Browse entries in the PDBbind-CN Database
HEADER PROTEIN BINDING 04-APR-11 3REB TITLE HIV-1 NEF PROTEIN IN COMPLEX WITH ENGINEERED HCK-SH3 DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN NEF; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: 3'ORF, NEGATIVE FACTOR, F-PROTEIN, C-TERMINAL CORE PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: TYROSINE-PROTEIN KINASE HCK; COMPND 9 CHAIN: B, D; COMPND 10 SYNONYM: HEMOPOIETIC CELL KINASE, P59-HCK/P60-HCK; COMPND 11 EC: 2.7.10.2; COMPND 12 ENGINEERED: YES; COMPND 13 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HIV-1 M:B_ARV2/SF2; SOURCE 3 ORGANISM_COMMON: HIV-1; SOURCE 4 ORGANISM_TAXID: 11685; SOURCE 5 STRAIN: SF2; SOURCE 6 GENE: HIV-1 NEF, NEF; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1 TEV; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 GENE: HCK; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PET-28B KEYWDS HIV-1 NEF, SH3 DOMAIN BINDING, SIGNALING, HCK SH3 DOMAIN, PROTEIN KEYWDS 2 BINDING EXPDTA X-RAY DIFFRACTION AUTHOR A.SCHULTE,W.BLANKENFELDT,M.GEYER REVDAT 2 10-OCT-18 3REB 1 COMPND JRNL REVDAT 1 01-JUN-11 3REB 0 JRNL AUTH S.BREUER,S.I.SCHIEVINK,A.SCHULTE,W.BLANKENFELDT,O.T.FACKLER, JRNL AUTH 2 M.GEYER JRNL TITL MOLECULAR DESIGN, FUNCTIONAL CHARACTERIZATION AND STRUCTURAL JRNL TITL 2 BASIS OF A PROTEIN INHIBITOR AGAINST THE HIV-1 PATHOGENICITY JRNL TITL 3 FACTOR NEF. JRNL REF PLOS ONE V. 6 20033 2011 JRNL REFN ESSN 1932-6203 JRNL PMID 21625496 JRNL DOI 10.1371/JOURNAL.PONE.0020033 REMARK 2 REMARK 2 RESOLUTION. 3.45 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0102 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.45 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.86 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.080 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 12282 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.216 REMARK 3 FREE R VALUE : 0.243 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160 REMARK 3 FREE R VALUE TEST SET COUNT : 634 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.45 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.71 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2321 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.2799 REMARK 3 BIN FREE R VALUE SET COUNT : 121 REMARK 3 BIN FREE R VALUE : 0.3549 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2761 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.00320 REMARK 3 B22 (A**2) : -1.00320 REMARK 3 B33 (A**2) : 2.00640 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.370 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : NULL REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 NULL NULL NULL NULL NULL REMARK 3 1 NULL NULL NULL NULL NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : NULL REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 NULL NULL NULL NULL NULL REMARK 3 1 NULL NULL NULL NULL NULL REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 74 A 207 REMARK 3 ORIGIN FOR THE GROUP (A): -46.2891 42.4247 7.3628 REMARK 3 T TENSOR REMARK 3 T11: 1.2837 T22: 1.7166 REMARK 3 T33: 0.6259 T12: -0.4276 REMARK 3 T13: -0.1348 T23: -0.0265 REMARK 3 L TENSOR REMARK 3 L11: 7.0332 L22: 8.6195 REMARK 3 L33: 6.7958 L12: 2.2722 REMARK 3 L13: -2.4795 L23: 0.8355 REMARK 3 S TENSOR REMARK 3 S11: -1.0620 S12: 2.3124 S13: 0.2351 REMARK 3 S21: -2.2116 S22: 0.7510 S23: 0.4008 REMARK 3 S31: -1.1049 S32: -1.0202 S33: -0.0000 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 80 B 138 REMARK 3 ORIGIN FOR THE GROUP (A): -22.3197 40.9210 19.8466 REMARK 3 T TENSOR REMARK 3 T11: 1.0250 T22: 0.9853 REMARK 3 T33: 1.4387 T12: -0.1934 REMARK 3 T13: 0.1707 T23: 0.0611 REMARK 3 L TENSOR REMARK 3 L11: 8.5678 L22: 3.1834 REMARK 3 L33: 3.1892 L12: 2.6816 REMARK 3 L13: -2.7914 L23: 2.3240 REMARK 3 S TENSOR REMARK 3 S11: -0.7654 S12: -0.0574 S13: -1.3978 REMARK 3 S21: 0.2451 S22: 0.6277 S23: -1.1232 REMARK 3 S31: -0.3946 S32: -0.4465 S33: 0.0000 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 69 C 207 REMARK 3 ORIGIN FOR THE GROUP (A): -47.1548 21.9080 -7.9378 REMARK 3 T TENSOR REMARK 3 T11: 0.8698 T22: 0.9105 REMARK 3 T33: 0.8783 T12: 0.1500 REMARK 3 T13: -0.1465 T23: 0.0477 REMARK 3 L TENSOR REMARK 3 L11: 10.5309 L22: 4.2412 REMARK 3 L33: 4.5166 L12: -3.0725 REMARK 3 L13: -1.0755 L23: 1.0314 REMARK 3 S TENSOR REMARK 3 S11: -0.5285 S12: -0.6139 S13: 0.3669 REMARK 3 S21: 0.4592 S22: 0.2075 S23: -0.8615 REMARK 3 S31: -0.1458 S32: 0.6283 S33: 0.0000 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 79 D 138 REMARK 3 ORIGIN FOR THE GROUP (A): -73.9081 24.3088 -11.1676 REMARK 3 T TENSOR REMARK 3 T11: 0.8160 T22: 0.9816 REMARK 3 T33: 1.2186 T12: 0.0179 REMARK 3 T13: -0.1663 T23: -0.2878 REMARK 3 L TENSOR REMARK 3 L11: 6.9919 L22: 6.3410 REMARK 3 L33: 4.6660 L12: -1.1814 REMARK 3 L13: -5.3397 L23: -1.7621 REMARK 3 S TENSOR REMARK 3 S11: -0.0680 S12: -0.2422 S13: 0.0665 REMARK 3 S21: 0.0349 S22: -0.2004 S23: 1.1192 REMARK 3 S31: -0.0595 S32: -0.3718 S33: 0.0000 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.11 REMARK 3 ION PROBE RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3REB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-11. REMARK 100 THE DEPOSITION ID IS D_1000064825. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-MAY-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763 REMARK 200 MONOCHROMATOR : DIAMOND(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12282 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.450 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.55 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: REFMAC 5.5.0102 REMARK 200 STARTING MODEL: PDB ENTRY 3REA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 69.51 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.03 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 0.05 M SODIUM CITRATE, REMARK 280 15% ISOPROPANOL, 30% GLYCEROL, PH 7.0, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 285K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.34333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 86.68667 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 65.01500 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 108.35833 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 21.67167 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1390 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 9570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10130 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 45 REMARK 465 ALA A 46 REMARK 465 MET A 47 REMARK 465 ALA A 48 REMARK 465 SER A 49 REMARK 465 SER A 50 REMARK 465 ASN A 51 REMARK 465 THR A 52 REMARK 465 ALA A 53 REMARK 465 ALA A 54 REMARK 465 THR A 55 REMARK 465 ASN A 56 REMARK 465 ALA A 57 REMARK 465 ASP A 58 REMARK 465 SER A 59 REMARK 465 ALA A 60 REMARK 465 TRP A 61 REMARK 465 LEU A 62 REMARK 465 GLU A 63 REMARK 465 ALA A 64 REMARK 465 GLN A 65 REMARK 465 GLU A 66 REMARK 465 GLU A 67 REMARK 465 GLU A 68 REMARK 465 GLU A 69 REMARK 465 VAL A 70 REMARK 465 GLY A 71 REMARK 465 PHE A 72 REMARK 465 PRO A 73 REMARK 465 GLU A 155 REMARK 465 LYS A 156 REMARK 465 VAL A 157 REMARK 465 GLU A 158 REMARK 465 GLU A 159 REMARK 465 ALA A 160 REMARK 465 ASN A 161 REMARK 465 GLU A 162 REMARK 465 GLY A 163 REMARK 465 GLU A 164 REMARK 465 ASN A 165 REMARK 465 ASN A 166 REMARK 465 SER A 167 REMARK 465 LEU A 168 REMARK 465 LEU A 169 REMARK 465 HIS A 170 REMARK 465 PRO A 171 REMARK 465 MET A 172 REMARK 465 SER A 173 REMARK 465 LEU A 174 REMARK 465 HIS A 175 REMARK 465 GLY A 176 REMARK 465 MET A 177 REMARK 465 GLU A 178 REMARK 465 ASP A 179 REMARK 465 ALA A 180 REMARK 465 GLU A 181 REMARK 465 LYS A 182 REMARK 465 LYS A 208 REMARK 465 ASP A 209 REMARK 465 ALA A 210 REMARK 465 MET B 78 REMARK 465 GLU B 79 REMARK 465 GLY B 139 REMARK 465 GLY B 140 REMARK 465 GLY B 141 REMARK 465 THR B 142 REMARK 465 SER B 143 REMARK 465 GLY B 144 REMARK 465 GLY B 145 REMARK 465 GLY B 146 REMARK 465 ARG B 147 REMARK 465 HIS B 148 REMARK 465 ARG B 149 REMARK 465 ARG B 150 REMARK 465 ARG B 151 REMARK 465 GLN B 152 REMARK 465 ALA B 153 REMARK 465 GLU B 154 REMARK 465 ARG B 155 REMARK 465 MET B 156 REMARK 465 SER B 157 REMARK 465 GLN B 158 REMARK 465 ILE B 159 REMARK 465 LYS B 160 REMARK 465 ARG B 161 REMARK 465 LEU B 162 REMARK 465 LEU B 163 REMARK 465 SER B 164 REMARK 465 GLU B 165 REMARK 465 LYS B 166 REMARK 465 LYS B 167 REMARK 465 GLY C 45 REMARK 465 ALA C 46 REMARK 465 MET C 47 REMARK 465 ALA C 48 REMARK 465 SER C 49 REMARK 465 SER C 50 REMARK 465 ASN C 51 REMARK 465 THR C 52 REMARK 465 ALA C 53 REMARK 465 ALA C 54 REMARK 465 THR C 55 REMARK 465 ASN C 56 REMARK 465 ALA C 57 REMARK 465 ASP C 58 REMARK 465 SER C 59 REMARK 465 ALA C 60 REMARK 465 TRP C 61 REMARK 465 LEU C 62 REMARK 465 GLU C 63 REMARK 465 ALA C 64 REMARK 465 GLN C 65 REMARK 465 GLU C 66 REMARK 465 GLU C 67 REMARK 465 GLU C 68 REMARK 465 LYS C 156 REMARK 465 VAL C 157 REMARK 465 GLU C 158 REMARK 465 GLU C 159 REMARK 465 ALA C 160 REMARK 465 ASN C 161 REMARK 465 GLU C 162 REMARK 465 GLY C 163 REMARK 465 GLU C 164 REMARK 465 ASN C 165 REMARK 465 ASN C 166 REMARK 465 SER C 167 REMARK 465 LEU C 168 REMARK 465 LEU C 169 REMARK 465 HIS C 170 REMARK 465 PRO C 171 REMARK 465 MET C 172 REMARK 465 SER C 173 REMARK 465 LEU C 174 REMARK 465 HIS C 175 REMARK 465 GLY C 176 REMARK 465 MET C 177 REMARK 465 GLU C 178 REMARK 465 ASP C 179 REMARK 465 ALA C 180 REMARK 465 LYS C 208 REMARK 465 ASP C 209 REMARK 465 ALA C 210 REMARK 465 MET D 78 REMARK 465 GLY D 139 REMARK 465 GLY D 140 REMARK 465 GLY D 141 REMARK 465 THR D 142 REMARK 465 SER D 143 REMARK 465 GLY D 144 REMARK 465 GLY D 145 REMARK 465 GLY D 146 REMARK 465 ARG D 147 REMARK 465 HIS D 148 REMARK 465 ARG D 149 REMARK 465 ARG D 150 REMARK 465 ARG D 151 REMARK 465 GLN D 152 REMARK 465 ALA D 153 REMARK 465 GLU D 154 REMARK 465 ARG D 155 REMARK 465 MET D 156 REMARK 465 SER D 157 REMARK 465 GLN D 158 REMARK 465 ILE D 159 REMARK 465 LYS D 160 REMARK 465 ARG D 161 REMARK 465 LEU D 162 REMARK 465 LEU D 163 REMARK 465 SER D 164 REMARK 465 GLU D 165 REMARK 465 LYS D 166 REMARK 465 LYS D 167 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 153 CG CD OE1 OE2 REMARK 470 LEU A 193 CG CD1 CD2 REMARK 470 GLU A 201 CG CD OE1 OE2 REMARK 470 TYR A 207 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU C 69 CB CG CD OE1 OE2 REMARK 470 VAL C 70 CB CG1 CG2 REMARK 470 PHE C 72 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 PRO C 73 CB CG CD REMARK 470 LYS C 96 CG CD CE NZ REMARK 470 ARG C 109 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 153 CG CD OE1 OE2 REMARK 470 GLU C 155 CG CD OE1 OE2 REMARK 470 GLU C 181 CG CD OE1 OE2 REMARK 470 LEU C 202 CG CD1 CD2 REMARK 470 HIS C 203 CG ND1 CD2 CE1 NE2 REMARK 470 TYR C 207 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG D 135 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ALA C 88 OG SER C 92 2.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS C 146 CB CYS C 146 SG -0.108 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG C 75 N - CA - CB ANGL. DEV. = 33.6 DEGREES REMARK 500 ARG C 75 N - CA - C ANGL. DEV. = -26.4 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO A 76 -175.39 -66.86 REMARK 500 LEU A 101 -54.95 -163.29 REMARK 500 PHE A 125 164.06 -44.84 REMARK 500 PRO A 126 66.62 -108.07 REMARK 500 HIS A 197 69.55 -103.94 REMARK 500 HIS A 203 154.74 177.10 REMARK 500 PRO A 204 91.55 -53.38 REMARK 500 ASP B 137 31.22 -85.56 REMARK 500 VAL C 70 -99.29 133.83 REMARK 500 PHE C 72 156.24 85.15 REMARK 500 PRO C 73 171.95 151.15 REMARK 500 ARG C 75 125.14 123.70 REMARK 500 PRO C 76 -178.61 -67.43 REMARK 500 LEU C 101 -58.40 -162.24 REMARK 500 PHE C 125 163.46 -44.84 REMARK 500 PRO C 126 75.16 -107.16 REMARK 500 HIS C 197 66.94 -105.83 REMARK 500 HIS C 203 140.81 156.39 REMARK 500 PRO C 204 93.97 -54.20 REMARK 500 ASP D 137 -74.46 169.40 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LEU A 202 HIS A 203 69.35 REMARK 500 LEU C 202 HIS C 203 111.05 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3REA RELATED DB: PDB REMARK 900 RELATED ID: 3RBB RELATED DB: PDB DBREF 3REB A 45 210 UNP P03407 NEF_HV1A2 45 210 DBREF 3REB B 79 138 UNP P08631 HCK_HUMAN 79 138 DBREF 3REB C 45 210 UNP P03407 NEF_HV1A2 45 210 DBREF 3REB D 79 138 UNP P08631 HCK_HUMAN 79 138 SEQADV 3REB MET A 47 UNP P03407 ILE 47 ENGINEERED MUTATION SEQADV 3REB ALA A 48 UNP P03407 THR 48 ENGINEERED MUTATION SEQADV 3REB SER A 59 UNP P03407 CYS 59 ENGINEERED MUTATION SEQADV 3REB ALA A 210 UNP P03407 CYS 210 ENGINEERED MUTATION SEQADV 3REB MET B 78 UNP P08631 INITIATING METHIONINE SEQADV 3REB VAL B 90 UNP P08631 GLU 90 ENGINEERED MUTATION SEQADV 3REB SER B 91 UNP P08631 ALA 91 ENGINEERED MUTATION SEQADV 3REB TRP B 92 UNP P08631 ILE 92 ENGINEERED MUTATION SEQADV 3REB SER B 93 UNP P08631 HIS 93 ENGINEERED MUTATION SEQADV 3REB PRO B 94 UNP P08631 HIS 94 ENGINEERED MUTATION SEQADV 3REB ASP B 95 UNP P08631 GLU 95 ENGINEERED MUTATION SEQADV 3REB GLY B 139 UNP P08631 EXPRESSION TAG SEQADV 3REB GLY B 140 UNP P08631 EXPRESSION TAG SEQADV 3REB GLY B 141 UNP P08631 EXPRESSION TAG SEQADV 3REB THR B 142 UNP P08631 EXPRESSION TAG SEQADV 3REB SER B 143 UNP P08631 EXPRESSION TAG SEQADV 3REB GLY B 144 UNP P08631 EXPRESSION TAG SEQADV 3REB GLY B 145 UNP P08631 EXPRESSION TAG SEQADV 3REB GLY B 146 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG B 147 UNP P08631 EXPRESSION TAG SEQADV 3REB HIS B 148 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG B 149 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG B 150 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG B 151 UNP P08631 EXPRESSION TAG SEQADV 3REB GLN B 152 UNP P08631 EXPRESSION TAG SEQADV 3REB ALA B 153 UNP P08631 EXPRESSION TAG SEQADV 3REB GLU B 154 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG B 155 UNP P08631 EXPRESSION TAG SEQADV 3REB MET B 156 UNP P08631 EXPRESSION TAG SEQADV 3REB SER B 157 UNP P08631 EXPRESSION TAG SEQADV 3REB GLN B 158 UNP P08631 EXPRESSION TAG SEQADV 3REB ILE B 159 UNP P08631 EXPRESSION TAG SEQADV 3REB LYS B 160 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG B 161 UNP P08631 EXPRESSION TAG SEQADV 3REB LEU B 162 UNP P08631 EXPRESSION TAG SEQADV 3REB LEU B 163 UNP P08631 EXPRESSION TAG SEQADV 3REB SER B 164 UNP P08631 EXPRESSION TAG SEQADV 3REB GLU B 165 UNP P08631 EXPRESSION TAG SEQADV 3REB LYS B 166 UNP P08631 EXPRESSION TAG SEQADV 3REB LYS B 167 UNP P08631 EXPRESSION TAG SEQADV 3REB MET C 47 UNP P03407 ILE 47 ENGINEERED MUTATION SEQADV 3REB ALA C 48 UNP P03407 THR 48 ENGINEERED MUTATION SEQADV 3REB SER C 59 UNP P03407 CYS 59 ENGINEERED MUTATION SEQADV 3REB ALA C 210 UNP P03407 CYS 210 ENGINEERED MUTATION SEQADV 3REB MET D 78 UNP P08631 INITIATING METHIONINE SEQADV 3REB VAL D 90 UNP P08631 GLU 90 ENGINEERED MUTATION SEQADV 3REB SER D 91 UNP P08631 ALA 91 ENGINEERED MUTATION SEQADV 3REB TRP D 92 UNP P08631 ILE 92 ENGINEERED MUTATION SEQADV 3REB SER D 93 UNP P08631 HIS 93 ENGINEERED MUTATION SEQADV 3REB PRO D 94 UNP P08631 HIS 94 ENGINEERED MUTATION SEQADV 3REB ASP D 95 UNP P08631 GLU 95 ENGINEERED MUTATION SEQADV 3REB GLY D 139 UNP P08631 EXPRESSION TAG SEQADV 3REB GLY D 140 UNP P08631 EXPRESSION TAG SEQADV 3REB GLY D 141 UNP P08631 EXPRESSION TAG SEQADV 3REB THR D 142 UNP P08631 EXPRESSION TAG SEQADV 3REB SER D 143 UNP P08631 EXPRESSION TAG SEQADV 3REB GLY D 144 UNP P08631 EXPRESSION TAG SEQADV 3REB GLY D 145 UNP P08631 EXPRESSION TAG SEQADV 3REB GLY D 146 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG D 147 UNP P08631 EXPRESSION TAG SEQADV 3REB HIS D 148 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG D 149 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG D 150 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG D 151 UNP P08631 EXPRESSION TAG SEQADV 3REB GLN D 152 UNP P08631 EXPRESSION TAG SEQADV 3REB ALA D 153 UNP P08631 EXPRESSION TAG SEQADV 3REB GLU D 154 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG D 155 UNP P08631 EXPRESSION TAG SEQADV 3REB MET D 156 UNP P08631 EXPRESSION TAG SEQADV 3REB SER D 157 UNP P08631 EXPRESSION TAG SEQADV 3REB GLN D 158 UNP P08631 EXPRESSION TAG SEQADV 3REB ILE D 159 UNP P08631 EXPRESSION TAG SEQADV 3REB LYS D 160 UNP P08631 EXPRESSION TAG SEQADV 3REB ARG D 161 UNP P08631 EXPRESSION TAG SEQADV 3REB LEU D 162 UNP P08631 EXPRESSION TAG SEQADV 3REB LEU D 163 UNP P08631 EXPRESSION TAG SEQADV 3REB SER D 164 UNP P08631 EXPRESSION TAG SEQADV 3REB GLU D 165 UNP P08631 EXPRESSION TAG SEQADV 3REB LYS D 166 UNP P08631 EXPRESSION TAG SEQADV 3REB LYS D 167 UNP P08631 EXPRESSION TAG SEQRES 1 A 166 GLY ALA MET ALA SER SER ASN THR ALA ALA THR ASN ALA SEQRES 2 A 166 ASP SER ALA TRP LEU GLU ALA GLN GLU GLU GLU GLU VAL SEQRES 3 A 166 GLY PHE PRO VAL ARG PRO GLN VAL PRO LEU ARG PRO MET SEQRES 4 A 166 THR TYR LYS ALA ALA LEU ASP ILE SER HIS PHE LEU LYS SEQRES 5 A 166 GLU LYS GLY GLY LEU GLU GLY LEU ILE TRP SER GLN ARG SEQRES 6 A 166 ARG GLN GLU ILE LEU ASP LEU TRP ILE TYR HIS THR GLN SEQRES 7 A 166 GLY TYR PHE PRO ASP TRP GLN ASN TYR THR PRO GLY PRO SEQRES 8 A 166 GLY ILE ARG TYR PRO LEU THR PHE GLY TRP CYS PHE LYS SEQRES 9 A 166 LEU VAL PRO VAL GLU PRO GLU LYS VAL GLU GLU ALA ASN SEQRES 10 A 166 GLU GLY GLU ASN ASN SER LEU LEU HIS PRO MET SER LEU SEQRES 11 A 166 HIS GLY MET GLU ASP ALA GLU LYS GLU VAL LEU VAL TRP SEQRES 12 A 166 ARG PHE ASP SER LYS LEU ALA PHE HIS HIS MET ALA ARG SEQRES 13 A 166 GLU LEU HIS PRO GLU TYR TYR LYS ASP ALA SEQRES 1 B 90 MET GLU ASP ILE ILE VAL VAL ALA LEU TYR ASP TYR VAL SEQRES 2 B 90 SER TRP SER PRO ASP ASP LEU SER PHE GLN LYS GLY ASP SEQRES 3 B 90 GLN MET VAL VAL LEU GLU GLU SER GLY GLU TRP TRP LYS SEQRES 4 B 90 ALA ARG SER LEU ALA THR ARG LYS GLU GLY TYR ILE PRO SEQRES 5 B 90 SER ASN TYR VAL ALA ARG VAL ASP SER GLY GLY GLY THR SEQRES 6 B 90 SER GLY GLY GLY ARG HIS ARG ARG ARG GLN ALA GLU ARG SEQRES 7 B 90 MET SER GLN ILE LYS ARG LEU LEU SER GLU LYS LYS SEQRES 1 C 166 GLY ALA MET ALA SER SER ASN THR ALA ALA THR ASN ALA SEQRES 2 C 166 ASP SER ALA TRP LEU GLU ALA GLN GLU GLU GLU GLU VAL SEQRES 3 C 166 GLY PHE PRO VAL ARG PRO GLN VAL PRO LEU ARG PRO MET SEQRES 4 C 166 THR TYR LYS ALA ALA LEU ASP ILE SER HIS PHE LEU LYS SEQRES 5 C 166 GLU LYS GLY GLY LEU GLU GLY LEU ILE TRP SER GLN ARG SEQRES 6 C 166 ARG GLN GLU ILE LEU ASP LEU TRP ILE TYR HIS THR GLN SEQRES 7 C 166 GLY TYR PHE PRO ASP TRP GLN ASN TYR THR PRO GLY PRO SEQRES 8 C 166 GLY ILE ARG TYR PRO LEU THR PHE GLY TRP CYS PHE LYS SEQRES 9 C 166 LEU VAL PRO VAL GLU PRO GLU LYS VAL GLU GLU ALA ASN SEQRES 10 C 166 GLU GLY GLU ASN ASN SER LEU LEU HIS PRO MET SER LEU SEQRES 11 C 166 HIS GLY MET GLU ASP ALA GLU LYS GLU VAL LEU VAL TRP SEQRES 12 C 166 ARG PHE ASP SER LYS LEU ALA PHE HIS HIS MET ALA ARG SEQRES 13 C 166 GLU LEU HIS PRO GLU TYR TYR LYS ASP ALA SEQRES 1 D 90 MET GLU ASP ILE ILE VAL VAL ALA LEU TYR ASP TYR VAL SEQRES 2 D 90 SER TRP SER PRO ASP ASP LEU SER PHE GLN LYS GLY ASP SEQRES 3 D 90 GLN MET VAL VAL LEU GLU GLU SER GLY GLU TRP TRP LYS SEQRES 4 D 90 ALA ARG SER LEU ALA THR ARG LYS GLU GLY TYR ILE PRO SEQRES 5 D 90 SER ASN TYR VAL ALA ARG VAL ASP SER GLY GLY GLY THR SEQRES 6 D 90 SER GLY GLY GLY ARG HIS ARG ARG ARG GLN ALA GLU ARG SEQRES 7 D 90 MET SER GLN ILE LYS ARG LEU LEU SER GLU LYS LYS HELIX 1 1 THR A 84 GLY A 99 1 16 HELIX 2 2 SER A 107 GLY A 123 1 17 HELIX 3 3 SER A 191 PHE A 195 5 5 HELIX 4 4 HIS A 197 LEU A 202 1 6 HELIX 5 5 THR C 84 GLY C 99 1 16 HELIX 6 6 SER C 107 GLY C 123 1 17 HELIX 7 7 SER C 191 PHE C 195 5 5 HELIX 8 8 HIS C 197 LEU C 202 1 6 SHEET 1 A 2 PHE A 147 PRO A 151 0 SHEET 2 A 2 LEU A 185 PHE A 189 -1 O VAL A 186 N VAL A 150 SHEET 1 B 5 GLU B 125 PRO B 129 0 SHEET 2 B 5 TRP B 114 SER B 119 -1 N ALA B 117 O GLY B 126 SHEET 3 B 5 GLN B 104 GLU B 109 -1 N LEU B 108 O LYS B 116 SHEET 4 B 5 ILE B 82 ALA B 85 -1 N VAL B 83 O MET B 105 SHEET 5 B 5 VAL B 133 VAL B 136 -1 O ALA B 134 N VAL B 84 SHEET 1 C 2 PHE C 147 PRO C 151 0 SHEET 2 C 2 LEU C 185 PHE C 189 -1 O ARG C 188 N LYS C 148 SHEET 1 D 5 GLU D 125 PRO D 129 0 SHEET 2 D 5 TRP D 114 SER D 119 -1 N ALA D 117 O GLY D 126 SHEET 3 D 5 GLN D 104 GLU D 109 -1 N LEU D 108 O LYS D 116 SHEET 4 D 5 ILE D 82 ALA D 85 -1 N VAL D 83 O MET D 105 SHEET 5 D 5 VAL D 133 VAL D 136 -1 O ALA D 134 N VAL D 84 CISPEP 1 GLY A 134 PRO A 135 0 -8.12 CISPEP 2 PHE C 72 PRO C 73 0 -1.10 CISPEP 3 PRO C 73 VAL C 74 0 1.40 CISPEP 4 GLY C 134 PRO C 135 0 -7.78 CRYST1 112.460 112.460 130.030 90.00 90.00 120.00 P 61 12 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 0.008892 0.005134 0.000000 0.00000 SCALE2 0.000000 0.010268 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007691 0.00000 ATOM 1 N VAL A 74 -21.234 47.427 2.237 1.00217.16 N ANISOU 1 N VAL A 74 26729 30666 25116 -12748 10469 -2844 N ATOM 2 CA VAL A 74 -20.290 47.496 3.393 1.00216.61 C ANISOU 2 CA VAL A 74 25573 30550 26180 -12592 10296 -3052 C ATOM 3 C VAL A 74 -20.896 46.851 4.641 1.00207.80 C ANISOU 3 C VAL A 74 23974 29450 25532 -11709 9368 -3028 C ATOM 4 O VAL A 74 -20.668 47.315 5.767 1.00205.30 O ANISOU 4 O VAL A 74 23224 29023 25758 -11507 8778 -2927 O ATOM 5 CB VAL A 74 -19.819 48.965 3.698 1.00219.99 C ANISOU 5 CB VAL A 74 26216 30692 26677 -13118 10191 -2757 C ATOM 6 CG1 VAL A 74 -19.234 49.612 2.443 1.00229.38 C ANISOU 6 CG1 VAL A 74 27959 31830 27366 -14035 11165 -2736 C ATOM 7 CG2 VAL A 74 -20.956 49.824 4.262 1.00213.95 C ANISOU 7 CG2 VAL A 74 26254 29619 25419 -12798 9235 -2199 C ATOM 8 N ARG A 75 -21.692 45.800 4.445 1.00204.84 N ANISOU 8 N ARG A 75 23723 29207 24898 -11227 9248 -3125 N ATOM 9 CA ARG A 75 -21.950 44.849 5.535 1.00198.54 C ANISOU 9 CA ARG A 75 22237 28459 24739 -10440 8670 -3248 C ATOM 10 C ARG A 75 -22.413 43.507 5.018 1.00197.35 C ANISOU 10 C ARG A 75 22068 28451 24466 -10126 8972 -3545 C ATOM 11 O ARG A 75 -23.101 43.447 4.010 1.00198.30 O ANISOU 11 O ARG A 75 22976 28634 23734 -10367 9209 -3508 O ATOM 12 CB ARG A 75 -22.987 45.375 6.515 1.00190.95 C ANISOU 12 CB ARG A 75 21663 27332 23556 -9972 7623 -2814 C ATOM 13 CG ARG A 75 -24.339 45.699 5.893 1.00187.96 C ANISOU 13 CG ARG A 75 22360 26891 22165 -9939 7315 -2459 C ATOM 14 CD ARG A 75 -25.248 46.444 6.852 1.00181.97 C ANISOU 14 CD ARG A 75 21955 25916 21268 -9544 6381 -2034 C ATOM 15 NE ARG A 75 -24.561 47.512 7.595 1.00183.62 N ANISOU 15 NE ARG A 75 21973 25914 21880 -9771 6189 -1917 N ATOM 16 CZ ARG A 75 -25.148 48.363 8.441 1.00180.08 C ANISOU 16 CZ ARG A 75 21845 25211 21365 -9551 5497 -1602 C ATOM 17 NH1 ARG A 75 -26.458 48.308 8.664 1.00174.58 N ANISOU 17 NH1 ARG A 75 21646 24443 20243 -9060 4922 -1335 N ATOM 18 NH2 ARG A 75 -24.420 49.284 9.068 1.00182.66 N ANISOU 18 NH2 ARG A 75 21979 25350 22074 -9851 5408 -1589 N ATOM 19 N PRO A 76 -22.023 42.422 5.695 1.00161.91 N ANISOU 19 N PRO A 76 16691 24004 20822 -9604 8966 -3840 N ATOM 20 CA PRO A 76 -22.506 41.139 5.235 1.00161.08 C ANISOU 20 CA PRO A 76 16618 23951 20632 -9312 9274 -4141 C ATOM 21 C PRO A 76 -24.002 40.953 5.401 1.00153.92 C ANISOU 21 C PRO A 76 16410 23012 19059 -8937 8571 -3871 C ATOM 22 O PRO A 76 -24.719 41.877 5.756 1.00149.88 O ANISOU 22 O PRO A 76 16431 22440 18079 -8909 7886 -3431 O ATOM 23 CB PRO A 76 -21.727 40.148 6.102 1.00161.61 C ANISOU 23 CB PRO A 76 15562 23987 21857 -8770 9320 -4408 C ATOM 24 CG PRO A 76 -20.437 40.825 6.325 1.00167.17 C ANISOU 24 CG PRO A 76 15589 24745 23182 -9106 9572 -4464 C ATOM 25 CD PRO A 76 -20.804 42.274 6.508 1.00164.87 C ANISOU 25 CD PRO A 76 15953 24407 22284 -9470 9029 -4026 C ATOM 26 N GLN A 77 -24.432 39.746 5.071 1.00157.92 N ANISOU 26 N GLN A 77 16897 23546 19559 -8691 8834 -4183 N ATOM 27 CA GLN A 77 -25.798 39.308 5.176 1.00152.19 C ANISOU 27 CA GLN A 77 16684 22820 18323 -8351 8290 -4050 C ATOM 28 C GLN A 77 -25.876 38.579 6.492 1.00147.25 C ANISOU 28 C GLN A 77 15403 22042 18501 -7623 7794 -4012 C ATOM 29 O GLN A 77 -25.174 37.594 6.710 1.00149.74 O ANISOU 29 O GLN A 77 15024 22273 19596 -7365 8215 -4337 O ATOM 30 CB GLN A 77 -26.093 38.362 4.011 1.00156.00 C ANISOU 30 CB GLN A 77 17493 23410 18369 -8609 8975 -4497 C ATOM 31 CG GLN A 77 -27.292 37.448 4.161 1.00151.50 C ANISOU 31 CG GLN A 77 17159 22825 17577 -8227 8608 -4568 C ATOM 32 CD GLN A 77 -28.605 38.171 3.933 1.00147.87 C ANISOU 32 CD GLN A 77 17522 22515 16145 -8317 7896 -4160 C ATOM 33 OE1 GLN A 77 -28.904 38.616 2.810 1.00151.80 O ANISOU 33 OE1 GLN A 77 18708 23224 15747 -8852 8096 -4139 O ATOM 34 NE2 GLN A 77 -29.413 38.272 4.993 1.00141.02 N ANISOU 34 NE2 GLN A 77 16588 21549 15444 -7784 7066 -3823 N ATOM 35 N VAL A 78 -26.728 39.065 7.378 1.00137.84 N ANISOU 35 N VAL A 78 14447 20797 17129 -7280 6919 -3598 N ATOM 36 CA VAL A 78 -26.793 38.537 8.733 1.00133.48 C ANISOU 36 CA VAL A 78 13353 20113 17250 -6630 6388 -3484 C ATOM 37 C VAL A 78 -27.402 37.152 8.681 1.00132.10 C ANISOU 37 C VAL A 78 13126 19858 17209 -6274 6553 -3732 C ATOM 38 O VAL A 78 -28.261 36.902 7.840 1.00131.89 O ANISOU 38 O VAL A 78 13673 19907 16533 -6483 6701 -3857 O ATOM 39 CB VAL A 78 -27.629 39.444 9.651 1.00127.58 C ANISOU 39 CB VAL A 78 12960 19323 16191 -6405 5487 -3020 C ATOM 40 CG1 VAL A 78 -27.117 40.902 9.578 1.00129.62 C ANISOU 40 CG1 VAL A 78 13417 19590 16241 -6839 5377 -2792 C ATOM 41 CG2 VAL A 78 -29.101 39.363 9.291 1.00123.74 C ANISOU 41 CG2 VAL A 78 13173 18868 14974 -6333 5181 -2899 C ATOM 42 N PRO A 79 -26.957 36.244 9.561 1.00125.93 N ANISOU 42 N PRO A 79 11670 18916 17260 -5758 6524 -3798 N ATOM 43 CA PRO A 79 -27.454 34.886 9.530 1.00125.53 C ANISOU 43 CA PRO A 79 11566 18698 17431 -5430 6764 -4041 C ATOM 44 C PRO A 79 -28.954 34.808 9.617 1.00120.08 C ANISOU 44 C PRO A 79 11508 18020 16098 -5334 6284 -3892 C ATOM 45 O PRO A 79 -29.600 35.643 10.251 1.00115.39 O ANISOU 45 O PRO A 79 11189 17491 15161 -5232 5579 -3503 O ATOM 46 CB PRO A 79 -26.841 34.258 10.777 1.00125.42 C ANISOU 46 CB PRO A 79 10807 18494 18354 -4813 6518 -3901 C ATOM 47 CG PRO A 79 -25.634 34.993 10.983 1.00128.92 C ANISOU 47 CG PRO A 79 10727 19058 19198 -4956 6536 -3832 C ATOM 48 CD PRO A 79 -25.973 36.407 10.630 1.00126.87 C ANISOU 48 CD PRO A 79 11051 18997 18156 -5457 6248 -3635 C ATOM 49 N LEU A 80 -29.512 33.793 8.986 1.00128.03 N ANISOU 49 N LEU A 80 12717 18955 16975 -5380 6692 -4238 N ATOM 50 CA LEU A 80 -30.963 33.646 8.968 1.00123.86 C ANISOU 50 CA LEU A 80 12726 18481 15856 -5350 6280 -4161 C ATOM 51 C LEU A 80 -31.446 33.077 10.277 1.00119.51 C ANISOU 51 C LEU A 80 11932 17704 15773 -4751 5808 -3927 C ATOM 52 O LEU A 80 -30.751 32.293 10.968 1.00120.95 O ANISOU 52 O LEU A 80 11578 17625 16752 -4348 5981 -3951 O ATOM 53 CB LEU A 80 -31.401 32.770 7.792 1.00127.58 C ANISOU 53 CB LEU A 80 13517 18986 15971 -5708 6884 -4668 C ATOM 54 CG LEU A 80 -32.646 31.883 7.806 1.00125.65 C ANISOU 54 CG LEU A 80 13538 18678 15524 -5617 6758 -4831 C ATOM 55 CD1 LEU A 80 -33.133 31.716 6.372 1.00129.85 C ANISOU 55 CD1 LEU A 80 14597 19467 15272 -6237 7150 -5251 C ATOM 56 CD2 LEU A 80 -32.351 30.505 8.465 1.00126.69 C ANISOU 56 CD2 LEU A 80 13208 18372 16556 -5168 7122 -5043 C ATOM 57 N ARG A 81 -32.663 33.462 10.608 1.00125.21 N ANISOU 57 N ARG A 81 13054 18523 15997 -4685 5220 -3683 N ATOM 58 CA ARG A 81 -33.233 33.052 11.869 1.00121.15 C ANISOU 58 CA ARG A 81 12402 17824 15808 -4175 4768 -3433 C ATOM 59 C ARG A 81 -34.749 33.118 11.824 1.00117.76 C ANISOU 59 C ARG A 81 12422 17508 14813 -4216 4391 -3373 C ATOM 60 O ARG A 81 -35.316 34.078 11.292 1.00116.85 O ANISOU 60 O ARG A 81 12691 17653 14054 -4488 4097 -3251 O ATOM 61 CB ARG A 81 -32.692 33.938 12.968 1.00118.90 C ANISOU 61 CB ARG A 81 11886 17543 15748 -3911 4246 -3017 C ATOM 62 CG ARG A 81 -32.644 35.426 12.565 1.00118.32 C ANISOU 62 CG ARG A 81 12123 17706 15128 -4262 3971 -2832 C ATOM 63 CD ARG A 81 -32.527 36.272 13.813 1.00115.37 C ANISOU 63 CD ARG A 81 11654 17304 14878 -3994 3355 -2448 C ATOM 64 NE ARG A 81 -32.460 37.696 13.557 1.00115.24 N ANISOU 64 NE ARG A 81 11942 17408 14435 -4297 3107 -2262 N ATOM 65 CZ ARG A 81 -32.500 38.609 14.517 1.00113.06 C ANISOU 65 CZ ARG A 81 11718 17096 14142 -4158 2586 -1977 C ATOM 66 NH1 ARG A 81 -32.596 38.244 15.787 1.00110.87 N ANISOU 66 NH1 ARG A 81 11217 16726 14183 -3742 2243 -1842 N ATOM 67 NH2 ARG A 81 -32.440 39.893 14.203 1.00113.68 N ANISOU 67 NH2 ARG A 81 12121 17209 13865 -4459 2435 -1828 N ATOM 68 N PRO A 82 -35.398 32.100 12.416 1.00118.38 N ANISOU 68 N PRO A 82 12429 17375 15176 -3930 4396 -3430 N ATOM 69 CA PRO A 82 -36.815 31.818 12.229 1.00116.72 C ANISOU 69 CA PRO A 82 12535 17259 14555 -4028 4217 -3518 C ATOM 70 C PRO A 82 -37.589 32.903 12.855 1.00112.55 C ANISOU 70 C PRO A 82 12192 16902 13670 -3888 3534 -3117 C ATOM 71 O PRO A 82 -37.181 33.419 13.888 1.00110.28 O ANISOU 71 O PRO A 82 11755 16515 13630 -3572 3219 -2788 O ATOM 72 CB PRO A 82 -37.033 30.589 13.060 1.00116.50 C ANISOU 72 CB PRO A 82 12302 16869 15093 -3679 4388 -3568 C ATOM 73 CG PRO A 82 -36.058 30.789 14.241 1.00115.47 C ANISOU 73 CG PRO A 82 11824 16547 15503 -3223 4189 -3195 C ATOM 74 CD PRO A 82 -34.877 31.516 13.673 1.00117.70 C ANISOU 74 CD PRO A 82 11950 16978 15793 -3417 4327 -3221 C ATOM 75 N MET A 83 -38.709 33.229 12.257 1.00102.48 N ANISOU 75 N MET A 83 11223 15882 11832 -4115 3300 -3158 N ATOM 76 CA MET A 83 -39.438 34.419 12.639 1.00 99.61 C ANISOU 76 CA MET A 83 11051 15684 11112 -3999 2687 -2789 C ATOM 77 C MET A 83 -40.350 34.007 13.758 1.00 96.64 C ANISOU 77 C MET A 83 10570 15172 10977 -3641 2447 -2677 C ATOM 78 O MET A 83 -40.467 32.817 14.047 1.00 97.20 O ANISOU 78 O MET A 83 10484 15047 11401 -3561 2758 -2883 O ATOM 79 CB MET A 83 -40.179 34.955 11.446 1.00101.75 C ANISOU 79 CB MET A 83 11654 16304 10702 -4369 2525 -2841 C ATOM 80 CG MET A 83 -41.579 35.382 11.655 1.00100.25 C ANISOU 80 CG MET A 83 11574 16286 10230 -4241 2008 -2664 C ATOM 81 SD MET A 83 -41.510 37.101 11.994 1.00 98.69 S ANISOU 81 SD MET A 83 11586 16095 9816 -4059 1494 -2155 S ATOM 82 CE MET A 83 -41.220 37.804 10.362 1.00103.48 C ANISOU 82 CE MET A 83 12590 16997 9730 -4561 1532 -2129 C ATOM 83 N THR A 84 -40.958 34.972 14.430 1.00 87.45 N ANISOU 83 N THR A 84 9507 14062 9659 -3424 1955 -2355 N ATOM 84 CA THR A 84 -41.587 34.676 15.685 1.00 84.93 C ANISOU 84 CA THR A 84 9084 13578 9608 -3067 1793 -2224 C ATOM 85 C THR A 84 -42.464 35.812 16.075 1.00 83.23 C ANISOU 85 C THR A 84 9023 13475 9124 -2916 1315 -1966 C ATOM 86 O THR A 84 -42.294 36.916 15.533 1.00 83.83 O ANISOU 86 O THR A 84 9286 13673 8894 -3025 1090 -1815 O ATOM 87 CB THR A 84 -40.527 34.516 16.728 1.00 84.03 C ANISOU 87 CB THR A 84 8802 13207 9918 -2799 1853 -2064 C ATOM 88 OG1 THR A 84 -39.823 35.757 16.917 1.00 83.44 O ANISOU 88 OG1 THR A 84 8802 13177 9726 -2788 1577 -1833 O ATOM 89 CG2 THR A 84 -39.516 33.457 16.295 1.00 86.65 C ANISOU 89 CG2 THR A 84 8921 13388 10616 -2888 2350 -2294 C ATOM 90 N TYR A 85 -43.386 35.565 17.014 1.00 78.48 N ANISOU 90 N TYR A 85 8360 12798 8659 -2664 1202 -1911 N ATOM 91 CA TYR A 85 -44.454 36.542 17.277 1.00 77.79 C ANISOU 91 CA TYR A 85 8371 12823 8363 -2510 816 -1739 C ATOM 92 C TYR A 85 -43.801 37.814 17.597 1.00 77.02 C ANISOU 92 C TYR A 85 8451 12639 8173 -2404 569 -1479 C ATOM 93 O TYR A 85 -44.185 38.849 17.048 1.00 78.03 O ANISOU 93 O TYR A 85 8748 12871 8029 -2433 301 -1339 O ATOM 94 CB TYR A 85 -45.348 36.204 18.479 1.00 76.52 C ANISOU 94 CB TYR A 85 8116 12545 8414 -2232 808 -1708 C ATOM 95 CG TYR A 85 -46.267 37.348 18.928 1.00 76.25 C ANISOU 95 CG TYR A 85 8158 12556 8257 -2004 467 -1530 C ATOM 96 CD1 TYR A 85 -47.524 37.524 18.373 1.00 77.99 C ANISOU 96 CD1 TYR A 85 8265 13005 8364 -2018 300 -1588 C ATOM 97 CD2 TYR A 85 -45.852 38.229 19.899 1.00 75.00 C ANISOU 97 CD2 TYR A 85 8162 12208 8125 -1779 323 -1328 C ATOM 98 CE1 TYR A 85 -48.330 38.542 18.764 1.00 78.53 C ANISOU 98 CE1 TYR A 85 8351 13073 8412 -1754 31 -1426 C ATOM 99 CE2 TYR A 85 -46.632 39.266 20.298 1.00 75.40 C ANISOU 99 CE2 TYR A 85 8303 12230 8113 -1562 93 -1208 C ATOM 100 CZ TYR A 85 -47.877 39.443 19.733 1.00 77.18 C ANISOU 100 CZ TYR A 85 8390 12644 8291 -1515 -41 -1242 C ATOM 101 OH TYR A 85 -48.645 40.536 20.175 1.00 78.29 O ANISOU 101 OH TYR A 85 8587 12702 8458 -1226 -245 -1110 O ATOM 102 N LYS A 86 -42.826 37.744 18.498 1.00 77.32 N ANISOU 102 N LYS A 86 8455 12478 8446 -2284 640 -1402 N ATOM 103 CA LYS A 86 -42.213 38.948 18.933 1.00 77.03 C ANISOU 103 CA LYS A 86 8579 12346 8341 -2229 406 -1203 C ATOM 104 C LYS A 86 -41.435 39.623 17.812 1.00 78.77 C ANISOU 104 C LYS A 86 8914 12642 8372 -2528 418 -1176 C ATOM 105 O LYS A 86 -41.493 40.844 17.682 1.00 79.44 O ANISOU 105 O LYS A 86 9237 12680 8267 -2548 191 -1004 O ATOM 106 CB LYS A 86 -41.315 38.689 20.085 1.00 76.37 C ANISOU 106 CB LYS A 86 8401 12107 8509 -2090 425 -1143 C ATOM 107 CG LYS A 86 -40.597 39.937 20.568 1.00 76.73 C ANISOU 107 CG LYS A 86 8603 12068 8484 -2112 179 -1000 C ATOM 108 CD LYS A 86 -41.426 40.806 21.459 1.00 76.13 C ANISOU 108 CD LYS A 86 8764 11884 8278 -1907 -55 -908 C ATOM 109 CE LYS A 86 -40.522 41.885 22.084 1.00 77.15 C ANISOU 109 CE LYS A 86 9046 11889 8377 -1985 -253 -833 C ATOM 110 NZ LYS A 86 -39.109 41.487 22.494 1.00 78.13 N ANISOU 110 NZ LYS A 86 8942 12055 8690 -2101 -254 -840 N ATOM 111 N ALA A 87 -40.712 38.857 17.004 1.00 75.85 N ANISOU 111 N ALA A 87 8405 12354 8060 -2770 730 -1349 N ATOM 112 CA ALA A 87 -40.061 39.420 15.807 1.00 78.28 C ANISOU 112 CA ALA A 87 8856 12766 8121 -3120 831 -1352 C ATOM 113 C ALA A 87 -41.069 40.190 14.963 1.00 79.59 C ANISOU 113 C ALA A 87 9322 13082 7838 -3204 583 -1223 C ATOM 114 O ALA A 87 -40.963 41.400 14.751 1.00 80.76 O ANISOU 114 O ALA A 87 9740 13165 7782 -3255 379 -987 O ATOM 115 CB ALA A 87 -39.441 38.318 14.982 1.00 80.15 C ANISOU 115 CB ALA A 87 8912 13088 8455 -3367 1282 -1637 C ATOM 116 N ALA A 88 -42.076 39.486 14.505 1.00 75.53 N ANISOU 116 N ALA A 88 8753 12754 7190 -3213 581 -1362 N ATOM 117 CA ALA A 88 -43.123 40.168 13.831 1.00 77.38 C ANISOU 117 CA ALA A 88 9189 13169 7041 -3221 249 -1202 C ATOM 118 C ALA A 88 -43.516 41.432 14.619 1.00 76.51 C ANISOU 118 C ALA A 88 9230 12851 6990 -2893 -110 -882 C ATOM 119 O ALA A 88 -43.432 42.524 14.097 1.00 78.70 O ANISOU 119 O ALA A 88 9802 13082 7017 -2954 -297 -625 O ATOM 120 CB ALA A 88 -44.291 39.243 13.636 1.00 77.80 C ANISOU 120 CB ALA A 88 9049 13444 7067 -3201 218 -1408 C ATOM 121 N LEU A 89 -43.903 41.282 15.879 1.00 75.39 N ANISOU 121 N LEU A 89 8927 12545 7172 -2565 -155 -904 N ATOM 122 CA LEU A 89 -44.284 42.424 16.702 1.00 75.07 C ANISOU 122 CA LEU A 89 9041 12273 7209 -2263 -412 -683 C ATOM 123 C LEU A 89 -43.212 43.509 16.684 1.00 75.98 C ANISOU 123 C LEU A 89 9437 12161 7270 -2400 -434 -514 C ATOM 124 O LEU A 89 -43.501 44.680 16.454 1.00 78.07 O ANISOU 124 O LEU A 89 9984 12274 7405 -2328 -645 -273 O ATOM 125 CB LEU A 89 -44.553 42.019 18.165 1.00 72.52 C ANISOU 125 CB LEU A 89 8555 11798 7200 -1977 -348 -784 C ATOM 126 CG LEU A 89 -45.231 43.100 19.027 1.00 72.91 C ANISOU 126 CG LEU A 89 8758 11623 7321 -1653 -550 -644 C ATOM 127 CD1 LEU A 89 -46.673 43.327 18.565 1.00 74.93 C ANISOU 127 CD1 LEU A 89 8921 12012 7538 -1445 -741 -575 C ATOM 128 CD2 LEU A 89 -45.206 42.790 20.484 1.00 71.07 C ANISOU 128 CD2 LEU A 89 8471 11241 7291 -1467 -437 -750 C ATOM 129 N ASP A 90 -41.974 43.127 16.946 1.00 88.39 N ANISOU 129 N ASP A 90 10911 13686 8986 -2594 -208 -635 N ATOM 130 CA ASP A 90 -40.878 44.106 17.022 1.00 89.69 C ANISOU 130 CA ASP A 90 11269 13652 9159 -2787 -202 -528 C ATOM 131 C ASP A 90 -40.631 44.833 15.693 1.00 93.04 C ANISOU 131 C ASP A 90 11989 14103 9257 -3096 -178 -358 C ATOM 132 O ASP A 90 -40.399 46.052 15.675 1.00 95.07 O ANISOU 132 O ASP A 90 12566 14112 9445 -3159 -285 -151 O ATOM 133 CB ASP A 90 -39.571 43.443 17.511 1.00 88.91 C ANISOU 133 CB ASP A 90 10883 13567 9331 -2938 18 -703 C ATOM 134 CG ASP A 90 -39.519 43.272 19.019 1.00 87.01 C ANISOU 134 CG ASP A 90 10512 13213 9336 -2675 -106 -747 C ATOM 135 OD1 ASP A 90 -40.117 44.087 19.726 1.00 86.85 O ANISOU 135 OD1 ASP A 90 10714 13019 9265 -2489 -313 -662 O ATOM 136 OD2 ASP A 90 -38.856 42.337 19.495 1.00 86.35 O ANISOU 136 OD2 ASP A 90 10122 13200 9487 -2653 14 -858 O ATOM 137 N ILE A 91 -40.669 44.081 14.597 1.00 93.69 N ANISOU 137 N ILE A 91 12011 14465 9119 -3317 -9 -451 N ATOM 138 CA ILE A 91 -40.561 44.694 13.288 1.00 97.58 C ANISOU 138 CA ILE A 91 12849 15038 9187 -3629 8 -267 C ATOM 139 C ILE A 91 -41.751 45.590 13.084 1.00 99.38 C ANISOU 139 C ILE A 91 13366 15202 9192 -3371 -398 60 C ATOM 140 O ILE A 91 -41.627 46.698 12.585 1.00102.70 O ANISOU 140 O ILE A 91 14185 15443 9395 -3469 -503 372 O ATOM 141 CB ILE A 91 -40.533 43.670 12.158 1.00 99.16 C ANISOU 141 CB ILE A 91 12971 15592 9111 -3929 258 -477 C ATOM 142 CG1 ILE A 91 -39.183 42.962 12.156 1.00 98.96 C ANISOU 142 CG1 ILE A 91 12691 15569 9340 -4204 737 -768 C ATOM 143 CG2 ILE A 91 -40.771 44.353 10.807 1.00103.96 C ANISOU 143 CG2 ILE A 91 14027 16343 9129 -4211 163 -221 C ATOM 144 CD1 ILE A 91 -39.133 41.798 11.169 1.00100.69 C ANISOU 144 CD1 ILE A 91 12808 16078 9373 -4483 1091 -1081 C ATOM 145 N SER A 92 -42.915 45.097 13.475 1.00105.00 N ANISOU 145 N SER A 92 13857 16041 9997 -3033 -610 -1 N ATOM 146 CA SER A 92 -44.128 45.840 13.249 1.00107.46 C ANISOU 146 CA SER A 92 14322 16339 10171 -2734 -1008 295 C ATOM 147 C SER A 92 -43.934 47.192 13.891 1.00108.36 C ANISOU 147 C SER A 92 14730 15981 10461 -2539 -1112 551 C ATOM 148 O SER A 92 -44.260 48.207 13.316 1.00112.34 O ANISOU 148 O SER A 92 15581 16328 10775 -2471 -1330 915 O ATOM 149 CB SER A 92 -45.362 45.122 13.817 1.00105.70 C ANISOU 149 CB SER A 92 13713 16290 10158 -2388 -1160 135 C ATOM 150 OG SER A 92 -45.295 43.712 13.629 1.00103.93 O ANISOU 150 OG SER A 92 13183 16373 9933 -2599 -926 -221 O ATOM 151 N HIS A 93 -43.358 47.213 15.071 1.00131.48 N ANISOU 151 N HIS A 93 17553 18665 13738 -2472 -953 364 N ATOM 152 CA HIS A 93 -43.173 48.478 15.755 1.00132.77 C ANISOU 152 CA HIS A 93 18015 18360 14072 -2338 -1019 520 C ATOM 153 C HIS A 93 -42.209 49.378 15.047 1.00136.12 C ANISOU 153 C HIS A 93 18839 18567 14313 -2713 -918 728 C ATOM 154 O HIS A 93 -42.438 50.572 14.911 1.00139.66 O ANISOU 154 O HIS A 93 19682 18642 14740 -2614 -1042 1026 O ATOM 155 CB HIS A 93 -42.576 48.258 17.122 1.00129.58 C ANISOU 155 CB HIS A 93 17441 17813 13983 -2310 -875 236 C ATOM 156 CG HIS A 93 -42.723 49.435 18.028 1.00131.04 C ANISOU 156 CG HIS A 93 17903 17535 14350 -2113 -951 293 C ATOM 157 ND1 HIS A 93 -42.276 50.699 17.700 1.00134.76 N ANISOU 157 ND1 HIS A 93 18808 17615 14780 -2273 -954 505 N ATOM 158 CD2 HIS A 93 -43.277 49.532 19.260 1.00129.86 C ANISOU 158 CD2 HIS A 93 17698 17225 14419 -1797 -976 135 C ATOM 159 CE1 HIS A 93 -42.554 51.527 18.694 1.00135.81 C ANISOU 159 CE1 HIS A 93 19134 17341 15128 -2053 -980 448 C ATOM 160 NE2 HIS A 93 -43.156 50.846 19.654 1.00132.90 N ANISOU 160 NE2 HIS A 93 18477 17124 14897 -1767 -988 213 N ATOM 161 N PHE A 94 -41.098 48.781 14.644 1.00115.81 N ANISOU 161 N PHE A 94 16149 16194 11661 -3144 -641 555 N ATOM 162 CA PHE A 94 -39.958 49.510 14.097 1.00118.98 C ANISOU 162 CA PHE A 94 16847 16410 11952 -3598 -427 664 C ATOM 163 C PHE A 94 -40.299 50.280 12.848 1.00124.00 C ANISOU 163 C PHE A 94 17969 16978 12168 -3721 -513 1078 C ATOM 164 O PHE A 94 -39.765 51.343 12.624 1.00127.65 O ANISOU 164 O PHE A 94 18838 17078 12584 -3944 -426 1302 O ATOM 165 CB PHE A 94 -38.828 48.527 13.792 1.00117.85 C ANISOU 165 CB PHE A 94 16373 16571 11835 -3996 -71 367 C ATOM 166 CG PHE A 94 -37.715 49.098 12.983 1.00121.86 C ANISOU 166 CG PHE A 94 17121 16992 12189 -4526 232 450 C ATOM 167 CD1 PHE A 94 -36.668 49.716 13.590 1.00122.84 C ANISOU 167 CD1 PHE A 94 17218 16855 12600 -4773 376 360 C ATOM 168 CD2 PHE A 94 -37.713 48.983 11.619 1.00125.23 C ANISOU 168 CD2 PHE A 94 17794 17628 12161 -4823 392 591 C ATOM 169 CE1 PHE A 94 -35.654 50.215 12.861 1.00126.97 C ANISOU 169 CE1 PHE A 94 17918 17302 13023 -5299 706 410 C ATOM 170 CE2 PHE A 94 -36.695 49.478 10.880 1.00129.41 C ANISOU 170 CE2 PHE A 94 18559 18080 12531 -5345 745 657 C ATOM 171 CZ PHE A 94 -35.668 50.095 11.498 1.00130.24 C ANISOU 171 CZ PHE A 94 18597 17900 12987 -5582 921 567 C ATOM 172 N LEU A 95 -41.165 49.722 12.026 1.00109.32 N ANISOU 172 N LEU A 95 16079 15475 9982 -3610 -687 1182 N ATOM 173 CA LEU A 95 -41.564 50.390 10.818 1.00114.87 C ANISOU 173 CA LEU A 95 17256 16187 10205 -3703 -854 1627 C ATOM 174 C LEU A 95 -42.644 51.414 11.136 1.00117.31 C ANISOU 174 C LEU A 95 17793 16138 10642 -3182 -1263 2015 C ATOM 175 O LEU A 95 -42.588 52.543 10.650 1.00122.43 O ANISOU 175 O LEU A 95 18963 16421 11135 -3218 -1334 2453 O ATOM 176 CB LEU A 95 -42.026 49.373 9.782 1.00115.77 C ANISOU 176 CB LEU A 95 17244 16880 9863 -3849 -912 1554 C ATOM 177 CG LEU A 95 -40.938 48.386 9.362 1.00114.53 C ANISOU 177 CG LEU A 95 16900 17014 9600 -4364 -420 1153 C ATOM 178 CD1 LEU A 95 -41.467 47.387 8.378 1.00115.98 C ANISOU 178 CD1 LEU A 95 17006 17734 9327 -4529 -451 1012 C ATOM 179 CD2 LEU A 95 -39.764 49.103 8.764 1.00118.38 C ANISOU 179 CD2 LEU A 95 17786 17301 9893 -4865 -59 1297 C ATOM 180 N LYS A 96 -43.615 51.036 11.964 1.00124.78 N ANISOU 180 N LYS A 96 18354 17146 11909 -2693 -1487 1860 N ATOM 181 CA LYS A 96 -44.679 51.956 12.359 1.00127.42 C ANISOU 181 CA LYS A 96 18808 17129 12477 -2138 -1817 2166 C ATOM 182 C LYS A 96 -44.053 53.268 12.801 1.00129.91 C ANISOU 182 C LYS A 96 19590 16760 13010 -2176 -1664 2341 C ATOM 183 O LYS A 96 -44.520 54.342 12.439 1.00135.32 O ANISOU 183 O LYS A 96 20682 17050 13682 -1937 -1856 2799 O ATOM 184 CB LYS A 96 -45.522 51.347 13.497 1.00123.22 C ANISOU 184 CB LYS A 96 17759 16690 12370 -1697 -1887 1832 C ATOM 185 CG LYS A 96 -46.719 52.195 13.963 1.00126.31 C ANISOU 185 CG LYS A 96 18160 16745 13089 -1073 -2162 2070 C ATOM 186 CD LYS A 96 -47.051 52.013 15.461 1.00122.52 C ANISOU 186 CD LYS A 96 17372 16083 13098 -764 -1998 1678 C ATOM 187 CE LYS A 96 -47.128 53.382 16.191 1.00125.72 C ANISOU 187 CE LYS A 96 18146 15770 13853 -468 -1932 1803 C ATOM 188 NZ LYS A 96 -45.810 54.145 16.231 1.00126.55 N ANISOU 188 NZ LYS A 96 18749 15450 13885 -910 -1691 1824 N ATOM 189 N GLU A 97 -42.985 53.160 13.578 1.00151.62 N ANISOU 189 N GLU A 97 22270 19367 15973 -2488 -1327 1976 N ATOM 190 CA GLU A 97 -42.300 54.321 14.114 1.00153.97 C ANISOU 190 CA GLU A 97 22961 19039 16501 -2626 -1148 2019 C ATOM 191 C GLU A 97 -41.521 55.048 13.040 1.00159.11 C ANISOU 191 C GLU A 97 24133 19486 16837 -3092 -993 2370 C ATOM 192 O GLU A 97 -41.654 56.270 12.872 1.00164.42 O ANISOU 192 O GLU A 97 25331 19580 17560 -3011 -1022 2744 O ATOM 193 CB GLU A 97 -41.337 53.900 15.229 1.00149.58 C ANISOU 193 CB GLU A 97 22111 18505 16217 -2886 -895 1507 C ATOM 194 CG GLU A 97 -40.848 55.038 16.109 1.00151.83 C ANISOU 194 CG GLU A 97 22720 18170 16800 -2974 -768 1421 C ATOM 195 CD GLU A 97 -41.988 55.768 16.810 1.00153.56 C ANISOU 195 CD GLU A 97 23108 17948 17289 -2394 -928 1502 C ATOM 196 OE1 GLU A 97 -43.163 55.325 16.675 1.00152.66 O ANISOU 196 OE1 GLU A 97 22764 18066 17175 -1903 -1154 1617 O ATOM 197 OE2 GLU A 97 -41.708 56.791 17.490 1.00156.41 O ANISOU 197 OE2 GLU A 97 23815 17723 17890 -2450 -798 1419 O ATOM 198 N LYS A 98 -40.701 54.287 12.320 1.00150.03 N ANISOU 198 N LYS A 98 22853 18775 15377 -3588 -775 2241 N ATOM 199 CA LYS A 98 -39.911 54.818 11.213 1.00155.19 C ANISOU 199 CA LYS A 98 23979 19327 15658 -4117 -539 2536 C ATOM 200 C LYS A 98 -40.802 55.549 10.222 1.00161.34 C ANISOU 200 C LYS A 98 25290 19948 16062 -3883 -842 3177 C ATOM 201 O LYS A 98 -40.348 56.463 9.534 1.00167.26 O ANISOU 201 O LYS A 98 26632 20333 16584 -4191 -693 3572 O ATOM 202 CB LYS A 98 -39.179 53.689 10.491 1.00153.51 C ANISOU 202 CB LYS A 98 23480 19710 15135 -4586 -261 2272 C ATOM 203 CG LYS A 98 -38.324 54.139 9.318 1.00159.23 C ANISOU 203 CG LYS A 98 24679 20391 15430 -5198 80 2521 C ATOM 204 CD LYS A 98 -37.496 52.981 8.767 1.00157.63 C ANISOU 204 CD LYS A 98 24116 20740 15037 -5663 471 2132 C ATOM 205 CE LYS A 98 -36.377 53.462 7.839 1.00163.36 C ANISOU 205 CE LYS A 98 25236 21371 15463 -6365 978 2252 C ATOM 206 NZ LYS A 98 -35.152 52.598 7.918 1.00161.45 N ANISOU 206 NZ LYS A 98 24463 21428 15451 -6811 1499 1713 N ATOM 207 N GLY A 99 -42.070 55.146 10.142 1.00177.35 N ANISOU 207 N GLY A 99 27097 22257 18031 -3346 -1277 3304 N ATOM 208 CA GLY A 99 -43.021 55.802 9.250 1.00183.88 C ANISOU 208 CA GLY A 99 28335 22996 18536 -3031 -1684 3950 C ATOM 209 C GLY A 99 -42.791 55.343 7.826 1.00187.39 C ANISOU 209 C GLY A 99 29018 23955 18228 -3481 -1686 4171 C ATOM 210 O GLY A 99 -42.008 54.416 7.585 1.00184.20 O ANISOU 210 O GLY A 99 28381 23983 17622 -3976 -1343 3752 O ATOM 211 N GLY A 100 -43.463 55.990 6.880 1.00187.87 N ANISOU 211 N GLY A 100 29554 23963 17863 -3307 -2063 4833 N ATOM 212 CA GLY A 100 -43.407 55.550 5.493 1.00192.26 C ANISOU 212 CA GLY A 100 30390 25078 17583 -3722 -2142 5069 C ATOM 213 C GLY A 100 -43.814 54.088 5.374 1.00187.58 C ANISOU 213 C GLY A 100 29173 25291 16810 -3768 -2257 4563 C ATOM 214 O GLY A 100 -43.008 53.219 5.012 1.00185.25 O ANISOU 214 O GLY A 100 28765 25384 16239 -4330 -1835 4131 O ATOM 215 N LEU A 101 -45.057 53.813 5.742 1.00189.51 N ANISOU 215 N LEU A 101 28975 25739 17292 -3173 -2774 4575 N ATOM 216 CA LEU A 101 -45.698 52.555 5.397 1.00187.59 C ANISOU 216 CA LEU A 101 28235 26261 16779 -3211 -3002 4231 C ATOM 217 C LEU A 101 -47.193 52.725 5.590 1.00189.95 C ANISOU 217 C LEU A 101 28196 26674 17301 -2515 -3680 4505 C ATOM 218 O LEU A 101 -47.967 52.501 4.662 1.00195.31 O ANISOU 218 O LEU A 101 28886 27873 17451 -2496 -4182 4776 O ATOM 219 CB LEU A 101 -45.163 51.398 6.234 1.00179.04 C ANISOU 219 CB LEU A 101 26567 25357 16103 -3397 -2545 3445 C ATOM 220 CG LEU A 101 -45.352 50.019 5.599 1.00178.02 C ANISOU 220 CG LEU A 101 26118 25962 15558 -3734 -2525 3020 C ATOM 221 CD1 LEU A 101 -44.514 49.877 4.343 1.00182.52 C ANISOU 221 CD1 LEU A 101 27192 26797 15359 -4427 -2221 3067 C ATOM 222 CD2 LEU A 101 -45.011 48.905 6.599 1.00169.95 C ANISOU 222 CD2 LEU A 101 24482 25005 15087 -3750 -2131 2316 C ATOM 223 N GLU A 102 -47.590 53.142 6.792 1.00179.07 N ANISOU 223 N GLU A 102 26511 24826 16702 -1963 -3688 4421 N ATOM 224 CA GLU A 102 -48.979 53.521 7.060 1.00182.35 C ANISOU 224 CA GLU A 102 26601 25215 17470 -1232 -4257 4717 C ATOM 225 C GLU A 102 -49.515 54.422 5.937 1.00192.43 C ANISOU 225 C GLU A 102 28367 26477 18271 -1040 -4818 5547 C ATOM 226 O GLU A 102 -49.031 55.547 5.737 1.00196.82 O ANISOU 226 O GLU A 102 29578 26417 18787 -1026 -4720 6049 O ATOM 227 CB GLU A 102 -49.087 54.252 8.404 1.00179.62 C ANISOU 227 CB GLU A 102 26139 24146 17965 -724 -4055 4626 C ATOM 228 CG GLU A 102 -50.514 54.633 8.822 1.00183.07 C ANISOU 228 CG GLU A 102 26152 24497 18911 77 -4522 4846 C ATOM 229 CD GLU A 102 -51.288 53.461 9.410 1.00178.22 C ANISOU 229 CD GLU A 102 24712 24429 18576 218 -4574 4287 C ATOM 230 OE1 GLU A 102 -50.844 52.308 9.252 1.00173.35 O ANISOU 230 OE1 GLU A 102 23894 24322 17651 -295 -4364 3824 O ATOM 231 OE2 GLU A 102 -52.340 53.680 10.045 1.00179.71 O ANISOU 231 OE2 GLU A 102 24447 24505 19330 835 -4774 4294 O ATOM 232 N GLY A 103 -50.502 53.912 5.201 1.00201.51 N ANISOU 232 N GLY A 103 29209 28308 19047 -922 -5415 5699 N ATOM 233 CA GLY A 103 -51.104 54.652 4.103 1.00211.98 C ANISOU 233 CA GLY A 103 30938 29749 19855 -715 -6073 6521 C ATOM 234 C GLY A 103 -50.283 54.651 2.822 1.00216.53 C ANISOU 234 C GLY A 103 32268 30591 19411 -1432 -5992 6805 C ATOM 235 O GLY A 103 -50.527 55.474 1.931 1.00225.87 O ANISOU 235 O GLY A 103 34016 31703 20101 -1319 -6440 7600 O ATOM 236 N LEU A 104 -49.302 53.754 2.720 1.00181.41 N ANISOU 236 N LEU A 104 27858 26424 14648 -2156 -5399 6188 N ATOM 237 CA LEU A 104 -48.600 53.537 1.456 1.00186.01 C ANISOU 237 CA LEU A 104 29065 27397 14212 -2900 -5261 6321 C ATOM 238 C LEU A 104 -49.435 52.607 0.599 1.00189.82 C ANISOU 238 C LEU A 104 29260 28828 14036 -3075 -5809 6203 C ATOM 239 O LEU A 104 -50.064 51.686 1.097 1.00185.23 O ANISOU 239 O LEU A 104 27924 28637 13819 -2931 -5926 5654 O ATOM 240 CB LEU A 104 -47.211 52.931 1.670 1.00179.25 C ANISOU 240 CB LEU A 104 28300 26457 13348 -3587 -4362 5668 C ATOM 241 CG LEU A 104 -46.482 52.407 0.426 1.00183.19 C ANISOU 241 CG LEU A 104 29297 27462 12844 -4423 -4066 5570 C ATOM 242 CD1 LEU A 104 -46.442 53.462 -0.658 1.00193.68 C ANISOU 242 CD1 LEU A 104 31524 28668 13397 -4557 -4342 6448 C ATOM 243 CD2 LEU A 104 -45.074 51.966 0.769 1.00177.07 C ANISOU 243 CD2 LEU A 104 28530 26473 12277 -4984 -3134 4964 C ATOM 244 N ILE A 105 -49.445 52.867 -0.698 1.00212.02 N ANISOU 244 N ILE A 105 32709 32008 15841 -3425 -6143 6725 N ATOM 245 CA ILE A 105 -50.135 52.005 -1.640 1.00217.01 C ANISOU 245 CA ILE A 105 33179 33598 15678 -3735 -6664 6594 C ATOM 246 C ILE A 105 -49.346 50.705 -1.780 1.00211.21 C ANISOU 246 C ILE A 105 32318 33270 14661 -4516 -5956 5669 C ATOM 247 O ILE A 105 -48.152 50.722 -2.091 1.00210.26 O ANISOU 247 O ILE A 105 32736 32942 14211 -5092 -5241 5525 O ATOM 248 CB ILE A 105 -50.283 52.679 -3.029 1.00229.51 C ANISOU 248 CB ILE A 105 35598 35477 16128 -3957 -7211 7445 C ATOM 249 CG1 ILE A 105 -51.060 53.997 -2.921 1.00236.43 C ANISOU 249 CG1 ILE A 105 36624 35873 17337 -3114 -7923 8442 C ATOM 250 CG2 ILE A 105 -50.963 51.737 -4.012 1.00235.24 C ANISOU 250 CG2 ILE A 105 36171 37269 15941 -4375 -7764 7229 C ATOM 251 CD1 ILE A 105 -52.503 53.832 -2.524 1.00237.98 C ANISOU 251 CD1 ILE A 105 35933 36410 18077 -2375 -8763 8500 C ATOM 252 N TRP A 106 -50.017 49.581 -1.546 1.00217.26 N ANISOU 252 N TRP A 106 32354 34585 15610 -4532 -6119 5037 N ATOM 253 CA TRP A 106 -49.389 48.281 -1.701 1.00212.77 C ANISOU 253 CA TRP A 106 31641 34380 14823 -5223 -5474 4153 C ATOM 254 C TRP A 106 -48.916 48.039 -3.113 1.00220.48 C ANISOU 254 C TRP A 106 33334 35878 14559 -6024 -5369 4177 C ATOM 255 O TRP A 106 -49.384 48.661 -4.052 1.00230.12 O ANISOU 255 O TRP A 106 35054 37416 14967 -6055 -6011 4849 O ATOM 256 CB TRP A 106 -50.344 47.156 -1.329 1.00209.94 C ANISOU 256 CB TRP A 106 30439 34528 14803 -5127 -5744 3540 C ATOM 257 CG TRP A 106 -49.647 45.844 -1.293 1.00204.69 C ANISOU 257 CG TRP A 106 29609 34037 14126 -5741 -4978 2621 C ATOM 258 CD1 TRP A 106 -48.825 45.390 -0.312 1.00195.43 C ANISOU 258 CD1 TRP A 106 28161 32364 13730 -5718 -4195 2104 C ATOM 259 CD2 TRP A 106 -49.671 44.833 -2.292 1.00209.22 C ANISOU 259 CD2 TRP A 106 30316 35301 13878 -6467 -4901 2119 C ATOM 260 NE1 TRP A 106 -48.348 44.142 -0.625 1.00193.88 N ANISOU 260 NE1 TRP A 106 27883 32461 13323 -6323 -3626 1337 N ATOM 261 CE2 TRP A 106 -48.853 43.776 -1.839 1.00202.18 C ANISOU 261 CE2 TRP A 106 29197 34224 13400 -6813 -4005 1294 C ATOM 262 CE3 TRP A 106 -50.309 44.711 -3.518 1.00219.18 C ANISOU 262 CE3 TRP A 106 31873 37323 14084 -6866 -5513 2277 C ATOM 263 CZ2 TRP A 106 -48.652 42.618 -2.570 1.00204.71 C ANISOU 263 CZ2 TRP A 106 29591 35020 13170 -7528 -3631 595 C ATOM 264 CZ3 TRP A 106 -50.114 43.554 -4.246 1.00221.65 C ANISOU 264 CZ3 TRP A 106 32277 38170 13769 -7642 -5165 1544 C ATOM 265 CH2 TRP A 106 -49.291 42.521 -3.769 1.00214.38 C ANISOU 265 CH2 TRP A 106 31138 36977 13339 -7960 -4194 695 C ATOM 266 N SER A 107 -47.967 47.129 -3.237 1.00195.39 N ANISOU 266 N SER A 107 30214 32771 11255 -6661 -4529 3441 N ATOM 267 CA SER A 107 -47.566 46.617 -4.513 1.00202.29 C ANISOU 267 CA SER A 107 31660 34208 10993 -7491 -4300 3220 C ATOM 268 C SER A 107 -46.982 45.260 -4.273 1.00196.32 C ANISOU 268 C SER A 107 30520 33555 10519 -7946 -3493 2186 C ATOM 269 O SER A 107 -46.630 44.929 -3.155 1.00187.15 O ANISOU 269 O SER A 107 28808 31921 10379 -7632 -3046 1799 O ATOM 270 CB SER A 107 -46.486 47.490 -5.126 1.00206.59 C ANISOU 270 CB SER A 107 33098 34413 10985 -7862 -3822 3686 C ATOM 271 OG SER A 107 -45.263 46.777 -5.196 1.00203.09 O ANISOU 271 OG SER A 107 32740 33861 10562 -8476 -2759 2973 O ATOM 272 N GLN A 108 -46.843 44.486 -5.335 1.00232.59 N ANISOU 272 N GLN A 108 35451 38741 14183 -8696 -3280 1748 N ATOM 273 CA GLN A 108 -46.150 43.224 -5.237 1.00228.37 C ANISOU 273 CA GLN A 108 34667 38224 13880 -9176 -2386 766 C ATOM 274 C GLN A 108 -44.683 43.525 -4.982 1.00224.62 C ANISOU 274 C GLN A 108 34449 37139 13756 -9335 -1415 696 C ATOM 275 O GLN A 108 -44.054 42.905 -4.136 1.00216.86 O ANISOU 275 O GLN A 108 32966 35761 13669 -9221 -763 148 O ATOM 276 CB GLN A 108 -46.329 42.395 -6.521 1.00237.07 C ANISOU 276 CB GLN A 108 36165 40087 13825 -10002 -2339 291 C ATOM 277 CG GLN A 108 -45.762 40.985 -6.433 1.00233.64 C ANISOU 277 CG GLN A 108 35433 39649 13692 -10469 -1422 -791 C ATOM 278 CD GLN A 108 -45.797 40.431 -5.013 1.00222.64 C ANISOU 278 CD GLN A 108 33162 37736 13694 -9883 -1188 -1164 C ATOM 279 OE1 GLN A 108 -46.872 40.200 -4.443 1.00220.19 O ANISOU 279 OE1 GLN A 108 32283 37562 13817 -9467 -1824 -1160 O ATOM 280 NE2 GLN A 108 -44.618 40.239 -4.427 1.00216.60 N ANISOU 280 NE2 GLN A 108 32275 36387 13635 -9849 -281 -1460 N ATOM 281 N ARG A 109 -44.164 44.507 -5.713 1.00222.85 N ANISOU 281 N ARG A 109 34998 36846 12829 -9592 -1356 1295 N ATOM 282 CA ARG A 109 -42.761 44.902 -5.642 1.00221.35 C ANISOU 282 CA ARG A 109 35110 36141 12853 -9855 -439 1272 C ATOM 283 C ARG A 109 -42.434 45.588 -4.323 1.00212.90 C ANISOU 283 C ARG A 109 33605 34324 12962 -9187 -401 1545 C ATOM 284 O ARG A 109 -41.594 45.109 -3.561 1.00206.09 O ANISOU 284 O ARG A 109 32283 33096 12928 -9155 287 1028 O ATOM 285 CB ARG A 109 -42.430 45.835 -6.819 1.00231.59 C ANISOU 285 CB ARG A 109 37414 37575 13004 -10339 -444 1917 C ATOM 286 CG ARG A 109 -40.990 46.338 -6.854 1.00231.64 C ANISOU 286 CG ARG A 109 37775 37074 13164 -10699 527 1933 C ATOM 287 CD ARG A 109 -40.858 47.695 -7.544 1.00239.88 C ANISOU 287 CD ARG A 109 39733 37959 13452 -10845 308 2888 C ATOM 288 NE ARG A 109 -39.703 48.439 -7.029 1.00237.06 N ANISOU 288 NE ARG A 109 39441 36887 13743 -10870 1010 3036 N ATOM 289 CZ ARG A 109 -38.486 48.465 -7.575 1.00240.89 C ANISOU 289 CZ ARG A 109 40318 37271 13938 -11567 2004 2802 C ATOM 290 NH1 ARG A 109 -38.214 47.798 -8.700 1.00248.02 N ANISOU 290 NH1 ARG A 109 41668 38720 13847 -12321 2495 2400 N ATOM 291 NH2 ARG A 109 -37.527 49.180 -6.990 1.00238.20 N ANISOU 291 NH2 ARG A 109 39916 36280 14308 -11543 2538 2941 N ATOM 292 N ARG A 110 -43.093 46.715 -4.068 1.00208.48 N ANISOU 292 N ARG A 110 33206 33541 12465 -8656 -1148 2358 N ATOM 293 CA ARG A 110 -42.912 47.465 -2.820 1.00201.51 C ANISOU 293 CA ARG A 110 31980 31949 12637 -8021 -1181 2631 C ATOM 294 C ARG A 110 -42.832 46.557 -1.579 1.00191.34 C ANISOU 294 C ARG A 110 29803 30474 12425 -7685 -908 1943 C ATOM 295 O ARG A 110 -42.022 46.796 -0.680 1.00185.61 O ANISOU 295 O ARG A 110 28833 29211 12479 -7521 -461 1830 O ATOM 296 CB ARG A 110 -44.035 48.497 -2.644 1.00204.28 C ANISOU 296 CB ARG A 110 32434 32178 13004 -7370 -2148 3452 C ATOM 297 CG ARG A 110 -43.839 49.776 -3.441 1.00212.95 C ANISOU 297 CG ARG A 110 34428 33067 13414 -7506 -2320 4324 C ATOM 298 CD ARG A 110 -45.017 50.729 -3.265 1.00216.47 C ANISOU 298 CD ARG A 110 34915 33368 13965 -6773 -3298 5138 C ATOM 299 NE ARG A 110 -44.681 52.102 -3.649 1.00223.11 N ANISOU 299 NE ARG A 110 36563 33694 14516 -6749 -3342 6005 N ATOM 300 CZ ARG A 110 -45.568 53.075 -3.872 1.00229.80 C ANISOU 300 CZ ARG A 110 37717 34398 15198 -6223 -4146 6887 C ATOM 301 NH1 ARG A 110 -46.877 52.852 -3.755 1.00230.91 N ANISOU 301 NH1 ARG A 110 37356 34931 15449 -5660 -5019 7019 N ATOM 302 NH2 ARG A 110 -45.144 54.289 -4.222 1.00236.14 N ANISOU 302 NH2 ARG A 110 39322 34639 15763 -6255 -4064 7657 N ATOM 303 N GLN A 111 -43.670 45.523 -1.545 1.00177.52 N ANISOU 303 N GLN A 111 27593 29175 10683 -7616 -1188 1501 N ATOM 304 CA GLN A 111 -43.629 44.540 -0.475 1.00169.06 C ANISOU 304 CA GLN A 111 25755 27955 10527 -7362 -895 856 C ATOM 305 C GLN A 111 -42.343 43.725 -0.564 1.00167.19 C ANISOU 305 C GLN A 111 25457 27617 10450 -7856 85 208 C ATOM 306 O GLN A 111 -41.691 43.490 0.437 1.00160.60 O ANISOU 306 O GLN A 111 24177 26365 10477 -7623 493 -57 O ATOM 307 CB GLN A 111 -44.844 43.609 -0.529 1.00169.30 C ANISOU 307 CB GLN A 111 25360 28489 10478 -7265 -1376 529 C ATOM 308 CG GLN A 111 -45.149 42.907 0.794 1.00160.82 C ANISOU 308 CG GLN A 111 23510 27162 10433 -6793 -1305 120 C ATOM 309 CD GLN A 111 -45.892 41.588 0.609 1.00161.26 C ANISOU 309 CD GLN A 111 23173 27678 10421 -6997 -1353 -494 C ATOM 310 OE1 GLN A 111 -46.990 41.543 0.033 1.00166.37 O ANISOU 310 OE1 GLN A 111 23811 28833 10568 -7037 -2003 -375 O ATOM 311 NE2 GLN A 111 -45.291 40.502 1.096 1.00156.59 N ANISOU 311 NE2 GLN A 111 22242 26898 10356 -7132 -670 -1150 N ATOM 312 N GLU A 112 -41.979 43.289 -1.760 1.00177.82 N ANISOU 312 N GLU A 112 27241 29355 10966 -8533 464 -52 N ATOM 313 CA GLU A 112 -40.727 42.566 -1.945 1.00177.46 C ANISOU 313 CA GLU A 112 27146 29199 11082 -9006 1467 -668 C ATOM 314 C GLU A 112 -39.514 43.378 -1.503 1.00175.54 C ANISOU 314 C GLU A 112 26961 28423 11312 -8985 1961 -437 C ATOM 315 O GLU A 112 -38.575 42.800 -0.958 1.00171.65 O ANISOU 315 O GLU A 112 26029 27667 11523 -9008 2630 -915 O ATOM 316 CB GLU A 112 -40.548 42.145 -3.408 1.00186.36 C ANISOU 316 CB GLU A 112 28863 30836 11110 -9791 1823 -941 C ATOM 317 CG GLU A 112 -41.509 41.045 -3.852 1.00188.63 C ANISOU 317 CG GLU A 112 29012 31660 10996 -9979 1556 -1440 C ATOM 318 CD GLU A 112 -41.837 41.082 -5.323 1.00199.08 C ANISOU 318 CD GLU A 112 31075 33612 10955 -10650 1404 -1390 C ATOM 319 OE1 GLU A 112 -41.132 41.781 -6.086 1.00204.88 O ANISOU 319 OE1 GLU A 112 32471 34350 11025 -11065 1732 -1077 O ATOM 320 OE2 GLU A 112 -42.803 40.393 -5.704 1.00201.97 O ANISOU 320 OE2 GLU A 112 31361 34480 10897 -10796 964 -1678 O ATOM 321 N ILE A 113 -39.520 44.697 -1.738 1.00192.50 N ANISOU 321 N ILE A 113 29633 30401 13107 -8948 1637 289 N ATOM 322 CA ILE A 113 -38.398 45.554 -1.303 1.00191.34 C ANISOU 322 CA ILE A 113 29554 29723 13423 -8982 2087 510 C ATOM 323 C ILE A 113 -38.326 45.573 0.209 1.00182.51 C ANISOU 323 C ILE A 113 27745 28160 13442 -8362 1950 425 C ATOM 324 O ILE A 113 -37.315 45.169 0.782 1.00179.05 O ANISOU 324 O ILE A 113 26868 27492 13672 -8423 2544 10 O ATOM 325 CB ILE A 113 -38.499 47.000 -1.802 1.00197.16 C ANISOU 325 CB ILE A 113 31036 30274 13601 -9047 1755 1340 C ATOM 326 CG1 ILE A 113 -38.257 47.058 -3.314 1.00206.97 C ANISOU 326 CG1 ILE A 113 33063 31913 13662 -9782 2062 1447 C ATOM 327 CG2 ILE A 113 -37.479 47.873 -1.075 1.00194.82 C ANISOU 327 CG2 ILE A 113 30677 29356 13991 -9003 2137 1514 C ATOM 328 CD1 ILE A 113 -38.382 48.454 -3.903 1.00214.06 C ANISOU 328 CD1 ILE A 113 34798 32619 13916 -9871 1736 2343 C ATOM 329 N LEU A 114 -39.402 46.030 0.847 1.00155.80 N ANISOU 329 N LEU A 114 24253 24679 10265 -7768 1168 813 N ATOM 330 CA LEU A 114 -39.573 45.849 2.295 1.00147.66 C ANISOU 330 CA LEU A 114 22568 23327 10211 -7174 990 657 C ATOM 331 C LEU A 114 -39.057 44.455 2.672 1.00143.49 C ANISOU 331 C LEU A 114 21445 22911 10165 -7264 1523 -84 C ATOM 332 O LEU A 114 -38.029 44.302 3.310 1.00140.48 O ANISOU 332 O LEU A 114 20725 22247 10403 -7279 2000 -335 O ATOM 333 CB LEU A 114 -41.062 45.958 2.698 1.00146.00 C ANISOU 333 CB LEU A 114 22207 23226 10040 -6601 164 926 C ATOM 334 CG LEU A 114 -41.470 46.808 3.901 1.00141.78 C ANISOU 334 CG LEU A 114 21482 22222 10167 -5968 -248 1267 C ATOM 335 CD1 LEU A 114 -42.892 46.506 4.320 1.00139.93 C ANISOU 335 CD1 LEU A 114 20904 22186 10080 -5450 -881 1306 C ATOM 336 CD2 LEU A 114 -40.531 46.568 5.043 1.00135.64 C ANISOU 336 CD2 LEU A 114 20264 21080 10195 -5875 194 909 C ATOM 337 N ASP A 115 -39.747 43.437 2.193 1.00152.67 N ANISOU 337 N ASP A 115 22502 24491 11015 -7361 1450 -428 N ATOM 338 CA ASP A 115 -39.512 42.099 2.669 1.00148.75 C ANISOU 338 CA ASP A 115 21442 24017 11057 -7325 1859 -1078 C ATOM 339 C ASP A 115 -38.079 41.629 2.421 1.00150.12 C ANISOU 339 C ASP A 115 21513 24071 11453 -7731 2747 -1501 C ATOM 340 O ASP A 115 -37.589 40.763 3.130 1.00146.30 O ANISOU 340 O ASP A 115 20489 23413 11687 -7560 3112 -1919 O ATOM 341 CB ASP A 115 -40.545 41.112 2.072 1.00150.87 C ANISOU 341 CB ASP A 115 21684 24748 10890 -7459 1654 -1405 C ATOM 342 CG ASP A 115 -41.951 41.173 2.782 1.00147.54 C ANISOU 342 CG ASP A 115 20979 24391 10687 -6911 866 -1183 C ATOM 343 OD1 ASP A 115 -42.024 41.523 3.995 1.00141.85 O ANISOU 343 OD1 ASP A 115 19922 23302 10671 -6383 674 -1000 O ATOM 344 OD2 ASP A 115 -42.975 40.831 2.118 1.00151.23 O ANISOU 344 OD2 ASP A 115 21537 25307 10615 -7046 466 -1235 O ATOM 345 N LEU A 116 -37.394 42.187 1.435 1.00170.38 N ANISOU 345 N LEU A 116 24577 26716 13442 -8253 3117 -1382 N ATOM 346 CA LEU A 116 -36.012 41.764 1.184 1.00172.50 C ANISOU 346 CA LEU A 116 24682 26877 13983 -8646 4027 -1812 C ATOM 347 C LEU A 116 -35.078 42.422 2.185 1.00168.96 C ANISOU 347 C LEU A 116 23876 25991 14330 -8409 4142 -1637 C ATOM 348 O LEU A 116 -34.335 41.748 2.924 1.00165.83 O ANISOU 348 O LEU A 116 22853 25409 14744 -8233 4515 -2009 O ATOM 349 CB LEU A 116 -35.582 42.053 -0.258 1.00181.06 C ANISOU 349 CB LEU A 116 26429 28228 14138 -9367 4494 -1812 C ATOM 350 CG LEU A 116 -36.206 40.984 -1.159 1.00184.83 C ANISOU 350 CG LEU A 116 27086 29155 13985 -9686 4613 -2278 C ATOM 351 CD1 LEU A 116 -36.456 41.536 -2.536 1.00193.36 C ANISOU 351 CD1 LEU A 116 29019 30624 13827 -10274 4569 -2015 C ATOM 352 CD2 LEU A 116 -35.365 39.698 -1.183 1.00185.19 C ANISOU 352 CD2 LEU A 116 26674 29137 14551 -9874 5517 -3078 C ATOM 353 N TRP A 117 -35.156 43.742 2.230 1.00160.38 N ANISOU 353 N TRP A 117 23188 24730 13017 -8392 3779 -1055 N ATOM 354 CA TRP A 117 -34.366 44.539 3.147 1.00157.91 C ANISOU 354 CA TRP A 117 22630 24006 13363 -8238 3809 -864 C ATOM 355 C TRP A 117 -34.298 43.979 4.563 1.00150.82 C ANISOU 355 C TRP A 117 20994 22912 13397 -7690 3630 -1090 C ATOM 356 O TRP A 117 -33.309 44.180 5.256 1.00149.68 O ANISOU 356 O TRP A 117 20458 22533 13881 -7677 3868 -1178 O ATOM 357 CB TRP A 117 -34.952 45.932 3.178 1.00159.07 C ANISOU 357 CB TRP A 117 23328 23944 13168 -8116 3233 -190 C ATOM 358 CG TRP A 117 -34.352 46.807 4.158 1.00156.78 C ANISOU 358 CG TRP A 117 22859 23212 13497 -7957 3171 -4 C ATOM 359 CD1 TRP A 117 -33.031 47.046 4.348 1.00158.36 C ANISOU 359 CD1 TRP A 117 22817 23226 14127 -8291 3722 -183 C ATOM 360 CD2 TRP A 117 -35.042 47.614 5.073 1.00153.36 C ANISOU 360 CD2 TRP A 117 22480 22470 13321 -7465 2536 373 C ATOM 361 NE1 TRP A 117 -32.851 47.951 5.350 1.00156.06 N ANISOU 361 NE1 TRP A 117 22436 22540 14320 -8070 3427 46 N ATOM 362 CE2 TRP A 117 -34.082 48.322 5.812 1.00152.94 C ANISOU 362 CE2 TRP A 117 22257 22040 13816 -7556 2722 383 C ATOM 363 CE3 TRP A 117 -36.389 47.810 5.351 1.00151.17 C ANISOU 363 CE3 TRP A 117 22347 22198 12892 -6963 1845 673 C ATOM 364 CZ2 TRP A 117 -34.426 49.214 6.816 1.00150.40 C ANISOU 364 CZ2 TRP A 117 21977 21323 13844 -7185 2264 654 C ATOM 365 CZ3 TRP A 117 -36.737 48.687 6.361 1.00148.53 C ANISOU 365 CZ3 TRP A 117 22014 21457 12964 -6542 1425 954 C ATOM 366 CH2 TRP A 117 -35.759 49.380 7.084 1.00148.15 C ANISOU 366 CH2 TRP A 117 21867 21012 13410 -6666 1646 930 C ATOM 367 N ILE A 118 -35.341 43.276 4.987 1.00129.92 N ANISOU 367 N ILE A 118 18161 20382 10819 -7270 3206 -1177 N ATOM 368 CA ILE A 118 -35.373 42.711 6.329 1.00123.74 C ANISOU 368 CA ILE A 118 16764 19420 10831 -6755 3028 -1344 C ATOM 369 C ILE A 118 -34.560 41.438 6.389 1.00123.73 C ANISOU 369 C ILE A 118 16236 19459 11319 -6825 3632 -1887 C ATOM 370 O ILE A 118 -33.834 41.191 7.359 1.00121.17 O ANISOU 370 O ILE A 118 15383 18932 11722 -6580 3729 -1999 O ATOM 371 CB ILE A 118 -36.796 42.410 6.784 1.00119.99 C ANISOU 371 CB ILE A 118 16275 19030 10286 -6306 2424 -1243 C ATOM 372 CG1 ILE A 118 -37.582 43.701 6.869 1.00120.30 C ANISOU 372 CG1 ILE A 118 16741 18961 10006 -6122 1822 -692 C ATOM 373 CG2 ILE A 118 -36.787 41.768 8.123 1.00114.46 C ANISOU 373 CG2 ILE A 118 15011 18147 10331 -5837 2325 -1413 C ATOM 374 CD1 ILE A 118 -38.990 43.487 7.190 1.00117.91 C ANISOU 374 CD1 ILE A 118 16393 18778 9629 -5711 1263 -589 C ATOM 375 N TYR A 119 -34.709 40.611 5.357 1.00142.86 N ANISOU 375 N TYR A 119 18806 22137 13338 -7146 4023 -2226 N ATOM 376 CA TYR A 119 -33.987 39.346 5.303 1.00143.93 C ANISOU 376 CA TYR A 119 18480 22254 13952 -7206 4679 -2778 C ATOM 377 C TYR A 119 -32.527 39.652 5.312 1.00146.76 C ANISOU 377 C TYR A 119 18556 22470 14738 -7426 5227 -2868 C ATOM 378 O TYR A 119 -31.716 38.996 5.974 1.00145.91 O ANISOU 378 O TYR A 119 17821 22194 15424 -7202 5528 -3117 O ATOM 379 CB TYR A 119 -34.292 38.568 4.026 1.00148.86 C ANISOU 379 CB TYR A 119 19425 23165 13968 -7650 5109 -3176 C ATOM 380 CG TYR A 119 -33.459 37.309 3.893 1.00151.15 C ANISOU 380 CG TYR A 119 19275 23356 14801 -7731 5910 -3785 C ATOM 381 CD1 TYR A 119 -32.922 36.671 5.018 1.00147.67 C ANISOU 381 CD1 TYR A 119 18154 22607 15348 -7247 5997 -3898 C ATOM 382 CD2 TYR A 119 -33.238 36.728 2.656 1.00157.49 C ANISOU 382 CD2 TYR A 119 20355 24355 15128 -8269 6580 -4245 C ATOM 383 CE1 TYR A 119 -32.176 35.520 4.902 1.00150.55 C ANISOU 383 CE1 TYR A 119 18098 22820 16284 -7247 6724 -4410 C ATOM 384 CE2 TYR A 119 -32.496 35.558 2.538 1.00160.26 C ANISOU 384 CE2 TYR A 119 20297 24545 16048 -8305 7376 -4837 C ATOM 385 CZ TYR A 119 -31.966 34.958 3.662 1.00156.80 C ANISOU 385 CZ TYR A 119 19152 23757 16670 -7763 7443 -4900 C ATOM 386 OH TYR A 119 -31.220 33.797 3.563 1.00160.29 O ANISOU 386 OH TYR A 119 19161 23977 17765 -7722 8232 -5443 O ATOM 387 N HIS A 120 -32.211 40.667 4.539 1.00169.34 N ANISOU 387 N HIS A 120 21884 25402 17056 -7879 5349 -2639 N ATOM 388 CA HIS A 120 -30.861 41.076 4.381 1.00173.26 C ANISOU 388 CA HIS A 120 22167 25799 17865 -8213 5919 -2725 C ATOM 389 C HIS A 120 -30.312 41.573 5.697 1.00169.47 C ANISOU 389 C HIS A 120 21172 25060 18158 -7851 5586 -2529 C ATOM 390 O HIS A 120 -29.259 41.126 6.159 1.00170.41 O ANISOU 390 O HIS A 120 20628 25095 19025 -7788 5958 -2794 O ATOM 391 CB HIS A 120 -30.795 42.174 3.353 1.00178.54 C ANISOU 391 CB HIS A 120 23551 26558 17727 -8774 6041 -2425 C ATOM 392 CG HIS A 120 -29.570 42.107 2.522 1.00185.41 C ANISOU 392 CG HIS A 120 24358 27483 18607 -9358 6966 -2743 C ATOM 393 ND1 HIS A 120 -29.532 41.432 1.319 1.00190.97 N ANISOU 393 ND1 HIS A 120 25366 28440 18755 -9808 7601 -3123 N ATOM 394 CD2 HIS A 120 -28.322 42.598 2.733 1.00188.24 C ANISOU 394 CD2 HIS A 120 24343 27687 19491 -9593 7409 -2789 C ATOM 395 CE1 HIS A 120 -28.316 41.538 0.807 1.00196.97 C ANISOU 395 CE1 HIS A 120 25968 29182 19689 -10285 8443 -3376 C ATOM 396 NE2 HIS A 120 -27.564 42.243 1.641 1.00195.46 N ANISOU 396 NE2 HIS A 120 25336 28755 20177 -10166 8335 -3172 N ATOM 397 N THR A 121 -31.065 42.475 6.304 1.00125.47 N ANISOU 397 N THR A 121 15898 19372 12403 -7602 4867 -2077 N ATOM 398 CA THR A 121 -30.602 43.226 7.432 1.00123.05 C ANISOU 398 CA THR A 121 15300 18829 12626 -7394 4529 -1864 C ATOM 399 C THR A 121 -30.604 42.391 8.689 1.00118.21 C ANISOU 399 C THR A 121 14041 18149 12724 -6835 4260 -2015 C ATOM 400 O THR A 121 -29.634 42.401 9.418 1.00118.64 O ANISOU 400 O THR A 121 13546 18120 13411 -6775 4330 -2103 O ATOM 401 CB THR A 121 -31.513 44.415 7.623 1.00121.35 C ANISOU 401 CB THR A 121 15679 18467 11960 -7292 3905 -1370 C ATOM 402 OG1 THR A 121 -31.305 45.351 6.558 1.00126.88 O ANISOU 402 OG1 THR A 121 16987 19153 12069 -7824 4155 -1138 O ATOM 403 CG2 THR A 121 -31.255 45.066 8.946 1.00118.27 C ANISOU 403 CG2 THR A 121 15016 17821 12102 -7014 3491 -1219 C ATOM 404 N GLN A 122 -31.693 41.648 8.898 1.00117.58 N ANISOU 404 N GLN A 122 14031 18127 12516 -6459 3959 -2039 N ATOM 405 CA GLN A 122 -32.026 41.013 10.181 1.00112.63 C ANISOU 405 CA GLN A 122 12985 17399 12410 -5892 3574 -2048 C ATOM 406 C GLN A 122 -32.244 39.504 10.132 1.00111.95 C ANISOU 406 C GLN A 122 12590 17363 12584 -5672 3850 -2386 C ATOM 407 O GLN A 122 -32.468 38.884 11.172 1.00108.60 O ANISOU 407 O GLN A 122 11838 16829 12596 -5218 3597 -2375 O ATOM 408 CB GLN A 122 -33.317 41.619 10.703 1.00108.56 C ANISOU 408 CB GLN A 122 12866 16826 11554 -5594 2908 -1716 C ATOM 409 CG GLN A 122 -33.320 43.112 10.770 1.00109.41 C ANISOU 409 CG GLN A 122 13373 16794 11403 -5746 2614 -1363 C ATOM 410 CD GLN A 122 -32.381 43.621 11.792 1.00109.16 C ANISOU 410 CD GLN A 122 12995 16592 11890 -5707 2516 -1337 C ATOM 411 OE1 GLN A 122 -31.748 42.848 12.530 1.00108.25 O ANISOU 411 OE1 GLN A 122 12303 16500 12329 -5507 2584 -1535 O ATOM 412 NE2 GLN A 122 -32.284 44.940 11.871 1.00110.60 N ANISOU 412 NE2 GLN A 122 13532 16588 11903 -5897 2329 -1082 N ATOM 413 N GLY A 123 -32.219 38.916 8.941 1.00127.76 N ANISOU 413 N GLY A 123 14751 19506 14286 -6011 4380 -2685 N ATOM 414 CA GLY A 123 -32.130 37.455 8.813 1.00128.73 C ANISOU 414 CA GLY A 123 14541 19596 14776 -5883 4828 -3100 C ATOM 415 C GLY A 123 -33.441 36.700 8.736 1.00126.34 C ANISOU 415 C GLY A 123 14474 19344 14184 -5724 4622 -3193 C ATOM 416 O GLY A 123 -33.453 35.456 8.754 1.00127.08 O ANISOU 416 O GLY A 123 14318 19331 14634 -5595 4977 -3533 O ATOM 417 N TYR A 124 -34.540 37.448 8.648 1.00132.76 N ANISOU 417 N TYR A 124 15745 20296 14403 -5735 4067 -2897 N ATOM 418 CA TYR A 124 -35.862 36.847 8.603 1.00130.91 C ANISOU 418 CA TYR A 124 15678 20161 13900 -5609 3800 -2968 C ATOM 419 C TYR A 124 -36.170 36.660 7.155 1.00135.67 C ANISOU 419 C TYR A 124 16688 21050 13810 -6126 4091 -3221 C ATOM 420 O TYR A 124 -36.374 37.626 6.419 1.00137.93 O ANISOU 420 O TYR A 124 17422 21540 13443 -6420 3893 -2977 O ATOM 421 CB TYR A 124 -36.918 37.714 9.309 1.00126.86 C ANISOU 421 CB TYR A 124 15354 19663 13185 -5302 3047 -2533 C ATOM 422 CG TYR A 124 -36.595 37.863 10.773 1.00122.81 C ANISOU 422 CG TYR A 124 14491 18886 13285 -4842 2795 -2334 C ATOM 423 CD1 TYR A 124 -36.712 36.790 11.632 1.00120.61 C ANISOU 423 CD1 TYR A 124 13857 18447 13524 -4498 2860 -2477 C ATOM 424 CD2 TYR A 124 -36.087 39.050 11.280 1.00122.06 C ANISOU 424 CD2 TYR A 124 14448 18689 13240 -4796 2530 -2017 C ATOM 425 CE1 TYR A 124 -36.355 36.899 12.963 1.00117.84 C ANISOU 425 CE1 TYR A 124 13226 17894 13652 -4109 2619 -2277 C ATOM 426 CE2 TYR A 124 -35.735 39.165 12.605 1.00119.24 C ANISOU 426 CE2 TYR A 124 13792 18137 13375 -4441 2296 -1881 C ATOM 427 CZ TYR A 124 -35.870 38.090 13.440 1.00117.19 C ANISOU 427 CZ TYR A 124 13197 17776 13555 -4094 2320 -1997 C ATOM 428 OH TYR A 124 -35.518 38.208 14.757 1.00115.16 O ANISOU 428 OH TYR A 124 12695 17369 13693 -3764 2049 -1831 O ATOM 429 N PHE A 125 -36.158 35.399 6.741 1.00155.70 N ANISOU 429 N PHE A 125 19097 23579 16484 -6255 4590 -3714 N ATOM 430 CA PHE A 125 -36.459 35.028 5.352 1.00161.10 C ANISOU 430 CA PHE A 125 20180 24557 16474 -6810 4928 -4075 C ATOM 431 C PHE A 125 -37.681 35.798 4.894 1.00161.17 C ANISOU 431 C PHE A 125 20653 24917 15668 -6936 4248 -3755 C ATOM 432 O PHE A 125 -38.409 36.347 5.748 1.00156.65 O ANISOU 432 O PHE A 125 20003 24293 15224 -6522 3596 -3352 O ATOM 433 CB PHE A 125 -36.768 33.550 5.286 1.00162.30 C ANISOU 433 CB PHE A 125 20148 24603 16917 -6819 5335 -4617 C ATOM 434 CG PHE A 125 -36.701 32.988 3.930 1.00168.90 C ANISOU 434 CG PHE A 125 21316 25661 17199 -7428 5905 -5142 C ATOM 435 CD1 PHE A 125 -35.599 32.241 3.542 1.00173.17 C ANISOU 435 CD1 PHE A 125 21672 25985 18139 -7605 6800 -5624 C ATOM 436 CD2 PHE A 125 -37.736 33.156 3.058 1.00171.60 C ANISOU 436 CD2 PHE A 125 22128 26431 16642 -7820 5564 -5183 C ATOM 437 CE1 PHE A 125 -35.529 31.670 2.290 1.00179.98 C ANISOU 437 CE1 PHE A 125 22878 27033 18472 -8204 7418 -6191 C ATOM 438 CE2 PHE A 125 -37.670 32.613 1.796 1.00178.50 C ANISOU 438 CE2 PHE A 125 23359 27548 16913 -8445 6091 -5711 C ATOM 439 CZ PHE A 125 -36.563 31.859 1.404 1.00182.69 C ANISOU 439 CZ PHE A 125 23765 27836 17811 -8660 7061 -6246 C ATOM 440 N PRO A 126 -37.929 35.856 3.574 1.00145.73 N ANISOU 440 N PRO A 126 19174 23325 12873 -7487 4378 -3918 N ATOM 441 CA PRO A 126 -39.104 36.656 3.241 1.00146.22 C ANISOU 441 CA PRO A 126 19610 23722 12225 -7507 3608 -3509 C ATOM 442 C PRO A 126 -40.291 35.843 2.780 1.00148.30 C ANISOU 442 C PRO A 126 19933 24311 12102 -7680 3381 -3824 C ATOM 443 O PRO A 126 -40.685 35.970 1.640 1.00154.04 O ANISOU 443 O PRO A 126 21102 25459 11966 -8155 3282 -3886 O ATOM 444 CB PRO A 126 -38.602 37.573 2.124 1.00151.89 C ANISOU 444 CB PRO A 126 20891 24662 12160 -7992 3732 -3291 C ATOM 445 CG PRO A 126 -37.187 37.127 1.839 1.00154.45 C ANISOU 445 CG PRO A 126 21093 24795 12798 -8284 4661 -3697 C ATOM 446 CD PRO A 126 -37.016 35.776 2.437 1.00152.10 C ANISOU 446 CD PRO A 126 20263 24252 13277 -8062 5083 -4230 C ATOM 447 N ASP A 127 -40.864 35.042 3.677 1.00140.31 N ANISOU 447 N ASP A 127 18493 23119 11701 -7324 3281 -4004 N ATOM 448 CA ASP A 127 -42.077 34.266 3.405 1.00142.08 C ANISOU 448 CA ASP A 127 18682 23623 11680 -7476 3033 -4312 C ATOM 449 C ASP A 127 -43.110 34.422 4.539 1.00136.83 C ANISOU 449 C ASP A 127 17662 22869 11459 -6929 2410 -4003 C ATOM 450 O ASP A 127 -43.926 33.526 4.758 1.00136.80 O ANISOU 450 O ASP A 127 17426 22906 11644 -6942 2381 -4326 O ATOM 451 CB ASP A 127 -41.731 32.776 3.173 1.00144.46 C ANISOU 451 CB ASP A 127 18844 23754 12290 -7763 3803 -5056 C ATOM 452 CG ASP A 127 -41.042 32.130 4.360 1.00139.65 C ANISOU 452 CG ASP A 127 17769 22558 12733 -7288 4225 -5133 C ATOM 453 OD1 ASP A 127 -40.894 32.826 5.382 1.00134.36 O ANISOU 453 OD1 ASP A 127 16889 21680 12484 -6778 3872 -4636 O ATOM 454 OD2 ASP A 127 -40.661 30.939 4.300 1.00141.64 O ANISOU 454 OD2 ASP A 127 17881 22541 13394 -7412 4891 -5673 O ATOM 455 N TRP A 128 -43.075 35.542 5.260 1.00129.97 N ANISOU 455 N TRP A 128 16759 21855 10767 -6485 1974 -3420 N ATOM 456 CA TRP A 128 -43.946 35.729 6.426 1.00125.22 C ANISOU 456 CA TRP A 128 15827 21117 10634 -5950 1495 -3154 C ATOM 457 C TRP A 128 -45.031 36.770 6.180 1.00126.81 C ANISOU 457 C TRP A 128 16163 21643 10375 -5816 719 -2699 C ATOM 458 O TRP A 128 -46.095 36.727 6.825 1.00125.07 O ANISOU 458 O TRP A 128 15648 21466 10407 -5500 321 -2616 O ATOM 459 CB TRP A 128 -43.137 36.116 7.675 1.00119.73 C ANISOU 459 CB TRP A 128 14929 19944 10620 -5480 1613 -2892 C ATOM 460 CG TRP A 128 -42.400 37.381 7.506 1.00120.03 C ANISOU 460 CG TRP A 128 15242 19917 10445 -5466 1495 -2476 C ATOM 461 CD1 TRP A 128 -41.126 37.507 7.081 1.00121.68 C ANISOU 461 CD1 TRP A 128 15583 20016 10633 -5725 1970 -2551 C ATOM 462 CD2 TRP A 128 -42.894 38.715 7.720 1.00119.48 C ANISOU 462 CD2 TRP A 128 15355 19858 10182 -5205 907 -1935 C ATOM 463 NE1 TRP A 128 -40.782 38.833 7.004 1.00122.17 N ANISOU 463 NE1 TRP A 128 15922 20025 10471 -5697 1721 -2092 N ATOM 464 CE2 TRP A 128 -41.854 39.594 7.397 1.00120.84 C ANISOU 464 CE2 TRP A 128 15815 19898 10199 -5363 1069 -1702 C ATOM 465 CE3 TRP A 128 -44.117 39.251 8.146 1.00118.60 C ANISOU 465 CE3 TRP A 128 15175 19827 10060 -4850 303 -1640 C ATOM 466 CZ2 TRP A 128 -41.992 40.984 7.495 1.00121.30 C ANISOU 466 CZ2 TRP A 128 16153 19850 10085 -5188 649 -1174 C ATOM 467 CZ3 TRP A 128 -44.251 40.638 8.241 1.00119.15 C ANISOU 467 CZ3 TRP A 128 15494 19791 9986 -4622 -115 -1116 C ATOM 468 CH2 TRP A 128 -43.200 41.483 7.921 1.00120.45 C ANISOU 468 CH2 TRP A 128 16002 19775 9990 -4796 60 -885 C ATOM 469 N GLN A 129 -44.765 37.714 5.276 1.00135.94 N ANISOU 469 N GLN A 129 17755 23001 10896 -6032 524 -2382 N ATOM 470 CA GLN A 129 -45.682 38.845 5.080 1.00138.08 C ANISOU 470 CA GLN A 129 18179 23491 10795 -5809 -231 -1832 C ATOM 471 C GLN A 129 -46.856 38.481 4.177 1.00143.74 C ANISOU 471 C GLN A 129 18900 24791 10926 -6083 -682 -1957 C ATOM 472 O GLN A 129 -47.146 39.180 3.220 1.00149.37 O ANISOU 472 O GLN A 129 19984 25852 10920 -6268 -1104 -1625 O ATOM 473 CB GLN A 129 -44.964 40.078 4.525 1.00140.65 C ANISOU 473 CB GLN A 129 19014 23737 10689 -5898 -294 -1347 C ATOM 474 CG GLN A 129 -45.940 41.224 4.252 1.00144.07 C ANISOU 474 CG GLN A 129 19640 24346 10752 -5630 -1079 -734 C ATOM 475 CD GLN A 129 -45.347 42.595 4.364 1.00144.33 C ANISOU 475 CD GLN A 129 20057 24019 10764 -5445 -1163 -158 C ATOM 476 OE1 GLN A 129 -45.955 43.585 3.927 1.00148.67 O ANISOU 476 OE1 GLN A 129 20895 24658 10935 -5283 -1724 393 O ATOM 477 NE2 GLN A 129 -44.159 42.682 4.963 1.00140.34 N ANISOU 477 NE2 GLN A 129 19544 23085 10696 -5459 -623 -264 N ATOM 478 N ASN A 130 -47.554 37.402 4.509 1.00142.02 N ANISOU 478 N ASN A 130 18265 24681 11018 -6116 -621 -2412 N ATOM 479 CA ASN A 130 -48.632 36.902 3.683 1.00147.87 C ANISOU 479 CA ASN A 130 18930 26003 11251 -6465 -1009 -2651 C ATOM 480 C ASN A 130 -49.894 37.444 4.245 1.00147.65 C ANISOU 480 C ASN A 130 18511 26112 11478 -5981 -1719 -2294 C ATOM 481 O ASN A 130 -49.929 37.908 5.349 1.00142.50 O ANISOU 481 O ASN A 130 17631 25058 11454 -5434 -1745 -2028 O ATOM 482 CB ASN A 130 -48.626 35.391 3.720 1.00147.71 C ANISOU 482 CB ASN A 130 18677 25963 11484 -6834 -450 -3403 C ATOM 483 CG ASN A 130 -47.228 34.844 3.773 1.00145.38 C ANISOU 483 CG ASN A 130 18573 25242 11423 -7014 407 -3721 C ATOM 484 OD1 ASN A 130 -46.481 34.944 2.800 1.00149.31 O ANISOU 484 OD1 ASN A 130 19504 25876 11351 -7444 691 -3818 O ATOM 485 ND2 ASN A 130 -46.838 34.313 4.925 1.00139.53 N ANISOU 485 ND2 ASN A 130 17506 23982 11525 -6665 824 -3846 N ATOM 486 N TYR A 131 -50.940 37.442 3.472 1.00148.72 N ANISOU 486 N TYR A 131 18561 26837 11110 -6182 -2316 -2279 N ATOM 487 CA TYR A 131 -52.188 37.942 3.969 1.00149.56 C ANISOU 487 CA TYR A 131 18198 27105 11524 -5701 -2989 -1958 C ATOM 488 C TYR A 131 -53.314 37.026 3.512 1.00154.81 C ANISOU 488 C TYR A 131 18443 28353 12024 -6077 -3285 -2417 C ATOM 489 O TYR A 131 -53.173 36.210 2.586 1.00159.21 O ANISOU 489 O TYR A 131 19204 29269 12021 -6750 -3107 -2901 O ATOM 490 CB TYR A 131 -52.436 39.370 3.469 1.00153.83 C ANISOU 490 CB TYR A 131 19025 27796 11630 -5389 -3689 -1193 C ATOM 491 CG TYR A 131 -51.419 40.387 3.915 1.00149.62 C ANISOU 491 CG TYR A 131 18904 26672 11274 -5047 -3439 -726 C ATOM 492 CD1 TYR A 131 -51.758 41.384 4.824 1.00147.02 C ANISOU 492 CD1 TYR A 131 18403 25959 11498 -4357 -3711 -241 C ATOM 493 CD2 TYR A 131 -50.126 40.366 3.421 1.00148.97 C ANISOU 493 CD2 TYR A 131 19369 26409 10825 -5443 -2900 -806 C ATOM 494 CE1 TYR A 131 -50.829 42.328 5.241 1.00143.78 C ANISOU 494 CE1 TYR A 131 18384 24993 11251 -4106 -3476 138 C ATOM 495 CE2 TYR A 131 -49.194 41.297 3.828 1.00145.76 C ANISOU 495 CE2 TYR A 131 19294 25480 10606 -5193 -2670 -413 C ATOM 496 CZ TYR A 131 -49.547 42.281 4.739 1.00143.15 C ANISOU 496 CZ TYR A 131 18815 24769 10805 -4542 -2975 55 C ATOM 497 OH TYR A 131 -48.618 43.211 5.147 1.00140.54 O ANISOU 497 OH TYR A 131 18830 23908 10660 -4357 -2738 395 O ATOM 498 N THR A 132 -54.450 37.184 4.166 1.00165.23 N ANISOU 498 N THR A 132 19163 29773 13845 -5663 -3719 -2293 N ATOM 499 CA THR A 132 -55.655 36.517 3.749 1.00171.30 C ANISOU 499 CA THR A 132 19433 31154 14498 -5976 -4137 -2646 C ATOM 500 C THR A 132 -55.972 36.989 2.331 1.00180.49 C ANISOU 500 C THR A 132 20890 33023 14663 -6316 -4868 -2394 C ATOM 501 O THR A 132 -55.763 38.176 2.022 1.00182.18 O ANISOU 501 O THR A 132 21457 33213 14551 -5968 -5293 -1701 O ATOM 502 CB THR A 132 -56.814 36.908 4.659 1.00170.91 C ANISOU 502 CB THR A 132 18671 31105 15164 -5377 -4544 -2415 C ATOM 503 OG1 THR A 132 -57.128 38.295 4.451 1.00174.04 O ANISOU 503 OG1 THR A 132 19135 31595 15396 -4838 -5249 -1656 O ATOM 504 CG2 THR A 132 -56.445 36.670 6.135 1.00162.09 C ANISOU 504 CG2 THR A 132 17383 29258 14945 -4972 -3855 -2526 C ATOM 505 N PRO A 133 -56.439 36.063 1.456 1.00182.50 N ANISOU 505 N PRO A 133 21061 33889 14391 -7029 -4999 -2951 N ATOM 506 CA PRO A 133 -57.097 36.490 0.213 1.00192.85 C ANISOU 506 CA PRO A 133 22478 36022 14773 -7316 -5904 -2693 C ATOM 507 C PRO A 133 -58.308 37.380 0.469 1.00196.79 C ANISOU 507 C PRO A 133 22366 36826 15581 -6673 -6849 -2092 C ATOM 508 O PRO A 133 -58.843 37.424 1.591 1.00192.26 O ANISOU 508 O PRO A 133 21164 35921 15965 -6135 -6753 -2074 O ATOM 509 CB PRO A 133 -57.554 35.174 -0.434 1.00198.49 C ANISOU 509 CB PRO A 133 23011 37282 15123 -8176 -5814 -3549 C ATOM 510 CG PRO A 133 -57.352 34.118 0.587 1.00191.20 C ANISOU 510 CG PRO A 133 21766 35780 15100 -8220 -4925 -4183 C ATOM 511 CD PRO A 133 -56.247 34.602 1.473 1.00181.52 C ANISOU 511 CD PRO A 133 20865 33703 14402 -7663 -4290 -3838 C ATOM 512 N GLY A 134 -58.730 38.076 -0.575 1.00186.68 N ANISOU 512 N GLY A 134 21277 36169 13483 -6728 -7737 -1598 N ATOM 513 CA GLY A 134 -59.786 39.067 -0.463 1.00191.83 C ANISOU 513 CA GLY A 134 21410 37087 14389 -6039 -8692 -900 C ATOM 514 C GLY A 134 -61.115 38.491 -0.914 1.00200.88 C ANISOU 514 C GLY A 134 21782 39118 15426 -6351 -9438 -1223 C ATOM 515 O GLY A 134 -61.392 37.313 -0.684 1.00199.72 O ANISOU 515 O GLY A 134 21228 39104 15552 -6867 -9028 -2042 O ATOM 516 N PRO A 135 -61.969 39.324 -1.528 1.00241.18 N ANISOU 516 N PRO A 135 26638 44815 20186 -6024 -10552 -566 N ATOM 517 CA PRO A 135 -61.856 40.769 -1.682 1.00243.66 C ANISOU 517 CA PRO A 135 27309 44906 20365 -5285 -11100 476 C ATOM 518 C PRO A 135 -62.312 41.449 -0.406 1.00238.50 C ANISOU 518 C PRO A 135 26023 43630 20965 -4299 -11011 818 C ATOM 519 O PRO A 135 -63.212 40.946 0.280 1.00238.16 O ANISOU 519 O PRO A 135 25043 43723 21725 -4156 -11016 416 O ATOM 520 CB PRO A 135 -62.826 41.071 -2.802 1.00257.63 C ANISOU 520 CB PRO A 135 28842 47673 21371 -5399 -12365 879 C ATOM 521 CG PRO A 135 -63.906 40.072 -2.602 1.00260.91 C ANISOU 521 CG PRO A 135 28224 48686 22224 -5726 -12581 157 C ATOM 522 CD PRO A 135 -63.248 38.828 -2.055 1.00251.44 C ANISOU 522 CD PRO A 135 27144 47073 21320 -6352 -11397 -841 C ATOM 523 N GLY A 136 -61.704 42.595 -0.116 1.00202.71 N ANISOU 523 N GLY A 136 22023 38422 16577 -3669 -10904 1535 N ATOM 524 CA GLY A 136 -61.819 43.249 1.187 1.00196.18 C ANISOU 524 CA GLY A 136 20835 36811 16895 -2805 -10553 1769 C ATOM 525 C GLY A 136 -60.450 43.361 1.829 1.00185.24 C ANISOU 525 C GLY A 136 20190 34538 15656 -2828 -9546 1671 C ATOM 526 O GLY A 136 -59.446 42.955 1.242 1.00183.11 O ANISOU 526 O GLY A 136 20644 34266 14662 -3466 -9134 1450 O ATOM 527 N ILE A 137 -60.423 43.929 3.030 1.00178.33 N ANISOU 527 N ILE A 137 19107 32931 15720 -2138 -9157 1821 N ATOM 528 CA ILE A 137 -59.199 44.051 3.820 1.00168.14 C ANISOU 528 CA ILE A 137 18385 30805 14694 -2110 -8243 1703 C ATOM 529 C ILE A 137 -58.423 42.744 3.875 1.00161.73 C ANISOU 529 C ILE A 137 17752 30022 13677 -2870 -7480 910 C ATOM 530 O ILE A 137 -58.974 41.715 4.252 1.00160.41 O ANISOU 530 O ILE A 137 16990 30100 13859 -3110 -7286 299 O ATOM 531 CB ILE A 137 -59.524 44.411 5.263 1.00162.64 C ANISOU 531 CB ILE A 137 17214 29486 15094 -1418 -7875 1674 C ATOM 532 CG1 ILE A 137 -59.948 45.872 5.369 1.00167.55 C ANISOU 532 CG1 ILE A 137 17863 29770 16030 -590 -8378 2474 C ATOM 533 CG2 ILE A 137 -58.325 44.137 6.147 1.00152.08 C ANISOU 533 CG2 ILE A 137 16318 27457 14007 -1565 -6918 1333 C ATOM 534 CD1 ILE A 137 -60.222 46.289 6.801 1.00162.70 C ANISOU 534 CD1 ILE A 137 16861 28497 16460 70 -7936 2401 C ATOM 535 N ARG A 138 -57.144 42.783 3.527 1.00197.43 N ANISOU 535 N ARG A 138 23070 34249 17696 -3237 -7004 918 N ATOM 536 CA ARG A 138 -56.325 41.579 3.589 1.00191.85 C ANISOU 536 CA ARG A 138 22535 33486 16875 -3887 -6228 193 C ATOM 537 C ARG A 138 -55.641 41.561 4.952 1.00182.00 C ANISOU 537 C ARG A 138 21260 31456 16436 -3555 -5471 31 C ATOM 538 O ARG A 138 -54.841 42.450 5.266 1.00178.86 O ANISOU 538 O ARG A 138 21319 30521 16119 -3265 -5273 429 O ATOM 539 CB ARG A 138 -55.294 41.540 2.472 1.00194.15 C ANISOU 539 CB ARG A 138 23632 33915 16220 -4495 -6054 216 C ATOM 540 CG ARG A 138 -55.778 42.113 1.149 1.00204.66 C ANISOU 540 CG ARG A 138 25258 35881 16625 -4660 -6897 708 C ATOM 541 CD ARG A 138 -56.983 41.376 0.601 1.00211.78 C ANISOU 541 CD ARG A 138 25578 37610 17279 -4958 -7510 383 C ATOM 542 NE ARG A 138 -57.217 41.699 -0.806 1.00222.34 N ANISOU 542 NE ARG A 138 27334 39640 17504 -5326 -8242 743 N ATOM 543 CZ ARG A 138 -56.924 40.891 -1.825 1.00226.76 C ANISOU 543 CZ ARG A 138 28270 40733 17154 -6185 -8137 273 C ATOM 544 NH1 ARG A 138 -56.386 39.689 -1.608 1.00221.53 N ANISOU 544 NH1 ARG A 138 27588 39944 16640 -6738 -7299 -593 N ATOM 545 NH2 ARG A 138 -57.183 41.280 -3.078 1.00237.25 N ANISOU 545 NH2 ARG A 138 30022 42722 17399 -6496 -8871 673 N ATOM 546 N TYR A 139 -55.976 40.564 5.769 1.00152.86 N ANISOU 546 N TYR A 139 17048 27707 13325 -3617 -5065 -538 N ATOM 547 CA TYR A 139 -55.465 40.468 7.134 1.00144.45 C ANISOU 547 CA TYR A 139 15912 25969 13002 -3297 -4414 -686 C ATOM 548 C TYR A 139 -54.219 39.603 7.146 1.00139.35 C ANISOU 548 C TYR A 139 15654 25068 12224 -3781 -3672 -1116 C ATOM 549 O TYR A 139 -54.157 38.623 6.429 1.00141.65 O ANISOU 549 O TYR A 139 15970 25708 12144 -4364 -3522 -1566 O ATOM 550 CB TYR A 139 -56.533 39.876 8.039 1.00143.63 C ANISOU 550 CB TYR A 139 15062 25920 13591 -3088 -4359 -1010 C ATOM 551 CG TYR A 139 -57.619 40.861 8.359 1.00147.58 C ANISOU 551 CG TYR A 139 15124 26480 14469 -2444 -4928 -572 C ATOM 552 CD1 TYR A 139 -57.411 41.859 9.279 1.00144.24 C ANISOU 552 CD1 TYR A 139 14823 25472 14512 -1827 -4801 -204 C ATOM 553 CD2 TYR A 139 -58.845 40.800 7.728 1.00155.41 C ANISOU 553 CD2 TYR A 139 15564 28115 15371 -2458 -5591 -546 C ATOM 554 CE1 TYR A 139 -58.379 42.761 9.593 1.00148.36 C ANISOU 554 CE1 TYR A 139 14949 25971 15450 -1203 -5236 164 C ATOM 555 CE2 TYR A 139 -59.840 41.712 8.025 1.00159.83 C ANISOU 555 CE2 TYR A 139 15650 28707 16370 -1802 -6101 -131 C ATOM 556 CZ TYR A 139 -59.597 42.696 8.975 1.00156.17 C ANISOU 556 CZ TYR A 139 15339 27576 16420 -1152 -5879 219 C ATOM 557 OH TYR A 139 -60.574 43.627 9.285 1.00161.15 O ANISOU 557 OH TYR A 139 15507 28165 17558 -456 -6311 609 O ATOM 558 N PRO A 140 -53.220 39.957 7.961 1.00120.19 N ANISOU 558 N PRO A 140 13509 22034 10125 -3545 -3202 -1002 N ATOM 559 CA PRO A 140 -51.942 39.279 7.893 1.00116.42 C ANISOU 559 CA PRO A 140 13378 21316 9540 -3943 -2552 -1323 C ATOM 560 C PRO A 140 -52.005 37.939 8.545 1.00113.12 C ANISOU 560 C PRO A 140 12617 20794 9568 -4116 -2039 -1895 C ATOM 561 O PRO A 140 -52.727 37.774 9.509 1.00111.13 O ANISOU 561 O PRO A 140 11949 20417 9859 -3795 -2035 -1949 O ATOM 562 CB PRO A 140 -51.017 40.193 8.674 1.00111.69 C ANISOU 562 CB PRO A 140 13070 20140 9228 -3570 -2339 -973 C ATOM 563 CG PRO A 140 -51.868 40.929 9.581 1.00110.96 C ANISOU 563 CG PRO A 140 12683 19868 9610 -2977 -2648 -688 C ATOM 564 CD PRO A 140 -53.284 40.865 9.107 1.00116.59 C ANISOU 564 CD PRO A 140 12976 21086 10239 -2910 -3205 -662 C ATOM 565 N LEU A 141 -51.264 36.985 8.010 1.00128.02 N ANISOU 565 N LEU A 141 14700 22707 11237 -4625 -1567 -2319 N ATOM 566 CA LEU A 141 -51.366 35.608 8.463 1.00126.36 C ANISOU 566 CA LEU A 141 14209 22380 11423 -4845 -1063 -2876 C ATOM 567 C LEU A 141 -50.427 35.349 9.628 1.00119.95 C ANISOU 567 C LEU A 141 13431 20953 11194 -4565 -503 -2882 C ATOM 568 O LEU A 141 -50.770 34.567 10.517 1.00117.72 O ANISOU 568 O LEU A 141 12856 20450 11423 -4459 -219 -3106 O ATOM 569 CB LEU A 141 -51.074 34.624 7.327 1.00130.60 C ANISOU 569 CB LEU A 141 14933 23194 11496 -5528 -776 -3389 C ATOM 570 CG LEU A 141 -51.966 34.689 6.048 1.00138.34 C ANISOU 570 CG LEU A 141 15920 24885 11758 -5953 -1339 -3477 C ATOM 571 CD1 LEU A 141 -51.366 33.910 4.904 1.00142.58 C ANISOU 571 CD1 LEU A 141 16823 25629 11722 -6654 -965 -3965 C ATOM 572 CD2 LEU A 141 -53.372 34.190 6.234 1.00141.34 C ANISOU 572 CD2 LEU A 141 15741 25605 12356 -5999 -1673 -3710 C ATOM 573 N THR A 142 -49.259 36.014 9.639 1.00129.20 N ANISOU 573 N THR A 142 14950 21860 12280 -4461 -364 -2618 N ATOM 574 CA THR A 142 -48.221 35.823 10.705 1.00123.92 C ANISOU 574 CA THR A 142 14301 20658 12126 -4212 101 -2596 C ATOM 575 C THR A 142 -48.573 36.645 11.956 1.00120.38 C ANISOU 575 C THR A 142 13725 19956 12057 -3656 -146 -2228 C ATOM 576 O THR A 142 -48.455 37.877 11.963 1.00120.31 O ANISOU 576 O THR A 142 13904 19907 11902 -3430 -474 -1830 O ATOM 577 CB THR A 142 -46.764 36.199 10.212 1.00123.68 C ANISOU 577 CB THR A 142 14624 20476 11893 -4378 373 -2510 C ATOM 578 OG1 THR A 142 -46.247 35.203 9.330 1.00126.50 O ANISOU 578 OG1 THR A 142 15069 20930 12065 -4860 829 -2956 O ATOM 579 CG2 THR A 142 -45.819 36.277 11.359 1.00119.09 C ANISOU 579 CG2 THR A 142 13990 19430 11827 -4057 645 -2386 C ATOM 580 N PHE A 143 -48.987 35.969 13.017 1.00 99.44 N ANISOU 580 N PHE A 143 10802 17100 9882 -3461 60 -2369 N ATOM 581 CA PHE A 143 -49.463 36.684 14.201 1.00 97.01 C ANISOU 581 CA PHE A 143 10385 16591 9883 -2982 -126 -2091 C ATOM 582 C PHE A 143 -48.329 37.507 14.808 1.00 93.93 C ANISOU 582 C PHE A 143 10267 15859 9562 -2755 -83 -1806 C ATOM 583 O PHE A 143 -47.289 36.967 15.207 1.00 91.78 O ANISOU 583 O PHE A 143 10058 15343 9472 -2808 271 -1894 O ATOM 584 CB PHE A 143 -50.057 35.683 15.205 1.00 95.73 C ANISOU 584 CB PHE A 143 9939 16275 10160 -2895 180 -2318 C ATOM 585 CG PHE A 143 -50.798 36.311 16.382 1.00 94.44 C ANISOU 585 CG PHE A 143 9638 15973 10274 -2461 46 -2116 C ATOM 586 CD1 PHE A 143 -51.583 37.427 16.246 1.00 96.32 C ANISOU 586 CD1 PHE A 143 9798 16373 10427 -2212 -389 -1886 C ATOM 587 CD2 PHE A 143 -50.708 35.744 17.635 1.00 92.08 C ANISOU 587 CD2 PHE A 143 9305 15359 10322 -2301 395 -2160 C ATOM 588 CE1 PHE A 143 -52.231 37.969 17.359 1.00 95.69 C ANISOU 588 CE1 PHE A 143 9594 16120 10643 -1815 -406 -1764 C ATOM 589 CE2 PHE A 143 -51.363 36.287 18.714 1.00 91.51 C ANISOU 589 CE2 PHE A 143 9156 15166 10450 -1955 352 -2025 C ATOM 590 CZ PHE A 143 -52.117 37.387 18.576 1.00 93.27 C ANISOU 590 CZ PHE A 143 9283 15532 10622 -1718 -15 -1861 C ATOM 591 N GLY A 144 -48.509 38.822 14.828 1.00108.38 N ANISOU 591 N GLY A 144 12245 17669 11264 -2517 -452 -1466 N ATOM 592 CA GLY A 144 -47.459 39.713 15.345 1.00106.29 C ANISOU 592 CA GLY A 144 12256 17084 11043 -2374 -432 -1226 C ATOM 593 C GLY A 144 -47.054 40.818 14.379 1.00108.78 C ANISOU 593 C GLY A 144 12896 17453 10981 -2489 -682 -949 C ATOM 594 O GLY A 144 -46.610 41.907 14.798 1.00108.30 O ANISOU 594 O GLY A 144 13066 17122 10961 -2316 -789 -690 O ATOM 595 N TRP A 145 -47.156 40.515 13.086 1.00120.29 N ANISOU 595 N TRP A 145 14418 19242 12044 -2829 -738 -1019 N ATOM 596 CA TRP A 145 -47.149 41.544 12.099 1.00124.01 C ANISOU 596 CA TRP A 145 15212 19828 12078 -2918 -1052 -695 C ATOM 597 C TRP A 145 -48.442 42.291 12.365 1.00125.94 C ANISOU 597 C TRP A 145 15329 20109 12413 -2503 -1518 -433 C ATOM 598 O TRP A 145 -49.453 41.669 12.612 1.00126.24 O ANISOU 598 O TRP A 145 14993 20347 12627 -2392 -1602 -616 O ATOM 599 CB TRP A 145 -47.114 40.928 10.720 1.00127.74 C ANISOU 599 CB TRP A 145 15780 20708 12046 -3393 -1015 -866 C ATOM 600 CG TRP A 145 -47.097 41.945 9.628 1.00132.52 C ANISOU 600 CG TRP A 145 16793 21466 12095 -3528 -1343 -484 C ATOM 601 CD1 TRP A 145 -48.010 42.089 8.627 1.00137.85 C ANISOU 601 CD1 TRP A 145 17522 22566 12290 -3629 -1787 -338 C ATOM 602 CD2 TRP A 145 -46.121 42.967 9.421 1.00133.25 C ANISOU 602 CD2 TRP A 145 17313 21286 12031 -3599 -1268 -166 C ATOM 603 NE1 TRP A 145 -47.661 43.133 7.806 1.00141.94 N ANISOU 603 NE1 TRP A 145 18526 23075 12328 -3730 -1997 99 N ATOM 604 CE2 TRP A 145 -46.502 43.686 8.277 1.00139.10 C ANISOU 604 CE2 TRP A 145 18411 22264 12176 -3730 -1644 199 C ATOM 605 CE3 TRP A 145 -44.960 43.342 10.094 1.00130.15 C ANISOU 605 CE3 TRP A 145 17027 20484 11941 -3591 -932 -151 C ATOM 606 CZ2 TRP A 145 -45.771 44.755 7.802 1.00141.77 C ANISOU 606 CZ2 TRP A 145 19253 22385 12230 -3855 -1630 587 C ATOM 607 CZ3 TRP A 145 -44.240 44.401 9.623 1.00132.73 C ANISOU 607 CZ3 TRP A 145 17791 20623 12018 -3745 -923 177 C ATOM 608 CH2 TRP A 145 -44.643 45.098 8.490 1.00138.41 C ANISOU 608 CH2 TRP A 145 18908 21526 12157 -3878 -1237 549 C ATOM 609 N CYS A 146 -48.402 43.613 12.421 1.00115.22 N ANISOU 609 N CYS A 146 14251 18505 11025 -2254 -1768 -26 N ATOM 610 CA CYS A 146 -49.597 44.387 12.771 1.00117.61 C ANISOU 610 CA CYS A 146 14402 18751 11533 -1771 -2161 229 C ATOM 611 C CYS A 146 -49.951 45.389 11.694 1.00123.53 C ANISOU 611 C CYS A 146 15435 19604 11896 -1714 -2625 698 C ATOM 612 O CYS A 146 -50.336 46.547 11.948 1.00125.99 O ANISOU 612 O CYS A 146 15884 19605 12379 -1300 -2873 1072 O ATOM 613 CB CYS A 146 -49.399 45.065 14.108 1.00114.70 C ANISOU 613 CB CYS A 146 14086 17877 11618 -1404 -2003 273 C ATOM 614 SG CYS A 146 -49.141 43.824 15.324 1.00109.15 S ANISOU 614 SG CYS A 146 13068 17129 11274 -1455 -1549 -194 S ATOM 615 N PHE A 147 -49.831 44.905 10.468 1.00131.57 N ANISOU 615 N PHE A 147 16568 21052 12372 -2139 -2726 674 N ATOM 616 CA PHE A 147 -50.209 45.686 9.311 1.00138.25 C ANISOU 616 CA PHE A 147 17709 22104 12715 -2152 -3214 1141 C ATOM 617 C PHE A 147 -51.190 44.909 8.427 1.00142.61 C ANISOU 617 C PHE A 147 17948 23326 12911 -2340 -3590 1008 C ATOM 618 O PHE A 147 -50.918 43.774 8.013 1.00141.58 O ANISOU 618 O PHE A 147 17730 23527 12537 -2825 -3329 561 O ATOM 619 CB PHE A 147 -48.966 46.054 8.520 1.00139.42 C ANISOU 619 CB PHE A 147 18460 22146 12367 -2595 -2985 1301 C ATOM 620 CG PHE A 147 -48.300 47.319 8.980 1.00139.12 C ANISOU 620 CG PHE A 147 18831 21498 12529 -2387 -2888 1670 C ATOM 621 CD1 PHE A 147 -49.006 48.511 8.994 1.00143.49 C ANISOU 621 CD1 PHE A 147 19542 21790 13186 -1914 -3318 2196 C ATOM 622 CD2 PHE A 147 -46.960 47.329 9.353 1.00135.38 C ANISOU 622 CD2 PHE A 147 18575 20703 12159 -2680 -2367 1489 C ATOM 623 CE1 PHE A 147 -48.406 49.679 9.380 1.00143.98 C ANISOU 623 CE1 PHE A 147 20030 21238 13439 -1769 -3190 2504 C ATOM 624 CE2 PHE A 147 -46.355 48.496 9.742 1.00135.86 C ANISOU 624 CE2 PHE A 147 19010 20219 12393 -2569 -2280 1785 C ATOM 625 CZ PHE A 147 -47.080 49.676 9.758 1.00140.11 C ANISOU 625 CZ PHE A 147 19766 20452 13018 -2131 -2671 2280 C ATOM 626 N LYS A 148 -52.333 45.528 8.152 1.00136.15 N ANISOU 626 N LYS A 148 16941 22692 12098 -1954 -4202 1382 N ATOM 627 CA LYS A 148 -53.328 44.928 7.294 1.00141.64 C ANISOU 627 CA LYS A 148 17299 24074 12442 -2127 -4681 1303 C ATOM 628 C LYS A 148 -53.350 45.740 6.016 1.00149.39 C ANISOU 628 C LYS A 148 18766 25295 12701 -2220 -5219 1882 C ATOM 629 O LYS A 148 -52.993 46.926 6.025 1.00151.01 O ANISOU 629 O LYS A 148 19416 25051 12912 -1924 -5309 2426 O ATOM 630 CB LYS A 148 -54.698 44.930 7.952 1.00143.24 C ANISOU 630 CB LYS A 148 16793 24394 13237 -1611 -5019 1281 C ATOM 631 CG LYS A 148 -55.157 46.281 8.486 1.00145.57 C ANISOU 631 CG LYS A 148 17089 24235 13987 -882 -5300 1823 C ATOM 632 CD LYS A 148 -56.559 46.168 9.085 1.00148.03 C ANISOU 632 CD LYS A 148 16599 24726 14918 -402 -5572 1725 C ATOM 633 CE LYS A 148 -57.080 47.502 9.627 1.00151.29 C ANISOU 633 CE LYS A 148 16970 24646 15867 376 -5795 2222 C ATOM 634 NZ LYS A 148 -58.510 47.403 10.086 1.00155.21 N ANISOU 634 NZ LYS A 148 16606 25381 16986 850 -6068 2130 N ATOM 635 N LEU A 149 -53.752 45.101 4.917 1.00151.80 N ANISOU 635 N LEU A 149 19032 26291 12352 -2666 -5562 1764 N ATOM 636 CA LEU A 149 -53.825 45.759 3.615 1.00160.36 C ANISOU 636 CA LEU A 149 20615 27715 12601 -2825 -6126 2322 C ATOM 637 C LEU A 149 -55.252 46.190 3.448 1.00167.48 C ANISOU 637 C LEU A 149 21019 28976 13639 -2322 -6986 2713 C ATOM 638 O LEU A 149 -56.140 45.349 3.333 1.00169.60 O ANISOU 638 O LEU A 149 20676 29820 13944 -2456 -7266 2335 O ATOM 639 CB LEU A 149 -53.401 44.811 2.494 1.00163.09 C ANISOU 639 CB LEU A 149 21252 28643 12072 -3657 -5995 1932 C ATOM 640 CG LEU A 149 -52.085 44.089 2.809 1.00155.73 C ANISOU 640 CG LEU A 149 20571 27381 11219 -4122 -5051 1371 C ATOM 641 CD1 LEU A 149 -51.713 43.065 1.774 1.00158.70 C ANISOU 641 CD1 LEU A 149 21182 28281 10837 -4924 -4812 877 C ATOM 642 CD2 LEU A 149 -50.954 45.078 2.980 1.00153.50 C ANISOU 642 CD2 LEU A 149 20890 26472 10960 -4027 -4686 1773 C ATOM 643 N VAL A 150 -55.470 47.502 3.484 1.00211.44 N ANISOU 643 N VAL A 150 26811 34164 19364 -1728 -7375 3454 N ATOM 644 CA VAL A 150 -56.812 48.066 3.396 1.00219.02 C ANISOU 644 CA VAL A 150 27253 35368 20598 -1102 -8201 3917 C ATOM 645 C VAL A 150 -57.113 48.583 1.987 1.00230.09 C ANISOU 645 C VAL A 150 29067 37275 21083 -1215 -9018 4589 C ATOM 646 O VAL A 150 -56.309 49.320 1.406 1.00232.44 O ANISOU 646 O VAL A 150 30212 37275 20831 -1354 -8953 5091 O ATOM 647 CB VAL A 150 -57.020 49.219 4.414 1.00217.80 C ANISOU 647 CB VAL A 150 27012 34408 21332 -248 -8131 4328 C ATOM 648 CG1 VAL A 150 -57.941 50.308 3.836 1.00228.70 C ANISOU 648 CG1 VAL A 150 28347 35852 22697 389 -9017 5184 C ATOM 649 CG2 VAL A 150 -57.577 48.676 5.726 1.00211.64 C ANISOU 649 CG2 VAL A 150 25435 33473 21504 63 -7758 3748 C ATOM 650 N PRO A 151 -58.281 48.199 1.435 1.00209.48 N ANISOU 650 N PRO A 151 25854 35452 18286 -1181 -9803 4612 N ATOM 651 CA PRO A 151 -58.715 48.819 0.201 1.00221.35 C ANISOU 651 CA PRO A 151 27685 37438 18979 -1145 -10724 5368 C ATOM 652 C PRO A 151 -59.413 50.138 0.508 1.00227.26 C ANISOU 652 C PRO A 151 28265 37731 20354 -142 -11278 6219 C ATOM 653 O PRO A 151 -60.189 50.220 1.464 1.00225.46 O ANISOU 653 O PRO A 151 27230 37288 21145 485 -11282 6070 O ATOM 654 CB PRO A 151 -59.699 47.798 -0.367 1.00226.86 C ANISOU 654 CB PRO A 151 27681 39176 19341 -1523 -11327 4944 C ATOM 655 CG PRO A 151 -60.314 47.179 0.834 1.00220.34 C ANISOU 655 CG PRO A 151 25883 38225 19610 -1237 -10975 4300 C ATOM 656 CD PRO A 151 -59.265 47.212 1.922 1.00208.32 C ANISOU 656 CD PRO A 151 24695 35792 18666 -1185 -9903 3974 C ATOM 657 N VAL A 152 -59.110 51.162 -0.282 1.00199.72 N ANISOU 657 N VAL A 152 25567 34042 16276 2 -11669 7097 N ATOM 658 CA VAL A 152 -59.775 52.457 -0.185 1.00207.57 C ANISOU 658 CA VAL A 152 26502 34588 17778 961 -12266 8015 C ATOM 659 C VAL A 152 -60.544 52.687 -1.471 1.00221.56 C ANISOU 659 C VAL A 152 28309 37157 18716 999 -13438 8735 C ATOM 660 O VAL A 152 -60.567 51.817 -2.344 1.00224.43 O ANISOU 660 O VAL A 152 28721 38422 18130 244 -13734 8427 O ATOM 661 CB VAL A 152 -58.759 53.600 0.000 1.00205.80 C ANISOU 661 CB VAL A 152 27262 33321 17612 1154 -11746 8560 C ATOM 662 CG1 VAL A 152 -57.789 53.270 1.139 1.00192.24 C ANISOU 662 CG1 VAL A 152 25624 30937 16481 910 -10596 7797 C ATOM 663 CG2 VAL A 152 -58.005 53.867 -1.300 1.00212.00 C ANISOU 663 CG2 VAL A 152 29127 34317 17106 543 -11921 9097 C ATOM 664 N GLU A 153 -61.175 53.852 -1.594 1.00335.18 N ANISOU 664 N GLU A 153 42688 51216 33449 1874 -14114 9694 N ATOM 665 CA GLU A 153 -61.734 54.275 -2.885 1.00349.81 C ANISOU 665 CA GLU A 153 44800 53716 34397 1952 -15267 10597 C ATOM 666 C GLU A 153 -60.585 54.709 -3.808 1.00352.10 C ANISOU 666 C GLU A 153 46496 53789 33497 1349 -15041 11101 C ATOM 667 O GLU A 153 -59.474 54.975 -3.334 1.00343.51 O ANISOU 667 O GLU A 153 46082 51875 32562 1124 -14057 10911 O ATOM 668 CB GLU A 153 -62.735 55.422 -2.708 1.00359.99 C ANISOU 668 CB GLU A 153 45650 54624 36505 3157 -16038 11534 C ATOM 669 N PRO A 154 -60.843 54.784 -5.127 1.00323.50 N ANISOU 669 N PRO A 154 43319 50932 28663 1052 -15946 11738 N ATOM 670 CA PRO A 154 -59.775 55.133 -6.067 1.00326.65 C ANISOU 670 CA PRO A 154 45083 51203 27826 388 -15691 12192 C ATOM 671 C PRO A 154 -59.328 56.587 -5.936 1.00330.15 C ANISOU 671 C PRO A 154 46349 50501 28592 1015 -15516 13195 C ATOM 672 O PRO A 154 -58.268 56.854 -5.373 1.00321.17 O ANISOU 672 O PRO A 154 45768 48491 27770 806 -14465 12934 O ATOM 673 CB PRO A 154 -60.420 54.893 -7.435 1.00340.73 C ANISOU 673 CB PRO A 154 47006 54156 28301 45 -16867 12682 C ATOM 674 CG PRO A 154 -61.875 55.096 -7.206 1.00348.49 C ANISOU 674 CG PRO A 154 46837 55511 30061 968 -17949 13044 C ATOM 675 CD PRO A 154 -62.132 54.582 -5.811 1.00335.88 C ANISOU 675 CD PRO A 154 44157 53538 29926 1303 -17260 12091 C ATOM 676 N GLU A 183 -59.176 46.940 -7.469 1.00271.47 N ANISOU 676 N GLU A 183 36493 48691 17961 -5005 -13918 5930 N ATOM 677 CA GLU A 183 -59.240 47.507 -6.119 1.00262.29 C ANISOU 677 CA GLU A 183 34786 46589 18282 -4073 -13539 6081 C ATOM 678 C GLU A 183 -57.835 47.661 -5.502 1.00250.72 C ANISOU 678 C GLU A 183 33970 44137 17155 -4194 -12272 5851 C ATOM 679 O GLU A 183 -57.124 46.674 -5.262 1.00242.63 O ANISOU 679 O GLU A 183 32979 43052 16156 -4821 -11375 4945 O ATOM 680 CB GLU A 183 -60.137 46.644 -5.220 1.00257.31 C ANISOU 680 CB GLU A 183 32900 46173 18694 -3877 -13541 5314 C ATOM 681 CG GLU A 183 -60.569 47.315 -3.914 1.00251.46 C ANISOU 681 CG GLU A 183 31469 44657 19417 -2827 -13427 5573 C ATOM 682 CD GLU A 183 -61.515 46.453 -3.082 1.00247.94 C ANISOU 682 CD GLU A 183 29794 44483 19929 -2690 -13421 4834 C ATOM 683 OE1 GLU A 183 -61.097 45.379 -2.587 1.00239.09 O ANISOU 683 OE1 GLU A 183 28513 43282 19049 -3225 -12585 3895 O ATOM 684 OE2 GLU A 183 -62.684 46.866 -2.920 1.00254.68 O ANISOU 684 OE2 GLU A 183 29831 45606 21331 -2027 -14239 5220 O ATOM 685 N VAL A 184 -57.459 48.908 -5.228 1.00254.46 N ANISOU 685 N VAL A 184 34917 43822 17945 -3575 -12218 6678 N ATOM 686 CA VAL A 184 -56.090 49.259 -4.827 1.00246.15 C ANISOU 686 CA VAL A 184 34587 41884 17053 -3734 -11153 6619 C ATOM 687 C VAL A 184 -55.942 49.144 -3.315 1.00233.78 C ANISOU 687 C VAL A 184 32377 39563 16885 -3239 -10458 6129 C ATOM 688 O VAL A 184 -56.878 49.443 -2.571 1.00233.55 O ANISOU 688 O VAL A 184 31590 39391 17757 -2477 -10873 6286 O ATOM 689 CB VAL A 184 -55.725 50.698 -5.280 1.00252.96 C ANISOU 689 CB VAL A 184 36346 42213 17555 -3380 -11395 7747 C ATOM 690 CG1 VAL A 184 -56.155 51.735 -4.238 1.00250.70 C ANISOU 690 CG1 VAL A 184 35673 41082 18500 -2309 -11530 8278 C ATOM 691 CG2 VAL A 184 -54.228 50.806 -5.566 1.00249.20 C ANISOU 691 CG2 VAL A 184 36857 41277 16551 -4043 -10409 7632 C ATOM 692 N LEU A 185 -54.767 48.722 -2.860 1.00237.92 N ANISOU 692 N LEU A 185 33196 39619 17584 -3665 -9402 5546 N ATOM 693 CA LEU A 185 -54.559 48.449 -1.440 1.00226.38 C ANISOU 693 CA LEU A 185 31158 37538 17320 -3313 -8730 5005 C ATOM 694 C LEU A 185 -53.537 49.360 -0.784 1.00220.92 C ANISOU 694 C LEU A 185 30973 35870 17094 -3063 -8083 5290 C ATOM 695 O LEU A 185 -52.572 49.788 -1.407 1.00222.96 O ANISOU 695 O LEU A 185 32064 35925 16727 -3474 -7753 5563 O ATOM 696 CB LEU A 185 -54.142 46.993 -1.242 1.00219.35 C ANISOU 696 CB LEU A 185 29964 36938 16442 -3971 -8056 3959 C ATOM 697 CG LEU A 185 -55.176 45.959 -1.698 1.00223.80 C ANISOU 697 CG LEU A 185 29918 38401 16715 -4271 -8580 3495 C ATOM 698 CD1 LEU A 185 -54.624 44.543 -1.503 1.00217.08 C ANISOU 698 CD1 LEU A 185 28897 37675 15910 -4945 -7774 2464 C ATOM 699 CD2 LEU A 185 -56.520 46.140 -0.977 1.00224.94 C ANISOU 699 CD2 LEU A 185 29124 38633 17712 -3523 -9218 3637 C ATOM 700 N VAL A 186 -53.760 49.632 0.494 1.00221.08 N ANISOU 700 N VAL A 186 30480 35307 18215 -2432 -7874 5180 N ATOM 701 CA VAL A 186 -52.873 50.476 1.274 1.00215.86 C ANISOU 701 CA VAL A 186 30202 33717 18097 -2186 -7282 5358 C ATOM 702 C VAL A 186 -52.504 49.786 2.598 1.00204.59 C ANISOU 702 C VAL A 186 28246 31953 17536 -2144 -6571 4582 C ATOM 703 O VAL A 186 -53.379 49.256 3.313 1.00201.89 O ANISOU 703 O VAL A 186 27130 31780 17797 -1802 -6721 4232 O ATOM 704 CB VAL A 186 -53.494 51.867 1.542 1.00221.32 C ANISOU 704 CB VAL A 186 30982 33859 19252 -1351 -7780 6187 C ATOM 705 CG1 VAL A 186 -53.503 52.672 0.276 1.00232.23 C ANISOU 705 CG1 VAL A 186 33117 35376 19744 -1441 -8324 7051 C ATOM 706 CG2 VAL A 186 -54.907 51.747 2.104 1.00222.92 C ANISOU 706 CG2 VAL A 186 30262 34289 20149 -660 -8353 6157 C ATOM 707 N TRP A 187 -51.196 49.773 2.889 1.00187.35 N ANISOU 707 N TRP A 187 26478 29326 15380 -2524 -5803 4328 N ATOM 708 CA TRP A 187 -50.648 49.297 4.162 1.00177.47 C ANISOU 708 CA TRP A 187 24860 27668 14902 -2473 -5139 3720 C ATOM 709 C TRP A 187 -51.254 50.145 5.263 1.00176.15 C ANISOU 709 C TRP A 187 24410 26934 15585 -1696 -5294 3964 C ATOM 710 O TRP A 187 -51.356 51.374 5.132 1.00181.15 O ANISOU 710 O TRP A 187 25444 27123 16263 -1327 -5550 4610 O ATOM 711 CB TRP A 187 -49.126 49.446 4.188 1.00173.85 C ANISOU 711 CB TRP A 187 24937 26800 14319 -2949 -4416 3587 C ATOM 712 CG TRP A 187 -48.376 48.229 3.831 1.00170.60 C ANISOU 712 CG TRP A 187 24474 26771 13574 -3619 -3903 2953 C ATOM 713 CD1 TRP A 187 -48.260 47.117 4.578 1.00163.75 C ANISOU 713 CD1 TRP A 187 23065 25988 13165 -3691 -3520 2272 C ATOM 714 CD2 TRP A 187 -47.591 48.005 2.662 1.00174.60 C ANISOU 714 CD2 TRP A 187 25519 27568 13255 -4307 -3642 2935 C ATOM 715 NE1 TRP A 187 -47.460 46.192 3.958 1.00163.21 N ANISOU 715 NE1 TRP A 187 23125 26211 12676 -4338 -3038 1817 N ATOM 716 CE2 TRP A 187 -47.038 46.712 2.771 1.00169.81 C ANISOU 716 CE2 TRP A 187 24612 27197 12712 -4743 -3081 2179 C ATOM 717 CE3 TRP A 187 -47.312 48.762 1.519 1.00182.47 C ANISOU 717 CE3 TRP A 187 27252 28634 13443 -4606 -3796 3492 C ATOM 718 CZ2 TRP A 187 -46.216 46.155 1.788 1.00172.57 C ANISOU 718 CZ2 TRP A 187 25332 27842 12393 -5454 -2631 1904 C ATOM 719 CZ3 TRP A 187 -46.492 48.207 0.529 1.00185.19 C ANISOU 719 CZ3 TRP A 187 28005 29319 13039 -5366 -3350 3229 C ATOM 720 CH2 TRP A 187 -45.958 46.915 0.674 1.00180.22 C ANISOU 720 CH2 TRP A 187 27020 28917 12539 -5776 -2757 2413 C ATOM 721 N ARG A 188 -51.679 49.492 6.337 1.00201.58 N ANISOU 721 N ARG A 188 26974 30142 19475 -1452 -5109 3451 N ATOM 722 CA ARG A 188 -52.313 50.202 7.443 1.00200.59 C ANISOU 722 CA ARG A 188 26544 29511 20159 -740 -5176 3578 C ATOM 723 C ARG A 188 -52.107 49.476 8.757 1.00192.07 C ANISOU 723 C ARG A 188 25031 28253 19695 -716 -4634 2927 C ATOM 724 O ARG A 188 -52.224 48.249 8.836 1.00188.59 O ANISOU 724 O ARG A 188 24182 28255 19219 -1014 -4474 2408 O ATOM 725 CB ARG A 188 -53.804 50.413 7.188 1.00207.30 C ANISOU 725 CB ARG A 188 26902 30694 21168 -203 -5890 3892 C ATOM 726 CG ARG A 188 -54.412 51.492 8.078 1.00209.11 C ANISOU 726 CG ARG A 188 26985 30291 22174 589 -5975 4198 C ATOM 727 CD ARG A 188 -55.916 51.661 7.851 1.00216.45 C ANISOU 727 CD ARG A 188 27292 31574 23377 1173 -6670 4488 C ATOM 728 NE ARG A 188 -56.256 52.532 6.719 1.00226.41 N ANISOU 728 NE ARG A 188 28912 32918 24196 1390 -7360 5298 N ATOM 729 CZ ARG A 188 -57.493 52.696 6.244 1.00234.75 C ANISOU 729 CZ ARG A 188 29458 34394 25340 1852 -8117 5669 C ATOM 730 NH1 ARG A 188 -58.515 52.052 6.801 1.00234.18 N ANISOU 730 NH1 ARG A 188 28459 34699 25820 2111 -8231 5254 N ATOM 731 NH2 ARG A 188 -57.717 53.503 5.206 1.00244.38 N ANISOU 731 NH2 ARG A 188 31080 35673 26099 2050 -8772 6478 N ATOM 732 N PHE A 189 -51.795 50.258 9.781 1.00158.75 N ANISOU 732 N PHE A 189 20949 23357 16011 -378 -4347 2971 N ATOM 733 CA PHE A 189 -51.423 49.732 11.074 1.00151.32 C ANISOU 733 CA PHE A 189 19749 22182 15563 -382 -3825 2429 C ATOM 734 C PHE A 189 -52.666 49.524 11.907 1.00151.34 C ANISOU 734 C PHE A 189 19118 22246 16139 133 -3943 2250 C ATOM 735 O PHE A 189 -53.603 50.329 11.853 1.00156.90 O ANISOU 735 O PHE A 189 19691 22820 17105 669 -4318 2615 O ATOM 736 CB PHE A 189 -50.507 50.715 11.805 1.00149.47 C ANISOU 736 CB PHE A 189 19989 21221 15584 -319 -3475 2523 C ATOM 737 CG PHE A 189 -49.953 50.179 13.085 1.00142.48 C ANISOU 737 CG PHE A 189 18919 20145 15073 -405 -2980 1996 C ATOM 738 CD1 PHE A 189 -50.666 50.326 14.274 1.00141.22 C ANISOU 738 CD1 PHE A 189 18448 19739 15470 58 -2891 1809 C ATOM 739 CD2 PHE A 189 -48.740 49.527 13.104 1.00137.97 C ANISOU 739 CD2 PHE A 189 18476 19653 14295 -933 -2606 1699 C ATOM 740 CE1 PHE A 189 -50.179 49.836 15.445 1.00135.66 C ANISOU 740 CE1 PHE A 189 17633 18896 15015 -36 -2478 1371 C ATOM 741 CE2 PHE A 189 -48.240 49.044 14.275 1.00132.51 C ANISOU 741 CE2 PHE A 189 17612 18810 13923 -977 -2235 1287 C ATOM 742 CZ PHE A 189 -48.963 49.191 15.454 1.00131.33 C ANISOU 742 CZ PHE A 189 17218 18441 14238 -542 -2189 1135 C ATOM 743 N ASP A 190 -52.648 48.459 12.699 1.00146.04 N ANISOU 743 N ASP A 190 18059 21734 15694 -19 -3584 1702 N ATOM 744 CA ASP A 190 -53.699 48.218 13.654 1.00145.61 C ANISOU 744 CA ASP A 190 17439 21684 16203 396 -3536 1465 C ATOM 745 C ASP A 190 -53.164 47.518 14.904 1.00138.71 C ANISOU 745 C ASP A 190 16491 20617 15597 253 -2961 971 C ATOM 746 O ASP A 190 -52.815 46.331 14.872 1.00135.00 O ANISOU 746 O ASP A 190 15870 20455 14968 -154 -2738 621 O ATOM 747 CB ASP A 190 -54.804 47.395 13.013 1.00148.97 C ANISOU 747 CB ASP A 190 17275 22772 16554 360 -3894 1363 C ATOM 748 CG ASP A 190 -56.079 47.422 13.824 1.00151.02 C ANISOU 748 CG ASP A 190 16901 23036 17445 866 -3924 1235 C ATOM 749 OD1 ASP A 190 -55.973 47.408 15.080 1.00147.05 O ANISOU 749 OD1 ASP A 190 16360 22150 17362 1027 -3447 958 O ATOM 750 OD2 ASP A 190 -57.176 47.471 13.206 1.00157.23 O ANISOU 750 OD2 ASP A 190 17222 24227 18291 1088 -4424 1409 O ATOM 751 N SER A 191 -53.118 48.258 16.011 1.00128.60 N ANISOU 751 N SER A 191 15338 18809 14715 592 -2721 951 N ATOM 752 CA SER A 191 -52.679 47.706 17.292 1.00123.19 C ANISOU 752 CA SER A 191 14624 17942 14240 498 -2232 538 C ATOM 753 C SER A 191 -53.505 46.494 17.692 1.00121.80 C ANISOU 753 C SER A 191 13878 18152 14248 471 -2087 180 C ATOM 754 O SER A 191 -52.955 45.519 18.197 1.00117.29 O ANISOU 754 O SER A 191 13292 17655 13620 167 -1756 -124 O ATOM 755 CB SER A 191 -52.747 48.772 18.385 1.00124.12 C ANISOU 755 CB SER A 191 14960 17476 14726 886 -2037 552 C ATOM 756 OG SER A 191 -53.987 49.436 18.340 1.00129.62 O ANISOU 756 OG SER A 191 15372 18095 15784 1418 -2246 728 O ATOM 757 N LYS A 192 -54.811 46.533 17.443 1.00114.34 N ANISOU 757 N LYS A 192 12449 17450 13545 779 -2336 232 N ATOM 758 CA LYS A 192 -55.644 45.397 17.781 1.00113.86 C ANISOU 758 CA LYS A 192 11818 17756 13687 697 -2173 -125 C ATOM 759 C LYS A 192 -55.041 44.112 17.256 1.00110.47 C ANISOU 759 C LYS A 192 11397 17675 12902 125 -2066 -358 C ATOM 760 O LYS A 192 -55.235 43.040 17.821 1.00108.17 O ANISOU 760 O LYS A 192 10850 17500 12750 -61 -1727 -706 O ATOM 761 CB LYS A 192 -57.039 45.570 17.224 1.00120.25 C ANISOU 761 CB LYS A 192 12040 18912 14739 1001 -2575 -12 C ATOM 762 CG LYS A 192 -57.918 46.490 18.037 1.00124.02 C ANISOU 762 CG LYS A 192 12280 19060 15782 1615 -2500 55 C ATOM 763 CD LYS A 192 -58.431 47.688 17.231 1.00130.84 C ANISOU 763 CD LYS A 192 13117 19856 16742 2077 -3053 552 C ATOM 764 CE LYS A 192 -59.371 47.318 16.090 1.00136.56 C ANISOU 764 CE LYS A 192 13268 21233 17387 2065 -3648 699 C ATOM 765 NZ LYS A 192 -59.638 48.519 15.240 1.00143.41 N ANISOU 765 NZ LYS A 192 14263 21994 18231 2501 -4243 1301 N ATOM 766 N LEU A 193 -54.296 44.217 16.173 1.00116.75 N ANISOU 766 N LEU A 193 12518 18597 13245 -164 -2303 -170 N ATOM 767 CA LEU A 193 -53.725 43.032 15.566 1.00114.53 C ANISOU 767 CA LEU A 193 12254 18624 12639 -703 -2162 -421 C ATOM 768 C LEU A 193 -52.653 42.408 16.441 1.00108.79 C ANISOU 768 C LEU A 193 11753 17603 11977 -897 -1649 -656 C ATOM 769 O LEU A 193 -52.278 41.252 16.238 1.00106.91 O ANISOU 769 O LEU A 193 11449 17529 11642 -1268 -1406 -932 O ATOM 770 CB LEU A 193 -53.171 43.344 14.159 1.00117.08 C ANISOU 770 CB LEU A 193 12910 19161 12414 -989 -2488 -175 C ATOM 771 N ALA A 194 -52.148 43.166 17.406 1.00100.30 N ANISOU 771 N ALA A 194 10950 16087 11072 -650 -1495 -549 N ATOM 772 CA ALA A 194 -51.143 42.630 18.308 1.00 95.74 C ANISOU 772 CA ALA A 194 10560 15270 10548 -800 -1097 -727 C ATOM 773 C ALA A 194 -51.696 41.442 19.034 1.00 94.41 C ANISOU 773 C ALA A 194 10061 15200 10609 -842 -785 -1031 C ATOM 774 O ALA A 194 -50.965 40.508 19.295 1.00 91.69 O ANISOU 774 O ALA A 194 9775 14819 10244 -1080 -502 -1189 O ATOM 775 CB ALA A 194 -50.724 43.651 19.282 1.00 94.89 C ANISOU 775 CB ALA A 194 10754 14736 10563 -546 -1033 -607 C ATOM 776 N PHE A 195 -52.997 41.488 19.329 1.00103.20 N ANISOU 776 N PHE A 195 10813 16423 11975 -603 -823 -1096 N ATOM 777 CA PHE A 195 -53.668 40.492 20.157 1.00102.79 C ANISOU 777 CA PHE A 195 10456 16415 12186 -630 -466 -1373 C ATOM 778 C PHE A 195 -54.720 39.671 19.454 1.00105.85 C ANISOU 778 C PHE A 195 10346 17213 12661 -815 -534 -1574 C ATOM 779 O PHE A 195 -55.059 38.599 19.960 1.00105.43 O ANISOU 779 O PHE A 195 10091 17184 12782 -990 -172 -1834 O ATOM 780 CB PHE A 195 -54.365 41.173 21.311 1.00104.04 C ANISOU 780 CB PHE A 195 10556 16340 12633 -238 -315 -1370 C ATOM 781 CG PHE A 195 -53.500 42.114 22.052 1.00102.23 C ANISOU 781 CG PHE A 195 10808 15717 12320 -67 -273 -1224 C ATOM 782 CD1 PHE A 195 -52.749 41.676 23.122 1.00 99.30 C ANISOU 782 CD1 PHE A 195 10715 15133 11883 -166 48 -1312 C ATOM 783 CD2 PHE A 195 -53.445 43.441 21.687 1.00104.22 C ANISOU 783 CD2 PHE A 195 11245 15800 12552 177 -570 -990 C ATOM 784 CE1 PHE A 195 -51.959 42.550 23.828 1.00 98.38 C ANISOU 784 CE1 PHE A 195 11022 14699 11658 -65 49 -1221 C ATOM 785 CE2 PHE A 195 -52.662 44.323 22.382 1.00103.19 C ANISOU 785 CE2 PHE A 195 11567 15280 12358 274 -505 -911 C ATOM 786 CZ PHE A 195 -51.900 43.880 23.456 1.00100.22 C ANISOU 786 CZ PHE A 195 11439 14751 11889 128 -208 -1052 C ATOM 787 N HIS A 196 -55.270 40.182 18.342 1.00125.76 N ANISOU 787 N HIS A 196 12673 20048 15062 -785 -1001 -1443 N ATOM 788 CA HIS A 196 -56.398 39.533 17.631 1.00130.05 C ANISOU 788 CA HIS A 196 12670 21067 15677 -967 -1181 -1640 C ATOM 789 C HIS A 196 -55.918 38.969 16.337 1.00130.77 C ANISOU 789 C HIS A 196 12878 21474 15336 -1426 -1380 -1709 C ATOM 790 O HIS A 196 -55.499 39.713 15.466 1.00132.06 O ANISOU 790 O HIS A 196 13306 21723 15147 -1414 -1760 -1435 O ATOM 791 CB HIS A 196 -57.496 40.547 17.318 1.00135.44 C ANISOU 791 CB HIS A 196 12980 21942 16538 -563 -1647 -1421 C ATOM 792 CG HIS A 196 -58.695 39.956 16.648 1.00140.79 C ANISOU 792 CG HIS A 196 13006 23165 17323 -735 -1906 -1619 C ATOM 793 ND1 HIS A 196 -58.611 39.212 15.493 1.00142.57 N ANISOU 793 ND1 HIS A 196 13186 23820 17162 -1234 -2137 -1768 N ATOM 794 CD2 HIS A 196 -60.012 40.014 16.956 1.00145.51 C ANISOU 794 CD2 HIS A 196 12938 23974 18376 -505 -1972 -1723 C ATOM 795 CE1 HIS A 196 -59.820 38.818 15.126 1.00148.11 C ANISOU 795 CE1 HIS A 196 13230 24996 18050 -1335 -2377 -1962 C ATOM 796 NE2 HIS A 196 -60.689 39.296 15.995 1.00150.01 N ANISOU 796 NE2 HIS A 196 13045 25121 18831 -885 -2287 -1926 N ATOM 797 N HIS A 197 -56.019 37.663 16.182 1.00105.05 N ANISOU 797 N HIS A 197 9448 18373 12091 -1855 -1094 -2087 N ATOM 798 CA HIS A 197 -55.396 36.999 15.047 1.00105.59 C ANISOU 798 CA HIS A 197 9715 18662 11744 -2349 -1129 -2246 C ATOM 799 C HIS A 197 -56.423 36.610 13.970 1.00111.66 C ANISOU 799 C HIS A 197 10066 20022 12336 -2668 -1507 -2451 C ATOM 800 O HIS A 197 -56.703 35.443 13.756 1.00113.09 O ANISOU 800 O HIS A 197 10049 20360 12560 -3108 -1255 -2875 O ATOM 801 CB HIS A 197 -54.623 35.806 15.594 1.00101.88 C ANISOU 801 CB HIS A 197 9424 17874 11412 -2616 -508 -2535 C ATOM 802 CG HIS A 197 -53.737 35.140 14.605 1.00101.98 C ANISOU 802 CG HIS A 197 9711 17961 11077 -3070 -381 -2724 C ATOM 803 ND1 HIS A 197 -53.081 33.962 14.883 1.00100.08 N ANISOU 803 ND1 HIS A 197 9590 17441 10996 -3324 172 -3009 N ATOM 804 CD2 HIS A 197 -53.423 35.462 13.334 1.00104.54 C ANISOU 804 CD2 HIS A 197 10224 18592 10905 -3320 -692 -2681 C ATOM 805 CE1 HIS A 197 -52.394 33.592 13.822 1.00101.40 C ANISOU 805 CE1 HIS A 197 9975 17727 10824 -3702 231 -3179 C ATOM 806 NE2 HIS A 197 -52.576 34.490 12.872 1.00104.03 N ANISOU 806 NE2 HIS A 197 10377 18434 10715 -3734 -279 -2991 N ATOM 807 N MET A 198 -56.964 37.627 13.302 1.00128.11 N ANISOU 807 N MET A 198 12036 22418 14223 -2442 -2132 -2130 N ATOM 808 CA MET A 198 -58.034 37.497 12.307 1.00135.15 C ANISOU 808 CA MET A 198 12475 23947 14927 -2655 -2668 -2223 C ATOM 809 C MET A 198 -57.915 36.275 11.421 1.00137.27 C ANISOU 809 C MET A 198 12762 24556 14838 -3370 -2544 -2697 C ATOM 810 O MET A 198 -58.842 35.484 11.302 1.00141.17 O ANISOU 810 O MET A 198 12750 25392 15497 -3675 -2560 -3079 O ATOM 811 CB MET A 198 -58.029 38.712 11.377 1.00139.10 C ANISOU 811 CB MET A 198 13178 24680 14995 -2424 -3360 -1713 C ATOM 812 CG MET A 198 -58.775 39.928 11.870 1.00141.49 C ANISOU 812 CG MET A 198 13201 24874 15684 -1730 -3728 -1279 C ATOM 813 SD MET A 198 -60.558 39.758 11.908 1.00148.91 S ANISOU 813 SD MET A 198 13138 26344 17096 -1565 -4129 -1427 S ATOM 814 CE MET A 198 -60.899 39.350 10.215 1.00156.42 C ANISOU 814 CE MET A 198 13990 28117 17324 -2129 -4832 -1484 C ATOM 815 N ALA A 199 -56.770 36.151 10.766 1.00130.10 N ANISOU 815 N ALA A 199 12434 23552 13445 -3666 -2399 -2697 N ATOM 816 CA ALA A 199 -56.546 35.108 9.777 1.00132.95 C ANISOU 816 CA ALA A 199 12919 24216 13382 -4360 -2262 -3157 C ATOM 817 C ALA A 199 -56.917 33.762 10.319 1.00132.46 C ANISOU 817 C ALA A 199 12544 24033 13752 -4686 -1719 -3718 C ATOM 818 O ALA A 199 -57.531 32.982 9.651 1.00137.52 O ANISOU 818 O ALA A 199 12939 25079 14234 -5201 -1795 -4145 O ATOM 819 CB ALA A 199 -55.102 35.095 9.377 1.00129.73 C ANISOU 819 CB ALA A 199 13166 23522 12604 -4543 -1918 -3121 C ATOM 820 N ARG A 200 -56.536 33.500 11.553 1.00139.81 N ANISOU 820 N ARG A 200 13516 24390 15214 -4404 -1169 -3706 N ATOM 821 CA ARG A 200 -56.834 32.229 12.201 1.00139.39 C ANISOU 821 CA ARG A 200 13243 24105 15613 -4672 -580 -4160 C ATOM 822 C ARG A 200 -58.338 32.082 12.512 1.00143.79 C ANISOU 822 C ARG A 200 13110 24993 16531 -4683 -775 -4324 C ATOM 823 O ARG A 200 -58.855 30.979 12.649 1.00146.18 O ANISOU 823 O ARG A 200 13151 25294 17096 -5101 -405 -4788 O ATOM 824 CB ARG A 200 -56.006 32.107 13.487 1.00132.89 C ANISOU 824 CB ARG A 200 12696 22598 15200 -4310 -14 -3990 C ATOM 825 CG ARG A 200 -55.554 30.713 13.772 1.00132.06 C ANISOU 825 CG ARG A 200 12728 22108 15341 -4661 682 -4384 C ATOM 826 CD ARG A 200 -55.362 30.486 15.233 1.00128.02 C ANISOU 826 CD ARG A 200 12267 21053 15321 -4305 1138 -4218 C ATOM 827 NE ARG A 200 -55.057 29.086 15.478 1.00128.51 N ANISOU 827 NE ARG A 200 12446 20721 15659 -4632 1792 -4560 N ATOM 828 CZ ARG A 200 -54.132 28.637 16.326 1.00125.05 C ANISOU 828 CZ ARG A 200 12329 19713 15472 -4422 2257 -4407 C ATOM 829 NH1 ARG A 200 -53.376 29.475 17.043 1.00120.60 N ANISOU 829 NH1 ARG A 200 11995 18943 14885 -3928 2130 -3955 N ATOM 830 NH2 ARG A 200 -53.936 27.325 16.450 1.00126.72 N ANISOU 830 NH2 ARG A 200 12640 19540 15968 -4716 2845 -4707 N ATOM 831 N GLU A 201 -59.023 33.207 12.661 1.00127.93 N ANISOU 831 N GLU A 201 10793 23220 14595 -4212 -1310 -3945 N ATOM 832 CA GLU A 201 -60.472 33.223 12.745 1.00133.57 C ANISOU 832 CA GLU A 201 10755 24361 15635 -4198 -1608 -4075 C ATOM 833 C GLU A 201 -61.055 32.851 11.400 1.00140.86 C ANISOU 833 C GLU A 201 11407 25985 16129 -4754 -2121 -4368 C ATOM 834 O GLU A 201 -61.830 31.917 11.314 1.00145.14 O ANISOU 834 O GLU A 201 11498 26775 16875 -5231 -1978 -4858 O ATOM 835 CB GLU A 201 -60.988 34.606 13.154 1.00134.22 C ANISOU 835 CB GLU A 201 10584 24489 15923 -3487 -2067 -3566 C ATOM 836 N LEU A 202 -60.655 33.552 10.345 1.00148.93 N ANISOU 836 N LEU A 202 12745 27325 16517 -4751 -2698 -4083 N ATOM 837 CA LEU A 202 -61.251 33.359 9.012 1.00157.05 C ANISOU 837 CA LEU A 202 13550 29117 17004 -5259 -3325 -4287 C ATOM 838 C LEU A 202 -60.273 32.741 8.011 1.00157.18 C ANISOU 838 C LEU A 202 14220 29177 16325 -5880 -3133 -4575 C ATOM 839 O LEU A 202 -60.238 33.161 6.862 1.00162.12 O ANISOU 839 O LEU A 202 15044 30311 16244 -6088 -3722 -4434 O ATOM 840 CB LEU A 202 -61.723 34.713 8.470 1.00161.47 C ANISOU 840 CB LEU A 202 13949 30102 17301 -4773 -4238 -3678 C ATOM 841 CG LEU A 202 -60.925 35.969 8.760 1.00156.69 C ANISOU 841 CG LEU A 202 13862 29052 16621 -4114 -4323 -3011 C ATOM 842 CD1 LEU A 202 -61.320 37.049 7.777 1.00163.40 C ANISOU 842 CD1 LEU A 202 14692 30405 16988 -3876 -5261 -2478 C ATOM 843 CD2 LEU A 202 -61.212 36.392 10.173 1.00152.34 C ANISOU 843 CD2 LEU A 202 13022 27992 16867 -3480 -3978 -2843 C ATOM 844 N HIS A 203 -59.557 31.676 8.342 1.00160.50 N ANISOU 844 N HIS A 203 14956 29119 16907 -6233 -2321 -5014 N ATOM 845 CA HIS A 203 -60.040 30.339 8.557 1.00162.70 C ANISOU 845 CA HIS A 203 14938 29346 17535 -6781 -1819 -5677 C ATOM 846 C HIS A 203 -58.776 29.594 8.823 1.00157.28 C ANISOU 846 C HIS A 203 14870 27982 16907 -6926 -991 -5876 C ATOM 847 O HIS A 203 -57.731 29.994 8.333 1.00154.94 O ANISOU 847 O HIS A 203 15128 27570 16170 -6864 -981 -5669 O ATOM 848 CB HIS A 203 -60.637 29.743 7.258 1.00171.61 C ANISOU 848 CB HIS A 203 15899 31195 18108 -7573 -2207 -6193 C ATOM 849 CG HIS A 203 -59.664 28.932 6.409 1.00172.35 C ANISOU 849 CG HIS A 203 16646 31164 17673 -8207 -1756 -6650 C ATOM 850 ND1 HIS A 203 -59.327 27.617 6.682 1.00171.55 N ANISOU 850 ND1 HIS A 203 16701 30572 17907 -8667 -896 -7257 N ATOM 851 CD2 HIS A 203 -58.999 29.248 5.267 1.00174.80 C ANISOU 851 CD2 HIS A 203 17492 31775 17150 -8472 -2014 -6604 C ATOM 852 CE1 HIS A 203 -58.475 27.178 5.773 1.00173.23 C ANISOU 852 CE1 HIS A 203 17489 30760 17571 -9141 -622 -7584 C ATOM 853 NE2 HIS A 203 -58.268 28.144 4.897 1.00175.25 N ANISOU 853 NE2 HIS A 203 17985 31519 17083 -9063 -1278 -7215 N ATOM 854 N PRO A 204 -58.867 28.489 9.544 1.00142.47 N ANISOU 854 N PRO A 204 12893 25662 15579 -7143 -288 -6278 N ATOM 855 CA PRO A 204 -57.751 27.587 9.786 1.00138.85 C ANISOU 855 CA PRO A 204 12953 24532 15272 -7301 529 -6513 C ATOM 856 C PRO A 204 -56.968 27.050 8.547 1.00141.99 C ANISOU 856 C PRO A 204 13830 25028 15092 -7882 706 -6926 C ATOM 857 O PRO A 204 -57.319 26.024 7.933 1.00147.68 O ANISOU 857 O PRO A 204 14510 25879 15725 -8581 957 -7580 O ATOM 858 CB PRO A 204 -58.397 26.464 10.580 1.00140.21 C ANISOU 858 CB PRO A 204 12819 24364 16090 -7548 1111 -6911 C ATOM 859 CG PRO A 204 -59.476 27.147 11.321 1.00140.35 C ANISOU 859 CG PRO A 204 12254 24629 16443 -7156 727 -6611 C ATOM 860 CD PRO A 204 -60.001 28.208 10.431 1.00143.95 C ANISOU 860 CD PRO A 204 12453 25845 16394 -7070 -194 -6383 C ATOM 861 N GLU A 205 -55.918 27.810 8.209 1.00150.32 N ANISOU 861 N GLU A 205 15341 26014 15761 -7599 596 -6549 N ATOM 862 CA GLU A 205 -54.699 27.336 7.538 1.00150.33 C ANISOU 862 CA GLU A 205 15900 25753 15467 -7896 1097 -6808 C ATOM 863 C GLU A 205 -53.706 26.954 8.639 1.00143.90 C ANISOU 863 C GLU A 205 15273 24099 15302 -7458 1797 -6641 C ATOM 864 O GLU A 205 -52.502 26.934 8.404 1.00141.99 O ANISOU 864 O GLU A 205 15427 23553 14971 -7401 2154 -6607 O ATOM 865 CB GLU A 205 -54.099 28.460 6.680 1.00150.49 C ANISOU 865 CB GLU A 205 16269 26142 14767 -7792 612 -6420 C ATOM 866 CG GLU A 205 -54.793 28.651 5.351 1.00158.34 C ANISOU 866 CG GLU A 205 17261 27951 14952 -8343 3 -6632 C ATOM 867 CD GLU A 205 -55.037 30.090 5.012 1.00158.84 C ANISOU 867 CD GLU A 205 17332 28483 14537 -7967 -849 -5964 C ATOM 868 OE1 GLU A 205 -55.133 30.902 5.954 1.00153.73 O ANISOU 868 OE1 GLU A 205 16489 27593 14330 -7282 -1052 -5409 O ATOM 869 OE2 GLU A 205 -55.150 30.400 3.799 1.00165.02 O ANISOU 869 OE2 GLU A 205 18350 29863 14488 -8373 -1305 -5996 O ATOM 870 N TYR A 206 -54.235 26.659 9.840 1.00146.52 N ANISOU 870 N TYR A 206 15302 24090 16279 -7158 1979 -6526 N ATOM 871 CA TYR A 206 -53.468 26.499 11.098 1.00140.59 C ANISOU 871 CA TYR A 206 14683 22621 16114 -6627 2457 -6200 C ATOM 872 C TYR A 206 -53.852 25.185 11.821 1.00142.12 C ANISOU 872 C TYR A 206 14764 22314 16920 -6818 3106 -6542 C ATOM 873 O TYR A 206 -55.028 24.976 12.137 1.00144.58 O ANISOU 873 O TYR A 206 14699 22816 17420 -6978 3000 -6682 O ATOM 874 CB TYR A 206 -53.727 27.674 12.054 1.00135.86 C ANISOU 874 CB TYR A 206 13913 22071 15638 -5973 2004 -5568 C ATOM 875 CG TYR A 206 -53.534 29.049 11.456 1.00134.97 C ANISOU 875 CG TYR A 206 13893 22392 14998 -5749 1345 -5173 C ATOM 876 CD1 TYR A 206 -54.436 29.560 10.547 1.00139.63 C ANISOU 876 CD1 TYR A 206 14270 23649 15134 -5984 727 -5225 C ATOM 877 CD2 TYR A 206 -52.474 29.852 11.826 1.00130.16 C ANISOU 877 CD2 TYR A 206 13576 21520 14361 -5303 1318 -4721 C ATOM 878 CE1 TYR A 206 -54.287 30.810 10.002 1.00139.64 C ANISOU 878 CE1 TYR A 206 14404 23991 14662 -5760 130 -4801 C ATOM 879 CE2 TYR A 206 -52.315 31.115 11.285 1.00129.96 C ANISOU 879 CE2 TYR A 206 13677 21823 13878 -5129 764 -4348 C ATOM 880 CZ TYR A 206 -53.232 31.585 10.370 1.00134.75 C ANISOU 880 CZ TYR A 206 14123 23040 14035 -5343 181 -4367 C ATOM 881 OH TYR A 206 -53.094 32.839 9.831 1.00135.32 O ANISOU 881 OH TYR A 206 14370 23385 13659 -5146 -368 -3932 O ATOM 882 N TYR A 207 -52.848 24.333 12.089 1.00142.90 N ANISOU 882 N TYR A 207 15177 21757 17361 -6781 3782 -6645 N ATOM 883 CA TYR A 207 -53.021 22.999 12.703 1.00145.15 C ANISOU 883 CA TYR A 207 15480 21428 18241 -6959 4491 -6937 C ATOM 884 C TYR A 207 -53.862 22.065 11.839 1.00152.29 C ANISOU 884 C TYR A 207 16269 22524 19070 -7752 4703 -7677 C ATOM 885 O TYR A 207 -55.083 22.199 11.767 1.00155.05 O ANISOU 885 O TYR A 207 16237 23344 19332 -8030 4355 -7833 O ATOM 886 CB TYR A 207 -53.628 23.109 14.104 1.00142.38 C ANISOU 886 CB TYR A 207 14932 20849 18316 -6558 4496 -6534 C TER 887 TYR A 207 ATOM 888 N ASP B 80 -13.593 34.711 30.052 1.00190.76 N ANISOU 888 N ASP B 80 20146 21267 31066 307 -1125 4720 N ATOM 889 CA ASP B 80 -14.692 35.160 29.135 1.00184.67 C ANISOU 889 CA ASP B 80 19764 20469 29934 29 -685 4220 C ATOM 890 C ASP B 80 -14.276 35.054 27.670 1.00182.21 C ANISOU 890 C ASP B 80 19286 19649 30297 -249 -272 3546 C ATOM 891 O ASP B 80 -13.121 35.260 27.342 1.00183.32 O ANISOU 891 O ASP B 80 19165 19627 30861 -291 -375 3224 O ATOM 892 CB ASP B 80 -15.099 36.613 29.442 1.00180.95 C ANISOU 892 CB ASP B 80 19733 20604 28415 -42 -876 3918 C ATOM 893 CG ASP B 80 -15.646 36.794 30.866 1.00183.26 C ANISOU 893 CG ASP B 80 20208 21483 27941 147 -1223 4477 C ATOM 894 OD1 ASP B 80 -16.718 37.445 31.015 1.00180.12 O ANISOU 894 OD1 ASP B 80 20200 21425 26814 68 -1133 4359 O ATOM 895 OD2 ASP B 80 -15.000 36.283 31.826 1.00188.65 O ANISOU 895 OD2 ASP B 80 20620 22306 28753 364 -1585 5030 O ATOM 896 N ILE B 81 -15.216 34.706 26.801 1.00161.05 N ANISOU 896 N ILE B 81 16726 16759 27705 -466 204 3312 N ATOM 897 CA ILE B 81 -14.994 34.770 25.361 1.00158.41 C ANISOU 897 CA ILE B 81 16298 16105 27786 -814 616 2610 C ATOM 898 C ILE B 81 -15.269 36.188 24.875 1.00153.56 C ANISOU 898 C ILE B 81 16109 15882 26354 -995 582 2125 C ATOM 899 O ILE B 81 -16.400 36.691 25.022 1.00150.75 O ANISOU 899 O ILE B 81 16135 15876 25269 -986 605 2196 O ATOM 900 CB ILE B 81 -15.966 33.879 24.590 1.00157.60 C ANISOU 900 CB ILE B 81 16140 15731 28012 -1019 1155 2508 C ATOM 901 CG1 ILE B 81 -15.807 32.424 24.955 1.00162.69 C ANISOU 901 CG1 ILE B 81 16367 15880 29568 -874 1312 2960 C ATOM 902 CG2 ILE B 81 -15.734 33.997 23.099 1.00155.34 C ANISOU 902 CG2 ILE B 81 15743 15234 28046 -1437 1573 1754 C ATOM 903 CD1 ILE B 81 -16.741 31.537 24.148 1.00162.25 C ANISOU 903 CD1 ILE B 81 16213 15544 29890 -1133 1920 2752 C ATOM 904 N ILE B 82 -14.265 36.826 24.264 1.00140.57 N ANISOU 904 N ILE B 82 14391 14150 24869 -1167 558 1625 N ATOM 905 CA ILE B 82 -14.432 38.188 23.733 1.00136.65 C ANISOU 905 CA ILE B 82 14295 13941 23683 -1352 566 1182 C ATOM 906 C ILE B 82 -14.460 38.225 22.211 1.00134.52 C ANISOU 906 C ILE B 82 14015 13457 23639 -1765 1012 604 C ATOM 907 O ILE B 82 -13.841 37.400 21.542 1.00136.39 O ANISOU 907 O ILE B 82 13862 13303 24658 -1961 1273 353 O ATOM 908 CB ILE B 82 -13.336 39.151 24.211 1.00137.51 C ANISOU 908 CB ILE B 82 14423 14208 23617 -1288 217 1011 C ATOM 909 CG1 ILE B 82 -12.930 38.884 25.666 1.00141.27 C ANISOU 909 CG1 ILE B 82 14723 14895 24058 -928 -241 1542 C ATOM 910 CG2 ILE B 82 -13.828 40.563 24.062 1.00134.08 C ANISOU 910 CG2 ILE B 82 14476 14106 22363 -1371 194 764 C ATOM 911 CD1 ILE B 82 -13.968 39.267 26.670 1.00140.53 C ANISOU 911 CD1 ILE B 82 14963 15269 23162 -726 -446 1962 C ATOM 912 N VAL B 83 -15.191 39.195 21.678 1.00111.47 N ANISOU 912 N VAL B 83 11508 10815 20029 -1903 1101 399 N ATOM 913 CA VAL B 83 -15.303 39.382 20.234 1.00109.76 C ANISOU 913 CA VAL B 83 11337 10529 19838 -2315 1486 -98 C ATOM 914 C VAL B 83 -15.100 40.846 19.862 1.00107.77 C ANISOU 914 C VAL B 83 11474 10469 19002 -2428 1402 -365 C ATOM 915 O VAL B 83 -15.372 41.749 20.662 1.00106.87 O ANISOU 915 O VAL B 83 11670 10602 18333 -2177 1117 -155 O ATOM 916 CB VAL B 83 -16.680 38.905 19.684 1.00108.28 C ANISOU 916 CB VAL B 83 11227 10498 19416 -2418 1781 -35 C ATOM 917 CG1 VAL B 83 -16.866 37.439 19.969 1.00110.67 C ANISOU 917 CG1 VAL B 83 11138 10539 20373 -2359 1958 177 C ATOM 918 CG2 VAL B 83 -17.826 39.702 20.275 1.00106.08 C ANISOU 918 CG2 VAL B 83 11375 10628 18302 -2165 1574 276 C ATOM 919 N VAL B 84 -14.599 41.085 18.656 1.00105.45 N ANISOU 919 N VAL B 84 11154 10053 18860 -2830 1681 -844 N ATOM 920 CA VAL B 84 -14.523 42.438 18.145 1.00103.98 C ANISOU 920 CA VAL B 84 11367 10011 18128 -2977 1679 -1058 C ATOM 921 C VAL B 84 -15.385 42.576 16.925 1.00102.68 C ANISOU 921 C VAL B 84 11373 10026 17616 -3277 1984 -1189 C ATOM 922 O VAL B 84 -15.469 41.684 16.090 1.00103.43 O ANISOU 922 O VAL B 84 11184 10064 18053 -3584 2298 -1411 O ATOM 923 CB VAL B 84 -13.148 42.821 17.735 1.00105.37 C ANISOU 923 CB VAL B 84 11433 9952 18649 -3240 1738 -1505 C ATOM 924 CG1 VAL B 84 -13.110 44.333 17.569 1.00104.28 C ANISOU 924 CG1 VAL B 84 11765 9942 17914 -3287 1683 -1603 C ATOM 925 CG2 VAL B 84 -12.143 42.339 18.757 1.00107.66 C ANISOU 925 CG2 VAL B 84 11372 10061 19474 -3005 1476 -1445 C ATOM 926 N ALA B 85 -15.994 43.737 16.811 1.00107.95 N ANISOU 926 N ALA B 85 12480 10924 17612 -3200 1898 -1067 N ATOM 927 CA ALA B 85 -17.004 43.940 15.812 1.00107.15 C ANISOU 927 CA ALA B 85 12554 11093 17063 -3383 2094 -1052 C ATOM 928 C ALA B 85 -16.358 44.272 14.503 1.00108.18 C ANISOU 928 C ALA B 85 12709 11180 17216 -3884 2371 -1450 C ATOM 929 O ALA B 85 -15.692 45.284 14.382 1.00108.56 O ANISOU 929 O ALA B 85 13010 11115 17122 -3958 2330 -1563 O ATOM 930 CB ALA B 85 -17.922 45.043 16.243 1.00105.92 C ANISOU 930 CB ALA B 85 12826 11167 16250 -3060 1881 -718 C ATOM 931 N LEU B 86 -16.554 43.408 13.528 1.00129.02 N ANISOU 931 N LEU B 86 15069 13920 20031 -4264 2686 -1693 N ATOM 932 CA LEU B 86 -15.987 43.616 12.223 1.00130.51 C ANISOU 932 CA LEU B 86 15241 14146 20202 -4822 2989 -2105 C ATOM 933 C LEU B 86 -16.859 44.505 11.373 1.00130.55 C ANISOU 933 C LEU B 86 15617 14556 19431 -4937 3018 -1922 C ATOM 934 O LEU B 86 -16.450 44.891 10.281 1.00132.20 O ANISOU 934 O LEU B 86 15903 14861 19464 -5403 3239 -2174 O ATOM 935 CB LEU B 86 -15.786 42.288 11.499 1.00132.10 C ANISOU 935 CB LEU B 86 14926 14320 20946 -5252 3363 -2524 C ATOM 936 CG LEU B 86 -14.872 41.268 12.170 1.00133.10 C ANISOU 936 CG LEU B 86 14598 13990 21984 -5175 3391 -2714 C ATOM 937 CD1 LEU B 86 -13.997 40.698 11.107 1.00135.54 C ANISOU 937 CD1 LEU B 86 14532 14157 22810 -5787 3808 -3350 C ATOM 938 CD2 LEU B 86 -14.031 41.867 13.300 1.00132.66 C ANISOU 938 CD2 LEU B 86 14679 13640 22084 -4781 3026 -2539 C ATOM 939 N TYR B 87 -18.065 44.804 11.825 1.00133.01 N ANISOU 939 N TYR B 87 16131 15125 19282 -4538 2807 -1483 N ATOM 940 CA TYR B 87 -18.926 45.698 11.065 1.00133.65 C ANISOU 940 CA TYR B 87 16542 15587 18651 -4573 2786 -1238 C ATOM 941 C TYR B 87 -19.867 46.388 12.026 1.00132.20 C ANISOU 941 C TYR B 87 16644 15464 18123 -3981 2459 -759 C ATOM 942 O TYR B 87 -19.893 46.060 13.166 1.00130.77 O ANISOU 942 O TYR B 87 16383 15109 18196 -3634 2293 -662 O ATOM 943 CB TYR B 87 -19.711 44.929 9.989 1.00134.92 C ANISOU 943 CB TYR B 87 16438 16235 18591 -4940 3033 -1373 C ATOM 944 CG TYR B 87 -18.926 43.849 9.279 1.00136.36 C ANISOU 944 CG TYR B 87 16175 16350 19284 -5509 3410 -1938 C ATOM 945 CD1 TYR B 87 -18.372 44.066 8.038 1.00138.75 C ANISOU 945 CD1 TYR B 87 16468 16820 19429 -6106 3678 -2266 C ATOM 946 CD2 TYR B 87 -18.744 42.599 9.864 1.00135.82 C ANISOU 946 CD2 TYR B 87 15679 16035 19892 -5460 3522 -2143 C ATOM 947 CE1 TYR B 87 -17.639 43.068 7.391 1.00140.44 C ANISOU 947 CE1 TYR B 87 16229 16966 20165 -6668 4067 -2868 C ATOM 948 CE2 TYR B 87 -18.019 41.597 9.235 1.00137.64 C ANISOU 948 CE2 TYR B 87 15455 16134 20709 -5968 3905 -2694 C ATOM 949 CZ TYR B 87 -17.463 41.837 7.990 1.00139.89 C ANISOU 949 CZ TYR B 87 15708 16599 20844 -6587 4188 -3098 C ATOM 950 OH TYR B 87 -16.738 40.858 7.333 1.00142.10 O ANISOU 950 OH TYR B 87 15499 16755 21736 -7143 4613 -3727 O ATOM 951 N ASP B 88 -20.606 47.376 11.566 1.00115.79 N ANISOU 951 N ASP B 88 14889 13629 15477 -3876 2373 -456 N ATOM 952 CA ASP B 88 -21.671 47.938 12.345 1.00114.92 C ANISOU 952 CA ASP B 88 14976 13623 15065 -3347 2112 -53 C ATOM 953 C ASP B 88 -22.864 47.020 12.220 1.00114.54 C ANISOU 953 C ASP B 88 14653 14008 14858 -3294 2137 10 C ATOM 954 O ASP B 88 -23.083 46.434 11.173 1.00115.83 O ANISOU 954 O ASP B 88 14601 14512 14898 -3681 2345 -161 O ATOM 955 CB ASP B 88 -22.059 49.304 11.803 1.00116.80 C ANISOU 955 CB ASP B 88 15613 13937 14831 -3246 2034 266 C ATOM 956 CG ASP B 88 -21.131 50.420 12.274 1.00117.21 C ANISOU 956 CG ASP B 88 15993 13505 15035 -3147 1990 264 C ATOM 957 OD1 ASP B 88 -21.009 51.443 11.549 1.00119.55 O ANISOU 957 OD1 ASP B 88 16601 13743 15080 -3253 2050 429 O ATOM 958 OD2 ASP B 88 -20.529 50.293 13.369 1.00115.65 O ANISOU 958 OD2 ASP B 88 15738 13005 15198 -2974 1905 108 O ATOM 959 N TYR B 89 -23.640 46.891 13.293 1.00104.08 N ANISOU 959 N TYR B 89 13318 12702 13523 -2852 1951 212 N ATOM 960 CA TYR B 89 -24.961 46.239 13.253 1.00103.97 C ANISOU 960 CA TYR B 89 13101 13121 13283 -2738 1960 302 C ATOM 961 C TYR B 89 -25.983 47.145 13.866 1.00103.92 C ANISOU 961 C TYR B 89 13336 13230 12918 -2250 1707 652 C ATOM 962 O TYR B 89 -25.754 47.675 14.945 1.00102.97 O ANISOU 962 O TYR B 89 13396 12808 12920 -1933 1540 756 O ATOM 963 CB TYR B 89 -24.949 44.949 14.072 1.00102.61 C ANISOU 963 CB TYR B 89 12611 12833 13545 -2708 2043 159 C ATOM 964 CG TYR B 89 -26.327 44.302 14.220 1.00102.55 C ANISOU 964 CG TYR B 89 12412 13220 13332 -2568 2076 229 C ATOM 965 CD1 TYR B 89 -26.871 43.568 13.194 1.00103.84 C ANISOU 965 CD1 TYR B 89 12282 13790 13382 -2912 2326 13 C ATOM 966 CD2 TYR B 89 -27.075 44.431 15.375 1.00101.56 C ANISOU 966 CD2 TYR B 89 12377 13098 13114 -2138 1886 457 C ATOM 967 CE1 TYR B 89 -28.098 42.989 13.304 1.00104.08 C ANISOU 967 CE1 TYR B 89 12113 14197 13234 -2817 2386 15 C ATOM 968 CE2 TYR B 89 -28.311 43.855 15.480 1.00101.74 C ANISOU 968 CE2 TYR B 89 12220 13480 12957 -2046 1947 472 C ATOM 969 CZ TYR B 89 -28.814 43.131 14.431 1.00102.98 C ANISOU 969 CZ TYR B 89 12082 14020 13024 -2381 2199 246 C ATOM 970 OH TYR B 89 -30.052 42.542 14.472 1.00103.49 O ANISOU 970 OH TYR B 89 11932 14482 12908 -2328 2296 195 O ATOM 971 N VAL B 90 -27.119 47.320 13.218 1.00110.62 N ANISOU 971 N VAL B 90 14150 14541 13339 -2191 1679 805 N ATOM 972 CA VAL B 90 -28.219 47.998 13.900 1.00110.76 C ANISOU 972 CA VAL B 90 14303 14672 13110 -1699 1456 1087 C ATOM 973 C VAL B 90 -29.376 47.056 14.173 1.00110.30 C ANISOU 973 C VAL B 90 13942 15005 12962 -1613 1495 1020 C ATOM 974 O VAL B 90 -29.918 46.424 13.255 1.00111.50 O ANISOU 974 O VAL B 90 13835 15613 12919 -1871 1636 900 O ATOM 975 CB VAL B 90 -28.730 49.214 13.133 1.00113.46 C ANISOU 975 CB VAL B 90 14873 15186 13052 -1553 1327 1404 C ATOM 976 CG1 VAL B 90 -30.025 49.720 13.718 1.00114.15 C ANISOU 976 CG1 VAL B 90 14979 15453 12939 -1063 1131 1636 C ATOM 977 CG2 VAL B 90 -27.726 50.280 13.210 1.00114.01 C ANISOU 977 CG2 VAL B 90 15290 14768 13259 -1532 1296 1498 C ATOM 978 N SER B 91 -29.746 46.974 15.446 1.00104.89 N ANISOU 978 N SER B 91 13281 14171 12401 -1285 1392 1066 N ATOM 979 CA SER B 91 -30.873 46.191 15.842 1.00104.66 C ANISOU 979 CA SER B 91 13010 14470 12286 -1179 1440 1008 C ATOM 980 C SER B 91 -32.114 47.050 15.678 1.00106.37 C ANISOU 980 C SER B 91 13285 15028 12101 -848 1267 1202 C ATOM 981 O SER B 91 -32.047 48.261 15.874 1.00107.19 O ANISOU 981 O SER B 91 13663 14930 12135 -572 1085 1414 O ATOM 982 CB SER B 91 -30.717 45.740 17.288 1.00103.02 C ANISOU 982 CB SER B 91 12811 13984 12348 -1006 1410 999 C ATOM 983 OG SER B 91 -31.417 46.598 18.159 1.00103.27 O ANISOU 983 OG SER B 91 13016 14029 12191 -607 1214 1149 O ATOM 984 N TRP B 92 -33.232 46.420 15.299 1.00117.91 N ANISOU 984 N TRP B 92 14460 16996 13344 -882 1346 1105 N ATOM 985 CA TRP B 92 -34.550 47.062 15.354 1.00119.71 C ANISOU 985 CA TRP B 92 14657 17577 13251 -517 1174 1248 C ATOM 986 C TRP B 92 -35.355 46.575 16.538 1.00118.70 C ANISOU 986 C TRP B 92 14421 17481 13198 -309 1201 1126 C ATOM 987 O TRP B 92 -36.502 47.008 16.730 1.00120.20 O ANISOU 987 O TRP B 92 14538 17953 13179 -7 1086 1169 O ATOM 988 CB TRP B 92 -35.404 46.762 14.129 1.00122.22 C ANISOU 988 CB TRP B 92 14680 18559 13200 -679 1218 1197 C ATOM 989 CG TRP B 92 -34.790 47.092 12.833 1.00124.03 C ANISOU 989 CG TRP B 92 14953 18931 13240 -967 1220 1302 C ATOM 990 CD1 TRP B 92 -33.649 47.777 12.621 1.00123.80 C ANISOU 990 CD1 TRP B 92 15234 18469 13334 -1048 1179 1462 C ATOM 991 CD2 TRP B 92 -35.284 46.734 11.549 1.00126.80 C ANISOU 991 CD2 TRP B 92 15013 19959 13205 -1265 1289 1225 C ATOM 992 NE1 TRP B 92 -33.391 47.859 11.284 1.00126.22 N ANISOU 992 NE1 TRP B 92 15486 19117 13355 -1390 1227 1509 N ATOM 993 CE2 TRP B 92 -34.388 47.225 10.606 1.00128.19 C ANISOU 993 CE2 TRP B 92 15360 20082 13266 -1532 1283 1372 C ATOM 994 CE3 TRP B 92 -36.395 46.033 11.113 1.00128.55 C ANISOU 994 CE3 TRP B 92 14826 20871 13147 -1364 1372 1011 C ATOM 995 CZ2 TRP B 92 -34.568 47.060 9.267 1.00131.41 C ANISOU 995 CZ2 TRP B 92 15555 21125 13250 -1899 1338 1347 C ATOM 996 CZ3 TRP B 92 -36.575 45.871 9.774 1.00131.75 C ANISOU 996 CZ3 TRP B 92 14991 21930 13140 -1719 1420 959 C ATOM 997 CH2 TRP B 92 -35.667 46.384 8.862 1.00133.24 C ANISOU 997 CH2 TRP B 92 15366 22079 13180 -1989 1396 1140 C ATOM 998 N SER B 93 -34.795 45.651 17.315 1.00106.74 N ANISOU 998 N SER B 93 12871 15700 11983 -476 1360 983 N ATOM 999 CA SER B 93 -35.542 45.069 18.420 1.00106.22 C ANISOU 999 CA SER B 93 12707 15695 11958 -347 1425 889 C ATOM 1000 C SER B 93 -34.758 45.034 19.682 1.00104.74 C ANISOU 1000 C SER B 93 12714 15064 12019 -280 1380 967 C ATOM 1001 O SER B 93 -33.599 44.626 19.686 1.00103.72 O ANISOU 1001 O SER B 93 12626 14612 12170 -484 1436 984 O ATOM 1002 CB SER B 93 -35.934 43.642 18.130 1.00106.30 C ANISOU 1002 CB SER B 93 12382 15953 12056 -661 1733 645 C ATOM 1003 OG SER B 93 -36.361 43.024 19.326 1.00105.83 O ANISOU 1003 OG SER B 93 12294 15815 12104 -584 1827 607 O ATOM 1004 N PRO B 94 -35.414 45.358 20.778 1.00 91.33 N ANISOU 1004 N PRO B 94 11086 13397 10218 -24 1294 986 N ATOM 1005 CA PRO B 94 -34.725 45.462 21.996 1.00 90.61 C ANISOU 1005 CA PRO B 94 11170 12995 10263 34 1216 1068 C ATOM 1006 C PRO B 94 -34.200 44.141 22.441 1.00 89.95 C ANISOU 1006 C PRO B 94 10967 12783 10427 -207 1384 1084 C ATOM 1007 O PRO B 94 -33.559 44.055 23.455 1.00 89.82 O ANISOU 1007 O PRO B 94 11056 12558 10513 -186 1306 1200 O ATOM 1008 CB PRO B 94 -35.798 45.935 22.938 1.00 91.68 C ANISOU 1008 CB PRO B 94 11326 13325 10182 288 1153 1011 C ATOM 1009 CG PRO B 94 -36.890 46.344 22.094 1.00 92.94 C ANISOU 1009 CG PRO B 94 11355 13810 10150 429 1143 934 C ATOM 1010 CD PRO B 94 -36.844 45.474 20.980 1.00 92.66 C ANISOU 1010 CD PRO B 94 11119 13946 10143 168 1299 883 C ATOM 1011 N ASP B 95 -34.475 43.094 21.705 1.00114.65 N ANISOU 1011 N ASP B 95 13850 16045 13669 -442 1626 971 N ATOM 1012 CA ASP B 95 -33.892 41.820 22.027 1.00114.60 C ANISOU 1012 CA ASP B 95 13706 15815 14021 -670 1827 1007 C ATOM 1013 C ASP B 95 -32.520 41.650 21.370 1.00113.98 C ANISOU 1013 C ASP B 95 13612 15399 14296 -871 1842 1018 C ATOM 1014 O ASP B 95 -31.694 40.896 21.855 1.00114.18 O ANISOU 1014 O ASP B 95 13577 15112 14692 -970 1902 1126 O ATOM 1015 CB ASP B 95 -34.861 40.713 21.604 1.00115.53 C ANISOU 1015 CB ASP B 95 13526 16196 14175 -863 2162 808 C ATOM 1016 CG ASP B 95 -36.198 40.757 22.385 1.00116.42 C ANISOU 1016 CG ASP B 95 13632 16626 13977 -695 2184 759 C ATOM 1017 OD1 ASP B 95 -36.269 41.447 23.442 1.00116.43 O ANISOU 1017 OD1 ASP B 95 13851 16593 13795 -464 1968 901 O ATOM 1018 OD2 ASP B 95 -37.169 40.083 21.943 1.00117.41 O ANISOU 1018 OD2 ASP B 95 13507 17056 14047 -829 2445 525 O ATOM 1019 N ASP B 96 -32.266 42.362 20.279 1.00110.96 N ANISOU 1019 N ASP B 96 13273 15079 13807 -930 1784 923 N ATOM 1020 CA ASP B 96 -31.006 42.239 19.552 1.00110.63 C ANISOU 1020 CA ASP B 96 13204 14754 14077 -1173 1835 863 C ATOM 1021 C ASP B 96 -30.123 43.434 19.904 1.00110.05 C ANISOU 1021 C ASP B 96 13435 14428 13952 -1001 1554 995 C ATOM 1022 O ASP B 96 -30.629 44.558 20.090 1.00110.19 O ANISOU 1022 O ASP B 96 13663 14565 13638 -748 1367 1073 O ATOM 1023 CB ASP B 96 -31.271 42.204 18.055 1.00111.28 C ANISOU 1023 CB ASP B 96 13127 15121 14034 -1435 1998 648 C ATOM 1024 CG ASP B 96 -32.266 41.119 17.660 1.00112.29 C ANISOU 1024 CG ASP B 96 12917 15589 14158 -1628 2302 431 C ATOM 1025 OD1 ASP B 96 -32.243 40.057 18.315 1.00112.47 O ANISOU 1025 OD1 ASP B 96 12785 15419 14527 -1697 2499 414 O ATOM 1026 OD2 ASP B 96 -33.073 41.308 16.703 1.00113.35 O ANISOU 1026 OD2 ASP B 96 12923 16196 13950 -1719 2357 284 O ATOM 1027 N LEU B 97 -28.809 43.198 19.999 1.00 90.41 N ANISOU 1027 N LEU B 97 10940 11577 11835 -1139 1548 991 N ATOM 1028 CA LEU B 97 -27.861 44.210 20.527 1.00 90.16 C ANISOU 1028 CA LEU B 97 11156 11294 11805 -1003 1310 1066 C ATOM 1029 C LEU B 97 -27.164 44.968 19.440 1.00 90.18 C ANISOU 1029 C LEU B 97 11274 11183 11806 -1167 1324 945 C ATOM 1030 O LEU B 97 -26.183 44.501 18.899 1.00 90.26 O ANISOU 1030 O LEU B 97 11160 10984 12149 -1438 1442 805 O ATOM 1031 CB LEU B 97 -26.782 43.564 21.395 1.00 90.45 C ANISOU 1031 CB LEU B 97 11097 11035 12234 -1033 1254 1140 C ATOM 1032 CG LEU B 97 -25.714 44.490 21.965 1.00 90.60 C ANISOU 1032 CG LEU B 97 11300 10848 12275 -942 1029 1148 C ATOM 1033 CD1 LEU B 97 -26.356 45.495 22.835 1.00 90.78 C ANISOU 1033 CD1 LEU B 97 11549 11045 11896 -669 849 1226 C ATOM 1034 CD2 LEU B 97 -24.690 43.711 22.754 1.00 91.53 C ANISOU 1034 CD2 LEU B 97 11243 10756 12780 -969 951 1243 C ATOM 1035 N SER B 98 -27.671 46.146 19.131 1.00103.74 N ANISOU 1035 N SER B 98 13221 13019 13177 -1006 1219 1005 N ATOM 1036 CA SER B 98 -27.043 46.997 18.148 1.00104.35 C ANISOU 1036 CA SER B 98 13464 12973 13210 -1149 1233 961 C ATOM 1037 C SER B 98 -25.619 47.191 18.609 1.00104.08 C ANISOU 1037 C SER B 98 13504 12547 13494 -1236 1187 863 C ATOM 1038 O SER B 98 -25.410 47.431 19.789 1.00103.92 O ANISOU 1038 O SER B 98 13548 12419 13517 -1028 1038 911 O ATOM 1039 CB SER B 98 -27.761 48.361 18.061 1.00105.45 C ANISOU 1039 CB SER B 98 13868 13191 13007 -865 1099 1127 C ATOM 1040 OG SER B 98 -28.937 48.313 17.241 1.00106.45 O ANISOU 1040 OG SER B 98 13904 13717 12826 -830 1130 1216 O ATOM 1041 N PHE B 99 -24.646 47.041 17.705 1.00 96.40 N ANISOU 1041 N PHE B 99 12484 11410 12733 -1570 1324 692 N ATOM 1042 CA PHE B 99 -23.247 47.392 18.018 1.00 96.55 C ANISOU 1042 CA PHE B 99 12572 11066 13047 -1667 1286 547 C ATOM 1043 C PHE B 99 -22.512 48.098 16.884 1.00 97.52 C ANISOU 1043 C PHE B 99 12852 11043 13158 -1956 1414 404 C ATOM 1044 O PHE B 99 -22.952 48.073 15.738 1.00 98.23 O ANISOU 1044 O PHE B 99 12941 11338 13044 -2158 1550 415 O ATOM 1045 CB PHE B 99 -22.436 46.178 18.452 1.00 96.31 C ANISOU 1045 CB PHE B 99 12227 10877 13489 -1802 1326 426 C ATOM 1046 CG PHE B 99 -22.316 45.142 17.407 1.00 96.58 C ANISOU 1046 CG PHE B 99 11980 10939 13775 -2160 1588 242 C ATOM 1047 CD1 PHE B 99 -21.573 45.350 16.296 1.00 97.30 C ANISOU 1047 CD1 PHE B 99 12072 10935 13963 -2524 1761 -7 C ATOM 1048 CD2 PHE B 99 -22.962 43.942 17.547 1.00 96.48 C ANISOU 1048 CD2 PHE B 99 11688 11055 13916 -2169 1702 282 C ATOM 1049 CE1 PHE B 99 -21.479 44.391 15.346 1.00 97.96 C ANISOU 1049 CE1 PHE B 99 11858 11084 14278 -2904 2039 -247 C ATOM 1050 CE2 PHE B 99 -22.869 42.984 16.590 1.00 97.17 C ANISOU 1050 CE2 PHE B 99 11475 11164 14279 -2533 2000 40 C ATOM 1051 CZ PHE B 99 -22.123 43.212 15.489 1.00 97.92 C ANISOU 1051 CZ PHE B 99 11550 11197 14458 -2909 2166 -243 C ATOM 1052 N GLN B 100 -21.370 48.692 17.241 1.00124.79 N ANISOU 1052 N GLN B 100 16419 14179 16815 -2000 1377 255 N ATOM 1053 CA GLN B 100 -20.546 49.478 16.341 1.00126.03 C ANISOU 1053 CA GLN B 100 16767 14134 16984 -2279 1515 99 C ATOM 1054 C GLN B 100 -19.239 48.779 16.052 1.00126.21 C ANISOU 1054 C GLN B 100 16552 13949 17452 -2639 1647 -247 C ATOM 1055 O GLN B 100 -18.651 48.191 16.943 1.00125.78 O ANISOU 1055 O GLN B 100 16280 13775 17736 -2550 1543 -342 O ATOM 1056 CB GLN B 100 -20.214 50.788 17.003 1.00126.85 C ANISOU 1056 CB GLN B 100 17170 14003 17026 -2074 1423 114 C ATOM 1057 CG GLN B 100 -21.254 51.836 16.881 1.00127.84 C ANISOU 1057 CG GLN B 100 17583 14197 16793 -1810 1384 399 C ATOM 1058 CD GLN B 100 -20.826 52.922 15.927 1.00130.01 C ANISOU 1058 CD GLN B 100 18164 14247 16988 -1996 1544 418 C ATOM 1059 OE1 GLN B 100 -21.296 52.986 14.791 1.00131.18 O ANISOU 1059 OE1 GLN B 100 18387 14564 16892 -2141 1630 606 O ATOM 1060 NE2 GLN B 100 -19.899 53.768 16.373 1.00131.02 N ANISOU 1060 NE2 GLN B 100 18457 14017 17307 -2025 1600 218 N ATOM 1061 N LYS B 101 -18.776 48.869 14.811 1.00107.61 N ANISOU 1061 N LYS B 101 14226 11566 15095 -3050 1873 -430 N ATOM 1062 CA LYS B 101 -17.549 48.206 14.384 1.00108.19 C ANISOU 1062 CA LYS B 101 14040 11442 15627 -3451 2051 -834 C ATOM 1063 C LYS B 101 -16.403 48.575 15.290 1.00108.43 C ANISOU 1063 C LYS B 101 14064 11148 15987 -3357 1936 -1026 C ATOM 1064 O LYS B 101 -16.214 49.725 15.582 1.00109.01 O ANISOU 1064 O LYS B 101 14444 11095 15877 -3242 1880 -994 O ATOM 1065 CB LYS B 101 -17.248 48.570 12.931 1.00109.91 C ANISOU 1065 CB LYS B 101 14378 11711 15672 -3935 2320 -1004 C ATOM 1066 CG LYS B 101 -15.778 48.661 12.517 1.00111.24 C ANISOU 1066 CG LYS B 101 14481 11574 16213 -4352 2514 -1459 C ATOM 1067 CD LYS B 101 -15.642 48.676 10.973 1.00113.25 C ANISOU 1067 CD LYS B 101 14767 12000 16263 -4928 2829 -1647 C ATOM 1068 CE LYS B 101 -14.737 49.811 10.483 1.00115.25 C ANISOU 1068 CE LYS B 101 15355 12008 16427 -5206 2975 -1799 C ATOM 1069 NZ LYS B 101 -14.225 49.628 9.086 1.00117.64 N ANISOU 1069 NZ LYS B 101 15600 12439 16661 -5880 3321 -2123 N ATOM 1070 N GLY B 102 -15.656 47.583 15.747 1.00100.21 N ANISOU 1070 N GLY B 102 12639 9979 15455 -3401 1909 -1228 N ATOM 1071 CA GLY B 102 -14.584 47.799 16.699 1.00100.90 C ANISOU 1071 CA GLY B 102 12632 9852 15852 -3283 1747 -1397 C ATOM 1072 C GLY B 102 -14.992 47.638 18.156 1.00100.33 C ANISOU 1072 C GLY B 102 12499 9904 15719 -2819 1426 -1099 C ATOM 1073 O GLY B 102 -14.150 47.651 19.059 1.00101.36 O ANISOU 1073 O GLY B 102 12472 9961 16080 -2704 1245 -1201 O ATOM 1074 N ASP B 103 -16.285 47.485 18.405 1.00115.45 N ANISOU 1074 N ASP B 103 14516 12056 17294 -2572 1351 -741 N ATOM 1075 CA ASP B 103 -16.753 47.222 19.756 1.00115.22 C ANISOU 1075 CA ASP B 103 14416 12189 17172 -2188 1080 -457 C ATOM 1076 C ASP B 103 -16.362 45.838 20.242 1.00115.93 C ANISOU 1076 C ASP B 103 14082 12234 17733 -2151 1006 -383 C ATOM 1077 O ASP B 103 -16.287 44.881 19.473 1.00116.05 O ANISOU 1077 O ASP B 103 13851 12137 18105 -2369 1210 -476 O ATOM 1078 CB ASP B 103 -18.262 47.393 19.844 1.00113.99 C ANISOU 1078 CB ASP B 103 14461 12293 16557 -1965 1056 -141 C ATOM 1079 CG ASP B 103 -18.695 48.856 19.803 1.00114.07 C ANISOU 1079 CG ASP B 103 14868 12325 16150 -1854 1048 -119 C ATOM 1080 OD1 ASP B 103 -17.818 49.766 19.824 1.00115.11 O ANISOU 1080 OD1 ASP B 103 15142 12258 16337 -1946 1071 -346 O ATOM 1081 OD2 ASP B 103 -19.922 49.097 19.761 1.00113.47 O ANISOU 1081 OD2 ASP B 103 14941 12443 15731 -1669 1036 112 O ATOM 1082 N GLN B 104 -16.098 45.766 21.540 1.00111.23 N ANISOU 1082 N GLN B 104 13386 11732 17143 -1885 723 -215 N ATOM 1083 CA GLN B 104 -15.766 44.519 22.213 1.00112.74 C ANISOU 1083 CA GLN B 104 13192 11890 17755 -1767 592 -8 C ATOM 1084 C GLN B 104 -16.958 44.021 23.009 1.00112.37 C ANISOU 1084 C GLN B 104 13183 12094 17420 -1500 484 431 C ATOM 1085 O GLN B 104 -17.499 44.741 23.864 1.00112.20 O ANISOU 1085 O GLN B 104 13385 12343 16903 -1296 303 577 O ATOM 1086 CB GLN B 104 -14.608 44.716 23.171 1.00115.10 C ANISOU 1086 CB GLN B 104 13310 12204 18218 -1662 312 -65 C ATOM 1087 CG GLN B 104 -13.278 44.576 22.519 1.00116.42 C ANISOU 1087 CG GLN B 104 13227 12073 18935 -1914 413 -464 C ATOM 1088 CD GLN B 104 -12.164 45.022 23.421 1.00118.90 C ANISOU 1088 CD GLN B 104 13385 12479 19311 -1822 131 -597 C ATOM 1089 OE1 GLN B 104 -12.085 46.181 23.785 1.00118.77 O ANISOU 1089 OE1 GLN B 104 13622 12629 18876 -1812 63 -767 O ATOM 1090 NE2 GLN B 104 -11.294 44.097 23.794 1.00121.65 N ANISOU 1090 NE2 GLN B 104 13281 12726 20215 -1752 -25 -531 N ATOM 1091 N MET B 105 -17.363 42.788 22.736 1.00104.81 N ANISOU 1091 N MET B 105 11991 11037 16796 -1530 635 597 N ATOM 1092 CA MET B 105 -18.481 42.203 23.419 1.00104.78 C ANISOU 1092 CA MET B 105 12005 11234 16571 -1324 594 988 C ATOM 1093 C MET B 105 -18.062 40.861 24.017 1.00107.48 C ANISOU 1093 C MET B 105 11969 11403 17465 -1230 541 1290 C ATOM 1094 O MET B 105 -17.136 40.199 23.530 1.00108.96 O ANISOU 1094 O MET B 105 11838 11257 18306 -1369 648 1141 O ATOM 1095 CB MET B 105 -19.624 42.025 22.448 1.00102.82 C ANISOU 1095 CB MET B 105 11860 11050 16158 -1460 895 910 C ATOM 1096 CG MET B 105 -20.137 43.305 21.867 1.00100.92 C ANISOU 1096 CG MET B 105 11976 10979 15388 -1501 924 726 C ATOM 1097 SD MET B 105 -21.205 43.058 20.446 1.00 99.53 S ANISOU 1097 SD MET B 105 11824 10922 15073 -1731 1265 583 S ATOM 1098 CE MET B 105 -20.102 42.812 19.055 1.00100.10 C ANISOU 1098 CE MET B 105 11703 10724 15605 -2178 1534 163 C ATOM 1099 N VAL B 106 -18.746 40.491 25.096 1.00121.43 N ANISOU 1099 N VAL B 106 13768 13391 18980 -996 383 1725 N ATOM 1100 CA VAL B 106 -18.581 39.210 25.747 1.00124.55 C ANISOU 1100 CA VAL B 106 13855 13635 19832 -871 344 2147 C ATOM 1101 C VAL B 106 -19.703 38.338 25.260 1.00123.80 C ANISOU 1101 C VAL B 106 13732 13453 19852 -954 699 2223 C ATOM 1102 O VAL B 106 -20.866 38.738 25.358 1.00121.91 O ANISOU 1102 O VAL B 106 13759 13514 19047 -923 751 2245 O ATOM 1103 CB VAL B 106 -18.780 39.338 27.243 1.00126.69 C ANISOU 1103 CB VAL B 106 14213 14271 19654 -611 -12 2607 C ATOM 1104 CG1 VAL B 106 -18.854 37.971 27.859 1.00130.24 C ANISOU 1104 CG1 VAL B 106 14398 14565 20524 -482 -7 3145 C ATOM 1105 CG2 VAL B 106 -17.665 40.120 27.859 1.00128.24 C ANISOU 1105 CG2 VAL B 106 14372 14636 19718 -539 -371 2526 C ATOM 1106 N VAL B 107 -19.385 37.160 24.732 1.00114.27 N ANISOU 1106 N VAL B 107 12175 11840 19402 -1072 970 2219 N ATOM 1107 CA VAL B 107 -20.441 36.259 24.302 1.00114.12 C ANISOU 1107 CA VAL B 107 12083 11740 19539 -1185 1360 2244 C ATOM 1108 C VAL B 107 -20.973 35.608 25.551 1.00116.72 C ANISOU 1108 C VAL B 107 12421 12151 19775 -938 1236 2842 C ATOM 1109 O VAL B 107 -20.201 35.252 26.432 1.00120.05 O ANISOU 1109 O VAL B 107 12690 12463 20459 -742 967 3252 O ATOM 1110 CB VAL B 107 -19.956 35.188 23.331 1.00115.74 C ANISOU 1110 CB VAL B 107 11874 11461 20641 -1436 1767 1981 C ATOM 1111 CG1 VAL B 107 -21.126 34.401 22.802 1.00115.48 C ANISOU 1111 CG1 VAL B 107 11771 11424 20683 -1613 2219 1883 C ATOM 1112 CG2 VAL B 107 -19.226 35.811 22.175 1.00113.98 C ANISOU 1112 CG2 VAL B 107 11616 11170 20522 -1718 1867 1402 C ATOM 1113 N LEU B 108 -22.292 35.486 25.637 1.00106.60 N ANISOU 1113 N LEU B 108 11315 11103 18085 -956 1419 2900 N ATOM 1114 CA LEU B 108 -22.954 34.822 26.762 1.00109.23 C ANISOU 1114 CA LEU B 108 11685 11529 18287 -785 1382 3443 C ATOM 1115 C LEU B 108 -23.601 33.502 26.347 1.00110.95 C ANISOU 1115 C LEU B 108 11672 11421 19063 -930 1879 3479 C ATOM 1116 O LEU B 108 -23.665 32.556 27.133 1.00114.77 O ANISOU 1116 O LEU B 108 12040 11706 19863 -816 1927 3990 O ATOM 1117 CB LEU B 108 -24.008 35.743 27.351 1.00107.13 C ANISOU 1117 CB LEU B 108 11796 11809 17098 -701 1220 3454 C ATOM 1118 CG LEU B 108 -23.469 37.069 27.872 1.00105.98 C ANISOU 1118 CG LEU B 108 11873 11991 16405 -576 785 3390 C ATOM 1119 CD1 LEU B 108 -24.573 37.923 28.437 1.00104.45 C ANISOU 1119 CD1 LEU B 108 12000 12283 15401 -511 694 3350 C ATOM 1120 CD2 LEU B 108 -22.420 36.824 28.928 1.00109.75 C ANISOU 1120 CD2 LEU B 108 12213 12448 17040 -406 428 3836 C ATOM 1121 N GLU B 109 -24.076 33.452 25.107 1.00157.17 N ANISOU 1121 N GLU B 109 17451 17240 25028 -1201 2264 2936 N ATOM 1122 CA GLU B 109 -24.675 32.255 24.550 1.00158.83 C ANISOU 1122 CA GLU B 109 17393 17170 25786 -1415 2810 2807 C ATOM 1123 C GLU B 109 -24.249 32.098 23.095 1.00157.82 C ANISOU 1123 C GLU B 109 16990 16836 26139 -1751 3153 2183 C ATOM 1124 O GLU B 109 -24.467 32.999 22.288 1.00154.52 O ANISOU 1124 O GLU B 109 16722 16760 25229 -1897 3116 1754 O ATOM 1125 CB GLU B 109 -26.193 32.373 24.614 1.00157.27 C ANISOU 1125 CB GLU B 109 17400 17390 24964 -1466 2988 2716 C ATOM 1126 CG GLU B 109 -26.948 31.138 24.142 1.00159.32 C ANISOU 1126 CG GLU B 109 17386 17425 25725 -1707 3589 2550 C ATOM 1127 CD GLU B 109 -28.361 31.457 23.684 1.00156.99 C ANISOU 1127 CD GLU B 109 17215 17629 24807 -1854 3800 2172 C ATOM 1128 OE1 GLU B 109 -28.535 31.715 22.470 1.00155.08 O ANISOU 1128 OE1 GLU B 109 16851 17564 24507 -2108 3997 1612 O ATOM 1129 OE2 GLU B 109 -29.281 31.455 24.541 1.00157.47 O ANISOU 1129 OE2 GLU B 109 17474 17935 24422 -1725 3759 2436 O ATOM 1130 N GLU B 110 -23.649 30.951 22.771 1.00171.57 N ANISOU 1130 N GLU B 110 18315 18020 28853 -1887 3501 2142 N ATOM 1131 CA GLU B 110 -23.233 30.630 21.396 1.00171.51 C ANISOU 1131 CA GLU B 110 17970 17800 29396 -2282 3915 1489 C ATOM 1132 C GLU B 110 -24.194 29.633 20.733 1.00172.92 C ANISOU 1132 C GLU B 110 17885 17916 29901 -2608 4561 1143 C ATOM 1133 O GLU B 110 -23.776 28.865 19.857 1.00175.05 O ANISOU 1133 O GLU B 110 17731 17827 30953 -2940 5027 698 O ATOM 1134 CB GLU B 110 -21.844 29.968 21.385 1.00175.03 C ANISOU 1134 CB GLU B 110 18027 17613 30864 -2267 3950 1544 C ATOM 1135 CG GLU B 110 -20.708 30.684 22.092 1.00175.06 C ANISOU 1135 CG GLU B 110 18151 17592 30771 -1957 3363 1875 C ATOM 1136 CD GLU B 110 -19.514 29.750 22.295 1.00179.91 C ANISOU 1136 CD GLU B 110 18305 17541 32511 -1866 3417 2061 C ATOM 1137 OE1 GLU B 110 -18.433 30.010 21.718 1.00180.01 O ANISOU 1137 OE1 GLU B 110 18114 17373 32909 -1989 3369 1690 O ATOM 1138 OE2 GLU B 110 -19.671 28.734 23.011 1.00184.04 O ANISOU 1138 OE2 GLU B 110 18655 17702 33571 -1678 3533 2578 O ATOM 1139 N SER B 111 -25.461 29.619 21.125 1.00153.74 N ANISOU 1139 N SER B 111 15661 15835 26917 -2552 4631 1277 N ATOM 1140 CA SER B 111 -26.305 28.501 20.723 1.00156.15 C ANISOU 1140 CA SER B 111 15671 16003 27654 -2834 5271 1012 C ATOM 1141 C SER B 111 -26.405 28.353 19.202 1.00155.64 C ANISOU 1141 C SER B 111 15284 16091 27761 -3341 5737 184 C ATOM 1142 O SER B 111 -26.181 27.259 18.674 1.00159.07 O ANISOU 1142 O SER B 111 15264 16086 29091 -3646 6303 -143 O ATOM 1143 CB SER B 111 -27.701 28.569 21.356 1.00155.39 C ANISOU 1143 CB SER B 111 15843 16321 26879 -2722 5283 1213 C ATOM 1144 OG SER B 111 -27.793 27.708 22.490 1.00159.09 O ANISOU 1144 OG SER B 111 16311 16383 27751 -2509 5357 1823 O ATOM 1145 N GLY B 112 -26.724 29.442 18.504 1.00139.32 N ANISOU 1145 N GLY B 112 13430 14645 24860 -3447 5515 -146 N ATOM 1146 CA GLY B 112 -26.985 29.370 17.063 1.00139.21 C ANISOU 1146 CA GLY B 112 13133 14955 24804 -3958 5926 -899 C ATOM 1147 C GLY B 112 -25.962 30.094 16.223 1.00137.86 C ANISOU 1147 C GLY B 112 12956 14840 24583 -4139 5748 -1199 C ATOM 1148 O GLY B 112 -24.796 30.191 16.600 1.00138.28 O ANISOU 1148 O GLY B 112 13018 14442 25079 -3973 5515 -975 O ATOM 1149 N GLU B 113 -26.411 30.574 15.063 1.00162.50 N ANISOU 1149 N GLU B 113 16037 18547 27157 -4502 5876 -1713 N ATOM 1150 CA GLU B 113 -25.675 31.574 14.270 1.00160.78 C ANISOU 1150 CA GLU B 113 15958 18563 26570 -4657 5627 -1923 C ATOM 1151 C GLU B 113 -25.855 32.961 14.863 1.00157.32 C ANISOU 1151 C GLU B 113 16082 18433 25261 -4212 4981 -1442 C ATOM 1152 O GLU B 113 -25.128 33.848 14.519 1.00156.02 O ANISOU 1152 O GLU B 113 16108 18316 24855 -4227 4715 -1464 O ATOM 1153 CB GLU B 113 -26.176 31.612 12.819 1.00161.56 C ANISOU 1153 CB GLU B 113 15821 19267 26297 -5219 5980 -2577 C ATOM 1154 CG GLU B 113 -26.042 30.286 12.025 1.00165.47 C ANISOU 1154 CG GLU B 113 15690 19563 27617 -5794 6715 -3240 C ATOM 1155 CD GLU B 113 -25.015 30.343 10.880 1.00166.92 C ANISOU 1155 CD GLU B 113 15610 19733 28077 -6322 6941 -3812 C ATOM 1156 OE1 GLU B 113 -25.283 29.698 9.850 1.00169.69 O ANISOU 1156 OE1 GLU B 113 15513 20372 28591 -6919 7498 -4493 O ATOM 1157 OE2 GLU B 113 -23.957 31.025 10.992 1.00165.60 O ANISOU 1157 OE2 GLU B 113 15660 19310 27952 -6186 6596 -3635 O ATOM 1158 N TRP B 114 -26.876 33.139 15.695 1.00121.77 N ANISOU 1158 N TRP B 114 11818 14150 20298 -3862 4789 -1072 N ATOM 1159 CA TRP B 114 -27.095 34.357 16.470 1.00119.06 C ANISOU 1159 CA TRP B 114 11969 14020 19249 -3410 4221 -613 C ATOM 1160 C TRP B 114 -26.725 34.077 17.910 1.00119.45 C ANISOU 1160 C TRP B 114 12142 13629 19615 -3011 3991 -86 C ATOM 1161 O TRP B 114 -27.145 33.067 18.476 1.00121.37 O ANISOU 1161 O TRP B 114 12213 13662 20242 -2975 4237 54 O ATOM 1162 CB TRP B 114 -28.554 34.788 16.437 1.00118.05 C ANISOU 1162 CB TRP B 114 11992 14496 18367 -3306 4164 -599 C ATOM 1163 CG TRP B 114 -28.940 35.433 15.207 1.00117.69 C ANISOU 1163 CG TRP B 114 11935 14998 17784 -3562 4188 -933 C ATOM 1164 CD1 TRP B 114 -29.247 34.834 14.062 1.00119.53 C ANISOU 1164 CD1 TRP B 114 11799 15534 18082 -4037 4610 -1437 C ATOM 1165 CD2 TRP B 114 -29.085 36.822 14.988 1.00115.97 C ANISOU 1165 CD2 TRP B 114 12077 15126 16862 -3368 3778 -766 C ATOM 1166 NE1 TRP B 114 -29.575 35.749 13.115 1.00119.21 N ANISOU 1166 NE1 TRP B 114 11865 16070 17359 -4159 4456 -1561 N ATOM 1167 CE2 TRP B 114 -29.477 36.990 13.660 1.00117.07 C ANISOU 1167 CE2 TRP B 114 12053 15791 16637 -3731 3946 -1122 C ATOM 1168 CE3 TRP B 114 -28.902 37.949 15.784 1.00114.09 C ANISOU 1168 CE3 TRP B 114 12265 14801 16285 -2939 3307 -357 C ATOM 1169 CZ2 TRP B 114 -29.698 38.230 13.094 1.00116.54 C ANISOU 1169 CZ2 TRP B 114 12254 16131 15897 -3645 3638 -1000 C ATOM 1170 CZ3 TRP B 114 -29.122 39.189 15.227 1.00113.41 C ANISOU 1170 CZ3 TRP B 114 12436 15058 15597 -2858 3046 -297 C ATOM 1171 CH2 TRP B 114 -29.514 39.321 13.887 1.00114.72 C ANISOU 1171 CH2 TRP B 114 12451 15710 15425 -3192 3201 -575 C ATOM 1172 N TRP B 115 -25.969 34.986 18.508 1.00120.33 N ANISOU 1172 N TRP B 115 12550 13639 19533 -2729 3532 210 N ATOM 1173 CA TRP B 115 -25.395 34.769 19.813 1.00121.33 C ANISOU 1173 CA TRP B 115 12750 13410 19939 -2395 3272 695 C ATOM 1174 C TRP B 115 -25.833 35.848 20.744 1.00119.48 C ANISOU 1174 C TRP B 115 12935 13491 18971 -2033 2820 1035 C ATOM 1175 O TRP B 115 -26.024 36.968 20.315 1.00117.37 O ANISOU 1175 O TRP B 115 12911 13534 18151 -2014 2635 894 O ATOM 1176 CB TRP B 115 -23.889 34.840 19.730 1.00122.13 C ANISOU 1176 CB TRP B 115 12737 13108 20558 -2426 3142 662 C ATOM 1177 CG TRP B 115 -23.245 33.827 18.866 1.00124.41 C ANISOU 1177 CG TRP B 115 12574 13011 21686 -2786 3580 286 C ATOM 1178 CD1 TRP B 115 -23.781 32.665 18.414 1.00126.51 C ANISOU 1178 CD1 TRP B 115 12490 13147 22431 -3045 4093 60 C ATOM 1179 CD2 TRP B 115 -21.894 33.857 18.401 1.00125.35 C ANISOU 1179 CD2 TRP B 115 12499 12789 22340 -2945 3578 45 C ATOM 1180 NE1 TRP B 115 -22.856 31.978 17.676 1.00128.77 N ANISOU 1180 NE1 TRP B 115 12365 13024 23538 -3364 4427 -323 N ATOM 1181 CE2 TRP B 115 -21.685 32.686 17.659 1.00128.08 C ANISOU 1181 CE2 TRP B 115 12364 12800 23499 -3303 4107 -334 C ATOM 1182 CE3 TRP B 115 -20.843 34.768 18.538 1.00124.42 C ANISOU 1182 CE3 TRP B 115 12546 12615 22112 -2841 3213 63 C ATOM 1183 CZ2 TRP B 115 -20.476 32.404 17.043 1.00129.87 C ANISOU 1183 CZ2 TRP B 115 12265 12645 24434 -3558 4271 -701 C ATOM 1184 CZ3 TRP B 115 -19.654 34.491 17.936 1.00126.05 C ANISOU 1184 CZ3 TRP B 115 12449 12462 22983 -3087 3361 -286 C ATOM 1185 CH2 TRP B 115 -19.472 33.318 17.194 1.00128.75 C ANISOU 1185 CH2 TRP B 115 12305 12475 24140 -3440 3880 -665 C ATOM 1186 N LYS B 116 -25.972 35.518 22.021 1.00118.64 N ANISOU 1186 N LYS B 116 12903 13299 18876 -1762 2658 1487 N ATOM 1187 CA LYS B 116 -26.301 36.512 23.020 1.00117.48 C ANISOU 1187 CA LYS B 116 13114 13454 18068 -1455 2248 1770 C ATOM 1188 C LYS B 116 -25.000 37.018 23.540 1.00117.90 C ANISOU 1188 C LYS B 116 13228 13317 18253 -1316 1895 1936 C ATOM 1189 O LYS B 116 -24.093 36.226 23.779 1.00120.24 O ANISOU 1189 O LYS B 116 13280 13239 19168 -1321 1915 2101 O ATOM 1190 CB LYS B 116 -27.091 35.915 24.166 1.00119.20 C ANISOU 1190 CB LYS B 116 13376 13756 18159 -1292 2259 2155 C ATOM 1191 CG LYS B 116 -27.675 36.952 25.096 1.00118.15 C ANISOU 1191 CG LYS B 116 13583 14028 17282 -1052 1920 2320 C ATOM 1192 CD LYS B 116 -29.026 36.496 25.605 1.00118.94 C ANISOU 1192 CD LYS B 116 13721 14374 17095 -1033 2106 2412 C ATOM 1193 CE LYS B 116 -29.433 37.197 26.896 1.00119.35 C ANISOU 1193 CE LYS B 116 14044 14754 16551 -816 1794 2668 C ATOM 1194 NZ LYS B 116 -30.621 36.534 27.546 1.00120.99 N ANISOU 1194 NZ LYS B 116 14260 15146 16564 -836 2010 2805 N ATOM 1195 N ALA B 117 -24.904 38.333 23.709 1.00117.10 N ANISOU 1195 N ALA B 117 13420 13462 17612 -1191 1588 1875 N ATOM 1196 CA ALA B 117 -23.672 38.956 24.174 1.00117.57 C ANISOU 1196 CA ALA B 117 13534 13402 17736 -1090 1265 1941 C ATOM 1197 C ALA B 117 -23.952 40.178 25.018 1.00116.76 C ANISOU 1197 C ALA B 117 13754 13636 16975 -880 944 2022 C ATOM 1198 O ALA B 117 -25.096 40.651 25.113 1.00115.60 O ANISOU 1198 O ALA B 117 13798 13786 16340 -809 972 1993 O ATOM 1199 CB ALA B 117 -22.800 39.322 23.012 1.00116.57 C ANISOU 1199 CB ALA B 117 13339 13074 17881 -1313 1360 1552 C ATOM 1200 N ARG B 118 -22.885 40.660 25.647 1.00130.17 N ANISOU 1200 N ARG B 118 15465 15289 18702 -792 657 2086 N ATOM 1201 CA ARG B 118 -22.922 41.868 26.461 1.00130.00 C ANISOU 1201 CA ARG B 118 15697 15564 18132 -644 381 2073 C ATOM 1202 C ARG B 118 -21.865 42.849 25.975 1.00129.32 C ANISOU 1202 C ARG B 118 15680 15341 18117 -721 290 1753 C ATOM 1203 O ARG B 118 -20.774 42.456 25.551 1.00130.08 O ANISOU 1203 O ARG B 118 15571 15155 18697 -835 304 1661 O ATOM 1204 CB ARG B 118 -22.674 41.546 27.929 1.00132.91 C ANISOU 1204 CB ARG B 118 16000 16134 18365 -491 110 2453 C ATOM 1205 CG ARG B 118 -22.810 42.772 28.805 1.00133.17 C ANISOU 1205 CG ARG B 118 16255 16538 17805 -397 -119 2357 C ATOM 1206 CD ARG B 118 -22.850 42.448 30.280 1.00136.41 C ANISOU 1206 CD ARG B 118 16612 17301 17918 -298 -358 2730 C ATOM 1207 NE ARG B 118 -21.619 41.800 30.726 1.00139.43 N ANISOU 1207 NE ARG B 118 16728 17592 18655 -269 -579 3000 N ATOM 1208 CZ ARG B 118 -21.478 40.497 30.981 1.00141.92 C ANISOU 1208 CZ ARG B 118 16822 17753 19349 -221 -575 3457 C ATOM 1209 NH1 ARG B 118 -22.503 39.639 30.843 1.00141.67 N ANISOU 1209 NH1 ARG B 118 16809 17630 19387 -232 -318 3671 N ATOM 1210 NH2 ARG B 118 -20.288 40.047 31.393 1.00145.19 N ANISOU 1210 NH2 ARG B 118 16967 18093 20106 -155 -821 3704 N ATOM 1211 N SER B 119 -22.192 44.130 26.040 1.00127.38 N ANISOU 1211 N SER B 119 15706 15266 17428 -668 227 1563 N ATOM 1212 CA SER B 119 -21.287 45.147 25.552 1.00126.99 C ANISOU 1212 CA SER B 119 15762 15060 17430 -761 201 1246 C ATOM 1213 C SER B 119 -20.421 45.630 26.664 1.00129.06 C ANISOU 1213 C SER B 119 15987 15456 17596 -688 -64 1231 C ATOM 1214 O SER B 119 -20.937 46.205 27.622 1.00129.89 O ANISOU 1214 O SER B 119 16213 15866 17273 -565 -189 1277 O ATOM 1215 CB SER B 119 -22.056 46.340 25.022 1.00125.54 C ANISOU 1215 CB SER B 119 15881 14932 16885 -733 303 1063 C ATOM 1216 OG SER B 119 -21.315 47.524 25.222 1.00126.23 O ANISOU 1216 OG SER B 119 16114 14954 16893 -746 225 824 O ATOM 1217 N LEU B 120 -19.107 45.449 26.509 1.00108.38 N ANISOU 1217 N LEU B 120 13175 12638 15365 -792 -134 1107 N ATOM 1218 CA LEU B 120 -18.145 45.806 27.560 1.00110.99 C ANISOU 1218 CA LEU B 120 13387 13156 15629 -742 -411 1070 C ATOM 1219 C LEU B 120 -18.152 47.304 27.760 1.00110.83 C ANISOU 1219 C LEU B 120 13623 13255 15234 -766 -401 723 C ATOM 1220 O LEU B 120 -17.767 47.804 28.816 1.00113.11 O ANISOU 1220 O LEU B 120 13861 13848 15269 -728 -598 650 O ATOM 1221 CB LEU B 120 -16.731 45.316 27.235 1.00112.47 C ANISOU 1221 CB LEU B 120 13274 13090 16369 -849 -470 951 C ATOM 1222 CG LEU B 120 -16.467 43.815 27.370 1.00114.22 C ANISOU 1222 CG LEU B 120 13143 13180 17073 -783 -532 1322 C ATOM 1223 CD1 LEU B 120 -17.166 43.075 26.286 1.00112.05 C ANISOU 1223 CD1 LEU B 120 12878 12613 17084 -885 -206 1346 C ATOM 1224 CD2 LEU B 120 -15.007 43.506 27.294 1.00116.58 C ANISOU 1224 CD2 LEU B 120 13103 13285 17907 -841 -653 1180 C ATOM 1225 N ALA B 121 -18.601 48.008 26.728 1.00120.96 N ANISOU 1225 N ALA B 121 15161 14306 16491 -841 -154 515 N ATOM 1226 CA ALA B 121 -18.786 49.440 26.803 1.00121.08 C ANISOU 1226 CA ALA B 121 15443 14333 16229 -840 -74 230 C ATOM 1227 C ALA B 121 -20.068 49.773 27.545 1.00121.15 C ANISOU 1227 C ALA B 121 15588 14636 15809 -662 -98 366 C ATOM 1228 O ALA B 121 -20.039 50.341 28.632 1.00123.13 O ANISOU 1228 O ALA B 121 15827 15168 15790 -622 -209 249 O ATOM 1229 CB ALA B 121 -18.830 50.030 25.404 1.00119.45 C ANISOU 1229 CB ALA B 121 15458 13764 16165 -968 189 58 C ATOM 1230 N THR B 122 -21.188 49.373 26.955 1.00139.28 N ANISOU 1230 N THR B 122 17972 16904 18045 -585 21 571 N ATOM 1231 CA THR B 122 -22.506 49.884 27.315 1.00139.17 C ANISOU 1231 CA THR B 122 18114 17081 17682 -426 70 615 C ATOM 1232 C THR B 122 -23.149 49.064 28.421 1.00140.07 C ANISOU 1232 C THR B 122 18090 17575 17554 -337 -66 864 C ATOM 1233 O THR B 122 -24.114 49.508 29.032 1.00140.69 O ANISOU 1233 O THR B 122 18253 17886 17318 -235 -48 834 O ATOM 1234 CB THR B 122 -23.471 49.881 26.076 1.00137.21 C ANISOU 1234 CB THR B 122 18000 16677 17458 -384 258 702 C ATOM 1235 OG1 THR B 122 -24.021 48.578 25.881 1.00136.17 O ANISOU 1235 OG1 THR B 122 17706 16659 17372 -390 273 952 O ATOM 1236 CG2 THR B 122 -22.756 50.282 24.774 1.00136.51 C ANISOU 1236 CG2 THR B 122 18011 16235 17621 -543 398 569 C ATOM 1237 N ARG B 123 -22.623 47.862 28.648 1.00154.19 N ANISOU 1237 N ARG B 123 19661 19402 19523 -383 -180 1116 N ATOM 1238 CA ARG B 123 -23.216 46.886 29.561 1.00155.40 C ANISOU 1238 CA ARG B 123 19691 19858 19498 -319 -276 1454 C ATOM 1239 C ARG B 123 -24.612 46.421 29.152 1.00153.84 C ANISOU 1239 C ARG B 123 19561 19693 19200 -256 -93 1582 C ATOM 1240 O ARG B 123 -25.260 45.675 29.901 1.00154.97 O ANISOU 1240 O ARG B 123 19636 20080 19165 -222 -117 1836 O ATOM 1241 CB ARG B 123 -23.262 47.420 30.988 1.00158.13 C ANISOU 1241 CB ARG B 123 20035 20641 19406 -299 -452 1415 C ATOM 1242 CG ARG B 123 -21.918 47.467 31.664 1.00160.71 C ANISOU 1242 CG ARG B 123 20186 21102 19776 -369 -689 1390 C ATOM 1243 CD ARG B 123 -21.362 46.067 31.954 1.00162.35 C ANISOU 1243 CD ARG B 123 20139 21326 20220 -349 -862 1851 C ATOM 1244 NE ARG B 123 -22.180 45.324 32.923 1.00164.30 N ANISOU 1244 NE ARG B 123 20355 21935 20138 -301 -934 2252 N ATOM 1245 CZ ARG B 123 -21.797 44.955 34.150 1.00168.29 C ANISOU 1245 CZ ARG B 123 20702 22875 20365 -308 -1203 2551 C ATOM 1246 NH1 ARG B 123 -20.576 45.232 34.618 1.00170.93 N ANISOU 1246 NH1 ARG B 123 20850 23387 20708 -341 -1461 2485 N ATOM 1247 NH2 ARG B 123 -22.653 44.283 34.916 1.00170.08 N ANISOU 1247 NH2 ARG B 123 20945 23397 20279 -296 -1212 2928 N ATOM 1248 N LYS B 124 -25.064 46.836 27.971 1.00138.52 N ANISOU 1248 N LYS B 124 17737 17538 17355 -257 91 1417 N ATOM 1249 CA LYS B 124 -26.333 46.392 27.442 1.00137.29 C ANISOU 1249 CA LYS B 124 17593 17452 17119 -212 262 1491 C ATOM 1250 C LYS B 124 -26.108 45.041 26.792 1.00136.69 C ANISOU 1250 C LYS B 124 17317 17211 17407 -336 381 1657 C ATOM 1251 O LYS B 124 -25.082 44.821 26.160 1.00136.39 O ANISOU 1251 O LYS B 124 17191 16906 17727 -459 396 1601 O ATOM 1252 CB LYS B 124 -26.892 47.407 26.436 1.00136.08 C ANISOU 1252 CB LYS B 124 17610 17200 16894 -155 378 1287 C ATOM 1253 CG LYS B 124 -26.947 48.876 26.944 1.00137.19 C ANISOU 1253 CG LYS B 124 17935 17359 16831 -37 317 1078 C ATOM 1254 CD LYS B 124 -27.819 49.056 28.220 1.00138.73 C ANISOU 1254 CD LYS B 124 18123 17896 16692 71 268 1055 C ATOM 1255 CE LYS B 124 -27.407 50.296 29.075 1.00140.72 C ANISOU 1255 CE LYS B 124 18464 18184 16821 90 210 784 C ATOM 1256 NZ LYS B 124 -28.570 51.073 29.668 1.00142.16 N ANISOU 1256 NZ LYS B 124 18692 18555 16767 221 286 599 N ATOM 1257 N GLU B 125 -27.061 44.131 26.980 1.00133.58 N ANISOU 1257 N GLU B 125 16831 16966 16958 -325 501 1821 N ATOM 1258 CA GLU B 125 -27.022 42.797 26.366 1.00133.48 C ANISOU 1258 CA GLU B 125 16599 16779 17339 -462 699 1934 C ATOM 1259 C GLU B 125 -27.958 42.673 25.163 1.00131.97 C ANISOU 1259 C GLU B 125 16378 16634 17132 -543 953 1744 C ATOM 1260 O GLU B 125 -28.862 43.487 24.946 1.00131.29 O ANISOU 1260 O GLU B 125 16430 16761 16691 -441 951 1614 O ATOM 1261 CB GLU B 125 -27.417 41.743 27.387 1.00135.45 C ANISOU 1261 CB GLU B 125 16738 17141 17586 -434 717 2254 C ATOM 1262 CG GLU B 125 -26.423 41.567 28.480 1.00137.80 C ANISOU 1262 CG GLU B 125 16985 17431 17941 -384 462 2530 C ATOM 1263 CD GLU B 125 -26.911 40.624 29.569 1.00140.47 C ANISOU 1263 CD GLU B 125 17259 17935 18177 -354 464 2928 C ATOM 1264 OE1 GLU B 125 -27.904 39.886 29.323 1.00140.32 O ANISOU 1264 OE1 GLU B 125 17198 17919 18199 -407 735 2965 O ATOM 1265 OE2 GLU B 125 -26.294 40.627 30.670 1.00143.11 O ANISOU 1265 OE2 GLU B 125 17577 18428 18369 -298 202 3204 O ATOM 1266 N GLY B 126 -27.758 41.633 24.382 1.00110.90 N ANISOU 1266 N GLY B 126 13486 13787 14863 -734 1181 1713 N ATOM 1267 CA GLY B 126 -28.725 41.318 23.355 1.00110.18 C ANISOU 1267 CA GLY B 126 13297 13850 14718 -856 1444 1522 C ATOM 1268 C GLY B 126 -28.216 40.231 22.451 1.00110.59 C ANISOU 1268 C GLY B 126 13065 13669 15287 -1137 1725 1398 C ATOM 1269 O GLY B 126 -27.147 39.675 22.682 1.00111.53 O ANISOU 1269 O GLY B 126 13055 13457 15863 -1200 1714 1492 O ATOM 1270 N TYR B 127 -28.997 39.916 21.429 1.00105.37 N ANISOU 1270 N TYR B 127 12263 13203 14568 -1315 1987 1160 N ATOM 1271 CA TYR B 127 -28.543 38.982 20.433 1.00106.05 C ANISOU 1271 CA TYR B 127 12048 13117 15130 -1650 2308 929 C ATOM 1272 C TYR B 127 -27.855 39.717 19.289 1.00105.32 C ANISOU 1272 C TYR B 127 12003 13022 14990 -1834 2278 694 C ATOM 1273 O TYR B 127 -28.283 40.811 18.925 1.00104.49 O ANISOU 1273 O TYR B 127 12122 13184 14397 -1732 2113 682 O ATOM 1274 CB TYR B 127 -29.695 38.135 19.918 1.00106.86 C ANISOU 1274 CB TYR B 127 11910 13483 15209 -1828 2663 728 C ATOM 1275 CG TYR B 127 -30.022 36.964 20.813 1.00108.47 C ANISOU 1275 CG TYR B 127 11962 13506 15744 -1801 2861 905 C ATOM 1276 CD1 TYR B 127 -31.042 37.051 21.733 1.00108.63 C ANISOU 1276 CD1 TYR B 127 12121 13761 15393 -1588 2787 1086 C ATOM 1277 CD2 TYR B 127 -29.308 35.773 20.738 1.00110.31 C ANISOU 1277 CD2 TYR B 127 11907 13308 16696 -1998 3146 895 C ATOM 1278 CE1 TYR B 127 -31.361 35.991 22.561 1.00110.57 C ANISOU 1278 CE1 TYR B 127 12259 13845 15907 -1589 2990 1287 C ATOM 1279 CE2 TYR B 127 -29.618 34.700 21.568 1.00112.45 C ANISOU 1279 CE2 TYR B 127 12056 13365 17306 -1961 3347 1131 C ATOM 1280 CZ TYR B 127 -30.653 34.820 22.481 1.00112.56 C ANISOU 1280 CZ TYR B 127 12251 13646 16871 -1765 3267 1344 C ATOM 1281 OH TYR B 127 -30.998 33.790 23.326 1.00115.08 O ANISOU 1281 OH TYR B 127 12487 13768 17470 -1749 3481 1615 O ATOM 1282 N ILE B 128 -26.795 39.089 18.754 1.00 95.27 N ANISOU 1282 N ILE B 128 10508 11425 14263 -2106 2457 522 N ATOM 1283 CA ILE B 128 -25.949 39.658 17.701 1.00 95.04 C ANISOU 1283 CA ILE B 128 10502 11344 14264 -2354 2475 271 C ATOM 1284 C ILE B 128 -25.714 38.634 16.627 1.00 96.46 C ANISOU 1284 C ILE B 128 10295 11474 14882 -2807 2898 -112 C ATOM 1285 O ILE B 128 -25.676 37.475 16.937 1.00 97.76 O ANISOU 1285 O ILE B 128 10170 11402 15572 -2877 3134 -137 O ATOM 1286 CB ILE B 128 -24.547 40.114 18.216 1.00 94.93 C ANISOU 1286 CB ILE B 128 10601 10935 14532 -2265 2243 357 C ATOM 1287 CG1 ILE B 128 -23.580 38.931 18.382 1.00 96.59 C ANISOU 1287 CG1 ILE B 128 10457 10711 15531 -2412 2419 288 C ATOM 1288 CG2 ILE B 128 -24.680 40.921 19.494 1.00 94.19 C ANISOU 1288 CG2 ILE B 128 10809 10873 14105 -1853 1869 694 C ATOM 1289 CD1 ILE B 128 -22.293 39.294 19.081 1.00 96.98 C ANISOU 1289 CD1 ILE B 128 10562 10437 15850 -2264 2145 406 C ATOM 1290 N PRO B 129 -25.542 39.066 15.369 1.00 98.90 N ANISOU 1290 N PRO B 129 10588 12002 14989 -3136 3015 -411 N ATOM 1291 CA PRO B 129 -25.274 38.151 14.284 1.00100.68 C ANISOU 1291 CA PRO B 129 10416 12240 15599 -3646 3450 -865 C ATOM 1292 C PRO B 129 -23.832 37.773 14.340 1.00101.48 C ANISOU 1292 C PRO B 129 10357 11800 16401 -3797 3526 -1013 C ATOM 1293 O PRO B 129 -23.017 38.626 14.177 1.00100.90 O ANISOU 1293 O PRO B 129 10494 11626 16217 -3804 3334 -1014 O ATOM 1294 CB PRO B 129 -25.568 38.988 13.043 1.00100.97 C ANISOU 1294 CB PRO B 129 10567 12776 15021 -3910 3454 -1043 C ATOM 1295 CG PRO B 129 -25.297 40.373 13.451 1.00 99.48 C ANISOU 1295 CG PRO B 129 10844 12533 14422 -3572 3033 -702 C ATOM 1296 CD PRO B 129 -25.675 40.455 14.892 1.00 98.08 C ANISOU 1296 CD PRO B 129 10836 12176 14256 -3062 2766 -324 C ATOM 1297 N SER B 130 -23.526 36.504 14.555 1.00132.11 N ANISOU 1297 N SER B 130 13847 15316 21034 -3916 3825 -1146 N ATOM 1298 CA SER B 130 -22.172 36.053 14.865 1.00133.39 C ANISOU 1298 CA SER B 130 13809 14893 21979 -3942 3846 -1201 C ATOM 1299 C SER B 130 -21.176 36.243 13.743 1.00134.35 C ANISOU 1299 C SER B 130 13781 14947 22318 -4406 4041 -1695 C ATOM 1300 O SER B 130 -19.967 36.319 13.998 1.00134.95 O ANISOU 1300 O SER B 130 13800 14609 22867 -4377 3935 -1733 O ATOM 1301 CB SER B 130 -22.166 34.578 15.157 1.00135.93 C ANISOU 1301 CB SER B 130 13686 14825 23137 -4008 4205 -1257 C ATOM 1302 OG SER B 130 -22.291 33.864 13.931 1.00137.84 O ANISOU 1302 OG SER B 130 13532 15168 23673 -4565 4743 -1853 O ATOM 1303 N ASN B 131 -21.661 36.271 12.505 1.00142.10 N ANISOU 1303 N ASN B 131 14662 16364 22965 -4862 4339 -2097 N ATOM 1304 CA ASN B 131 -20.787 36.551 11.363 1.00143.31 C ANISOU 1304 CA ASN B 131 14712 16556 23183 -5373 4537 -2580 C ATOM 1305 C ASN B 131 -20.289 38.014 11.271 1.00141.70 C ANISOU 1305 C ASN B 131 14990 16460 22391 -5264 4162 -2398 C ATOM 1306 O ASN B 131 -19.491 38.350 10.405 1.00142.81 O ANISOU 1306 O ASN B 131 15105 16605 22552 -5678 4304 -2755 O ATOM 1307 CB ASN B 131 -21.513 36.223 10.078 1.00144.98 C ANISOU 1307 CB ASN B 131 14689 17326 23072 -5920 4940 -3029 C ATOM 1308 CG ASN B 131 -22.608 37.204 9.798 1.00143.63 C ANISOU 1308 CG ASN B 131 14895 17814 21864 -5780 4677 -2740 C ATOM 1309 OD1 ASN B 131 -23.175 37.762 10.736 1.00141.47 O ANISOU 1309 OD1 ASN B 131 14961 17541 21249 -5231 4291 -2223 O ATOM 1310 ND2 ASN B 131 -22.904 37.451 8.520 1.00145.33 N ANISOU 1310 ND2 ASN B 131 15039 18613 21568 -6273 4873 -3059 N ATOM 1311 N TYR B 132 -20.774 38.890 12.137 1.00117.49 N ANISOU 1311 N TYR B 132 12352 13476 18813 -4746 3729 -1878 N ATOM 1312 CA TYR B 132 -20.269 40.240 12.181 1.00116.40 C ANISOU 1312 CA TYR B 132 12647 13333 18246 -4614 3419 -1710 C ATOM 1313 C TYR B 132 -19.179 40.384 13.240 1.00115.94 C ANISOU 1313 C TYR B 132 12633 12759 18658 -4316 3173 -1582 C ATOM 1314 O TYR B 132 -18.601 41.453 13.380 1.00115.33 O ANISOU 1314 O TYR B 132 12873 12607 18341 -4223 2953 -1511 O ATOM 1315 CB TYR B 132 -21.379 41.214 12.535 1.00114.80 C ANISOU 1315 CB TYR B 132 12861 13493 17266 -4224 3106 -1265 C ATOM 1316 CG TYR B 132 -22.284 41.622 11.433 1.00115.63 C ANISOU 1316 CG TYR B 132 13048 14167 16718 -4458 3204 -1301 C ATOM 1317 CD1 TYR B 132 -22.650 40.744 10.431 1.00117.45 C ANISOU 1317 CD1 TYR B 132 12903 14730 16992 -4932 3579 -1676 C ATOM 1318 CD2 TYR B 132 -22.831 42.895 11.430 1.00115.10 C ANISOU 1318 CD2 TYR B 132 13408 14335 15991 -4189 2916 -943 C ATOM 1319 CE1 TYR B 132 -23.528 41.137 9.434 1.00118.78 C ANISOU 1319 CE1 TYR B 132 13119 15537 16474 -5141 3624 -1675 C ATOM 1320 CE2 TYR B 132 -23.707 43.293 10.448 1.00116.51 C ANISOU 1320 CE2 TYR B 132 13646 15073 15552 -4347 2951 -884 C ATOM 1321 CZ TYR B 132 -24.057 42.419 9.461 1.00118.35 C ANISOU 1321 CZ TYR B 132 13502 15713 15752 -4819 3280 -1235 C ATOM 1322 OH TYR B 132 -24.921 42.877 8.512 1.00120.27 O ANISOU 1322 OH TYR B 132 13793 16598 15308 -4961 3262 -1137 O ATOM 1323 N VAL B 133 -18.898 39.363 14.024 1.00116.84 N ANISOU 1323 N VAL B 133 12434 12536 19426 -4150 3198 -1524 N ATOM 1324 CA VAL B 133 -17.872 39.551 15.020 1.00117.00 C ANISOU 1324 CA VAL B 133 12472 12171 19813 -3860 2914 -1369 C ATOM 1325 C VAL B 133 -16.665 38.692 14.736 1.00119.42 C ANISOU 1325 C VAL B 133 12319 12043 21011 -4132 3145 -1750 C ATOM 1326 O VAL B 133 -16.735 37.791 13.908 1.00121.00 O ANISOU 1326 O VAL B 133 12158 12196 21621 -4518 3559 -2112 O ATOM 1327 CB VAL B 133 -18.394 39.271 16.368 1.00116.51 C ANISOU 1327 CB VAL B 133 12460 12078 19731 -3360 2638 -872 C ATOM 1328 CG1 VAL B 133 -19.647 40.051 16.527 1.00114.49 C ANISOU 1328 CG1 VAL B 133 12592 12249 18660 -3148 2480 -597 C ATOM 1329 CG2 VAL B 133 -18.635 37.810 16.529 1.00118.32 C ANISOU 1329 CG2 VAL B 133 12265 12096 20595 -3390 2894 -850 C ATOM 1330 N ALA B 134 -15.555 39.007 15.407 1.00131.74 N ANISOU 1330 N ALA B 134 13867 13312 22878 -3949 2890 -1712 N ATOM 1331 CA ALA B 134 -14.298 38.268 15.269 1.00134.48 C ANISOU 1331 CA ALA B 134 13746 13212 24136 -4134 3044 -2057 C ATOM 1332 C ALA B 134 -13.792 37.920 16.654 1.00135.80 C ANISOU 1332 C ALA B 134 13768 13123 24707 -3641 2679 -1637 C ATOM 1333 O ALA B 134 -13.605 38.793 17.496 1.00134.82 O ANISOU 1333 O ALA B 134 13936 13135 24154 -3324 2277 -1364 O ATOM 1334 CB ALA B 134 -13.275 39.100 14.534 1.00134.75 C ANISOU 1334 CB ALA B 134 13867 13205 24125 -4484 3105 -2524 C ATOM 1335 N ARG B 135 -13.570 36.642 16.894 1.00154.98 N ANISOU 1335 N ARG B 135 15723 15194 27970 -3586 2831 -1579 N ATOM 1336 CA ARG B 135 -13.212 36.184 18.219 1.00157.06 C ANISOU 1336 CA ARG B 135 15825 15256 28596 -3099 2475 -1060 C ATOM 1337 C ARG B 135 -11.792 36.568 18.522 1.00158.91 C ANISOU 1337 C ARG B 135 15888 15303 29189 -3037 2222 -1228 C ATOM 1338 O ARG B 135 -10.950 36.476 17.650 1.00160.15 O ANISOU 1338 O ARG B 135 15782 15226 29841 -3406 2484 -1797 O ATOM 1339 CB ARG B 135 -13.357 34.677 18.262 1.00160.28 C ANISOU 1339 CB ARG B 135 15749 15261 29891 -3085 2773 -947 C ATOM 1340 CG ARG B 135 -13.305 34.086 19.649 1.00162.91 C ANISOU 1340 CG ARG B 135 15958 15436 30503 -2562 2427 -241 C ATOM 1341 CD ARG B 135 -14.213 32.857 19.774 1.00164.68 C ANISOU 1341 CD ARG B 135 15988 15448 31135 -2513 2746 51 C ATOM 1342 NE ARG B 135 -13.497 31.738 20.374 1.00169.90 N ANISOU 1342 NE ARG B 135 16152 15563 32839 -2270 2733 379 N ATOM 1343 CZ ARG B 135 -14.085 30.698 20.952 1.00172.71 C ANISOU 1343 CZ ARG B 135 16355 15669 33597 -2061 2862 884 C ATOM 1344 NH1 ARG B 135 -15.417 30.634 21.020 1.00170.48 N ANISOU 1344 NH1 ARG B 135 16378 15669 32729 -2087 3023 1058 N ATOM 1345 NH2 ARG B 135 -13.339 29.717 21.469 1.00178.20 N ANISOU 1345 NH2 ARG B 135 16580 15818 35309 -1818 2836 1229 N ATOM 1346 N VAL B 136 -11.520 36.991 19.749 1.00177.00 N ANISOU 1346 N VAL B 136 18298 17736 31220 -2607 1728 -780 N ATOM 1347 CA VAL B 136 -10.174 37.459 20.097 1.00178.98 C ANISOU 1347 CA VAL B 136 18377 17904 31722 -2543 1452 -971 C ATOM 1348 C VAL B 136 -9.667 36.731 21.328 1.00183.05 C ANISOU 1348 C VAL B 136 18532 18295 32722 -2089 1078 -435 C ATOM 1349 O VAL B 136 -10.366 36.626 22.345 1.00183.17 O ANISOU 1349 O VAL B 136 18716 18552 32328 -1734 799 190 O ATOM 1350 CB VAL B 136 -10.093 39.008 20.283 1.00176.28 C ANISOU 1350 CB VAL B 136 18526 17957 30495 -2549 1207 -1103 C ATOM 1351 CG1 VAL B 136 -10.462 39.716 18.983 1.00173.27 C ANISOU 1351 CG1 VAL B 136 18469 17652 29712 -3003 1578 -1586 C ATOM 1352 CG2 VAL B 136 -10.975 39.484 21.427 1.00174.93 C ANISOU 1352 CG2 VAL B 136 18716 18190 29558 -2159 848 -526 C ATOM 1353 N ASP B 137 -8.453 36.192 21.207 1.00159.56 N ANISOU 1353 N ASP B 137 15034 14949 30644 -2117 1083 -677 N ATOM 1354 CA ASP B 137 -7.849 35.399 22.267 1.00164.58 C ANISOU 1354 CA ASP B 137 15231 15422 31880 -1683 729 -149 C ATOM 1355 C ASP B 137 -7.137 36.302 23.274 1.00165.67 C ANISOU 1355 C ASP B 137 15445 15979 31524 -1418 165 -2 C ATOM 1356 O ASP B 137 -6.148 35.905 23.893 1.00170.45 O ANISOU 1356 O ASP B 137 15588 16487 32686 -1165 -148 168 O ATOM 1357 CB ASP B 137 -6.881 34.384 21.663 1.00168.88 C ANISOU 1357 CB ASP B 137 15113 15354 33698 -1812 1001 -491 C ATOM 1358 CG ASP B 137 -6.771 33.120 22.492 1.00174.36 C ANISOU 1358 CG ASP B 137 15346 15706 35197 -1382 844 199 C ATOM 1359 OD1 ASP B 137 -5.718 32.439 22.408 1.00179.29 O ANISOU 1359 OD1 ASP B 137 15364 15882 36879 -1316 857 62 O ATOM 1360 OD2 ASP B 137 -7.743 32.805 23.222 1.00174.12 O ANISOU 1360 OD2 ASP B 137 15552 15840 34768 -1112 723 888 O ATOM 1361 N SER B 138 -7.669 37.515 23.442 1.00219.02 N ANISOU 1361 N SER B 138 22755 23215 37248 -1478 47 -76 N ATOM 1362 CA SER B 138 -7.058 38.547 24.281 1.00219.71 C ANISOU 1362 CA SER B 138 22952 23746 36783 -1332 -392 -102 C ATOM 1363 C SER B 138 -7.402 38.337 25.758 1.00222.30 C ANISOU 1363 C SER B 138 23275 24475 36714 -883 -878 675 C ATOM 1364 O SER B 138 -6.511 38.105 26.581 1.00227.01 O ANISOU 1364 O SER B 138 23479 25202 37573 -628 -1280 904 O ATOM 1365 CB SER B 138 -7.460 39.970 23.805 1.00214.98 C ANISOU 1365 CB SER B 138 22927 23426 35329 -1612 -248 -549 C ATOM 1366 OG SER B 138 -8.853 40.111 23.530 1.00211.09 O ANISOU 1366 OG SER B 138 22889 23043 34272 -1658 -40 -342 O TER 1367 SER B 138 ATOM 1368 N GLU C 69 -81.162 31.936 8.945 1.00175.87 N ANISOU 1368 N GLU C 69 20158 30799 15866 8436 2326 -4926 N ATOM 1369 CA GLU C 69 -80.779 30.897 7.998 1.00170.09 C ANISOU 1369 CA GLU C 69 19444 29578 15605 7800 2398 -4315 C ATOM 1370 C GLU C 69 -80.023 31.492 6.823 1.00164.06 C ANISOU 1370 C GLU C 69 18983 27975 15375 7568 1784 -4506 C ATOM 1371 O GLU C 69 -79.688 32.675 6.827 1.00164.51 O ANISOU 1371 O GLU C 69 19267 27783 15456 7874 1323 -5049 O ATOM 1372 N VAL C 70 -79.753 30.671 5.815 1.00162.25 N ANISOU 1372 N VAL C 70 18744 27305 15600 7033 1799 -4061 N ATOM 1373 CA VAL C 70 -79.068 31.158 4.626 1.00156.92 C ANISOU 1373 CA VAL C 70 18322 25900 15400 6811 1277 -4159 C ATOM 1374 C VAL C 70 -77.928 30.258 4.151 1.00151.91 C ANISOU 1374 C VAL C 70 17926 24878 14912 6325 1228 -3691 C ATOM 1375 O VAL C 70 -78.155 29.256 3.476 1.00149.70 O ANISOU 1375 O VAL C 70 17453 24487 14938 5917 1462 -3307 O ATOM 1376 N GLY C 71 -76.704 30.634 4.504 1.00166.17 N ANISOU 1376 N GLY C 71 20123 26482 16532 6379 912 -3781 N ATOM 1377 CA GLY C 71 -75.512 29.982 3.988 1.00161.46 C ANISOU 1377 CA GLY C 71 19771 25472 16105 5972 780 -3414 C ATOM 1378 C GLY C 71 -74.244 30.507 4.635 1.00161.65 C ANISOU 1378 C GLY C 71 20152 25415 15851 6122 440 -3609 C ATOM 1379 O GLY C 71 -74.239 30.816 5.823 1.00166.11 O ANISOU 1379 O GLY C 71 20746 26460 15907 6500 486 -3854 O ATOM 1380 N PHE C 72 -73.169 30.613 3.858 1.00184.78 N ANISOU 1380 N PHE C 72 23320 27784 19103 5841 96 -3533 N ATOM 1381 CA PHE C 72 -71.915 31.168 4.361 1.00185.14 C ANISOU 1381 CA PHE C 72 23652 27695 18996 5935 -274 -3772 C ATOM 1382 C PHE C 72 -71.116 30.073 5.042 1.00185.06 C ANISOU 1382 C PHE C 72 23715 27990 18610 5826 -77 -3356 C ATOM 1383 O PHE C 72 -71.702 29.090 5.486 1.00186.59 O ANISOU 1383 O PHE C 72 23740 28603 18554 5823 389 -2963 O ATOM 1384 N PRO C 73 -69.792 30.221 5.137 1.00280.71 N ANISOU 1384 N PRO C 73 36051 39894 30713 5748 -407 -3410 N ATOM 1385 CA PRO C 73 -69.032 31.364 4.608 1.00279.52 C ANISOU 1385 CA PRO C 73 36066 39188 30952 5700 -921 -3836 C ATOM 1386 C PRO C 73 -67.761 31.614 5.435 1.00281.66 C ANISOU 1386 C PRO C 73 36484 39582 30951 5813 -1238 -4091 C ATOM 1387 O PRO C 73 -67.591 30.982 6.473 1.00284.48 O ANISOU 1387 O PRO C 73 36821 40546 30723 6018 -1071 -3966 O ATOM 1388 N VAL C 74 -66.886 32.510 4.984 1.00218.01 N ANISOU 1388 N VAL C 74 28540 30977 23315 5691 -1676 -4424 N ATOM 1389 CA VAL C 74 -67.131 33.255 3.766 1.00215.50 C ANISOU 1389 CA VAL C 74 28247 29972 23660 5499 -1819 -4467 C ATOM 1390 C VAL C 74 -66.885 32.444 2.509 1.00209.87 C ANISOU 1390 C VAL C 74 27543 28911 23287 5062 -1673 -3856 C ATOM 1391 O VAL C 74 -65.992 32.758 1.730 1.00207.68 O ANISOU 1391 O VAL C 74 27356 28120 23431 4803 -1903 -3784 O ATOM 1392 CB VAL C 74 -66.240 34.489 3.694 1.00217.46 C ANISOU 1392 CB VAL C 74 28597 29697 24332 5494 -2287 -4969 C ATOM 1393 CG1 VAL C 74 -64.859 34.160 4.223 1.00217.87 C ANISOU 1393 CG1 VAL C 74 28699 29862 24221 5374 -2494 -5004 C ATOM 1394 CG2 VAL C 74 -66.161 34.987 2.266 1.00214.32 C ANISOU 1394 CG2 VAL C 74 28248 28551 24632 5209 -2379 -4741 C ATOM 1395 N ARG C 75 -67.679 31.406 2.301 1.00161.06 N ANISOU 1395 N ARG C 75 21239 23011 16946 4981 -1280 -3441 N ATOM 1396 CA ARG C 75 -67.741 30.792 0.965 1.00156.51 C ANISOU 1396 CA ARG C 75 20622 22102 16745 4617 -1159 -3007 C ATOM 1397 C ARG C 75 -67.354 29.500 1.699 1.00156.45 C ANISOU 1397 C ARG C 75 20594 22488 16362 4548 -884 -2659 C ATOM 1398 O ARG C 75 -66.354 29.489 2.439 1.00157.73 O ANISOU 1398 O ARG C 75 20866 22769 16293 4617 -1042 -2721 O ATOM 1399 CB ARG C 75 -67.145 30.825 -0.450 1.00152.59 C ANISOU 1399 CB ARG C 75 20182 21072 16722 4281 -1301 -2767 C ATOM 1400 CG ARG C 75 -65.615 30.882 -0.472 1.00151.46 C ANISOU 1400 CG ARG C 75 20190 20661 16698 4094 -1542 -2716 C ATOM 1401 CD ARG C 75 -65.052 31.123 -1.862 1.00148.56 C ANISOU 1401 CD ARG C 75 19866 19792 16788 3815 -1669 -2499 C ATOM 1402 NE ARG C 75 -65.777 32.166 -2.599 1.00149.54 N ANISOU 1402 NE ARG C 75 19979 19630 17208 3938 -1780 -2623 N ATOM 1403 CZ ARG C 75 -65.402 32.644 -3.787 1.00148.35 C ANISOU 1403 CZ ARG C 75 19870 19061 17434 3793 -1895 -2426 C ATOM 1404 NH1 ARG C 75 -64.295 32.191 -4.403 1.00145.95 N ANISOU 1404 NH1 ARG C 75 19607 18580 17266 3495 -1912 -2135 N ATOM 1405 NH2 ARG C 75 -66.137 33.595 -4.365 1.00150.09 N ANISOU 1405 NH2 ARG C 75 20079 19061 17887 3983 -1978 -2490 N ATOM 1406 N PRO C 76 -68.154 28.427 1.540 1.00118.75 N ANISOU 1406 N PRO C 76 15652 17921 11547 4434 -471 -2301 N ATOM 1407 CA PRO C 76 -67.770 27.148 2.107 1.00119.04 C ANISOU 1407 CA PRO C 76 15671 18209 11350 4348 -167 -1868 C ATOM 1408 C PRO C 76 -66.560 26.530 1.464 1.00115.63 C ANISOU 1408 C PRO C 76 15349 17430 11157 4041 -270 -1581 C ATOM 1409 O PRO C 76 -65.962 27.102 0.561 1.00112.98 O ANISOU 1409 O PRO C 76 15097 16683 11145 3874 -572 -1708 O ATOM 1410 CB PRO C 76 -68.980 26.272 1.836 1.00119.35 C ANISOU 1410 CB PRO C 76 15461 18379 11507 4227 288 -1605 C ATOM 1411 CG PRO C 76 -70.096 27.204 1.868 1.00121.31 C ANISOU 1411 CG PRO C 76 15587 18772 11733 4458 245 -1989 C ATOM 1412 CD PRO C 76 -69.586 28.445 1.208 1.00119.58 C ANISOU 1412 CD PRO C 76 15535 18153 11747 4489 -241 -2352 C ATOM 1413 N GLN C 77 -66.225 25.350 1.960 1.00133.02 N ANISOU 1413 N GLN C 77 17533 19811 13197 3995 17 -1158 N ATOM 1414 CA GLN C 77 -65.098 24.550 1.499 1.00130.54 C ANISOU 1414 CA GLN C 77 17293 19227 13080 3752 -9 -837 C ATOM 1415 C GLN C 77 -65.648 23.568 0.469 1.00128.28 C ANISOU 1415 C GLN C 77 16852 18662 13225 3419 298 -572 C ATOM 1416 O GLN C 77 -66.487 22.729 0.778 1.00130.26 O ANISOU 1416 O GLN C 77 16941 19066 13486 3398 715 -327 O ATOM 1417 CB GLN C 77 -64.494 23.827 2.713 1.00133.72 C ANISOU 1417 CB GLN C 77 17749 20008 13052 3972 141 -517 C ATOM 1418 CG GLN C 77 -63.658 22.599 2.438 1.00132.49 C ANISOU 1418 CG GLN C 77 17607 19646 13087 3780 306 -34 C ATOM 1419 CD GLN C 77 -62.250 22.953 2.011 1.00130.18 C ANISOU 1419 CD GLN C 77 17433 19110 12919 3685 -109 -164 C ATOM 1420 OE1 GLN C 77 -61.435 23.470 2.831 1.00132.35 O ANISOU 1420 OE1 GLN C 77 17788 19657 12842 3930 -404 -331 O ATOM 1421 NE2 GLN C 77 -61.927 22.658 0.716 1.00126.29 N ANISOU 1421 NE2 GLN C 77 16916 18145 12925 3336 -135 -112 N ATOM 1422 N VAL C 78 -65.182 23.681 -0.761 1.00105.99 N ANISOU 1422 N VAL C 78 14050 15447 10773 3160 100 -644 N ATOM 1423 CA VAL C 78 -65.764 22.907 -1.845 1.00104.34 C ANISOU 1423 CA VAL C 78 13663 15024 10955 2874 315 -550 C ATOM 1424 C VAL C 78 -65.437 21.440 -1.582 1.00105.24 C ANISOU 1424 C VAL C 78 13719 15073 11193 2738 671 -138 C ATOM 1425 O VAL C 78 -64.444 21.154 -0.919 1.00105.90 O ANISOU 1425 O VAL C 78 13945 15197 11094 2842 637 89 O ATOM 1426 CB VAL C 78 -65.252 23.374 -3.228 1.00101.02 C ANISOU 1426 CB VAL C 78 13283 14287 10815 2687 20 -706 C ATOM 1427 CG1 VAL C 78 -65.339 24.909 -3.332 1.00100.99 C ANISOU 1427 CG1 VAL C 78 13383 14267 10721 2867 -334 -1020 C ATOM 1428 CG2 VAL C 78 -63.838 22.914 -3.476 1.00 99.34 C ANISOU 1428 CG2 VAL C 78 13190 13865 10692 2556 -77 -514 C ATOM 1429 N PRO C 79 -66.272 20.509 -2.064 1.00 99.03 N ANISOU 1429 N PRO C 79 12701 14178 10748 2524 1010 -50 N ATOM 1430 CA PRO C 79 -66.059 19.108 -1.785 1.00100.85 C ANISOU 1430 CA PRO C 79 12855 14255 11207 2396 1396 353 C ATOM 1431 C PRO C 79 -64.770 18.609 -2.347 1.00 98.68 C ANISOU 1431 C PRO C 79 12704 13674 11117 2273 1259 471 C ATOM 1432 O PRO C 79 -64.304 19.089 -3.357 1.00 95.62 O ANISOU 1432 O PRO C 79 12359 13138 10833 2161 953 213 O ATOM 1433 CB PRO C 79 -67.211 18.432 -2.503 1.00101.90 C ANISOU 1433 CB PRO C 79 12667 14247 11804 2127 1684 238 C ATOM 1434 CG PRO C 79 -68.259 19.408 -2.495 1.00102.25 C ANISOU 1434 CG PRO C 79 12606 14576 11667 2246 1577 -83 C ATOM 1435 CD PRO C 79 -67.563 20.716 -2.718 1.00 99.32 C ANISOU 1435 CD PRO C 79 12493 14262 10983 2427 1078 -326 C ATOM 1436 N LEU C 80 -64.191 17.631 -1.694 1.00105.18 N ANISOU 1436 N LEU C 80 13569 14418 11977 2321 1509 899 N ATOM 1437 CA LEU C 80 -62.904 17.130 -2.116 1.00103.66 C ANISOU 1437 CA LEU C 80 13479 13962 11945 2258 1387 1028 C ATOM 1438 C LEU C 80 -63.076 16.237 -3.300 1.00102.90 C ANISOU 1438 C LEU C 80 13203 13465 12430 1936 1544 915 C ATOM 1439 O LEU C 80 -64.114 15.635 -3.507 1.00104.83 O ANISOU 1439 O LEU C 80 13223 13594 13014 1764 1852 872 O ATOM 1440 CB LEU C 80 -62.236 16.395 -0.958 1.00106.92 C ANISOU 1440 CB LEU C 80 13990 14460 12176 2493 1593 1554 C ATOM 1441 CG LEU C 80 -61.314 15.209 -1.150 1.00107.83 C ANISOU 1441 CG LEU C 80 14108 14225 12637 2440 1755 1897 C ATOM 1442 CD1 LEU C 80 -60.405 15.192 0.053 1.00110.31 C ANISOU 1442 CD1 LEU C 80 14584 14846 12484 2817 1689 2291 C ATOM 1443 CD2 LEU C 80 -62.103 13.901 -1.268 1.00111.05 C ANISOU 1443 CD2 LEU C 80 14317 14268 13611 2247 2292 2164 C ATOM 1444 N ARG C 81 -62.035 16.143 -4.088 1.00 95.09 N ANISOU 1444 N ARG C 81 12278 12281 11571 1857 1330 824 N ATOM 1445 CA ARG C 81 -62.105 15.353 -5.293 1.00 94.66 C ANISOU 1445 CA ARG C 81 12047 11901 12016 1589 1429 616 C ATOM 1446 C ARG C 81 -60.716 14.966 -5.789 1.00 93.40 C ANISOU 1446 C ARG C 81 11974 11547 11968 1588 1298 679 C ATOM 1447 O ARG C 81 -59.788 15.734 -5.749 1.00 91.38 O ANISOU 1447 O ARG C 81 11874 11440 11406 1709 988 683 O ATOM 1448 CB ARG C 81 -62.866 16.147 -6.346 1.00 92.63 C ANISOU 1448 CB ARG C 81 11675 11782 11737 1466 1211 137 C ATOM 1449 CG ARG C 81 -62.479 17.648 -6.401 1.00 89.87 C ANISOU 1449 CG ARG C 81 11517 11694 10936 1626 794 10 C ATOM 1450 CD ARG C 81 -62.916 18.252 -7.709 1.00 88.24 C ANISOU 1450 CD ARG C 81 11207 11561 10760 1531 585 -367 C ATOM 1451 NE ARG C 81 -62.593 19.649 -7.851 1.00 86.40 N ANISOU 1451 NE ARG C 81 11137 11476 10215 1669 240 -437 N ATOM 1452 CZ ARG C 81 -62.825 20.318 -8.954 1.00 85.41 C ANISOU 1452 CZ ARG C 81 10961 11435 10055 1654 45 -652 C ATOM 1453 NH1 ARG C 81 -63.361 19.721 -9.989 1.00 85.99 N ANISOU 1453 NH1 ARG C 81 10818 11546 10308 1530 122 -875 N ATOM 1454 NH2 ARG C 81 -62.511 21.581 -9.035 1.00 84.45 N ANISOU 1454 NH2 ARG C 81 10989 11364 9736 1780 -226 -649 N ATOM 1455 N PRO C 82 -60.579 13.765 -6.283 1.00101.58 N ANISOU 1455 N PRO C 82 12872 12228 13496 1443 1543 693 N ATOM 1456 CA PRO C 82 -59.279 13.225 -6.547 1.00101.39 C ANISOU 1456 CA PRO C 82 12908 12009 13605 1496 1494 816 C ATOM 1457 C PRO C 82 -58.686 13.972 -7.652 1.00 98.15 C ANISOU 1457 C PRO C 82 12513 11739 13041 1439 1151 466 C ATOM 1458 O PRO C 82 -59.435 14.436 -8.511 1.00 97.00 O ANISOU 1458 O PRO C 82 12263 11711 12881 1307 1054 93 O ATOM 1459 CB PRO C 82 -59.589 11.837 -7.039 1.00104.39 C ANISOU 1459 CB PRO C 82 13083 11941 14640 1316 1845 751 C ATOM 1460 CG PRO C 82 -60.883 12.020 -7.774 1.00104.38 C ANISOU 1460 CG PRO C 82 12868 11999 14792 1086 1868 290 C ATOM 1461 CD PRO C 82 -61.611 13.120 -7.089 1.00103.11 C ANISOU 1461 CD PRO C 82 12797 12225 14157 1186 1750 359 C ATOM 1462 N MET C 83 -57.365 14.065 -7.627 1.00 92.73 N ANISOU 1462 N MET C 83 11927 11064 12243 1557 987 613 N ATOM 1463 CA MET C 83 -56.618 14.920 -8.535 1.00 90.09 C ANISOU 1463 CA MET C 83 11612 10898 11719 1528 675 391 C ATOM 1464 C MET C 83 -56.292 14.058 -9.710 1.00 90.71 C ANISOU 1464 C MET C 83 11531 10792 12144 1414 786 155 C ATOM 1465 O MET C 83 -56.501 12.857 -9.657 1.00 93.22 O ANISOU 1465 O MET C 83 11745 10804 12869 1373 1066 170 O ATOM 1466 CB MET C 83 -55.375 15.448 -7.858 1.00 89.59 C ANISOU 1466 CB MET C 83 11675 10960 11405 1697 457 637 C ATOM 1467 CG MET C 83 -54.088 15.396 -8.646 1.00 88.94 C ANISOU 1467 CG MET C 83 11530 10858 11406 1684 337 590 C ATOM 1468 SD MET C 83 -54.037 16.973 -9.424 1.00 86.46 S ANISOU 1468 SD MET C 83 11242 10782 10826 1587 28 373 S ATOM 1469 CE MET C 83 -53.481 18.034 -8.066 1.00 86.64 C ANISOU 1469 CE MET C 83 11400 10962 10557 1733 -253 545 C ATOM 1470 N THR C 84 -55.818 14.674 -10.780 1.00 78.79 N ANISOU 1470 N THR C 84 9985 9464 10488 1372 587 -69 N ATOM 1471 CA THR C 84 -55.765 14.021 -12.056 1.00 79.72 C ANISOU 1471 CA THR C 84 9923 9546 10823 1285 669 -414 C ATOM 1472 C THR C 84 -54.933 14.833 -13.023 1.00 78.30 C ANISOU 1472 C THR C 84 9735 9646 10371 1312 461 -488 C ATOM 1473 O THR C 84 -54.677 16.047 -12.785 1.00 76.54 O ANISOU 1473 O THR C 84 9636 9603 9844 1346 250 -309 O ATOM 1474 CB THR C 84 -57.136 13.905 -12.645 1.00 80.54 C ANISOU 1474 CB THR C 84 9882 9712 11009 1160 731 -785 C ATOM 1475 OG1 THR C 84 -57.586 15.213 -13.016 1.00 78.60 O ANISOU 1475 OG1 THR C 84 9695 9816 10355 1183 491 -844 O ATOM 1476 CG2 THR C 84 -58.084 13.285 -11.641 1.00 82.27 C ANISOU 1476 CG2 THR C 84 10080 9678 11500 1102 964 -666 C ATOM 1477 N TYR C 85 -54.519 14.157 -14.112 1.00 77.36 N ANISOU 1477 N TYR C 85 9451 9552 10391 1302 544 -761 N ATOM 1478 CA TYR C 85 -53.457 14.689 -14.945 1.00 76.93 C ANISOU 1478 CA TYR C 85 9360 9751 10119 1359 434 -736 C ATOM 1479 C TYR C 85 -53.985 15.989 -15.344 1.00 75.50 C ANISOU 1479 C TYR C 85 9244 9871 9573 1344 252 -709 C ATOM 1480 O TYR C 85 -53.270 17.000 -15.261 1.00 74.44 O ANISOU 1480 O TYR C 85 9192 9841 9252 1365 112 -437 O ATOM 1481 CB TYR C 85 -53.202 13.909 -16.204 1.00 79.14 C ANISOU 1481 CB TYR C 85 9432 10149 10489 1384 546 -1119 C ATOM 1482 CG TYR C 85 -52.371 14.650 -17.242 1.00 79.18 C ANISOU 1482 CG TYR C 85 9375 10555 10154 1454 461 -1083 C ATOM 1483 CD1 TYR C 85 -51.019 14.553 -17.246 1.00 79.60 C ANISOU 1483 CD1 TYR C 85 9384 10602 10258 1518 496 -889 C ATOM 1484 CD2 TYR C 85 -52.980 15.408 -18.245 1.00 79.46 C ANISOU 1484 CD2 TYR C 85 9367 11006 9820 1480 370 -1224 C ATOM 1485 CE1 TYR C 85 -50.278 15.192 -18.196 1.00 80.29 C ANISOU 1485 CE1 TYR C 85 9378 11060 10068 1570 479 -818 C ATOM 1486 CE2 TYR C 85 -52.262 16.079 -19.192 1.00 80.28 C ANISOU 1486 CE2 TYR C 85 9408 11490 9604 1565 349 -1101 C ATOM 1487 CZ TYR C 85 -50.897 15.975 -19.176 1.00 80.71 C ANISOU 1487 CZ TYR C 85 9411 11514 9742 1593 422 -891 C ATOM 1488 OH TYR C 85 -50.111 16.637 -20.124 1.00 82.14 O ANISOU 1488 OH TYR C 85 9492 12084 9634 1666 459 -713 O ATOM 1489 N LYS C 86 -55.245 15.981 -15.787 1.00 77.94 N ANISOU 1489 N LYS C 86 9487 10304 9823 1312 253 -995 N ATOM 1490 CA LYS C 86 -55.771 17.216 -16.331 1.00 77.25 C ANISOU 1490 CA LYS C 86 9442 10534 9375 1357 80 -960 C ATOM 1491 C LYS C 86 -55.845 18.277 -15.249 1.00 75.35 C ANISOU 1491 C LYS C 86 9409 10164 9056 1359 -58 -625 C ATOM 1492 O LYS C 86 -55.417 19.414 -15.452 1.00 74.84 O ANISOU 1492 O LYS C 86 9426 10202 8808 1397 -195 -403 O ATOM 1493 CB LYS C 86 -57.113 16.999 -16.981 1.00 78.65 C ANISOU 1493 CB LYS C 86 9470 10923 9491 1361 75 -1354 C ATOM 1494 CG LYS C 86 -57.737 18.283 -17.529 1.00 78.49 C ANISOU 1494 CG LYS C 86 9489 11248 9085 1473 -110 -1273 C ATOM 1495 CD LYS C 86 -57.171 18.700 -18.874 1.00 80.07 C ANISOU 1495 CD LYS C 86 9610 11861 8950 1609 -151 -1249 C ATOM 1496 CE LYS C 86 -58.040 19.848 -19.448 1.00 80.91 C ANISOU 1496 CE LYS C 86 9731 12314 8695 1772 -313 -1160 C ATOM 1497 NZ LYS C 86 -59.551 19.778 -19.223 1.00 81.37 N ANISOU 1497 NZ LYS C 86 9700 12446 8770 1789 -393 -1468 N ATOM 1498 N ALA C 87 -56.361 17.891 -14.093 1.00 81.97 N ANISOU 1498 N ALA C 87 10315 10771 10057 1327 0 -592 N ATOM 1499 CA ALA C 87 -56.383 18.806 -12.963 1.00 80.79 C ANISOU 1499 CA ALA C 87 10347 10542 9807 1367 -133 -347 C ATOM 1500 C ALA C 87 -54.989 19.390 -12.806 1.00 80.35 C ANISOU 1500 C ALA C 87 10358 10450 9722 1380 -256 -105 C ATOM 1501 O ALA C 87 -54.782 20.604 -12.937 1.00 80.06 O ANISOU 1501 O ALA C 87 10388 10465 9567 1391 -425 4 O ATOM 1502 CB ALA C 87 -56.855 18.101 -11.651 1.00 81.22 C ANISOU 1502 CB ALA C 87 10450 10406 10002 1375 1 -277 C ATOM 1503 N ALA C 88 -54.026 18.532 -12.560 1.00 63.11 N ANISOU 1503 N ALA C 88 8124 8155 7699 1381 -165 -24 N ATOM 1504 CA ALA C 88 -52.708 19.063 -12.460 1.00 63.17 C ANISOU 1504 CA ALA C 88 8127 8167 7707 1383 -287 165 C ATOM 1505 C ALA C 88 -52.407 19.995 -13.655 1.00 63.36 C ANISOU 1505 C ALA C 88 8092 8357 7625 1335 -347 192 C ATOM 1506 O ALA C 88 -51.978 21.121 -13.477 1.00 63.49 O ANISOU 1506 O ALA C 88 8152 8344 7628 1302 -501 345 O ATOM 1507 CB ALA C 88 -51.729 17.972 -12.368 1.00 64.13 C ANISOU 1507 CB ALA C 88 8149 8207 8012 1422 -166 218 C ATOM 1508 N LEU C 89 -52.672 19.542 -14.870 1.00 71.25 N ANISOU 1508 N LEU C 89 8979 9538 8556 1346 -218 42 N ATOM 1509 CA LEU C 89 -52.426 20.374 -16.061 1.00 72.25 C ANISOU 1509 CA LEU C 89 9042 9905 8505 1359 -230 143 C ATOM 1510 C LEU C 89 -53.183 21.691 -16.004 1.00 72.05 C ANISOU 1510 C LEU C 89 9142 9878 8356 1379 -377 267 C ATOM 1511 O LEU C 89 -52.601 22.746 -16.188 1.00 72.92 O ANISOU 1511 O LEU C 89 9268 9946 8491 1351 -440 530 O ATOM 1512 CB LEU C 89 -52.788 19.610 -17.353 1.00 73.70 C ANISOU 1512 CB LEU C 89 9072 10397 8534 1433 -87 -118 C ATOM 1513 CG LEU C 89 -52.252 20.216 -18.658 1.00 75.72 C ANISOU 1513 CG LEU C 89 9221 11009 8540 1508 -33 40 C ATOM 1514 CD1 LEU C 89 -50.718 20.113 -18.715 1.00 76.56 C ANISOU 1514 CD1 LEU C 89 9220 11084 8787 1460 61 248 C ATOM 1515 CD2 LEU C 89 -52.894 19.608 -19.911 1.00 77.78 C ANISOU 1515 CD2 LEU C 89 9331 11700 8523 1646 50 -297 C ATOM 1516 N ASP C 90 -54.481 21.612 -15.727 1.00 82.69 N ANISOU 1516 N ASP C 90 10554 11236 9628 1428 -414 78 N ATOM 1517 CA ASP C 90 -55.327 22.809 -15.665 1.00 82.84 C ANISOU 1517 CA ASP C 90 10680 11253 9541 1498 -553 160 C ATOM 1518 C ASP C 90 -54.871 23.772 -14.583 1.00 82.49 C ANISOU 1518 C ASP C 90 10773 10909 9662 1451 -704 327 C ATOM 1519 O ASP C 90 -54.859 24.975 -14.819 1.00 83.64 O ANISOU 1519 O ASP C 90 10974 10972 9834 1480 -798 508 O ATOM 1520 CB ASP C 90 -56.807 22.471 -15.435 1.00 82.47 C ANISOU 1520 CB ASP C 90 10631 11289 9414 1563 -559 -111 C ATOM 1521 CG ASP C 90 -57.534 22.047 -16.710 1.00 83.93 C ANISOU 1521 CG ASP C 90 10650 11845 9394 1652 -504 -329 C ATOM 1522 OD1 ASP C 90 -57.236 22.575 -17.770 1.00 85.47 O ANISOU 1522 OD1 ASP C 90 10801 12285 9387 1751 -516 -179 O ATOM 1523 OD2 ASP C 90 -58.437 21.186 -16.663 1.00 84.14 O ANISOU 1523 OD2 ASP C 90 10563 11948 9460 1635 -445 -661 O ATOM 1524 N ILE C 91 -54.516 23.249 -13.407 1.00 74.25 N ANISOU 1524 N ILE C 91 9768 9708 8735 1404 -728 258 N ATOM 1525 CA ILE C 91 -53.997 24.096 -12.342 1.00 74.62 C ANISOU 1525 CA ILE C 91 9902 9545 8905 1382 -909 318 C ATOM 1526 C ILE C 91 -52.717 24.654 -12.806 1.00 75.90 C ANISOU 1526 C ILE C 91 9972 9626 9239 1276 -942 512 C ATOM 1527 O ILE C 91 -52.466 25.826 -12.613 1.00 77.29 O ANISOU 1527 O ILE C 91 10178 9611 9576 1234 -1082 586 O ATOM 1528 CB ILE C 91 -53.744 23.366 -11.035 1.00 74.20 C ANISOU 1528 CB ILE C 91 9878 9456 8859 1411 -932 237 C ATOM 1529 CG1 ILE C 91 -55.076 23.116 -10.367 1.00 73.71 C ANISOU 1529 CG1 ILE C 91 9906 9447 8655 1514 -890 94 C ATOM 1530 CG2 ILE C 91 -52.894 24.181 -10.111 1.00 75.41 C ANISOU 1530 CG2 ILE C 91 10050 9488 9117 1397 -1154 240 C ATOM 1531 CD1 ILE C 91 -54.967 22.326 -9.157 1.00 73.99 C ANISOU 1531 CD1 ILE C 91 9970 9501 8641 1587 -845 101 C ATOM 1532 N SER C 92 -51.905 23.836 -13.444 1.00 84.21 N ANISOU 1532 N SER C 92 10888 10803 10306 1229 -797 584 N ATOM 1533 CA SER C 92 -50.587 24.299 -13.850 1.00 85.87 C ANISOU 1533 CA SER C 92 10957 10967 10705 1116 -792 785 C ATOM 1534 C SER C 92 -50.755 25.526 -14.730 1.00 87.66 C ANISOU 1534 C SER C 92 11189 11143 10973 1091 -775 1014 C ATOM 1535 O SER C 92 -50.062 26.515 -14.567 1.00 89.63 O ANISOU 1535 O SER C 92 11387 11164 11504 974 -854 1167 O ATOM 1536 CB SER C 92 -49.816 23.196 -14.594 1.00 86.06 C ANISOU 1536 CB SER C 92 10811 11195 10694 1117 -596 811 C ATOM 1537 OG SER C 92 -50.112 21.869 -14.108 1.00 84.73 O ANISOU 1537 OG SER C 92 10663 11060 10469 1198 -532 611 O ATOM 1538 N HIS C 93 -51.726 25.473 -15.623 1.00104.10 N ANISOU 1538 N HIS C 93 13321 13431 12801 1216 -678 1034 N ATOM 1539 CA HIS C 93 -51.941 26.564 -16.521 1.00106.40 C ANISOU 1539 CA HIS C 93 13623 13726 13077 1265 -637 1331 C ATOM 1540 C HIS C 93 -52.347 27.800 -15.789 1.00107.27 C ANISOU 1540 C HIS C 93 13867 13462 13429 1255 -818 1363 C ATOM 1541 O HIS C 93 -51.823 28.866 -16.043 1.00110.03 O ANISOU 1541 O HIS C 93 14185 13562 14060 1180 -808 1651 O ATOM 1542 CB HIS C 93 -53.073 26.237 -17.468 1.00106.41 C ANISOU 1542 CB HIS C 93 13644 14093 12695 1467 -561 1276 C ATOM 1543 CG HIS C 93 -53.105 27.121 -18.677 1.00109.65 C ANISOU 1543 CG HIS C 93 14021 14667 12973 1591 -456 1676 C ATOM 1544 ND1 HIS C 93 -53.130 28.505 -18.604 1.00111.97 N ANISOU 1544 ND1 HIS C 93 14398 14630 13514 1597 -506 2012 N ATOM 1545 CD2 HIS C 93 -53.100 26.812 -20.000 1.00111.67 C ANISOU 1545 CD2 HIS C 93 14160 15403 12869 1746 -287 1817 C ATOM 1546 CE1 HIS C 93 -53.143 29.009 -19.828 1.00115.30 C ANISOU 1546 CE1 HIS C 93 14767 15302 13740 1755 -348 2428 C ATOM 1547 NE2 HIS C 93 -53.122 28.007 -20.693 1.00115.19 N ANISOU 1547 NE2 HIS C 93 14630 15834 13305 1862 -221 2313 N ATOM 1548 N PHE C 94 -53.327 27.627 -14.907 1.00 90.86 N ANISOU 1548 N PHE C 94 11920 11341 11260 1341 -957 1060 N ATOM 1549 CA PHE C 94 -54.050 28.711 -14.243 1.00 91.77 C ANISOU 1549 CA PHE C 94 12173 11175 11522 1414 -1129 988 C ATOM 1550 C PHE C 94 -53.131 29.574 -13.478 1.00 93.66 C ANISOU 1550 C PHE C 94 12392 11019 12177 1261 -1271 982 C ATOM 1551 O PHE C 94 -53.344 30.758 -13.438 1.00 96.14 O ANISOU 1551 O PHE C 94 12761 11009 12757 1284 -1354 1060 O ATOM 1552 CB PHE C 94 -55.100 28.131 -13.296 1.00 89.57 C ANISOU 1552 CB PHE C 94 11989 11002 11043 1524 -1211 631 C ATOM 1553 CG PHE C 94 -55.695 29.121 -12.347 1.00 90.65 C ANISOU 1553 CG PHE C 94 12245 10880 11317 1612 -1399 458 C ATOM 1554 CD1 PHE C 94 -56.778 29.864 -12.698 1.00 91.80 C ANISOU 1554 CD1 PHE C 94 12461 10995 11422 1795 -1428 485 C ATOM 1555 CD2 PHE C 94 -55.196 29.261 -11.078 1.00 90.94 C ANISOU 1555 CD2 PHE C 94 12305 10759 11490 1556 -1557 226 C ATOM 1556 CE1 PHE C 94 -57.315 30.746 -11.834 1.00 93.16 C ANISOU 1556 CE1 PHE C 94 12730 10928 11738 1904 -1590 282 C ATOM 1557 CE2 PHE C 94 -55.749 30.146 -10.206 1.00 92.47 C ANISOU 1557 CE2 PHE C 94 12591 10762 11780 1669 -1733 -14 C ATOM 1558 CZ PHE C 94 -56.804 30.888 -10.598 1.00 93.52 C ANISOU 1558 CZ PHE C 94 12800 10814 11919 1837 -1739 11 C ATOM 1559 N LEU C 95 -52.120 28.972 -12.866 1.00 87.94 N ANISOU 1559 N LEU C 95 11564 10315 11535 1120 -1310 862 N ATOM 1560 CA LEU C 95 -51.133 29.719 -12.103 1.00 90.32 C ANISOU 1560 CA LEU C 95 11773 10300 12244 958 -1485 769 C ATOM 1561 C LEU C 95 -50.040 30.328 -12.985 1.00 93.32 C ANISOU 1561 C LEU C 95 11966 10495 12998 760 -1358 1121 C ATOM 1562 O LEU C 95 -49.615 31.473 -12.753 1.00 96.78 O ANISOU 1562 O LEU C 95 12338 10515 13918 624 -1458 1136 O ATOM 1563 CB LEU C 95 -50.503 28.838 -11.037 1.00 89.11 C ANISOU 1563 CB LEU C 95 11551 10314 11992 939 -1607 499 C ATOM 1564 CG LEU C 95 -51.476 28.280 -10.005 1.00 87.15 C ANISOU 1564 CG LEU C 95 11465 10244 11405 1136 -1698 211 C ATOM 1565 CD1 LEU C 95 -50.703 27.380 -9.029 1.00 86.86 C ANISOU 1565 CD1 LEU C 95 11344 10406 11254 1160 -1785 69 C ATOM 1566 CD2 LEU C 95 -52.224 29.385 -9.272 1.00 88.81 C ANISOU 1566 CD2 LEU C 95 11797 10239 11709 1230 -1896 -39 C ATOM 1567 N LYS C 96 -49.579 29.579 -13.989 1.00100.34 N ANISOU 1567 N LYS C 96 12743 11678 13703 740 -1119 1389 N ATOM 1568 CA LYS C 96 -48.612 30.136 -14.948 1.00103.70 C ANISOU 1568 CA LYS C 96 12972 12006 14424 580 -922 1803 C ATOM 1569 C LYS C 96 -49.148 31.442 -15.490 1.00106.89 C ANISOU 1569 C LYS C 96 13463 12082 15067 614 -866 2118 C ATOM 1570 O LYS C 96 -48.412 32.422 -15.571 1.00110.95 O ANISOU 1570 O LYS C 96 13838 12197 16121 419 -827 2337 O ATOM 1571 CB LYS C 96 -48.341 29.211 -16.130 1.00103.01 C ANISOU 1571 CB LYS C 96 12784 12375 13979 651 -639 2048 C ATOM 1572 N GLU C 97 -50.439 31.455 -15.842 1.00133.47 N ANISOU 1572 N GLU C 97 17037 15598 18079 866 -858 2142 N ATOM 1573 CA GLU C 97 -51.088 32.632 -16.398 1.00136.72 C ANISOU 1573 CA GLU C 97 17550 15741 18658 990 -804 2480 C ATOM 1574 C GLU C 97 -51.203 33.689 -15.341 1.00138.67 C ANISOU 1574 C GLU C 97 17861 15395 19431 909 -1040 2231 C ATOM 1575 O GLU C 97 -50.725 34.794 -15.539 1.00143.24 O ANISOU 1575 O GLU C 97 18367 15484 20575 782 -981 2511 O ATOM 1576 CB GLU C 97 -52.479 32.286 -16.924 1.00134.90 C ANISOU 1576 CB GLU C 97 17482 15890 17883 1315 -792 2471 C ATOM 1577 CG GLU C 97 -53.063 33.319 -17.846 1.00138.83 C ANISOU 1577 CG GLU C 97 18046 16283 18419 1527 -677 2962 C ATOM 1578 CD GLU C 97 -52.171 33.561 -19.050 1.00142.63 C ANISOU 1578 CD GLU C 97 18372 16881 18939 1482 -367 3585 C ATOM 1579 OE1 GLU C 97 -51.098 32.916 -19.136 1.00141.93 O ANISOU 1579 OE1 GLU C 97 18110 16951 18868 1268 -253 3571 O ATOM 1580 OE2 GLU C 97 -52.533 34.398 -19.914 1.00146.79 O ANISOU 1580 OE2 GLU C 97 18938 17365 19471 1688 -217 4124 O ATOM 1581 N LYS C 98 -51.811 33.333 -14.210 1.00113.47 N ANISOU 1581 N LYS C 98 14787 12250 16077 987 -1289 1694 N ATOM 1582 CA LYS C 98 -52.005 34.258 -13.099 1.00115.48 C ANISOU 1582 CA LYS C 98 15101 12036 16741 967 -1547 1321 C ATOM 1583 C LYS C 98 -50.694 34.903 -12.733 1.00119.23 C ANISOU 1583 C LYS C 98 15362 12081 17860 655 -1614 1273 C ATOM 1584 O LYS C 98 -50.669 36.013 -12.216 1.00123.12 O ANISOU 1584 O LYS C 98 15842 12031 18906 592 -1765 1089 O ATOM 1585 CB LYS C 98 -52.580 33.539 -11.886 1.00112.06 C ANISOU 1585 CB LYS C 98 14767 11873 15939 1088 -1763 763 C ATOM 1586 CG LYS C 98 -52.837 34.413 -10.683 1.00114.42 C ANISOU 1586 CG LYS C 98 15118 11817 16538 1131 -2042 287 C ATOM 1587 CD LYS C 98 -53.561 33.637 -9.581 1.00111.38 C ANISOU 1587 CD LYS C 98 14839 11827 15655 1321 -2184 -165 C ATOM 1588 CE LYS C 98 -54.125 34.572 -8.505 1.00114.15 C ANISOU 1588 CE LYS C 98 15266 11918 16188 1470 -2434 -652 C ATOM 1589 NZ LYS C 98 -55.409 34.079 -7.917 1.00111.80 N ANISOU 1589 NZ LYS C 98 15116 11994 15370 1759 -2442 -884 N ATOM 1590 N GLY C 99 -49.594 34.216 -13.002 1.00149.90 N ANISOU 1590 N GLY C 99 19042 16191 21722 458 -1507 1398 N ATOM 1591 CA GLY C 99 -48.279 34.768 -12.694 1.00153.88 C ANISOU 1591 CA GLY C 99 19264 16338 22865 136 -1567 1337 C ATOM 1592 C GLY C 99 -47.995 34.641 -11.202 1.00153.65 C ANISOU 1592 C GLY C 99 19174 16312 22893 98 -1944 645 C ATOM 1593 O GLY C 99 -48.763 33.980 -10.461 1.00150.07 O ANISOU 1593 O GLY C 99 18908 16199 21912 333 -2097 308 O ATOM 1594 N GLY C 100 -46.903 35.268 -10.751 1.00155.54 N ANISOU 1594 N GLY C 100 19125 16210 23763 -184 -2087 432 N ATOM 1595 CA GLY C 100 -46.468 35.139 -9.354 1.00156.33 C ANISOU 1595 CA GLY C 100 19100 16420 23880 -198 -2479 -258 C ATOM 1596 C GLY C 100 -46.293 33.670 -8.972 1.00151.68 C ANISOU 1596 C GLY C 100 18528 16514 22590 -37 -2512 -337 C ATOM 1597 O GLY C 100 -47.013 33.111 -8.124 1.00148.97 O ANISOU 1597 O GLY C 100 18382 16500 21720 229 -2673 -647 O ATOM 1598 N LEU C 101 -45.368 33.030 -9.655 1.00117.74 N ANISOU 1598 N LEU C 101 14020 12418 18297 -178 -2313 -3 N ATOM 1599 CA LEU C 101 -44.864 31.772 -9.195 1.00115.11 C ANISOU 1599 CA LEU C 101 13607 12612 17518 -66 -2379 -120 C ATOM 1600 C LEU C 101 -43.570 31.584 -9.941 1.00117.08 C ANISOU 1600 C LEU C 101 13502 12891 18090 -308 -2196 174 C ATOM 1601 O LEU C 101 -42.532 31.478 -9.330 1.00119.54 O ANISOU 1601 O LEU C 101 13502 13305 18612 -413 -2398 -92 O ATOM 1602 CB LEU C 101 -45.865 30.630 -9.438 1.00109.70 C ANISOU 1602 CB LEU C 101 13230 12319 16132 221 -2204 60 C ATOM 1603 CG LEU C 101 -45.691 29.362 -8.571 1.00107.40 C ANISOU 1603 CG LEU C 101 12946 12497 15363 430 -2320 -135 C ATOM 1604 CD1 LEU C 101 -45.920 29.721 -7.094 1.00109.15 C ANISOU 1604 CD1 LEU C 101 13210 12778 15485 576 -2694 -648 C ATOM 1605 CD2 LEU C 101 -46.593 28.170 -9.037 1.00102.81 C ANISOU 1605 CD2 LEU C 101 12610 12202 14253 642 -2061 101 C ATOM 1606 N GLU C 102 -43.633 31.582 -11.267 1.00135.85 N ANISOU 1606 N GLU C 102 15901 15224 20493 -374 -1814 716 N ATOM 1607 CA GLU C 102 -42.444 31.459 -12.091 1.00138.27 C ANISOU 1607 CA GLU C 102 15857 15590 21090 -590 -1570 1051 C ATOM 1608 C GLU C 102 -41.369 32.367 -11.543 1.00143.90 C ANISOU 1608 C GLU C 102 16174 15953 22548 -910 -1766 803 C ATOM 1609 O GLU C 102 -41.534 33.568 -11.537 1.00147.64 O ANISOU 1609 O GLU C 102 16628 15895 23575 -1090 -1798 791 O ATOM 1610 CB GLU C 102 -42.754 31.858 -13.530 1.00139.13 C ANISOU 1610 CB GLU C 102 16035 15591 21238 -626 -1151 1667 C ATOM 1611 CG GLU C 102 -41.557 31.778 -14.479 1.00142.32 C ANISOU 1611 CG GLU C 102 16062 16106 21906 -828 -823 2083 C ATOM 1612 CD GLU C 102 -41.258 30.361 -14.945 1.00139.02 C ANISOU 1612 CD GLU C 102 15606 16290 20925 -639 -658 2151 C ATOM 1613 OE1 GLU C 102 -41.886 29.412 -14.421 1.00134.52 O ANISOU 1613 OE1 GLU C 102 15276 15989 19845 -388 -820 1856 O ATOM 1614 OE2 GLU C 102 -40.394 30.188 -15.839 1.00141.43 O ANISOU 1614 OE2 GLU C 102 15625 16787 21326 -734 -343 2501 O ATOM 1615 N GLY C 103 -40.272 31.790 -11.064 1.00159.34 N ANISOU 1615 N GLY C 103 17789 18193 24561 -971 -1911 575 N ATOM 1616 CA GLY C 103 -39.156 32.563 -10.482 1.00165.30 C ANISOU 1616 CA GLY C 103 18073 18693 26042 -1286 -2147 237 C ATOM 1617 C GLY C 103 -39.378 33.040 -9.048 1.00167.05 C ANISOU 1617 C GLY C 103 18310 18812 26350 -1227 -2667 -487 C ATOM 1618 O GLY C 103 -38.660 33.924 -8.578 1.00172.85 O ANISOU 1618 O GLY C 103 18672 19225 27776 -1508 -2895 -865 O ATOM 1619 N LEU C 104 -40.382 32.480 -8.361 1.00122.05 N ANISOU 1619 N LEU C 104 13013 13394 19969 -864 -2842 -703 N ATOM 1620 CA LEU C 104 -40.553 32.691 -6.928 1.00123.70 C ANISOU 1620 CA LEU C 104 13230 13721 20051 -705 -3328 -1394 C ATOM 1621 C LEU C 104 -39.628 31.729 -6.204 1.00124.14 C ANISOU 1621 C LEU C 104 13011 14364 19791 -549 -3565 -1626 C ATOM 1622 O LEU C 104 -39.449 30.579 -6.620 1.00120.60 O ANISOU 1622 O LEU C 104 12612 14292 18917 -386 -3348 -1251 O ATOM 1623 CB LEU C 104 -41.993 32.440 -6.481 1.00119.46 C ANISOU 1623 CB LEU C 104 13201 13309 18881 -354 -3366 -1467 C ATOM 1624 CG LEU C 104 -42.247 32.380 -4.972 1.00120.75 C ANISOU 1624 CG LEU C 104 13410 13802 18668 -73 -3815 -2114 C ATOM 1625 CD1 LEU C 104 -41.669 33.568 -4.294 1.00127.42 C ANISOU 1625 CD1 LEU C 104 13927 14336 20150 -282 -4191 -2751 C ATOM 1626 CD2 LEU C 104 -43.720 32.311 -4.673 1.00117.30 C ANISOU 1626 CD2 LEU C 104 13441 13411 17718 224 -3769 -2127 C ATOM 1627 N ILE C 105 -39.045 32.212 -5.115 1.00134.04 N ANISOU 1627 N ILE C 105 13960 15703 21266 -572 -4025 -2275 N ATOM 1628 CA ILE C 105 -38.201 31.394 -4.268 1.00135.50 C ANISOU 1628 CA ILE C 105 13867 16509 21107 -350 -4329 -2552 C ATOM 1629 C ILE C 105 -39.065 30.434 -3.467 1.00131.52 C ANISOU 1629 C ILE C 105 13772 16520 19681 161 -4419 -2556 C ATOM 1630 O ILE C 105 -39.974 30.856 -2.744 1.00131.58 O ANISOU 1630 O ILE C 105 14048 16516 19430 337 -4601 -2885 O ATOM 1631 CB ILE C 105 -37.422 32.238 -3.276 1.00142.72 C ANISOU 1631 CB ILE C 105 14322 17440 22466 -476 -4849 -3332 C ATOM 1632 CG1 ILE C 105 -36.528 33.263 -4.003 1.00147.92 C ANISOU 1632 CG1 ILE C 105 14504 17507 24191 -1040 -4749 -3356 C ATOM 1633 CG2 ILE C 105 -36.633 31.328 -2.357 1.00144.44 C ANISOU 1633 CG2 ILE C 105 14269 18419 22190 -144 -5193 -3590 C ATOM 1634 CD1 ILE C 105 -35.381 32.670 -4.803 1.00148.37 C ANISOU 1634 CD1 ILE C 105 14161 17727 24485 -1223 -4491 -2922 C ATOM 1635 N TRP C 106 -38.769 29.144 -3.588 1.00113.82 N ANISOU 1635 N TRP C 106 11554 14712 16979 406 -4267 -2182 N ATOM 1636 CA TRP C 106 -39.501 28.115 -2.855 1.00110.77 C ANISOU 1636 CA TRP C 106 11517 14785 15785 885 -4285 -2078 C ATOM 1637 C TRP C 106 -39.368 28.279 -1.352 1.00115.12 C ANISOU 1637 C TRP C 106 11956 15808 15978 1196 -4790 -2652 C ATOM 1638 O TRP C 106 -38.452 28.924 -0.843 1.00120.73 O ANISOU 1638 O TRP C 106 12230 16618 17022 1083 -5180 -3170 O ATOM 1639 CB TRP C 106 -39.021 26.712 -3.221 1.00108.37 C ANISOU 1639 CB TRP C 106 11184 14797 15194 1089 -4048 -1601 C ATOM 1640 CG TRP C 106 -39.889 25.646 -2.658 1.00105.33 C ANISOU 1640 CG TRP C 106 11186 14724 14109 1527 -3944 -1365 C ATOM 1641 CD1 TRP C 106 -41.078 25.237 -3.140 1.00100.55 C ANISOU 1641 CD1 TRP C 106 11009 13926 13271 1573 -3593 -1034 C ATOM 1642 CD2 TRP C 106 -39.644 24.873 -1.500 1.00107.62 C ANISOU 1642 CD2 TRP C 106 11440 15577 13872 1982 -4179 -1419 C ATOM 1643 NE1 TRP C 106 -41.595 24.244 -2.359 1.00 99.73 N ANISOU 1643 NE1 TRP C 106 11129 14169 12595 1987 -3560 -869 N ATOM 1644 CE2 TRP C 106 -40.723 24.003 -1.343 1.00104.09 C ANISOU 1644 CE2 TRP C 106 11420 15193 12936 2264 -3903 -1057 C ATOM 1645 CE3 TRP C 106 -38.617 24.828 -0.581 1.00112.87 C ANISOU 1645 CE3 TRP C 106 11730 16727 14430 2198 -4594 -1726 C ATOM 1646 CZ2 TRP C 106 -40.802 23.107 -0.312 1.00105.78 C ANISOU 1646 CZ2 TRP C 106 11718 15893 12580 2748 -3981 -913 C ATOM 1647 CZ3 TRP C 106 -38.690 23.926 0.441 1.00114.47 C ANISOU 1647 CZ3 TRP C 106 12024 17482 13986 2729 -4710 -1596 C ATOM 1648 CH2 TRP C 106 -39.767 23.078 0.571 1.00111.02 C ANISOU 1648 CH2 TRP C 106 12036 17056 13089 3000 -4383 -1155 C ATOM 1649 N SER C 107 -40.321 27.691 -0.659 1.00134.50 N ANISOU 1649 N SER C 107 14786 18577 17741 1598 -4767 -2566 N ATOM 1650 CA SER C 107 -40.275 27.556 0.769 1.00138.50 C ANISOU 1650 CA SER C 107 15237 19701 17684 2026 -5170 -2964 C ATOM 1651 C SER C 107 -41.150 26.408 1.147 1.00135.19 C ANISOU 1651 C SER C 107 15218 19616 16533 2459 -4915 -2492 C ATOM 1652 O SER C 107 -41.994 25.985 0.368 1.00129.99 O ANISOU 1652 O SER C 107 14891 18623 15875 2369 -4482 -2030 O ATOM 1653 CB SER C 107 -40.861 28.772 1.435 1.00141.59 C ANISOU 1653 CB SER C 107 15675 19989 18133 1994 -5470 -3616 C ATOM 1654 OG SER C 107 -41.947 28.355 2.243 1.00140.43 O ANISOU 1654 OG SER C 107 15903 20220 17234 2428 -5427 -3560 O ATOM 1655 N GLN C 108 -41.002 25.932 2.365 1.00145.13 N ANISOU 1655 N GLN C 108 16431 21546 17164 2942 -5180 -2616 N ATOM 1656 CA GLN C 108 -41.885 24.891 2.823 1.00143.03 C ANISOU 1656 CA GLN C 108 16535 21578 16232 3362 -4902 -2127 C ATOM 1657 C GLN C 108 -43.246 25.504 2.976 1.00141.17 C ANISOU 1657 C GLN C 108 16644 21154 15838 3335 -4784 -2282 C ATOM 1658 O GLN C 108 -44.232 24.928 2.540 1.00136.74 O ANISOU 1658 O GLN C 108 16420 20374 15161 3339 -4356 -1817 O ATOM 1659 CB GLN C 108 -41.395 24.288 4.137 1.00148.43 C ANISOU 1659 CB GLN C 108 17079 23088 16230 3944 -5201 -2159 C ATOM 1660 CG GLN C 108 -42.199 23.092 4.627 1.00147.28 C ANISOU 1660 CG GLN C 108 17281 23237 15441 4402 -4847 -1513 C ATOM 1661 CD GLN C 108 -42.803 22.280 3.488 1.00140.91 C ANISOU 1661 CD GLN C 108 16754 21825 14962 4158 -4263 -875 C ATOM 1662 OE1 GLN C 108 -42.076 21.640 2.725 1.00139.38 O ANISOU 1662 OE1 GLN C 108 16425 21403 15130 4032 -4112 -569 O ATOM 1663 NE2 GLN C 108 -44.129 22.305 3.363 1.00137.67 N ANISOU 1663 NE2 GLN C 108 16697 21180 14433 4103 -3945 -726 N ATOM 1664 N ARG C 109 -43.277 26.701 3.548 1.00129.23 N ANISOU 1664 N ARG C 109 15009 19698 14394 3290 -5170 -2986 N ATOM 1665 CA ARG C 109 -44.530 27.415 3.813 1.00128.56 C ANISOU 1665 CA ARG C 109 15208 19476 14162 3317 -5118 -3247 C ATOM 1666 C ARG C 109 -45.189 27.884 2.544 1.00123.44 C ANISOU 1666 C ARG C 109 14751 18046 14107 2868 -4783 -3049 C ATOM 1667 O ARG C 109 -46.284 27.466 2.234 1.00119.44 O ANISOU 1667 O ARG C 109 14569 17414 13400 2920 -4415 -2668 O ATOM 1668 CB ARG C 109 -44.281 28.631 4.703 1.00134.81 C ANISOU 1668 CB ARG C 109 15770 20472 14978 3379 -5649 -4152 C ATOM 1669 N ARG C 110 -44.506 28.751 1.811 1.00127.38 N ANISOU 1669 N ARG C 110 15015 18042 15342 2437 -4905 -3291 N ATOM 1670 CA ARG C 110 -45.020 29.269 0.550 1.00123.49 C ANISOU 1670 CA ARG C 110 14670 16837 15413 2039 -4596 -3053 C ATOM 1671 C ARG C 110 -45.719 28.196 -0.269 1.00117.49 C ANISOU 1671 C ARG C 110 14202 16003 14438 2062 -4101 -2346 C ATOM 1672 O ARG C 110 -46.757 28.473 -0.885 1.00114.39 O ANISOU 1672 O ARG C 110 14061 15273 14131 1963 -3851 -2191 O ATOM 1673 CB ARG C 110 -43.907 29.904 -0.287 1.00125.13 C ANISOU 1673 CB ARG C 110 14536 16595 16411 1592 -4664 -3119 C ATOM 1674 CG ARG C 110 -43.549 31.322 0.140 1.00130.87 C ANISOU 1674 CG ARG C 110 15010 17043 17673 1400 -5055 -3842 C ATOM 1675 CD ARG C 110 -42.386 31.881 -0.674 1.00133.26 C ANISOU 1675 CD ARG C 110 14918 16893 18823 929 -5068 -3838 C ATOM 1676 NE ARG C 110 -42.297 33.343 -0.593 1.00138.35 N ANISOU 1676 NE ARG C 110 15379 16986 20201 644 -5298 -4407 N ATOM 1677 CZ ARG C 110 -41.243 34.070 -0.983 1.00142.85 C ANISOU 1677 CZ ARG C 110 15514 17147 21615 225 -5400 -4598 C ATOM 1678 NH1 ARG C 110 -40.154 33.489 -1.483 1.00142.78 N ANISOU 1678 NH1 ARG C 110 15190 17283 21778 53 -5303 -4279 N ATOM 1679 NH2 ARG C 110 -41.269 35.397 -0.865 1.00148.03 N ANISOU 1679 NH2 ARG C 110 16022 17218 23005 -26 -5585 -5124 N ATOM 1680 N GLN C 111 -45.160 26.983 -0.270 1.00121.61 N ANISOU 1680 N GLN C 111 14664 16835 14709 2209 -3976 -1956 N ATOM 1681 CA GLN C 111 -45.802 25.863 -0.946 1.00116.85 C ANISOU 1681 CA GLN C 111 14302 16163 13931 2253 -3524 -1367 C ATOM 1682 C GLN C 111 -47.094 25.505 -0.223 1.00116.02 C ANISOU 1682 C GLN C 111 14499 16292 13290 2560 -3386 -1297 C ATOM 1683 O GLN C 111 -48.143 25.399 -0.860 1.00112.51 O ANISOU 1683 O GLN C 111 14279 15588 12881 2465 -3079 -1089 O ATOM 1684 CB GLN C 111 -44.874 24.652 -1.066 1.00116.78 C ANISOU 1684 CB GLN C 111 14143 16375 13855 2367 -3422 -1001 C ATOM 1685 CG GLN C 111 -45.261 23.689 -2.199 1.00112.27 C ANISOU 1685 CG GLN C 111 13722 15535 13401 2256 -2959 -496 C ATOM 1686 CD GLN C 111 -44.719 22.293 -2.010 1.00112.68 C ANISOU 1686 CD GLN C 111 13718 15821 13273 2511 -2813 -126 C ATOM 1687 OE1 GLN C 111 -43.501 22.081 -1.884 1.00115.19 O ANISOU 1687 OE1 GLN C 111 13753 16316 13698 2566 -2987 -142 O ATOM 1688 NE2 GLN C 111 -45.621 21.322 -1.996 1.00110.70 N ANISOU 1688 NE2 GLN C 111 13712 15547 12803 2672 -2481 211 N ATOM 1689 N GLU C 112 -47.030 25.366 1.095 1.00123.03 N ANISOU 1689 N GLU C 112 15362 17710 13673 2937 -3612 -1484 N ATOM 1690 CA GLU C 112 -48.227 25.058 1.882 1.00123.23 C ANISOU 1690 CA GLU C 112 15638 18031 13151 3258 -3454 -1397 C ATOM 1691 C GLU C 112 -49.364 26.082 1.676 1.00122.02 C ANISOU 1691 C GLU C 112 15651 17590 13120 3127 -3425 -1704 C ATOM 1692 O GLU C 112 -50.541 25.718 1.673 1.00120.02 O ANISOU 1692 O GLU C 112 15613 17346 12642 3223 -3119 -1478 O ATOM 1693 CB GLU C 112 -47.890 24.966 3.368 1.00128.75 C ANISOU 1693 CB GLU C 112 16246 19437 13236 3724 -3752 -1615 C ATOM 1694 CG GLU C 112 -47.009 23.778 3.752 1.00130.58 C ANISOU 1694 CG GLU C 112 16361 20054 13201 4002 -3726 -1188 C ATOM 1695 CD GLU C 112 -46.049 24.054 4.971 1.00137.22 C ANISOU 1695 CD GLU C 112 16936 21586 13616 4376 -4234 -1592 C ATOM 1696 OE1 GLU C 112 -46.215 25.055 5.734 1.00140.99 O ANISOU 1696 OE1 GLU C 112 17348 22350 13871 4496 -4589 -2230 O ATOM 1697 OE2 GLU C 112 -45.111 23.243 5.163 1.00139.17 O ANISOU 1697 OE2 GLU C 112 17015 22116 13748 4580 -4292 -1298 O ATOM 1698 N ILE C 113 -49.026 27.358 1.504 1.00122.62 N ANISOU 1698 N ILE C 113 15602 17385 13601 2914 -3731 -2212 N ATOM 1699 CA ILE C 113 -50.059 28.369 1.263 1.00122.00 C ANISOU 1699 CA ILE C 113 15672 16972 13710 2819 -3707 -2484 C ATOM 1700 C ILE C 113 -50.671 28.068 -0.082 1.00116.82 C ANISOU 1700 C ILE C 113 15162 15861 13362 2554 -3317 -2018 C ATOM 1701 O ILE C 113 -51.853 27.787 -0.156 1.00114.73 O ANISOU 1701 O ILE C 113 15091 15624 12876 2657 -3059 -1849 O ATOM 1702 CB ILE C 113 -49.543 29.822 1.281 1.00125.62 C ANISOU 1702 CB ILE C 113 15956 17092 14683 2625 -4086 -3099 C ATOM 1703 CG1 ILE C 113 -49.157 30.230 2.710 1.00131.66 C ANISOU 1703 CG1 ILE C 113 16565 18375 15084 2940 -4519 -3737 C ATOM 1704 CG2 ILE C 113 -50.614 30.763 0.710 1.00124.40 C ANISOU 1704 CG2 ILE C 113 15975 16442 14849 2505 -3970 -3208 C ATOM 1705 CD1 ILE C 113 -48.574 31.611 2.804 1.00136.29 C ANISOU 1705 CD1 ILE C 113 16921 18600 16263 2732 -4918 -4441 C ATOM 1706 N LEU C 114 -49.868 28.098 -1.139 1.00109.36 N ANISOU 1706 N LEU C 114 14093 14559 12900 2232 -3270 -1821 N ATOM 1707 CA LEU C 114 -50.325 27.627 -2.442 1.00104.97 C ANISOU 1707 CA LEU C 114 13643 13710 12532 2034 -2904 -1368 C ATOM 1708 C LEU C 114 -51.189 26.390 -2.230 1.00102.61 C ANISOU 1708 C LEU C 114 13507 13691 11790 2242 -2597 -1046 C ATOM 1709 O LEU C 114 -52.390 26.377 -2.500 1.00100.77 O ANISOU 1709 O LEU C 114 13431 13391 11468 2272 -2393 -977 O ATOM 1710 CB LEU C 114 -49.130 27.241 -3.325 1.00104.18 C ANISOU 1710 CB LEU C 114 13350 13466 12768 1793 -2843 -1111 C ATOM 1711 CG LEU C 114 -49.123 27.728 -4.771 1.00102.42 C ANISOU 1711 CG LEU C 114 13112 12815 12989 1490 -2663 -896 C ATOM 1712 CD1 LEU C 114 -48.146 26.886 -5.583 1.00101.23 C ANISOU 1712 CD1 LEU C 114 12798 12698 12968 1356 -2491 -568 C ATOM 1713 CD2 LEU C 114 -50.516 27.664 -5.358 1.00 99.57 C ANISOU 1713 CD2 LEU C 114 12983 12362 12486 1539 -2416 -739 C ATOM 1714 N ASP C 115 -50.569 25.353 -1.692 1.00115.31 N ANISOU 1714 N ASP C 115 15050 15609 13152 2401 -2565 -849 N ATOM 1715 CA ASP C 115 -51.204 24.061 -1.662 1.00113.58 C ANISOU 1715 CA ASP C 115 14945 15527 12682 2538 -2213 -455 C ATOM 1716 C ASP C 115 -52.471 24.062 -0.847 1.00114.39 C ANISOU 1716 C ASP C 115 15205 15856 12403 2770 -2101 -502 C ATOM 1717 O ASP C 115 -53.343 23.281 -1.124 1.00112.64 O ANISOU 1717 O ASP C 115 15070 15591 12138 2771 -1760 -227 O ATOM 1718 CB ASP C 115 -50.229 22.944 -1.218 1.00115.05 C ANISOU 1718 CB ASP C 115 15026 15957 12732 2707 -2187 -175 C ATOM 1719 CG ASP C 115 -49.198 22.522 -2.349 1.00113.36 C ANISOU 1719 CG ASP C 115 14656 15482 12933 2465 -2120 0 C ATOM 1720 OD1 ASP C 115 -49.507 22.608 -3.582 1.00110.42 O ANISOU 1720 OD1 ASP C 115 14308 14783 12865 2201 -1935 62 O ATOM 1721 OD2 ASP C 115 -48.064 22.088 -1.978 1.00115.50 O ANISOU 1721 OD2 ASP C 115 14758 15941 13185 2583 -2255 72 O ATOM 1722 N LEU C 116 -52.620 24.950 0.110 1.00103.27 N ANISOU 1722 N LEU C 116 13804 14682 10752 2956 -2371 -886 N ATOM 1723 CA LEU C 116 -53.863 24.948 0.904 1.00104.51 C ANISOU 1723 CA LEU C 116 14089 15117 10502 3211 -2226 -930 C ATOM 1724 C LEU C 116 -55.011 25.646 0.214 1.00102.36 C ANISOU 1724 C LEU C 116 13905 14541 10446 3062 -2119 -1077 C ATOM 1725 O LEU C 116 -56.116 25.132 0.154 1.00101.25 O ANISOU 1725 O LEU C 116 13835 14454 10182 3111 -1805 -880 O ATOM 1726 CB LEU C 116 -53.639 25.595 2.262 1.00109.37 C ANISOU 1726 CB LEU C 116 14666 16202 10688 3543 -2554 -1341 C ATOM 1727 CG LEU C 116 -52.908 24.631 3.190 1.00112.37 C ANISOU 1727 CG LEU C 116 14983 17086 10625 3852 -2562 -1067 C ATOM 1728 CD1 LEU C 116 -51.978 25.378 4.165 1.00117.35 C ANISOU 1728 CD1 LEU C 116 15460 18128 11002 4077 -3065 -1585 C ATOM 1729 CD2 LEU C 116 -53.936 23.704 3.888 1.00113.55 C ANISOU 1729 CD2 LEU C 116 15254 17596 10295 4150 -2156 -643 C ATOM 1730 N TRP C 117 -54.725 26.834 -0.288 1.00105.50 N ANISOU 1730 N TRP C 117 14271 14612 11201 2891 -2381 -1416 N ATOM 1731 CA TRP C 117 -55.654 27.628 -1.052 1.00104.00 C ANISOU 1731 CA TRP C 117 14151 14090 11275 2774 -2325 -1529 C ATOM 1732 C TRP C 117 -56.323 26.842 -2.152 1.00100.24 C ANISOU 1732 C TRP C 117 13707 13459 10921 2611 -1976 -1139 C ATOM 1733 O TRP C 117 -57.417 27.171 -2.537 1.00 99.43 O ANISOU 1733 O TRP C 117 13653 13275 10852 2627 -1864 -1183 O ATOM 1734 CB TRP C 117 -54.904 28.790 -1.660 1.00104.81 C ANISOU 1734 CB TRP C 117 14186 13765 11874 2557 -2596 -1761 C ATOM 1735 CG TRP C 117 -55.669 29.573 -2.573 1.00103.72 C ANISOU 1735 CG TRP C 117 14112 13251 12047 2455 -2533 -1762 C ATOM 1736 CD1 TRP C 117 -56.870 30.142 -2.348 1.00104.53 C ANISOU 1736 CD1 TRP C 117 14303 13359 12056 2634 -2506 -1959 C ATOM 1737 CD2 TRP C 117 -55.287 29.933 -3.882 1.00102.26 C ANISOU 1737 CD2 TRP C 117 13893 12654 12307 2190 -2485 -1533 C ATOM 1738 NE1 TRP C 117 -57.275 30.841 -3.447 1.00103.66 N ANISOU 1738 NE1 TRP C 117 14222 12848 12317 2514 -2464 -1856 N ATOM 1739 CE2 TRP C 117 -56.312 30.715 -4.413 1.00102.34 C ANISOU 1739 CE2 TRP C 117 13986 12435 12462 2243 -2440 -1567 C ATOM 1740 CE3 TRP C 117 -54.170 29.665 -4.672 1.00101.33 C ANISOU 1740 CE3 TRP C 117 13665 12377 12457 1941 -2459 -1277 C ATOM 1741 CZ2 TRP C 117 -56.257 31.237 -5.714 1.00101.73 C ANISOU 1741 CZ2 TRP C 117 13903 11993 12756 2078 -2367 -1304 C ATOM 1742 CZ3 TRP C 117 -54.116 30.181 -5.974 1.00100.65 C ANISOU 1742 CZ3 TRP C 117 13566 11942 12736 1755 -2361 -1030 C ATOM 1743 CH2 TRP C 117 -55.148 30.952 -6.477 1.00100.96 C ANISOU 1743 CH2 TRP C 117 13705 11778 12876 1834 -2317 -1023 C ATOM 1744 N ILE C 118 -55.678 25.811 -2.674 1.00 95.11 N ANISOU 1744 N ILE C 118 13004 12783 10350 2474 -1819 -806 N ATOM 1745 CA ILE C 118 -56.285 25.019 -3.736 1.00 92.22 C ANISOU 1745 CA ILE C 118 12634 12290 10117 2324 -1510 -536 C ATOM 1746 C ILE C 118 -57.280 24.062 -3.140 1.00 92.57 C ANISOU 1746 C ILE C 118 12698 12568 9904 2467 -1217 -389 C ATOM 1747 O ILE C 118 -58.409 23.968 -3.586 1.00 91.65 O ANISOU 1747 O ILE C 118 12572 12423 9826 2433 -1033 -397 O ATOM 1748 CB ILE C 118 -55.236 24.272 -4.564 1.00 90.72 C ANISOU 1748 CB ILE C 118 12358 11965 10146 2138 -1439 -296 C ATOM 1749 CG1 ILE C 118 -54.318 25.278 -5.245 1.00 90.88 C ANISOU 1749 CG1 ILE C 118 12319 11748 10461 1969 -1670 -391 C ATOM 1750 CG2 ILE C 118 -55.895 23.463 -5.621 1.00 88.54 C ANISOU 1750 CG2 ILE C 118 12054 11600 9989 2012 -1150 -133 C ATOM 1751 CD1 ILE C 118 -53.197 24.677 -5.911 1.00 90.16 C ANISOU 1751 CD1 ILE C 118 12112 11593 10550 1822 -1618 -195 C ATOM 1752 N TYR C 119 -56.866 23.359 -2.103 1.00105.16 N ANISOU 1752 N TYR C 119 14295 14416 11243 2645 -1164 -236 N ATOM 1753 CA TYR C 119 -57.739 22.375 -1.472 1.00106.39 C ANISOU 1753 CA TYR C 119 14455 14775 11194 2783 -817 11 C ATOM 1754 C TYR C 119 -59.014 23.056 -1.081 1.00107.38 C ANISOU 1754 C TYR C 119 14604 15056 11141 2903 -777 -209 C ATOM 1755 O TYR C 119 -60.124 22.537 -1.243 1.00107.26 O ANISOU 1755 O TYR C 119 14534 15051 11169 2866 -467 -101 O ATOM 1756 CB TYR C 119 -57.103 21.804 -0.206 1.00109.64 C ANISOU 1756 CB TYR C 119 14882 15528 11249 3064 -810 227 C ATOM 1757 CG TYR C 119 -57.987 20.832 0.533 1.00111.95 C ANISOU 1757 CG TYR C 119 15174 16032 11332 3235 -400 579 C ATOM 1758 CD1 TYR C 119 -59.023 20.175 -0.101 1.00110.74 C ANISOU 1758 CD1 TYR C 119 14959 15652 11466 3043 -32 722 C ATOM 1759 CD2 TYR C 119 -57.760 20.538 1.851 1.00116.02 C ANISOU 1759 CD2 TYR C 119 15718 16990 11376 3593 -365 787 C ATOM 1760 CE1 TYR C 119 -59.825 19.286 0.561 1.00113.52 C ANISOU 1760 CE1 TYR C 119 15267 16140 11726 3156 388 1072 C ATOM 1761 CE2 TYR C 119 -58.558 19.625 2.527 1.00118.90 C ANISOU 1761 CE2 TYR C 119 16068 17539 11569 3755 78 1215 C ATOM 1762 CZ TYR C 119 -59.590 18.998 1.866 1.00117.60 C ANISOU 1762 CZ TYR C 119 15831 17063 11790 3507 473 1366 C ATOM 1763 OH TYR C 119 -60.411 18.090 2.504 1.00121.04 O ANISOU 1763 OH TYR C 119 16210 17616 12166 3617 962 1811 O ATOM 1764 N HIS C 120 -58.819 24.241 -0.544 1.00127.05 N ANISOU 1764 N HIS C 120 17145 17662 13467 3050 -1103 -562 N ATOM 1765 CA HIS C 120 -59.910 25.030 -0.068 1.00128.66 C ANISOU 1765 CA HIS C 120 17368 18031 13487 3225 -1115 -844 C ATOM 1766 C HIS C 120 -60.832 25.395 -1.195 1.00126.28 C ANISOU 1766 C HIS C 120 17033 17448 13501 3047 -1038 -922 C ATOM 1767 O HIS C 120 -62.037 25.194 -1.105 1.00126.82 O ANISOU 1767 O HIS C 120 17041 17654 13491 3113 -801 -912 O ATOM 1768 CB HIS C 120 -59.384 26.298 0.556 1.00131.08 C ANISOU 1768 CB HIS C 120 17716 18404 13683 3387 -1525 -1298 C ATOM 1769 CG HIS C 120 -60.180 26.733 1.715 1.00134.74 C ANISOU 1769 CG HIS C 120 18192 19286 13717 3732 -1520 -1561 C ATOM 1770 ND1 HIS C 120 -59.855 26.355 2.998 1.00138.44 N ANISOU 1770 ND1 HIS C 120 18659 20278 13665 4041 -1524 -1534 N ATOM 1771 CD2 HIS C 120 -61.318 27.460 1.796 1.00135.76 C ANISOU 1771 CD2 HIS C 120 18320 19450 13814 3861 -1487 -1838 C ATOM 1772 CE1 HIS C 120 -60.745 26.871 3.831 1.00141.69 C ANISOU 1772 CE1 HIS C 120 19069 21052 13716 4344 -1493 -1814 C ATOM 1773 NE2 HIS C 120 -61.642 27.546 3.128 1.00140.05 N ANISOU 1773 NE2 HIS C 120 18856 20534 13821 4234 -1469 -2016 N ATOM 1774 N THR C 121 -60.226 25.910 -2.255 1.00 91.11 N ANISOU 1774 N THR C 121 12590 12638 9389 2838 -1230 -975 N ATOM 1775 CA THR C 121 -60.936 26.525 -3.340 1.00 89.67 C ANISOU 1775 CA THR C 121 12385 12226 9459 2740 -1246 -1062 C ATOM 1776 C THR C 121 -61.553 25.514 -4.279 1.00 87.62 C ANISOU 1776 C THR C 121 12019 11950 9321 2572 -959 -841 C ATOM 1777 O THR C 121 -62.687 25.680 -4.718 1.00 87.62 O ANISOU 1777 O THR C 121 11942 11995 9354 2602 -868 -929 O ATOM 1778 CB THR C 121 -59.980 27.399 -4.121 1.00 89.04 C ANISOU 1778 CB THR C 121 12343 11802 9686 2598 -1511 -1110 C ATOM 1779 OG1 THR C 121 -59.674 28.550 -3.330 1.00 91.77 O ANISOU 1779 OG1 THR C 121 12746 12088 10035 2744 -1797 -1440 O ATOM 1780 CG2 THR C 121 -60.564 27.834 -5.434 1.00 87.76 C ANISOU 1780 CG2 THR C 121 12154 11438 9754 2511 -1485 -1050 C ATOM 1781 N GLN C 122 -60.803 24.461 -4.566 1.00 81.21 N ANISOU 1781 N GLN C 122 11176 11085 8594 2414 -831 -600 N ATOM 1782 CA GLN C 122 -61.131 23.535 -5.637 1.00 79.63 C ANISOU 1782 CA GLN C 122 10856 10804 8596 2222 -614 -480 C ATOM 1783 C GLN C 122 -61.158 22.075 -5.236 1.00 80.24 C ANISOU 1783 C GLN C 122 10856 10922 8709 2166 -296 -260 C ATOM 1784 O GLN C 122 -61.384 21.217 -6.086 1.00 79.56 O ANISOU 1784 O GLN C 122 10644 10729 8856 1994 -116 -230 O ATOM 1785 CB GLN C 122 -60.075 23.671 -6.713 1.00 78.00 C ANISOU 1785 CB GLN C 122 10658 10400 8578 2064 -752 -418 C ATOM 1786 CG GLN C 122 -59.850 25.078 -7.191 1.00 78.06 C ANISOU 1786 CG GLN C 122 10735 10279 8648 2093 -1023 -524 C ATOM 1787 CD GLN C 122 -61.046 25.617 -7.924 1.00 78.22 C ANISOU 1787 CD GLN C 122 10703 10340 8676 2157 -1018 -634 C ATOM 1788 OE1 GLN C 122 -62.060 24.944 -8.112 1.00 78.20 O ANISOU 1788 OE1 GLN C 122 10580 10498 8633 2157 -835 -690 O ATOM 1789 NE2 GLN C 122 -60.924 26.845 -8.367 1.00 78.92 N ANISOU 1789 NE2 GLN C 122 10857 10271 8859 2217 -1219 -658 N ATOM 1790 N GLY C 123 -60.866 21.774 -3.975 1.00 80.85 N ANISOU 1790 N GLY C 123 10999 11148 8573 2326 -229 -105 N ATOM 1791 CA GLY C 123 -61.143 20.451 -3.432 1.00 82.58 C ANISOU 1791 CA GLY C 123 11145 11399 8834 2328 142 186 C ATOM 1792 C GLY C 123 -60.054 19.427 -3.616 1.00 82.42 C ANISOU 1792 C GLY C 123 11124 11191 8999 2250 228 448 C ATOM 1793 O GLY C 123 -60.253 18.258 -3.312 1.00 84.24 O ANISOU 1793 O GLY C 123 11286 11340 9382 2235 565 725 O ATOM 1794 N TYR C 124 -58.899 19.858 -4.101 1.00 95.30 N ANISOU 1794 N TYR C 124 12814 12733 10664 2208 -51 380 N ATOM 1795 CA TYR C 124 -57.792 18.948 -4.318 1.00 95.32 C ANISOU 1795 CA TYR C 124 12792 12580 10845 2164 8 597 C ATOM 1796 C TYR C 124 -56.955 18.931 -3.059 1.00 97.57 C ANISOU 1796 C TYR C 124 13157 13080 10834 2422 -97 805 C ATOM 1797 O TYR C 124 -56.263 19.914 -2.709 1.00 97.62 O ANISOU 1797 O TYR C 124 13216 13242 10636 2513 -442 635 O ATOM 1798 CB TYR C 124 -56.975 19.351 -5.560 1.00 92.95 C ANISOU 1798 CB TYR C 124 12458 12123 10736 1990 -197 432 C ATOM 1799 CG TYR C 124 -57.813 19.308 -6.798 1.00 91.55 C ANISOU 1799 CG TYR C 124 12184 11844 10756 1805 -103 232 C ATOM 1800 CD1 TYR C 124 -58.194 18.095 -7.341 1.00 92.12 C ANISOU 1800 CD1 TYR C 124 12126 11764 11111 1687 182 242 C ATOM 1801 CD2 TYR C 124 -58.284 20.459 -7.391 1.00 90.40 C ANISOU 1801 CD2 TYR C 124 12057 11763 10528 1777 -297 17 C ATOM 1802 CE1 TYR C 124 -59.024 18.020 -8.455 1.00 91.59 C ANISOU 1802 CE1 TYR C 124 11924 11686 11192 1542 237 -24 C ATOM 1803 CE2 TYR C 124 -59.104 20.390 -8.518 1.00 89.79 C ANISOU 1803 CE2 TYR C 124 11866 11688 10561 1669 -228 -161 C ATOM 1804 CZ TYR C 124 -59.471 19.157 -9.043 1.00 90.41 C ANISOU 1804 CZ TYR C 124 11789 11690 10871 1551 23 -214 C ATOM 1805 OH TYR C 124 -60.268 19.042 -10.153 1.00 90.50 O ANISOU 1805 OH TYR C 124 11641 11775 10969 1463 54 -473 O ATOM 1806 N PHE C 125 -57.030 17.805 -2.365 1.00115.83 N ANISOU 1806 N PHE C 125 15457 15408 13144 2553 205 1173 N ATOM 1807 CA PHE C 125 -56.271 17.629 -1.129 1.00118.89 C ANISOU 1807 CA PHE C 125 15903 16086 13183 2874 134 1445 C ATOM 1808 C PHE C 125 -54.861 18.120 -1.329 1.00118.03 C ANISOU 1808 C PHE C 125 15781 16013 13052 2890 -248 1304 C ATOM 1809 O PHE C 125 -54.452 18.278 -2.473 1.00115.30 O ANISOU 1809 O PHE C 125 15379 15402 13028 2641 -336 1127 O ATOM 1810 CB PHE C 125 -56.214 16.163 -0.775 1.00121.70 C ANISOU 1810 CB PHE C 125 16227 16300 13714 2976 531 1953 C ATOM 1811 CG PHE C 125 -55.834 15.907 0.621 1.00125.97 C ANISOU 1811 CG PHE C 125 16827 17232 13806 3382 556 2335 C ATOM 1812 CD1 PHE C 125 -56.803 15.581 1.560 1.00129.45 C ANISOU 1812 CD1 PHE C 125 17290 17896 13998 3573 888 2648 C ATOM 1813 CD2 PHE C 125 -54.525 15.981 0.999 1.00127.13 C ANISOU 1813 CD2 PHE C 125 16974 17579 13752 3599 260 2395 C ATOM 1814 CE1 PHE C 125 -56.479 15.334 2.848 1.00134.13 C ANISOU 1814 CE1 PHE C 125 17933 18938 14092 4006 933 3047 C ATOM 1815 CE2 PHE C 125 -54.189 15.743 2.298 1.00131.76 C ANISOU 1815 CE2 PHE C 125 17596 18623 13846 4035 256 2743 C ATOM 1816 CZ PHE C 125 -55.177 15.414 3.238 1.00135.40 C ANISOU 1816 CZ PHE C 125 18106 19342 13996 4260 600 3092 C ATOM 1817 N PRO C 126 -54.109 18.359 -0.238 1.00119.43 N ANISOU 1817 N PRO C 126 15976 16560 12842 3192 -473 1371 N ATOM 1818 CA PRO C 126 -52.781 18.837 -0.557 1.00118.80 C ANISOU 1818 CA PRO C 126 15815 16477 12847 3144 -834 1181 C ATOM 1819 C PRO C 126 -51.745 17.781 -0.307 1.00120.92 C ANISOU 1819 C PRO C 126 16009 16775 13161 3327 -770 1549 C ATOM 1820 O PRO C 126 -51.046 17.860 0.660 1.00124.16 O ANISOU 1820 O PRO C 126 16383 17568 13224 3632 -984 1613 O ATOM 1821 CB PRO C 126 -52.603 20.064 0.375 1.00120.86 C ANISOU 1821 CB PRO C 126 16086 17133 12703 3325 -1233 823 C ATOM 1822 CG PRO C 126 -53.824 20.106 1.239 1.00122.72 C ANISOU 1822 CG PRO C 126 16428 17635 12564 3531 -1049 874 C ATOM 1823 CD PRO C 126 -54.471 18.756 1.125 1.00122.93 C ANISOU 1823 CD PRO C 126 16481 17493 12735 3533 -545 1382 C ATOM 1824 N ASP C 127 -51.664 16.795 -1.179 1.00105.06 N ANISOU 1824 N ASP C 127 13960 14381 11577 3172 -486 1757 N ATOM 1825 CA ASP C 127 -50.587 15.830 -1.138 1.00107.01 C ANISOU 1825 CA ASP C 127 14115 14573 11972 3335 -436 2063 C ATOM 1826 C ASP C 127 -50.048 15.471 -2.518 1.00104.44 C ANISOU 1826 C ASP C 127 13679 13858 12146 3060 -370 1941 C ATOM 1827 O ASP C 127 -49.553 14.358 -2.706 1.00105.97 O ANISOU 1827 O ASP C 127 13810 13846 12608 3158 -164 2210 O ATOM 1828 CB ASP C 127 -51.084 14.570 -0.434 1.00110.44 C ANISOU 1828 CB ASP C 127 14613 14948 12400 3587 -27 2604 C ATOM 1829 CG ASP C 127 -52.292 13.965 -1.110 1.00109.05 C ANISOU 1829 CG ASP C 127 14471 14341 12621 3321 394 2640 C ATOM 1830 OD1 ASP C 127 -52.738 14.542 -2.122 1.00105.34 O ANISOU 1830 OD1 ASP C 127 13979 13699 12345 2986 328 2228 O ATOM 1831 OD2 ASP C 127 -52.798 12.917 -0.638 1.00112.21 O ANISOU 1831 OD2 ASP C 127 14895 14580 13160 3454 794 3085 O ATOM 1832 N TRP C 128 -50.150 16.400 -3.470 1.00 95.21 N ANISOU 1832 N TRP C 128 12482 12599 11093 2753 -525 1554 N ATOM 1833 CA TRP C 128 -49.797 16.139 -4.887 1.00 93.04 C ANISOU 1833 CA TRP C 128 12100 12039 11211 2502 -431 1415 C ATOM 1834 C TRP C 128 -48.553 16.886 -5.332 1.00 92.63 C ANISOU 1834 C TRP C 128 11895 12095 11203 2420 -726 1245 C ATOM 1835 O TRP C 128 -47.854 16.472 -6.278 1.00 92.21 O ANISOU 1835 O TRP C 128 11704 11912 11420 2327 -644 1225 O ATOM 1836 CB TRP C 128 -50.958 16.491 -5.847 1.00 90.29 C ANISOU 1836 CB TRP C 128 11807 11524 10977 2229 -302 1173 C ATOM 1837 CG TRP C 128 -51.360 17.890 -5.790 1.00 88.88 C ANISOU 1837 CG TRP C 128 11692 11493 10585 2134 -552 937 C ATOM 1838 CD1 TRP C 128 -52.318 18.406 -5.012 1.00 89.19 C ANISOU 1838 CD1 TRP C 128 11850 11660 10376 2209 -584 889 C ATOM 1839 CD2 TRP C 128 -50.801 18.987 -6.511 1.00 87.60 C ANISOU 1839 CD2 TRP C 128 11466 11343 10475 1966 -786 732 C ATOM 1840 NE1 TRP C 128 -52.400 19.781 -5.184 1.00 88.16 N ANISOU 1840 NE1 TRP C 128 11746 11590 10161 2112 -852 624 N ATOM 1841 CE2 TRP C 128 -51.475 20.153 -6.110 1.00 87.28 C ANISOU 1841 CE2 TRP C 128 11525 11379 10259 1950 -967 555 C ATOM 1842 CE3 TRP C 128 -49.798 19.100 -7.449 1.00 87.23 C ANISOU 1842 CE3 TRP C 128 11272 11243 10629 1839 -831 704 C ATOM 1843 CZ2 TRP C 128 -51.172 21.411 -6.616 1.00 86.81 C ANISOU 1843 CZ2 TRP C 128 11433 11268 10283 1801 -1186 379 C ATOM 1844 CZ3 TRP C 128 -49.497 20.368 -7.963 1.00 86.75 C ANISOU 1844 CZ3 TRP C 128 11166 11179 10614 1676 -1027 566 C ATOM 1845 CH2 TRP C 128 -50.177 21.495 -7.541 1.00 86.64 C ANISOU 1845 CH2 TRP C 128 11264 11168 10486 1654 -1199 419 C ATOM 1846 N GLN C 129 -48.277 18.007 -4.671 1.00101.01 N ANISOU 1846 N GLN C 129 12952 13395 12034 2446 -1057 1088 N ATOM 1847 CA GLN C 129 -47.178 18.867 -5.088 1.00101.18 C ANISOU 1847 CA GLN C 129 12788 13471 12186 2304 -1328 898 C ATOM 1848 C GLN C 129 -45.875 18.358 -4.496 1.00104.18 C ANISOU 1848 C GLN C 129 12973 14055 12555 2526 -1474 1023 C ATOM 1849 O GLN C 129 -45.200 19.075 -3.778 1.00106.41 O ANISOU 1849 O GLN C 129 13130 14587 12712 2598 -1813 861 O ATOM 1850 CB GLN C 129 -47.414 20.332 -4.696 1.00101.35 C ANISOU 1850 CB GLN C 129 12841 13576 12093 2203 -1630 603 C ATOM 1851 CG GLN C 129 -46.238 21.200 -5.091 1.00102.47 C ANISOU 1851 CG GLN C 129 12744 13705 12484 2020 -1877 428 C ATOM 1852 CD GLN C 129 -46.581 22.610 -5.429 1.00102.05 C ANISOU 1852 CD GLN C 129 12714 13485 12574 1783 -2024 180 C ATOM 1853 OE1 GLN C 129 -45.681 23.450 -5.625 1.00103.82 O ANISOU 1853 OE1 GLN C 129 12728 13648 13072 1608 -2222 32 O ATOM 1854 NE2 GLN C 129 -47.880 22.898 -5.531 1.00100.20 N ANISOU 1854 NE2 GLN C 129 12709 13144 12218 1770 -1914 143 N ATOM 1855 N ASN C 130 -45.515 17.126 -4.806 1.00104.94 N ANISOU 1855 N ASN C 130 13017 14046 12810 2650 -1234 1271 N ATOM 1856 CA ASN C 130 -44.298 16.548 -4.274 1.00108.18 C ANISOU 1856 CA ASN C 130 13230 14653 13221 2919 -1355 1430 C ATOM 1857 C ASN C 130 -43.297 16.548 -5.368 1.00107.77 C ANISOU 1857 C ASN C 130 12929 14508 13509 2742 -1336 1333 C ATOM 1858 O ASN C 130 -43.656 16.592 -6.516 1.00105.29 O ANISOU 1858 O ASN C 130 12643 13967 13396 2492 -1130 1243 O ATOM 1859 CB ASN C 130 -44.574 15.141 -3.839 1.00109.95 C ANISOU 1859 CB ASN C 130 13557 14774 13446 3225 -1066 1817 C ATOM 1860 CG ASN C 130 -45.903 15.033 -3.190 1.00109.66 C ANISOU 1860 CG ASN C 130 13781 14705 13179 3287 -903 1949 C ATOM 1861 OD1 ASN C 130 -46.118 15.639 -2.139 1.00111.17 O ANISOU 1861 OD1 ASN C 130 14037 15232 12970 3448 -1119 1925 O ATOM 1862 ND2 ASN C 130 -46.848 14.321 -3.842 1.00108.05 N ANISOU 1862 ND2 ASN C 130 13697 14122 13233 3145 -524 2026 N ATOM 1863 N TYR C 131 -42.033 16.501 -5.023 1.00 86.10 N ANISOU 1863 N TYR C 131 9914 11997 10802 2896 -1548 1345 N ATOM 1864 CA TYR C 131 -41.020 16.532 -6.038 1.00 86.27 C ANISOU 1864 CA TYR C 131 9650 11980 11148 2735 -1509 1261 C ATOM 1865 C TYR C 131 -39.976 15.454 -5.767 1.00 89.58 C ANISOU 1865 C TYR C 131 9852 12519 11663 3080 -1489 1465 C ATOM 1866 O TYR C 131 -39.893 14.893 -4.655 1.00 92.30 O ANISOU 1866 O TYR C 131 10241 13041 11788 3458 -1592 1679 O ATOM 1867 CB TYR C 131 -40.357 17.896 -6.062 1.00 87.10 C ANISOU 1867 CB TYR C 131 9522 12242 11329 2481 -1824 987 C ATOM 1868 CG TYR C 131 -41.273 19.045 -6.377 1.00 84.58 C ANISOU 1868 CG TYR C 131 9388 11756 10993 2163 -1849 804 C ATOM 1869 CD1 TYR C 131 -41.165 19.718 -7.576 1.00 83.27 C ANISOU 1869 CD1 TYR C 131 9130 11421 11089 1825 -1721 742 C ATOM 1870 CD2 TYR C 131 -42.208 19.488 -5.471 1.00 84.16 C ANISOU 1870 CD2 TYR C 131 9580 11743 10654 2236 -1994 716 C ATOM 1871 CE1 TYR C 131 -41.992 20.803 -7.881 1.00 81.58 C ANISOU 1871 CE1 TYR C 131 9081 11031 10884 1577 -1740 628 C ATOM 1872 CE2 TYR C 131 -43.028 20.557 -5.757 1.00 82.30 C ANISOU 1872 CE2 TYR C 131 9497 11336 10438 1983 -2023 539 C ATOM 1873 CZ TYR C 131 -42.928 21.218 -6.968 1.00 81.01 C ANISOU 1873 CZ TYR C 131 9254 10955 10570 1657 -1901 509 C ATOM 1874 OH TYR C 131 -43.761 22.281 -7.288 1.00 79.67 O ANISOU 1874 OH TYR C 131 9240 10588 10442 1449 -1916 394 O ATOM 1875 N THR C 132 -39.180 15.169 -6.790 1.00100.13 N ANISOU 1875 N THR C 132 10946 13793 13307 2989 -1343 1422 N ATOM 1876 CA THR C 132 -38.063 14.283 -6.642 1.00103.62 C ANISOU 1876 CA THR C 132 11117 14360 13892 3310 -1345 1565 C ATOM 1877 C THR C 132 -37.087 14.891 -5.643 1.00107.12 C ANISOU 1877 C THR C 132 11271 15235 14195 3455 -1785 1494 C ATOM 1878 O THR C 132 -36.933 16.107 -5.615 1.00106.81 O ANISOU 1878 O THR C 132 11109 15326 14150 3160 -2030 1228 O ATOM 1879 CB THR C 132 -37.373 14.123 -7.957 1.00103.49 C ANISOU 1879 CB THR C 132 10848 14277 14199 3149 -1131 1452 C ATOM 1880 OG1 THR C 132 -36.806 15.381 -8.341 1.00103.45 O ANISOU 1880 OG1 THR C 132 10589 14455 14261 2810 -1309 1246 O ATOM 1881 CG2 THR C 132 -38.376 13.646 -8.992 1.00100.50 C ANISOU 1881 CG2 THR C 132 10723 13555 13909 2998 -751 1406 C ATOM 1882 N PRO C 133 -36.455 14.056 -4.796 1.00118.74 N ANISOU 1882 N PRO C 133 12622 16926 15569 3927 -1896 1721 N ATOM 1883 CA PRO C 133 -35.354 14.544 -3.984 1.00122.96 C ANISOU 1883 CA PRO C 133 12778 17953 15990 4099 -2339 1591 C ATOM 1884 C PRO C 133 -34.232 15.037 -4.845 1.00123.93 C ANISOU 1884 C PRO C 133 12440 18157 16489 3828 -2388 1345 C ATOM 1885 O PRO C 133 -34.213 14.751 -6.052 1.00121.85 O ANISOU 1885 O PRO C 133 12161 17615 16521 3626 -2037 1361 O ATOM 1886 CB PRO C 133 -34.902 13.306 -3.203 1.00127.20 C ANISOU 1886 CB PRO C 133 13272 18661 16396 4715 -2340 1975 C ATOM 1887 CG PRO C 133 -35.657 12.162 -3.773 1.00125.23 C ANISOU 1887 CG PRO C 133 13345 17897 16339 4799 -1847 2288 C ATOM 1888 CD PRO C 133 -36.898 12.733 -4.333 1.00120.11 C ANISOU 1888 CD PRO C 133 13032 16922 15680 4349 -1656 2125 C ATOM 1889 N GLY C 134 -33.304 15.762 -4.224 1.00116.12 N ANISOU 1889 N GLY C 134 11050 17585 15486 3835 -2817 1099 N ATOM 1890 CA GLY C 134 -32.216 16.405 -4.942 1.00117.85 C ANISOU 1890 CA GLY C 134 10762 17902 16115 3518 -2880 849 C ATOM 1891 C GLY C 134 -30.939 15.606 -4.828 1.00122.52 C ANISOU 1891 C GLY C 134 10898 18814 16839 3897 -2957 939 C ATOM 1892 O GLY C 134 -30.967 14.380 -4.793 1.00123.05 O ANISOU 1892 O GLY C 134 11103 18813 16837 4324 -2752 1262 O ATOM 1893 N PRO C 135 -29.795 16.286 -4.822 1.00146.25 N ANISOU 1893 N PRO C 135 13326 22136 20108 3736 -3229 652 N ATOM 1894 CA PRO C 135 -29.587 17.694 -5.063 1.00146.64 C ANISOU 1894 CA PRO C 135 13116 22160 20442 3179 -3394 281 C ATOM 1895 C PRO C 135 -29.590 17.946 -6.556 1.00143.93 C ANISOU 1895 C PRO C 135 12737 21462 20489 2735 -2922 368 C ATOM 1896 O PRO C 135 -29.203 17.073 -7.336 1.00143.87 O ANISOU 1896 O PRO C 135 12637 21431 20595 2892 -2586 576 O ATOM 1897 CB PRO C 135 -28.209 17.940 -4.491 1.00153.15 C ANISOU 1897 CB PRO C 135 13249 23490 21452 3291 -3813 3 C ATOM 1898 CG PRO C 135 -27.497 16.679 -4.766 1.00155.01 C ANISOU 1898 CG PRO C 135 13295 23887 21714 3739 -3626 295 C ATOM 1899 CD PRO C 135 -28.520 15.577 -4.677 1.00151.32 C ANISOU 1899 CD PRO C 135 13461 23151 20884 4120 -3341 705 C ATOM 1900 N GLY C 136 -30.027 19.144 -6.930 1.00139.73 N ANISOU 1900 N GLY C 136 12271 20674 20145 2221 -2900 209 N ATOM 1901 CA GLY C 136 -30.319 19.491 -8.317 1.00136.96 C ANISOU 1901 CA GLY C 136 12007 19994 20040 1826 -2434 367 C ATOM 1902 C GLY C 136 -31.778 19.878 -8.472 1.00131.94 C ANISOU 1902 C GLY C 136 11979 18987 19166 1666 -2304 435 C ATOM 1903 O GLY C 136 -32.519 19.942 -7.491 1.00130.73 O ANISOU 1903 O GLY C 136 12147 18822 18701 1822 -2567 337 O ATOM 1904 N ILE C 137 -32.183 20.156 -9.702 1.00119.19 N ANISOU 1904 N ILE C 137 10493 17125 17669 1381 -1900 604 N ATOM 1905 CA ILE C 137 -33.568 20.453 -10.006 1.00114.67 C ANISOU 1905 CA ILE C 137 10462 16238 16870 1262 -1747 686 C ATOM 1906 C ILE C 137 -34.514 19.421 -9.417 1.00111.55 C ANISOU 1906 C ILE C 137 10529 15810 16045 1643 -1758 746 C ATOM 1907 O ILE C 137 -34.350 18.235 -9.650 1.00111.38 O ANISOU 1907 O ILE C 137 10525 15856 15938 1942 -1568 876 O ATOM 1908 CB ILE C 137 -33.789 20.421 -11.512 1.00113.09 C ANISOU 1908 CB ILE C 137 10316 15929 16723 1089 -1266 910 C ATOM 1909 CG1 ILE C 137 -33.166 21.662 -12.161 1.00116.11 C ANISOU 1909 CG1 ILE C 137 10338 16249 17528 654 -1172 967 C ATOM 1910 CG2 ILE C 137 -35.307 20.282 -11.851 1.00108.31 C ANISOU 1910 CG2 ILE C 137 10287 15087 15780 1116 -1097 988 C ATOM 1911 CD1 ILE C 137 -33.381 21.721 -13.675 1.00115.41 C ANISOU 1911 CD1 ILE C 137 10292 16149 17410 525 -675 1255 C ATOM 1912 N ARG C 138 -35.526 19.864 -8.686 1.00108.05 N ANISOU 1912 N ARG C 138 10448 15235 15373 1632 -1944 659 N ATOM 1913 CA ARG C 138 -36.507 18.938 -8.139 1.00105.52 C ANISOU 1913 CA ARG C 138 10552 14862 14679 1956 -1896 767 C ATOM 1914 C ARG C 138 -37.679 18.835 -9.120 1.00101.40 C ANISOU 1914 C ARG C 138 10396 14055 14076 1811 -1541 871 C ATOM 1915 O ARG C 138 -38.384 19.822 -9.383 1.00 99.72 O ANISOU 1915 O ARG C 138 10347 13679 13863 1542 -1549 807 O ATOM 1916 CB ARG C 138 -36.982 19.377 -6.765 1.00106.20 C ANISOU 1916 CB ARG C 138 10801 15052 14497 2084 -2267 617 C ATOM 1917 CG ARG C 138 -35.924 20.053 -5.905 1.00110.81 C ANISOU 1917 CG ARG C 138 10973 15939 15192 2088 -2709 347 C ATOM 1918 CD ARG C 138 -34.753 19.165 -5.623 1.00114.35 C ANISOU 1918 CD ARG C 138 11061 16715 15672 2412 -2794 431 C ATOM 1919 NE ARG C 138 -33.926 19.681 -4.534 1.00119.24 N ANISOU 1919 NE ARG C 138 11315 17728 16263 2525 -3294 128 N ATOM 1920 CZ ARG C 138 -33.925 19.179 -3.301 1.00121.74 C ANISOU 1920 CZ ARG C 138 11681 18418 16155 2990 -3581 135 C ATOM 1921 NH1 ARG C 138 -34.699 18.129 -2.978 1.00119.86 N ANISOU 1921 NH1 ARG C 138 11852 18146 15545 3368 -3372 501 N ATOM 1922 NH2 ARG C 138 -33.140 19.716 -2.369 1.00126.84 N ANISOU 1922 NH2 ARG C 138 11941 19499 16752 3097 -4075 -223 N ATOM 1923 N TYR C 139 -37.854 17.638 -9.675 1.00 97.38 N ANISOU 1923 N TYR C 139 9981 13489 13528 2008 -1242 1001 N ATOM 1924 CA TYR C 139 -38.846 17.394 -10.699 1.00 94.38 C ANISOU 1924 CA TYR C 139 9862 12915 13083 1903 -918 1023 C ATOM 1925 C TYR C 139 -40.137 16.936 -10.047 1.00 92.10 C ANISOU 1925 C TYR C 139 9974 12451 12569 2037 -908 1045 C ATOM 1926 O TYR C 139 -40.096 16.209 -9.071 1.00 93.30 O ANISOU 1926 O TYR C 139 10185 12620 12644 2319 -992 1143 O ATOM 1927 CB TYR C 139 -38.316 16.345 -11.691 1.00 95.42 C ANISOU 1927 CB TYR C 139 9826 13084 13346 2039 -604 1045 C ATOM 1928 CG TYR C 139 -37.285 16.899 -12.637 1.00 97.47 C ANISOU 1928 CG TYR C 139 9708 13543 13783 1859 -501 1045 C ATOM 1929 CD1 TYR C 139 -37.669 17.693 -13.690 1.00 96.49 C ANISOU 1929 CD1 TYR C 139 9617 13430 13616 1591 -325 1066 C ATOM 1930 CD2 TYR C 139 -35.971 16.673 -12.460 1.00100.84 C ANISOU 1930 CD2 TYR C 139 9735 14170 14411 1969 -567 1062 C ATOM 1931 CE1 TYR C 139 -36.782 18.237 -14.534 1.00 98.94 C ANISOU 1931 CE1 TYR C 139 9585 13930 14078 1428 -178 1148 C ATOM 1932 CE2 TYR C 139 -35.062 17.212 -13.310 1.00103.15 C ANISOU 1932 CE2 TYR C 139 9651 14653 14888 1782 -433 1089 C ATOM 1933 CZ TYR C 139 -35.474 17.999 -14.357 1.00102.26 C ANISOU 1933 CZ TYR C 139 9591 14534 14729 1503 -216 1156 C ATOM 1934 OH TYR C 139 -34.574 18.568 -15.248 1.00105.26 O ANISOU 1934 OH TYR C 139 9583 15122 15291 1316 -15 1270 O ATOM 1935 N PRO C 140 -41.289 17.352 -10.581 1.00 93.11 N ANISOU 1935 N PRO C 140 10357 12434 12588 1856 -790 989 N ATOM 1936 CA PRO C 140 -42.526 17.084 -9.884 1.00 91.37 C ANISOU 1936 CA PRO C 140 10465 12074 12177 1945 -793 999 C ATOM 1937 C PRO C 140 -42.962 15.696 -10.117 1.00 91.32 C ANISOU 1937 C PRO C 140 10554 11905 12240 2124 -516 1046 C ATOM 1938 O PRO C 140 -42.728 15.198 -11.182 1.00 91.56 O ANISOU 1938 O PRO C 140 10469 11907 12410 2097 -301 963 O ATOM 1939 CB PRO C 140 -43.511 18.047 -10.529 1.00 88.99 C ANISOU 1939 CB PRO C 140 10329 11699 11785 1692 -762 900 C ATOM 1940 CG PRO C 140 -42.988 18.343 -11.838 1.00 89.36 C ANISOU 1940 CG PRO C 140 10189 11817 11947 1534 -609 891 C ATOM 1941 CD PRO C 140 -41.528 17.976 -11.885 1.00 92.03 C ANISOU 1941 CD PRO C 140 10196 12297 12476 1611 -616 945 C ATOM 1942 N LEU C 141 -43.587 15.085 -9.122 1.00 92.03 N ANISOU 1942 N LEU C 141 10831 11888 12247 2314 -506 1174 N ATOM 1943 CA LEU C 141 -43.948 13.681 -9.174 1.00 93.08 C ANISOU 1943 CA LEU C 141 11031 11770 12566 2493 -221 1266 C ATOM 1944 C LEU C 141 -45.294 13.498 -9.853 1.00 91.06 C ANISOU 1944 C LEU C 141 10945 11307 12349 2315 -1 1094 C ATOM 1945 O LEU C 141 -45.471 12.512 -10.571 1.00 91.94 O ANISOU 1945 O LEU C 141 11009 11204 12721 2337 255 976 O ATOM 1946 CB LEU C 141 -43.965 13.068 -7.772 1.00 95.41 C ANISOU 1946 CB LEU C 141 11422 12046 12783 2804 -260 1579 C ATOM 1947 CG LEU C 141 -42.662 13.165 -6.962 1.00 98.28 C ANISOU 1947 CG LEU C 141 11589 12698 13054 3061 -525 1738 C ATOM 1948 CD1 LEU C 141 -42.884 12.829 -5.507 1.00100.78 C ANISOU 1948 CD1 LEU C 141 12037 13133 13121 3393 -606 2059 C ATOM 1949 CD2 LEU C 141 -41.588 12.237 -7.529 1.00100.65 C ANISOU 1949 CD2 LEU C 141 11648 12922 13674 3234 -394 1782 C ATOM 1950 N THR C 142 -46.226 14.445 -9.644 1.00100.84 N ANISOU 1950 N THR C 142 12346 12615 13352 2152 -114 1030 N ATOM 1951 CA THR C 142 -47.632 14.341 -10.165 1.00 99.24 C ANISOU 1951 CA THR C 142 12280 12270 13156 2001 58 858 C ATOM 1952 C THR C 142 -47.767 14.772 -11.628 1.00 97.98 C ANISOU 1952 C THR C 142 12032 12214 12983 1812 102 584 C ATOM 1953 O THR C 142 -47.799 15.986 -11.933 1.00 96.60 O ANISOU 1953 O THR C 142 11874 12220 12611 1680 -62 557 O ATOM 1954 CB THR C 142 -48.640 15.206 -9.346 1.00 97.82 C ANISOU 1954 CB THR C 142 12293 12163 12712 1949 -77 894 C ATOM 1955 OG1 THR C 142 -48.971 14.555 -8.112 1.00 99.50 O ANISOU 1955 OG1 THR C 142 12610 12295 12900 2144 0 1142 O ATOM 1956 CG2 THR C 142 -49.921 15.414 -10.127 1.00 96.16 C ANISOU 1956 CG2 THR C 142 12147 11905 12485 1772 32 662 C ATOM 1957 N PHE C 143 -47.866 13.786 -12.526 1.00 89.90 N ANISOU 1957 N PHE C 143 10907 11081 12172 1825 330 380 N ATOM 1958 CA PHE C 143 -47.754 14.084 -13.953 1.00 89.79 C ANISOU 1958 CA PHE C 143 10762 11285 12069 1732 376 128 C ATOM 1959 C PHE C 143 -48.888 15.033 -14.299 1.00 87.89 C ANISOU 1959 C PHE C 143 10639 11185 11571 1587 290 32 C ATOM 1960 O PHE C 143 -50.080 14.681 -14.107 1.00 87.55 O ANISOU 1960 O PHE C 143 10683 11010 11572 1551 356 -107 O ATOM 1961 CB PHE C 143 -47.827 12.796 -14.774 1.00 92.00 C ANISOU 1961 CB PHE C 143 10905 11440 12610 1802 617 -185 C ATOM 1962 CG PHE C 143 -47.548 12.956 -16.253 1.00 92.93 C ANISOU 1962 CG PHE C 143 10850 11890 12569 1789 679 -470 C ATOM 1963 CD1 PHE C 143 -46.576 13.789 -16.712 1.00 92.93 C ANISOU 1963 CD1 PHE C 143 10744 12204 12360 1784 612 -303 C ATOM 1964 CD2 PHE C 143 -48.234 12.215 -17.172 1.00 94.59 C ANISOU 1964 CD2 PHE C 143 10968 12118 12854 1796 822 -917 C ATOM 1965 CE1 PHE C 143 -46.304 13.875 -18.066 1.00 94.56 C ANISOU 1965 CE1 PHE C 143 10780 12777 12374 1819 721 -506 C ATOM 1966 CE2 PHE C 143 -47.965 12.324 -18.491 1.00 96.16 C ANISOU 1966 CE2 PHE C 143 10998 12715 12824 1847 876 -1189 C ATOM 1967 CZ PHE C 143 -46.992 13.146 -18.940 1.00 96.17 C ANISOU 1967 CZ PHE C 143 10915 13066 12558 1875 844 -948 C ATOM 1968 N GLY C 144 -48.520 16.235 -14.761 1.00 79.09 N ANISOU 1968 N GLY C 144 9504 10311 10235 1512 159 134 N ATOM 1969 CA GLY C 144 -49.517 17.251 -15.139 1.00 77.83 C ANISOU 1969 CA GLY C 144 9452 10283 9838 1423 70 102 C ATOM 1970 C GLY C 144 -49.287 18.570 -14.435 1.00 76.92 C ANISOU 1970 C GLY C 144 9437 10140 9651 1355 -145 345 C ATOM 1971 O GLY C 144 -49.621 19.635 -14.919 1.00 76.73 O ANISOU 1971 O GLY C 144 9452 10215 9487 1297 -217 411 O ATOM 1972 N TRP C 145 -48.735 18.489 -13.248 1.00 84.13 N ANISOU 1972 N TRP C 145 10380 10910 10675 1390 -256 465 N ATOM 1973 CA TRP C 145 -48.174 19.665 -12.648 1.00 84.33 C ANISOU 1973 CA TRP C 145 10415 10925 10703 1324 -480 604 C ATOM 1974 C TRP C 145 -46.974 19.979 -13.529 1.00 85.87 C ANISOU 1974 C TRP C 145 10387 11239 11000 1248 -429 710 C ATOM 1975 O TRP C 145 -46.174 19.093 -13.769 1.00 86.91 O ANISOU 1975 O TRP C 145 10361 11433 11229 1319 -312 704 O ATOM 1976 CB TRP C 145 -47.750 19.365 -11.208 1.00 84.91 C ANISOU 1976 CB TRP C 145 10516 10930 10815 1432 -625 656 C ATOM 1977 CG TRP C 145 -47.161 20.510 -10.495 1.00 85.87 C ANISOU 1977 CG TRP C 145 10602 11061 10961 1375 -900 675 C ATOM 1978 CD1 TRP C 145 -45.940 20.572 -9.920 1.00 87.80 C ANISOU 1978 CD1 TRP C 145 10667 11373 11320 1404 -1059 709 C ATOM 1979 CD2 TRP C 145 -47.771 21.763 -10.284 1.00 85.58 C ANISOU 1979 CD2 TRP C 145 10680 10954 10883 1284 -1063 604 C ATOM 1980 NE1 TRP C 145 -45.760 21.790 -9.335 1.00 88.90 N ANISOU 1980 NE1 TRP C 145 10789 11484 11506 1312 -1326 614 N ATOM 1981 CE2 TRP C 145 -46.876 22.541 -9.562 1.00 87.56 C ANISOU 1981 CE2 TRP C 145 10812 11197 11261 1239 -1319 555 C ATOM 1982 CE3 TRP C 145 -49.001 22.297 -10.622 1.00 84.29 C ANISOU 1982 CE3 TRP C 145 10686 10731 10609 1256 -1027 549 C ATOM 1983 CZ2 TRP C 145 -47.160 23.818 -9.192 1.00 88.42 C ANISOU 1983 CZ2 TRP C 145 10976 11181 11439 1152 -1525 429 C ATOM 1984 CZ3 TRP C 145 -49.288 23.568 -10.259 1.00 84.94 C ANISOU 1984 CZ3 TRP C 145 10838 10703 10731 1202 -1221 480 C ATOM 1985 CH2 TRP C 145 -48.384 24.318 -9.545 1.00 87.03 C ANISOU 1985 CH2 TRP C 145 10997 10903 11169 1145 -1462 408 C ATOM 1986 N CYS C 146 -46.850 21.208 -14.020 1.00 88.43 N ANISOU 1986 N CYS C 146 10682 11581 11335 1117 -486 829 N ATOM 1987 CA CYS C 146 -45.760 21.536 -14.927 1.00 90.55 C ANISOU 1987 CA CYS C 146 10712 11980 11712 1033 -370 995 C ATOM 1988 C CYS C 146 -44.786 22.542 -14.360 1.00 92.42 C ANISOU 1988 C CYS C 146 10802 12085 12227 876 -542 1118 C ATOM 1989 O CYS C 146 -44.283 23.422 -15.079 1.00 94.54 O ANISOU 1989 O CYS C 146 10926 12356 12639 732 -458 1327 O ATOM 1990 CB CYS C 146 -46.314 22.033 -16.224 1.00 91.13 C ANISOU 1990 CB CYS C 146 10807 12217 11601 1023 -205 1107 C ATOM 1991 SG CYS C 146 -47.146 20.771 -17.011 1.00 90.27 S ANISOU 1991 SG CYS C 146 10739 12340 11218 1196 -24 850 S ATOM 1992 N PHE C 147 -44.496 22.397 -13.071 1.00 89.18 N ANISOU 1992 N PHE C 147 10397 11579 11906 914 -774 988 N ATOM 1993 CA PHE C 147 -43.565 23.291 -12.405 1.00 91.58 C ANISOU 1993 CA PHE C 147 10513 11785 12498 772 -999 977 C ATOM 1994 C PHE C 147 -42.486 22.441 -11.775 1.00 92.86 C ANISOU 1994 C PHE C 147 10455 12099 12731 884 -1082 915 C ATOM 1995 O PHE C 147 -42.770 21.434 -11.125 1.00 91.70 O ANISOU 1995 O PHE C 147 10426 12020 12396 1106 -1106 847 O ATOM 1996 CB PHE C 147 -44.297 24.129 -11.355 1.00 91.26 C ANISOU 1996 CB PHE C 147 10668 11560 12447 761 -1276 803 C ATOM 1997 CG PHE C 147 -44.848 25.398 -11.881 1.00 91.92 C ANISOU 1997 CG PHE C 147 10836 11416 12672 603 -1263 885 C ATOM 1998 CD1 PHE C 147 -44.026 26.323 -12.470 1.00 94.98 C ANISOU 1998 CD1 PHE C 147 10993 11658 13438 377 -1211 1055 C ATOM 1999 CD2 PHE C 147 -46.181 25.686 -11.767 1.00 90.07 C ANISOU 1999 CD2 PHE C 147 10891 11094 12237 692 -1285 820 C ATOM 2000 CE1 PHE C 147 -44.519 27.501 -12.953 1.00 96.35 C ANISOU 2000 CE1 PHE C 147 11248 11562 13799 258 -1169 1204 C ATOM 2001 CE2 PHE C 147 -46.686 26.886 -12.251 1.00 91.23 C ANISOU 2001 CE2 PHE C 147 11114 11007 12541 594 -1276 928 C ATOM 2002 CZ PHE C 147 -45.851 27.783 -12.851 1.00 94.45 C ANISOU 2002 CZ PHE C 147 11316 11231 13338 387 -1212 1143 C ATOM 2003 N LYS C 148 -41.249 22.832 -12.001 1.00110.47 N ANISOU 2003 N LYS C 148 12339 14378 15254 743 -1099 973 N ATOM 2004 CA LYS C 148 -40.135 22.162 -11.364 1.00112.42 C ANISOU 2004 CA LYS C 148 12317 14804 15596 866 -1225 900 C ATOM 2005 C LYS C 148 -39.494 23.139 -10.396 1.00115.38 C ANISOU 2005 C LYS C 148 12481 15133 16225 732 -1585 712 C ATOM 2006 O LYS C 148 -39.691 24.350 -10.518 1.00116.44 O ANISOU 2006 O LYS C 148 12613 15039 16589 483 -1653 676 O ATOM 2007 CB LYS C 148 -39.136 21.662 -12.419 1.00114.13 C ANISOU 2007 CB LYS C 148 12217 15193 15956 846 -949 1054 C ATOM 2008 CG LYS C 148 -38.684 22.690 -13.461 1.00116.36 C ANISOU 2008 CG LYS C 148 12279 15435 16498 551 -761 1244 C ATOM 2009 CD LYS C 148 -37.676 22.072 -14.426 1.00118.51 C ANISOU 2009 CD LYS C 148 12214 15973 16842 590 -464 1385 C ATOM 2010 CE LYS C 148 -37.200 23.094 -15.449 1.00121.56 C ANISOU 2010 CE LYS C 148 12355 16358 17472 312 -218 1664 C ATOM 2011 NZ LYS C 148 -36.115 22.550 -16.321 1.00124.45 N ANISOU 2011 NZ LYS C 148 12331 17051 17903 359 85 1796 N ATOM 2012 N LEU C 149 -38.750 22.624 -9.425 1.00106.71 N ANISOU 2012 N LEU C 149 11196 14248 15102 919 -1829 571 N ATOM 2013 CA LEU C 149 -38.039 23.491 -8.490 1.00110.44 C ANISOU 2013 CA LEU C 149 11392 14763 15809 815 -2220 290 C ATOM 2014 C LEU C 149 -36.613 23.552 -8.972 1.00114.09 C ANISOU 2014 C LEU C 149 11335 15344 16668 662 -2178 326 C ATOM 2015 O LEU C 149 -35.926 22.537 -8.984 1.00114.77 O ANISOU 2015 O LEU C 149 11244 15693 16672 889 -2119 411 O ATOM 2016 CB LEU C 149 -38.132 22.963 -7.054 1.00111.21 C ANISOU 2016 CB LEU C 149 11571 15128 15555 1167 -2555 94 C ATOM 2017 CG LEU C 149 -39.568 22.607 -6.670 1.00107.62 C ANISOU 2017 CG LEU C 149 11616 14604 14670 1363 -2481 154 C ATOM 2018 CD1 LEU C 149 -39.670 21.990 -5.316 1.00108.93 C ANISOU 2018 CD1 LEU C 149 11868 15085 14438 1754 -2725 80 C ATOM 2019 CD2 LEU C 149 -40.446 23.831 -6.737 1.00106.74 C ANISOU 2019 CD2 LEU C 149 11701 14209 14646 1127 -2541 -6 C ATOM 2020 N VAL C 150 -36.181 24.728 -9.415 1.00123.56 N ANISOU 2020 N VAL C 150 12278 16325 18344 279 -2169 292 N ATOM 2021 CA VAL C 150 -34.827 24.897 -9.956 1.00127.69 C ANISOU 2021 CA VAL C 150 12250 16944 19323 72 -2070 358 C ATOM 2022 C VAL C 150 -33.934 25.590 -8.950 1.00132.77 C ANISOU 2022 C VAL C 150 12456 17647 20345 -60 -2513 -55 C ATOM 2023 O VAL C 150 -34.304 26.624 -8.407 1.00134.25 O ANISOU 2023 O VAL C 150 12695 17572 20743 -248 -2762 -334 O ATOM 2024 CB VAL C 150 -34.816 25.745 -11.253 1.00128.71 C ANISOU 2024 CB VAL C 150 12296 16789 19820 -296 -1680 680 C ATOM 2025 CG1 VAL C 150 -33.571 26.633 -11.321 1.00134.80 C ANISOU 2025 CG1 VAL C 150 12461 17473 21284 -666 -1727 609 C ATOM 2026 CG2 VAL C 150 -34.912 24.855 -12.483 1.00126.40 C ANISOU 2026 CG2 VAL C 150 12100 16685 19242 -152 -1213 1056 C ATOM 2027 N PRO C 151 -32.748 25.033 -8.704 1.00134.20 N ANISOU 2027 N PRO C 151 12173 18184 20635 52 -2629 -143 N ATOM 2028 CA PRO C 151 -31.776 25.740 -7.909 1.00140.05 C ANISOU 2028 CA PRO C 151 12381 19022 21810 -118 -3043 -575 C ATOM 2029 C PRO C 151 -31.037 26.738 -8.790 1.00144.18 C ANISOU 2029 C PRO C 151 12445 19246 23092 -643 -2808 -477 C ATOM 2030 O PRO C 151 -30.690 26.403 -9.932 1.00143.74 O ANISOU 2030 O PRO C 151 12275 19212 23128 -723 -2344 -50 O ATOM 2031 CB PRO C 151 -30.838 24.630 -7.458 1.00141.88 C ANISOU 2031 CB PRO C 151 12292 19789 21829 259 -3198 -619 C ATOM 2032 CG PRO C 151 -30.852 23.664 -8.566 1.00138.73 C ANISOU 2032 CG PRO C 151 12023 19429 21261 393 -2695 -146 C ATOM 2033 CD PRO C 151 -32.222 23.753 -9.199 1.00133.27 C ANISOU 2033 CD PRO C 151 11953 18386 20297 340 -2383 116 C ATOM 2034 N VAL C 152 -30.811 27.946 -8.270 1.00157.34 N ANISOU 2034 N VAL C 152 13839 20632 25310 -988 -3102 -872 N ATOM 2035 CA VAL C 152 -30.019 28.968 -8.960 1.00162.79 C ANISOU 2035 CA VAL C 152 14009 20973 26869 -1528 -2894 -798 C ATOM 2036 C VAL C 152 -28.782 29.229 -8.149 1.00169.63 C ANISOU 2036 C VAL C 152 14156 22080 28215 -1655 -3328 -1345 C ATOM 2037 O VAL C 152 -28.552 28.568 -7.140 1.00169.87 O ANISOU 2037 O VAL C 152 14121 22605 27815 -1271 -3770 -1722 O ATOM 2038 CB VAL C 152 -30.796 30.275 -9.078 1.00163.66 C ANISOU 2038 CB VAL C 152 14352 20420 27411 -1879 -2855 -831 C ATOM 2039 CG1 VAL C 152 -32.235 30.003 -9.653 1.00156.65 C ANISOU 2039 CG1 VAL C 152 14233 19370 25917 -1657 -2548 -395 C ATOM 2040 CG2 VAL C 152 -30.853 30.972 -7.720 1.00167.17 C ANISOU 2040 CG2 VAL C 152 14684 20779 28052 -1908 -3479 -1601 C ATOM 2041 N GLU C 153 -27.971 30.187 -8.581 1.00278.57 N ANISOU 2041 N GLU C 153 27377 35549 42918 -2181 -3200 -1379 N ATOM 2042 CA GLU C 153 -26.882 30.696 -7.721 1.00286.29 C ANISOU 2042 CA GLU C 153 27610 36661 44506 -2395 -3687 -2054 C ATOM 2043 C GLU C 153 -27.521 31.541 -6.605 1.00287.94 C ANISOU 2043 C GLU C 153 28000 36607 44798 -2430 -4227 -2739 C ATOM 2044 O GLU C 153 -28.666 32.016 -6.741 1.00284.32 O ANISOU 2044 O GLU C 153 28132 35689 44209 -2453 -4103 -2598 O ATOM 2045 CB GLU C 153 -25.835 31.517 -8.506 1.00293.40 C ANISOU 2045 CB GLU C 153 27784 37222 46473 -3005 -3359 -1905 C ATOM 2046 N PRO C 154 -26.799 31.720 -5.494 1.00248.28 N ANISOU 2046 N PRO C 154 22454 31925 39956 -2394 -4843 -3519 N ATOM 2047 CA PRO C 154 -27.397 32.409 -4.351 1.00250.25 C ANISOU 2047 CA PRO C 154 22868 32068 40148 -2328 -5400 -4264 C ATOM 2048 C PRO C 154 -27.282 33.939 -4.422 1.00256.94 C ANISOU 2048 C PRO C 154 23373 32118 42135 -2966 -5443 -4678 C ATOM 2049 O PRO C 154 -28.274 34.650 -4.203 1.00255.75 O ANISOU 2049 O PRO C 154 23674 31473 42024 -3012 -5498 -4848 O ATOM 2050 CB PRO C 154 -26.576 31.877 -3.179 1.00254.64 C ANISOU 2050 CB PRO C 154 22944 33446 40362 -1964 -6047 -4929 C ATOM 2051 CG PRO C 154 -25.161 31.640 -3.782 1.00259.34 C ANISOU 2051 CG PRO C 154 22746 34240 41552 -2222 -5872 -4770 C ATOM 2052 CD PRO C 154 -25.392 31.327 -5.255 1.00254.03 C ANISOU 2052 CD PRO C 154 22376 33196 40950 -2394 -5065 -3790 C ATOM 2053 N GLU C 155 -26.084 34.409 -4.775 1.00235.91 N ANISOU 2053 N GLU C 155 19903 29300 40431 -3451 -5374 -4797 N ATOM 2054 CA GLU C 155 -25.603 35.753 -4.463 1.00245.19 C ANISOU 2054 CA GLU C 155 20482 29875 42804 -4035 -5620 -5483 C ATOM 2055 C GLU C 155 -24.831 35.694 -3.143 1.00251.71 C ANISOU 2055 C GLU C 155 20696 31354 43589 -3863 -6431 -6561 C ATOM 2056 O GLU C 155 -24.645 34.616 -2.564 1.00249.00 O ANISOU 2056 O GLU C 155 20403 31913 42292 -3285 -6735 -6635 O ATOM 2057 CB GLU C 155 -26.746 36.769 -4.378 1.00244.53 C ANISOU 2057 CB GLU C 155 20926 28987 42998 -4191 -5597 -5618 C ATOM 2058 N GLU C 181 -25.026 26.582 4.396 1.00196.76 N ANISOU 2058 N GLU C 181 15129 32319 27312 2678 -9455 -6656 N ATOM 2059 CA GLU C 181 -24.930 26.490 2.940 1.00191.12 C ANISOU 2059 CA GLU C 181 14492 30798 27327 2132 -8762 -6017 C ATOM 2060 C GLU C 181 -25.883 25.431 2.365 1.00181.87 C ANISOU 2060 C GLU C 181 14156 29357 25591 2428 -8136 -5022 C ATOM 2061 O GLU C 181 -25.836 24.264 2.758 1.00181.18 O ANISOU 2061 O GLU C 181 14241 29801 24799 3087 -8137 -4573 O ATOM 2062 CB GLU C 181 -23.484 26.174 2.533 1.00195.99 C ANISOU 2062 CB GLU C 181 14293 31702 28473 2044 -8812 -6026 C ATOM 2063 N LYS C 182 -26.755 25.842 1.448 1.00185.53 N ANISOU 2063 N LYS C 182 15115 28988 26390 1956 -7611 -4688 N ATOM 2064 CA LYS C 182 -27.613 24.892 0.728 1.00177.18 C ANISOU 2064 CA LYS C 182 14762 27612 24946 2137 -6994 -3816 C ATOM 2065 C LYS C 182 -28.264 25.520 -0.498 1.00171.76 C ANISOU 2065 C LYS C 182 14393 26041 24826 1512 -6443 -3535 C ATOM 2066 O LYS C 182 -28.314 26.752 -0.641 1.00173.94 O ANISOU 2066 O LYS C 182 14496 25885 25709 986 -6534 -3971 O ATOM 2067 CB LYS C 182 -28.724 24.317 1.628 1.00174.36 C ANISOU 2067 CB LYS C 182 15064 27553 23633 2720 -7072 -3631 C ATOM 2068 CG LYS C 182 -29.080 22.858 1.296 1.00169.35 C ANISOU 2068 CG LYS C 182 14878 26963 22504 3179 -6624 -2784 C ATOM 2069 CD LYS C 182 -30.526 22.507 1.606 1.00164.17 C ANISOU 2069 CD LYS C 182 14997 26155 21224 3433 -6393 -2439 C ATOM 2070 CE LYS C 182 -30.748 20.987 1.601 1.00161.64 C ANISOU 2070 CE LYS C 182 15015 25987 20414 3989 -6062 -1689 C ATOM 2071 NZ LYS C 182 -31.983 20.567 2.344 1.00159.42 N ANISOU 2071 NZ LYS C 182 15348 25808 19417 4386 -5972 -1412 N ATOM 2072 N GLU C 183 -28.769 24.652 -1.375 1.00178.66 N ANISOU 2072 N GLU C 183 15724 26654 25504 1603 -5876 -2808 N ATOM 2073 CA GLU C 183 -29.505 25.073 -2.544 1.00173.32 C ANISOU 2073 CA GLU C 183 15418 25262 25176 1144 -5341 -2458 C ATOM 2074 C GLU C 183 -30.655 25.935 -2.071 1.00171.68 C ANISOU 2074 C GLU C 183 15651 24752 24830 1027 -5476 -2740 C ATOM 2075 O GLU C 183 -31.363 25.539 -1.147 1.00170.57 O ANISOU 2075 O GLU C 183 15881 24924 24003 1471 -5683 -2800 O ATOM 2076 CB GLU C 183 -30.016 23.847 -3.317 1.00167.11 C ANISOU 2076 CB GLU C 183 15096 24386 24011 1407 -4811 -1748 C ATOM 2077 CG GLU C 183 -28.901 23.094 -4.075 1.00168.61 C ANISOU 2077 CG GLU C 183 14849 24748 24467 1450 -4566 -1461 C ATOM 2078 CD GLU C 183 -29.398 21.990 -5.023 1.00163.04 C ANISOU 2078 CD GLU C 183 14566 23861 23522 1635 -4005 -854 C ATOM 2079 OE1 GLU C 183 -30.587 21.596 -4.947 1.00158.16 O ANISOU 2079 OE1 GLU C 183 14572 23055 22466 1810 -3843 -632 O ATOM 2080 OE2 GLU C 183 -28.577 21.505 -5.841 1.00164.11 O ANISOU 2080 OE2 GLU C 183 14366 24060 23930 1610 -3728 -643 O ATOM 2081 N VAL C 184 -30.784 27.141 -2.633 1.00165.18 N ANISOU 2081 N VAL C 184 14737 23347 24678 458 -5373 -2925 N ATOM 2082 CA VAL C 184 -32.065 27.850 -2.615 1.00161.95 C ANISOU 2082 CA VAL C 184 14863 22479 24191 329 -5292 -2977 C ATOM 2083 C VAL C 184 -32.813 27.505 -3.902 1.00155.34 C ANISOU 2083 C VAL C 184 14486 21203 23334 196 -4655 -2273 C ATOM 2084 O VAL C 184 -32.204 27.411 -4.980 1.00155.27 O ANISOU 2084 O VAL C 184 14236 21019 23740 -68 -4290 -1914 O ATOM 2085 CB VAL C 184 -31.907 29.380 -2.504 1.00167.04 C ANISOU 2085 CB VAL C 184 15201 22658 25609 -173 -5521 -3551 C ATOM 2086 CG1 VAL C 184 -31.783 30.028 -3.898 1.00166.37 C ANISOU 2086 CG1 VAL C 184 15027 21879 26307 -739 -5009 -3132 C ATOM 2087 CG2 VAL C 184 -33.081 29.986 -1.731 1.00166.18 C ANISOU 2087 CG2 VAL C 184 15541 22411 25187 -40 -5751 -3928 C ATOM 2088 N LEU C 185 -34.128 27.321 -3.786 1.00132.57 N ANISOU 2088 N LEU C 185 12226 18195 19949 396 -4527 -2102 N ATOM 2089 CA LEU C 185 -34.931 26.857 -4.917 1.00126.51 C ANISOU 2089 CA LEU C 185 11898 17125 19044 355 -3979 -1498 C ATOM 2090 C LEU C 185 -35.949 27.894 -5.412 1.00124.66 C ANISOU 2090 C LEU C 185 11990 16323 19049 59 -3809 -1468 C ATOM 2091 O LEU C 185 -36.431 28.737 -4.652 1.00126.53 O ANISOU 2091 O LEU C 185 12315 16422 19338 31 -4113 -1904 O ATOM 2092 CB LEU C 185 -35.623 25.535 -4.573 1.00122.17 C ANISOU 2092 CB LEU C 185 11775 16904 17741 854 -3874 -1208 C ATOM 2093 CG LEU C 185 -34.663 24.391 -4.250 1.00123.95 C ANISOU 2093 CG LEU C 185 11721 17622 17755 1199 -3952 -1095 C ATOM 2094 CD1 LEU C 185 -35.448 23.155 -3.877 1.00120.40 C ANISOU 2094 CD1 LEU C 185 11717 17370 16659 1673 -3809 -771 C ATOM 2095 CD2 LEU C 185 -33.736 24.117 -5.415 1.00124.40 C ANISOU 2095 CD2 LEU C 185 11432 17594 18242 980 -3628 -814 C ATOM 2096 N VAL C 186 -36.241 27.815 -6.708 1.00143.58 N ANISOU 2096 N VAL C 186 14543 18430 21580 -122 -3325 -963 N ATOM 2097 CA VAL C 186 -37.177 28.706 -7.356 1.00142.02 C ANISOU 2097 CA VAL C 186 14646 17729 21586 -349 -3107 -807 C ATOM 2098 C VAL C 186 -38.137 27.928 -8.234 1.00136.24 C ANISOU 2098 C VAL C 186 14361 17016 20389 -176 -2695 -322 C ATOM 2099 O VAL C 186 -37.723 27.075 -9.019 1.00134.81 O ANISOU 2099 O VAL C 186 14099 17029 20093 -119 -2400 15 O ATOM 2100 CB VAL C 186 -36.455 29.778 -8.191 1.00146.36 C ANISOU 2100 CB VAL C 186 14817 17850 22945 -828 -2930 -684 C ATOM 2101 CG1 VAL C 186 -35.790 30.742 -7.272 1.00152.50 C ANISOU 2101 CG1 VAL C 186 15190 18474 24277 -1045 -3367 -1281 C ATOM 2102 CG2 VAL C 186 -35.403 29.183 -9.133 1.00147.31 C ANISOU 2102 CG2 VAL C 186 14572 18173 23225 -929 -2601 -297 C ATOM 2103 N TRP C 187 -39.428 28.201 -8.052 1.00122.58 N ANISOU 2103 N TRP C 187 13073 15114 18388 -71 -2699 -353 N ATOM 2104 CA TRP C 187 -40.489 27.619 -8.871 1.00117.70 C ANISOU 2104 CA TRP C 187 12856 14488 17375 67 -2349 22 C ATOM 2105 C TRP C 187 -40.236 28.026 -10.314 1.00118.39 C ANISOU 2105 C TRP C 187 12831 14368 17782 -186 -1965 442 C ATOM 2106 O TRP C 187 -39.837 29.146 -10.587 1.00122.11 O ANISOU 2106 O TRP C 187 13097 14500 18798 -481 -1958 471 O ATOM 2107 CB TRP C 187 -41.857 28.132 -8.416 1.00115.80 C ANISOU 2107 CB TRP C 187 13016 14064 16919 172 -2449 -131 C ATOM 2108 CG TRP C 187 -42.617 27.251 -7.488 1.00113.06 C ANISOU 2108 CG TRP C 187 12946 14022 15991 523 -2568 -275 C ATOM 2109 CD1 TRP C 187 -43.242 26.112 -7.812 1.00109.27 C ANISOU 2109 CD1 TRP C 187 12696 13727 15094 729 -2322 -28 C ATOM 2110 CD2 TRP C 187 -42.902 27.479 -6.111 1.00114.58 C ANISOU 2110 CD2 TRP C 187 13204 14359 15972 712 -2926 -686 C ATOM 2111 NE1 TRP C 187 -43.887 25.578 -6.725 1.00108.32 N ANISOU 2111 NE1 TRP C 187 12779 13824 14554 1017 -2464 -182 N ATOM 2112 CE2 TRP C 187 -43.693 26.406 -5.665 1.00111.51 C ANISOU 2112 CE2 TRP C 187 13095 14256 15019 1036 -2833 -572 C ATOM 2113 CE3 TRP C 187 -42.559 28.475 -5.210 1.00118.84 C ANISOU 2113 CE3 TRP C 187 13570 14832 16751 649 -3311 -1168 C ATOM 2114 CZ2 TRP C 187 -44.147 26.295 -4.369 1.00112.53 C ANISOU 2114 CZ2 TRP C 187 13348 14655 14754 1321 -3074 -837 C ATOM 2115 CZ3 TRP C 187 -43.019 28.367 -3.907 1.00119.80 C ANISOU 2115 CZ3 TRP C 187 13816 15264 16437 956 -3598 -1524 C ATOM 2116 CH2 TRP C 187 -43.805 27.281 -3.501 1.00116.63 C ANISOU 2116 CH2 TRP C 187 13708 15196 15410 1301 -3461 -1315 C ATOM 2117 N ARG C 188 -40.429 27.098 -11.234 1.00131.06 N ANISOU 2117 N ARG C 188 14543 16190 19063 -56 -1633 765 N ATOM 2118 CA ARG C 188 -40.165 27.372 -12.637 1.00132.22 C ANISOU 2118 CA ARG C 188 14571 16287 19380 -218 -1246 1183 C ATOM 2119 C ARG C 188 -40.984 26.476 -13.563 1.00128.53 C ANISOU 2119 C ARG C 188 14377 16055 18404 3 -945 1407 C ATOM 2120 O ARG C 188 -41.094 25.249 -13.356 1.00125.98 O ANISOU 2120 O ARG C 188 14137 15995 17736 236 -937 1292 O ATOM 2121 CB ARG C 188 -38.678 27.223 -12.957 1.00135.84 C ANISOU 2121 CB ARG C 188 14537 16897 20182 -374 -1144 1277 C ATOM 2122 CG ARG C 188 -38.291 27.920 -14.254 1.00138.95 C ANISOU 2122 CG ARG C 188 14734 17180 20881 -607 -752 1734 C ATOM 2123 CD ARG C 188 -36.820 27.721 -14.608 1.00142.89 C ANISOU 2123 CD ARG C 188 14699 17877 21715 -757 -599 1843 C ATOM 2124 NE ARG C 188 -35.913 28.668 -13.955 1.00147.89 N ANISOU 2124 NE ARG C 188 14920 18228 23042 -1086 -820 1653 N ATOM 2125 CZ ARG C 188 -34.578 28.569 -13.990 1.00151.99 C ANISOU 2125 CZ ARG C 188 14895 18909 23944 -1245 -781 1634 C ATOM 2126 NH1 ARG C 188 -33.995 27.561 -14.652 1.00151.50 N ANISOU 2126 NH1 ARG C 188 14661 19292 23610 -1072 -513 1819 N ATOM 2127 NH2 ARG C 188 -33.812 29.476 -13.365 1.00157.10 N ANISOU 2127 NH2 ARG C 188 15131 19278 25283 -1573 -1015 1383 N ATOM 2128 N PHE C 189 -41.550 27.110 -14.588 1.00112.94 N ANISOU 2128 N PHE C 189 12519 13976 16416 -58 -700 1721 N ATOM 2129 CA PHE C 189 -42.488 26.469 -15.483 1.00110.19 C ANISOU 2129 CA PHE C 189 12420 13867 15579 154 -469 1859 C ATOM 2130 C PHE C 189 -41.748 25.784 -16.588 1.00111.50 C ANISOU 2130 C PHE C 189 12354 14394 15618 201 -139 2075 C ATOM 2131 O PHE C 189 -40.749 26.313 -17.074 1.00115.29 O ANISOU 2131 O PHE C 189 12517 14871 16415 21 27 2334 O ATOM 2132 CB PHE C 189 -43.410 27.484 -16.125 1.00110.91 C ANISOU 2132 CB PHE C 189 12711 13775 15654 135 -370 2117 C ATOM 2133 CG PHE C 189 -44.493 26.861 -16.943 1.00108.43 C ANISOU 2133 CG PHE C 189 12633 13761 14804 381 -210 2165 C ATOM 2134 CD1 PHE C 189 -44.296 26.564 -18.279 1.00110.01 C ANISOU 2134 CD1 PHE C 189 12721 14326 14750 471 116 2449 C ATOM 2135 CD2 PHE C 189 -45.706 26.555 -16.373 1.00105.10 C ANISOU 2135 CD2 PHE C 189 12506 13307 14121 533 -385 1891 C ATOM 2136 CE1 PHE C 189 -45.291 25.990 -19.032 1.00108.43 C ANISOU 2136 CE1 PHE C 189 12692 14458 14049 711 218 2397 C ATOM 2137 CE2 PHE C 189 -46.705 25.980 -17.133 1.00103.43 C ANISOU 2137 CE2 PHE C 189 12448 13382 13470 737 -258 1872 C ATOM 2138 CZ PHE C 189 -46.491 25.707 -18.469 1.00105.19 C ANISOU 2138 CZ PHE C 189 12547 13972 13446 826 22 2097 C ATOM 2139 N ASP C 190 -42.257 24.623 -16.996 1.00118.30 N ANISOU 2139 N ASP C 190 13346 15555 16045 440 -29 1948 N ATOM 2140 CA ASP C 190 -41.711 23.915 -18.129 1.00119.79 C ANISOU 2140 CA ASP C 190 13339 16137 16040 547 289 2069 C ATOM 2141 C ASP C 190 -42.795 23.145 -18.859 1.00117.75 C ANISOU 2141 C ASP C 190 13303 16142 15294 787 408 1932 C ATOM 2142 O ASP C 190 -43.287 22.141 -18.354 1.00115.09 O ANISOU 2142 O ASP C 190 13104 15789 14834 923 303 1601 O ATOM 2143 CB ASP C 190 -40.603 22.980 -17.680 1.00120.33 C ANISOU 2143 CB ASP C 190 13145 16317 16260 590 264 1890 C ATOM 2144 CG ASP C 190 -39.776 22.472 -18.835 1.00123.12 C ANISOU 2144 CG ASP C 190 13203 17065 16512 672 609 2025 C ATOM 2145 OD1 ASP C 190 -40.354 22.271 -19.926 1.00123.39 O ANISOU 2145 OD1 ASP C 190 13327 17386 16169 817 841 2090 O ATOM 2146 OD2 ASP C 190 -38.554 22.273 -18.654 1.00125.47 O ANISOU 2146 OD2 ASP C 190 13155 17438 17081 619 641 2040 O ATOM 2147 N SER C 191 -43.150 23.632 -20.052 1.00120.64 N ANISOU 2147 N SER C 191 13675 16761 15403 848 634 2198 N ATOM 2148 CA SER C 191 -44.143 23.002 -20.924 1.00119.89 C ANISOU 2148 CA SER C 191 13720 17024 14810 1092 737 2033 C ATOM 2149 C SER C 191 -43.769 21.578 -21.288 1.00119.92 C ANISOU 2149 C SER C 191 13581 17329 14653 1262 860 1684 C ATOM 2150 O SER C 191 -44.629 20.723 -21.368 1.00118.22 O ANISOU 2150 O SER C 191 13498 17196 14226 1411 812 1311 O ATOM 2151 CB SER C 191 -44.347 23.810 -22.203 1.00123.37 C ANISOU 2151 CB SER C 191 14121 17801 14952 1182 973 2445 C ATOM 2152 OG SER C 191 -43.105 24.172 -22.777 1.00127.38 O ANISOU 2152 OG SER C 191 14324 18472 15602 1099 1243 2823 O ATOM 2153 N LYS C 192 -42.497 21.297 -21.487 1.00119.86 N ANISOU 2153 N LYS C 192 13280 17457 14805 1240 1020 1769 N ATOM 2154 CA LYS C 192 -42.098 19.922 -21.734 1.00120.24 C ANISOU 2154 CA LYS C 192 13187 17718 14779 1428 1125 1400 C ATOM 2155 C LYS C 192 -42.694 18.982 -20.682 1.00116.78 C ANISOU 2155 C LYS C 192 12949 16924 14498 1469 900 1011 C ATOM 2156 O LYS C 192 -43.038 17.838 -20.966 1.00116.73 O ANISOU 2156 O LYS C 192 12951 17003 14397 1645 966 631 O ATOM 2157 CB LYS C 192 -40.573 19.806 -21.731 1.00122.99 C ANISOU 2157 CB LYS C 192 13177 18157 15396 1382 1266 1545 C ATOM 2158 CG LYS C 192 -39.909 20.293 -23.023 1.00127.56 C ANISOU 2158 CG LYS C 192 13481 19228 15759 1423 1618 1874 C ATOM 2159 CD LYS C 192 -38.929 21.449 -22.800 1.00130.11 C ANISOU 2159 CD LYS C 192 13567 19400 16469 1145 1683 2366 C ATOM 2160 CE LYS C 192 -37.728 21.062 -21.954 1.00130.60 C ANISOU 2160 CE LYS C 192 13342 19288 16992 1047 1586 2255 C ATOM 2161 NZ LYS C 192 -36.948 22.285 -21.586 1.00133.15 N ANISOU 2161 NZ LYS C 192 13431 19375 17784 715 1574 2642 N ATOM 2162 N LEU C 193 -42.843 19.469 -19.460 1.00 95.62 N ANISOU 2162 N LEU C 193 10418 13841 12073 1317 649 1101 N ATOM 2163 CA LEU C 193 -43.313 18.616 -18.398 1.00 93.13 C ANISOU 2163 CA LEU C 193 10271 13226 11889 1379 481 842 C ATOM 2164 C LEU C 193 -44.719 18.148 -18.641 1.00 91.46 C ANISOU 2164 C LEU C 193 10284 13002 11464 1460 485 578 C ATOM 2165 O LEU C 193 -45.143 17.203 -17.989 1.00 90.27 O ANISOU 2165 O LEU C 193 10231 12627 11442 1531 444 355 O ATOM 2166 CB LEU C 193 -43.231 19.320 -17.050 1.00 91.71 C ANISOU 2166 CB LEU C 193 10193 12725 11926 1241 206 978 C ATOM 2167 CG LEU C 193 -41.813 19.550 -16.529 1.00 93.72 C ANISOU 2167 CG LEU C 193 10175 12966 12470 1173 130 1117 C ATOM 2168 CD1 LEU C 193 -41.845 20.421 -15.279 1.00 93.04 C ANISOU 2168 CD1 LEU C 193 10175 12628 12548 1040 -182 1163 C ATOM 2169 CD2 LEU C 193 -41.124 18.247 -16.228 1.00 94.54 C ANISOU 2169 CD2 LEU C 193 10135 13099 12685 1374 178 972 C ATOM 2170 N ALA C 194 -45.444 18.806 -19.548 1.00 87.71 N ANISOU 2170 N ALA C 194 9868 12768 10689 1460 538 625 N ATOM 2171 CA ALA C 194 -46.811 18.408 -19.899 1.00 86.78 C ANISOU 2171 CA ALA C 194 9898 12723 10352 1544 523 324 C ATOM 2172 C ALA C 194 -46.846 17.009 -20.467 1.00 88.24 C ANISOU 2172 C ALA C 194 9955 13041 10533 1697 670 -118 C ATOM 2173 O ALA C 194 -47.822 16.286 -20.305 1.00 87.53 O ANISOU 2173 O ALA C 194 9945 12817 10494 1723 640 -463 O ATOM 2174 CB ALA C 194 -47.391 19.364 -20.893 1.00 88.05 C ANISOU 2174 CB ALA C 194 10084 13223 10148 1585 554 486 C ATOM 2175 N PHE C 195 -45.759 16.649 -21.143 1.00102.47 N ANISOU 2175 N PHE C 195 11524 15094 12317 1793 844 -124 N ATOM 2176 CA PHE C 195 -45.642 15.365 -21.841 1.00104.91 C ANISOU 2176 CA PHE C 195 11664 15565 12631 1974 1004 -598 C ATOM 2177 C PHE C 195 -44.551 14.456 -21.285 1.00105.73 C ANISOU 2177 C PHE C 195 11633 15409 13130 2036 1077 -642 C ATOM 2178 O PHE C 195 -44.617 13.246 -21.470 1.00107.39 O ANISOU 2178 O PHE C 195 11763 15512 13528 2171 1174 -1065 O ATOM 2179 CB PHE C 195 -45.331 15.600 -23.321 1.00108.52 C ANISOU 2179 CB PHE C 195 11919 16674 12641 2136 1186 -649 C ATOM 2180 CG PHE C 195 -46.231 16.585 -23.975 1.00108.74 C ANISOU 2180 CG PHE C 195 12046 17049 12220 2149 1132 -494 C ATOM 2181 CD1 PHE C 195 -47.400 16.168 -24.583 1.00109.66 C ANISOU 2181 CD1 PHE C 195 12183 17413 12071 2271 1074 -955 C ATOM 2182 CD2 PHE C 195 -45.926 17.933 -23.965 1.00108.57 C ANISOU 2182 CD2 PHE C 195 12075 17085 12092 2047 1131 105 C ATOM 2183 CE1 PHE C 195 -48.256 17.081 -25.180 1.00110.30 C ANISOU 2183 CE1 PHE C 195 12340 17859 11709 2339 1000 -792 C ATOM 2184 CE2 PHE C 195 -46.771 18.848 -24.553 1.00109.29 C ANISOU 2184 CE2 PHE C 195 12268 17458 11800 2105 1090 308 C ATOM 2185 CZ PHE C 195 -47.941 18.423 -25.165 1.00110.09 C ANISOU 2185 CZ PHE C 195 12396 17871 11562 2275 1017 -126 C ATOM 2186 N HIS C 196 -43.540 15.035 -20.641 1.00120.24 N ANISOU 2186 N HIS C 196 13414 17147 15125 1952 1027 -232 N ATOM 2187 CA HIS C 196 -42.383 14.270 -20.179 1.00121.68 C ANISOU 2187 CA HIS C 196 13414 17181 15639 2058 1082 -231 C ATOM 2188 C HIS C 196 -42.464 14.129 -18.675 1.00119.41 C ANISOU 2188 C HIS C 196 13294 16419 15656 2004 880 -67 C ATOM 2189 O HIS C 196 -42.475 15.122 -17.947 1.00117.59 O ANISOU 2189 O HIS C 196 13165 16110 15403 1844 692 232 O ATOM 2190 CB HIS C 196 -41.066 14.968 -20.555 1.00123.82 C ANISOU 2190 CB HIS C 196 13407 17766 15874 2028 1171 81 C ATOM 2191 CG HIS C 196 -39.837 14.189 -20.185 1.00125.91 C ANISOU 2191 CG HIS C 196 13421 17962 16457 2177 1226 56 C ATOM 2192 ND1 HIS C 196 -39.607 13.711 -18.913 1.00124.84 N ANISOU 2192 ND1 HIS C 196 13353 17429 16652 2221 1050 121 N ATOM 2193 CD2 HIS C 196 -38.764 13.817 -20.925 1.00129.51 C ANISOU 2193 CD2 HIS C 196 13540 18743 16925 2332 1441 -8 C ATOM 2194 CE1 HIS C 196 -38.457 13.063 -18.890 1.00127.65 C ANISOU 2194 CE1 HIS C 196 13425 17846 17229 2406 1135 97 C ATOM 2195 NE2 HIS C 196 -37.923 13.113 -20.096 1.00130.41 N ANISOU 2195 NE2 HIS C 196 13519 18619 17411 2465 1375 -1 N ATOM 2196 N HIS C 197 -42.482 12.889 -18.212 1.00 98.14 N ANISOU 2196 N HIS C 197 10612 13420 13255 2164 930 -260 N ATOM 2197 CA HIS C 197 -42.688 12.613 -16.815 1.00 96.75 C ANISOU 2197 CA HIS C 197 10610 12844 13308 2179 783 -73 C ATOM 2198 C HIS C 197 -41.397 12.183 -16.119 1.00 98.72 C ANISOU 2198 C HIS C 197 10677 13029 13803 2357 744 125 C ATOM 2199 O HIS C 197 -41.280 11.045 -15.668 1.00100.43 O ANISOU 2199 O HIS C 197 10894 12950 14315 2568 824 84 O ATOM 2200 CB HIS C 197 -43.780 11.565 -16.701 1.00 96.89 C ANISOU 2200 CB HIS C 197 10781 12513 13518 2232 891 -339 C ATOM 2201 CG HIS C 197 -44.307 11.400 -15.319 1.00 95.60 C ANISOU 2201 CG HIS C 197 10835 11989 13500 2233 788 -87 C ATOM 2202 ND1 HIS C 197 -45.192 10.405 -14.984 1.00 96.45 N ANISOU 2202 ND1 HIS C 197 11055 11700 13892 2273 926 -209 N ATOM 2203 CD2 HIS C 197 -44.071 12.096 -14.185 1.00 94.22 C ANISOU 2203 CD2 HIS C 197 10761 11819 13218 2215 578 272 C ATOM 2204 CE1 HIS C 197 -45.473 10.492 -13.698 1.00 95.60 C ANISOU 2204 CE1 HIS C 197 11122 11399 13804 2298 836 137 C ATOM 2205 NE2 HIS C 197 -44.819 11.522 -13.195 1.00 94.19 N ANISOU 2205 NE2 HIS C 197 10945 11491 13352 2279 603 398 N ATOM 2206 N MET C 198 -40.452 13.126 -16.022 1.00118.21 N ANISOU 2206 N MET C 198 12972 15759 16184 2273 619 350 N ATOM 2207 CA MET C 198 -39.114 12.916 -15.431 1.00120.56 C ANISOU 2207 CA MET C 198 13011 16115 16682 2429 536 516 C ATOM 2208 C MET C 198 -39.088 11.969 -14.257 1.00121.43 C ANISOU 2208 C MET C 198 13217 15919 17002 2684 455 627 C ATOM 2209 O MET C 198 -38.364 10.985 -14.271 1.00124.33 O ANISOU 2209 O MET C 198 13409 16218 17613 2956 564 601 O ATOM 2210 CB MET C 198 -38.546 14.245 -14.923 1.00120.13 C ANISOU 2210 CB MET C 198 12847 16244 16554 2224 293 745 C ATOM 2211 CG MET C 198 -37.873 15.115 -15.968 1.00121.50 C ANISOU 2211 CG MET C 198 12747 16742 16674 2035 411 786 C ATOM 2212 SD MET C 198 -36.322 14.450 -16.604 1.00125.90 S ANISOU 2212 SD MET C 198 12816 17589 17431 2237 612 747 S ATOM 2213 CE MET C 198 -35.484 14.101 -15.051 1.00127.31 C ANISOU 2213 CE MET C 198 12861 17650 17859 2430 293 866 C ATOM 2214 N ALA C 199 -39.862 12.298 -13.227 1.00108.80 N ANISOU 2214 N ALA C 199 11886 14159 15295 2627 276 783 N ATOM 2215 CA ALA C 199 -39.826 11.564 -11.978 1.00110.18 C ANISOU 2215 CA ALA C 199 12156 14126 15581 2895 193 1005 C ATOM 2216 C ALA C 199 -39.969 10.084 -12.230 1.00112.48 C ANISOU 2216 C ALA C 199 12463 14072 16203 3141 472 938 C ATOM 2217 O ALA C 199 -39.284 9.297 -11.610 1.00115.52 O ANISOU 2217 O ALA C 199 12751 14351 16791 3460 476 1135 O ATOM 2218 CB ALA C 199 -40.902 12.037 -11.065 1.00107.92 C ANISOU 2218 CB ALA C 199 12179 13741 15086 2800 57 1131 C ATOM 2219 N ARG C 200 -40.853 9.703 -13.144 1.00127.91 N ANISOU 2219 N ARG C 200 14515 15845 18240 3010 698 639 N ATOM 2220 CA ARG C 200 -41.087 8.297 -13.447 1.00130.71 C ANISOU 2220 CA ARG C 200 14865 15789 19010 3200 973 470 C ATOM 2221 C ARG C 200 -39.883 7.691 -14.174 1.00134.07 C ANISOU 2221 C ARG C 200 14974 16314 19654 3426 1092 296 C ATOM 2222 O ARG C 200 -39.614 6.492 -14.071 1.00137.64 O ANISOU 2222 O ARG C 200 15365 16403 20531 3707 1265 273 O ATOM 2223 CB ARG C 200 -42.350 8.144 -14.279 1.00129.45 C ANISOU 2223 CB ARG C 200 14831 15480 18875 2977 1134 82 C ATOM 2224 CG ARG C 200 -43.117 6.894 -13.975 1.00131.85 C ANISOU 2224 CG ARG C 200 15242 15203 19654 3070 1360 20 C ATOM 2225 CD ARG C 200 -43.928 6.419 -15.165 1.00132.74 C ANISOU 2225 CD ARG C 200 15296 15202 19937 2925 1542 -579 C ATOM 2226 NE ARG C 200 -44.561 5.121 -14.898 1.00136.20 N ANISOU 2226 NE ARG C 200 15769 14983 20998 2994 1789 -685 N ATOM 2227 CZ ARG C 200 -45.823 4.793 -15.174 1.00136.56 C ANISOU 2227 CZ ARG C 200 15868 14760 21257 2781 1908 -1013 C ATOM 2228 NH1 ARG C 200 -46.645 5.656 -15.760 1.00133.48 N ANISOU 2228 NH1 ARG C 200 15515 14753 20449 2522 1781 -1285 N ATOM 2229 NH2 ARG C 200 -46.266 3.582 -14.874 1.00140.61 N ANISOU 2229 NH2 ARG C 200 16370 14600 22455 2835 2163 -1067 N ATOM 2230 N GLU C 201 -39.154 8.528 -14.899 1.00130.80 N ANISOU 2230 N GLU C 201 14343 16375 18979 3316 1023 198 N ATOM 2231 CA GLU C 201 -37.880 8.141 -15.456 1.00134.15 C ANISOU 2231 CA GLU C 201 14417 17005 19548 3536 1115 97 C ATOM 2232 C GLU C 201 -36.910 7.921 -14.289 1.00136.23 C ANISOU 2232 C GLU C 201 14560 17240 19960 3811 943 484 C ATOM 2233 O GLU C 201 -36.409 6.823 -14.108 1.00139.88 O ANISOU 2233 O GLU C 201 14917 17452 20777 4161 1060 504 O ATOM 2234 CB GLU C 201 -37.380 9.242 -16.393 1.00133.27 C ANISOU 2234 CB GLU C 201 14094 17441 19101 3316 1103 12 C ATOM 2235 CG GLU C 201 -36.519 8.772 -17.541 1.00136.81 C ANISOU 2235 CG GLU C 201 14201 18162 19618 3487 1340 -279 C ATOM 2236 CD GLU C 201 -36.094 9.912 -18.475 1.00136.52 C ANISOU 2236 CD GLU C 201 13956 18691 19224 3265 1389 -258 C ATOM 2237 OE1 GLU C 201 -34.866 10.068 -18.698 1.00139.26 O ANISOU 2237 OE1 GLU C 201 13932 19357 19624 3356 1442 -169 O ATOM 2238 OE2 GLU C 201 -36.984 10.640 -18.985 1.00134.07 O ANISOU 2238 OE2 GLU C 201 13833 18508 18600 3016 1394 -298 O ATOM 2239 N LEU C 202 -36.719 8.954 -13.465 1.00109.89 N ANISOU 2239 N LEU C 202 11244 14147 16360 3675 651 769 N ATOM 2240 CA LEU C 202 -35.679 8.997 -12.419 1.00112.28 C ANISOU 2240 CA LEU C 202 11350 14618 16694 3923 407 1071 C ATOM 2241 C LEU C 202 -36.176 8.576 -11.018 1.00112.75 C ANISOU 2241 C LEU C 202 11674 14431 16734 4149 270 1420 C ATOM 2242 O LEU C 202 -35.760 9.089 -9.966 1.00113.44 O ANISOU 2242 O LEU C 202 11709 14774 16621 4246 -38 1659 O ATOM 2243 CB LEU C 202 -35.022 10.389 -12.402 1.00111.30 C ANISOU 2243 CB LEU C 202 10994 14957 16337 3652 156 1090 C ATOM 2244 N HIS C 203 -37.211 7.765 -11.057 1.00146.21 N ANISOU 2244 N HIS C 203 16200 18208 21145 4181 506 1414 N ATOM 2245 CA HIS C 203 -37.137 6.388 -10.668 1.00150.17 C ANISOU 2245 CA HIS C 203 16736 18279 22043 4580 701 1604 C ATOM 2246 C HIS C 203 -38.521 5.965 -10.288 1.00149.10 C ANISOU 2246 C HIS C 203 16964 17686 21999 4486 872 1711 C ATOM 2247 O HIS C 203 -39.268 6.744 -9.688 1.00146.13 O ANISOU 2247 O HIS C 203 16804 17444 21276 4281 722 1844 O ATOM 2248 CB HIS C 203 -36.152 6.118 -9.527 1.00153.96 C ANISOU 2248 CB HIS C 203 17066 18931 22501 5024 496 2036 C ATOM 2249 N PRO C 204 -38.874 4.741 -10.665 1.00145.38 N ANISOU 2249 N PRO C 204 16534 16660 22043 4623 1199 1615 N ATOM 2250 CA PRO C 204 -40.142 4.141 -10.269 1.00145.74 C ANISOU 2250 CA PRO C 204 16863 16177 22336 4548 1424 1747 C ATOM 2251 C PRO C 204 -40.432 4.112 -8.748 1.00146.99 C ANISOU 2251 C PRO C 204 17227 16303 22319 4764 1354 2407 C ATOM 2252 O PRO C 204 -39.969 3.238 -7.985 1.00151.78 O ANISOU 2252 O PRO C 204 17820 16669 23180 5200 1451 2875 O ATOM 2253 CB PRO C 204 -40.058 2.752 -10.877 1.00150.37 C ANISOU 2253 CB PRO C 204 17348 16155 23631 4744 1766 1534 C ATOM 2254 CG PRO C 204 -39.234 2.974 -12.127 1.00149.99 C ANISOU 2254 CG PRO C 204 17013 16443 23533 4700 1727 991 C ATOM 2255 CD PRO C 204 -38.231 4.012 -11.775 1.00148.12 C ANISOU 2255 CD PRO C 204 16627 16873 22778 4745 1398 1207 C ATOM 2256 N GLU C 205 -41.149 5.166 -8.350 1.00137.63 N ANISOU 2256 N GLU C 205 16214 15438 20639 4485 1168 2434 N ATOM 2257 CA GLU C 205 -42.014 5.201 -7.161 1.00138.03 C ANISOU 2257 CA GLU C 205 16521 15427 20496 4543 1198 2896 C ATOM 2258 C GLU C 205 -43.457 4.920 -7.559 1.00136.70 C ANISOU 2258 C GLU C 205 16526 14818 20597 4209 1491 2702 C ATOM 2259 O GLU C 205 -44.376 5.350 -6.866 1.00135.33 O ANISOU 2259 O GLU C 205 16545 14725 20151 4094 1488 2905 O ATOM 2260 CB GLU C 205 -41.978 6.594 -6.499 1.00134.74 C ANISOU 2260 CB GLU C 205 16160 15651 19383 4438 804 2941 C ATOM 2261 CG GLU C 205 -40.748 6.839 -5.601 1.00137.42 C ANISOU 2261 CG GLU C 205 16341 16468 19406 4831 481 3245 C ATOM 2262 CD GLU C 205 -40.020 8.167 -5.877 1.00134.51 C ANISOU 2262 CD GLU C 205 15779 16663 18667 4618 77 2890 C ATOM 2263 OE1 GLU C 205 -40.149 8.659 -7.007 1.00131.18 O ANISOU 2263 OE1 GLU C 205 15296 16205 18340 4240 113 2460 O ATOM 2264 OE2 GLU C 205 -39.292 8.695 -4.994 1.00136.24 O ANISOU 2264 OE2 GLU C 205 15875 17359 18529 4838 -268 3037 O ATOM 2265 N TYR C 206 -43.667 4.211 -8.662 1.00145.67 N ANISOU 2265 N TYR C 206 17561 15527 22258 4063 1733 2265 N ATOM 2266 CA TYR C 206 -45.005 4.087 -9.219 1.00144.34 C ANISOU 2266 CA TYR C 206 17478 15044 22322 3694 1940 1915 C ATOM 2267 C TYR C 206 -45.388 2.605 -9.284 1.00149.77 C ANISOU 2267 C TYR C 206 18131 14934 23842 3792 2359 1957 C ATOM 2268 O TYR C 206 -44.635 1.785 -9.823 1.00153.16 O ANISOU 2268 O TYR C 206 18395 15068 24731 3992 2474 1777 O ATOM 2269 CB TYR C 206 -45.072 4.827 -10.570 1.00140.48 C ANISOU 2269 CB TYR C 206 16873 14888 21616 3372 1791 1229 C ATOM 2270 CG TYR C 206 -44.650 6.302 -10.456 1.00136.02 C ANISOU 2270 CG TYR C 206 16331 15007 20344 3273 1416 1266 C ATOM 2271 CD1 TYR C 206 -43.318 6.679 -10.480 1.00136.20 C ANISOU 2271 CD1 TYR C 206 16191 15392 20167 3453 1208 1342 C ATOM 2272 CD2 TYR C 206 -45.592 7.305 -10.287 1.00132.28 C ANISOU 2272 CD2 TYR C 206 16013 14775 19473 3002 1282 1224 C ATOM 2273 CE1 TYR C 206 -42.949 8.014 -10.360 1.00132.98 C ANISOU 2273 CE1 TYR C 206 15768 15517 19240 3322 888 1355 C ATOM 2274 CE2 TYR C 206 -45.226 8.637 -10.164 1.00129.01 C ANISOU 2274 CE2 TYR C 206 15612 14877 18527 2909 959 1244 C ATOM 2275 CZ TYR C 206 -43.912 8.990 -10.204 1.00129.46 C ANISOU 2275 CZ TYR C 206 15500 15236 18453 3048 767 1304 C ATOM 2276 OH TYR C 206 -43.573 10.325 -10.071 1.00126.92 O ANISOU 2276 OH TYR C 206 15161 15350 17714 2913 463 1300 O ATOM 2277 N TYR C 207 -46.540 2.287 -8.682 1.00160.08 N ANISOU 2277 N TYR C 207 19574 15882 25366 3662 2600 2213 N ATOM 2278 CA TYR C 207 -47.014 0.910 -8.477 1.00166.18 C ANISOU 2278 CA TYR C 207 20324 15811 27007 3736 3049 2411 C ATOM 2279 C TYR C 207 -45.879 -0.055 -8.120 1.00171.60 C ANISOU 2279 C TYR C 207 20945 16149 28106 4225 3175 2827 C ATOM 2280 O TYR C 207 -46.054 -0.969 -7.310 1.00177.15 O ANISOU 2280 O TYR C 207 21712 16296 29299 4461 3506 3442 O ATOM 2281 CB TYR C 207 -47.773 0.408 -9.709 1.00167.01 C ANISOU 2281 CB TYR C 207 20263 15485 27708 3371 3225 1605 C TER 2282 TYR C 207 ATOM 2283 N GLU D 79 -89.968 16.916 -15.910 1.00202.73 N ANISOU 2283 N GLU D 79 17564 26149 33316 -2610 -3403 -5392 N ATOM 2284 CA GLU D 79 -89.330 18.201 -15.463 1.00196.73 C ANISOU 2284 CA GLU D 79 17176 25410 32163 -2012 -3322 -4885 C ATOM 2285 C GLU D 79 -87.829 18.065 -15.098 1.00189.53 C ANISOU 2285 C GLU D 79 17126 24181 30706 -1863 -2956 -4801 C ATOM 2286 O GLU D 79 -87.416 17.078 -14.493 1.00188.13 O ANISOU 2286 O GLU D 79 17211 23605 30663 -2054 -2433 -4922 O ATOM 2287 CB GLU D 79 -90.099 18.766 -14.264 1.00197.02 C ANISOU 2287 CB GLU D 79 16840 25243 32773 -1730 -2855 -4531 C ATOM 2288 CG GLU D 79 -89.935 20.281 -14.081 1.00194.15 C ANISOU 2288 CG GLU D 79 16589 25027 32152 -1177 -2924 -4075 C ATOM 2289 CD GLU D 79 -89.689 20.687 -12.627 1.00190.22 C ANISOU 2289 CD GLU D 79 16379 24102 31795 -872 -2196 -3788 C ATOM 2290 OE1 GLU D 79 -88.515 20.990 -12.281 1.00184.51 O ANISOU 2290 OE1 GLU D 79 16325 23232 30547 -691 -2005 -3701 O ATOM 2291 OE2 GLU D 79 -90.669 20.701 -11.837 1.00193.36 O ANISOU 2291 OE2 GLU D 79 16324 24329 32816 -823 -1818 -3657 O ATOM 2292 N ASP D 80 -87.029 19.072 -15.449 1.00175.98 N ANISOU 2292 N ASP D 80 15805 22643 28416 -1502 -3200 -4554 N ATOM 2293 CA ASP D 80 -85.579 19.037 -15.207 1.00169.76 C ANISOU 2293 CA ASP D 80 15762 21628 27111 -1363 -2936 -4456 C ATOM 2294 C ASP D 80 -85.194 19.602 -13.845 1.00165.50 C ANISOU 2294 C ASP D 80 15440 20822 26622 -1044 -2394 -4129 C ATOM 2295 O ASP D 80 -85.904 20.465 -13.325 1.00166.58 O ANISOU 2295 O ASP D 80 15265 20998 27031 -808 -2322 -3919 O ATOM 2296 CB ASP D 80 -84.830 19.793 -16.307 1.00168.03 C ANISOU 2296 CB ASP D 80 15875 21705 26263 -1166 -3436 -4379 C ATOM 2297 CG ASP D 80 -84.296 18.862 -17.383 1.00169.24 C ANISOU 2297 CG ASP D 80 16324 21917 26063 -1485 -3684 -4720 C ATOM 2298 OD1 ASP D 80 -83.052 18.888 -17.616 1.00165.05 O ANISOU 2298 OD1 ASP D 80 16387 21271 25052 -1368 -3601 -4636 O ATOM 2299 OD2 ASP D 80 -85.119 18.089 -17.966 1.00174.84 O ANISOU 2299 OD2 ASP D 80 16666 22768 26997 -1872 -3926 -5088 O ATOM 2300 N ILE D 81 -84.067 19.131 -13.287 1.00154.38 N ANISOU 2300 N ILE D 81 14563 19168 24928 -1028 -2012 -4079 N ATOM 2301 CA ILE D 81 -83.619 19.547 -11.948 1.00151.05 C ANISOU 2301 CA ILE D 81 14376 18560 24457 -767 -1515 -3815 C ATOM 2302 C ILE D 81 -82.902 20.880 -11.996 1.00147.69 C ANISOU 2302 C ILE D 81 14240 18270 23605 -453 -1697 -3614 C ATOM 2303 O ILE D 81 -81.821 20.964 -12.595 1.00144.85 O ANISOU 2303 O ILE D 81 14273 17973 22788 -430 -1892 -3604 O ATOM 2304 CB ILE D 81 -82.598 18.576 -11.344 1.00148.40 C ANISOU 2304 CB ILE D 81 14468 18003 23915 -831 -1074 -3777 C ATOM 2305 CG1 ILE D 81 -83.211 17.203 -11.159 1.00151.89 C ANISOU 2305 CG1 ILE D 81 14680 18202 24829 -1124 -719 -3948 C ATOM 2306 CG2 ILE D 81 -82.091 19.075 -9.993 1.00145.70 C ANISOU 2306 CG2 ILE D 81 14366 17596 23397 -555 -653 -3512 C ATOM 2307 CD1 ILE D 81 -82.250 16.253 -10.445 1.00149.90 C ANISOU 2307 CD1 ILE D 81 14822 17714 24418 -1100 -165 -3802 C ATOM 2308 N ILE D 82 -83.465 21.894 -11.330 1.00125.13 N ANISOU 2308 N ILE D 82 11208 15404 20931 -217 -1555 -3455 N ATOM 2309 CA ILE D 82 -82.841 23.214 -11.287 1.00122.68 C ANISOU 2309 CA ILE D 82 11167 15147 20300 57 -1621 -3299 C ATOM 2310 C ILE D 82 -82.243 23.568 -9.919 1.00120.37 C ANISOU 2310 C ILE D 82 11201 14698 19836 178 -1144 -3214 C ATOM 2311 O ILE D 82 -82.742 23.133 -8.866 1.00121.68 O ANISOU 2311 O ILE D 82 11269 14730 20234 166 -721 -3197 O ATOM 2312 CB ILE D 82 -83.792 24.324 -11.645 1.00125.63 C ANISOU 2312 CB ILE D 82 11172 15618 20946 272 -1787 -3172 C ATOM 2313 CG1 ILE D 82 -84.757 23.908 -12.744 1.00129.81 C ANISOU 2313 CG1 ILE D 82 11202 16385 21736 147 -2234 -3244 C ATOM 2314 CG2 ILE D 82 -82.969 25.500 -12.116 1.00123.45 C ANISOU 2314 CG2 ILE D 82 11211 15390 20305 501 -1943 -3049 C ATOM 2315 CD1 ILE D 82 -84.076 23.743 -14.064 1.00129.02 C ANISOU 2315 CD1 ILE D 82 11310 16509 21203 79 -2734 -3332 C ATOM 2316 N VAL D 83 -81.180 24.376 -9.952 1.00 93.76 N ANISOU 2316 N VAL D 83 8210 11362 16051 289 -1212 -3168 N ATOM 2317 CA VAL D 83 -80.491 24.800 -8.739 1.00 92.19 C ANISOU 2317 CA VAL D 83 8334 11101 15592 357 -851 -3148 C ATOM 2318 C VAL D 83 -80.184 26.298 -8.755 1.00 91.93 C ANISOU 2318 C VAL D 83 8455 11030 15444 519 -863 -3137 C ATOM 2319 O VAL D 83 -79.927 26.879 -9.810 1.00 91.42 O ANISOU 2319 O VAL D 83 8401 11004 15331 591 -1176 -3094 O ATOM 2320 CB VAL D 83 -79.195 24.010 -8.553 1.00 89.32 C ANISOU 2320 CB VAL D 83 8315 10820 14802 243 -839 -3138 C ATOM 2321 CG1 VAL D 83 -79.504 22.532 -8.420 1.00 90.17 C ANISOU 2321 CG1 VAL D 83 8299 10884 15079 106 -675 -3127 C ATOM 2322 CG2 VAL D 83 -78.250 24.250 -9.724 1.00 87.08 C ANISOU 2322 CG2 VAL D 83 8220 10614 14251 226 -1231 -3126 C ATOM 2323 N VAL D 84 -80.219 26.918 -7.579 1.00103.00 N ANISOU 2323 N VAL D 84 9997 12335 16801 581 -473 -3183 N ATOM 2324 CA VAL D 84 -79.847 28.315 -7.451 1.00103.31 C ANISOU 2324 CA VAL D 84 10237 12271 16744 679 -374 -3238 C ATOM 2325 C VAL D 84 -78.547 28.405 -6.714 1.00101.53 C ANISOU 2325 C VAL D 84 10410 12144 16023 546 -297 -3372 C ATOM 2326 O VAL D 84 -78.303 27.619 -5.777 1.00101.41 O ANISOU 2326 O VAL D 84 10496 12258 15775 463 -127 -3395 O ATOM 2327 CB VAL D 84 -80.813 29.121 -6.636 1.00106.64 C ANISOU 2327 CB VAL D 84 10568 12485 17464 818 63 -3255 C ATOM 2328 CG1 VAL D 84 -80.538 30.560 -6.896 1.00107.51 C ANISOU 2328 CG1 VAL D 84 10830 12423 17598 927 154 -3291 C ATOM 2329 CG2 VAL D 84 -82.186 28.795 -7.009 1.00109.16 C ANISOU 2329 CG2 VAL D 84 10418 12757 18302 932 61 -3095 C ATOM 2330 N ALA D 85 -77.722 29.374 -7.115 1.00106.94 N ANISOU 2330 N ALA D 85 11292 12782 16557 537 -399 -3441 N ATOM 2331 CA ALA D 85 -76.371 29.482 -6.573 1.00105.66 C ANISOU 2331 CA ALA D 85 11442 12766 15939 365 -417 -3577 C ATOM 2332 C ALA D 85 -76.417 30.275 -5.270 1.00108.44 C ANISOU 2332 C ALA D 85 11986 13064 16152 301 -27 -3823 C ATOM 2333 O ALA D 85 -76.788 31.449 -5.235 1.00110.65 O ANISOU 2333 O ALA D 85 12315 13078 16650 357 212 -3946 O ATOM 2334 CB ALA D 85 -75.432 30.121 -7.570 1.00104.14 C ANISOU 2334 CB ALA D 85 11354 12523 15692 351 -664 -3559 C ATOM 2335 N LEU D 86 -76.049 29.603 -4.191 1.00107.33 N ANISOU 2335 N LEU D 86 11971 13180 15630 199 75 -3882 N ATOM 2336 CA LEU D 86 -76.036 30.226 -2.896 1.00110.56 C ANISOU 2336 CA LEU D 86 12609 13621 15778 118 420 -4148 C ATOM 2337 C LEU D 86 -74.760 31.005 -2.712 1.00111.10 C ANISOU 2337 C LEU D 86 12909 13821 15483 -117 296 -4412 C ATOM 2338 O LEU D 86 -74.704 31.829 -1.821 1.00114.49 O ANISOU 2338 O LEU D 86 13557 14218 15726 -244 569 -4739 O ATOM 2339 CB LEU D 86 -76.162 29.175 -1.797 1.00111.59 C ANISOU 2339 CB LEU D 86 12778 14037 15584 145 584 -4066 C ATOM 2340 CG LEU D 86 -77.453 28.370 -1.779 1.00111.98 C ANISOU 2340 CG LEU D 86 12586 13924 16037 343 806 -3839 C ATOM 2341 CD1 LEU D 86 -77.983 28.317 -0.364 1.00115.62 C ANISOU 2341 CD1 LEU D 86 13204 14428 16297 416 1281 -3915 C ATOM 2342 CD2 LEU D 86 -78.483 28.986 -2.678 1.00112.19 C ANISOU 2342 CD2 LEU D 86 12371 13577 16679 460 827 -3794 C ATOM 2343 N TYR D 87 -73.733 30.745 -3.525 1.00117.64 N ANISOU 2343 N TYR D 87 13693 14788 16219 -195 -84 -4295 N ATOM 2344 CA TYR D 87 -72.457 31.448 -3.393 1.00118.51 C ANISOU 2344 CA TYR D 87 13952 15030 16046 -445 -216 -4531 C ATOM 2345 C TYR D 87 -71.802 31.608 -4.727 1.00115.73 C ANISOU 2345 C TYR D 87 13514 14535 15925 -425 -493 -4365 C ATOM 2346 O TYR D 87 -72.202 30.971 -5.667 1.00113.08 O ANISOU 2346 O TYR D 87 13035 14111 15818 -232 -642 -4067 O ATOM 2347 CB TYR D 87 -71.513 30.682 -2.501 1.00119.17 C ANISOU 2347 CB TYR D 87 14080 15655 15545 -589 -380 -4521 C ATOM 2348 CG TYR D 87 -72.183 30.055 -1.324 1.00121.30 C ANISOU 2348 CG TYR D 87 14408 16143 15538 -497 -135 -4505 C ATOM 2349 CD1 TYR D 87 -72.197 30.681 -0.089 1.00125.76 C ANISOU 2349 CD1 TYR D 87 15194 16863 15726 -644 99 -4869 C ATOM 2350 CD2 TYR D 87 -72.800 28.841 -1.439 1.00119.44 C ANISOU 2350 CD2 TYR D 87 14027 15939 15416 -269 -95 -4145 C ATOM 2351 CE1 TYR D 87 -72.813 30.100 0.995 1.00128.12 C ANISOU 2351 CE1 TYR D 87 15579 17363 15737 -512 367 -4819 C ATOM 2352 CE2 TYR D 87 -73.417 28.256 -0.369 1.00121.72 C ANISOU 2352 CE2 TYR D 87 14366 16385 15497 -149 199 -4087 C ATOM 2353 CZ TYR D 87 -73.428 28.884 0.838 1.00125.95 C ANISOU 2353 CZ TYR D 87 15133 17090 15632 -243 431 -4397 C ATOM 2354 OH TYR D 87 -74.047 28.268 1.890 1.00128.51 O ANISOU 2354 OH TYR D 87 15533 17571 15723 -74 763 -4294 O ATOM 2355 N ASP D 88 -70.805 32.469 -4.823 1.00107.67 N ANISOU 2355 N ASP D 88 12582 13480 14846 -633 -541 -4576 N ATOM 2356 CA ASP D 88 -70.025 32.533 -6.041 1.00105.25 C ANISOU 2356 CA ASP D 88 12211 13063 14718 -598 -775 -4376 C ATOM 2357 C ASP D 88 -69.047 31.370 -6.116 1.00103.03 C ANISOU 2357 C ASP D 88 11849 13186 14112 -638 -1096 -4117 C ATOM 2358 O ASP D 88 -68.466 30.975 -5.119 1.00104.53 O ANISOU 2358 O ASP D 88 12039 13788 13890 -801 -1159 -4193 O ATOM 2359 CB ASP D 88 -69.219 33.824 -6.082 1.00107.75 C ANISOU 2359 CB ASP D 88 12621 13172 15145 -826 -658 -4680 C ATOM 2360 CG ASP D 88 -70.023 34.991 -6.535 1.00109.46 C ANISOU 2360 CG ASP D 88 12902 12856 15833 -689 -301 -4778 C ATOM 2361 OD1 ASP D 88 -69.691 36.113 -6.093 1.00113.05 O ANISOU 2361 OD1 ASP D 88 13484 13091 16378 -920 -20 -5158 O ATOM 2362 OD2 ASP D 88 -70.960 34.780 -7.351 1.00107.75 O ANISOU 2362 OD2 ASP D 88 12589 12451 15899 -357 -293 -4471 O ATOM 2363 N TYR D 89 -68.847 30.849 -7.315 1.00 95.70 N ANISOU 2363 N TYR D 89 10858 12149 13355 -470 -1274 -3793 N ATOM 2364 CA TYR D 89 -67.771 29.906 -7.574 1.00 93.94 C ANISOU 2364 CA TYR D 89 10581 12201 12910 -492 -1500 -3518 C ATOM 2365 C TYR D 89 -66.919 30.374 -8.735 1.00 92.85 C ANISOU 2365 C TYR D 89 10461 11838 12979 -468 -1597 -3393 C ATOM 2366 O TYR D 89 -67.413 30.779 -9.775 1.00 91.92 O ANISOU 2366 O TYR D 89 10390 11376 13158 -286 -1562 -3318 O ATOM 2367 CB TYR D 89 -68.316 28.518 -7.892 1.00 91.67 C ANISOU 2367 CB TYR D 89 10244 11986 12600 -300 -1546 -3211 C ATOM 2368 CG TYR D 89 -67.235 27.513 -8.254 1.00 90.14 C ANISOU 2368 CG TYR D 89 10022 11992 12236 -279 -1679 -2879 C ATOM 2369 CD1 TYR D 89 -66.488 26.892 -7.290 1.00 91.36 C ANISOU 2369 CD1 TYR D 89 10104 12569 12041 -355 -1688 -2758 C ATOM 2370 CD2 TYR D 89 -66.982 27.185 -9.575 1.00 88.02 C ANISOU 2370 CD2 TYR D 89 9805 11496 12143 -151 -1765 -2655 C ATOM 2371 CE1 TYR D 89 -65.524 25.971 -7.631 1.00 90.42 C ANISOU 2371 CE1 TYR D 89 9931 12607 11816 -290 -1744 -2385 C ATOM 2372 CE2 TYR D 89 -66.025 26.255 -9.921 1.00 86.99 C ANISOU 2372 CE2 TYR D 89 9675 11484 11893 -110 -1801 -2333 C ATOM 2373 CZ TYR D 89 -65.296 25.647 -8.948 1.00 88.14 C ANISOU 2373 CZ TYR D 89 9717 12017 11756 -172 -1773 -2177 C ATOM 2374 OH TYR D 89 -64.317 24.735 -9.302 1.00 87.57 O ANISOU 2374 OH TYR D 89 9620 12042 11609 -90 -1749 -1787 O ATOM 2375 N VAL D 90 -65.618 30.306 -8.557 1.00 97.92 N ANISOU 2375 N VAL D 90 11045 12704 13456 -631 -1712 -3335 N ATOM 2376 CA VAL D 90 -64.758 30.446 -9.697 1.00 96.69 C ANISOU 2376 CA VAL D 90 10897 12344 13495 -561 -1773 -3110 C ATOM 2377 C VAL D 90 -64.020 29.150 -10.023 1.00 94.82 C ANISOU 2377 C VAL D 90 10610 12333 13086 -462 -1898 -2699 C ATOM 2378 O VAL D 90 -63.296 28.580 -9.201 1.00 95.92 O ANISOU 2378 O VAL D 90 10615 12884 12947 -578 -1974 -2600 O ATOM 2379 CB VAL D 90 -63.780 31.556 -9.526 1.00 99.31 C ANISOU 2379 CB VAL D 90 11174 12614 13944 -810 -1733 -3331 C ATOM 2380 CG1 VAL D 90 -62.769 31.496 -10.667 1.00 98.13 C ANISOU 2380 CG1 VAL D 90 11011 12281 13992 -707 -1765 -3009 C ATOM 2381 CG2 VAL D 90 -64.525 32.815 -9.571 1.00101.05 C ANISOU 2381 CG2 VAL D 90 11497 12444 14452 -830 -1497 -3657 C ATOM 2382 N SER D 91 -64.197 28.705 -11.249 1.00 95.13 N ANISOU 2382 N SER D 91 10762 12105 13276 -231 -1894 -2446 N ATOM 2383 CA SER D 91 -63.459 27.580 -11.732 1.00 93.76 C ANISOU 2383 CA SER D 91 10601 12020 13004 -127 -1917 -2064 C ATOM 2384 C SER D 91 -62.105 28.088 -12.199 1.00 94.52 C ANISOU 2384 C SER D 91 10649 12045 13220 -176 -1916 -1911 C ATOM 2385 O SER D 91 -62.011 29.248 -12.639 1.00 95.39 O ANISOU 2385 O SER D 91 10796 11877 13571 -205 -1867 -2074 O ATOM 2386 CB SER D 91 -64.219 26.932 -12.896 1.00 91.84 C ANISOU 2386 CB SER D 91 10541 11507 12846 102 -1898 -1929 C ATOM 2387 OG SER D 91 -63.774 27.405 -14.183 1.00 91.43 O ANISOU 2387 OG SER D 91 10640 11146 12954 247 -1884 -1795 O ATOM 2388 N TRP D 92 -61.080 27.237 -12.083 1.00 94.80 N ANISOU 2388 N TRP D 92 10578 12308 13133 -167 -1917 -1570 N ATOM 2389 CA TRP D 92 -59.798 27.477 -12.743 1.00 95.44 C ANISOU 2389 CA TRP D 92 10603 12270 13388 -151 -1872 -1311 C ATOM 2390 C TRP D 92 -59.688 26.623 -13.980 1.00 93.50 C ANISOU 2390 C TRP D 92 10592 11734 13201 128 -1728 -947 C ATOM 2391 O TRP D 92 -58.702 26.719 -14.711 1.00 93.90 O ANISOU 2391 O TRP D 92 10660 11603 13415 212 -1620 -674 O ATOM 2392 CB TRP D 92 -58.588 27.166 -11.844 1.00 97.81 C ANISOU 2392 CB TRP D 92 10575 13038 13549 -312 -1951 -1111 C ATOM 2393 CG TRP D 92 -58.565 27.896 -10.610 1.00100.60 C ANISOU 2393 CG TRP D 92 10711 13762 13752 -620 -2116 -1486 C ATOM 2394 CD1 TRP D 92 -59.382 28.908 -10.257 1.00101.29 C ANISOU 2394 CD1 TRP D 92 10888 13714 13885 -780 -2128 -1985 C ATOM 2395 CD2 TRP D 92 -57.702 27.676 -9.512 1.00103.85 C ANISOU 2395 CD2 TRP D 92 10783 14776 13900 -809 -2283 -1406 C ATOM 2396 NE1 TRP D 92 -59.088 29.337 -8.998 1.00104.78 N ANISOU 2396 NE1 TRP D 92 11118 14603 14090 -1091 -2273 -2284 N ATOM 2397 CE2 TRP D 92 -58.045 28.595 -8.521 1.00106.54 C ANISOU 2397 CE2 TRP D 92 11059 15332 14089 -1120 -2412 -1940 C ATOM 2398 CE3 TRP D 92 -56.682 26.791 -9.266 1.00105.29 C ANISOU 2398 CE3 TRP D 92 10702 15361 13944 -730 -2321 -916 C ATOM 2399 CZ2 TRP D 92 -57.385 28.671 -7.307 1.00110.84 C ANISOU 2399 CZ2 TRP D 92 11296 16530 14289 -1386 -2635 -2050 C ATOM 2400 CZ3 TRP D 92 -56.026 26.864 -8.065 1.00109.51 C ANISOU 2400 CZ3 TRP D 92 10874 16572 14163 -954 -2555 -954 C ATOM 2401 CH2 TRP D 92 -56.374 27.805 -7.101 1.00112.35 C ANISOU 2401 CH2 TRP D 92 11187 17185 14317 -1296 -2739 -1544 C ATOM 2402 N SER D 93 -60.652 25.749 -14.211 1.00 91.07 N ANISOU 2402 N SER D 93 10464 11371 12767 255 -1696 -948 N ATOM 2403 CA SER D 93 -60.472 24.785 -15.272 1.00 90.06 C ANISOU 2403 CA SER D 93 10578 11006 12636 463 -1533 -646 C ATOM 2404 C SER D 93 -61.658 24.736 -16.132 1.00 89.09 C ANISOU 2404 C SER D 93 10715 10636 12501 570 -1575 -852 C ATOM 2405 O SER D 93 -62.789 24.643 -15.653 1.00 88.86 O ANISOU 2405 O SER D 93 10637 10707 12418 501 -1676 -1116 O ATOM 2406 CB SER D 93 -60.277 23.377 -14.742 1.00 90.20 C ANISOU 2406 CB SER D 93 10542 11223 12506 494 -1378 -373 C ATOM 2407 OG SER D 93 -60.484 22.445 -15.791 1.00 89.55 O ANISOU 2407 OG SER D 93 10770 10831 12423 651 -1179 -233 O ATOM 2408 N PRO D 94 -61.413 24.658 -17.410 1.00 93.69 N ANISOU 2408 N PRO D 94 11568 10924 13108 749 -1486 -704 N ATOM 2409 CA PRO D 94 -62.500 24.680 -18.311 1.00 93.64 C ANISOU 2409 CA PRO D 94 11785 10762 13031 854 -1586 -898 C ATOM 2410 C PRO D 94 -63.430 23.501 -18.111 1.00 93.52 C ANISOU 2410 C PRO D 94 11805 10835 12893 772 -1594 -1036 C ATOM 2411 O PRO D 94 -64.496 23.472 -18.690 1.00 94.05 O ANISOU 2411 O PRO D 94 11967 10865 12904 794 -1742 -1261 O ATOM 2412 CB PRO D 94 -61.813 24.599 -19.657 1.00 94.19 C ANISOU 2412 CB PRO D 94 12175 10548 13066 1069 -1437 -652 C ATOM 2413 CG PRO D 94 -60.394 24.820 -19.363 1.00 94.37 C ANISOU 2413 CG PRO D 94 12072 10538 13247 1068 -1254 -343 C ATOM 2414 CD PRO D 94 -60.184 24.247 -18.064 1.00 94.10 C ANISOU 2414 CD PRO D 94 11743 10808 13201 877 -1258 -316 C ATOM 2415 N ASP D 95 -63.052 22.531 -17.303 1.00103.01 N ANISOU 2415 N ASP D 95 12903 12163 14074 683 -1421 -889 N ATOM 2416 CA ASP D 95 -63.929 21.433 -17.042 1.00103.36 C ANISOU 2416 CA ASP D 95 12959 12233 14079 597 -1342 -1019 C ATOM 2417 C ASP D 95 -64.929 21.785 -15.966 1.00103.27 C ANISOU 2417 C ASP D 95 12679 12445 14115 472 -1493 -1282 C ATOM 2418 O ASP D 95 -65.987 21.169 -15.895 1.00103.86 O ANISOU 2418 O ASP D 95 12733 12503 14227 396 -1486 -1482 O ATOM 2419 CB ASP D 95 -63.105 20.226 -16.659 1.00103.82 C ANISOU 2419 CB ASP D 95 13033 12286 14128 618 -988 -678 C ATOM 2420 CG ASP D 95 -62.174 19.798 -17.790 1.00104.34 C ANISOU 2420 CG ASP D 95 13408 12061 14174 759 -754 -407 C ATOM 2421 OD1 ASP D 95 -62.272 20.412 -18.880 1.00104.37 O ANISOU 2421 OD1 ASP D 95 13638 11891 14127 835 -896 -524 O ATOM 2422 OD2 ASP D 95 -61.343 18.861 -17.606 1.00105.11 O ANISOU 2422 OD2 ASP D 95 13533 12101 14305 830 -390 -40 O ATOM 2423 N ASP D 96 -64.624 22.776 -15.139 1.00 86.41 N ANISOU 2423 N ASP D 96 10341 10495 11994 433 -1600 -1310 N ATOM 2424 CA ASP D 96 -65.501 23.124 -14.034 1.00 86.76 C ANISOU 2424 CA ASP D 96 10174 10736 12056 327 -1675 -1551 C ATOM 2425 C ASP D 96 -66.192 24.396 -14.389 1.00 86.92 C ANISOU 2425 C ASP D 96 10178 10659 12187 345 -1866 -1809 C ATOM 2426 O ASP D 96 -65.593 25.240 -15.042 1.00 86.86 O ANISOU 2426 O ASP D 96 10254 10522 12227 418 -1917 -1754 O ATOM 2427 CB ASP D 96 -64.705 23.312 -12.750 1.00 87.39 C ANISOU 2427 CB ASP D 96 10058 11129 12017 248 -1628 -1442 C ATOM 2428 CG ASP D 96 -63.807 22.124 -12.438 1.00 87.83 C ANISOU 2428 CG ASP D 96 10086 11323 11961 305 -1410 -1051 C ATOM 2429 OD1 ASP D 96 -64.255 20.971 -12.725 1.00 87.82 O ANISOU 2429 OD1 ASP D 96 10191 11177 12001 361 -1204 -961 O ATOM 2430 OD2 ASP D 96 -62.647 22.352 -11.935 1.00 88.70 O ANISOU 2430 OD2 ASP D 96 10050 11681 11972 290 -1424 -827 O ATOM 2431 N LEU D 97 -67.448 24.535 -13.953 1.00 76.02 N ANISOU 2431 N LEU D 97 8677 9318 10888 305 -1917 -2048 N ATOM 2432 CA LEU D 97 -68.317 25.639 -14.399 1.00 76.75 C ANISOU 2432 CA LEU D 97 8732 9299 11130 381 -2053 -2236 C ATOM 2433 C LEU D 97 -68.382 26.804 -13.432 1.00 77.56 C ANISOU 2433 C LEU D 97 8714 9446 11309 318 -1996 -2400 C ATOM 2434 O LEU D 97 -69.178 26.803 -12.500 1.00 78.37 O ANISOU 2434 O LEU D 97 8685 9643 11448 249 -1927 -2559 O ATOM 2435 CB LEU D 97 -69.747 25.147 -14.638 1.00 77.70 C ANISOU 2435 CB LEU D 97 8749 9418 11357 389 -2133 -2382 C ATOM 2436 CG LEU D 97 -70.701 26.257 -15.077 1.00 79.12 C ANISOU 2436 CG LEU D 97 8823 9535 11705 520 -2262 -2492 C ATOM 2437 CD1 LEU D 97 -70.209 26.838 -16.402 1.00 79.33 C ANISOU 2437 CD1 LEU D 97 9029 9444 11670 711 -2381 -2348 C ATOM 2438 CD2 LEU D 97 -72.120 25.710 -15.162 1.00 80.71 C ANISOU 2438 CD2 LEU D 97 8819 9802 12044 495 -2359 -2623 C ATOM 2439 N SER D 98 -67.577 27.821 -13.673 1.00 94.10 N ANISOU 2439 N SER D 98 10867 11432 13454 334 -1977 -2381 N ATOM 2440 CA SER D 98 -67.598 28.997 -12.813 1.00 95.62 C ANISOU 2440 CA SER D 98 10982 11606 13742 226 -1871 -2606 C ATOM 2441 C SER D 98 -69.026 29.503 -12.782 1.00 96.80 C ANISOU 2441 C SER D 98 11054 11646 14079 331 -1828 -2757 C ATOM 2442 O SER D 98 -69.627 29.605 -13.828 1.00 96.95 O ANISOU 2442 O SER D 98 11084 11538 14214 533 -1914 -2650 O ATOM 2443 CB SER D 98 -66.653 30.095 -13.367 1.00 96.36 C ANISOU 2443 CB SER D 98 11148 11483 13980 244 -1803 -2575 C ATOM 2444 OG SER D 98 -65.263 29.925 -13.004 1.00 96.34 O ANISOU 2444 OG SER D 98 11119 11619 13866 71 -1808 -2498 O ATOM 2445 N PHE D 99 -69.576 29.786 -11.605 1.00 92.22 N ANISOU 2445 N PHE D 99 10389 11142 13509 212 -1690 -2977 N ATOM 2446 CA PHE D 99 -70.886 30.474 -11.531 1.00 93.98 C ANISOU 2446 CA PHE D 99 10518 11206 13985 334 -1566 -3089 C ATOM 2447 C PHE D 99 -71.037 31.593 -10.466 1.00 96.47 C ANISOU 2447 C PHE D 99 10854 11412 14390 216 -1277 -3371 C ATOM 2448 O PHE D 99 -70.268 31.715 -9.509 1.00 97.19 O ANISOU 2448 O PHE D 99 11015 11643 14270 -22 -1209 -3563 O ATOM 2449 CB PHE D 99 -72.015 29.477 -11.337 1.00 93.84 C ANISOU 2449 CB PHE D 99 10352 11313 13991 376 -1619 -3060 C ATOM 2450 CG PHE D 99 -71.913 28.745 -10.098 1.00 93.78 C ANISOU 2450 CG PHE D 99 10334 11514 13785 211 -1512 -3146 C ATOM 2451 CD1 PHE D 99 -72.129 29.368 -8.913 1.00 95.71 C ANISOU 2451 CD1 PHE D 99 10593 11775 13996 120 -1281 -3359 C ATOM 2452 CD2 PHE D 99 -71.586 27.431 -10.102 1.00 92.34 C ANISOU 2452 CD2 PHE D 99 10150 11502 13431 167 -1592 -3001 C ATOM 2453 CE1 PHE D 99 -72.025 28.682 -7.748 1.00 96.21 C ANISOU 2453 CE1 PHE D 99 10667 12085 13803 12 -1174 -3405 C ATOM 2454 CE2 PHE D 99 -71.496 26.742 -8.937 1.00 92.80 C ANISOU 2454 CE2 PHE D 99 10192 11771 13297 78 -1443 -3009 C ATOM 2455 CZ PHE D 99 -71.707 27.368 -7.759 1.00 94.75 C ANISOU 2455 CZ PHE D 99 10451 12095 13455 12 -1256 -3199 C ATOM 2456 N GLN D 100 -72.075 32.389 -10.633 1.00125.55 N ANISOU 2456 N GLN D 100 14467 14862 18373 387 -1096 -3394 N ATOM 2457 CA GLN D 100 -72.295 33.521 -9.785 1.00128.48 C ANISOU 2457 CA GLN D 100 14901 15027 18888 305 -732 -3658 C ATOM 2458 C GLN D 100 -73.460 33.228 -8.883 1.00129.82 C ANISOU 2458 C GLN D 100 14977 15251 19098 326 -563 -3746 C ATOM 2459 O GLN D 100 -74.441 32.617 -9.303 1.00129.35 O ANISOU 2459 O GLN D 100 14723 15242 19184 510 -673 -3547 O ATOM 2460 CB GLN D 100 -72.635 34.708 -10.658 1.00130.40 C ANISOU 2460 CB GLN D 100 15134 14897 19513 552 -525 -3541 C ATOM 2461 CG GLN D 100 -71.451 35.399 -11.189 1.00130.52 C ANISOU 2461 CG GLN D 100 15289 14732 19569 491 -477 -3551 C ATOM 2462 CD GLN D 100 -71.233 36.692 -10.461 1.00134.07 C ANISOU 2462 CD GLN D 100 15862 14855 20225 317 -20 -3884 C ATOM 2463 OE1 GLN D 100 -70.255 36.829 -9.700 1.00134.79 O ANISOU 2463 OE1 GLN D 100 16058 15029 20129 -50 1 -4208 O ATOM 2464 NE2 GLN D 100 -72.166 37.661 -10.655 1.00137.03 N ANISOU 2464 NE2 GLN D 100 16209 14864 20992 570 376 -3817 N ATOM 2465 N LYS D 101 -73.380 33.704 -7.652 1.00112.38 N ANISOU 2465 N LYS D 101 12900 13026 16773 129 -276 -4062 N ATOM 2466 CA LYS D 101 -74.477 33.558 -6.690 1.00114.35 C ANISOU 2466 CA LYS D 101 13109 13271 17068 169 -8 -4153 C ATOM 2467 C LYS D 101 -75.771 34.067 -7.296 1.00115.92 C ANISOU 2467 C LYS D 101 13113 13173 17759 479 182 -3952 C ATOM 2468 O LYS D 101 -75.807 35.150 -7.870 1.00117.59 O ANISOU 2468 O LYS D 101 13344 13074 18259 610 371 -3915 O ATOM 2469 CB LYS D 101 -74.118 34.290 -5.391 1.00117.62 C ANISOU 2469 CB LYS D 101 13772 13657 17262 -86 329 -4573 C ATOM 2470 CG LYS D 101 -75.216 34.888 -4.586 1.00121.24 C ANISOU 2470 CG LYS D 101 14289 13863 17914 -7 820 -4726 C ATOM 2471 CD LYS D 101 -74.708 35.260 -3.180 1.00124.58 C ANISOU 2471 CD LYS D 101 15015 14409 17911 -321 1066 -5193 C ATOM 2472 CE LYS D 101 -75.108 36.703 -2.788 1.00129.33 C ANISOU 2472 CE LYS D 101 15828 14523 18790 -369 1653 -5524 C ATOM 2473 NZ LYS D 101 -75.096 37.038 -1.310 1.00133.86 N ANISOU 2473 NZ LYS D 101 16726 15166 18970 -624 2014 -6005 N ATOM 2474 N GLY D 102 -76.821 33.257 -7.188 1.00118.75 N ANISOU 2474 N GLY D 102 13245 13635 18238 609 145 -3788 N ATOM 2475 CA GLY D 102 -78.130 33.597 -7.725 1.00120.82 C ANISOU 2475 CA GLY D 102 13218 13712 18975 904 270 -3551 C ATOM 2476 C GLY D 102 -78.364 32.986 -9.086 1.00119.14 C ANISOU 2476 C GLY D 102 12738 13667 18862 1062 -192 -3249 C ATOM 2477 O GLY D 102 -79.496 32.974 -9.587 1.00121.08 O ANISOU 2477 O GLY D 102 12646 13909 19449 1285 -226 -3025 O ATOM 2478 N ASP D 103 -77.308 32.470 -9.698 1.00119.06 N ANISOU 2478 N ASP D 103 12864 13828 18546 944 -548 -3242 N ATOM 2479 CA ASP D 103 -77.462 31.846 -10.991 1.00117.91 C ANISOU 2479 CA ASP D 103 12541 13851 18410 1064 -974 -3012 C ATOM 2480 C ASP D 103 -78.301 30.563 -10.910 1.00117.83 C ANISOU 2480 C ASP D 103 12267 14046 18455 995 -1153 -2985 C ATOM 2481 O ASP D 103 -78.302 29.829 -9.902 1.00117.19 O ANISOU 2481 O ASP D 103 12229 14020 18278 821 -1005 -3116 O ATOM 2482 CB ASP D 103 -76.098 31.543 -11.612 1.00114.98 C ANISOU 2482 CB ASP D 103 12417 13566 17702 955 -1232 -3009 C ATOM 2483 CG ASP D 103 -75.403 32.775 -12.115 1.00115.66 C ANISOU 2483 CG ASP D 103 12674 13426 17845 1072 -1100 -2964 C ATOM 2484 OD1 ASP D 103 -76.063 33.826 -12.122 1.00118.54 O ANISOU 2484 OD1 ASP D 103 12953 13567 18520 1273 -818 -2901 O ATOM 2485 OD2 ASP D 103 -74.213 32.697 -12.515 1.00113.72 O ANISOU 2485 OD2 ASP D 103 12631 13194 17382 982 -1225 -2960 O ATOM 2486 N GLN D 104 -79.021 30.312 -11.995 1.00112.83 N ANISOU 2486 N GLN D 104 11352 13538 17980 1138 -1458 -2810 N ATOM 2487 CA GLN D 104 -79.794 29.091 -12.130 1.00113.44 C ANISOU 2487 CA GLN D 104 11146 13800 18156 1021 -1665 -2829 C ATOM 2488 C GLN D 104 -79.061 28.155 -13.056 1.00111.34 C ANISOU 2488 C GLN D 104 11023 13700 17579 886 -2041 -2856 C ATOM 2489 O GLN D 104 -78.640 28.541 -14.154 1.00111.24 O ANISOU 2489 O GLN D 104 11108 13751 17408 1018 -2294 -2745 O ATOM 2490 CB GLN D 104 -81.196 29.380 -12.674 1.00117.50 C ANISOU 2490 CB GLN D 104 11180 14400 19064 1218 -1778 -2662 C ATOM 2491 CG GLN D 104 -82.183 29.727 -11.608 1.00120.01 C ANISOU 2491 CG GLN D 104 11268 14554 19775 1284 -1360 -2645 C ATOM 2492 CD GLN D 104 -83.442 30.233 -12.199 1.00124.45 C ANISOU 2492 CD GLN D 104 11330 15206 20750 1540 -1448 -2395 C ATOM 2493 OE1 GLN D 104 -83.429 31.250 -12.904 1.00126.00 O ANISOU 2493 OE1 GLN D 104 11502 15400 20974 1826 -1489 -2172 O ATOM 2494 NE2 GLN D 104 -84.558 29.552 -11.920 1.00127.11 N ANISOU 2494 NE2 GLN D 104 11224 15624 21448 1464 -1446 -2390 N ATOM 2495 N MET D 105 -78.909 26.925 -12.603 1.00105.96 N ANISOU 2495 N MET D 105 10378 13061 16820 650 -2010 -2980 N ATOM 2496 CA MET D 105 -78.296 25.903 -13.416 1.00104.55 C ANISOU 2496 CA MET D 105 10346 12982 16398 503 -2267 -3020 C ATOM 2497 C MET D 105 -79.192 24.682 -13.456 1.00106.55 C ANISOU 2497 C MET D 105 10319 13295 16872 307 -2317 -3143 C ATOM 2498 O MET D 105 -80.030 24.475 -12.575 1.00108.12 O ANISOU 2498 O MET D 105 10267 13431 17384 265 -2070 -3178 O ATOM 2499 CB MET D 105 -76.922 25.533 -12.864 1.00101.24 C ANISOU 2499 CB MET D 105 10304 12505 15658 398 -2095 -3022 C ATOM 2500 CG MET D 105 -75.917 26.677 -12.819 1.00 99.70 C ANISOU 2500 CG MET D 105 10364 12245 15274 515 -2045 -2953 C ATOM 2501 SD MET D 105 -74.499 26.196 -11.763 1.00 97.10 S ANISOU 2501 SD MET D 105 10322 11951 14620 355 -1825 -2957 S ATOM 2502 CE MET D 105 -75.013 26.825 -10.188 1.00 98.62 C ANISOU 2502 CE MET D 105 10444 12129 14899 340 -1482 -3083 C ATOM 2503 N VAL D 106 -79.016 23.910 -14.521 1.00111.81 N ANISOU 2503 N VAL D 106 11038 14056 17388 182 -2607 -3223 N ATOM 2504 CA VAL D 106 -79.651 22.622 -14.690 1.00114.01 C ANISOU 2504 CA VAL D 106 11120 14348 17851 -87 -2634 -3416 C ATOM 2505 C VAL D 106 -78.652 21.565 -14.330 1.00111.56 C ANISOU 2505 C VAL D 106 11151 13879 17358 -247 -2359 -3443 C ATOM 2506 O VAL D 106 -77.571 21.552 -14.881 1.00109.42 O ANISOU 2506 O VAL D 106 11235 13598 16740 -209 -2434 -3377 O ATOM 2507 CB VAL D 106 -80.003 22.395 -16.149 1.00116.87 C ANISOU 2507 CB VAL D 106 11387 14923 18096 -161 -3110 -3541 C ATOM 2508 CG1 VAL D 106 -80.412 20.954 -16.360 1.00119.31 C ANISOU 2508 CG1 VAL D 106 11588 15189 18556 -529 -3089 -3829 C ATOM 2509 CG2 VAL D 106 -81.101 23.344 -16.568 1.00120.39 C ANISOU 2509 CG2 VAL D 106 11400 15606 18736 29 -3408 -3449 C ATOM 2510 N VAL D 107 -78.980 20.665 -13.426 1.00106.14 N ANISOU 2510 N VAL D 107 10356 13054 16919 -392 -1993 -3492 N ATOM 2511 CA VAL D 107 -78.028 19.610 -13.145 1.00104.47 C ANISOU 2511 CA VAL D 107 10451 12697 16548 -493 -1683 -3445 C ATOM 2512 C VAL D 107 -78.138 18.609 -14.276 1.00106.65 C ANISOU 2512 C VAL D 107 10766 12914 16841 -741 -1828 -3668 C ATOM 2513 O VAL D 107 -79.232 18.332 -14.759 1.00110.32 O ANISOU 2513 O VAL D 107 10903 13426 17588 -928 -2017 -3911 O ATOM 2514 CB VAL D 107 -78.292 18.901 -11.821 1.00105.05 C ANISOU 2514 CB VAL D 107 10425 12629 16862 -519 -1166 -3369 C ATOM 2515 CG1 VAL D 107 -77.162 17.930 -11.512 1.00103.50 C ANISOU 2515 CG1 VAL D 107 10551 12322 16453 -529 -815 -3202 C ATOM 2516 CG2 VAL D 107 -78.427 19.900 -10.708 1.00104.15 C ANISOU 2516 CG2 VAL D 107 10257 12592 16725 -309 -1030 -3231 C ATOM 2517 N LEU D 108 -77.009 18.086 -14.720 1.00122.06 N ANISOU 2517 N LEU D 108 13110 14773 18493 -758 -1738 -3600 N ATOM 2518 CA LEU D 108 -76.996 17.072 -15.747 1.00124.46 C ANISOU 2518 CA LEU D 108 13550 14963 18776 -1009 -1774 -3841 C ATOM 2519 C LEU D 108 -76.525 15.742 -15.190 1.00124.75 C ANISOU 2519 C LEU D 108 13750 14691 18957 -1134 -1183 -3783 C ATOM 2520 O LEU D 108 -76.979 14.686 -15.640 1.00128.21 O ANISOU 2520 O LEU D 108 14161 14934 19620 -1432 -1025 -4067 O ATOM 2521 CB LEU D 108 -76.088 17.521 -16.878 1.00123.08 C ANISOU 2521 CB LEU D 108 13741 14874 18151 -897 -2076 -3789 C ATOM 2522 CG LEU D 108 -76.494 18.850 -17.504 1.00123.30 C ANISOU 2522 CG LEU D 108 13631 15190 18026 -708 -2596 -3775 C ATOM 2523 CD1 LEU D 108 -75.574 19.171 -18.661 1.00122.50 C ANISOU 2523 CD1 LEU D 108 13926 15131 17486 -576 -2811 -3699 C ATOM 2524 CD2 LEU D 108 -77.920 18.819 -17.959 1.00127.79 C ANISOU 2524 CD2 LEU D 108 13774 15951 18828 -878 -2931 -4059 C ATOM 2525 N GLU D 109 -75.607 15.790 -14.226 1.00144.74 N ANISOU 2525 N GLU D 109 16442 17191 21362 -909 -841 -3415 N ATOM 2526 CA GLU D 109 -75.066 14.588 -13.598 1.00145.23 C ANISOU 2526 CA GLU D 109 16644 17001 21536 -921 -222 -3223 C ATOM 2527 C GLU D 109 -74.901 14.797 -12.097 1.00143.85 C ANISOU 2527 C GLU D 109 16353 16933 21371 -686 92 -2886 C ATOM 2528 O GLU D 109 -74.140 15.671 -11.681 1.00141.05 O ANISOU 2528 O GLU D 109 16092 16817 20685 -467 -70 -2653 O ATOM 2529 CB GLU D 109 -73.707 14.247 -14.209 1.00143.70 C ANISOU 2529 CB GLU D 109 16864 16714 21020 -838 -108 -3017 C ATOM 2530 CG GLU D 109 -73.102 12.947 -13.683 1.00144.88 C ANISOU 2530 CG GLU D 109 17161 16581 21307 -809 593 -2752 C ATOM 2531 CD GLU D 109 -71.583 12.893 -13.820 1.00142.74 C ANISOU 2531 CD GLU D 109 17208 16320 20706 -581 748 -2336 C ATOM 2532 OE1 GLU D 109 -70.894 13.308 -12.854 1.00140.73 O ANISOU 2532 OE1 GLU D 109 16889 16311 20272 -320 813 -1936 O ATOM 2533 OE2 GLU D 109 -71.081 12.438 -14.883 1.00143.56 O ANISOU 2533 OE2 GLU D 109 17615 16205 20724 -669 808 -2415 O ATOM 2534 N GLU D 110 -75.590 13.978 -11.297 1.00139.30 N ANISOU 2534 N GLU D 110 15584 16179 21164 -740 563 -2874 N ATOM 2535 CA GLU D 110 -75.508 14.050 -9.829 1.00138.95 C ANISOU 2535 CA GLU D 110 15455 16249 21090 -493 926 -2544 C ATOM 2536 C GLU D 110 -74.577 12.973 -9.254 1.00139.56 C ANISOU 2536 C GLU D 110 15720 16215 21092 -328 1533 -2130 C ATOM 2537 O GLU D 110 -74.765 12.529 -8.110 1.00141.18 O ANISOU 2537 O GLU D 110 15827 16418 21398 -157 2015 -1869 O ATOM 2538 CB GLU D 110 -76.882 13.830 -9.177 1.00141.94 C ANISOU 2538 CB GLU D 110 15488 16496 21946 -573 1168 -2695 C ATOM 2539 CG GLU D 110 -78.036 14.703 -9.629 1.00142.71 C ANISOU 2539 CG GLU D 110 15286 16676 22263 -717 691 -3044 C ATOM 2540 CD GLU D 110 -79.388 14.134 -9.149 1.00146.74 C ANISOU 2540 CD GLU D 110 15411 16959 23385 -855 1035 -3188 C ATOM 2541 OE1 GLU D 110 -80.071 14.789 -8.328 1.00147.21 O ANISOU 2541 OE1 GLU D 110 15259 17106 23567 -711 1083 -3125 O ATOM 2542 OE2 GLU D 110 -79.763 13.013 -9.576 1.00149.90 O ANISOU 2542 OE2 GLU D 110 15723 17056 24175 -1118 1312 -3373 O ATOM 2543 N SER D 111 -73.576 12.546 -10.011 1.00136.72 N ANISOU 2543 N SER D 111 15628 15765 20556 -335 1565 -2015 N ATOM 2544 CA SER D 111 -72.864 11.344 -9.610 1.00138.43 C ANISOU 2544 CA SER D 111 15981 15784 20833 -188 2244 -1612 C ATOM 2545 C SER D 111 -72.244 11.484 -8.215 1.00138.07 C ANISOU 2545 C SER D 111 15881 16086 20493 186 2488 -1083 C ATOM 2546 O SER D 111 -72.510 10.666 -7.321 1.00140.84 O ANISOU 2546 O SER D 111 16143 16329 21040 340 3096 -813 O ATOM 2547 CB SER D 111 -71.828 10.931 -10.658 1.00137.83 C ANISOU 2547 CB SER D 111 16216 15542 20610 -220 2274 -1531 C ATOM 2548 OG SER D 111 -72.379 9.954 -11.530 1.00140.90 O ANISOU 2548 OG SER D 111 16697 15457 21383 -529 2562 -1881 O ATOM 2549 N GLY D 112 -71.458 12.540 -8.024 1.00159.74 N ANISOU 2549 N GLY D 112 18668 19261 22765 323 2020 -955 N ATOM 2550 CA GLY D 112 -70.691 12.708 -6.783 1.00160.04 C ANISOU 2550 CA GLY D 112 18662 19736 22409 643 2155 -480 C ATOM 2551 C GLY D 112 -71.144 13.873 -5.914 1.00159.35 C ANISOU 2551 C GLY D 112 18451 20021 22075 675 1803 -646 C ATOM 2552 O GLY D 112 -72.334 14.236 -5.909 1.00159.65 O ANISOU 2552 O GLY D 112 18374 19901 22383 530 1713 -1015 O ATOM 2553 N GLU D 113 -70.192 14.421 -5.142 1.00131.55 N ANISOU 2553 N GLU D 113 14937 16999 18047 862 1642 -366 N ATOM 2554 CA GLU D 113 -70.369 15.698 -4.448 1.00131.03 C ANISOU 2554 CA GLU D 113 14826 17296 17663 838 1252 -593 C ATOM 2555 C GLU D 113 -70.205 16.792 -5.476 1.00128.01 C ANISOU 2555 C GLU D 113 14501 16845 17291 616 683 -962 C ATOM 2556 O GLU D 113 -70.654 17.891 -5.259 1.00127.48 O ANISOU 2556 O GLU D 113 14409 16870 17155 529 396 -1274 O ATOM 2557 CB GLU D 113 -69.332 15.874 -3.332 1.00132.76 C ANISOU 2557 CB GLU D 113 15026 18114 17302 1055 1245 -219 C ATOM 2558 CG GLU D 113 -69.396 14.836 -2.205 1.00136.50 C ANISOU 2558 CG GLU D 113 15446 18762 17658 1371 1830 255 C ATOM 2559 CD GLU D 113 -69.851 15.425 -0.850 1.00139.04 C ANISOU 2559 CD GLU D 113 15753 19482 17592 1484 1848 186 C ATOM 2560 OE1 GLU D 113 -69.397 14.883 0.203 1.00142.58 O ANISOU 2560 OE1 GLU D 113 16170 20361 17642 1796 2153 656 O ATOM 2561 OE2 GLU D 113 -70.647 16.414 -0.828 1.00138.01 O ANISOU 2561 OE2 GLU D 113 15655 19249 17534 1292 1595 -304 O ATOM 2562 N TRP D 114 -69.529 16.479 -6.580 1.00 96.35 N ANISOU 2562 N TRP D 114 10589 12653 13366 559 589 -889 N ATOM 2563 CA TRP D 114 -69.397 17.396 -7.707 1.00 93.87 C ANISOU 2563 CA TRP D 114 10356 12219 13093 396 121 -1187 C ATOM 2564 C TRP D 114 -70.350 16.947 -8.786 1.00 93.76 C ANISOU 2564 C TRP D 114 10371 11775 13479 242 135 -1466 C ATOM 2565 O TRP D 114 -70.446 15.762 -9.076 1.00 95.07 O ANISOU 2565 O TRP D 114 10582 11686 13853 229 498 -1357 O ATOM 2566 CB TRP D 114 -67.968 17.405 -8.275 1.00 92.75 C ANISOU 2566 CB TRP D 114 10320 12172 12750 448 7 -914 C ATOM 2567 CG TRP D 114 -66.995 18.160 -7.444 1.00 93.11 C ANISOU 2567 CG TRP D 114 10281 12689 12409 511 -188 -753 C ATOM 2568 CD1 TRP D 114 -66.395 17.730 -6.323 1.00 95.36 C ANISOU 2568 CD1 TRP D 114 10452 13380 12398 672 5 -387 C ATOM 2569 CD2 TRP D 114 -66.522 19.473 -7.678 1.00 91.93 C ANISOU 2569 CD2 TRP D 114 10132 12669 12127 396 -607 -969 C ATOM 2570 NE1 TRP D 114 -65.588 18.693 -5.828 1.00 95.85 N ANISOU 2570 NE1 TRP D 114 10429 13867 12121 621 -327 -411 N ATOM 2571 CE2 TRP D 114 -65.649 19.785 -6.645 1.00 93.71 C ANISOU 2571 CE2 TRP D 114 10231 13390 11983 432 -678 -788 C ATOM 2572 CE3 TRP D 114 -66.762 20.419 -8.659 1.00 90.09 C ANISOU 2572 CE3 TRP D 114 9985 12187 12056 275 -904 -1288 C ATOM 2573 CZ2 TRP D 114 -65.003 21.017 -6.552 1.00 93.78 C ANISOU 2573 CZ2 TRP D 114 10194 13612 11826 286 -1028 -986 C ATOM 2574 CZ3 TRP D 114 -66.104 21.647 -8.575 1.00 89.92 C ANISOU 2574 CZ3 TRP D 114 9936 12333 11897 189 -1187 -1418 C ATOM 2575 CH2 TRP D 114 -65.245 21.931 -7.524 1.00 91.78 C ANISOU 2575 CH2 TRP D 114 10042 13019 11812 163 -1240 -1302 C ATOM 2576 N TRP D 115 -71.048 17.904 -9.378 1.00111.00 N ANISOU 2576 N TRP D 115 12516 13892 15765 123 -246 -1826 N ATOM 2577 CA TRP D 115 -72.127 17.626 -10.313 1.00111.81 C ANISOU 2577 CA TRP D 115 12565 13712 16207 -36 -333 -2133 C ATOM 2578 C TRP D 115 -71.887 18.357 -11.613 1.00110.43 C ANISOU 2578 C TRP D 115 12512 13494 15950 -84 -764 -2292 C ATOM 2579 O TRP D 115 -71.366 19.473 -11.612 1.00108.89 O ANISOU 2579 O TRP D 115 12359 13453 15560 -4 -1021 -2267 O ATOM 2580 CB TRP D 115 -73.462 18.136 -9.770 1.00113.11 C ANISOU 2580 CB TRP D 115 12481 13886 16609 -75 -376 -2369 C ATOM 2581 CG TRP D 115 -73.922 17.537 -8.495 1.00114.99 C ANISOU 2581 CG TRP D 115 12593 14140 16957 -3 68 -2240 C ATOM 2582 CD1 TRP D 115 -73.485 16.394 -7.919 1.00116.19 C ANISOU 2582 CD1 TRP D 115 12799 14253 17096 83 537 -1948 C ATOM 2583 CD2 TRP D 115 -74.947 18.051 -7.646 1.00116.40 C ANISOU 2583 CD2 TRP D 115 12578 14354 17294 33 151 -2357 C ATOM 2584 NE1 TRP D 115 -74.158 16.170 -6.749 1.00118.27 N ANISOU 2584 NE1 TRP D 115 12923 14548 17467 184 897 -1869 N ATOM 2585 CE2 TRP D 115 -75.070 17.170 -6.564 1.00118.39 C ANISOU 2585 CE2 TRP D 115 12794 14598 17591 143 669 -2133 C ATOM 2586 CE3 TRP D 115 -75.766 19.182 -7.694 1.00116.54 C ANISOU 2586 CE3 TRP D 115 12457 14392 17433 18 -107 -2588 C ATOM 2587 CZ2 TRP D 115 -75.966 17.378 -5.535 1.00120.41 C ANISOU 2587 CZ2 TRP D 115 12907 14863 17982 229 926 -2155 C ATOM 2588 CZ3 TRP D 115 -76.664 19.387 -6.677 1.00118.54 C ANISOU 2588 CZ3 TRP D 115 12554 14633 17854 90 160 -2612 C ATOM 2589 CH2 TRP D 115 -76.758 18.489 -5.607 1.00120.41 C ANISOU 2589 CH2 TRP D 115 12784 14859 18107 190 667 -2410 C ATOM 2590 N LYS D 116 -72.303 17.747 -12.717 1.00102.70 N ANISOU 2590 N LYS D 116 11595 12305 15120 -221 -821 -2474 N ATOM 2591 CA LYS D 116 -72.198 18.400 -13.999 1.00102.16 C ANISOU 2591 CA LYS D 116 11656 12231 14930 -230 -1224 -2614 C ATOM 2592 C LYS D 116 -73.446 19.193 -14.187 1.00103.38 C ANISOU 2592 C LYS D 116 11553 12474 15253 -265 -1545 -2873 C ATOM 2593 O LYS D 116 -74.517 18.707 -13.881 1.00105.55 O ANISOU 2593 O LYS D 116 11584 12703 15816 -393 -1454 -3043 O ATOM 2594 CB LYS D 116 -72.063 17.394 -15.105 1.00103.67 C ANISOU 2594 CB LYS D 116 12062 12208 15119 -364 -1148 -2717 C ATOM 2595 CG LYS D 116 -71.688 18.027 -16.403 1.00103.29 C ANISOU 2595 CG LYS D 116 12231 12183 14830 -306 -1507 -2775 C ATOM 2596 CD LYS D 116 -70.742 17.104 -17.156 1.00103.70 C ANISOU 2596 CD LYS D 116 12653 12010 14739 -329 -1251 -2671 C ATOM 2597 CE LYS D 116 -70.712 17.375 -18.664 1.00104.98 C ANISOU 2597 CE LYS D 116 13074 12152 14660 -330 -1563 -2842 C ATOM 2598 NZ LYS D 116 -70.009 16.283 -19.422 1.00106.46 N ANISOU 2598 NZ LYS D 116 13658 12054 14739 -406 -1229 -2828 N ATOM 2599 N ALA D 117 -73.325 20.416 -14.674 1.00 99.13 N ANISOU 2599 N ALA D 117 11037 12045 14582 -133 -1873 -2870 N ATOM 2600 CA ALA D 117 -74.489 21.254 -14.863 1.00100.74 C ANISOU 2600 CA ALA D 117 10970 12345 14961 -99 -2141 -3029 C ATOM 2601 C ALA D 117 -74.321 22.170 -16.043 1.00100.88 C ANISOU 2601 C ALA D 117 11093 12432 14806 50 -2494 -3008 C ATOM 2602 O ALA D 117 -73.249 22.281 -16.615 1.00 99.39 O ANISOU 2602 O ALA D 117 11203 12192 14369 132 -2508 -2873 O ATOM 2603 CB ALA D 117 -74.739 22.045 -13.656 1.00100.16 C ANISOU 2603 CB ALA D 117 10737 12323 14995 -9 -1998 -2976 C ATOM 2604 N ARG D 118 -75.424 22.796 -16.414 1.00117.68 N ANISOU 2604 N ARG D 118 12948 14680 17086 113 -2747 -3100 N ATOM 2605 CA ARG D 118 -75.470 23.728 -17.517 1.00118.79 C ANISOU 2605 CA ARG D 118 13127 14931 17077 324 -3063 -3023 C ATOM 2606 C ARG D 118 -76.074 25.020 -17.001 1.00119.41 C ANISOU 2606 C ARG D 118 12957 15040 17373 527 -3043 -2924 C ATOM 2607 O ARG D 118 -76.980 25.013 -16.162 1.00120.55 O ANISOU 2607 O ARG D 118 12798 15190 17813 468 -2925 -2996 O ATOM 2608 CB ARG D 118 -76.329 23.189 -18.661 1.00122.57 C ANISOU 2608 CB ARG D 118 13471 15599 17499 235 -3421 -3198 C ATOM 2609 CG ARG D 118 -76.319 24.133 -19.853 1.00124.30 C ANISOU 2609 CG ARG D 118 13758 15998 17473 522 -3746 -3051 C ATOM 2610 CD ARG D 118 -76.956 23.545 -21.104 1.00128.65 C ANISOU 2610 CD ARG D 118 14253 16825 17801 427 -4155 -3238 C ATOM 2611 NE ARG D 118 -78.380 23.215 -20.924 1.00132.51 N ANISOU 2611 NE ARG D 118 14222 17536 18588 246 -4365 -3441 N ATOM 2612 CZ ARG D 118 -78.868 21.987 -20.735 1.00134.27 C ANISOU 2612 CZ ARG D 118 14312 17727 18976 -149 -4336 -3774 C ATOM 2613 NH1 ARG D 118 -78.064 20.912 -20.704 1.00132.58 N ANISOU 2613 NH1 ARG D 118 14475 17254 18645 -391 -4071 -3933 N ATOM 2614 NH2 ARG D 118 -80.181 21.827 -20.589 1.00138.27 N ANISOU 2614 NH2 ARG D 118 14280 18439 19816 -298 -4528 -3930 N ATOM 2615 N SER D 119 -75.583 26.131 -17.527 1.00117.51 N ANISOU 2615 N SER D 119 12855 14774 17017 782 -3095 -2745 N ATOM 2616 CA SER D 119 -76.040 27.435 -17.091 1.00118.48 C ANISOU 2616 CA SER D 119 12802 14846 17371 996 -2973 -2634 C ATOM 2617 C SER D 119 -77.158 27.889 -17.967 1.00122.40 C ANISOU 2617 C SER D 119 12996 15548 17963 1212 -3249 -2531 C ATOM 2618 O SER D 119 -76.953 28.075 -19.163 1.00123.78 O ANISOU 2618 O SER D 119 13285 15851 17893 1392 -3497 -2403 O ATOM 2619 CB SER D 119 -74.913 28.462 -17.184 1.00116.84 C ANISOU 2619 CB SER D 119 12880 14451 17063 1162 -2799 -2482 C ATOM 2620 OG SER D 119 -75.437 29.761 -17.449 1.00119.24 O ANISOU 2620 OG SER D 119 13045 14700 17559 1460 -2734 -2318 O ATOM 2621 N LEU D 120 -78.314 28.128 -17.358 1.00102.44 N ANISOU 2621 N LEU D 120 10078 13064 15781 1231 -3183 -2545 N ATOM 2622 CA LEU D 120 -79.498 28.549 -18.108 1.00107.03 C ANISOU 2622 CA LEU D 120 10254 13907 16505 1454 -3457 -2394 C ATOM 2623 C LEU D 120 -79.255 29.923 -18.734 1.00108.35 C ANISOU 2623 C LEU D 120 10503 14032 16633 1880 -3392 -2064 C ATOM 2624 O LEU D 120 -79.891 30.313 -19.721 1.00112.33 O ANISOU 2624 O LEU D 120 10775 14821 17084 2163 -3674 -1836 O ATOM 2625 CB LEU D 120 -80.742 28.578 -17.216 1.00109.33 C ANISOU 2625 CB LEU D 120 10084 14199 17256 1411 -3305 -2421 C ATOM 2626 CG LEU D 120 -81.318 27.234 -16.805 1.00109.82 C ANISOU 2626 CG LEU D 120 9931 14338 17456 1043 -3382 -2694 C ATOM 2627 CD1 LEU D 120 -80.378 26.527 -15.882 1.00105.51 C ANISOU 2627 CD1 LEU D 120 9756 13538 16796 790 -3069 -2875 C ATOM 2628 CD2 LEU D 120 -82.621 27.441 -16.111 1.00113.02 C ANISOU 2628 CD2 LEU D 120 9831 14750 18362 1084 -3229 -2640 C ATOM 2629 N ALA D 121 -78.323 30.649 -18.137 1.00127.93 N ANISOU 2629 N ALA D 121 13296 16166 19144 1924 -3001 -2036 N ATOM 2630 CA ALA D 121 -77.906 31.923 -18.654 1.00129.04 C ANISOU 2630 CA ALA D 121 13576 16151 19304 2289 -2814 -1753 C ATOM 2631 C ALA D 121 -76.998 31.711 -19.853 1.00128.35 C ANISOU 2631 C ALA D 121 13808 16152 18806 2391 -3048 -1647 C ATOM 2632 O ALA D 121 -77.359 32.007 -20.992 1.00131.68 O ANISOU 2632 O ALA D 121 14149 16815 19068 2715 -3289 -1387 O ATOM 2633 CB ALA D 121 -77.169 32.695 -17.557 1.00126.83 C ANISOU 2633 CB ALA D 121 13524 15452 19216 2200 -2302 -1857 C ATOM 2634 N THR D 122 -75.830 31.153 -19.570 1.00153.80 N ANISOU 2634 N THR D 122 17385 19210 21844 2127 -2966 -1826 N ATOM 2635 CA THR D 122 -74.691 31.200 -20.466 1.00152.71 C ANISOU 2635 CA THR D 122 17620 18992 21410 2240 -2987 -1696 C ATOM 2636 C THR D 122 -74.699 30.037 -21.432 1.00153.22 C ANISOU 2636 C THR D 122 17797 19341 21080 2153 -3386 -1765 C ATOM 2637 O THR D 122 -73.981 30.060 -22.434 1.00153.55 O ANISOU 2637 O THR D 122 18142 19376 20823 2326 -3443 -1612 O ATOM 2638 CB THR D 122 -73.356 31.142 -19.659 1.00148.76 C ANISOU 2638 CB THR D 122 17405 18187 20930 1988 -2687 -1830 C ATOM 2639 OG1 THR D 122 -73.025 29.784 -19.342 1.00146.32 O ANISOU 2639 OG1 THR D 122 17184 17983 20430 1653 -2824 -2037 O ATOM 2640 CG2 THR D 122 -73.447 31.954 -18.340 1.00148.40 C ANISOU 2640 CG2 THR D 122 17240 17914 21231 1881 -2322 -1956 C ATOM 2641 N ARG D 123 -75.486 29.011 -21.107 1.00146.00 N ANISOU 2641 N ARG D 123 16660 18633 20180 1868 -3606 -2017 N ATOM 2642 CA ARG D 123 -75.490 27.746 -21.844 1.00146.76 C ANISOU 2642 CA ARG D 123 16879 18934 19947 1659 -3913 -2206 C ATOM 2643 C ARG D 123 -74.172 26.986 -21.781 1.00143.20 C ANISOU 2643 C ARG D 123 16861 18247 19303 1464 -3723 -2283 C ATOM 2644 O ARG D 123 -74.032 25.954 -22.443 1.00144.02 O ANISOU 2644 O ARG D 123 17154 18435 19132 1303 -3876 -2433 O ATOM 2645 CB ARG D 123 -75.871 27.963 -23.310 1.00151.11 C ANISOU 2645 CB ARG D 123 17452 19817 20147 1944 -4282 -2055 C ATOM 2646 CG ARG D 123 -77.344 28.265 -23.519 1.00155.92 C ANISOU 2646 CG ARG D 123 17539 20818 20886 2066 -4603 -2010 C ATOM 2647 CD ARG D 123 -78.239 27.056 -23.199 1.00157.42 C ANISOU 2647 CD ARG D 123 17421 21208 21182 1629 -4849 -2398 C ATOM 2648 NE ARG D 123 -78.007 25.932 -24.113 1.00159.07 N ANISOU 2648 NE ARG D 123 17887 21590 20960 1381 -5132 -2677 N ATOM 2649 CZ ARG D 123 -78.889 25.452 -24.984 1.00164.59 C ANISOU 2649 CZ ARG D 123 18354 22754 21427 1280 -5619 -2859 C ATOM 2650 NH1 ARG D 123 -80.111 25.975 -25.089 1.00169.15 N ANISOU 2650 NH1 ARG D 123 18361 23730 22178 1432 -5926 -2736 N ATOM 2651 NH2 ARG D 123 -78.542 24.426 -25.753 1.00166.11 N ANISOU 2651 NH2 ARG D 123 18878 23022 21213 1010 -5786 -3175 N ATOM 2652 N LYS D 124 -73.221 27.481 -20.983 1.00144.10 N ANISOU 2652 N LYS D 124 17112 18073 19567 1463 -3376 -2187 N ATOM 2653 CA LYS D 124 -71.942 26.810 -20.785 1.00141.06 C ANISOU 2653 CA LYS D 124 17048 17494 19056 1299 -3173 -2190 C ATOM 2654 C LYS D 124 -72.113 25.733 -19.723 1.00139.52 C ANISOU 2654 C LYS D 124 16734 17301 18978 958 -3069 -2401 C ATOM 2655 O LYS D 124 -72.796 25.927 -18.722 1.00139.47 O ANISOU 2655 O LYS D 124 16446 17329 19218 871 -3001 -2500 O ATOM 2656 CB LYS D 124 -70.852 27.808 -20.371 1.00139.09 C ANISOU 2656 CB LYS D 124 16921 16999 18928 1415 -2883 -2006 C ATOM 2657 CG LYS D 124 -70.726 29.076 -21.268 1.00141.03 C ANISOU 2657 CG LYS D 124 17249 17157 19179 1796 -2853 -1753 C ATOM 2658 CD LYS D 124 -70.409 28.751 -22.748 1.00142.71 C ANISOU 2658 CD LYS D 124 17766 17431 19027 2015 -3001 -1591 C ATOM 2659 CE LYS D 124 -70.886 29.864 -23.734 1.00146.28 C ANISOU 2659 CE LYS D 124 18198 17956 19425 2468 -3065 -1320 C ATOM 2660 NZ LYS D 124 -69.968 30.133 -24.907 1.00147.35 N ANISOU 2660 NZ LYS D 124 18719 17960 19306 2779 -2950 -1033 N ATOM 2661 N GLU D 125 -71.506 24.579 -19.979 1.00127.20 N ANISOU 2661 N GLU D 125 15406 15679 17244 798 -2999 -2443 N ATOM 2662 CA GLU D 125 -71.549 23.435 -19.056 1.00126.19 C ANISOU 2662 CA GLU D 125 15205 15514 17226 521 -2808 -2573 C ATOM 2663 C GLU D 125 -70.246 23.268 -18.261 1.00123.38 C ANISOU 2663 C GLU D 125 14991 15031 16858 492 -2496 -2382 C ATOM 2664 O GLU D 125 -69.183 23.817 -18.612 1.00122.29 O ANISOU 2664 O GLU D 125 15045 14799 16621 632 -2434 -2178 O ATOM 2665 CB GLU D 125 -71.823 22.133 -19.820 1.00128.17 C ANISOU 2665 CB GLU D 125 15597 15756 17346 341 -2856 -2754 C ATOM 2666 CG GLU D 125 -73.214 22.048 -20.417 1.00131.86 C ANISOU 2666 CG GLU D 125 15822 16436 17842 264 -3200 -3012 C ATOM 2667 CD GLU D 125 -73.408 20.819 -21.305 1.00134.76 C ANISOU 2667 CD GLU D 125 16374 16794 18034 28 -3263 -3277 C ATOM 2668 OE1 GLU D 125 -72.638 19.831 -21.150 1.00133.69 O ANISOU 2668 OE1 GLU D 125 16507 16412 17876 -113 -2917 -3274 O ATOM 2669 OE2 GLU D 125 -74.336 20.843 -22.162 1.00138.70 O ANISOU 2669 OE2 GLU D 125 16741 17545 18415 -18 -3645 -3490 O ATOM 2670 N GLY D 126 -70.330 22.497 -17.189 1.00 92.91 N ANISOU 2670 N GLY D 126 11005 11188 13109 325 -2289 -2419 N ATOM 2671 CA GLY D 126 -69.139 22.143 -16.467 1.00 91.18 C ANISOU 2671 CA GLY D 126 10875 10940 12829 309 -2021 -2198 C ATOM 2672 C GLY D 126 -69.508 21.528 -15.170 1.00 91.25 C ANISOU 2672 C GLY D 126 10684 11042 12945 191 -1816 -2225 C ATOM 2673 O GLY D 126 -70.685 21.375 -14.891 1.00 92.50 O ANISOU 2673 O GLY D 126 10653 11227 13267 113 -1854 -2427 O ATOM 2674 N TYR D 127 -68.500 21.164 -14.385 1.00 92.24 N ANISOU 2674 N TYR D 127 10830 11237 12978 201 -1588 -1984 N ATOM 2675 CA TYR D 127 -68.735 20.590 -13.064 1.00 92.77 C ANISOU 2675 CA TYR D 127 10726 11447 13077 152 -1354 -1934 C ATOM 2676 C TYR D 127 -68.817 21.678 -12.041 1.00 92.69 C ANISOU 2676 C TYR D 127 10558 11646 13013 156 -1448 -2016 C ATOM 2677 O TYR D 127 -68.187 22.720 -12.218 1.00 92.06 O ANISOU 2677 O TYR D 127 10514 11603 12860 179 -1609 -2021 O ATOM 2678 CB TYR D 127 -67.659 19.589 -12.712 1.00 92.84 C ANISOU 2678 CB TYR D 127 10809 11491 12977 205 -1044 -1580 C ATOM 2679 CG TYR D 127 -67.917 18.218 -13.307 1.00 93.99 C ANISOU 2679 CG TYR D 127 11088 11373 13250 163 -759 -1551 C ATOM 2680 CD1 TYR D 127 -67.330 17.837 -14.484 1.00 93.98 C ANISOU 2680 CD1 TYR D 127 11348 11146 13212 180 -717 -1482 C ATOM 2681 CD2 TYR D 127 -68.758 17.305 -12.673 1.00 95.61 C ANISOU 2681 CD2 TYR D 127 11175 11518 13634 97 -473 -1611 C ATOM 2682 CE1 TYR D 127 -67.562 16.572 -15.022 1.00 95.73 C ANISOU 2682 CE1 TYR D 127 11735 11084 13552 98 -398 -1519 C ATOM 2683 CE2 TYR D 127 -68.998 16.037 -13.216 1.00 97.35 C ANISOU 2683 CE2 TYR D 127 11524 11435 14031 10 -143 -1637 C ATOM 2684 CZ TYR D 127 -68.395 15.680 -14.392 1.00 97.48 C ANISOU 2684 CZ TYR D 127 11824 11228 13987 -7 -110 -1616 C ATOM 2685 OH TYR D 127 -68.598 14.445 -14.962 1.00 99.82 O ANISOU 2685 OH TYR D 127 12297 11183 14447 -133 261 -1704 O ATOM 2686 N ILE D 128 -69.640 21.453 -11.012 1.00 82.24 N ANISOU 2686 N ILE D 128 9077 10419 11753 123 -1304 -2107 N ATOM 2687 CA ILE D 128 -69.875 22.440 -9.953 1.00 82.89 C ANISOU 2687 CA ILE D 128 9052 10680 11764 111 -1329 -2242 C ATOM 2688 C ILE D 128 -69.843 21.787 -8.597 1.00 84.26 C ANISOU 2688 C ILE D 128 9150 11084 11783 133 -1057 -2113 C ATOM 2689 O ILE D 128 -70.166 20.628 -8.478 1.00 84.92 O ANISOU 2689 O ILE D 128 9205 11101 11961 168 -808 -1974 O ATOM 2690 CB ILE D 128 -71.211 23.162 -10.110 1.00 83.67 C ANISOU 2690 CB ILE D 128 9039 10638 12115 105 -1418 -2516 C ATOM 2691 CG1 ILE D 128 -72.400 22.326 -9.609 1.00 85.18 C ANISOU 2691 CG1 ILE D 128 9070 10775 12520 88 -1205 -2571 C ATOM 2692 CG2 ILE D 128 -71.403 23.573 -11.562 1.00 83.09 C ANISOU 2692 CG2 ILE D 128 9016 10380 12172 142 -1675 -2576 C ATOM 2693 CD1 ILE D 128 -73.785 22.985 -9.911 1.00 86.49 C ANISOU 2693 CD1 ILE D 128 9048 10807 13006 97 -1308 -2789 C ATOM 2694 N PRO D 129 -69.416 22.534 -7.565 1.00 91.40 N ANISOU 2694 N PRO D 129 10033 12267 12429 111 -1078 -2161 N ATOM 2695 CA PRO D 129 -69.445 21.980 -6.210 1.00 93.47 C ANISOU 2695 CA PRO D 129 10239 12822 12453 172 -827 -2030 C ATOM 2696 C PRO D 129 -70.869 22.028 -5.647 1.00 94.81 C ANISOU 2696 C PRO D 129 10347 12854 12825 195 -626 -2227 C ATOM 2697 O PRO D 129 -71.430 23.109 -5.433 1.00 95.41 O ANISOU 2697 O PRO D 129 10426 12868 12957 139 -697 -2514 O ATOM 2698 CB PRO D 129 -68.524 22.922 -5.436 1.00 94.78 C ANISOU 2698 CB PRO D 129 10417 13357 12237 89 -991 -2110 C ATOM 2699 CG PRO D 129 -68.687 24.271 -6.131 1.00 93.81 C ANISOU 2699 CG PRO D 129 10348 12987 12310 -38 -1215 -2449 C ATOM 2700 CD PRO D 129 -68.859 23.914 -7.594 1.00 91.37 C ANISOU 2700 CD PRO D 129 10069 12323 12325 19 -1302 -2355 C ATOM 2701 N SER D 130 -71.443 20.857 -5.415 1.00101.84 N ANISOU 2701 N SER D 130 11171 13652 13870 284 -314 -2054 N ATOM 2702 CA SER D 130 -72.867 20.749 -5.150 1.00103.17 C ANISOU 2702 CA SER D 130 11226 13597 14378 296 -102 -2212 C ATOM 2703 C SER D 130 -73.275 21.480 -3.899 1.00105.33 C ANISOU 2703 C SER D 130 11521 14046 14456 346 44 -2338 C ATOM 2704 O SER D 130 -74.435 21.911 -3.798 1.00106.35 O ANISOU 2704 O SER D 130 11559 13959 14890 345 146 -2534 O ATOM 2705 CB SER D 130 -73.297 19.296 -4.996 1.00104.47 C ANISOU 2705 CB SER D 130 11309 13615 14769 369 297 -1991 C ATOM 2706 OG SER D 130 -72.888 18.775 -3.743 1.00106.55 O ANISOU 2706 OG SER D 130 11612 14164 14708 544 636 -1702 O ATOM 2707 N ASN D 131 -72.355 21.594 -2.937 1.00102.21 N ANISOU 2707 N ASN D 131 11232 14058 13545 395 71 -2220 N ATOM 2708 CA ASN D 131 -72.647 22.330 -1.706 1.00105.00 C ANISOU 2708 CA ASN D 131 11673 14624 13599 417 208 -2396 C ATOM 2709 C ASN D 131 -72.707 23.858 -1.871 1.00104.91 C ANISOU 2709 C ASN D 131 11746 14525 13590 250 -22 -2803 C ATOM 2710 O ASN D 131 -72.848 24.576 -0.907 1.00107.59 O ANISOU 2710 O ASN D 131 12210 15013 13658 220 99 -3018 O ATOM 2711 CB ASN D 131 -71.597 22.033 -0.673 1.00107.30 C ANISOU 2711 CB ASN D 131 12040 15469 13261 494 237 -2179 C ATOM 2712 CG ASN D 131 -70.315 22.654 -1.022 1.00106.43 C ANISOU 2712 CG ASN D 131 11951 15624 12864 332 -173 -2239 C ATOM 2713 OD1 ASN D 131 -70.014 22.774 -2.206 1.00103.43 O ANISOU 2713 OD1 ASN D 131 11530 14984 12784 242 -400 -2253 O ATOM 2714 ND2 ASN D 131 -69.541 23.075 -0.019 1.00109.53 N ANISOU 2714 ND2 ASN D 131 12400 16549 12668 282 -276 -2290 N ATOM 2715 N TYR D 132 -72.553 24.364 -3.075 1.00 91.69 N ANISOU 2715 N TYR D 132 10034 12606 12198 150 -307 -2904 N ATOM 2716 CA TYR D 132 -72.736 25.776 -3.304 1.00 92.01 C ANISOU 2716 CA TYR D 132 10139 12469 12351 41 -414 -3235 C ATOM 2717 C TYR D 132 -74.098 26.079 -3.925 1.00 91.81 C ANISOU 2717 C TYR D 132 9985 12030 12870 121 -317 -3315 C ATOM 2718 O TYR D 132 -74.451 27.236 -4.147 1.00 92.55 O ANISOU 2718 O TYR D 132 10105 11914 13147 99 -312 -3524 O ATOM 2719 CB TYR D 132 -71.659 26.268 -4.260 1.00 89.97 C ANISOU 2719 CB TYR D 132 9910 12205 12068 -71 -752 -3246 C ATOM 2720 CG TYR D 132 -70.328 26.612 -3.656 1.00 91.24 C ANISOU 2720 CG TYR D 132 10155 12749 11765 -222 -892 -3300 C ATOM 2721 CD1 TYR D 132 -69.803 25.897 -2.611 1.00 93.17 C ANISOU 2721 CD1 TYR D 132 10397 13452 11549 -197 -831 -3140 C ATOM 2722 CD2 TYR D 132 -69.587 27.641 -4.172 1.00 91.05 C ANISOU 2722 CD2 TYR D 132 10172 12641 11780 -381 -1083 -3486 C ATOM 2723 CE1 TYR D 132 -68.574 26.211 -2.077 1.00 95.11 C ANISOU 2723 CE1 TYR D 132 10648 14138 11350 -351 -1026 -3183 C ATOM 2724 CE2 TYR D 132 -68.374 27.962 -3.644 1.00 92.85 C ANISOU 2724 CE2 TYR D 132 10410 13233 11634 -569 -1236 -3567 C ATOM 2725 CZ TYR D 132 -67.858 27.244 -2.589 1.00 94.99 C ANISOU 2725 CZ TYR D 132 10644 14036 11413 -567 -1244 -3422 C ATOM 2726 OH TYR D 132 -66.628 27.565 -2.051 1.00 97.61 O ANISOU 2726 OH TYR D 132 10918 14828 11342 -773 -1461 -3498 O ATOM 2727 N VAL D 133 -74.860 25.054 -4.258 1.00112.00 N ANISOU 2727 N VAL D 133 12368 14462 15723 211 -230 -3137 N ATOM 2728 CA VAL D 133 -76.147 25.306 -4.890 1.00112.50 C ANISOU 2728 CA VAL D 133 12223 14213 16309 269 -204 -3196 C ATOM 2729 C VAL D 133 -77.294 24.924 -3.969 1.00115.17 C ANISOU 2729 C VAL D 133 12438 14461 16861 363 200 -3176 C ATOM 2730 O VAL D 133 -77.090 24.243 -2.945 1.00116.36 O ANISOU 2730 O VAL D 133 12682 14780 16748 408 473 -3074 O ATOM 2731 CB VAL D 133 -76.261 24.560 -6.211 1.00110.70 C ANISOU 2731 CB VAL D 133 11838 13886 16338 245 -470 -3084 C ATOM 2732 CG1 VAL D 133 -75.037 24.855 -7.056 1.00108.30 C ANISOU 2732 CG1 VAL D 133 11700 13660 15789 189 -795 -3055 C ATOM 2733 CG2 VAL D 133 -76.423 23.064 -5.968 1.00111.02 C ANISOU 2733 CG2 VAL D 133 11796 13945 16441 233 -274 -2924 C ATOM 2734 N ALA D 134 -78.489 25.376 -4.343 1.00109.28 N ANISOU 2734 N ALA D 134 11462 13463 16597 425 258 -3228 N ATOM 2735 CA ALA D 134 -79.711 25.037 -3.623 1.00112.16 C ANISOU 2735 CA ALA D 134 11635 13675 17304 523 661 -3181 C ATOM 2736 C ALA D 134 -80.763 24.580 -4.609 1.00112.78 C ANISOU 2736 C ALA D 134 11299 13583 17968 510 518 -3120 C ATOM 2737 O ALA D 134 -81.061 25.292 -5.555 1.00112.67 O ANISOU 2737 O ALA D 134 11133 13513 18164 527 229 -3154 O ATOM 2738 CB ALA D 134 -80.203 26.217 -2.869 1.00114.67 C ANISOU 2738 CB ALA D 134 12055 13867 17648 618 960 -3311 C ATOM 2739 N ARG D 135 -81.319 23.393 -4.387 1.00117.12 N ANISOU 2739 N ARG D 135 11650 14069 18780 480 731 -3027 N ATOM 2740 CA ARG D 135 -82.248 22.799 -5.342 1.00118.40 C ANISOU 2740 CA ARG D 135 11386 14114 19485 380 554 -3034 C ATOM 2741 C ARG D 135 -83.517 23.590 -5.291 1.00121.49 C ANISOU 2741 C ARG D 135 11439 14363 20360 494 663 -3026 C ATOM 2742 O ARG D 135 -83.870 24.078 -4.226 1.00123.23 O ANISOU 2742 O ARG D 135 11747 14475 20600 645 1098 -2986 O ATOM 2743 CB ARG D 135 -82.539 21.343 -4.979 1.00119.79 C ANISOU 2743 CB ARG D 135 11435 14189 19892 293 876 -2964 C ATOM 2744 N VAL D 136 -84.191 23.745 -6.427 1.00150.39 N ANISOU 2744 N VAL D 136 14716 18046 24381 443 284 -3045 N ATOM 2745 CA VAL D 136 -85.436 24.529 -6.454 1.00153.99 C ANISOU 2745 CA VAL D 136 14763 18404 25344 595 376 -2957 C ATOM 2746 C VAL D 136 -86.580 23.990 -7.304 1.00157.47 C ANISOU 2746 C VAL D 136 14577 18894 26362 480 118 -2948 C ATOM 2747 O VAL D 136 -86.361 23.194 -8.230 1.00156.98 O ANISOU 2747 O VAL D 136 14421 18977 26246 252 -283 -3076 O ATOM 2748 CB VAL D 136 -85.206 25.944 -6.998 1.00153.45 C ANISOU 2748 CB VAL D 136 14791 18386 25127 773 153 -2910 C ATOM 2749 CG1 VAL D 136 -84.225 26.664 -6.137 1.00151.27 C ANISOU 2749 CG1 VAL D 136 15065 18043 24370 845 425 -2979 C ATOM 2750 CG2 VAL D 136 -84.721 25.895 -8.433 1.00151.85 C ANISOU 2750 CG2 VAL D 136 14553 18409 24735 690 -467 -2941 C ATOM 2751 N ASP D 137 -87.788 24.457 -6.952 1.00199.55 N ANISOU 2751 N ASP D 137 19481 24103 32235 633 376 -2804 N ATOM 2752 CA ASP D 137 -88.932 24.638 -7.871 1.00203.82 C ANISOU 2752 CA ASP D 137 19347 24789 33306 638 35 -2712 C ATOM 2753 C ASP D 137 -90.199 24.934 -7.076 1.00208.42 C ANISOU 2753 C ASP D 137 19496 25153 34543 816 539 -2509 C ATOM 2754 O ASP D 137 -90.656 26.073 -7.049 1.00210.37 O ANISOU 2754 O ASP D 137 19613 25358 34958 1105 656 -2291 O ATOM 2755 CB ASP D 137 -89.160 23.468 -8.855 1.00205.29 C ANISOU 2755 CB ASP D 137 19180 25180 33642 288 -438 -2909 C ATOM 2756 CG ASP D 137 -88.792 23.828 -10.310 1.00204.81 C ANISOU 2756 CG ASP D 137 19090 25485 33241 259 -1163 -2958 C ATOM 2757 OD1 ASP D 137 -89.331 23.169 -11.224 1.00208.08 O ANISOU 2757 OD1 ASP D 137 19071 26138 33850 11 -1603 -3105 O ATOM 2758 OD2 ASP D 137 -87.989 24.771 -10.548 1.00201.77 O ANISOU 2758 OD2 ASP D 137 19107 25154 32402 477 -1277 -2862 O ATOM 2759 N SER D 138 -90.759 23.913 -6.432 1.00171.07 N ANISOU 2759 N SER D 138 14544 20239 30215 664 903 -2552 N ATOM 2760 CA SER D 138 -91.834 24.109 -5.453 1.00175.22 C ANISOU 2760 CA SER D 138 14763 20474 31337 855 1539 -2343 C ATOM 2761 C SER D 138 -93.034 24.867 -6.018 1.00180.28 C ANISOU 2761 C SER D 138 14701 21212 32585 1024 1382 -2096 C ATOM 2762 O SER D 138 -94.173 24.428 -5.872 1.00185.26 O ANISOU 2762 O SER D 138 14694 21755 33940 976 1572 -1986 O ATOM 2763 CB SER D 138 -91.275 24.818 -4.204 1.00173.14 C ANISOU 2763 CB SER D 138 15153 19962 30669 1123 2148 -2279 C ATOM 2764 OG SER D 138 -89.948 25.309 -4.423 1.00168.20 O ANISOU 2764 OG SER D 138 15147 19493 29270 1117 1862 -2424 O TER 2765 SER D 138 MASTER 653 0 0 8 14 0 0 6 2761 4 0 40 END
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Related entries of code: 3reb
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
2jkr
RCSB PDB
PDBbind
11aa, >2JKR_5|Chains... at 100%
3rbb
RCSB PDB
PDBbind
61aa, >3RBB_2|Chains... at 91%
3rea
RCSB PDB
PDBbind
61aa, >3REA_2|Chains... at 100%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
3reb
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
HIV-1 Nef protein (delta 1-44)
Ligand Name
engineered Tyrosine-protein kinase Hck-SH3 domain (NI3-13)
EC.Number
E.C.-.-.-.-
Resolution
3.45(Å)
Affinity (Kd/Ki/IC50)
Kd=96nM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2011) PLOS ONE Vol. 6: pp. e20033
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P08631
P03407
Entrez Gene ID
NCBI Entrez Gene ID:
3055
ASD
Information of known allosteric effects of PDB entries
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