648 1.679 -40.396 1.00 77.39 C ANISOU 4324 CA TYR C 32 10426 10429 8548 384 -772 -276 C ATOM 4325 C TYR C 32 61.194 2.119 -40.583 1.00 79.32 C ANISOU 4325 C TYR C 32 10938 10431 8769 328 -760 -141 C ATOM 4326 O TYR C 32 60.966 3.318 -40.770 1.00 79.21 O ANISOU 4326 O TYR C 32 11013 10358 8723 134 -723 -92 O ATOM 4327 CB TYR C 32 63.316 2.537 -39.276 1.00 80.00 C ANISOU 4327 CB TYR C 32 10672 10855 8870 271 -843 -298 C ATOM 4328 CG TYR C 32 64.812 2.377 -39.124 1.00 85.22 C ANISOU 4328 CG TYR C 32 11026 11805 9548 274 -861 -436 C ATOM 4329 CD1 TYR C 32 65.359 1.209 -38.595 1.00 88.47 C ANISOU 4329 CD1 TYR C 32 11278 12303 10036 540 -984 -488 C ATOM 4330 CD2 TYR C 32 65.673 3.440 -39.374 1.00 88.18 C ANISOU 4330 CD2 TYR C 32 11269 12359 9877 5 -784 -506 C ATOM 4331 CE1 TYR C 32 66.737 1.061 -38.437 1.00 92.65 C ANISOU 4331 CE1 TYR C 32 11480 13118 10604 577 -1024 -630 C ATOM 4332 CE2 TYR C 32 67.052 3.311 -39.206 1.00 92.19 C ANISOU 4332 CE2 TYR C 32 11446 13180 10401 -7 -801 -652 C ATOM 4333 CZ TYR C 32 67.581 2.118 -38.738 1.00102.36 C ANISOU 4333 CZ TYR C 32 12540 14577 11775 299 -923 -723 C ATOM 4334 OH TYR C 32 68.941 1.989 -38.563 1.00107.68 O ANISOU 4334 OH TYR C 32 12847 15580 12488 320 -961 -880 O ATOM 4335 N PRO C 33 60.189 1.210 -40.529 1.00 74.47 N ANISOU 4335 N PRO C 33 10449 9664 8181 487 -803 -81 N ATOM 4336 CA PRO C 33 58.794 1.672 -40.603 1.00 73.26 C ANISOU 4336 CA PRO C 33 10497 9322 8015 441 -802 28 C ATOM 4337 C PRO C 33 58.488 2.540 -39.380 1.00 78.63 C ANISOU 4337 C PRO C 33 11230 9944 8701 391 -856 51 C ATOM 4338 O PRO C 33 58.587 2.059 -38.245 1.00 78.01 O ANISOU 4338 O PRO C 33 11123 9899 8617 477 -931 43 O ATOM 4339 CB PRO C 33 57.984 0.367 -40.645 1.00 74.08 C ANISOU 4339 CB PRO C 33 10675 9327 8146 602 -841 60 C ATOM 4340 CG PRO C 33 58.977 -0.722 -40.888 1.00 79.47 C ANISOU 4340 CG PRO C 33 11223 10102 8869 734 -853 -40 C ATOM 4341 CD PRO C 33 60.252 -0.243 -40.297 1.00 76.22 C ANISOU 4341 CD PRO C 33 10635 9861 8463 709 -873 -108 C ATOM 4342 N MET C 34 58.242 3.852 -39.611 1.00 76.61 N ANISOU 4342 N MET C 34 11049 9608 8451 239 -825 68 N ATOM 4343 CA MET C 34 58.054 4.844 -38.547 1.00 77.07 C ANISOU 4343 CA MET C 34 11152 9600 8529 178 -861 30 C ATOM 4344 C MET C 34 56.826 5.753 -38.766 1.00 81.02 C ANISOU 4344 C MET C 34 11807 9884 9091 159 -860 73 C ATOM 4345 O MET C 34 56.578 6.637 -37.940 1.00 81.49 O ANISOU 4345 O MET C 34 11910 9860 9192 125 -882 0 O ATOM 4346 CB MET C 34 59.308 5.735 -38.451 1.00 81.25 C ANISOU 4346 CB MET C 34 11594 10226 9052 -2 -850 -42 C ATOM 4347 CG MET C 34 60.539 5.011 -37.911 1.00 86.13 C ANISOU 4347 CG MET C 34 12012 11085 9629 37 -884 -118 C ATOM 4348 SD MET C 34 62.079 5.973 -37.970 1.00 92.89 S ANISOU 4348 SD MET C 34 12703 12123 10469 -212 -859 -218 S ATOM 4349 CE MET C 34 61.641 7.378 -36.917 1.00 90.22 C ANISOU 4349 CE MET C 34 12515 11611 10154 -359 -906 -276 C ATOM 4350 N GLY C 35 56.072 5.536 -39.840 1.00 76.91 N ANISOU 4350 N GLY C 35 11357 9283 8583 191 -849 169 N ATOM 4351 CA GLY C 35 54.904 6.361 -40.122 1.00 76.67 C ANISOU 4351 CA GLY C 35 11445 9053 8632 207 -883 221 C ATOM 4352 C GLY C 35 53.713 5.672 -40.756 1.00 78.73 C ANISOU 4352 C GLY C 35 11738 9283 8893 317 -900 299 C ATOM 4353 O GLY C 35 53.828 4.579 -41.316 1.00 77.38 O ANISOU 4353 O GLY C 35 11533 9217 8651 343 -876 328 O ATOM 4354 N TRP C 36 52.552 6.335 -40.662 1.00 75.33 N ANISOU 4354 N TRP C 36 11361 8703 8557 386 -949 308 N ATOM 4355 CA TRP C 36 51.289 5.901 -41.242 1.00 74.49 C ANISOU 4355 CA TRP C 36 11261 8572 8470 479 -987 374 C ATOM 4356 C TRP C 36 50.594 7.063 -41.928 1.00 80.83 C ANISOU 4356 C TRP C 36 12146 9182 9384 495 -1084 456 C ATOM 4357 O TRP C 36 50.464 8.145 -41.345 1.00 81.10 O ANISOU 4357 O TRP C 36 12212 9056 9545 527 -1119 389 O ATOM 4358 CB TRP C 36 50.355 5.285 -40.190 1.00 72.33 C ANISOU 4358 CB TRP C 36 10909 8366 8208 590 -961 282 C ATOM 4359 CG TRP C 36 50.850 4.023 -39.553 1.00 72.03 C ANISOU 4359 CG TRP C 36 10825 8480 8063 579 -909 258 C ATOM 4360 CD1 TRP C 36 51.355 3.881 -38.294 1.00 74.85 C ANISOU 4360 CD1 TRP C 36 11148 8919 8372 570 -880 177 C ATOM 4361 CD2 TRP C 36 50.873 2.715 -40.146 1.00 71.06 C ANISOU 4361 CD2 TRP C 36 10703 8425 7872 577 -904 320 C ATOM 4362 NE1 TRP C 36 51.644 2.559 -38.047 1.00 73.51 N ANISOU 4362 NE1 TRP C 36 10964 8846 8120 576 -877 220 N ATOM 4363 CE2 TRP C 36 51.395 1.826 -39.181 1.00 74.36 C ANISOU 4363 CE2 TRP C 36 11097 8925 8232 587 -888 293 C ATOM 4364 CE3 TRP C 36 50.510 2.207 -41.409 1.00 72.06 C ANISOU 4364 CE3 TRP C 36 10858 8543 7977 564 -924 388 C ATOM 4365 CZ2 TRP C 36 51.561 0.459 -39.434 1.00 73.09 C ANISOU 4365 CZ2 TRP C 36 10952 8787 8034 604 -899 332 C ATOM 4366 CZ3 TRP C 36 50.672 0.851 -41.657 1.00 72.77 C ANISOU 4366 CZ3 TRP C 36 10953 8683 8014 567 -912 388 C ATOM 4367 CH2 TRP C 36 51.192 -0.006 -40.678 1.00 73.26 C ANISOU 4367 CH2 TRP C 36 11001 8774 8059 597 -903 361 C ATOM 4368 N PHE C 37 50.171 6.839 -43.178 1.00 79.44 N ANISOU 4368 N PHE C 37 12013 9011 9159 472 -1144 597 N ATOM 4369 CA PHE C 37 49.420 7.786 -44.011 1.00 81.88 C ANISOU 4369 CA PHE C 37 12408 9147 9555 497 -1285 732 C ATOM 4370 C PHE C 37 48.224 7.069 -44.629 1.00 85.63 C ANISOU 4370 C PHE C 37 12823 9710 10004 586 -1350 784 C ATOM 4371 O PHE C 37 48.254 5.844 -44.738 1.00 84.05 O ANISOU 4371 O PHE C 37 12563 9690 9682 558 -1274 746 O ATOM 4372 CB PHE C 37 50.317 8.422 -45.095 1.00 85.45 C ANISOU 4372 CB PHE C 37 13002 9546 9919 297 -1324 901 C ATOM 4373 CG PHE C 37 51.269 9.486 -44.586 1.00 88.63 C ANISOU 4373 CG PHE C 37 13482 9799 10395 185 -1307 875 C ATOM 4374 CD1 PHE C 37 52.488 9.138 -44.010 1.00 91.34 C ANISOU 4374 CD1 PHE C 37 13758 10291 10656 74 -1173 759 C ATOM 4375 CD2 PHE C 37 50.971 10.837 -44.733 1.00 93.46 C ANISOU 4375 CD2 PHE C 37 14234 10110 11165 181 -1447 970 C ATOM 4376 CE1 PHE C 37 53.365 10.124 -43.535 1.00 93.61 C ANISOU 4376 CE1 PHE C 37 14102 10462 11005 -62 -1164 720 C ATOM 4377 CE2 PHE C 37 51.857 11.822 -44.277 1.00 97.83 C ANISOU 4377 CE2 PHE C 37 14879 10499 11793 40 -1437 935 C ATOM 4378 CZ PHE C 37 53.048 11.458 -43.682 1.00 94.95 C ANISOU 4378 CZ PHE C 37 14431 10320 11326 -97 -1289 805 C ATOM 4379 N ARG C 38 47.151 7.801 -44.978 1.00 83.71 N ANISOU 4379 N ARG C 38 12585 9331 9891 702 -1503 857 N ATOM 4380 CA ARG C 38 45.978 7.165 -45.581 1.00 84.07 C ANISOU 4380 CA ARG C 38 12542 9490 9911 774 -1585 901 C ATOM 4381 C ARG C 38 45.423 8.033 -46.702 1.00 91.85 C ANISOU 4381 C ARG C 38 13616 10343 10941 797 -1804 1108 C ATOM 4382 O ARG C 38 45.500 9.260 -46.630 1.00 93.64 O ANISOU 4382 O ARG C 38 13938 10319 11323 851 -1912 1173 O ATOM 4383 CB ARG C 38 44.873 6.862 -44.539 1.00 83.51 C ANISOU 4383 CB ARG C 38 12280 9482 9967 945 -1549 724 C ATOM 4384 CG ARG C 38 44.225 8.073 -43.864 1.00 92.62 C ANISOU 4384 CG ARG C 38 13376 10449 11365 1139 -1626 630 C ATOM 4385 CD ARG C 38 43.191 7.638 -42.845 1.00 98.57 C ANISOU 4385 CD ARG C 38 13904 11358 12190 1267 -1542 420 C ATOM 4386 NE ARG C 38 42.559 8.775 -42.178 1.00108.77 N ANISOU 4386 NE ARG C 38 15107 12496 13724 1478 -1594 264 N ATOM 4387 CZ ARG C 38 41.666 8.667 -41.200 1.00124.52 C ANISOU 4387 CZ ARG C 38 16882 14635 15797 1599 -1505 33 C ATOM 4388 NH1 ARG C 38 41.313 7.471 -40.745 1.00110.29 N ANISOU 4388 NH1 ARG C 38 14948 13123 13833 1494 -1365 -30 N ATOM 4389 NH2 ARG C 38 41.138 9.752 -40.651 1.00114.78 N ANISOU 4389 NH2 ARG C 38 15559 13252 14800 1813 -1549 -151 N ATOM 4390 N ARG C 39 44.864 7.397 -47.740 1.00 89.69 N ANISOU 4390 N ARG C 39 13325 10223 10530 746 -1889 1216 N ATOM 4391 CA ARG C 39 44.285 8.147 -48.840 1.00 92.83 C ANISOU 4391 CA ARG C 39 13807 10530 10936 760 -2133 1444 C ATOM 4392 C ARG C 39 42.852 7.664 -49.058 1.00 99.57 C ANISOU 4392 C ARG C 39 14476 11518 11838 901 -2257 1418 C ATOM 4393 O ARG C 39 42.636 6.513 -49.433 1.00 98.03 O ANISOU 4393 O ARG C 39 14212 11563 11471 801 -2194 1368 O ATOM 4394 CB ARG C 39 45.146 8.019 -50.111 1.00 93.12 C ANISOU 4394 CB ARG C 39 14024 10663 10692 495 -2145 1638 C ATOM 4395 CG ARG C 39 44.833 9.075 -51.152 1.00106.25 C ANISOU 4395 CG ARG C 39 15847 12179 12345 460 -2412 1936 C ATOM 4396 CD ARG C 39 45.814 9.041 -52.303 1.00118.58 C ANISOU 4396 CD ARG C 39 17596 13870 13589 143 -2385 2121 C ATOM 4397 NE ARG C 39 45.577 10.146 -53.232 1.00134.68 N ANISOU 4397 NE ARG C 39 19831 15741 15602 72 -2659 2457 N ATOM 4398 CZ ARG C 39 44.789 10.074 -54.300 1.00154.74 C ANISOU 4398 CZ ARG C 39 22401 18396 17996 45 -2883 2656 C ATOM 4399 NH1 ARG C 39 44.195 8.930 -54.620 1.00142.72 N ANISOU 4399 NH1 ARG C 39 20723 17175 16331 57 -2846 2525 N ATOM 4400 NH2 ARG C 39 44.619 11.135 -55.078 1.00146.70 N ANISOU 4400 NH2 ARG C 39 21587 17193 16962 -19 -3162 2999 N ATOM 4401 N ALA C 40 41.873 8.536 -48.754 1.00100.18 N ANISOU 4401 N ALA C 40 14454 11437 12171 1141 -2430 1417 N ATOM 4402 CA ALA C 40 40.441 8.260 -48.916 1.00102.33 C ANISOU 4402 CA ALA C 40 14499 11849 12534 1302 -2573 1379 C ATOM 4403 C ALA C 40 40.064 8.181 -50.425 1.00110.37 C ANISOU 4403 C ALA C 40 15592 12969 13375 1203 -2814 1637 C ATOM 4404 O ALA C 40 40.845 8.669 -51.253 1.00110.97 O ANISOU 4404 O ALA C 40 15914 12942 13308 1048 -2895 1864 O ATOM 4405 CB ALA C 40 39.626 9.338 -48.210 1.00105.44 C ANISOU 4405 CB ALA C 40 14755 12035 13274 1614 -2698 1284 C ATOM 4406 N PRO C 41 38.899 7.576 -50.818 1.00108.92 N ANISOU 4406 N PRO C 41 15200 13015 13170 1253 -2933 1611 N ATOM 4407 CA PRO C 41 38.563 7.467 -52.257 1.00110.78 C ANISOU 4407 CA PRO C 41 15510 13386 13195 1132 -3174 1850 C ATOM 4408 C PRO C 41 38.661 8.800 -53.027 1.00116.97 C ANISOU 4408 C PRO C 41 16493 13916 14035 1196 -3476 2169 C ATOM 4409 O PRO C 41 39.106 8.803 -54.178 1.00117.86 O ANISOU 4409 O PRO C 41 16813 14100 13867 971 -3584 2410 O ATOM 4410 CB PRO C 41 37.102 6.984 -52.249 1.00114.13 C ANISOU 4410 CB PRO C 41 15616 14037 13712 1266 -3301 1743 C ATOM 4411 CG PRO C 41 36.642 7.079 -50.813 1.00117.92 C ANISOU 4411 CG PRO C 41 15856 14466 14480 1484 -3141 1470 C ATOM 4412 CD PRO C 41 37.871 6.908 -49.993 1.00110.26 C ANISOU 4412 CD PRO C 41 15056 13375 13465 1373 -2843 1361 C ATOM 4413 N GLY C 42 38.270 9.902 -52.393 1.00114.38 N ANISOU 4413 N GLY C 42 16114 13289 14055 1485 -3605 2162 N ATOM 4414 CA GLY C 42 38.324 11.217 -53.017 1.00117.59 C ANISOU 4414 CA GLY C 42 16733 13370 14575 1569 -3920 2473 C ATOM 4415 C GLY C 42 39.433 12.112 -52.500 1.00120.24 C ANISOU 4415 C GLY C 42 17321 13346 15020 1524 -3816 2506 C ATOM 4416 O GLY C 42 40.194 12.676 -53.293 1.00121.43 O ANISOU 4416 O GLY C 42 17776 13351 15013 1311 -3923 2804 O ATOM 4417 N LYS C 43 39.529 12.241 -51.157 1.00114.19 N ANISOU 4417 N LYS C 43 16427 12457 14502 1691 -3603 2195 N ATOM 4418 CA LYS C 43 40.477 13.110 -50.443 1.00113.38 C ANISOU 4418 CA LYS C 43 16516 12014 14552 1676 -3497 2148 C ATOM 4419 C LYS C 43 41.961 12.772 -50.763 1.00113.90 C ANISOU 4419 C LYS C 43 16825 12158 14295 1284 -3284 2248 C ATOM 4420 O LYS C 43 42.269 11.680 -51.227 1.00111.16 O ANISOU 4420 O LYS C 43 16445 12152 13637 1070 -3135 2241 O ATOM 4421 CB LYS C 43 40.259 13.017 -48.919 1.00114.22 C ANISOU 4421 CB LYS C 43 16394 12112 14894 1883 -3265 1741 C ATOM 4422 CG LYS C 43 38.925 13.600 -48.440 1.00130.05 C ANISOU 4422 CG LYS C 43 18143 14000 17270 2291 -3443 1577 C ATOM 4423 CD LYS C 43 38.830 13.631 -46.914 1.00136.71 C ANISOU 4423 CD LYS C 43 18790 14848 18307 2452 -3189 1160 C ATOM 4424 CE LYS C 43 37.551 14.273 -46.426 1.00145.45 C ANISOU 4424 CE LYS C 43 19614 15858 19790 2867 -3339 944 C ATOM 4425 NZ LYS C 43 37.496 14.344 -44.941 1.00150.35 N ANISOU 4425 NZ LYS C 43 20051 16519 20556 2990 -3069 514 N ATOM 4426 N GLU C 44 42.863 13.742 -50.489 1.00110.75 N ANISOU 4426 N GLU C 44 16653 11433 13994 1198 -3273 2314 N ATOM 4427 CA GLU C 44 44.314 13.657 -50.692 1.00109.02 C ANISOU 4427 CA GLU C 44 16637 11261 13523 837 -3080 2391 C ATOM 4428 C GLU C 44 44.939 12.778 -49.573 1.00108.17 C ANISOU 4428 C GLU C 44 16363 11369 13369 806 -2724 2042 C ATOM 4429 O GLU C 44 44.203 12.250 -48.728 1.00106.51 O ANISOU 4429 O GLU C 44 15915 11265 13287 1029 -2640 1786 O ATOM 4430 CB GLU C 44 44.905 15.089 -50.722 1.00113.75 C ANISOU 4430 CB GLU C 44 17520 11410 14291 761 -3228 2579 C ATOM 4431 CG GLU C 44 46.411 15.240 -50.943 1.00126.57 C ANISOU 4431 CG GLU C 44 19350 13058 15684 359 -3056 2677 C ATOM 4432 CD GLU C 44 47.015 14.716 -52.234 1.00150.48 C ANISOU 4432 CD GLU C 44 22492 16399 18284 -4 -3024 2931 C ATOM 4433 OE1 GLU C 44 47.606 15.535 -52.974 1.00149.66 O ANISOU 4433 OE1 GLU C 44 22658 16133 18071 -279 -3144 3240 O ATOM 4434 OE2 GLU C 44 46.920 13.494 -52.500 1.00141.08 O ANISOU 4434 OE2 GLU C 44 21130 15615 16860 -34 -2873 2810 O ATOM 4435 N ARG C 45 46.256 12.638 -49.552 1.00102.39 N ANISOU 4435 N ARG C 45 15741 10709 12452 529 -2532 2040 N ATOM 4436 CA ARG C 45 46.887 11.828 -48.525 1.00 98.08 C ANISOU 4436 CA ARG C 45 15047 10355 11864 510 -2243 1746 C ATOM 4437 C ARG C 45 46.709 12.517 -47.199 1.00 99.25 C ANISOU 4437 C ARG C 45 15138 10263 12309 712 -2217 1524 C ATOM 4438 O ARG C 45 46.674 13.724 -47.120 1.00101.71 O ANISOU 4438 O ARG C 45 15590 10225 12828 762 -2367 1594 O ATOM 4439 CB ARG C 45 48.357 11.597 -48.824 1.00 98.60 C ANISOU 4439 CB ARG C 45 15211 10565 11689 191 -2067 1784 C ATOM 4440 CG ARG C 45 49.200 12.837 -48.662 1.00116.22 C ANISOU 4440 CG ARG C 45 17632 12511 14017 36 -2104 1875 C ATOM 4441 CD ARG C 45 50.678 12.517 -48.755 1.00130.73 C ANISOU 4441 CD ARG C 45 19482 14560 15629 -272 -1892 1842 C ATOM 4442 NE ARG C 45 51.066 12.032 -50.074 1.00144.18 N ANISOU 4442 NE ARG C 45 21240 16527 17014 -518 -1868 2026 N ATOM 4443 CZ ARG C 45 52.180 11.355 -50.323 1.00158.77 C ANISOU 4443 CZ ARG C 45 23014 18685 18626 -738 -1655 1942 C ATOM 4444 NH1 ARG C 45 52.452 10.961 -51.555 1.00147.69 N ANISOU 4444 NH1 ARG C 45 21655 17538 16924 -959 -1628 2078 N ATOM 4445 NH2 ARG C 45 53.019 11.070 -49.341 1.00143.64 N ANISOU 4445 NH2 ARG C 45 20965 16844 16767 -730 -1476 1707 N ATOM 4446 N GLU C 46 46.597 11.734 -46.150 1.00 90.74 N ANISOU 4446 N GLU C 46 13865 9371 11242 814 -2031 1251 N ATOM 4447 CA GLU C 46 46.374 12.270 -44.823 1.00 89.79 C ANISOU 4447 CA GLU C 46 13663 9102 11352 991 -1977 994 C ATOM 4448 C GLU C 46 47.265 11.570 -43.813 1.00 90.18 C ANISOU 4448 C GLU C 46 13634 9356 11274 883 -1733 789 C ATOM 4449 O GLU C 46 47.331 10.336 -43.796 1.00 87.18 O ANISOU 4449 O GLU C 46 13145 9268 10712 835 -1611 755 O ATOM 4450 CB GLU C 46 44.889 12.067 -44.473 1.00 91.52 C ANISOU 4450 CB GLU C 46 13669 9375 11729 1281 -2041 859 C ATOM 4451 CG GLU C 46 44.507 12.469 -43.059 1.00 99.93 C ANISOU 4451 CG GLU C 46 14597 10378 12995 1470 -1947 535 C ATOM 4452 CD GLU C 46 43.077 12.158 -42.669 1.00113.61 C ANISOU 4452 CD GLU C 46 16064 12255 14849 1722 -1962 364 C ATOM 4453 OE1 GLU C 46 42.237 11.936 -43.574 1.00104.35 O ANISOU 4453 OE1 GLU C 46 14824 11138 13687 1802 -2118 518 O ATOM 4454 OE2 GLU C 46 42.796 12.142 -41.448 1.00102.70 O ANISOU 4454 OE2 GLU C 46 14526 10962 13533 1821 -1814 67 O ATOM 4455 N PHE C 47 47.942 12.358 -42.960 1.00 86.80 N ANISOU 4455 N PHE C 47 13269 8762 10949 846 -1684 652 N ATOM 4456 CA PHE C 47 48.787 11.825 -41.891 1.00 84.05 C ANISOU 4456 CA PHE C 47 12842 8604 10489 754 -1491 456 C ATOM 4457 C PHE C 47 47.924 11.113 -40.859 1.00 86.29 C ANISOU 4457 C PHE C 47 12925 9081 10781 930 -1394 236 C ATOM 4458 O PHE C 47 46.919 11.670 -40.411 1.00 87.89 O ANISOU 4458 O PHE C 47 13053 9171 11169 1130 -1444 96 O ATOM 4459 CB PHE C 47 49.616 12.943 -41.235 1.00 87.08 C ANISOU 4459 CB PHE C 47 13340 8763 10984 658 -1489 347 C ATOM 4460 CG PHE C 47 50.391 12.535 -40.002 1.00 86.67 C ANISOU 4460 CG PHE C 47 13193 8910 10828 584 -1326 125 C ATOM 4461 CD1 PHE C 47 51.635 11.927 -40.114 1.00 87.95 C ANISOU 4461 CD1 PHE C 47 13344 9280 10792 374 -1236 185 C ATOM 4462 CD2 PHE C 47 49.904 12.816 -38.729 1.00 89.13 C ANISOU 4462 CD2 PHE C 47 13417 9214 11234 722 -1275 -154 C ATOM 4463 CE1 PHE C 47 52.360 11.571 -38.975 1.00 88.06 C ANISOU 4463 CE1 PHE C 47 13265 9480 10712 317 -1129 2 C ATOM 4464 CE2 PHE C 47 50.629 12.459 -37.591 1.00 91.08 C ANISOU 4464 CE2 PHE C 47 13591 9668 11347 629 -1150 -336 C ATOM 4465 CZ PHE C 47 51.857 11.849 -37.721 1.00 87.80 C ANISOU 4465 CZ PHE C 47 13173 9441 10746 433 -1096 -240 C ATOM 4466 N VAL C 48 48.310 9.883 -40.495 1.00 79.57 N ANISOU 4466 N VAL C 48 11984 8520 9730 851 -1258 205 N ATOM 4467 CA VAL C 48 47.583 9.093 -39.505 1.00 78.17 C ANISOU 4467 CA VAL C 48 11641 8553 9508 947 -1158 39 C ATOM 4468 C VAL C 48 48.322 9.198 -38.163 1.00 80.85 C ANISOU 4468 C VAL C 48 11961 8970 9787 884 -1049 -151 C ATOM 4469 O VAL C 48 47.793 9.778 -37.210 1.00 81.45 O ANISOU 4469 O VAL C 48 11973 9025 9950 977 -1014 -367 O ATOM 4470 CB VAL C 48 47.404 7.620 -39.960 1.00 80.17 C ANISOU 4470 CB VAL C 48 11834 9037 9591 895 -1114 150 C ATOM 4471 CG1 VAL C 48 46.655 6.810 -38.911 1.00 79.63 C ANISOU 4471 CG1 VAL C 48 11620 9175 9462 939 -1015 12 C ATOM 4472 CG2 VAL C 48 46.690 7.541 -41.301 1.00 80.43 C ANISOU 4472 CG2 VAL C 48 11885 9023 9653 931 -1232 318 C ATOM 4473 N ALA C 49 49.548 8.647 -38.101 1.00 75.58 N ANISOU 4473 N ALA C 49 11336 8415 8966 729 -1001 -89 N ATOM 4474 CA ALA C 49 50.379 8.642 -36.904 1.00 75.15 C ANISOU 4474 CA ALA C 49 11259 8474 8821 648 -930 -233 C ATOM 4475 C ALA C 49 51.831 8.356 -37.240 1.00 77.98 C ANISOU 4475 C ALA C 49 11657 8894 9077 493 -929 -135 C ATOM 4476 O ALA C 49 52.125 7.701 -38.238 1.00 76.56 O ANISOU 4476 O ALA C 49 11489 8757 8844 460 -940 22 O ATOM 4477 CB ALA C 49 49.870 7.602 -35.912 1.00 75.20 C ANISOU 4477 CB ALA C 49 11157 8728 8687 678 -849 -307 C ATOM 4478 N SER C 50 52.733 8.833 -36.388 1.00 75.44 N ANISOU 4478 N SER C 50 11334 8608 8722 397 -913 -258 N ATOM 4479 CA SER C 50 54.171 8.610 -36.486 1.00 74.98 C ANISOU 4479 CA SER C 50 11256 8663 8571 251 -911 -213 C ATOM 4480 C SER C 50 54.721 8.147 -35.132 1.00 77.86 C ANISOU 4480 C SER C 50 11536 9247 8802 224 -894 -334 C ATOM 4481 O SER C 50 54.008 8.205 -34.127 1.00 77.98 O ANISOU 4481 O SER C 50 11536 9309 8782 280 -869 -463 O ATOM 4482 CB SER C 50 54.879 9.881 -36.956 1.00 80.35 C ANISOU 4482 CB SER C 50 12025 9157 9349 97 -946 -217 C ATOM 4483 OG SER C 50 56.285 9.704 -37.032 1.00 90.36 O ANISOU 4483 OG SER C 50 13227 10583 10522 -67 -932 -200 O ATOM 4484 N ILE C 51 55.975 7.673 -35.111 1.00 72.86 N ANISOU 4484 N ILE C 51 10831 8772 8079 138 -911 -296 N ATOM 4485 CA ILE C 51 56.659 7.272 -33.888 1.00 72.66 C ANISOU 4485 CA ILE C 51 10723 8966 7920 104 -940 -379 C ATOM 4486 C ILE C 51 58.172 7.406 -34.149 1.00 77.65 C ANISOU 4486 C ILE C 51 11262 9706 8535 -23 -975 -377 C ATOM 4487 O ILE C 51 58.605 7.360 -35.306 1.00 76.80 O ANISOU 4487 O ILE C 51 11136 9561 8482 -59 -951 -286 O ATOM 4488 CB ILE C 51 56.235 5.853 -33.402 1.00 74.42 C ANISOU 4488 CB ILE C 51 10912 9340 8026 221 -957 -286 C ATOM 4489 CG1 ILE C 51 56.525 5.667 -31.889 1.00 75.43 C ANISOU 4489 CG1 ILE C 51 11002 9674 7984 175 -1003 -368 C ATOM 4490 CG2 ILE C 51 56.827 4.729 -34.278 1.00 74.34 C ANISOU 4490 CG2 ILE C 51 10849 9373 8024 287 -986 -137 C ATOM 4491 CD1 ILE C 51 55.861 4.483 -31.255 1.00 79.99 C ANISOU 4491 CD1 ILE C 51 11597 10366 8430 240 -1021 -263 C ATOM 4492 N THR C 52 58.959 7.636 -33.084 1.00 75.79 N ANISOU 4492 N THR C 52 10952 9634 8209 -115 -1025 -493 N ATOM 4493 CA THR C 52 60.409 7.800 -33.192 1.00 76.66 C ANISOU 4493 CA THR C 52 10927 9900 8302 -250 -1067 -522 C ATOM 4494 C THR C 52 61.063 6.432 -33.386 1.00 79.76 C ANISOU 4494 C THR C 52 11170 10491 8643 -119 -1119 -412 C ATOM 4495 O THR C 52 60.408 5.404 -33.173 1.00 78.35 O ANISOU 4495 O THR C 52 11031 10314 8426 48 -1144 -318 O ATOM 4496 CB THR C 52 60.970 8.528 -31.955 1.00 87.89 C ANISOU 4496 CB THR C 52 12312 11442 9640 -398 -1125 -701 C ATOM 4497 OG1 THR C 52 60.557 7.847 -30.770 1.00 89.37 O ANISOU 4497 OG1 THR C 52 12497 11786 9673 -303 -1181 -717 O ATOM 4498 CG2 THR C 52 60.519 9.976 -31.879 1.00 88.18 C ANISOU 4498 CG2 THR C 52 12495 11235 9775 -535 -1079 -853 C ATOM 4499 N TRP C 53 62.353 6.423 -33.821 1.00 77.27 N ANISOU 4499 N TRP C 53 10679 10338 8343 -200 -1136 -436 N ATOM 4500 CA TRP C 53 63.139 5.201 -34.034 1.00 77.23 C ANISOU 4500 CA TRP C 53 10489 10523 8332 -48 -1196 -383 C ATOM 4501 C TRP C 53 63.109 4.341 -32.779 1.00 79.31 C ANISOU 4501 C TRP C 53 10731 10902 8499 92 -1344 -343 C ATOM 4502 O TRP C 53 62.925 3.130 -32.865 1.00 78.07 O ANISOU 4502 O TRP C 53 10574 10732 8358 292 -1402 -233 O ATOM 4503 CB TRP C 53 64.596 5.528 -34.435 1.00 78.35 C ANISOU 4503 CB TRP C 53 10387 10886 8494 -184 -1192 -475 C ATOM 4504 CG TRP C 53 65.489 4.316 -34.458 1.00 80.93 C ANISOU 4504 CG TRP C 53 10477 11432 8842 14 -1281 -473 C ATOM 4505 CD1 TRP C 53 65.637 3.421 -35.480 1.00 83.53 C ANISOU 4505 CD1 TRP C 53 10721 11768 9247 174 -1225 -452 C ATOM 4506 CD2 TRP C 53 66.286 3.821 -33.370 1.00 82.56 C ANISOU 4506 CD2 TRP C 53 10507 11860 9001 103 -1465 -498 C ATOM 4507 NE1 TRP C 53 66.477 2.398 -35.096 1.00 84.79 N ANISOU 4507 NE1 TRP C 53 10661 12107 9446 386 -1363 -479 N ATOM 4508 CE2 TRP C 53 66.892 2.620 -33.805 1.00 87.65 C ANISOU 4508 CE2 TRP C 53 10963 12605 9733 350 -1527 -484 C ATOM 4509 CE3 TRP C 53 66.539 4.273 -32.060 1.00 84.95 C ANISOU 4509 CE3 TRP C 53 10797 12292 9188 1 -1599 -539 C ATOM 4510 CZ2 TRP C 53 67.754 1.876 -32.984 1.00 89.20 C ANISOU 4510 CZ2 TRP C 53 10955 13004 9934 519 -1741 -483 C ATOM 4511 CZ3 TRP C 53 67.397 3.542 -31.254 1.00 88.57 C ANISOU 4511 CZ3 TRP C 53 11054 12990 9607 133 -1807 -526 C ATOM 4512 CH2 TRP C 53 67.996 2.361 -31.716 1.00 90.11 C ANISOU 4512 CH2 TRP C 53 11061 13260 9918 401 -1889 -484 C ATOM 4513 N SER C 54 63.255 4.988 -31.617 1.00 76.03 N ANISOU 4513 N SER C 54 10324 10589 7975 -34 -1413 -428 N ATOM 4514 CA SER C 54 63.236 4.372 -30.298 1.00 76.67 C ANISOU 4514 CA SER C 54 10407 10821 7901 29 -1564 -384 C ATOM 4515 C SER C 54 61.878 3.717 -29.978 1.00 78.60 C ANISOU 4515 C SER C 54 10853 10927 8084 135 -1538 -263 C ATOM 4516 O SER C 54 61.825 2.811 -29.146 1.00 78.78 O ANISOU 4516 O SER C 54 10896 11051 7985 215 -1670 -143 O ATOM 4517 CB SER C 54 63.554 5.421 -29.236 1.00 81.99 C ANISOU 4517 CB SER C 54 11071 11637 8446 -183 -1605 -547 C ATOM 4518 OG SER C 54 62.653 6.518 -29.271 1.00 89.09 O ANISOU 4518 OG SER C 54 12141 12339 9371 -309 -1464 -671 O ATOM 4519 N GLY C 55 60.812 4.183 -30.634 1.00 73.52 N ANISOU 4519 N GLY C 55 10349 10065 7521 120 -1383 -283 N ATOM 4520 CA GLY C 55 59.451 3.705 -30.422 1.00 72.44 C ANISOU 4520 CA GLY C 55 10366 9819 7337 187 -1331 -203 C ATOM 4521 C GLY C 55 58.833 4.245 -29.143 1.00 78.47 C ANISOU 4521 C GLY C 55 11203 10685 7928 76 -1317 -309 C ATOM 4522 O GLY C 55 57.870 3.663 -28.625 1.00 77.86 O ANISOU 4522 O GLY C 55 11214 10629 7741 99 -1296 -237 O ATOM 4523 N ILE C 56 59.379 5.382 -28.631 1.00 76.68 N ANISOU 4523 N ILE C 56 10935 10535 7665 -72 -1317 -504 N ATOM 4524 CA ILE C 56 58.945 6.021 -27.385 1.00 77.96 C ANISOU 4524 CA ILE C 56 11148 10825 7649 -196 -1296 -679 C ATOM 4525 C ILE C 56 57.892 7.115 -27.673 1.00 81.83 C ANISOU 4525 C ILE C 56 11730 11098 8266 -211 -1135 -868 C ATOM 4526 O ILE C 56 56.832 7.079 -27.052 1.00 81.99 O ANISOU 4526 O ILE C 56 11804 11163 8185 -200 -1057 -941 O ATOM 4527 CB ILE C 56 60.148 6.626 -26.572 1.00 83.13 C ANISOU 4527 CB ILE C 56 11705 11693 8185 -358 -1407 -822 C ATOM 4528 CG1 ILE C 56 61.257 5.574 -26.311 1.00 84.02 C ANISOU 4528 CG1 ILE C 56 11689 12030 8206 -305 -1604 -637 C ATOM 4529 CG2 ILE C 56 59.659 7.260 -25.249 1.00 85.83 C ANISOU 4529 CG2 ILE C 56 12110 12196 8307 -501 -1375 -1043 C ATOM 4530 CD1 ILE C 56 62.534 6.072 -25.587 1.00 89.99 C ANISOU 4530 CD1 ILE C 56 12301 13042 8850 -458 -1748 -760 C ATOM 4531 N ASP C 57 58.200 8.110 -28.552 1.00 77.95 N ANISOU 4531 N ASP C 57 11249 10381 7987 -248 -1096 -953 N ATOM 4532 CA ASP C 57 57.311 9.254 -28.792 1.00 77.66 C ANISOU 4532 CA ASP C 57 11309 10090 8106 -245 -994 -1132 C ATOM 4533 C ASP C 57 56.388 9.042 -30.007 1.00 77.28 C ANISOU 4533 C ASP C 57 11316 9804 8243 -91 -933 -985 C ATOM 4534 O ASP C 57 56.808 9.242 -31.149 1.00 75.04 O ANISOU 4534 O ASP C 57 11049 9356 8107 -100 -948 -870 O ATOM 4535 CB ASP C 57 58.116 10.551 -28.998 1.00 81.38 C ANISOU 4535 CB ASP C 57 11807 10407 8706 -406 -1015 -1291 C ATOM 4536 CG ASP C 57 58.851 11.054 -27.770 1.00 97.48 C ANISOU 4536 CG ASP C 57 13806 12651 10583 -585 -1068 -1514 C ATOM 4537 OD1 ASP C 57 58.703 10.434 -26.685 1.00 98.09 O ANISOU 4537 OD1 ASP C 57 13840 13013 10417 -583 -1090 -1548 O ATOM 4538 OD2 ASP C 57 59.532 12.097 -27.876 1.00109.08 O ANISOU 4538 OD2 ASP C 57 15299 13995 12151 -754 -1091 -1657 O ATOM 4539 N PRO C 58 55.083 8.762 -29.758 1.00 73.58 N ANISOU 4539 N PRO C 58 10868 9332 7756 23 -861 -1012 N ATOM 4540 CA PRO C 58 54.144 8.602 -30.872 1.00 72.29 C ANISOU 4540 CA PRO C 58 10737 8968 7761 161 -824 -889 C ATOM 4541 C PRO C 58 53.386 9.902 -31.176 1.00 78.65 C ANISOU 4541 C PRO C 58 11603 9498 8783 221 -791 -1061 C ATOM 4542 O PRO C 58 52.788 10.506 -30.278 1.00 80.44 O ANISOU 4542 O PRO C 58 11817 9747 9001 240 -736 -1312 O ATOM 4543 CB PRO C 58 53.193 7.509 -30.369 1.00 73.28 C ANISOU 4543 CB PRO C 58 10822 9279 7740 228 -776 -824 C ATOM 4544 CG PRO C 58 53.328 7.524 -28.841 1.00 79.26 C ANISOU 4544 CG PRO C 58 11550 10302 8263 122 -757 -987 C ATOM 4545 CD PRO C 58 54.409 8.505 -28.468 1.00 76.15 C ANISOU 4545 CD PRO C 58 11167 9887 7878 7 -807 -1150 C ATOM 4546 N THR C 59 53.422 10.338 -32.440 1.00 75.28 N ANISOU 4546 N THR C 59 11244 8811 8548 250 -834 -931 N ATOM 4547 CA THR C 59 52.706 11.533 -32.894 1.00 77.10 C ANISOU 4547 CA THR C 59 11557 8719 9020 332 -854 -1029 C ATOM 4548 C THR C 59 51.399 11.083 -33.538 1.00 80.64 C ANISOU 4548 C THR C 59 11967 9123 9549 520 -845 -929 C ATOM 4549 O THR C 59 51.409 10.109 -34.286 1.00 78.16 O ANISOU 4549 O THR C 59 11633 8901 9164 526 -854 -704 O ATOM 4550 CB THR C 59 53.591 12.346 -33.847 1.00 88.97 C ANISOU 4550 CB THR C 59 13180 9971 10654 201 -933 -914 C ATOM 4551 OG1 THR C 59 54.849 12.601 -33.217 1.00 91.60 O ANISOU 4551 OG1 THR C 59 13502 10415 10885 -1 -937 -1007 O ATOM 4552 CG2 THR C 59 52.940 13.652 -34.284 1.00 89.77 C ANISOU 4552 CG2 THR C 59 13410 9674 11025 276 -999 -983 C ATOM 4553 N TYR C 60 50.271 11.737 -33.216 1.00 79.21 N ANISOU 4553 N TYR C 60 11755 8829 9514 675 -826 -1123 N ATOM 4554 CA TYR C 60 48.983 11.347 -33.803 1.00 78.78 C ANISOU 4554 CA TYR C 60 11621 8768 9545 854 -829 -1049 C ATOM 4555 C TYR C 60 48.244 12.529 -34.382 1.00 85.60 C ANISOU 4555 C TYR C 60 12531 9283 10711 1025 -925 -1117 C ATOM 4556 O TYR C 60 48.332 13.636 -33.842 1.00 88.15 O ANISOU 4556 O TYR C 60 12906 9405 11181 1056 -940 -1352 O ATOM 4557 CB TYR C 60 48.048 10.666 -32.777 1.00 80.25 C ANISOU 4557 CB TYR C 60 11638 9262 9589 909 -703 -1218 C ATOM 4558 CG TYR C 60 48.610 9.512 -31.976 1.00 80.65 C ANISOU 4558 CG TYR C 60 11657 9649 9336 748 -629 -1155 C ATOM 4559 CD1 TYR C 60 48.649 8.227 -32.504 1.00 80.32 C ANISOU 4559 CD1 TYR C 60 11609 9732 9175 705 -642 -894 C ATOM 4560 CD2 TYR C 60 48.910 9.664 -30.625 1.00 82.99 C ANISOU 4560 CD2 TYR C 60 11924 10147 9462 651 -552 -1375 C ATOM 4561 CE1 TYR C 60 49.095 7.145 -31.746 1.00 80.68 C ANISOU 4561 CE1 TYR C 60 11644 10038 8971 579 -608 -816 C ATOM 4562 CE2 TYR C 60 49.352 8.591 -29.856 1.00 83.34 C ANISOU 4562 CE2 TYR C 60 11952 10498 9217 506 -519 -1282 C ATOM 4563 CZ TYR C 60 49.454 7.335 -30.422 1.00 89.75 C ANISOU 4563 CZ TYR C 60 12776 11378 9945 480 -558 -988 C ATOM 4564 OH TYR C 60 49.894 6.282 -29.654 1.00 93.34 O ANISOU 4564 OH TYR C 60 13239 12082 10143 353 -561 -873 O ATOM 4565 N ALA C 61 47.442 12.278 -35.429 1.00 81.81 N ANISOU 4565 N ALA C 61 12025 8730 10329 1149 -1004 -930 N ATOM 4566 CA ALA C 61 46.560 13.275 -36.018 1.00 84.18 C ANISOU 4566 CA ALA C 61 12343 8716 10925 1359 -1136 -960 C ATOM 4567 C ALA C 61 45.338 13.459 -35.124 1.00 91.11 C ANISOU 4567 C ALA C 61 13011 9703 11903 1574 -1057 -1286 C ATOM 4568 O ALA C 61 44.804 12.459 -34.643 1.00 89.46 O ANISOU 4568 O ALA C 61 12628 9852 11512 1558 -929 -1333 O ATOM 4569 CB ALA C 61 46.157 12.851 -37.420 1.00 83.81 C ANISOU 4569 CB ALA C 61 12322 8622 10899 1394 -1261 -640 C ATOM 4570 N ASP C 62 44.910 14.722 -34.873 1.00 91.82 N ANISOU 4570 N ASP C 62 13115 9489 12282 1764 -1127 -1527 N ATOM 4571 CA ASP C 62 43.763 15.064 -34.009 1.00 94.79 C ANISOU 4571 CA ASP C 62 13262 9962 12791 2000 -1041 -1915 C ATOM 4572 C ASP C 62 42.517 14.189 -34.300 1.00 99.11 C ANISOU 4572 C ASP C 62 13550 10808 13301 2130 -1007 -1865 C ATOM 4573 O ASP C 62 41.809 13.809 -33.366 1.00 99.63 O ANISOU 4573 O ASP C 62 13379 11212 13265 2166 -831 -2140 O ATOM 4574 CB ASP C 62 43.374 16.551 -34.176 1.00100.86 C ANISOU 4574 CB ASP C 62 14101 10249 13972 2258 -1201 -2104 C ATOM 4575 CG ASP C 62 44.389 17.576 -33.684 1.00113.05 C ANISOU 4575 CG ASP C 62 15876 11474 15604 2143 -1223 -2264 C ATOM 4576 OD1 ASP C 62 45.326 17.184 -32.952 1.00112.11 O ANISOU 4576 OD1 ASP C 62 15804 11584 15207 1879 -1082 -2320 O ATOM 4577 OD2 ASP C 62 44.190 18.782 -33.948 1.00122.17 O ANISOU 4577 OD2 ASP C 62 17151 12152 17116 2325 -1389 -2363 O ATOM 4578 N SER C 63 42.274 13.866 -35.589 1.00 95.17 N ANISOU 4578 N SER C 63 13093 10212 12855 2163 -1170 -1520 N ATOM 4579 CA SER C 63 41.138 13.075 -36.072 1.00 94.81 C ANISOU 4579 CA SER C 63 12820 10415 12788 2259 -1183 -1436 C ATOM 4580 C SER C 63 41.122 11.637 -35.515 1.00 95.57 C ANISOU 4580 C SER C 63 12797 10980 12536 2034 -978 -1411 C ATOM 4581 O SER C 63 40.048 11.141 -35.163 1.00 96.57 O ANISOU 4581 O SER C 63 12657 11403 12632 2096 -884 -1553 O ATOM 4582 CB SER C 63 41.166 13.005 -37.597 1.00 98.01 C ANISOU 4582 CB SER C 63 13359 10623 13256 2265 -1411 -1044 C ATOM 4583 OG SER C 63 40.097 12.227 -38.112 1.00108.61 O ANISOU 4583 OG SER C 63 14484 12215 14567 2332 -1441 -964 O ATOM 4584 N VAL C 64 42.296 10.968 -35.461 1.00 87.86 N ANISOU 4584 N VAL C 64 12009 10063 11310 1773 -922 -1223 N ATOM 4585 CA VAL C 64 42.399 9.557 -35.066 1.00 84.35 C ANISOU 4585 CA VAL C 64 11513 9978 10559 1560 -782 -1130 C ATOM 4586 C VAL C 64 43.150 9.372 -33.703 1.00 86.57 C ANISOU 4586 C VAL C 64 11830 10444 10619 1393 -619 -1293 C ATOM 4587 O VAL C 64 43.239 8.243 -33.230 1.00 84.53 O ANISOU 4587 O VAL C 64 11546 10464 10107 1217 -520 -1211 O ATOM 4588 CB VAL C 64 43.120 8.740 -36.181 1.00 84.88 C ANISOU 4588 CB VAL C 64 11750 9986 10515 1416 -874 -770 C ATOM 4589 CG1 VAL C 64 42.333 8.779 -37.486 1.00 85.10 C ANISOU 4589 CG1 VAL C 64 11738 9910 10687 1536 -1033 -603 C ATOM 4590 CG2 VAL C 64 44.555 9.216 -36.405 1.00 83.51 C ANISOU 4590 CG2 VAL C 64 11810 9593 10326 1315 -927 -662 C ATOM 4591 N ALA C 65 43.651 10.465 -33.079 1.00 84.31 N ANISOU 4591 N ALA C 65 11611 9997 10426 1439 -610 -1516 N ATOM 4592 CA ALA C 65 44.417 10.455 -31.814 1.00 84.12 C ANISOU 4592 CA ALA C 65 11629 10144 10188 1276 -487 -1688 C ATOM 4593 C ALA C 65 43.660 9.780 -30.645 1.00 88.57 C ANISOU 4593 C ALA C 65 11998 11139 10515 1196 -297 -1880 C ATOM 4594 O ALA C 65 44.287 9.160 -29.783 1.00 87.03 O ANISOU 4594 O ALA C 65 11854 11182 10030 987 -219 -1856 O ATOM 4595 CB ALA C 65 44.760 11.878 -31.411 1.00 87.34 C ANISOU 4595 CB ALA C 65 12108 10289 10787 1367 -516 -1965 C ATOM 4596 N ASP C 66 42.327 9.924 -30.626 1.00 87.71 N ANISOU 4596 N ASP C 66 11658 11143 10524 1352 -235 -2064 N ATOM 4597 CA ASP C 66 41.408 9.417 -29.609 1.00 89.76 C ANISOU 4597 CA ASP C 66 11685 11839 10581 1272 -34 -2282 C ATOM 4598 C ASP C 66 41.103 7.905 -29.750 1.00 91.69 C ANISOU 4598 C ASP C 66 11896 12363 10578 1060 9 -1990 C ATOM 4599 O ASP C 66 40.763 7.275 -28.747 1.00 92.42 O ANISOU 4599 O ASP C 66 11890 12837 10387 864 175 -2075 O ATOM 4600 CB ASP C 66 40.071 10.194 -29.690 1.00 95.43 C ANISOU 4600 CB ASP C 66 12123 12565 11571 1549 3 -2604 C ATOM 4601 CG ASP C 66 39.359 10.186 -31.049 1.00108.85 C ANISOU 4601 CG ASP C 66 13749 14061 13548 1749 -168 -2409 C ATOM 4602 OD1 ASP C 66 40.050 10.319 -32.093 1.00107.51 O ANISOU 4602 OD1 ASP C 66 13804 13543 13502 1780 -362 -2114 O ATOM 4603 OD2 ASP C 66 38.108 10.205 -31.062 1.00118.37 O ANISOU 4603 OD2 ASP C 66 14655 15457 14863 1892 -116 -2589 O ATOM 4604 N ARG C 67 41.215 7.332 -30.972 1.00 85.92 N ANISOU 4604 N ARG C 67 11260 11445 9941 1074 -138 -1658 N ATOM 4605 CA ARG C 67 40.845 5.931 -31.251 1.00 84.11 C ANISOU 4605 CA ARG C 67 11011 11411 9537 890 -119 -1403 C ATOM 4606 C ARG C 67 42.052 5.046 -31.664 1.00 84.52 C ANISOU 4606 C ARG C 67 11330 11326 9458 737 -220 -1062 C ATOM 4607 O ARG C 67 42.112 3.883 -31.268 1.00 83.51 O ANISOU 4607 O ARG C 67 11249 11381 9102 526 -175 -904 O ATOM 4608 CB ARG C 67 39.800 5.903 -32.379 1.00 84.13 C ANISOU 4608 CB ARG C 67 10859 11349 9758 1040 -206 -1348 C ATOM 4609 CG ARG C 67 38.481 6.578 -31.993 1.00 96.28 C ANISOU 4609 CG ARG C 67 12067 13078 11436 1206 -112 -1687 C ATOM 4610 CD ARG C 67 37.518 6.832 -33.146 1.00102.66 C ANISOU 4610 CD ARG C 67 12707 13784 12518 1421 -256 -1654 C ATOM 4611 NE ARG C 67 37.980 7.885 -34.057 1.00104.90 N ANISOU 4611 NE ARG C 67 13136 13635 13085 1671 -466 -1591 N ATOM 4612 CZ ARG C 67 38.601 7.664 -35.210 1.00110.76 C ANISOU 4612 CZ ARG C 67 14099 14123 13860 1647 -642 -1269 C ATOM 4613 NH1 ARG C 67 38.807 6.423 -35.634 1.00 93.02 N ANISOU 4613 NH1 ARG C 67 11940 11989 11415 1425 -639 -1016 N ATOM 4614 NH2 ARG C 67 38.982 8.681 -35.972 1.00 93.52 N ANISOU 4614 NH2 ARG C 67 12053 11572 11909 1834 -825 -1206 N ATOM 4615 N PHE C 68 42.976 5.602 -32.440 1.00 79.82 N ANISOU 4615 N PHE C 68 10898 10416 9014 840 -356 -962 N ATOM 4616 CA PHE C 68 44.140 4.851 -32.902 1.00 77.39 C ANISOU 4616 CA PHE C 68 10795 9995 8615 732 -443 -692 C ATOM 4617 C PHE C 68 45.328 4.928 -31.946 1.00 80.90 C ANISOU 4617 C PHE C 68 11354 10485 8897 626 -425 -719 C ATOM 4618 O PHE C 68 45.471 5.887 -31.187 1.00 82.45 O ANISOU 4618 O PHE C 68 11521 10702 9103 658 -376 -950 O ATOM 4619 CB PHE C 68 44.560 5.324 -34.296 1.00 78.13 C ANISOU 4619 CB PHE C 68 10987 9789 8911 851 -585 -559 C ATOM 4620 CG PHE C 68 43.550 5.027 -35.367 1.00 80.05 C ANISOU 4620 CG PHE C 68 11146 10006 9265 922 -646 -468 C ATOM 4621 CD1 PHE C 68 42.199 4.977 -35.069 1.00 85.60 C ANISOU 4621 CD1 PHE C 68 11635 10890 9998 966 -583 -603 C ATOM 4622 CD2 PHE C 68 43.952 4.797 -36.672 1.00 80.83 C ANISOU 4622 CD2 PHE C 68 11357 9936 9418 930 -765 -264 C ATOM 4623 CE1 PHE C 68 41.267 4.703 -36.052 1.00 86.96 C ANISOU 4623 CE1 PHE C 68 11705 11067 10268 1022 -660 -524 C ATOM 4624 CE2 PHE C 68 43.025 4.522 -37.660 1.00 84.16 C ANISOU 4624 CE2 PHE C 68 11704 10362 9913 976 -838 -183 C ATOM 4625 CZ PHE C 68 41.680 4.476 -37.350 1.00 84.27 C ANISOU 4625 CZ PHE C 68 11502 10548 9971 1025 -798 -307 C ATOM 4626 N THR C 69 46.175 3.905 -31.995 1.00 75.34 N ANISOU 4626 N THR C 69 10774 9796 8056 510 -478 -497 N ATOM 4627 CA THR C 69 47.373 3.832 -31.150 1.00 75.05 C ANISOU 4627 CA THR C 69 10831 9824 7862 415 -503 -481 C ATOM 4628 C THR C 69 48.498 3.181 -31.968 1.00 75.96 C ANISOU 4628 C THR C 69 11064 9787 8012 420 -622 -256 C ATOM 4629 O THR C 69 48.274 2.138 -32.582 1.00 74.72 O ANISOU 4629 O THR C 69 10940 9596 7855 408 -656 -83 O ATOM 4630 CB THR C 69 47.067 3.065 -29.847 1.00 87.54 C ANISOU 4630 CB THR C 69 12395 11704 9164 244 -431 -475 C ATOM 4631 OG1 THR C 69 45.828 3.524 -29.296 1.00 91.03 O ANISOU 4631 OG1 THR C 69 12681 12329 9576 235 -288 -699 O ATOM 4632 CG2 THR C 69 48.203 3.168 -28.811 1.00 86.47 C ANISOU 4632 CG2 THR C 69 12333 11683 8839 147 -474 -492 C ATOM 4633 N THR C 70 49.690 3.797 -32.008 1.00 71.12 N ANISOU 4633 N THR C 70 10498 9089 7435 433 -680 -285 N ATOM 4634 CA THR C 70 50.789 3.227 -32.790 1.00 69.30 C ANISOU 4634 CA THR C 70 10328 8760 7240 445 -773 -118 C ATOM 4635 C THR C 70 51.927 2.797 -31.852 1.00 72.34 C ANISOU 4635 C THR C 70 10732 9282 7471 376 -838 -80 C ATOM 4636 O THR C 70 52.092 3.358 -30.767 1.00 73.30 O ANISOU 4636 O THR C 70 10834 9540 7477 306 -821 -209 O ATOM 4637 CB THR C 70 51.297 4.215 -33.878 1.00 77.83 C ANISOU 4637 CB THR C 70 11425 9648 8498 496 -798 -147 C ATOM 4638 OG1 THR C 70 52.237 3.550 -34.719 1.00 77.55 O ANISOU 4638 OG1 THR C 70 11414 9575 8478 499 -853 -11 O ATOM 4639 CG2 THR C 70 51.919 5.494 -33.309 1.00 76.98 C ANISOU 4639 CG2 THR C 70 11317 9513 8418 452 -796 -315 C ATOM 4640 N SER C 71 52.681 1.772 -32.268 1.00 67.51 N ANISOU 4640 N SER C 71 10149 8642 6859 405 -925 84 N ATOM 4641 CA SER C 71 53.830 1.259 -31.520 1.00 68.06 C ANISOU 4641 CA SER C 71 10216 8825 6819 383 -1034 149 C ATOM 4642 C SER C 71 54.889 0.732 -32.483 1.00 70.25 C ANISOU 4642 C SER C 71 10464 9010 7216 478 -1110 225 C ATOM 4643 O SER C 71 54.583 0.427 -33.638 1.00 68.26 O ANISOU 4643 O SER C 71 10229 8623 7083 539 -1074 259 O ATOM 4644 CB SER C 71 53.418 0.169 -30.530 1.00 72.54 C ANISOU 4644 CB SER C 71 10849 9508 7207 321 -1086 289 C ATOM 4645 OG SER C 71 53.001 -1.032 -31.161 1.00 79.46 O ANISOU 4645 OG SER C 71 11794 10254 8144 365 -1119 453 O ATOM 4646 N ARG C 72 56.138 0.646 -32.018 1.00 67.17 N ANISOU 4646 N ARG C 72 10010 8723 6788 489 -1213 227 N ATOM 4647 CA ARG C 72 57.215 0.150 -32.853 1.00 66.33 C ANISOU 4647 CA ARG C 72 9824 8579 6797 593 -1275 253 C ATOM 4648 C ARG C 72 58.032 -0.870 -32.064 1.00 71.16 C ANISOU 4648 C ARG C 72 10409 9278 7352 671 -1451 362 C ATOM 4649 O ARG C 72 58.504 -0.590 -30.950 1.00 72.21 O ANISOU 4649 O ARG C 72 10508 9577 7350 607 -1540 358 O ATOM 4650 CB ARG C 72 58.093 1.304 -33.371 1.00 65.27 C ANISOU 4650 CB ARG C 72 9580 8492 6730 534 -1225 113 C ATOM 4651 CG ARG C 72 59.086 0.895 -34.447 1.00 71.09 C ANISOU 4651 CG ARG C 72 10202 9233 7578 615 -1231 100 C ATOM 4652 CD ARG C 72 60.002 2.036 -34.859 1.00 78.33 C ANISOU 4652 CD ARG C 72 11001 10236 8523 492 -1177 -21 C ATOM 4653 NE ARG C 72 60.953 1.596 -35.881 1.00 85.99 N ANISOU 4653 NE ARG C 72 11826 11275 9571 549 -1156 -58 N ATOM 4654 CZ ARG C 72 62.129 1.032 -35.618 1.00 98.21 C ANISOU 4654 CZ ARG C 72 13186 12988 11140 640 -1249 -101 C ATOM 4655 NH1 ARG C 72 62.516 0.839 -34.367 1.00 82.92 N ANISOU 4655 NH1 ARG C 72 11205 11157 9141 673 -1397 -75 N ATOM 4656 NH2 ARG C 72 62.919 0.646 -36.606 1.00 85.38 N ANISOU 4656 NH2 ARG C 72 11402 11447 9590 701 -1200 -179 N ATOM 4657 N ASP C 73 58.126 -2.082 -32.628 1.00 66.82 N ANISOU 4657 N ASP C 73 9888 8599 6903 811 -1518 461 N ATOM 4658 CA ASP C 73 58.905 -3.181 -32.095 1.00 67.90 C ANISOU 4658 CA ASP C 73 10009 8737 7053 943 -1720 580 C ATOM 4659 C ASP C 73 60.285 -3.054 -32.670 1.00 70.84 C ANISOU 4659 C ASP C 73 10169 9193 7554 1068 -1760 457 C ATOM 4660 O ASP C 73 60.525 -3.501 -33.786 1.00 69.76 O ANISOU 4660 O ASP C 73 9977 8956 7571 1187 -1710 386 O ATOM 4661 CB ASP C 73 58.234 -4.536 -32.416 1.00 70.05 C ANISOU 4661 CB ASP C 73 10439 8777 7400 1028 -1774 725 C ATOM 4662 CG ASP C 73 58.876 -5.769 -31.789 1.00 82.68 C ANISOU 4662 CG ASP C 73 12082 10295 9036 1175 -2023 893 C ATOM 4663 OD1 ASP C 73 59.949 -5.629 -31.135 1.00 84.74 O ANISOU 4663 OD1 ASP C 73 12215 10713 9269 1244 -2174 898 O ATOM 4664 OD2 ASP C 73 58.296 -6.866 -31.920 1.00 88.79 O ANISOU 4664 OD2 ASP C 73 13024 10843 9871 1212 -2087 1027 O ATOM 4665 N VAL C 74 61.170 -2.350 -31.948 1.00 68.00 N ANISOU 4665 N VAL C 74 9669 9051 7115 1012 -1830 397 N ATOM 4666 CA VAL C 74 62.550 -2.059 -32.352 1.00 68.65 C ANISOU 4666 CA VAL C 74 9496 9293 7294 1080 -1862 257 C ATOM 4667 C VAL C 74 63.300 -3.378 -32.709 1.00 74.16 C ANISOU 4667 C VAL C 74 10091 9923 8163 1358 -2014 288 C ATOM 4668 O VAL C 74 64.034 -3.402 -33.699 1.00 73.71 O ANISOU 4668 O VAL C 74 9844 9916 8247 1451 -1940 129 O ATOM 4669 CB VAL C 74 63.316 -1.258 -31.256 1.00 73.83 C ANISOU 4669 CB VAL C 74 10030 10209 7813 957 -1964 212 C ATOM 4670 CG1 VAL C 74 62.823 0.181 -31.176 1.00 71.84 C ANISOU 4670 CG1 VAL C 74 9835 9997 7463 706 -1792 93 C ATOM 4671 CG2 VAL C 74 63.235 -1.938 -29.885 1.00 75.77 C ANISOU 4671 CG2 VAL C 74 10371 10510 7909 989 -2191 397 C ATOM 4672 N ALA C 75 63.053 -4.469 -31.941 1.00 72.50 N ANISOU 4672 N ALA C 75 10019 9585 7941 1480 -2219 487 N ATOM 4673 CA ALA C 75 63.673 -5.780 -32.116 1.00 74.80 C ANISOU 4673 CA ALA C 75 10260 9737 8423 1771 -2414 538 C ATOM 4674 C ALA C 75 63.302 -6.404 -33.467 1.00 79.32 C ANISOU 4674 C ALA C 75 10875 10080 9183 1889 -2273 429 C ATOM 4675 O ALA C 75 64.194 -6.789 -34.223 1.00 80.72 O ANISOU 4675 O ALA C 75 10843 10280 9545 2094 -2279 256 O ATOM 4676 CB ALA C 75 63.253 -6.701 -30.989 1.00 77.17 C ANISOU 4676 CB ALA C 75 10782 9897 8642 1804 -2659 825 C ATOM 4677 N ASN C 76 61.990 -6.482 -33.774 1.00 74.75 N ANISOU 4677 N ASN C 76 10543 9316 8545 1751 -2140 503 N ATOM 4678 CA ASN C 76 61.478 -7.055 -35.021 1.00 74.14 C ANISOU 4678 CA ASN C 76 10536 9032 8601 1815 -2011 404 C ATOM 4679 C ASN C 76 61.455 -6.037 -36.165 1.00 77.44 C ANISOU 4679 C ASN C 76 10835 9596 8992 1688 -1753 200 C ATOM 4680 O ASN C 76 61.180 -6.425 -37.303 1.00 77.58 O ANISOU 4680 O ASN C 76 10876 9509 9093 1729 -1640 86 O ATOM 4681 CB ASN C 76 60.062 -7.607 -34.820 1.00 74.09 C ANISOU 4681 CB ASN C 76 10828 8790 8532 1694 -2004 583 C ATOM 4682 CG ASN C 76 59.973 -8.920 -34.085 1.00119.02 C ANISOU 4682 CG ASN C 76 16696 14238 14289 1809 -2249 794 C ATOM 4683 OD1 ASN C 76 60.894 -9.737 -34.131 1.00118.80 O ANISOU 4683 OD1 ASN C 76 16893 14112 14136 1642 -2283 1001 O ATOM 4684 ND2 ASN C 76 58.882 -9.146 -33.353 1.00118.87 N ANISOU 4684 ND2 ASN C 76 16580 14106 14477 2092 -2430 748 N ATOM 4685 N ASN C 77 61.757 -4.750 -35.878 1.00 73.08 N ANISOU 4685 N ASN C 77 10171 9276 8318 1520 -1672 158 N ATOM 4686 CA ASN C 77 61.729 -3.637 -36.843 1.00 71.35 C ANISOU 4686 CA ASN C 77 9879 9177 8054 1353 -1456 20 C ATOM 4687 C ASN C 77 60.306 -3.566 -37.440 1.00 73.41 C ANISOU 4687 C ASN C 77 10359 9264 8271 1241 -1335 80 C ATOM 4688 O ASN C 77 60.124 -3.389 -38.651 1.00 72.83 O ANISOU 4688 O ASN C 77 10277 9184 8211 1196 -1197 -13 O ATOM 4689 CB ASN C 77 62.828 -3.801 -37.924 1.00 73.38 C ANISOU 4689 CB ASN C 77 9896 9570 8415 1452 -1379 -188 C ATOM 4690 CG ASN C 77 63.025 -2.597 -38.815 1.00 96.20 C ANISOU 4690 CG ASN C 77 12698 12630 11223 1231 -1179 -295 C ATOM 4691 OD1 ASN C 77 62.762 -1.456 -38.424 1.00 91.54 O ANISOU 4691 OD1 ASN C 77 12165 12085 10533 1026 -1139 -236 O ATOM 4692 ND2 ASN C 77 63.586 -2.816 -39.998 1.00 87.16 N ANISOU 4692 ND2 ASN C 77 11407 11592 10117 1261 -1057 -466 N ATOM 4693 N THR C 78 59.298 -3.770 -36.569 1.00 68.99 N ANISOU 4693 N THR C 78 9982 8589 7641 1189 -1398 238 N ATOM 4694 CA THR C 78 57.894 -3.817 -36.964 1.00 67.15 C ANISOU 4694 CA THR C 78 9925 8216 7373 1094 -1311 298 C ATOM 4695 C THR C 78 57.144 -2.600 -36.425 1.00 69.22 C ANISOU 4695 C THR C 78 10231 8550 7521 922 -1237 324 C ATOM 4696 O THR C 78 57.302 -2.243 -35.265 1.00 69.87 O ANISOU 4696 O THR C 78 10305 8725 7516 875 -1297 361 O ATOM 4697 CB THR C 78 57.249 -5.126 -36.457 1.00 76.30 C ANISOU 4697 CB THR C 78 11244 9192 8555 1154 -1428 439 C ATOM 4698 OG1 THR C 78 58.052 -6.241 -36.840 1.00 76.20 O ANISOU 4698 OG1 THR C 78 11195 9068 8689 1352 -1530 395 O ATOM 4699 CG2 THR C 78 55.820 -5.321 -36.971 1.00 74.99 C ANISOU 4699 CG2 THR C 78 11223 8904 8365 1045 -1340 480 C ATOM 4700 N LEU C 79 56.320 -1.980 -37.269 1.00 64.06 N ANISOU 4700 N LEU C 79 9621 7851 6867 837 -1119 292 N ATOM 4701 CA LEU C 79 55.471 -0.850 -36.903 1.00 63.22 C ANISOU 4701 CA LEU C 79 9554 7763 6704 719 -1055 290 C ATOM 4702 C LEU C 79 54.026 -1.326 -36.795 1.00 66.40 C ANISOU 4702 C LEU C 79 10061 8084 7084 692 -1037 362 C ATOM 4703 O LEU C 79 53.580 -2.121 -37.629 1.00 65.46 O ANISOU 4703 O LEU C 79 9990 7874 7009 720 -1033 389 O ATOM 4704 CB LEU C 79 55.620 0.280 -37.940 1.00 62.97 C ANISOU 4704 CB LEU C 79 9489 7730 6708 651 -970 222 C ATOM 4705 CG LEU C 79 54.810 1.558 -37.727 1.00 67.37 C ANISOU 4705 CG LEU C 79 10089 8243 7264 567 -927 203 C ATOM 4706 CD1 LEU C 79 55.202 2.264 -36.449 1.00 68.23 C ANISOU 4706 CD1 LEU C 79 10168 8427 7329 520 -949 138 C ATOM 4707 CD2 LEU C 79 54.983 2.496 -38.887 1.00 69.71 C ANISOU 4707 CD2 LEU C 79 10395 8489 7603 495 -883 194 C ATOM 4708 N TYR C 80 53.307 -0.880 -35.754 1.00 63.28 N ANISOU 4708 N TYR C 80 9686 7748 6610 624 -1022 368 N ATOM 4709 CA TYR C 80 51.922 -1.298 -35.535 1.00 63.25 C ANISOU 4709 CA TYR C 80 9736 7728 6568 569 -988 418 C ATOM 4710 C TYR C 80 50.976 -0.100 -35.504 1.00 67.45 C ANISOU 4710 C TYR C 80 10220 8294 7113 534 -903 321 C ATOM 4711 O TYR C 80 51.393 1.002 -35.154 1.00 67.00 O ANISOU 4711 O TYR C 80 10124 8268 7063 532 -884 224 O ATOM 4712 CB TYR C 80 51.781 -2.093 -34.223 1.00 65.64 C ANISOU 4712 CB TYR C 80 10093 8108 6740 505 -1041 514 C ATOM 4713 CG TYR C 80 52.645 -3.333 -34.117 1.00 68.18 C ANISOU 4713 CG TYR C 80 10480 8348 7075 568 -1172 636 C ATOM 4714 CD1 TYR C 80 52.224 -4.550 -34.650 1.00 69.97 C ANISOU 4714 CD1 TYR C 80 10803 8419 7363 577 -1214 727 C ATOM 4715 CD2 TYR C 80 53.830 -3.318 -33.384 1.00 70.16 C ANISOU 4715 CD2 TYR C 80 10699 8675 7285 618 -1274 655 C ATOM 4716 CE1 TYR C 80 53.000 -5.704 -34.523 1.00 71.13 C ANISOU 4716 CE1 TYR C 80 11026 8437 7565 667 -1357 827 C ATOM 4717 CE2 TYR C 80 54.611 -4.467 -33.244 1.00 72.42 C ANISOU 4717 CE2 TYR C 80 11033 8869 7615 717 -1429 770 C ATOM 4718 CZ TYR C 80 54.189 -5.660 -33.810 1.00 77.99 C ANISOU 4718 CZ TYR C 80 11849 9373 8412 754 -1472 855 C ATOM 4719 OH TYR C 80 54.959 -6.791 -33.664 1.00 78.23 O ANISOU 4719 OH TYR C 80 11939 9259 8527 884 -1647 955 O ATOM 4720 N LEU C 81 49.697 -0.325 -35.866 1.00 64.83 N ANISOU 4720 N LEU C 81 9884 7949 6801 511 -864 334 N ATOM 4721 CA LEU C 81 48.666 0.713 -35.847 1.00 65.43 C ANISOU 4721 CA LEU C 81 9882 8054 6923 521 -803 230 C ATOM 4722 C LEU C 81 47.340 0.110 -35.399 1.00 70.88 C ANISOU 4722 C LEU C 81 10525 8853 7553 449 -754 237 C ATOM 4723 O LEU C 81 46.589 -0.441 -36.213 1.00 70.21 O ANISOU 4723 O LEU C 81 10430 8734 7512 435 -767 289 O ATOM 4724 CB LEU C 81 48.514 1.411 -37.221 1.00 64.77 C ANISOU 4724 CB LEU C 81 9793 7843 6972 590 -829 226 C ATOM 4725 CG LEU C 81 47.534 2.603 -37.293 1.00 69.69 C ANISOU 4725 CG LEU C 81 10341 8441 7699 653 -815 127 C ATOM 4726 CD1 LEU C 81 47.976 3.748 -36.380 1.00 70.69 C ANISOU 4726 CD1 LEU C 81 10454 8557 7848 674 -787 -12 C ATOM 4727 CD2 LEU C 81 47.407 3.107 -38.701 1.00 70.99 C ANISOU 4727 CD2 LEU C 81 10534 8474 7966 702 -885 192 C ATOM 4728 N GLN C 82 47.065 0.209 -34.091 1.00 68.95 N ANISOU 4728 N GLN C 82 10242 8773 7184 373 -693 176 N ATOM 4729 CA GLN C 82 45.831 -0.285 -33.492 1.00 70.18 C ANISOU 4729 CA GLN C 82 10324 9100 7242 256 -615 164 C ATOM 4730 C GLN C 82 44.714 0.696 -33.810 1.00 74.64 C ANISOU 4730 C GLN C 82 10721 9714 7926 342 -550 -9 C ATOM 4731 O GLN C 82 44.772 1.851 -33.390 1.00 74.81 O ANISOU 4731 O GLN C 82 10676 9751 7996 431 -512 -183 O ATOM 4732 CB GLN C 82 45.994 -0.500 -31.965 1.00 72.96 C ANISOU 4732 CB GLN C 82 10694 9657 7370 116 -565 157 C ATOM 4733 CG GLN C 82 44.799 -1.197 -31.301 1.00 82.24 C ANISOU 4733 CG GLN C 82 11808 11051 8390 -78 -471 181 C ATOM 4734 CD GLN C 82 44.602 -2.608 -31.806 1.00 98.28 C ANISOU 4734 CD GLN C 82 13954 12974 10414 -193 -542 405 C ATOM 4735 OE1 GLN C 82 45.550 -3.374 -31.957 1.00 93.83 O ANISOU 4735 OE1 GLN C 82 13559 12238 9854 -181 -663 574 O ATOM 4736 NE2 GLN C 82 43.358 -3.010 -31.998 1.00 90.50 N ANISOU 4736 NE2 GLN C 82 12871 12097 9420 -317 -470 395 N ATOM 4737 N MET C 83 43.730 0.251 -34.589 1.00 71.06 N ANISOU 4737 N MET C 83 10197 9265 7539 329 -558 29 N ATOM 4738 CA MET C 83 42.615 1.098 -34.989 1.00 71.82 C ANISOU 4738 CA MET C 83 10105 9410 7774 441 -535 -118 C ATOM 4739 C MET C 83 41.316 0.594 -34.369 1.00 77.49 C ANISOU 4739 C MET C 83 10644 10400 8400 306 -427 -191 C ATOM 4740 O MET C 83 40.755 -0.395 -34.846 1.00 77.21 O ANISOU 4740 O MET C 83 10604 10401 8333 178 -448 -76 O ATOM 4741 CB MET C 83 42.494 1.145 -36.516 1.00 73.16 C ANISOU 4741 CB MET C 83 10298 9404 8094 537 -657 -26 C ATOM 4742 CG MET C 83 43.770 1.491 -37.233 1.00 75.14 C ANISOU 4742 CG MET C 83 10720 9435 8396 610 -743 62 C ATOM 4743 SD MET C 83 43.486 1.718 -39.005 1.00 79.01 S ANISOU 4743 SD MET C 83 11227 9785 9008 690 -876 158 S ATOM 4744 CE MET C 83 42.848 0.135 -39.459 1.00 75.68 C ANISOU 4744 CE MET C 83 10806 9458 8492 533 -880 247 C ATOM 4745 N ASN C 84 40.851 1.255 -33.297 1.00 75.80 N ANISOU 4745 N ASN C 84 10278 10393 8131 311 -302 -401 N ATOM 4746 CA ASN C 84 39.616 0.874 -32.604 1.00 78.15 C ANISOU 4746 CA ASN C 84 10360 11021 8312 159 -160 -511 C ATOM 4747 C ASN C 84 38.513 1.899 -32.869 1.00 83.76 C ANISOU 4747 C ASN C 84 10777 11825 9224 365 -129 -768 C ATOM 4748 O ASN C 84 38.809 3.007 -33.328 1.00 83.24 O ANISOU 4748 O ASN C 84 10717 11543 9369 621 -215 -864 O ATOM 4749 CB ASN C 84 39.858 0.727 -31.096 1.00 81.42 C ANISOU 4749 CB ASN C 84 10795 11681 8460 -26 -19 -579 C ATOM 4750 CG ASN C 84 40.837 -0.361 -30.714 1.00107.16 C ANISOU 4750 CG ASN C 84 14327 14871 11519 -227 -80 -304 C ATOM 4751 OD1 ASN C 84 41.427 -1.043 -31.560 1.00101.70 O ANISOU 4751 OD1 ASN C 84 13812 13926 10904 -211 -218 -86 O ATOM 4752 ND2 ASN C 84 41.028 -0.550 -29.420 1.00101.32 N ANISOU 4752 ND2 ASN C 84 13622 14363 10512 -414 12 -318 N ATOM 4753 N SER C 85 37.232 1.514 -32.594 1.00 82.14 N ANISOU 4753 N SER C 85 10308 11938 8964 246 -17 -875 N ATOM 4754 CA SER C 85 36.023 2.329 -32.800 1.00 84.31 C ANISOU 4754 CA SER C 85 10233 12366 9436 444 12 -1139 C ATOM 4755 C SER C 85 36.038 2.945 -34.213 1.00 88.11 C ANISOU 4755 C SER C 85 10737 12527 10213 725 -213 -1063 C ATOM 4756 O SER C 85 35.811 4.150 -34.379 1.00 89.25 O ANISOU 4756 O SER C 85 10760 12559 10591 1021 -272 -1251 O ATOM 4757 CB SER C 85 35.912 3.413 -31.729 1.00 89.54 C ANISOU 4757 CB SER C 85 10739 13172 10112 582 157 -1487 C ATOM 4758 OG SER C 85 35.892 2.849 -30.429 1.00 99.13 O ANISOU 4758 OG SER C 85 11936 14728 11000 288 364 -1548 O ATOM 4759 N LEU C 86 36.353 2.101 -35.226 1.00 82.93 N ANISOU 4759 N LEU C 86 10263 11712 9534 621 -347 -782 N ATOM 4760 CA LEU C 86 36.492 2.493 -36.627 1.00 81.83 C ANISOU 4760 CA LEU C 86 10199 11302 9590 808 -563 -653 C ATOM 4761 C LEU C 86 35.152 2.950 -37.212 1.00 88.75 C ANISOU 4761 C LEU C 86 10749 12315 10658 975 -648 -776 C ATOM 4762 O LEU C 86 34.165 2.214 -37.181 1.00 89.60 O ANISOU 4762 O LEU C 86 10639 12708 10699 817 -594 -809 O ATOM 4763 CB LEU C 86 37.074 1.336 -37.473 1.00 79.48 C ANISOU 4763 CB LEU C 86 10147 10877 9176 617 -649 -378 C ATOM 4764 CG LEU C 86 38.587 1.068 -37.311 1.00 81.33 C ANISOU 4764 CG LEU C 86 10708 10887 9305 556 -648 -234 C ATOM 4765 CD1 LEU C 86 38.968 -0.312 -37.799 1.00 80.15 C ANISOU 4765 CD1 LEU C 86 10743 10683 9029 345 -681 -38 C ATOM 4766 CD2 LEU C 86 39.424 2.145 -37.993 1.00 81.26 C ANISOU 4766 CD2 LEU C 86 10832 10602 9441 772 -770 -203 C ATOM 4767 N LYS C 87 35.139 4.197 -37.713 1.00 86.52 N ANISOU 4767 N LYS C 87 10433 11819 10622 1292 -796 -841 N ATOM 4768 CA LYS C 87 33.998 4.848 -38.351 1.00 89.39 C ANISOU 4768 CA LYS C 87 10505 12236 11224 1536 -946 -939 C ATOM 4769 C LYS C 87 34.199 4.874 -39.878 1.00 93.61 C ANISOU 4769 C LYS C 87 11204 12539 11826 1594 -1214 -665 C ATOM 4770 O LYS C 87 35.286 4.548 -40.358 1.00 89.75 O ANISOU 4770 O LYS C 87 11044 11841 11215 1469 -1251 -450 O ATOM 4771 CB LYS C 87 33.799 6.270 -37.790 1.00 94.41 C ANISOU 4771 CB LYS C 87 10999 12760 12111 1870 -950 -1210 C ATOM 4772 CG LYS C 87 35.010 7.190 -37.939 1.00107.53 C ANISOU 4772 CG LYS C 87 12997 13995 13866 1998 -1044 -1124 C ATOM 4773 CD LYS C 87 34.739 8.573 -37.385 1.00121.33 C ANISOU 4773 CD LYS C 87 14615 15593 15891 2323 -1061 -1419 C ATOM 4774 CE LYS C 87 35.963 9.448 -37.475 1.00132.36 C ANISOU 4774 CE LYS C 87 16361 16564 17367 2386 -1145 -1334 C ATOM 4775 NZ LYS C 87 35.698 10.824 -36.983 1.00145.32 N ANISOU 4775 NZ LYS C 87 17910 17991 19315 2705 -1186 -1634 N ATOM 4776 N HIS C 88 33.164 5.292 -40.642 1.00 94.65 N ANISOU 4776 N HIS C 88 11091 12730 12144 1787 -1409 -681 N ATOM 4777 CA HIS C 88 33.231 5.348 -42.107 1.00 94.84 C ANISOU 4777 CA HIS C 88 11250 12588 12197 1826 -1685 -418 C ATOM 4778 C HIS C 88 34.355 6.285 -42.593 1.00 97.80 C ANISOU 4778 C HIS C 88 11969 12546 12645 1954 -1819 -250 C ATOM 4779 O HIS C 88 35.013 5.968 -43.585 1.00 95.41 O ANISOU 4779 O HIS C 88 11923 12119 12209 1821 -1930 2 O ATOM 4780 CB HIS C 88 31.893 5.799 -42.709 1.00 99.75 C ANISOU 4780 CB HIS C 88 11520 13354 13027 2053 -1903 -477 C ATOM 4781 CG HIS C 88 31.944 5.963 -44.198 1.00103.97 C ANISOU 4781 CG HIS C 88 12202 13734 13567 2094 -2217 -190 C ATOM 4782 ND1 HIS C 88 31.917 4.868 -45.046 1.00104.83 N ANISOU 4782 ND1 HIS C 88 12390 13995 13444 1813 -2264 -22 N ATOM 4783 CD2 HIS C 88 32.033 7.090 -44.941 1.00107.79 C ANISOU 4783 CD2 HIS C 88 12786 13927 14243 2361 -2498 -47 C ATOM 4784 CE1 HIS C 88 31.995 5.362 -46.272 1.00105.31 C ANISOU 4784 CE1 HIS C 88 12583 13900 13530 1908 -2556 208 C ATOM 4785 NE2 HIS C 88 32.061 6.695 -46.260 1.00107.50 N ANISOU 4785 NE2 HIS C 88 12884 13904 14056 2229 -2715 227 N ATOM 4786 N GLU C 89 34.592 7.409 -41.878 1.00 96.11 N ANISOU 4786 N GLU C 89 11760 12130 12626 2180 -1792 -408 N ATOM 4787 CA GLU C 89 35.623 8.407 -42.210 1.00 95.60 C ANISOU 4787 CA GLU C 89 12012 11656 12655 2277 -1910 -272 C ATOM 4788 C GLU C 89 37.048 7.790 -42.251 1.00 95.27 C ANISOU 4788 C GLU C 89 12312 11533 12355 1989 -1784 -106 C ATOM 4789 O GLU C 89 37.979 8.430 -42.751 1.00 94.44 O ANISOU 4789 O GLU C 89 12477 11138 12268 1987 -1882 57 O ATOM 4790 CB GLU C 89 35.601 9.559 -41.191 1.00 99.18 C ANISOU 4790 CB GLU C 89 12394 11938 13351 2523 -1851 -548 C ATOM 4791 CG GLU C 89 34.276 10.301 -41.102 1.00115.70 C ANISOU 4791 CG GLU C 89 14134 14072 15755 2872 -1980 -765 C ATOM 4792 CD GLU C 89 34.237 11.472 -40.134 1.00145.27 C ANISOU 4792 CD GLU C 89 17808 17618 19768 3144 -1925 -1090 C ATOM 4793 OE1 GLU C 89 33.126 11.994 -39.889 1.00147.09 O ANISOU 4793 OE1 GLU C 89 17695 17932 20262 3448 -1984 -1348 O ATOM 4794 OE2 GLU C 89 35.308 11.867 -39.616 1.00138.76 O ANISOU 4794 OE2 GLU C 89 17255 16569 18899 3057 -1825 -1116 O ATOM 4795 N ASP C 90 37.200 6.545 -41.747 1.00 88.84 N ANISOU 4795 N ASP C 90 11474 10972 11307 1745 -1579 -142 N ATOM 4796 CA ASP C 90 38.476 5.836 -41.685 1.00 84.99 C ANISOU 4796 CA ASP C 90 11255 10436 10599 1509 -1462 -22 C ATOM 4797 C ASP C 90 38.681 4.907 -42.899 1.00 86.95 C ANISOU 4797 C ASP C 90 11630 10728 10682 1333 -1550 199 C ATOM 4798 O ASP C 90 39.817 4.489 -43.134 1.00 84.38 O ANISOU 4798 O ASP C 90 11531 10317 10212 1188 -1498 307 O ATOM 4799 CB ASP C 90 38.566 5.016 -40.388 1.00 85.37 C ANISOU 4799 CB ASP C 90 11237 10698 10502 1357 -1219 -176 C ATOM 4800 CG ASP C 90 38.519 5.844 -39.113 1.00 92.44 C ANISOU 4800 CG ASP C 90 12032 11599 11492 1480 -1098 -426 C ATOM 4801 OD1 ASP C 90 38.971 7.013 -39.141 1.00 92.85 O ANISOU 4801 OD1 ASP C 90 12179 11395 11706 1644 -1176 -464 O ATOM 4802 OD2 ASP C 90 38.113 5.298 -38.073 1.00 97.94 O ANISOU 4802 OD2 ASP C 90 12582 12552 12078 1377 -919 -581 O ATOM 4803 N THR C 91 37.606 4.606 -43.673 1.00 84.50 N ANISOU 4803 N THR C 91 11155 10562 10390 1350 -1684 242 N ATOM 4804 CA THR C 91 37.672 3.760 -44.876 1.00 83.35 C ANISOU 4804 CA THR C 91 11112 10481 10077 1178 -1779 412 C ATOM 4805 C THR C 91 38.622 4.442 -45.890 1.00 86.25 C ANISOU 4805 C THR C 91 11741 10621 10408 1189 -1916 613 C ATOM 4806 O THR C 91 38.271 5.480 -46.462 1.00 88.61 O ANISOU 4806 O THR C 91 12032 10796 10839 1351 -2120 711 O ATOM 4807 CB THR C 91 36.245 3.521 -45.438 1.00 94.12 C ANISOU 4807 CB THR C 91 12213 12062 11488 1209 -1925 395 C ATOM 4808 OG1 THR C 91 35.451 2.865 -44.456 1.00 94.96 O ANISOU 4808 OG1 THR C 91 12075 12406 11600 1141 -1764 207 O ATOM 4809 CG2 THR C 91 36.234 2.717 -46.731 1.00 92.28 C ANISOU 4809 CG2 THR C 91 12080 11911 11070 1023 -2045 544 C ATOM 4810 N ALA C 92 39.851 3.881 -46.050 1.00 79.32 N ANISOU 4810 N ALA C 92 11090 9691 9358 1014 -1803 672 N ATOM 4811 CA ALA C 92 40.909 4.418 -46.925 1.00 78.39 C ANISOU 4811 CA ALA C 92 11211 9417 9158 959 -1873 840 C ATOM 4812 C ALA C 92 42.014 3.393 -47.184 1.00 78.16 C ANISOU 4812 C ALA C 92 11335 9442 8920 756 -1729 840 C ATOM 4813 O ALA C 92 42.034 2.336 -46.556 1.00 76.24 O ANISOU 4813 O ALA C 92 11046 9292 8632 687 -1590 724 O ATOM 4814 CB ALA C 92 41.522 5.665 -46.287 1.00 79.58 C ANISOU 4814 CB ALA C 92 11439 9333 9462 1080 -1864 832 C ATOM 4815 N VAL C 93 42.950 3.721 -48.094 1.00 74.25 N ANISOU 4815 N VAL C 93 11021 8888 8303 660 -1765 969 N ATOM 4816 CA VAL C 93 44.120 2.887 -48.373 1.00 72.75 C ANISOU 4816 CA VAL C 93 10948 8756 7938 501 -1622 933 C ATOM 4817 C VAL C 93 45.238 3.361 -47.452 1.00 77.10 C ANISOU 4817 C VAL C 93 11553 9187 8556 527 -1496 884 C ATOM 4818 O VAL C 93 45.722 4.482 -47.606 1.00 77.69 O ANISOU 4818 O VAL C 93 11713 9135 8671 530 -1548 980 O ATOM 4819 CB VAL C 93 44.537 2.899 -49.864 1.00 77.58 C ANISOU 4819 CB VAL C 93 11688 9450 8338 347 -1696 1059 C ATOM 4820 CG1 VAL C 93 45.683 1.927 -50.107 1.00 76.11 C ANISOU 4820 CG1 VAL C 93 11571 9356 7993 214 -1525 947 C ATOM 4821 CG2 VAL C 93 43.361 2.566 -50.770 1.00 79.11 C ANISOU 4821 CG2 VAL C 93 11824 9779 8456 317 -1859 1115 C ATOM 4822 N TYR C 94 45.598 2.547 -46.457 1.00 73.44 N ANISOU 4822 N TYR C 94 11044 8752 8108 535 -1353 748 N ATOM 4823 CA TYR C 94 46.611 2.908 -45.466 1.00 72.83 C ANISOU 4823 CA TYR C 94 10991 8600 8081 558 -1250 687 C ATOM 4824 C TYR C 94 48.007 2.501 -45.935 1.00 76.66 C ANISOU 4824 C TYR C 94 11557 9129 8442 450 -1166 680 C ATOM 4825 O TYR C 94 48.257 1.336 -46.256 1.00 75.55 O ANISOU 4825 O TYR C 94 11418 9076 8214 406 -1113 618 O ATOM 4826 CB TYR C 94 46.292 2.266 -44.110 1.00 73.31 C ANISOU 4826 CB TYR C 94 10962 8695 8197 612 -1164 568 C ATOM 4827 CG TYR C 94 45.146 2.944 -43.391 1.00 75.97 C ANISOU 4827 CG TYR C 94 11182 9019 8665 723 -1200 519 C ATOM 4828 CD1 TYR C 94 43.827 2.711 -43.764 1.00 79.00 C ANISOU 4828 CD1 TYR C 94 11454 9482 9079 753 -1273 525 C ATOM 4829 CD2 TYR C 94 45.378 3.791 -42.312 1.00 76.82 C ANISOU 4829 CD2 TYR C 94 11265 9059 8864 796 -1155 433 C ATOM 4830 CE1 TYR C 94 42.770 3.339 -43.113 1.00 81.20 C ANISOU 4830 CE1 TYR C 94 11576 9783 9494 876 -1296 441 C ATOM 4831 CE2 TYR C 94 44.326 4.404 -41.636 1.00 78.90 C ANISOU 4831 CE2 TYR C 94 11395 9330 9253 915 -1168 330 C ATOM 4832 CZ TYR C 94 43.023 4.175 -42.042 1.00 87.79 C ANISOU 4832 CZ TYR C 94 12386 10546 10423 966 -1234 331 C ATOM 4833 OH TYR C 94 41.978 4.784 -41.395 1.00 91.47 O ANISOU 4833 OH TYR C 94 12673 11052 11027 1104 -1238 194 O ATOM 4834 N TYR C 95 48.913 3.490 -45.971 1.00 74.27 N ANISOU 4834 N TYR C 95 11312 8762 8146 405 -1156 724 N ATOM 4835 CA TYR C 95 50.292 3.316 -46.400 1.00 74.54 C ANISOU 4835 CA TYR C 95 11377 8878 8068 290 -1067 702 C ATOM 4836 C TYR C 95 51.257 3.435 -45.241 1.00 78.04 C ANISOU 4836 C TYR C 95 11772 9304 8576 317 -986 607 C ATOM 4837 O TYR C 95 51.148 4.329 -44.396 1.00 77.30 O ANISOU 4837 O TYR C 95 11680 9099 8590 357 -1012 603 O ATOM 4838 CB TYR C 95 50.676 4.340 -47.471 1.00 77.66 C ANISOU 4838 CB TYR C 95 11871 9261 8376 142 -1116 847 C ATOM 4839 CG TYR C 95 49.718 4.388 -48.633 1.00 81.47 C ANISOU 4839 CG TYR C 95 12414 9770 8771 103 -1238 978 C ATOM 4840 CD1 TYR C 95 49.810 3.474 -49.677 1.00 83.97 C ANISOU 4840 CD1 TYR C 95 12737 10275 8895 4 -1202 949 C ATOM 4841 CD2 TYR C 95 48.745 5.381 -48.718 1.00 83.93 C ANISOU 4841 CD2 TYR C 95 12774 9924 9193 170 -1406 1121 C ATOM 4842 CE1 TYR C 95 48.931 3.518 -50.756 1.00 86.77 C ANISOU 4842 CE1 TYR C 95 13145 10688 9134 -55 -1333 1070 C ATOM 4843 CE2 TYR C 95 47.874 5.449 -49.802 1.00 86.80 C ANISOU 4843 CE2 TYR C 95 13181 10330 9468 139 -1557 1265 C ATOM 4844 CZ TYR C 95 47.970 4.514 -50.819 1.00 96.59 C ANISOU 4844 CZ TYR C 95 14431 11789 10482 11 -1521 1247 C ATOM 4845 OH TYR C 95 47.104 4.573 -51.886 1.00102.42 O ANISOU 4845 OH TYR C 95 15211 12602 11103 -40 -1687 1386 O ATOM 4846 N CYS C 96 52.223 2.535 -45.237 1.00 74.86 N ANISOU 4846 N CYS C 96 11318 9018 8108 302 -899 513 N ATOM 4847 CA CYS C 96 53.307 2.475 -44.284 1.00 74.43 C ANISOU 4847 CA CYS C 96 11192 8998 8089 324 -843 425 C ATOM 4848 C CYS C 96 54.414 3.407 -44.735 1.00 78.35 C ANISOU 4848 C CYS C 96 11683 9551 8536 175 -802 442 C ATOM 4849 O CYS C 96 54.794 3.377 -45.906 1.00 79.01 O ANISOU 4849 O CYS C 96 11778 9739 8501 57 -761 467 O ATOM 4850 CB CYS C 96 53.792 1.034 -44.158 1.00 74.78 C ANISOU 4850 CB CYS C 96 11172 9125 8115 405 -803 321 C ATOM 4851 SG CYS C 96 55.263 0.826 -43.128 1.00 79.29 S ANISOU 4851 SG CYS C 96 11624 9778 8725 456 -774 222 S ATOM 4852 N ALA C 97 54.918 4.248 -43.829 1.00 74.19 N ANISOU 4852 N ALA C 97 11138 8973 8078 147 -808 421 N ATOM 4853 CA ALA C 97 56.012 5.164 -44.133 1.00 74.97 C ANISOU 4853 CA ALA C 97 11226 9123 8138 -38 -769 433 C ATOM 4854 C ALA C 97 57.270 4.722 -43.395 1.00 78.17 C ANISOU 4854 C ALA C 97 11470 9690 8541 -27 -712 295 C ATOM 4855 O ALA C 97 57.243 4.520 -42.178 1.00 76.74 O ANISOU 4855 O ALA C 97 11247 9483 8427 84 -749 231 O ATOM 4856 CB ALA C 97 55.632 6.589 -43.767 1.00 76.54 C ANISOU 4856 CB ALA C 97 11540 9109 8433 -107 -841 506 C ATOM 4857 N ALA C 98 58.352 4.506 -44.143 1.00 76.08 N ANISOU 4857 N ALA C 98 11097 9626 8183 -140 -625 242 N ATOM 4858 CA ALA C 98 59.615 4.040 -43.590 1.00 76.86 C ANISOU 4858 CA ALA C 98 10993 9919 8291 -111 -584 97 C ATOM 4859 C ALA C 98 60.721 5.041 -43.837 1.00 84.54 C ANISOU 4859 C ALA C 98 11885 11025 9210 -366 -522 81 C ATOM 4860 O ALA C 98 60.738 5.696 -44.881 1.00 85.09 O ANISOU 4860 O ALA C 98 12035 11114 9182 -583 -469 174 O ATOM 4861 CB ALA C 98 59.988 2.697 -44.200 1.00 77.78 C ANISOU 4861 CB ALA C 98 10986 10193 8372 20 -526 -18 C ATOM 4862 N ARG C 99 61.654 5.159 -42.883 1.00 83.89 N ANISOU 4862 N ARG C 99 11647 11053 9176 -370 -539 -23 N ATOM 4863 CA ARG C 99 62.790 6.060 -43.033 1.00 86.98 C ANISOU 4863 CA ARG C 99 11925 11604 9518 -643 -479 -61 C ATOM 4864 C ARG C 99 64.066 5.247 -43.267 1.00 94.60 C ANISOU 4864 C ARG C 99 12579 12920 10446 -610 -396 -236 C ATOM 4865 O ARG C 99 64.243 4.198 -42.652 1.00 92.66 O ANISOU 4865 O ARG C 99 12201 12731 10273 -340 -454 -337 O ATOM 4866 CB ARG C 99 62.948 6.985 -41.811 1.00 88.20 C ANISOU 4866 CB ARG C 99 12113 11647 9751 -721 -566 -78 C ATOM 4867 CG ARG C 99 63.485 8.368 -42.214 1.00102.05 C ANISOU 4867 CG ARG C 99 13929 13375 11473 -1087 -527 -25 C ATOM 4868 CD ARG C 99 63.996 9.235 -41.072 1.00112.21 C ANISOU 4868 CD ARG C 99 15192 14619 12825 -1216 -595 -110 C ATOM 4869 NE ARG C 99 65.336 8.830 -40.630 1.00123.41 N ANISOU 4869 NE ARG C 99 16294 16390 14208 -1258 -572 -271 N ATOM 4870 CZ ARG C 99 66.468 9.302 -41.154 1.00141.30 C ANISOU 4870 CZ ARG C 99 18389 18893 16404 -1560 -484 -317 C ATOM 4871 NH1 ARG C 99 66.439 10.184 -42.144 1.00129.29 N ANISOU 4871 NH1 ARG C 99 17019 17284 14821 -1875 -408 -188 N ATOM 4872 NH2 ARG C 99 67.641 8.880 -40.694 1.00129.96 N ANISOU 4872 NH2 ARG C 99 16622 17803 14956 -1558 -481 -484 N ATOM 4873 N ALA C 100 64.951 5.727 -44.153 1.00 97.17 N ANISOU 4873 N ALA C 100 12781 13481 10659 -885 -267 -272 N ATOM 4874 CA ALA C 100 66.220 5.061 -44.463 1.00101.16 C ANISOU 4874 CA ALA C 100 12935 14372 11128 -870 -162 -481 C ATOM 4875 C ALA C 100 67.183 5.112 -43.253 1.00110.67 C ANISOU 4875 C ALA C 100 13898 15719 12433 -818 -248 -604 C ATOM 4876 O ALA C 100 67.001 5.966 -42.380 1.00109.70 O ANISOU 4876 O ALA C 100 13900 15432 12351 -926 -346 -525 O ATOM 4877 CB ALA C 100 66.863 5.713 -45.681 1.00104.66 C ANISOU 4877 CB ALA C 100 13310 15067 11389 -1247 16 -479 C ATOM 4878 N PRO C 101 68.203 4.217 -43.161 1.00112.84 N ANISOU 4878 N PRO C 101 13822 16299 12754 -643 -230 -813 N ATOM 4879 CA PRO C 101 69.108 4.259 -41.991 1.00115.48 C ANISOU 4879 CA PRO C 101 13914 16789 13176 -585 -352 -912 C ATOM 4880 C PRO C 101 69.951 5.546 -41.942 1.00125.75 C ANISOU 4880 C PRO C 101 15101 18279 14398 -1007 -291 -931 C ATOM 4881 O PRO C 101 70.077 6.154 -40.875 1.00124.97 O ANISOU 4881 O PRO C 101 15032 18114 14339 -1083 -419 -908 O ATOM 4882 CB PRO C 101 70.007 3.028 -42.187 1.00119.10 C ANISOU 4882 CB PRO C 101 14002 17537 13713 -297 -341 -1137 C ATOM 4883 CG PRO C 101 69.306 2.178 -43.205 1.00121.93 C ANISOU 4883 CG PRO C 101 14488 17782 14056 -131 -245 -1152 C ATOM 4884 CD PRO C 101 68.570 3.123 -44.083 1.00116.04 C ANISOU 4884 CD PRO C 101 14027 16917 13147 -467 -115 -988 C ATOM 4885 N VAL C 102 70.519 5.955 -43.099 1.00128.10 N ANISOU 4885 N VAL C 102 15281 18824 14569 -1311 -92 -978 N ATOM 4886 CA VAL C 102 71.338 7.162 -43.245 1.00132.31 C ANISOU 4886 CA VAL C 102 15717 19547 15008 -1785 -7 -980 C ATOM 4887 C VAL C 102 70.663 8.082 -44.277 1.00140.17 C ANISOU 4887 C VAL C 102 17055 20341 15861 -2139 103 -764 C ATOM 4888 O VAL C 102 70.410 7.656 -45.411 1.00140.05 O ANISOU 4888 O VAL C 102 17072 20413 15729 -2143 238 -746 O ATOM 4889 CB VAL C 102 72.812 6.820 -43.638 1.00140.10 C ANISOU 4889 CB VAL C 102 16186 21095 15950 -1880 129 -1238 C ATOM 4890 CG1 VAL C 102 73.643 8.087 -43.841 1.00143.12 C ANISOU 4890 CG1 VAL C 102 16471 21692 16214 -2442 232 -1227 C ATOM 4891 CG2 VAL C 102 73.467 5.914 -42.600 1.00140.43 C ANISOU 4891 CG2 VAL C 102 15888 21310 16158 -1492 -33 -1428 C ATOM 4892 N GLY C 103 70.365 9.318 -43.867 1.00139.67 N ANISOU 4892 N GLY C 103 17256 20000 15813 -2422 26 -605 N ATOM 4893 CA GLY C 103 69.720 10.307 -44.728 1.00141.23 C ANISOU 4893 CA GLY C 103 17812 19936 15911 -2751 69 -360 C ATOM 4894 C GLY C 103 69.916 11.751 -44.307 1.00149.77 C ANISOU 4894 C GLY C 103 19075 20805 17026 -3152 4 -257 C ATOM 4895 O GLY C 103 69.892 12.057 -43.109 1.00148.76 O ANISOU 4895 O GLY C 103 18968 20515 17040 -3062 -136 -331 O ATOM 4896 N GLN C 104 70.092 12.654 -45.315 1.00150.97 N ANISOU 4896 N GLN C 104 19381 20948 17034 -3620 99 -79 N ATOM 4897 CA GLN C 104 70.265 14.114 -45.160 1.00154.13 C ANISOU 4897 CA GLN C 104 20016 21085 17461 -4077 39 62 C ATOM 4898 C GLN C 104 69.104 14.731 -44.363 1.00157.64 C ANISOU 4898 C GLN C 104 20853 20925 18117 -3877 -173 169 C ATOM 4899 O GLN C 104 69.339 15.536 -43.456 1.00158.36 O ANISOU 4899 O GLN C 104 21007 20828 18335 -4019 -271 97 O ATOM 4900 CB GLN C 104 70.367 14.800 -46.544 1.00158.56 C ANISOU 4900 CB GLN C 104 20760 21674 17811 -4561 152 314 C ATOM 4901 CG GLN C 104 71.661 14.539 -47.325 1.00173.35 C ANISOU 4901 CG GLN C 104 22244 24178 19443 -4922 394 195 C ATOM 4902 CD GLN C 104 72.841 15.336 -46.812 1.00193.13 C ANISOU 4902 CD GLN C 104 24546 26876 21958 -5368 428 86 C ATOM 4903 OE1 GLN C 104 73.211 16.364 -47.386 1.00191.95 O ANISOU 4903 OE1 GLN C 104 24555 26691 21685 -5942 480 273 O ATOM 4904 NE2 GLN C 104 73.454 14.895 -45.722 1.00183.39 N ANISOU 4904 NE2 GLN C 104 22968 25849 20864 -5142 383 -201 N ATOM 4905 N SER C 105 67.855 14.333 -44.697 1.00152.49 N ANISOU 4905 N SER C 105 20440 19997 17501 -3547 -238 307 N ATOM 4906 CA SER C 105 66.638 14.790 -44.028 1.00150.66 C ANISOU 4906 CA SER C 105 20533 19239 17471 -3298 -420 379 C ATOM 4907 C SER C 105 66.262 13.810 -42.905 1.00151.91 C ANISOU 4907 C SER C 105 20531 19455 17735 -2817 -474 169 C ATOM 4908 O SER C 105 65.772 12.706 -43.175 1.00148.97 O ANISOU 4908 O SER C 105 20079 19200 17321 -2494 -444 162 O ATOM 4909 CB SER C 105 65.499 14.940 -45.034 1.00153.40 C ANISOU 4909 CB SER C 105 21197 19294 17793 -3234 -474 652 C ATOM 4910 OG SER C 105 65.827 15.867 -46.057 1.00165.10 O ANISOU 4910 OG SER C 105 22867 20709 19155 -3703 -452 892 O ATOM 4911 N SER C 106 66.543 14.207 -41.646 1.00149.26 N ANISOU 4911 N SER C 106 20148 19050 17512 -2809 -556 -2 N ATOM 4912 CA SER C 106 66.275 13.399 -40.452 1.00146.76 C ANISOU 4912 CA SER C 106 19697 18806 17259 -2426 -624 -182 C ATOM 4913 C SER C 106 65.189 14.062 -39.565 1.00150.37 C ANISOU 4913 C SER C 106 20433 18827 17873 -2276 -752 -207 C ATOM 4914 O SER C 106 64.936 13.595 -38.449 1.00148.52 O ANISOU 4914 O SER C 106 20123 18641 17666 -2028 -810 -358 O ATOM 4915 CB SER C 106 67.564 13.191 -39.658 1.00151.61 C ANISOU 4915 CB SER C 106 19974 19801 17829 -2530 -618 -393 C ATOM 4916 OG SER C 106 67.361 12.353 -38.531 1.00157.95 O ANISOU 4916 OG SER C 106 20656 20701 18658 -2179 -705 -526 O ATOM 4917 N SER C 107 64.529 15.128 -40.083 1.00148.60 N ANISOU 4917 N SER C 107 20527 18186 17747 -2419 -801 -58 N ATOM 4918 CA SER C 107 63.450 15.845 -39.388 1.00148.39 C ANISOU 4918 CA SER C 107 20758 17719 17904 -2259 -918 -106 C ATOM 4919 C SER C 107 62.174 14.972 -39.322 1.00148.87 C ANISOU 4919 C SER C 107 20846 17725 17991 -1823 -937 -76 C ATOM 4920 O SER C 107 62.024 14.084 -40.168 1.00147.15 O ANISOU 4920 O SER C 107 20553 17685 17670 -1718 -879 58 O ATOM 4921 CB SER C 107 63.156 17.175 -40.083 1.00155.02 C ANISOU 4921 CB SER C 107 21922 18110 18869 -2512 -992 65 C ATOM 4922 OG SER C 107 62.700 16.995 -41.414 1.00163.79 O ANISOU 4922 OG SER C 107 23148 19168 19917 -2517 -983 347 O ATOM 4923 N PRO C 108 61.241 15.189 -38.351 1.00143.94 N ANISOU 4923 N PRO C 108 20317 16882 17494 -1586 -1005 -217 N ATOM 4924 CA PRO C 108 60.039 14.329 -38.288 1.00140.56 C ANISOU 4924 CA PRO C 108 19882 16449 17074 -1215 -1008 -190 C ATOM 4925 C PRO C 108 59.106 14.505 -39.500 1.00142.38 C ANISOU 4925 C PRO C 108 20290 16435 17372 -1143 -1050 45 C ATOM 4926 O PRO C 108 59.173 15.521 -40.206 1.00144.38 O ANISOU 4926 O PRO C 108 20738 16413 17707 -1346 -1112 185 O ATOM 4927 CB PRO C 108 59.337 14.791 -37.006 1.00142.77 C ANISOU 4927 CB PRO C 108 20219 16559 17467 -1058 -1055 -421 C ATOM 4928 CG PRO C 108 59.835 16.173 -36.773 1.00150.62 C ANISOU 4928 CG PRO C 108 21361 17282 18585 -1320 -1110 -517 C ATOM 4929 CD PRO C 108 61.254 16.170 -37.246 1.00147.33 C ANISOU 4929 CD PRO C 108 20836 17098 18043 -1658 -1067 -441 C ATOM 4930 N TYR C 109 58.220 13.495 -39.716 1.00134.41 N ANISOU 4930 N TYR C 109 19222 15526 16322 -866 -1034 99 N ATOM 4931 CA TYR C 109 57.205 13.379 -40.786 1.00132.80 C ANISOU 4931 CA TYR C 109 19134 15176 16149 -746 -1085 302 C ATOM 4932 C TYR C 109 57.886 13.287 -42.181 1.00133.58 C ANISOU 4932 C TYR C 109 19260 15394 16100 -989 -1051 524 C ATOM 4933 O TYR C 109 57.296 13.698 -43.188 1.00133.92 O ANISOU 4933 O TYR C 109 19470 15252 16160 -1022 -1132 737 O ATOM 4934 CB TYR C 109 56.188 14.551 -40.766 1.00136.50 C ANISOU 4934 CB TYR C 109 19815 15202 16847 -655 -1221 327 C ATOM 4935 CG TYR C 109 55.836 15.047 -39.380 1.00139.66 C ANISOU 4935 CG TYR C 109 20203 15467 17394 -521 -1234 48 C ATOM 4936 CD1 TYR C 109 55.069 14.272 -38.514 1.00139.89 C ANISOU 4936 CD1 TYR C 109 20089 15659 17402 -258 -1183 -119 C ATOM 4937 CD2 TYR C 109 56.223 16.313 -38.953 1.00143.54 C ANISOU 4937 CD2 TYR C 109 20837 15665 18036 -677 -1294 -57 C ATOM 4938 CE1 TYR C 109 54.762 14.716 -37.229 1.00141.95 C ANISOU 4938 CE1 TYR C 109 20327 15858 17751 -163 -1172 -400 C ATOM 4939 CE2 TYR C 109 55.910 16.774 -37.677 1.00145.56 C ANISOU 4939 CE2 TYR C 109 21078 15819 18409 -562 -1293 -363 C ATOM 4940 CZ TYR C 109 55.174 15.974 -36.818 1.00151.52 C ANISOU 4940 CZ TYR C 109 21670 16794 19107 -303 -1224 -539 C ATOM 4941 OH TYR C 109 54.854 16.431 -35.562 1.00154.01 O ANISOU 4941 OH TYR C 109 21963 17060 19496 -213 -1204 -861 O ATOM 4942 N ASP C 110 59.115 12.722 -42.232 1.00127.08 N ANISOU 4942 N ASP C 110 18255 14910 15119 -1153 -936 467 N ATOM 4943 CA ASP C 110 59.866 12.536 -43.475 1.00126.40 C ANISOU 4943 CA ASP C 110 18135 15034 14857 -1398 -858 612 C ATOM 4944 C ASP C 110 59.872 11.061 -43.873 1.00124.15 C ANISOU 4944 C ASP C 110 17664 15075 14434 -1221 -765 569 C ATOM 4945 O ASP C 110 60.544 10.239 -43.242 1.00122.68 O ANISOU 4945 O ASP C 110 17256 15142 14215 -1130 -697 398 O ATOM 4946 CB ASP C 110 61.313 13.067 -43.362 1.00130.36 C ANISOU 4946 CB ASP C 110 18536 15702 15293 -1744 -783 548 C ATOM 4947 CG ASP C 110 61.453 14.577 -43.249 1.00142.49 C ANISOU 4947 CG ASP C 110 20296 16898 16948 -2019 -872 621 C ATOM 4948 OD1 ASP C 110 60.417 15.266 -43.100 1.00143.28 O ANISOU 4948 OD1 ASP C 110 20628 16591 17221 -1888 -1007 689 O ATOM 4949 OD2 ASP C 110 62.597 15.068 -43.309 1.00150.03 O ANISOU 4949 OD2 ASP C 110 21183 17985 17835 -2366 -812 598 O ATOM 4950 N TYR C 111 59.095 10.736 -44.916 1.00116.98 N ANISOU 4950 N TYR C 111 16854 14137 13455 -1166 -785 724 N ATOM 4951 CA TYR C 111 58.988 9.398 -45.489 1.00113.46 C ANISOU 4951 CA TYR C 111 16278 13950 12882 -1024 -707 683 C ATOM 4952 C TYR C 111 60.074 9.226 -46.561 1.00113.19 C ANISOU 4952 C TYR C 111 16142 14228 12638 -1294 -573 697 C ATOM 4953 O TYR C 111 60.261 10.111 -47.400 1.00115.13 O ANISOU 4953 O TYR C 111 16526 14432 12785 -1589 -579 873 O ATOM 4954 CB TYR C 111 57.565 9.148 -46.064 1.00114.30 C ANISOU 4954 CB TYR C 111 16528 13896 13002 -853 -803 815 C ATOM 4955 CG TYR C 111 57.109 10.178 -47.081 1.00119.34 C ANISOU 4955 CG TYR C 111 17394 14347 13602 -1040 -905 1068 C ATOM 4956 CD1 TYR C 111 56.435 11.331 -46.683 1.00122.73 C ANISOU 4956 CD1 TYR C 111 18006 14404 14224 -1007 -1059 1168 C ATOM 4957 CD2 TYR C 111 57.335 9.994 -48.443 1.00121.75 C ANISOU 4957 CD2 TYR C 111 17739 14843 13678 -1244 -862 1204 C ATOM 4958 CE1 TYR C 111 56.039 12.296 -47.610 1.00126.58 C ANISOU 4958 CE1 TYR C 111 18724 14673 14699 -1165 -1197 1434 C ATOM 4959 CE2 TYR C 111 56.954 10.956 -49.377 1.00125.34 C ANISOU 4959 CE2 TYR C 111 18426 15130 14068 -1444 -985 1483 C ATOM 4960 CZ TYR C 111 56.297 12.102 -48.957 1.00134.69 C ANISOU 4960 CZ TYR C 111 19804 15901 15470 -1394 -1169 1617 C ATOM 4961 OH TYR C 111 55.898 13.043 -49.876 1.00139.87 O ANISOU 4961 OH TYR C 111 20711 16346 16087 -1569 -1335 1924 O ATOM 4962 N ASP C 112 60.837 8.130 -46.483 1.00104.32 N ANISOU 4962 N ASP C 112 14770 13418 11450 -1204 -454 505 N ATOM 4963 CA ASP C 112 61.891 7.834 -47.453 1.00103.84 C ANISOU 4963 CA ASP C 112 14546 13716 11193 -1422 -295 443 C ATOM 4964 C ASP C 112 61.433 6.700 -48.358 1.00101.86 C ANISOU 4964 C ASP C 112 14268 13610 10823 -1280 -239 395 C ATOM 4965 O ASP C 112 61.754 6.682 -49.548 1.00102.62 O ANISOU 4965 O ASP C 112 14356 13934 10703 -1499 -133 423 O ATOM 4966 CB ASP C 112 63.210 7.491 -46.742 1.00106.13 C ANISOU 4966 CB ASP C 112 14533 14273 11520 -1418 -208 215 C ATOM 4967 CG ASP C 112 63.794 8.630 -45.919 1.00116.55 C ANISOU 4967 CG ASP C 112 15860 15501 12924 -1622 -255 233 C ATOM 4968 OD1 ASP C 112 63.177 9.719 -45.882 1.00117.84 O ANISOU 4968 OD1 ASP C 112 16285 15348 13140 -1758 -352 412 O ATOM 4969 OD2 ASP C 112 64.875 8.441 -45.331 1.00122.78 O ANISOU 4969 OD2 ASP C 112 16387 16527 13735 -1644 -207 57 O ATOM 4970 N TYR C 113 60.651 5.773 -47.788 1.00 92.86 N ANISOU 4970 N TYR C 113 13130 12342 9809 -943 -311 323 N ATOM 4971 CA TYR C 113 60.056 4.636 -48.481 1.00 90.29 C ANISOU 4971 CA TYR C 113 12808 12083 9415 -785 -288 261 C ATOM 4972 C TYR C 113 58.590 4.537 -48.124 1.00 90.10 C ANISOU 4972 C TYR C 113 12968 11765 9501 -596 -436 381 C ATOM 4973 O TYR C 113 58.245 4.512 -46.945 1.00 87.23 O ANISOU 4973 O TYR C 113 12605 11228 9310 -420 -515 363 O ATOM 4974 CB TYR C 113 60.786 3.329 -48.145 1.00 90.52 C ANISOU 4974 CB TYR C 113 12595 12297 9501 -567 -209 -4 C ATOM 4975 CG TYR C 113 62.268 3.360 -48.439 1.00 93.78 C ANISOU 4975 CG TYR C 113 12753 13048 9831 -713 -58 -173 C ATOM 4976 CD1 TYR C 113 62.752 3.100 -49.717 1.00 97.63 C ANISOU 4976 CD1 TYR C 113 13150 13837 10108 -881 102 -276 C ATOM 4977 CD2 TYR C 113 63.192 3.609 -47.429 1.00 94.79 C ANISOU 4977 CD2 TYR C 113 12702 13237 10077 -689 -71 -256 C ATOM 4978 CE1 TYR C 113 64.117 3.130 -49.993 1.00100.39 C ANISOU 4978 CE1 TYR C 113 13218 14551 10374 -1026 264 -464 C ATOM 4979 CE2 TYR C 113 64.561 3.618 -47.688 1.00 98.20 C ANISOU 4979 CE2 TYR C 113 12848 14021 10444 -821 65 -433 C ATOM 4980 CZ TYR C 113 65.020 3.378 -48.972 1.00106.55 C ANISOU 4980 CZ TYR C 113 13798 15386 11301 -987 242 -543 C ATOM 4981 OH TYR C 113 66.367 3.390 -49.230 1.00109.41 O ANISOU 4981 OH TYR C 113 13834 16144 11593 -1126 398 -747 O ATOM 4982 N TRP C 114 57.722 4.518 -49.135 1.00 86.90 N ANISOU 4982 N TRP C 114 12704 11334 8979 -653 -476 501 N ATOM 4983 CA TRP C 114 56.282 4.419 -48.929 1.00 85.07 C ANISOU 4983 CA TRP C 114 12608 10872 8843 -489 -618 605 C ATOM 4984 C TRP C 114 55.834 2.948 -49.012 1.00 88.25 C ANISOU 4984 C TRP C 114 12947 11335 9249 -298 -596 453 C ATOM 4985 O TRP C 114 56.602 2.086 -49.451 1.00 88.56 O ANISOU 4985 O TRP C 114 12869 11575 9205 -298 -480 276 O ATOM 4986 CB TRP C 114 55.538 5.280 -49.959 1.00 85.06 C ANISOU 4986 CB TRP C 114 12793 10801 8726 -655 -720 843 C ATOM 4987 N GLY C 115 54.610 2.679 -48.561 1.00 83.38 N ANISOU 4987 N GLY C 115 12399 10541 8742 -143 -706 504 N ATOM 4988 CA GLY C 115 54.019 1.346 -48.590 1.00 82.48 C ANISOU 4988 CA GLY C 115 12261 10433 8646 -1 -709 391 C ATOM 4989 C GLY C 115 53.130 1.156 -49.804 1.00 87.85 C ANISOU 4989 C GLY C 115 13028 11168 9181 -86 -762 454 C ATOM 4990 O GLY C 115 52.644 2.143 -50.370 1.00 89.09 O ANISOU 4990 O GLY C 115 13282 11301 9269 -201 -849 640 O ATOM 4991 N GLN C 116 52.910 -0.119 -50.224 1.00 83.73 N ANISOU 4991 N GLN C 116 12486 10712 8616 -35 -729 301 N ATOM 4992 CA GLN C 116 52.064 -0.459 -51.383 1.00 84.11 C ANISOU 4992 CA GLN C 116 12607 10846 8504 -131 -783 320 C ATOM 4993 C GLN C 116 50.592 -0.099 -51.092 1.00 86.38 C ANISOU 4993 C GLN C 116 12950 10990 8881 -79 -949 486 C ATOM 4994 O GLN C 116 49.876 0.353 -51.992 1.00 87.58 O ANISOU 4994 O GLN C 116 13167 11204 8906 -182 -1054 617 O ATOM 4995 CB GLN C 116 52.203 -1.959 -51.745 1.00 85.88 C ANISOU 4995 CB GLN C 116 12798 11131 8702 -79 -710 69 C ATOM 4996 CG GLN C 116 51.385 -2.436 -52.971 1.00100.20 C ANISOU 4996 CG GLN C 116 14682 13064 10326 -204 -758 33 C ATOM 4997 CD GLN C 116 51.731 -1.785 -54.304 1.00126.26 C ANISOU 4997 CD GLN C 116 18023 16622 13328 -432 -726 88 C ATOM 4998 OE1 GLN C 116 52.761 -1.118 -54.478 1.00125.50 O ANISOU 4998 OE1 GLN C 116 17892 16649 13143 -528 -625 111 O ATOM 4999 NE2 GLN C 116 50.894 -2.020 -55.303 1.00119.07 N ANISOU 4999 NE2 GLN C 116 17184 15828 12230 -556 -809 106 N ATOM 5000 N GLY C 117 50.184 -0.268 -49.839 1.00 80.20 N ANISOU 5000 N GLY C 117 12125 10045 8302 74 -973 477 N ATOM 5001 CA GLY C 117 48.839 0.042 -49.391 1.00 79.08 C ANISOU 5001 CA GLY C 117 11979 9802 8267 140 -1098 582 C ATOM 5002 C GLY C 117 48.062 -1.151 -48.896 1.00 81.74 C ANISOU 5002 C GLY C 117 12279 10103 8677 199 -1103 484 C ATOM 5003 O GLY C 117 48.238 -2.272 -49.380 1.00 82.50 O ANISOU 5003 O GLY C 117 12397 10242 8708 158 -1061 355 O ATOM 5004 N THR C 118 47.161 -0.882 -47.957 1.00 76.56 N ANISOU 5004 N THR C 118 11567 9369 8154 278 -1155 534 N ATOM 5005 CA THR C 118 46.278 -1.851 -47.326 1.00 75.64 C ANISOU 5005 CA THR C 118 11405 9230 8103 290 -1160 478 C ATOM 5006 C THR C 118 44.884 -1.250 -47.300 1.00 79.03 C ANISOU 5006 C THR C 118 11743 9700 8586 308 -1266 553 C ATOM 5007 O THR C 118 44.654 -0.262 -46.599 1.00 78.98 O ANISOU 5007 O THR C 118 11677 9651 8683 404 -1283 598 O ATOM 5008 CB THR C 118 46.821 -2.203 -45.925 1.00 81.80 C ANISOU 5008 CB THR C 118 12176 9924 8980 360 -1080 436 C ATOM 5009 OG1 THR C 118 48.124 -2.777 -46.050 1.00 79.79 O ANISOU 5009 OG1 THR C 118 11977 9643 8698 375 -1013 359 O ATOM 5010 CG2 THR C 118 45.915 -3.140 -45.170 1.00 79.94 C ANISOU 5010 CG2 THR C 118 11914 9669 8790 326 -1083 416 C ATOM 5011 N GLN C 119 43.967 -1.802 -48.088 1.00 75.53 N ANISOU 5011 N GLN C 119 11273 9346 8079 225 -1345 545 N ATOM 5012 CA GLN C 119 42.615 -1.265 -48.125 1.00 76.15 C ANISOU 5012 CA GLN C 119 11217 9499 8218 258 -1465 603 C ATOM 5013 C GLN C 119 41.889 -1.603 -46.821 1.00 77.90 C ANISOU 5013 C GLN C 119 11312 9728 8558 286 -1402 540 C ATOM 5014 O GLN C 119 41.738 -2.777 -46.468 1.00 77.88 O ANISOU 5014 O GLN C 119 11326 9732 8532 176 -1339 473 O ATOM 5015 CB GLN C 119 41.832 -1.789 -49.355 1.00 79.29 C ANISOU 5015 CB GLN C 119 11599 10034 8493 135 -1584 605 C ATOM 5016 CG GLN C 119 40.336 -1.384 -49.429 1.00 96.40 C ANISOU 5016 CG GLN C 119 13575 12321 10731 171 -1734 649 C ATOM 5017 CD GLN C 119 40.034 0.102 -49.539 1.00118.01 C ANISOU 5017 CD GLN C 119 16248 15024 13565 341 -1873 780 C ATOM 5018 OE1 GLN C 119 40.873 0.923 -49.917 1.00112.58 O ANISOU 5018 OE1 GLN C 119 15696 14234 12846 379 -1897 885 O ATOM 5019 NE2 GLN C 119 38.783 0.463 -49.296 1.00113.43 N ANISOU 5019 NE2 GLN C 119 15454 14532 13111 436 -1983 775 N ATOM 5020 N VAL C 120 41.496 -0.560 -46.090 1.00 72.33 N ANISOU 5020 N VAL C 120 10495 9013 7976 420 -1414 554 N ATOM 5021 CA VAL C 120 40.690 -0.691 -44.887 1.00 71.88 C ANISOU 5021 CA VAL C 120 10279 9030 8003 438 -1344 475 C ATOM 5022 C VAL C 120 39.316 -0.192 -45.249 1.00 77.09 C ANISOU 5022 C VAL C 120 10726 9824 8740 499 -1466 466 C ATOM 5023 O VAL C 120 39.174 0.942 -45.712 1.00 77.62 O ANISOU 5023 O VAL C 120 10761 9839 8892 652 -1590 523 O ATOM 5024 CB VAL C 120 41.287 0.013 -43.638 1.00 74.96 C ANISOU 5024 CB VAL C 120 10672 9345 8465 543 -1240 430 C ATOM 5025 CG1 VAL C 120 40.289 0.044 -42.478 1.00 75.45 C ANISOU 5025 CG1 VAL C 120 10536 9549 8583 553 -1163 323 C ATOM 5026 CG2 VAL C 120 42.597 -0.644 -43.211 1.00 73.38 C ANISOU 5026 CG2 VAL C 120 10646 9051 8185 477 -1142 439 C ATOM 5027 N THR C 121 38.317 -1.064 -45.132 1.00 74.26 N ANISOU 5027 N THR C 121 10228 9631 8356 369 -1454 408 N ATOM 5028 CA THR C 121 36.942 -0.718 -45.462 1.00 75.84 C ANISOU 5028 CA THR C 121 10169 10014 8632 417 -1575 377 C ATOM 5029 C THR C 121 36.073 -0.925 -44.213 1.00 81.07 C ANISOU 5029 C THR C 121 10596 10855 9353 381 -1442 242 C ATOM 5030 O THR C 121 36.094 -2.003 -43.605 1.00 80.79 O ANISOU 5030 O THR C 121 10605 10869 9222 166 -1311 216 O ATOM 5031 CB THR C 121 36.452 -1.538 -46.666 1.00 77.46 C ANISOU 5031 CB THR C 121 10382 10325 8725 249 -1699 414 C ATOM 5032 OG1 THR C 121 37.379 -1.415 -47.744 1.00 72.62 O ANISOU 5032 OG1 THR C 121 10001 9585 8007 246 -1778 515 O ATOM 5033 CG2 THR C 121 35.080 -1.121 -47.123 1.00 77.72 C ANISOU 5033 CG2 THR C 121 10127 10570 8834 311 -1867 396 C ATOM 5034 N VAL C 122 35.332 0.121 -43.824 1.00 78.38 N ANISOU 5034 N VAL C 122 10011 10604 9168 586 -1477 154 N ATOM 5035 CA VAL C 122 34.436 0.080 -42.670 1.00 79.30 C ANISOU 5035 CA VAL C 122 9848 10951 9330 565 -1335 -18 C ATOM 5036 C VAL C 122 32.985 0.068 -43.217 1.00 85.81 C ANISOU 5036 C VAL C 122 10331 12043 10232 576 -1460 -85 C ATOM 5037 O VAL C 122 32.414 1.130 -43.481 1.00 87.48 O ANISOU 5037 O VAL C 122 10339 12274 10624 848 -1600 -138 O ATOM 5038 CB VAL C 122 34.721 1.256 -41.682 1.00 82.98 C ANISOU 5038 CB VAL C 122 10260 11344 9924 801 -1250 -142 C ATOM 5039 CG1 VAL C 122 33.870 1.136 -40.425 1.00 84.65 C ANISOU 5039 CG1 VAL C 122 10186 11848 10129 741 -1059 -354 C ATOM 5040 CG2 VAL C 122 36.198 1.321 -41.307 1.00 79.97 C ANISOU 5040 CG2 VAL C 122 10206 10714 9465 783 -1170 -63 C ATOM 5041 N SER C 123 32.433 -1.141 -43.461 1.00 82.85 N ANISOU 5041 N SER C 123 9905 11846 9730 282 -1439 -74 N ATOM 5042 CA SER C 123 31.086 -1.320 -44.017 1.00 85.96 C ANISOU 5042 CA SER C 123 9965 12530 10166 229 -1562 -138 C ATOM 5043 C SER C 123 30.261 -2.335 -43.191 1.00 91.98 C ANISOU 5043 C SER C 123 10522 13592 10835 -94 -1378 -253 C ATOM 5044 O SER C 123 30.760 -2.862 -42.196 1.00 90.55 O ANISOU 5044 O SER C 123 10489 13367 10548 -265 -1170 -254 O ATOM 5045 CB SER C 123 31.165 -1.775 -45.472 1.00 89.75 C ANISOU 5045 CB SER C 123 10593 12947 10561 135 -1776 2 C ATOM 5046 OG SER C 123 31.746 -0.778 -46.298 1.00 97.71 O ANISOU 5046 OG SER C 123 11749 13745 11631 397 -1962 125 O ATOM 5047 N SER C 124 29.002 -2.608 -43.625 1.00 92.04 N ANISOU 5047 N SER C 124 10187 13915 10869 -199 -1469 -332 N ATOM 5048 CA SER C 124 28.022 -3.478 -42.960 1.00 94.89 C ANISOU 5048 CA SER C 124 10282 14625 11148 -537 -1312 -449 C ATOM 5049 C SER C 124 28.418 -4.987 -42.921 1.00 99.91 C ANISOU 5049 C SER C 124 11231 15148 11582 -986 -1221 -334 C ATOM 5050 O SER C 124 27.699 -5.766 -42.288 1.00102.06 O ANISOU 5050 O SER C 124 11342 15670 11765 -1328 -1079 -394 O ATOM 5051 CB SER C 124 26.675 -3.371 -43.662 1.00102.02 C ANISOU 5051 CB SER C 124 10747 15877 12137 -532 -1483 -551 C ATOM 5052 N HIS C 125 29.523 -5.406 -43.568 1.00 94.88 N ANISOU 5052 N HIS C 125 11026 14143 10882 -998 -1299 -181 N ATOM 5053 CA HIS C 125 29.926 -6.820 -43.512 1.00 94.78 C ANISOU 5053 CA HIS C 125 11319 13966 10728 -1373 -1232 -96 C ATOM 5054 C HIS C 125 31.434 -6.938 -43.171 1.00 94.01 C ANISOU 5054 C HIS C 125 11651 13476 10593 -1275 -1165 23 C ATOM 5055 O HIS C 125 32.255 -6.374 -43.893 1.00 91.54 O ANISOU 5055 O HIS C 125 11506 12956 10321 -1021 -1271 70 O ATOM 5056 CB HIS C 125 29.616 -7.542 -44.840 1.00 97.36 C ANISOU 5056 CB HIS C 125 11707 14274 11011 -1550 -1418 -86 C ATOM 5057 CG HIS C 125 28.292 -7.191 -45.463 1.00104.64 C ANISOU 5057 CG HIS C 125 12204 15572 11984 -1553 -1562 -188 C ATOM 5058 ND1 HIS C 125 28.220 -6.515 -46.673 1.00107.01 N ANISOU 5058 ND1 HIS C 125 12449 15888 12324 -1318 -1804 -169 N ATOM 5059 CD2 HIS C 125 27.036 -7.367 -44.995 1.00110.24 C ANISOU 5059 CD2 HIS C 125 12510 16670 12706 -1751 -1504 -305 C ATOM 5060 CE1 HIS C 125 26.930 -6.355 -46.925 1.00109.88 C ANISOU 5060 CE1 HIS C 125 12385 16629 12735 -1366 -1911 -268 C ATOM 5061 NE2 HIS C 125 26.177 -6.847 -45.943 1.00112.27 N ANISOU 5061 NE2 HIS C 125 12446 17179 13032 -1620 -1727 -369 N ATOM 5062 N HIS C 126 31.775 -7.662 -42.107 1.00 89.18 N ANISOU 5062 N HIS C 126 11201 12787 9897 -1489 -1005 80 N ATOM 5063 CA HIS C 126 33.162 -7.842 -41.700 1.00 85.89 C ANISOU 5063 CA HIS C 126 11153 12028 9451 -1399 -961 191 C ATOM 5064 C HIS C 126 33.689 -9.223 -41.944 1.00 88.19 C ANISOU 5064 C HIS C 126 11784 12036 9690 -1649 -994 286 C ATOM 5065 O HIS C 126 34.880 -9.430 -41.937 1.00 84.94 O ANISOU 5065 O HIS C 126 11667 11320 9286 -1531 -1009 358 O ATOM 5066 CB HIS C 126 33.306 -7.553 -40.215 1.00 86.97 C ANISOU 5066 CB HIS C 126 11251 12264 9529 -1412 -784 204 C ATOM 5067 CG HIS C 126 33.428 -8.780 -39.378 1.00 91.56 C ANISOU 5067 CG HIS C 126 12041 12766 9982 -1768 -698 328 C ATOM 5068 ND1 HIS C 126 32.396 -9.263 -38.611 1.00 96.31 N ANISOU 5068 ND1 HIS C 126 12459 13660 10476 -2113 -577 317 N ATOM 5069 CD2 HIS C 126 34.450 -9.649 -39.227 1.00 92.17 C ANISOU 5069 CD2 HIS C 126 12500 12494 10027 -1842 -734 478 C ATOM 5070 CE1 HIS C 126 32.786 -10.364 -37.998 1.00 96.45 C ANISOU 5070 CE1 HIS C 126 12771 13490 10385 -2406 -549 488 C ATOM 5071 NE2 HIS C 126 34.029 -10.620 -38.356 1.00 94.32 N ANISOU 5071 NE2 HIS C 126 12847 12814 10177 -2224 -657 586 N ATOM 5072 N HIS C 127 32.780 -10.170 -42.077 1.00 87.87 N ANISOU 5072 N HIS C 127 11685 12096 9605 -2000 -1003 272 N ATOM 5073 CA HIS C 127 33.104 -11.569 -42.326 1.00 88.96 C ANISOU 5073 CA HIS C 127 12146 11935 9721 -2276 -1051 339 C ATOM 5074 C HIS C 127 32.159 -12.207 -43.356 1.00 94.46 C ANISOU 5074 C HIS C 127 12743 12730 10415 -2530 -1157 240 C ATOM 5075 O HIS C 127 32.637 -12.949 -44.214 1.00 94.44 O ANISOU 5075 O HIS C 127 12998 12450 10436 -2578 -1260 210 O ATOM 5076 CB HIS C 127 33.045 -12.367 -41.018 1.00 91.74 C ANISOU 5076 CB HIS C 127 12627 12239 9990 -2582 -936 477 C ATOM 5077 N HIS C 128 30.827 -11.952 -43.261 1.00 92.64 N ANISOU 5077 N HIS C 128 12130 12912 10159 -2701 -1132 164 N ATOM 5078 CA HIS C 128 29.878 -12.569 -44.194 1.00 94.77 C ANISOU 5078 CA HIS C 128 12273 13319 10415 -2978 -1245 64 C ATOM 5079 C HIS C 128 28.702 -11.593 -44.505 1.00 98.92 C ANISOU 5079 C HIS C 128 12286 14335 10962 -2874 -1290 -56 C ATOM 5080 O HIS C 128 28.765 -10.885 -45.508 1.00 97.49 O ANISOU 5080 O HIS C 128 12022 14199 10822 -2599 -1443 -108 O ATOM 5081 CB HIS C 128 29.362 -13.896 -43.608 1.00 98.70 C ANISOU 5081 CB HIS C 128 12888 13759 10853 -3499 -1178 120 C ATOM 5082 CG HIS C 128 28.909 -14.887 -44.632 1.00104.55 C ANISOU 5082 CG HIS C 128 13721 14411 11593 -3810 -1314 29 C ATOM 5083 ND1 HIS C 128 27.601 -14.925 -45.077 1.00109.46 N ANISOU 5083 ND1 HIS C 128 13976 15433 12182 -4065 -1366 -90 N ATOM 5084 CD2 HIS C 128 29.602 -15.888 -45.224 1.00106.60 C ANISOU 5084 CD2 HIS C 128 14390 14229 11885 -3911 -1404 20 C ATOM 5085 CE1 HIS C 128 27.546 -15.923 -45.947 1.00110.73 C ANISOU 5085 CE1 HIS C 128 14349 15385 12338 -4331 -1490 -165 C ATOM 5086 NE2 HIS C 128 28.728 -16.531 -46.068 1.00109.44 N ANISOU 5086 NE2 HIS C 128 14660 14703 12219 -4241 -1511 -115 N ATOM 5087 N HIS C 129 27.656 -11.546 -43.652 1.00 97.38 N ANISOU 5087 N HIS C 129 11746 14515 10740 -3088 -1165 -98 N ATOM 5088 CA HIS C 129 26.477 -10.691 -43.850 1.00114.38 C ANISOU 5088 CA HIS C 129 13361 17155 12945 -2982 -1206 -243 C ATOM 5089 C HIS C 129 26.370 -9.621 -42.749 1.00111.52 C ANISOU 5089 C HIS C 129 12732 17016 12624 -2720 -1040 -290 C ATOM 5090 O HIS C 129 25.525 -8.724 -42.825 1.00 56.30 O ANISOU 5090 O HIS C 129 5285 10385 5721 -2516 -1074 -433 O ATOM 5091 CB HIS C 129 25.199 -11.546 -43.873 1.00119.38 C ANISOU 5091 CB HIS C 129 13722 18122 13516 -3476 -1193 -324 C TER 5092 HIS C 129 ATOM 5093 N VAL D 4 62.905 0.504 50.865 1.00 85.60 N ANISOU 5093 N VAL D 4 13370 10625 8531 -1231 -1209 -1909 N ATOM 5094 CA VAL D 4 62.440 -0.785 50.360 1.00 82.27 C ANISOU 5094 CA VAL D 4 12910 10224 8125 -951 -1247 -1552 C ATOM 5095 C VAL D 4 63.264 -1.199 49.135 1.00 86.65 C ANISOU 5095 C VAL D 4 13172 10872 8880 -1133 -1207 -1615 C ATOM 5096 O VAL D 4 63.552 -0.363 48.275 1.00 87.44 O ANISOU 5096 O VAL D 4 13259 10817 9147 -1487 -996 -1725 O ATOM 5097 CB VAL D 4 60.934 -0.759 50.022 1.00 82.70 C ANISOU 5097 CB VAL D 4 13293 9939 8189 -836 -1048 -1134 C ATOM 5098 N GLN D 5 63.648 -2.489 49.063 1.00 82.57 N ANISOU 5098 N GLN D 5 12453 10588 8331 -873 -1382 -1540 N ATOM 5099 CA GLN D 5 64.434 -3.026 47.948 1.00 82.56 C ANISOU 5099 CA GLN D 5 12171 10705 8492 -980 -1360 -1592 C ATOM 5100 C GLN D 5 63.534 -3.192 46.716 1.00 84.46 C ANISOU 5100 C GLN D 5 12586 10629 8874 -1038 -1133 -1252 C ATOM 5101 O GLN D 5 63.729 -2.488 45.721 1.00 84.18 O ANISOU 5101 O GLN D 5 12539 10456 8989 -1338 -926 -1304 O ATOM 5102 CB GLN D 5 65.093 -4.360 48.343 1.00 84.59 C ANISOU 5102 CB GLN D 5 12209 11299 8632 -619 -1620 -1618 C ATOM 5103 CG GLN D 5 65.949 -5.007 47.247 1.00 86.88 C ANISOU 5103 CG GLN D 5 12201 11743 9066 -673 -1612 -1680 C ATOM 5104 CD GLN D 5 66.379 -6.420 47.583 1.00 89.24 C ANISOU 5104 CD GLN D 5 12386 12296 9226 -236 -1834 -1623 C ATOM 5105 OE1 GLN D 5 65.642 -7.207 48.199 1.00 75.21 O ANISOU 5105 OE1 GLN D 5 10862 10415 7299 107 -1893 -1357 O ATOM 5106 NE2 GLN D 5 67.508 -6.827 47.040 1.00 83.49 N ANISOU 5106 NE2 GLN D 5 11307 11858 8556 -237 -1908 -1833 N ATOM 5107 N LEU D 6 62.549 -4.117 46.794 1.00 79.26 N ANISOU 5107 N LEU D 6 12097 9863 8156 -749 -1158 -921 N ATOM 5108 CA LEU D 6 61.577 -4.379 45.727 1.00 76.56 C ANISOU 5108 CA LEU D 6 11894 9275 7921 -762 -987 -627 C ATOM 5109 C LEU D 6 60.405 -3.383 45.821 1.00 79.88 C ANISOU 5109 C LEU D 6 12607 9427 8317 -829 -814 -479 C ATOM 5110 O LEU D 6 59.541 -3.515 46.698 1.00 78.93 O ANISOU 5110 O LEU D 6 12657 9249 8083 -640 -843 -334 O ATOM 5111 CB LEU D 6 61.058 -5.833 45.780 1.00 75.05 C ANISOU 5111 CB LEU D 6 11727 9092 7696 -466 -1070 -391 C ATOM 5112 CG LEU D 6 62.011 -6.977 45.417 1.00 80.07 C ANISOU 5112 CG LEU D 6 12141 9925 8356 -337 -1197 -461 C ATOM 5113 CD1 LEU D 6 61.364 -8.279 45.689 1.00 79.37 C ANISOU 5113 CD1 LEU D 6 12183 9759 8214 -54 -1231 -225 C ATOM 5114 CD2 LEU D 6 62.478 -6.903 43.978 1.00 81.29 C ANISOU 5114 CD2 LEU D 6 12140 10072 8674 -542 -1092 -515 C ATOM 5115 N VAL D 7 60.404 -2.366 44.928 1.00 76.34 N ANISOU 5115 N VAL D 7 12234 8813 7959 -1075 -613 -515 N ATOM 5116 CA VAL D 7 59.401 -1.299 44.916 1.00 75.72 C ANISOU 5116 CA VAL D 7 12456 8477 7836 -1108 -429 -394 C ATOM 5117 C VAL D 7 58.201 -1.758 44.059 1.00 77.48 C ANISOU 5117 C VAL D 7 12772 8589 8079 -949 -349 -93 C ATOM 5118 O VAL D 7 58.215 -1.649 42.827 1.00 76.20 O ANISOU 5118 O VAL D 7 12606 8358 7987 -1025 -230 -40 O ATOM 5119 CB VAL D 7 59.993 0.051 44.421 1.00 81.29 C ANISOU 5119 CB VAL D 7 13264 9025 8599 -1419 -216 -579 C ATOM 5120 CG1 VAL D 7 58.961 1.172 44.514 1.00 81.18 C ANISOU 5120 CG1 VAL D 7 13621 8723 8499 -1388 -20 -447 C ATOM 5121 CG2 VAL D 7 61.246 0.423 45.210 1.00 83.88 C ANISOU 5121 CG2 VAL D 7 13417 9517 8937 -1628 -307 -949 C ATOM 5122 N GLU D 8 57.153 -2.241 44.749 1.00 73.99 N ANISOU 5122 N GLU D 8 12408 8143 7560 -729 -406 85 N ATOM 5123 CA GLU D 8 55.917 -2.773 44.166 1.00 72.74 C ANISOU 5123 CA GLU D 8 12279 7938 7420 -579 -356 321 C ATOM 5124 C GLU D 8 54.801 -1.723 44.124 1.00 76.68 C ANISOU 5124 C GLU D 8 13009 8290 7837 -506 -201 438 C ATOM 5125 O GLU D 8 54.527 -1.068 45.131 1.00 76.56 O ANISOU 5125 O GLU D 8 13152 8218 7720 -456 -175 422 O ATOM 5126 CB GLU D 8 55.433 -3.988 44.977 1.00 73.75 C ANISOU 5126 CB GLU D 8 12340 8151 7529 -405 -465 429 C ATOM 5127 CG GLU D 8 56.400 -5.157 44.997 1.00 85.74 C ANISOU 5127 CG GLU D 8 13680 9798 9097 -388 -607 355 C ATOM 5128 CD GLU D 8 55.988 -6.249 45.963 1.00107.38 C ANISOU 5128 CD GLU D 8 16455 12564 11782 -194 -664 471 C ATOM 5129 OE1 GLU D 8 56.276 -6.104 47.172 1.00100.42 O ANISOU 5129 OE1 GLU D 8 15656 11735 10765 -87 -730 424 O ATOM 5130 OE2 GLU D 8 55.357 -7.235 45.518 1.00103.59 O ANISOU 5130 OE2 GLU D 8 15937 12040 11382 -149 -624 601 O ATOM 5131 N SER D 9 54.131 -1.604 42.963 1.00 73.42 N ANISOU 5131 N SER D 9 12616 7838 7442 -455 -108 552 N ATOM 5132 CA SER D 9 53.008 -0.684 42.736 1.00 73.93 C ANISOU 5132 CA SER D 9 12885 7806 7401 -304 30 676 C ATOM 5133 C SER D 9 52.100 -1.194 41.594 1.00 76.94 C ANISOU 5133 C SER D 9 13156 8284 7796 -163 30 796 C ATOM 5134 O SER D 9 52.483 -2.106 40.853 1.00 75.36 O ANISOU 5134 O SER D 9 12765 8175 7693 -229 -51 766 O ATOM 5135 CB SER D 9 53.512 0.726 42.421 1.00 78.87 C ANISOU 5135 CB SER D 9 13780 8226 7959 -400 208 606 C ATOM 5136 OG SER D 9 54.334 0.761 41.266 1.00 86.84 O ANISOU 5136 OG SER D 9 14758 9203 9035 -545 274 548 O ATOM 5137 N GLY D 10 50.907 -0.610 41.485 1.00 74.00 N ANISOU 5137 N GLY D 10 12891 7914 7309 49 109 908 N ATOM 5138 CA GLY D 10 49.944 -0.950 40.443 1.00 73.58 C ANISOU 5138 CA GLY D 10 12715 8010 7231 223 91 981 C ATOM 5139 C GLY D 10 48.782 -1.820 40.882 1.00 76.22 C ANISOU 5139 C GLY D 10 12814 8534 7613 320 18 1024 C ATOM 5140 O GLY D 10 48.025 -2.300 40.031 1.00 76.26 O ANISOU 5140 O GLY D 10 12634 8715 7627 419 -30 1023 O ATOM 5141 N GLY D 11 48.650 -2.033 42.198 1.00 71.38 N ANISOU 5141 N GLY D 11 12203 7893 7023 286 21 1043 N ATOM 5142 CA GLY D 11 47.579 -2.841 42.778 1.00 70.88 C ANISOU 5142 CA GLY D 11 11944 7971 7016 339 18 1088 C ATOM 5143 C GLY D 11 46.305 -2.063 43.059 1.00 74.73 C ANISOU 5143 C GLY D 11 12470 8550 7375 577 114 1161 C ATOM 5144 O GLY D 11 45.942 -1.150 42.311 1.00 75.42 O ANISOU 5144 O GLY D 11 12662 8665 7330 766 150 1180 O ATOM 5145 N GLY D 12 45.615 -2.453 44.124 1.00 70.54 N ANISOU 5145 N GLY D 12 11865 8071 6865 599 172 1208 N ATOM 5146 CA GLY D 12 44.394 -1.805 44.585 1.00 71.41 C ANISOU 5146 CA GLY D 12 11980 8294 6858 831 280 1271 C ATOM 5147 C GLY D 12 43.118 -2.370 44.002 1.00 75.04 C ANISOU 5147 C GLY D 12 12087 9043 7380 908 285 1239 C ATOM 5148 O GLY D 12 43.085 -3.521 43.556 1.00 74.46 O ANISOU 5148 O GLY D 12 11757 9055 7481 720 231 1166 O ATOM 5149 N LEU D 13 42.050 -1.562 44.024 1.00 72.20 N ANISOU 5149 N LEU D 13 11709 8850 6876 1191 356 1271 N ATOM 5150 CA LEU D 13 40.745 -1.930 43.486 1.00 73.85 C ANISOU 5150 CA LEU D 13 11533 9413 7114 1309 352 1197 C ATOM 5151 C LEU D 13 40.698 -1.835 41.969 1.00 79.59 C ANISOU 5151 C LEU D 13 12143 10310 7789 1425 209 1105 C ATOM 5152 O LEU D 13 41.258 -0.903 41.378 1.00 79.61 O ANISOU 5152 O LEU D 13 12446 10180 7621 1597 183 1158 O ATOM 5153 CB LEU D 13 39.647 -1.035 44.064 1.00 75.83 C ANISOU 5153 CB LEU D 13 11796 9824 7192 1637 470 1254 C ATOM 5154 CG LEU D 13 39.183 -1.337 45.468 1.00 80.73 C ANISOU 5154 CG LEU D 13 12384 10423 7867 1566 636 1315 C ATOM 5155 CD1 LEU D 13 38.368 -0.197 46.012 1.00 82.80 C ANISOU 5155 CD1 LEU D 13 12775 10779 7908 1938 751 1387 C ATOM 5156 CD2 LEU D 13 38.386 -2.630 45.516 1.00 83.60 C ANISOU 5156 CD2 LEU D 13 12291 11016 8457 1340 696 1218 C ATOM 5157 N VAL D 14 39.966 -2.777 41.346 1.00 76.98 N ANISOU 5157 N VAL D 14 11383 10278 7589 1339 138 955 N ATOM 5158 CA VAL D 14 39.754 -2.848 39.899 1.00 77.35 C ANISOU 5158 CA VAL D 14 11249 10568 7571 1469 -21 824 C ATOM 5159 C VAL D 14 38.364 -3.504 39.651 1.00 83.07 C ANISOU 5159 C VAL D 14 11436 11747 8380 1490 -53 627 C ATOM 5160 O VAL D 14 37.966 -4.398 40.405 1.00 82.84 O ANISOU 5160 O VAL D 14 11169 11734 8573 1202 54 570 O ATOM 5161 CB VAL D 14 40.922 -3.599 39.193 1.00 79.20 C ANISOU 5161 CB VAL D 14 11550 10608 7934 1193 -123 776 C ATOM 5162 CG1 VAL D 14 41.069 -5.037 39.694 1.00 78.42 C ANISOU 5162 CG1 VAL D 14 11236 10432 8127 786 -93 695 C ATOM 5163 CG2 VAL D 14 40.785 -3.555 37.675 1.00 80.21 C ANISOU 5163 CG2 VAL D 14 11562 10970 7943 1375 -283 654 C ATOM 5164 N ARG D 15 37.633 -3.047 38.639 1.00 81.36 N ANISOU 5164 N ARG D 15 11037 11901 7975 1833 -181 515 N ATOM 5165 CA ARG D 15 36.327 -3.629 38.317 1.00 84.12 C ANISOU 5165 CA ARG D 15 10813 12755 8395 1857 -241 264 C ATOM 5166 C ARG D 15 36.492 -5.014 37.688 1.00 87.08 C ANISOU 5166 C ARG D 15 10872 13187 9028 1450 -337 31 C ATOM 5167 O ARG D 15 37.478 -5.260 36.994 1.00 85.11 O ANISOU 5167 O ARG D 15 10833 12724 8781 1352 -438 47 O ATOM 5168 CB ARG D 15 35.547 -2.711 37.375 1.00 87.48 C ANISOU 5168 CB ARG D 15 11141 13605 8491 2416 -386 192 C ATOM 5169 CG ARG D 15 35.675 -1.232 37.701 1.00100.08 C ANISOU 5169 CG ARG D 15 13218 15030 9776 2872 -293 450 C ATOM 5170 CD ARG D 15 34.328 -0.531 37.626 1.00118.06 C ANISOU 5170 CD ARG D 15 15242 17802 11813 3388 -316 377 C ATOM 5171 NE ARG D 15 34.406 0.855 38.077 1.00130.50 N ANISOU 5171 NE ARG D 15 17322 19161 13101 3819 -184 629 N ATOM 5172 CZ ARG D 15 33.446 1.476 38.755 1.00148.10 C ANISOU 5172 CZ ARG D 15 19462 21611 15197 4149 -82 660 C ATOM 5173 NH1 ARG D 15 32.328 0.833 39.063 1.00139.90 N ANISOU 5173 NH1 ARG D 15 17807 21048 14301 4080 -90 450 N ATOM 5174 NH2 ARG D 15 33.603 2.739 39.125 1.00133.34 N ANISOU 5174 NH2 ARG D 15 18122 19482 13059 4537 51 887 N ATOM 5175 N PRO D 16 35.533 -5.931 37.922 1.00 85.07 N ANISOU 5175 N PRO D 16 10115 13209 8997 1195 -283 -201 N ATOM 5176 CA PRO D 16 35.711 -7.255 37.298 1.00 84.85 C ANISOU 5176 CA PRO D 16 9835 13185 9220 787 -353 -446 C ATOM 5177 C PRO D 16 35.693 -7.138 35.776 1.00 89.54 C ANISOU 5177 C PRO D 16 10300 14092 9631 1030 -634 -645 C ATOM 5178 O PRO D 16 34.777 -6.542 35.200 1.00 91.76 O ANISOU 5178 O PRO D 16 10311 14859 9695 1417 -770 -788 O ATOM 5179 CB PRO D 16 34.527 -8.068 37.834 1.00 90.03 C ANISOU 5179 CB PRO D 16 9969 14110 10128 493 -200 -681 C ATOM 5180 CG PRO D 16 34.078 -7.333 39.059 1.00 94.73 C ANISOU 5180 CG PRO D 16 10665 14672 10657 655 10 -465 C ATOM 5181 CD PRO D 16 34.300 -5.893 38.730 1.00 89.44 C ANISOU 5181 CD PRO D 16 10312 14059 9614 1215 -128 -276 C ATOM 5182 N GLY D 17 36.759 -7.636 35.158 1.00 84.19 N ANISOU 5182 N GLY D 17 9854 13133 9001 860 -717 -631 N ATOM 5183 CA GLY D 17 36.984 -7.542 33.723 1.00 85.23 C ANISOU 5183 CA GLY D 17 9974 13473 8937 1089 -961 -774 C ATOM 5184 C GLY D 17 37.932 -6.404 33.405 1.00 87.65 C ANISOU 5184 C GLY D 17 10819 13532 8951 1447 -980 -476 C ATOM 5185 O GLY D 17 38.252 -6.155 32.238 1.00 87.81 O ANISOU 5185 O GLY D 17 10944 13662 8756 1695 -1138 -522 O ATOM 5186 N GLY D 18 38.369 -5.721 34.460 1.00 82.84 N ANISOU 5186 N GLY D 18 10559 12584 8334 1460 -797 -184 N ATOM 5187 CA GLY D 18 39.290 -4.596 34.394 1.00 81.29 C ANISOU 5187 CA GLY D 18 10896 12081 7909 1714 -744 93 C ATOM 5188 C GLY D 18 40.734 -5.035 34.366 1.00 83.21 C ANISOU 5188 C GLY D 18 11436 11891 8288 1404 -707 192 C ATOM 5189 O GLY D 18 41.030 -6.221 34.541 1.00 81.88 O ANISOU 5189 O GLY D 18 11101 11624 8385 1018 -712 81 O ATOM 5190 N SER D 19 41.643 -4.072 34.162 1.00 79.10 N ANISOU 5190 N SER D 19 11364 11104 7584 1574 -645 393 N ATOM 5191 CA SER D 19 43.068 -4.356 34.045 1.00 76.42 C ANISOU 5191 CA SER D 19 11284 10407 7347 1318 -607 468 C ATOM 5192 C SER D 19 43.905 -3.621 35.101 1.00 78.12 C ANISOU 5192 C SER D 19 11864 10239 7577 1227 -438 677 C ATOM 5193 O SER D 19 43.487 -2.591 35.632 1.00 78.52 O ANISOU 5193 O SER D 19 12095 10259 7478 1449 -341 796 O ATOM 5194 CB SER D 19 43.562 -3.960 32.658 1.00 80.71 C ANISOU 5194 CB SER D 19 12009 10986 7670 1545 -669 465 C ATOM 5195 OG SER D 19 42.848 -4.660 31.652 1.00 93.22 O ANISOU 5195 OG SER D 19 13257 12947 9216 1642 -855 237 O ATOM 5196 N LEU D 20 45.094 -4.179 35.397 1.00 72.11 N ANISOU 5196 N LEU D 20 11202 9207 6990 911 -413 695 N ATOM 5197 CA LEU D 20 46.114 -3.631 36.296 1.00 69.96 C ANISOU 5197 CA LEU D 20 11230 8606 6747 776 -292 824 C ATOM 5198 C LEU D 20 47.493 -4.018 35.813 1.00 71.29 C ANISOU 5198 C LEU D 20 11493 8599 6996 573 -305 797 C ATOM 5199 O LEU D 20 47.723 -5.188 35.496 1.00 70.22 O ANISOU 5199 O LEU D 20 11151 8518 7010 405 -399 692 O ATOM 5200 CB LEU D 20 45.934 -4.088 37.766 1.00 69.18 C ANISOU 5200 CB LEU D 20 11054 8425 6804 597 -246 853 C ATOM 5201 CG LEU D 20 44.768 -3.540 38.581 1.00 74.88 C ANISOU 5201 CG LEU D 20 11743 9259 7451 773 -173 910 C ATOM 5202 CD1 LEU D 20 44.720 -4.190 39.934 1.00 74.05 C ANISOU 5202 CD1 LEU D 20 11575 9060 7499 576 -111 938 C ATOM 5203 CD2 LEU D 20 44.884 -2.028 38.774 1.00 78.48 C ANISOU 5203 CD2 LEU D 20 12555 9576 7687 1007 -66 1032 C ATOM 5204 N ARG D 21 48.413 -3.056 35.766 1.00 66.77 N ANISOU 5204 N ARG D 21 11228 7811 6331 575 -191 875 N ATOM 5205 CA ARG D 21 49.787 -3.341 35.379 1.00 66.04 C ANISOU 5205 CA ARG D 21 11196 7575 6321 370 -177 833 C ATOM 5206 C ARG D 21 50.677 -3.246 36.609 1.00 71.16 C ANISOU 5206 C ARG D 21 11922 8035 7082 149 -131 836 C ATOM 5207 O ARG D 21 50.996 -2.141 37.060 1.00 71.54 O ANISOU 5207 O ARG D 21 12215 7918 7048 152 -3 882 O ATOM 5208 CB ARG D 21 50.254 -2.396 34.269 1.00 67.20 C ANISOU 5208 CB ARG D 21 11604 7641 6290 501 -53 880 C ATOM 5209 CG ARG D 21 51.699 -2.620 33.803 1.00 74.94 C ANISOU 5209 CG ARG D 21 12625 8494 7356 279 2 825 C ATOM 5210 CD ARG D 21 52.100 -1.574 32.774 1.00 83.10 C ANISOU 5210 CD ARG D 21 13969 9404 8202 401 200 895 C ATOM 5211 NE ARG D 21 51.340 -1.712 31.531 1.00 89.94 N ANISOU 5211 NE ARG D 21 14827 10462 8883 703 141 914 N ATOM 5212 CZ ARG D 21 51.353 -0.827 30.542 1.00105.80 C ANISOU 5212 CZ ARG D 21 17145 12404 10652 939 309 1009 C ATOM 5213 NH1 ARG D 21 52.019 0.312 30.668 1.00 94.71 N ANISOU 5213 NH1 ARG D 21 16104 10697 9184 875 586 1101 N ATOM 5214 NH2 ARG D 21 50.641 -1.046 29.443 1.00 94.24 N ANISOU 5214 NH2 ARG D 21 15648 11171 8990 1257 212 1003 N ATOM 5215 N LEU D 22 51.038 -4.401 37.183 1.00 68.09 N ANISOU 5215 N LEU D 22 11340 7670 6862 -20 -232 775 N ATOM 5216 CA LEU D 22 51.903 -4.432 38.355 1.00 67.90 C ANISOU 5216 CA LEU D 22 11365 7527 6909 -173 -228 756 C ATOM 5217 C LEU D 22 53.349 -4.183 37.941 1.00 73.99 C ANISOU 5217 C LEU D 22 12190 8219 7705 -319 -196 675 C ATOM 5218 O LEU D 22 53.755 -4.597 36.857 1.00 74.05 O ANISOU 5218 O LEU D 22 12125 8275 7735 -337 -210 633 O ATOM 5219 CB LEU D 22 51.775 -5.760 39.113 1.00 67.36 C ANISOU 5219 CB LEU D 22 11122 7502 6970 -237 -323 740 C ATOM 5220 CG LEU D 22 50.409 -6.088 39.744 1.00 72.63 C ANISOU 5220 CG LEU D 22 11714 8233 7649 -157 -305 805 C ATOM 5221 CD1 LEU D 22 50.433 -7.453 40.388 1.00 72.75 C ANISOU 5221 CD1 LEU D 22 11622 8226 7795 -246 -337 796 C ATOM 5222 CD2 LEU D 22 50.014 -5.066 40.789 1.00 75.71 C ANISOU 5222 CD2 LEU D 22 12269 8567 7931 -70 -224 882 C ATOM 5223 N SER D 23 54.109 -3.446 38.766 1.00 72.38 N ANISOU 5223 N SER D 23 12105 7909 7487 -427 -139 629 N ATOM 5224 CA SER D 23 55.509 -3.129 38.481 1.00 73.40 C ANISOU 5224 CA SER D 23 12239 7992 7659 -610 -85 506 C ATOM 5225 C SER D 23 56.356 -3.212 39.756 1.00 79.06 C ANISOU 5225 C SER D 23 12892 8728 8420 -729 -164 384 C ATOM 5226 O SER D 23 55.981 -2.682 40.806 1.00 78.56 O ANISOU 5226 O SER D 23 12945 8611 8296 -699 -159 397 O ATOM 5227 CB SER D 23 55.641 -1.749 37.848 1.00 78.50 C ANISOU 5227 CB SER D 23 13139 8475 8210 -644 133 521 C ATOM 5228 OG SER D 23 55.121 -0.736 38.691 1.00 89.52 O ANISOU 5228 OG SER D 23 14757 9739 9519 -602 219 560 O ATOM 5229 N CYS D 24 57.504 -3.887 39.642 1.00 77.43 N ANISOU 5229 N CYS D 24 12496 8626 8296 -831 -244 254 N ATOM 5230 CA CYS D 24 58.453 -4.138 40.718 1.00 78.74 C ANISOU 5230 CA CYS D 24 12542 8894 8481 -891 -363 102 C ATOM 5231 C CYS D 24 59.837 -3.719 40.264 1.00 84.00 C ANISOU 5231 C CYS D 24 13086 9621 9207 -1101 -302 -104 C ATOM 5232 O CYS D 24 60.313 -4.201 39.231 1.00 83.44 O ANISOU 5232 O CYS D 24 12897 9608 9198 -1129 -275 -120 O ATOM 5233 CB CYS D 24 58.406 -5.609 41.113 1.00 78.81 C ANISOU 5233 CB CYS D 24 12410 9020 8515 -734 -535 147 C ATOM 5234 SG CYS D 24 59.553 -6.073 42.433 1.00 84.42 S ANISOU 5234 SG CYS D 24 12987 9909 9179 -681 -714 -24 S ATOM 5235 N VAL D 25 60.476 -2.797 41.001 1.00 82.04 N ANISOU 5235 N VAL D 25 12860 9365 8945 -1267 -262 -284 N ATOM 5236 CA VAL D 25 61.779 -2.289 40.584 1.00 83.61 C ANISOU 5236 CA VAL D 25 12914 9628 9227 -1531 -160 -524 C ATOM 5237 C VAL D 25 62.746 -2.225 41.790 1.00 88.69 C ANISOU 5237 C VAL D 25 13357 10478 9863 -1615 -317 -807 C ATOM 5238 O VAL D 25 62.370 -1.813 42.890 1.00 88.13 O ANISOU 5238 O VAL D 25 13406 10375 9704 -1569 -387 -836 O ATOM 5239 CB VAL D 25 61.637 -0.892 39.900 1.00 88.59 C ANISOU 5239 CB VAL D 25 13811 9988 9861 -1738 155 -513 C ATOM 5240 CG1 VAL D 25 60.889 0.116 40.780 1.00 88.81 C ANISOU 5240 CG1 VAL D 25 14128 9819 9796 -1732 219 -481 C ATOM 5241 CG2 VAL D 25 62.987 -0.340 39.437 1.00 91.18 C ANISOU 5241 CG2 VAL D 25 13993 10350 10299 -2073 331 -773 C ATOM 5242 N ASP D 26 63.997 -2.643 41.548 1.00 86.69 N ANISOU 5242 N ASP D 26 12784 10468 9687 -1715 -377 -1030 N ATOM 5243 CA ASP D 26 65.079 -2.559 42.515 1.00 89.22 C ANISOU 5243 CA ASP D 26 12836 11067 9996 -1797 -535 -1365 C ATOM 5244 C ASP D 26 66.106 -1.568 41.974 1.00 95.52 C ANISOU 5244 C ASP D 26 13493 11874 10927 -2212 -308 -1657 C ATOM 5245 O ASP D 26 67.001 -1.938 41.209 1.00 95.58 O ANISOU 5245 O ASP D 26 13229 12054 11032 -2306 -259 -1776 O ATOM 5246 CB ASP D 26 65.685 -3.943 42.810 1.00 91.22 C ANISOU 5246 CB ASP D 26 12802 11654 10203 -1512 -809 -1409 C ATOM 5247 CG ASP D 26 66.775 -3.960 43.875 1.00106.48 C ANISOU 5247 CG ASP D 26 14432 13957 12068 -1493 -1030 -1765 C ATOM 5248 OD1 ASP D 26 66.966 -2.925 44.558 1.00108.90 O ANISOU 5248 OD1 ASP D 26 14754 14261 12361 -1711 -1003 -1995 O ATOM 5249 OD2 ASP D 26 67.378 -5.024 44.081 1.00114.62 O ANISOU 5249 OD2 ASP D 26 15234 15281 13035 -1222 -1241 -1819 O ATOM 5250 N SER D 27 65.928 -0.291 42.339 1.00 93.97 N ANISOU 5250 N SER D 27 13510 11457 10737 -2468 -131 -1766 N ATOM 5251 CA SER D 27 66.760 0.828 41.902 1.00 97.38 C ANISOU 5251 CA SER D 27 13902 11792 11307 -2926 166 -2043 C ATOM 5252 C SER D 27 68.212 0.696 42.403 1.00105.19 C ANISOU 5252 C SER D 27 14387 13205 12374 -3128 25 -2511 C ATOM 5253 O SER D 27 69.135 1.081 41.681 1.00107.03 O ANISOU 5253 O SER D 27 14417 13484 12764 -3472 257 -2730 O ATOM 5254 CB SER D 27 66.164 2.140 42.397 1.00101.95 C ANISOU 5254 CB SER D 27 14870 12019 11847 -3106 361 -2063 C ATOM 5255 OG SER D 27 64.838 2.303 41.920 1.00106.87 O ANISOU 5255 OG SER D 27 15926 12301 12379 -2882 488 -1653 O ATOM 5256 N GLU D 28 68.412 0.125 43.619 1.00102.97 N ANISOU 5256 N GLU D 28 13897 13259 11970 -2888 -348 -2665 N ATOM 5257 CA GLU D 28 69.746 -0.070 44.221 1.00106.88 C ANISOU 5257 CA GLU D 28 13877 14247 12485 -2982 -557 -3136 C ATOM 5258 C GLU D 28 70.539 -1.166 43.475 1.00109.34 C ANISOU 5258 C GLU D 28 13804 14891 12850 -2827 -644 -3146 C ATOM 5259 O GLU D 28 71.751 -1.292 43.677 1.00112.33 O ANISOU 5259 O GLU D 28 13698 15707 13275 -2931 -758 -3550 O ATOM 5260 CB GLU D 28 69.669 -0.429 45.727 1.00109.18 C ANISOU 5260 CB GLU D 28 14105 14818 12560 -2661 -948 -3264 C ATOM 5261 CG GLU D 28 68.901 0.546 46.614 1.00121.52 C ANISOU 5261 CG GLU D 28 16036 16106 14031 -2745 -908 -3273 C ATOM 5262 CD GLU D 28 67.395 0.356 46.716 1.00145.00 C ANISOU 5262 CD GLU D 28 19502 18709 16883 -2436 -877 -2775 C ATOM 5263 OE1 GLU D 28 66.917 -0.782 46.497 1.00137.17 O ANISOU 5263 OE1 GLU D 28 18536 17758 15823 -2062 -1004 -2449 O ATOM 5264 OE2 GLU D 28 66.717 1.306 47.171 1.00143.84 O ANISOU 5264 OE2 GLU D 28 19695 18268 16691 -2546 -752 -2752 O ATOM 5265 N ARG D 29 69.844 -1.952 42.617 1.00101.38 N ANISOU 5265 N ARG D 29 13000 13692 11828 -2569 -594 -2725 N ATOM 5266 CA ARG D 29 70.397 -3.030 41.785 1.00100.60 C ANISOU 5266 CA ARG D 29 12644 13815 11765 -2383 -643 -2664 C ATOM 5267 C ARG D 29 71.064 -4.101 42.681 1.00105.51 C ANISOU 5267 C ARG D 29 12923 14922 12243 -1992 -1041 -2833 C ATOM 5268 O ARG D 29 72.168 -4.561 42.380 1.00107.87 O ANISOU 5268 O ARG D 29 12798 15601 12585 -1971 -1103 -3075 O ATOM 5269 CB ARG D 29 71.413 -2.459 40.751 1.00103.60 C ANISOU 5269 CB ARG D 29 12759 14259 12345 -2807 -332 -2908 C ATOM 5270 CG ARG D 29 70.948 -1.211 39.975 1.00111.07 C ANISOU 5270 CG ARG D 29 14068 14728 13407 -3214 109 -2802 C ATOM 5271 CD ARG D 29 69.990 -1.448 38.824 1.00111.04 C ANISOU 5271 CD ARG D 29 14453 14361 13378 -3060 298 -2352 C ATOM 5272 NE ARG D 29 69.436 -0.174 38.351 1.00114.85 N ANISOU 5272 NE ARG D 29 15353 14386 13899 -3354 682 -2243 N ATOM 5273 CZ ARG D 29 68.839 0.001 37.176 1.00124.02 C ANISOU 5273 CZ ARG D 29 16845 15235 15043 -3320 953 -1939 C ATOM 5274 NH1 ARG D 29 68.820 -0.973 36.277 1.00109.90 N ANISOU 5274 NH1 ARG D 29 14976 13553 13229 -3077 900 -1759 N ATOM 5275 NH2 ARG D 29 68.349 1.192 36.850 1.00107.87 N ANISOU 5275 NH2 ARG D 29 15218 12774 12992 -3527 1300 -1840 N ATOM 5276 N THR D 30 70.396 -4.470 43.795 1.00100.12 N ANISOU 5276 N THR D 30 12440 14231 11369 -1658 -1291 -2704 N ATOM 5277 CA THR D 30 70.894 -5.476 44.748 1.00100.90 C ANISOU 5277 CA THR D 30 12329 14741 11267 -1201 -1656 -2809 C ATOM 5278 C THR D 30 70.276 -6.865 44.415 1.00100.53 C ANISOU 5278 C THR D 30 12500 14565 11131 -749 -1728 -2403 C ATOM 5279 O THR D 30 70.715 -7.880 44.967 1.00100.94 O ANISOU 5279 O THR D 30 12432 14907 11012 -315 -1977 -2429 O ATOM 5280 CB THR D 30 70.600 -5.053 46.218 1.00106.57 C ANISOU 5280 CB THR D 30 13166 15531 11794 -1083 -1861 -2926 C ATOM 5281 OG1 THR D 30 69.216 -4.734 46.369 1.00 99.83 O ANISOU 5281 OG1 THR D 30 12808 14207 10915 -1085 -1730 -2567 O ATOM 5282 CG2 THR D 30 71.431 -3.854 46.660 1.00108.60 C ANISOU 5282 CG2 THR D 30 13132 16012 12120 -1495 -1850 -3431 C ATOM 5283 N SER D 31 69.296 -6.898 43.482 1.00 93.15 N ANISOU 5283 N SER D 31 11883 13204 10304 -850 -1500 -2055 N ATOM 5284 CA SER D 31 68.589 -8.103 43.023 1.00 90.10 C ANISOU 5284 CA SER D 31 11723 12631 9880 -530 -1512 -1699 C ATOM 5285 C SER D 31 67.892 -7.863 41.681 1.00 92.57 C ANISOU 5285 C SER D 31 12223 12599 10352 -763 -1241 -1477 C ATOM 5286 O SER D 31 67.740 -6.709 41.262 1.00 92.21 O ANISOU 5286 O SER D 31 12235 12392 10407 -1120 -1033 -1526 O ATOM 5287 CB SER D 31 67.557 -8.556 44.056 1.00 90.85 C ANISOU 5287 CB SER D 31 12154 12553 9811 -233 -1628 -1451 C ATOM 5288 OG SER D 31 66.511 -7.612 44.222 1.00 94.13 O ANISOU 5288 OG SER D 31 12845 12659 10261 -457 -1484 -1318 O ATOM 5289 N TYR D 32 67.446 -8.954 41.019 1.00 87.97 N ANISOU 5289 N TYR D 32 11764 11891 9769 -539 -1237 -1239 N ATOM 5290 CA TYR D 32 66.716 -8.876 39.752 1.00 85.55 C ANISOU 5290 CA TYR D 32 11636 11300 9568 -684 -1027 -1036 C ATOM 5291 C TYR D 32 65.271 -9.335 39.942 1.00 85.64 C ANISOU 5291 C TYR D 32 11986 11017 9537 -537 -1034 -733 C ATOM 5292 O TYR D 32 65.056 -10.535 40.126 1.00 85.35 O ANISOU 5292 O TYR D 32 12017 10962 9449 -262 -1138 -618 O ATOM 5293 CB TYR D 32 67.383 -9.715 38.625 1.00 87.47 C ANISOU 5293 CB TYR D 32 11717 11652 9864 -598 -992 -1063 C ATOM 5294 CG TYR D 32 68.877 -9.545 38.467 1.00 93.20 C ANISOU 5294 CG TYR D 32 12045 12739 10628 -678 -998 -1375 C ATOM 5295 CD1 TYR D 32 69.413 -8.373 37.944 1.00 96.90 C ANISOU 5295 CD1 TYR D 32 12370 13238 11209 -1067 -782 -1553 C ATOM 5296 CD2 TYR D 32 69.744 -10.606 38.701 1.00 96.30 C ANISOU 5296 CD2 TYR D 32 12213 13431 10948 -359 -1179 -1487 C ATOM 5297 CE1 TYR D 32 70.788 -8.220 37.772 1.00102.12 C ANISOU 5297 CE1 TYR D 32 12616 14253 11931 -1186 -754 -1873 C ATOM 5298 CE2 TYR D 32 71.119 -10.474 38.516 1.00100.84 C ANISOU 5298 CE2 TYR D 32 12362 14396 11558 -415 -1187 -1800 C ATOM 5299 CZ TYR D 32 71.638 -9.278 38.051 1.00111.14 C ANISOU 5299 CZ TYR D 32 13473 15755 13000 -855 -971 -2005 C ATOM 5300 OH TYR D 32 72.995 -9.151 37.859 1.00116.90 O ANISOU 5300 OH TYR D 32 13737 16893 13788 -953 -948 -2345 O ATOM 5301 N PRO D 33 64.259 -8.438 39.899 1.00 79.27 N ANISOU 5301 N PRO D 33 11397 9973 8748 -705 -906 -607 N ATOM 5302 CA PRO D 33 62.871 -8.913 39.979 1.00 76.89 C ANISOU 5302 CA PRO D 33 11350 9442 8422 -578 -899 -349 C ATOM 5303 C PRO D 33 62.569 -9.781 38.754 1.00 80.85 C ANISOU 5303 C PRO D 33 11867 9867 8986 -521 -850 -248 C ATOM 5304 O PRO D 33 62.662 -9.298 37.620 1.00 80.29 O ANISOU 5304 O PRO D 33 11776 9767 8964 -664 -720 -266 O ATOM 5305 CB PRO D 33 62.051 -7.617 40.030 1.00 77.85 C ANISOU 5305 CB PRO D 33 11646 9391 8540 -760 -761 -285 C ATOM 5306 CG PRO D 33 63.036 -6.520 40.282 1.00 84.23 C ANISOU 5306 CG PRO D 33 12340 10304 9361 -977 -709 -515 C ATOM 5307 CD PRO D 33 64.309 -6.984 39.684 1.00 81.25 C ANISOU 5307 CD PRO D 33 11685 10145 9043 -1009 -732 -695 C ATOM 5308 N MET D 34 62.329 -11.094 38.980 1.00 77.84 N ANISOU 5308 N MET D 34 11536 9453 8588 -301 -943 -162 N ATOM 5309 CA MET D 34 62.142 -12.085 37.914 1.00 77.28 C ANISOU 5309 CA MET D 34 11480 9311 8571 -236 -916 -114 C ATOM 5310 C MET D 34 60.919 -13.002 38.139 1.00 79.61 C ANISOU 5310 C MET D 34 11968 9398 8883 -144 -911 48 C ATOM 5311 O MET D 34 60.675 -13.891 37.317 1.00 79.84 O ANISOU 5311 O MET D 34 12027 9346 8964 -108 -889 60 O ATOM 5312 CB MET D 34 63.399 -12.965 37.806 1.00 81.63 C ANISOU 5312 CB MET D 34 11877 10036 9102 -62 -1001 -238 C ATOM 5313 CG MET D 34 64.619 -12.228 37.264 1.00 87.09 C ANISOU 5313 CG MET D 34 12317 10958 9815 -190 -965 -432 C ATOM 5314 SD MET D 34 66.165 -13.178 37.314 1.00 94.42 S ANISOU 5314 SD MET D 34 12993 12186 10699 61 -1084 -615 S ATOM 5315 CE MET D 34 65.733 -14.595 36.251 1.00 90.21 C ANISOU 5315 CE MET D 34 12624 11463 10189 238 -1050 -496 C ATOM 5316 N GLY D 35 60.165 -12.787 39.214 1.00 74.26 N ANISOU 5316 N GLY D 35 11415 8634 8168 -126 -909 150 N ATOM 5317 CA GLY D 35 59.001 -13.619 39.502 1.00 72.76 C ANISOU 5317 CA GLY D 35 11387 8246 8011 -82 -856 287 C ATOM 5318 C GLY D 35 57.809 -12.934 40.139 1.00 72.98 C ANISOU 5318 C GLY D 35 11508 8191 8030 -164 -788 396 C ATOM 5319 O GLY D 35 57.925 -11.843 40.699 1.00 71.64 O ANISOU 5319 O GLY D 35 11333 8093 7794 -202 -800 385 O ATOM 5320 N TRP D 36 56.647 -13.599 40.049 1.00 68.15 N ANISOU 5320 N TRP D 36 10973 7429 7490 -201 -702 480 N ATOM 5321 CA TRP D 36 55.382 -13.165 40.631 1.00 66.82 C ANISOU 5321 CA TRP D 36 10865 7198 7328 -262 -614 581 C ATOM 5322 C TRP D 36 54.691 -14.325 41.326 1.00 72.96 C ANISOU 5322 C TRP D 36 11777 7794 8152 -226 -504 675 C ATOM 5323 O TRP D 36 54.558 -15.408 40.747 1.00 72.74 O ANISOU 5323 O TRP D 36 11764 7652 8221 -263 -458 639 O ATOM 5324 CB TRP D 36 54.442 -12.555 39.579 1.00 63.92 C ANISOU 5324 CB TRP D 36 10391 6883 7014 -391 -582 549 C ATOM 5325 CG TRP D 36 54.933 -11.293 38.939 1.00 63.63 C ANISOU 5325 CG TRP D 36 10303 6964 6909 -417 -618 498 C ATOM 5326 CD1 TRP D 36 55.436 -11.153 37.680 1.00 66.09 C ANISOU 5326 CD1 TRP D 36 10541 7345 7227 -448 -642 413 C ATOM 5327 CD2 TRP D 36 54.958 -9.987 39.531 1.00 62.82 C ANISOU 5327 CD2 TRP D 36 10263 6891 6715 -419 -595 531 C ATOM 5328 NE1 TRP D 36 55.725 -9.832 37.431 1.00 65.11 N ANISOU 5328 NE1 TRP D 36 10444 7270 7025 -477 -605 407 N ATOM 5329 CE2 TRP D 36 55.480 -9.100 38.564 1.00 66.44 C ANISOU 5329 CE2 TRP D 36 10699 7405 7140 -470 -578 467 C ATOM 5330 CE3 TRP D 36 54.597 -9.479 40.791 1.00 64.02 C ANISOU 5330 CE3 TRP D 36 10515 7009 6801 -377 -566 603 C ATOM 5331 CZ2 TRP D 36 55.646 -7.735 38.817 1.00 65.77 C ANISOU 5331 CZ2 TRP D 36 10708 7307 6975 -507 -516 469 C ATOM 5332 CZ3 TRP D 36 54.759 -8.127 41.038 1.00 65.17 C ANISOU 5332 CZ3 TRP D 36 10732 7169 6860 -400 -538 589 C ATOM 5333 CH2 TRP D 36 55.279 -7.271 40.061 1.00 65.74 C ANISOU 5333 CH2 TRP D 36 10798 7263 6917 -476 -504 520 C ATOM 5334 N PHE D 37 54.273 -14.098 42.578 1.00 71.48 N ANISOU 5334 N PHE D 37 11714 7557 7887 -158 -437 790 N ATOM 5335 CA PHE D 37 53.524 -15.042 43.416 1.00 73.66 C ANISOU 5335 CA PHE D 37 12164 7636 8188 -130 -265 912 C ATOM 5336 C PHE D 37 52.326 -14.321 44.030 1.00 77.76 C ANISOU 5336 C PHE D 37 12674 8171 8702 -203 -151 993 C ATOM 5337 O PHE D 37 52.350 -13.095 44.129 1.00 76.14 O ANISOU 5337 O PHE D 37 12402 8112 8415 -189 -232 976 O ATOM 5338 CB PHE D 37 54.422 -15.670 44.503 1.00 77.38 C ANISOU 5338 CB PHE D 37 12862 8033 8507 130 -276 996 C ATOM 5339 CG PHE D 37 55.376 -16.732 44.002 1.00 80.52 C ANISOU 5339 CG PHE D 37 13314 8366 8912 249 -327 943 C ATOM 5340 CD1 PHE D 37 56.592 -16.383 43.420 1.00 83.45 C ANISOU 5340 CD1 PHE D 37 13530 8940 9236 324 -524 809 C ATOM 5341 CD2 PHE D 37 55.081 -18.084 44.157 1.00 84.93 C ANISOU 5341 CD2 PHE D 37 14100 8649 9520 295 -147 1023 C ATOM 5342 CE1 PHE D 37 57.468 -17.370 42.944 1.00 85.55 C ANISOU 5342 CE1 PHE D 37 13836 9171 9498 470 -566 756 C ATOM 5343 CE2 PHE D 37 55.967 -19.068 43.704 1.00 89.06 C ANISOU 5343 CE2 PHE D 37 14715 9094 10031 448 -183 978 C ATOM 5344 CZ PHE D 37 57.155 -18.705 43.104 1.00 86.43 C ANISOU 5344 CZ PHE D 37 14198 9001 9639 554 -405 846 C ATOM 5345 N ARG D 38 51.258 -15.053 44.388 1.00 76.09 N ANISOU 5345 N ARG D 38 12523 7804 8583 -293 60 1065 N ATOM 5346 CA ARG D 38 50.082 -14.416 44.989 1.00 76.32 C ANISOU 5346 CA ARG D 38 12512 7877 8607 -349 191 1135 C ATOM 5347 C ARG D 38 49.534 -15.284 46.111 1.00 83.33 C ANISOU 5347 C ARG D 38 13621 8549 9493 -324 451 1283 C ATOM 5348 O ARG D 38 49.617 -16.512 46.041 1.00 83.99 O ANISOU 5348 O ARG D 38 13835 8414 9662 -370 585 1298 O ATOM 5349 CB ARG D 38 48.974 -14.117 43.945 1.00 75.11 C ANISOU 5349 CB ARG D 38 12078 7857 8603 -550 209 1016 C ATOM 5350 CG ARG D 38 48.323 -15.331 43.277 1.00 80.98 C ANISOU 5350 CG ARG D 38 12724 8491 9553 -764 339 914 C ATOM 5351 CD ARG D 38 47.289 -14.904 42.259 1.00 82.07 C ANISOU 5351 CD ARG D 38 12539 8854 9790 -909 296 752 C ATOM 5352 NE ARG D 38 46.659 -16.048 41.601 1.00 91.36 N ANISOU 5352 NE ARG D 38 13585 9957 11172 -1149 405 590 N ATOM 5353 CZ ARG D 38 45.760 -15.949 40.626 1.00105.38 C ANISOU 5353 CZ ARG D 38 15046 11953 13042 -1286 353 387 C ATOM 5354 NH1 ARG D 38 45.394 -14.757 40.172 1.00 92.33 N ANISOU 5354 NH1 ARG D 38 13208 10599 11273 -1156 199 356 N ATOM 5355 NH2 ARG D 38 45.236 -17.041 40.085 1.00 94.18 N ANISOU 5355 NH2 ARG D 38 13508 10459 11817 -1536 454 196 N ATOM 5356 N ARG D 39 48.979 -14.648 47.149 1.00 82.24 N ANISOU 5356 N ARG D 39 13559 8445 9244 -242 551 1397 N ATOM 5357 CA ARG D 39 48.405 -15.396 48.253 1.00 85.84 C ANISOU 5357 CA ARG D 39 14248 8692 9675 -208 845 1559 C ATOM 5358 C ARG D 39 46.968 -14.923 48.472 1.00 93.82 C ANISOU 5358 C ARG D 39 15091 9787 10769 -359 1039 1572 C ATOM 5359 O ARG D 39 46.738 -13.774 48.853 1.00 92.29 O ANISOU 5359 O ARG D 39 14843 9771 10453 -254 962 1593 O ATOM 5360 CB ARG D 39 49.261 -15.257 49.521 1.00 86.46 C ANISOU 5360 CB ARG D 39 14644 8732 9477 120 802 1702 C ATOM 5361 CG ARG D 39 48.955 -16.321 50.568 1.00 99.61 C ANISOU 5361 CG ARG D 39 16655 10117 11075 223 1121 1896 C ATOM 5362 CD ARG D 39 49.913 -16.263 51.737 1.00111.23 C ANISOU 5362 CD ARG D 39 18450 11589 12221 622 1033 2018 C ATOM 5363 NE ARG D 39 49.662 -17.347 52.689 1.00125.55 N ANISOU 5363 NE ARG D 39 20666 13102 13934 775 1367 2232 N ATOM 5364 CZ ARG D 39 50.283 -18.524 52.679 1.00142.39 C ANISOU 5364 CZ ARG D 39 23074 15001 16027 923 1449 2301 C ATOM 5365 NH1 ARG D 39 51.210 -18.789 51.766 1.00126.41 N ANISOU 5365 NH1 ARG D 39 20929 13038 14062 938 1201 2160 N ATOM 5366 NH2 ARG D 39 49.989 -19.443 53.590 1.00134.35 N ANISOU 5366 NH2 ARG D 39 22484 13672 14893 1081 1805 2522 N ATOM 5367 N ALA D 40 46.003 -15.808 48.158 1.00 95.44 N ANISOU 5367 N ALA D 40 15192 9877 11195 -619 1293 1527 N ATOM 5368 CA ALA D 40 44.566 -15.560 48.302 1.00 98.27 C ANISOU 5368 CA ALA D 40 15322 10345 11671 -797 1512 1498 C ATOM 5369 C ALA D 40 44.172 -15.501 49.803 1.00107.70 C ANISOU 5369 C ALA D 40 16778 11425 12718 -656 1788 1717 C ATOM 5370 O ALA D 40 44.953 -15.975 50.636 1.00108.62 O ANISOU 5370 O ALA D 40 17277 11323 12670 -453 1846 1881 O ATOM 5371 CB ALA D 40 43.782 -16.647 47.579 1.00101.36 C ANISOU 5371 CB ALA D 40 15523 10638 12351 -1149 1718 1342 C ATOM 5372 N PRO D 41 42.988 -14.929 50.183 1.00107.05 N ANISOU 5372 N PRO D 41 16506 11506 12663 -717 1962 1722 N ATOM 5373 CA PRO D 41 42.634 -14.827 51.620 1.00109.05 C ANISOU 5373 CA PRO D 41 17026 11658 12748 -556 2236 1937 C ATOM 5374 C PRO D 41 42.766 -16.156 52.392 1.00116.09 C ANISOU 5374 C PRO D 41 18301 12163 13647 -585 2595 2105 C ATOM 5375 O PRO D 41 43.215 -16.151 53.542 1.00116.90 O ANISOU 5375 O PRO D 41 18795 12131 13492 -297 2683 2315 O ATOM 5376 CB PRO D 41 41.159 -14.384 51.598 1.00112.50 C ANISOU 5376 CB PRO D 41 17108 12322 13315 -720 2438 1860 C ATOM 5377 CG PRO D 41 40.714 -14.494 50.149 1.00116.50 C ANISOU 5377 CG PRO D 41 17165 13026 14074 -988 2290 1590 C ATOM 5378 CD PRO D 41 41.953 -14.289 49.348 1.00108.73 C ANISOU 5378 CD PRO D 41 16258 12036 13017 -872 1902 1534 C ATOM 5379 N GLY D 42 42.398 -17.265 51.754 1.00114.04 N ANISOU 5379 N GLY D 42 17956 11718 13656 -910 2799 2003 N ATOM 5380 CA GLY D 42 42.470 -18.582 52.370 1.00117.15 C ANISOU 5380 CA GLY D 42 18753 11680 14078 -967 3196 2156 C ATOM 5381 C GLY D 42 43.591 -19.457 51.849 1.00119.86 C ANISOU 5381 C GLY D 42 19344 11778 14419 -903 3058 2143 C ATOM 5382 O GLY D 42 44.350 -20.021 52.641 1.00120.61 O ANISOU 5382 O GLY D 42 19926 11603 14300 -615 3160 2354 O ATOM 5383 N LYS D 43 43.702 -19.570 50.503 1.00114.43 N ANISOU 5383 N LYS D 43 18329 11204 13943 -1129 2821 1890 N ATOM 5384 CA LYS D 43 44.672 -20.418 49.789 1.00113.57 C ANISOU 5384 CA LYS D 43 18385 10893 13874 -1110 2689 1828 C ATOM 5385 C LYS D 43 46.144 -20.061 50.122 1.00114.16 C ANISOU 5385 C LYS D 43 18726 11014 13635 -649 2352 1956 C ATOM 5386 O LYS D 43 46.442 -18.967 50.625 1.00111.93 O ANISOU 5386 O LYS D 43 18399 10989 13140 -404 2128 2017 O ATOM 5387 CB LYS D 43 44.466 -20.304 48.270 1.00114.32 C ANISOU 5387 CB LYS D 43 18021 11207 14206 -1393 2441 1515 C ATOM 5388 N GLU D 44 47.059 -21.018 49.850 1.00110.23 N ANISOU 5388 N GLU D 44 18503 10269 13110 -533 2332 1973 N ATOM 5389 CA GLU D 44 48.500 -20.887 50.088 1.00108.10 C ANISOU 5389 CA GLU D 44 18450 10062 12562 -100 2027 2050 C ATOM 5390 C GLU D 44 49.158 -20.041 48.987 1.00107.26 C ANISOU 5390 C GLU D 44 17953 10310 12490 -120 1571 1837 C ATOM 5391 O GLU D 44 48.459 -19.481 48.138 1.00105.29 O ANISOU 5391 O GLU D 44 17316 10256 12435 -411 1491 1665 O ATOM 5392 CB GLU D 44 49.147 -22.282 50.158 1.00112.29 C ANISOU 5392 CB GLU D 44 19418 10198 13050 54 2210 2143 C ATOM 5393 N ARG D 45 50.507 -19.961 49.003 1.00101.91 N ANISOU 5393 N ARG D 45 17382 9728 11611 208 1288 1841 N ATOM 5394 CA ARG D 45 51.320 -19.234 48.022 1.00 98.01 C ANISOU 5394 CA ARG D 45 16574 9536 11130 212 901 1653 C ATOM 5395 C ARG D 45 51.149 -19.875 46.632 1.00 99.06 C ANISOU 5395 C ARG D 45 16528 9591 11520 -68 903 1476 C ATOM 5396 O ARG D 45 51.371 -21.080 46.483 1.00100.89 O ANISOU 5396 O ARG D 45 16997 9534 11801 -47 1060 1496 O ATOM 5397 CB ARG D 45 52.798 -19.251 48.474 1.00 99.56 C ANISOU 5397 CB ARG D 45 16936 9831 11059 624 668 1686 C ATOM 5398 CG ARG D 45 53.723 -18.318 47.697 1.00110.02 C ANISOU 5398 CG ARG D 45 17938 11498 12368 634 299 1497 C ATOM 5399 CD ARG D 45 55.198 -18.612 47.955 1.00124.84 C ANISOU 5399 CD ARG D 45 19917 13484 14030 1004 93 1471 C ATOM 5400 NE ARG D 45 55.612 -19.886 47.354 1.00139.31 N ANISOU 5400 NE ARG D 45 21898 15107 15928 1076 168 1466 N ATOM 5401 CZ ARG D 45 56.847 -20.381 47.405 1.00157.36 C ANISOU 5401 CZ ARG D 45 24274 17471 18046 1421 18 1437 C ATOM 5402 NH1 ARG D 45 57.811 -19.722 48.037 1.00145.44 N ANISOU 5402 NH1 ARG D 45 22680 16278 16302 1707 -232 1382 N ATOM 5403 NH2 ARG D 45 57.126 -21.542 46.825 1.00147.02 N ANISOU 5403 NH2 ARG D 45 23127 15936 16796 1489 115 1437 N ATOM 5404 N GLU D 46 50.700 -19.089 45.639 1.00 91.52 N ANISOU 5404 N GLU D 46 15190 8877 10708 -308 749 1304 N ATOM 5405 CA GLU D 46 50.459 -19.578 44.277 1.00 90.46 C ANISOU 5405 CA GLU D 46 14854 8729 10787 -559 719 1105 C ATOM 5406 C GLU D 46 51.365 -18.854 43.265 1.00 90.32 C ANISOU 5406 C GLU D 46 14612 8984 10719 -486 386 969 C ATOM 5407 O GLU D 46 51.424 -17.622 43.263 1.00 87.69 O ANISOU 5407 O GLU D 46 14108 8907 10303 -446 223 961 O ATOM 5408 CB GLU D 46 48.970 -19.381 43.903 1.00 92.31 C ANISOU 5408 CB GLU D 46 14822 9031 11222 -896 862 996 C ATOM 5409 CG GLU D 46 48.582 -19.846 42.503 1.00100.97 C ANISOU 5409 CG GLU D 46 15676 10167 12522 -1158 813 744 C ATOM 5410 CD GLU D 46 47.135 -19.617 42.093 1.00118.43 C ANISOU 5410 CD GLU D 46 17553 12537 14908 -1458 907 582 C ATOM 5411 OE1 GLU D 46 46.309 -19.259 42.964 1.00117.82 O ANISOU 5411 OE1 GLU D 46 17448 12487 14832 -1501 1082 680 O ATOM 5412 OE2 GLU D 46 46.821 -19.831 40.900 1.00108.20 O ANISOU 5412 OE2 GLU D 46 16012 11360 13737 -1634 806 339 O ATOM 5413 N PHE D 47 52.049 -19.626 42.394 1.00 86.45 N ANISOU 5413 N PHE D 47 14150 8417 10282 -473 320 862 N ATOM 5414 CA PHE D 47 52.893 -19.087 41.323 1.00 83.80 C ANISOU 5414 CA PHE D 47 13611 8315 9914 -426 59 727 C ATOM 5415 C PHE D 47 52.029 -18.384 40.286 1.00 86.30 C ANISOU 5415 C PHE D 47 13620 8832 10338 -655 -11 580 C ATOM 5416 O PHE D 47 51.030 -18.951 39.837 1.00 87.19 O ANISOU 5416 O PHE D 47 13652 8867 10609 -877 110 474 O ATOM 5417 CB PHE D 47 53.725 -20.203 40.670 1.00 86.46 C ANISOU 5417 CB PHE D 47 14072 8502 10275 -341 45 650 C ATOM 5418 CG PHE D 47 54.496 -19.797 39.434 1.00 86.13 C ANISOU 5418 CG PHE D 47 13820 8684 10221 -322 -172 497 C ATOM 5419 CD1 PHE D 47 55.741 -19.186 39.540 1.00 87.97 C ANISOU 5419 CD1 PHE D 47 14004 9117 10305 -106 -346 512 C ATOM 5420 CD2 PHE D 47 54.008 -20.084 38.162 1.00 88.28 C ANISOU 5420 CD2 PHE D 47 13946 8973 10623 -518 -186 318 C ATOM 5421 CE1 PHE D 47 56.465 -18.832 38.395 1.00 87.81 C ANISOU 5421 CE1 PHE D 47 13800 9287 10278 -105 -491 377 C ATOM 5422 CE2 PHE D 47 54.731 -19.728 37.018 1.00 89.91 C ANISOU 5422 CE2 PHE D 47 13997 9376 10789 -471 -357 195 C ATOM 5423 CZ PHE D 47 55.960 -19.114 37.143 1.00 86.78 C ANISOU 5423 CZ PHE D 47 13568 9149 10257 -272 -487 238 C ATOM 5424 N VAL D 48 52.407 -17.152 39.915 1.00 80.25 N ANISOU 5424 N VAL D 48 12691 8326 9475 -592 -192 558 N ATOM 5425 CA VAL D 48 51.677 -16.368 38.921 1.00 78.93 C ANISOU 5425 CA VAL D 48 12281 8367 9343 -714 -267 444 C ATOM 5426 C VAL D 48 52.416 -16.478 37.577 1.00 81.57 C ANISOU 5426 C VAL D 48 12531 8793 9669 -694 -405 304 C ATOM 5427 O VAL D 48 51.888 -17.062 36.628 1.00 82.53 O ANISOU 5427 O VAL D 48 12554 8922 9883 -811 -406 152 O ATOM 5428 CB VAL D 48 51.494 -14.895 39.369 1.00 81.61 C ANISOU 5428 CB VAL D 48 12566 8881 9562 -644 -319 529 C ATOM 5429 CG1 VAL D 48 50.743 -14.091 38.320 1.00 81.19 C ANISOU 5429 CG1 VAL D 48 12311 9037 9499 -692 -385 431 C ATOM 5430 CG2 VAL D 48 50.781 -14.814 40.707 1.00 82.19 C ANISOU 5430 CG2 VAL D 48 12734 8870 9623 -638 -175 665 C ATOM 5431 N ALA D 49 53.642 -15.926 37.510 1.00 75.69 N ANISOU 5431 N ALA D 49 11816 8132 8813 -554 -510 333 N ATOM 5432 CA ALA D 49 54.469 -15.926 36.309 1.00 74.43 C ANISOU 5432 CA ALA D 49 11585 8070 8626 -517 -608 221 C ATOM 5433 C ALA D 49 55.921 -15.632 36.641 1.00 76.66 C ANISOU 5433 C ALA D 49 11904 8407 8816 -377 -671 252 C ATOM 5434 O ALA D 49 56.215 -14.974 37.637 1.00 75.79 O ANISOU 5434 O ALA D 49 11830 8330 8636 -324 -679 335 O ATOM 5435 CB ALA D 49 53.952 -14.894 35.308 1.00 74.37 C ANISOU 5435 CB ALA D 49 11438 8252 8565 -556 -659 163 C ATOM 5436 N SER D 50 56.823 -16.106 35.787 1.00 73.04 N ANISOU 5436 N SER D 50 11414 7986 8353 -317 -718 157 N ATOM 5437 CA SER D 50 58.261 -15.873 35.878 1.00 72.69 C ANISOU 5437 CA SER D 50 11328 8058 8233 -195 -778 130 C ATOM 5438 C SER D 50 58.804 -15.420 34.524 1.00 74.78 C ANISOU 5438 C SER D 50 11473 8466 8475 -227 -793 26 C ATOM 5439 O SER D 50 58.086 -15.487 33.522 1.00 74.44 O ANISOU 5439 O SER D 50 11416 8416 8451 -294 -779 -21 O ATOM 5440 CB SER D 50 58.979 -17.134 36.353 1.00 78.45 C ANISOU 5440 CB SER D 50 12165 8686 8956 -13 -787 129 C ATOM 5441 OG SER D 50 60.385 -16.951 36.417 1.00 88.49 O ANISOU 5441 OG SER D 50 13336 10139 10148 133 -863 66 O ATOM 5442 N ILE D 51 60.059 -14.938 34.495 1.00 70.04 N ANISOU 5442 N ILE D 51 10776 8014 7823 -179 -812 -24 N ATOM 5443 CA ILE D 51 60.735 -14.535 33.264 1.00 69.43 C ANISOU 5443 CA ILE D 51 10600 8064 7718 -206 -775 -113 C ATOM 5444 C ILE D 51 62.249 -14.650 33.515 1.00 72.97 C ANISOU 5444 C ILE D 51 10913 8668 8143 -114 -799 -203 C ATOM 5445 O ILE D 51 62.687 -14.593 34.670 1.00 73.43 O ANISOU 5445 O ILE D 51 10939 8778 8183 -53 -859 -199 O ATOM 5446 CB ILE D 51 60.297 -13.117 32.776 1.00 71.64 C ANISOU 5446 CB ILE D 51 10882 8387 7951 -341 -692 -77 C ATOM 5447 CG1 ILE D 51 60.574 -12.938 31.260 1.00 72.06 C ANISOU 5447 CG1 ILE D 51 10919 8511 7950 -337 -619 -137 C ATOM 5448 CG2 ILE D 51 60.886 -11.984 33.647 1.00 72.33 C ANISOU 5448 CG2 ILE D 51 10927 8534 8019 -428 -653 -70 C ATOM 5449 CD1 ILE D 51 59.902 -11.766 30.626 1.00 76.52 C ANISOU 5449 CD1 ILE D 51 11572 9075 8426 -388 -524 -74 C ATOM 5450 N THR D 52 63.033 -14.869 32.444 1.00 68.38 N ANISOU 5450 N THR D 52 10241 8189 7549 -76 -759 -299 N ATOM 5451 CA THR D 52 64.486 -15.006 32.544 1.00 69.14 C ANISOU 5451 CA THR D 52 10152 8490 7629 20 -771 -418 C ATOM 5452 C THR D 52 65.121 -13.619 32.733 1.00 71.51 C ANISOU 5452 C THR D 52 10292 8947 7931 -171 -688 -481 C ATOM 5453 O THR D 52 64.450 -12.606 32.521 1.00 69.50 O ANISOU 5453 O THR D 52 10130 8601 7677 -349 -592 -413 O ATOM 5454 CB THR D 52 65.052 -15.730 31.309 1.00 80.05 C ANISOU 5454 CB THR D 52 11495 9926 8994 128 -727 -502 C ATOM 5455 OG1 THR D 52 64.625 -15.060 30.120 1.00 80.08 O ANISOU 5455 OG1 THR D 52 11544 9907 8976 -9 -608 -488 O ATOM 5456 CG2 THR D 52 64.624 -17.183 31.245 1.00 79.86 C ANISOU 5456 CG2 THR D 52 11639 9731 8973 316 -798 -483 C ATOM 5457 N TRP D 53 66.409 -13.579 33.162 1.00 69.27 N ANISOU 5457 N TRP D 53 9771 8905 7646 -126 -718 -631 N ATOM 5458 CA TRP D 53 67.173 -12.344 33.366 1.00 69.99 C ANISOU 5458 CA TRP D 53 9665 9162 7766 -352 -621 -761 C ATOM 5459 C TRP D 53 67.122 -11.499 32.119 1.00 73.92 C ANISOU 5459 C TRP D 53 10209 9593 8283 -563 -384 -746 C ATOM 5460 O TRP D 53 66.916 -10.287 32.206 1.00 74.18 O ANISOU 5460 O TRP D 53 10304 9547 8333 -797 -246 -733 O ATOM 5461 CB TRP D 53 68.638 -12.643 33.753 1.00 71.62 C ANISOU 5461 CB TRP D 53 9535 9707 7968 -250 -692 -983 C ATOM 5462 CG TRP D 53 69.509 -11.418 33.774 1.00 74.70 C ANISOU 5462 CG TRP D 53 9673 10287 8423 -548 -550 -1180 C ATOM 5463 CD1 TRP D 53 69.655 -10.535 34.802 1.00 78.51 C ANISOU 5463 CD1 TRP D 53 10067 10841 8921 -720 -586 -1292 C ATOM 5464 CD2 TRP D 53 70.295 -10.901 32.684 1.00 76.33 C ANISOU 5464 CD2 TRP D 53 9712 10598 8690 -747 -307 -1297 C ATOM 5465 NE1 TRP D 53 70.473 -9.494 34.420 1.00 80.22 N ANISOU 5465 NE1 TRP D 53 10071 11182 9227 -1049 -374 -1490 N ATOM 5466 CE2 TRP D 53 70.880 -9.695 33.125 1.00 82.20 C ANISOU 5466 CE2 TRP D 53 10273 11451 9509 -1074 -182 -1484 C ATOM 5467 CE3 TRP D 53 70.536 -11.326 31.365 1.00 77.82 C ANISOU 5467 CE3 TRP D 53 9913 10784 8871 -689 -160 -1266 C ATOM 5468 CZ2 TRP D 53 71.731 -8.936 32.311 1.00 83.84 C ANISOU 5468 CZ2 TRP D 53 10299 11753 9802 -1365 114 -1639 C ATOM 5469 CZ3 TRP D 53 71.372 -10.570 30.558 1.00 81.38 C ANISOU 5469 CZ3 TRP D 53 10192 11347 9382 -936 122 -1396 C ATOM 5470 CH2 TRP D 53 71.956 -9.390 31.030 1.00 84.03 C ANISOU 5470 CH2 TRP D 53 10344 11774 9810 -1283 273 -1576 C ATOM 5471 N SER D 54 67.281 -12.152 30.953 1.00 70.30 N ANISOU 5471 N SER D 54 9766 9143 7801 -454 -324 -738 N ATOM 5472 CA SER D 54 67.248 -11.542 29.626 1.00 70.57 C ANISOU 5472 CA SER D 54 9888 9122 7804 -570 -92 -706 C ATOM 5473 C SER D 54 65.882 -10.913 29.307 1.00 71.72 C ANISOU 5473 C SER D 54 10336 9026 7890 -624 -43 -528 C ATOM 5474 O SER D 54 65.816 -10.010 28.476 1.00 71.70 O ANISOU 5474 O SER D 54 10454 8957 7831 -732 177 -481 O ATOM 5475 CB SER D 54 67.577 -12.590 28.569 1.00 76.00 C ANISOU 5475 CB SER D 54 10559 9873 8446 -369 -93 -737 C ATOM 5476 OG SER D 54 66.693 -13.700 28.614 1.00 86.01 O ANISOU 5476 OG SER D 54 11990 11005 9687 -167 -279 -661 O ATOM 5477 N GLY D 55 64.826 -11.393 29.969 1.00 66.46 N ANISOU 5477 N GLY D 55 9790 8239 7222 -528 -228 -433 N ATOM 5478 CA GLY D 55 63.456 -10.936 29.762 1.00 64.98 C ANISOU 5478 CA GLY D 55 9831 7882 6975 -534 -222 -291 C ATOM 5479 C GLY D 55 62.840 -11.498 28.492 1.00 69.47 C ANISOU 5479 C GLY D 55 10512 8425 7459 -397 -227 -264 C ATOM 5480 O GLY D 55 61.872 -10.933 27.972 1.00 69.17 O ANISOU 5480 O GLY D 55 10638 8318 7326 -373 -187 -177 O ATOM 5481 N ILE D 56 63.399 -12.628 27.985 1.00 66.27 N ANISOU 5481 N ILE D 56 10022 8093 7066 -274 -287 -357 N ATOM 5482 CA ILE D 56 62.967 -13.272 26.744 1.00 66.29 C ANISOU 5482 CA ILE D 56 10117 8092 6979 -139 -303 -385 C ATOM 5483 C ILE D 56 61.936 -14.388 27.043 1.00 70.49 C ANISOU 5483 C ILE D 56 10703 8522 7559 -66 -495 -405 C ATOM 5484 O ILE D 56 60.874 -14.372 26.427 1.00 70.52 O ANISOU 5484 O ILE D 56 10801 8501 7493 -36 -538 -403 O ATOM 5485 CB ILE D 56 64.176 -13.850 25.916 1.00 70.26 C ANISOU 5485 CB ILE D 56 10521 8719 7456 -46 -223 -495 C ATOM 5486 CG1 ILE D 56 65.265 -12.777 25.645 1.00 70.66 C ANISOU 5486 CG1 ILE D 56 10480 8876 7491 -172 19 -504 C ATOM 5487 CG2 ILE D 56 63.690 -14.506 24.599 1.00 71.41 C ANISOU 5487 CG2 ILE D 56 10789 8860 7481 110 -248 -544 C ATOM 5488 CD1 ILE D 56 66.546 -13.270 24.926 1.00 71.01 C ANISOU 5488 CD1 ILE D 56 10371 9087 7524 -94 131 -624 C ATOM 5489 N ASP D 57 62.264 -15.374 27.924 1.00 66.68 N ANISOU 5489 N ASP D 57 10168 7987 7181 -24 -593 -440 N ATOM 5490 CA ASP D 57 61.389 -16.531 28.169 1.00 66.19 C ANISOU 5490 CA ASP D 57 10195 7773 7180 16 -707 -469 C ATOM 5491 C ASP D 57 60.459 -16.324 29.396 1.00 68.86 C ANISOU 5491 C ASP D 57 10571 7998 7592 -82 -753 -369 C ATOM 5492 O ASP D 57 60.885 -16.512 30.541 1.00 67.25 O ANISOU 5492 O ASP D 57 10360 7755 7439 -57 -773 -318 O ATOM 5493 CB ASP D 57 62.212 -17.813 28.370 1.00 68.90 C ANISOU 5493 CB ASP D 57 10547 8067 7565 165 -740 -542 C ATOM 5494 N PRO D 58 59.148 -16.052 29.152 1.00 66.08 N ANISOU 5494 N PRO D 58 10259 7614 7233 -161 -776 -357 N ATOM 5495 CA PRO D 58 58.214 -15.892 30.269 1.00 65.44 C ANISOU 5495 CA PRO D 58 10201 7441 7223 -249 -795 -269 C ATOM 5496 C PRO D 58 57.464 -17.191 30.581 1.00 71.79 C ANISOU 5496 C PRO D 58 11065 8073 8139 -288 -820 -330 C ATOM 5497 O PRO D 58 56.857 -17.795 29.686 1.00 72.25 O ANISOU 5497 O PRO D 58 11119 8124 8210 -318 -848 -467 O ATOM 5498 CB PRO D 58 57.255 -14.808 29.765 1.00 66.60 C ANISOU 5498 CB PRO D 58 10333 7688 7283 -286 -787 -239 C ATOM 5499 CG PRO D 58 57.381 -14.828 28.239 1.00 71.83 C ANISOU 5499 CG PRO D 58 10997 8466 7831 -199 -792 -342 C ATOM 5500 CD PRO D 58 58.466 -15.809 27.865 1.00 68.20 C ANISOU 5500 CD PRO D 58 10538 7973 7403 -140 -788 -431 C ATOM 5501 N THR D 59 57.509 -17.624 31.850 1.00 69.59 N ANISOU 5501 N THR D 59 10860 7649 7932 -289 -792 -241 N ATOM 5502 CA THR D 59 56.805 -18.826 32.314 1.00 71.22 C ANISOU 5502 CA THR D 59 11181 7627 8252 -349 -743 -268 C ATOM 5503 C THR D 59 55.496 -18.389 32.958 1.00 75.38 C ANISOU 5503 C THR D 59 11671 8133 8836 -499 -703 -211 C ATOM 5504 O THR D 59 55.494 -17.402 33.694 1.00 74.30 O ANISOU 5504 O THR D 59 11507 8077 8646 -482 -705 -83 O ATOM 5505 CB THR D 59 57.695 -19.624 33.268 1.00 83.68 C ANISOU 5505 CB THR D 59 12916 9049 9831 -194 -703 -187 C ATOM 5506 OG1 THR D 59 58.950 -19.878 32.631 1.00 87.44 O ANISOU 5506 OG1 THR D 59 13369 9617 10237 -25 -749 -253 O ATOM 5507 CG2 THR D 59 57.053 -20.933 33.714 1.00 84.31 C ANISOU 5507 CG2 THR D 59 13198 8819 10018 -244 -586 -197 C ATOM 5508 N TYR D 60 54.383 -19.088 32.664 1.00 73.11 N ANISOU 5508 N TYR D 60 11365 7755 8657 -655 -661 -331 N ATOM 5509 CA TYR D 60 53.076 -18.715 33.206 1.00 73.11 C ANISOU 5509 CA TYR D 60 11275 7781 8721 -805 -610 -310 C ATOM 5510 C TYR D 60 52.336 -19.880 33.830 1.00 79.24 C ANISOU 5510 C TYR D 60 12148 8295 9665 -975 -452 -352 C ATOM 5511 O TYR D 60 52.415 -21.001 33.329 1.00 80.78 O ANISOU 5511 O TYR D 60 12431 8318 9945 -1043 -404 -496 O ATOM 5512 CB TYR D 60 52.171 -18.129 32.109 1.00 74.45 C ANISOU 5512 CB TYR D 60 11231 8207 8849 -857 -708 -466 C ATOM 5513 CG TYR D 60 52.672 -16.859 31.466 1.00 74.86 C ANISOU 5513 CG TYR D 60 11235 8489 8719 -692 -807 -404 C ATOM 5514 CD1 TYR D 60 52.452 -15.619 32.062 1.00 75.60 C ANISOU 5514 CD1 TYR D 60 11314 8680 8730 -637 -794 -248 C ATOM 5515 CD2 TYR D 60 53.261 -16.880 30.206 1.00 76.00 C ANISOU 5515 CD2 TYR D 60 11372 8740 8763 -594 -883 -511 C ATOM 5516 CE1 TYR D 60 52.888 -14.438 31.460 1.00 75.18 C ANISOU 5516 CE1 TYR D 60 11274 8780 8512 -503 -830 -189 C ATOM 5517 CE2 TYR D 60 53.690 -15.704 29.587 1.00 76.05 C ANISOU 5517 CE2 TYR D 60 11380 8922 8595 -451 -913 -441 C ATOM 5518 CZ TYR D 60 53.503 -14.485 30.219 1.00 80.96 C ANISOU 5518 CZ TYR D 60 12016 9596 9149 -416 -875 -279 C ATOM 5519 OH TYR D 60 53.918 -13.328 29.608 1.00 80.58 O ANISOU 5519 OH TYR D 60 12025 9660 8932 -291 -852 -206 O ATOM 5520 N ALA D 61 51.536 -19.590 34.872 1.00 75.95 N ANISOU 5520 N ALA D 61 11722 7838 9297 -1061 -343 -240 N ATOM 5521 CA ALA D 61 50.644 -20.574 35.478 1.00 78.49 C ANISOU 5521 CA ALA D 61 12118 7914 9790 -1273 -132 -280 C ATOM 5522 C ALA D 61 49.425 -20.760 34.591 1.00 85.05 C ANISOU 5522 C ALA D 61 12682 8891 10743 -1518 -145 -554 C ATOM 5523 O ALA D 61 48.896 -19.761 34.101 1.00 84.32 O ANISOU 5523 O ALA D 61 12339 9129 10571 -1482 -289 -609 O ATOM 5524 CB ALA D 61 50.242 -20.131 36.872 1.00 78.95 C ANISOU 5524 CB ALA D 61 12249 7914 9834 -1259 2 -65 C ATOM 5525 N ASP D 62 48.992 -22.023 34.348 1.00 84.22 N ANISOU 5525 N ASP D 62 12633 8551 10815 -1752 2 -748 N ATOM 5526 CA ASP D 62 47.852 -22.366 33.474 1.00 86.31 C ANISOU 5526 CA ASP D 62 12611 8968 11215 -2026 -16 -1090 C ATOM 5527 C ASP D 62 46.608 -21.477 33.741 1.00 89.84 C ANISOU 5527 C ASP D 62 12721 9737 11678 -2117 -32 -1128 C ATOM 5528 O ASP D 62 45.920 -21.087 32.790 1.00 90.25 O ANISOU 5528 O ASP D 62 12448 10145 11695 -2144 -207 -1374 O ATOM 5529 CB ASP D 62 47.455 -23.847 33.651 1.00 91.90 C ANISOU 5529 CB ASP D 62 13479 9282 12157 -2339 253 -1260 C ATOM 5530 CG ASP D 62 48.467 -24.877 33.156 1.00101.88 C ANISOU 5530 CG ASP D 62 15058 10235 13417 -2263 275 -1310 C ATOM 5531 OD1 ASP D 62 49.422 -24.485 32.442 1.00 99.84 O ANISOU 5531 OD1 ASP D 62 14814 10137 12982 -1992 48 -1278 O ATOM 5532 OD2 ASP D 62 48.243 -26.086 33.387 1.00110.53 O ANISOU 5532 OD2 ASP D 62 16377 10931 14688 -2491 537 -1413 O ATOM 5533 N SER D 63 46.351 -21.148 35.023 1.00 85.54 N ANISOU 5533 N SER D 63 12261 9089 11152 -2115 142 -886 N ATOM 5534 CA SER D 63 45.215 -20.353 35.491 1.00 85.72 C ANISOU 5534 CA SER D 63 12007 9376 11187 -2173 177 -882 C ATOM 5535 C SER D 63 45.209 -18.919 34.927 1.00 88.45 C ANISOU 5535 C SER D 63 12155 10144 11309 -1892 -98 -843 C ATOM 5536 O SER D 63 44.141 -18.427 34.550 1.00 90.19 O ANISOU 5536 O SER D 63 12038 10708 11523 -1924 -169 -1014 O ATOM 5537 CB SER D 63 45.229 -20.277 37.016 1.00 88.09 C ANISOU 5537 CB SER D 63 12535 9436 11498 -2152 419 -582 C ATOM 5538 OG SER D 63 44.162 -19.493 37.525 1.00 96.63 O ANISOU 5538 OG SER D 63 13366 10769 12580 -2182 471 -563 O ATOM 5539 N VAL D 64 46.386 -18.251 34.889 1.00 81.24 N ANISOU 5539 N VAL D 64 11456 9204 10207 -1614 -229 -630 N ATOM 5540 CA VAL D 64 46.500 -16.841 34.492 1.00 77.96 C ANISOU 5540 CA VAL D 64 10958 9091 9573 -1349 -416 -543 C ATOM 5541 C VAL D 64 47.273 -16.655 33.139 1.00 79.57 C ANISOU 5541 C VAL D 64 11176 9420 9636 -1191 -618 -640 C ATOM 5542 O VAL D 64 47.383 -15.522 32.674 1.00 77.50 O ANISOU 5542 O VAL D 64 10890 9375 9181 -970 -738 -573 O ATOM 5543 CB VAL D 64 47.210 -16.032 35.614 1.00 79.19 C ANISOU 5543 CB VAL D 64 11347 9121 9620 -1183 -362 -229 C ATOM 5544 CG1 VAL D 64 46.413 -16.073 36.913 1.00 79.97 C ANISOU 5544 CG1 VAL D 64 11448 9133 9806 -1282 -164 -119 C ATOM 5545 CG2 VAL D 64 48.642 -16.512 35.844 1.00 77.59 C ANISOU 5545 CG2 VAL D 64 11422 8659 9398 -1116 -359 -111 C ATOM 5546 N ALA D 65 47.775 -17.749 32.515 1.00 76.92 N ANISOU 5546 N ALA D 65 10909 8933 9386 -1292 -628 -792 N ATOM 5547 CA ALA D 65 48.559 -17.731 31.263 1.00 76.29 C ANISOU 5547 CA ALA D 65 10866 8945 9175 -1146 -785 -886 C ATOM 5548 C ALA D 65 47.816 -17.025 30.104 1.00 81.83 C ANISOU 5548 C ALA D 65 11334 10041 9716 -1015 -963 -1064 C ATOM 5549 O ALA D 65 48.439 -16.320 29.299 1.00 79.91 O ANISOU 5549 O ALA D 65 11165 9929 9268 -782 -1069 -1009 O ATOM 5550 CB ALA D 65 48.889 -19.155 30.845 1.00 78.66 C ANISOU 5550 CB ALA D 65 11253 9021 9615 -1304 -741 -1072 C ATOM 5551 N ASP D 66 46.493 -17.219 30.043 1.00 81.72 N ANISOU 5551 N ASP D 66 11040 10228 9783 -1149 -979 -1279 N ATOM 5552 CA ASP D 66 45.588 -16.694 29.023 1.00 83.86 C ANISOU 5552 CA ASP D 66 11037 10933 9895 -1002 -1164 -1502 C ATOM 5553 C ASP D 66 45.314 -15.176 29.157 1.00 85.81 C ANISOU 5553 C ASP D 66 11279 11418 9908 -689 -1216 -1295 C ATOM 5554 O ASP D 66 45.043 -14.535 28.143 1.00 85.99 O ANISOU 5554 O ASP D 66 11224 11758 9690 -417 -1378 -1383 O ATOM 5555 CB ASP D 66 44.234 -17.438 29.099 1.00 89.98 C ANISOU 5555 CB ASP D 66 11458 11867 10864 -1282 -1143 -1832 C ATOM 5556 CG ASP D 66 43.514 -17.409 30.453 1.00105.68 C ANISOU 5556 CG ASP D 66 13361 13757 13037 -1476 -937 -1719 C ATOM 5557 OD1 ASP D 66 44.191 -17.578 31.497 1.00104.21 O ANISOU 5557 OD1 ASP D 66 13456 13194 12945 -1549 -752 -1443 O ATOM 5558 OD2 ASP D 66 42.266 -17.387 30.459 1.00117.59 O ANISOU 5558 OD2 ASP D 66 14506 15564 14607 -1577 -948 -1945 O ATOM 5559 N ARG D 67 45.341 -14.620 30.388 1.00 80.71 N ANISOU 5559 N ARG D 67 10737 10617 9310 -702 -1072 -1032 N ATOM 5560 CA ARG D 67 45.001 -13.211 30.663 1.00 79.65 C ANISOU 5560 CA ARG D 67 10631 10656 8975 -428 -1083 -842 C ATOM 5561 C ARG D 67 46.218 -12.337 30.998 1.00 81.44 C ANISOU 5561 C ARG D 67 11210 10652 9079 -279 -1016 -534 C ATOM 5562 O ARG D 67 46.316 -11.198 30.533 1.00 80.44 O ANISOU 5562 O ARG D 67 11199 10648 8716 -1 -1052 -426 O ATOM 5563 CB ARG D 67 44.037 -13.144 31.853 1.00 79.42 C ANISOU 5563 CB ARG D 67 10449 10645 9082 -553 -955 -801 C ATOM 5564 CG ARG D 67 42.724 -13.888 31.665 1.00 90.82 C ANISOU 5564 CG ARG D 67 11486 12349 10673 -743 -975 -1126 C ATOM 5565 CD ARG D 67 41.997 -13.998 32.985 1.00 98.91 C ANISOU 5565 CD ARG D 67 12411 13294 11875 -931 -770 -1051 C ATOM 5566 NE ARG D 67 42.755 -14.814 33.935 1.00101.69 N ANISOU 5566 NE ARG D 67 13028 13184 12425 -1186 -570 -893 N ATOM 5567 CZ ARG D 67 42.410 -15.003 35.201 1.00110.94 C ANISOU 5567 CZ ARG D 67 14240 14178 13733 -1339 -346 -761 C ATOM 5568 NH1 ARG D 67 41.332 -14.408 35.700 1.00 99.21 N ANISOU 5568 NH1 ARG D 67 12529 12938 12230 -1288 -284 -767 N ATOM 5569 NH2 ARG D 67 43.154 -15.767 35.989 1.00 91.93 N ANISOU 5569 NH2 ARG D 67 12117 11359 11453 -1500 -175 -613 N ATOM 5570 N PHE D 68 47.090 -12.861 31.852 1.00 77.51 N ANISOU 5570 N PHE D 68 10883 9830 8739 -462 -903 -407 N ATOM 5571 CA PHE D 68 48.266 -12.129 32.302 1.00 75.76 C ANISOU 5571 CA PHE D 68 10934 9414 8436 -376 -841 -173 C ATOM 5572 C PHE D 68 49.444 -12.211 31.344 1.00 78.22 C ANISOU 5572 C PHE D 68 11377 9675 8668 -314 -888 -189 C ATOM 5573 O PHE D 68 49.614 -13.190 30.618 1.00 78.72 O ANISOU 5573 O PHE D 68 11375 9742 8793 -384 -948 -355 O ATOM 5574 CB PHE D 68 48.692 -12.613 33.691 1.00 77.17 C ANISOU 5574 CB PHE D 68 11218 9327 8774 -541 -721 -46 C ATOM 5575 CG PHE D 68 47.660 -12.382 34.757 1.00 80.05 C ANISOU 5575 CG PHE D 68 11507 9717 9192 -582 -630 17 C ATOM 5576 CD1 PHE D 68 46.309 -12.453 34.458 1.00 86.27 C ANISOU 5576 CD1 PHE D 68 12035 10739 10003 -598 -649 -132 C ATOM 5577 CD2 PHE D 68 48.039 -12.093 36.057 1.00 81.40 C ANISOU 5577 CD2 PHE D 68 11844 9709 9376 -592 -526 202 C ATOM 5578 CE1 PHE D 68 45.356 -12.240 35.437 1.00 88.40 C ANISOU 5578 CE1 PHE D 68 12210 11054 10324 -634 -539 -80 C ATOM 5579 CE2 PHE D 68 47.092 -11.880 37.040 1.00 85.48 C ANISOU 5579 CE2 PHE D 68 12307 10248 9923 -613 -421 267 C ATOM 5580 CZ PHE D 68 45.748 -11.953 36.730 1.00 86.02 C ANISOU 5580 CZ PHE D 68 12113 10541 10031 -639 -414 134 C ATOM 5581 N THR D 69 50.255 -11.160 31.358 1.00 73.17 N ANISOU 5581 N THR D 69 10927 8980 7894 -193 -836 -27 N ATOM 5582 CA THR D 69 51.450 -11.077 30.512 1.00 72.34 C ANISOU 5582 CA THR D 69 10946 8830 7711 -143 -827 -24 C ATOM 5583 C THR D 69 52.576 -10.439 31.340 1.00 74.04 C ANISOU 5583 C THR D 69 11321 8868 7942 -198 -719 130 C ATOM 5584 O THR D 69 52.354 -9.397 31.957 1.00 73.47 O ANISOU 5584 O THR D 69 11344 8768 7804 -155 -649 249 O ATOM 5585 CB THR D 69 51.153 -10.298 29.213 1.00 79.47 C ANISOU 5585 CB THR D 69 11900 9922 8373 92 -855 -48 C ATOM 5586 OG1 THR D 69 49.916 -10.743 28.653 1.00 81.60 O ANISOU 5586 OG1 THR D 69 11971 10427 8607 166 -987 -221 O ATOM 5587 CG2 THR D 69 52.281 -10.419 28.182 1.00 75.80 C ANISOU 5587 CG2 THR D 69 11544 9428 7828 137 -825 -73 C ATOM 5588 N THR D 70 53.763 -11.069 31.390 1.00 68.97 N ANISOU 5588 N THR D 70 10696 8124 7384 -284 -709 104 N ATOM 5589 CA THR D 70 54.863 -10.505 32.174 1.00 67.52 C ANISOU 5589 CA THR D 70 10599 7838 7218 -343 -631 189 C ATOM 5590 C THR D 70 55.997 -10.075 31.230 1.00 70.77 C ANISOU 5590 C THR D 70 11064 8274 7551 -323 -556 164 C ATOM 5591 O THR D 70 56.160 -10.638 30.143 1.00 70.41 O ANISOU 5591 O THR D 70 10987 8293 7471 -265 -584 82 O ATOM 5592 CB THR D 70 55.369 -11.491 33.262 1.00 73.48 C ANISOU 5592 CB THR D 70 11313 8493 8115 -423 -669 180 C ATOM 5593 OG1 THR D 70 56.312 -10.825 34.100 1.00 70.78 O ANISOU 5593 OG1 THR D 70 11017 8117 7760 -457 -627 227 O ATOM 5594 CG2 THR D 70 55.981 -12.778 32.694 1.00 72.43 C ANISOU 5594 CG2 THR D 70 11129 8341 8050 -416 -719 74 C ATOM 5595 N SER D 71 56.749 -9.041 31.643 1.00 67.20 N ANISOU 5595 N SER D 71 10697 7767 7070 -386 -440 221 N ATOM 5596 CA SER D 71 57.893 -8.530 30.890 1.00 67.83 C ANISOU 5596 CA SER D 71 10819 7852 7101 -425 -306 191 C ATOM 5597 C SER D 71 58.959 -7.998 31.842 1.00 71.14 C ANISOU 5597 C SER D 71 11207 8227 7595 -585 -234 161 C ATOM 5598 O SER D 71 58.665 -7.698 33.003 1.00 69.85 O ANISOU 5598 O SER D 71 11060 8015 7466 -629 -274 192 O ATOM 5599 CB SER D 71 57.477 -7.443 29.900 1.00 72.53 C ANISOU 5599 CB SER D 71 11609 8431 7516 -323 -158 269 C ATOM 5600 OG SER D 71 57.058 -6.244 30.536 1.00 81.77 O ANISOU 5600 OG SER D 71 12944 9497 8630 -336 -53 368 O ATOM 5601 N ARG D 72 60.195 -7.880 31.349 1.00 68.88 N ANISOU 5601 N ARG D 72 10858 7985 7329 -672 -126 76 N ATOM 5602 CA ARG D 72 61.272 -7.368 32.166 1.00 69.56 C ANISOU 5602 CA ARG D 72 10852 8086 7489 -846 -64 -17 C ATOM 5603 C ARG D 72 62.061 -6.314 31.382 1.00 75.55 C ANISOU 5603 C ARG D 72 11687 8803 8216 -995 209 -53 C ATOM 5604 O ARG D 72 62.494 -6.548 30.248 1.00 75.33 O ANISOU 5604 O ARG D 72 11649 8821 8149 -959 312 -68 O ATOM 5605 CB ARG D 72 62.189 -8.503 32.658 1.00 70.31 C ANISOU 5605 CB ARG D 72 10705 8331 7679 -821 -218 -143 C ATOM 5606 CG ARG D 72 63.153 -8.036 33.732 1.00 84.06 C ANISOU 5606 CG ARG D 72 12304 10158 9477 -959 -224 -276 C ATOM 5607 CD ARG D 72 64.092 -9.108 34.237 1.00 93.30 C ANISOU 5607 CD ARG D 72 13235 11521 10692 -856 -389 -405 C ATOM 5608 NE ARG D 72 64.968 -8.559 35.277 1.00101.73 N ANISOU 5608 NE ARG D 72 14138 12729 11785 -970 -421 -572 N ATOM 5609 CZ ARG D 72 66.139 -7.975 35.035 1.00115.54 C ANISOU 5609 CZ ARG D 72 15683 14631 13585 -1157 -300 -770 C ATOM 5610 NH1 ARG D 72 66.605 -7.883 33.799 1.00102.72 N ANISOU 5610 NH1 ARG D 72 14020 13021 11988 -1236 -114 -792 N ATOM 5611 NH2 ARG D 72 66.859 -7.492 36.038 1.00102.61 N ANISOU 5611 NH2 ARG D 72 13868 13151 11969 -1271 -358 -968 N ATOM 5612 N ASP D 73 62.195 -5.131 31.994 1.00 74.19 N ANISOU 5612 N ASP D 73 11623 8516 8050 -1166 355 -66 N ATOM 5613 CA ASP D 73 62.970 -4.014 31.474 1.00 76.47 C ANISOU 5613 CA ASP D 73 12018 8704 8335 -1378 674 -119 C ATOM 5614 C ASP D 73 64.367 -4.144 32.037 1.00 82.28 C ANISOU 5614 C ASP D 73 12440 9605 9219 -1609 675 -360 C ATOM 5615 O ASP D 73 64.636 -3.706 33.155 1.00 82.34 O ANISOU 5615 O ASP D 73 12370 9624 9291 -1759 626 -482 O ATOM 5616 CB ASP D 73 62.303 -2.664 31.813 1.00 78.67 C ANISOU 5616 CB ASP D 73 12622 8733 8536 -1437 854 -21 C ATOM 5617 CG ASP D 73 62.941 -1.424 31.199 1.00 91.72 C ANISOU 5617 CG ASP D 73 14497 10184 10168 -1657 1261 -42 C ATOM 5618 OD1 ASP D 73 63.993 -1.559 30.520 1.00 94.01 O ANISOU 5618 OD1 ASP D 73 14648 10551 10523 -1807 1426 -151 O ATOM 5619 OD2 ASP D 73 62.370 -0.324 31.366 1.00 98.35 O ANISOU 5619 OD2 ASP D 73 15674 10774 10920 -1667 1443 56 O ATOM 5620 N VAL D 74 65.228 -4.843 31.283 1.00 79.93 N ANISOU 5620 N VAL D 74 11933 9476 8960 -1597 699 -448 N ATOM 5621 CA VAL D 74 66.620 -5.140 31.624 1.00 81.37 C ANISOU 5621 CA VAL D 74 11746 9903 9268 -1756 686 -701 C ATOM 5622 C VAL D 74 67.386 -3.834 31.946 1.00 87.10 C ANISOU 5622 C VAL D 74 12447 10564 10081 -2135 963 -879 C ATOM 5623 O VAL D 74 68.174 -3.820 32.891 1.00 88.66 O ANISOU 5623 O VAL D 74 12350 10961 10377 -2283 855 -1123 O ATOM 5624 CB VAL D 74 67.333 -5.941 30.492 1.00 86.32 C ANISOU 5624 CB VAL D 74 12212 10690 9894 -1662 747 -739 C ATOM 5625 CG1 VAL D 74 66.816 -7.373 30.430 1.00 83.92 C ANISOU 5625 CG1 VAL D 74 11869 10476 9541 -1330 444 -654 C ATOM 5626 CG2 VAL D 74 67.202 -5.260 29.124 1.00 87.40 C ANISOU 5626 CG2 VAL D 74 12618 10647 9942 -1709 1093 -613 C ATOM 5627 N ALA D 75 67.108 -2.743 31.199 1.00 83.54 N ANISOU 5627 N ALA D 75 12332 9832 9580 -2276 1319 -766 N ATOM 5628 CA ALA D 75 67.750 -1.439 31.358 1.00 86.25 C ANISOU 5628 CA ALA D 75 12745 10019 10009 -2671 1670 -921 C ATOM 5629 C ALA D 75 67.430 -0.811 32.723 1.00 88.32 C ANISOU 5629 C ALA D 75 13052 10201 10305 -2795 1547 -1017 C ATOM 5630 O ALA D 75 68.349 -0.430 33.447 1.00 89.48 O ANISOU 5630 O ALA D 75 12936 10476 10585 -3100 1576 -1320 O ATOM 5631 CB ALA D 75 67.300 -0.506 30.243 1.00 88.40 C ANISOU 5631 CB ALA D 75 13486 9939 10162 -2690 2082 -705 C ATOM 5632 N ASN D 76 66.140 -0.736 33.076 1.00 82.41 N ANISOU 5632 N ASN D 76 12604 9276 9430 -2550 1401 -786 N ATOM 5633 CA ASN D 76 65.652 -0.120 34.306 1.00 82.17 C ANISOU 5633 CA ASN D 76 12691 9137 9392 -2607 1303 -829 C ATOM 5634 C ASN D 76 65.470 -1.154 35.441 1.00 84.44 C ANISOU 5634 C ASN D 76 12705 9696 9683 -2401 859 -883 C ATOM 5635 O ASN D 76 64.923 -0.801 36.489 1.00 84.01 O ANISOU 5635 O ASN D 76 12759 9573 9587 -2373 740 -883 O ATOM 5636 CB ASN D 76 64.312 0.592 34.036 1.00 82.28 C ANISOU 5636 CB ASN D 76 13200 8817 9245 -2419 1428 -538 C ATOM 5637 CG ASN D 76 64.333 1.709 33.003 1.00113.89 C ANISOU 5637 CG ASN D 76 17600 12491 13184 -2538 1890 -435 C ATOM 5638 OD1 ASN D 76 65.402 2.119 32.546 1.00111.94 O ANISOU 5638 OD1 ASN D 76 17759 12008 12764 -2303 1994 -185 O ATOM 5639 ND2 ASN D 76 63.174 2.242 32.610 1.00108.91 N ANISOU 5639 ND2 ASN D 76 16873 11836 12672 -2882 2201 -619 N ATOM 5640 N ASN D 77 65.921 -2.387 35.232 1.00 80.25 N ANISOU 5640 N ASN D 77 11868 9444 9180 -2241 648 -918 N ATOM 5641 CA ASN D 77 65.778 -3.423 36.248 1.00 78.87 C ANISOU 5641 CA ASN D 77 11498 9487 8982 -2008 275 -940 C ATOM 5642 C ASN D 77 64.369 -3.373 36.827 1.00 80.98 C ANISOU 5642 C ASN D 77 12055 9567 9148 -1809 163 -710 C ATOM 5643 O ASN D 77 64.184 -3.243 38.037 1.00 80.88 O ANISOU 5643 O ASN D 77 12040 9586 9105 -1784 14 -768 O ATOM 5644 CB ASN D 77 66.814 -3.235 37.358 1.00 83.03 C ANISOU 5644 CB ASN D 77 11722 10258 9568 -2170 156 -1266 C ATOM 5645 CG ASN D 77 67.039 -4.499 38.164 1.00108.46 C ANISOU 5645 CG ASN D 77 14700 13772 12739 -1871 -202 -1310 C ATOM 5646 OD1 ASN D 77 66.481 -5.553 37.858 1.00102.83 O ANISOU 5646 OD1 ASN D 77 14050 13045 11976 -1586 -328 -1103 O ATOM 5647 ND2 ASN D 77 67.862 -4.400 39.201 1.00101.88 N ANISOU 5647 ND2 ASN D 77 13604 13203 11903 -1924 -359 -1595 N ATOM 5648 N THR D 78 63.380 -3.479 35.947 1.00 75.64 N ANISOU 5648 N THR D 78 11609 8726 8405 -1654 236 -465 N ATOM 5649 CA THR D 78 61.968 -3.430 36.340 1.00 73.56 C ANISOU 5649 CA THR D 78 11582 8319 8048 -1461 156 -255 C ATOM 5650 C THR D 78 61.224 -4.647 35.795 1.00 75.58 C ANISOU 5650 C THR D 78 11800 8639 8280 -1209 1 -102 C ATOM 5651 O THR D 78 61.387 -4.998 34.633 1.00 75.14 O ANISOU 5651 O THR D 78 11723 8608 8220 -1171 67 -75 O ATOM 5652 CB THR D 78 61.313 -2.120 35.841 1.00 81.71 C ANISOU 5652 CB THR D 78 12963 9085 8996 -1511 421 -135 C ATOM 5653 OG1 THR D 78 62.112 -1.002 36.229 1.00 81.62 O ANISOU 5653 OG1 THR D 78 13011 8969 9034 -1802 620 -310 O ATOM 5654 CG2 THR D 78 59.876 -1.938 36.350 1.00 79.03 C ANISOU 5654 CG2 THR D 78 12834 8641 8552 -1298 344 51 C ATOM 5655 N LEU D 79 60.396 -5.276 36.640 1.00 71.22 N ANISOU 5655 N LEU D 79 11251 8102 7707 -1050 -183 -16 N ATOM 5656 CA LEU D 79 59.552 -6.413 36.273 1.00 69.44 C ANISOU 5656 CA LEU D 79 11001 7902 7480 -861 -306 101 C ATOM 5657 C LEU D 79 58.108 -5.942 36.163 1.00 72.94 C ANISOU 5657 C LEU D 79 11629 8238 7846 -761 -263 258 C ATOM 5658 O LEU D 79 57.661 -5.149 36.998 1.00 73.11 O ANISOU 5658 O LEU D 79 11776 8181 7822 -771 -226 298 O ATOM 5659 CB LEU D 79 59.704 -7.539 37.309 1.00 68.94 C ANISOU 5659 CB LEU D 79 10815 7924 7456 -764 -495 75 C ATOM 5660 CG LEU D 79 58.894 -8.818 37.099 1.00 72.74 C ANISOU 5660 CG LEU D 79 11289 8385 7964 -618 -586 168 C ATOM 5661 CD1 LEU D 79 59.284 -9.522 35.823 1.00 73.19 C ANISOU 5661 CD1 LEU D 79 11264 8491 8056 -596 -581 120 C ATOM 5662 CD2 LEU D 79 59.067 -9.757 38.261 1.00 74.63 C ANISOU 5662 CD2 LEU D 79 11500 8644 8211 -510 -707 171 C ATOM 5663 N TYR D 80 57.388 -6.390 35.125 1.00 68.39 N ANISOU 5663 N TYR D 80 11061 7684 7241 -647 -272 323 N ATOM 5664 CA TYR D 80 56.002 -5.974 34.910 1.00 67.76 C ANISOU 5664 CA TYR D 80 11099 7577 7069 -512 -251 438 C ATOM 5665 C TYR D 80 55.058 -7.174 34.885 1.00 69.08 C ANISOU 5665 C TYR D 80 11130 7829 7290 -423 -393 447 C ATOM 5666 O TYR D 80 55.477 -8.280 34.540 1.00 68.24 O ANISOU 5666 O TYR D 80 10898 7766 7265 -446 -472 376 O ATOM 5667 CB TYR D 80 55.858 -5.182 33.595 1.00 70.56 C ANISOU 5667 CB TYR D 80 11606 7912 7290 -427 -113 481 C ATOM 5668 CG TYR D 80 56.719 -3.938 33.488 1.00 74.45 C ANISOU 5668 CG TYR D 80 12290 8262 7735 -546 107 477 C ATOM 5669 CD1 TYR D 80 56.292 -2.722 34.019 1.00 77.25 C ANISOU 5669 CD1 TYR D 80 12880 8468 8003 -530 240 549 C ATOM 5670 CD2 TYR D 80 57.903 -3.948 32.756 1.00 76.34 C ANISOU 5670 CD2 TYR D 80 12497 8501 8009 -673 220 396 C ATOM 5671 CE1 TYR D 80 57.061 -1.566 33.890 1.00 79.86 C ANISOU 5671 CE1 TYR D 80 13425 8615 8302 -677 489 527 C ATOM 5672 CE2 TYR D 80 58.677 -2.796 32.613 1.00 79.21 C ANISOU 5672 CE2 TYR D 80 13035 8711 8349 -834 478 372 C ATOM 5673 CZ TYR D 80 58.248 -1.604 33.176 1.00 88.09 C ANISOU 5673 CZ TYR D 80 14416 9651 9402 -849 619 434 C ATOM 5674 OH TYR D 80 59.007 -0.465 33.032 1.00 91.36 O ANISOU 5674 OH TYR D 80 15040 9865 9809 -1048 916 391 O ATOM 5675 N LEU D 81 53.781 -6.950 35.246 1.00 64.70 N ANISOU 5675 N LEU D 81 10598 7292 6693 -329 -403 518 N ATOM 5676 CA LEU D 81 52.749 -7.986 35.235 1.00 64.19 C ANISOU 5676 CA LEU D 81 10382 7312 6697 -294 -495 496 C ATOM 5677 C LEU D 81 51.427 -7.384 34.793 1.00 68.72 C ANISOU 5677 C LEU D 81 10952 8001 7158 -139 -484 528 C ATOM 5678 O LEU D 81 50.678 -6.834 35.611 1.00 68.64 O ANISOU 5678 O LEU D 81 10980 7987 7113 -83 -444 600 O ATOM 5679 CB LEU D 81 52.599 -8.681 36.610 1.00 63.69 C ANISOU 5679 CB LEU D 81 10280 7178 6741 -366 -515 524 C ATOM 5680 CG LEU D 81 51.621 -9.877 36.684 1.00 68.26 C ANISOU 5680 CG LEU D 81 10719 7786 7432 -399 -545 487 C ATOM 5681 CD1 LEU D 81 52.060 -11.028 35.764 1.00 68.48 C ANISOU 5681 CD1 LEU D 81 10661 7816 7544 -454 -606 370 C ATOM 5682 CD2 LEU D 81 51.492 -10.379 38.096 1.00 69.77 C ANISOU 5682 CD2 LEU D 81 10954 7867 7690 -442 -499 558 C ATOM 5683 N GLN D 82 51.149 -7.481 33.486 1.00 65.86 N ANISOU 5683 N GLN D 82 10543 7768 6714 -32 -527 463 N ATOM 5684 CA GLN D 82 49.915 -6.984 32.890 1.00 66.78 C ANISOU 5684 CA GLN D 82 10623 8070 6683 183 -554 459 C ATOM 5685 C GLN D 82 48.801 -7.964 33.207 1.00 70.89 C ANISOU 5685 C GLN D 82 10871 8736 7328 124 -647 351 C ATOM 5686 O GLN D 82 48.855 -9.119 32.782 1.00 70.47 O ANISOU 5686 O GLN D 82 10662 8718 7396 1 -724 213 O ATOM 5687 CB GLN D 82 50.072 -6.763 31.365 1.00 68.78 C ANISOU 5687 CB GLN D 82 10935 8436 6763 357 -577 412 C ATOM 5688 CG GLN D 82 48.877 -6.067 30.708 1.00 68.79 C ANISOU 5688 CG GLN D 82 10939 8663 6535 677 -613 415 C ATOM 5689 CD GLN D 82 48.687 -4.660 31.212 1.00 78.51 C ANISOU 5689 CD GLN D 82 12433 9785 7610 845 -467 589 C ATOM 5690 OE1 GLN D 82 49.640 -3.899 31.359 1.00 73.72 O ANISOU 5690 OE1 GLN D 82 12102 8936 6972 784 -305 699 O ATOM 5691 NE2 GLN D 82 47.443 -4.255 31.407 1.00 69.01 N ANISOU 5691 NE2 GLN D 82 11155 8771 6296 1073 -508 596 N ATOM 5692 N MET D 83 47.822 -7.519 33.997 1.00 67.69 N ANISOU 5692 N MET D 83 10420 8395 6906 191 -611 404 N ATOM 5693 CA MET D 83 46.706 -8.363 34.401 1.00 68.38 C ANISOU 5693 CA MET D 83 10232 8622 7128 99 -643 296 C ATOM 5694 C MET D 83 45.405 -7.855 33.782 1.00 73.13 C ANISOU 5694 C MET D 83 10656 9551 7579 340 -708 212 C ATOM 5695 O MET D 83 44.847 -6.865 34.259 1.00 72.74 O ANISOU 5695 O MET D 83 10680 9556 7401 533 -648 321 O ATOM 5696 CB MET D 83 46.590 -8.410 35.927 1.00 69.97 C ANISOU 5696 CB MET D 83 10479 8666 7440 -21 -530 409 C ATOM 5697 CG MET D 83 47.865 -8.757 36.634 1.00 71.81 C ANISOU 5697 CG MET D 83 10897 8629 7760 -174 -488 492 C ATOM 5698 SD MET D 83 47.582 -8.993 38.401 1.00 76.08 S ANISOU 5698 SD MET D 83 11491 9025 8389 -264 -365 606 S ATOM 5699 CE MET D 83 46.951 -7.400 38.868 1.00 73.06 C ANISOU 5699 CE MET D 83 11225 8718 7817 -45 -306 719 C ATOM 5700 N ASN D 84 44.937 -8.515 32.708 1.00 70.13 N ANISOU 5700 N ASN D 84 10044 9408 7194 360 -840 1 N ATOM 5701 CA ASN D 84 43.703 -8.135 32.019 1.00 72.02 C ANISOU 5701 CA ASN D 84 10055 10044 7267 625 -947 -137 C ATOM 5702 C ASN D 84 42.604 -9.162 32.288 1.00 76.78 C ANISOU 5702 C ASN D 84 10235 10859 8078 409 -982 -378 C ATOM 5703 O ASN D 84 42.902 -10.268 32.747 1.00 75.75 O ANISOU 5703 O ASN D 84 10048 10526 8208 56 -917 -441 O ATOM 5704 CB ASN D 84 43.943 -7.987 30.509 1.00 73.41 C ANISOU 5704 CB ASN D 84 10275 10393 7223 861 -1085 -235 C ATOM 5705 CG ASN D 84 44.916 -6.895 30.126 1.00 92.19 C ANISOU 5705 CG ASN D 84 13077 12572 9379 1080 -997 -6 C ATOM 5706 OD1 ASN D 84 45.509 -6.218 30.972 1.00 84.63 O ANISOU 5706 OD1 ASN D 84 12379 11334 8444 1027 -843 205 O ATOM 5707 ND2 ASN D 84 45.102 -6.699 28.832 1.00 85.72 N ANISOU 5707 ND2 ASN D 84 12345 11892 8334 1323 -1076 -59 N ATOM 5708 N SER D 85 41.325 -8.780 32.016 1.00 75.11 N ANISOU 5708 N SER D 85 9732 11062 7746 631 -1063 -521 N ATOM 5709 CA SER D 85 40.116 -9.596 32.221 1.00 77.21 C ANISOU 5709 CA SER D 85 9523 11614 8199 432 -1079 -800 C ATOM 5710 C SER D 85 40.130 -10.211 33.631 1.00 79.94 C ANISOU 5710 C SER D 85 9880 11655 8840 57 -851 -700 C ATOM 5711 O SER D 85 39.896 -11.413 33.793 1.00 80.80 O ANISOU 5711 O SER D 85 9784 11702 9215 -316 -784 -889 O ATOM 5712 CB SER D 85 40.008 -10.680 31.151 1.00 82.08 C ANISOU 5712 CB SER D 85 9881 12403 8904 260 -1234 -1141 C ATOM 5713 OG SER D 85 39.988 -10.118 29.849 1.00 91.70 O ANISOU 5713 OG SER D 85 11111 13923 9807 652 -1446 -1230 O ATOM 5714 N LEU D 86 40.447 -9.368 34.647 1.00 74.22 N ANISOU 5714 N LEU D 86 9441 10712 8047 169 -713 -401 N ATOM 5715 CA LEU D 86 40.592 -9.761 36.049 1.00 72.65 C ANISOU 5715 CA LEU D 86 9349 10210 8047 -90 -496 -251 C ATOM 5716 C LEU D 86 39.257 -10.217 36.633 1.00 80.73 C ANISOU 5716 C LEU D 86 9984 11461 9230 -246 -371 -407 C ATOM 5717 O LEU D 86 38.268 -9.482 36.604 1.00 81.99 O ANISOU 5717 O LEU D 86 9921 11975 9257 0 -400 -459 O ATOM 5718 CB LEU D 86 41.176 -8.606 36.894 1.00 70.03 C ANISOU 5718 CB LEU D 86 9397 9659 7552 119 -413 58 C ATOM 5719 CG LEU D 86 42.687 -8.336 36.728 1.00 70.60 C ANISOU 5719 CG LEU D 86 9862 9406 7555 129 -448 218 C ATOM 5720 CD1 LEU D 86 43.070 -6.958 37.218 1.00 69.21 C ANISOU 5720 CD1 LEU D 86 10008 9113 7175 374 -395 436 C ATOM 5721 CD2 LEU D 86 43.520 -9.409 37.405 1.00 69.43 C ANISOU 5721 CD2 LEU D 86 9826 8936 7620 -184 -363 257 C ATOM 5722 N LYS D 87 39.250 -11.466 37.133 1.00 79.39 N ANISOU 5722 N LYS D 87 9742 11079 9343 -652 -211 -488 N ATOM 5723 CA LYS D 87 38.111 -12.125 37.757 1.00 82.83 C ANISOU 5723 CA LYS D 87 9838 11637 9995 -918 -9 -644 C ATOM 5724 C LYS D 87 38.270 -12.122 39.279 1.00 87.48 C ANISOU 5724 C LYS D 87 10690 11898 10649 -1004 269 -366 C ATOM 5725 O LYS D 87 39.354 -11.849 39.803 1.00 83.53 O ANISOU 5725 O LYS D 87 10617 11063 10058 -912 277 -102 O ATOM 5726 CB LYS D 87 37.964 -13.561 37.223 1.00 87.28 C ANISOU 5726 CB LYS D 87 10191 12142 10829 -1333 32 -943 C ATOM 5727 N HIS D 88 37.163 -12.403 39.972 1.00 89.11 N ANISOU 5727 N HIS D 88 10619 12242 10998 -1169 496 -448 N ATOM 5728 CA HIS D 88 37.000 -12.442 41.425 1.00 90.07 C ANISOU 5728 CA HIS D 88 10921 12130 11173 -1243 804 -222 C ATOM 5729 C HIS D 88 37.807 -13.609 42.068 1.00 93.82 C ANISOU 5729 C HIS D 88 11741 12085 11819 -1545 1017 -98 C ATOM 5730 O HIS D 88 37.691 -13.832 43.275 1.00 94.03 O ANISOU 5730 O HIS D 88 11955 11886 11887 -1619 1304 87 O ATOM 5731 CB HIS D 88 35.496 -12.571 41.769 1.00 95.72 C ANISOU 5731 CB HIS D 88 11160 13187 12022 -1381 1012 -412 C ATOM 5732 CG HIS D 88 34.687 -13.294 40.723 1.00103.20 C ANISOU 5732 CG HIS D 88 11582 14472 13158 -1639 941 -840 C ATOM 5733 ND1 HIS D 88 34.520 -14.671 40.753 1.00107.80 N ANISOU 5733 ND1 HIS D 88 12062 14839 14056 -2142 1170 -1033 N ATOM 5734 CD2 HIS D 88 34.044 -12.801 39.636 1.00106.79 C ANISOU 5734 CD2 HIS D 88 11617 15456 13503 -1438 663 -1117 C ATOM 5735 CE1 HIS D 88 33.785 -14.966 39.691 1.00110.36 C ANISOU 5735 CE1 HIS D 88 11879 15579 14474 -2271 1013 -1450 C ATOM 5736 NE2 HIS D 88 33.478 -13.875 38.987 1.00110.24 N ANISOU 5736 NE2 HIS D 88 11646 16046 14196 -1836 690 -1516 N ATOM 5737 N GLU D 89 38.645 -14.310 41.274 1.00 89.99 N ANISOU 5737 N GLU D 89 11378 11416 11399 -1664 881 -184 N ATOM 5738 CA GLU D 89 39.546 -15.370 41.751 1.00 89.66 C ANISOU 5738 CA GLU D 89 11711 10887 11468 -1855 1041 -60 C ATOM 5739 C GLU D 89 40.984 -14.844 41.812 1.00 90.74 C ANISOU 5739 C GLU D 89 12256 10829 11394 -1573 840 176 C ATOM 5740 O GLU D 89 41.851 -15.468 42.428 1.00 89.32 O ANISOU 5740 O GLU D 89 12431 10284 11223 -1599 946 339 O ATOM 5741 CB GLU D 89 39.479 -16.640 40.872 1.00 93.19 C ANISOU 5741 CB GLU D 89 12019 11241 12149 -2198 1068 -345 C ATOM 5742 CG GLU D 89 38.168 -17.414 40.918 1.00109.04 C ANISOU 5742 CG GLU D 89 13647 13358 14426 -2591 1336 -621 C ATOM 5743 CD GLU D 89 36.952 -16.806 40.245 1.00131.37 C ANISOU 5743 CD GLU D 89 15891 16768 17256 -2572 1194 -920 C ATOM 5744 OE1 GLU D 89 37.125 -15.961 39.336 1.00116.21 O ANISOU 5744 OE1 GLU D 89 13848 15175 15133 -2264 837 -982 O ATOM 5745 OE2 GLU D 89 35.826 -17.257 40.555 1.00132.62 O ANISOU 5745 OE2 GLU D 89 15706 17061 17624 -2875 1453 -1121 O ATOM 5746 N ASP D 90 41.230 -13.690 41.163 1.00 86.46 N ANISOU 5746 N ASP D 90 11660 10538 10653 -1293 566 181 N ATOM 5747 CA ASP D 90 42.543 -13.054 41.098 1.00 83.39 C ANISOU 5747 CA ASP D 90 11592 10014 10078 -1062 385 352 C ATOM 5748 C ASP D 90 42.744 -12.087 42.269 1.00 87.26 C ANISOU 5748 C ASP D 90 12318 10440 10397 -850 447 596 C ATOM 5749 O ASP D 90 43.844 -11.545 42.427 1.00 84.49 O ANISOU 5749 O ASP D 90 12232 9965 9903 -696 330 721 O ATOM 5750 CB ASP D 90 42.716 -12.314 39.760 1.00 83.95 C ANISOU 5750 CB ASP D 90 11535 10343 10022 -891 114 231 C ATOM 5751 CG ASP D 90 42.689 -13.219 38.541 1.00 94.17 C ANISOU 5751 CG ASP D 90 12636 11706 11438 -1057 12 -22 C ATOM 5752 OD1 ASP D 90 42.660 -14.460 38.718 1.00 96.57 O ANISOU 5752 OD1 ASP D 90 12939 11808 11946 -1332 152 -107 O ATOM 5753 OD2 ASP D 90 42.733 -12.692 37.414 1.00 98.92 O ANISOU 5753 OD2 ASP D 90 13131 12539 11915 -899 -194 -131 O ATOM 5754 N THR D 91 41.698 -11.889 43.102 1.00 86.39 N ANISOU 5754 N THR D 91 12101 10422 10302 -855 640 639 N ATOM 5755 CA THR D 91 41.780 -11.033 44.288 1.00 85.60 C ANISOU 5755 CA THR D 91 12233 10259 10033 -652 723 852 C ATOM 5756 C THR D 91 42.726 -11.729 45.306 1.00 88.97 C ANISOU 5756 C THR D 91 13023 10329 10451 -691 835 1022 C ATOM 5757 O THR D 91 42.404 -12.801 45.833 1.00 91.39 O ANISOU 5757 O THR D 91 13364 10464 10896 -874 1072 1045 O ATOM 5758 CB THR D 91 40.377 -10.713 44.859 1.00 96.96 C ANISOU 5758 CB THR D 91 13442 11913 11486 -633 918 842 C ATOM 5759 OG1 THR D 91 40.519 -9.928 46.040 1.00 95.88 O ANISOU 5759 OG1 THR D 91 13575 11688 11168 -425 1004 1048 O ATOM 5760 CG2 THR D 91 39.533 -11.951 45.149 1.00100.36 C ANISOU 5760 CG2 THR D 91 13672 12298 12163 -952 1199 748 C ATOM 5761 N ALA D 92 43.948 -11.161 45.472 1.00 82.21 N ANISOU 5761 N ALA D 92 12435 9368 9431 -519 663 1116 N ATOM 5762 CA ALA D 92 45.010 -11.694 46.341 1.00 81.38 C ANISOU 5762 CA ALA D 92 12656 9003 9259 -470 691 1245 C ATOM 5763 C ALA D 92 46.113 -10.663 46.596 1.00 82.80 C ANISOU 5763 C ALA D 92 13033 9191 9236 -268 490 1291 C ATOM 5764 O ALA D 92 46.129 -9.610 45.958 1.00 81.68 O ANISOU 5764 O ALA D 92 12809 9196 9030 -203 353 1229 O ATOM 5765 CB ALA D 92 45.626 -12.935 45.699 1.00 82.31 C ANISOU 5765 CB ALA D 92 12791 8964 9521 -619 668 1172 C ATOM 5766 N VAL D 93 47.052 -10.980 47.513 1.00 78.70 N ANISOU 5766 N VAL D 93 12779 8517 8606 -162 482 1383 N ATOM 5767 CA VAL D 93 48.219 -10.136 47.775 1.00 77.01 C ANISOU 5767 CA VAL D 93 12711 8330 8220 -16 285 1365 C ATOM 5768 C VAL D 93 49.336 -10.607 46.854 1.00 80.85 C ANISOU 5768 C VAL D 93 13146 8800 8772 -74 113 1260 C ATOM 5769 O VAL D 93 49.820 -11.729 47.006 1.00 81.29 O ANISOU 5769 O VAL D 93 13287 8736 8865 -66 139 1286 O ATOM 5770 CB VAL D 93 48.645 -10.131 49.259 1.00 81.39 C ANISOU 5770 CB VAL D 93 13538 8807 8579 174 327 1473 C ATOM 5771 N TYR D 94 49.693 -9.789 45.853 1.00 76.47 N ANISOU 5771 N TYR D 94 12472 8355 8228 -119 -30 1151 N ATOM 5772 CA TYR D 94 50.701 -10.157 44.861 1.00 75.70 C ANISOU 5772 CA TYR D 94 12301 8267 8194 -180 -169 1045 C ATOM 5773 C TYR D 94 52.102 -9.750 45.320 1.00 80.52 C ANISOU 5773 C TYR D 94 13013 8897 8682 -95 -306 991 C ATOM 5774 O TYR D 94 52.353 -8.585 45.633 1.00 79.88 O ANISOU 5774 O TYR D 94 12985 8868 8497 -70 -347 953 O ATOM 5775 CB TYR D 94 50.381 -9.523 43.505 1.00 75.74 C ANISOU 5775 CB TYR D 94 12144 8380 8253 -257 -219 958 C ATOM 5776 CG TYR D 94 49.236 -10.206 42.789 1.00 77.86 C ANISOU 5776 CG TYR D 94 12233 8692 8656 -349 -146 929 C ATOM 5777 CD1 TYR D 94 47.915 -9.978 43.165 1.00 80.80 C ANISOU 5777 CD1 TYR D 94 12528 9133 9038 -342 -23 971 C ATOM 5778 CD2 TYR D 94 49.469 -11.054 41.709 1.00 78.39 C ANISOU 5778 CD2 TYR D 94 12185 8762 8838 -446 -201 825 C ATOM 5779 CE1 TYR D 94 46.859 -10.611 42.516 1.00 82.40 C ANISOU 5779 CE1 TYR D 94 12505 9427 9377 -453 37 887 C ATOM 5780 CE2 TYR D 94 48.417 -11.673 41.035 1.00 80.20 C ANISOU 5780 CE2 TYR D 94 12223 9058 9192 -555 -150 740 C ATOM 5781 CZ TYR D 94 47.112 -11.447 41.443 1.00 88.22 C ANISOU 5781 CZ TYR D 94 13126 10166 10229 -570 -35 758 C ATOM 5782 OH TYR D 94 46.070 -12.057 40.794 1.00 90.99 O ANISOU 5782 OH TYR D 94 13229 10631 10713 -702 10 621 O ATOM 5783 N TYR D 95 53.010 -10.738 45.358 1.00 78.24 N ANISOU 5783 N TYR D 95 12747 8574 8406 -47 -371 965 N ATOM 5784 CA TYR D 95 54.391 -10.568 45.786 1.00 78.47 C ANISOU 5784 CA TYR D 95 12808 8686 8322 56 -521 874 C ATOM 5785 C TYR D 95 55.354 -10.690 44.626 1.00 81.18 C ANISOU 5785 C TYR D 95 12993 9105 8746 -24 -626 739 C ATOM 5786 O TYR D 95 55.242 -11.582 43.780 1.00 80.07 O ANISOU 5786 O TYR D 95 12794 8909 8719 -67 -601 742 O ATOM 5787 CB TYR D 95 54.770 -11.594 46.858 1.00 81.45 C ANISOU 5787 CB TYR D 95 13349 9008 8589 270 -519 953 C ATOM 5788 CG TYR D 95 53.813 -11.631 48.021 1.00 85.07 C ANISOU 5788 CG TYR D 95 13999 9370 8956 366 -368 1111 C ATOM 5789 CD1 TYR D 95 53.911 -10.710 49.058 1.00 87.80 C ANISOU 5789 CD1 TYR D 95 14441 9798 9120 477 -413 1101 C ATOM 5790 CD2 TYR D 95 52.844 -12.621 48.116 1.00 87.16 C ANISOU 5790 CD2 TYR D 95 14354 9453 9309 338 -158 1255 C ATOM 5791 CE1 TYR D 95 53.033 -10.743 50.139 1.00 90.46 C ANISOU 5791 CE1 TYR D 95 14967 10052 9351 589 -256 1253 C ATOM 5792 CE2 TYR D 95 51.977 -12.682 49.205 1.00 89.72 C ANISOU 5792 CE2 TYR D 95 14856 9685 9548 419 27 1407 C ATOM 5793 CZ TYR D 95 52.072 -11.738 50.213 1.00 98.54 C ANISOU 5793 CZ TYR D 95 16073 10900 10466 563 -25 1418 C ATOM 5794 OH TYR D 95 51.214 -11.794 51.284 1.00102.85 O ANISOU 5794 OH TYR D 95 16806 11363 10911 664 175 1574 O ATOM 5795 N CYS D 96 56.325 -9.805 44.628 1.00 77.99 N ANISOU 5795 N CYS D 96 12525 8826 8281 -53 -728 601 N ATOM 5796 CA CYS D 96 57.404 -9.750 43.671 1.00 77.87 C ANISOU 5796 CA CYS D 96 12349 8914 8324 -134 -805 452 C ATOM 5797 C CYS D 96 58.516 -10.683 44.118 1.00 81.88 C ANISOU 5797 C CYS D 96 12815 9526 8770 42 -928 382 C ATOM 5798 O CYS D 96 58.899 -10.668 45.289 1.00 82.64 O ANISOU 5798 O CYS D 96 12977 9700 8722 204 -1007 359 O ATOM 5799 CB CYS D 96 57.887 -8.311 43.542 1.00 78.83 C ANISOU 5799 CB CYS D 96 12428 9104 8418 -282 -803 320 C ATOM 5800 SG CYS D 96 59.350 -8.099 42.505 1.00 83.69 S ANISOU 5800 SG CYS D 96 12832 9862 9104 -419 -844 109 S ATOM 5801 N ALA D 97 59.021 -11.509 43.202 1.00 77.67 N ANISOU 5801 N ALA D 97 12185 9009 8318 54 -949 343 N ATOM 5802 CA ALA D 97 60.118 -12.426 43.499 1.00 78.61 C ANISOU 5802 CA ALA D 97 12261 9244 8365 273 -1063 272 C ATOM 5803 C ALA D 97 61.378 -11.980 42.763 1.00 81.51 C ANISOU 5803 C ALA D 97 12374 9833 8765 187 -1145 57 C ATOM 5804 O ALA D 97 61.346 -11.770 41.550 1.00 80.37 O ANISOU 5804 O ALA D 97 12139 9658 8738 11 -1072 28 O ATOM 5805 CB ALA D 97 59.737 -13.845 43.121 1.00 79.57 C ANISOU 5805 CB ALA D 97 12503 9188 8540 387 -995 391 C ATOM 5806 N ALA D 98 62.463 -11.756 43.511 1.00 78.28 N ANISOU 5806 N ALA D 98 11836 9666 8239 307 -1286 -110 N ATOM 5807 CA ALA D 98 63.722 -11.288 42.951 1.00 78.55 C ANISOU 5807 CA ALA D 98 11578 9955 8313 199 -1346 -358 C ATOM 5808 C ALA D 98 64.834 -12.281 43.182 1.00 84.07 C ANISOU 5808 C ALA D 98 12137 10891 8913 505 -1498 -467 C ATOM 5809 O ALA D 98 64.863 -12.939 44.219 1.00 85.41 O ANISOU 5809 O ALA D 98 12437 11100 8915 826 -1603 -407 O ATOM 5810 CB ALA D 98 64.095 -9.959 43.564 1.00 80.17 C ANISOU 5810 CB ALA D 98 11679 10299 8484 14 -1375 -546 C ATOM 5811 N ARG D 99 65.765 -12.380 42.230 1.00 80.87 N ANISOU 5811 N ARG D 99 11482 10657 8589 442 -1496 -624 N ATOM 5812 CA ARG D 99 66.914 -13.270 42.365 1.00 83.32 C ANISOU 5812 CA ARG D 99 11613 11246 8797 763 -1643 -757 C ATOM 5813 C ARG D 99 68.182 -12.445 42.597 1.00 89.67 C ANISOU 5813 C ARG D 99 12020 12467 9584 662 -1751 -1103 C ATOM 5814 O ARG D 99 68.344 -11.388 41.988 1.00 88.24 O ANISOU 5814 O ARG D 99 11680 12298 9547 271 -1626 -1235 O ATOM 5815 CB ARG D 99 67.061 -14.176 41.128 1.00 83.21 C ANISOU 5815 CB ARG D 99 11596 11144 8876 817 -1558 -697 C ATOM 5816 N ALA D 100 69.075 -12.923 43.480 1.00 90.27 N ANISOU 5816 N ALA D 100 11940 12888 9472 1021 -1968 -1264 N ATOM 5817 CA ALA D 100 70.339 -12.244 43.782 1.00 94.10 C ANISOU 5817 CA ALA D 100 11975 13849 9928 948 -2104 -1658 C ATOM 5818 C ALA D 100 71.295 -12.285 42.563 1.00100.47 C ANISOU 5818 C ALA D 100 12427 14858 10889 794 -2013 -1842 C ATOM 5819 O ALA D 100 71.114 -13.140 41.687 1.00 98.69 O ANISOU 5819 O ALA D 100 12327 14460 10711 917 -1921 -1659 O ATOM 5820 CB ALA D 100 70.999 -12.884 44.996 1.00 98.31 C ANISOU 5820 CB ALA D 100 12434 14742 10176 1464 -2386 -1779 C ATOM 5821 N PRO D 101 72.305 -11.379 42.466 1.00100.58 N ANISOU 5821 N PRO D 101 11999 15228 10988 506 -2013 -2217 N ATOM 5822 CA PRO D 101 73.203 -11.410 41.292 1.00101.81 C ANISOU 5822 CA PRO D 101 11816 15573 11294 345 -1878 -2384 C ATOM 5823 C PRO D 101 74.058 -12.690 41.232 1.00107.69 C ANISOU 5823 C PRO D 101 12370 16650 11896 862 -2049 -2443 C ATOM 5824 O PRO D 101 74.188 -13.284 40.155 1.00106.26 O ANISOU 5824 O PRO D 101 12198 16383 11791 907 -1916 -2342 O ATOM 5825 CB PRO D 101 74.092 -10.173 41.484 1.00106.84 C ANISOU 5825 CB PRO D 101 12019 16538 12039 -73 -1840 -2810 C ATOM 5826 CG PRO D 101 73.387 -9.327 42.507 1.00110.63 C ANISOU 5826 CG PRO D 101 12717 16849 12468 -230 -1893 -2804 C ATOM 5827 CD PRO D 101 72.667 -10.282 43.389 1.00104.59 C ANISOU 5827 CD PRO D 101 12299 15970 11471 282 -2106 -2526 C ATOM 5828 N VAL D 102 74.613 -13.122 42.393 1.00106.85 N ANISOU 5828 N VAL D 102 12125 16921 11553 1294 -2343 -2601 N ATOM 5829 CA VAL D 102 75.467 -14.307 42.533 1.00125.32 C ANISOU 5829 CA VAL D 102 14303 19622 13692 1888 -2537 -2671 C ATOM 5830 C VAL D 102 74.655 -15.568 42.175 1.00134.66 C ANISOU 5830 C VAL D 102 16010 20351 14803 2245 -2463 -2243 C ATOM 5831 O VAL D 102 74.766 -16.069 41.058 1.00 89.08 O ANISOU 5831 O VAL D 102 10245 14459 9142 2224 -2311 -2163 O ATOM 5832 CB VAL D 102 76.079 -14.404 43.964 1.00133.28 C ANISOU 5832 CB VAL D 102 15124 21111 14407 2320 -2878 -2910 C ATOM 5833 CG1 VAL D 102 74.999 -14.453 45.049 1.00131.23 C ANISOU 5833 CG1 VAL D 102 15371 20514 13975 2487 -2952 -2636 C ATOM 5834 CG2 VAL D 102 77.035 -15.590 44.086 1.00136.96 C ANISOU 5834 CG2 VAL D 102 15411 21998 14630 3000 -3081 -2999 C ATOM 5835 N SER D 107 69.179 -23.684 39.306 1.00154.11 N ANISOU 5835 N SER D 107 21874 19389 17290 3428 -1443 -256 N ATOM 5836 CA SER D 107 68.537 -22.570 40.004 1.00151.65 C ANISOU 5836 CA SER D 107 21465 19120 17034 3098 -1481 -221 C ATOM 5837 C SER D 107 67.270 -22.065 39.234 1.00151.39 C ANISOU 5837 C SER D 107 21492 18766 17263 2528 -1322 -149 C ATOM 5838 O SER D 107 67.175 -20.864 38.953 1.00148.97 O ANISOU 5838 O SER D 107 20890 18642 17068 2164 -1356 -242 O ATOM 5839 CB SER D 107 69.536 -21.428 40.187 1.00155.53 C ANISOU 5839 CB SER D 107 21433 20170 17493 3033 -1672 -464 C ATOM 5840 OG SER D 107 70.050 -20.985 38.940 1.00162.92 O ANISOU 5840 OG SER D 107 22025 21291 18587 2769 -1639 -639 O ATOM 5841 N PRO D 108 66.262 -22.929 38.919 1.00146.82 N ANISOU 5841 N PRO D 108 21294 17717 16775 2446 -1140 0 N ATOM 5842 CA PRO D 108 65.105 -22.442 38.147 1.00143.23 C ANISOU 5842 CA PRO D 108 20825 17052 16544 1948 -1028 17 C ATOM 5843 C PRO D 108 63.855 -22.143 39.005 1.00144.30 C ANISOU 5843 C PRO D 108 21157 16946 16726 1745 -937 179 C ATOM 5844 O PRO D 108 63.405 -22.980 39.802 1.00145.57 O ANISOU 5844 O PRO D 108 21676 16813 16820 1921 -822 332 O ATOM 5845 CB PRO D 108 64.813 -23.607 37.193 1.00145.93 C ANISOU 5845 CB PRO D 108 21404 17077 16966 1963 -893 8 C ATOM 5846 CG PRO D 108 65.462 -24.838 37.846 1.00154.11 C ANISOU 5846 CG PRO D 108 22755 17983 17818 2474 -864 83 C ATOM 5847 CD PRO D 108 66.183 -24.392 39.096 1.00150.98 C ANISOU 5847 CD PRO D 108 22260 17892 17212 2791 -1015 118 C ATOM 5848 N TYR D 109 63.248 -20.983 38.778 1.00136.47 N ANISOU 5848 N TYR D 109 19958 16049 15846 1378 -953 153 N ATOM 5849 CA TYR D 109 62.018 -20.602 39.477 1.00134.08 C ANISOU 5849 CA TYR D 109 19791 15557 15596 1172 -862 287 C ATOM 5850 C TYR D 109 62.098 -20.639 41.002 1.00135.49 C ANISOU 5850 C TYR D 109 20146 15732 15603 1426 -879 416 C ATOM 5851 O TYR D 109 61.157 -21.058 41.676 1.00135.27 O ANISOU 5851 O TYR D 109 20395 15418 15582 1403 -725 574 O ATOM 5852 CB TYR D 109 60.849 -21.468 38.998 1.00135.87 C ANISOU 5852 CB TYR D 109 20250 15403 15972 988 -674 344 C ATOM 5853 CG TYR D 109 60.749 -21.583 37.494 1.00137.30 C ANISOU 5853 CG TYR D 109 20293 15590 16283 792 -674 197 C ATOM 5854 CD1 TYR D 109 60.509 -20.464 36.707 1.00137.00 C ANISOU 5854 CD1 TYR D 109 19983 15762 16311 539 -740 112 C ATOM 5855 CD2 TYR D 109 60.894 -22.810 36.860 1.00140.10 C ANISOU 5855 CD2 TYR D 109 20830 15729 16670 890 -594 143 C ATOM 5856 CE1 TYR D 109 60.417 -20.564 35.332 1.00137.68 C ANISOU 5856 CE1 TYR D 109 19970 15872 16470 411 -741 -17 C ATOM 5857 CE2 TYR D 109 60.804 -22.920 35.486 1.00140.68 C ANISOU 5857 CE2 TYR D 109 20790 15827 16836 733 -605 -11 C ATOM 5858 CZ TYR D 109 60.565 -21.794 34.726 1.00146.94 C ANISOU 5858 CZ TYR D 109 21300 16860 17671 505 -686 -88 C ATOM 5859 OH TYR D 109 60.474 -21.898 33.357 1.00149.26 O ANISOU 5859 OH TYR D 109 21506 17195 18013 397 -698 -235 O ATOM 5860 N ASP D 110 63.236 -20.185 41.520 1.00130.11 N ANISOU 5860 N ASP D 110 19284 15392 14758 1665 -1058 326 N ATOM 5861 CA ASP D 110 63.492 -20.107 42.951 1.00130.05 C ANISOU 5861 CA ASP D 110 19399 15480 14534 1963 -1131 400 C ATOM 5862 C ASP D 110 63.994 -18.695 43.224 1.00128.52 C ANISOU 5862 C ASP D 110 18854 15666 14312 1821 -1304 238 C ATOM 5863 O ASP D 110 64.994 -18.267 42.647 1.00128.07 O ANISOU 5863 O ASP D 110 18471 15920 14272 1796 -1427 35 O ATOM 5864 CB ASP D 110 64.539 -21.137 43.372 1.00135.37 C ANISOU 5864 CB ASP D 110 20210 16239 14985 2494 -1205 398 C ATOM 5865 CG ASP D 110 65.552 -21.418 42.280 1.00145.71 C ANISOU 5865 CG ASP D 110 21273 17751 16339 2565 -1290 219 C ATOM 5866 OD1 ASP D 110 65.921 -20.472 41.553 1.00144.68 O ANISOU 5866 OD1 ASP D 110 20756 17885 16330 2279 -1373 41 O ATOM 5867 OD2 ASP D 110 65.980 -22.584 42.149 1.00152.95 O ANISOU 5867 OD2 ASP D 110 22407 18546 17160 2919 -1246 261 O ATOM 5868 N TYR D 111 63.305 -17.971 44.099 1.00121.05 N ANISOU 5868 N TYR D 111 17982 14685 13328 1713 -1287 315 N ATOM 5869 CA TYR D 111 63.678 -16.595 44.388 1.00118.55 C ANISOU 5869 CA TYR D 111 17385 14666 12994 1540 -1419 150 C ATOM 5870 C TYR D 111 64.442 -16.475 45.715 1.00118.63 C ANISOU 5870 C TYR D 111 17385 14953 12735 1894 -1601 71 C ATOM 5871 O TYR D 111 64.249 -17.267 46.641 1.00120.04 O ANISOU 5871 O TYR D 111 17873 15016 12722 2250 -1580 231 O ATOM 5872 CB TYR D 111 62.441 -15.686 44.417 1.00118.30 C ANISOU 5872 CB TYR D 111 17414 14450 13083 1187 -1296 245 C ATOM 5873 CG TYR D 111 61.362 -16.068 45.410 1.00121.86 C ANISOU 5873 CG TYR D 111 18200 14642 13458 1285 -1170 471 C ATOM 5874 CD1 TYR D 111 60.328 -16.928 45.049 1.00123.63 C ANISOU 5874 CD1 TYR D 111 18647 14524 13805 1204 -964 646 C ATOM 5875 CD2 TYR D 111 61.299 -15.468 46.665 1.00123.98 C ANISOU 5875 CD2 TYR D 111 18545 15011 13549 1407 -1231 487 C ATOM 5876 CE1 TYR D 111 59.303 -17.243 45.942 1.00125.71 C ANISOU 5876 CE1 TYR D 111 19196 14546 14022 1245 -795 844 C ATOM 5877 CE2 TYR D 111 60.279 -15.774 47.565 1.00125.47 C ANISOU 5877 CE2 TYR D 111 19047 14963 13664 1491 -1076 705 C ATOM 5878 CZ TYR D 111 59.278 -16.655 47.195 1.00133.47 C ANISOU 5878 CZ TYR D 111 20268 15631 14814 1397 -843 889 C ATOM 5879 OH TYR D 111 58.265 -16.952 48.070 1.00136.92 O ANISOU 5879 OH TYR D 111 20993 15832 15196 1442 -643 1093 O ATOM 5880 N ASP D 112 65.290 -15.439 45.785 1.00110.52 N ANISOU 5880 N ASP D 112 16010 14291 11691 1778 -1763 -192 N ATOM 5881 CA ASP D 112 66.151 -15.127 46.915 1.00110.73 C ANISOU 5881 CA ASP D 112 15912 14688 11474 2058 -1984 -374 C ATOM 5882 C ASP D 112 65.565 -13.992 47.763 1.00108.75 C ANISOU 5882 C ASP D 112 15710 14429 11183 1863 -1992 -397 C ATOM 5883 O ASP D 112 65.798 -13.964 48.972 1.00110.65 O ANISOU 5883 O ASP D 112 16030 14844 11167 2167 -2134 -440 O ATOM 5884 CB ASP D 112 67.545 -14.741 46.395 1.00113.99 C ANISOU 5884 CB ASP D 112 15851 15543 11918 2014 -2146 -720 C ATOM 5885 CG ASP D 112 68.195 -15.802 45.515 1.00122.13 C ANISOU 5885 CG ASP D 112 16807 16617 12978 2225 -2137 -720 C ATOM 5886 OD1 ASP D 112 67.651 -16.926 45.435 1.00122.00 O ANISOU 5886 OD1 ASP D 112 17144 16287 12924 2462 -2028 -463 O ATOM 5887 OD2 ASP D 112 69.233 -15.505 44.902 1.00128.38 O ANISOU 5887 OD2 ASP D 112 17198 17742 13837 2138 -2213 -985 O ATOM 5888 N TYR D 113 64.820 -13.053 47.133 1.00 98.57 N ANISOU 5888 N TYR D 113 14391 12946 10116 1400 -1842 -372 N ATOM 5889 CA TYR D 113 64.201 -11.926 47.833 1.00 95.90 C ANISOU 5889 CA TYR D 113 14128 12559 9751 1207 -1819 -388 C ATOM 5890 C TYR D 113 62.727 -11.840 47.484 1.00 95.49 C ANISOU 5890 C TYR D 113 14332 12110 9840 999 -1588 -112 C ATOM 5891 O TYR D 113 62.376 -11.803 46.308 1.00 93.21 O ANISOU 5891 O TYR D 113 13986 11673 9758 750 -1462 -64 O ATOM 5892 CB TYR D 113 64.907 -10.595 47.499 1.00 96.32 C ANISOU 5892 CB TYR D 113 13858 12832 9906 854 -1869 -705 C ATOM 5893 CG TYR D 113 66.391 -10.600 47.783 1.00100.05 C ANISOU 5893 CG TYR D 113 13980 13761 10272 997 -2095 -1049 C ATOM 5894 CD1 TYR D 113 66.878 -10.337 49.058 1.00104.63 C ANISOU 5894 CD1 TYR D 113 14511 14633 10609 1225 -2306 -1243 C ATOM 5895 CD2 TYR D 113 67.313 -10.832 46.768 1.00101.11 C ANISOU 5895 CD2 TYR D 113 13805 14075 10538 907 -2100 -1209 C ATOM 5896 CE1 TYR D 113 68.245 -10.353 49.327 1.00108.56 C ANISOU 5896 CE1 TYR D 113 14627 15623 10996 1375 -2541 -1607 C ATOM 5897 CE2 TYR D 113 68.683 -10.825 47.020 1.00105.31 C ANISOU 5897 CE2 TYR D 113 13951 15082 10979 1035 -2304 -1560 C ATOM 5898 CZ TYR D 113 69.146 -10.582 48.301 1.00114.31 C ANISOU 5898 CZ TYR D 113 15012 16541 11879 1266 -2535 -1772 C ATOM 5899 OH TYR D 113 70.496 -10.572 48.549 1.00118.37 O ANISOU 5899 OH TYR D 113 15089 17590 12296 1402 -2760 -2165 O ATOM 5900 N TRP D 114 61.865 -11.834 48.499 1.00 91.57 N ANISOU 5900 N TRP D 114 14107 11471 9216 1127 -1531 57 N ATOM 5901 CA TRP D 114 60.423 -11.744 48.298 1.00 89.41 C ANISOU 5901 CA TRP D 114 14036 10875 9062 951 -1311 294 C ATOM 5902 C TRP D 114 59.965 -10.281 48.391 1.00 93.38 C ANISOU 5902 C TRP D 114 14501 11373 9605 683 -1274 217 C ATOM 5903 O TRP D 114 60.731 -9.416 48.829 1.00 94.37 O ANISOU 5903 O TRP D 114 14504 11708 9646 644 -1405 -11 O ATOM 5904 CB TRP D 114 59.685 -12.617 49.324 1.00 89.25 C ANISOU 5904 CB TRP D 114 14346 10677 8889 1235 -1209 538 C ATOM 5905 N GLY D 115 58.737 -10.017 47.952 1.00 88.60 N ANISOU 5905 N GLY D 115 13996 10541 9126 504 -1092 383 N ATOM 5906 CA GLY D 115 58.156 -8.680 47.987 1.00 87.69 C ANISOU 5906 CA GLY D 115 13905 10379 9033 304 -1022 351 C ATOM 5907 C GLY D 115 57.271 -8.477 49.197 1.00 91.98 C ANISOU 5907 C GLY D 115 14677 10843 9429 447 -953 486 C ATOM 5908 O GLY D 115 56.770 -9.453 49.764 1.00 91.86 O ANISOU 5908 O GLY D 115 14816 10738 9349 641 -883 667 O ATOM 5909 N GLN D 116 57.071 -7.202 49.602 1.00 88.91 N ANISOU 5909 N GLN D 116 14340 10462 8981 350 -939 399 N ATOM 5910 CA GLN D 116 56.229 -6.830 50.749 1.00 89.40 C ANISOU 5910 CA GLN D 116 14622 10460 8885 487 -865 508 C ATOM 5911 C GLN D 116 54.748 -7.152 50.448 1.00 91.49 C ANISOU 5911 C GLN D 116 14972 10539 9252 463 -646 762 C ATOM 5912 O GLN D 116 54.013 -7.572 51.347 1.00 92.58 O ANISOU 5912 O GLN D 116 15277 10613 9286 630 -540 924 O ATOM 5913 CB GLN D 116 56.411 -5.331 51.104 1.00 91.35 C ANISOU 5913 CB GLN D 116 14911 10737 9060 367 -891 321 C ATOM 5914 CG GLN D 116 55.603 -4.829 52.325 1.00105.22 C ANISOU 5914 CG GLN D 116 16910 12441 10626 528 -820 404 C ATOM 5915 CD GLN D 116 55.930 -5.484 53.660 1.00126.69 C ANISOU 5915 CD GLN D 116 19757 15284 13097 841 -926 415 C ATOM 5916 OE1 GLN D 116 56.948 -6.167 53.839 1.00123.68 O ANISOU 5916 OE1 GLN D 116 19281 15073 12641 972 -1101 307 O ATOM 5917 NE2 GLN D 116 55.088 -5.237 54.654 1.00119.71 N ANISOU 5917 NE2 GLN D 116 19103 14335 12046 1007 -821 541 N ATOM 5918 N GLY D 117 54.351 -6.989 49.188 1.00 85.09 N ANISOU 5918 N GLY D 117 14031 9666 8632 268 -576 778 N ATOM 5919 CA GLY D 117 52.994 -7.263 48.731 1.00 83.62 C ANISOU 5919 CA GLY D 117 13840 9376 8556 226 -402 950 C ATOM 5920 C GLY D 117 52.295 -6.031 48.194 1.00 86.07 C ANISOU 5920 C GLY D 117 14146 9666 8889 134 -326 938 C ATOM 5921 O GLY D 117 52.487 -4.925 48.711 1.00 86.68 O ANISOU 5921 O GLY D 117 14343 9741 8851 150 -338 863 O ATOM 5922 N THR D 118 51.515 -6.197 47.124 1.00 80.51 N ANISOU 5922 N THR D 118 13320 8952 8320 55 -252 993 N ATOM 5923 CA THR D 118 50.744 -5.116 46.517 1.00 79.63 C ANISOU 5923 CA THR D 118 13217 8841 8197 47 -175 1005 C ATOM 5924 C THR D 118 49.344 -5.732 46.297 1.00 82.95 C ANISOU 5924 C THR D 118 13515 9307 8697 81 -61 1117 C ATOM 5925 O THR D 118 49.012 -6.205 45.208 1.00 83.33 O ANISOU 5925 O THR D 118 13390 9409 8862 12 -72 1094 O ATOM 5926 CB THR D 118 51.463 -4.515 45.253 1.00 86.44 C ANISOU 5926 CB THR D 118 14036 9700 9106 -67 -225 897 C ATOM 5927 OG1 THR D 118 50.640 -3.512 44.643 1.00 86.47 O ANISOU 5927 OG1 THR D 118 14104 9690 9060 -6 -130 939 O ATOM 5928 CG2 THR D 118 51.871 -5.565 44.212 1.00 83.98 C ANISOU 5928 CG2 THR D 118 13541 9433 8933 -156 -293 863 C ATOM 5929 N GLN D 119 48.558 -5.776 47.389 1.00 78.58 N ANISOU 5929 N GLN D 119 13037 8745 8074 182 52 1216 N ATOM 5930 CA GLN D 119 47.224 -6.380 47.466 1.00 78.94 C ANISOU 5930 CA GLN D 119 12948 8847 8199 190 204 1302 C ATOM 5931 C GLN D 119 46.315 -5.865 46.309 1.00 81.60 C ANISOU 5931 C GLN D 119 13093 9325 8584 198 213 1259 C ATOM 5932 O GLN D 119 46.125 -4.653 46.150 1.00 81.39 O ANISOU 5932 O GLN D 119 13158 9331 8435 325 208 1257 O ATOM 5933 CB GLN D 119 46.597 -6.069 48.848 1.00 81.68 C ANISOU 5933 CB GLN D 119 13447 9175 8412 330 347 1408 C ATOM 5934 CG GLN D 119 45.387 -6.939 49.259 1.00100.13 C ANISOU 5934 CG GLN D 119 15663 11543 10840 302 563 1501 C ATOM 5935 CD GLN D 119 44.086 -6.655 48.538 1.00119.47 C ANISOU 5935 CD GLN D 119 17846 14174 13374 291 645 1467 C ATOM 5936 OE1 GLN D 119 43.797 -5.520 48.133 1.00116.59 O ANISOU 5936 OE1 GLN D 119 17475 13912 12912 423 590 1436 O ATOM 5937 NE2 GLN D 119 43.210 -7.652 48.495 1.00108.73 N ANISOU 5937 NE2 GLN D 119 16277 12859 12175 156 809 1469 N ATOM 5938 N VAL D 120 45.782 -6.815 45.504 1.00 76.94 N ANISOU 5938 N VAL D 120 12257 8818 8158 81 225 1211 N ATOM 5939 CA VAL D 120 44.893 -6.566 44.358 1.00 76.69 C ANISOU 5939 CA VAL D 120 11991 8985 8163 110 200 1132 C ATOM 5940 C VAL D 120 43.484 -7.063 44.690 1.00 82.53 C ANISOU 5940 C VAL D 120 12494 9876 8989 87 354 1127 C ATOM 5941 O VAL D 120 43.323 -8.235 45.025 1.00 84.15 O ANISOU 5941 O VAL D 120 12617 10009 9347 -95 458 1119 O ATOM 5942 CB VAL D 120 45.444 -7.248 43.075 1.00 79.38 C ANISOU 5942 CB VAL D 120 12202 9345 8616 -19 70 1017 C ATOM 5943 CG1 VAL D 120 44.423 -7.242 41.942 1.00 80.18 C ANISOU 5943 CG1 VAL D 120 12022 9695 8746 22 32 903 C ATOM 5944 CG2 VAL D 120 46.757 -6.617 42.632 1.00 77.68 C ANISOU 5944 CG2 VAL D 120 12179 9022 8315 5 -47 1008 C ATOM 5945 N THR D 121 42.469 -6.188 44.592 1.00 78.92 N ANISOU 5945 N THR D 121 11931 9623 8431 273 392 1123 N ATOM 5946 CA THR D 121 41.082 -6.572 44.872 1.00 80.60 C ANISOU 5946 CA THR D 121 11850 10046 8726 254 546 1083 C ATOM 5947 C THR D 121 40.236 -6.367 43.614 1.00 86.80 C ANISOU 5947 C THR D 121 12301 11166 9514 345 440 919 C ATOM 5948 O THR D 121 40.299 -5.303 42.990 1.00 86.16 O ANISOU 5948 O THR D 121 12312 11177 9247 606 323 928 O ATOM 5949 CB THR D 121 40.518 -5.779 46.071 1.00 82.40 C ANISOU 5949 CB THR D 121 12215 10284 8810 447 703 1211 C ATOM 5950 OG1 THR D 121 41.325 -6.015 47.217 1.00 77.08 O ANISOU 5950 OG1 THR D 121 11852 9333 8101 391 776 1339 O ATOM 5951 CG2 THR D 121 39.090 -6.154 46.400 1.00 81.71 C ANISOU 5951 CG2 THR D 121 11794 10440 8813 421 896 1162 C ATOM 5952 N VAL D 122 39.441 -7.391 43.251 1.00 85.96 N ANISOU 5952 N VAL D 122 11819 11237 9603 138 492 756 N ATOM 5953 CA VAL D 122 38.546 -7.353 42.093 1.00 87.88 C ANISOU 5953 CA VAL D 122 11670 11870 9851 216 372 540 C ATOM 5954 C VAL D 122 37.091 -7.334 42.641 1.00 96.61 C ANISOU 5954 C VAL D 122 12419 13286 11000 248 543 461 C ATOM 5955 O VAL D 122 36.510 -8.391 42.896 1.00 98.46 O ANISOU 5955 O VAL D 122 12377 13562 11470 -66 704 334 O ATOM 5956 CB VAL D 122 38.823 -8.529 41.103 1.00 91.28 C ANISOU 5956 CB VAL D 122 11907 12303 10474 -67 270 338 C ATOM 5957 CG1 VAL D 122 37.969 -8.406 39.853 1.00 93.20 C ANISOU 5957 CG1 VAL D 122 11753 12989 10670 61 98 84 C ATOM 5958 CG2 VAL D 122 40.298 -8.593 40.721 1.00 87.87 C ANISOU 5958 CG2 VAL D 122 11824 11560 10004 -97 142 432 C ATOM 5959 N SER D 123 36.546 -6.120 42.890 1.00 94.80 N ANISOU 5959 N SER D 123 12231 13244 10544 625 545 544 N ATOM 5960 CA SER D 123 35.199 -5.931 43.445 1.00 98.34 C ANISOU 5960 CA SER D 123 12350 14023 10993 729 709 482 C ATOM 5961 C SER D 123 34.388 -4.906 42.624 1.00105.39 C ANISOU 5961 C SER D 123 13030 15364 11648 1182 547 379 C ATOM 5962 O SER D 123 34.889 -4.385 41.628 1.00103.70 O ANISOU 5962 O SER D 123 12969 15164 11268 1401 329 373 O ATOM 5963 CB SER D 123 35.281 -5.486 44.901 1.00101.53 C ANISOU 5963 CB SER D 123 13069 14188 11322 799 933 720 C ATOM 5964 OG SER D 123 35.841 -6.501 45.717 1.00109.46 O ANISOU 5964 OG SER D 123 14235 14841 12513 440 1106 807 O ATOM 5965 N SER D 124 33.140 -4.614 43.065 1.00106.53 N ANISOU 5965 N SER D 124 12839 15879 11757 1353 674 306 N ATOM 5966 CA SER D 124 32.164 -3.745 42.400 1.00110.22 C ANISOU 5966 CA SER D 124 13028 16859 11990 1831 543 182 C ATOM 5967 C SER D 124 32.576 -2.241 42.344 1.00115.65 C ANISOU 5967 C SER D 124 14227 17407 12307 2369 466 414 C ATOM 5968 O SER D 124 31.869 -1.466 41.691 1.00118.40 O ANISOU 5968 O SER D 124 14435 18145 12408 2847 347 340 O ATOM 5969 CB SER D 124 30.819 -3.837 43.110 1.00117.50 C ANISOU 5969 CB SER D 124 13486 18177 12983 1858 749 66 C ATOM 5970 N HIS D 125 33.685 -1.820 42.996 1.00110.07 N ANISOU 5970 N HIS D 125 14106 16165 11549 2312 539 670 N ATOM 5971 CA HIS D 125 34.096 -0.408 42.921 1.00109.73 C ANISOU 5971 CA HIS D 125 14571 15940 11183 2758 506 857 C ATOM 5972 C HIS D 125 35.604 -0.301 42.594 1.00109.53 C ANISOU 5972 C HIS D 125 15030 15428 11156 2580 426 976 C ATOM 5973 O HIS D 125 36.413 -0.875 43.319 1.00106.19 O ANISOU 5973 O HIS D 125 14768 14668 10912 2206 498 1044 O ATOM 5974 CB HIS D 125 33.777 0.335 44.235 1.00111.76 C ANISOU 5974 CB HIS D 125 15068 16072 11322 2941 722 1022 C ATOM 5975 CG HIS D 125 32.443 0.006 44.848 1.00119.03 C ANISOU 5975 CG HIS D 125 15504 17405 12315 2985 873 920 C ATOM 5976 ND1 HIS D 125 32.355 -0.650 46.065 1.00120.78 N ANISOU 5976 ND1 HIS D 125 1