Browse entries in the PDBbind-CN Database
HEADER VIRAL PROTEIN, PROTEIN BINDING 29-MAR-11 3RBB 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, DILEUCINE MOTIF, SH3 DOMAIN, RECEPTOR INTERNALIZATION, KEYWDS 2 PXXP MOTIF, PROTEIN BINDING, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR F.A.HORENKAMP,A.SCHULTE,M.WEYAND,M.GEYER REVDAT 3 29-JUN-11 3RBB 1 JRNL REVDAT 2 22-JUN-11 3RBB 1 JRNL REVDAT 1 27-APR-11 3RBB 0 JRNL AUTH F.A.HORENKAMP,S.BREUER,A.SCHULTE,S.LULF,M.WEYAND,K.SAKSELA, JRNL AUTH 2 M.GEYER JRNL TITL CONFORMATION OF THE DILEUCINE-BASED SORTING MOTIF IN HIV-1 JRNL TITL 2 NEF REVEALED BY INTERMOLECULAR DOMAIN ASSEMBLY. JRNL REF TRAFFIC V. 12 867 2011 JRNL REFN ISSN 1398-9219 JRNL PMID 21477083 JRNL DOI 10.1111/J.1600-0854.2011.01205.X REMARK 2 REMARK 2 RESOLUTION. 2.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.99 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 27143 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) : 0.206 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.245 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1429 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.35 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1984 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.3040 REMARK 3 BIN FREE R VALUE SET COUNT : 104 REMARK 3 BIN FREE R VALUE : 0.3430 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3120 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 8 REMARK 3 SOLVENT ATOMS : 208 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.81 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.87000 REMARK 3 B22 (A**2) : 2.58000 REMARK 3 B33 (A**2) : -3.45000 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): 0.206 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.127 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.523 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3268 ; 0.014 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4450 ; 1.329 ; 1.943 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 380 ; 5.926 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 161 ;34.616 ;23.043 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 511 ;16.141 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;19.430 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 449 ; 0.102 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2554 ; 0.007 ; 0.021 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): 1901 ; 0.739 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3068 ; 1.364 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1367 ; 1.966 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1378 ; 3.194 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 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 72 A 208 REMARK 3 ORIGIN FOR THE GROUP (A): 35.3980 59.2643 3.0359 REMARK 3 T TENSOR REMARK 3 T11: 0.0309 T22: 0.1352 REMARK 3 T33: 0.1553 T12: -0.0145 REMARK 3 T13: 0.0230 T23: -0.0144 REMARK 3 L TENSOR REMARK 3 L11: 1.4880 L22: 2.2613 REMARK 3 L33: 2.6334 L12: 0.1011 REMARK 3 L13: 0.4979 L23: 0.0762 REMARK 3 S TENSOR REMARK 3 S11: 0.0556 S12: 0.0006 S13: -0.0988 REMARK 3 S21: -0.0010 S22: -0.0501 S23: 0.1341 REMARK 3 S31: 0.2641 S32: -0.1123 S33: -0.0054 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 79 B 138 REMARK 3 ORIGIN FOR THE GROUP (A): 43.1758 70.7861 33.3010 REMARK 3 T TENSOR REMARK 3 T11: 0.3147 T22: 0.2808 REMARK 3 T33: 0.0702 T12: -0.1401 REMARK 3 T13: -0.0252 T23: 0.0117 REMARK 3 L TENSOR REMARK 3 L11: 3.4501 L22: 3.7758 REMARK 3 L33: 9.6026 L12: -1.8964 REMARK 3 L13: -1.7204 L23: 1.5551 REMARK 3 S TENSOR REMARK 3 S11: 0.1405 S12: -0.3713 S13: 0.1838 REMARK 3 S21: 0.6240 S22: -0.1109 S23: -0.3956 REMARK 3 S31: -0.4464 S32: 0.6004 S33: -0.0296 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 208 REMARK 3 ORIGIN FOR THE GROUP (A): 32.4478 30.6924 -4.7379 REMARK 3 T TENSOR REMARK 3 T11: 0.0902 T22: 0.0296 REMARK 3 T33: 0.0670 T12: -0.0241 REMARK 3 T13: 0.0112 T23: -0.0047 REMARK 3 L TENSOR REMARK 3 L11: 1.9350 L22: 4.1162 REMARK 3 L33: 4.0561 L12: 0.8734 REMARK 3 L13: 0.9388 L23: 1.6543 REMARK 3 S TENSOR REMARK 3 S11: 0.0520 S12: 0.0808 S13: 0.2002 REMARK 3 S21: 0.1786 S22: -0.1642 S23: 0.1869 REMARK 3 S31: 0.4112 S32: 0.0412 S33: 0.1121 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 80 D 137 REMARK 3 ORIGIN FOR THE GROUP (A): 33.6164 18.7551 -31.6847 REMARK 3 T TENSOR REMARK 3 T11: 0.4214 T22: 0.2886 REMARK 3 T33: 0.0334 T12: 0.0397 REMARK 3 T13: 0.0003 T23: -0.0046 REMARK 3 L TENSOR REMARK 3 L11: 2.9765 L22: 5.0167 REMARK 3 L33: 10.3464 L12: 0.2755 REMARK 3 L13: 1.8816 L23: 3.2874 REMARK 3 S TENSOR REMARK 3 S11: 0.0133 S12: 0.2912 S13: -0.2655 REMARK 3 S21: -0.3176 S22: 0.1489 S23: -0.1805 REMARK 3 S31: 0.9010 S32: 0.7994 S33: -0.1621 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3RBB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-11. REMARK 100 THE RCSB ID CODE IS RCSB064719. 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 : 7.5 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) : 0.977032 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 : 28573 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350 REMARK 200 RESOLUTION RANGE LOW (A) : 48.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 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 : 22.1800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8 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 5.5.0109 REMARK 200 STARTING MODEL: PDB ENTRY 1EFN REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 8% ETHYLENE GLYCOL, 22% REMARK 280 PEG 8000, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 21.59500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.76500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.44000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.76500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.59500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.44000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1560 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 12530 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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: 1170 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 11660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 ASP A 209 REMARK 465 ALA A 210 REMARK 465 MET B 78 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 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 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 ASP C 209 REMARK 465 ALA C 210 REMARK 465 MET D 78 REMARK 465 GLU D 79 REMARK 465 SER D 138 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 PHE A 72 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 156 CG CD CE NZ REMARK 470 GLU A 158 CG CD OE1 OE2 REMARK 470 GLU A 159 CG CD OE1 OE2 REMARK 470 LYS A 208 CG CD CE NZ REMARK 470 GLU B 79 CG CD OE1 OE2 REMARK 470 ARG B 123 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 69 CG CD OE1 OE2 REMARK 470 LYS C 156 CG CD CE NZ REMARK 470 LYS C 208 CG CD CE NZ 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 GLY C 99 O HOH C 264 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1EFN RELATED DB: PDB REMARK 900 RELATED ID: 1AVZ RELATED DB: PDB REMARK 900 RELATED ID: 2NEF RELATED DB: PDB REMARK 900 RELATED ID: 3REA RELATED DB: PDB REMARK 900 RELATED ID: 3REB RELATED DB: PDB DBREF 3RBB A 45 210 UNP P03407 NEF_HV1A2 45 210 DBREF 3RBB B 79 138 UNP P08631 HCK_HUMAN 79 138 DBREF 3RBB C 45 210 UNP P03407 NEF_HV1A2 45 210 DBREF 3RBB D 79 138 UNP P08631 HCK_HUMAN 79 138 SEQADV 3RBB MET A 47 UNP P03407 ILE 47 ENGINEERED MUTATION SEQADV 3RBB ALA A 48 UNP P03407 THR 48 ENGINEERED MUTATION SEQADV 3RBB SER A 59 UNP P03407 CYS 59 ENGINEERED MUTATION SEQADV 3RBB ALA A 210 UNP P03407 CYS 210 ENGINEERED MUTATION SEQADV 3RBB MET B 78 UNP P08631 INITIATING METHIONINE SEQADV 3RBB TYR B 90 UNP P08631 GLU 90 ENGINEERED MUTATION SEQADV 3RBB SER B 91 UNP P08631 ALA 91 ENGINEERED MUTATION SEQADV 3RBB PRO B 92 UNP P08631 ILE 92 ENGINEERED MUTATION SEQADV 3RBB PHE B 93 UNP P08631 HIS 93 ENGINEERED MUTATION SEQADV 3RBB SER B 94 UNP P08631 HIS 94 ENGINEERED MUTATION SEQADV 3RBB TRP B 95 UNP P08631 GLU 95 ENGINEERED MUTATION SEQADV 3RBB MET C 47 UNP P03407 ILE 47 ENGINEERED MUTATION SEQADV 3RBB ALA C 48 UNP P03407 THR 48 ENGINEERED MUTATION SEQADV 3RBB SER C 59 UNP P03407 CYS 59 ENGINEERED MUTATION SEQADV 3RBB ALA C 210 UNP P03407 CYS 210 ENGINEERED MUTATION SEQADV 3RBB MET D 78 UNP P08631 INITIATING METHIONINE SEQADV 3RBB TYR D 90 UNP P08631 GLU 90 ENGINEERED MUTATION SEQADV 3RBB SER D 91 UNP P08631 ALA 91 ENGINEERED MUTATION SEQADV 3RBB PRO D 92 UNP P08631 ILE 92 ENGINEERED MUTATION SEQADV 3RBB PHE D 93 UNP P08631 HIS 93 ENGINEERED MUTATION SEQADV 3RBB SER D 94 UNP P08631 HIS 94 ENGINEERED MUTATION SEQADV 3RBB TRP D 95 UNP P08631 GLU 95 ENGINEERED MUTATION 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 61 MET GLU ASP ILE ILE VAL VAL ALA LEU TYR ASP TYR TYR SEQRES 2 B 61 SER PRO PHE SER TRP ASP LEU SER PHE GLN LYS GLY ASP SEQRES 3 B 61 GLN MET VAL VAL LEU GLU GLU SER GLY GLU TRP TRP LYS SEQRES 4 B 61 ALA ARG SER LEU ALA THR ARG LYS GLU GLY TYR ILE PRO SEQRES 5 B 61 SER ASN TYR VAL ALA ARG VAL ASP SER 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 61 MET GLU ASP ILE ILE VAL VAL ALA LEU TYR ASP TYR TYR SEQRES 2 D 61 SER PRO PHE SER TRP ASP LEU SER PHE GLN LYS GLY ASP SEQRES 3 D 61 GLN MET VAL VAL LEU GLU GLU SER GLY GLU TRP TRP LYS SEQRES 4 D 61 ALA ARG SER LEU ALA THR ARG LYS GLU GLY TYR ILE PRO SEQRES 5 D 61 SER ASN TYR VAL ALA ARG VAL ASP SER HET EDO A 2 4 HET EDO C 1 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 5 EDO 2(C2 H6 O2) FORMUL 7 HOH *208(H2 O) 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 ASN A 165 HIS A 170 1 6 HELIX 4 4 PRO A 171 LEU A 174 5 4 HELIX 5 5 SER A 191 PHE A 195 5 5 HELIX 6 6 HIS A 197 HIS A 203 1 7 HELIX 7 7 PRO A 204 TYR A 207 5 4 HELIX 8 8 THR C 84 GLY C 99 1 16 HELIX 9 9 SER C 107 GLY C 123 1 17 HELIX 10 10 SER C 191 PHE C 195 5 5 HELIX 11 11 HIS C 197 HIS C 203 1 7 HELIX 12 12 PRO C 204 TYR C 207 5 4 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 VAL B 136 N ILE B 82 SHEET 1 C 2 PHE C 147 PRO C 151 0 SHEET 2 C 2 LEU C 185 PHE C 189 -1 O VAL C 186 N VAL C 150 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 ARG D 135 -1 O ALA D 134 N VAL D 84 CISPEP 1 GLY A 134 PRO A 135 0 4.61 CISPEP 2 GLU A 159 ALA A 160 0 1.28 CISPEP 3 GLY C 134 PRO C 135 0 5.32 SITE 1 AC1 3 ALA A 180 VAL A 184 ARG C 110 SITE 1 AC2 5 HOH A 31 HOH A 36 TRP A 106 ARG A 138 SITE 2 AC2 5 LEU A 149 CRYST1 43.190 90.880 169.530 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.023154 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011004 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005899 0.00000 ATOM 1 N PHE A 72 28.389 57.062 24.992 1.00 73.53 N ANISOU 1 N PHE A 72 9578 10360 8000 -1298 1761 363 N ATOM 2 CA PHE A 72 29.072 58.006 25.923 1.00 73.43 C ANISOU 2 CA PHE A 72 9701 10380 7820 -1186 1739 290 C ATOM 3 C PHE A 72 28.333 58.055 27.261 1.00 75.61 C ANISOU 3 C PHE A 72 10071 10795 7862 -1275 1953 300 C ATOM 4 O PHE A 72 27.098 58.079 27.288 1.00 77.35 O ANISOU 4 O PHE A 72 10135 11150 8106 -1349 2161 277 O ATOM 5 CB PHE A 72 29.183 59.417 25.305 1.00 72.06 C ANISOU 5 CB PHE A 72 9369 10236 7773 -1011 1706 123 C ATOM 6 N PRO A 73 29.088 58.036 28.379 1.00 75.86 N ANISOU 6 N PRO A 73 10358 10804 7661 -1272 1900 338 N ATOM 7 CA PRO A 73 28.491 58.269 29.698 1.00 77.24 C ANISOU 7 CA PRO A 73 10648 11120 7579 -1332 2103 325 C ATOM 8 C PRO A 73 28.169 59.763 29.918 1.00 76.27 C ANISOU 8 C PRO A 73 10428 11114 7438 -1183 2205 125 C ATOM 9 O PRO A 73 28.828 60.641 29.334 1.00 74.24 O ANISOU 9 O PRO A 73 10115 10789 7305 -1032 2055 17 O ATOM 10 CB PRO A 73 29.578 57.791 30.677 1.00 78.27 C ANISOU 10 CB PRO A 73 11099 11162 7479 -1355 1955 427 C ATOM 11 CG PRO A 73 30.624 57.083 29.828 1.00 77.06 C ANISOU 11 CG PRO A 73 10973 10820 7486 -1325 1691 517 C ATOM 12 CD PRO A 73 30.524 57.693 28.470 1.00 74.97 C ANISOU 12 CD PRO A 73 10441 10538 7507 -1220 1647 405 C ATOM 13 N VAL A 74 27.168 60.041 30.754 1.00 76.89 N ANISOU 13 N VAL A 74 10491 11363 7361 -1226 2461 77 N ATOM 14 CA VAL A 74 26.720 61.421 31.011 1.00 75.67 C ANISOU 14 CA VAL A 74 10247 11321 7183 -1075 2586 -123 C ATOM 15 C VAL A 74 27.784 62.297 31.711 1.00 73.63 C ANISOU 15 C VAL A 74 10217 10999 6760 -952 2444 -219 C ATOM 16 O VAL A 74 28.218 62.008 32.839 1.00 75.27 O ANISOU 16 O VAL A 74 10686 11216 6696 -1013 2439 -164 O ATOM 17 CB VAL A 74 25.380 61.447 31.787 1.00 79.01 C ANISOU 17 CB VAL A 74 10595 11958 7467 -1145 2915 -156 C ATOM 18 CG1 VAL A 74 24.962 62.887 32.140 1.00 80.62 C ANISOU 18 CG1 VAL A 74 10735 12268 7628 -960 3044 -377 C ATOM 19 CG2 VAL A 74 24.293 60.730 30.981 1.00 79.83 C ANISOU 19 CG2 VAL A 74 10424 12134 7774 -1264 3041 -83 C ATOM 20 N ARG A 75 28.195 63.355 31.012 1.00 68.93 N ANISOU 20 N ARG A 75 9525 10334 6331 -791 2318 -355 N ATOM 21 CA ARG A 75 29.130 64.367 31.532 1.00 65.88 C ANISOU 21 CA ARG A 75 9316 9882 5831 -674 2178 -473 C ATOM 22 C ARG A 75 28.813 65.695 30.821 1.00 61.94 C ANISOU 22 C ARG A 75 8641 9374 5519 -505 2190 -656 C ATOM 23 O ARG A 75 28.185 65.659 29.749 1.00 60.99 O ANISOU 23 O ARG A 75 8271 9262 5639 -480 2229 -655 O ATOM 24 CB ARG A 75 30.594 63.922 31.308 1.00 64.60 C ANISOU 24 CB ARG A 75 9293 9559 5693 -695 1878 -371 C ATOM 25 CG ARG A 75 30.951 63.558 29.864 1.00 62.24 C ANISOU 25 CG ARG A 75 8804 9151 5692 -682 1728 -308 C ATOM 26 CD ARG A 75 32.465 63.364 29.681 1.00 62.77 C ANISOU 26 CD ARG A 75 8988 9078 5784 -666 1440 -246 C ATOM 27 NE ARG A 75 32.915 63.744 28.336 1.00 60.37 N ANISOU 27 NE ARG A 75 8502 8683 5752 -589 1304 -278 N ATOM 28 CZ ARG A 75 34.144 63.538 27.861 1.00 58.94 C ANISOU 28 CZ ARG A 75 8345 8392 5657 -570 1074 -224 C ATOM 29 NH1 ARG A 75 35.067 62.943 28.612 1.00 61.29 N ANISOU 29 NH1 ARG A 75 8832 8651 5804 -611 934 -136 N ATOM 30 NH2 ARG A 75 34.457 63.924 26.631 1.00 54.18 N ANISOU 30 NH2 ARG A 75 7573 7726 5287 -507 985 -256 N ATOM 31 N PRO A 76 29.218 66.859 31.398 1.00 59.46 N ANISOU 31 N PRO A 76 8464 9034 5095 -389 2149 -813 N ATOM 32 CA PRO A 76 28.963 68.130 30.683 1.00 56.28 C ANISOU 32 CA PRO A 76 7917 8588 4878 -225 2139 -978 C ATOM 33 C PRO A 76 29.675 68.169 29.330 1.00 51.30 C ANISOU 33 C PRO A 76 7159 7814 4520 -203 1916 -927 C ATOM 34 O PRO A 76 30.763 67.633 29.198 1.00 48.65 O ANISOU 34 O PRO A 76 6917 7385 4185 -273 1718 -822 O ATOM 35 CB PRO A 76 29.519 69.215 31.626 1.00 57.38 C ANISOU 35 CB PRO A 76 8291 8685 4825 -138 2086 -1134 C ATOM 36 CG PRO A 76 30.311 68.493 32.657 1.00 59.12 C ANISOU 36 CG PRO A 76 8769 8907 4787 -259 2003 -1035 C ATOM 37 CD PRO A 76 29.801 67.085 32.735 1.00 61.14 C ANISOU 37 CD PRO A 76 8973 9256 5002 -404 2121 -852 C ATOM 38 N GLN A 77 29.030 68.780 28.340 1.00 48.61 N ANISOU 38 N GLN A 77 6601 7466 4403 -102 1955 -999 N ATOM 39 CA GLN A 77 29.519 68.800 26.987 1.00 44.92 C ANISOU 39 CA GLN A 77 5998 6883 4185 -84 1780 -947 C ATOM 40 C GLN A 77 30.780 69.651 26.966 1.00 43.22 C ANISOU 40 C GLN A 77 5930 6522 3969 -36 1563 -1005 C ATOM 41 O GLN A 77 30.779 70.766 27.467 1.00 44.83 O ANISOU 41 O GLN A 77 6233 6697 4102 59 1574 -1152 O ATOM 42 CB GLN A 77 28.439 69.346 26.032 1.00 44.42 C ANISOU 42 CB GLN A 77 5688 6857 4334 22 1878 -1018 C ATOM 43 CG GLN A 77 28.931 69.696 24.612 1.00 40.58 C ANISOU 43 CG GLN A 77 5087 6242 4091 70 1695 -997 C ATOM 44 CD GLN A 77 29.590 68.515 23.868 1.00 38.02 C ANISOU 44 CD GLN A 77 4726 5871 3850 -54 1566 -829 C ATOM 45 OE1 GLN A 77 29.016 67.435 23.758 1.00 38.38 O ANISOU 45 OE1 GLN A 77 4685 5993 3906 -149 1651 -732 O ATOM 46 NE2 GLN A 77 30.793 68.737 23.335 1.00 33.96 N ANISOU 46 NE2 GLN A 77 4276 5228 3400 -53 1362 -800 N ATOM 47 N VAL A 78 31.863 69.099 26.430 1.00 40.71 N ANISOU 47 N VAL A 78 5630 6115 3722 -107 1367 -891 N ATOM 48 CA VAL A 78 33.137 69.829 26.357 1.00 38.58 C ANISOU 48 CA VAL A 78 5472 5719 3468 -87 1152 -929 C ATOM 49 C VAL A 78 32.993 70.990 25.369 1.00 37.44 C ANISOU 49 C VAL A 78 5215 5490 3520 19 1113 -1024 C ATOM 50 O VAL A 78 32.159 70.933 24.470 1.00 36.51 O ANISOU 50 O VAL A 78 4913 5398 3561 64 1195 -1013 O ATOM 51 CB VAL A 78 34.331 68.913 25.992 1.00 36.78 C ANISOU 51 CB VAL A 78 5260 5435 3281 -178 963 -783 C ATOM 52 CG1 VAL A 78 34.528 67.842 27.069 1.00 37.83 C ANISOU 52 CG1 VAL A 78 5543 5629 3202 -271 978 -688 C ATOM 53 CG2 VAL A 78 34.146 68.281 24.601 1.00 33.56 C ANISOU 53 CG2 VAL A 78 4645 5009 3097 -188 950 -688 C ATOM 54 N PRO A 79 33.790 72.056 25.548 1.00 37.32 N ANISOU 54 N PRO A 79 5322 5368 3489 54 978 -1115 N ATOM 55 CA PRO A 79 33.523 73.295 24.821 1.00 37.23 C ANISOU 55 CA PRO A 79 5253 5263 3628 161 960 -1220 C ATOM 56 C PRO A 79 33.614 73.143 23.314 1.00 35.72 C ANISOU 56 C PRO A 79 4875 5023 3674 161 890 -1132 C ATOM 57 O PRO A 79 34.458 72.391 22.797 1.00 34.31 O ANISOU 57 O PRO A 79 4656 4830 3551 72 776 -1010 O ATOM 58 CB PRO A 79 34.608 74.235 25.320 1.00 37.38 C ANISOU 58 CB PRO A 79 5461 5164 3578 145 792 -1300 C ATOM 59 CG PRO A 79 34.935 73.691 26.722 1.00 40.20 C ANISOU 59 CG PRO A 79 5999 5596 3679 76 801 -1300 C ATOM 60 CD PRO A 79 34.947 72.200 26.444 1.00 37.70 C ANISOU 60 CD PRO A 79 5573 5370 3380 -9 826 -1127 C ATOM 61 N LEU A 80 32.739 73.886 22.655 1.00 35.99 N ANISOU 61 N LEU A 80 4807 5032 3835 273 959 -1202 N ATOM 62 CA ALEU A 80 32.579 73.896 21.214 0.50 34.91 C ANISOU 62 CA ALEU A 80 4502 4854 3909 297 911 -1137 C ATOM 63 CA BLEU A 80 32.610 73.846 21.224 0.50 34.98 C ANISOU 63 CA BLEU A 80 4512 4865 3915 291 909 -1132 C ATOM 64 C LEU A 80 33.723 74.642 20.558 1.00 33.98 C ANISOU 64 C LEU A 80 4444 4589 3880 270 724 -1123 C ATOM 65 O LEU A 80 34.185 75.627 21.083 1.00 35.45 O ANISOU 65 O LEU A 80 4778 4680 4011 289 657 -1216 O ATOM 66 CB ALEU A 80 31.267 74.613 20.846 0.50 35.76 C ANISOU 66 CB ALEU A 80 4502 4975 4108 445 1028 -1229 C ATOM 67 CB BLEU A 80 31.225 74.369 20.809 0.50 35.88 C ANISOU 67 CB BLEU A 80 4497 5013 4125 429 1039 -1208 C ATOM 68 CG ALEU A 80 30.918 74.688 19.347 0.50 35.11 C ANISOU 68 CG ALEU A 80 4250 4857 4234 487 979 -1168 C ATOM 69 CG BLEU A 80 30.053 73.498 21.276 0.50 37.70 C ANISOU 69 CG BLEU A 80 4611 5414 4298 430 1234 -1199 C ATOM 70 CD1ALEU A 80 30.194 73.427 18.945 0.50 33.97 C ANISOU 70 CD1ALEU A 80 3926 4849 4130 435 1071 -1074 C ATOM 71 CD1BLEU A 80 28.774 73.713 20.457 0.50 38.47 C ANISOU 71 CD1BLEU A 80 4499 5565 4552 541 1324 -1226 C ATOM 72 CD2ALEU A 80 30.077 75.935 18.999 0.50 36.41 C ANISOU 72 CD2ALEU A 80 4386 4955 4494 659 1005 -1282 C ATOM 73 CD2BLEU A 80 30.461 72.050 21.239 0.50 37.31 C ANISOU 73 CD2BLEU A 80 4531 5433 4212 279 1219 -1051 C ATOM 74 N ARG A 81 34.148 74.193 19.382 1.00 32.80 N ANISOU 74 N ARG A 81 4178 4420 3865 221 645 -1011 N ATOM 75 CA ARG A 81 35.184 74.914 18.613 1.00 32.21 C ANISOU 75 CA ARG A 81 4134 4218 3886 186 487 -987 C ATOM 76 C ARG A 81 35.094 74.440 17.175 1.00 30.68 C ANISOU 76 C ARG A 81 3782 4032 3843 177 468 -882 C ATOM 77 O ARG A 81 34.625 73.327 16.924 1.00 29.90 O ANISOU 77 O ARG A 81 3574 4032 3753 160 536 -814 O ATOM 78 CB ARG A 81 36.593 74.700 19.206 1.00 31.48 C ANISOU 78 CB ARG A 81 4144 4107 3710 69 360 -952 C ATOM 79 CG ARG A 81 36.871 73.242 19.604 1.00 32.23 C ANISOU 79 CG ARG A 81 4203 4316 3728 -2 379 -857 C ATOM 80 CD ARG A 81 38.291 73.010 20.071 1.00 31.53 C ANISOU 80 CD ARG A 81 4187 4213 3578 -98 231 -814 C ATOM 81 NE ARG A 81 38.437 71.641 20.577 1.00 30.24 N ANISOU 81 NE ARG A 81 4018 4145 3327 -141 249 -729 N ATOM 82 CZ ARG A 81 39.559 71.160 21.110 1.00 30.37 C ANISOU 82 CZ ARG A 81 4089 4174 3275 -208 125 -679 C ATOM 83 NH1 ARG A 81 40.630 71.939 21.199 1.00 28.85 N ANISOU 83 NH1 ARG A 81 3941 3922 3099 -253 -21 -709 N ATOM 84 NH2 ARG A 81 39.612 69.910 21.562 1.00 29.83 N ANISOU 84 NH2 ARG A 81 4033 4174 3127 -232 139 -597 N ATOM 85 N PRO A 82 35.495 75.290 16.216 1.00 31.14 N ANISOU 85 N PRO A 82 3839 3982 4012 185 376 -869 N ATOM 86 CA PRO A 82 35.477 74.838 14.810 1.00 30.14 C ANISOU 86 CA PRO A 82 3579 3867 4006 172 354 -768 C ATOM 87 C PRO A 82 36.647 73.893 14.477 1.00 29.60 C ANISOU 87 C PRO A 82 3473 3839 3935 59 287 -662 C ATOM 88 O PRO A 82 37.746 74.043 15.022 1.00 31.15 O ANISOU 88 O PRO A 82 3743 4009 4082 -16 206 -660 O ATOM 89 CB PRO A 82 35.615 76.148 14.032 1.00 30.42 C ANISOU 89 CB PRO A 82 3663 3763 4131 209 276 -786 C ATOM 90 CG PRO A 82 36.448 77.051 14.960 1.00 31.66 C ANISOU 90 CG PRO A 82 3985 3825 4222 163 202 -858 C ATOM 91 CD PRO A 82 36.165 76.602 16.377 1.00 31.90 C ANISOU 91 CD PRO A 82 4072 3936 4114 176 275 -931 C ATOM 92 N MET A 83 36.391 72.923 13.606 1.00 29.09 N ANISOU 92 N MET A 83 3291 3839 3925 52 315 -583 N ATOM 93 CA MET A 83 37.385 71.982 13.092 1.00 27.94 C ANISOU 93 CA MET A 83 3094 3728 3793 -25 263 -490 C ATOM 94 C MET A 83 38.532 72.737 12.425 1.00 28.30 C ANISOU 94 C MET A 83 3155 3704 3893 -77 165 -459 C ATOM 95 O MET A 83 38.296 73.783 11.808 1.00 29.13 O ANISOU 95 O MET A 83 3282 3729 4057 -51 145 -476 O ATOM 96 CB MET A 83 36.712 71.032 12.086 1.00 27.23 C ANISOU 96 CB MET A 83 2892 3693 3761 -6 312 -432 C ATOM 97 CG MET A 83 37.651 69.977 11.401 1.00 25.47 C ANISOU 97 CG MET A 83 2619 3502 3557 -60 270 -346 C ATOM 98 SD MET A 83 38.643 69.058 12.586 1.00 26.99 S ANISOU 98 SD MET A 83 2863 3733 3657 -114 236 -322 S ATOM 99 CE MET A 83 37.368 68.002 13.373 1.00 20.28 C ANISOU 99 CE MET A 83 2024 2943 2739 -103 341 -327 C ATOM 100 N THR A 84 39.768 72.237 12.582 1.00 26.70 N ANISOU 100 N THR A 84 2942 3531 3673 -151 101 -411 N ATOM 101 CA THR A 84 40.927 72.871 11.962 1.00 25.37 C ANISOU 101 CA THR A 84 2759 3320 3558 -220 19 -374 C ATOM 102 C THR A 84 41.672 71.825 11.153 1.00 25.08 C ANISOU 102 C THR A 84 2614 3358 3557 -245 14 -290 C ATOM 103 O THR A 84 41.455 70.590 11.343 1.00 23.60 O ANISOU 103 O THR A 84 2392 3237 3340 -214 50 -268 O ATOM 104 CB THR A 84 41.914 73.405 13.007 1.00 26.88 C ANISOU 104 CB THR A 84 3024 3487 3701 -292 -71 -409 C ATOM 105 OG1 THR A 84 42.332 72.299 13.832 1.00 25.70 O ANISOU 105 OG1 THR A 84 2861 3421 3481 -299 -86 -391 O ATOM 106 CG2 THR A 84 41.280 74.588 13.894 1.00 26.22 C ANISOU 106 CG2 THR A 84 3084 3310 3569 -266 -76 -515 C ATOM 107 N TYR A 85 42.538 72.302 10.243 1.00 23.73 N ANISOU 107 N TYR A 85 2396 3172 3447 -302 -23 -243 N ATOM 108 CA TYR A 85 43.455 71.409 9.553 1.00 22.86 C ANISOU 108 CA TYR A 85 2179 3142 3365 -322 -25 -177 C ATOM 109 C TYR A 85 44.174 70.503 10.576 1.00 22.92 C ANISOU 109 C TYR A 85 2167 3212 3328 -324 -71 -176 C ATOM 110 O TYR A 85 44.252 69.266 10.429 1.00 22.16 O ANISOU 110 O TYR A 85 2021 3173 3224 -277 -48 -145 O ATOM 111 CB TYR A 85 44.487 72.198 8.708 1.00 23.05 C ANISOU 111 CB TYR A 85 2154 3156 3446 -407 -57 -131 C ATOM 112 CG TYR A 85 45.617 71.317 8.218 1.00 21.74 C ANISOU 112 CG TYR A 85 1861 3093 3305 -423 -56 -78 C ATOM 113 CD1 TYR A 85 45.562 70.739 6.949 1.00 18.18 C ANISOU 113 CD1 TYR A 85 1347 2686 2874 -387 13 -34 C ATOM 114 CD2 TYR A 85 46.750 71.062 9.026 1.00 21.86 C ANISOU 114 CD2 TYR A 85 1819 3165 3320 -463 -129 -77 C ATOM 115 CE1 TYR A 85 46.582 69.903 6.489 1.00 19.62 C ANISOU 115 CE1 TYR A 85 1412 2965 3076 -378 27 1 C ATOM 116 CE2 TYR A 85 47.814 70.247 8.550 1.00 22.04 C ANISOU 116 CE2 TYR A 85 1704 3291 3378 -455 -126 -33 C ATOM 117 CZ TYR A 85 47.711 69.676 7.288 1.00 20.83 C ANISOU 117 CZ TYR A 85 1492 3178 3245 -406 -39 1 C ATOM 118 OH TYR A 85 48.695 68.835 6.816 1.00 21.99 O ANISOU 118 OH TYR A 85 1507 3426 3420 -373 -22 29 O ATOM 119 N LYS A 86 44.733 71.109 11.614 1.00 23.95 N ANISOU 119 N LYS A 86 2349 3324 3426 -378 -149 -210 N ATOM 120 CA LYS A 86 45.537 70.318 12.563 1.00 24.82 C ANISOU 120 CA LYS A 86 2444 3496 3491 -382 -220 -201 C ATOM 121 C LYS A 86 44.748 69.284 13.379 1.00 23.72 C ANISOU 121 C LYS A 86 2373 3373 3266 -313 -184 -210 C ATOM 122 O LYS A 86 45.238 68.187 13.617 1.00 24.48 O ANISOU 122 O LYS A 86 2436 3519 3345 -283 -214 -169 O ATOM 123 CB LYS A 86 46.277 71.249 13.517 1.00 26.75 C ANISOU 123 CB LYS A 86 2742 3716 3707 -465 -330 -241 C ATOM 124 CG LYS A 86 47.256 70.519 14.444 1.00 32.00 C ANISOU 124 CG LYS A 86 3379 4450 4329 -473 -435 -224 C ATOM 125 CD LYS A 86 47.956 71.551 15.359 1.00 40.56 C ANISOU 125 CD LYS A 86 4524 5506 5382 -572 -561 -273 C ATOM 126 CE LYS A 86 48.753 70.849 16.479 1.00 43.93 C ANISOU 126 CE LYS A 86 4954 6000 5739 -569 -686 -264 C ATOM 127 NZ LYS A 86 49.705 69.828 15.924 1.00 43.80 N ANISOU 127 NZ LYS A 86 4763 6080 5798 -530 -716 -188 N ATOM 128 N ALA A 87 43.550 69.634 13.850 1.00 23.12 N ANISOU 128 N ALA A 87 2394 3255 3136 -289 -121 -261 N ATOM 129 CA ALA A 87 42.728 68.658 14.585 1.00 23.38 C ANISOU 129 CA ALA A 87 2487 3313 3085 -245 -66 -260 C ATOM 130 C ALA A 87 42.334 67.488 13.646 1.00 22.32 C ANISOU 130 C ALA A 87 2277 3204 3000 -203 -2 -204 C ATOM 131 O ALA A 87 42.409 66.284 14.021 1.00 22.79 O ANISOU 131 O ALA A 87 2353 3287 3019 -184 -7 -162 O ATOM 132 CB ALA A 87 41.446 69.341 15.216 1.00 22.30 C ANISOU 132 CB ALA A 87 2443 3143 2885 -225 14 -335 C ATOM 133 N ALA A 88 41.951 67.841 12.421 1.00 20.85 N ANISOU 133 N ALA A 88 2025 3000 2895 -190 45 -201 N ATOM 134 CA ALA A 88 41.546 66.836 11.439 1.00 20.43 C ANISOU 134 CA ALA A 88 1914 2965 2885 -155 96 -161 C ATOM 135 C ALA A 88 42.714 65.878 11.170 1.00 20.86 C ANISOU 135 C ALA A 88 1917 3051 2958 -141 44 -111 C ATOM 136 O ALA A 88 42.531 64.635 11.097 1.00 20.71 O ANISOU 136 O ALA A 88 1906 3035 2928 -108 59 -81 O ATOM 137 CB ALA A 88 41.039 67.517 10.129 1.00 18.21 C ANISOU 137 CB ALA A 88 1582 2662 2674 -145 135 -167 C ATOM 138 N LEU A 89 43.916 66.441 11.046 1.00 21.25 N ANISOU 138 N LEU A 89 1912 3121 3041 -167 -21 -102 N ATOM 139 CA LEU A 89 45.151 65.620 10.871 1.00 22.66 C ANISOU 139 CA LEU A 89 2015 3348 3248 -138 -75 -62 C ATOM 140 C LEU A 89 45.417 64.722 12.071 1.00 23.54 C ANISOU 140 C LEU A 89 2187 3464 3295 -111 -140 -45 C ATOM 141 O LEU A 89 45.635 63.505 11.922 1.00 23.54 O ANISOU 141 O LEU A 89 2180 3466 3299 -48 -147 -12 O ATOM 142 CB LEU A 89 46.402 66.501 10.652 1.00 22.38 C ANISOU 142 CB LEU A 89 1887 3353 3265 -190 -134 -57 C ATOM 143 CG LEU A 89 47.741 65.865 10.232 1.00 23.09 C ANISOU 143 CG LEU A 89 1846 3518 3408 -156 -174 -23 C ATOM 144 CD1 LEU A 89 47.726 65.523 8.731 1.00 18.40 C ANISOU 144 CD1 LEU A 89 1178 2948 2864 -118 -82 -7 C ATOM 145 CD2 LEU A 89 48.899 66.852 10.540 1.00 19.33 C ANISOU 145 CD2 LEU A 89 1286 3087 2969 -242 -255 -22 C ATOM 146 N ASP A 90 45.422 65.316 13.259 1.00 24.30 N ANISOU 146 N ASP A 90 2359 3552 3322 -154 -193 -69 N ATOM 147 CA ASP A 90 45.764 64.527 14.479 1.00 26.01 C ANISOU 147 CA ASP A 90 2652 3775 3455 -134 -272 -44 C ATOM 148 C ASP A 90 44.755 63.389 14.763 1.00 25.39 C ANISOU 148 C ASP A 90 2672 3661 3315 -102 -208 -16 C ATOM 149 O ASP A 90 45.129 62.251 15.110 1.00 25.89 O ANISOU 149 O ASP A 90 2770 3714 3351 -57 -259 35 O ATOM 150 CB ASP A 90 45.883 65.452 15.689 1.00 26.62 C ANISOU 150 CB ASP A 90 2815 3851 3447 -194 -339 -85 C ATOM 151 CG ASP A 90 47.084 66.407 15.600 1.00 29.17 C ANISOU 151 CG ASP A 90 3049 4205 3828 -246 -440 -102 C ATOM 152 OD1 ASP A 90 48.091 66.120 14.890 1.00 30.69 O ANISOU 152 OD1 ASP A 90 3102 4446 4113 -227 -480 -67 O ATOM 153 OD2 ASP A 90 47.018 67.453 16.274 1.00 31.71 O ANISOU 153 OD2 ASP A 90 3443 4503 4101 -310 -477 -155 O ATOM 154 N ILE A 91 43.479 63.688 14.567 1.00 24.74 N ANISOU 154 N ILE A 91 2626 3556 3218 -127 -99 -45 N ATOM 155 CA ILE A 91 42.426 62.715 14.851 1.00 24.07 C ANISOU 155 CA ILE A 91 2619 3446 3079 -128 -27 -19 C ATOM 156 C ILE A 91 42.421 61.618 13.799 1.00 23.86 C ANISOU 156 C ILE A 91 2546 3393 3125 -86 -9 19 C ATOM 157 O ILE A 91 42.291 60.412 14.122 1.00 24.67 O ANISOU 157 O ILE A 91 2724 3459 3192 -74 -20 68 O ATOM 158 CB ILE A 91 41.026 63.421 15.034 1.00 24.06 C ANISOU 158 CB ILE A 91 2647 3449 3047 -166 85 -70 C ATOM 159 CG1 ILE A 91 41.043 64.261 16.340 1.00 24.55 C ANISOU 159 CG1 ILE A 91 2802 3527 3001 -195 67 -113 C ATOM 160 CG2 ILE A 91 39.879 62.406 15.011 1.00 21.75 C ANISOU 160 CG2 ILE A 91 2387 3144 2732 -185 175 -40 C ATOM 161 CD1 ILE A 91 39.923 65.301 16.467 1.00 25.57 C ANISOU 161 CD1 ILE A 91 2938 3663 3116 -203 167 -189 C ATOM 162 N SER A 92 42.581 61.988 12.535 1.00 22.87 N ANISOU 162 N SER A 92 2318 3279 3094 -65 14 -2 N ATOM 163 CA SER A 92 42.640 60.911 11.546 1.00 22.93 C ANISOU 163 CA SER A 92 2300 3260 3155 -18 26 21 C ATOM 164 C SER A 92 43.886 60.057 11.735 1.00 23.88 C ANISOU 164 C SER A 92 2416 3375 3284 52 -62 57 C ATOM 165 O SER A 92 43.808 58.841 11.588 1.00 24.48 O ANISOU 165 O SER A 92 2547 3396 3359 94 -71 86 O ATOM 166 CB SER A 92 42.448 61.366 10.103 1.00 21.33 C ANISOU 166 CB SER A 92 2008 3070 3026 -9 77 -8 C ATOM 167 OG SER A 92 43.332 62.360 9.739 1.00 22.10 O ANISOU 167 OG SER A 92 2023 3212 3162 -9 52 -21 O ATOM 168 N HIS A 93 45.017 60.661 12.092 1.00 24.06 N ANISOU 168 N HIS A 93 2377 3448 3317 65 -137 56 N ATOM 169 CA HIS A 93 46.193 59.824 12.458 1.00 26.64 C ANISOU 169 CA HIS A 93 2689 3779 3653 146 -240 92 C ATOM 170 C HIS A 93 45.909 58.897 13.626 1.00 25.92 C ANISOU 170 C HIS A 93 2748 3629 3471 153 -293 141 C ATOM 171 O HIS A 93 46.257 57.745 13.562 1.00 26.55 O ANISOU 171 O HIS A 93 2867 3658 3563 232 -338 177 O ATOM 172 CB HIS A 93 47.487 60.629 12.676 1.00 26.10 C ANISOU 172 CB HIS A 93 2504 3792 3621 147 -325 84 C ATOM 173 CG HIS A 93 48.180 60.919 11.392 1.00 32.95 C ANISOU 173 CG HIS A 93 3215 4717 4587 177 -285 64 C ATOM 174 ND1 HIS A 93 47.622 61.732 10.419 1.00 36.33 N ANISOU 174 ND1 HIS A 93 3605 5154 5045 120 -187 35 N ATOM 175 CD2 HIS A 93 49.300 60.388 10.843 1.00 35.72 C ANISOU 175 CD2 HIS A 93 3445 5120 5008 268 -316 72 C ATOM 176 CE1 HIS A 93 48.427 61.769 9.372 1.00 36.42 C ANISOU 176 CE1 HIS A 93 3487 5225 5126 157 -158 31 C ATOM 177 NE2 HIS A 93 49.455 60.967 9.607 1.00 36.78 N ANISOU 177 NE2 HIS A 93 3469 5304 5200 248 -227 47 N ATOM 178 N PHE A 94 45.240 59.407 14.658 1.00 25.68 N ANISOU 178 N PHE A 94 2814 3598 3346 73 -282 141 N ATOM 179 CA PHE A 94 44.851 58.582 15.800 1.00 26.06 C ANISOU 179 CA PHE A 94 3025 3595 3283 58 -313 196 C ATOM 180 C PHE A 94 44.003 57.410 15.297 1.00 26.64 C ANISOU 180 C PHE A 94 3168 3586 3368 61 -244 229 C ATOM 181 O PHE A 94 44.278 56.258 15.634 1.00 28.30 O ANISOU 181 O PHE A 94 3476 3725 3553 107 -308 290 O ATOM 182 CB PHE A 94 44.138 59.440 16.851 1.00 24.94 C ANISOU 182 CB PHE A 94 2966 3482 3027 -33 -274 173 C ATOM 183 CG PHE A 94 43.524 58.651 17.994 1.00 29.58 C ANISOU 183 CG PHE A 94 3733 4029 3477 -73 -267 233 C ATOM 184 CD1 PHE A 94 44.203 58.502 19.207 1.00 29.79 C ANISOU 184 CD1 PHE A 94 3867 4061 3390 -65 -385 275 C ATOM 185 CD2 PHE A 94 42.261 58.067 17.860 1.00 29.19 C ANISOU 185 CD2 PHE A 94 3744 3941 3405 -131 -145 253 C ATOM 186 CE1 PHE A 94 43.624 57.795 20.265 1.00 33.17 C ANISOU 186 CE1 PHE A 94 4480 4452 3670 -112 -371 341 C ATOM 187 CE2 PHE A 94 41.671 57.341 18.913 1.00 31.87 C ANISOU 187 CE2 PHE A 94 4251 4249 3611 -190 -122 320 C ATOM 188 CZ PHE A 94 42.354 57.204 20.111 1.00 32.78 C ANISOU 188 CZ PHE A 94 4491 4364 3599 -180 -230 368 C ATOM 189 N LEU A 95 42.998 57.686 14.457 1.00 25.75 N ANISOU 189 N LEU A 95 3009 3474 3299 13 -128 189 N ATOM 190 CA LEU A 95 42.119 56.629 14.004 1.00 25.62 C ANISOU 190 CA LEU A 95 3058 3383 3295 -11 -72 214 C ATOM 191 C LEU A 95 42.875 55.569 13.216 1.00 27.12 C ANISOU 191 C LEU A 95 3246 3503 3554 90 -133 229 C ATOM 192 O LEU A 95 42.613 54.358 13.340 1.00 26.84 O ANISOU 192 O LEU A 95 3332 3367 3500 93 -152 276 O ATOM 193 CB LEU A 95 40.935 57.179 13.219 1.00 24.45 C ANISOU 193 CB LEU A 95 2841 3262 3188 -77 43 164 C ATOM 194 CG LEU A 95 39.919 57.894 14.130 1.00 24.86 C ANISOU 194 CG LEU A 95 2921 3362 3162 -168 121 153 C ATOM 195 CD1 LEU A 95 39.074 58.810 13.328 1.00 22.14 C ANISOU 195 CD1 LEU A 95 2468 3066 2878 -192 204 89 C ATOM 196 CD2 LEU A 95 39.008 56.906 14.901 1.00 29.41 C ANISOU 196 CD2 LEU A 95 3623 3894 3659 -251 169 213 C ATOM 197 N LYS A 96 43.843 56.020 12.431 1.00 27.91 N ANISOU 197 N LYS A 96 3218 3657 3732 172 -161 188 N ATOM 198 CA LYS A 96 44.619 55.108 11.654 1.00 29.87 C ANISOU 198 CA LYS A 96 3447 3857 4043 288 -204 185 C ATOM 199 C LYS A 96 45.449 54.207 12.583 1.00 32.28 C ANISOU 199 C LYS A 96 3844 4105 4316 372 -325 246 C ATOM 200 O LYS A 96 45.444 52.975 12.415 1.00 31.93 O ANISOU 200 O LYS A 96 3904 3947 4281 434 -358 273 O ATOM 201 CB LYS A 96 45.508 55.855 10.657 1.00 30.07 C ANISOU 201 CB LYS A 96 3299 3977 4149 351 -191 131 C ATOM 202 CG LYS A 96 46.590 54.987 9.989 1.00 31.58 C ANISOU 202 CG LYS A 96 3445 4150 4402 501 -235 120 C ATOM 203 CD LYS A 96 45.961 53.915 9.055 1.00 39.45 C ANISOU 203 CD LYS A 96 4533 5042 5415 534 -189 96 C ATOM 204 CE LYS A 96 47.093 52.977 8.483 1.00 43.75 C ANISOU 204 CE LYS A 96 5050 5557 6015 714 -234 72 C ATOM 205 NZ LYS A 96 46.551 51.958 7.576 1.00 45.06 N ANISOU 205 NZ LYS A 96 5323 5608 6188 751 -198 34 N ATOM 206 N GLU A 97 46.137 54.805 13.553 1.00 32.94 N ANISOU 206 N GLU A 97 3901 4254 4360 374 -403 269 N ATOM 207 CA GLU A 97 46.974 53.999 14.427 1.00 36.83 C ANISOU 207 CA GLU A 97 4475 4700 4820 464 -540 331 C ATOM 208 C GLU A 97 46.171 53.098 15.404 1.00 37.21 C ANISOU 208 C GLU A 97 4751 4631 4758 404 -559 412 C ATOM 209 O GLU A 97 46.611 51.996 15.708 1.00 38.35 O ANISOU 209 O GLU A 97 5006 4674 4893 493 -655 470 O ATOM 210 CB GLU A 97 48.055 54.844 15.118 1.00 37.99 C ANISOU 210 CB GLU A 97 4520 4957 4960 487 -645 330 C ATOM 211 CG GLU A 97 47.640 55.494 16.426 1.00 46.41 C ANISOU 211 CG GLU A 97 5687 6050 5898 375 -672 357 C ATOM 212 CD GLU A 97 48.453 56.780 16.773 1.00 55.31 C ANISOU 212 CD GLU A 97 6682 7300 7033 347 -735 316 C ATOM 213 OE1 GLU A 97 48.352 57.241 17.948 1.00 55.29 O ANISOU 213 OE1 GLU A 97 6777 7317 6915 278 -792 332 O ATOM 214 OE2 GLU A 97 49.165 57.322 15.868 1.00 57.48 O ANISOU 214 OE2 GLU A 97 6768 7648 7423 382 -724 267 O ATOM 215 N LYS A 98 44.992 53.532 15.854 1.00 36.18 N ANISOU 215 N LYS A 98 4690 4511 4546 256 -462 417 N ATOM 216 CA LYS A 98 44.185 52.682 16.767 1.00 37.68 C ANISOU 216 CA LYS A 98 5091 4604 4624 175 -455 502 C ATOM 217 C LYS A 98 43.390 51.565 16.089 1.00 37.36 C ANISOU 217 C LYS A 98 5141 4435 4621 145 -399 522 C ATOM 218 O LYS A 98 43.151 50.529 16.709 1.00 39.70 O ANISOU 218 O LYS A 98 5622 4610 4850 118 -440 609 O ATOM 219 CB LYS A 98 43.267 53.516 17.676 1.00 36.75 C ANISOU 219 CB LYS A 98 5016 4561 4388 31 -367 503 C ATOM 220 CG LYS A 98 44.050 54.417 18.642 1.00 41.22 C ANISOU 220 CG LYS A 98 5566 5219 4877 49 -454 496 C ATOM 221 CD LYS A 98 45.061 53.627 19.479 1.00 47.43 C ANISOU 221 CD LYS A 98 6470 5949 5603 137 -627 579 C ATOM 222 CE LYS A 98 45.717 54.477 20.564 1.00 53.32 C ANISOU 222 CE LYS A 98 7227 6786 6247 130 -727 575 C ATOM 223 NZ LYS A 98 46.687 55.467 19.957 1.00 55.97 N ANISOU 223 NZ LYS A 98 7346 7221 6700 191 -780 491 N ATOM 224 N GLY A 99 43.021 51.754 14.823 1.00 35.06 N ANISOU 224 N GLY A 99 4733 4159 4431 145 -318 447 N ATOM 225 CA GLY A 99 42.224 50.792 14.101 1.00 35.02 C ANISOU 225 CA GLY A 99 4805 4037 4463 101 -271 449 C ATOM 226 C GLY A 99 40.728 51.077 14.200 1.00 34.58 C ANISOU 226 C GLY A 99 4757 4011 4370 -79 -145 449 C ATOM 227 O GLY A 99 40.289 52.000 14.888 1.00 34.88 O ANISOU 227 O GLY A 99 4751 4156 4346 -156 -83 446 O ATOM 228 N GLY A 100 39.931 50.287 13.500 1.00 34.49 N ANISOU 228 N GLY A 100 4796 3908 4401 -144 -107 445 N ATOM 229 CA GLY A 100 38.491 50.436 13.594 1.00 33.26 C ANISOU 229 CA GLY A 100 4629 3785 4222 -319 5 450 C ATOM 230 C GLY A 100 37.875 51.217 12.457 1.00 31.18 C ANISOU 230 C GLY A 100 4193 3613 4042 -339 78 356 C ATOM 231 O GLY A 100 36.681 51.149 12.265 1.00 31.31 O ANISOU 231 O GLY A 100 4183 3643 4069 -469 153 351 O ATOM 232 N LEU A 101 38.655 51.979 11.697 1.00 29.60 N ANISOU 232 N LEU A 101 3868 3481 3899 -219 56 286 N ATOM 233 CA LEU A 101 38.028 52.806 10.669 1.00 28.11 C ANISOU 233 CA LEU A 101 3532 3378 3772 -243 120 210 C ATOM 234 C LEU A 101 38.500 52.451 9.272 1.00 28.53 C ANISOU 234 C LEU A 101 3558 3387 3896 -153 82 151 C ATOM 235 O LEU A 101 37.663 52.316 8.371 1.00 29.87 O ANISOU 235 O LEU A 101 3700 3547 4102 -211 110 112 O ATOM 236 CB LEU A 101 38.178 54.302 10.952 1.00 26.51 C ANISOU 236 CB LEU A 101 3202 3311 3558 -223 159 176 C ATOM 237 CG LEU A 101 37.342 55.206 10.033 1.00 24.97 C ANISOU 237 CG LEU A 101 2874 3196 3419 -256 222 111 C ATOM 238 CD1 LEU A 101 35.829 55.024 10.294 1.00 24.22 C ANISOU 238 CD1 LEU A 101 2772 3117 3316 -390 296 122 C ATOM 239 CD2 LEU A 101 37.730 56.676 10.244 1.00 24.72 C ANISOU 239 CD2 LEU A 101 2744 3265 3383 -213 238 78 C ATOM 240 N GLU A 102 39.814 52.310 9.109 1.00 28.17 N ANISOU 240 N GLU A 102 3514 3325 3863 -13 21 143 N ATOM 241 CA GLU A 102 40.444 51.753 7.900 1.00 28.67 C ANISOU 241 CA GLU A 102 3579 3337 3977 98 -10 88 C ATOM 242 C GLU A 102 39.741 50.473 7.477 1.00 29.33 C ANISOU 242 C GLU A 102 3803 3274 4068 46 -30 86 C ATOM 243 O GLU A 102 39.735 49.500 8.219 1.00 30.18 O ANISOU 243 O GLU A 102 4056 3261 4150 28 -77 146 O ATOM 244 CB GLU A 102 41.930 51.406 8.204 1.00 28.59 C ANISOU 244 CB GLU A 102 3581 3307 3975 256 -82 102 C ATOM 245 CG GLU A 102 42.760 50.795 7.016 1.00 30.18 C ANISOU 245 CG GLU A 102 3776 3467 4225 406 -101 36 C ATOM 246 CD GLU A 102 42.830 51.701 5.763 1.00 32.03 C ANISOU 246 CD GLU A 102 3868 3818 4483 421 -31 -38 C ATOM 247 OE1 GLU A 102 42.967 51.177 4.651 1.00 36.08 O ANISOU 247 OE1 GLU A 102 4407 4293 5010 489 -19 -101 O ATOM 248 OE2 GLU A 102 42.691 52.932 5.860 1.00 30.59 O ANISOU 248 OE2 GLU A 102 3568 3757 4298 361 11 -34 O ATOM 249 N GLY A 103 39.160 50.469 6.282 1.00 29.19 N ANISOU 249 N GLY A 103 3755 3258 4079 18 -5 20 N ATOM 250 CA GLY A 103 38.507 49.259 5.761 1.00 28.57 C ANISOU 250 CA GLY A 103 3815 3032 4009 -40 -38 3 C ATOM 251 C GLY A 103 37.078 49.049 6.229 1.00 28.66 C ANISOU 251 C GLY A 103 3855 3021 4013 -240 -13 46 C ATOM 252 O GLY A 103 36.471 48.022 5.912 1.00 28.93 O ANISOU 252 O GLY A 103 4010 2926 4058 -323 -48 42 O ATOM 253 N LEU A 104 36.511 50.026 6.941 1.00 27.81 N ANISOU 253 N LEU A 104 3635 3043 3890 -323 50 80 N ATOM 254 CA LEU A 104 35.105 49.922 7.373 1.00 28.44 C ANISOU 254 CA LEU A 104 3702 3137 3968 -511 97 115 C ATOM 255 C LEU A 104 34.129 50.370 6.267 1.00 27.97 C ANISOU 255 C LEU A 104 3522 3148 3956 -576 113 47 C ATOM 256 O LEU A 104 34.348 51.421 5.641 1.00 27.01 O ANISOU 256 O LEU A 104 3277 3136 3850 -495 128 -4 O ATOM 257 CB LEU A 104 34.901 50.775 8.645 1.00 28.71 C ANISOU 257 CB LEU A 104 3668 3285 3957 -554 167 169 C ATOM 258 CG LEU A 104 33.552 50.767 9.391 1.00 29.13 C ANISOU 258 CG LEU A 104 3690 3386 3991 -737 246 214 C ATOM 259 CD1 LEU A 104 33.348 49.443 10.125 1.00 28.44 C ANISOU 259 CD1 LEU A 104 3785 3157 3862 -849 228 302 C ATOM 260 CD2 LEU A 104 33.399 51.945 10.388 1.00 27.47 C ANISOU 260 CD2 LEU A 104 3381 3323 3733 -735 331 227 C ATOM 261 N ILE A 105 33.043 49.614 6.035 1.00 28.70 N ANISOU 261 N ILE A 105 3650 3180 4072 -729 101 51 N ATOM 262 CA ILE A 105 32.018 50.038 5.078 1.00 28.14 C ANISOU 262 CA ILE A 105 3453 3190 4049 -801 99 -8 C ATOM 263 C ILE A 105 31.331 51.333 5.545 1.00 28.53 C ANISOU 263 C ILE A 105 3311 3418 4111 -827 180 -1 C ATOM 264 O ILE A 105 30.874 51.453 6.698 1.00 28.74 O ANISOU 264 O ILE A 105 3311 3492 4118 -909 253 56 O ATOM 265 CB ILE A 105 30.956 48.920 4.785 1.00 30.60 C ANISOU 265 CB ILE A 105 3832 3403 4392 -984 56 -5 C ATOM 266 CG1 ILE A 105 31.582 47.678 4.108 1.00 30.75 C ANISOU 266 CG1 ILE A 105 4057 3225 4402 -943 -38 -38 C ATOM 267 CG2 ILE A 105 29.805 49.445 3.934 1.00 28.16 C ANISOU 267 CG2 ILE A 105 3360 3204 4135 -1067 44 -59 C ATOM 268 CD1 ILE A 105 31.927 47.848 2.615 1.00 31.82 C ANISOU 268 CD1 ILE A 105 4188 3363 4541 -831 -99 -144 C ATOM 269 N TRP A 106 31.286 52.314 4.648 1.00 28.47 N ANISOU 269 N TRP A 106 3185 3505 4128 -749 169 -61 N ATOM 270 CA TRP A 106 30.596 53.593 4.911 1.00 27.67 C ANISOU 270 CA TRP A 106 2907 3556 4050 -750 229 -68 C ATOM 271 C TRP A 106 29.112 53.356 5.036 1.00 29.43 C ANISOU 271 C TRP A 106 3028 3833 4320 -907 251 -62 C ATOM 272 O TRP A 106 28.524 52.544 4.279 1.00 31.17 O ANISOU 272 O TRP A 106 3271 3999 4574 -1002 185 -83 O ATOM 273 CB TRP A 106 30.834 54.620 3.789 1.00 25.92 C ANISOU 273 CB TRP A 106 2605 3400 3845 -637 192 -125 C ATOM 274 CG TRP A 106 30.253 55.971 4.121 1.00 25.42 C ANISOU 274 CG TRP A 106 2387 3466 3807 -610 244 -132 C ATOM 275 CD1 TRP A 106 30.858 56.979 4.846 1.00 22.90 C ANISOU 275 CD1 TRP A 106 2044 3194 3463 -525 297 -121 C ATOM 276 CD2 TRP A 106 28.948 56.456 3.767 1.00 27.46 C ANISOU 276 CD2 TRP A 106 2496 3816 4123 -661 240 -156 C ATOM 277 NE1 TRP A 106 30.001 58.050 4.962 1.00 26.24 N ANISOU 277 NE1 TRP A 106 2331 3717 3923 -513 331 -142 N ATOM 278 CE2 TRP A 106 28.818 57.748 4.325 1.00 27.82 C ANISOU 278 CE2 TRP A 106 2441 3952 4178 -587 300 -162 C ATOM 279 CE3 TRP A 106 27.854 55.899 3.074 1.00 27.16 C ANISOU 279 CE3 TRP A 106 2395 3790 4134 -763 184 -177 C ATOM 280 CZ2 TRP A 106 27.653 58.503 4.189 1.00 28.63 C ANISOU 280 CZ2 TRP A 106 2380 4157 4341 -589 309 -188 C ATOM 281 CZ3 TRP A 106 26.707 56.657 2.922 1.00 29.82 C ANISOU 281 CZ3 TRP A 106 2552 4244 4535 -776 186 -198 C ATOM 282 CH2 TRP A 106 26.610 57.946 3.479 1.00 29.24 C ANISOU 282 CH2 TRP A 106 2377 4260 4474 -679 251 -204 C ATOM 283 N SER A 107 28.510 54.051 5.997 1.00 29.25 N ANISOU 283 N SER A 107 2892 3921 4301 -938 345 -40 N ATOM 284 CA SER A 107 27.074 54.316 5.991 1.00 30.18 C ANISOU 284 CA SER A 107 2832 4152 4481 -1041 382 -53 C ATOM 285 C SER A 107 26.857 55.641 6.715 1.00 30.89 C ANISOU 285 C SER A 107 2793 4375 4567 -958 476 -67 C ATOM 286 O SER A 107 27.730 56.083 7.495 1.00 30.02 O ANISOU 286 O SER A 107 2761 4252 4393 -874 521 -50 O ATOM 287 CB SER A 107 26.313 53.229 6.719 1.00 30.72 C ANISOU 287 CB SER A 107 2924 4197 4550 -1236 431 2 C ATOM 288 OG SER A 107 26.681 53.230 8.083 1.00 30.75 O ANISOU 288 OG SER A 107 2999 4205 4479 -1244 533 61 O ATOM 289 N GLN A 108 25.683 56.234 6.497 1.00 32.63 N ANISOU 289 N GLN A 108 2821 4719 4859 -980 498 -101 N ATOM 290 CA GLN A 108 25.282 57.489 7.149 1.00 34.15 C ANISOU 290 CA GLN A 108 2880 5035 5059 -892 589 -128 C ATOM 291 C GLN A 108 25.334 57.307 8.672 1.00 35.01 C ANISOU 291 C GLN A 108 3040 5171 5092 -949 725 -87 C ATOM 292 O GLN A 108 25.863 58.145 9.385 1.00 33.86 O ANISOU 292 O GLN A 108 2928 5047 4890 -846 780 -100 O ATOM 293 CB GLN A 108 23.870 57.938 6.685 1.00 36.06 C ANISOU 293 CB GLN A 108 2889 5408 5403 -914 588 -170 C ATOM 294 CG GLN A 108 23.479 59.366 7.095 1.00 38.63 C ANISOU 294 CG GLN A 108 3078 5845 5753 -773 657 -219 C ATOM 295 CD GLN A 108 24.530 60.365 6.649 1.00 44.61 C ANISOU 295 CD GLN A 108 3935 6534 6481 -602 591 -242 C ATOM 296 OE1 GLN A 108 24.806 60.495 5.447 1.00 48.43 O ANISOU 296 OE1 GLN A 108 4443 6968 6991 -552 469 -252 O ATOM 297 NE2 GLN A 108 25.161 61.049 7.610 1.00 46.56 N ANISOU 297 NE2 GLN A 108 4254 6775 6663 -525 670 -248 N ATOM 298 N ARG A 109 24.813 56.182 9.145 1.00 36.92 N ANISOU 298 N ARG A 109 3305 5402 5322 -1123 771 -33 N ATOM 299 CA ARG A 109 24.830 55.858 10.556 1.00 38.65 C ANISOU 299 CA ARG A 109 3597 5640 5447 -1201 898 23 C ATOM 300 C ARG A 109 26.242 55.690 11.163 1.00 37.14 C ANISOU 300 C ARG A 109 3632 5332 5145 -1131 872 63 C ATOM 301 O ARG A 109 26.508 56.202 12.260 1.00 36.98 O ANISOU 301 O ARG A 109 3655 5359 5037 -1091 960 71 O ATOM 302 CB ARG A 109 23.979 54.622 10.819 1.00 40.91 C ANISOU 302 CB ARG A 109 3875 5922 5745 -1425 941 87 C ATOM 303 CG ARG A 109 23.783 54.335 12.296 1.00 47.58 C ANISOU 303 CG ARG A 109 4780 6816 6484 -1528 1095 154 C ATOM 304 CD ARG A 109 23.047 55.502 13.010 1.00 56.69 C ANISOU 304 CD ARG A 109 5749 8163 7628 -1461 1248 98 C ATOM 305 NE ARG A 109 22.968 55.294 14.462 1.00 63.25 N ANISOU 305 NE ARG A 109 6664 9045 8323 -1544 1405 157 N ATOM 306 CZ ARG A 109 23.576 56.057 15.369 1.00 64.29 C ANISOU 306 CZ ARG A 109 6886 9203 8340 -1425 1468 136 C ATOM 307 NH1 ARG A 109 24.292 57.116 14.987 1.00 60.59 N ANISOU 307 NH1 ARG A 109 6422 8711 7889 -1225 1390 58 N ATOM 308 NH2 ARG A 109 23.443 55.768 16.664 1.00 65.61 N ANISOU 308 NH2 ARG A 109 7144 9418 8365 -1519 1608 193 N ATOM 309 N ARG A 110 27.146 54.989 10.467 1.00 35.67 N ANISOU 309 N ARG A 110 3588 5002 4962 -1109 750 82 N ATOM 310 CA ARG A 110 28.528 54.877 10.970 1.00 33.45 C ANISOU 310 CA ARG A 110 3491 4625 4596 -1021 710 115 C ATOM 311 C ARG A 110 29.219 56.243 10.996 1.00 31.43 C ANISOU 311 C ARG A 110 3193 4422 4327 -853 705 58 C ATOM 312 O ARG A 110 29.977 56.547 11.923 1.00 29.89 O ANISOU 312 O ARG A 110 3090 4221 4046 -802 725 77 O ATOM 313 CB ARG A 110 29.339 53.853 10.190 1.00 32.69 C ANISOU 313 CB ARG A 110 3536 4371 4514 -1010 589 135 C ATOM 314 CG ARG A 110 28.919 52.414 10.464 1.00 33.61 C ANISOU 314 CG ARG A 110 3767 4386 4616 -1176 585 206 C ATOM 315 CD ARG A 110 29.621 51.447 9.519 1.00 32.67 C ANISOU 315 CD ARG A 110 3785 4103 4526 -1145 458 201 C ATOM 316 NE ARG A 110 29.465 50.061 9.954 1.00 35.46 N ANISOU 316 NE ARG A 110 4304 4317 4851 -1285 440 279 N ATOM 317 CZ ARG A 110 29.596 48.987 9.175 1.00 36.39 C ANISOU 317 CZ ARG A 110 4542 4279 5005 -1321 343 273 C ATOM 318 NH1 ARG A 110 29.907 49.096 7.883 1.00 32.86 N ANISOU 318 NH1 ARG A 110 4069 3805 4613 -1223 259 189 N ATOM 319 NH2 ARG A 110 29.441 47.779 9.709 1.00 39.58 N ANISOU 319 NH2 ARG A 110 5117 4542 5379 -1456 329 354 N ATOM 320 N GLN A 111 28.930 57.084 10.003 1.00 31.02 N ANISOU 320 N GLN A 111 3011 4420 4356 -776 671 -8 N ATOM 321 CA GLN A 111 29.530 58.427 9.984 1.00 30.30 C ANISOU 321 CA GLN A 111 2889 4364 4258 -633 662 -57 C ATOM 322 C GLN A 111 29.002 59.302 11.125 1.00 31.65 C ANISOU 322 C GLN A 111 3005 4635 4385 -618 775 -82 C ATOM 323 O GLN A 111 29.763 60.084 11.732 1.00 31.21 O ANISOU 323 O GLN A 111 3012 4575 4271 -536 779 -100 O ATOM 324 CB GLN A 111 29.324 59.137 8.666 1.00 28.93 C ANISOU 324 CB GLN A 111 2613 4208 4171 -556 595 -109 C ATOM 325 CG GLN A 111 30.394 60.193 8.482 1.00 30.79 C ANISOU 325 CG GLN A 111 2886 4421 4390 -428 553 -133 C ATOM 326 CD GLN A 111 30.157 61.092 7.318 1.00 31.12 C ANISOU 326 CD GLN A 111 2843 4483 4500 -352 498 -174 C ATOM 327 OE1 GLN A 111 30.064 60.646 6.182 1.00 32.81 O ANISOU 327 OE1 GLN A 111 3047 4670 4749 -363 430 -174 O ATOM 328 NE2 GLN A 111 30.086 62.386 7.588 1.00 34.57 N ANISOU 328 NE2 GLN A 111 3236 4955 4944 -270 521 -210 N ATOM 329 N GLU A 112 27.707 59.161 11.421 1.00 33.27 N ANISOU 329 N GLU A 112 3093 4933 4616 -701 868 -88 N ATOM 330 CA GLU A 112 27.082 59.898 12.510 1.00 35.28 C ANISOU 330 CA GLU A 112 3286 5297 4822 -685 1000 -121 C ATOM 331 C GLU A 112 27.795 59.534 13.815 1.00 34.79 C ANISOU 331 C GLU A 112 3398 5204 4617 -723 1049 -72 C ATOM 332 O GLU A 112 28.165 60.421 14.590 1.00 35.04 O ANISOU 332 O GLU A 112 3474 5263 4575 -642 1087 -112 O ATOM 333 CB GLU A 112 25.570 59.612 12.582 1.00 37.37 C ANISOU 333 CB GLU A 112 3374 5681 5143 -785 1102 -128 C ATOM 334 CG GLU A 112 24.758 60.378 11.516 1.00 44.42 C ANISOU 334 CG GLU A 112 4068 6639 6169 -704 1058 -196 C ATOM 335 CD GLU A 112 23.228 60.150 11.556 1.00 54.96 C ANISOU 335 CD GLU A 112 5185 8117 7581 -794 1150 -209 C ATOM 336 OE1 GLU A 112 22.615 60.204 10.463 1.00 59.88 O ANISOU 336 OE1 GLU A 112 5667 8764 8319 -785 1064 -233 O ATOM 337 OE2 GLU A 112 22.625 59.934 12.649 1.00 59.29 O ANISOU 337 OE2 GLU A 112 5694 8764 8072 -877 1305 -196 O ATOM 338 N ILE A 113 28.006 58.238 14.032 1.00 34.59 N ANISOU 338 N ILE A 113 3484 5110 4549 -843 1032 13 N ATOM 339 CA ILE A 113 28.732 57.748 15.213 1.00 35.35 C ANISOU 339 CA ILE A 113 3768 5160 4502 -880 1050 78 C ATOM 340 C ILE A 113 30.123 58.398 15.335 1.00 33.17 C ANISOU 340 C ILE A 113 3598 4823 4183 -746 951 56 C ATOM 341 O ILE A 113 30.465 58.927 16.377 1.00 33.76 O ANISOU 341 O ILE A 113 3749 4929 4147 -715 990 45 O ATOM 342 CB ILE A 113 28.808 56.183 15.247 1.00 36.45 C ANISOU 342 CB ILE A 113 4031 5198 4619 -1019 1015 181 C ATOM 343 CG1 ILE A 113 27.401 55.592 15.458 1.00 37.70 C ANISOU 343 CG1 ILE A 113 4094 5435 4796 -1190 1137 213 C ATOM 344 CG2 ILE A 113 29.718 55.692 16.398 1.00 37.31 C ANISOU 344 CG2 ILE A 113 4358 5240 4579 -1031 997 258 C ATOM 345 CD1 ILE A 113 27.294 54.098 15.175 1.00 40.03 C ANISOU 345 CD1 ILE A 113 4490 5611 5109 -1343 1085 304 C ATOM 346 N LEU A 114 30.869 58.412 14.241 1.00 31.21 N ANISOU 346 N LEU A 114 3341 4497 4019 -673 829 43 N ATOM 347 CA LEU A 114 32.189 59.007 14.186 1.00 29.89 C ANISOU 347 CA LEU A 114 3239 4282 3835 -561 733 24 C ATOM 348 C LEU A 114 32.109 60.504 14.499 1.00 29.40 C ANISOU 348 C LEU A 114 3117 4290 3763 -479 772 -57 C ATOM 349 O LEU A 114 32.807 60.967 15.389 1.00 29.71 O ANISOU 349 O LEU A 114 3248 4329 3713 -446 758 -64 O ATOM 350 CB LEU A 114 32.817 58.781 12.797 1.00 28.15 C ANISOU 350 CB LEU A 114 2989 3991 3715 -506 625 18 C ATOM 351 CG LEU A 114 34.286 59.095 12.589 1.00 28.58 C ANISOU 351 CG LEU A 114 3098 3996 3766 -410 524 16 C ATOM 352 CD1 LEU A 114 35.138 58.365 13.636 1.00 28.71 C ANISOU 352 CD1 LEU A 114 3259 3964 3686 -422 483 79 C ATOM 353 CD2 LEU A 114 34.740 58.723 11.171 1.00 27.02 C ANISOU 353 CD2 LEU A 114 2866 3745 3656 -367 450 10 C ATOM 354 N ASP A 115 31.252 61.240 13.786 1.00 28.55 N ANISOU 354 N ASP A 115 2867 4236 3746 -444 808 -117 N ATOM 355 CA ASP A 115 31.026 62.659 14.056 1.00 29.28 C ANISOU 355 CA ASP A 115 2910 4377 3840 -356 846 -199 C ATOM 356 C ASP A 115 30.640 62.992 15.502 1.00 29.91 C ANISOU 356 C ASP A 115 3043 4523 3798 -370 958 -227 C ATOM 357 O ASP A 115 31.163 63.943 16.086 1.00 30.26 O ANISOU 357 O ASP A 115 3154 4559 3785 -303 946 -280 O ATOM 358 CB ASP A 115 29.976 63.248 13.107 1.00 30.20 C ANISOU 358 CB ASP A 115 2862 4540 4074 -312 867 -250 C ATOM 359 CG ASP A 115 30.531 63.494 11.702 1.00 31.76 C ANISOU 359 CG ASP A 115 3032 4672 4364 -258 747 -248 C ATOM 360 OD1 ASP A 115 31.729 63.781 11.547 1.00 32.85 O ANISOU 360 OD1 ASP A 115 3254 4744 4484 -221 669 -238 O ATOM 361 OD2 ASP A 115 29.753 63.411 10.740 1.00 38.78 O ANISOU 361 OD2 ASP A 115 3811 5583 5341 -258 731 -256 O ATOM 362 N LEU A 116 29.759 62.194 16.078 1.00 30.06 N ANISOU 362 N LEU A 116 3044 4607 3771 -467 1067 -191 N ATOM 363 CA LEU A 116 29.284 62.451 17.418 1.00 31.32 C ANISOU 363 CA LEU A 116 3251 4848 3800 -488 1199 -216 C ATOM 364 C LEU A 116 30.400 62.162 18.442 1.00 30.95 C ANISOU 364 C LEU A 116 3411 4748 3599 -510 1149 -171 C ATOM 365 O LEU A 116 30.510 62.851 19.451 1.00 30.98 O ANISOU 365 O LEU A 116 3498 4790 3485 -475 1199 -222 O ATOM 366 CB LEU A 116 28.030 61.610 17.697 1.00 32.17 C ANISOU 366 CB LEU A 116 3272 5051 3902 -610 1339 -176 C ATOM 367 CG LEU A 116 26.711 62.097 17.077 1.00 36.67 C ANISOU 367 CG LEU A 116 3611 5723 4598 -580 1422 -242 C ATOM 368 CD1 LEU A 116 25.522 61.122 17.370 1.00 37.37 C ANISOU 368 CD1 LEU A 116 3599 5915 4685 -737 1557 -188 C ATOM 369 CD2 LEU A 116 26.344 63.497 17.609 1.00 40.37 C ANISOU 369 CD2 LEU A 116 4032 6265 5041 -443 1506 -360 C ATOM 370 N TRP A 117 31.204 61.135 18.172 1.00 29.39 N ANISOU 370 N TRP A 117 3301 4462 3403 -560 1042 -79 N ATOM 371 CA TRP A 117 32.307 60.783 19.049 1.00 31.13 C ANISOU 371 CA TRP A 117 3706 4628 3494 -569 964 -27 C ATOM 372 C TRP A 117 33.357 61.909 19.070 1.00 30.47 C ANISOU 372 C TRP A 117 3654 4514 3408 -462 860 -95 C ATOM 373 O TRP A 117 33.871 62.246 20.133 1.00 31.27 O ANISOU 373 O TRP A 117 3883 4625 3374 -455 843 -107 O ATOM 374 CB TRP A 117 32.959 59.457 18.605 1.00 30.59 C ANISOU 374 CB TRP A 117 3707 4459 3455 -616 858 78 C ATOM 375 CG TRP A 117 34.209 59.067 19.377 1.00 31.68 C ANISOU 375 CG TRP A 117 4021 4534 3483 -599 743 137 C ATOM 376 CD1 TRP A 117 34.267 58.541 20.654 1.00 32.72 C ANISOU 376 CD1 TRP A 117 4319 4671 3443 -662 767 203 C ATOM 377 CD2 TRP A 117 35.575 59.131 18.909 1.00 30.00 C ANISOU 377 CD2 TRP A 117 3826 4249 3323 -512 580 141 C ATOM 378 NE1 TRP A 117 35.588 58.284 20.996 1.00 34.86 N ANISOU 378 NE1 TRP A 117 4711 4872 3662 -611 610 248 N ATOM 379 CE2 TRP A 117 36.401 58.644 19.945 1.00 32.97 C ANISOU 379 CE2 TRP A 117 4368 4592 3567 -518 499 207 C ATOM 380 CE3 TRP A 117 36.173 59.556 17.722 1.00 30.57 C ANISOU 380 CE3 TRP A 117 3787 4292 3536 -434 500 100 C ATOM 381 CZ2 TRP A 117 37.794 58.569 19.818 1.00 32.96 C ANISOU 381 CZ2 TRP A 117 4397 4536 3588 -440 334 225 C ATOM 382 CZ3 TRP A 117 37.564 59.490 17.598 1.00 29.86 C ANISOU 382 CZ3 TRP A 117 3729 4153 3462 -366 357 118 C ATOM 383 CH2 TRP A 117 38.354 59.002 18.642 1.00 31.49 C ANISOU 383 CH2 TRP A 117 4076 4335 3553 -366 274 178 C ATOM 384 N ILE A 118 33.670 62.472 17.901 1.00 28.38 N ANISOU 384 N ILE A 118 3284 4213 3287 -393 786 -134 N ATOM 385 CA ILE A 118 34.600 63.584 17.826 1.00 28.12 C ANISOU 385 CA ILE A 118 3268 4148 3268 -316 694 -193 C ATOM 386 C ILE A 118 34.041 64.839 18.522 1.00 29.91 C ANISOU 386 C ILE A 118 3505 4422 3437 -271 774 -297 C ATOM 387 O ILE A 118 34.760 65.545 19.249 1.00 31.33 O ANISOU 387 O ILE A 118 3788 4583 3534 -247 718 -340 O ATOM 388 CB ILE A 118 34.990 63.889 16.357 1.00 26.67 C ANISOU 388 CB ILE A 118 2973 3917 3242 -266 614 -201 C ATOM 389 CG1 ILE A 118 35.754 62.700 15.786 1.00 24.24 C ANISOU 389 CG1 ILE A 118 2682 3559 2971 -289 530 -116 C ATOM 390 CG2 ILE A 118 35.768 65.166 16.281 1.00 23.87 C ANISOU 390 CG2 ILE A 118 2629 3533 2907 -208 541 -262 C ATOM 391 CD1 ILE A 118 36.089 62.771 14.306 1.00 26.27 C ANISOU 391 CD1 ILE A 118 2839 3781 3360 -249 472 -117 C ATOM 392 N TYR A 119 32.755 65.095 18.311 1.00 30.27 N ANISOU 392 N TYR A 119 3445 4529 3528 -257 900 -342 N ATOM 393 CA TYR A 119 32.037 66.116 19.037 1.00 31.12 C ANISOU 393 CA TYR A 119 3557 4691 3575 -201 1005 -445 C ATOM 394 C TYR A 119 32.047 65.934 20.573 1.00 32.59 C ANISOU 394 C TYR A 119 3895 4928 3558 -244 1079 -452 C ATOM 395 O TYR A 119 32.310 66.892 21.313 1.00 33.53 O ANISOU 395 O TYR A 119 4112 5041 3588 -191 1076 -539 O ATOM 396 CB TYR A 119 30.608 66.156 18.537 1.00 31.80 C ANISOU 396 CB TYR A 119 3475 4855 3753 -181 1130 -476 C ATOM 397 CG TYR A 119 29.744 67.207 19.205 1.00 34.21 C ANISOU 397 CG TYR A 119 3756 5227 4015 -95 1255 -594 C ATOM 398 CD1 TYR A 119 30.081 68.554 19.158 1.00 36.58 C ANISOU 398 CD1 TYR A 119 4099 5461 4337 18 1200 -693 C ATOM 399 CD2 TYR A 119 28.585 66.850 19.844 1.00 38.17 C ANISOU 399 CD2 TYR A 119 4190 5854 4461 -126 1432 -609 C ATOM 400 CE1 TYR A 119 29.261 69.534 19.745 1.00 39.65 C ANISOU 400 CE1 TYR A 119 4475 5897 4692 121 1314 -816 C ATOM 401 CE2 TYR A 119 27.760 67.806 20.462 1.00 42.69 C ANISOU 401 CE2 TYR A 119 4727 6500 4993 -26 1564 -730 C ATOM 402 CZ TYR A 119 28.105 69.145 20.403 1.00 43.65 C ANISOU 402 CZ TYR A 119 4904 6543 5138 108 1501 -839 C ATOM 403 OH TYR A 119 27.282 70.080 20.999 1.00 46.65 O ANISOU 403 OH TYR A 119 5260 6983 5482 227 1630 -970 O ATOM 404 N HIS A 120 31.728 64.727 21.036 1.00 32.07 N ANISOU 404 N HIS A 120 3862 4907 3414 -344 1144 -361 N ATOM 405 CA HIS A 120 31.677 64.417 22.448 1.00 33.48 C ANISOU 405 CA HIS A 120 4197 5139 3384 -401 1222 -346 C ATOM 406 C HIS A 120 33.041 64.427 23.142 1.00 32.52 C ANISOU 406 C HIS A 120 4266 4950 3141 -404 1070 -320 C ATOM 407 O HIS A 120 33.138 64.790 24.312 1.00 32.73 O ANISOU 407 O HIS A 120 4438 5012 2987 -405 1105 -362 O ATOM 408 CB HIS A 120 30.976 63.062 22.679 1.00 34.33 C ANISOU 408 CB HIS A 120 4298 5298 3447 -528 1325 -234 C ATOM 409 CG HIS A 120 29.513 63.072 22.345 1.00 38.56 C ANISOU 409 CG HIS A 120 4650 5939 4063 -548 1500 -267 C ATOM 410 ND1 HIS A 120 28.831 61.936 21.937 1.00 40.66 N ANISOU 410 ND1 HIS A 120 4832 6228 4389 -666 1555 -173 N ATOM 411 CD2 HIS A 120 28.596 64.076 22.371 1.00 38.70 C ANISOU 411 CD2 HIS A 120 4543 6046 4116 -463 1624 -386 C ATOM 412 CE1 HIS A 120 27.558 62.241 21.736 1.00 40.93 C ANISOU 412 CE1 HIS A 120 4681 6377 4494 -663 1706 -230 C ATOM 413 NE2 HIS A 120 27.393 63.533 21.978 1.00 41.75 N ANISOU 413 NE2 HIS A 120 4751 6524 4588 -529 1751 -359 N ATOM 414 N THR A 121 34.091 64.036 22.433 1.00 30.77 N ANISOU 414 N THR A 121 4039 4640 3014 -401 902 -256 N ATOM 415 CA THR A 121 35.416 63.961 23.060 1.00 31.23 C ANISOU 415 CA THR A 121 4247 4647 2973 -403 742 -224 C ATOM 416 C THR A 121 36.200 65.254 22.935 1.00 31.33 C ANISOU 416 C THR A 121 4261 4619 3024 -334 633 -322 C ATOM 417 O THR A 121 36.969 65.612 23.839 1.00 31.70 O ANISOU 417 O THR A 121 4448 4656 2942 -337 541 -346 O ATOM 418 CB THR A 121 36.275 62.825 22.485 1.00 30.45 C ANISOU 418 CB THR A 121 4145 4478 2946 -426 609 -105 C ATOM 419 OG1 THR A 121 36.294 62.928 21.047 1.00 29.39 O ANISOU 419 OG1 THR A 121 3843 4308 3016 -387 580 -115 O ATOM 420 CG2 THR A 121 35.695 61.492 22.892 1.00 30.03 C ANISOU 420 CG2 THR A 121 4160 4435 2814 -512 684 3 C ATOM 421 N GLN A 122 36.013 65.959 21.818 1.00 30.07 N ANISOU 421 N GLN A 122 3956 4431 3037 -280 633 -375 N ATOM 422 CA GLN A 122 36.862 67.105 21.542 1.00 29.96 C ANISOU 422 CA GLN A 122 3945 4359 3081 -236 514 -445 C ATOM 423 C GLN A 122 36.113 68.398 21.306 1.00 30.23 C ANISOU 423 C GLN A 122 3936 4382 3167 -169 591 -565 C ATOM 424 O GLN A 122 36.728 69.441 21.283 1.00 30.93 O ANISOU 424 O GLN A 122 4065 4409 3276 -145 502 -632 O ATOM 425 CB GLN A 122 37.817 66.795 20.360 1.00 28.68 C ANISOU 425 CB GLN A 122 3679 4142 3075 -236 386 -378 C ATOM 426 CG GLN A 122 38.816 65.683 20.651 1.00 27.50 C ANISOU 426 CG GLN A 122 3582 3987 2881 -273 274 -276 C ATOM 427 CD GLN A 122 40.010 66.128 21.517 1.00 31.97 C ANISOU 427 CD GLN A 122 4254 4540 3353 -286 124 -294 C ATOM 428 OE1 GLN A 122 41.056 66.596 20.992 1.00 31.04 O ANISOU 428 OE1 GLN A 122 4073 4392 3329 -281 -2 -299 O ATOM 429 NE2 GLN A 122 39.886 65.934 22.845 1.00 27.84 N ANISOU 429 NE2 GLN A 122 3890 4047 2639 -313 133 -297 N ATOM 430 N GLY A 123 34.796 68.342 21.095 1.00 31.35 N ANISOU 430 N GLY A 123 3991 4579 3341 -138 748 -591 N ATOM 431 CA GLY A 123 33.996 69.570 20.958 1.00 31.41 C ANISOU 431 CA GLY A 123 3960 4580 3396 -47 824 -712 C ATOM 432 C GLY A 123 33.856 70.117 19.545 1.00 30.75 C ANISOU 432 C GLY A 123 3739 4438 3509 8 780 -716 C ATOM 433 O GLY A 123 33.334 71.236 19.353 1.00 31.23 O ANISOU 433 O GLY A 123 3782 4462 3620 98 808 -812 O ATOM 434 N TYR A 124 34.293 69.360 18.544 1.00 28.36 N ANISOU 434 N TYR A 124 3349 4118 3308 -35 709 -616 N ATOM 435 CA TYR A 124 34.181 69.875 17.177 1.00 29.03 C ANISOU 435 CA TYR A 124 3321 4152 3557 12 665 -614 C ATOM 436 C TYR A 124 32.777 69.680 16.658 1.00 30.03 C ANISOU 436 C TYR A 124 3311 4341 3757 56 778 -626 C ATOM 437 O TYR A 124 32.331 68.550 16.556 1.00 28.89 O ANISOU 437 O TYR A 124 3104 4262 3612 -1 832 -561 O ATOM 438 CB TYR A 124 35.235 69.229 16.246 1.00 27.57 C ANISOU 438 CB TYR A 124 3100 3930 3445 -42 550 -516 C ATOM 439 CG TYR A 124 36.641 69.614 16.679 1.00 27.30 C ANISOU 439 CG TYR A 124 3165 3844 3365 -79 427 -514 C ATOM 440 CD1 TYR A 124 37.095 70.913 16.518 1.00 25.99 C ANISOU 440 CD1 TYR A 124 3039 3602 3236 -58 359 -573 C ATOM 441 CD2 TYR A 124 37.491 68.691 17.253 1.00 25.04 C ANISOU 441 CD2 TYR A 124 2931 3581 3003 -136 370 -451 C ATOM 442 CE1 TYR A 124 38.356 71.289 16.917 1.00 26.81 C ANISOU 442 CE1 TYR A 124 3218 3664 3306 -111 241 -572 C ATOM 443 CE2 TYR A 124 38.763 69.059 17.652 1.00 27.46 C ANISOU 443 CE2 TYR A 124 3303 3855 3278 -169 244 -451 C ATOM 444 CZ TYR A 124 39.181 70.370 17.504 1.00 28.21 C ANISOU 444 CZ TYR A 124 3423 3884 3410 -165 183 -515 C ATOM 445 OH TYR A 124 40.440 70.754 17.920 1.00 29.79 O ANISOU 445 OH TYR A 124 3677 4058 3585 -218 51 -517 O ATOM 446 N PHE A 125 32.051 70.761 16.349 1.00 32.73 N ANISOU 446 N PHE A 125 3608 4662 4166 156 808 -708 N ATOM 447 CA APHE A 125 30.690 70.617 15.817 0.70 34.23 C ANISOU 447 CA APHE A 125 3640 4925 4442 209 900 -722 C ATOM 448 CA BPHE A 125 30.692 70.560 15.869 0.30 33.86 C ANISOU 448 CA BPHE A 125 3594 4882 4388 204 905 -720 C ATOM 449 C PHE A 125 30.694 69.705 14.602 1.00 32.74 C ANISOU 449 C PHE A 125 3344 4745 4352 153 846 -624 C ATOM 450 O PHE A 125 31.518 69.883 13.732 1.00 33.32 O ANISOU 450 O PHE A 125 3438 4739 4481 145 733 -582 O ATOM 451 CB APHE A 125 30.050 71.975 15.454 0.70 35.70 C ANISOU 451 CB APHE A 125 3791 5062 4710 350 900 -816 C ATOM 452 CB BPHE A 125 29.786 71.822 15.775 0.30 35.33 C ANISOU 452 CB BPHE A 125 3734 5053 4636 349 947 -828 C ATOM 453 CG APHE A 125 28.530 71.932 15.423 0.70 38.31 C ANISOU 453 CG APHE A 125 3959 5501 5094 427 1024 -863 C ATOM 454 CG BPHE A 125 30.500 73.153 15.755 0.30 35.79 C ANISOU 454 CG BPHE A 125 3922 4974 4703 416 850 -890 C ATOM 455 CD1APHE A 125 27.794 72.074 16.592 0.70 40.37 C ANISOU 455 CD1APHE A 125 4221 5853 5266 470 1174 -948 C ATOM 456 CD1BPHE A 125 30.385 74.023 16.830 0.30 37.31 C ANISOU 456 CD1BPHE A 125 4229 5141 4806 486 901 -1006 C ATOM 457 CD2APHE A 125 27.841 71.701 14.225 0.70 39.28 C ANISOU 457 CD2APHE A 125 3920 5651 5353 451 992 -821 C ATOM 458 CD2BPHE A 125 31.194 73.581 14.639 0.30 34.89 C ANISOU 458 CD2BPHE A 125 3819 4754 4683 410 716 -839 C ATOM 459 CE1APHE A 125 26.384 72.009 16.580 0.70 42.83 C ANISOU 459 CE1APHE A 125 4349 6289 5635 538 1302 -993 C ATOM 460 CE1BPHE A 125 30.998 75.266 16.811 0.30 37.18 C ANISOU 460 CE1BPHE A 125 4346 4979 4803 538 803 -1068 C ATOM 461 CE2APHE A 125 26.436 71.631 14.206 0.70 41.15 C ANISOU 461 CE2APHE A 125 3979 6006 5652 515 1096 -864 C ATOM 462 CE2BPHE A 125 31.803 74.833 14.617 0.30 34.65 C ANISOU 462 CE2BPHE A 125 3912 4587 4665 452 628 -889 C ATOM 463 CZ APHE A 125 25.709 71.784 15.381 0.70 41.85 C ANISOU 463 CZ APHE A 125 4043 6193 5664 559 1256 -949 C ATOM 464 CZ BPHE A 125 31.707 75.669 15.701 0.30 35.19 C ANISOU 464 CZ BPHE A 125 4102 4615 4654 513 664 -1004 C ATOM 465 N PRO A 126 29.769 68.733 14.533 1.00 33.30 N ANISOU 465 N PRO A 126 3302 4911 4439 106 930 -590 N ATOM 466 CA PRO A 126 29.808 67.807 13.402 1.00 32.07 C ANISOU 466 CA PRO A 126 3071 4751 4364 44 867 -507 C ATOM 467 C PRO A 126 29.225 68.378 12.133 1.00 32.34 C ANISOU 467 C PRO A 126 2990 4770 4528 120 812 -522 C ATOM 468 O PRO A 126 28.196 67.917 11.684 1.00 32.44 O ANISOU 468 O PRO A 126 2867 4854 4604 109 847 -515 O ATOM 469 CB PRO A 126 28.918 66.653 13.872 1.00 33.31 C ANISOU 469 CB PRO A 126 3156 5009 4490 -46 976 -474 C ATOM 470 CG PRO A 126 27.847 67.353 14.740 1.00 34.00 C ANISOU 470 CG PRO A 126 3180 5188 4551 20 1113 -562 C ATOM 471 CD PRO A 126 28.670 68.406 15.484 1.00 34.71 C ANISOU 471 CD PRO A 126 3423 5209 4557 93 1088 -626 C ATOM 472 N ASP A 127 29.887 69.350 11.535 1.00 32.59 N ANISOU 472 N ASP A 127 3079 4709 4597 185 717 -534 N ATOM 473 CA ASP A 127 29.436 69.821 10.243 1.00 33.85 C ANISOU 473 CA ASP A 127 3156 4842 4863 248 646 -527 C ATOM 474 C ASP A 127 30.636 69.949 9.302 1.00 31.02 C ANISOU 474 C ASP A 127 2880 4390 4515 220 531 -467 C ATOM 475 O ASP A 127 30.616 70.754 8.366 1.00 31.10 O ANISOU 475 O ASP A 127 2889 4343 4586 280 458 -462 O ATOM 476 CB ASP A 127 28.766 71.200 10.422 1.00 36.50 C ANISOU 476 CB ASP A 127 3476 5152 5242 388 659 -612 C ATOM 477 CG ASP A 127 29.750 72.254 10.913 1.00 40.48 C ANISOU 477 CG ASP A 127 4140 5542 5697 418 617 -647 C ATOM 478 OD1 ASP A 127 30.988 72.022 10.836 1.00 43.81 O ANISOU 478 OD1 ASP A 127 4659 5910 6076 333 555 -594 O ATOM 479 OD2 ASP A 127 29.297 73.319 11.390 1.00 48.80 O ANISOU 479 OD2 ASP A 127 5222 6560 6759 528 642 -733 O ATOM 480 N TRP A 128 31.699 69.188 9.569 1.00 28.42 N ANISOU 480 N TRP A 128 2623 4049 4124 133 516 -419 N ATOM 481 CA TRP A 128 32.945 69.367 8.829 1.00 25.93 C ANISOU 481 CA TRP A 128 2373 3665 3813 107 428 -371 C ATOM 482 C TRP A 128 33.170 68.151 7.894 1.00 25.69 C ANISOU 482 C TRP A 128 2306 3660 3797 51 401 -307 C ATOM 483 O TRP A 128 33.909 68.256 6.905 1.00 26.23 O ANISOU 483 O TRP A 128 2393 3691 3881 45 341 -268 O ATOM 484 CB TRP A 128 34.125 69.506 9.831 1.00 24.69 C ANISOU 484 CB TRP A 128 2318 3478 3583 66 417 -374 C ATOM 485 CG TRP A 128 34.198 68.272 10.739 1.00 24.00 C ANISOU 485 CG TRP A 128 2246 3449 3426 6 465 -354 C ATOM 486 CD1 TRP A 128 33.553 68.086 11.935 1.00 23.64 C ANISOU 486 CD1 TRP A 128 2218 3451 3313 0 547 -390 C ATOM 487 CD2 TRP A 128 34.889 67.043 10.464 1.00 18.23 C ANISOU 487 CD2 TRP A 128 1521 2727 2680 -52 438 -288 C ATOM 488 NE1 TRP A 128 33.837 66.837 12.430 1.00 22.25 N ANISOU 488 NE1 TRP A 128 2071 3304 3078 -70 563 -339 N ATOM 489 CE2 TRP A 128 34.633 66.171 11.533 1.00 20.77 C ANISOU 489 CE2 TRP A 128 1876 3086 2928 -94 492 -279 C ATOM 490 CE3 TRP A 128 35.711 66.611 9.419 1.00 20.70 C ANISOU 490 CE3 TRP A 128 1821 3017 3028 -64 377 -239 C ATOM 491 CZ2 TRP A 128 35.167 64.874 11.596 1.00 20.54 C ANISOU 491 CZ2 TRP A 128 1880 3054 2871 -143 470 -218 C ATOM 492 CZ3 TRP A 128 36.263 65.321 9.479 1.00 21.39 C ANISOU 492 CZ3 TRP A 128 1928 3111 3089 -100 365 -193 C ATOM 493 CH2 TRP A 128 35.969 64.461 10.555 1.00 20.95 C ANISOU 493 CH2 TRP A 128 1916 3075 2971 -136 404 -181 C ATOM 494 N GLN A 129 32.572 66.992 8.204 1.00 24.15 N ANISOU 494 N GLN A 129 2068 3520 3587 5 450 -297 N ATOM 495 CA GLN A 129 33.005 65.760 7.532 1.00 22.94 C ANISOU 495 CA GLN A 129 1922 3364 3430 -51 419 -245 C ATOM 496 C GLN A 129 32.231 65.489 6.211 1.00 22.51 C ANISOU 496 C GLN A 129 1796 3323 3434 -45 382 -238 C ATOM 497 O GLN A 129 31.581 64.448 6.059 1.00 21.79 O ANISOU 497 O GLN A 129 1667 3260 3353 -98 394 -229 O ATOM 498 CB GLN A 129 32.988 64.549 8.499 1.00 22.47 C ANISOU 498 CB GLN A 129 1895 3326 3317 -120 468 -224 C ATOM 499 CG GLN A 129 33.826 63.366 7.994 1.00 24.90 C ANISOU 499 CG GLN A 129 2253 3596 3611 -155 422 -175 C ATOM 500 CD GLN A 129 33.635 62.036 8.744 1.00 28.81 C ANISOU 500 CD GLN A 129 2795 4088 4064 -226 454 -142 C ATOM 501 OE1 GLN A 129 33.964 60.982 8.203 1.00 30.31 O ANISOU 501 OE1 GLN A 129 3021 4236 4258 -249 418 -113 O ATOM 502 NE2 GLN A 129 33.109 62.077 9.971 1.00 29.87 N ANISOU 502 NE2 GLN A 129 2942 4257 4148 -261 524 -146 N ATOM 503 N ASN A 130 32.304 66.437 5.267 1.00 21.81 N ANISOU 503 N ASN A 130 1701 3208 3378 11 327 -239 N ATOM 504 CA ASN A 130 31.690 66.259 3.968 1.00 21.82 C ANISOU 504 CA ASN A 130 1656 3219 3415 21 271 -229 C ATOM 505 C ASN A 130 32.720 65.710 3.012 1.00 21.66 C ANISOU 505 C ASN A 130 1702 3168 3358 -3 230 -192 C ATOM 506 O ASN A 130 33.935 66.055 3.123 1.00 20.68 O ANISOU 506 O ASN A 130 1640 3014 3204 0 233 -171 O ATOM 507 CB ASN A 130 31.172 67.568 3.393 1.00 23.03 C ANISOU 507 CB ASN A 130 1786 3356 3611 102 225 -241 C ATOM 508 CG ASN A 130 30.053 68.177 4.206 1.00 24.25 C ANISOU 508 CG ASN A 130 1858 3544 3811 158 266 -293 C ATOM 509 OD1 ASN A 130 28.923 67.692 4.195 1.00 23.37 O ANISOU 509 OD1 ASN A 130 1637 3502 3741 151 280 -313 O ATOM 510 ND2 ASN A 130 30.351 69.289 4.871 1.00 25.37 N ANISOU 510 ND2 ASN A 130 2049 3641 3950 216 284 -320 N ATOM 511 N TYR A 131 32.240 64.876 2.068 1.00 20.36 N ANISOU 511 N TYR A 131 1520 3018 3196 -28 192 -188 N ATOM 512 CA TYR A 131 33.077 64.309 1.011 1.00 19.03 C ANISOU 512 CA TYR A 131 1419 2828 2985 -37 159 -168 C ATOM 513 C TYR A 131 32.486 64.736 -0.305 1.00 19.67 C ANISOU 513 C TYR A 131 1492 2916 3065 -11 88 -164 C ATOM 514 O TYR A 131 31.292 64.997 -0.380 1.00 19.95 O ANISOU 514 O TYR A 131 1455 2979 3147 0 52 -181 O ATOM 515 CB TYR A 131 33.066 62.772 1.087 1.00 19.86 C ANISOU 515 CB TYR A 131 1548 2925 3073 -93 167 -177 C ATOM 516 CG TYR A 131 33.644 62.212 2.368 1.00 18.14 C ANISOU 516 CG TYR A 131 1357 2690 2843 -117 222 -168 C ATOM 517 CD1 TYR A 131 34.995 61.923 2.465 1.00 18.48 C ANISOU 517 CD1 TYR A 131 1461 2707 2851 -95 232 -151 C ATOM 518 CD2 TYR A 131 32.837 62.010 3.492 1.00 17.43 C ANISOU 518 CD2 TYR A 131 1229 2621 2774 -160 265 -174 C ATOM 519 CE1 TYR A 131 35.547 61.430 3.651 1.00 16.99 C ANISOU 519 CE1 TYR A 131 1304 2503 2648 -108 260 -138 C ATOM 520 CE2 TYR A 131 33.372 61.499 4.675 1.00 16.74 C ANISOU 520 CE2 TYR A 131 1189 2516 2654 -185 307 -157 C ATOM 521 CZ TYR A 131 34.724 61.214 4.735 1.00 18.19 C ANISOU 521 CZ TYR A 131 1443 2664 2804 -155 293 -137 C ATOM 522 OH TYR A 131 35.260 60.726 5.888 1.00 19.29 O ANISOU 522 OH TYR A 131 1635 2786 2910 -170 313 -115 O ATOM 523 N THR A 132 33.330 64.829 -1.338 1.00 19.51 N ANISOU 523 N THR A 132 1543 2881 2989 1 67 -140 N ATOM 524 CA THR A 132 32.925 65.195 -2.665 1.00 19.44 C ANISOU 524 CA THR A 132 1560 2878 2949 22 -5 -127 C ATOM 525 C THR A 132 31.928 64.133 -3.168 1.00 21.09 C ANISOU 525 C THR A 132 1744 3107 3160 -12 -61 -162 C ATOM 526 O THR A 132 32.048 62.948 -2.802 1.00 21.42 O ANISOU 526 O THR A 132 1797 3141 3201 -59 -33 -188 O ATOM 527 CB THR A 132 34.161 65.250 -3.663 1.00 19.56 C ANISOU 527 CB THR A 132 1669 2887 2876 26 11 -96 C ATOM 528 OG1 THR A 132 34.939 64.058 -3.555 1.00 20.90 O ANISOU 528 OG1 THR A 132 1866 3059 3014 6 61 -120 O ATOM 529 CG2 THR A 132 35.063 66.384 -3.378 1.00 17.95 C ANISOU 529 CG2 THR A 132 1483 2664 2672 35 49 -52 C ATOM 530 N PRO A 133 30.977 64.538 -4.042 1.00 21.82 N ANISOU 530 N PRO A 133 1814 3219 3256 7 -155 -161 N ATOM 531 CA PRO A 133 29.946 63.620 -4.506 1.00 23.42 C ANISOU 531 CA PRO A 133 1978 3447 3472 -39 -229 -197 C ATOM 532 C PRO A 133 30.483 62.548 -5.436 1.00 25.33 C ANISOU 532 C PRO A 133 2332 3668 3624 -76 -250 -219 C ATOM 533 O PRO A 133 31.537 62.706 -6.059 1.00 25.36 O ANISOU 533 O PRO A 133 2437 3656 3543 -46 -219 -202 O ATOM 534 CB PRO A 133 28.916 64.532 -5.242 1.00 24.79 C ANISOU 534 CB PRO A 133 2099 3651 3669 11 -342 -184 C ATOM 535 CG PRO A 133 29.649 65.755 -5.667 1.00 23.20 C ANISOU 535 CG PRO A 133 1980 3416 3420 80 -340 -131 C ATOM 536 CD PRO A 133 30.828 65.896 -4.618 1.00 22.95 C ANISOU 536 CD PRO A 133 1973 3353 3393 72 -210 -121 C ATOM 537 N GLY A 134 29.764 61.445 -5.526 1.00 26.81 N ANISOU 537 N GLY A 134 2503 3855 3830 -145 -296 -262 N ATOM 538 CA GLY A 134 30.198 60.408 -6.414 1.00 29.18 C ANISOU 538 CA GLY A 134 2926 4119 4041 -173 -325 -299 C ATOM 539 C GLY A 134 29.819 60.683 -7.863 1.00 31.40 C ANISOU 539 C GLY A 134 3269 4422 4239 -156 -439 -306 C ATOM 540 O GLY A 134 29.267 61.771 -8.185 1.00 31.50 O ANISOU 540 O GLY A 134 3229 4475 4267 -114 -503 -268 O ATOM 541 N PRO A 135 30.109 59.704 -8.755 1.00 31.52 N ANISOU 541 N PRO A 135 3413 4406 4159 -180 -474 -356 N ATOM 542 CA PRO A 135 30.655 58.414 -8.376 1.00 30.70 C ANISOU 542 CA PRO A 135 3379 4237 4050 -215 -417 -404 C ATOM 543 C PRO A 135 32.190 58.387 -8.245 1.00 29.27 C ANISOU 543 C PRO A 135 3277 4035 3811 -140 -291 -395 C ATOM 544 O PRO A 135 32.884 59.346 -8.605 1.00 29.73 O ANISOU 544 O PRO A 135 3344 4134 3817 -79 -244 -353 O ATOM 545 CB PRO A 135 30.187 57.489 -9.527 1.00 33.12 C ANISOU 545 CB PRO A 135 3798 4512 4273 -262 -531 -475 C ATOM 546 CG PRO A 135 30.037 58.407 -10.736 1.00 34.49 C ANISOU 546 CG PRO A 135 4014 4745 4346 -215 -607 -454 C ATOM 547 CD PRO A 135 29.988 59.856 -10.226 1.00 33.27 C ANISOU 547 CD PRO A 135 3742 4646 4256 -162 -573 -369 C ATOM 548 N GLY A 136 32.721 57.277 -7.751 1.00 27.84 N ANISOU 548 N GLY A 136 3149 3787 3641 -148 -241 -433 N ATOM 549 CA GLY A 136 34.162 57.101 -7.617 1.00 25.37 C ANISOU 549 CA GLY A 136 2892 3461 3287 -66 -133 -434 C ATOM 550 C GLY A 136 34.583 57.506 -6.217 1.00 23.97 C ANISOU 550 C GLY A 136 2615 3290 3203 -58 -57 -380 C ATOM 551 O GLY A 136 33.769 57.567 -5.300 1.00 22.29 O ANISOU 551 O GLY A 136 2323 3072 3076 -119 -76 -357 O ATOM 552 N ILE A 137 35.874 57.772 -6.057 1.00 23.67 N ANISOU 552 N ILE A 137 2579 3273 3142 15 32 -361 N ATOM 553 CA ILE A 137 36.452 58.086 -4.767 1.00 21.98 C ANISOU 553 CA ILE A 137 2288 3063 3000 28 92 -317 C ATOM 554 C ILE A 137 35.857 59.397 -4.300 1.00 21.59 C ANISOU 554 C ILE A 137 2141 3062 2999 -5 83 -263 C ATOM 555 O ILE A 137 35.625 60.329 -5.114 1.00 21.75 O ANISOU 555 O ILE A 137 2156 3124 2983 1 59 -244 O ATOM 556 CB ILE A 137 38.003 58.074 -4.861 1.00 23.18 C ANISOU 556 CB ILE A 137 2449 3242 3118 113 175 -315 C ATOM 557 CG1 ILE A 137 38.473 56.648 -5.244 1.00 23.97 C ANISOU 557 CG1 ILE A 137 2650 3276 3180 169 179 -383 C ATOM 558 CG2 ILE A 137 38.651 58.525 -3.529 1.00 20.46 C ANISOU 558 CG2 ILE A 137 2018 2911 2843 120 216 -267 C ATOM 559 CD1 ILE A 137 39.960 56.552 -5.778 1.00 25.15 C ANISOU 559 CD1 ILE A 137 2804 3475 3276 277 266 -405 C ATOM 560 N ARG A 138 35.485 59.423 -3.021 1.00 19.77 N ANISOU 560 N ARG A 138 1851 2819 2844 -39 93 -244 N ATOM 561 CA ARG A 138 34.981 60.638 -2.371 1.00 18.47 C ANISOU 561 CA ARG A 138 1599 2691 2730 -53 97 -207 C ATOM 562 C ARG A 138 36.072 61.226 -1.491 1.00 18.04 C ANISOU 562 C ARG A 138 1520 2647 2688 -23 158 -175 C ATOM 563 O ARG A 138 36.509 60.555 -0.523 1.00 17.81 O ANISOU 563 O ARG A 138 1498 2593 2676 -26 184 -175 O ATOM 564 CB ARG A 138 33.750 60.330 -1.490 1.00 17.32 C ANISOU 564 CB ARG A 138 1394 2539 2648 -114 80 -214 C ATOM 565 CG ARG A 138 32.821 59.277 -2.082 1.00 20.15 C ANISOU 565 CG ARG A 138 1777 2873 3006 -174 19 -250 C ATOM 566 CD ARG A 138 32.302 59.681 -3.465 1.00 19.98 C ANISOU 566 CD ARG A 138 1763 2879 2948 -162 -58 -266 C ATOM 567 NE ARG A 138 31.510 58.612 -4.077 1.00 25.96 N ANISOU 567 NE ARG A 138 2558 3609 3698 -228 -133 -309 N ATOM 568 CZ ARG A 138 30.218 58.384 -3.814 1.00 30.18 C ANISOU 568 CZ ARG A 138 3005 4163 4297 -308 -183 -318 C ATOM 569 NH1 ARG A 138 29.564 59.145 -2.925 1.00 25.11 N ANISOU 569 NH1 ARG A 138 2233 3577 3731 -314 -151 -292 N ATOM 570 NH2 ARG A 138 29.580 57.380 -4.427 1.00 30.71 N ANISOU 570 NH2 ARG A 138 3115 4198 4357 -386 -263 -360 N ATOM 571 N TYR A 139 36.452 62.476 -1.778 1.00 17.13 N ANISOU 571 N TYR A 139 1384 2561 2565 -4 167 -145 N ATOM 572 CA TYR A 139 37.569 63.149 -1.087 1.00 17.35 C ANISOU 572 CA TYR A 139 1388 2600 2604 8 211 -116 C ATOM 573 C TYR A 139 37.064 64.126 -0.052 1.00 17.46 C ANISOU 573 C TYR A 139 1362 2606 2666 -8 207 -106 C ATOM 574 O TYR A 139 36.074 64.797 -0.282 1.00 19.23 O ANISOU 574 O TYR A 139 1570 2827 2910 -6 176 -107 O ATOM 575 CB TYR A 139 38.420 63.878 -2.113 1.00 17.09 C ANISOU 575 CB TYR A 139 1372 2597 2525 20 230 -87 C ATOM 576 CG TYR A 139 39.128 62.921 -3.046 1.00 17.07 C ANISOU 576 CG TYR A 139 1408 2616 2462 51 260 -108 C ATOM 577 CD1 TYR A 139 40.294 62.237 -2.626 1.00 14.63 C ANISOU 577 CD1 TYR A 139 1077 2324 2158 85 306 -119 C ATOM 578 CD2 TYR A 139 38.626 62.673 -4.330 1.00 17.94 C ANISOU 578 CD2 TYR A 139 1579 2732 2505 58 235 -125 C ATOM 579 CE1 TYR A 139 40.963 61.347 -3.505 1.00 17.80 C ANISOU 579 CE1 TYR A 139 1513 2746 2504 138 343 -152 C ATOM 580 CE2 TYR A 139 39.291 61.787 -5.220 1.00 20.87 C ANISOU 580 CE2 TYR A 139 2003 3122 2804 97 272 -160 C ATOM 581 CZ TYR A 139 40.455 61.136 -4.782 1.00 20.67 C ANISOU 581 CZ TYR A 139 1949 3111 2792 143 333 -177 C ATOM 582 OH TYR A 139 41.102 60.265 -5.617 1.00 25.45 O ANISOU 582 OH TYR A 139 2603 3736 3332 204 376 -223 O ATOM 583 N PRO A 140 37.712 64.186 1.108 1.00 18.16 N ANISOU 583 N PRO A 140 1437 2691 2771 -14 231 -101 N ATOM 584 CA PRO A 140 37.156 65.020 2.175 1.00 18.16 C ANISOU 584 CA PRO A 140 1417 2681 2803 -25 232 -108 C ATOM 585 C PRO A 140 37.327 66.512 1.858 1.00 19.49 C ANISOU 585 C PRO A 140 1590 2833 2981 -18 217 -90 C ATOM 586 O PRO A 140 38.390 66.928 1.339 1.00 20.38 O ANISOU 586 O PRO A 140 1715 2950 3077 -31 220 -59 O ATOM 587 CB PRO A 140 37.999 64.627 3.397 1.00 17.37 C ANISOU 587 CB PRO A 140 1324 2581 2694 -35 250 -106 C ATOM 588 CG PRO A 140 39.298 64.197 2.835 1.00 16.95 C ANISOU 588 CG PRO A 140 1271 2545 2624 -21 251 -87 C ATOM 589 CD PRO A 140 38.997 63.551 1.502 1.00 17.80 C ANISOU 589 CD PRO A 140 1394 2656 2713 -3 252 -93 C ATOM 590 N LEU A 141 36.287 67.297 2.105 1.00 19.33 N ANISOU 590 N LEU A 141 1560 2794 2992 2 201 -108 N ATOM 591 CA LEU A 141 36.373 68.737 1.907 1.00 20.68 C ANISOU 591 CA LEU A 141 1759 2920 3178 15 175 -93 C ATOM 592 C LEU A 141 37.321 69.374 2.924 1.00 20.88 C ANISOU 592 C LEU A 141 1810 2919 3203 -14 186 -96 C ATOM 593 O LEU A 141 37.892 70.421 2.617 1.00 21.67 O ANISOU 593 O LEU A 141 1949 2975 3308 -34 163 -69 O ATOM 594 CB LEU A 141 35.019 69.395 2.098 1.00 21.77 C ANISOU 594 CB LEU A 141 1876 3038 3357 70 154 -125 C ATOM 595 CG LEU A 141 33.872 69.271 1.069 1.00 26.03 C ANISOU 595 CG LEU A 141 2382 3595 3914 109 108 -122 C ATOM 596 CD1 LEU A 141 33.485 70.543 0.403 1.00 26.75 C ANISOU 596 CD1 LEU A 141 2509 3630 4026 164 46 -101 C ATOM 597 CD2 LEU A 141 33.966 68.073 0.105 1.00 24.91 C ANISOU 597 CD2 LEU A 141 2236 3496 3734 76 97 -106 C ATOM 598 N THR A 142 37.419 68.793 4.132 1.00 19.56 N ANISOU 598 N THR A 142 1631 2773 3027 -24 212 -127 N ATOM 599 CA THR A 142 38.314 69.284 5.191 1.00 19.70 C ANISOU 599 CA THR A 142 1678 2774 3033 -56 206 -137 C ATOM 600 C THR A 142 39.758 68.874 4.927 1.00 19.72 C ANISOU 600 C THR A 142 1663 2807 3024 -98 196 -97 C ATOM 601 O THR A 142 40.105 67.703 5.061 1.00 19.24 O ANISOU 601 O THR A 142 1576 2788 2947 -92 209 -91 O ATOM 602 CB THR A 142 37.890 68.797 6.604 1.00 19.81 C ANISOU 602 CB THR A 142 1702 2806 3019 -50 232 -179 C ATOM 603 OG1 THR A 142 36.567 69.285 6.883 1.00 21.00 O ANISOU 603 OG1 THR A 142 1849 2945 3186 -5 258 -223 O ATOM 604 CG2 THR A 142 38.860 69.327 7.690 1.00 17.06 C ANISOU 604 CG2 THR A 142 1399 2440 2643 -85 205 -193 C ATOM 605 N PHE A 143 40.583 69.844 4.521 1.00 19.70 N ANISOU 605 N PHE A 143 1669 2781 3034 -141 173 -69 N ATOM 606 CA PHE A 143 42.035 69.639 4.328 1.00 19.61 C ANISOU 606 CA PHE A 143 1611 2817 3024 -190 170 -33 C ATOM 607 C PHE A 143 42.609 69.255 5.685 1.00 20.47 C ANISOU 607 C PHE A 143 1709 2945 3123 -201 142 -58 C ATOM 608 O PHE A 143 42.317 69.922 6.691 1.00 20.38 O ANISOU 608 O PHE A 143 1752 2889 3102 -215 113 -94 O ATOM 609 CB PHE A 143 42.680 70.950 3.843 1.00 20.27 C ANISOU 609 CB PHE A 143 1713 2862 3127 -262 150 4 C ATOM 610 CG PHE A 143 44.106 70.818 3.392 1.00 20.55 C ANISOU 610 CG PHE A 143 1671 2968 3170 -324 164 49 C ATOM 611 CD1 PHE A 143 44.594 69.601 2.867 1.00 20.07 C ANISOU 611 CD1 PHE A 143 1535 2996 3095 -281 208 58 C ATOM 612 CD2 PHE A 143 44.961 71.932 3.436 1.00 19.38 C ANISOU 612 CD2 PHE A 143 1523 2795 3047 -427 136 80 C ATOM 613 CE1 PHE A 143 45.908 69.478 2.408 1.00 19.22 C ANISOU 613 CE1 PHE A 143 1332 2970 2999 -321 236 92 C ATOM 614 CE2 PHE A 143 46.290 71.831 2.992 1.00 20.03 C ANISOU 614 CE2 PHE A 143 1503 2964 3144 -495 160 124 C ATOM 615 CZ PHE A 143 46.766 70.606 2.475 1.00 22.47 C ANISOU 615 CZ PHE A 143 1717 3380 3440 -434 216 129 C ATOM 616 N GLY A 144 43.405 68.183 5.726 1.00 20.52 N ANISOU 616 N GLY A 144 1658 3015 3125 -184 144 -43 N ATOM 617 CA GLY A 144 43.911 67.689 6.991 1.00 20.64 C ANISOU 617 CA GLY A 144 1673 3048 3121 -182 101 -57 C ATOM 618 C GLY A 144 43.317 66.336 7.377 1.00 20.88 C ANISOU 618 C GLY A 144 1730 3083 3120 -122 118 -65 C ATOM 619 O GLY A 144 43.989 65.543 8.012 1.00 22.02 O ANISOU 619 O GLY A 144 1864 3252 3251 -101 83 -54 O ATOM 620 N TRP A 145 42.083 66.070 6.970 1.00 19.59 N ANISOU 620 N TRP A 145 1601 2893 2950 -99 163 -78 N ATOM 621 CA TRP A 145 41.410 64.791 7.279 1.00 20.58 C ANISOU 621 CA TRP A 145 1758 3012 3050 -68 182 -80 C ATOM 622 C TRP A 145 41.942 63.761 6.281 1.00 20.44 C ANISOU 622 C TRP A 145 1710 3010 3048 -27 189 -61 C ATOM 623 O TRP A 145 41.755 63.919 5.084 1.00 19.95 O ANISOU 623 O TRP A 145 1625 2954 3001 -20 216 -62 O ATOM 624 CB TRP A 145 39.872 64.922 7.137 1.00 18.62 C ANISOU 624 CB TRP A 145 1532 2741 2800 -72 225 -104 C ATOM 625 CG TRP A 145 39.050 63.632 7.451 1.00 20.30 C ANISOU 625 CG TRP A 145 1775 2946 2992 -73 250 -100 C ATOM 626 CD1 TRP A 145 38.340 62.888 6.554 1.00 20.67 C ANISOU 626 CD1 TRP A 145 1812 2984 3057 -71 267 -100 C ATOM 627 CD2 TRP A 145 38.854 62.997 8.729 1.00 20.84 C ANISOU 627 CD2 TRP A 145 1899 3009 3011 -94 256 -92 C ATOM 628 NE1 TRP A 145 37.709 61.849 7.183 1.00 24.25 N ANISOU 628 NE1 TRP A 145 2305 3420 3487 -99 284 -92 N ATOM 629 CE2 TRP A 145 38.015 61.876 8.514 1.00 22.51 C ANISOU 629 CE2 TRP A 145 2128 3203 3222 -113 283 -81 C ATOM 630 CE3 TRP A 145 39.308 63.263 10.039 1.00 22.57 C ANISOU 630 CE3 TRP A 145 2167 3235 3176 -107 237 -91 C ATOM 631 CZ2 TRP A 145 37.608 61.021 9.552 1.00 20.94 C ANISOU 631 CZ2 TRP A 145 1994 2990 2972 -152 302 -57 C ATOM 632 CZ3 TRP A 145 38.897 62.417 11.079 1.00 23.13 C ANISOU 632 CZ3 TRP A 145 2309 3299 3183 -134 254 -70 C ATOM 633 CH2 TRP A 145 38.045 61.310 10.825 1.00 19.76 C ANISOU 633 CH2 TRP A 145 1898 2851 2759 -160 292 -48 C ATOM 634 N CYS A 146 42.578 62.719 6.788 1.00 21.02 N ANISOU 634 N CYS A 146 1793 3083 3109 7 162 -48 N ATOM 635 CA CYS A 146 43.313 61.750 5.946 1.00 22.02 C ANISOU 635 CA CYS A 146 1892 3221 3253 71 165 -42 C ATOM 636 C CYS A 146 42.573 60.442 5.646 1.00 21.46 C ANISOU 636 C CYS A 146 1892 3094 3169 100 177 -50 C ATOM 637 O CYS A 146 43.198 59.405 5.392 1.00 22.42 O ANISOU 637 O CYS A 146 2027 3197 3295 168 162 -51 O ATOM 638 CB CYS A 146 44.723 61.484 6.516 1.00 21.77 C ANISOU 638 CB CYS A 146 1809 3227 3235 114 113 -25 C ATOM 639 SG CYS A 146 45.784 63.012 6.521 1.00 23.96 S ANISOU 639 SG CYS A 146 1978 3580 3545 55 96 -17 S ATOM 640 N PHE A 147 41.250 60.506 5.625 1.00 20.15 N ANISOU 640 N PHE A 147 1767 2897 2991 49 201 -60 N ATOM 641 CA PHE A 147 40.439 59.401 5.133 1.00 20.19 C ANISOU 641 CA PHE A 147 1831 2850 2992 47 209 -71 C ATOM 642 C PHE A 147 39.648 59.898 3.911 1.00 19.95 C ANISOU 642 C PHE A 147 1773 2837 2972 27 233 -97 C ATOM 643 O PHE A 147 39.197 61.036 3.895 1.00 19.42 O ANISOU 643 O PHE A 147 1664 2802 2913 -2 244 -98 O ATOM 644 CB PHE A 147 39.477 58.880 6.248 1.00 19.86 C ANISOU 644 CB PHE A 147 1851 2767 2927 -13 211 -53 C ATOM 645 CG PHE A 147 40.168 58.009 7.278 1.00 20.37 C ANISOU 645 CG PHE A 147 1986 2790 2964 11 172 -18 C ATOM 646 CD1 PHE A 147 40.249 56.627 7.104 1.00 19.09 C ANISOU 646 CD1 PHE A 147 1907 2547 2800 38 145 -6 C ATOM 647 CD2 PHE A 147 40.780 58.583 8.385 1.00 17.64 C ANISOU 647 CD2 PHE A 147 1635 2477 2591 13 148 3 C ATOM 648 CE1 PHE A 147 40.914 55.834 8.042 1.00 21.83 C ANISOU 648 CE1 PHE A 147 2332 2842 3121 74 94 36 C ATOM 649 CE2 PHE A 147 41.459 57.800 9.336 1.00 21.59 C ANISOU 649 CE2 PHE A 147 2206 2941 3057 43 92 43 C ATOM 650 CZ PHE A 147 41.524 56.419 9.170 1.00 22.19 C ANISOU 650 CZ PHE A 147 2365 2932 3134 79 64 65 C ATOM 651 N LYS A 148 39.513 59.052 2.902 1.00 20.06 N ANISOU 651 N LYS A 148 1822 2822 2978 50 229 -120 N ATOM 652 CA LYS A 148 38.609 59.266 1.760 1.00 20.20 C ANISOU 652 CA LYS A 148 1838 2846 2991 25 229 -145 C ATOM 653 C LYS A 148 37.740 58.003 1.682 1.00 21.36 C ANISOU 653 C LYS A 148 2054 2926 3137 -12 205 -164 C ATOM 654 O LYS A 148 38.011 57.013 2.400 1.00 21.92 O ANISOU 654 O LYS A 148 2184 2936 3207 -8 194 -152 O ATOM 655 CB LYS A 148 39.407 59.442 0.458 1.00 20.14 C ANISOU 655 CB LYS A 148 1825 2871 2955 80 243 -161 C ATOM 656 CG LYS A 148 40.267 58.204 0.100 1.00 20.98 C ANISOU 656 CG LYS A 148 1984 2944 3043 153 247 -189 C ATOM 657 CD LYS A 148 41.403 58.515 -0.871 1.00 22.53 C ANISOU 657 CD LYS A 148 2146 3205 3209 220 292 -200 C ATOM 658 CE LYS A 148 42.184 57.221 -1.305 1.00 24.49 C ANISOU 658 CE LYS A 148 2446 3419 3439 320 304 -247 C ATOM 659 NZ LYS A 148 43.318 57.571 -2.296 1.00 24.80 N ANISOU 659 NZ LYS A 148 2429 3551 3442 388 375 -263 N ATOM 660 N LEU A 149 36.688 58.036 0.857 1.00 22.01 N ANISOU 660 N LEU A 149 2132 3011 3220 -55 184 -187 N ATOM 661 CA LEU A 149 35.801 56.875 0.682 1.00 22.25 C ANISOU 661 CA LEU A 149 2222 2977 3255 -116 149 -209 C ATOM 662 C LEU A 149 36.060 56.256 -0.691 1.00 23.55 C ANISOU 662 C LEU A 149 2459 3109 3380 -77 117 -258 C ATOM 663 O LEU A 149 35.999 56.962 -1.693 1.00 23.69 O ANISOU 663 O LEU A 149 2452 3180 3369 -55 109 -274 O ATOM 664 CB LEU A 149 34.346 57.294 0.805 1.00 21.39 C ANISOU 664 CB LEU A 149 2042 2905 3181 -202 136 -207 C ATOM 665 CG LEU A 149 33.965 58.123 2.041 1.00 23.11 C ANISOU 665 CG LEU A 149 2180 3174 3428 -226 183 -175 C ATOM 666 CD1 LEU A 149 32.514 58.615 2.033 1.00 20.20 C ANISOU 666 CD1 LEU A 149 1713 2861 3102 -286 179 -185 C ATOM 667 CD2 LEU A 149 34.255 57.399 3.338 1.00 24.31 C ANISOU 667 CD2 LEU A 149 2384 3283 3569 -258 214 -143 C ATOM 668 N VAL A 150 36.352 54.954 -0.738 1.00 24.64 N ANISOU 668 N VAL A 150 2703 3154 3505 -63 97 -283 N ATOM 669 CA VAL A 150 36.793 54.302 -1.975 1.00 25.22 C ANISOU 669 CA VAL A 150 2866 3188 3527 -2 77 -346 C ATOM 670 C VAL A 150 35.764 53.240 -2.387 1.00 27.72 C ANISOU 670 C VAL A 150 3277 3412 3843 -88 7 -387 C ATOM 671 O VAL A 150 35.280 52.494 -1.528 1.00 28.71 O ANISOU 671 O VAL A 150 3440 3459 4008 -165 -12 -363 O ATOM 672 CB VAL A 150 38.231 53.679 -1.807 1.00 26.03 C ANISOU 672 CB VAL A 150 3022 3251 3617 123 110 -359 C ATOM 673 CG1 VAL A 150 38.666 52.888 -3.065 1.00 24.78 C ANISOU 673 CG1 VAL A 150 2971 3047 3398 203 103 -441 C ATOM 674 CG2 VAL A 150 39.290 54.781 -1.513 1.00 21.23 C ANISOU 674 CG2 VAL A 150 2301 2752 3015 191 170 -320 C ATOM 675 N PRO A 151 35.365 53.203 -3.679 1.00 29.30 N ANISOU 675 N PRO A 151 3520 3622 3993 -95 -36 -445 N ATOM 676 CA PRO A 151 34.401 52.157 -4.053 1.00 30.88 C ANISOU 676 CA PRO A 151 3814 3726 4195 -194 -120 -490 C ATOM 677 C PRO A 151 34.998 50.798 -3.834 1.00 32.29 C ANISOU 677 C PRO A 151 4145 3756 4367 -155 -130 -524 C ATOM 678 O PRO A 151 36.178 50.585 -4.102 1.00 33.08 O ANISOU 678 O PRO A 151 4301 3839 4429 -16 -88 -555 O ATOM 679 CB PRO A 151 34.167 52.404 -5.544 1.00 31.20 C ANISOU 679 CB PRO A 151 3893 3807 4157 -177 -168 -553 C ATOM 680 CG PRO A 151 34.336 53.899 -5.684 1.00 31.02 C ANISOU 680 CG PRO A 151 3741 3922 4124 -134 -123 -504 C ATOM 681 CD PRO A 151 35.496 54.221 -4.745 1.00 29.49 C ANISOU 681 CD PRO A 151 3500 3747 3958 -51 -27 -457 C ATOM 682 N VAL A 152 34.189 49.909 -3.294 1.00 34.65 N ANISOU 682 N VAL A 152 4504 3951 4712 -279 -183 -513 N ATOM 683 CA VAL A 152 34.529 48.505 -3.148 1.00 37.31 C ANISOU 683 CA VAL A 152 5021 4108 5046 -266 -219 -544 C ATOM 684 C VAL A 152 34.631 47.723 -4.468 1.00 40.95 C ANISOU 684 C VAL A 152 5643 4477 5440 -224 -282 -658 C ATOM 685 O VAL A 152 35.638 47.052 -4.684 1.00 41.71 O ANISOU 685 O VAL A 152 5863 4483 5503 -83 -266 -709 O ATOM 686 CB VAL A 152 33.536 47.837 -2.213 1.00 38.13 C ANISOU 686 CB VAL A 152 5150 4125 5213 -444 -257 -488 C ATOM 687 CG1 VAL A 152 33.869 46.327 -2.035 1.00 35.75 C ANISOU 687 CG1 VAL A 152 5070 3602 4910 -441 -309 -510 C ATOM 688 CG2 VAL A 152 33.545 48.618 -0.886 1.00 34.87 C ANISOU 688 CG2 VAL A 152 4598 3811 4842 -465 -180 -385 C ATOM 689 N GLU A 153 33.623 47.791 -5.343 1.00 44.05 N ANISOU 689 N GLU A 153 6036 4893 5809 -333 -356 -705 N ATOM 690 CA GLU A 153 33.728 47.107 -6.642 1.00 48.80 C ANISOU 690 CA GLU A 153 6805 5413 6323 -291 -421 -823 C ATOM 691 C GLU A 153 35.062 47.474 -7.302 1.00 51.12 C ANISOU 691 C GLU A 153 7122 5770 6531 -80 -334 -872 C ATOM 692 O GLU A 153 35.367 48.666 -7.418 1.00 49.18 O ANISOU 692 O GLU A 153 6731 5689 6268 -29 -266 -827 O ATOM 693 CB GLU A 153 32.613 47.530 -7.625 1.00 49.63 C ANISOU 693 CB GLU A 153 6870 5597 6392 -407 -512 -861 C ATOM 694 CG GLU A 153 31.145 47.355 -7.192 1.00 50.53 C ANISOU 694 CG GLU A 153 6905 5701 6592 -629 -602 -821 C ATOM 695 CD GLU A 153 30.722 45.916 -7.030 1.00 52.86 C ANISOU 695 CD GLU A 153 7373 5795 6917 -754 -687 -860 C ATOM 696 OE1 GLU A 153 29.605 45.584 -7.454 1.00 54.93 O ANISOU 696 OE1 GLU A 153 7637 6035 7197 -924 -802 -891 O ATOM 697 OE2 GLU A 153 31.480 45.120 -6.452 1.00 55.47 O ANISOU 697 OE2 GLU A 153 7836 5983 7259 -688 -649 -856 O ATOM 698 N PRO A 154 35.839 46.461 -7.767 1.00 55.27 N ANISOU 698 N PRO A 154 7831 6165 7005 42 -334 -965 N ATOM 699 CA PRO A 154 37.075 46.742 -8.536 1.00 58.10 C ANISOU 699 CA PRO A 154 8203 6600 7272 243 -238 -1027 C ATOM 700 C PRO A 154 36.817 47.652 -9.753 1.00 60.73 C ANISOU 700 C PRO A 154 8496 7084 7495 232 -230 -1059 C ATOM 701 O PRO A 154 35.755 47.554 -10.408 1.00 61.34 O ANISOU 701 O PRO A 154 8632 7143 7532 105 -337 -1096 O ATOM 702 CB PRO A 154 37.531 45.358 -9.014 1.00 59.68 C ANISOU 702 CB PRO A 154 8637 6612 7427 344 -271 -1150 C ATOM 703 CG PRO A 154 36.320 44.509 -8.957 1.00 59.72 C ANISOU 703 CG PRO A 154 8773 6455 7464 160 -410 -1171 C ATOM 704 CD PRO A 154 35.440 45.045 -7.870 1.00 56.91 C ANISOU 704 CD PRO A 154 8252 6152 7218 -17 -433 -1037 C ATOM 705 N GLU A 155 37.774 48.542 -10.024 1.00 63.59 N ANISOU 705 N GLU A 155 8756 7596 7809 352 -113 -1036 N ATOM 706 CA GLU A 155 37.666 49.511 -11.119 1.00 67.13 C ANISOU 706 CA GLU A 155 9171 8192 8143 347 -90 -1042 C ATOM 707 C GLU A 155 37.617 48.790 -12.473 1.00 70.60 C ANISOU 707 C GLU A 155 9817 8578 8431 389 -129 -1179 C ATOM 708 O GLU A 155 38.421 47.884 -12.742 1.00 71.93 O ANISOU 708 O GLU A 155 10113 8662 8554 523 -80 -1277 O ATOM 709 CB GLU A 155 38.824 50.508 -11.065 1.00 66.98 C ANISOU 709 CB GLU A 155 9014 8328 8107 457 55 -984 C ATOM 710 CG GLU A 155 38.426 51.943 -11.438 1.00 69.29 C ANISOU 710 CG GLU A 155 9192 8772 8363 382 62 -900 C ATOM 711 CD GLU A 155 39.616 52.910 -11.499 1.00 73.13 C ANISOU 711 CD GLU A 155 9561 9401 8822 469 206 -845 C ATOM 712 OE1 GLU A 155 40.724 52.565 -10.999 1.00 73.11 O ANISOU 712 OE1 GLU A 155 9514 9402 8864 579 299 -855 O ATOM 713 OE2 GLU A 155 39.432 54.024 -12.052 1.00 75.09 O ANISOU 713 OE2 GLU A 155 9763 9758 9009 422 219 -786 O ATOM 714 N LYS A 156 36.651 49.190 -13.304 1.00 73.14 N ANISOU 714 N LYS A 156 10173 8944 8673 281 -225 -1189 N ATOM 715 CA LYS A 156 36.311 48.465 -14.537 1.00 77.14 C ANISOU 715 CA LYS A 156 10894 9384 9032 278 -306 -1321 C ATOM 716 C LYS A 156 37.339 48.642 -15.671 1.00 79.47 C ANISOU 716 C LYS A 156 11283 9771 9143 432 -185 -1397 C ATOM 717 O LYS A 156 37.815 49.755 -15.919 1.00 79.04 O ANISOU 717 O LYS A 156 11114 9881 9037 466 -86 -1320 O ATOM 718 CB LYS A 156 34.899 48.852 -15.012 1.00 77.18 C ANISOU 718 CB LYS A 156 10892 9417 9016 106 -471 -1301 C ATOM 719 N VAL A 157 37.690 47.539 -16.335 1.00 82.92 N ANISOU 719 N VAL A 157 11931 10096 9478 522 -187 -1547 N ATOM 720 CA VAL A 157 38.552 47.596 -17.528 1.00 85.86 C ANISOU 720 CA VAL A 157 12417 10558 9648 665 -69 -1641 C ATOM 721 C VAL A 157 37.645 47.674 -18.763 1.00 87.95 C ANISOU 721 C VAL A 157 12845 10838 9734 568 -198 -1705 C ATOM 722 O VAL A 157 37.207 46.643 -19.295 1.00 89.78 O ANISOU 722 O VAL A 157 13293 10925 9893 551 -309 -1842 O ATOM 723 CB VAL A 157 39.568 46.409 -17.594 1.00 87.52 C ANISOU 723 CB VAL A 157 12766 10653 9833 857 22 -1782 C ATOM 724 CG1 VAL A 157 40.312 46.376 -18.936 1.00 89.90 C ANISOU 724 CG1 VAL A 157 13207 11049 9902 998 144 -1904 C ATOM 725 CG2 VAL A 157 40.568 46.499 -16.439 1.00 86.66 C ANISOU 725 CG2 VAL A 157 12472 10567 9889 969 147 -1705 C ATOM 726 N GLU A 158 37.366 48.914 -19.185 1.00 88.04 N ANISOU 726 N GLU A 158 12759 11016 9677 503 -195 -1601 N ATOM 727 CA GLU A 158 36.352 49.245 -20.203 1.00 89.67 C ANISOU 727 CA GLU A 158 13075 11259 9738 390 -350 -1615 C ATOM 728 C GLU A 158 36.517 48.475 -21.514 1.00 92.68 C ANISOU 728 C GLU A 158 13736 11600 9877 455 -368 -1787 C ATOM 729 O GLU A 158 35.533 48.210 -22.214 1.00 94.05 O ANISOU 729 O GLU A 158 14053 11726 9957 349 -555 -1848 O ATOM 730 CB GLU A 158 36.330 50.759 -20.475 1.00 88.76 C ANISOU 730 CB GLU A 158 12826 11329 9571 357 -310 -1468 C ATOM 731 N GLU A 159 37.763 48.122 -21.826 1.00 94.02 N ANISOU 731 N GLU A 159 13977 11796 9951 632 -174 -1870 N ATOM 732 CA GLU A 159 38.096 47.326 -23.005 1.00 96.91 C ANISOU 732 CA GLU A 159 14616 12124 10081 731 -150 -2055 C ATOM 733 C GLU A 159 38.031 45.815 -22.690 1.00 98.18 C ANISOU 733 C GLU A 159 14940 12048 10316 777 -224 -2213 C ATOM 734 O GLU A 159 38.277 45.417 -21.544 1.00 96.89 O ANISOU 734 O GLU A 159 14658 11786 10368 803 -200 -2174 O ATOM 735 CB GLU A 159 39.489 47.723 -23.519 1.00 97.81 C ANISOU 735 CB GLU A 159 14710 12402 10052 908 116 -2069 C ATOM 736 N ALA A 160 37.711 44.968 -23.678 1.00100.55 N ANISOU 736 N ALA A 160 15526 12244 10433 785 -321 -2390 N ATOM 737 CA ALA A 160 37.438 45.362 -25.065 1.00102.16 C ANISOU 737 CA ALA A 160 15903 12558 10353 758 -360 -2447 C ATOM 738 C ALA A 160 36.296 44.532 -25.668 1.00103.94 C ANISOU 738 C ALA A 160 16376 12621 10495 625 -623 -2578 C ATOM 739 O ALA A 160 36.467 43.347 -25.992 1.00105.96 O ANISOU 739 O ALA A 160 16873 12704 10684 698 -651 -2768 O ATOM 740 CB ALA A 160 38.711 45.236 -25.925 1.00104.26 C ANISOU 740 CB ALA A 160 16295 12925 10393 975 -120 -2563 C ATOM 741 N ASN A 161 35.139 45.176 -25.830 1.00102.93 N ANISOU 741 N ASN A 161 16186 12548 10374 432 -822 -2481 N ATOM 742 CA ASN A 161 33.901 44.511 -26.261 1.00103.83 C ANISOU 742 CA ASN A 161 16470 12525 10453 262 -1107 -2575 C ATOM 743 C ASN A 161 34.030 43.617 -27.503 1.00106.46 C ANISOU 743 C ASN A 161 17171 12770 10508 324 -1159 -2804 C ATOM 744 O ASN A 161 34.653 44.003 -28.494 1.00107.88 O ANISOU 744 O ASN A 161 17478 13086 10425 441 -1035 -2852 O ATOM 745 CB ASN A 161 32.794 45.550 -26.463 1.00103.17 C ANISOU 745 CB ASN A 161 16248 12576 10375 87 -1288 -2432 C ATOM 746 CG ASN A 161 31.465 45.097 -25.897 1.00103.26 C ANISOU 746 CG ASN A 161 16187 12462 10584 -127 -1548 -2417 C ATOM 747 OD1 ASN A 161 30.762 44.278 -26.499 1.00105.72 O ANISOU 747 OD1 ASN A 161 16706 12651 10810 -230 -1753 -2555 O ATOM 748 ND2 ASN A 161 31.107 45.634 -24.731 1.00100.52 N ANISOU 748 ND2 ASN A 161 15544 12150 10500 -203 -1538 -2252 N ATOM 749 N GLU A 162 33.435 42.425 -27.427 1.00106.96 N ANISOU 749 N GLU A 162 17411 12601 10627 237 -1339 -2944 N ATOM 750 CA GLU A 162 33.470 41.435 -28.510 1.00109.15 C ANISOU 750 CA GLU A 162 18064 12747 10660 284 -1418 -3184 C ATOM 751 C GLU A 162 32.162 41.481 -29.319 1.00109.82 C ANISOU 751 C GLU A 162 18275 12831 10622 67 -1727 -3220 C ATOM 752 O GLU A 162 31.412 42.459 -29.230 1.00108.24 O ANISOU 752 O GLU A 162 17866 12783 10479 -69 -1837 -3054 O ATOM 753 CB GLU A 162 33.711 40.031 -27.928 1.00110.26 C ANISOU 753 CB GLU A 162 18354 12601 10937 331 -1430 -3328 C ATOM 754 CG GLU A 162 34.403 39.045 -28.880 1.00113.80 C ANISOU 754 CG GLU A 162 19177 12923 11141 513 -1368 -3589 C ATOM 755 CD GLU A 162 33.883 37.611 -28.749 1.00116.13 C ANISOU 755 CD GLU A 162 19732 12885 11507 428 -1568 -3762 C ATOM 756 OE1 GLU A 162 33.785 36.914 -29.783 1.00119.11 O ANISOU 756 OE1 GLU A 162 20455 13153 11648 452 -1664 -3979 O ATOM 757 OE2 GLU A 162 33.568 37.181 -27.619 1.00114.71 O ANISOU 757 OE2 GLU A 162 19428 12548 11610 330 -1631 -3680 O ATOM 758 N GLY A 163 31.896 40.426 -30.096 1.00111.80 N ANISOU 758 N GLY A 163 18864 12907 10708 42 -1877 -3441 N ATOM 759 CA GLY A 163 30.690 40.318 -30.928 1.00112.30 C ANISOU 759 CA GLY A 163 19080 12951 10637 -164 -2194 -3506 C ATOM 760 C GLY A 163 29.475 39.703 -30.242 1.00111.16 C ANISOU 760 C GLY A 163 18857 12632 10747 -425 -2469 -3488 C ATOM 761 O GLY A 163 29.136 40.066 -29.112 1.00108.53 O ANISOU 761 O GLY A 163 18209 12323 10705 -517 -2456 -3312 O ATOM 762 N GLU A 164 28.824 38.767 -30.934 1.00112.99 N ANISOU 762 N GLU A 164 19381 12691 10861 -552 -2714 -3676 N ATOM 763 CA GLU A 164 27.565 38.148 -30.480 1.00112.37 C ANISOU 763 CA GLU A 164 19253 12453 10989 -840 -3009 -3676 C ATOM 764 C GLU A 164 27.697 37.249 -29.234 1.00110.36 C ANISOU 764 C GLU A 164 18939 11960 11031 -882 -2950 -3663 C ATOM 765 O GLU A 164 26.718 37.035 -28.509 1.00109.89 O ANISOU 765 O GLU A 164 18710 11831 11213 -1126 -3121 -3577 O ATOM 766 CB GLU A 164 26.933 37.347 -31.630 1.00116.45 C ANISOU 766 CB GLU A 164 20134 12836 11275 -963 -3289 -3899 C ATOM 767 CG GLU A 164 25.409 37.263 -31.577 1.00117.47 C ANISOU 767 CG GLU A 164 20146 12948 11540 -1295 -3646 -3856 C ATOM 768 CD GLU A 164 24.860 36.022 -32.259 1.00121.74 C ANISOU 768 CD GLU A 164 21053 13237 11966 -1453 -3917 -4095 C ATOM 769 OE1 GLU A 164 25.295 34.900 -31.910 1.00122.35 O ANISOU 769 OE1 GLU A 164 21344 13037 12107 -1421 -3862 -4229 O ATOM 770 OE2 GLU A 164 23.981 36.166 -33.136 1.00124.34 O ANISOU 770 OE2 GLU A 164 21462 13637 12144 -1612 -4200 -4149 O ATOM 771 N ASN A 165 28.900 36.728 -28.996 1.00108.61 N ANISOU 771 N ASN A 165 18856 11623 10788 -643 -2709 -3745 N ATOM 772 CA ASN A 165 29.141 35.792 -27.899 1.00106.53 C ANISOU 772 CA ASN A 165 18598 11108 10772 -649 -2656 -3747 C ATOM 773 C ASN A 165 29.796 36.416 -26.660 1.00102.15 C ANISOU 773 C ASN A 165 17710 10659 10444 -534 -2408 -3540 C ATOM 774 O ASN A 165 30.283 35.705 -25.772 1.00101.47 O ANISOU 774 O ASN A 165 17645 10383 10527 -470 -2316 -3537 O ATOM 775 CB ASN A 165 29.955 34.596 -28.406 1.00109.26 C ANISOU 775 CB ASN A 165 19351 11197 10964 -465 -2601 -3997 C ATOM 776 CG ASN A 165 29.120 33.626 -29.241 1.00112.42 C ANISOU 776 CG ASN A 165 20100 11380 11234 -651 -2900 -4206 C ATOM 777 OD1 ASN A 165 28.017 33.243 -28.849 1.00111.73 O ANISOU 777 OD1 ASN A 165 19962 11173 11316 -948 -3143 -4164 O ATOM 778 ND2 ASN A 165 29.652 33.221 -30.392 1.00114.20 N ANISOU 778 ND2 ASN A 165 20680 11556 11154 -483 -2880 -4436 N ATOM 779 N ASN A 166 29.776 37.747 -26.597 1.00 98.43 N ANISOU 779 N ASN A 166 16943 10481 9974 -514 -2319 -3364 N ATOM 780 CA ASN A 166 30.415 38.498 -25.523 1.00 93.96 C ANISOU 780 CA ASN A 166 16064 10046 9592 -404 -2088 -3171 C ATOM 781 C ASN A 166 29.901 38.135 -24.128 1.00 92.00 C ANISOU 781 C ASN A 166 15626 9669 9661 -565 -2134 -3044 C ATOM 782 O ASN A 166 30.644 38.226 -23.146 1.00 89.67 O ANISOU 782 O ASN A 166 15187 9368 9514 -443 -1943 -2947 O ATOM 783 CB ASN A 166 30.260 40.005 -25.769 1.00 91.99 C ANISOU 783 CB ASN A 166 15555 10110 9287 -401 -2038 -3008 C ATOM 784 CG ASN A 166 31.097 40.849 -24.820 1.00 88.13 C ANISOU 784 CG ASN A 166 14779 9764 8941 -259 -1782 -2832 C ATOM 785 OD1 ASN A 166 32.323 40.885 -24.918 1.00 87.81 O ANISOU 785 OD1 ASN A 166 14790 9758 8815 -26 -1554 -2871 O ATOM 786 ND2 ASN A 166 30.433 41.539 -23.902 1.00 84.67 N ANISOU 786 ND2 ASN A 166 14033 9417 8720 -399 -1820 -2644 N ATOM 787 N SER A 167 28.636 37.725 -24.044 1.00 92.45 N ANISOU 787 N SER A 167 15680 9632 9814 -846 -2386 -3043 N ATOM 788 CA SER A 167 28.033 37.351 -22.760 1.00 90.92 C ANISOU 788 CA SER A 167 15314 9324 9907 -1036 -2434 -2920 C ATOM 789 C SER A 167 28.605 36.034 -22.210 1.00 91.82 C ANISOU 789 C SER A 167 15666 9122 10098 -981 -2392 -3012 C ATOM 790 O SER A 167 28.707 35.858 -20.986 1.00 90.01 O ANISOU 790 O SER A 167 15298 8820 10083 -1013 -2311 -2885 O ATOM 791 CB SER A 167 26.508 37.284 -22.876 1.00 92.16 C ANISOU 791 CB SER A 167 15384 9488 10145 -1365 -2711 -2895 C ATOM 792 OG SER A 167 26.106 36.404 -23.909 1.00 95.27 O ANISOU 792 OG SER A 167 16103 9716 10379 -1460 -2924 -3096 O ATOM 793 N LEU A 168 28.995 35.138 -23.122 1.00 93.98 N ANISOU 793 N LEU A 168 16310 9209 10189 -884 -2447 -3232 N ATOM 794 CA LEU A 168 29.611 33.854 -22.772 1.00 95.46 C ANISOU 794 CA LEU A 168 16777 9072 10420 -789 -2418 -3348 C ATOM 795 C LEU A 168 31.058 33.992 -22.291 1.00 93.95 C ANISOU 795 C LEU A 168 16548 8908 10241 -454 -2136 -3323 C ATOM 796 O LEU A 168 31.467 33.312 -21.355 1.00 93.70 O ANISOU 796 O LEU A 168 16555 8679 10367 -404 -2081 -3287 O ATOM 797 CB LEU A 168 29.550 32.871 -23.948 1.00 99.04 C ANISOU 797 CB LEU A 168 17654 9312 10664 -780 -2572 -3611 C ATOM 798 CG LEU A 168 28.210 32.532 -24.612 1.00101.48 C ANISOU 798 CG LEU A 168 18076 9554 10926 -1100 -2884 -3689 C ATOM 799 CD1 LEU A 168 28.298 31.223 -25.391 1.00104.36 C ANISOU 799 CD1 LEU A 168 18912 9595 11145 -1088 -3026 -3953 C ATOM 800 CD2 LEU A 168 27.093 32.451 -23.591 1.00100.71 C ANISOU 800 CD2 LEU A 168 17748 9417 11101 -1433 -3022 -3517 C ATOM 801 N LEU A 169 31.823 34.869 -22.940 1.00 93.27 N ANISOU 801 N LEU A 169 16386 9068 9985 -233 -1965 -3337 N ATOM 802 CA LEU A 169 33.233 35.098 -22.609 1.00 92.24 C ANISOU 802 CA LEU A 169 16188 9008 9850 85 -1693 -3319 C ATOM 803 C LEU A 169 33.382 35.966 -21.377 1.00 88.83 C ANISOU 803 C LEU A 169 15381 8741 9631 70 -1566 -3076 C ATOM 804 O LEU A 169 34.320 35.794 -20.595 1.00 88.06 O ANISOU 804 O LEU A 169 15224 8598 9638 253 -1407 -3030 O ATOM 805 CB LEU A 169 33.973 35.727 -23.802 1.00 93.04 C ANISOU 805 CB LEU A 169 16346 9324 9682 299 -1550 -3421 C ATOM 806 CG LEU A 169 35.408 36.286 -23.746 1.00 92.39 C ANISOU 806 CG LEU A 169 16138 9419 9549 613 -1251 -3398 C ATOM 807 CD1 LEU A 169 36.404 35.374 -23.030 1.00 93.50 C ANISOU 807 CD1 LEU A 169 16361 9356 9810 836 -1133 -3456 C ATOM 808 CD2 LEU A 169 35.891 36.567 -25.165 1.00 94.72 C ANISOU 808 CD2 LEU A 169 16598 9861 9530 766 -1163 -3551 C ATOM 809 N HIS A 170 32.457 36.905 -21.213 1.00 87.16 N ANISOU 809 N HIS A 170 14918 8721 9477 -141 -1643 -2925 N ATOM 810 CA HIS A 170 32.469 37.801 -20.075 1.00 84.10 C ANISOU 810 CA HIS A 170 14179 8495 9278 -175 -1538 -2702 C ATOM 811 C HIS A 170 31.153 37.629 -19.316 1.00 83.71 C ANISOU 811 C HIS A 170 14014 8375 9418 -487 -1718 -2592 C ATOM 812 O HIS A 170 30.133 38.190 -19.718 1.00 84.00 O ANISOU 812 O HIS A 170 13940 8542 9435 -675 -1853 -2554 O ATOM 813 CB HIS A 170 32.660 39.264 -20.526 1.00 82.44 C ANISOU 813 CB HIS A 170 13742 8612 8969 -109 -1428 -2609 C ATOM 814 CG HIS A 170 33.895 39.499 -21.348 1.00 83.60 C ANISOU 814 CG HIS A 170 13989 8861 8916 166 -1241 -2707 C ATOM 815 ND1 HIS A 170 35.132 39.745 -20.788 1.00 82.83 N ANISOU 815 ND1 HIS A 170 13773 8828 8869 390 -1013 -2657 N ATOM 816 CD2 HIS A 170 34.078 39.537 -22.691 1.00 85.94 C ANISOU 816 CD2 HIS A 170 14481 9219 8954 247 -1244 -2851 C ATOM 817 CE1 HIS A 170 36.024 39.917 -21.749 1.00 84.09 C ANISOU 817 CE1 HIS A 170 14037 9091 8822 594 -872 -2765 C ATOM 818 NE2 HIS A 170 35.410 39.794 -22.913 1.00 86.13 N ANISOU 818 NE2 HIS A 170 14496 9348 8881 513 -1002 -2884 N ATOM 819 N PRO A 171 31.159 36.822 -18.235 1.00 83.56 N ANISOU 819 N PRO A 171 14024 8148 9577 -545 -1723 -2542 N ATOM 820 CA PRO A 171 29.979 36.697 -17.373 1.00 83.15 C ANISOU 820 CA PRO A 171 13830 8049 9713 -846 -1853 -2415 C ATOM 821 C PRO A 171 29.612 37.979 -16.634 1.00 80.41 C ANISOU 821 C PRO A 171 13097 7974 9480 -912 -1772 -2214 C ATOM 822 O PRO A 171 28.453 38.155 -16.263 1.00 79.90 O ANISOU 822 O PRO A 171 12873 7958 9529 -1165 -1887 -2127 O ATOM 823 CB PRO A 171 30.377 35.601 -16.373 1.00 83.78 C ANISOU 823 CB PRO A 171 14054 7851 9926 -832 -1829 -2398 C ATOM 824 CG PRO A 171 31.856 35.449 -16.503 1.00 83.54 C ANISOU 824 CG PRO A 171 14143 7784 9814 -487 -1656 -2474 C ATOM 825 CD PRO A 171 32.177 35.807 -17.910 1.00 84.57 C ANISOU 825 CD PRO A 171 14375 8038 9720 -347 -1641 -2627 C ATOM 826 N MET A 172 30.582 38.868 -16.426 1.00 78.82 N ANISOU 826 N MET A 172 12744 7950 9253 -689 -1575 -2146 N ATOM 827 CA MET A 172 30.323 40.136 -15.723 1.00 77.01 C ANISOU 827 CA MET A 172 12170 7967 9125 -729 -1491 -1965 C ATOM 828 C MET A 172 29.383 41.062 -16.485 1.00 77.08 C ANISOU 828 C MET A 172 12037 8179 9071 -848 -1598 -1946 C ATOM 829 O MET A 172 28.786 41.964 -15.894 1.00 75.26 O ANISOU 829 O MET A 172 11532 8114 8950 -942 -1587 -1806 O ATOM 830 CB MET A 172 31.626 40.876 -15.424 1.00 75.02 C ANISOU 830 CB MET A 172 11809 7848 8848 -469 -1270 -1909 C ATOM 831 CG MET A 172 32.575 40.111 -14.540 1.00 76.17 C ANISOU 831 CG MET A 172 12041 7826 9076 -333 -1168 -1902 C ATOM 832 SD MET A 172 31.781 39.375 -13.091 1.00 78.00 S ANISOU 832 SD MET A 172 12238 7878 9521 -561 -1246 -1782 S ATOM 833 CE MET A 172 31.849 37.618 -13.463 1.00 80.30 C ANISOU 833 CE MET A 172 12929 7803 9780 -573 -1373 -1946 C ATOM 834 N SER A 173 29.272 40.815 -17.791 1.00 79.66 N ANISOU 834 N SER A 173 12566 8486 9217 -833 -1705 -2093 N ATOM 835 CA SER A 173 28.449 41.604 -18.715 1.00 80.73 C ANISOU 835 CA SER A 173 12622 8797 9253 -923 -1836 -2095 C ATOM 836 C SER A 173 27.051 41.023 -18.941 1.00 82.57 C ANISOU 836 C SER A 173 12882 8949 9541 -1201 -2089 -2136 C ATOM 837 O SER A 173 26.242 41.607 -19.671 1.00 83.02 O ANISOU 837 O SER A 173 12863 9147 9534 -1294 -2235 -2136 O ATOM 838 CB SER A 173 29.171 41.783 -20.056 1.00 81.80 C ANISOU 838 CB SER A 173 12962 8989 9129 -740 -1802 -2222 C ATOM 839 OG SER A 173 30.151 42.806 -19.941 1.00 81.51 O ANISOU 839 OG SER A 173 12789 9131 9051 -539 -1589 -2135 O ATOM 840 N LEU A 174 26.776 39.881 -18.312 1.00 83.60 N ANISOU 840 N LEU A 174 13119 8853 9792 -1339 -2149 -2164 N ATOM 841 CA LEU A 174 25.422 39.336 -18.256 1.00 85.37 C ANISOU 841 CA LEU A 174 13313 9005 10119 -1644 -2371 -2171 C ATOM 842 C LEU A 174 24.478 40.281 -17.495 1.00 84.23 C ANISOU 842 C LEU A 174 12782 9074 10149 -1791 -2377 -1996 C ATOM 843 O LEU A 174 24.872 40.904 -16.488 1.00 81.50 O ANISOU 843 O LEU A 174 12233 8823 9912 -1706 -2196 -1859 O ATOM 844 CB LEU A 174 25.424 37.949 -17.612 1.00 86.58 C ANISOU 844 CB LEU A 174 13664 8858 10374 -1763 -2405 -2212 C ATOM 845 CG LEU A 174 25.926 36.783 -18.474 1.00 88.81 C ANISOU 845 CG LEU A 174 14359 8880 10503 -1695 -2486 -2418 C ATOM 846 CD1 LEU A 174 26.263 35.590 -17.614 1.00 88.67 C ANISOU 846 CD1 LEU A 174 14525 8565 10600 -1730 -2456 -2423 C ATOM 847 CD2 LEU A 174 24.907 36.398 -19.558 1.00 91.24 C ANISOU 847 CD2 LEU A 174 14800 9150 10717 -1903 -2755 -2548 C ATOM 848 N HIS A 175 23.246 40.397 -18.001 1.00 86.06 N ANISOU 848 N HIS A 175 12914 9386 10400 -2001 -2591 -2010 N ATOM 849 CA HIS A 175 22.217 41.227 -17.371 1.00 85.41 C ANISOU 849 CA HIS A 175 12456 9508 10487 -2144 -2620 -1866 C ATOM 850 C HIS A 175 21.778 40.617 -16.039 1.00 84.69 C ANISOU 850 C HIS A 175 12247 9320 10612 -2336 -2566 -1771 C ATOM 851 O HIS A 175 21.314 39.470 -15.986 1.00 86.76 O ANISOU 851 O HIS A 175 12658 9384 10923 -2546 -2687 -1831 O ATOM 852 CB HIS A 175 21.009 41.466 -18.305 1.00 87.97 C ANISOU 852 CB HIS A 175 12695 9950 10780 -2311 -2881 -1913 C ATOM 853 CG HIS A 175 20.020 42.465 -17.769 1.00 89.63 C ANISOU 853 CG HIS A 175 12501 10400 11154 -2401 -2903 -1773 C ATOM 854 ND1 HIS A 175 18.712 42.137 -17.471 1.00 93.08 N ANISOU 854 ND1 HIS A 175 12741 10871 11755 -2681 -3063 -1747 N ATOM 855 CD2 HIS A 175 20.159 43.779 -17.454 1.00 88.68 C ANISOU 855 CD2 HIS A 175 12135 10496 11065 -2242 -2779 -1656 C ATOM 856 CE1 HIS A 175 18.085 43.208 -17.013 1.00 92.86 C ANISOU 856 CE1 HIS A 175 12354 11079 11849 -2673 -3032 -1627 C ATOM 857 NE2 HIS A 175 18.942 44.216 -16.988 1.00 90.12 N ANISOU 857 NE2 HIS A 175 11984 10834 11424 -2406 -2865 -1571 N ATOM 858 N GLY A 176 21.933 41.405 -14.978 1.00 81.59 N ANISOU 858 N GLY A 176 11598 9064 10337 -2268 -2384 -1622 N ATOM 859 CA GLY A 176 21.702 40.962 -13.612 1.00 80.60 C ANISOU 859 CA GLY A 176 11365 8869 10389 -2409 -2284 -1514 C ATOM 860 C GLY A 176 22.947 41.185 -12.771 1.00 78.14 C ANISOU 860 C GLY A 176 11093 8524 10072 -2185 -2046 -1445 C ATOM 861 O GLY A 176 22.854 41.384 -11.550 1.00 76.73 O ANISOU 861 O GLY A 176 10742 8389 10023 -2231 -1917 -1317 O ATOM 862 N MET A 177 24.111 41.162 -13.432 1.00 77.35 N ANISOU 862 N MET A 177 11215 8359 9816 -1944 -1988 -1532 N ATOM 863 CA MET A 177 25.415 41.311 -12.766 1.00 75.19 C ANISOU 863 CA MET A 177 10993 8049 9526 -1713 -1779 -1485 C ATOM 864 C MET A 177 25.779 42.765 -12.474 1.00 72.77 C ANISOU 864 C MET A 177 10435 7990 9223 -1550 -1635 -1383 C ATOM 865 O MET A 177 26.814 43.030 -11.845 1.00 70.75 O ANISOU 865 O MET A 177 10176 7737 8969 -1374 -1466 -1331 O ATOM 866 CB MET A 177 26.538 40.662 -13.591 1.00 75.71 C ANISOU 866 CB MET A 177 11382 7954 9432 -1515 -1765 -1627 C ATOM 867 CG MET A 177 26.440 39.125 -13.767 1.00 77.80 C ANISOU 867 CG MET A 177 11955 7915 9689 -1629 -1885 -1738 C ATOM 868 SD MET A 177 26.707 38.100 -12.288 1.00 75.35 S ANISOU 868 SD MET A 177 11731 7367 9532 -1703 -1810 -1646 S ATOM 869 CE MET A 177 28.458 38.313 -11.918 1.00 71.41 C ANISOU 869 CE MET A 177 11303 6854 8974 -1336 -1595 -1637 C ATOM 870 N GLU A 178 24.937 43.698 -12.934 1.00 73.01 N ANISOU 870 N GLU A 178 10261 8219 9258 -1607 -1715 -1356 N ATOM 871 CA GLU A 178 25.204 45.150 -12.802 1.00 70.97 C ANISOU 871 CA GLU A 178 9786 8184 8995 -1454 -1605 -1268 C ATOM 872 C GLU A 178 25.440 45.570 -11.363 1.00 68.95 C ANISOU 872 C GLU A 178 9349 7977 8872 -1432 -1434 -1137 C ATOM 873 O GLU A 178 24.836 45.026 -10.433 1.00 68.82 O ANISOU 873 O GLU A 178 9263 7904 8983 -1601 -1432 -1083 O ATOM 874 CB GLU A 178 24.063 46.007 -13.380 1.00 71.42 C ANISOU 874 CB GLU A 178 9641 8427 9069 -1540 -1744 -1248 C ATOM 875 CG GLU A 178 23.947 46.001 -14.897 1.00 73.67 C ANISOU 875 CG GLU A 178 10085 8722 9184 -1511 -1906 -1359 C ATOM 876 CD GLU A 178 23.133 44.821 -15.436 1.00 77.36 C ANISOU 876 CD GLU A 178 10695 9051 9646 -1722 -2112 -1465 C ATOM 877 OE1 GLU A 178 22.658 43.977 -14.640 1.00 76.19 O ANISOU 877 OE1 GLU A 178 10526 8790 9634 -1902 -2126 -1448 O ATOM 878 OE2 GLU A 178 22.959 44.747 -16.670 1.00 80.68 O ANISOU 878 OE2 GLU A 178 11261 9475 9920 -1717 -2266 -1566 O ATOM 879 N ASP A 179 26.326 46.550 -11.209 1.00 67.38 N ANISOU 879 N ASP A 179 9084 7886 8632 -1233 -1293 -1087 N ATOM 880 CA ASP A 179 26.585 47.206 -9.934 1.00 66.18 C ANISOU 880 CA ASP A 179 8750 7811 8582 -1189 -1139 -968 C ATOM 881 C ASP A 179 25.301 47.817 -9.354 1.00 66.32 C ANISOU 881 C ASP A 179 8498 7971 8732 -1337 -1174 -890 C ATOM 882 O ASP A 179 24.376 48.161 -10.102 1.00 67.33 O ANISOU 882 O ASP A 179 8534 8191 8858 -1408 -1309 -917 O ATOM 883 CB ASP A 179 27.683 48.272 -10.094 1.00 64.25 C ANISOU 883 CB ASP A 179 8479 7671 8261 -965 -1013 -940 C ATOM 884 CG ASP A 179 29.082 47.666 -10.325 1.00 65.41 C ANISOU 884 CG ASP A 179 8843 7699 8311 -805 -928 -999 C ATOM 885 OD1 ASP A 179 29.244 46.420 -10.262 1.00 67.29 O ANISOU 885 OD1 ASP A 179 9263 7756 8547 -846 -962 -1061 O ATOM 886 OD2 ASP A 179 30.034 48.445 -10.569 1.00 64.47 O ANISOU 886 OD2 ASP A 179 8709 7666 8122 -636 -826 -985 O ATOM 887 N ALA A 180 25.238 47.919 -8.025 1.00 65.64 N ANISOU 887 N ALA A 180 8285 7903 8752 -1378 -1055 -799 N ATOM 888 CA ALA A 180 24.093 48.547 -7.347 1.00 66.06 C ANISOU 888 CA ALA A 180 8064 8106 8929 -1494 -1049 -727 C ATOM 889 C ALA A 180 23.992 50.033 -7.741 1.00 64.70 C ANISOU 889 C ALA A 180 7722 8119 8743 -1354 -1043 -703 C ATOM 890 O ALA A 180 25.017 50.711 -7.886 1.00 62.86 O ANISOU 890 O ALA A 180 7547 7902 8433 -1171 -961 -693 O ATOM 891 CB ALA A 180 24.201 48.377 -5.801 1.00 65.21 C ANISOU 891 CB ALA A 180 7888 7980 8907 -1545 -898 -635 C ATOM 892 N GLU A 181 22.764 50.523 -7.926 1.00 65.39 N ANISOU 892 N GLU A 181 7599 8338 8907 -1442 -1137 -694 N ATOM 893 CA GLU A 181 22.536 51.936 -8.273 1.00 64.47 C ANISOU 893 CA GLU A 181 7320 8383 8791 -1309 -1151 -666 C ATOM 894 C GLU A 181 23.263 52.893 -7.322 1.00 60.87 C ANISOU 894 C GLU A 181 6796 7978 8354 -1162 -971 -595 C ATOM 895 O GLU A 181 23.754 53.947 -7.749 1.00 60.45 O ANISOU 895 O GLU A 181 6742 7983 8244 -1003 -957 -580 O ATOM 896 CB GLU A 181 21.038 52.262 -8.331 1.00 66.76 C ANISOU 896 CB GLU A 181 7356 8813 9198 -1422 -1264 -659 C ATOM 897 CG GLU A 181 20.310 51.627 -9.528 1.00 72.31 C ANISOU 897 CG GLU A 181 8111 9495 9867 -1542 -1486 -734 C ATOM 898 CD GLU A 181 18.881 52.139 -9.705 1.00 78.51 C ANISOU 898 CD GLU A 181 8614 10448 10769 -1618 -1618 -725 C ATOM 899 OE1 GLU A 181 18.455 53.040 -8.934 1.00 79.94 O ANISOU 899 OE1 GLU A 181 8556 10762 11055 -1557 -1528 -665 O ATOM 900 OE2 GLU A 181 18.181 51.638 -10.621 1.00 82.23 O ANISOU 900 OE2 GLU A 181 9099 10919 11226 -1734 -1819 -784 O ATOM 901 N LYS A 182 23.333 52.511 -6.046 1.00 58.47 N ANISOU 901 N LYS A 182 6450 7646 8120 -1226 -843 -550 N ATOM 902 CA LYS A 182 24.111 53.234 -5.037 1.00 54.79 C ANISOU 902 CA LYS A 182 5954 7205 7658 -1106 -677 -491 C ATOM 903 C LYS A 182 25.474 52.543 -4.828 1.00 51.83 C ANISOU 903 C LYS A 182 5805 6686 7201 -1045 -602 -495 C ATOM 904 O LYS A 182 25.557 51.335 -4.490 1.00 52.40 O ANISOU 904 O LYS A 182 5996 6635 7278 -1151 -601 -503 O ATOM 905 CB LYS A 182 23.332 53.324 -3.722 1.00 55.80 C ANISOU 905 CB LYS A 182 5894 7410 7897 -1202 -580 -437 C ATOM 906 CG LYS A 182 23.974 54.205 -2.658 1.00 55.85 C ANISOU 906 CG LYS A 182 5856 7461 7905 -1081 -424 -385 C ATOM 907 CD LYS A 182 23.715 53.647 -1.251 1.00 61.32 C ANISOU 907 CD LYS A 182 6506 8146 8646 -1198 -302 -336 C ATOM 908 CE LYS A 182 24.150 54.642 -0.158 1.00 62.63 C ANISOU 908 CE LYS A 182 6606 8380 8810 -1085 -159 -294 C ATOM 909 NZ LYS A 182 24.842 53.942 0.985 1.00 62.21 N ANISOU 909 NZ LYS A 182 6679 8241 8719 -1128 -52 -246 N ATOM 910 N GLU A 183 26.532 53.312 -5.056 1.00 46.87 N ANISOU 910 N GLU A 183 5234 6071 6503 -875 -545 -488 N ATOM 911 CA GLU A 183 27.904 52.803 -4.966 1.00 43.68 C ANISOU 911 CA GLU A 183 5012 5559 6025 -785 -477 -497 C ATOM 912 C GLU A 183 28.276 52.449 -3.523 1.00 41.15 C ANISOU 912 C GLU A 183 4688 5193 5752 -810 -364 -440 C ATOM 913 O GLU A 183 28.117 53.296 -2.627 1.00 40.15 O ANISOU 913 O GLU A 183 4425 5157 5672 -791 -285 -386 O ATOM 914 CB GLU A 183 28.862 53.862 -5.516 1.00 42.12 C ANISOU 914 CB GLU A 183 4831 5419 5754 -617 -436 -492 C ATOM 915 CG GLU A 183 30.179 53.349 -6.010 1.00 40.63 C ANISOU 915 CG GLU A 183 4819 5147 5471 -515 -400 -529 C ATOM 916 CD GLU A 183 30.909 54.374 -6.873 1.00 40.76 C ANISOU 916 CD GLU A 183 4846 5239 5403 -387 -377 -528 C ATOM 917 OE1 GLU A 183 30.841 55.598 -6.573 1.00 37.03 O ANISOU 917 OE1 GLU A 183 4252 4859 4960 -349 -342 -471 O ATOM 918 OE2 GLU A 183 31.557 53.945 -7.859 1.00 41.54 O ANISOU 918 OE2 GLU A 183 5086 5299 5399 -328 -391 -585 O ATOM 919 N VAL A 184 28.762 51.221 -3.307 1.00 38.26 N ANISOU 919 N VAL A 184 4487 4684 5367 -845 -365 -454 N ATOM 920 CA VAL A 184 29.218 50.783 -1.985 1.00 35.38 C ANISOU 920 CA VAL A 184 4159 4257 5027 -860 -276 -393 C ATOM 921 C VAL A 184 30.645 51.277 -1.708 1.00 34.20 C ANISOU 921 C VAL A 184 4053 4111 4829 -682 -198 -376 C ATOM 922 O VAL A 184 31.554 51.127 -2.570 1.00 34.65 O ANISOU 922 O VAL A 184 4215 4127 4824 -565 -216 -428 O ATOM 923 CB VAL A 184 29.138 49.257 -1.824 1.00 36.30 C ANISOU 923 CB VAL A 184 4448 4198 5147 -969 -323 -403 C ATOM 924 CG1 VAL A 184 29.689 48.840 -0.500 1.00 33.87 C ANISOU 924 CG1 VAL A 184 4200 3822 4849 -968 -243 -329 C ATOM 925 CG2 VAL A 184 27.669 48.779 -1.942 1.00 35.93 C ANISOU 925 CG2 VAL A 184 4332 4157 5163 -1185 -396 -407 C ATOM 926 N LEU A 185 30.856 51.856 -0.524 1.00 31.36 N ANISOU 926 N LEU A 185 3612 3808 4495 -664 -112 -310 N ATOM 927 CA LEU A 185 32.121 52.527 -0.240 1.00 29.04 C ANISOU 927 CA LEU A 185 3321 3545 4167 -512 -50 -293 C ATOM 928 C LEU A 185 32.778 52.063 1.043 1.00 28.43 C ANISOU 928 C LEU A 185 3305 3407 4089 -500 0 -236 C ATOM 929 O LEU A 185 32.108 51.590 1.968 1.00 29.69 O ANISOU 929 O LEU A 185 3469 3538 4273 -617 18 -189 O ATOM 930 CB LEU A 185 31.912 54.059 -0.140 1.00 27.67 C ANISOU 930 CB LEU A 185 2987 3516 4009 -470 -8 -273 C ATOM 931 CG LEU A 185 31.301 54.804 -1.318 1.00 25.97 C ANISOU 931 CG LEU A 185 2700 3377 3790 -460 -63 -310 C ATOM 932 CD1 LEU A 185 30.599 56.137 -0.872 1.00 21.03 C ANISOU 932 CD1 LEU A 185 1909 2870 3211 -458 -32 -281 C ATOM 933 CD2 LEU A 185 32.352 55.025 -2.393 1.00 22.62 C ANISOU 933 CD2 LEU A 185 2354 2946 3295 -342 -74 -344 C ATOM 934 N VAL A 186 34.088 52.266 1.115 1.00 26.21 N ANISOU 934 N VAL A 186 3060 3120 3777 -361 25 -235 N ATOM 935 CA VAL A 186 34.865 51.903 2.284 1.00 26.42 C ANISOU 935 CA VAL A 186 3144 3097 3797 -323 52 -181 C ATOM 936 C VAL A 186 35.822 53.063 2.643 1.00 24.82 C ANISOU 936 C VAL A 186 2848 2997 3583 -215 98 -163 C ATOM 937 O VAL A 186 36.358 53.758 1.758 1.00 23.52 O ANISOU 937 O VAL A 186 2631 2896 3408 -133 105 -200 O ATOM 938 CB VAL A 186 35.625 50.525 2.038 1.00 27.90 C ANISOU 938 CB VAL A 186 3507 3126 3968 -259 2 -203 C ATOM 939 CG1 VAL A 186 36.853 50.695 1.111 1.00 27.65 C ANISOU 939 CG1 VAL A 186 3482 3113 3911 -87 4 -262 C ATOM 940 CG2 VAL A 186 36.066 49.970 3.282 1.00 28.19 C ANISOU 940 CG2 VAL A 186 3621 3090 4001 -255 3 -135 C ATOM 941 N TRP A 187 35.961 53.325 3.938 1.00 24.78 N ANISOU 941 N TRP A 187 2827 3014 3575 -234 129 -105 N ATOM 942 CA TRP A 187 36.949 54.302 4.445 1.00 23.24 C ANISOU 942 CA TRP A 187 2565 2897 3369 -146 154 -88 C ATOM 943 C TRP A 187 38.391 53.822 4.205 1.00 23.82 C ANISOU 943 C TRP A 187 2688 2929 3434 -14 125 -98 C ATOM 944 O TRP A 187 38.775 52.718 4.639 1.00 23.52 O ANISOU 944 O TRP A 187 2760 2788 3389 15 88 -78 O ATOM 945 CB TRP A 187 36.768 54.501 5.943 1.00 22.35 C ANISOU 945 CB TRP A 187 2455 2801 3234 -199 180 -30 C ATOM 946 CG TRP A 187 35.897 55.648 6.378 1.00 22.32 C ANISOU 946 CG TRP A 187 2347 2898 3235 -261 234 -30 C ATOM 947 CD1 TRP A 187 36.216 56.985 6.341 1.00 20.94 C ANISOU 947 CD1 TRP A 187 2081 2808 3065 -212 254 -49 C ATOM 948 CD2 TRP A 187 34.585 55.566 6.998 1.00 21.45 C ANISOU 948 CD2 TRP A 187 2214 2811 3125 -380 281 -13 C ATOM 949 NE1 TRP A 187 35.166 57.748 6.860 1.00 21.32 N ANISOU 949 NE1 TRP A 187 2061 2922 3119 -272 304 -53 N ATOM 950 CE2 TRP A 187 34.165 56.905 7.277 1.00 22.11 C ANISOU 950 CE2 TRP A 187 2188 2998 3215 -372 329 -33 C ATOM 951 CE3 TRP A 187 33.727 54.504 7.331 1.00 21.95 C ANISOU 951 CE3 TRP A 187 2338 2817 3185 -497 290 18 C ATOM 952 CZ2 TRP A 187 32.922 57.203 7.883 1.00 23.01 C ANISOU 952 CZ2 TRP A 187 2233 3175 3333 -455 395 -32 C ATOM 953 CZ3 TRP A 187 32.458 54.795 7.931 1.00 22.71 C ANISOU 953 CZ3 TRP A 187 2354 2987 3286 -608 362 30 C ATOM 954 CH2 TRP A 187 32.076 56.139 8.196 1.00 25.16 C ANISOU 954 CH2 TRP A 187 2539 3417 3605 -574 418 0 C ATOM 955 N ARG A 188 39.187 54.661 3.545 1.00 24.10 N ANISOU 955 N ARG A 188 2639 3046 3473 67 143 -125 N ATOM 956 CA ARG A 188 40.603 54.383 3.342 1.00 25.85 C ANISOU 956 CA ARG A 188 2859 3268 3695 195 133 -136 C ATOM 957 C ARG A 188 41.464 55.559 3.771 1.00 25.55 C ANISOU 957 C ARG A 188 2704 3337 3665 225 151 -113 C ATOM 958 O ARG A 188 41.206 56.709 3.373 1.00 25.55 O ANISOU 958 O ARG A 188 2624 3416 3667 185 185 -119 O ATOM 959 CB ARG A 188 40.889 54.078 1.861 1.00 25.74 C ANISOU 959 CB ARG A 188 2858 3253 3670 264 147 -202 C ATOM 960 CG ARG A 188 40.323 52.762 1.387 1.00 30.40 C ANISOU 960 CG ARG A 188 3586 3715 4249 255 111 -240 C ATOM 961 CD ARG A 188 41.046 51.538 1.968 1.00 33.41 C ANISOU 961 CD ARG A 188 4073 3979 4641 344 67 -232 C ATOM 962 NE ARG A 188 40.419 50.315 1.461 1.00 35.72 N ANISOU 962 NE ARG A 188 4521 4126 4924 319 26 -273 N ATOM 963 CZ ARG A 188 40.415 49.129 2.082 1.00 35.16 C ANISOU 963 CZ ARG A 188 4595 3902 4863 326 -31 -251 C ATOM 964 NH1 ARG A 188 41.005 48.979 3.264 1.00 34.53 N ANISOU 964 NH1 ARG A 188 4525 3798 4795 367 -57 -181 N ATOM 965 NH2 ARG A 188 39.821 48.094 1.503 1.00 34.00 N ANISOU 965 NH2 ARG A 188 4595 3614 4709 288 -73 -296 N ATOM 966 N PHE A 189 42.486 55.263 4.575 1.00 26.01 N ANISOU 966 N PHE A 189 2761 3391 3732 295 117 -86 N ATOM 967 CA PHE A 189 43.497 56.234 4.950 1.00 25.51 C ANISOU 967 CA PHE A 189 2585 3426 3683 324 116 -70 C ATOM 968 C PHE A 189 44.402 56.553 3.756 1.00 25.96 C ANISOU 968 C PHE A 189 2549 3558 3758 398 157 -107 C ATOM 969 O PHE A 189 44.778 55.658 2.979 1.00 25.92 O ANISOU 969 O PHE A 189 2575 3521 3753 489 168 -145 O ATOM 970 CB PHE A 189 44.372 55.692 6.070 1.00 26.23 C ANISOU 970 CB PHE A 189 2696 3493 3777 387 47 -32 C ATOM 971 CG PHE A 189 45.389 56.705 6.613 1.00 27.04 C ANISOU 971 CG PHE A 189 2678 3700 3896 395 23 -14 C ATOM 972 CD1 PHE A 189 46.711 56.700 6.161 1.00 29.10 C ANISOU 972 CD1 PHE A 189 2826 4030 4199 494 15 -29 C ATOM 973 CD2 PHE A 189 45.013 57.641 7.578 1.00 24.37 C ANISOU 973 CD2 PHE A 189 2337 3390 3531 300 10 11 C ATOM 974 CE1 PHE A 189 47.651 57.611 6.681 1.00 29.68 C ANISOU 974 CE1 PHE A 189 2778 4201 4297 480 -19 -10 C ATOM 975 CE2 PHE A 189 45.931 58.535 8.108 1.00 23.98 C ANISOU 975 CE2 PHE A 189 2195 3420 3494 293 -29 21 C ATOM 976 CZ PHE A 189 47.244 58.538 7.650 1.00 27.42 C ANISOU 976 CZ PHE A 189 2510 3926 3981 372 -48 14 C ATOM 977 N ASP A 190 44.750 57.830 3.620 1.00 24.95 N ANISOU 977 N ASP A 190 2314 3526 3639 355 186 -96 N ATOM 978 CA ASP A 190 45.638 58.262 2.538 1.00 24.91 C ANISOU 978 CA ASP A 190 2212 3609 3642 398 241 -117 C ATOM 979 C ASP A 190 46.517 59.372 3.051 1.00 23.91 C ANISOU 979 C ASP A 190 1966 3574 3546 360 233 -84 C ATOM 980 O ASP A 190 46.032 60.481 3.268 1.00 22.32 O ANISOU 980 O ASP A 190 1758 3384 3340 262 234 -64 O ATOM 981 CB ASP A 190 44.839 58.741 1.326 1.00 23.90 C ANISOU 981 CB ASP A 190 2111 3491 3479 348 296 -137 C ATOM 982 CG ASP A 190 45.724 59.033 0.146 1.00 27.05 C ANISOU 982 CG ASP A 190 2437 3979 3862 390 367 -154 C ATOM 983 OD1 ASP A 190 46.951 59.126 0.332 1.00 31.12 O ANISOU 983 OD1 ASP A 190 2845 4571 4410 439 382 -145 O ATOM 984 OD2 ASP A 190 45.215 59.176 -0.976 1.00 29.90 O ANISOU 984 OD2 ASP A 190 2842 4346 4174 373 408 -174 O ATOM 985 N SER A 191 47.819 59.102 3.194 1.00 24.98 N ANISOU 985 N SER A 191 2001 3774 3718 438 220 -83 N ATOM 986 CA SER A 191 48.710 60.092 3.830 1.00 25.16 C ANISOU 986 CA SER A 191 1901 3881 3777 385 189 -51 C ATOM 987 C SER A 191 48.864 61.359 2.972 1.00 24.96 C ANISOU 987 C SER A 191 1801 3932 3752 291 259 -39 C ATOM 988 O SER A 191 49.161 62.417 3.486 1.00 25.36 O ANISOU 988 O SER A 191 1798 4014 3823 198 229 -11 O ATOM 989 CB SER A 191 50.073 59.465 4.112 1.00 27.01 C ANISOU 989 CB SER A 191 2020 4183 4062 496 152 -53 C ATOM 990 OG SER A 191 50.683 59.157 2.866 1.00 31.54 O ANISOU 990 OG SER A 191 2512 4827 4644 573 245 -85 O ATOM 991 N LYS A 192 48.594 61.259 1.669 1.00 24.79 N ANISOU 991 N LYS A 192 1800 3924 3697 308 345 -58 N ATOM 992 CA LYS A 192 48.742 62.384 0.752 1.00 24.95 C ANISOU 992 CA LYS A 192 1773 4008 3700 220 415 -34 C ATOM 993 C LYS A 192 47.695 63.484 0.991 1.00 24.54 C ANISOU 993 C LYS A 192 1805 3887 3631 106 385 -8 C ATOM 994 O LYS A 192 47.912 64.642 0.622 1.00 25.09 O ANISOU 994 O LYS A 192 1844 3988 3702 13 409 28 O ATOM 995 CB LYS A 192 48.710 61.881 -0.688 1.00 25.84 C ANISOU 995 CB LYS A 192 1910 4151 3756 279 509 -63 C ATOM 996 CG LYS A 192 49.727 60.717 -0.947 1.00 29.64 C ANISOU 996 CG LYS A 192 2315 4693 4253 424 548 -108 C ATOM 997 CD LYS A 192 49.963 60.363 -2.493 1.00 35.94 C ANISOU 997 CD LYS A 192 3122 5556 4979 484 670 -148 C ATOM 998 CE LYS A 192 48.656 59.944 -3.256 1.00 39.35 C ANISOU 998 CE LYS A 192 3738 5887 5327 485 667 -182 C ATOM 999 NZ LYS A 192 47.891 58.845 -2.496 1.00 40.16 N ANISOU 999 NZ LYS A 192 3951 5854 5452 545 574 -218 N ATOM 1000 N LEU A 193 46.574 63.133 1.631 1.00 22.87 N ANISOU 1000 N LEU A 193 1699 3582 3408 113 334 -24 N ATOM 1001 CA LEU A 193 45.566 64.128 1.936 1.00 22.01 C ANISOU 1001 CA LEU A 193 1655 3416 3292 32 309 -11 C ATOM 1002 C LEU A 193 46.068 65.200 2.889 1.00 22.35 C ANISOU 1002 C LEU A 193 1659 3465 3367 -44 263 10 C ATOM 1003 O LEU A 193 45.450 66.248 3.006 1.00 24.57 O ANISOU 1003 O LEU A 193 1988 3701 3647 -108 250 19 O ATOM 1004 CB LEU A 193 44.281 63.485 2.473 1.00 21.19 C ANISOU 1004 CB LEU A 193 1646 3233 3172 52 279 -36 C ATOM 1005 CG LEU A 193 43.580 62.548 1.454 1.00 21.20 C ANISOU 1005 CG LEU A 193 1704 3210 3141 99 307 -62 C ATOM 1006 CD1 LEU A 193 42.564 61.610 2.121 1.00 18.82 C ANISOU 1006 CD1 LEU A 193 1475 2838 2836 108 275 -82 C ATOM 1007 CD2 LEU A 193 42.925 63.329 0.321 1.00 20.86 C ANISOU 1007 CD2 LEU A 193 1687 3170 3070 63 330 -55 C ATOM 1008 N ALA A 194 47.199 64.967 3.538 1.00 22.29 N ANISOU 1008 N ALA A 194 1567 3512 3392 -33 231 16 N ATOM 1009 CA ALA A 194 47.775 65.942 4.453 1.00 21.65 C ANISOU 1009 CA ALA A 194 1448 3439 3338 -115 170 30 C ATOM 1010 C ALA A 194 48.471 67.085 3.709 1.00 21.96 C ANISOU 1010 C ALA A 194 1418 3524 3402 -212 203 65 C ATOM 1011 O ALA A 194 48.678 68.142 4.284 1.00 21.84 O ANISOU 1011 O ALA A 194 1408 3483 3405 -307 153 75 O ATOM 1012 CB ALA A 194 48.802 65.244 5.402 1.00 20.87 C ANISOU 1012 CB ALA A 194 1271 3392 3265 -69 102 27 C ATOM 1013 N PHE A 195 48.889 66.849 2.457 1.00 21.23 N ANISOU 1013 N PHE A 195 1266 3499 3302 -193 289 83 N ATOM 1014 CA PHE A 195 49.613 67.871 1.744 1.00 22.07 C ANISOU 1014 CA PHE A 195 1306 3658 3422 -300 333 129 C ATOM 1015 C PHE A 195 48.911 68.288 0.440 1.00 23.30 C ANISOU 1015 C PHE A 195 1547 3784 3520 -321 407 156 C ATOM 1016 O PHE A 195 49.169 69.406 -0.089 1.00 22.94 O ANISOU 1016 O PHE A 195 1509 3736 3472 -435 430 209 O ATOM 1017 CB PHE A 195 51.105 67.469 1.533 1.00 21.68 C ANISOU 1017 CB PHE A 195 1069 3752 3415 -291 372 140 C ATOM 1018 CG PHE A 195 51.299 66.284 0.620 1.00 22.27 C ANISOU 1018 CG PHE A 195 1104 3898 3461 -162 462 115 C ATOM 1019 CD1 PHE A 195 51.659 65.032 1.147 1.00 20.82 C ANISOU 1019 CD1 PHE A 195 869 3740 3301 -25 430 72 C ATOM 1020 CD2 PHE A 195 51.137 66.412 -0.788 1.00 20.18 C ANISOU 1020 CD2 PHE A 195 869 3666 3132 -171 574 132 C ATOM 1021 CE1 PHE A 195 51.879 63.943 0.284 1.00 24.38 C ANISOU 1021 CE1 PHE A 195 1295 4240 3726 106 511 36 C ATOM 1022 CE2 PHE A 195 51.364 65.318 -1.669 1.00 18.95 C ANISOU 1022 CE2 PHE A 195 688 3576 2936 -46 663 93 C ATOM 1023 CZ PHE A 195 51.701 64.082 -1.140 1.00 18.98 C ANISOU 1023 CZ PHE A 195 644 3594 2974 96 632 39 C ATOM 1024 N HIS A 196 48.024 67.407 -0.072 1.00 22.68 N ANISOU 1024 N HIS A 196 1546 3676 3393 -221 432 123 N ATOM 1025 CA HIS A 196 47.306 67.698 -1.320 1.00 22.56 C ANISOU 1025 CA HIS A 196 1622 3637 3312 -230 481 145 C ATOM 1026 C HIS A 196 45.803 67.778 -1.092 1.00 20.89 C ANISOU 1026 C HIS A 196 1535 3315 3086 -202 422 122 C ATOM 1027 O HIS A 196 45.124 66.766 -0.734 1.00 21.33 O ANISOU 1027 O HIS A 196 1620 3345 3140 -121 399 73 O ATOM 1028 CB HIS A 196 47.643 66.688 -2.431 1.00 24.09 C ANISOU 1028 CB HIS A 196 1792 3913 3449 -150 569 124 C ATOM 1029 CG HIS A 196 47.036 67.041 -3.764 1.00 27.22 C ANISOU 1029 CG HIS A 196 2288 4299 3757 -170 614 152 C ATOM 1030 ND1 HIS A 196 47.243 68.261 -4.375 1.00 33.38 N ANISOU 1030 ND1 HIS A 196 3093 5082 4508 -279 641 226 N ATOM 1031 CD2 HIS A 196 46.272 66.328 -4.616 1.00 28.87 C ANISOU 1031 CD2 HIS A 196 2586 4491 3891 -100 627 118 C ATOM 1032 CE1 HIS A 196 46.598 68.292 -5.527 1.00 33.05 C ANISOU 1032 CE1 HIS A 196 3158 5028 4372 -267 664 242 C ATOM 1033 NE2 HIS A 196 46.017 67.123 -5.703 1.00 29.74 N ANISOU 1033 NE2 HIS A 196 2774 4603 3923 -159 655 172 N ATOM 1034 N HIS A 197 45.269 68.987 -1.225 1.00 19.41 N ANISOU 1034 N HIS A 197 1419 3059 2898 -269 391 158 N ATOM 1035 CA HIS A 197 43.857 69.217 -0.938 1.00 17.72 C ANISOU 1035 CA HIS A 197 1296 2750 2685 -235 333 135 C ATOM 1036 C HIS A 197 43.044 68.772 -2.162 1.00 18.19 C ANISOU 1036 C HIS A 197 1416 2813 2682 -186 349 135 C ATOM 1037 O HIS A 197 42.655 69.607 -2.985 1.00 17.47 O ANISOU 1037 O HIS A 197 1394 2687 2557 -215 337 180 O ATOM 1038 CB HIS A 197 43.571 70.689 -0.590 1.00 16.89 C ANISOU 1038 CB HIS A 197 1252 2556 2609 -300 283 163 C ATOM 1039 CG HIS A 197 42.250 70.892 0.108 1.00 18.94 C ANISOU 1039 CG HIS A 197 1570 2733 2891 -245 228 118 C ATOM 1040 ND1 HIS A 197 41.767 72.142 0.462 1.00 17.21 N ANISOU 1040 ND1 HIS A 197 1422 2416 2699 -266 178 123 N ATOM 1041 CD2 HIS A 197 41.286 69.995 0.472 1.00 15.01 C ANISOU 1041 CD2 HIS A 197 1067 2240 2394 -170 221 67 C ATOM 1042 CE1 HIS A 197 40.572 72.001 1.027 1.00 17.66 C ANISOU 1042 CE1 HIS A 197 1500 2438 2774 -191 152 70 C ATOM 1043 NE2 HIS A 197 40.257 70.711 1.040 1.00 14.38 N ANISOU 1043 NE2 HIS A 197 1033 2088 2342 -144 180 40 N ATOM 1044 N MET A 198 42.827 67.460 -2.293 1.00 18.16 N ANISOU 1044 N MET A 198 1399 2843 2659 -116 365 88 N ATOM 1045 CA MET A 198 42.193 66.918 -3.503 1.00 20.56 C ANISOU 1045 CA MET A 198 1764 3156 2893 -78 374 78 C ATOM 1046 C MET A 198 40.774 67.489 -3.796 1.00 20.54 C ANISOU 1046 C MET A 198 1833 3087 2886 -73 302 85 C ATOM 1047 O MET A 198 40.501 67.886 -4.928 1.00 21.08 O ANISOU 1047 O MET A 198 1965 3156 2889 -80 293 119 O ATOM 1048 CB MET A 198 42.152 65.388 -3.502 1.00 20.72 C ANISOU 1048 CB MET A 198 1775 3197 2899 -9 388 17 C ATOM 1049 CG MET A 198 41.560 64.883 -4.856 1.00 26.05 C ANISOU 1049 CG MET A 198 2531 3881 3488 19 388 -2 C ATOM 1050 SD MET A 198 42.713 65.098 -6.292 1.00 32.91 S ANISOU 1050 SD MET A 198 3415 4841 4249 11 487 31 S ATOM 1051 CE MET A 198 43.893 63.783 -5.933 1.00 30.45 C ANISOU 1051 CE MET A 198 3025 4588 3958 89 560 -30 C ATOM 1052 N ALA A 199 39.904 67.539 -2.773 1.00 19.18 N ANISOU 1052 N ALA A 199 1645 2865 2777 -56 253 54 N ATOM 1053 CA ALA A 199 38.568 68.121 -2.916 1.00 19.68 C ANISOU 1053 CA ALA A 199 1742 2878 2857 -36 187 52 C ATOM 1054 C ALA A 199 38.596 69.513 -3.548 1.00 21.07 C ANISOU 1054 C ALA A 199 1979 3010 3016 -59 158 115 C ATOM 1055 O ALA A 199 37.753 69.835 -4.390 1.00 21.13 O ANISOU 1055 O ALA A 199 2038 2997 2996 -32 102 134 O ATOM 1056 CB ALA A 199 37.874 68.189 -1.549 1.00 18.22 C ANISOU 1056 CB ALA A 199 1517 2661 2745 -20 168 11 C ATOM 1057 N ARG A 200 39.568 70.332 -3.158 1.00 21.77 N ANISOU 1057 N ARG A 200 2069 3081 3122 -114 185 152 N ATOM 1058 CA ARG A 200 39.647 71.694 -3.685 1.00 24.37 C ANISOU 1058 CA ARG A 200 2476 3344 3439 -152 155 220 C ATOM 1059 C ARG A 200 40.194 71.728 -5.105 1.00 25.53 C ANISOU 1059 C ARG A 200 2677 3533 3489 -192 189 288 C ATOM 1060 O ARG A 200 39.819 72.575 -5.881 1.00 26.74 O ANISOU 1060 O ARG A 200 2924 3632 3603 -202 144 349 O ATOM 1061 CB ARG A 200 40.466 72.589 -2.777 1.00 24.85 C ANISOU 1061 CB ARG A 200 2531 3358 3552 -219 162 235 C ATOM 1062 CG ARG A 200 40.366 74.044 -3.151 1.00 28.71 C ANISOU 1062 CG ARG A 200 3125 3741 4043 -259 113 300 C ATOM 1063 CD ARG A 200 41.038 74.890 -2.079 1.00 32.85 C ANISOU 1063 CD ARG A 200 3653 4200 4628 -327 102 293 C ATOM 1064 NE ARG A 200 40.819 76.303 -2.340 1.00 38.71 N ANISOU 1064 NE ARG A 200 4520 4805 5382 -358 40 347 N ATOM 1065 CZ ARG A 200 40.963 77.263 -1.441 1.00 42.62 C ANISOU 1065 CZ ARG A 200 5068 5192 5934 -391 -3 326 C ATOM 1066 NH1 ARG A 200 41.326 76.943 -0.205 1.00 45.53 N ANISOU 1066 NH1 ARG A 200 5368 5590 6342 -401 8 253 N ATOM 1067 NH2 ARG A 200 40.743 78.536 -1.777 1.00 42.98 N ANISOU 1067 NH2 ARG A 200 5251 5091 5990 -412 -67 379 N ATOM 1068 N GLU A 201 41.037 70.767 -5.460 1.00 25.74 N ANISOU 1068 N GLU A 201 2653 3657 3468 -205 269 274 N ATOM 1069 CA GLU A 201 41.494 70.659 -6.843 1.00 27.14 C ANISOU 1069 CA GLU A 201 2885 3895 3533 -230 321 323 C ATOM 1070 C GLU A 201 40.312 70.247 -7.741 1.00 26.58 C ANISOU 1070 C GLU A 201 2893 3813 3395 -165 253 306 C ATOM 1071 O GLU A 201 40.131 70.826 -8.782 1.00 27.57 O ANISOU 1071 O GLU A 201 3118 3924 3432 -184 230 370 O ATOM 1072 CB GLU A 201 42.636 69.632 -6.979 1.00 26.48 C ANISOU 1072 CB GLU A 201 2719 3926 3419 -231 429 291 C ATOM 1073 CG GLU A 201 43.004 69.333 -8.426 1.00 33.68 C ANISOU 1073 CG GLU A 201 3690 4913 4194 -236 499 318 C ATOM 1074 CD GLU A 201 44.199 68.382 -8.581 1.00 40.88 C ANISOU 1074 CD GLU A 201 4510 5944 5079 -216 621 278 C ATOM 1075 OE1 GLU A 201 45.175 68.496 -7.802 1.00 42.27 O ANISOU 1075 OE1 GLU A 201 4569 6159 5334 -250 667 282 O ATOM 1076 OE2 GLU A 201 44.148 67.511 -9.477 1.00 44.26 O ANISOU 1076 OE2 GLU A 201 4983 6425 5408 -158 662 235 O ATOM 1077 N LEU A 202 39.543 69.235 -7.333 1.00 25.13 N ANISOU 1077 N LEU A 202 2668 3635 3247 -99 217 225 N ATOM 1078 CA LEU A 202 38.400 68.751 -8.110 1.00 25.82 C ANISOU 1078 CA LEU A 202 2810 3719 3283 -50 139 198 C ATOM 1079 C LEU A 202 37.247 69.774 -8.124 1.00 25.66 C ANISOU 1079 C LEU A 202 2827 3621 3301 -25 24 233 C ATOM 1080 O LEU A 202 36.589 69.929 -9.129 1.00 26.42 O ANISOU 1080 O LEU A 202 3000 3712 3325 -4 -51 259 O ATOM 1081 CB LEU A 202 37.894 67.399 -7.564 1.00 24.00 C ANISOU 1081 CB LEU A 202 2517 3506 3096 -9 129 106 C ATOM 1082 CG LEU A 202 38.910 66.261 -7.703 1.00 27.64 C ANISOU 1082 CG LEU A 202 2963 4026 3512 -3 222 62 C ATOM 1083 CD1 LEU A 202 38.447 64.971 -7.005 1.00 23.71 C ANISOU 1083 CD1 LEU A 202 2424 3514 3070 28 204 -18 C ATOM 1084 CD2 LEU A 202 39.201 65.984 -9.222 1.00 28.08 C ANISOU 1084 CD2 LEU A 202 3118 4132 3420 1 249 69 C ATOM 1085 N HIS A 203 37.023 70.459 -7.004 1.00 25.02 N ANISOU 1085 N HIS A 203 2695 3481 3329 -17 6 228 N ATOM 1086 CA HIS A 203 35.876 71.332 -6.868 1.00 25.68 C ANISOU 1086 CA HIS A 203 2795 3492 3468 37 -97 239 C ATOM 1087 C HIS A 203 36.210 72.698 -6.305 1.00 25.68 C ANISOU 1087 C HIS A 203 2835 3400 3522 22 -103 286 C ATOM 1088 O HIS A 203 35.750 73.029 -5.203 1.00 26.41 O ANISOU 1088 O HIS A 203 2875 3450 3711 61 -117 239 O ATOM 1089 CB HIS A 203 34.790 70.643 -6.018 1.00 24.33 C ANISOU 1089 CB HIS A 203 2518 3339 3386 92 -128 154 C ATOM 1090 CG HIS A 203 34.170 69.478 -6.710 1.00 25.90 C ANISOU 1090 CG HIS A 203 2700 3601 3541 102 -164 115 C ATOM 1091 ND1 HIS A 203 33.246 69.628 -7.736 1.00 24.35 N ANISOU 1091 ND1 HIS A 203 2544 3406 3303 137 -274 133 N ATOM 1092 CD2 HIS A 203 34.376 68.144 -6.569 1.00 23.31 C ANISOU 1092 CD2 HIS A 203 2335 3325 3199 76 -116 59 C ATOM 1093 CE1 HIS A 203 32.902 68.431 -8.179 1.00 26.30 C ANISOU 1093 CE1 HIS A 203 2775 3706 3510 122 -293 83 C ATOM 1094 NE2 HIS A 203 33.567 67.514 -7.488 1.00 25.12 N ANISOU 1094 NE2 HIS A 203 2586 3581 3380 86 -195 37 N ATOM 1095 N PRO A 204 36.968 73.515 -7.058 1.00 26.28 N ANISOU 1095 N PRO A 204 3015 3441 3530 -40 -92 376 N ATOM 1096 CA PRO A 204 37.263 74.832 -6.496 1.00 26.60 C ANISOU 1096 CA PRO A 204 3111 3369 3628 -68 -111 418 C ATOM 1097 C PRO A 204 35.988 75.645 -6.216 1.00 28.94 C ANISOU 1097 C PRO A 204 3438 3562 3997 39 -226 403 C ATOM 1098 O PRO A 204 35.991 76.535 -5.330 1.00 29.77 O ANISOU 1098 O PRO A 204 3564 3568 4180 51 -242 387 O ATOM 1099 CB PRO A 204 38.080 75.535 -7.608 1.00 27.60 C ANISOU 1099 CB PRO A 204 3361 3471 3653 -160 -94 536 C ATOM 1100 CG PRO A 204 37.849 74.705 -8.906 1.00 27.56 C ANISOU 1100 CG PRO A 204 3389 3560 3523 -143 -93 554 C ATOM 1101 CD PRO A 204 37.619 73.290 -8.374 1.00 26.73 C ANISOU 1101 CD PRO A 204 3150 3554 3452 -96 -53 442 C ATOM 1102 N GLU A 205 34.904 75.375 -6.953 1.00 29.62 N ANISOU 1102 N GLU A 205 3527 3668 4059 122 -311 400 N ATOM 1103 CA GLU A 205 33.653 76.128 -6.709 1.00 31.16 C ANISOU 1103 CA GLU A 205 3724 3780 4335 246 -425 381 C ATOM 1104 C GLU A 205 33.113 75.959 -5.278 1.00 30.19 C ANISOU 1104 C GLU A 205 3474 3666 4332 309 -392 272 C ATOM 1105 O GLU A 205 32.309 76.763 -4.842 1.00 31.54 O ANISOU 1105 O GLU A 205 3645 3757 4580 412 -456 246 O ATOM 1106 CB GLU A 205 32.568 75.863 -7.795 1.00 31.16 C ANISOU 1106 CB GLU A 205 3731 3815 4293 325 -543 400 C ATOM 1107 CG GLU A 205 31.887 74.455 -7.754 1.00 29.68 C ANISOU 1107 CG GLU A 205 3399 3761 4115 342 -535 315 C ATOM 1108 CD GLU A 205 32.788 73.328 -8.239 1.00 31.09 C ANISOU 1108 CD GLU A 205 3588 4034 4191 240 -445 313 C ATOM 1109 OE1 GLU A 205 33.991 73.612 -8.515 1.00 31.51 O ANISOU 1109 OE1 GLU A 205 3727 4071 4173 158 -368 372 O ATOM 1110 OE2 GLU A 205 32.305 72.156 -8.318 1.00 26.68 O ANISOU 1110 OE2 GLU A 205 2946 3563 3629 241 -447 249 O ATOM 1111 N TYR A 206 33.583 74.954 -4.525 1.00 30.41 N ANISOU 1111 N TYR A 206 3404 3784 4368 252 -291 211 N ATOM 1112 CA TYR A 206 33.123 74.771 -3.112 1.00 29.18 C ANISOU 1112 CA TYR A 206 3144 3642 4301 297 -248 116 C ATOM 1113 C TYR A 206 33.779 75.764 -2.158 1.00 31.69 C ANISOU 1113 C TYR A 206 3526 3861 4655 278 -220 105 C ATOM 1114 O TYR A 206 33.390 75.863 -0.959 1.00 31.36 O ANISOU 1114 O TYR A 206 3431 3812 4672 325 -188 25 O ATOM 1115 CB TYR A 206 33.402 73.373 -2.568 1.00 26.69 C ANISOU 1115 CB TYR A 206 2727 3439 3974 242 -161 63 C ATOM 1116 CG TYR A 206 32.759 72.214 -3.288 1.00 22.74 C ANISOU 1116 CG TYR A 206 2163 3030 3446 245 -183 51 C ATOM 1117 CD1 TYR A 206 31.775 72.411 -4.238 1.00 19.19 C ANISOU 1117 CD1 TYR A 206 1716 2581 2993 307 -285 70 C ATOM 1118 CD2 TYR A 206 33.140 70.908 -2.997 1.00 16.73 C ANISOU 1118 CD2 TYR A 206 1348 2346 2663 187 -115 17 C ATOM 1119 CE1 TYR A 206 31.194 71.364 -4.898 1.00 16.61 C ANISOU 1119 CE1 TYR A 206 1339 2335 2639 296 -321 52 C ATOM 1120 CE2 TYR A 206 32.562 69.829 -3.662 1.00 14.37 C ANISOU 1120 CE2 TYR A 206 1012 2112 2338 179 -144 -1 C ATOM 1121 CZ TYR A 206 31.592 70.076 -4.601 1.00 17.35 C ANISOU 1121 CZ TYR A 206 1389 2492 2710 226 -247 13 C ATOM 1122 OH TYR A 206 31.027 69.041 -5.285 1.00 18.25 O ANISOU 1122 OH TYR A 206 1475 2665 2794 205 -292 -10 O ATOM 1123 N TYR A 207 34.772 76.490 -2.670 1.00 34.21 N ANISOU 1123 N TYR A 207 3962 4106 4931 197 -228 185 N ATOM 1124 CA TYR A 207 35.641 77.320 -1.812 1.00 37.53 C ANISOU 1124 CA TYR A 207 4447 4437 5377 134 -203 179 C ATOM 1125 C TYR A 207 35.679 78.783 -2.277 1.00 42.11 C ANISOU 1125 C TYR A 207 5184 4849 5965 138 -285 247 C ATOM 1126 O TYR A 207 36.325 79.626 -1.655 1.00 44.80 O ANISOU 1126 O TYR A 207 5605 5087 6331 79 -287 245 O ATOM 1127 CB TYR A 207 37.062 76.741 -1.742 1.00 35.08 C ANISOU 1127 CB TYR A 207 4108 4200 5020 -6 -123 208 C ATOM 1128 CG TYR A 207 37.126 75.305 -1.245 1.00 29.16 C ANISOU 1128 CG TYR A 207 3228 3589 4263 -6 -53 148 C ATOM 1129 CD1 TYR A 207 36.981 74.237 -2.130 1.00 24.21 C ANISOU 1129 CD1 TYR A 207 2552 3060 3585 -1 -33 164 C ATOM 1130 CD2 TYR A 207 37.335 75.017 0.105 1.00 25.41 C ANISOU 1130 CD2 TYR A 207 2700 3134 3821 -12 -15 75 C ATOM 1131 CE1 TYR A 207 37.030 72.926 -1.705 1.00 21.20 C ANISOU 1131 CE1 TYR A 207 2077 2780 3200 0 20 113 C ATOM 1132 CE2 TYR A 207 37.373 73.669 0.565 1.00 21.96 C ANISOU 1132 CE2 TYR A 207 2164 2808 3373 -11 40 32 C ATOM 1133 CZ TYR A 207 37.228 72.645 -0.343 1.00 22.18 C ANISOU 1133 CZ TYR A 207 2150 2916 3363 -6 56 53 C ATOM 1134 OH TYR A 207 37.281 71.331 0.097 1.00 20.21 O ANISOU 1134 OH TYR A 207 1827 2749 3105 -7 102 14 O ATOM 1135 N LYS A 208 35.008 79.061 -3.385 1.00 45.49 N ANISOU 1135 N LYS A 208 5670 5246 6368 201 -362 309 N ATOM 1136 CA LYS A 208 34.754 80.420 -3.883 1.00 49.72 C ANISOU 1136 CA LYS A 208 6370 5607 6915 241 -465 378 C ATOM 1137 C LYS A 208 34.650 80.403 -5.404 1.00 51.51 C ANISOU 1137 C LYS A 208 6675 5845 7052 226 -522 493 C ATOM 1138 O LYS A 208 33.666 80.908 -5.964 1.00 54.62 O ANISOU 1138 O LYS A 208 7127 6169 7458 349 -637 520 O ATOM 1139 CB LYS A 208 35.794 81.464 -3.398 1.00 50.99 C ANISOU 1139 CB LYS A 208 6660 5625 7089 127 -456 410 C TER 1140 LYS A 208 ATOM 1141 N GLU B 79 52.591 78.066 39.836 1.00 92.21 N ANISOU 1141 N GLU B 79 11825 13844 9367 -4900 -1893 -2065 N ATOM 1142 CA GLU B 79 52.376 79.370 39.135 1.00 93.36 C ANISOU 1142 CA GLU B 79 12352 13412 9708 -5395 -1548 -2147 C ATOM 1143 C GLU B 79 51.041 80.010 39.542 1.00 91.12 C ANISOU 1143 C GLU B 79 12824 12487 9312 -5220 -1373 -2131 C ATOM 1144 O GLU B 79 50.149 79.320 40.048 1.00 87.51 O ANISOU 1144 O GLU B 79 12532 12015 8702 -4691 -1434 -1973 O ATOM 1145 CB GLU B 79 52.428 79.173 37.613 1.00 90.79 C ANISOU 1145 CB GLU B 79 11860 12961 9676 -5353 -1240 -1856 C ATOM 1146 N ASP B 80 50.915 81.321 39.301 1.00 93.28 N ANISOU 1146 N ASP B 80 13562 12230 9649 -5659 -1128 -2292 N ATOM 1147 CA ASP B 80 49.735 82.125 39.686 1.00 91.94 C ANISOU 1147 CA ASP B 80 14151 11438 9343 -5501 -944 -2326 C ATOM 1148 C ASP B 80 48.315 81.461 39.577 1.00 85.27 C ANISOU 1148 C ASP B 80 13534 10428 8437 -4771 -829 -2006 C ATOM 1149 O ASP B 80 47.499 81.642 40.487 1.00 85.76 O ANISOU 1149 O ASP B 80 13982 10336 8267 -4527 -865 -2089 O ATOM 1150 CB ASP B 80 49.772 83.514 38.999 1.00 95.17 C ANISOU 1150 CB ASP B 80 15071 11211 9877 -5969 -590 -2422 C ATOM 1151 CG ASP B 80 50.661 84.543 39.749 1.00103.47 C ANISOU 1151 CG ASP B 80 16272 12198 10845 -6717 -692 -2891 C ATOM 1152 OD1 ASP B 80 51.511 85.207 39.100 1.00106.94 O ANISOU 1152 OD1 ASP B 80 16651 12515 11468 -7347 -512 -3002 O ATOM 1153 OD2 ASP B 80 50.507 84.710 40.984 1.00105.78 O ANISOU 1153 OD2 ASP B 80 16759 12556 10876 -6707 -934 -3167 O ATOM 1154 N ILE B 81 48.023 80.696 38.517 1.00 79.31 N ANISOU 1154 N ILE B 81 12525 9740 7867 -4445 -693 -1676 N ATOM 1155 CA ILE B 81 46.643 80.175 38.292 1.00 73.09 C ANISOU 1155 CA ILE B 81 11935 8794 7041 -3846 -549 -1422 C ATOM 1156 C ILE B 81 46.416 78.658 38.538 1.00 68.31 C ANISOU 1156 C ILE B 81 10932 8620 6402 -3431 -721 -1230 C ATOM 1157 O ILE B 81 46.863 77.807 37.760 1.00 65.98 O ANISOU 1157 O ILE B 81 10222 8574 6271 -3348 -742 -1053 O ATOM 1158 CB ILE B 81 46.084 80.559 36.889 1.00 71.38 C ANISOU 1158 CB ILE B 81 11902 8216 7001 -3700 -214 -1208 C ATOM 1159 CG1 ILE B 81 46.202 82.071 36.645 1.00 75.96 C ANISOU 1159 CG1 ILE B 81 13025 8262 7577 -4050 17 -1356 C ATOM 1160 CG2 ILE B 81 44.628 80.090 36.732 1.00 66.85 C ANISOU 1160 CG2 ILE B 81 11478 7564 6359 -3111 -95 -1020 C ATOM 1161 CD1 ILE B 81 45.931 82.493 35.201 1.00 75.12 C ANISOU 1161 CD1 ILE B 81 13104 7826 7613 -3940 347 -1133 C ATOM 1162 N ILE B 82 45.674 78.349 39.605 1.00 66.20 N ANISOU 1162 N ILE B 82 10856 8393 5903 -3163 -802 -1261 N ATOM 1163 CA ILE B 82 45.440 76.979 40.051 1.00 62.32 C ANISOU 1163 CA ILE B 82 10120 8234 5324 -2816 -931 -1094 C ATOM 1164 C ILE B 82 43.962 76.643 39.956 1.00 58.45 C ANISOU 1164 C ILE B 82 9844 7565 4799 -2426 -707 -932 C ATOM 1165 O ILE B 82 43.113 77.440 40.346 1.00 58.83 O ANISOU 1165 O ILE B 82 10276 7361 4717 -2351 -570 -1029 O ATOM 1166 CB ILE B 82 45.928 76.780 41.517 1.00 65.78 C ANISOU 1166 CB ILE B 82 10572 8959 5463 -2848 -1219 -1266 C ATOM 1167 CG1 ILE B 82 47.359 77.321 41.707 1.00 69.63 C ANISOU 1167 CG1 ILE B 82 10823 9683 5950 -3293 -1462 -1523 C ATOM 1168 CG2 ILE B 82 45.797 75.320 41.965 1.00 63.45 C ANISOU 1168 CG2 ILE B 82 10093 8968 5047 -2473 -1325 -1056 C ATOM 1169 CD1 ILE B 82 48.425 76.613 40.866 1.00 68.68 C ANISOU 1169 CD1 ILE B 82 10143 9919 6035 -3359 -1562 -1412 C ATOM 1170 N VAL B 83 43.662 75.464 39.414 1.00 54.89 N ANISOU 1170 N VAL B 83 9136 7263 4458 -2184 -662 -706 N ATOM 1171 CA VAL B 83 42.276 74.994 39.249 1.00 51.81 C ANISOU 1171 CA VAL B 83 8843 6787 4057 -1874 -448 -575 C ATOM 1172 C VAL B 83 42.064 73.612 39.868 1.00 50.50 C ANISOU 1172 C VAL B 83 8567 6834 3787 -1689 -497 -435 C ATOM 1173 O VAL B 83 43.006 72.829 39.992 1.00 51.18 O ANISOU 1173 O VAL B 83 8452 7121 3872 -1704 -681 -368 O ATOM 1174 CB VAL B 83 41.845 74.927 37.762 1.00 49.25 C ANISOU 1174 CB VAL B 83 8375 6362 3977 -1776 -267 -453 C ATOM 1175 CG1 VAL B 83 41.942 76.282 37.102 1.00 50.34 C ANISOU 1175 CG1 VAL B 83 8721 6228 4179 -1897 -157 -543 C ATOM 1176 CG2 VAL B 83 42.657 73.874 36.994 1.00 47.94 C ANISOU 1176 CG2 VAL B 83 7838 6387 3991 -1789 -360 -311 C ATOM 1177 N VAL B 84 40.823 73.323 40.242 1.00 48.89 N ANISOU 1177 N VAL B 84 8507 6589 3480 -1505 -308 -389 N ATOM 1178 CA VAL B 84 40.452 72.025 40.789 1.00 48.10 C ANISOU 1178 CA VAL B 84 8385 6612 3279 -1370 -263 -239 C ATOM 1179 C VAL B 84 39.385 71.421 39.881 1.00 46.11 C ANISOU 1179 C VAL B 84 7993 6324 3204 -1280 -21 -144 C ATOM 1180 O VAL B 84 38.424 72.107 39.480 1.00 45.60 O ANISOU 1180 O VAL B 84 7949 6204 3173 -1218 148 -224 O ATOM 1181 CB VAL B 84 39.933 72.159 42.270 1.00 50.62 C ANISOU 1181 CB VAL B 84 9006 6967 3260 -1293 -225 -294 C ATOM 1182 CG1 VAL B 84 39.370 70.840 42.799 1.00 50.47 C ANISOU 1182 CG1 VAL B 84 9037 7014 3124 -1174 -80 -109 C ATOM 1183 CG2 VAL B 84 41.042 72.644 43.187 1.00 51.69 C ANISOU 1183 CG2 VAL B 84 9258 7198 3186 -1379 -511 -423 C ATOM 1184 N ALA B 85 39.557 70.150 39.534 1.00 45.41 N ANISOU 1184 N ALA B 85 7768 6278 3209 -1255 -12 5 N ATOM 1185 CA ALA B 85 38.622 69.464 38.635 1.00 43.77 C ANISOU 1185 CA ALA B 85 7405 6053 3172 -1232 194 52 C ATOM 1186 C ALA B 85 37.257 69.269 39.304 1.00 45.53 C ANISOU 1186 C ALA B 85 7726 6316 3258 -1219 449 27 C ATOM 1187 O ALA B 85 37.191 68.903 40.489 1.00 47.59 O ANISOU 1187 O ALA B 85 8204 6584 3293 -1217 493 86 O ATOM 1188 CB ALA B 85 39.182 68.139 38.251 1.00 42.94 C ANISOU 1188 CB ALA B 85 7224 5930 3160 -1222 152 194 C ATOM 1189 N LEU B 86 36.184 69.483 38.544 1.00 44.77 N ANISOU 1189 N LEU B 86 7450 6290 3272 -1195 622 -62 N ATOM 1190 CA LEU B 86 34.824 69.285 39.048 1.00 47.03 C ANISOU 1190 CA LEU B 86 7714 6709 3445 -1203 889 -117 C ATOM 1191 C LEU B 86 34.240 67.917 38.634 1.00 47.71 C ANISOU 1191 C LEU B 86 7643 6830 3654 -1369 1069 -71 C ATOM 1192 O LEU B 86 33.303 67.424 39.240 1.00 49.17 O ANISOU 1192 O LEU B 86 7835 7109 3739 -1480 1320 -83 O ATOM 1193 CB LEU B 86 33.912 70.455 38.622 1.00 46.75 C ANISOU 1193 CB LEU B 86 7564 6811 3389 -1028 972 -283 C ATOM 1194 CG LEU B 86 34.441 71.859 38.990 1.00 47.35 C ANISOU 1194 CG LEU B 86 7894 6759 3339 -889 836 -348 C ATOM 1195 CD1 LEU B 86 33.773 72.987 38.190 1.00 45.11 C ANISOU 1195 CD1 LEU B 86 7560 6517 3064 -644 894 -474 C ATOM 1196 CD2 LEU B 86 34.342 72.134 40.499 1.00 46.58 C ANISOU 1196 CD2 LEU B 86 8089 6657 2954 -874 882 -369 C ATOM 1197 N TYR B 87 34.806 67.325 37.585 1.00 47.04 N ANISOU 1197 N TYR B 87 7431 6663 3778 -1408 959 -36 N ATOM 1198 CA TYR B 87 34.375 66.024 37.073 1.00 48.38 C ANISOU 1198 CA TYR B 87 7505 6801 4076 -1589 1108 -26 C ATOM 1199 C TYR B 87 35.617 65.309 36.582 1.00 47.12 C ANISOU 1199 C TYR B 87 7444 6437 4021 -1554 924 104 C ATOM 1200 O TYR B 87 36.604 65.964 36.246 1.00 45.88 O ANISOU 1200 O TYR B 87 7260 6272 3901 -1407 694 132 O ATOM 1201 CB TYR B 87 33.417 66.184 35.881 1.00 48.07 C ANISOU 1201 CB TYR B 87 7093 6982 4189 -1604 1178 -222 C ATOM 1202 CG TYR B 87 32.378 67.261 36.048 1.00 49.86 C ANISOU 1202 CG TYR B 87 7149 7491 4307 -1470 1272 -375 C ATOM 1203 CD1 TYR B 87 31.119 66.962 36.574 1.00 54.19 C ANISOU 1203 CD1 TYR B 87 7549 8272 4766 -1613 1543 -482 C ATOM 1204 CD2 TYR B 87 32.649 68.581 35.681 1.00 48.31 C ANISOU 1204 CD2 TYR B 87 6954 7324 4076 -1192 1119 -413 C ATOM 1205 CE1 TYR B 87 30.151 67.955 36.749 1.00 56.72 C ANISOU 1205 CE1 TYR B 87 7688 8910 4951 -1412 1634 -630 C ATOM 1206 CE2 TYR B 87 31.687 69.583 35.829 1.00 52.21 C ANISOU 1206 CE2 TYR B 87 7354 8051 4431 -980 1214 -547 C ATOM 1207 CZ TYR B 87 30.436 69.260 36.373 1.00 56.62 C ANISOU 1207 CZ TYR B 87 7726 8899 4887 -1058 1460 -659 C ATOM 1208 OH TYR B 87 29.474 70.237 36.541 1.00 59.78 O ANISOU 1208 OH TYR B 87 8008 9588 5119 -779 1558 -799 O ATOM 1209 N ASP B 88 35.560 63.979 36.555 1.00 48.13 N ANISOU 1209 N ASP B 88 7702 6401 4186 -1694 1052 175 N ATOM 1210 CA ASP B 88 36.511 63.158 35.825 1.00 47.67 C ANISOU 1210 CA ASP B 88 7704 6167 4241 -1622 924 258 C ATOM 1211 C ASP B 88 36.595 63.625 34.354 1.00 45.40 C ANISOU 1211 C ASP B 88 7084 6011 4155 -1549 795 121 C ATOM 1212 O ASP B 88 35.554 63.909 33.735 1.00 45.48 O ANISOU 1212 O ASP B 88 6845 6195 4240 -1638 895 -59 O ATOM 1213 CB ASP B 88 36.050 61.688 35.857 1.00 49.49 C ANISOU 1213 CB ASP B 88 8154 6160 4488 -1828 1162 293 C ATOM 1214 CG ASP B 88 36.212 61.042 37.216 1.00 52.55 C ANISOU 1214 CG ASP B 88 8986 6339 4644 -1835 1300 497 C ATOM 1215 OD1 ASP B 88 36.649 61.712 38.174 1.00 54.58 O ANISOU 1215 OD1 ASP B 88 9345 6684 4708 -1670 1186 592 O ATOM 1216 OD2 ASP B 88 35.896 59.842 37.344 1.00 54.62 O ANISOU 1216 OD2 ASP B 88 9539 6325 4889 -2008 1536 560 O ATOM 1217 N TYR B 89 37.808 63.730 33.803 1.00 44.08 N ANISOU 1217 N TYR B 89 6894 5810 4045 -1366 580 200 N ATOM 1218 CA TYR B 89 37.958 63.911 32.345 1.00 42.69 C ANISOU 1218 CA TYR B 89 6467 5718 4034 -1287 500 104 C ATOM 1219 C TYR B 89 38.830 62.817 31.764 1.00 43.47 C ANISOU 1219 C TYR B 89 6659 5665 4195 -1192 440 183 C ATOM 1220 O TYR B 89 40.046 62.827 31.955 1.00 44.06 O ANISOU 1220 O TYR B 89 6787 5728 4226 -1018 285 318 O ATOM 1221 CB TYR B 89 38.503 65.293 31.951 1.00 41.27 C ANISOU 1221 CB TYR B 89 6132 5679 3871 -1151 351 98 C ATOM 1222 CG TYR B 89 38.711 65.454 30.440 1.00 38.97 C ANISOU 1222 CG TYR B 89 5634 5464 3706 -1037 300 38 C ATOM 1223 CD1 TYR B 89 37.627 65.334 29.562 1.00 38.29 C ANISOU 1223 CD1 TYR B 89 5388 5493 3670 -1046 391 -127 C ATOM 1224 CD2 TYR B 89 39.975 65.708 29.897 1.00 35.82 C ANISOU 1224 CD2 TYR B 89 5181 5075 3354 -918 168 132 C ATOM 1225 CE1 TYR B 89 37.779 65.455 28.183 1.00 35.99 C ANISOU 1225 CE1 TYR B 89 4938 5293 3443 -900 341 -185 C ATOM 1226 CE2 TYR B 89 40.147 65.843 28.497 1.00 35.72 C ANISOU 1226 CE2 TYR B 89 5009 5137 3425 -796 157 93 C ATOM 1227 CZ TYR B 89 39.028 65.707 27.653 1.00 36.64 C ANISOU 1227 CZ TYR B 89 5022 5338 3563 -769 239 -60 C ATOM 1228 OH TYR B 89 39.125 65.796 26.286 1.00 34.23 O ANISOU 1228 OH TYR B 89 4588 5129 3290 -611 223 -108 O ATOM 1229 N TYR B 90 38.203 61.858 31.089 1.00 44.44 N ANISOU 1229 N TYR B 90 6796 5690 4398 -1303 565 75 N ATOM 1230 CA TYR B 90 38.929 60.864 30.342 1.00 45.82 C ANISOU 1230 CA TYR B 90 7078 5705 4627 -1177 522 107 C ATOM 1231 C TYR B 90 38.999 61.262 28.881 1.00 44.38 C ANISOU 1231 C TYR B 90 6608 5697 4556 -1068 434 -23 C ATOM 1232 O TYR B 90 37.996 61.677 28.262 1.00 44.80 O ANISOU 1232 O TYR B 90 6443 5923 4657 -1172 483 -212 O ATOM 1233 CB TYR B 90 38.306 59.473 30.446 1.00 49.52 C ANISOU 1233 CB TYR B 90 7834 5882 5098 -1379 725 52 C ATOM 1234 CG TYR B 90 38.960 58.508 29.466 1.00 53.74 C ANISOU 1234 CG TYR B 90 8497 6237 5684 -1217 685 32 C ATOM 1235 CD1 TYR B 90 40.157 57.845 29.792 1.00 57.13 C ANISOU 1235 CD1 TYR B 90 9220 6472 6015 -915 613 239 C ATOM 1236 CD2 TYR B 90 38.410 58.290 28.187 1.00 55.50 C ANISOU 1236 CD2 TYR B 90 8537 6529 6021 -1306 700 -209 C ATOM 1237 CE1 TYR B 90 40.771 56.964 28.878 1.00 59.48 C ANISOU 1237 CE1 TYR B 90 9656 6609 6334 -700 588 215 C ATOM 1238 CE2 TYR B 90 39.021 57.412 27.270 1.00 57.04 C ANISOU 1238 CE2 TYR B 90 8882 6552 6237 -1130 666 -247 C ATOM 1239 CZ TYR B 90 40.197 56.763 27.627 1.00 59.32 C ANISOU 1239 CZ TYR B 90 9487 6616 6435 -823 622 -29 C ATOM 1240 OH TYR B 90 40.798 55.910 26.731 1.00 63.81 O ANISOU 1240 OH TYR B 90 10223 7022 7000 -592 602 -72 O ATOM 1241 N SER B 91 40.198 61.126 28.336 1.00 43.09 N ANISOU 1241 N SER B 91 6437 5532 4404 -819 307 78 N ATOM 1242 CA SER B 91 40.446 61.429 26.950 1.00 41.01 C ANISOU 1242 CA SER B 91 5952 5420 4210 -673 243 -5 C ATOM 1243 C SER B 91 41.338 60.361 26.388 1.00 40.80 C ANISOU 1243 C SER B 91 6062 5260 4181 -464 214 41 C ATOM 1244 O SER B 91 42.372 60.026 26.984 1.00 41.41 O ANISOU 1244 O SER B 91 6264 5280 4192 -288 149 213 O ATOM 1245 CB SER B 91 41.123 62.779 26.806 1.00 39.78 C ANISOU 1245 CB SER B 91 5587 5477 4052 -564 142 85 C ATOM 1246 OG SER B 91 41.310 63.073 25.441 1.00 39.99 O ANISOU 1246 OG SER B 91 5443 5637 4115 -415 126 29 O ATOM 1247 N PRO B 92 40.942 59.815 25.235 1.00 40.23 N ANISOU 1247 N PRO B 92 5967 5169 4151 -443 251 -131 N ATOM 1248 CA PRO B 92 41.783 58.792 24.604 1.00 41.11 C ANISOU 1248 CA PRO B 92 6245 5139 4238 -195 235 -110 C ATOM 1249 C PRO B 92 43.034 59.382 23.929 1.00 39.06 C ANISOU 1249 C PRO B 92 5755 5125 3961 123 128 15 C ATOM 1250 O PRO B 92 43.908 58.618 23.505 1.00 40.54 O ANISOU 1250 O PRO B 92 6042 5260 4101 403 111 63 O ATOM 1251 CB PRO B 92 40.861 58.200 23.541 1.00 41.83 C ANISOU 1251 CB PRO B 92 6351 5178 4363 -312 299 -387 C ATOM 1252 CG PRO B 92 39.952 59.352 23.173 1.00 40.74 C ANISOU 1252 CG PRO B 92 5875 5353 4252 -445 274 -511 C ATOM 1253 CD PRO B 92 39.727 60.107 24.454 1.00 39.30 C ANISOU 1253 CD PRO B 92 5666 5197 4070 -601 293 -375 C ATOM 1254 N PHE B 93 43.115 60.710 23.834 1.00 35.82 N ANISOU 1254 N PHE B 93 5065 4970 3575 78 86 64 N ATOM 1255 CA PHE B 93 44.142 61.357 23.001 1.00 34.89 C ANISOU 1255 CA PHE B 93 4715 5093 3450 287 50 152 C ATOM 1256 C PHE B 93 45.314 61.811 23.840 1.00 35.12 C ANISOU 1256 C PHE B 93 4630 5253 3460 326 -25 336 C ATOM 1257 O PHE B 93 45.111 62.395 24.894 1.00 35.04 O ANISOU 1257 O PHE B 93 4635 5229 3449 133 -60 378 O ATOM 1258 CB PHE B 93 43.569 62.557 22.236 1.00 32.14 C ANISOU 1258 CB PHE B 93 4188 4909 3112 220 88 95 C ATOM 1259 CG PHE B 93 42.332 62.247 21.440 1.00 32.44 C ANISOU 1259 CG PHE B 93 4260 4934 3131 199 121 -124 C ATOM 1260 CD1 PHE B 93 42.392 61.425 20.322 1.00 30.02 C ANISOU 1260 CD1 PHE B 93 3989 4635 2784 380 127 -248 C ATOM 1261 CD2 PHE B 93 41.088 62.794 21.812 1.00 29.61 C ANISOU 1261 CD2 PHE B 93 3873 4604 2772 10 139 -238 C ATOM 1262 CE1 PHE B 93 41.242 61.159 19.574 1.00 32.21 C ANISOU 1262 CE1 PHE B 93 4255 4963 3021 338 126 -504 C ATOM 1263 CE2 PHE B 93 39.936 62.524 21.064 1.00 30.94 C ANISOU 1263 CE2 PHE B 93 3986 4870 2902 -6 145 -483 C ATOM 1264 CZ PHE B 93 40.002 61.704 19.957 1.00 29.81 C ANISOU 1264 CZ PHE B 93 3860 4746 2719 134 127 -629 C ATOM 1265 N SER B 94 46.526 61.580 23.348 1.00 36.41 N ANISOU 1265 N SER B 94 4649 5595 3592 576 -51 419 N ATOM 1266 CA SER B 94 47.757 61.835 24.114 1.00 39.00 C ANISOU 1266 CA SER B 94 4794 6145 3878 640 -148 551 C ATOM 1267 C SER B 94 47.990 63.323 24.359 1.00 38.44 C ANISOU 1267 C SER B 94 4487 6259 3859 358 -149 582 C ATOM 1268 O SER B 94 48.773 63.681 25.241 1.00 39.37 O ANISOU 1268 O SER B 94 4459 6556 3944 286 -252 634 O ATOM 1269 CB SER B 94 48.987 61.268 23.385 1.00 41.25 C ANISOU 1269 CB SER B 94 4901 6668 4106 997 -153 605 C ATOM 1270 OG SER B 94 49.196 61.960 22.131 1.00 42.02 O ANISOU 1270 OG SER B 94 4776 6946 4246 985 -38 592 O ATOM 1271 N TRP B 95 47.346 64.184 23.554 1.00 36.71 N ANISOU 1271 N TRP B 95 4253 6000 3694 218 -35 537 N ATOM 1272 CA TRP B 95 47.587 65.619 23.656 1.00 35.68 C ANISOU 1272 CA TRP B 95 3997 5961 3598 -39 14 573 C ATOM 1273 C TRP B 95 46.695 66.225 24.730 1.00 35.10 C ANISOU 1273 C TRP B 95 4106 5706 3524 -275 -25 526 C ATOM 1274 O TRP B 95 46.828 67.394 25.065 1.00 35.50 O ANISOU 1274 O TRP B 95 4142 5760 3586 -503 4 535 O ATOM 1275 CB TRP B 95 47.389 66.314 22.308 1.00 35.35 C ANISOU 1275 CB TRP B 95 3932 5937 3561 -6 180 585 C ATOM 1276 CG TRP B 95 46.046 66.013 21.659 1.00 32.47 C ANISOU 1276 CG TRP B 95 3762 5412 3164 121 215 482 C ATOM 1277 CD1 TRP B 95 44.819 66.533 22.002 1.00 30.59 C ANISOU 1277 CD1 TRP B 95 3680 5029 2912 15 221 404 C ATOM 1278 CD2 TRP B 95 45.811 65.111 20.576 1.00 30.33 C ANISOU 1278 CD2 TRP B 95 3511 5164 2847 382 238 411 C ATOM 1279 NE1 TRP B 95 43.839 66.015 21.178 1.00 29.76 N ANISOU 1279 NE1 TRP B 95 3636 4913 2760 180 234 278 N ATOM 1280 CE2 TRP B 95 44.418 65.140 20.298 1.00 29.57 C ANISOU 1280 CE2 TRP B 95 3549 4969 2716 385 238 269 C ATOM 1281 CE3 TRP B 95 46.646 64.287 19.800 1.00 30.42 C ANISOU 1281 CE3 TRP B 95 3433 5301 2825 633 256 430 C ATOM 1282 CZ2 TRP B 95 43.840 64.392 19.266 1.00 28.89 C ANISOU 1282 CZ2 TRP B 95 3501 4909 2565 581 238 122 C ATOM 1283 CZ3 TRP B 95 46.068 63.520 18.785 1.00 32.19 C ANISOU 1283 CZ3 TRP B 95 3759 5490 2981 852 270 299 C ATOM 1284 CH2 TRP B 95 44.672 63.581 18.530 1.00 30.03 C ANISOU 1284 CH2 TRP B 95 3612 5120 2679 799 251 134 C ATOM 1285 N ASP B 96 45.786 65.431 25.281 1.00 34.81 N ANISOU 1285 N ASP B 96 4264 5498 3464 -235 -65 469 N ATOM 1286 CA ASP B 96 44.903 65.928 26.336 1.00 34.10 C ANISOU 1286 CA ASP B 96 4335 5273 3349 -430 -77 423 C ATOM 1287 C ASP B 96 45.460 65.517 27.699 1.00 36.21 C ANISOU 1287 C ASP B 96 4651 5561 3544 -463 -205 473 C ATOM 1288 O ASP B 96 46.083 64.452 27.828 1.00 36.85 O ANISOU 1288 O ASP B 96 4736 5682 3582 -269 -273 528 O ATOM 1289 CB ASP B 96 43.521 65.332 26.178 1.00 32.86 C ANISOU 1289 CB ASP B 96 4329 4966 3190 -411 -9 319 C ATOM 1290 CG ASP B 96 42.624 66.125 25.242 1.00 32.23 C ANISOU 1290 CG ASP B 96 4219 4913 3115 -392 84 234 C ATOM 1291 OD1 ASP B 96 43.004 67.228 24.766 1.00 31.43 O ANISOU 1291 OD1 ASP B 96 4070 4864 3007 -390 127 288 O ATOM 1292 OD2 ASP B 96 41.511 65.616 24.974 1.00 30.70 O ANISOU 1292 OD2 ASP B 96 4059 4694 2912 -375 123 105 O ATOM 1293 N LEU B 97 45.255 66.350 28.720 1.00 36.20 N ANISOU 1293 N LEU B 97 4723 5538 3495 -658 -242 450 N ATOM 1294 CA LEU B 97 45.551 65.882 30.060 1.00 37.86 C ANISOU 1294 CA LEU B 97 5036 5765 3583 -648 -365 484 C ATOM 1295 C LEU B 97 44.276 65.236 30.590 1.00 37.90 C ANISOU 1295 C LEU B 97 5312 5546 3542 -658 -270 465 C ATOM 1296 O LEU B 97 43.261 65.921 30.738 1.00 37.02 O ANISOU 1296 O LEU B 97 5273 5353 3438 -802 -176 388 O ATOM 1297 CB LEU B 97 46.005 67.030 30.954 1.00 38.80 C ANISOU 1297 CB LEU B 97 5113 5989 3639 -860 -461 439 C ATOM 1298 CG LEU B 97 46.376 66.713 32.398 1.00 42.11 C ANISOU 1298 CG LEU B 97 5629 6493 3878 -831 -622 453 C ATOM 1299 CD1 LEU B 97 47.570 65.746 32.505 1.00 43.64 C ANISOU 1299 CD1 LEU B 97 5668 6928 3986 -566 -780 534 C ATOM 1300 CD2 LEU B 97 46.658 68.041 33.140 1.00 45.37 C ANISOU 1300 CD2 LEU B 97 6020 6985 4234 -1103 -704 341 C ATOM 1301 N SER B 98 44.311 63.919 30.814 1.00 39.12 N ANISOU 1301 N SER B 98 5626 5598 3640 -500 -264 529 N ATOM 1302 CA SER B 98 43.244 63.249 31.543 1.00 40.62 C ANISOU 1302 CA SER B 98 6103 5568 3761 -576 -142 527 C ATOM 1303 C SER B 98 43.456 63.544 33.008 1.00 42.25 C ANISOU 1303 C SER B 98 6452 5814 3787 -603 -223 588 C ATOM 1304 O SER B 98 44.609 63.706 33.454 1.00 43.71 O ANISOU 1304 O SER B 98 6549 6186 3874 -474 -410 645 O ATOM 1305 CB SER B 98 43.271 61.730 31.334 1.00 42.09 C ANISOU 1305 CB SER B 98 6519 5549 3923 -420 -70 587 C ATOM 1306 OG SER B 98 42.730 61.393 30.062 1.00 43.31 O ANISOU 1306 OG SER B 98 6599 5634 4224 -454 31 472 O ATOM 1307 N PHE B 99 42.352 63.596 33.752 1.00 42.24 N ANISOU 1307 N PHE B 99 6644 5686 3720 -760 -85 559 N ATOM 1308 CA PHE B 99 42.396 63.829 35.184 1.00 43.84 C ANISOU 1308 CA PHE B 99 7036 5911 3709 -770 -132 611 C ATOM 1309 C PHE B 99 41.155 63.279 35.925 1.00 45.64 C ANISOU 1309 C PHE B 99 7550 5947 3842 -898 106 629 C ATOM 1310 O PHE B 99 40.130 62.961 35.288 1.00 45.05 O ANISOU 1310 O PHE B 99 7441 5773 3902 -1052 303 547 O ATOM 1311 CB PHE B 99 42.597 65.335 35.465 1.00 42.87 C ANISOU 1311 CB PHE B 99 6752 5962 3573 -889 -247 506 C ATOM 1312 CG PHE B 99 41.555 66.234 34.831 1.00 40.08 C ANISOU 1312 CG PHE B 99 6302 5574 3351 -1042 -104 376 C ATOM 1313 CD1 PHE B 99 40.313 66.429 35.441 1.00 37.14 C ANISOU 1313 CD1 PHE B 99 6066 5145 2901 -1134 66 319 C ATOM 1314 CD2 PHE B 99 41.829 66.906 33.643 1.00 37.32 C ANISOU 1314 CD2 PHE B 99 5732 5280 3167 -1052 -128 319 C ATOM 1315 CE1 PHE B 99 39.354 67.264 34.882 1.00 35.64 C ANISOU 1315 CE1 PHE B 99 5770 4986 2786 -1182 181 194 C ATOM 1316 CE2 PHE B 99 40.871 67.749 33.062 1.00 36.16 C ANISOU 1316 CE2 PHE B 99 5542 5113 3085 -1098 -4 216 C ATOM 1317 CZ PHE B 99 39.632 67.927 33.677 1.00 36.77 C ANISOU 1317 CZ PHE B 99 5731 5165 3073 -1138 135 146 C ATOM 1318 N GLN B 100 41.272 63.174 37.258 1.00 47.47 N ANISOU 1318 N GLN B 100 8041 6171 3826 -840 89 723 N ATOM 1319 CA GLN B 100 40.173 62.805 38.160 1.00 49.82 C ANISOU 1319 CA GLN B 100 8621 6325 3983 -974 342 759 C ATOM 1320 C GLN B 100 39.546 64.017 38.841 1.00 48.37 C ANISOU 1320 C GLN B 100 8376 6291 3712 -1092 364 646 C ATOM 1321 O GLN B 100 40.225 65.008 39.103 1.00 48.05 O ANISOU 1321 O GLN B 100 8233 6412 3613 -1030 144 584 O ATOM 1322 CB GLN B 100 40.665 61.864 39.273 1.00 53.63 C ANISOU 1322 CB GLN B 100 9523 6680 4173 -774 348 967 C ATOM 1323 CG GLN B 100 41.106 60.483 38.804 1.00 58.85 C ANISOU 1323 CG GLN B 100 10415 7096 4851 -607 403 1108 C ATOM 1324 CD GLN B 100 41.584 59.614 39.950 1.00 68.30 C ANISOU 1324 CD GLN B 100 12104 8150 5698 -324 420 1342 C ATOM 1325 OE1 GLN B 100 41.902 58.438 39.756 1.00 72.83 O ANISOU 1325 OE1 GLN B 100 13002 8455 6215 -132 503 1487 O ATOM 1326 NE2 GLN B 100 41.628 60.184 41.162 1.00 71.64 N ANISOU 1326 NE2 GLN B 100 12636 8735 5847 -258 347 1379 N ATOM 1327 N LYS B 101 38.253 63.923 39.135 1.00 47.98 N ANISOU 1327 N LYS B 101 8393 6194 3643 -1272 646 600 N ATOM 1328 CA LYS B 101 37.560 64.935 39.928 1.00 47.92 C ANISOU 1328 CA LYS B 101 8392 6323 3493 -1322 715 505 C ATOM 1329 C LYS B 101 38.336 65.216 41.228 1.00 49.67 C ANISOU 1329 C LYS B 101 8877 6588 3406 -1164 549 588 C ATOM 1330 O LYS B 101 38.751 64.287 41.935 1.00 51.35 O ANISOU 1330 O LYS B 101 9387 6702 3422 -1052 562 765 O ATOM 1331 CB LYS B 101 36.124 64.483 40.249 1.00 49.38 C ANISOU 1331 CB LYS B 101 8626 6494 3642 -1520 1084 477 C ATOM 1332 CG LYS B 101 35.340 65.446 41.135 1.00 49.14 C ANISOU 1332 CG LYS B 101 8614 6635 3423 -1516 1197 385 C ATOM 1333 CD LYS B 101 33.926 64.952 41.339 1.00 52.01 C ANISOU 1333 CD LYS B 101 8925 7067 3769 -1733 1587 340 C ATOM 1334 CE LYS B 101 33.202 65.791 42.381 1.00 53.37 C ANISOU 1334 CE LYS B 101 9160 7427 3691 -1671 1729 275 C ATOM 1335 NZ LYS B 101 31.995 65.099 42.830 1.00 56.19 N ANISOU 1335 NZ LYS B 101 9510 7864 3975 -1908 2148 281 N ATOM 1336 N GLY B 102 38.539 66.497 41.523 1.00 49.15 N ANISOU 1336 N GLY B 102 8739 6661 3276 -1138 391 450 N ATOM 1337 CA GLY B 102 39.302 66.891 42.705 1.00 51.50 C ANISOU 1337 CA GLY B 102 9245 7050 3272 -1015 187 458 C ATOM 1338 C GLY B 102 40.782 67.088 42.426 1.00 51.63 C ANISOU 1338 C GLY B 102 9113 7180 3324 -932 -171 437 C ATOM 1339 O GLY B 102 41.498 67.575 43.272 1.00 53.00 O ANISOU 1339 O GLY B 102 9368 7502 3269 -866 -396 373 O ATOM 1340 N ASP B 103 41.251 66.717 41.234 1.00 50.65 N ANISOU 1340 N ASP B 103 8744 7031 3471 -941 -225 468 N ATOM 1341 CA ASP B 103 42.661 66.927 40.897 1.00 51.45 C ANISOU 1341 CA ASP B 103 8627 7308 3616 -879 -533 435 C ATOM 1342 C ASP B 103 42.992 68.424 40.833 1.00 51.28 C ANISOU 1342 C ASP B 103 8459 7383 3644 -1068 -672 218 C ATOM 1343 O ASP B 103 42.172 69.245 40.372 1.00 49.08 O ANISOU 1343 O ASP B 103 8175 6975 3499 -1204 -512 118 O ATOM 1344 CB ASP B 103 43.035 66.245 39.573 1.00 50.09 C ANISOU 1344 CB ASP B 103 8228 7093 3712 -836 -519 509 C ATOM 1345 CG ASP B 103 43.380 64.760 39.740 1.00 52.53 C ANISOU 1345 CG ASP B 103 8715 7334 3909 -583 -504 710 C ATOM 1346 OD1 ASP B 103 43.543 64.288 40.887 1.00 55.45 O ANISOU 1346 OD1 ASP B 103 9370 7726 3973 -408 -546 814 O ATOM 1347 OD2 ASP B 103 43.502 64.066 38.703 1.00 52.76 O ANISOU 1347 OD2 ASP B 103 8643 7271 4133 -528 -444 766 O ATOM 1348 N GLN B 104 44.182 68.762 41.324 1.00 53.38 N ANISOU 1348 N GLN B 104 8625 7881 3774 -1065 -963 135 N ATOM 1349 CA GLN B 104 44.727 70.118 41.189 1.00 54.30 C ANISOU 1349 CA GLN B 104 8603 8072 3957 -1323 -1098 -92 C ATOM 1350 C GLN B 104 45.694 70.225 40.011 1.00 53.41 C ANISOU 1350 C GLN B 104 8116 8073 4106 -1432 -1184 -107 C ATOM 1351 O GLN B 104 46.568 69.370 39.820 1.00 54.18 O ANISOU 1351 O GLN B 104 7997 8394 4193 -1264 -1327 -12 O ATOM 1352 CB GLN B 104 45.413 70.549 42.491 1.00 58.18 C ANISOU 1352 CB GLN B 104 9184 8796 4127 -1341 -1363 -247 C ATOM 1353 CG GLN B 104 44.421 70.971 43.556 1.00 59.02 C ANISOU 1353 CG GLN B 104 9680 8760 3984 -1316 -1247 -309 C ATOM 1354 CD GLN B 104 45.021 71.050 44.935 1.00 63.69 C ANISOU 1354 CD GLN B 104 10412 9610 4179 -1230 -1510 -422 C ATOM 1355 OE1 GLN B 104 44.634 70.297 45.824 1.00 65.26 O ANISOU 1355 OE1 GLN B 104 10867 9838 4090 -967 -1467 -280 O ATOM 1356 NE2 GLN B 104 45.961 71.967 45.127 1.00 66.15 N ANISOU 1356 NE2 GLN B 104 10570 10112 4450 -1466 -1773 -690 N ATOM 1357 N MET B 105 45.518 71.278 39.218 1.00 52.47 N ANISOU 1357 N MET B 105 7949 7794 4191 -1676 -1071 -214 N ATOM 1358 CA MET B 105 46.368 71.550 38.057 1.00 52.03 C ANISOU 1358 CA MET B 105 7576 7819 4374 -1826 -1086 -227 C ATOM 1359 C MET B 105 46.787 73.028 38.004 1.00 53.97 C ANISOU 1359 C MET B 105 7848 7992 4667 -2207 -1095 -441 C ATOM 1360 O MET B 105 46.080 73.896 38.535 1.00 54.11 O ANISOU 1360 O MET B 105 8198 7772 4588 -2302 -1013 -557 O ATOM 1361 CB MET B 105 45.629 71.171 36.761 1.00 48.74 C ANISOU 1361 CB MET B 105 7130 7201 4187 -1710 -847 -81 C ATOM 1362 CG MET B 105 45.349 69.690 36.591 1.00 47.23 C ANISOU 1362 CG MET B 105 6910 7040 3994 -1415 -815 100 C ATOM 1363 SD MET B 105 44.066 69.405 35.340 1.00 47.45 S ANISOU 1363 SD MET B 105 6982 6820 4227 -1332 -531 176 S ATOM 1364 CE MET B 105 42.546 69.624 36.285 1.00 44.78 C ANISOU 1364 CE MET B 105 6959 6317 3737 -1322 -372 129 C ATOM 1365 N VAL B 106 47.939 73.293 37.372 1.00 55.82 N ANISOU 1365 N VAL B 106 7751 8423 5034 -2429 -1170 -498 N ATOM 1366 CA VAL B 106 48.383 74.660 37.012 1.00 58.26 C ANISOU 1366 CA VAL B 106 8094 8595 5446 -2870 -1091 -676 C ATOM 1367 C VAL B 106 47.960 74.925 35.586 1.00 56.08 C ANISOU 1367 C VAL B 106 7862 8046 5401 -2855 -805 -531 C ATOM 1368 O VAL B 106 48.213 74.097 34.719 1.00 54.57 O ANISOU 1368 O VAL B 106 7393 8008 5332 -2670 -773 -370 O ATOM 1369 CB VAL B 106 49.934 74.827 36.954 1.00 61.89 C ANISOU 1369 CB VAL B 106 8101 9470 5944 -3193 -1275 -823 C ATOM 1370 CG1 VAL B 106 50.311 76.293 37.028 1.00 65.24 C ANISOU 1370 CG1 VAL B 106 8676 9707 6406 -3748 -1202 -1075 C ATOM 1371 CG2 VAL B 106 50.635 74.068 38.027 1.00 64.65 C ANISOU 1371 CG2 VAL B 106 8198 10301 6064 -3035 -1616 -900 C ATOM 1372 N VAL B 107 47.361 76.083 35.330 1.00 56.73 N ANISOU 1372 N VAL B 107 8316 7729 5508 -3012 -598 -593 N ATOM 1373 CA VAL B 107 47.049 76.482 33.960 1.00 55.91 C ANISOU 1373 CA VAL B 107 8297 7376 5571 -2979 -327 -459 C ATOM 1374 C VAL B 107 48.275 77.128 33.301 1.00 59.51 C ANISOU 1374 C VAL B 107 8563 7888 6160 -3409 -255 -514 C ATOM 1375 O VAL B 107 48.928 77.974 33.900 1.00 63.16 O ANISOU 1375 O VAL B 107 9095 8322 6582 -3842 -304 -725 O ATOM 1376 CB VAL B 107 45.831 77.434 33.891 1.00 55.63 C ANISOU 1376 CB VAL B 107 8789 6885 5463 -2858 -110 -471 C ATOM 1377 CG1 VAL B 107 45.475 77.736 32.449 1.00 53.59 C ANISOU 1377 CG1 VAL B 107 8622 6422 5319 -2712 148 -309 C ATOM 1378 CG2 VAL B 107 44.632 76.826 34.603 1.00 52.57 C ANISOU 1378 CG2 VAL B 107 8520 6518 4936 -2484 -156 -445 C ATOM 1379 N LEU B 108 48.580 76.709 32.072 1.00 58.95 N ANISOU 1379 N LEU B 108 8248 7915 6236 -3310 -126 -342 N ATOM 1380 CA LEU B 108 49.746 77.197 31.330 1.00 62.82 C ANISOU 1380 CA LEU B 108 8500 8514 6853 -3703 -4 -360 C ATOM 1381 C LEU B 108 49.380 78.131 30.169 1.00 64.10 C ANISOU 1381 C LEU B 108 9033 8242 7081 -3764 362 -238 C ATOM 1382 O LEU B 108 50.210 78.919 29.718 1.00 67.46 O ANISOU 1382 O LEU B 108 9454 8597 7582 -4210 547 -278 O ATOM 1383 CB LEU B 108 50.593 76.023 30.811 1.00 61.75 C ANISOU 1383 CB LEU B 108 7782 8884 6796 -3538 -117 -258 C ATOM 1384 CG LEU B 108 51.211 75.023 31.799 1.00 61.76 C ANISOU 1384 CG LEU B 108 7386 9377 6702 -3412 -467 -343 C ATOM 1385 CD1 LEU B 108 51.851 73.877 31.039 1.00 59.90 C ANISOU 1385 CD1 LEU B 108 6694 9536 6528 -3113 -506 -198 C ATOM 1386 CD2 LEU B 108 52.238 75.687 32.719 1.00 66.85 C ANISOU 1386 CD2 LEU B 108 7824 10289 7285 -3902 -640 -615 C ATOM 1387 N GLU B 109 48.137 78.027 29.697 1.00 62.11 N ANISOU 1387 N GLU B 109 9096 7725 6776 -3312 473 -94 N ATOM 1388 CA GLU B 109 47.667 78.747 28.509 1.00 63.73 C ANISOU 1388 CA GLU B 109 9661 7572 6982 -3190 795 61 C ATOM 1389 C GLU B 109 46.141 78.746 28.498 1.00 61.31 C ANISOU 1389 C GLU B 109 9706 7042 6546 -2680 822 116 C ATOM 1390 O GLU B 109 45.516 77.718 28.728 1.00 57.71 O ANISOU 1390 O GLU B 109 9028 6824 6076 -2347 650 132 O ATOM 1391 CB GLU B 109 48.207 78.067 27.240 1.00 62.95 C ANISOU 1391 CB GLU B 109 9202 7733 6984 -3063 892 239 C ATOM 1392 CG GLU B 109 48.114 78.860 25.937 1.00 65.99 C ANISOU 1392 CG GLU B 109 9915 7811 7348 -3022 1251 411 C ATOM 1393 CD GLU B 109 48.461 78.003 24.706 1.00 66.44 C ANISOU 1393 CD GLU B 109 9613 8172 7457 -2771 1315 582 C ATOM 1394 OE1 GLU B 109 47.636 77.139 24.298 1.00 61.77 O ANISOU 1394 OE1 GLU B 109 8946 7704 6821 -2270 1210 648 O ATOM 1395 OE2 GLU B 109 49.565 78.199 24.148 1.00 70.05 O ANISOU 1395 OE2 GLU B 109 9861 8761 7993 -3097 1481 630 O ATOM 1396 N GLU B 110 45.564 79.916 28.242 1.00 64.25 N ANISOU 1396 N GLU B 110 10639 6963 6812 -2627 1054 135 N ATOM 1397 CA GLU B 110 44.119 80.097 28.143 1.00 63.51 C ANISOU 1397 CA GLU B 110 10876 6697 6557 -2098 1107 175 C ATOM 1398 C GLU B 110 43.703 80.673 26.783 1.00 65.02 C ANISOU 1398 C GLU B 110 11388 6654 6662 -1778 1383 361 C ATOM 1399 O GLU B 110 43.054 81.727 26.731 1.00 67.29 O ANISOU 1399 O GLU B 110 12248 6541 6778 -1581 1567 375 O ATOM 1400 CB GLU B 110 43.632 81.048 29.241 1.00 66.01 C ANISOU 1400 CB GLU B 110 11670 6681 6731 -2166 1119 12 C ATOM 1401 CG GLU B 110 43.702 80.500 30.650 1.00 66.49 C ANISOU 1401 CG GLU B 110 11502 6976 6786 -2324 846 -169 C ATOM 1402 CD GLU B 110 42.864 81.307 31.645 1.00 70.18 C ANISOU 1402 CD GLU B 110 12454 7159 7054 -2201 868 -319 C ATOM 1403 OE1 GLU B 110 42.840 80.928 32.835 1.00 69.86 O ANISOU 1403 OE1 GLU B 110 12291 7293 6958 -2291 666 -464 O ATOM 1404 OE2 GLU B 110 42.221 82.305 31.244 1.00 72.22 O ANISOU 1404 OE2 GLU B 110 13239 7024 7178 -1964 1094 -286 O ATOM 1405 N SER B 111 44.086 80.001 25.692 1.00 64.04 N ANISOU 1405 N SER B 111 10941 6774 6619 -1680 1417 506 N ATOM 1406 CA SER B 111 43.633 80.387 24.349 1.00 65.52 C ANISOU 1406 CA SER B 111 11397 6821 6675 -1284 1649 691 C ATOM 1407 C SER B 111 42.277 79.739 24.059 1.00 62.53 C ANISOU 1407 C SER B 111 10899 6689 6170 -662 1514 680 C ATOM 1408 O SER B 111 42.198 78.540 23.731 1.00 60.64 O ANISOU 1408 O SER B 111 10181 6846 6015 -533 1346 669 O ATOM 1409 CB SER B 111 44.646 79.982 23.271 1.00 65.99 C ANISOU 1409 CB SER B 111 11176 7058 6841 -1440 1763 837 C ATOM 1410 OG SER B 111 45.791 80.812 23.298 1.00 71.19 O ANISOU 1410 OG SER B 111 12003 7469 7576 -2004 1983 861 O ATOM 1411 N GLY B 112 41.214 80.530 24.179 1.00 63.10 N ANISOU 1411 N GLY B 112 11406 6541 6029 -279 1595 663 N ATOM 1412 CA GLY B 112 39.864 80.010 24.040 1.00 60.20 C ANISOU 1412 CA GLY B 112 10871 6477 5524 279 1464 598 C ATOM 1413 C GLY B 112 39.485 79.170 25.243 1.00 56.92 C ANISOU 1413 C GLY B 112 10086 6328 5213 137 1225 416 C ATOM 1414 O GLY B 112 39.961 79.409 26.356 1.00 57.45 O ANISOU 1414 O GLY B 112 10237 6239 5353 -240 1181 332 O ATOM 1415 N GLU B 113 38.635 78.176 25.016 1.00 53.58 N ANISOU 1415 N GLU B 113 9268 6309 4780 419 1082 344 N ATOM 1416 CA GLU B 113 38.075 77.397 26.107 1.00 50.96 C ANISOU 1416 CA GLU B 113 8648 6210 4504 328 918 188 C ATOM 1417 C GLU B 113 38.713 76.043 26.329 1.00 47.12 C ANISOU 1417 C GLU B 113 7722 5949 4232 8 759 171 C ATOM 1418 O GLU B 113 38.333 75.331 27.260 1.00 46.73 O ANISOU 1418 O GLU B 113 7486 6049 4220 -98 654 71 O ATOM 1419 CB GLU B 113 36.565 77.258 25.954 1.00 51.30 C ANISOU 1419 CB GLU B 113 8573 6546 4374 801 900 76 C ATOM 1420 CG GLU B 113 35.816 78.515 26.314 1.00 57.15 C ANISOU 1420 CG GLU B 113 9747 7094 4872 1142 1026 48 C ATOM 1421 CD GLU B 113 34.443 78.536 25.694 1.00 62.64 C ANISOU 1421 CD GLU B 113 10304 8152 5345 1739 1025 -36 C ATOM 1422 OE1 GLU B 113 33.452 78.579 26.448 1.00 63.89 O ANISOU 1422 OE1 GLU B 113 10370 8518 5388 1924 1013 -181 O ATOM 1423 OE2 GLU B 113 34.355 78.486 24.445 1.00 65.28 O ANISOU 1423 OE2 GLU B 113 10588 8618 5599 2035 1033 30 O ATOM 1424 N TRP B 114 39.657 75.669 25.482 1.00 44.76 N ANISOU 1424 N TRP B 114 7289 5672 4046 -109 764 275 N ATOM 1425 CA TRP B 114 40.499 74.519 25.768 1.00 41.74 C ANISOU 1425 CA TRP B 114 6572 5445 3843 -390 627 276 C ATOM 1426 C TRP B 114 41.858 75.000 26.242 1.00 42.76 C ANISOU 1426 C TRP B 114 6769 5417 4061 -780 636 331 C ATOM 1427 O TRP B 114 42.626 75.588 25.468 1.00 44.23 O ANISOU 1427 O TRP B 114 7044 5495 4268 -868 767 432 O ATOM 1428 CB TRP B 114 40.637 73.614 24.546 1.00 40.24 C ANISOU 1428 CB TRP B 114 6125 5462 3702 -228 608 317 C ATOM 1429 CG TRP B 114 39.406 72.805 24.294 1.00 38.54 C ANISOU 1429 CG TRP B 114 5730 5480 3435 24 540 189 C ATOM 1430 CD1 TRP B 114 38.241 73.234 23.705 1.00 37.37 C ANISOU 1430 CD1 TRP B 114 5633 5445 3119 381 586 117 C ATOM 1431 CD2 TRP B 114 39.199 71.434 24.644 1.00 33.53 C ANISOU 1431 CD2 TRP B 114 4835 5009 2897 -78 424 95 C ATOM 1432 NE1 TRP B 114 37.330 72.218 23.678 1.00 35.88 N ANISOU 1432 NE1 TRP B 114 5163 5531 2938 445 495 -48 N ATOM 1433 CE2 TRP B 114 37.896 71.091 24.221 1.00 33.73 C ANISOU 1433 CE2 TRP B 114 4733 5248 2835 142 416 -58 C ATOM 1434 CE3 TRP B 114 39.998 70.460 25.248 1.00 31.78 C ANISOU 1434 CE3 TRP B 114 4498 4775 2803 -314 336 123 C ATOM 1435 CZ2 TRP B 114 37.364 69.807 24.381 1.00 32.59 C ANISOU 1435 CZ2 TRP B 114 4368 5257 2757 39 353 -197 C ATOM 1436 CZ3 TRP B 114 39.475 69.167 25.413 1.00 33.73 C ANISOU 1436 CZ3 TRP B 114 4600 5123 3094 -341 280 23 C ATOM 1437 CH2 TRP B 114 38.159 68.855 24.984 1.00 32.72 C ANISOU 1437 CH2 TRP B 114 4367 5159 2906 -213 304 -142 C ATOM 1438 N TRP B 115 42.148 74.748 27.516 1.00 42.20 N ANISOU 1438 N TRP B 115 6644 5367 4023 -1022 504 254 N ATOM 1439 CA TRP B 115 43.328 75.318 28.173 1.00 44.04 C ANISOU 1439 CA TRP B 115 6923 5508 4302 -1413 474 235 C ATOM 1440 C TRP B 115 44.472 74.323 28.224 1.00 43.92 C ANISOU 1440 C TRP B 115 6518 5766 4405 -1572 329 264 C ATOM 1441 O TRP B 115 44.251 73.116 28.229 1.00 42.76 O ANISOU 1441 O TRP B 115 6156 5807 4283 -1395 222 281 O ATOM 1442 CB TRP B 115 42.984 75.763 29.601 1.00 44.16 C ANISOU 1442 CB TRP B 115 7147 5414 4218 -1538 396 105 C ATOM 1443 CG TRP B 115 42.003 76.908 29.690 1.00 44.48 C ANISOU 1443 CG TRP B 115 7622 5168 4112 -1371 548 58 C ATOM 1444 CD1 TRP B 115 41.570 77.711 28.662 1.00 44.51 C ANISOU 1444 CD1 TRP B 115 7891 4970 4050 -1145 747 135 C ATOM 1445 CD2 TRP B 115 41.365 77.399 30.877 1.00 43.92 C ANISOU 1445 CD2 TRP B 115 7810 4980 3897 -1358 523 -69 C ATOM 1446 NE1 TRP B 115 40.682 78.646 29.136 1.00 45.21 N ANISOU 1446 NE1 TRP B 115 8389 4826 3964 -953 841 63 N ATOM 1447 CE2 TRP B 115 40.542 78.483 30.492 1.00 45.11 C ANISOU 1447 CE2 TRP B 115 8369 4862 3907 -1092 712 -71 C ATOM 1448 CE3 TRP B 115 41.379 77.002 32.230 1.00 44.58 C ANISOU 1448 CE3 TRP B 115 7843 5174 3922 -1488 368 -175 C ATOM 1449 CZ2 TRP B 115 39.755 79.207 31.420 1.00 46.26 C ANISOU 1449 CZ2 TRP B 115 8865 4845 3868 -958 753 -192 C ATOM 1450 CZ3 TRP B 115 40.593 77.720 33.154 1.00 46.12 C ANISOU 1450 CZ3 TRP B 115 8378 5213 3931 -1389 414 -294 C ATOM 1451 CH2 TRP B 115 39.796 78.814 32.737 1.00 46.72 C ANISOU 1451 CH2 TRP B 115 8845 5022 3884 -1126 607 -308 C ATOM 1452 N LYS B 116 45.696 74.811 28.277 1.00 46.34 N ANISOU 1452 N LYS B 116 6735 6103 4768 -1904 335 256 N ATOM 1453 CA LYS B 116 46.809 73.903 28.507 1.00 47.50 C ANISOU 1453 CA LYS B 116 6474 6589 4984 -2003 167 256 C ATOM 1454 C LYS B 116 47.100 73.866 30.009 1.00 48.27 C ANISOU 1454 C LYS B 116 6555 6780 5005 -2184 -47 124 C ATOM 1455 O LYS B 116 47.158 74.907 30.663 1.00 50.27 O ANISOU 1455 O LYS B 116 7031 6865 5204 -2460 -31 5 O ATOM 1456 CB LYS B 116 48.052 74.302 27.691 1.00 49.80 C ANISOU 1456 CB LYS B 116 6548 7007 5367 -2249 283 301 C ATOM 1457 CG LYS B 116 49.114 73.210 27.601 1.00 52.43 C ANISOU 1457 CG LYS B 116 6399 7772 5751 -2189 135 325 C ATOM 1458 CD LYS B 116 50.068 73.485 26.421 1.00 60.26 C ANISOU 1458 CD LYS B 116 7162 8910 6824 -2317 331 407 C ATOM 1459 CE LYS B 116 51.392 72.726 26.530 1.00 65.11 C ANISOU 1459 CE LYS B 116 7241 10031 7466 -2343 189 381 C ATOM 1460 NZ LYS B 116 52.349 73.147 25.433 1.00 70.88 N ANISOU 1460 NZ LYS B 116 7724 10939 8269 -2538 432 447 N ATOM 1461 N ALA B 117 47.269 72.664 30.544 1.00 47.25 N ANISOU 1461 N ALA B 117 6215 6896 4842 -2003 -237 142 N ATOM 1462 CA ALA B 117 47.449 72.498 31.974 1.00 48.81 C ANISOU 1462 CA ALA B 117 6432 7205 4907 -2074 -447 41 C ATOM 1463 C ALA B 117 48.515 71.460 32.312 1.00 50.58 C ANISOU 1463 C ALA B 117 6303 7824 5093 -1965 -661 64 C ATOM 1464 O ALA B 117 48.895 70.634 31.457 1.00 49.38 O ANISOU 1464 O ALA B 117 5928 7818 5017 -1756 -636 175 O ATOM 1465 CB ALA B 117 46.127 72.146 32.625 1.00 46.17 C ANISOU 1465 CB ALA B 117 6388 6686 4471 -1863 -429 51 C ATOM 1466 N ARG B 118 49.006 71.543 33.557 1.00 53.43 N ANISOU 1466 N ARG B 118 6632 8369 5299 -2068 -877 -52 N ATOM 1467 CA ARG B 118 49.921 70.571 34.141 1.00 55.76 C ANISOU 1467 CA ARG B 118 6649 9069 5468 -1867 -1122 -39 C ATOM 1468 C ARG B 118 49.370 70.048 35.465 1.00 56.07 C ANISOU 1468 C ARG B 118 6960 9070 5276 -1669 -1262 -35 C ATOM 1469 O ARG B 118 48.987 70.824 36.335 1.00 56.69 O ANISOU 1469 O ARG B 118 7263 9033 5243 -1861 -1296 -165 O ATOM 1470 CB ARG B 118 51.294 71.205 34.355 1.00 60.61 C ANISOU 1470 CB ARG B 118 6871 10091 6065 -2178 -1280 -213 C ATOM 1471 CG ARG B 118 52.289 70.374 35.181 1.00 64.31 C ANISOU 1471 CG ARG B 118 7023 11085 6325 -1935 -1596 -252 C ATOM 1472 CD ARG B 118 53.705 70.802 34.877 1.00 70.78 C ANISOU 1472 CD ARG B 118 7280 12421 7193 -2204 -1697 -407 C ATOM 1473 NE ARG B 118 53.995 72.135 35.379 1.00 75.68 N ANISOU 1473 NE ARG B 118 7887 13051 7818 -2787 -1730 -674 N ATOM 1474 CZ ARG B 118 54.682 73.062 34.713 1.00 80.17 C ANISOU 1474 CZ ARG B 118 8195 13708 8558 -3292 -1589 -805 C ATOM 1475 NH1 ARG B 118 55.133 72.818 33.485 1.00 80.29 N ANISOU 1475 NH1 ARG B 118 7917 13839 8748 -3256 -1397 -672 N ATOM 1476 NH2 ARG B 118 54.905 74.250 35.273 1.00 82.67 N ANISOU 1476 NH2 ARG B 118 8585 13967 8859 -3857 -1613 -1074 N ATOM 1477 N SER B 119 49.345 68.728 35.617 1.00 56.49 N ANISOU 1477 N SER B 119 7037 9196 5233 -1273 -1320 117 N ATOM 1478 CA SER B 119 48.961 68.110 36.895 1.00 58.17 C ANISOU 1478 CA SER B 119 7532 9389 5181 -1053 -1429 161 C ATOM 1479 C SER B 119 49.962 68.422 38.004 1.00 62.69 C ANISOU 1479 C SER B 119 7942 10370 5506 -1082 -1736 14 C ATOM 1480 O SER B 119 51.171 68.191 37.860 1.00 65.45 O ANISOU 1480 O SER B 119 7895 11156 5817 -990 -1928 -28 O ATOM 1481 CB SER B 119 48.815 66.593 36.753 1.00 57.43 C ANISOU 1481 CB SER B 119 7568 9230 5023 -624 -1389 371 C ATOM 1482 OG SER B 119 48.786 65.976 38.032 1.00 61.13 O ANISOU 1482 OG SER B 119 8296 9750 5180 -378 -1513 435 O ATOM 1483 N LEU B 120 49.449 68.932 39.119 1.00 64.37 N ANISOU 1483 N LEU B 120 8441 10490 5527 -1186 -1787 -83 N ATOM 1484 CA LEU B 120 50.283 69.188 40.296 1.00 69.36 C ANISOU 1484 CA LEU B 120 8970 11522 5862 -1185 -2104 -252 C ATOM 1485 C LEU B 120 50.903 67.921 40.858 1.00 72.23 C ANISOU 1485 C LEU B 120 9291 12208 5945 -667 -2309 -107 C ATOM 1486 O LEU B 120 52.028 67.945 41.361 1.00 76.73 O ANISOU 1486 O LEU B 120 9536 13306 6313 -578 -2622 -243 O ATOM 1487 CB LEU B 120 49.492 69.906 41.384 1.00 69.92 C ANISOU 1487 CB LEU B 120 9434 11390 5743 -1336 -2092 -376 C ATOM 1488 CG LEU B 120 49.255 71.400 41.142 1.00 70.23 C ANISOU 1488 CG LEU B 120 9518 11220 5948 -1836 -1994 -609 C ATOM 1489 CD1 LEU B 120 48.817 72.075 42.436 1.00 72.17 C ANISOU 1489 CD1 LEU B 120 10113 11400 5909 -1925 -2076 -790 C ATOM 1490 CD2 LEU B 120 50.519 72.057 40.625 1.00 72.86 C ANISOU 1490 CD2 LEU B 120 9391 11875 6417 -2185 -2139 -809 C ATOM 1491 N ALA B 121 50.177 66.815 40.737 1.00 70.83 N ANISOU 1491 N ALA B 121 9446 11721 5743 -323 -2123 158 N ATOM 1492 CA ALA B 121 50.606 65.523 41.276 1.00 73.95 C ANISOU 1492 CA ALA B 121 9979 12279 5840 234 -2247 350 C ATOM 1493 C ALA B 121 51.620 64.754 40.405 1.00 75.38 C ANISOU 1493 C ALA B 121 9805 12743 6095 552 -2334 433 C ATOM 1494 O ALA B 121 52.519 64.109 40.946 1.00 79.36 O ANISOU 1494 O ALA B 121 10209 13650 6293 1004 -2584 474 O ATOM 1495 CB ALA B 121 49.384 64.647 41.587 1.00 72.50 C ANISOU 1495 CB ALA B 121 10383 11585 5578 417 -1963 592 C ATOM 1496 N THR B 122 51.482 64.816 39.077 1.00 72.26 N ANISOU 1496 N THR B 122 9227 12169 6061 375 -2133 455 N ATOM 1497 CA THR B 122 52.352 64.024 38.189 1.00 73.70 C ANISOU 1497 CA THR B 122 9117 12583 6301 717 -2169 543 C ATOM 1498 C THR B 122 53.315 64.835 37.323 1.00 74.35 C ANISOU 1498 C THR B 122 8567 13081 6600 433 -2242 363 C ATOM 1499 O THR B 122 54.284 64.285 36.789 1.00 76.62 O ANISOU 1499 O THR B 122 8501 13748 6864 747 -2331 392 O ATOM 1500 CB THR B 122 51.545 63.120 37.241 1.00 70.43 C ANISOU 1500 CB THR B 122 9023 11659 6077 858 -1864 738 C ATOM 1501 OG1 THR B 122 50.887 63.929 36.259 1.00 68.21 O ANISOU 1501 OG1 THR B 122 8643 11130 6146 399 -1649 653 O ATOM 1502 CG2 THR B 122 50.509 62.297 38.003 1.00 69.79 C ANISOU 1502 CG2 THR B 122 9582 11114 5820 1032 -1711 912 C ATOM 1503 N ARG B 123 53.035 66.130 37.179 1.00 72.80 N ANISOU 1503 N ARG B 123 8263 12798 6599 -146 -2171 183 N ATOM 1504 CA ARG B 123 53.767 67.018 36.258 1.00 73.28 C ANISOU 1504 CA ARG B 123 7826 13113 6902 -536 -2132 31 C ATOM 1505 C ARG B 123 53.445 66.762 34.769 1.00 69.96 C ANISOU 1505 C ARG B 123 7395 12417 6768 -520 -1841 168 C ATOM 1506 O ARG B 123 53.986 67.434 33.887 1.00 70.25 O ANISOU 1506 O ARG B 123 7079 12613 6999 -815 -1744 89 O ATOM 1507 CB ARG B 123 55.280 66.996 36.529 1.00 78.90 C ANISOU 1507 CB ARG B 123 7935 14588 7456 -437 -2426 -120 C ATOM 1508 N LYS B 124 52.550 65.807 34.501 1.00 66.94 N ANISOU 1508 N LYS B 124 7418 11619 6396 -204 -1690 360 N ATOM 1509 CA LYS B 124 52.043 65.559 33.147 1.00 63.85 C ANISOU 1509 CA LYS B 124 7088 10929 6244 -192 -1428 456 C ATOM 1510 C LYS B 124 51.270 66.768 32.623 1.00 60.16 C ANISOU 1510 C LYS B 124 6706 10161 5990 -667 -1228 377 C ATOM 1511 O LYS B 124 50.573 67.440 33.388 1.00 59.60 O ANISOU 1511 O LYS B 124 6883 9885 5878 -902 -1227 306 O ATOM 1512 CB LYS B 124 51.174 64.300 33.103 1.00 62.71 C ANISOU 1512 CB LYS B 124 7389 10391 6046 168 -1316 622 C ATOM 1513 CG LYS B 124 51.951 62.991 32.834 1.00 68.07 C ANISOU 1513 CG LYS B 124 8023 11245 6594 716 -1386 741 C ATOM 1514 CD LYS B 124 51.045 61.758 33.049 1.00 71.82 C ANISOU 1514 CD LYS B 124 9070 11238 6979 1000 -1259 888 C ATOM 1515 CE LYS B 124 51.241 60.673 31.963 1.00 74.21 C ANISOU 1515 CE LYS B 124 9448 11417 7331 1363 -1143 969 C ATOM 1516 NZ LYS B 124 52.325 59.693 32.299 1.00 79.32 N ANISOU 1516 NZ LYS B 124 10085 12338 7716 1965 -1303 1069 N ATOM 1517 N GLU B 125 51.430 67.049 31.330 1.00 57.82 N ANISOU 1517 N GLU B 125 6228 9855 5886 -757 -1054 395 N ATOM 1518 CA GLU B 125 50.894 68.252 30.700 1.00 55.40 C ANISOU 1518 CA GLU B 125 6001 9304 5744 -1141 -854 341 C ATOM 1519 C GLU B 125 49.945 67.926 29.541 1.00 51.67 C ANISOU 1519 C GLU B 125 5731 8510 5391 -993 -633 437 C ATOM 1520 O GLU B 125 50.097 66.905 28.868 1.00 51.36 O ANISOU 1520 O GLU B 125 5633 8523 5360 -675 -610 519 O ATOM 1521 CB GLU B 125 52.036 69.135 30.186 1.00 58.35 C ANISOU 1521 CB GLU B 125 5975 9991 6203 -1455 -818 260 C ATOM 1522 CG GLU B 125 52.588 70.102 31.235 1.00 62.66 C ANISOU 1522 CG GLU B 125 6411 10717 6679 -1858 -967 73 C ATOM 1523 CD GLU B 125 53.894 70.774 30.836 1.00 66.97 C ANISOU 1523 CD GLU B 125 6472 11677 7296 -2213 -946 -42 C ATOM 1524 OE1 GLU B 125 53.978 71.313 29.714 1.00 68.02 O ANISOU 1524 OE1 GLU B 125 6567 11695 7583 -2406 -680 12 O ATOM 1525 OE2 GLU B 125 54.836 70.774 31.662 1.00 71.12 O ANISOU 1525 OE2 GLU B 125 6648 12673 7702 -2307 -1190 -197 O ATOM 1526 N GLY B 126 48.969 68.795 29.313 1.00 48.66 N ANISOU 1526 N GLY B 126 5597 7818 5074 -1190 -481 408 N ATOM 1527 CA GLY B 126 48.121 68.663 28.162 1.00 45.38 C ANISOU 1527 CA GLY B 126 5313 7189 4740 -1056 -296 461 C ATOM 1528 C GLY B 126 46.955 69.610 28.177 1.00 43.71 C ANISOU 1528 C GLY B 126 5390 6684 4533 -1189 -171 415 C ATOM 1529 O GLY B 126 46.843 70.470 29.062 1.00 44.62 O ANISOU 1529 O GLY B 126 5640 6715 4599 -1411 -202 344 O ATOM 1530 N TYR B 127 46.077 69.416 27.195 1.00 41.17 N ANISOU 1530 N TYR B 127 5165 6234 4243 -1012 -41 438 N ATOM 1531 CA TYR B 127 44.873 70.203 27.014 1.00 39.32 C ANISOU 1531 CA TYR B 127 5170 5790 3978 -1009 79 395 C ATOM 1532 C TYR B 127 43.687 69.707 27.837 1.00 37.61 C ANISOU 1532 C TYR B 127 5099 5488 3701 -944 39 325 C ATOM 1533 O TYR B 127 43.474 68.494 28.027 1.00 36.61 O ANISOU 1533 O TYR B 127 4933 5399 3578 -843 -16 324 O ATOM 1534 CB TYR B 127 44.521 70.271 25.524 1.00 39.13 C ANISOU 1534 CB TYR B 127 5137 5760 3969 -811 218 432 C ATOM 1535 CG TYR B 127 45.501 71.117 24.737 1.00 43.34 C ANISOU 1535 CG TYR B 127 5620 6319 4530 -919 346 518 C ATOM 1536 CD1 TYR B 127 46.478 70.527 23.934 1.00 47.18 C ANISOU 1536 CD1 TYR B 127 5858 7006 5061 -847 365 587 C ATOM 1537 CD2 TYR B 127 45.479 72.514 24.833 1.00 46.34 C ANISOU 1537 CD2 TYR B 127 6228 6503 4875 -1108 476 530 C ATOM 1538 CE1 TYR B 127 47.393 71.308 23.212 1.00 50.29 C ANISOU 1538 CE1 TYR B 127 6183 7452 5474 -992 532 672 C ATOM 1539 CE2 TYR B 127 46.380 73.298 24.127 1.00 50.44 C ANISOU 1539 CE2 TYR B 127 6746 7002 5418 -1279 649 615 C ATOM 1540 CZ TYR B 127 47.329 72.690 23.317 1.00 53.38 C ANISOU 1540 CZ TYR B 127 6819 7619 5843 -1238 685 689 C ATOM 1541 OH TYR B 127 48.220 73.472 22.618 1.00 59.27 O ANISOU 1541 OH TYR B 127 7544 8369 6606 -1449 904 779 O ATOM 1542 N ILE B 128 42.912 70.661 28.333 1.00 37.20 N ANISOU 1542 N ILE B 128 5247 5307 3582 -1005 98 266 N ATOM 1543 CA ILE B 128 41.777 70.348 29.193 1.00 36.26 C ANISOU 1543 CA ILE B 128 5240 5151 3386 -969 98 193 C ATOM 1544 C ILE B 128 40.580 71.193 28.793 1.00 36.37 C ANISOU 1544 C ILE B 128 5380 5108 3332 -830 226 124 C ATOM 1545 O ILE B 128 40.751 72.316 28.287 1.00 37.86 O ANISOU 1545 O ILE B 128 5701 5191 3492 -801 303 146 O ATOM 1546 CB ILE B 128 42.117 70.529 30.718 1.00 36.93 C ANISOU 1546 CB ILE B 128 5442 5208 3382 -1138 0 172 C ATOM 1547 CG1 ILE B 128 42.441 71.982 31.071 1.00 36.98 C ANISOU 1547 CG1 ILE B 128 5619 5097 3335 -1295 17 121 C ATOM 1548 CG2 ILE B 128 43.256 69.599 31.141 1.00 37.07 C ANISOU 1548 CG2 ILE B 128 5322 5352 3410 -1173 -153 239 C ATOM 1549 CD1 ILE B 128 42.135 72.326 32.517 1.00 36.67 C ANISOU 1549 CD1 ILE B 128 5776 5007 3148 -1386 -36 39 C ATOM 1550 N PRO B 129 39.368 70.655 28.979 1.00 36.00 N ANISOU 1550 N PRO B 129 5295 5143 3241 -733 267 38 N ATOM 1551 CA PRO B 129 38.158 71.452 28.757 1.00 36.54 C ANISOU 1551 CA PRO B 129 5432 5251 3199 -540 370 -53 C ATOM 1552 C PRO B 129 37.915 72.320 29.983 1.00 38.14 C ANISOU 1552 C PRO B 129 5866 5342 3282 -597 398 -87 C ATOM 1553 O PRO B 129 37.770 71.783 31.070 1.00 37.98 O ANISOU 1553 O PRO B 129 5852 5348 3232 -731 374 -109 O ATOM 1554 CB PRO B 129 37.056 70.402 28.612 1.00 35.99 C ANISOU 1554 CB PRO B 129 5149 5388 3135 -493 398 -169 C ATOM 1555 CG PRO B 129 37.579 69.192 29.354 1.00 36.40 C ANISOU 1555 CG PRO B 129 5181 5383 3265 -724 348 -121 C ATOM 1556 CD PRO B 129 39.080 69.232 29.249 1.00 35.42 C ANISOU 1556 CD PRO B 129 5103 5143 3210 -787 243 15 C ATOM 1557 N SER B 130 37.871 73.643 29.803 1.00 39.58 N ANISOU 1557 N SER B 130 6291 5376 3374 -479 467 -87 N ATOM 1558 CA SER B 130 37.863 74.578 30.923 1.00 41.12 C ANISOU 1558 CA SER B 130 6782 5395 3446 -551 490 -134 C ATOM 1559 C SER B 130 36.563 74.562 31.729 1.00 42.61 C ANISOU 1559 C SER B 130 6984 5721 3484 -387 560 -245 C ATOM 1560 O SER B 130 36.544 74.975 32.895 1.00 43.32 O ANISOU 1560 O SER B 130 7280 5719 3461 -470 562 -296 O ATOM 1561 CB SER B 130 38.187 76.002 30.467 1.00 42.76 C ANISOU 1561 CB SER B 130 7338 5323 3587 -483 584 -109 C ATOM 1562 OG SER B 130 37.172 76.528 29.639 1.00 43.27 O ANISOU 1562 OG SER B 130 7486 5425 3529 -74 703 -119 O ATOM 1563 N ASN B 131 35.478 74.069 31.141 1.00 42.66 N ANISOU 1563 N ASN B 131 6745 5992 3473 -168 619 -305 N ATOM 1564 CA ASN B 131 34.255 73.929 31.944 1.00 44.38 C ANISOU 1564 CA ASN B 131 6881 6426 3556 -65 711 -425 C ATOM 1565 C ASN B 131 34.292 72.716 32.914 1.00 44.28 C ANISOU 1565 C ASN B 131 6732 6493 3599 -372 703 -418 C ATOM 1566 O ASN B 131 33.385 72.543 33.721 1.00 46.20 O ANISOU 1566 O ASN B 131 6926 6902 3727 -360 815 -497 O ATOM 1567 CB ASN B 131 32.995 73.936 31.061 1.00 44.97 C ANISOU 1567 CB ASN B 131 6694 6837 3554 272 783 -540 C ATOM 1568 CG ASN B 131 32.989 72.814 30.036 1.00 43.25 C ANISOU 1568 CG ASN B 131 6126 6815 3492 182 722 -560 C ATOM 1569 OD1 ASN B 131 34.008 72.159 29.809 1.00 40.36 O ANISOU 1569 OD1 ASN B 131 5766 6281 3290 -62 638 -457 O ATOM 1570 ND2 ASN B 131 31.838 72.591 29.407 1.00 42.14 N ANISOU 1570 ND2 ASN B 131 5668 7061 3281 396 758 -719 N ATOM 1571 N TYR B 132 35.351 71.904 32.859 1.00 43.38 N ANISOU 1571 N TYR B 132 6590 6262 3632 -613 592 -311 N ATOM 1572 CA TYR B 132 35.516 70.770 33.802 1.00 43.76 C ANISOU 1572 CA TYR B 132 6624 6314 3687 -845 592 -263 C ATOM 1573 C TYR B 132 36.243 71.167 35.086 1.00 45.84 C ANISOU 1573 C TYR B 132 7162 6428 3825 -946 518 -213 C ATOM 1574 O TYR B 132 36.598 70.324 35.911 1.00 46.93 O ANISOU 1574 O TYR B 132 7362 6547 3921 -1079 490 -139 O ATOM 1575 CB TYR B 132 36.232 69.603 33.119 1.00 41.42 C ANISOU 1575 CB TYR B 132 6193 5984 3562 -963 512 -180 C ATOM 1576 CG TYR B 132 35.280 68.726 32.331 1.00 40.26 C ANISOU 1576 CG TYR B 132 5796 6006 3494 -972 613 -276 C ATOM 1577 CD1 TYR B 132 34.434 69.277 31.349 1.00 37.05 C ANISOU 1577 CD1 TYR B 132 5195 5803 3079 -775 651 -407 C ATOM 1578 CD2 TYR B 132 35.218 67.355 32.564 1.00 37.20 C ANISOU 1578 CD2 TYR B 132 5393 5578 3165 -1170 673 -253 C ATOM 1579 CE1 TYR B 132 33.555 68.486 30.634 1.00 38.01 C ANISOU 1579 CE1 TYR B 132 5038 6149 3254 -810 714 -552 C ATOM 1580 CE2 TYR B 132 34.322 66.552 31.869 1.00 37.56 C ANISOU 1580 CE2 TYR B 132 5219 5768 3284 -1261 776 -393 C ATOM 1581 CZ TYR B 132 33.496 67.122 30.906 1.00 38.46 C ANISOU 1581 CZ TYR B 132 5067 6150 3396 -1098 780 -562 C ATOM 1582 OH TYR B 132 32.624 66.329 30.207 1.00 38.09 O ANISOU 1582 OH TYR B 132 4754 6310 3407 -1214 850 -752 O ATOM 1583 N VAL B 133 36.426 72.465 35.271 1.00 47.58 N ANISOU 1583 N VAL B 133 7587 6537 3954 -864 492 -265 N ATOM 1584 CA VAL B 133 37.425 72.962 36.185 1.00 49.08 C ANISOU 1584 CA VAL B 133 8011 6580 4055 -1005 360 -259 C ATOM 1585 C VAL B 133 36.984 74.307 36.787 1.00 51.27 C ANISOU 1585 C VAL B 133 8595 6739 4146 -899 425 -383 C ATOM 1586 O VAL B 133 36.177 75.040 36.192 1.00 51.79 O ANISOU 1586 O VAL B 133 8711 6787 4181 -669 552 -439 O ATOM 1587 CB VAL B 133 38.789 72.992 35.410 1.00 49.12 C ANISOU 1587 CB VAL B 133 7929 6505 4228 -1142 205 -192 C ATOM 1588 CG1 VAL B 133 39.515 74.330 35.478 1.00 49.93 C ANISOU 1588 CG1 VAL B 133 8258 6417 4296 -1254 153 -265 C ATOM 1589 CG2 VAL B 133 39.659 71.783 35.776 1.00 48.92 C ANISOU 1589 CG2 VAL B 133 7768 6577 4243 -1256 64 -93 C ATOM 1590 N ALA B 134 37.478 74.599 37.985 1.00 53.06 N ANISOU 1590 N ALA B 134 9048 6899 4213 -1020 335 -435 N ATOM 1591 CA ALA B 134 37.156 75.841 38.691 1.00 55.82 C ANISOU 1591 CA ALA B 134 9758 7096 4355 -937 387 -580 C ATOM 1592 C ALA B 134 38.438 76.444 39.220 1.00 57.75 C ANISOU 1592 C ALA B 134 10204 7177 4560 -1206 193 -663 C ATOM 1593 O ALA B 134 39.233 75.749 39.860 1.00 57.47 O ANISOU 1593 O ALA B 134 10064 7276 4496 -1374 18 -635 O ATOM 1594 CB ALA B 134 36.190 75.574 39.849 1.00 56.68 C ANISOU 1594 CB ALA B 134 9953 7358 4227 -801 506 -624 C ATOM 1595 N ARG B 135 38.639 77.729 38.933 1.00 60.29 N ANISOU 1595 N ARG B 135 10824 7219 4865 -1244 231 -774 N ATOM 1596 CA ARG B 135 39.784 78.469 39.449 1.00 63.60 C ANISOU 1596 CA ARG B 135 11458 7470 5239 -1577 74 -920 C ATOM 1597 C ARG B 135 39.571 78.770 40.919 1.00 66.44 C ANISOU 1597 C ARG B 135 12103 7839 5300 -1563 14 -1087 C ATOM 1598 O ARG B 135 38.472 79.137 41.338 1.00 66.54 O ANISOU 1598 O ARG B 135 12353 7801 5129 -1271 180 -1135 O ATOM 1599 CB ARG B 135 39.994 79.771 38.675 1.00 65.73 C ANISOU 1599 CB ARG B 135 12050 7354 5570 -1661 196 -990 C ATOM 1600 CG ARG B 135 41.266 80.549 39.052 1.00 70.13 C ANISOU 1600 CG ARG B 135 12791 7726 6127 -2137 62 -1173 C ATOM 1601 CD ARG B 135 41.124 82.029 38.696 1.00 75.38 C ANISOU 1601 CD ARG B 135 14021 7880 6740 -2183 263 -1286 C ATOM 1602 NE ARG B 135 42.255 82.839 39.155 1.00 80.27 N ANISOU 1602 NE ARG B 135 14864 8291 7345 -2722 165 -1521 N ATOM 1603 CZ ARG B 135 43.105 83.473 38.347 1.00 82.48 C ANISOU 1603 CZ ARG B 135 15225 8319 7795 -3110 258 -1534 C ATOM 1604 NH1 ARG B 135 42.962 83.404 37.024 1.00 80.46 N ANISOU 1604 NH1 ARG B 135 14884 7973 7713 -2961 448 -1298 N ATOM 1605 NH2 ARG B 135 44.100 84.181 38.863 1.00 85.27 N ANISOU 1605 NH2 ARG B 135 15744 8526 8127 -3670 170 -1798 N ATOM 1606 N VAL B 136 40.639 78.609 41.691 1.00 69.19 N ANISOU 1606 N VAL B 136 12407 8304 5577 -1849 -230 -1188 N ATOM 1607 CA VAL B 136 40.611 78.896 43.118 1.00 73.55 C ANISOU 1607 CA VAL B 136 13241 8898 5809 -1853 -334 -1373 C ATOM 1608 C VAL B 136 41.660 79.937 43.512 1.00 78.76 C ANISOU 1608 C VAL B 136 14135 9389 6401 -2245 -509 -1656 C ATOM 1609 O VAL B 136 42.695 80.068 42.855 1.00 79.20 O ANISOU 1609 O VAL B 136 13983 9442 6666 -2584 -613 -1681 O ATOM 1610 CB VAL B 136 40.790 77.607 43.957 1.00 72.63 C ANISOU 1610 CB VAL B 136 12885 9158 5552 -1767 -486 -1259 C ATOM 1611 CG1 VAL B 136 39.574 76.708 43.796 1.00 69.72 C ANISOU 1611 CG1 VAL B 136 12400 8895 5196 -1446 -250 -1039 C ATOM 1612 CG2 VAL B 136 42.079 76.866 43.573 1.00 71.70 C ANISOU 1612 CG2 VAL B 136 12370 9271 5601 -1979 -730 -1184 C ATOM 1613 N ASP B 137 41.373 80.676 44.579 1.00 83.59 N ANISOU 1613 N ASP B 137 15175 9874 6710 -2216 -523 -1888 N ATOM 1614 CA ASP B 137 42.334 81.607 45.156 1.00 90.05 C ANISOU 1614 CA ASP B 137 16240 10560 7412 -2631 -713 -2223 C ATOM 1615 C ASP B 137 43.512 80.851 45.786 1.00 92.24 C ANISOU 1615 C ASP B 137 16122 11304 7621 -2867 -1079 -2294 C ATOM 1616 O ASP B 137 43.327 79.789 46.397 1.00 91.07 O ANISOU 1616 O ASP B 137 15777 11509 7317 -2588 -1178 -2142 O ATOM 1617 CB ASP B 137 41.659 82.523 46.198 1.00 93.58 C ANISOU 1617 CB ASP B 137 17286 10765 7507 -2483 -641 -2474 C ATOM 1618 CG ASP B 137 40.455 83.283 45.636 1.00 93.46 C ANISOU 1618 CG ASP B 137 17676 10337 7499 -2133 -283 -2410 C ATOM 1619 OD1 ASP B 137 40.270 83.306 44.396 1.00 91.15 O ANISOU 1619 OD1 ASP B 137 17254 9894 7483 -2079 -112 -2214 O ATOM 1620 OD2 ASP B 137 39.687 83.853 46.441 1.00 96.07 O ANISOU 1620 OD2 ASP B 137 18455 10526 7522 -1861 -177 -2559 O ATOM 1621 N SER B 138 44.710 81.425 45.632 1.00 96.55 N ANISOU 1621 N SER B 138 16569 11854 8263 -3373 -1260 -2531 N ATOM 1622 CA SER B 138 45.994 80.848 46.088 1.00 99.38 C ANISOU 1622 CA SER B 138 16468 12729 8564 -3624 -1636 -2652 C ATOM 1623 C SER B 138 46.220 79.399 45.628 1.00 95.62 C ANISOU 1623 C SER B 138 15445 12664 8223 -3349 -1711 -2307 C ATOM 1624 O SER B 138 47.254 79.076 45.036 1.00 96.09 O ANISOU 1624 O SER B 138 15041 12993 8475 -3579 -1852 -2294 O ATOM 1625 CB SER B 138 46.158 80.970 47.607 1.00103.66 C ANISOU 1625 CB SER B 138 17215 13503 8668 -3596 -1907 -2938 C ATOM 1626 OG SER B 138 45.351 80.019 48.281 1.00102.39 O ANISOU 1626 OG SER B 138 17103 13534 8267 -3057 -1881 -2700 O TER 1627 SER B 138 ATOM 1628 N GLU C 69 18.970 32.662 -21.375 1.00 80.05 N ANISOU 1628 N GLU C 69 9994 9728 10692 33 -3075 -289 N ATOM 1629 CA GLU C 69 17.853 33.413 -20.737 1.00 81.55 C ANISOU 1629 CA GLU C 69 9804 9893 11288 158 -3248 -463 C ATOM 1630 C GLU C 69 18.032 34.945 -20.801 1.00 82.51 C ANISOU 1630 C GLU C 69 9990 9859 11499 342 -3453 -325 C ATOM 1631 O GLU C 69 17.227 35.655 -21.438 1.00 85.35 O ANISOU 1631 O GLU C 69 10313 10128 11989 496 -3869 -346 O ATOM 1632 CB GLU C 69 17.671 32.956 -19.281 1.00 79.75 C ANISOU 1632 CB GLU C 69 9263 9754 11284 70 -2891 -650 C ATOM 1633 N VAL C 70 19.087 35.437 -20.143 1.00 79.65 N ANISOU 1633 N VAL C 70 9739 9454 11070 327 -3183 -189 N ATOM 1634 CA VAL C 70 19.273 36.877 -19.902 1.00 79.81 C ANISOU 1634 CA VAL C 70 9791 9313 11218 475 -3311 -89 C ATOM 1635 C VAL C 70 20.592 37.436 -20.499 1.00 78.43 C ANISOU 1635 C VAL C 70 10042 9045 10713 419 -3262 214 C ATOM 1636 O VAL C 70 21.494 37.927 -19.788 1.00 76.37 O ANISOU 1636 O VAL C 70 9824 8752 10440 385 -3019 302 O ATOM 1637 CB VAL C 70 19.092 37.213 -18.391 1.00 78.57 C ANISOU 1637 CB VAL C 70 9302 9176 11375 513 -3069 -260 C ATOM 1638 CG1 VAL C 70 20.345 36.789 -17.541 1.00 75.80 C ANISOU 1638 CG1 VAL C 70 9051 8894 10855 363 -2621 -174 C ATOM 1639 CG2 VAL C 70 18.713 38.681 -18.207 1.00 81.03 C ANISOU 1639 CG2 VAL C 70 9548 9305 11934 722 -3324 -264 C ATOM 1640 N GLY C 71 20.675 37.366 -21.826 1.00 79.38 N ANISOU 1640 N GLY C 71 10475 9127 10558 392 -3498 361 N ATOM 1641 CA GLY C 71 21.861 37.797 -22.554 1.00 78.38 C ANISOU 1641 CA GLY C 71 10767 8939 10076 294 -3439 633 C ATOM 1642 C GLY C 71 22.489 36.700 -23.402 1.00 76.95 C ANISOU 1642 C GLY C 71 10823 8898 9517 134 -3283 694 C ATOM 1643 O GLY C 71 23.191 37.002 -24.374 1.00 78.41 O ANISOU 1643 O GLY C 71 11381 9042 9368 48 -3323 897 O ATOM 1644 N PHE C 72 22.254 35.435 -23.037 1.00 74.07 N ANISOU 1644 N PHE C 72 10264 8689 9192 82 -3095 514 N ATOM 1645 CA PHE C 72 22.714 34.296 -23.844 1.00 72.72 C ANISOU 1645 CA PHE C 72 10307 8635 8690 -42 -2975 525 C ATOM 1646 C PHE C 72 21.947 34.231 -25.161 1.00 74.84 C ANISOU 1646 C PHE C 72 10777 8859 8800 -26 -3368 545 C ATOM 1647 O PHE C 72 20.720 34.322 -25.152 1.00 76.51 O ANISOU 1647 O PHE C 72 10783 9029 9257 73 -3678 411 O ATOM 1648 CB PHE C 72 22.526 32.958 -23.109 1.00 70.88 C ANISOU 1648 CB PHE C 72 9843 8531 8557 -97 -2726 318 C ATOM 1649 CG PHE C 72 23.284 32.844 -21.808 1.00 68.36 C ANISOU 1649 CG PHE C 72 9361 8257 8355 -118 -2353 291 C ATOM 1650 CD1 PHE C 72 24.632 33.163 -21.733 1.00 66.78 C ANISOU 1650 CD1 PHE C 72 9324 8076 7973 -159 -2117 443 C ATOM 1651 CD2 PHE C 72 22.641 32.387 -20.659 1.00 68.29 C ANISOU 1651 CD2 PHE C 72 9040 8281 8627 -116 -2241 103 C ATOM 1652 CE1 PHE C 72 25.321 33.047 -20.534 1.00 66.38 C ANISOU 1652 CE1 PHE C 72 9124 8066 8031 -169 -1817 409 C ATOM 1653 CE2 PHE C 72 23.328 32.266 -19.439 1.00 66.08 C ANISOU 1653 CE2 PHE C 72 8650 8031 8426 -140 -1922 82 C ATOM 1654 CZ PHE C 72 24.663 32.597 -19.376 1.00 64.66 C ANISOU 1654 CZ PHE C 72 8632 7860 8074 -153 -1731 236 C ATOM 1655 N PRO C 73 22.665 34.083 -26.298 1.00 74.92 N ANISOU 1655 N PRO C 73 11185 8886 8396 -127 -3361 697 N ATOM 1656 CA PRO C 73 21.990 33.715 -27.542 1.00 76.73 C ANISOU 1656 CA PRO C 73 11634 9101 8417 -141 -3697 687 C ATOM 1657 C PRO C 73 21.275 32.370 -27.384 1.00 75.21 C ANISOU 1657 C PRO C 73 11227 9022 8327 -167 -3672 444 C ATOM 1658 O PRO C 73 21.743 31.483 -26.645 1.00 72.48 O ANISOU 1658 O PRO C 73 10737 8778 8023 -228 -3308 338 O ATOM 1659 CB PRO C 73 23.140 33.578 -28.547 1.00 77.42 C ANISOU 1659 CB PRO C 73 12165 9237 8016 -287 -3525 858 C ATOM 1660 CG PRO C 73 24.219 34.426 -28.007 1.00 76.72 C ANISOU 1660 CG PRO C 73 12108 9123 7919 -325 -3256 1014 C ATOM 1661 CD PRO C 73 24.107 34.318 -26.508 1.00 74.04 C ANISOU 1661 CD PRO C 73 11333 8813 7986 -242 -3053 874 C ATOM 1662 N VAL C 74 20.143 32.236 -28.064 1.00 76.35 N ANISOU 1662 N VAL C 74 11361 9134 8515 -125 -4079 355 N ATOM 1663 CA VAL C 74 19.356 31.018 -28.015 1.00 75.06 C ANISOU 1663 CA VAL C 74 11006 9063 8450 -179 -4106 119 C ATOM 1664 C VAL C 74 20.137 29.931 -28.740 1.00 73.50 C ANISOU 1664 C VAL C 74 11134 8946 7846 -321 -3890 129 C ATOM 1665 O VAL C 74 20.534 30.104 -29.899 1.00 76.04 O ANISOU 1665 O VAL C 74 11853 9247 7792 -360 -4016 264 O ATOM 1666 CB VAL C 74 17.957 31.230 -28.655 1.00 79.08 C ANISOU 1666 CB VAL C 74 11417 9523 9106 -98 -4642 15 C ATOM 1667 CG1 VAL C 74 17.168 29.902 -28.758 1.00 79.79 C ANISOU 1667 CG1 VAL C 74 11345 9716 9255 -206 -4679 -233 C ATOM 1668 CG2 VAL C 74 17.177 32.283 -27.870 1.00 79.48 C ANISOU 1668 CG2 VAL C 74 11099 9500 9601 76 -4840 -41 C ATOM 1669 N ARG C 75 20.379 28.829 -28.034 1.00 69.02 N ANISOU 1669 N ARG C 75 10418 8461 7345 -395 -3559 -19 N ATOM 1670 CA ARG C 75 21.050 27.660 -28.587 1.00 66.31 C ANISOU 1670 CA ARG C 75 10340 8181 6674 -501 -3347 -65 C ATOM 1671 C ARG C 75 20.581 26.428 -27.796 1.00 63.55 C ANISOU 1671 C ARG C 75 9755 7862 6528 -572 -3192 -290 C ATOM 1672 O ARG C 75 20.029 26.584 -26.701 1.00 61.83 O ANISOU 1672 O ARG C 75 9183 7639 6668 -555 -3145 -374 O ATOM 1673 CB ARG C 75 22.581 27.845 -28.559 1.00 64.63 C ANISOU 1673 CB ARG C 75 10337 8009 6213 -508 -2976 85 C ATOM 1674 CG ARG C 75 23.240 27.844 -27.175 1.00 60.25 C ANISOU 1674 CG ARG C 75 9527 7476 5889 -474 -2614 73 C ATOM 1675 CD ARG C 75 24.767 27.744 -27.306 1.00 57.43 C ANISOU 1675 CD ARG C 75 9368 7189 5263 -491 -2261 166 C ATOM 1676 NE ARG C 75 25.403 27.331 -26.057 1.00 52.87 N ANISOU 1676 NE ARG C 75 8581 6639 4867 -458 -1934 106 N ATOM 1677 CZ ARG C 75 26.713 27.396 -25.810 1.00 50.65 C ANISOU 1677 CZ ARG C 75 8347 6424 4474 -441 -1628 167 C ATOM 1678 NH1 ARG C 75 27.545 27.856 -26.734 1.00 49.79 N ANISOU 1678 NH1 ARG C 75 8474 6377 4066 -480 -1562 283 N ATOM 1679 NH2 ARG C 75 27.191 27.013 -24.624 1.00 46.54 N ANISOU 1679 NH2 ARG C 75 7635 5912 4135 -396 -1392 105 N ATOM 1680 N PRO C 76 20.748 25.212 -28.358 1.00 62.62 N ANISOU 1680 N PRO C 76 9851 7766 6175 -664 -3120 -397 N ATOM 1681 CA PRO C 76 20.383 23.987 -27.615 1.00 60.85 C ANISOU 1681 CA PRO C 76 9473 7535 6111 -758 -2961 -596 C ATOM 1682 C PRO C 76 21.213 23.765 -26.349 1.00 56.64 C ANISOU 1682 C PRO C 76 8820 6999 5701 -735 -2561 -581 C ATOM 1683 O PRO C 76 22.420 24.000 -26.356 1.00 54.45 O ANISOU 1683 O PRO C 76 8695 6743 5249 -663 -2334 -460 O ATOM 1684 CB PRO C 76 20.650 22.848 -28.620 1.00 62.42 C ANISOU 1684 CB PRO C 76 10022 7729 5966 -835 -2961 -683 C ATOM 1685 CG PRO C 76 21.448 23.473 -29.743 1.00 64.04 C ANISOU 1685 CG PRO C 76 10562 7969 5803 -777 -3002 -520 C ATOM 1686 CD PRO C 76 21.093 24.928 -29.763 1.00 64.83 C ANISOU 1686 CD PRO C 76 10540 8059 6034 -701 -3234 -358 C ATOM 1687 N GLN C 77 20.555 23.304 -25.283 1.00 55.31 N ANISOU 1687 N GLN C 77 8384 6808 5822 -809 -2483 -713 N ATOM 1688 CA GLN C 77 21.220 23.028 -24.007 1.00 52.00 C ANISOU 1688 CA GLN C 77 7874 6367 5516 -803 -2140 -707 C ATOM 1689 C GLN C 77 22.289 21.968 -24.158 1.00 51.05 C ANISOU 1689 C GLN C 77 8049 6211 5138 -794 -1907 -722 C ATOM 1690 O GLN C 77 22.048 20.855 -24.638 1.00 52.36 O ANISOU 1690 O GLN C 77 8394 6327 5175 -881 -1945 -848 O ATOM 1691 CB GLN C 77 20.235 22.618 -22.896 1.00 51.99 C ANISOU 1691 CB GLN C 77 7584 6343 5825 -933 -2095 -859 C ATOM 1692 CG GLN C 77 20.923 22.249 -21.552 1.00 49.70 C ANISOU 1692 CG GLN C 77 7267 6010 5606 -945 -1754 -847 C ATOM 1693 CD GLN C 77 21.786 23.385 -20.981 1.00 47.63 C ANISOU 1693 CD GLN C 77 6922 5782 5392 -793 -1625 -686 C ATOM 1694 OE1 GLN C 77 21.329 24.524 -20.849 1.00 48.07 O ANISOU 1694 OE1 GLN C 77 6760 5877 5627 -738 -1747 -643 O ATOM 1695 NE2 GLN C 77 23.044 23.076 -20.652 1.00 46.11 N ANISOU 1695 NE2 GLN C 77 6902 5567 5049 -719 -1393 -609 N ATOM 1696 N VAL C 78 23.472 22.358 -23.733 1.00 48.62 N ANISOU 1696 N VAL C 78 7777 5926 4771 -681 -1679 -605 N ATOM 1697 CA VAL C 78 24.660 21.551 -23.764 1.00 48.15 C ANISOU 1697 CA VAL C 78 7939 5849 4506 -615 -1445 -620 C ATOM 1698 C VAL C 78 24.567 20.401 -22.697 1.00 48.04 C ANISOU 1698 C VAL C 78 7922 5721 4609 -673 -1297 -739 C ATOM 1699 O VAL C 78 23.946 20.576 -21.636 1.00 46.92 O ANISOU 1699 O VAL C 78 7566 5548 4713 -750 -1274 -753 O ATOM 1700 CB VAL C 78 25.822 22.561 -23.587 1.00 46.73 C ANISOU 1700 CB VAL C 78 7719 5753 4285 -490 -1287 -461 C ATOM 1701 CG1 VAL C 78 26.312 22.692 -22.143 1.00 42.90 C ANISOU 1701 CG1 VAL C 78 7055 5243 4003 -443 -1085 -434 C ATOM 1702 CG2 VAL C 78 26.908 22.305 -24.546 1.00 49.26 C ANISOU 1702 CG2 VAL C 78 8283 6137 4296 -421 -1174 -449 C ATOM 1703 N PRO C 79 25.164 19.221 -22.967 1.00 48.80 N ANISOU 1703 N PRO C 79 8279 5742 4521 -643 -1199 -831 N ATOM 1704 CA PRO C 79 24.851 18.055 -22.108 1.00 49.24 C ANISOU 1704 CA PRO C 79 8404 5641 4664 -736 -1129 -944 C ATOM 1705 C PRO C 79 25.159 18.249 -20.625 1.00 47.51 C ANISOU 1705 C PRO C 79 8042 5380 4631 -718 -960 -884 C ATOM 1706 O PRO C 79 26.219 18.732 -20.267 1.00 46.30 O ANISOU 1706 O PRO C 79 7855 5277 4459 -560 -827 -793 O ATOM 1707 CB PRO C 79 25.708 16.924 -22.700 1.00 50.34 C ANISOU 1707 CB PRO C 79 8872 5694 4559 -636 -1054 -1038 C ATOM 1708 CG PRO C 79 26.018 17.364 -24.099 1.00 51.54 C ANISOU 1708 CG PRO C 79 9121 5976 4486 -567 -1130 -1022 C ATOM 1709 CD PRO C 79 26.143 18.874 -24.008 1.00 50.08 C ANISOU 1709 CD PRO C 79 8694 5944 4391 -526 -1138 -851 C ATOM 1710 N LEU C 80 24.216 17.856 -19.779 1.00 47.94 N ANISOU 1710 N LEU C 80 8016 5347 4851 -903 -965 -947 N ATOM 1711 CA LEU C 80 24.282 18.095 -18.354 1.00 46.59 C ANISOU 1711 CA LEU C 80 7716 5141 4845 -936 -819 -900 C ATOM 1712 C LEU C 80 25.216 17.099 -17.649 1.00 46.07 C ANISOU 1712 C LEU C 80 7915 4913 4676 -861 -678 -905 C ATOM 1713 O LEU C 80 25.377 15.986 -18.102 1.00 47.44 O ANISOU 1713 O LEU C 80 8364 4955 4706 -860 -706 -990 O ATOM 1714 CB LEU C 80 22.858 18.036 -17.789 1.00 48.25 C ANISOU 1714 CB LEU C 80 7743 5339 5251 -1195 -858 -989 C ATOM 1715 CG LEU C 80 21.827 18.979 -18.462 1.00 49.88 C ANISOU 1715 CG LEU C 80 7659 5695 5600 -1245 -1047 -1017 C ATOM 1716 CD1 LEU C 80 20.496 19.003 -17.703 1.00 51.14 C ANISOU 1716 CD1 LEU C 80 7555 5874 6001 -1485 -1042 -1137 C ATOM 1717 CD2 LEU C 80 22.351 20.408 -18.601 1.00 47.54 C ANISOU 1717 CD2 LEU C 80 7185 5525 5351 -1050 -1073 -879 C ATOM 1718 N ARG C 81 25.851 17.520 -16.560 1.00 44.09 N ANISOU 1718 N ARG C 81 7594 4662 4498 -781 -552 -819 N ATOM 1719 CA ARG C 81 26.877 16.705 -15.895 1.00 44.17 C ANISOU 1719 CA ARG C 81 7849 4522 4413 -654 -463 -811 C ATOM 1720 C ARG C 81 27.211 17.213 -14.474 1.00 42.76 C ANISOU 1720 C ARG C 81 7573 4333 4341 -645 -355 -724 C ATOM 1721 O ARG C 81 26.970 18.387 -14.154 1.00 41.63 O ANISOU 1721 O ARG C 81 7150 4335 4331 -668 -327 -660 O ATOM 1722 CB ARG C 81 28.148 16.600 -16.758 1.00 43.86 C ANISOU 1722 CB ARG C 81 7910 4534 4222 -383 -458 -814 C ATOM 1723 CG ARG C 81 28.641 17.947 -17.302 1.00 42.95 C ANISOU 1723 CG ARG C 81 7540 4651 4128 -269 -439 -722 C ATOM 1724 CD ARG C 81 29.983 17.826 -18.013 1.00 41.96 C ANISOU 1724 CD ARG C 81 7492 4599 3852 -32 -379 -743 C ATOM 1725 NE ARG C 81 30.329 19.106 -18.625 1.00 40.29 N ANISOU 1725 NE ARG C 81 7074 4600 3635 6 -354 -650 N ATOM 1726 CZ ARG C 81 31.472 19.376 -19.258 1.00 39.76 C ANISOU 1726 CZ ARG C 81 6991 4665 3451 162 -264 -650 C ATOM 1727 NH1 ARG C 81 32.430 18.436 -19.379 1.00 37.34 N ANISOU 1727 NH1 ARG C 81 6828 4315 3043 340 -191 -766 N ATOM 1728 NH2 ARG C 81 31.652 20.594 -19.773 1.00 35.05 N ANISOU 1728 NH2 ARG C 81 6237 4239 2841 136 -245 -546 N ATOM 1729 N PRO C 82 27.758 16.333 -13.608 1.00 43.24 N ANISOU 1729 N PRO C 82 7890 4206 4335 -607 -314 -724 N ATOM 1730 CA PRO C 82 28.027 16.849 -12.261 1.00 41.94 C ANISOU 1730 CA PRO C 82 7653 4035 4246 -616 -230 -641 C ATOM 1731 C PRO C 82 29.376 17.556 -12.164 1.00 41.10 C ANISOU 1731 C PRO C 82 7434 4041 4142 -338 -213 -567 C ATOM 1732 O PRO C 82 30.335 17.149 -12.831 1.00 41.75 O ANISOU 1732 O PRO C 82 7610 4123 4132 -118 -247 -598 O ATOM 1733 CB PRO C 82 27.992 15.585 -11.382 1.00 43.43 C ANISOU 1733 CB PRO C 82 8213 3951 4336 -714 -225 -663 C ATOM 1734 CG PRO C 82 28.416 14.457 -12.299 1.00 44.89 C ANISOU 1734 CG PRO C 82 8676 3994 4387 -584 -318 -743 C ATOM 1735 CD PRO C 82 27.956 14.867 -13.709 1.00 44.88 C ANISOU 1735 CD PRO C 82 8480 4171 4401 -594 -360 -801 C ATOM 1736 N MET C 83 29.441 18.603 -11.343 1.00 40.00 N ANISOU 1736 N MET C 83 7083 4004 4112 -357 -154 -491 N ATOM 1737 CA MET C 83 30.696 19.322 -11.062 1.00 39.64 C ANISOU 1737 CA MET C 83 6916 4061 4086 -137 -137 -424 C ATOM 1738 C MET C 83 31.771 18.401 -10.505 1.00 40.99 C ANISOU 1738 C MET C 83 7330 4082 4161 48 -177 -437 C ATOM 1739 O MET C 83 31.475 17.531 -9.646 1.00 43.15 O ANISOU 1739 O MET C 83 7875 4145 4377 -44 -199 -444 O ATOM 1740 CB MET C 83 30.447 20.449 -10.046 1.00 38.44 C ANISOU 1740 CB MET C 83 6559 3988 4060 -230 -77 -356 C ATOM 1741 CG MET C 83 31.679 21.331 -9.709 1.00 38.61 C ANISOU 1741 CG MET C 83 6427 4124 4119 -44 -66 -289 C ATOM 1742 SD MET C 83 32.510 22.114 -11.142 1.00 40.20 S ANISOU 1742 SD MET C 83 6419 4536 4318 119 -71 -268 S ATOM 1743 CE MET C 83 31.279 23.336 -11.632 1.00 36.02 C ANISOU 1743 CE MET C 83 5667 4110 3908 -59 -77 -226 C ATOM 1744 N THR C 84 33.014 18.615 -10.946 1.00 40.32 N ANISOU 1744 N THR C 84 7152 4104 4063 299 -190 -446 N ATOM 1745 CA THR C 84 34.185 17.904 -10.398 1.00 40.84 C ANISOU 1745 CA THR C 84 7376 4061 4081 536 -256 -477 C ATOM 1746 C THR C 84 35.247 18.845 -9.838 1.00 40.13 C ANISOU 1746 C THR C 84 7049 4125 4075 679 -246 -429 C ATOM 1747 O THR C 84 35.243 20.058 -10.092 1.00 37.95 O ANISOU 1747 O THR C 84 6489 4050 3879 617 -172 -375 O ATOM 1748 CB THR C 84 34.915 17.111 -11.473 1.00 42.28 C ANISOU 1748 CB THR C 84 7639 4241 4183 759 -287 -594 C ATOM 1749 OG1 THR C 84 35.335 18.015 -12.514 1.00 41.02 O ANISOU 1749 OG1 THR C 84 7192 4349 4047 811 -199 -602 O ATOM 1750 CG2 THR C 84 34.024 16.001 -12.056 1.00 44.07 C ANISOU 1750 CG2 THR C 84 8153 4281 4311 647 -325 -666 C ATOM 1751 N TYR C 85 36.195 18.249 -9.121 1.00 41.26 N ANISOU 1751 N TYR C 85 7322 4157 4196 881 -344 -458 N ATOM 1752 CA TYR C 85 37.363 18.955 -8.625 1.00 40.80 C ANISOU 1752 CA TYR C 85 7044 4241 4219 1050 -369 -446 C ATOM 1753 C TYR C 85 38.091 19.692 -9.759 1.00 40.50 C ANISOU 1753 C TYR C 85 6679 4479 4232 1148 -269 -494 C ATOM 1754 O TYR C 85 38.395 20.898 -9.645 1.00 39.87 O ANISOU 1754 O TYR C 85 6326 4587 4237 1087 -205 -433 O ATOM 1755 CB TYR C 85 38.323 17.992 -7.895 1.00 42.28 C ANISOU 1755 CB TYR C 85 7436 4255 4374 1308 -539 -505 C ATOM 1756 CG TYR C 85 39.629 18.660 -7.554 1.00 42.58 C ANISOU 1756 CG TYR C 85 7193 4471 4513 1509 -583 -532 C ATOM 1757 CD1 TYR C 85 39.778 19.369 -6.354 1.00 40.58 C ANISOU 1757 CD1 TYR C 85 6890 4225 4302 1439 -638 -444 C ATOM 1758 CD2 TYR C 85 40.713 18.618 -8.444 1.00 42.70 C ANISOU 1758 CD2 TYR C 85 6975 4668 4582 1749 -557 -664 C ATOM 1759 CE1 TYR C 85 40.973 20.004 -6.036 1.00 41.09 C ANISOU 1759 CE1 TYR C 85 6681 4460 4470 1602 -694 -479 C ATOM 1760 CE2 TYR C 85 41.904 19.265 -8.144 1.00 43.89 C ANISOU 1760 CE2 TYR C 85 6821 5010 4845 1902 -585 -708 C ATOM 1761 CZ TYR C 85 42.024 19.949 -6.931 1.00 43.23 C ANISOU 1761 CZ TYR C 85 6696 4917 4812 1826 -668 -611 C ATOM 1762 OH TYR C 85 43.197 20.561 -6.611 1.00 43.84 O ANISOU 1762 OH TYR C 85 6472 5179 5006 1963 -717 -665 O ATOM 1763 N LYS C 86 38.379 18.983 -10.842 1.00 41.74 N ANISOU 1763 N LYS C 86 6883 4655 4323 1280 -247 -606 N ATOM 1764 CA LYS C 86 39.183 19.564 -11.935 1.00 42.85 C ANISOU 1764 CA LYS C 86 6746 5062 4474 1367 -127 -672 C ATOM 1765 C LYS C 86 38.440 20.669 -12.690 1.00 40.68 C ANISOU 1765 C LYS C 86 6324 4944 4189 1123 -9 -571 C ATOM 1766 O LYS C 86 39.030 21.692 -13.018 1.00 40.41 O ANISOU 1766 O LYS C 86 6036 5124 4196 1097 83 -539 O ATOM 1767 CB LYS C 86 39.737 18.492 -12.893 1.00 45.19 C ANISOU 1767 CB LYS C 86 7141 5345 4685 1584 -117 -849 C ATOM 1768 CG LYS C 86 40.547 19.065 -14.047 1.00 48.64 C ANISOU 1768 CG LYS C 86 7306 6076 5098 1638 50 -934 C ATOM 1769 CD LYS C 86 41.570 18.079 -14.640 1.00 54.56 C ANISOU 1769 CD LYS C 86 8059 6857 5814 1941 67 -1164 C ATOM 1770 CE LYS C 86 41.401 17.889 -16.154 1.00 59.02 C ANISOU 1770 CE LYS C 86 8664 7539 6222 1897 219 -1262 C ATOM 1771 NZ LYS C 86 40.974 19.121 -16.907 1.00 57.79 N ANISOU 1771 NZ LYS C 86 8365 7595 5999 1618 366 -1128 N ATOM 1772 N ALA C 87 37.155 20.467 -12.956 1.00 39.86 N ANISOU 1772 N ALA C 87 6385 4725 4035 941 -28 -525 N ATOM 1773 CA ALA C 87 36.348 21.532 -13.564 1.00 39.08 C ANISOU 1773 CA ALA C 87 6161 4741 3946 730 25 -427 C ATOM 1774 C ALA C 87 36.249 22.797 -12.667 1.00 37.40 C ANISOU 1774 C ALA C 87 5758 4585 3868 618 33 -306 C ATOM 1775 O ALA C 87 36.349 23.932 -13.176 1.00 37.27 O ANISOU 1775 O ALA C 87 5564 4721 3878 540 87 -235 O ATOM 1776 CB ALA C 87 34.973 21.025 -13.956 1.00 38.60 C ANISOU 1776 CB ALA C 87 6282 4550 3835 571 -27 -429 C ATOM 1777 N ALA C 88 36.112 22.605 -11.353 1.00 36.37 N ANISOU 1777 N ALA C 88 5694 4324 3803 610 -23 -285 N ATOM 1778 CA ALA C 88 36.021 23.726 -10.422 1.00 35.23 C ANISOU 1778 CA ALA C 88 5397 4216 3772 513 -16 -197 C ATOM 1779 C ALA C 88 37.306 24.528 -10.448 1.00 35.22 C ANISOU 1779 C ALA C 88 5174 4389 3821 612 21 -186 C ATOM 1780 O ALA C 88 37.285 25.770 -10.491 1.00 34.91 O ANISOU 1780 O ALA C 88 4959 4451 3854 506 60 -109 O ATOM 1781 CB ALA C 88 35.711 23.245 -9.006 1.00 34.80 C ANISOU 1781 CB ALA C 88 5504 3987 3732 480 -73 -193 C ATOM 1782 N LEU C 89 38.412 23.799 -10.490 1.00 36.45 N ANISOU 1782 N LEU C 89 5333 4573 3942 814 3 -277 N ATOM 1783 CA LEU C 89 39.746 24.361 -10.519 1.00 37.39 C ANISOU 1783 CA LEU C 89 5212 4876 4117 921 41 -311 C ATOM 1784 C LEU C 89 39.996 25.121 -11.808 1.00 38.10 C ANISOU 1784 C LEU C 89 5135 5169 4171 838 178 -296 C ATOM 1785 O LEU C 89 40.437 26.287 -11.788 1.00 37.96 O ANISOU 1785 O LEU C 89 4919 5287 4217 738 235 -233 O ATOM 1786 CB LEU C 89 40.785 23.248 -10.331 1.00 39.42 C ANISOU 1786 CB LEU C 89 5506 5111 4361 1190 -28 -452 C ATOM 1787 CG LEU C 89 42.247 23.675 -10.258 1.00 40.81 C ANISOU 1787 CG LEU C 89 5390 5493 4625 1328 -6 -533 C ATOM 1788 CD1 LEU C 89 42.539 24.360 -8.948 1.00 39.96 C ANISOU 1788 CD1 LEU C 89 5197 5365 4622 1292 -107 -469 C ATOM 1789 CD2 LEU C 89 43.175 22.478 -10.455 1.00 42.39 C ANISOU 1789 CD2 LEU C 89 5604 5686 4815 1631 -66 -718 C ATOM 1790 N ASP C 90 39.705 24.474 -12.927 1.00 38.89 N ANISOU 1790 N ASP C 90 5349 5277 4150 859 227 -351 N ATOM 1791 CA ASP C 90 39.841 25.118 -14.241 1.00 39.82 C ANISOU 1791 CA ASP C 90 5382 5570 4176 755 355 -330 C ATOM 1792 C ASP C 90 38.978 26.384 -14.381 1.00 38.68 C ANISOU 1792 C ASP C 90 5218 5419 4059 524 344 -164 C ATOM 1793 O ASP C 90 39.476 27.425 -14.797 1.00 38.94 O ANISOU 1793 O ASP C 90 5114 5592 4088 419 427 -99 O ATOM 1794 CB ASP C 90 39.525 24.110 -15.349 1.00 41.08 C ANISOU 1794 CB ASP C 90 5725 5706 4176 812 383 -425 C ATOM 1795 CG ASP C 90 40.527 22.952 -15.393 1.00 43.77 C ANISOU 1795 CG ASP C 90 6069 6069 4494 1069 406 -617 C ATOM 1796 OD1 ASP C 90 41.676 23.130 -14.928 1.00 44.60 O ANISOU 1796 OD1 ASP C 90 5961 6295 4692 1193 440 -686 O ATOM 1797 OD2 ASP C 90 40.164 21.868 -15.905 1.00 45.28 O ANISOU 1797 OD2 ASP C 90 6470 6151 4583 1155 377 -714 O ATOM 1798 N ILE C 91 37.701 26.309 -13.999 1.00 37.54 N ANISOU 1798 N ILE C 91 5206 5106 3951 444 239 -106 N ATOM 1799 CA ILE C 91 36.812 27.476 -14.097 1.00 37.01 C ANISOU 1799 CA ILE C 91 5109 5014 3941 269 196 23 C ATOM 1800 C ILE C 91 37.279 28.609 -13.134 1.00 37.04 C ANISOU 1800 C ILE C 91 4945 5044 4087 220 201 93 C ATOM 1801 O ILE C 91 37.255 29.790 -13.499 1.00 36.67 O ANISOU 1801 O ILE C 91 4829 5042 4062 101 211 191 O ATOM 1802 CB ILE C 91 35.295 27.049 -13.930 1.00 36.78 C ANISOU 1802 CB ILE C 91 5214 4821 3941 204 89 23 C ATOM 1803 CG1 ILE C 91 34.869 26.177 -15.128 1.00 36.61 C ANISOU 1803 CG1 ILE C 91 5352 4794 3765 213 72 -35 C ATOM 1804 CG2 ILE C 91 34.360 28.261 -13.784 1.00 34.52 C ANISOU 1804 CG2 ILE C 91 4854 4494 3770 71 18 120 C ATOM 1805 CD1 ILE C 91 33.751 25.194 -14.828 1.00 35.60 C ANISOU 1805 CD1 ILE C 91 5366 4509 3652 183 -10 -100 C ATOM 1806 N SER C 92 37.740 28.228 -11.936 1.00 37.26 N ANISOU 1806 N SER C 92 4937 5029 4193 310 180 41 N ATOM 1807 CA SER C 92 38.376 29.148 -10.967 1.00 37.22 C ANISOU 1807 CA SER C 92 4780 5057 4305 282 176 77 C ATOM 1808 C SER C 92 39.471 29.940 -11.603 1.00 38.47 C ANISOU 1808 C SER C 92 4770 5396 4452 239 267 99 C ATOM 1809 O SER C 92 39.503 31.167 -11.518 1.00 39.22 O ANISOU 1809 O SER C 92 4783 5509 4611 104 273 187 O ATOM 1810 CB SER C 92 39.059 28.367 -9.826 1.00 37.73 C ANISOU 1810 CB SER C 92 4854 5082 4401 428 125 -7 C ATOM 1811 OG SER C 92 38.142 27.961 -8.854 1.00 37.59 O ANISOU 1811 OG SER C 92 4990 4890 4402 404 53 -4 O ATOM 1812 N HIS C 93 40.405 29.220 -12.201 1.00 39.91 N ANISOU 1812 N HIS C 93 4900 5709 4554 351 345 1 N ATOM 1813 CA HIS C 93 41.552 29.855 -12.794 1.00 42.35 C ANISOU 1813 CA HIS C 93 5019 6225 4847 294 471 -13 C ATOM 1814 C HIS C 93 41.113 30.783 -13.915 1.00 41.51 C ANISOU 1814 C HIS C 93 4976 6153 4643 90 540 110 C ATOM 1815 O HIS C 93 41.527 31.925 -13.955 1.00 42.28 O ANISOU 1815 O HIS C 93 4978 6313 4775 -69 587 191 O ATOM 1816 CB HIS C 93 42.609 28.829 -13.214 1.00 44.97 C ANISOU 1816 CB HIS C 93 5257 6704 5124 475 555 -184 C ATOM 1817 CG HIS C 93 43.505 28.405 -12.085 1.00 50.14 C ANISOU 1817 CG HIS C 93 5766 7377 5909 654 473 -293 C ATOM 1818 ND1 HIS C 93 43.225 27.325 -11.272 1.00 54.92 N ANISOU 1818 ND1 HIS C 93 6519 7812 6535 846 324 -353 N ATOM 1819 CD2 HIS C 93 44.662 28.932 -11.615 1.00 54.78 C ANISOU 1819 CD2 HIS C 93 6087 8120 6605 659 494 -351 C ATOM 1820 CE1 HIS C 93 44.176 27.196 -10.361 1.00 55.20 C ANISOU 1820 CE1 HIS C 93 6405 7889 6678 984 237 -436 C ATOM 1821 NE2 HIS C 93 45.060 28.159 -10.545 1.00 55.90 N ANISOU 1821 NE2 HIS C 93 6220 8186 6835 880 334 -446 N ATOM 1822 N PHE C 94 40.222 30.313 -14.774 1.00 40.83 N ANISOU 1822 N PHE C 94 5079 6000 4433 85 519 130 N ATOM 1823 CA PHE C 94 39.631 31.168 -15.798 1.00 40.81 C ANISOU 1823 CA PHE C 94 5195 5986 4326 -95 521 262 C ATOM 1824 C PHE C 94 39.053 32.447 -15.214 1.00 39.68 C ANISOU 1824 C PHE C 94 5045 5717 4314 -221 414 400 C ATOM 1825 O PHE C 94 39.399 33.529 -15.658 1.00 40.51 O ANISOU 1825 O PHE C 94 5144 5861 4386 -382 455 503 O ATOM 1826 CB PHE C 94 38.556 30.425 -16.597 1.00 40.61 C ANISOU 1826 CB PHE C 94 5381 5870 4177 -63 446 254 C ATOM 1827 CG PHE C 94 37.932 31.258 -17.677 1.00 40.74 C ANISOU 1827 CG PHE C 94 5547 5860 4070 -226 398 389 C ATOM 1828 CD1 PHE C 94 38.494 31.301 -18.953 1.00 41.08 C ANISOU 1828 CD1 PHE C 94 5680 6044 3885 -316 526 398 C ATOM 1829 CD2 PHE C 94 36.786 32.013 -17.422 1.00 39.50 C ANISOU 1829 CD2 PHE C 94 5454 5536 4020 -285 218 498 C ATOM 1830 CE1 PHE C 94 37.908 32.079 -19.971 1.00 41.67 C ANISOU 1830 CE1 PHE C 94 5953 6070 3809 -475 450 543 C ATOM 1831 CE2 PHE C 94 36.202 32.807 -18.421 1.00 38.35 C ANISOU 1831 CE2 PHE C 94 5469 5337 3763 -408 121 628 C ATOM 1832 CZ PHE C 94 36.765 32.836 -19.696 1.00 40.64 C ANISOU 1832 CZ PHE C 94 5896 5747 3798 -509 225 664 C ATOM 1833 N LEU C 95 38.191 32.329 -14.208 1.00 38.40 N ANISOU 1833 N LEU C 95 4896 5399 4295 -156 287 391 N ATOM 1834 CA LEU C 95 37.553 33.517 -13.617 1.00 38.24 C ANISOU 1834 CA LEU C 95 4866 5249 4414 -248 185 486 C ATOM 1835 C LEU C 95 38.548 34.531 -13.039 1.00 39.60 C ANISOU 1835 C LEU C 95 4901 5474 4670 -337 237 524 C ATOM 1836 O LEU C 95 38.344 35.732 -13.143 1.00 39.86 O ANISOU 1836 O LEU C 95 4965 5432 4749 -463 187 630 O ATOM 1837 CB LEU C 95 36.490 33.116 -12.589 1.00 36.33 C ANISOU 1837 CB LEU C 95 4641 4861 4302 -171 84 430 C ATOM 1838 CG LEU C 95 35.263 32.489 -13.255 1.00 35.68 C ANISOU 1838 CG LEU C 95 4682 4705 4169 -151 4 413 C ATOM 1839 CD1 LEU C 95 34.415 31.724 -12.255 1.00 32.68 C ANISOU 1839 CD1 LEU C 95 4310 4226 3882 -96 -33 318 C ATOM 1840 CD2 LEU C 95 34.427 33.555 -14.000 1.00 35.87 C ANISOU 1840 CD2 LEU C 95 4763 4650 4214 -236 -117 516 C ATOM 1841 N LYS C 96 39.645 34.045 -12.473 1.00 41.24 N ANISOU 1841 N LYS C 96 4966 5806 4899 -269 319 430 N ATOM 1842 CA LYS C 96 40.662 34.925 -11.934 1.00 43.68 C ANISOU 1842 CA LYS C 96 5118 6189 5291 -363 361 442 C ATOM 1843 C LYS C 96 41.533 35.575 -13.023 1.00 46.89 C ANISOU 1843 C LYS C 96 5479 6747 5589 -537 499 499 C ATOM 1844 O LYS C 96 41.945 36.746 -12.901 1.00 47.33 O ANISOU 1844 O LYS C 96 5493 6795 5697 -715 512 576 O ATOM 1845 CB LYS C 96 41.541 34.167 -10.935 1.00 43.33 C ANISOU 1845 CB LYS C 96 4920 6227 5315 -218 364 308 C ATOM 1846 CG LYS C 96 42.702 34.991 -10.333 1.00 46.06 C ANISOU 1846 CG LYS C 96 5064 6677 5759 -311 389 289 C ATOM 1847 CD LYS C 96 42.187 36.184 -9.465 1.00 45.82 C ANISOU 1847 CD LYS C 96 5080 6483 5848 -430 288 371 C ATOM 1848 CE LYS C 96 43.307 36.778 -8.584 1.00 47.45 C ANISOU 1848 CE LYS C 96 5097 6773 6161 -494 273 318 C ATOM 1849 NZ LYS C 96 44.425 37.416 -9.348 1.00 49.87 N ANISOU 1849 NZ LYS C 96 5239 7264 6447 -674 404 330 N ATOM 1850 N GLU C 97 41.840 34.810 -14.066 1.00 49.02 N ANISOU 1850 N GLU C 97 5773 7154 5701 -505 614 449 N ATOM 1851 CA GLU C 97 42.746 35.299 -15.088 1.00 52.95 C ANISOU 1851 CA GLU C 97 6224 7830 6065 -689 793 475 C ATOM 1852 C GLU C 97 42.098 36.364 -15.999 1.00 54.00 C ANISOU 1852 C GLU C 97 6592 7847 6077 -908 761 666 C ATOM 1853 O GLU C 97 42.761 37.301 -16.428 1.00 55.79 O ANISOU 1853 O GLU C 97 6813 8140 6244 -1141 865 746 O ATOM 1854 CB GLU C 97 43.430 34.135 -15.821 1.00 54.64 C ANISOU 1854 CB GLU C 97 6361 8250 6148 -576 953 320 C ATOM 1855 CG GLU C 97 44.367 33.402 -14.839 1.00 59.02 C ANISOU 1855 CG GLU C 97 6651 8919 6856 -379 961 136 C ATOM 1856 CD GLU C 97 44.994 32.104 -15.342 1.00 66.46 C ANISOU 1856 CD GLU C 97 7504 10025 7722 -182 1072 -60 C ATOM 1857 OE1 GLU C 97 45.168 31.933 -16.574 1.00 69.55 O ANISOU 1857 OE1 GLU C 97 7955 10544 7926 -259 1240 -87 O ATOM 1858 OE2 GLU C 97 45.342 31.255 -14.472 1.00 68.50 O ANISOU 1858 OE2 GLU C 97 7648 10274 8103 58 981 -196 O ATOM 1859 N LYS C 98 40.798 36.244 -16.234 1.00 53.40 N ANISOU 1859 N LYS C 98 6725 7586 5978 -838 598 738 N ATOM 1860 CA LYS C 98 40.062 37.247 -16.999 1.00 55.55 C ANISOU 1860 CA LYS C 98 7239 7704 6162 -996 491 917 C ATOM 1861 C LYS C 98 39.691 38.477 -16.155 1.00 55.54 C ANISOU 1861 C LYS C 98 7246 7506 6350 -1061 343 1012 C ATOM 1862 O LYS C 98 39.531 39.604 -16.670 1.00 57.78 O ANISOU 1862 O LYS C 98 7706 7666 6581 -1235 276 1167 O ATOM 1863 CB LYS C 98 38.812 36.631 -17.627 1.00 54.87 C ANISOU 1863 CB LYS C 98 7345 7509 5993 -882 345 931 C ATOM 1864 CG LYS C 98 39.115 35.352 -18.420 1.00 56.40 C ANISOU 1864 CG LYS C 98 7557 7871 6000 -804 478 816 C ATOM 1865 CD LYS C 98 40.295 35.527 -19.373 1.00 60.12 C ANISOU 1865 CD LYS C 98 8034 8553 6255 -980 715 821 C ATOM 1866 CE LYS C 98 40.713 34.200 -19.985 1.00 62.10 C ANISOU 1866 CE LYS C 98 8258 8984 6355 -862 869 652 C ATOM 1867 NZ LYS C 98 41.353 34.414 -21.311 1.00 66.67 N ANISOU 1867 NZ LYS C 98 8964 9727 6642 -1064 1069 680 N ATOM 1868 N GLY C 99 39.580 38.272 -14.857 1.00 53.20 N ANISOU 1868 N GLY C 99 6787 7166 6260 -925 289 916 N ATOM 1869 CA GLY C 99 39.069 39.311 -14.000 1.00 52.73 C ANISOU 1869 CA GLY C 99 6744 6909 6383 -949 145 967 C ATOM 1870 C GLY C 99 37.549 39.301 -13.959 1.00 51.31 C ANISOU 1870 C GLY C 99 6685 6533 6280 -822 -50 980 C ATOM 1871 O GLY C 99 36.884 38.507 -14.615 1.00 51.44 O ANISOU 1871 O GLY C 99 6776 6563 6205 -736 -86 961 O ATOM 1872 N GLY C 100 37.000 40.183 -13.143 1.00 50.79 N ANISOU 1872 N GLY C 100 6616 6287 6395 -808 -176 988 N ATOM 1873 CA GLY C 100 35.582 40.372 -13.099 1.00 48.92 C ANISOU 1873 CA GLY C 100 6451 5870 6266 -695 -362 977 C ATOM 1874 C GLY C 100 34.996 39.734 -11.893 1.00 46.65 C ANISOU 1874 C GLY C 100 6018 5576 6132 -551 -357 819 C ATOM 1875 O GLY C 100 34.017 40.245 -11.363 1.00 48.06 O ANISOU 1875 O GLY C 100 6183 5603 6474 -482 -477 771 O ATOM 1876 N LEU C 101 35.547 38.603 -11.441 1.00 44.12 N ANISOU 1876 N LEU C 101 5597 5409 5757 -501 -222 727 N ATOM 1877 CA LEU C 101 35.012 38.022 -10.214 1.00 39.45 C ANISOU 1877 CA LEU C 101 4918 4791 5279 -401 -213 591 C ATOM 1878 C LEU C 101 35.778 38.510 -8.992 1.00 38.02 C ANISOU 1878 C LEU C 101 4654 4611 5182 -434 -167 549 C ATOM 1879 O LEU C 101 35.177 38.772 -7.938 1.00 36.69 O ANISOU 1879 O LEU C 101 4457 4346 5136 -400 -197 465 O ATOM 1880 CB LEU C 101 34.937 36.484 -10.275 1.00 37.94 C ANISOU 1880 CB LEU C 101 4726 4702 4989 -316 -143 511 C ATOM 1881 CG LEU C 101 34.111 35.854 -9.134 1.00 35.60 C ANISOU 1881 CG LEU C 101 4399 4346 4780 -252 -139 385 C ATOM 1882 CD1 LEU C 101 32.675 36.433 -9.115 1.00 32.71 C ANISOU 1882 CD1 LEU C 101 4018 3854 4556 -245 -240 347 C ATOM 1883 CD2 LEU C 101 34.076 34.278 -9.155 1.00 33.52 C ANISOU 1883 CD2 LEU C 101 4187 4145 4404 -189 -80 314 C ATOM 1884 N GLU C 102 37.100 38.634 -9.138 1.00 37.61 N ANISOU 1884 N GLU C 102 4554 4678 5060 -509 -90 591 N ATOM 1885 CA GLU C 102 37.993 39.053 -8.033 1.00 36.47 C ANISOU 1885 CA GLU C 102 4315 4558 4985 -551 -66 545 C ATOM 1886 C GLU C 102 37.544 40.418 -7.485 1.00 36.10 C ANISOU 1886 C GLU C 102 4307 4332 5076 -621 -155 563 C ATOM 1887 O GLU C 102 37.517 41.401 -8.220 1.00 36.65 O ANISOU 1887 O GLU C 102 4453 4317 5157 -721 -204 669 O ATOM 1888 CB GLU C 102 39.468 39.118 -8.517 1.00 37.65 C ANISOU 1888 CB GLU C 102 4368 4882 5056 -649 25 580 C ATOM 1889 CG GLU C 102 40.514 39.532 -7.435 1.00 37.63 C ANISOU 1889 CG GLU C 102 4235 4932 5131 -702 25 520 C ATOM 1890 CD GLU C 102 40.656 38.453 -6.339 1.00 40.91 C ANISOU 1890 CD GLU C 102 4601 5393 5549 -543 3 395 C ATOM 1891 OE1 GLU C 102 40.276 37.292 -6.576 1.00 41.66 O ANISOU 1891 OE1 GLU C 102 4741 5518 5569 -412 23 360 O ATOM 1892 OE2 GLU C 102 41.144 38.738 -5.237 1.00 40.74 O ANISOU 1892 OE2 GLU C 102 4526 5363 5589 -554 -49 334 O ATOM 1893 N GLY C 103 37.175 40.459 -6.210 1.00 35.01 N ANISOU 1893 N GLY C 103 4148 4123 5030 -569 -177 456 N ATOM 1894 CA GLY C 103 36.778 41.706 -5.546 1.00 35.19 C ANISOU 1894 CA GLY C 103 4205 3974 5191 -613 -251 430 C ATOM 1895 C GLY C 103 35.337 42.151 -5.758 1.00 35.71 C ANISOU 1895 C GLY C 103 4328 3874 5366 -538 -334 403 C ATOM 1896 O GLY C 103 34.923 43.182 -5.228 1.00 36.66 O ANISOU 1896 O GLY C 103 4476 3835 5619 -541 -404 356 O ATOM 1897 N LEU C 104 34.574 41.383 -6.527 1.00 34.11 N ANISOU 1897 N LEU C 104 4133 3706 5120 -461 -340 414 N ATOM 1898 CA LEU C 104 33.159 41.629 -6.723 1.00 34.28 C ANISOU 1898 CA LEU C 104 4159 3604 5262 -369 -433 355 C ATOM 1899 C LEU C 104 32.401 41.412 -5.435 1.00 32.97 C ANISOU 1899 C LEU C 104 3916 3413 5198 -311 -373 169 C ATOM 1900 O LEU C 104 32.658 40.438 -4.720 1.00 31.91 O ANISOU 1900 O LEU C 104 3764 3387 4975 -321 -257 105 O ATOM 1901 CB LEU C 104 32.613 40.635 -7.765 1.00 34.16 C ANISOU 1901 CB LEU C 104 4154 3669 5157 -320 -444 388 C ATOM 1902 CG LEU C 104 31.221 40.928 -8.322 1.00 37.37 C ANISOU 1902 CG LEU C 104 4550 3964 5684 -229 -590 348 C ATOM 1903 CD1 LEU C 104 31.195 42.261 -9.087 1.00 39.76 C ANISOU 1903 CD1 LEU C 104 4965 4097 6043 -238 -770 469 C ATOM 1904 CD2 LEU C 104 30.683 39.798 -9.189 1.00 35.02 C ANISOU 1904 CD2 LEU C 104 4254 3761 5290 -196 -598 350 C ATOM 1905 N ILE C 105 31.445 42.294 -5.155 1.00 33.37 N ANISOU 1905 N ILE C 105 3937 3316 5426 -249 -454 74 N ATOM 1906 CA ILE C 105 30.610 42.162 -3.973 1.00 32.88 C ANISOU 1906 CA ILE C 105 3789 3242 5462 -207 -368 -133 C ATOM 1907 C ILE C 105 29.632 40.978 -4.185 1.00 32.84 C ANISOU 1907 C ILE C 105 3703 3338 5439 -172 -304 -217 C ATOM 1908 O ILE C 105 28.958 40.884 -5.230 1.00 32.12 O ANISOU 1908 O ILE C 105 3576 3232 5395 -113 -413 -183 O ATOM 1909 CB ILE C 105 29.826 43.479 -3.668 1.00 34.83 C ANISOU 1909 CB ILE C 105 3999 3305 5932 -125 -470 -249 C ATOM 1910 CG1 ILE C 105 30.778 44.581 -3.204 1.00 35.90 C ANISOU 1910 CG1 ILE C 105 4236 3325 6078 -190 -511 -198 C ATOM 1911 CG2 ILE C 105 28.654 43.263 -2.589 1.00 32.64 C ANISOU 1911 CG2 ILE C 105 3583 3045 5774 -72 -350 -518 C ATOM 1912 CD1 ILE C 105 30.132 46.002 -3.342 1.00 37.76 C ANISOU 1912 CD1 ILE C 105 4497 3320 6529 -92 -682 -255 C ATOM 1913 N TRP C 106 29.557 40.098 -3.189 1.00 32.45 N ANISOU 1913 N TRP C 106 3647 3376 5309 -226 -141 -326 N ATOM 1914 CA TRP C 106 28.664 38.947 -3.262 1.00 33.66 C ANISOU 1914 CA TRP C 106 3746 3612 5431 -241 -58 -413 C ATOM 1915 C TRP C 106 27.220 39.367 -3.131 1.00 35.57 C ANISOU 1915 C TRP C 106 3817 3815 5883 -188 -65 -605 C ATOM 1916 O TRP C 106 26.892 40.281 -2.354 1.00 37.79 O ANISOU 1916 O TRP C 106 4035 4024 6299 -157 -42 -741 O ATOM 1917 CB TRP C 106 28.978 37.928 -2.165 1.00 33.25 C ANISOU 1917 CB TRP C 106 3786 3632 5215 -338 113 -468 C ATOM 1918 CG TRP C 106 28.041 36.734 -2.183 1.00 33.55 C ANISOU 1918 CG TRP C 106 3802 3734 5211 -398 213 -559 C ATOM 1919 CD1 TRP C 106 28.200 35.588 -2.903 1.00 31.37 C ANISOU 1919 CD1 TRP C 106 3601 3510 4807 -416 201 -471 C ATOM 1920 CD2 TRP C 106 26.787 36.612 -1.499 1.00 34.97 C ANISOU 1920 CD2 TRP C 106 3870 3931 5484 -463 344 -769 C ATOM 1921 NE1 TRP C 106 27.148 34.747 -2.691 1.00 33.43 N ANISOU 1921 NE1 TRP C 106 3828 3804 5071 -504 304 -598 N ATOM 1922 CE2 TRP C 106 26.258 35.352 -1.833 1.00 36.81 C ANISOU 1922 CE2 TRP C 106 4126 4225 5635 -546 405 -784 C ATOM 1923 CE3 TRP C 106 26.060 37.449 -0.639 1.00 38.70 C ANISOU 1923 CE3 TRP C 106 4219 4378 6105 -467 428 -965 C ATOM 1924 CZ2 TRP C 106 25.023 34.891 -1.328 1.00 38.54 C ANISOU 1924 CZ2 TRP C 106 4237 4493 5915 -665 559 -984 C ATOM 1925 CZ3 TRP C 106 24.842 36.997 -0.127 1.00 39.85 C ANISOU 1925 CZ3 TRP C 106 4240 4588 6312 -564 595 -1179 C ATOM 1926 CH2 TRP C 106 24.333 35.722 -0.482 1.00 41.51 C ANISOU 1926 CH2 TRP C 106 4464 4872 6437 -677 663 -1183 C ATOM 1927 N SER C 107 26.366 38.710 -3.904 1.00 35.45 N ANISOU 1927 N SER C 107 3714 3850 5904 -172 -103 -635 N ATOM 1928 CA SER C 107 24.931 38.711 -3.658 1.00 37.88 C ANISOU 1928 CA SER C 107 3812 4180 6400 -153 -65 -864 C ATOM 1929 C SER C 107 24.383 37.374 -4.154 1.00 37.85 C ANISOU 1929 C SER C 107 3783 4283 6315 -238 -17 -879 C ATOM 1930 O SER C 107 25.000 36.731 -5.018 1.00 37.12 O ANISOU 1930 O SER C 107 3826 4210 6067 -247 -90 -704 O ATOM 1931 CB SER C 107 24.231 39.874 -4.378 1.00 39.12 C ANISOU 1931 CB SER C 107 3828 4231 6804 16 -292 -910 C ATOM 1932 OG SER C 107 24.219 39.641 -5.782 1.00 39.37 O ANISOU 1932 OG SER C 107 3905 4256 6800 67 -492 -755 O ATOM 1933 N GLN C 108 23.231 36.971 -3.617 1.00 39.17 N ANISOU 1933 N GLN C 108 3775 4521 6588 -310 114 -1105 N ATOM 1934 CA GLN C 108 22.538 35.753 -4.040 1.00 40.00 C ANISOU 1934 CA GLN C 108 3833 4717 6646 -421 161 -1155 C ATOM 1935 C GLN C 108 22.325 35.779 -5.553 1.00 39.60 C ANISOU 1935 C GLN C 108 3745 4650 6651 -309 -100 -1052 C ATOM 1936 O GLN C 108 22.607 34.808 -6.252 1.00 37.46 O ANISOU 1936 O GLN C 108 3605 4410 6217 -368 -130 -938 O ATOM 1937 CB GLN C 108 21.187 35.615 -3.313 1.00 41.91 C ANISOU 1937 CB GLN C 108 3820 5046 7058 -520 329 -1452 C ATOM 1938 CG GLN C 108 20.534 34.237 -3.435 1.00 44.98 C ANISOU 1938 CG GLN C 108 4195 5531 7364 -718 447 -1522 C ATOM 1939 CD GLN C 108 21.442 33.081 -3.010 1.00 46.56 C ANISOU 1939 CD GLN C 108 4733 5712 7247 -880 587 -1365 C ATOM 1940 OE1 GLN C 108 21.979 33.050 -1.898 1.00 49.24 O ANISOU 1940 OE1 GLN C 108 5234 6028 7447 -964 757 -1359 O ATOM 1941 NE2 GLN C 108 21.593 32.116 -3.890 1.00 46.03 N ANISOU 1941 NE2 GLN C 108 4786 5642 7063 -916 498 -1250 N ATOM 1942 N ARG C 109 21.849 36.920 -6.028 1.00 41.16 N ANISOU 1942 N ARG C 109 3790 4781 7067 -141 -301 -1096 N ATOM 1943 CA ARG C 109 21.560 37.156 -7.428 1.00 43.00 C ANISOU 1943 CA ARG C 109 4007 4973 7357 -19 -592 -1005 C ATOM 1944 C ARG C 109 22.815 36.935 -8.304 1.00 41.08 C ANISOU 1944 C ARG C 109 4058 4692 6857 -24 -674 -716 C ATOM 1945 O ARG C 109 22.766 36.175 -9.277 1.00 41.72 O ANISOU 1945 O ARG C 109 4215 4815 6822 -53 -762 -639 O ATOM 1946 CB ARG C 109 20.908 38.550 -7.557 1.00 45.40 C ANISOU 1946 CB ARG C 109 4138 5169 7942 180 -803 -1107 C ATOM 1947 CG ARG C 109 20.798 39.179 -8.933 1.00 50.68 C ANISOU 1947 CG ARG C 109 4872 5729 8656 339 -1162 -969 C ATOM 1948 CD ARG C 109 20.206 38.254 -9.972 1.00 58.82 C ANISOU 1948 CD ARG C 109 5870 6845 9636 304 -1295 -964 C ATOM 1949 NE ARG C 109 19.426 39.004 -10.960 1.00 66.75 N ANISOU 1949 NE ARG C 109 6791 7754 10819 494 -1669 -984 N ATOM 1950 CZ ARG C 109 18.704 38.444 -11.931 1.00 70.28 C ANISOU 1950 CZ ARG C 109 7173 8254 11277 506 -1872 -1014 C ATOM 1951 NH1 ARG C 109 18.670 37.109 -12.070 1.00 69.22 N ANISOU 1951 NH1 ARG C 109 7054 8262 10983 325 -1720 -1028 N ATOM 1952 NH2 ARG C 109 18.020 39.225 -12.769 1.00 72.87 N ANISOU 1952 NH2 ARG C 109 7445 8473 11771 703 -2253 -1031 N ATOM 1953 N ARG C 110 23.946 37.538 -7.934 1.00 39.74 N ANISOU 1953 N ARG C 110 4046 4460 6593 -14 -625 -578 N ATOM 1954 CA ARG C 110 25.203 37.350 -8.673 1.00 37.55 C ANISOU 1954 CA ARG C 110 4006 4179 6083 -37 -657 -337 C ATOM 1955 C ARG C 110 25.710 35.917 -8.612 1.00 35.37 C ANISOU 1955 C ARG C 110 3839 4008 5591 -147 -496 -304 C ATOM 1956 O ARG C 110 26.277 35.415 -9.580 1.00 34.18 O ANISOU 1956 O ARG C 110 3828 3887 5272 -152 -549 -170 O ATOM 1957 CB ARG C 110 26.288 38.290 -8.146 1.00 37.63 C ANISOU 1957 CB ARG C 110 4116 4118 6065 -30 -620 -234 C ATOM 1958 CG ARG C 110 26.053 39.744 -8.543 1.00 41.09 C ANISOU 1958 CG ARG C 110 4546 4403 6663 79 -830 -199 C ATOM 1959 CD ARG C 110 27.068 40.668 -7.927 1.00 42.67 C ANISOU 1959 CD ARG C 110 4844 4523 6848 53 -784 -120 C ATOM 1960 NE ARG C 110 27.040 41.965 -8.598 1.00 48.21 N ANISOU 1960 NE ARG C 110 5630 5048 7642 130 -1012 -24 N ATOM 1961 CZ ARG C 110 27.690 43.052 -8.180 1.00 51.24 C ANISOU 1961 CZ ARG C 110 6101 5303 8064 114 -1033 30 C ATOM 1962 NH1 ARG C 110 28.421 43.025 -7.061 1.00 47.36 N ANISOU 1962 NH1 ARG C 110 5600 4859 7536 33 -846 -16 N ATOM 1963 NH2 ARG C 110 27.582 44.184 -8.876 1.00 53.20 N ANISOU 1963 NH2 ARG C 110 6471 5358 8386 176 -1265 129 N ATOM 1964 N GLN C 111 25.512 35.258 -7.477 1.00 34.55 N ANISOU 1964 N GLN C 111 3698 3948 5481 -237 -300 -430 N ATOM 1965 CA GLN C 111 25.930 33.872 -7.341 1.00 34.03 C ANISOU 1965 CA GLN C 111 3773 3940 5217 -334 -171 -405 C ATOM 1966 C GLN C 111 25.154 33.012 -8.333 1.00 34.96 C ANISOU 1966 C GLN C 111 3876 4094 5315 -363 -254 -438 C ATOM 1967 O GLN C 111 25.736 32.139 -9.009 1.00 34.60 O ANISOU 1967 O GLN C 111 3992 4067 5085 -374 -264 -343 O ATOM 1968 CB GLN C 111 25.747 33.385 -5.896 1.00 33.92 C ANISOU 1968 CB GLN C 111 3768 3937 5184 -448 38 -531 C ATOM 1969 CG GLN C 111 26.215 31.928 -5.579 1.00 35.61 C ANISOU 1969 CG GLN C 111 4188 4162 5178 -549 154 -498 C ATOM 1970 CD GLN C 111 25.980 31.567 -4.106 1.00 40.07 C ANISOU 1970 CD GLN C 111 4812 4715 5699 -685 347 -610 C ATOM 1971 OE1 GLN C 111 26.516 32.216 -3.198 1.00 41.55 O ANISOU 1971 OE1 GLN C 111 5027 4881 5879 -670 400 -607 O ATOM 1972 NE2 GLN C 111 25.136 30.585 -3.865 1.00 40.23 N ANISOU 1972 NE2 GLN C 111 4859 4745 5683 -842 453 -715 N ATOM 1973 N GLU C 112 23.855 33.287 -8.436 1.00 36.47 N ANISOU 1973 N GLU C 112 3858 4296 5704 -365 -324 -590 N ATOM 1974 CA GLU C 112 22.952 32.493 -9.257 1.00 38.73 C ANISOU 1974 CA GLU C 112 4087 4623 6003 -415 -413 -663 C ATOM 1975 C GLU C 112 23.225 32.734 -10.729 1.00 38.62 C ANISOU 1975 C GLU C 112 4170 4588 5915 -311 -650 -517 C ATOM 1976 O GLU C 112 23.144 31.812 -11.541 1.00 38.29 O ANISOU 1976 O GLU C 112 4229 4574 5743 -357 -702 -495 O ATOM 1977 CB GLU C 112 21.488 32.812 -8.934 1.00 41.09 C ANISOU 1977 CB GLU C 112 4082 4962 6570 -438 -436 -896 C ATOM 1978 CG GLU C 112 21.037 32.295 -7.562 1.00 44.58 C ANISOU 1978 CG GLU C 112 4444 5453 7042 -611 -157 -1072 C ATOM 1979 CD GLU C 112 19.585 32.685 -7.195 1.00 51.67 C ANISOU 1979 CD GLU C 112 4981 6424 8227 -640 -138 -1347 C ATOM 1980 OE1 GLU C 112 18.960 33.565 -7.847 1.00 52.73 O ANISOU 1980 OE1 GLU C 112 4904 6549 8581 -474 -368 -1412 O ATOM 1981 OE2 GLU C 112 19.077 32.094 -6.223 1.00 55.34 O ANISOU 1981 OE2 GLU C 112 5381 6954 8693 -835 111 -1510 O ATOM 1982 N ILE C 113 23.569 33.968 -11.077 1.00 38.72 N ANISOU 1982 N ILE C 113 4185 4539 5988 -186 -791 -416 N ATOM 1983 CA ILE C 113 23.935 34.212 -12.455 1.00 39.69 C ANISOU 1983 CA ILE C 113 4462 4635 5985 -121 -994 -254 C ATOM 1984 C ILE C 113 25.215 33.479 -12.824 1.00 37.52 C ANISOU 1984 C ILE C 113 4425 4401 5430 -170 -873 -107 C ATOM 1985 O ILE C 113 25.340 32.988 -13.930 1.00 37.99 O ANISOU 1985 O ILE C 113 4621 4486 5330 -175 -963 -39 O ATOM 1986 CB ILE C 113 24.080 35.699 -12.784 1.00 41.00 C ANISOU 1986 CB ILE C 113 4639 4694 6244 -4 -1176 -155 C ATOM 1987 CG1 ILE C 113 22.693 36.350 -12.872 1.00 44.02 C ANISOU 1987 CG1 ILE C 113 4798 5023 6903 99 -1396 -308 C ATOM 1988 CG2 ILE C 113 24.790 35.865 -14.135 1.00 41.20 C ANISOU 1988 CG2 ILE C 113 4912 4695 6046 5 -1318 54 C ATOM 1989 CD1 ILE C 113 22.771 37.848 -12.577 1.00 44.94 C ANISOU 1989 CD1 ILE C 113 4892 5001 7183 223 -1513 -276 C ATOM 1990 N LEU C 114 26.162 33.422 -11.902 1.00 35.76 N ANISOU 1990 N LEU C 114 4246 4191 5151 -195 -679 -74 N ATOM 1991 CA LEU C 114 27.393 32.718 -12.151 1.00 34.64 C ANISOU 1991 CA LEU C 114 4281 4099 4781 -212 -567 27 C ATOM 1992 C LEU C 114 27.115 31.231 -12.339 1.00 34.75 C ANISOU 1992 C LEU C 114 4374 4147 4683 -266 -510 -51 C ATOM 1993 O LEU C 114 27.678 30.623 -13.255 1.00 35.10 O ANISOU 1993 O LEU C 114 4567 4227 4543 -252 -523 11 O ATOM 1994 CB LEU C 114 28.373 32.947 -11.012 1.00 33.66 C ANISOU 1994 CB LEU C 114 4159 3978 4653 -216 -408 49 C ATOM 1995 CG LEU C 114 29.827 32.575 -11.277 1.00 35.29 C ANISOU 1995 CG LEU C 114 4492 4246 4670 -198 -322 151 C ATOM 1996 CD1 LEU C 114 30.441 33.458 -12.408 1.00 32.35 C ANISOU 1996 CD1 LEU C 114 4176 3895 4222 -187 -404 293 C ATOM 1997 CD2 LEU C 114 30.610 32.685 -9.956 1.00 35.69 C ANISOU 1997 CD2 LEU C 114 4518 4297 4747 -199 -200 134 C ATOM 1998 N ASP C 115 26.227 30.669 -11.504 1.00 33.91 N ANISOU 1998 N ASP C 115 4178 4027 4681 -343 -441 -194 N ATOM 1999 CA ASP C 115 25.774 29.295 -11.644 1.00 34.50 C ANISOU 1999 CA ASP C 115 4337 4102 4668 -432 -401 -279 C ATOM 2000 C ASP C 115 25.136 29.056 -13.016 1.00 35.73 C ANISOU 2000 C ASP C 115 4510 4276 4788 -428 -583 -287 C ATOM 2001 O ASP C 115 25.352 28.008 -13.624 1.00 35.76 O ANISOU 2001 O ASP C 115 4680 4280 4626 -455 -580 -289 O ATOM 2002 CB ASP C 115 24.727 28.937 -10.562 1.00 35.71 C ANISOU 2002 CB ASP C 115 4366 4243 4959 -565 -296 -443 C ATOM 2003 CG ASP C 115 25.336 28.711 -9.170 1.00 36.79 C ANISOU 2003 CG ASP C 115 4585 4348 5047 -612 -102 -446 C ATOM 2004 OD1 ASP C 115 26.562 28.467 -9.027 1.00 36.90 O ANISOU 2004 OD1 ASP C 115 4768 4343 4911 -542 -60 -339 O ATOM 2005 OD2 ASP C 115 24.559 28.805 -8.194 1.00 41.76 O ANISOU 2005 OD2 ASP C 115 5100 4978 5790 -723 5 -570 O ATOM 2006 N LEU C 116 24.333 30.011 -13.478 1.00 36.14 N ANISOU 2006 N LEU C 116 4404 4330 4997 -386 -760 -305 N ATOM 2007 CA LEU C 116 23.620 29.879 -14.738 1.00 38.64 C ANISOU 2007 CA LEU C 116 4734 4657 5291 -378 -981 -320 C ATOM 2008 C LEU C 116 24.605 29.943 -15.900 1.00 38.00 C ANISOU 2008 C LEU C 116 4890 4583 4964 -316 -1047 -155 C ATOM 2009 O LEU C 116 24.453 29.222 -16.877 1.00 38.64 O ANISOU 2009 O LEU C 116 5106 4681 4895 -343 -1136 -165 O ATOM 2010 CB LEU C 116 22.627 31.017 -14.887 1.00 40.82 C ANISOU 2010 CB LEU C 116 4792 4913 5804 -307 -1191 -372 C ATOM 2011 CG LEU C 116 21.188 30.898 -15.392 1.00 46.22 C ANISOU 2011 CG LEU C 116 5288 5618 6655 -324 -1409 -528 C ATOM 2012 CD1 LEU C 116 20.918 32.106 -16.300 1.00 49.87 C ANISOU 2012 CD1 LEU C 116 5742 6023 7185 -172 -1723 -445 C ATOM 2013 CD2 LEU C 116 20.828 29.587 -16.109 1.00 48.10 C ANISOU 2013 CD2 LEU C 116 5631 5893 6752 -439 -1447 -592 C ATOM 2014 N TRP C 117 25.636 30.771 -15.770 1.00 36.19 N ANISOU 2014 N TRP C 117 4717 4349 4683 -255 -984 -19 N ATOM 2015 CA TRP C 117 26.615 30.922 -16.838 1.00 36.87 C ANISOU 2015 CA TRP C 117 5011 4465 4533 -230 -1003 127 C ATOM 2016 C TRP C 117 27.397 29.617 -17.004 1.00 36.72 C ANISOU 2016 C TRP C 117 5143 4501 4306 -250 -837 97 C ATOM 2017 O TRP C 117 27.564 29.114 -18.121 1.00 38.04 O ANISOU 2017 O TRP C 117 5480 4702 4273 -257 -887 114 O ATOM 2018 CB TRP C 117 27.508 32.150 -16.599 1.00 35.51 C ANISOU 2018 CB TRP C 117 4841 4278 4374 -198 -959 264 C ATOM 2019 CG TRP C 117 28.697 32.248 -17.486 1.00 35.59 C ANISOU 2019 CG TRP C 117 5040 4349 4134 -216 -892 396 C ATOM 2020 CD1 TRP C 117 28.726 32.651 -18.809 1.00 37.64 C ANISOU 2020 CD1 TRP C 117 5481 4607 4214 -243 -1029 504 C ATOM 2021 CD2 TRP C 117 30.057 32.002 -17.113 1.00 33.15 C ANISOU 2021 CD2 TRP C 117 4753 4120 3721 -221 -666 425 C ATOM 2022 NE1 TRP C 117 30.022 32.633 -19.271 1.00 35.78 N ANISOU 2022 NE1 TRP C 117 5371 4462 3760 -287 -858 588 N ATOM 2023 CE2 TRP C 117 30.853 32.232 -18.249 1.00 34.29 C ANISOU 2023 CE2 TRP C 117 5060 4332 3634 -263 -640 530 C ATOM 2024 CE3 TRP C 117 30.677 31.607 -15.919 1.00 34.60 C ANISOU 2024 CE3 TRP C 117 4835 4328 3982 -195 -493 364 C ATOM 2025 CZ2 TRP C 117 32.242 32.067 -18.235 1.00 35.79 C ANISOU 2025 CZ2 TRP C 117 5263 4638 3698 -277 -427 550 C ATOM 2026 CZ3 TRP C 117 32.068 31.449 -15.900 1.00 35.53 C ANISOU 2026 CZ3 TRP C 117 4978 4543 3980 -183 -327 395 C ATOM 2027 CH2 TRP C 117 32.828 31.672 -17.059 1.00 36.30 C ANISOU 2027 CH2 TRP C 117 5188 4730 3877 -222 -286 475 C ATOM 2028 N ILE C 118 27.801 29.029 -15.882 1.00 35.49 N ANISOU 2028 N ILE C 118 4946 4341 4198 -254 -658 37 N ATOM 2029 CA ILE C 118 28.499 27.754 -15.908 1.00 34.97 C ANISOU 2029 CA ILE C 118 5029 4291 3968 -241 -530 -10 C ATOM 2030 C ILE C 118 27.621 26.598 -16.421 1.00 36.32 C ANISOU 2030 C ILE C 118 5294 4423 4081 -303 -604 -122 C ATOM 2031 O ILE C 118 28.111 25.743 -17.166 1.00 37.94 O ANISOU 2031 O ILE C 118 5679 4641 4095 -276 -580 -144 O ATOM 2032 CB ILE C 118 29.163 27.474 -14.560 1.00 34.07 C ANISOU 2032 CB ILE C 118 4881 4154 3910 -217 -369 -32 C ATOM 2033 CG1 ILE C 118 30.333 28.446 -14.388 1.00 34.08 C ANISOU 2033 CG1 ILE C 118 4827 4218 3904 -154 -302 74 C ATOM 2034 CG2 ILE C 118 29.650 26.020 -14.457 1.00 31.65 C ANISOU 2034 CG2 ILE C 118 4747 3812 3467 -187 -286 -106 C ATOM 2035 CD1 ILE C 118 30.840 28.616 -12.912 1.00 34.58 C ANISOU 2035 CD1 ILE C 118 4812 4256 4072 -137 -198 63 C ATOM 2036 N TYR C 119 26.334 26.610 -16.068 1.00 36.26 N ANISOU 2036 N TYR C 119 5157 4376 4243 -391 -692 -209 N ATOM 2037 CA TYR C 119 25.347 25.669 -16.573 1.00 36.48 C ANISOU 2037 CA TYR C 119 5233 4374 4252 -488 -788 -326 C ATOM 2038 C TYR C 119 25.166 25.832 -18.066 1.00 38.10 C ANISOU 2038 C TYR C 119 5537 4616 4323 -461 -979 -291 C ATOM 2039 O TYR C 119 25.115 24.850 -18.791 1.00 39.21 O ANISOU 2039 O TYR C 119 5852 4743 4304 -496 -1012 -350 O ATOM 2040 CB TYR C 119 24.000 25.929 -15.898 1.00 37.52 C ANISOU 2040 CB TYR C 119 5127 4497 4633 -593 -842 -439 C ATOM 2041 CG TYR C 119 22.843 25.033 -16.332 1.00 37.95 C ANISOU 2041 CG TYR C 119 5169 4537 4715 -733 -947 -585 C ATOM 2042 CD1 TYR C 119 22.712 23.737 -15.834 1.00 40.19 C ANISOU 2042 CD1 TYR C 119 5578 4753 4938 -870 -820 -678 C ATOM 2043 CD2 TYR C 119 21.864 25.494 -17.197 1.00 40.70 C ANISOU 2043 CD2 TYR C 119 5384 4925 5153 -736 -1191 -633 C ATOM 2044 CE1 TYR C 119 21.643 22.901 -16.218 1.00 41.12 C ANISOU 2044 CE1 TYR C 119 5686 4854 5084 -1037 -911 -822 C ATOM 2045 CE2 TYR C 119 20.784 24.661 -17.595 1.00 42.21 C ANISOU 2045 CE2 TYR C 119 5536 5118 5385 -881 -1304 -788 C ATOM 2046 CZ TYR C 119 20.695 23.375 -17.100 1.00 43.78 C ANISOU 2046 CZ TYR C 119 5854 5259 5522 -1044 -1149 -882 C ATOM 2047 OH TYR C 119 19.641 22.561 -17.469 1.00 50.59 O ANISOU 2047 OH TYR C 119 6678 6117 6426 -1221 -1252 -1040 O ATOM 2048 N HIS C 120 25.050 27.067 -18.535 1.00 38.11 N ANISOU 2048 N HIS C 120 5461 4647 4374 -406 -1119 -195 N ATOM 2049 CA AHIS C 120 24.813 27.270 -19.948 0.50 40.01 C ANISOU 2049 CA AHIS C 120 5836 4905 4460 -395 -1330 -149 C ATOM 2050 CA BHIS C 120 24.833 27.332 -19.962 0.50 39.18 C ANISOU 2050 CA BHIS C 120 5731 4801 4355 -391 -1333 -142 C ATOM 2051 C HIS C 120 26.038 26.992 -20.825 1.00 39.55 C ANISOU 2051 C HIS C 120 6038 4895 4093 -359 -1228 -62 C ATOM 2052 O HIS C 120 25.890 26.466 -21.931 1.00 41.69 O ANISOU 2052 O HIS C 120 6496 5180 4164 -385 -1332 -88 O ATOM 2053 CB AHIS C 120 24.143 28.616 -20.206 0.50 41.35 C ANISOU 2053 CB AHIS C 120 5878 5054 4778 -349 -1563 -82 C ATOM 2054 CB BHIS C 120 24.444 28.786 -20.215 0.50 39.53 C ANISOU 2054 CB BHIS C 120 5676 4826 4517 -335 -1532 -43 C ATOM 2055 CG AHIS C 120 22.673 28.601 -19.905 0.50 44.23 C ANISOU 2055 CG AHIS C 120 6002 5399 5404 -382 -1740 -233 C ATOM 2056 CG BHIS C 120 23.940 29.035 -21.605 0.50 40.22 C ANISOU 2056 CG BHIS C 120 5913 4905 4463 -331 -1817 1 C ATOM 2057 ND1AHIS C 120 21.856 27.543 -20.254 0.50 46.05 N ANISOU 2057 ND1AHIS C 120 6231 5642 5624 -478 -1822 -381 N ATOM 2058 ND1BHIS C 120 24.649 29.758 -22.538 0.50 39.37 N ANISOU 2058 ND1BHIS C 120 6030 4798 4130 -308 -1878 171 N ATOM 2059 CD2AHIS C 120 21.875 29.506 -19.291 0.50 44.35 C ANISOU 2059 CD2AHIS C 120 5752 5392 5708 -336 -1845 -285 C ATOM 2060 CD2BHIS C 120 22.793 28.655 -22.215 0.50 39.84 C ANISOU 2060 CD2BHIS C 120 5836 4846 4455 -363 -2070 -105 C ATOM 2061 CE1AHIS C 120 20.616 27.802 -19.875 0.50 48.22 C ANISOU 2061 CE1AHIS C 120 6223 5923 6177 -503 -1963 -518 C ATOM 2062 CE1BHIS C 120 23.959 29.814 -23.664 0.50 41.34 C ANISOU 2062 CE1BHIS C 120 6417 5026 4266 -318 -2166 180 C ATOM 2063 NE2AHIS C 120 20.601 28.988 -19.291 0.50 48.25 N ANISOU 2063 NE2AHIS C 120 6056 5908 6368 -403 -1978 -471 N ATOM 2064 NE2BHIS C 120 22.829 29.156 -23.493 0.50 41.79 N ANISOU 2064 NE2BHIS C 120 6309 5078 4492 -340 -2301 9 N ATOM 2065 N THR C 121 27.228 27.300 -20.319 1.00 37.40 N ANISOU 2065 N THR C 121 5767 4659 3785 -307 -1021 16 N ATOM 2066 CA THR C 121 28.455 27.125 -21.098 1.00 37.42 C ANISOU 2066 CA THR C 121 5959 4740 3520 -277 -888 72 C ATOM 2067 C THR C 121 29.000 25.717 -21.008 1.00 36.88 C ANISOU 2067 C THR C 121 5997 4678 3337 -241 -731 -54 C ATOM 2068 O THR C 121 29.549 25.201 -21.993 1.00 38.15 O ANISOU 2068 O THR C 121 6346 4895 3255 -224 -684 -84 O ATOM 2069 CB THR C 121 29.576 28.111 -20.694 1.00 36.61 C ANISOU 2069 CB THR C 121 5787 4695 3430 -247 -739 194 C ATOM 2070 OG1 THR C 121 29.827 28.009 -19.280 1.00 35.83 O ANISOU 2070 OG1 THR C 121 5514 4568 3531 -207 -612 154 O ATOM 2071 CG2 THR C 121 29.176 29.546 -21.029 1.00 36.73 C ANISOU 2071 CG2 THR C 121 5782 4675 3500 -283 -909 337 C ATOM 2072 N GLN C 122 28.843 25.086 -19.844 1.00 35.28 N ANISOU 2072 N GLN C 122 5703 4406 3296 -230 -655 -134 N ATOM 2073 CA GLN C 122 29.503 23.795 -19.592 1.00 34.88 C ANISOU 2073 CA GLN C 122 5779 4321 3152 -167 -518 -240 C ATOM 2074 C GLN C 122 28.572 22.661 -19.149 1.00 35.35 C ANISOU 2074 C GLN C 122 5904 4250 3277 -242 -573 -364 C ATOM 2075 O GLN C 122 29.008 21.507 -19.029 1.00 35.59 O ANISOU 2075 O GLN C 122 6098 4207 3219 -193 -500 -455 O ATOM 2076 CB GLN C 122 30.663 23.963 -18.593 1.00 33.02 C ANISOU 2076 CB GLN C 122 5453 4112 2981 -66 -345 -209 C ATOM 2077 CG GLN C 122 31.792 24.918 -19.028 1.00 33.46 C ANISOU 2077 CG GLN C 122 5447 4311 2957 -14 -247 -114 C ATOM 2078 CD GLN C 122 32.691 24.342 -20.120 1.00 38.05 C ANISOU 2078 CD GLN C 122 6173 4988 3295 53 -147 -178 C ATOM 2079 OE1 GLN C 122 33.756 23.777 -19.833 1.00 38.84 O ANISOU 2079 OE1 GLN C 122 6262 5131 3366 177 -6 -256 O ATOM 2080 NE2 GLN C 122 32.267 24.484 -21.379 1.00 37.76 N ANISOU 2080 NE2 GLN C 122 6274 4990 3081 -21 -228 -160 N ATOM 2081 N GLY C 123 27.306 22.977 -18.891 1.00 35.41 N ANISOU 2081 N GLY C 123 5784 4223 3448 -365 -701 -379 N ATOM 2082 CA GLY C 123 26.338 21.945 -18.488 1.00 36.51 C ANISOU 2082 CA GLY C 123 5966 4253 3654 -494 -737 -505 C ATOM 2083 C GLY C 123 26.373 21.464 -17.038 1.00 36.40 C ANISOU 2083 C GLY C 123 5932 4143 3755 -541 -599 -536 C ATOM 2084 O GLY C 123 25.618 20.555 -16.666 1.00 37.00 O ANISOU 2084 O GLY C 123 6080 4115 3861 -686 -603 -636 O ATOM 2085 N TYR C 124 27.230 22.051 -16.201 1.00 35.49 N ANISOU 2085 N TYR C 124 5740 4054 3689 -443 -481 -453 N ATOM 2086 CA TYR C 124 27.238 21.653 -14.786 1.00 35.79 C ANISOU 2086 CA TYR C 124 5793 3995 3809 -498 -370 -473 C ATOM 2087 C TYR C 124 25.965 22.044 -14.018 1.00 36.08 C ANISOU 2087 C TYR C 124 5641 4029 4039 -683 -370 -522 C ATOM 2088 O TYR C 124 25.630 23.231 -13.920 1.00 35.55 O ANISOU 2088 O TYR C 124 5338 4053 4116 -672 -402 -486 O ATOM 2089 CB TYR C 124 28.511 22.154 -14.075 1.00 34.97 C ANISOU 2089 CB TYR C 124 5662 3924 3701 -344 -268 -385 C ATOM 2090 CG TYR C 124 29.762 21.544 -14.670 1.00 34.33 C ANISOU 2090 CG TYR C 124 5744 3848 3452 -165 -241 -389 C ATOM 2091 CD1 TYR C 124 30.017 20.181 -14.526 1.00 33.21 C ANISOU 2091 CD1 TYR C 124 5852 3560 3205 -127 -233 -470 C ATOM 2092 CD2 TYR C 124 30.681 22.329 -15.396 1.00 33.32 C ANISOU 2092 CD2 TYR C 124 5523 3867 3269 -40 -217 -327 C ATOM 2093 CE1 TYR C 124 31.155 19.600 -15.060 1.00 35.46 C ANISOU 2093 CE1 TYR C 124 6263 3851 3359 70 -210 -512 C ATOM 2094 CE2 TYR C 124 31.823 21.748 -15.972 1.00 33.83 C ANISOU 2094 CE2 TYR C 124 5698 3967 3187 120 -162 -370 C ATOM 2095 CZ TYR C 124 32.052 20.374 -15.792 1.00 36.53 C ANISOU 2095 CZ TYR C 124 6261 4168 3451 195 -163 -475 C ATOM 2096 OH TYR C 124 33.160 19.757 -16.341 1.00 38.50 O ANISOU 2096 OH TYR C 124 6602 4448 3579 386 -114 -556 O ATOM 2097 N PHE C 125 25.261 21.041 -13.490 1.00 37.25 N ANISOU 2097 N PHE C 125 5898 4066 4189 -859 -329 -616 N ATOM 2098 CA PHE C 125 24.144 21.270 -12.563 1.00 38.64 C ANISOU 2098 CA PHE C 125 5899 4249 4535 -1065 -264 -692 C ATOM 2099 C PHE C 125 24.539 22.345 -11.518 1.00 36.93 C ANISOU 2099 C PHE C 125 5521 4087 4423 -999 -163 -627 C ATOM 2100 O PHE C 125 25.606 22.250 -10.924 1.00 36.46 O ANISOU 2100 O PHE C 125 5606 3977 4270 -891 -92 -546 O ATOM 2101 CB PHE C 125 23.766 19.981 -11.797 1.00 40.44 C ANISOU 2101 CB PHE C 125 6355 4320 4689 -1277 -162 -767 C ATOM 2102 CG PHE C 125 23.480 18.756 -12.665 1.00 45.18 C ANISOU 2102 CG PHE C 125 7183 4816 5167 -1361 -249 -839 C ATOM 2103 CD1 PHE C 125 22.455 18.757 -13.620 1.00 50.07 C ANISOU 2103 CD1 PHE C 125 7657 5509 5860 -1470 -378 -938 C ATOM 2104 CD2 PHE C 125 24.177 17.556 -12.449 1.00 48.62 C ANISOU 2104 CD2 PHE C 125 7996 5058 5421 -1339 -220 -823 C ATOM 2105 CE1 PHE C 125 22.160 17.594 -14.388 1.00 51.52 C ANISOU 2105 CE1 PHE C 125 8070 5585 5923 -1572 -465 -1020 C ATOM 2106 CE2 PHE C 125 23.899 16.393 -13.209 1.00 50.50 C ANISOU 2106 CE2 PHE C 125 8476 5168 5543 -1422 -302 -905 C ATOM 2107 CZ PHE C 125 22.886 16.420 -14.182 1.00 51.67 C ANISOU 2107 CZ PHE C 125 8476 5401 5755 -1551 -417 -1004 C ATOM 2108 N PRO C 126 23.687 23.361 -11.285 1.00 36.95 N ANISOU 2108 N PRO C 126 5224 4187 4626 -1051 -173 -678 N ATOM 2109 CA PRO C 126 24.044 24.386 -10.294 1.00 35.57 C ANISOU 2109 CA PRO C 126 4917 4050 4546 -991 -80 -634 C ATOM 2110 C PRO C 126 23.758 23.939 -8.837 1.00 36.67 C ANISOU 2110 C PRO C 126 5124 4128 4681 -1173 112 -699 C ATOM 2111 O PRO C 126 22.857 24.479 -8.183 1.00 37.49 O ANISOU 2111 O PRO C 126 5009 4292 4945 -1295 196 -808 O ATOM 2112 CB PRO C 126 23.147 25.565 -10.683 1.00 35.01 C ANISOU 2112 CB PRO C 126 4521 4083 4697 -965 -185 -692 C ATOM 2113 CG PRO C 126 21.928 24.947 -11.272 1.00 37.66 C ANISOU 2113 CG PRO C 126 4769 4440 5101 -1115 -265 -830 C ATOM 2114 CD PRO C 126 22.316 23.562 -11.809 1.00 38.46 C ANISOU 2114 CD PRO C 126 5179 4450 4982 -1170 -274 -806 C ATOM 2115 N ASP C 127 24.530 22.981 -8.331 1.00 36.51 N ANISOU 2115 N ASP C 127 5415 3984 4472 -1184 177 -641 N ATOM 2116 CA ASP C 127 24.322 22.452 -6.972 1.00 37.78 C ANISOU 2116 CA ASP C 127 5733 4055 4567 -1377 343 -678 C ATOM 2117 C ASP C 127 25.618 22.468 -6.181 1.00 37.16 C ANISOU 2117 C ASP C 127 5864 3900 4355 -1234 362 -560 C ATOM 2118 O ASP C 127 25.688 21.911 -5.085 1.00 38.37 O ANISOU 2118 O ASP C 127 6246 3942 4390 -1363 461 -557 O ATOM 2119 CB ASP C 127 23.728 21.009 -7.021 1.00 39.10 C ANISOU 2119 CB ASP C 127 6149 4089 4617 -1605 377 -743 C ATOM 2120 CG ASP C 127 24.680 19.988 -7.682 1.00 38.54 C ANISOU 2120 CG ASP C 127 6405 3877 4362 -1455 259 -661 C ATOM 2121 OD1 ASP C 127 25.833 20.316 -8.027 1.00 35.67 O ANISOU 2121 OD1 ASP C 127 6067 3532 3953 -1187 176 -565 O ATOM 2122 OD2 ASP C 127 24.285 18.826 -7.853 1.00 42.96 O ANISOU 2122 OD2 ASP C 127 7199 4301 4823 -1613 254 -708 O ATOM 2123 N TRP C 128 26.634 23.117 -6.747 1.00 36.62 N ANISOU 2123 N TRP C 128 5721 3895 4299 -980 259 -467 N ATOM 2124 CA TRP C 128 28.017 23.016 -6.285 1.00 36.48 C ANISOU 2124 CA TRP C 128 5874 3822 4164 -804 229 -368 C ATOM 2125 C TRP C 128 28.585 24.297 -5.638 1.00 36.07 C ANISOU 2125 C TRP C 128 5647 3861 4198 -712 249 -321 C ATOM 2126 O TRP C 128 29.574 24.230 -4.875 1.00 35.81 O ANISOU 2126 O TRP C 128 5749 3779 4078 -621 236 -265 O ATOM 2127 CB TRP C 128 28.907 22.630 -7.476 1.00 36.19 C ANISOU 2127 CB TRP C 128 5895 3798 4058 -595 113 -322 C ATOM 2128 CG TRP C 128 28.817 23.655 -8.581 1.00 36.60 C ANISOU 2128 CG TRP C 128 5681 4006 4221 -513 58 -303 C ATOM 2129 CD1 TRP C 128 27.921 23.686 -9.611 1.00 36.37 C ANISOU 2129 CD1 TRP C 128 5553 4025 4242 -578 1 -349 C ATOM 2130 CD2 TRP C 128 29.626 24.831 -8.718 1.00 35.33 C ANISOU 2130 CD2 TRP C 128 5346 3958 4121 -374 38 -227 C ATOM 2131 NE1 TRP C 128 28.138 24.807 -10.397 1.00 35.18 N ANISOU 2131 NE1 TRP C 128 5210 3994 4164 -475 -65 -293 N ATOM 2132 CE2 TRP C 128 29.174 25.526 -9.862 1.00 35.46 C ANISOU 2132 CE2 TRP C 128 5199 4068 4207 -364 -30 -216 C ATOM 2133 CE3 TRP C 128 30.698 25.362 -7.985 1.00 36.58 C ANISOU 2133 CE3 TRP C 128 5483 4140 4278 -271 57 -169 C ATOM 2134 CZ2 TRP C 128 29.765 26.732 -10.296 1.00 34.71 C ANISOU 2134 CZ2 TRP C 128 4953 4070 4165 -271 -64 -134 C ATOM 2135 CZ3 TRP C 128 31.277 26.580 -8.418 1.00 34.86 C ANISOU 2135 CZ3 TRP C 128 5072 4038 4133 -187 34 -104 C ATOM 2136 CH2 TRP C 128 30.798 27.239 -9.552 1.00 34.17 C ANISOU 2136 CH2 TRP C 128 4858 4023 4101 -197 -18 -81 C ATOM 2137 N GLN C 129 28.007 25.462 -5.946 1.00 35.53 N ANISOU 2137 N GLN C 129 5291 3909 4300 -722 254 -349 N ATOM 2138 CA GLN C 129 28.637 26.704 -5.493 1.00 34.29 C ANISOU 2138 CA GLN C 129 4989 3817 4223 -624 251 -300 C ATOM 2139 C GLN C 129 28.087 27.183 -4.150 1.00 35.14 C ANISOU 2139 C GLN C 129 5061 3909 4380 -760 372 -374 C ATOM 2140 O GLN C 129 27.556 28.292 -4.037 1.00 36.22 O ANISOU 2140 O GLN C 129 4971 4111 4680 -770 394 -427 O ATOM 2141 CB GLN C 129 28.562 27.818 -6.547 1.00 33.27 C ANISOU 2141 CB GLN C 129 4622 3786 4231 -527 163 -268 C ATOM 2142 CG GLN C 129 29.659 28.866 -6.349 1.00 33.47 C ANISOU 2142 CG GLN C 129 4577 3856 4283 -406 133 -181 C ATOM 2143 CD GLN C 129 29.314 30.261 -6.799 1.00 33.95 C ANISOU 2143 CD GLN C 129 4428 3965 4508 -378 75 -166 C ATOM 2144 OE1 GLN C 129 29.821 31.235 -6.230 1.00 34.80 O ANISOU 2144 OE1 GLN C 129 4470 4076 4675 -348 80 -138 O ATOM 2145 NE2 GLN C 129 28.447 30.380 -7.815 1.00 37.51 N ANISOU 2145 NE2 GLN C 129 4790 4433 5029 -386 -6 -187 N ATOM 2146 N ASN C 130 28.233 26.357 -3.128 1.00 35.20 N ANISOU 2146 N ASN C 130 5317 3821 4236 -860 446 -382 N ATOM 2147 CA ASN C 130 27.886 26.763 -1.793 1.00 35.62 C ANISOU 2147 CA ASN C 130 5394 3861 4278 -997 575 -446 C ATOM 2148 C ASN C 130 29.104 27.020 -0.907 1.00 34.98 C ANISOU 2148 C ASN C 130 5462 3740 4088 -895 526 -366 C ATOM 2149 O ASN C 130 30.201 26.527 -1.189 1.00 34.19 O ANISOU 2149 O ASN C 130 5496 3599 3895 -738 400 -271 O ATOM 2150 CB ASN C 130 26.903 25.774 -1.183 1.00 38.09 C ANISOU 2150 CB ASN C 130 5881 4101 4489 -1258 721 -534 C ATOM 2151 CG ASN C 130 25.583 25.752 -1.950 1.00 40.70 C ANISOU 2151 CG ASN C 130 5975 4509 4980 -1379 773 -655 C ATOM 2152 OD1 ASN C 130 24.754 26.698 -1.849 1.00 44.68 O ANISOU 2152 OD1 ASN C 130 6182 5120 5674 -1420 845 -777 O ATOM 2153 ND2 ASN C 130 25.403 24.722 -2.761 1.00 36.91 N ANISOU 2153 ND2 ASN C 130 5610 3974 4440 -1412 712 -637 N ATOM 2154 N TYR C 131 28.901 27.834 0.130 1.00 34.24 N ANISOU 2154 N TYR C 131 5320 3668 4020 -974 619 -427 N ATOM 2155 CA TYR C 131 29.968 28.248 1.011 1.00 34.07 C ANISOU 2155 CA TYR C 131 5412 3622 3912 -893 557 -371 C ATOM 2156 C TYR C 131 29.579 27.990 2.460 1.00 36.06 C ANISOU 2156 C TYR C 131 5900 3803 3999 -1092 690 -435 C ATOM 2157 O TYR C 131 28.395 27.974 2.790 1.00 37.43 O ANISOU 2157 O TYR C 131 6030 3997 4195 -1296 875 -556 O ATOM 2158 CB TYR C 131 30.287 29.740 0.786 1.00 32.50 C ANISOU 2158 CB TYR C 131 4932 3517 3899 -779 513 -376 C ATOM 2159 CG TYR C 131 30.626 30.107 -0.645 1.00 30.86 C ANISOU 2159 CG TYR C 131 4521 3378 3827 -624 400 -306 C ATOM 2160 CD1 TYR C 131 31.954 30.166 -1.079 1.00 29.05 C ANISOU 2160 CD1 TYR C 131 4294 3176 3567 -464 270 -200 C ATOM 2161 CD2 TYR C 131 29.622 30.414 -1.565 1.00 31.63 C ANISOU 2161 CD2 TYR C 131 4421 3520 4076 -646 420 -355 C ATOM 2162 CE1 TYR C 131 32.280 30.516 -2.420 1.00 27.50 C ANISOU 2162 CE1 TYR C 131 3935 3054 3460 -357 199 -137 C ATOM 2163 CE2 TYR C 131 29.925 30.747 -2.887 1.00 29.64 C ANISOU 2163 CE2 TYR C 131 4038 3319 3905 -523 309 -278 C ATOM 2164 CZ TYR C 131 31.270 30.792 -3.313 1.00 30.74 C ANISOU 2164 CZ TYR C 131 4210 3487 3981 -392 215 -165 C ATOM 2165 OH TYR C 131 31.576 31.120 -4.643 1.00 30.38 O ANISOU 2165 OH TYR C 131 4060 3503 3981 -306 137 -92 O ATOM 2166 N THR C 132 30.562 27.807 3.335 1.00 36.23 N ANISOU 2166 N THR C 132 6167 3749 3849 -1044 597 -366 N ATOM 2167 CA THR C 132 30.275 27.618 4.755 1.00 38.25 C ANISOU 2167 CA THR C 132 6702 3930 3902 -1243 709 -414 C ATOM 2168 C THR C 132 29.448 28.783 5.301 1.00 38.92 C ANISOU 2168 C THR C 132 6570 4114 4102 -1367 898 -565 C ATOM 2169 O THR C 132 29.494 29.866 4.740 1.00 38.59 O ANISOU 2169 O THR C 132 6208 4166 4288 -1237 862 -598 O ATOM 2170 CB THR C 132 31.566 27.427 5.587 1.00 38.08 C ANISOU 2170 CB THR C 132 6958 3818 3693 -1132 519 -318 C ATOM 2171 OG1 THR C 132 32.482 28.469 5.303 1.00 38.99 O ANISOU 2171 OG1 THR C 132 6821 4029 3965 -931 384 -295 O ATOM 2172 CG2 THR C 132 32.247 26.128 5.250 1.00 40.61 C ANISOU 2172 CG2 THR C 132 7543 4007 3878 -1017 341 -204 C ATOM 2173 N PRO C 133 28.669 28.571 6.381 1.00 41.64 N ANISOU 2173 N PRO C 133 7101 4431 4289 -1624 1106 -669 N ATOM 2174 CA PRO C 133 27.949 29.721 6.966 1.00 42.87 C ANISOU 2174 CA PRO C 133 7042 4687 4559 -1715 1293 -849 C ATOM 2175 C PRO C 133 28.863 30.701 7.739 1.00 43.73 C ANISOU 2175 C PRO C 133 7195 4790 4631 -1608 1192 -840 C ATOM 2176 O PRO C 133 29.971 30.339 8.151 1.00 43.25 O ANISOU 2176 O PRO C 133 7397 4645 4391 -1529 1006 -708 O ATOM 2177 CB PRO C 133 26.964 29.064 7.945 1.00 45.43 C ANISOU 2177 CB PRO C 133 7598 4990 4672 -2049 1568 -967 C ATOM 2178 CG PRO C 133 27.608 27.771 8.329 1.00 46.29 C ANISOU 2178 CG PRO C 133 8185 4934 4469 -2117 1458 -799 C ATOM 2179 CD PRO C 133 28.407 27.314 7.117 1.00 43.15 C ANISOU 2179 CD PRO C 133 7718 4493 4182 -1853 1190 -638 C ATOM 2180 N GLY C 134 28.387 31.932 7.926 1.00 44.62 N ANISOU 2180 N GLY C 134 7045 4984 4924 -1598 1295 -995 N ATOM 2181 CA GLY C 134 29.088 32.915 8.740 1.00 45.10 C ANISOU 2181 CA GLY C 134 7154 5031 4949 -1540 1229 -1024 C ATOM 2182 C GLY C 134 29.067 32.637 10.233 1.00 47.55 C ANISOU 2182 C GLY C 134 7834 5292 4942 -1749 1353 -1088 C ATOM 2183 O GLY C 134 28.434 31.670 10.690 1.00 49.17 O ANISOU 2183 O GLY C 134 8276 5468 4937 -1972 1524 -1112 O ATOM 2184 N PRO C 135 29.759 33.484 11.009 1.00 47.77 N ANISOU 2184 N PRO C 135 7940 5301 4911 -1703 1268 -1117 N ATOM 2185 CA PRO C 135 30.416 34.691 10.505 1.00 46.30 C ANISOU 2185 CA PRO C 135 7478 5138 4975 -1490 1094 -1107 C ATOM 2186 C PRO C 135 31.829 34.394 10.008 1.00 44.66 C ANISOU 2186 C PRO C 135 7321 4895 4752 -1309 782 -894 C ATOM 2187 O PRO C 135 32.286 33.253 10.121 1.00 45.36 O ANISOU 2187 O PRO C 135 7665 4929 4639 -1317 685 -770 O ATOM 2188 CB PRO C 135 30.446 35.606 11.743 1.00 47.58 C ANISOU 2188 CB PRO C 135 7757 5287 5034 -1578 1171 -1264 C ATOM 2189 CG PRO C 135 30.587 34.650 12.901 1.00 50.30 C ANISOU 2189 CG PRO C 135 8561 5572 4979 -1771 1219 -1235 C ATOM 2190 CD PRO C 135 29.943 33.328 12.469 1.00 50.42 C ANISOU 2190 CD PRO C 135 8673 5579 4907 -1883 1332 -1164 C ATOM 2191 N GLY C 136 32.512 35.404 9.468 1.00 42.72 N ANISOU 2191 N GLY C 136 6837 4676 4720 -1151 629 -865 N ATOM 2192 CA GLY C 136 33.889 35.232 9.002 1.00 40.63 C ANISOU 2192 CA GLY C 136 6559 4413 4465 -994 359 -700 C ATOM 2193 C GLY C 136 33.921 34.853 7.535 1.00 38.90 C ANISOU 2193 C GLY C 136 6118 4242 4421 -868 313 -592 C ATOM 2194 O GLY C 136 32.907 34.969 6.824 1.00 38.74 O ANISOU 2194 O GLY C 136 5924 4247 4550 -887 453 -641 O ATOM 2195 N ILE C 137 35.085 34.403 7.075 1.00 37.07 N ANISOU 2195 N ILE C 137 5883 4030 4173 -734 112 -463 N ATOM 2196 CA ILE C 137 35.267 34.005 5.702 1.00 34.76 C ANISOU 2196 CA ILE C 137 5407 3791 4009 -615 69 -368 C ATOM 2197 C ILE C 137 34.400 32.781 5.373 1.00 34.54 C ANISOU 2197 C ILE C 137 5507 3727 3891 -660 176 -356 C ATOM 2198 O ILE C 137 34.284 31.855 6.178 1.00 35.79 O ANISOU 2198 O ILE C 137 5961 3806 3833 -736 188 -356 O ATOM 2199 CB ILE C 137 36.757 33.742 5.399 1.00 35.03 C ANISOU 2199 CB ILE C 137 5402 3872 4034 -463 -149 -272 C ATOM 2200 CG1 ILE C 137 37.576 35.030 5.636 1.00 34.72 C ANISOU 2200 CG1 ILE C 137 5203 3881 4109 -460 -244 -294 C ATOM 2201 CG2 ILE C 137 36.926 33.262 3.961 1.00 32.51 C ANISOU 2201 CG2 ILE C 137 4914 3619 3820 -350 -161 -195 C ATOM 2202 CD1 ILE C 137 39.099 34.811 5.620 1.00 35.24 C ANISOU 2202 CD1 ILE C 137 5212 4015 4164 -339 -461 -243 C ATOM 2203 N ARG C 138 33.773 32.799 4.206 1.00 32.69 N ANISOU 2203 N ARG C 138 5072 3535 3811 -632 243 -346 N ATOM 2204 CA ARG C 138 32.916 31.685 3.787 1.00 33.81 C ANISOU 2204 CA ARG C 138 5307 3648 3893 -691 337 -347 C ATOM 2205 C ARG C 138 33.691 30.834 2.811 1.00 33.01 C ANISOU 2205 C ARG C 138 5211 3557 3772 -541 204 -237 C ATOM 2206 O ARG C 138 34.129 31.320 1.787 1.00 32.69 O ANISOU 2206 O ARG C 138 4952 3595 3872 -430 143 -191 O ATOM 2207 CB ARG C 138 31.641 32.190 3.121 1.00 32.90 C ANISOU 2207 CB ARG C 138 4965 3575 3959 -754 476 -432 C ATOM 2208 CG ARG C 138 30.923 33.291 3.864 1.00 34.45 C ANISOU 2208 CG ARG C 138 5059 3779 4249 -844 598 -574 C ATOM 2209 CD ARG C 138 30.589 32.984 5.344 1.00 40.94 C ANISOU 2209 CD ARG C 138 6129 4555 4869 -1017 735 -672 C ATOM 2210 NE ARG C 138 29.959 34.169 5.945 1.00 47.33 N ANISOU 2210 NE ARG C 138 6801 5387 5797 -1072 856 -837 N ATOM 2211 CZ ARG C 138 28.714 34.543 5.689 1.00 48.12 C ANISOU 2211 CZ ARG C 138 6687 5529 6067 -1123 1008 -989 C ATOM 2212 NH1 ARG C 138 27.964 33.798 4.880 1.00 46.72 N ANISOU 2212 NH1 ARG C 138 6419 5385 5947 -1154 1055 -987 N ATOM 2213 NH2 ARG C 138 28.227 35.650 6.231 1.00 49.77 N ANISOU 2213 NH2 ARG C 138 6765 5747 6398 -1133 1099 -1157 N ATOM 2214 N TYR C 139 33.869 29.571 3.138 1.00 33.42 N ANISOU 2214 N TYR C 139 5537 3521 3641 -542 161 -202 N ATOM 2215 CA TYR C 139 34.737 28.725 2.349 1.00 33.04 C ANISOU 2215 CA TYR C 139 5517 3470 3568 -366 18 -126 C ATOM 2216 C TYR C 139 33.941 27.833 1.413 1.00 32.87 C ANISOU 2216 C TYR C 139 5524 3417 3547 -397 89 -126 C ATOM 2217 O TYR C 139 32.829 27.424 1.740 1.00 33.54 O ANISOU 2217 O TYR C 139 5732 3439 3573 -579 222 -174 O ATOM 2218 CB TYR C 139 35.636 27.909 3.275 1.00 34.43 C ANISOU 2218 CB TYR C 139 5992 3539 3553 -291 -143 -90 C ATOM 2219 CG TYR C 139 36.681 28.765 3.988 1.00 34.15 C ANISOU 2219 CG TYR C 139 5880 3557 3537 -216 -275 -91 C ATOM 2220 CD1 TYR C 139 37.851 29.201 3.327 1.00 31.32 C ANISOU 2220 CD1 TYR C 139 5263 3321 3315 -35 -403 -73 C ATOM 2221 CD2 TYR C 139 36.496 29.139 5.314 1.00 36.16 C ANISOU 2221 CD2 TYR C 139 6321 3752 3666 -349 -260 -125 C ATOM 2222 CE1 TYR C 139 38.821 29.968 3.999 1.00 33.03 C ANISOU 2222 CE1 TYR C 139 5397 3594 3560 8 -534 -88 C ATOM 2223 CE2 TYR C 139 37.468 29.890 6.003 1.00 38.37 C ANISOU 2223 CE2 TYR C 139 6553 4073 3952 -290 -407 -136 C ATOM 2224 CZ TYR C 139 38.612 30.306 5.336 1.00 38.15 C ANISOU 2224 CZ TYR C 139 6250 4164 4082 -115 -549 -117 C ATOM 2225 OH TYR C 139 39.513 31.069 6.038 1.00 41.79 O ANISOU 2225 OH TYR C 139 6647 4670 4559 -90 -691 -143 O ATOM 2226 N PRO C 140 34.495 27.549 0.231 1.00 32.01 N ANISOU 2226 N PRO C 140 5293 3365 3503 -239 13 -87 N ATOM 2227 CA PRO C 140 33.708 26.803 -0.729 1.00 32.14 C ANISOU 2227 CA PRO C 140 5328 3359 3524 -275 71 -98 C ATOM 2228 C PRO C 140 33.582 25.347 -0.320 1.00 33.80 C ANISOU 2228 C PRO C 140 5891 3401 3550 -307 39 -93 C ATOM 2229 O PRO C 140 34.558 24.736 0.085 1.00 35.12 O ANISOU 2229 O PRO C 140 6242 3489 3613 -166 -103 -60 O ATOM 2230 CB PRO C 140 34.539 26.923 -2.017 1.00 30.44 C ANISOU 2230 CB PRO C 140 4923 3253 3389 -89 -4 -63 C ATOM 2231 CG PRO C 140 35.895 27.032 -1.542 1.00 31.54 C ANISOU 2231 CG PRO C 140 5059 3420 3505 63 -124 -42 C ATOM 2232 CD PRO C 140 35.821 27.893 -0.307 1.00 31.39 C ANISOU 2232 CD PRO C 140 5046 3388 3491 -42 -110 -50 C ATOM 2233 N LEU C 141 32.379 24.813 -0.421 1.00 35.05 N ANISOU 2233 N LEU C 141 6143 3497 3677 -495 156 -134 N ATOM 2234 CA LEU C 141 32.093 23.437 -0.047 1.00 37.67 C ANISOU 2234 CA LEU C 141 6846 3640 3825 -587 145 -127 C ATOM 2235 C LEU C 141 32.607 22.440 -1.098 1.00 37.42 C ANISOU 2235 C LEU C 141 6901 3548 3769 -410 24 -108 C ATOM 2236 O LEU C 141 32.941 21.303 -0.783 1.00 38.92 O ANISOU 2236 O LEU C 141 7431 3551 3804 -368 -75 -84 O ATOM 2237 CB LEU C 141 30.581 23.244 0.145 1.00 39.35 C ANISOU 2237 CB LEU C 141 7089 3830 4031 -891 337 -200 C ATOM 2238 CG LEU C 141 29.812 24.066 1.187 1.00 40.74 C ANISOU 2238 CG LEU C 141 7191 4064 4222 -1106 511 -270 C ATOM 2239 CD1 LEU C 141 28.721 23.193 1.706 1.00 42.27 C ANISOU 2239 CD1 LEU C 141 7621 4153 4285 -1413 670 -327 C ATOM 2240 CD2 LEU C 141 30.671 24.460 2.306 1.00 41.09 C ANISOU 2240 CD2 LEU C 141 7380 4074 4159 -1047 447 -225 C ATOM 2241 N THR C 142 32.673 22.889 -2.336 1.00 35.50 N ANISOU 2241 N THR C 142 6372 3450 3665 -304 26 -123 N ATOM 2242 CA THR C 142 33.267 22.113 -3.401 1.00 35.64 C ANISOU 2242 CA THR C 142 6431 3449 3663 -116 -70 -128 C ATOM 2243 C THR C 142 34.784 22.314 -3.496 1.00 35.40 C ANISOU 2243 C THR C 142 6308 3489 3653 163 -196 -110 C ATOM 2244 O THR C 142 35.274 23.360 -3.932 1.00 34.33 O ANISOU 2244 O THR C 142 5871 3538 3635 233 -175 -101 O ATOM 2245 CB THR C 142 32.603 22.459 -4.758 1.00 34.50 C ANISOU 2245 CB THR C 142 6052 3432 3625 -154 -7 -160 C ATOM 2246 OG1 THR C 142 31.226 22.078 -4.703 1.00 34.00 O ANISOU 2246 OG1 THR C 142 6065 3300 3552 -399 82 -204 O ATOM 2247 CG2 THR C 142 33.307 21.729 -5.922 1.00 35.14 C ANISOU 2247 CG2 THR C 142 6170 3517 3664 46 -87 -182 C ATOM 2248 N PHE C 143 35.504 21.273 -3.116 1.00 36.88 N ANISOU 2248 N PHE C 143 6763 3521 3730 315 -333 -115 N ATOM 2249 CA PHE C 143 36.952 21.212 -3.249 1.00 37.30 C ANISOU 2249 CA PHE C 143 6725 3633 3814 609 -474 -139 C ATOM 2250 C PHE C 143 37.325 21.418 -4.718 1.00 36.63 C ANISOU 2250 C PHE C 143 6369 3729 3820 734 -418 -191 C ATOM 2251 O PHE C 143 36.695 20.836 -5.589 1.00 36.59 O ANISOU 2251 O PHE C 143 6442 3682 3779 688 -366 -221 O ATOM 2252 CB PHE C 143 37.448 19.858 -2.710 1.00 39.08 C ANISOU 2252 CB PHE C 143 7333 3612 3906 766 -658 -154 C ATOM 2253 CG PHE C 143 38.930 19.795 -2.457 1.00 40.12 C ANISOU 2253 CG PHE C 143 7383 3782 4080 1079 -848 -196 C ATOM 2254 CD1 PHE C 143 39.643 20.938 -2.107 1.00 39.10 C ANISOU 2254 CD1 PHE C 143 6943 3854 4058 1117 -856 -189 C ATOM 2255 CD2 PHE C 143 39.612 18.574 -2.564 1.00 43.15 C ANISOU 2255 CD2 PHE C 143 7996 3991 4407 1342 -1036 -259 C ATOM 2256 CE1 PHE C 143 41.030 20.883 -1.857 1.00 43.37 C ANISOU 2256 CE1 PHE C 143 7365 4454 4661 1399 -1043 -252 C ATOM 2257 CE2 PHE C 143 40.996 18.489 -2.329 1.00 45.44 C ANISOU 2257 CE2 PHE C 143 8170 4328 4766 1663 -1236 -330 C ATOM 2258 CZ PHE C 143 41.712 19.654 -1.950 1.00 46.52 C ANISOU 2258 CZ PHE C 143 7960 4696 5019 1683 -1240 -328 C ATOM 2259 N GLY C 144 38.338 22.253 -4.988 1.00 36.41 N ANISOU 2259 N GLY C 144 6036 3904 3894 864 -421 -207 N ATOM 2260 CA GLY C 144 38.657 22.666 -6.368 1.00 35.21 C ANISOU 2260 CA GLY C 144 5621 3952 3804 919 -324 -245 C ATOM 2261 C GLY C 144 38.205 24.075 -6.722 1.00 33.41 C ANISOU 2261 C GLY C 144 5142 3889 3664 735 -202 -177 C ATOM 2262 O GLY C 144 38.846 24.766 -7.537 1.00 33.21 O ANISOU 2262 O GLY C 144 4874 4052 3691 771 -139 -184 O ATOM 2263 N TRP C 145 37.094 24.515 -6.140 1.00 31.82 N ANISOU 2263 N TRP C 145 5003 3611 3476 531 -163 -120 N ATOM 2264 CA TRP C 145 36.624 25.885 -6.389 1.00 30.84 C ANISOU 2264 CA TRP C 145 4660 3604 3454 384 -81 -66 C ATOM 2265 C TRP C 145 37.477 26.806 -5.528 1.00 30.63 C ANISOU 2265 C TRP C 145 4492 3648 3499 406 -113 -44 C ATOM 2266 O TRP C 145 37.456 26.694 -4.305 1.00 30.19 O ANISOU 2266 O TRP C 145 4560 3494 3419 384 -166 -45 O ATOM 2267 CB TRP C 145 35.139 26.001 -6.042 1.00 29.90 C ANISOU 2267 CB TRP C 145 4622 3388 3351 186 -32 -56 C ATOM 2268 CG TRP C 145 34.548 27.383 -6.211 1.00 31.19 C ANISOU 2268 CG TRP C 145 4579 3633 3639 68 19 -20 C ATOM 2269 CD1 TRP C 145 34.021 28.160 -5.230 1.00 31.76 C ANISOU 2269 CD1 TRP C 145 4609 3673 3785 -43 48 -23 C ATOM 2270 CD2 TRP C 145 34.390 28.121 -7.432 1.00 31.10 C ANISOU 2270 CD2 TRP C 145 4412 3725 3682 54 31 16 C ATOM 2271 NE1 TRP C 145 33.551 29.336 -5.751 1.00 33.73 N ANISOU 2271 NE1 TRP C 145 4674 3986 4156 -100 64 1 N ATOM 2272 CE2 TRP C 145 33.763 29.341 -7.102 1.00 31.16 C ANISOU 2272 CE2 TRP C 145 4291 3735 3813 -47 41 39 C ATOM 2273 CE3 TRP C 145 34.713 27.869 -8.767 1.00 33.28 C ANISOU 2273 CE3 TRP C 145 4669 4079 3896 116 29 28 C ATOM 2274 CZ2 TRP C 145 33.484 30.332 -8.048 1.00 30.38 C ANISOU 2274 CZ2 TRP C 145 4066 3693 3785 -78 19 91 C ATOM 2275 CZ3 TRP C 145 34.396 28.851 -9.730 1.00 35.56 C ANISOU 2275 CZ3 TRP C 145 4843 4440 4227 56 26 86 C ATOM 2276 CH2 TRP C 145 33.797 30.068 -9.354 1.00 31.90 C ANISOU 2276 CH2 TRP C 145 4273 3955 3894 -35 6 125 C ATOM 2277 N CYS C 146 38.238 27.687 -6.167 1.00 30.94 N ANISOU 2277 N CYS C 146 4297 3852 3607 430 -82 -26 N ATOM 2278 CA CYS C 146 39.249 28.508 -5.488 1.00 32.46 C ANISOU 2278 CA CYS C 146 4330 4131 3873 452 -122 -22 C ATOM 2279 C CYS C 146 38.824 29.929 -5.142 1.00 31.84 C ANISOU 2279 C CYS C 146 4142 4067 3890 285 -85 36 C ATOM 2280 O CYS C 146 39.668 30.832 -5.104 1.00 33.23 O ANISOU 2280 O CYS C 146 4141 4349 4136 264 -88 49 O ATOM 2281 CB CYS C 146 40.534 28.567 -6.311 1.00 32.80 C ANISOU 2281 CB CYS C 146 4168 4357 3937 565 -100 -64 C ATOM 2282 SG CYS C 146 41.333 26.958 -6.384 1.00 36.28 S ANISOU 2282 SG CYS C 146 4707 4772 4305 832 -187 -182 S ATOM 2283 N PHE C 147 37.534 30.139 -4.921 1.00 30.59 N ANISOU 2283 N PHE C 147 4076 3802 3744 165 -50 55 N ATOM 2284 CA PHE C 147 37.060 31.442 -4.438 1.00 29.51 C ANISOU 2284 CA PHE C 147 3856 3646 3710 38 -31 81 C ATOM 2285 C PHE C 147 36.401 31.270 -3.094 1.00 29.44 C ANISOU 2285 C PHE C 147 3990 3518 3678 -23 -32 34 C ATOM 2286 O PHE C 147 35.652 30.306 -2.867 1.00 30.20 O ANISOU 2286 O PHE C 147 4252 3527 3695 -45 -7 2 O ATOM 2287 CB PHE C 147 36.044 32.044 -5.406 1.00 29.01 C ANISOU 2287 CB PHE C 147 3737 3576 3710 -43 11 116 C ATOM 2288 CG PHE C 147 36.672 32.749 -6.562 1.00 28.18 C ANISOU 2288 CG PHE C 147 3507 3575 3623 -50 18 186 C ATOM 2289 CD1 PHE C 147 37.011 34.094 -6.459 1.00 29.31 C ANISOU 2289 CD1 PHE C 147 3547 3731 3858 -129 6 234 C ATOM 2290 CD2 PHE C 147 36.947 32.073 -7.738 1.00 25.36 C ANISOU 2290 CD2 PHE C 147 3165 3295 3175 5 43 199 C ATOM 2291 CE1 PHE C 147 37.632 34.757 -7.520 1.00 30.96 C ANISOU 2291 CE1 PHE C 147 3678 4027 4056 -179 27 311 C ATOM 2292 CE2 PHE C 147 37.560 32.723 -8.814 1.00 27.61 C ANISOU 2292 CE2 PHE C 147 3363 3688 3439 -36 78 262 C ATOM 2293 CZ PHE C 147 37.904 34.062 -8.713 1.00 28.96 C ANISOU 2293 CZ PHE C 147 3443 3871 3691 -140 73 326 C ATOM 2294 N LYS C 148 36.694 32.186 -2.194 1.00 29.43 N ANISOU 2294 N LYS C 148 3942 3510 3729 -73 -53 24 N ATOM 2295 CA LYS C 148 36.010 32.269 -0.915 1.00 29.60 C ANISOU 2295 CA LYS C 148 4095 3433 3720 -163 -24 -34 C ATOM 2296 C LYS C 148 35.367 33.644 -0.804 1.00 29.92 C ANISOU 2296 C LYS C 148 4010 3460 3900 -258 24 -58 C ATOM 2297 O LYS C 148 35.675 34.552 -1.616 1.00 28.89 O ANISOU 2297 O LYS C 148 3723 3378 3877 -250 -1 -7 O ATOM 2298 CB LYS C 148 37.002 32.033 0.230 1.00 30.45 C ANISOU 2298 CB LYS C 148 4313 3523 3734 -119 -122 -48 C ATOM 2299 CG LYS C 148 38.085 33.116 0.368 1.00 30.08 C ANISOU 2299 CG LYS C 148 4092 3559 3777 -104 -199 -37 C ATOM 2300 CD LYS C 148 39.364 32.554 1.056 1.00 31.67 C ANISOU 2300 CD LYS C 148 4348 3788 3897 8 -353 -51 C ATOM 2301 CE LYS C 148 40.322 33.742 1.357 1.00 33.71 C ANISOU 2301 CE LYS C 148 4420 4131 4257 -28 -425 -63 C ATOM 2302 NZ LYS C 148 41.643 33.348 1.930 1.00 36.08 N ANISOU 2302 NZ LYS C 148 4697 4490 4522 88 -604 -97 N ATOM 2303 N LEU C 149 34.488 33.813 0.192 1.00 30.32 N ANISOU 2303 N LEU C 149 4143 3435 3943 -352 96 -144 N ATOM 2304 CA LEU C 149 33.821 35.113 0.387 1.00 30.49 C ANISOU 2304 CA LEU C 149 4046 3426 4113 -412 137 -204 C ATOM 2305 C LEU C 149 34.350 35.757 1.654 1.00 32.24 C ANISOU 2305 C LEU C 149 4333 3615 4301 -456 117 -256 C ATOM 2306 O LEU C 149 34.290 35.163 2.734 1.00 32.69 O ANISOU 2306 O LEU C 149 4570 3637 4212 -508 152 -310 O ATOM 2307 CB LEU C 149 32.310 34.970 0.482 1.00 30.12 C ANISOU 2307 CB LEU C 149 3986 3341 4119 -484 255 -311 C ATOM 2308 CG LEU C 149 31.642 34.058 -0.561 1.00 30.62 C ANISOU 2308 CG LEU C 149 4027 3428 4178 -470 272 -287 C ATOM 2309 CD1 LEU C 149 30.162 33.892 -0.233 1.00 28.58 C ANISOU 2309 CD1 LEU C 149 3730 3150 3979 -572 398 -429 C ATOM 2310 CD2 LEU C 149 31.849 34.569 -1.995 1.00 27.55 C ANISOU 2310 CD2 LEU C 149 3497 3076 3893 -385 174 -193 C ATOM 2311 N VAL C 150 34.876 36.972 1.517 1.00 32.65 N ANISOU 2311 N VAL C 150 4268 3667 4471 -452 53 -237 N ATOM 2312 CA VAL C 150 35.600 37.594 2.611 1.00 33.29 C ANISOU 2312 CA VAL C 150 4406 3724 4518 -492 -1 -280 C ATOM 2313 C VAL C 150 34.872 38.852 3.051 1.00 33.54 C ANISOU 2313 C VAL C 150 4395 3669 4679 -549 47 -385 C ATOM 2314 O VAL C 150 34.571 39.701 2.229 1.00 33.75 O ANISOU 2314 O VAL C 150 4296 3661 4868 -528 24 -360 O ATOM 2315 CB VAL C 150 37.074 37.904 2.219 1.00 33.86 C ANISOU 2315 CB VAL C 150 4384 3872 4609 -459 -132 -188 C ATOM 2316 CG1 VAL C 150 37.867 38.496 3.404 1.00 32.27 C ANISOU 2316 CG1 VAL C 150 4239 3652 4371 -510 -218 -244 C ATOM 2317 CG2 VAL C 150 37.750 36.635 1.731 1.00 33.00 C ANISOU 2317 CG2 VAL C 150 4290 3851 4396 -365 -175 -120 C ATOM 2318 N PRO C 151 34.565 38.957 4.349 1.00 34.13 N ANISOU 2318 N PRO C 151 4600 3698 4671 -616 107 -510 N ATOM 2319 CA PRO C 151 33.977 40.187 4.893 1.00 35.16 C ANISOU 2319 CA PRO C 151 4698 3741 4920 -653 153 -646 C ATOM 2320 C PRO C 151 34.868 41.419 4.641 1.00 35.39 C ANISOU 2320 C PRO C 151 4653 3723 5071 -651 15 -595 C ATOM 2321 O PRO C 151 36.073 41.361 4.882 1.00 34.60 O ANISOU 2321 O PRO C 151 4585 3668 4892 -675 -94 -526 O ATOM 2322 CB PRO C 151 33.908 39.896 6.397 1.00 36.10 C ANISOU 2322 CB PRO C 151 5021 3845 4850 -743 227 -769 C ATOM 2323 CG PRO C 151 33.765 38.377 6.485 1.00 35.91 C ANISOU 2323 CG PRO C 151 5135 3874 4634 -764 283 -716 C ATOM 2324 CD PRO C 151 34.674 37.893 5.368 1.00 34.57 C ANISOU 2324 CD PRO C 151 4873 3764 4497 -663 141 -539 C ATOM 2325 N VAL C 152 34.275 42.506 4.138 1.00 36.30 N ANISOU 2325 N VAL C 152 4670 3740 5381 -624 6 -632 N ATOM 2326 CA VAL C 152 34.970 43.807 4.029 1.00 37.18 C ANISOU 2326 CA VAL C 152 4762 3757 5606 -658 -115 -603 C ATOM 2327 C VAL C 152 34.788 44.497 5.355 1.00 39.07 C ANISOU 2327 C VAL C 152 5107 3908 5832 -706 -84 -786 C ATOM 2328 O VAL C 152 33.690 44.913 5.705 1.00 40.39 O ANISOU 2328 O VAL C 152 5268 3994 6087 -667 8 -950 O ATOM 2329 CB VAL C 152 34.385 44.683 2.915 1.00 37.37 C ANISOU 2329 CB VAL C 152 4698 3668 5832 -601 -170 -557 C ATOM 2330 CG1 VAL C 152 35.099 46.019 2.842 1.00 39.67 C ANISOU 2330 CG1 VAL C 152 5023 3828 6221 -668 -294 -518 C ATOM 2331 CG2 VAL C 152 34.469 43.959 1.560 1.00 36.35 C ANISOU 2331 CG2 VAL C 152 4494 3633 5685 -563 -190 -385 C ATOM 2332 N GLU C 153 35.866 44.598 6.111 1.00 40.48 N ANISOU 2332 N GLU C 153 5372 4110 5897 -787 -164 -779 N ATOM 2333 CA GLU C 153 35.793 45.131 7.456 1.00 43.01 C ANISOU 2333 CA GLU C 153 5833 4359 6151 -848 -142 -956 C ATOM 2334 C GLU C 153 37.188 45.555 7.941 1.00 43.77 C ANISOU 2334 C GLU C 153 5982 4465 6185 -943 -307 -914 C ATOM 2335 O GLU C 153 38.180 45.215 7.328 1.00 41.42 O ANISOU 2335 O GLU C 153 5593 4264 5881 -956 -410 -764 O ATOM 2336 CB GLU C 153 35.152 44.092 8.395 1.00 43.60 C ANISOU 2336 CB GLU C 153 6040 4503 6022 -863 8 -1063 C ATOM 2337 CG GLU C 153 35.928 42.766 8.509 1.00 44.16 C ANISOU 2337 CG GLU C 153 6194 4702 5884 -874 -49 -933 C ATOM 2338 CD GLU C 153 35.266 41.771 9.464 1.00 47.61 C ANISOU 2338 CD GLU C 153 6831 5168 6092 -925 94 -1023 C ATOM 2339 OE1 GLU C 153 34.059 41.896 9.735 1.00 50.69 O ANISOU 2339 OE1 GLU C 153 7223 5528 6508 -951 287 -1172 O ATOM 2340 OE2 GLU C 153 35.953 40.854 9.955 1.00 48.66 O ANISOU 2340 OE2 GLU C 153 7126 5350 6013 -945 11 -951 O ATOM 2341 N PRO C 154 37.257 46.320 9.042 1.00 46.32 N ANISOU 2341 N PRO C 154 6437 4693 6469 -1012 -330 -1071 N ATOM 2342 CA PRO C 154 38.580 46.665 9.577 1.00 48.86 C ANISOU 2342 CA PRO C 154 6803 5035 6725 -1115 -508 -1050 C ATOM 2343 C PRO C 154 39.316 45.446 10.152 1.00 50.77 C ANISOU 2343 C PRO C 154 7120 5431 6740 -1114 -581 -999 C ATOM 2344 O PRO C 154 38.677 44.464 10.576 1.00 50.56 O ANISOU 2344 O PRO C 154 7214 5446 6550 -1071 -472 -1027 O ATOM 2345 CB PRO C 154 38.272 47.658 10.698 1.00 50.41 C ANISOU 2345 CB PRO C 154 7165 5085 6903 -1180 -500 -1259 C ATOM 2346 CG PRO C 154 36.821 47.883 10.679 1.00 50.11 C ANISOU 2346 CG PRO C 154 7137 4956 6948 -1096 -308 -1397 C ATOM 2347 CD PRO C 154 36.172 46.768 9.921 1.00 46.95 C ANISOU 2347 CD PRO C 154 6630 4671 6539 -1005 -189 -1295 C ATOM 2348 N GLU C 155 40.643 45.498 10.129 1.00 54.16 N ANISOU 2348 N GLU C 155 7473 5938 7166 -1164 -771 -927 N ATOM 2349 CA GLU C 155 41.487 44.513 10.831 1.00 57.69 C ANISOU 2349 CA GLU C 155 8002 6503 7414 -1143 -916 -909 C ATOM 2350 C GLU C 155 41.145 44.471 12.321 1.00 59.81 C ANISOU 2350 C GLU C 155 8572 6700 7454 -1195 -921 -1059 C ATOM 2351 O GLU C 155 41.111 45.520 12.982 1.00 61.58 O ANISOU 2351 O GLU C 155 8883 6820 7693 -1292 -943 -1190 O ATOM 2352 CB GLU C 155 42.975 44.858 10.677 1.00 59.06 C ANISOU 2352 CB GLU C 155 8003 6770 7667 -1202 -1138 -866 C ATOM 2353 CG GLU C 155 43.734 43.944 9.718 1.00 61.99 C ANISOU 2353 CG GLU C 155 8152 7315 8088 -1106 -1192 -730 C ATOM 2354 CD GLU C 155 45.181 44.389 9.512 1.00 67.75 C ANISOU 2354 CD GLU C 155 8646 8164 8932 -1186 -1377 -724 C ATOM 2355 OE1 GLU C 155 45.932 44.537 10.513 1.00 70.54 O ANISOU 2355 OE1 GLU C 155 9057 8536 9209 -1234 -1580 -814 O ATOM 2356 OE2 GLU C 155 45.564 44.600 8.338 1.00 69.56 O ANISOU 2356 OE2 GLU C 155 8630 8477 9321 -1218 -1317 -636 O ATOM 2357 N LYS C 156 40.899 43.257 12.820 1.00 60.64 N ANISOU 2357 N LYS C 156 8861 6848 7333 -1141 -900 -1038 N ATOM 2358 CA LYS C 156 40.523 42.985 14.215 1.00 63.00 C ANISOU 2358 CA LYS C 156 9504 7088 7345 -1210 -881 -1157 C ATOM 2359 C LYS C 156 41.426 43.653 15.258 1.00 65.59 C ANISOU 2359 C LYS C 156 9964 7386 7571 -1300 -1107 -1253 C ATOM 2360 O LYS C 156 42.611 43.870 15.016 1.00 66.50 O ANISOU 2360 O LYS C 156 9912 7568 7789 -1289 -1345 -1199 O ATOM 2361 CB LYS C 156 40.481 41.468 14.465 1.00 62.98 C ANISOU 2361 CB LYS C 156 9696 7130 7103 -1148 -905 -1066 C ATOM 2362 N SER C 167 34.509 52.234 24.587 1.00100.92 N ANISOU 2362 N SER C 167 16351 10837 11156 -2080 598 -4126 N ATOM 2363 CA SER C 167 33.611 53.059 23.791 1.00100.73 C ANISOU 2363 CA SER C 167 16002 10709 11561 -1890 754 -4278 C ATOM 2364 C SER C 167 34.228 54.427 23.467 1.00101.41 C ANISOU 2364 C SER C 167 16033 10558 11939 -1819 481 -4319 C ATOM 2365 O SER C 167 34.188 54.873 22.316 1.00 99.34 O ANISOU 2365 O SER C 167 15483 10197 12064 -1670 377 -4193 O ATOM 2366 CB SER C 167 32.256 53.222 24.491 1.00103.65 C ANISOU 2366 CB SER C 167 16415 11115 11851 -1884 1184 -4669 C ATOM 2367 OG SER C 167 32.374 53.961 25.701 1.00107.53 O ANISOU 2367 OG SER C 167 17233 11515 12106 -1992 1219 -4972 O ATOM 2368 N LEU C 168 34.799 55.083 24.482 1.00104.24 N ANISOU 2368 N LEU C 168 16698 10816 12094 -1946 358 -4493 N ATOM 2369 CA LEU C 168 35.480 56.365 24.286 1.00105.28 C ANISOU 2369 CA LEU C 168 16832 10707 12462 -1932 81 -4534 C ATOM 2370 C LEU C 168 36.819 56.248 23.549 1.00103.03 C ANISOU 2370 C LEU C 168 16434 10426 12286 -1997 -301 -4173 C ATOM 2371 O LEU C 168 37.296 57.228 22.990 1.00103.05 O ANISOU 2371 O LEU C 168 16348 10238 12570 -1984 -506 -4138 O ATOM 2372 CB LEU C 168 35.645 57.129 25.605 1.00109.18 C ANISOU 2372 CB LEU C 168 17694 11084 12707 -2058 70 -4860 C ATOM 2373 CG LEU C 168 34.434 57.888 26.173 1.00112.71 C ANISOU 2373 CG LEU C 168 18208 11419 13199 -1956 397 -5305 C ATOM 2374 CD1 LEU C 168 34.881 58.869 27.256 1.00116.23 C ANISOU 2374 CD1 LEU C 168 19008 11687 13467 -2076 282 -5591 C ATOM 2375 CD2 LEU C 168 33.622 58.626 25.103 1.00111.93 C ANISOU 2375 CD2 LEU C 168 17773 11152 13603 -1698 468 -5372 C ATOM 2376 N LEU C 169 37.416 55.058 23.537 1.00101.62 N ANISOU 2376 N LEU C 169 16261 10461 11890 -2071 -392 -3917 N ATOM 2377 CA LEU C 169 38.601 54.811 22.707 1.00 99.83 C ANISOU 2377 CA LEU C 169 15844 10285 11801 -2102 -710 -3588 C ATOM 2378 C LEU C 169 38.226 54.125 21.392 1.00 96.65 C ANISOU 2378 C LEU C 169 15109 9983 11632 -1958 -614 -3339 C ATOM 2379 O LEU C 169 38.894 54.318 20.370 1.00 94.96 O ANISOU 2379 O LEU C 169 14664 9750 11667 -1943 -798 -3120 O ATOM 2380 CB LEU C 169 39.665 54.002 23.465 1.00100.44 C ANISOU 2380 CB LEU C 169 16117 10514 11530 -2244 -947 -3470 C ATOM 2381 CG LEU C 169 41.142 54.283 23.128 1.00100.37 C ANISOU 2381 CG LEU C 169 15989 10510 11637 -2337 -1344 -3293 C ATOM 2382 CD1 LEU C 169 42.036 54.098 24.349 1.00103.00 C ANISOU 2382 CD1 LEU C 169 16623 10893 11620 -2490 -1605 -3363 C ATOM 2383 CD2 LEU C 169 41.658 53.447 21.965 1.00 97.38 C ANISOU 2383 CD2 LEU C 169 15283 10288 11428 -2261 -1434 -2970 C ATOM 2384 N HIS C 170 37.152 53.335 21.417 1.00 96.28 N ANISOU 2384 N HIS C 170 15042 10044 11494 -1876 -315 -3385 N ATOM 2385 CA HIS C 170 36.703 52.603 20.225 1.00 93.69 C ANISOU 2385 CA HIS C 170 14420 9817 11359 -1746 -216 -3171 C ATOM 2386 C HIS C 170 35.212 52.848 19.912 1.00 93.75 C ANISOU 2386 C HIS C 170 14290 9779 11553 -1600 101 -3364 C ATOM 2387 O HIS C 170 34.389 51.931 20.052 1.00 93.25 O ANISOU 2387 O HIS C 170 14213 9860 11356 -1586 353 -3397 O ATOM 2388 CB HIS C 170 36.958 51.090 20.372 1.00 92.63 C ANISOU 2388 CB HIS C 170 14351 9899 10946 -1790 -207 -2976 C ATOM 2389 CG HIS C 170 38.379 50.723 20.688 1.00 93.98 C ANISOU 2389 CG HIS C 170 14630 10134 10944 -1890 -538 -2805 C ATOM 2390 ND1 HIS C 170 39.274 50.308 19.723 1.00 92.67 N ANISOU 2390 ND1 HIS C 170 14230 10049 10933 -1848 -751 -2532 N ATOM 2391 CD2 HIS C 170 39.048 50.676 21.866 1.00 97.15 C ANISOU 2391 CD2 HIS C 170 15339 10543 11031 -2022 -700 -2885 C ATOM 2392 CE1 HIS C 170 40.436 50.037 20.291 1.00 94.36 C ANISOU 2392 CE1 HIS C 170 14564 10322 10964 -1935 -1034 -2465 C ATOM 2393 NE2 HIS C 170 40.327 50.254 21.591 1.00 97.05 N ANISOU 2393 NE2 HIS C 170 15245 10613 11017 -2040 -1028 -2667 N ATOM 2394 N PRO C 171 34.859 54.074 19.469 1.00 94.42 N ANISOU 2394 N PRO C 171 14267 9654 11956 -1492 76 -3496 N ATOM 2395 CA PRO C 171 33.455 54.385 19.180 1.00 95.00 C ANISOU 2395 CA PRO C 171 14179 9672 12244 -1316 333 -3713 C ATOM 2396 C PRO C 171 32.784 53.304 18.335 1.00 92.31 C ANISOU 2396 C PRO C 171 13595 9511 11969 -1229 484 -3551 C ATOM 2397 O PRO C 171 31.633 52.931 18.605 1.00 93.26 O ANISOU 2397 O PRO C 171 13646 9724 12067 -1177 780 -3754 O ATOM 2398 CB PRO C 171 33.539 55.698 18.389 1.00 95.52 C ANISOU 2398 CB PRO C 171 14142 9466 12685 -1194 142 -3719 C ATOM 2399 CG PRO C 171 34.954 55.790 17.923 1.00 94.22 C ANISOU 2399 CG PRO C 171 14004 9275 12520 -1327 -174 -3417 C ATOM 2400 CD PRO C 171 35.749 55.155 19.016 1.00 94.81 C ANISOU 2400 CD PRO C 171 14303 9504 12217 -1518 -214 -3413 C ATOM 2401 N MET C 172 33.519 52.804 17.337 1.00 89.23 N ANISOU 2401 N MET C 172 13074 9178 11653 -1230 290 -3207 N ATOM 2402 CA MET C 172 33.048 51.758 16.427 1.00 86.38 C ANISOU 2402 CA MET C 172 12497 8973 11349 -1157 384 -3020 C ATOM 2403 C MET C 172 33.714 50.439 16.790 1.00 84.96 C ANISOU 2403 C MET C 172 12445 8994 10844 -1293 368 -2829 C ATOM 2404 O MET C 172 33.046 49.472 17.139 1.00 85.22 O ANISOU 2404 O MET C 172 12517 9167 10696 -1330 587 -2874 O ATOM 2405 CB MET C 172 33.392 52.123 14.979 1.00 84.18 C ANISOU 2405 CB MET C 172 12004 8608 11375 -1053 180 -2776 C ATOM 2406 CG MET C 172 32.219 52.053 13.978 1.00 81.96 C ANISOU 2406 CG MET C 172 11466 8318 11357 -867 293 -2793 C ATOM 2407 SD MET C 172 31.510 53.671 13.491 1.00 80.38 S ANISOU 2407 SD MET C 172 11183 7810 11549 -667 205 -2986 S ATOM 2408 CE MET C 172 32.895 54.807 13.615 1.00 78.87 C ANISOU 2408 CE MET C 172 11203 7396 11369 -797 -90 -2884 C ATOM 2409 N ALA C 180 25.144 46.792 14.000 1.00 75.53 N ANISOU 2409 N ALA C 180 9693 8543 10463 -896 1967 -3574 N ATOM 2410 CA ALA C 180 26.039 47.734 13.321 1.00 74.57 C ANISOU 2410 CA ALA C 180 9592 8221 10522 -726 1611 -3388 C ATOM 2411 C ALA C 180 25.432 48.211 11.972 1.00 74.12 C ANISOU 2411 C ALA C 180 9209 8085 10869 -479 1444 -3359 C ATOM 2412 O ALA C 180 24.796 49.288 11.914 1.00 76.59 O ANISOU 2412 O ALA C 180 9366 8269 11465 -288 1414 -3602 O ATOM 2413 CB ALA C 180 27.452 47.094 13.122 1.00 71.79 C ANISOU 2413 CB ALA C 180 9482 7869 9927 -840 1394 -3005 C ATOM 2414 N GLU C 181 25.642 47.402 10.921 1.00 70.55 N ANISOU 2414 N GLU C 181 8681 7698 10428 -477 1321 -3071 N ATOM 2415 CA GLU C 181 25.081 47.555 9.561 1.00 69.20 C ANISOU 2415 CA GLU C 181 8240 7485 10567 -281 1154 -2994 C ATOM 2416 C GLU C 181 25.070 46.152 8.941 1.00 66.05 C ANISOU 2416 C GLU C 181 7805 7258 10031 -390 1196 -2778 C ATOM 2417 O GLU C 181 25.627 45.221 9.525 1.00 64.61 O ANISOU 2417 O GLU C 181 7829 7179 9539 -588 1306 -2667 O ATOM 2418 CB GLU C 181 25.955 48.476 8.679 1.00 68.18 C ANISOU 2418 CB GLU C 181 8183 7141 10581 -150 806 -2759 C ATOM 2419 CG GLU C 181 25.881 49.993 8.974 1.00 70.66 C ANISOU 2419 CG GLU C 181 8525 7217 11104 0 691 -2950 C ATOM 2420 CD GLU C 181 24.662 50.677 8.359 1.00 73.30 C ANISOU 2420 CD GLU C 181 8590 7451 11809 263 621 -3163 C ATOM 2421 OE1 GLU C 181 24.107 50.165 7.356 1.00 73.91 O ANISOU 2421 OE1 GLU C 181 8471 7599 12012 347 551 -3069 O ATOM 2422 OE2 GLU C 181 24.256 51.737 8.878 1.00 74.98 O ANISOU 2422 OE2 GLU C 181 8790 7505 12195 400 616 -3438 O ATOM 2423 N LYS C 182 24.450 45.986 7.773 1.00 64.74 N ANISOU 2423 N LYS C 182 7405 7107 10086 -259 1087 -2720 N ATOM 2424 CA LYS C 182 24.600 44.720 7.019 1.00 62.35 C ANISOU 2424 CA LYS C 182 7101 6932 9658 -350 1071 -2481 C ATOM 2425 C LYS C 182 26.070 44.461 6.659 1.00 58.55 C ANISOU 2425 C LYS C 182 6862 6404 8980 -406 882 -2133 C ATOM 2426 O LYS C 182 26.787 45.375 6.238 1.00 57.70 O ANISOU 2426 O LYS C 182 6811 6149 8962 -313 665 -2011 O ATOM 2427 CB LYS C 182 23.759 44.719 5.735 1.00 62.76 C ANISOU 2427 CB LYS C 182 6878 6986 9982 -185 932 -2471 C ATOM 2428 CG LYS C 182 22.441 43.944 5.828 1.00 67.51 C ANISOU 2428 CG LYS C 182 7229 7766 10657 -244 1157 -2702 C ATOM 2429 CD LYS C 182 21.318 44.684 5.077 1.00 72.80 C ANISOU 2429 CD LYS C 182 7555 8389 11717 -1 1023 -2899 C ATOM 2430 CE LYS C 182 19.942 44.111 5.403 1.00 76.39 C ANISOU 2430 CE LYS C 182 7698 9042 12286 -68 1283 -3223 C ATOM 2431 NZ LYS C 182 18.919 45.195 5.519 1.00 80.27 N ANISOU 2431 NZ LYS C 182 7874 9483 13140 167 1262 -3583 N ATOM 2432 N GLU C 183 26.496 43.215 6.850 1.00 56.07 N ANISOU 2432 N GLU C 183 6690 6211 8402 -564 971 -1993 N ATOM 2433 CA GLU C 183 27.808 42.724 6.436 1.00 52.86 C ANISOU 2433 CA GLU C 183 6459 5801 7822 -601 807 -1690 C ATOM 2434 C GLU C 183 27.932 42.673 4.906 1.00 50.08 C ANISOU 2434 C GLU C 183 5981 5431 7614 -483 612 -1487 C ATOM 2435 O GLU C 183 27.027 42.201 4.235 1.00 50.19 O ANISOU 2435 O GLU C 183 5836 5502 7730 -445 644 -1524 O ATOM 2436 CB GLU C 183 28.026 41.323 7.019 1.00 52.47 C ANISOU 2436 CB GLU C 183 6593 5868 7477 -770 946 -1629 C ATOM 2437 CG GLU C 183 29.344 40.644 6.621 1.00 51.80 C ANISOU 2437 CG GLU C 183 6666 5795 7219 -780 779 -1350 C ATOM 2438 CD GLU C 183 29.463 39.240 7.209 1.00 53.96 C ANISOU 2438 CD GLU C 183 7152 6140 7209 -920 886 -1302 C ATOM 2439 OE1 GLU C 183 28.525 38.436 6.959 1.00 56.27 O ANISOU 2439 OE1 GLU C 183 7388 6493 7500 -980 1026 -1356 O ATOM 2440 OE2 GLU C 183 30.465 38.948 7.921 1.00 50.91 O ANISOU 2440 OE2 GLU C 183 6997 5740 6607 -972 816 -1218 O ATOM 2441 N VAL C 184 29.049 43.163 4.372 1.00 47.29 N ANISOU 2441 N VAL C 184 5704 5007 7258 -447 416 -1285 N ATOM 2442 CA VAL C 184 29.339 43.082 2.938 1.00 44.29 C ANISOU 2442 CA VAL C 184 5260 4619 6950 -372 248 -1073 C ATOM 2443 C VAL C 184 30.477 42.081 2.675 1.00 42.24 C ANISOU 2443 C VAL C 184 5117 4460 6474 -445 220 -861 C ATOM 2444 O VAL C 184 31.550 42.163 3.276 1.00 42.30 O ANISOU 2444 O VAL C 184 5244 4471 6355 -507 188 -803 O ATOM 2445 CB VAL C 184 29.696 44.463 2.367 1.00 45.22 C ANISOU 2445 CB VAL C 184 5371 4571 7239 -290 57 -1009 C ATOM 2446 CG1 VAL C 184 30.142 44.371 0.920 1.00 42.25 C ANISOU 2446 CG1 VAL C 184 4985 4193 6874 -258 -100 -771 C ATOM 2447 CG2 VAL C 184 28.520 45.465 2.548 1.00 45.94 C ANISOU 2447 CG2 VAL C 184 5344 4532 7578 -165 46 -1237 C ATOM 2448 N LEU C 185 30.216 41.125 1.787 1.00 40.03 N ANISOU 2448 N LEU C 185 4789 4261 6158 -427 220 -767 N ATOM 2449 CA LEU C 185 31.169 40.087 1.418 1.00 37.21 C ANISOU 2449 CA LEU C 185 4523 3996 5618 -459 194 -596 C ATOM 2450 C LEU C 185 31.682 40.317 -0.004 1.00 35.40 C ANISOU 2450 C LEU C 185 4240 3769 5443 -400 54 -416 C ATOM 2451 O LEU C 185 30.982 40.871 -0.858 1.00 35.87 O ANISOU 2451 O LEU C 185 4210 3770 5650 -337 -18 -411 O ATOM 2452 CB LEU C 185 30.501 38.706 1.470 1.00 36.92 C ANISOU 2452 CB LEU C 185 4519 4041 5471 -501 313 -634 C ATOM 2453 CG LEU C 185 29.951 38.170 2.790 1.00 38.38 C ANISOU 2453 CG LEU C 185 4806 4240 5537 -612 488 -792 C ATOM 2454 CD1 LEU C 185 29.109 36.901 2.504 1.00 41.49 C ANISOU 2454 CD1 LEU C 185 5207 4693 5863 -675 595 -818 C ATOM 2455 CD2 LEU C 185 31.049 37.830 3.744 1.00 37.22 C ANISOU 2455 CD2 LEU C 185 4869 4094 5179 -667 471 -737 C ATOM 2456 N VAL C 186 32.891 39.845 -0.263 1.00 33.13 N ANISOU 2456 N VAL C 186 4009 3554 5024 -420 13 -278 N ATOM 2457 CA VAL C 186 33.555 40.059 -1.525 1.00 31.83 C ANISOU 2457 CA VAL C 186 3808 3417 4869 -402 -79 -118 C ATOM 2458 C VAL C 186 34.204 38.714 -1.988 1.00 31.04 C ANISOU 2458 C VAL C 186 3738 3447 4608 -383 -52 -38 C ATOM 2459 O VAL C 186 34.720 37.950 -1.166 1.00 30.28 O ANISOU 2459 O VAL C 186 3711 3399 4395 -388 -19 -70 O ATOM 2460 CB VAL C 186 34.527 41.246 -1.308 1.00 32.71 C ANISOU 2460 CB VAL C 186 3924 3475 5030 -460 -153 -71 C ATOM 2461 CG1 VAL C 186 35.945 40.822 -1.150 1.00 33.31 C ANISOU 2461 CG1 VAL C 186 4002 3668 4987 -503 -162 -2 C ATOM 2462 CG2 VAL C 186 34.331 42.344 -2.325 1.00 31.10 C ANISOU 2462 CG2 VAL C 186 3704 3164 4947 -464 -250 15 C ATOM 2463 N TRP C 187 34.106 38.388 -3.279 1.00 30.46 N ANISOU 2463 N TRP C 187 3638 3416 4519 -351 -78 53 N ATOM 2464 CA TRP C 187 34.774 37.188 -3.825 1.00 29.60 C ANISOU 2464 CA TRP C 187 3557 3422 4267 -316 -54 112 C ATOM 2465 C TRP C 187 36.277 37.423 -3.874 1.00 30.15 C ANISOU 2465 C TRP C 187 3587 3580 4291 -334 -75 177 C ATOM 2466 O TRP C 187 36.745 38.479 -4.320 1.00 30.50 O ANISOU 2466 O TRP C 187 3579 3615 4394 -400 -109 244 O ATOM 2467 CB TRP C 187 34.292 36.877 -5.245 1.00 28.94 C ANISOU 2467 CB TRP C 187 3466 3362 4166 -289 -75 178 C ATOM 2468 CG TRP C 187 33.148 35.897 -5.383 1.00 28.05 C ANISOU 2468 CG TRP C 187 3389 3236 4035 -262 -48 109 C ATOM 2469 CD1 TRP C 187 33.210 34.514 -5.253 1.00 26.64 C ANISOU 2469 CD1 TRP C 187 3291 3099 3731 -239 4 78 C ATOM 2470 CD2 TRP C 187 31.789 36.202 -5.754 1.00 26.33 C ANISOU 2470 CD2 TRP C 187 3122 2952 3931 -260 -87 57 C ATOM 2471 NE1 TRP C 187 31.960 33.968 -5.479 1.00 27.37 N ANISOU 2471 NE1 TRP C 187 3393 3157 3849 -258 19 11 N ATOM 2472 CE2 TRP C 187 31.077 34.971 -5.803 1.00 26.60 C ANISOU 2472 CE2 TRP C 187 3192 3012 3905 -266 -37 -11 C ATOM 2473 CE3 TRP C 187 31.098 37.398 -6.034 1.00 26.66 C ANISOU 2473 CE3 TRP C 187 3093 2905 4132 -246 -178 49 C ATOM 2474 CZ2 TRP C 187 29.705 34.898 -6.139 1.00 24.56 C ANISOU 2474 CZ2 TRP C 187 2859 2724 3748 -275 -65 -97 C ATOM 2475 CZ3 TRP C 187 29.737 37.328 -6.353 1.00 26.64 C ANISOU 2475 CZ3 TRP C 187 3016 2866 4240 -216 -226 -41 C ATOM 2476 CH2 TRP C 187 29.054 36.068 -6.401 1.00 26.33 C ANISOU 2476 CH2 TRP C 187 2974 2886 4145 -240 -162 -119 C ATOM 2477 N ARG C 188 37.015 36.420 -3.403 1.00 30.44 N ANISOU 2477 N ARG C 188 3650 3693 4224 -280 -65 148 N ATOM 2478 CA AARG C 188 38.472 36.453 -3.337 0.50 30.89 C ANISOU 2478 CA AARG C 188 3623 3862 4252 -271 -95 167 C ATOM 2479 CA BARG C 188 38.469 36.464 -3.364 0.50 30.64 C ANISOU 2479 CA BARG C 188 3590 3831 4222 -272 -94 169 C ATOM 2480 C ARG C 188 39.066 35.130 -3.803 1.00 31.12 C ANISOU 2480 C ARG C 188 3654 3994 4175 -155 -85 157 C ATOM 2481 O ARG C 188 38.781 34.071 -3.208 1.00 30.04 O ANISOU 2481 O ARG C 188 3642 3810 3961 -75 -104 107 O ATOM 2482 CB AARG C 188 38.935 36.723 -1.903 0.50 30.99 C ANISOU 2482 CB AARG C 188 3661 3842 4272 -289 -153 100 C ATOM 2483 CB BARG C 188 38.965 36.817 -1.959 0.50 30.65 C ANISOU 2483 CB BARG C 188 3608 3801 4237 -296 -153 105 C ATOM 2484 CG AARG C 188 38.993 38.198 -1.549 0.50 33.35 C ANISOU 2484 CG AARG C 188 3913 4077 4682 -406 -178 102 C ATOM 2485 CG BARG C 188 38.743 38.285 -1.574 0.50 31.54 C ANISOU 2485 CG BARG C 188 3697 3824 4464 -411 -170 101 C ATOM 2486 CD AARG C 188 40.252 38.847 -2.097 0.50 34.00 C ANISOU 2486 CD AARG C 188 3846 4267 4805 -479 -201 155 C ATOM 2487 CD BARG C 188 39.444 39.249 -2.533 0.50 29.76 C ANISOU 2487 CD BARG C 188 3354 3647 4306 -505 -175 188 C ATOM 2488 NE AARG C 188 40.051 40.264 -2.362 0.50 36.37 N ANISOU 2488 NE AARG C 188 4139 4472 5210 -612 -209 202 N ATOM 2489 NE BARG C 188 39.106 40.642 -2.240 0.50 28.72 N ANISOU 2489 NE BARG C 188 3248 3378 4285 -609 -210 191 N ATOM 2490 CZ AARG C 188 39.902 41.183 -1.413 0.50 37.63 C ANISOU 2490 CZ AARG C 188 4345 4514 5440 -678 -261 148 C ATOM 2491 CZ BARG C 188 39.609 41.684 -2.896 0.50 26.50 C ANISOU 2491 CZ BARG C 188 2926 3081 4063 -733 -227 271 C ATOM 2492 NH1AARG C 188 39.938 40.830 -0.131 0.50 36.64 N ANISOU 2492 NH1AARG C 188 4277 4373 5273 -637 -297 47 N ATOM 2493 NH1BARG C 188 40.457 41.482 -3.884 0.50 22.65 N ANISOU 2493 NH1BARG C 188 2351 2734 3522 -785 -182 349 N ATOM 2494 NH2AARG C 188 39.719 42.457 -1.746 0.50 38.71 N ANISOU 2494 NH2AARG C 188 4501 4531 5675 -787 -284 194 N ATOM 2495 NH2BARG C 188 39.258 42.924 -2.563 0.50 27.87 N ANISOU 2495 NH2BARG C 188 3161 3088 4340 -813 -281 265 N ATOM 2496 N PHE C 189 39.889 35.186 -4.847 1.00 31.41 N ANISOU 2496 N PHE C 189 3572 4162 4201 -154 -51 196 N ATOM 2497 CA PHE C 189 40.653 34.029 -5.247 1.00 32.67 C ANISOU 2497 CA PHE C 189 3698 4434 4281 -22 -41 151 C ATOM 2498 C PHE C 189 41.624 33.610 -4.138 1.00 33.64 C ANISOU 2498 C PHE C 189 3781 4591 4408 75 -139 72 C ATOM 2499 O PHE C 189 42.251 34.466 -3.494 1.00 34.44 O ANISOU 2499 O PHE C 189 3781 4724 4582 2 -187 62 O ATOM 2500 CB PHE C 189 41.459 34.344 -6.513 1.00 34.11 C ANISOU 2500 CB PHE C 189 3728 4781 4451 -68 46 182 C ATOM 2501 CG PHE C 189 42.166 33.145 -7.102 1.00 35.24 C ANISOU 2501 CG PHE C 189 3822 5051 4517 86 82 104 C ATOM 2502 CD1 PHE C 189 43.531 32.967 -6.914 1.00 38.38 C ANISOU 2502 CD1 PHE C 189 4022 5610 4952 160 73 14 C ATOM 2503 CD2 PHE C 189 41.450 32.192 -7.830 1.00 35.66 C ANISOU 2503 CD2 PHE C 189 4017 5058 4473 165 113 100 C ATOM 2504 CE1 PHE C 189 44.188 31.857 -7.462 1.00 41.34 C ANISOU 2504 CE1 PHE C 189 4334 6099 5276 337 103 -91 C ATOM 2505 CE2 PHE C 189 42.092 31.066 -8.379 1.00 37.96 C ANISOU 2505 CE2 PHE C 189 4283 5446 4695 325 143 7 C ATOM 2506 CZ PHE C 189 43.457 30.896 -8.195 1.00 38.92 C ANISOU 2506 CZ PHE C 189 4201 5724 4861 425 140 -94 C ATOM 2507 N ASP C 190 41.782 32.307 -3.932 1.00 33.94 N ANISOU 2507 N ASP C 190 3915 4612 4369 241 -192 14 N ATOM 2508 CA ASP C 190 42.807 31.820 -3.020 1.00 35.94 C ANISOU 2508 CA ASP C 190 4138 4896 4621 373 -329 -63 C ATOM 2509 C ASP C 190 43.371 30.521 -3.565 1.00 37.81 C ANISOU 2509 C ASP C 190 4374 5184 4807 583 -359 -135 C ATOM 2510 O ASP C 190 42.690 29.492 -3.567 1.00 37.77 O ANISOU 2510 O ASP C 190 4597 5046 4708 663 -377 -135 O ATOM 2511 CB ASP C 190 42.239 31.650 -1.604 1.00 35.41 C ANISOU 2511 CB ASP C 190 4304 4655 4495 358 -433 -63 C ATOM 2512 CG ASP C 190 43.303 31.298 -0.577 1.00 37.95 C ANISOU 2512 CG ASP C 190 4626 4989 4804 484 -625 -130 C ATOM 2513 OD1 ASP C 190 44.439 30.930 -0.966 1.00 41.39 O ANISOU 2513 OD1 ASP C 190 4873 5563 5292 633 -692 -199 O ATOM 2514 OD2 ASP C 190 43.004 31.381 0.631 1.00 36.59 O ANISOU 2514 OD2 ASP C 190 4643 4694 4566 439 -715 -128 O ATOM 2515 N SER C 191 44.613 30.561 -4.034 1.00 40.15 N ANISOU 2515 N SER C 191 4412 5673 5171 668 -359 -214 N ATOM 2516 CA SER C 191 45.195 29.373 -4.670 1.00 43.32 C ANISOU 2516 CA SER C 191 4777 6139 5542 893 -370 -317 C ATOM 2517 C SER C 191 45.409 28.217 -3.675 1.00 43.99 C ANISOU 2517 C SER C 191 5058 6074 5583 1122 -590 -380 C ATOM 2518 O SER C 191 45.434 27.061 -4.062 1.00 45.03 O ANISOU 2518 O SER C 191 5305 6146 5658 1310 -625 -442 O ATOM 2519 CB SER C 191 46.493 29.716 -5.421 1.00 45.24 C ANISOU 2519 CB SER C 191 4653 6655 5880 922 -288 -422 C ATOM 2520 OG SER C 191 47.425 30.295 -4.538 1.00 48.68 O ANISOU 2520 OG SER C 191 4892 7178 6428 917 -412 -476 O ATOM 2521 N LYS C 192 45.524 28.536 -2.394 1.00 44.45 N ANISOU 2521 N LYS C 192 5194 6047 5647 1098 -750 -360 N ATOM 2522 CA LYS C 192 45.622 27.491 -1.361 1.00 45.97 C ANISOU 2522 CA LYS C 192 5658 6055 5755 1284 -983 -388 C ATOM 2523 C LYS C 192 44.383 26.574 -1.333 1.00 44.64 C ANISOU 2523 C LYS C 192 5882 5648 5432 1258 -949 -316 C ATOM 2524 O LYS C 192 44.493 25.393 -1.013 1.00 46.34 O ANISOU 2524 O LYS C 192 6338 5706 5562 1442 -1103 -349 O ATOM 2525 CB LYS C 192 45.876 28.096 0.029 1.00 46.19 C ANISOU 2525 CB LYS C 192 5744 6030 5778 1219 -1154 -368 C ATOM 2526 CG LYS C 192 47.171 28.925 0.139 1.00 47.45 C ANISOU 2526 CG LYS C 192 5518 6413 6096 1240 -1233 -457 C ATOM 2527 CD LYS C 192 47.561 29.236 1.605 1.00 49.61 C ANISOU 2527 CD LYS C 192 5897 6612 6342 1236 -1480 -465 C ATOM 2528 CE LYS C 192 46.611 30.255 2.277 1.00 50.27 C ANISOU 2528 CE LYS C 192 6146 6595 6358 951 -1382 -361 C ATOM 2529 NZ LYS C 192 46.030 31.262 1.324 1.00 47.01 N ANISOU 2529 NZ LYS C 192 5558 6275 6028 732 -1105 -305 N ATOM 2530 N LEU C 193 43.216 27.113 -1.673 1.00 41.69 N ANISOU 2530 N LEU C 193 5570 5240 5028 1028 -760 -227 N ATOM 2531 CA LEU C 193 41.998 26.304 -1.713 1.00 40.43 C ANISOU 2531 CA LEU C 193 5730 4887 4744 963 -705 -178 C ATOM 2532 C LEU C 193 42.041 25.096 -2.693 1.00 41.44 C ANISOU 2532 C LEU C 193 5939 4977 4829 1129 -698 -232 C ATOM 2533 O LEU C 193 41.171 24.216 -2.637 1.00 40.96 O ANISOU 2533 O LEU C 193 6179 4729 4656 1092 -694 -207 O ATOM 2534 CB LEU C 193 40.792 27.183 -2.018 1.00 37.88 C ANISOU 2534 CB LEU C 193 5377 4573 4442 710 -515 -107 C ATOM 2535 CG LEU C 193 40.498 28.285 -1.007 1.00 35.72 C ANISOU 2535 CG LEU C 193 5087 4288 4197 541 -507 -72 C ATOM 2536 CD1 LEU C 193 39.472 29.214 -1.613 1.00 30.95 C ANISOU 2536 CD1 LEU C 193 4375 3720 3665 356 -336 -31 C ATOM 2537 CD2 LEU C 193 40.015 27.717 0.312 1.00 35.06 C ANISOU 2537 CD2 LEU C 193 5336 4013 3970 493 -586 -63 C ATOM 2538 N ALA C 194 43.044 25.067 -3.574 1.00 42.25 N ANISOU 2538 N ALA C 194 5776 5260 5017 1292 -684 -321 N ATOM 2539 CA ALA C 194 43.228 23.957 -4.510 1.00 43.76 C ANISOU 2539 CA ALA C 194 6024 5431 5171 1477 -676 -408 C ATOM 2540 C ALA C 194 43.865 22.750 -3.814 1.00 46.21 C ANISOU 2540 C ALA C 194 6545 5571 5441 1751 -920 -486 C ATOM 2541 O ALA C 194 43.785 21.618 -4.305 1.00 47.69 O ANISOU 2541 O ALA C 194 6918 5635 5568 1906 -958 -549 O ATOM 2542 CB ALA C 194 44.103 24.403 -5.689 1.00 44.26 C ANISOU 2542 CB ALA C 194 5718 5770 5329 1541 -544 -499 C ATOM 2543 N PHE C 195 44.519 22.984 -2.681 1.00 47.03 N ANISOU 2543 N PHE C 195 6641 5653 5574 1821 -1109 -486 N ATOM 2544 CA PHE C 195 45.221 21.902 -2.026 1.00 50.64 C ANISOU 2544 CA PHE C 195 7298 5942 5999 2111 -1390 -560 C ATOM 2545 C PHE C 195 44.791 21.596 -0.595 1.00 50.89 C ANISOU 2545 C PHE C 195 7744 5708 5885 2045 -1586 -455 C ATOM 2546 O PHE C 195 45.075 20.536 -0.082 1.00 52.70 O ANISOU 2546 O PHE C 195 8279 5714 6032 2251 -1827 -479 O ATOM 2547 CB PHE C 195 46.742 22.016 -2.201 1.00 53.06 C ANISOU 2547 CB PHE C 195 7219 6466 6477 2387 -1513 -727 C ATOM 2548 CG PHE C 195 47.341 23.316 -1.717 1.00 56.25 C ANISOU 2548 CG PHE C 195 7287 7088 6996 2263 -1509 -719 C ATOM 2549 CD1 PHE C 195 47.623 23.521 -0.346 1.00 58.73 C ANISOU 2549 CD1 PHE C 195 7733 7301 7281 2273 -1758 -679 C ATOM 2550 CD2 PHE C 195 47.696 24.318 -2.632 1.00 57.49 C ANISOU 2550 CD2 PHE C 195 7018 7548 7279 2132 -1272 -760 C ATOM 2551 CE1 PHE C 195 48.221 24.727 0.122 1.00 60.43 C ANISOU 2551 CE1 PHE C 195 7641 7712 7606 2154 -1773 -688 C ATOM 2552 CE2 PHE C 195 48.303 25.534 -2.184 1.00 59.57 C ANISOU 2552 CE2 PHE C 195 6980 8000 7655 1997 -1276 -760 C ATOM 2553 CZ PHE C 195 48.569 25.735 -0.803 1.00 60.66 C ANISOU 2553 CZ PHE C 195 7233 8036 7780 2013 -1530 -731 C ATOM 2554 N HIS C 196 44.088 22.535 0.042 1.00 50.13 N ANISOU 2554 N HIS C 196 7678 5625 5743 1754 -1480 -344 N ATOM 2555 CA HIS C 196 43.492 22.278 1.354 1.00 49.80 C ANISOU 2555 CA HIS C 196 8062 5340 5519 1624 -1596 -245 C ATOM 2556 C HIS C 196 41.990 22.538 1.360 1.00 47.08 C ANISOU 2556 C HIS C 196 7892 4923 5075 1286 -1345 -148 C ATOM 2557 O HIS C 196 41.555 23.659 1.166 1.00 45.51 O ANISOU 2557 O HIS C 196 7448 4885 4959 1091 -1154 -127 O ATOM 2558 CB HIS C 196 44.152 23.095 2.460 1.00 50.19 C ANISOU 2558 CB HIS C 196 8032 5454 5583 1611 -1753 -239 C ATOM 2559 CG HIS C 196 43.544 22.829 3.807 1.00 51.54 C ANISOU 2559 CG HIS C 196 8677 5380 5526 1459 -1857 -143 C ATOM 2560 ND1 HIS C 196 42.709 23.728 4.442 1.00 48.62 N ANISOU 2560 ND1 HIS C 196 8360 5029 5086 1150 -1685 -79 N ATOM 2561 CD2 HIS C 196 43.596 21.731 4.602 1.00 50.29 C ANISOU 2561 CD2 HIS C 196 8994 4941 5174 1559 -2098 -104 C ATOM 2562 CE1 HIS C 196 42.312 23.211 5.593 1.00 49.56 C ANISOU 2562 CE1 HIS C 196 8948 4915 4966 1051 -1795 -12 C ATOM 2563 NE2 HIS C 196 42.826 21.996 5.706 1.00 51.12 N ANISOU 2563 NE2 HIS C 196 9432 4918 5075 1284 -2051 -11 N ATOM 2564 N HIS C 197 41.208 21.497 1.611 1.00 47.75 N ANISOU 2564 N HIS C 197 8400 4754 4989 1216 -1358 -101 N ATOM 2565 CA HIS C 197 39.758 21.613 1.619 1.00 45.99 C ANISOU 2565 CA HIS C 197 8323 4469 4682 891 -1120 -40 C ATOM 2566 C HIS C 197 39.301 22.214 2.937 1.00 46.61 C ANISOU 2566 C HIS C 197 8571 4495 4643 662 -1093 16 C ATOM 2567 O HIS C 197 38.908 21.499 3.862 1.00 47.58 O ANISOU 2567 O HIS C 197 9136 4390 4553 555 -1160 68 O ATOM 2568 CB HIS C 197 39.110 20.242 1.383 1.00 47.13 C ANISOU 2568 CB HIS C 197 8857 4365 4685 864 -1131 -24 C ATOM 2569 CG HIS C 197 37.664 20.315 1.004 1.00 44.80 C ANISOU 2569 CG HIS C 197 8591 4065 4365 553 -869 -3 C ATOM 2570 ND1 HIS C 197 36.882 19.191 0.845 1.00 44.52 N ANISOU 2570 ND1 HIS C 197 8900 3815 4202 438 -840 9 N ATOM 2571 CD2 HIS C 197 36.857 21.375 0.752 1.00 43.02 C ANISOU 2571 CD2 HIS C 197 8084 4020 4241 338 -644 -7 C ATOM 2572 CE1 HIS C 197 35.660 19.552 0.496 1.00 44.15 C ANISOU 2572 CE1 HIS C 197 8746 3841 4187 159 -602 2 C ATOM 2573 NE2 HIS C 197 35.614 20.873 0.444 1.00 42.98 N ANISOU 2573 NE2 HIS C 197 8220 3929 4182 111 -488 -10 N ATOM 2574 N MET C 198 39.374 23.540 3.020 1.00 45.63 N ANISOU 2574 N MET C 198 8117 4576 4644 579 -993 2 N ATOM 2575 CA MET C 198 39.104 24.244 4.270 1.00 46.65 C ANISOU 2575 CA MET C 198 8367 4682 4676 394 -976 24 C ATOM 2576 C MET C 198 37.721 23.930 4.844 1.00 47.28 C ANISOU 2576 C MET C 198 8762 4620 4584 90 -785 51 C ATOM 2577 O MET C 198 37.581 23.704 6.040 1.00 49.42 O ANISOU 2577 O MET C 198 9384 4748 4644 -31 -838 81 O ATOM 2578 CB MET C 198 39.274 25.759 4.094 1.00 44.58 C ANISOU 2578 CB MET C 198 7691 4648 4599 339 -872 -10 C ATOM 2579 CG MET C 198 39.030 26.523 5.363 1.00 45.18 C ANISOU 2579 CG MET C 198 7886 4700 4578 162 -854 -13 C ATOM 2580 SD MET C 198 40.313 26.201 6.608 1.00 49.40 S ANISOU 2580 SD MET C 198 8669 5139 4963 326 -1206 -2 S ATOM 2581 CE MET C 198 41.567 27.396 6.162 1.00 50.28 C ANISOU 2581 CE MET C 198 8265 5503 5335 479 -1307 -63 C ATOM 2582 N ALA C 199 36.705 23.935 3.990 1.00 46.63 N ANISOU 2582 N ALA C 199 8546 4588 4586 -45 -563 31 N ATOM 2583 CA ALA C 199 35.331 23.672 4.420 1.00 48.19 C ANISOU 2583 CA ALA C 199 8956 4692 4661 -353 -351 22 C ATOM 2584 C ALA C 199 35.198 22.333 5.173 1.00 51.66 C ANISOU 2584 C ALA C 199 9939 4862 4825 -434 -441 78 C ATOM 2585 O ALA C 199 34.430 22.225 6.132 1.00 53.24 O ANISOU 2585 O ALA C 199 10420 4970 4840 -710 -311 81 O ATOM 2586 CB ALA C 199 34.376 23.729 3.220 1.00 45.65 C ANISOU 2586 CB ALA C 199 8384 4466 4497 -437 -162 -20 C ATOM 2587 N ARG C 200 35.967 21.338 4.742 1.00 54.03 N ANISOU 2587 N ARG C 200 10399 5033 5095 -197 -661 114 N ATOM 2588 CA ARG C 200 35.967 20.011 5.345 1.00 58.68 C ANISOU 2588 CA ARG C 200 11544 5322 5432 -227 -804 179 C ATOM 2589 C ARG C 200 36.727 19.988 6.656 1.00 61.50 C ANISOU 2589 C ARG C 200 12223 5550 5593 -169 -1032 236 C ATOM 2590 O ARG C 200 36.408 19.191 7.522 1.00 64.14 O ANISOU 2590 O ARG C 200 13083 5635 5652 -332 -1083 304 O ATOM 2591 CB ARG C 200 36.570 18.985 4.388 1.00 59.32 C ANISOU 2591 CB ARG C 200 11676 5294 5571 53 -987 174 C ATOM 2592 CG ARG C 200 36.481 17.536 4.862 1.00 64.01 C ANISOU 2592 CG ARG C 200 12878 5528 5916 25 -1146 240 C ATOM 2593 CD ARG C 200 36.674 16.627 3.664 1.00 65.02 C ANISOU 2593 CD ARG C 200 12988 5576 6141 234 -1223 196 C ATOM 2594 NE ARG C 200 36.363 15.238 3.944 1.00 69.79 N ANISOU 2594 NE ARG C 200 14177 5814 6524 158 -1336 252 N ATOM 2595 CZ ARG C 200 35.977 14.363 3.013 1.00 72.56 C ANISOU 2595 CZ ARG C 200 14620 6047 6901 165 -1307 213 C ATOM 2596 NH1 ARG C 200 35.826 14.754 1.744 1.00 69.17 N ANISOU 2596 NH1 ARG C 200 13731 5856 6694 240 -1162 120 N ATOM 2597 NH2 ARG C 200 35.724 13.099 3.349 1.00 74.39 N ANISOU 2597 NH2 ARG C 200 15437 5909 6920 80 -1428 271 N ATOM 2598 N GLU C 201 37.740 20.845 6.788 1.00 62.22 N ANISOU 2598 N GLU C 201 12020 5806 5815 48 -1180 208 N ATOM 2599 CA GLU C 201 38.403 21.045 8.070 1.00 65.49 C ANISOU 2599 CA GLU C 201 12687 6139 6056 77 -1395 245 C ATOM 2600 C GLU C 201 37.419 21.671 9.049 1.00 66.35 C ANISOU 2600 C GLU C 201 12951 6265 5996 -301 -1148 246 C ATOM 2601 O GLU C 201 37.420 21.335 10.224 1.00 69.27 O ANISOU 2601 O GLU C 201 13788 6455 6076 -428 -1247 304 O ATOM 2602 CB GLU C 201 39.653 21.929 7.960 1.00 64.77 C ANISOU 2602 CB GLU C 201 12187 6253 6170 354 -1588 190 C ATOM 2603 CG GLU C 201 40.243 22.313 9.344 1.00 68.00 C ANISOU 2603 CG GLU C 201 12829 6606 6402 343 -1804 213 C ATOM 2604 CD GLU C 201 41.223 23.502 9.320 1.00 69.36 C ANISOU 2604 CD GLU C 201 12536 7027 6791 496 -1909 139 C ATOM 2605 OE1 GLU C 201 41.884 23.710 8.277 1.00 69.86 O ANISOU 2605 OE1 GLU C 201 12160 7263 7123 718 -1937 80 O ATOM 2606 OE2 GLU C 201 41.345 24.214 10.352 1.00 68.71 O ANISOU 2606 OE2 GLU C 201 12545 6964 6597 378 -1959 133 O ATOM 2607 N LEU C 202 36.573 22.573 8.568 1.00 64.94 N ANISOU 2607 N LEU C 202 12394 6294 5987 -478 -830 174 N ATOM 2608 CA LEU C 202 35.688 23.304 9.478 1.00 65.99 C ANISOU 2608 CA LEU C 202 12595 6478 6002 -802 -582 129 C ATOM 2609 C LEU C 202 34.424 22.527 9.802 1.00 68.39 C ANISOU 2609 C LEU C 202 13248 6641 6095 -1147 -338 136 C ATOM 2610 O LEU C 202 34.064 22.418 10.975 1.00 70.43 O ANISOU 2610 O LEU C 202 13896 6794 6069 -1394 -267 148 O ATOM 2611 CB LEU C 202 35.357 24.703 8.949 1.00 62.58 C ANISOU 2611 CB LEU C 202 11613 6313 5852 -822 -377 27 C ATOM 2612 CG LEU C 202 36.555 25.644 8.854 1.00 60.73 C ANISOU 2612 CG LEU C 202 11066 6218 5790 -573 -580 14 C ATOM 2613 CD1 LEU C 202 36.134 26.920 8.151 1.00 58.37 C ANISOU 2613 CD1 LEU C 202 10272 6137 5770 -605 -379 -68 C ATOM 2614 CD2 LEU C 202 37.169 25.955 10.214 1.00 60.67 C ANISOU 2614 CD2 LEU C 202 11325 6148 5578 -598 -748 20 C ATOM 2615 N HIS C 203 33.759 21.988 8.772 1.00 68.42 N ANISOU 2615 N HIS C 203 13123 6649 6225 -1186 -206 120 N ATOM 2616 CA HIS C 203 32.561 21.174 8.981 1.00 71.04 C ANISOU 2616 CA HIS C 203 13760 6852 6379 -1535 24 116 C ATOM 2617 C HIS C 203 32.653 19.747 8.408 1.00 72.70 C ANISOU 2617 C HIS C 203 14287 6829 6507 -1474 -121 198 C ATOM 2618 O HIS C 203 32.051 19.457 7.370 1.00 71.24 O ANISOU 2618 O HIS C 203 13890 6694 6484 -1504 -3 153 O ATOM 2619 CB HIS C 203 31.314 21.896 8.457 1.00 69.84 C ANISOU 2619 CB HIS C 203 13182 6921 6434 -1751 378 -20 C ATOM 2620 CG HIS C 203 31.092 23.248 9.063 1.00 71.20 C ANISOU 2620 CG HIS C 203 13086 7286 6681 -1825 536 -124 C ATOM 2621 ND1 HIS C 203 30.313 24.211 8.456 1.00 70.99 N ANISOU 2621 ND1 HIS C 203 12562 7481 6931 -1866 752 -257 N ATOM 2622 CD2 HIS C 203 31.548 23.803 10.214 1.00 74.02 C ANISOU 2622 CD2 HIS C 203 13619 7634 6872 -1854 490 -125 C ATOM 2623 CE1 HIS C 203 30.311 25.304 9.200 1.00 71.71 C ANISOU 2623 CE1 HIS C 203 12531 7679 7035 -1906 838 -340 C ATOM 2624 NE2 HIS C 203 31.057 25.085 10.269 1.00 74.08 N ANISOU 2624 NE2 HIS C 203 13230 7851 7065 -1908 691 -264 N ATOM 2625 N PRO C 204 33.386 18.844 9.100 1.00 76.08 N ANISOU 2625 N PRO C 204 15250 6981 6675 -1386 -398 312 N ATOM 2626 CA PRO C 204 33.493 17.438 8.695 1.00 78.68 C ANISOU 2626 CA PRO C 204 15969 7028 6898 -1325 -565 389 C ATOM 2627 C PRO C 204 32.130 16.745 8.538 1.00 80.89 C ANISOU 2627 C PRO C 204 16445 7215 7074 -1739 -272 369 C ATOM 2628 O PRO C 204 31.985 15.846 7.704 1.00 81.05 O ANISOU 2628 O PRO C 204 16549 7101 7143 -1691 -327 379 O ATOM 2629 CB PRO C 204 34.293 16.799 9.837 1.00 81.96 C ANISOU 2629 CB PRO C 204 16994 7151 6995 -1251 -881 511 C ATOM 2630 CG PRO C 204 34.258 17.780 10.964 1.00 81.35 C ANISOU 2630 CG PRO C 204 16920 7201 6788 -1414 -787 497 C ATOM 2631 CD PRO C 204 34.184 19.112 10.312 1.00 78.03 C ANISOU 2631 CD PRO C 204 15786 7149 6713 -1322 -606 372 C ATOM 2632 N GLU C 205 31.154 17.199 9.327 1.00 82.84 N ANISOU 2632 N GLU C 205 16737 7550 7191 -2144 43 321 N ATOM 2633 CA GLU C 205 29.768 16.709 9.319 1.00 85.27 C ANISOU 2633 CA GLU C 205 17160 7830 7411 -2604 380 265 C ATOM 2634 C GLU C 205 29.036 16.825 7.981 1.00 83.42 C ANISOU 2634 C GLU C 205 16415 7782 7499 -2604 542 149 C ATOM 2635 O GLU C 205 28.152 16.010 7.697 1.00 85.48 O ANISOU 2635 O GLU C 205 16838 7940 7702 -2895 691 126 O ATOM 2636 CB GLU C 205 28.947 17.412 10.413 1.00 86.94 C ANISOU 2636 CB GLU C 205 17388 8177 7467 -2996 714 184 C ATOM 2637 CG GLU C 205 28.852 18.946 10.289 1.00 85.44 C ANISOU 2637 CG GLU C 205 16563 8343 7557 -2881 864 41 C ATOM 2638 CD GLU C 205 29.992 19.699 10.987 1.00 86.90 C ANISOU 2638 CD GLU C 205 16779 8552 7689 -2612 632 93 C ATOM 2639 OE1 GLU C 205 31.014 19.081 11.364 1.00 89.09 O ANISOU 2639 OE1 GLU C 205 17469 8602 7779 -2415 294 235 O ATOM 2640 OE2 GLU C 205 29.860 20.928 11.165 1.00 85.99 O ANISOU 2640 OE2 GLU C 205 16267 8677 7726 -2593 771 -21 O ATOM 2641 N TYR C 206 29.389 17.827 7.170 1.00 80.39 N ANISOU 2641 N TYR C 206 15444 7662 7440 -2302 505 79 N ATOM 2642 CA TYR C 206 28.787 18.004 5.841 1.00 78.42 C ANISOU 2642 CA TYR C 206 14723 7586 7487 -2262 606 -19 C ATOM 2643 C TYR C 206 29.191 16.890 4.894 1.00 78.49 C ANISOU 2643 C TYR C 206 14911 7405 7505 -2079 394 40 C ATOM 2644 O TYR C 206 28.601 16.746 3.812 1.00 77.54 O ANISOU 2644 O TYR C 206 14528 7371 7562 -2104 466 -34 O ATOM 2645 CB TYR C 206 29.229 19.324 5.180 1.00 75.86 C ANISOU 2645 CB TYR C 206 13806 7548 7470 -1962 570 -77 C ATOM 2646 CG TYR C 206 28.553 20.621 5.613 1.00 76.15 C ANISOU 2646 CG TYR C 206 13472 7829 7631 -2110 812 -196 C ATOM 2647 CD1 TYR C 206 27.312 20.631 6.258 1.00 78.59 C ANISOU 2647 CD1 TYR C 206 13820 8180 7861 -2513 1121 -304 C ATOM 2648 CD2 TYR C 206 29.151 21.853 5.321 1.00 74.84 C ANISOU 2648 CD2 TYR C 206 12899 7856 7680 -1844 738 -218 C ATOM 2649 CE1 TYR C 206 26.705 21.834 6.627 1.00 78.66 C ANISOU 2649 CE1 TYR C 206 13464 8413 8009 -2607 1337 -447 C ATOM 2650 CE2 TYR C 206 28.555 23.050 5.681 1.00 74.24 C ANISOU 2650 CE2 TYR C 206 12501 7972 7733 -1947 933 -336 C ATOM 2651 CZ TYR C 206 27.336 23.038 6.330 1.00 76.68 C ANISOU 2651 CZ TYR C 206 12844 8318 7973 -2307 1226 -459 C ATOM 2652 OH TYR C 206 26.760 24.232 6.689 1.00 77.35 O ANISOU 2652 OH TYR C 206 12596 8590 8203 -2374 1414 -607 O ATOM 2653 N TYR C 207 30.210 16.120 5.279 1.00 79.68 N ANISOU 2653 N TYR C 207 15505 7297 7473 -1875 111 158 N ATOM 2654 CA TYR C 207 30.826 15.160 4.351 1.00 79.93 C ANISOU 2654 CA TYR C 207 15672 7154 7545 -1598 -132 190 C ATOM 2655 C TYR C 207 30.702 13.677 4.747 1.00 83.58 C ANISOU 2655 C TYR C 207 16814 7213 7728 -1753 -246 274 C ATOM 2656 O TYR C 207 31.069 12.805 3.960 1.00 84.03 O ANISOU 2656 O TYR C 207 17012 7099 7819 -1551 -428 276 O ATOM 2657 CB TYR C 207 32.292 15.542 4.052 1.00 78.02 C ANISOU 2657 CB TYR C 207 15238 6976 7429 -1097 -419 213 C ATOM 2658 CG TYR C 207 32.455 16.921 3.440 1.00 74.29 C ANISOU 2658 CG TYR C 207 14118 6872 7238 -949 -320 137 C ATOM 2659 CD1 TYR C 207 32.391 17.108 2.063 1.00 72.13 C ANISOU 2659 CD1 TYR C 207 13451 6763 7193 -803 -287 67 C ATOM 2660 CD2 TYR C 207 32.673 18.041 4.245 1.00 72.31 C ANISOU 2660 CD2 TYR C 207 13686 6784 7003 -967 -269 138 C ATOM 2661 CE1 TYR C 207 32.538 18.372 1.504 1.00 68.36 C ANISOU 2661 CE1 TYR C 207 12440 6589 6945 -688 -209 17 C ATOM 2662 CE2 TYR C 207 32.814 19.296 3.707 1.00 69.08 C ANISOU 2662 CE2 TYR C 207 12735 6670 6841 -849 -192 78 C ATOM 2663 CZ TYR C 207 32.747 19.464 2.336 1.00 67.18 C ANISOU 2663 CZ TYR C 207 12131 6575 6819 -714 -164 26 C ATOM 2664 OH TYR C 207 32.890 20.723 1.801 1.00 62.19 O ANISOU 2664 OH TYR C 207 11013 6207 6408 -615 -100 -16 O ATOM 2665 N LYS C 208 30.178 13.401 5.944 1.00 86.48 N ANISOU 2665 N LYS C 208 17622 7423 7814 -2122 -132 337 N ATOM 2666 CA LYS C 208 29.985 12.017 6.423 1.00 90.74 C ANISOU 2666 CA LYS C 208 18884 7546 8047 -2339 -227 437 C ATOM 2667 C LYS C 208 28.785 11.338 5.764 1.00 91.79 C ANISOU 2667 C LYS C 208 19042 7631 8203 -2705 -1 367 C ATOM 2668 O LYS C 208 28.851 10.919 4.604 1.00 91.28 O ANISOU 2668 O LYS C 208 18814 7552 8316 -2518 -94 312 O ATOM 2669 CB LYS C 208 29.840 11.974 7.950 1.00 93.51 C ANISOU 2669 CB LYS C 208 19742 7744 8044 -2650 -169 537 C TER 2670 LYS C 208 ATOM 2671 N ASP D 80 38.497 7.425 -38.206 1.00 87.18 N ANISOU 2671 N ASP D 80 15611 10306 7207 4403 -609 -2441 N ATOM 2672 CA ASP D 80 37.306 6.524 -38.291 1.00 87.55 C ANISOU 2672 CA ASP D 80 16449 9583 7232 4132 -828 -2322 C ATOM 2673 C ASP D 80 35.973 7.201 -37.922 1.00 82.13 C ANISOU 2673 C ASP D 80 15744 8720 6741 3323 -776 -1928 C ATOM 2674 O ASP D 80 35.015 7.101 -38.688 1.00 81.81 O ANISOU 2674 O ASP D 80 15929 8485 6669 2919 -779 -1900 O ATOM 2675 CB ASP D 80 37.514 5.236 -37.477 1.00 92.02 C ANISOU 2675 CB ASP D 80 17725 9516 7722 4614 -1177 -2396 C ATOM 2676 CG ASP D 80 37.926 4.048 -38.342 1.00 99.19 C ANISOU 2676 CG ASP D 80 19169 10139 8378 5203 -1352 -2797 C ATOM 2677 OD1 ASP D 80 37.582 4.017 -39.545 1.00100.85 O ANISOU 2677 OD1 ASP D 80 19412 10426 8479 5033 -1237 -2944 O ATOM 2678 OD2 ASP D 80 38.586 3.124 -37.815 1.00105.20 O ANISOU 2678 OD2 ASP D 80 20373 10572 9026 5875 -1639 -2981 O ATOM 2679 N ILE D 81 35.892 7.870 -36.770 1.00 78.12 N ANISOU 2679 N ILE D 81 14958 8304 6417 3114 -748 -1664 N ATOM 2680 CA ILE D 81 34.629 8.524 -36.383 1.00 73.21 C ANISOU 2680 CA ILE D 81 14269 7576 5971 2408 -697 -1348 C ATOM 2681 C ILE D 81 34.623 10.006 -36.722 1.00 68.79 C ANISOU 2681 C ILE D 81 13030 7587 5521 2115 -463 -1243 C ATOM 2682 O ILE D 81 35.250 10.816 -36.033 1.00 66.85 O ANISOU 2682 O ILE D 81 12342 7686 5372 2178 -366 -1160 O ATOM 2683 CB ILE D 81 34.254 8.353 -34.897 1.00 72.44 C ANISOU 2683 CB ILE D 81 14383 7163 5979 2244 -806 -1105 C ATOM 2684 CG1 ILE D 81 34.512 6.920 -34.421 1.00 77.39 C ANISOU 2684 CG1 ILE D 81 15774 7189 6441 2613 -1068 -1187 C ATOM 2685 CG2 ILE D 81 32.786 8.731 -34.707 1.00 69.30 C ANISOU 2685 CG2 ILE D 81 13993 6629 5710 1522 -760 -882 C ATOM 2686 CD1 ILE D 81 34.156 6.685 -32.967 1.00 78.87 C ANISOU 2686 CD1 ILE D 81 16288 7028 6652 2421 -1173 -929 C ATOM 2687 N ILE D 82 33.894 10.336 -37.788 1.00 67.31 N ANISOU 2687 N ILE D 82 12826 7457 5293 1791 -408 -1253 N ATOM 2688 CA ILE D 82 33.815 11.687 -38.341 1.00 63.66 C ANISOU 2688 CA ILE D 82 11887 7439 4861 1520 -233 -1161 C ATOM 2689 C ILE D 82 32.441 12.275 -38.034 1.00 60.00 C ANISOU 2689 C ILE D 82 11388 6844 4567 1003 -304 -943 C ATOM 2690 O ILE D 82 31.414 11.623 -38.266 1.00 60.58 O ANISOU 2690 O ILE D 82 11786 6594 4639 773 -446 -966 O ATOM 2691 CB ILE D 82 34.063 11.659 -39.878 1.00 65.81 C ANISOU 2691 CB ILE D 82 12208 7906 4890 1604 -147 -1361 C ATOM 2692 CG1 ILE D 82 35.432 11.037 -40.196 1.00 70.14 C ANISOU 2692 CG1 ILE D 82 12728 8670 5252 2161 -55 -1653 C ATOM 2693 CG2 ILE D 82 33.909 13.039 -40.520 1.00 63.91 C ANISOU 2693 CG2 ILE D 82 11633 8037 4614 1282 0 -1232 C ATOM 2694 CD1 ILE D 82 36.640 11.856 -39.768 1.00 70.39 C ANISOU 2694 CD1 ILE D 82 12195 9246 5304 2321 153 -1673 C ATOM 2695 N VAL D 83 32.424 13.494 -37.496 1.00 55.91 N ANISOU 2695 N VAL D 83 10465 6592 4185 825 -217 -768 N ATOM 2696 CA VAL D 83 31.167 14.189 -37.241 1.00 53.22 C ANISOU 2696 CA VAL D 83 10016 6210 3994 421 -292 -617 C ATOM 2697 C VAL D 83 31.099 15.556 -37.922 1.00 51.48 C ANISOU 2697 C VAL D 83 9527 6288 3746 285 -239 -546 C ATOM 2698 O VAL D 83 32.124 16.182 -38.194 1.00 51.63 O ANISOU 2698 O VAL D 83 9370 6578 3670 404 -87 -541 O ATOM 2699 CB VAL D 83 30.895 14.378 -35.725 1.00 51.75 C ANISOU 2699 CB VAL D 83 9704 5959 4001 306 -298 -465 C ATOM 2700 CG1 VAL D 83 30.859 13.027 -35.004 1.00 54.28 C ANISOU 2700 CG1 VAL D 83 10422 5906 4295 378 -374 -492 C ATOM 2701 CG2 VAL D 83 31.918 15.337 -35.085 1.00 50.35 C ANISOU 2701 CG2 VAL D 83 9172 6081 3878 458 -176 -381 C ATOM 2702 N VAL D 84 29.886 16.022 -38.184 1.00 50.37 N ANISOU 2702 N VAL D 84 9370 6100 3667 26 -379 -505 N ATOM 2703 CA VAL D 84 29.696 17.375 -38.686 1.00 49.35 C ANISOU 2703 CA VAL D 84 9085 6163 3503 -74 -404 -415 C ATOM 2704 C VAL D 84 28.806 18.188 -37.758 1.00 47.90 C ANISOU 2704 C VAL D 84 8672 5992 3537 -229 -508 -318 C ATOM 2705 O VAL D 84 27.778 17.696 -37.277 1.00 48.63 O ANISOU 2705 O VAL D 84 8736 5983 3759 -366 -615 -374 O ATOM 2706 CB VAL D 84 29.138 17.398 -40.139 1.00 51.18 C ANISOU 2706 CB VAL D 84 9537 6380 3529 -125 -539 -502 C ATOM 2707 CG1 VAL D 84 27.761 16.740 -40.203 1.00 50.38 C ANISOU 2707 CG1 VAL D 84 9512 6112 3520 -279 -768 -615 C ATOM 2708 CG2 VAL D 84 29.085 18.848 -40.672 1.00 50.04 C ANISOU 2708 CG2 VAL D 84 9358 6373 3280 -193 -590 -378 C ATOM 2709 N ALA D 85 29.201 19.438 -37.524 1.00 46.85 N ANISOU 2709 N ALA D 85 8383 5996 3420 -229 -467 -197 N ATOM 2710 CA ALA D 85 28.451 20.346 -36.658 1.00 45.39 C ANISOU 2710 CA ALA D 85 7994 5834 3419 -305 -574 -136 C ATOM 2711 C ALA D 85 27.070 20.711 -37.203 1.00 46.31 C ANISOU 2711 C ALA D 85 8112 5932 3551 -358 -837 -221 C ATOM 2712 O ALA D 85 26.938 21.152 -38.336 1.00 47.44 O ANISOU 2712 O ALA D 85 8441 6064 3519 -324 -970 -226 O ATOM 2713 CB ALA D 85 29.254 21.610 -36.406 1.00 44.34 C ANISOU 2713 CB ALA D 85 7788 5796 3262 -296 -500 -5 C ATOM 2714 N LEU D 86 26.064 20.561 -36.348 1.00 46.41 N ANISOU 2714 N LEU D 86 7903 5980 3751 -437 -914 -304 N ATOM 2715 CA LEU D 86 24.684 20.950 -36.611 1.00 47.91 C ANISOU 2715 CA LEU D 86 7945 6260 4000 -454 -1175 -454 C ATOM 2716 C LEU D 86 24.391 22.397 -36.172 1.00 47.84 C ANISOU 2716 C LEU D 86 7788 6327 4061 -305 -1314 -430 C ATOM 2717 O LEU D 86 23.500 23.053 -36.715 1.00 49.65 O ANISOU 2717 O LEU D 86 7987 6611 4268 -178 -1605 -547 O ATOM 2718 CB LEU D 86 23.746 19.969 -35.896 1.00 48.65 C ANISOU 2718 CB LEU D 86 7828 6424 4231 -674 -1142 -607 C ATOM 2719 CG LEU D 86 23.129 18.756 -36.620 1.00 52.54 C ANISOU 2719 CG LEU D 86 8440 6862 4661 -871 -1214 -763 C ATOM 2720 CD1 LEU D 86 24.059 18.062 -37.609 1.00 52.11 C ANISOU 2720 CD1 LEU D 86 8786 6598 4414 -797 -1160 -703 C ATOM 2721 CD2 LEU D 86 22.517 17.762 -35.623 1.00 52.66 C ANISOU 2721 CD2 LEU D 86 8334 6893 4781 -1203 -1079 -846 C ATOM 2722 N TYR D 87 25.133 22.895 -35.183 1.00 46.31 N ANISOU 2722 N TYR D 87 7529 6125 3942 -287 -1146 -303 N ATOM 2723 CA TYR D 87 24.945 24.273 -34.700 1.00 47.05 C ANISOU 2723 CA TYR D 87 7553 6234 4090 -141 -1281 -289 C ATOM 2724 C TYR D 87 26.304 24.889 -34.425 1.00 45.59 C ANISOU 2724 C TYR D 87 7529 5951 3841 -162 -1113 -88 C ATOM 2725 O TYR D 87 27.278 24.160 -34.295 1.00 44.88 O ANISOU 2725 O TYR D 87 7461 5871 3720 -257 -876 -5 O ATOM 2726 CB TYR D 87 24.084 24.299 -33.422 1.00 47.14 C ANISOU 2726 CB TYR D 87 7191 6425 4296 -143 -1267 -439 C ATOM 2727 CG TYR D 87 22.921 23.319 -33.432 1.00 50.00 C ANISOU 2727 CG TYR D 87 7304 6967 4725 -286 -1296 -652 C ATOM 2728 CD1 TYR D 87 21.685 23.672 -33.983 1.00 53.00 C ANISOU 2728 CD1 TYR D 87 7497 7516 5125 -165 -1590 -891 C ATOM 2729 CD2 TYR D 87 23.061 22.036 -32.887 1.00 50.23 C ANISOU 2729 CD2 TYR D 87 7311 6997 4778 -554 -1050 -630 C ATOM 2730 CE1 TYR D 87 20.617 22.771 -34.003 1.00 56.29 C ANISOU 2730 CE1 TYR D 87 7625 8163 5599 -373 -1605 -1125 C ATOM 2731 CE2 TYR D 87 22.002 21.130 -32.886 1.00 53.18 C ANISOU 2731 CE2 TYR D 87 7502 7517 5186 -798 -1054 -822 C ATOM 2732 CZ TYR D 87 20.788 21.502 -33.455 1.00 57.19 C ANISOU 2732 CZ TYR D 87 7744 8256 5728 -738 -1315 -1079 C ATOM 2733 OH TYR D 87 19.750 20.605 -33.465 1.00 60.34 O ANISOU 2733 OH TYR D 87 7908 8860 6158 -1050 -1309 -1304 O ATOM 2734 N ASP D 88 26.382 26.219 -34.355 1.00 46.30 N ANISOU 2734 N ASP D 88 7744 5948 3899 -70 -1257 -34 N ATOM 2735 CA ASP D 88 27.597 26.883 -33.878 1.00 45.62 C ANISOU 2735 CA ASP D 88 7753 5803 3776 -168 -1098 122 C ATOM 2736 C ASP D 88 27.809 26.540 -32.404 1.00 43.95 C ANISOU 2736 C ASP D 88 7234 5717 3746 -185 -927 89 C ATOM 2737 O ASP D 88 26.859 26.536 -31.617 1.00 44.32 O ANISOU 2737 O ASP D 88 7064 5845 3929 -94 -1002 -44 O ATOM 2738 CB ASP D 88 27.496 28.401 -34.012 1.00 47.36 C ANISOU 2738 CB ASP D 88 8251 5829 3917 -96 -1329 171 C ATOM 2739 CG ASP D 88 27.535 28.875 -35.450 1.00 50.94 C ANISOU 2739 CG ASP D 88 9152 6099 4106 -122 -1491 266 C ATOM 2740 OD1 ASP D 88 27.811 28.067 -36.375 1.00 52.87 O ANISOU 2740 OD1 ASP D 88 9465 6408 4213 -218 -1377 297 O ATOM 2741 OD2 ASP D 88 27.262 30.070 -35.657 1.00 52.57 O ANISOU 2741 OD2 ASP D 88 9697 6068 4208 -27 -1755 302 O ATOM 2742 N TYR D 89 29.044 26.242 -32.021 1.00 42.87 N ANISOU 2742 N TYR D 89 7065 5637 3587 -295 -700 186 N ATOM 2743 CA TYR D 89 29.363 26.104 -30.600 1.00 41.01 C ANISOU 2743 CA TYR D 89 6614 5494 3475 -288 -587 172 C ATOM 2744 C TYR D 89 30.500 27.034 -30.252 1.00 41.28 C ANISOU 2744 C TYR D 89 6688 5529 3466 -380 -534 254 C ATOM 2745 O TYR D 89 31.655 26.770 -30.598 1.00 41.64 O ANISOU 2745 O TYR D 89 6728 5671 3422 -481 -380 309 O ATOM 2746 CB TYR D 89 29.684 24.660 -30.187 1.00 40.04 C ANISOU 2746 CB TYR D 89 6388 5453 3371 -288 -416 164 C ATOM 2747 CG TYR D 89 30.149 24.567 -28.737 1.00 39.44 C ANISOU 2747 CG TYR D 89 6172 5452 3359 -266 -329 174 C ATOM 2748 CD1 TYR D 89 29.268 24.860 -27.672 1.00 40.68 C ANISOU 2748 CD1 TYR D 89 6214 5641 3600 -255 -370 108 C ATOM 2749 CD2 TYR D 89 31.473 24.248 -28.427 1.00 38.83 C ANISOU 2749 CD2 TYR D 89 6060 5458 3234 -235 -219 219 C ATOM 2750 CE1 TYR D 89 29.694 24.806 -26.322 1.00 38.90 C ANISOU 2750 CE1 TYR D 89 5911 5484 3384 -238 -297 121 C ATOM 2751 CE2 TYR D 89 31.912 24.191 -27.082 1.00 39.66 C ANISOU 2751 CE2 TYR D 89 6066 5634 3369 -181 -191 220 C ATOM 2752 CZ TYR D 89 31.019 24.473 -26.043 1.00 39.34 C ANISOU 2752 CZ TYR D 89 5983 5579 3387 -196 -229 190 C ATOM 2753 OH TYR D 89 31.464 24.435 -24.733 1.00 41.52 O ANISOU 2753 OH TYR D 89 6209 5923 3644 -148 -207 195 O ATOM 2754 N TYR D 90 30.164 28.141 -29.600 1.00 41.56 N ANISOU 2754 N TYR D 90 6755 5481 3555 -348 -670 226 N ATOM 2755 CA TYR D 90 31.189 28.986 -29.030 1.00 43.22 C ANISOU 2755 CA TYR D 90 6992 5689 3741 -481 -629 276 C ATOM 2756 C TYR D 90 31.419 28.719 -27.523 1.00 42.21 C ANISOU 2756 C TYR D 90 6618 5700 3719 -419 -559 215 C ATOM 2757 O TYR D 90 30.482 28.672 -26.708 1.00 42.28 O ANISOU 2757 O TYR D 90 6534 5719 3812 -276 -619 122 O ATOM 2758 CB TYR D 90 30.912 30.471 -29.266 1.00 45.13 C ANISOU 2758 CB TYR D 90 7545 5680 3923 -515 -845 291 C ATOM 2759 CG TYR D 90 31.856 31.336 -28.465 1.00 47.61 C ANISOU 2759 CG TYR D 90 7887 5975 4228 -694 -819 308 C ATOM 2760 CD1 TYR D 90 33.056 31.798 -29.017 1.00 51.71 C ANISOU 2760 CD1 TYR D 90 8542 6503 4602 -1039 -709 409 C ATOM 2761 CD2 TYR D 90 31.570 31.662 -27.132 1.00 49.20 C ANISOU 2761 CD2 TYR D 90 7956 6195 4544 -559 -886 198 C ATOM 2762 CE1 TYR D 90 33.941 32.577 -28.264 1.00 53.87 C ANISOU 2762 CE1 TYR D 90 8807 6792 4867 -1269 -691 394 C ATOM 2763 CE2 TYR D 90 32.447 32.430 -26.364 1.00 51.03 C ANISOU 2763 CE2 TYR D 90 8216 6414 4760 -734 -887 189 C ATOM 2764 CZ TYR D 90 33.625 32.885 -26.935 1.00 53.07 C ANISOU 2764 CZ TYR D 90 8597 6670 4896 -1098 -801 284 C ATOM 2765 OH TYR D 90 34.472 33.652 -26.175 1.00 54.85 O ANISOU 2765 OH TYR D 90 8829 6906 5106 -1326 -815 245 O ATOM 2766 N SER D 91 32.688 28.580 -27.171 1.00 42.03 N ANISOU 2766 N SER D 91 6483 5822 3663 -530 -433 246 N ATOM 2767 CA SER D 91 33.105 28.406 -25.804 1.00 41.20 C ANISOU 2767 CA SER D 91 6199 5847 3609 -469 -405 197 C ATOM 2768 C SER D 91 34.283 29.343 -25.524 1.00 42.76 C ANISOU 2768 C SER D 91 6367 6116 3765 -669 -410 189 C ATOM 2769 O SER D 91 35.202 29.406 -26.321 1.00 44.34 O ANISOU 2769 O SER D 91 6538 6424 3884 -857 -315 219 O ATOM 2770 CB SER D 91 33.518 26.952 -25.594 1.00 40.13 C ANISOU 2770 CB SER D 91 5926 5863 3459 -344 -286 200 C ATOM 2771 OG SER D 91 34.237 26.809 -24.382 1.00 40.52 O ANISOU 2771 OG SER D 91 5843 6051 3503 -276 -288 163 O ATOM 2772 N PRO D 92 34.258 30.060 -24.386 1.00 43.47 N ANISOU 2772 N PRO D 92 6450 6176 3890 -660 -507 125 N ATOM 2773 CA PRO D 92 35.355 30.927 -23.921 1.00 45.27 C ANISOU 2773 CA PRO D 92 6636 6482 4083 -885 -537 84 C ATOM 2774 C PRO D 92 36.593 30.175 -23.432 1.00 45.59 C ANISOU 2774 C PRO D 92 6349 6871 4102 -875 -446 27 C ATOM 2775 O PRO D 92 37.649 30.776 -23.227 1.00 48.06 O ANISOU 2775 O PRO D 92 6534 7349 4379 -1109 -451 -40 O ATOM 2776 CB PRO D 92 34.734 31.648 -22.712 1.00 45.50 C ANISOU 2776 CB PRO D 92 6757 6380 4151 -772 -688 -6 C ATOM 2777 CG PRO D 92 33.700 30.694 -22.202 1.00 43.62 C ANISOU 2777 CG PRO D 92 6438 6183 3955 -481 -650 -25 C ATOM 2778 CD PRO D 92 33.112 30.087 -23.451 1.00 42.87 C ANISOU 2778 CD PRO D 92 6394 6021 3872 -452 -589 54 C ATOM 2779 N PHE D 93 36.466 28.877 -23.222 1.00 43.94 N ANISOU 2779 N PHE D 93 6022 6772 3902 -604 -391 33 N ATOM 2780 CA PHE D 93 37.496 28.154 -22.486 1.00 44.29 C ANISOU 2780 CA PHE D 93 5817 7099 3911 -454 -398 -48 C ATOM 2781 C PHE D 93 38.466 27.491 -23.446 1.00 45.93 C ANISOU 2781 C PHE D 93 5817 7563 4073 -444 -284 -95 C ATOM 2782 O PHE D 93 38.040 26.937 -24.459 1.00 45.43 O ANISOU 2782 O PHE D 93 5860 7406 3996 -403 -189 -33 O ATOM 2783 CB PHE D 93 36.857 27.114 -21.570 1.00 42.01 C ANISOU 2783 CB PHE D 93 5625 6734 3601 -147 -439 -17 C ATOM 2784 CG PHE D 93 35.803 27.671 -20.640 1.00 39.58 C ANISOU 2784 CG PHE D 93 5482 6252 3306 -152 -498 -8 C ATOM 2785 CD1 PHE D 93 36.166 28.457 -19.531 1.00 38.64 C ANISOU 2785 CD1 PHE D 93 5326 6199 3155 -185 -608 -95 C ATOM 2786 CD2 PHE D 93 34.451 27.390 -20.852 1.00 33.85 C ANISOU 2786 CD2 PHE D 93 4911 5344 2605 -119 -443 43 C ATOM 2787 CE1 PHE D 93 35.189 28.959 -18.649 1.00 36.91 C ANISOU 2787 CE1 PHE D 93 5249 5858 2917 -152 -646 -130 C ATOM 2788 CE2 PHE D 93 33.464 27.898 -19.984 1.00 33.44 C ANISOU 2788 CE2 PHE D 93 4934 5225 2547 -101 -470 -11 C ATOM 2789 CZ PHE D 93 33.832 28.678 -18.880 1.00 34.92 C ANISOU 2789 CZ PHE D 93 5109 5472 2689 -100 -563 -98 C ATOM 2790 N SER D 94 39.752 27.524 -23.108 1.00 48.21 N ANISOU 2790 N SER D 94 5781 8211 4325 -458 -302 -242 N ATOM 2791 CA SER D 94 40.803 26.993 -23.975 1.00 50.91 C ANISOU 2791 CA SER D 94 5821 8917 4606 -437 -179 -367 C ATOM 2792 C SER D 94 40.744 25.467 -24.118 1.00 50.80 C ANISOU 2792 C SER D 94 5837 8903 4561 36 -196 -391 C ATOM 2793 O SER D 94 41.316 24.922 -25.057 1.00 53.12 O ANISOU 2793 O SER D 94 5968 9419 4795 116 -78 -493 O ATOM 2794 CB SER D 94 42.189 27.406 -23.465 1.00 54.33 C ANISOU 2794 CB SER D 94 5809 9824 5010 -548 -219 -587 C ATOM 2795 OG SER D 94 42.501 26.741 -22.246 1.00 55.21 O ANISOU 2795 OG SER D 94 5818 10041 5120 -136 -431 -682 O ATOM 2796 N TRP D 95 40.057 24.784 -23.202 1.00 48.56 N ANISOU 2796 N TRP D 95 5804 8360 4285 325 -334 -307 N ATOM 2797 CA TRP D 95 39.977 23.318 -23.245 1.00 48.81 C ANISOU 2797 CA TRP D 95 5999 8291 4253 744 -387 -311 C ATOM 2798 C TRP D 95 38.855 22.823 -24.153 1.00 46.90 C ANISOU 2798 C TRP D 95 6080 7715 4026 683 -278 -172 C ATOM 2799 O TRP D 95 38.760 21.631 -24.416 1.00 47.65 O ANISOU 2799 O TRP D 95 6366 7680 4059 960 -306 -181 O ATOM 2800 CB TRP D 95 39.837 22.711 -21.835 1.00 48.95 C ANISOU 2800 CB TRP D 95 6226 8170 4204 1036 -588 -275 C ATOM 2801 CG TRP D 95 38.712 23.317 -21.008 1.00 46.06 C ANISOU 2801 CG TRP D 95 6102 7535 3863 810 -588 -119 C ATOM 2802 CD1 TRP D 95 37.378 23.010 -21.077 1.00 42.91 C ANISOU 2802 CD1 TRP D 95 6027 6807 3471 705 -508 32 C ATOM 2803 CD2 TRP D 95 38.837 24.340 -20.008 1.00 44.85 C ANISOU 2803 CD2 TRP D 95 5847 7475 3719 666 -668 -150 C ATOM 2804 NE1 TRP D 95 36.667 23.765 -20.162 1.00 42.05 N ANISOU 2804 NE1 TRP D 95 5987 6623 3368 540 -517 77 N ATOM 2805 CE2 TRP D 95 37.535 24.600 -19.507 1.00 43.77 C ANISOU 2805 CE2 TRP D 95 5983 7063 3585 525 -620 -25 C ATOM 2806 CE3 TRP D 95 39.919 25.065 -19.493 1.00 46.35 C ANISOU 2806 CE3 TRP D 95 5722 7983 3906 629 -778 -305 C ATOM 2807 CZ2 TRP D 95 37.288 25.555 -18.503 1.00 43.95 C ANISOU 2807 CZ2 TRP D 95 6009 7094 3596 403 -680 -53 C ATOM 2808 CZ3 TRP D 95 39.678 26.017 -18.503 1.00 46.94 C ANISOU 2808 CZ3 TRP D 95 5836 8023 3976 465 -856 -312 C ATOM 2809 CH2 TRP D 95 38.367 26.253 -18.014 1.00 45.84 C ANISOU 2809 CH2 TRP D 95 6011 7579 3829 380 -807 -186 C ATOM 2810 N ASP D 96 37.997 23.728 -24.614 1.00 44.61 N ANISOU 2810 N ASP D 96 5879 7267 3804 343 -192 -64 N ATOM 2811 CA ASP D 96 36.926 23.336 -25.508 1.00 43.36 C ANISOU 2811 CA ASP D 96 5973 6845 3657 282 -125 31 C ATOM 2812 C ASP D 96 37.383 23.544 -26.943 1.00 44.72 C ANISOU 2812 C ASP D 96 6053 7160 3781 155 4 -17 C ATOM 2813 O ASP D 96 38.232 24.387 -27.207 1.00 46.21 O ANISOU 2813 O ASP D 96 6015 7603 3940 -42 74 -78 O ATOM 2814 CB ASP D 96 35.665 24.167 -25.266 1.00 40.95 C ANISOU 2814 CB ASP D 96 5813 6316 3429 63 -149 133 C ATOM 2815 CG ASP D 96 34.791 23.630 -24.129 1.00 40.77 C ANISOU 2815 CG ASP D 96 5953 6131 3409 152 -204 181 C ATOM 2816 OD1 ASP D 96 35.072 22.518 -23.609 1.00 41.93 O ANISOU 2816 OD1 ASP D 96 6216 6241 3475 357 -236 185 O ATOM 2817 OD2 ASP D 96 33.820 24.341 -23.747 1.00 36.52 O ANISOU 2817 OD2 ASP D 96 5448 5503 2924 19 -220 200 O ATOM 2818 N LEU D 97 36.823 22.775 -27.869 1.00 44.75 N ANISOU 2818 N LEU D 97 6251 7008 3745 223 46 3 N ATOM 2819 CA LEU D 97 37.018 23.080 -29.279 1.00 46.61 C ANISOU 2819 CA LEU D 97 6480 7337 3893 58 172 -18 C ATOM 2820 C LEU D 97 35.793 23.856 -29.740 1.00 45.32 C ANISOU 2820 C LEU D 97 6549 6906 3763 -180 124 115 C ATOM 2821 O LEU D 97 34.705 23.278 -29.857 1.00 44.39 O ANISOU 2821 O LEU D 97 6626 6556 3686 -110 53 153 O ATOM 2822 CB LEU D 97 37.232 21.802 -30.104 1.00 47.25 C ANISOU 2822 CB LEU D 97 6644 7433 3875 313 221 -121 C ATOM 2823 CG LEU D 97 37.358 21.871 -31.637 1.00 49.28 C ANISOU 2823 CG LEU D 97 6954 7787 3985 187 363 -163 C ATOM 2824 CD1 LEU D 97 38.540 22.739 -32.111 1.00 50.88 C ANISOU 2824 CD1 LEU D 97 6857 8405 4068 -44 547 -247 C ATOM 2825 CD2 LEU D 97 37.459 20.462 -32.223 1.00 49.15 C ANISOU 2825 CD2 LEU D 97 7071 7724 3878 517 365 -296 C ATOM 2826 N SER D 98 35.961 25.165 -29.957 1.00 45.99 N ANISOU 2826 N SER D 98 6628 7022 3822 -460 137 167 N ATOM 2827 CA SER D 98 34.904 25.974 -30.591 1.00 45.68 C ANISOU 2827 CA SER D 98 6866 6722 3770 -616 40 268 C ATOM 2828 C SER D 98 34.770 25.621 -32.092 1.00 46.62 C ANISOU 2828 C SER D 98 7166 6820 3727 -660 104 278 C ATOM 2829 O SER D 98 35.759 25.313 -32.754 1.00 48.11 O ANISOU 2829 O SER D 98 7259 7249 3773 -713 280 218 O ATOM 2830 CB SER D 98 35.173 27.483 -30.408 1.00 46.49 C ANISOU 2830 CB SER D 98 7046 6775 3844 -892 -5 326 C ATOM 2831 OG SER D 98 34.828 27.913 -29.088 1.00 45.20 O ANISOU 2831 OG SER D 98 6817 6532 3826 -816 -129 310 O ATOM 2832 N PHE D 99 33.548 25.685 -32.621 1.00 46.32 N ANISOU 2832 N PHE D 99 7365 6540 3694 -625 -46 323 N ATOM 2833 CA PHE D 99 33.278 25.368 -34.039 1.00 47.66 C ANISOU 2833 CA PHE D 99 7757 6662 3689 -650 -37 327 C ATOM 2834 C PHE D 99 31.986 25.984 -34.552 1.00 48.12 C ANISOU 2834 C PHE D 99 8085 6466 3734 -643 -282 375 C ATOM 2835 O PHE D 99 31.126 26.394 -33.759 1.00 47.17 O ANISOU 2835 O PHE D 99 7916 6230 3778 -553 -453 358 O ATOM 2836 CB PHE D 99 33.221 23.850 -34.265 1.00 46.96 C ANISOU 2836 CB PHE D 99 7612 6623 3609 -444 23 222 C ATOM 2837 CG PHE D 99 32.219 23.144 -33.407 1.00 44.61 C ANISOU 2837 CG PHE D 99 7273 6177 3499 -304 -101 189 C ATOM 2838 CD1 PHE D 99 30.870 23.123 -33.755 1.00 43.46 C ANISOU 2838 CD1 PHE D 99 7247 5871 3394 -314 -274 172 C ATOM 2839 CD2 PHE D 99 32.627 22.467 -32.267 1.00 43.85 C ANISOU 2839 CD2 PHE D 99 7026 6129 3506 -181 -46 159 C ATOM 2840 CE1 PHE D 99 29.935 22.453 -32.976 1.00 41.26 C ANISOU 2840 CE1 PHE D 99 6892 5524 3259 -281 -339 115 C ATOM 2841 CE2 PHE D 99 31.699 21.783 -31.477 1.00 43.18 C ANISOU 2841 CE2 PHE D 99 6968 5903 3534 -140 -121 145 C ATOM 2842 CZ PHE D 99 30.342 21.788 -31.830 1.00 41.99 C ANISOU 2842 CZ PHE D 99 6891 5635 3426 -229 -241 119 C ATOM 2843 N GLN D 100 31.867 26.016 -35.881 1.00 50.00 N ANISOU 2843 N GLN D 100 8593 6653 3753 -706 -307 403 N ATOM 2844 CA GLN D 100 30.699 26.536 -36.605 1.00 51.50 C ANISOU 2844 CA GLN D 100 9081 6619 3870 -644 -591 424 C ATOM 2845 C GLN D 100 29.927 25.414 -37.268 1.00 51.00 C ANISOU 2845 C GLN D 100 9019 6561 3797 -503 -668 311 C ATOM 2846 O GLN D 100 30.475 24.349 -37.570 1.00 51.13 O ANISOU 2846 O GLN D 100 8963 6701 3762 -496 -480 251 O ATOM 2847 CB GLN D 100 31.122 27.564 -37.675 1.00 54.77 C ANISOU 2847 CB GLN D 100 9928 6918 3965 -856 -614 562 C ATOM 2848 CG GLN D 100 31.905 28.750 -37.089 1.00 58.89 C ANISOU 2848 CG GLN D 100 10527 7390 4460 -1097 -546 675 C ATOM 2849 CD GLN D 100 32.269 29.790 -38.113 1.00 66.00 C ANISOU 2849 CD GLN D 100 11964 8114 5001 -1393 -570 837 C ATOM 2850 OE1 GLN D 100 32.768 29.478 -39.192 1.00 70.95 O ANISOU 2850 OE1 GLN D 100 12757 8859 5342 -1568 -394 873 O ATOM 2851 NE2 GLN D 100 32.034 31.048 -37.776 1.00 69.72 N ANISOU 2851 NE2 GLN D 100 12764 8280 5448 -1462 -788 933 N ATOM 2852 N LYS D 101 28.649 25.658 -37.499 1.00 51.03 N ANISOU 2852 N LYS D 101 9105 6440 3844 -373 -969 250 N ATOM 2853 CA LYS D 101 27.805 24.703 -38.186 1.00 50.83 C ANISOU 2853 CA LYS D 101 9087 6428 3799 -290 -1091 116 C ATOM 2854 C LYS D 101 28.424 24.357 -39.550 1.00 52.37 C ANISOU 2854 C LYS D 101 9590 6628 3682 -366 -998 153 C ATOM 2855 O LYS D 101 28.922 25.242 -40.257 1.00 54.07 O ANISOU 2855 O LYS D 101 10122 6782 3641 -467 -996 284 O ATOM 2856 CB LYS D 101 26.389 25.280 -38.321 1.00 52.49 C ANISOU 2856 CB LYS D 101 9308 6568 4066 -126 -1474 10 C ATOM 2857 CG LYS D 101 26.318 26.618 -39.060 1.00 55.98 C ANISOU 2857 CG LYS D 101 10167 6821 4283 -53 -1729 117 C ATOM 2858 CD LYS D 101 24.932 27.270 -39.006 1.00 62.13 C ANISOU 2858 CD LYS D 101 10912 7552 5143 235 -2167 -42 C ATOM 2859 CE LYS D 101 23.851 26.360 -39.576 1.00 66.93 C ANISOU 2859 CE LYS D 101 11335 8312 5782 330 -2360 -267 C ATOM 2860 NZ LYS D 101 22.837 27.107 -40.405 1.00 74.09 N ANISOU 2860 NZ LYS D 101 12473 9139 6540 628 -2863 -381 N ATOM 2861 N GLY D 102 28.397 23.070 -39.906 1.00 51.63 N ANISOU 2861 N GLY D 102 9447 6593 3577 -341 -913 31 N ATOM 2862 CA GLY D 102 28.984 22.586 -41.147 1.00 52.51 C ANISOU 2862 CA GLY D 102 9821 6746 3383 -375 -801 11 C ATOM 2863 C GLY D 102 30.423 22.100 -41.007 1.00 52.27 C ANISOU 2863 C GLY D 102 9685 6895 3282 -409 -430 10 C ATOM 2864 O GLY D 102 30.921 21.402 -41.889 1.00 53.38 O ANISOU 2864 O GLY D 102 9960 7123 3199 -380 -299 -84 O ATOM 2865 N ASP D 103 31.086 22.464 -39.903 1.00 50.40 N ANISOU 2865 N ASP D 103 9186 6742 3220 -440 -281 75 N ATOM 2866 CA ASP D 103 32.454 22.013 -39.612 1.00 50.78 C ANISOU 2866 CA ASP D 103 9033 7027 3234 -417 27 22 C ATOM 2867 C ASP D 103 32.501 20.506 -39.365 1.00 50.93 C ANISOU 2867 C ASP D 103 8978 7027 3347 -184 57 -147 C ATOM 2868 O ASP D 103 31.630 19.938 -38.683 1.00 49.03 O ANISOU 2868 O ASP D 103 8717 6593 3317 -121 -101 -169 O ATOM 2869 CB ASP D 103 33.030 22.728 -38.380 1.00 49.29 C ANISOU 2869 CB ASP D 103 8572 6925 3231 -485 107 105 C ATOM 2870 CG ASP D 103 33.521 24.156 -38.681 1.00 50.95 C ANISOU 2870 CG ASP D 103 8897 7188 3274 -772 169 250 C ATOM 2871 OD1 ASP D 103 33.828 24.493 -39.845 1.00 49.42 O ANISOU 2871 OD1 ASP D 103 8959 7052 2765 -943 258 286 O ATOM 2872 OD2 ASP D 103 33.626 24.946 -37.721 1.00 52.91 O ANISOU 2872 OD2 ASP D 103 9020 7404 3679 -855 134 328 O ATOM 2873 N GLN D 104 33.526 19.873 -39.920 1.00 53.13 N ANISOU 2873 N GLN D 104 9239 7508 3439 -67 264 -282 N ATOM 2874 CA GLN D 104 33.765 18.456 -39.689 1.00 54.62 C ANISOU 2874 CA GLN D 104 9435 7642 3678 222 273 -463 C ATOM 2875 C GLN D 104 34.864 18.235 -38.657 1.00 54.90 C ANISOU 2875 C GLN D 104 9165 7868 3824 414 404 -523 C ATOM 2876 O GLN D 104 35.860 18.976 -38.625 1.00 56.04 O ANISOU 2876 O GLN D 104 9045 8354 3894 334 594 -525 O ATOM 2877 CB GLN D 104 34.142 17.756 -40.988 1.00 57.39 C ANISOU 2877 CB GLN D 104 9986 8087 3733 347 366 -651 C ATOM 2878 CG GLN D 104 32.986 17.593 -41.930 1.00 57.94 C ANISOU 2878 CG GLN D 104 10400 7918 3696 239 166 -648 C ATOM 2879 CD GLN D 104 33.408 16.934 -43.201 1.00 62.19 C ANISOU 2879 CD GLN D 104 11161 8561 3906 367 264 -847 C ATOM 2880 OE1 GLN D 104 33.981 17.579 -44.091 1.00 63.79 O ANISOU 2880 OE1 GLN D 104 11394 9031 3812 247 447 -840 O ATOM 2881 NE2 GLN D 104 33.142 15.636 -43.304 1.00 62.58 N ANISOU 2881 NE2 GLN D 104 11415 8391 3970 586 152 -1035 N ATOM 2882 N MET D 105 34.682 17.206 -37.833 1.00 54.63 N ANISOU 2882 N MET D 105 9199 7616 3940 644 286 -580 N ATOM 2883 CA MET D 105 35.638 16.869 -36.780 1.00 55.81 C ANISOU 2883 CA MET D 105 9132 7894 4181 908 325 -646 C ATOM 2884 C MET D 105 35.797 15.357 -36.631 1.00 58.39 C ANISOU 2884 C MET D 105 9727 7987 4470 1298 214 -818 C ATOM 2885 O MET D 105 34.849 14.605 -36.875 1.00 58.84 O ANISOU 2885 O MET D 105 10161 7667 4528 1245 74 -810 O ATOM 2886 CB MET D 105 35.191 17.481 -35.434 1.00 52.70 C ANISOU 2886 CB MET D 105 8613 7392 4019 753 234 -455 C ATOM 2887 CG MET D 105 35.325 19.007 -35.331 1.00 50.80 C ANISOU 2887 CG MET D 105 8115 7370 3815 452 319 -319 C ATOM 2888 SD MET D 105 34.350 19.742 -33.982 1.00 48.36 S ANISOU 2888 SD MET D 105 7764 6857 3753 263 172 -124 S ATOM 2889 CE MET D 105 32.691 19.619 -34.662 1.00 45.28 C ANISOU 2889 CE MET D 105 7649 6172 3383 91 15 -77 C ATOM 2890 N VAL D 106 36.992 14.918 -36.222 1.00 61.17 N ANISOU 2890 N VAL D 106 9903 8559 4780 1693 250 -994 N ATOM 2891 CA VAL D 106 37.199 13.533 -35.803 1.00 63.57 C ANISOU 2891 CA VAL D 106 10534 8565 5052 2142 71 -1140 C ATOM 2892 C VAL D 106 37.007 13.465 -34.314 1.00 62.42 C ANISOU 2892 C VAL D 106 10450 8198 5069 2156 -80 -972 C ATOM 2893 O VAL D 106 37.622 14.235 -33.575 1.00 61.78 O ANISOU 2893 O VAL D 106 9977 8425 5071 2154 -29 -929 O ATOM 2894 CB VAL D 106 38.629 13.015 -35.995 1.00 67.88 C ANISOU 2894 CB VAL D 106 10865 9472 5454 2701 115 -1469 C ATOM 2895 CG1 VAL D 106 38.594 11.586 -36.515 1.00 70.81 C ANISOU 2895 CG1 VAL D 106 11742 9489 5672 3128 -44 -1691 C ATOM 2896 CG2 VAL D 106 39.466 13.930 -36.865 1.00 69.47 C ANISOU 2896 CG2 VAL D 106 10550 10315 5532 2574 411 -1605 C ATOM 2897 N VAL D 107 36.192 12.510 -33.875 1.00 62.85 N ANISOU 2897 N VAL D 107 11026 7721 5134 2146 -263 -892 N ATOM 2898 CA VAL D 107 35.996 12.246 -32.465 1.00 62.31 C ANISOU 2898 CA VAL D 107 11146 7390 5139 2159 -405 -735 C ATOM 2899 C VAL D 107 37.148 11.393 -31.938 1.00 66.71 C ANISOU 2899 C VAL D 107 11847 7918 5582 2795 -574 -915 C ATOM 2900 O VAL D 107 37.432 10.331 -32.478 1.00 69.72 O ANISOU 2900 O VAL D 107 12604 8071 5815 3174 -695 -1111 O ATOM 2901 CB VAL D 107 34.669 11.522 -32.224 1.00 62.19 C ANISOU 2901 CB VAL D 107 11675 6830 5126 1815 -507 -586 C ATOM 2902 CG1 VAL D 107 34.503 11.183 -30.734 1.00 61.92 C ANISOU 2902 CG1 VAL D 107 11914 6519 5094 1793 -624 -415 C ATOM 2903 CG2 VAL D 107 33.522 12.373 -32.719 1.00 57.33 C ANISOU 2903 CG2 VAL D 107 10842 6312 4626 1267 -388 -470 C ATOM 2904 N LEU D 108 37.794 11.866 -30.873 1.00 67.02 N ANISOU 2904 N LEU D 108 11604 8182 5677 2943 -619 -871 N ATOM 2905 CA LEU D 108 38.969 11.186 -30.314 1.00 71.88 C ANISOU 2905 CA LEU D 108 12269 8861 6182 3617 -830 -1077 C ATOM 2906 C LEU D 108 38.627 10.335 -29.086 1.00 74.18 C ANISOU 2906 C LEU D 108 13212 8585 6389 3750 -1105 -909 C ATOM 2907 O LEU D 108 39.187 9.256 -28.901 1.00 78.88 O ANISOU 2907 O LEU D 108 14255 8898 6817 4329 -1373 -1063 O ATOM 2908 CB LEU D 108 40.071 12.198 -29.973 1.00 71.45 C ANISOU 2908 CB LEU D 108 11466 9481 6201 3745 -742 -1199 C ATOM 2909 CG LEU D 108 40.606 13.132 -31.068 1.00 70.41 C ANISOU 2909 CG LEU D 108 10688 9970 6097 3557 -445 -1362 C ATOM 2910 CD1 LEU D 108 41.553 14.163 -30.471 1.00 70.25 C ANISOU 2910 CD1 LEU D 108 9999 10542 6151 3526 -374 -1435 C ATOM 2911 CD2 LEU D 108 41.304 12.355 -32.178 1.00 73.84 C ANISOU 2911 CD2 LEU D 108 11107 10584 6363 4018 -418 -1717 C ATOM 2912 N GLU D 109 37.699 10.824 -28.263 1.00 71.68 N ANISOU 2912 N GLU D 109 12983 8098 6155 3222 -1042 -607 N ATOM 2913 CA GLU D 109 37.305 10.158 -27.026 1.00 73.88 C ANISOU 2913 CA GLU D 109 13878 7884 6308 3211 -1240 -408 C ATOM 2914 C GLU D 109 35.799 10.338 -26.798 1.00 71.26 C ANISOU 2914 C GLU D 109 13772 7274 6029 2460 -1075 -137 C ATOM 2915 O GLU D 109 35.251 11.407 -27.085 1.00 67.16 O ANISOU 2915 O GLU D 109 12740 7087 5691 2030 -849 -78 O ATOM 2916 CB GLU D 109 38.114 10.752 -25.863 1.00 74.25 C ANISOU 2916 CB GLU D 109 13607 8246 6361 3460 -1343 -392 C ATOM 2917 CG GLU D 109 37.991 10.029 -24.536 1.00 78.56 C ANISOU 2917 CG GLU D 109 14829 8321 6698 3587 -1596 -214 C ATOM 2918 CD GLU D 109 38.753 10.725 -23.419 1.00 81.22 C ANISOU 2918 CD GLU D 109 14805 9019 7035 3808 -1706 -213 C ATOM 2919 OE1 GLU D 109 38.600 11.963 -23.251 1.00 78.03 O ANISOU 2919 OE1 GLU D 109 13786 9048 6814 3428 -1488 -159 O ATOM 2920 OE2 GLU D 109 39.497 10.023 -22.698 1.00 86.19 O ANISOU 2920 OE2 GLU D 109 15815 9472 7462 4383 -2046 -277 O ATOM 2921 N GLU D 110 35.137 9.293 -26.301 1.00 74.39 N ANISOU 2921 N GLU D 110 14946 7073 6246 2303 -1197 3 N ATOM 2922 CA GLU D 110 33.706 9.345 -25.976 1.00 73.65 C ANISOU 2922 CA GLU D 110 15052 6767 6163 1556 -1029 218 C ATOM 2923 C GLU D 110 33.388 8.961 -24.523 1.00 76.26 C ANISOU 2923 C GLU D 110 15908 6776 6290 1365 -1096 447 C ATOM 2924 O GLU D 110 32.561 8.086 -24.260 1.00 79.53 O ANISOU 2924 O GLU D 110 16998 6697 6522 962 -1102 578 O ATOM 2925 CB GLU D 110 32.882 8.508 -26.964 1.00 75.33 C ANISOU 2925 CB GLU D 110 15680 6608 6333 1255 -1014 165 C ATOM 2926 CG GLU D 110 32.668 9.221 -28.290 1.00 73.08 C ANISOU 2926 CG GLU D 110 14797 6718 6253 1146 -857 12 C ATOM 2927 CD GLU D 110 31.821 8.461 -29.308 1.00 75.94 C ANISOU 2927 CD GLU D 110 15521 6761 6570 837 -864 -70 C ATOM 2928 OE1 GLU D 110 31.783 8.918 -30.470 1.00 76.83 O ANISOU 2928 OE1 GLU D 110 15246 7157 6789 849 -788 -214 O ATOM 2929 OE2 GLU D 110 31.191 7.438 -28.978 1.00 78.37 O ANISOU 2929 OE2 GLU D 110 16517 6543 6717 546 -948 7 O ATOM 2930 N SER D 111 34.042 9.633 -23.580 1.00 75.68 N ANISOU 2930 N SER D 111 15542 6993 6220 1606 -1139 492 N ATOM 2931 CA SER D 111 33.768 9.420 -22.159 1.00 77.90 C ANISOU 2931 CA SER D 111 16283 7041 6276 1422 -1185 712 C ATOM 2932 C SER D 111 32.599 10.316 -21.705 1.00 74.35 C ANISOU 2932 C SER D 111 15447 6871 5931 712 -864 837 C ATOM 2933 O SER D 111 32.799 11.445 -21.230 1.00 71.74 O ANISOU 2933 O SER D 111 14529 6995 5734 732 -775 825 O ATOM 2934 CB SER D 111 35.026 9.686 -21.329 1.00 78.94 C ANISOU 2934 CB SER D 111 16300 7364 6330 2050 -1424 667 C ATOM 2935 OG SER D 111 34.856 9.250 -19.988 1.00 84.26 O ANISOU 2935 OG SER D 111 17612 7706 6696 1959 -1538 883 O ATOM 2936 N GLY D 112 31.377 9.809 -21.864 1.00 74.85 N ANISOU 2936 N GLY D 112 15830 6683 5926 89 -700 919 N ATOM 2937 CA GLY D 112 30.178 10.589 -21.564 1.00 71.32 C ANISOU 2937 CA GLY D 112 14951 6566 5580 -558 -395 957 C ATOM 2938 C GLY D 112 29.750 11.404 -22.768 1.00 66.41 C ANISOU 2938 C GLY D 112 13614 6333 5288 -658 -271 782 C ATOM 2939 O GLY D 112 30.165 11.117 -23.887 1.00 65.97 O ANISOU 2939 O GLY D 112 13545 6198 5324 -388 -377 664 O ATOM 2940 N GLU D 113 28.918 12.418 -22.539 1.00 62.68 N ANISOU 2940 N GLU D 113 12581 6275 4960 -1012 -64 750 N ATOM 2941 CA GLU D 113 28.357 13.221 -23.626 1.00 58.72 C ANISOU 2941 CA GLU D 113 11473 6107 4728 -1119 14 590 C ATOM 2942 C GLU D 113 29.206 14.411 -24.055 1.00 54.00 C ANISOU 2942 C GLU D 113 10327 5851 4340 -690 -45 513 C ATOM 2943 O GLU D 113 28.875 15.094 -25.024 1.00 51.96 O ANISOU 2943 O GLU D 113 9668 5811 4263 -721 -23 403 O ATOM 2944 CB GLU D 113 26.953 13.675 -23.279 1.00 58.90 C ANISOU 2944 CB GLU D 113 11181 6407 4793 -1675 224 537 C ATOM 2945 CG GLU D 113 25.892 12.700 -23.686 1.00 64.58 C ANISOU 2945 CG GLU D 113 12183 6934 5422 -2208 299 494 C ATOM 2946 CD GLU D 113 24.613 12.889 -22.914 1.00 69.35 C ANISOU 2946 CD GLU D 113 12564 7827 5960 -2808 543 442 C ATOM 2947 OE1 GLU D 113 24.102 14.030 -22.858 1.00 69.45 O ANISOU 2947 OE1 GLU D 113 11917 8322 6149 -2793 623 298 O ATOM 2948 OE2 GLU D 113 24.113 11.891 -22.362 1.00 75.11 O ANISOU 2948 OE2 GLU D 113 13800 8302 6435 -3302 656 528 O ATOM 2949 N TRP D 114 30.288 14.664 -23.335 1.00 52.85 N ANISOU 2949 N TRP D 114 10192 5748 4141 -320 -133 567 N ATOM 2950 CA TRP D 114 31.282 15.655 -23.747 1.00 49.79 C ANISOU 2950 CA TRP D 114 9345 5661 3910 43 -191 485 C ATOM 2951 C TRP D 114 32.480 14.911 -24.318 1.00 51.25 C ANISOU 2951 C TRP D 114 9732 5713 4029 500 -347 424 C ATOM 2952 O TRP D 114 33.244 14.268 -23.588 1.00 53.67 O ANISOU 2952 O TRP D 114 10358 5859 4175 810 -493 456 O ATOM 2953 CB TRP D 114 31.689 16.572 -22.578 1.00 48.22 C ANISOU 2953 CB TRP D 114 8911 5697 3712 122 -191 522 C ATOM 2954 CG TRP D 114 30.676 17.640 -22.305 1.00 45.58 C ANISOU 2954 CG TRP D 114 8222 5603 3494 -201 -51 495 C ATOM 2955 CD1 TRP D 114 29.523 17.506 -21.573 1.00 47.44 C ANISOU 2955 CD1 TRP D 114 8542 5837 3645 -567 83 523 C ATOM 2956 CD2 TRP D 114 30.705 19.005 -22.759 1.00 41.03 C ANISOU 2956 CD2 TRP D 114 7173 5306 3111 -176 -41 407 C ATOM 2957 NE1 TRP D 114 28.840 18.695 -21.552 1.00 45.49 N ANISOU 2957 NE1 TRP D 114 7851 5888 3547 -689 159 418 N ATOM 2958 CE2 TRP D 114 29.543 19.630 -22.269 1.00 40.72 C ANISOU 2958 CE2 TRP D 114 6956 5406 3110 -442 60 362 C ATOM 2959 CE3 TRP D 114 31.605 19.759 -23.529 1.00 38.62 C ANISOU 2959 CE3 TRP D 114 6609 5145 2919 24 -103 352 C ATOM 2960 CZ2 TRP D 114 29.258 20.972 -22.513 1.00 40.44 C ANISOU 2960 CZ2 TRP D 114 6556 5580 3228 -430 43 265 C ATOM 2961 CZ3 TRP D 114 31.326 21.090 -23.776 1.00 36.33 C ANISOU 2961 CZ3 TRP D 114 6010 5033 2761 -61 -94 298 C ATOM 2962 CH2 TRP D 114 30.155 21.688 -23.283 1.00 37.75 C ANISOU 2962 CH2 TRP D 114 6079 5279 2985 -247 -50 254 C ATOM 2963 N TRP D 115 32.631 14.991 -25.630 1.00 50.48 N ANISOU 2963 N TRP D 115 9459 5696 4027 572 -330 310 N ATOM 2964 CA TRP D 115 33.657 14.237 -26.321 1.00 52.85 C ANISOU 2964 CA TRP D 115 9916 5917 4248 1006 -445 190 C ATOM 2965 C TRP D 115 34.887 15.085 -26.596 1.00 52.87 C ANISOU 2965 C TRP D 115 9414 6351 4325 1312 -438 66 C ATOM 2966 O TRP D 115 34.800 16.311 -26.662 1.00 50.19 O ANISOU 2966 O TRP D 115 8645 6310 4115 1102 -329 84 O ATOM 2967 CB TRP D 115 33.123 13.721 -27.652 1.00 52.94 C ANISOU 2967 CB TRP D 115 10069 5781 4264 889 -413 106 C ATOM 2968 CG TRP D 115 31.924 12.829 -27.576 1.00 53.49 C ANISOU 2968 CG TRP D 115 10611 5455 4258 515 -417 179 C ATOM 2969 CD1 TRP D 115 31.430 12.195 -26.471 1.00 54.66 C ANISOU 2969 CD1 TRP D 115 11188 5306 4275 307 -441 316 C ATOM 2970 CD2 TRP D 115 31.082 12.444 -28.674 1.00 53.43 C ANISOU 2970 CD2 TRP D 115 10715 5320 4267 253 -393 104 C ATOM 2971 NE1 TRP D 115 30.320 11.451 -26.809 1.00 57.53 N ANISOU 2971 NE1 TRP D 115 11897 5382 4581 -131 -406 326 N ATOM 2972 CE2 TRP D 115 30.084 11.583 -28.155 1.00 55.97 C ANISOU 2972 CE2 TRP D 115 11492 5286 4486 -153 -395 184 C ATOM 2973 CE3 TRP D 115 31.070 12.754 -30.048 1.00 52.59 C ANISOU 2973 CE3 TRP D 115 10384 5377 4221 291 -371 -29 C ATOM 2974 CZ2 TRP D 115 29.080 11.015 -28.960 1.00 56.90 C ANISOU 2974 CZ2 TRP D 115 11798 5229 4592 -529 -392 109 C ATOM 2975 CZ3 TRP D 115 30.066 12.188 -30.858 1.00 55.10 C ANISOU 2975 CZ3 TRP D 115 10919 5501 4516 -21 -394 -95 C ATOM 2976 CH2 TRP D 115 29.087 11.323 -30.302 1.00 57.36 C ANISOU 2976 CH2 TRP D 115 11610 5453 4731 -430 -412 -38 C ATOM 2977 N LYS D 116 36.033 14.433 -26.767 1.00 56.80 N ANISOU 2977 N LYS D 116 9972 6888 4723 1803 -561 -85 N ATOM 2978 CA LYS D 116 37.212 15.123 -27.294 1.00 58.42 C ANISOU 2978 CA LYS D 116 9638 7583 4975 2035 -508 -269 C ATOM 2979 C LYS D 116 37.210 15.015 -28.823 1.00 58.67 C ANISOU 2979 C LYS D 116 9595 7703 4995 2010 -383 -399 C ATOM 2980 O LYS D 116 36.892 13.965 -29.358 1.00 60.96 O ANISOU 2980 O LYS D 116 10300 7672 5191 2138 -450 -449 O ATOM 2981 CB LYS D 116 38.500 14.536 -26.709 1.00 62.00 C ANISOU 2981 CB LYS D 116 10074 8165 5318 2623 -710 -441 C ATOM 2982 CG LYS D 116 39.652 15.535 -26.663 1.00 64.09 C ANISOU 2982 CG LYS D 116 9659 9042 5649 2716 -650 -609 C ATOM 2983 CD LYS D 116 40.921 14.929 -26.042 1.00 71.38 C ANISOU 2983 CD LYS D 116 10491 10167 6463 3356 -899 -840 C ATOM 2984 CE LYS D 116 41.967 16.016 -25.769 1.00 73.56 C ANISOU 2984 CE LYS D 116 10043 11091 6814 3326 -845 -1005 C ATOM 2985 NZ LYS D 116 43.371 15.505 -25.835 1.00 78.21 N ANISOU 2985 NZ LYS D 116 10281 12125 7310 3956 -1006 -1384 N ATOM 2986 N ALA D 117 37.542 16.096 -29.520 1.00 57.80 N ANISOU 2986 N ALA D 117 9021 7993 4946 1814 -209 -449 N ATOM 2987 CA ALA D 117 37.537 16.083 -30.991 1.00 58.93 C ANISOU 2987 CA ALA D 117 9124 8244 5023 1749 -72 -557 C ATOM 2988 C ALA D 117 38.642 16.933 -31.601 1.00 60.59 C ANISOU 2988 C ALA D 117 8823 9009 5189 1735 106 -711 C ATOM 2989 O ALA D 117 39.181 17.822 -30.954 1.00 60.24 O ANISOU 2989 O ALA D 117 8427 9250 5212 1620 140 -692 O ATOM 2990 CB ALA D 117 36.176 16.505 -31.536 1.00 55.79 C ANISOU 2990 CB ALA D 117 8898 7614 4686 1300 -21 -388 C ATOM 2991 N ARG D 118 38.975 16.649 -32.854 1.00 63.35 N ANISOU 2991 N ARG D 118 9150 9522 5397 1812 232 -878 N ATOM 2992 CA ARG D 118 39.957 17.428 -33.580 1.00 65.94 C ANISOU 2992 CA ARG D 118 9024 10408 5623 1691 465 -1029 C ATOM 2993 C ARG D 118 39.308 18.016 -34.826 1.00 65.48 C ANISOU 2993 C ARG D 118 9112 10305 5464 1279 625 -923 C ATOM 2994 O ARG D 118 38.640 17.300 -35.577 1.00 65.75 O ANISOU 2994 O ARG D 118 9505 10058 5420 1352 578 -935 O ATOM 2995 CB ARG D 118 41.156 16.551 -33.950 1.00 70.72 C ANISOU 2995 CB ARG D 118 9414 11378 6078 2214 496 -1396 C ATOM 2996 CG ARG D 118 42.170 17.230 -34.863 1.00 74.26 C ANISOU 2996 CG ARG D 118 9362 12491 6361 2038 806 -1609 C ATOM 2997 CD ARG D 118 43.517 16.514 -34.880 1.00 81.41 C ANISOU 2997 CD ARG D 118 9851 13926 7154 2606 822 -2046 C ATOM 2998 NE ARG D 118 43.453 15.163 -35.442 1.00 84.96 N ANISOU 2998 NE ARG D 118 10650 14152 7480 3165 705 -2261 N ATOM 2999 CZ ARG D 118 43.857 14.061 -34.810 1.00 87.29 C ANISOU 2999 CZ ARG D 118 11074 14309 7785 3859 419 -2471 C ATOM 3000 NH1 ARG D 118 44.369 14.137 -33.586 1.00 87.47 N ANISOU 3000 NH1 ARG D 118 10873 14435 7927 4095 218 -2492 N ATOM 3001 NH2 ARG D 118 43.755 12.881 -35.407 1.00 89.35 N ANISOU 3001 NH2 ARG D 118 11743 14299 7908 4336 303 -2668 N ATOM 3002 N SER D 119 39.495 19.318 -35.035 1.00 65.58 N ANISOU 3002 N SER D 119 8903 10559 5453 842 782 -818 N ATOM 3003 CA SER D 119 38.997 19.981 -36.236 1.00 66.19 C ANISOU 3003 CA SER D 119 9177 10599 5373 462 909 -709 C ATOM 3004 C SER D 119 39.757 19.459 -37.442 1.00 70.64 C ANISOU 3004 C SER D 119 9667 11512 5662 587 1124 -956 C ATOM 3005 O SER D 119 40.990 19.448 -37.443 1.00 74.75 O ANISOU 3005 O SER D 119 9761 12555 6086 687 1308 -1192 O ATOM 3006 CB SER D 119 39.164 21.498 -36.127 1.00 65.64 C ANISOU 3006 CB SER D 119 8978 10669 5294 -31 1010 -545 C ATOM 3007 OG SER D 119 39.160 22.113 -37.407 1.00 67.80 O ANISOU 3007 OG SER D 119 9424 11035 5304 -377 1184 -495 O ATOM 3008 N LEU D 120 39.024 19.026 -38.463 1.00 71.08 N ANISOU 3008 N LEU D 120 10105 11326 5578 587 1097 -938 N ATOM 3009 CA LEU D 120 39.638 18.502 -39.678 1.00 75.44 C ANISOU 3009 CA LEU D 120 10651 12186 5827 714 1302 -1187 C ATOM 3010 C LEU D 120 40.368 19.574 -40.474 1.00 78.48 C ANISOU 3010 C LEU D 120 10839 13043 5939 262 1632 -1187 C ATOM 3011 O LEU D 120 41.236 19.261 -41.277 1.00 82.76 O ANISOU 3011 O LEU D 120 11188 14047 6208 339 1893 -1455 O ATOM 3012 CB LEU D 120 38.601 17.810 -40.569 1.00 75.04 C ANISOU 3012 CB LEU D 120 11107 11731 5676 789 1162 -1165 C ATOM 3013 CG LEU D 120 38.169 16.385 -40.202 1.00 74.93 C ANISOU 3013 CG LEU D 120 11346 11338 5787 1249 920 -1293 C ATOM 3014 CD1 LEU D 120 37.416 15.766 -41.367 1.00 76.16 C ANISOU 3014 CD1 LEU D 120 11944 11239 5753 1259 849 -1356 C ATOM 3015 CD2 LEU D 120 39.356 15.512 -39.837 1.00 77.55 C ANISOU 3015 CD2 LEU D 120 11419 11957 6089 1773 969 -1616 C ATOM 3016 N ALA D 121 40.020 20.836 -40.244 1.00 76.96 N ANISOU 3016 N ALA D 121 10722 12729 5789 -221 1623 -903 N ATOM 3017 CA ALA D 121 40.622 21.937 -40.996 1.00 80.18 C ANISOU 3017 CA ALA D 121 11093 13478 5895 -764 1919 -846 C ATOM 3018 C ALA D 121 41.872 22.523 -40.335 1.00 82.64 C ANISOU 3018 C ALA D 121 10842 14324 6233 -980 2143 -972 C ATOM 3019 O ALA D 121 42.796 22.945 -41.026 1.00 87.34 O ANISOU 3019 O ALA D 121 11219 15443 6523 -1334 2496 -1105 O ATOM 3020 CB ALA D 121 39.586 23.029 -41.255 1.00 78.27 C ANISOU 3020 CB ALA D 121 11358 12766 5614 -1175 1756 -484 C ATOM 3021 N THR D 122 41.901 22.551 -39.002 1.00 80.15 N ANISOU 3021 N THR D 122 10285 13910 6256 -805 1944 -948 N ATOM 3022 CA THR D 122 42.974 23.248 -38.270 1.00 82.04 C ANISOU 3022 CA THR D 122 10011 14615 6546 -1062 2089 -1050 C ATOM 3023 C THR D 122 43.863 22.345 -37.397 1.00 83.18 C ANISOU 3023 C THR D 122 9588 15156 6861 -518 2033 -1388 C ATOM 3024 O THR D 122 44.914 22.788 -36.929 1.00 85.96 O ANISOU 3024 O THR D 122 9404 16043 7214 -687 2169 -1572 O ATOM 3025 CB THR D 122 42.412 24.393 -37.378 1.00 78.85 C ANISOU 3025 CB THR D 122 9802 13815 6343 -1417 1895 -742 C ATOM 3026 OG1 THR D 122 41.760 23.832 -36.237 1.00 74.53 O ANISOU 3026 OG1 THR D 122 9289 12899 6129 -963 1567 -690 O ATOM 3027 CG2 THR D 122 41.421 25.268 -38.147 1.00 77.86 C ANISOU 3027 CG2 THR D 122 10311 13209 6064 -1821 1840 -417 C ATOM 3028 N ARG D 123 43.432 21.096 -37.182 1.00 81.25 N ANISOU 3028 N ARG D 123 9500 14633 6739 120 1804 -1476 N ATOM 3029 CA ARG D 123 44.097 20.140 -36.270 1.00 82.35 C ANISOU 3029 CA ARG D 123 9288 14972 7030 751 1634 -1757 C ATOM 3030 C ARG D 123 44.016 20.534 -34.764 1.00 79.62 C ANISOU 3030 C ARG D 123 8839 14451 6963 768 1383 -1617 C ATOM 3031 O ARG D 123 44.639 19.891 -33.903 1.00 80.95 O ANISOU 3031 O ARG D 123 8727 14800 7229 1261 1208 -1832 O ATOM 3032 CB ARG D 123 45.556 19.857 -36.687 1.00 88.85 C ANISOU 3032 CB ARG D 123 9461 16638 7659 937 1889 -2222 C ATOM 3033 CG ARG D 123 45.751 19.104 -38.010 1.00 92.74 C ANISOU 3033 CG ARG D 123 10019 17353 7865 1159 2098 -2475 C ATOM 3034 CD ARG D 123 47.153 18.497 -38.059 1.00100.25 C ANISOU 3034 CD ARG D 123 10270 19122 8696 1632 2231 -3032 C ATOM 3035 NE ARG D 123 47.577 18.104 -39.405 1.00105.70 N ANISOU 3035 NE ARG D 123 10867 20253 9040 1686 2558 -3334 N ATOM 3036 CZ ARG D 123 48.796 17.648 -39.714 1.00113.02 C ANISOU 3036 CZ ARG D 123 11135 22019 9790 2054 2758 -3885 C ATOM 3037 NH1 ARG D 123 49.726 17.521 -38.773 1.00116.02 N ANISOU 3037 NH1 ARG D 123 10873 22890 10321 2426 2626 -4200 N ATOM 3038 NH2 ARG D 123 49.093 17.316 -40.967 1.00116.19 N ANISOU 3038 NH2 ARG D 123 11494 22809 9843 2079 3081 -4157 N ATOM 3039 N LYS D 124 43.252 21.584 -34.458 1.00 75.62 N ANISOU 3039 N LYS D 124 8589 13589 6555 274 1340 -1279 N ATOM 3040 CA LYS D 124 43.036 22.009 -33.081 1.00 72.74 C ANISOU 3040 CA LYS D 124 8197 13019 6424 266 1112 -1139 C ATOM 3041 C LYS D 124 42.112 21.020 -32.386 1.00 68.92 C ANISOU 3041 C LYS D 124 8098 11993 6094 725 818 -1028 C ATOM 3042 O LYS D 124 41.105 20.586 -32.955 1.00 66.58 O ANISOU 3042 O LYS D 124 8238 11278 5783 747 776 -888 O ATOM 3043 CB LYS D 124 42.423 23.408 -33.029 1.00 70.85 C ANISOU 3043 CB LYS D 124 8180 12522 6216 -346 1138 -845 C ATOM 3044 CG LYS D 124 43.385 24.561 -33.331 1.00 76.17 C ANISOU 3044 CG LYS D 124 8533 13663 6747 -921 1387 -915 C ATOM 3045 CD LYS D 124 42.615 25.892 -33.335 1.00 77.09 C ANISOU 3045 CD LYS D 124 9073 13350 6869 -1465 1341 -597 C ATOM 3046 CE LYS D 124 43.452 27.059 -32.789 1.00 80.83 C ANISOU 3046 CE LYS D 124 9278 14105 7328 -1977 1418 -636 C ATOM 3047 NZ LYS D 124 44.419 27.577 -33.798 1.00 85.82 N ANISOU 3047 NZ LYS D 124 9708 15235 7666 -2528 1780 -754 N ATOM 3048 N GLU D 125 42.471 20.667 -31.157 1.00 68.27 N ANISOU 3048 N GLU D 125 7868 11938 6133 1054 614 -1098 N ATOM 3049 CA GLU D 125 41.713 19.702 -30.373 1.00 65.63 C ANISOU 3049 CA GLU D 125 7937 11108 5890 1440 350 -991 C ATOM 3050 C GLU D 125 41.034 20.351 -29.152 1.00 61.75 C ANISOU 3050 C GLU D 125 7583 10329 5552 1234 203 -754 C ATOM 3051 O GLU D 125 41.415 21.443 -28.705 1.00 61.46 O ANISOU 3051 O GLU D 125 7270 10519 5565 929 244 -737 O ATOM 3052 CB GLU D 125 42.631 18.563 -29.914 1.00 69.50 C ANISOU 3052 CB GLU D 125 8295 11789 6325 2093 179 -1270 C ATOM 3053 CG GLU D 125 43.179 17.695 -31.033 1.00 73.68 C ANISOU 3053 CG GLU D 125 8765 12537 6693 2442 276 -1551 C ATOM 3054 CD GLU D 125 44.299 16.761 -30.589 1.00 79.24 C ANISOU 3054 CD GLU D 125 9228 13550 7329 3156 83 -1912 C ATOM 3055 OE1 GLU D 125 44.605 16.682 -29.378 1.00 79.42 O ANISOU 3055 OE1 GLU D 125 9200 13558 7418 3409 -168 -1916 O ATOM 3056 OE2 GLU D 125 44.882 16.098 -31.472 1.00 84.92 O ANISOU 3056 OE2 GLU D 125 9821 14542 7904 3508 162 -2218 O ATOM 3057 N GLY D 126 40.044 19.652 -28.609 1.00 58.73 N ANISOU 3057 N GLY D 126 7638 9461 5217 1380 43 -596 N ATOM 3058 CA GLY D 126 39.340 20.096 -27.415 1.00 55.22 C ANISOU 3058 CA GLY D 126 7339 8766 4874 1231 -75 -406 C ATOM 3059 C GLY D 126 38.041 19.335 -27.232 1.00 52.92 C ANISOU 3059 C GLY D 126 7537 7976 4594 1232 -149 -239 C ATOM 3060 O GLY D 126 37.682 18.494 -28.067 1.00 53.78 O ANISOU 3060 O GLY D 126 7892 7899 4645 1323 -130 -263 O ATOM 3061 N TYR D 127 37.321 19.648 -26.155 1.00 50.18 N ANISOU 3061 N TYR D 127 7322 7441 4304 1089 -219 -92 N ATOM 3062 CA TYR D 127 36.058 18.978 -25.851 1.00 48.27 C ANISOU 3062 CA TYR D 127 7487 6802 4052 992 -250 47 C ATOM 3063 C TYR D 127 34.893 19.629 -26.548 1.00 45.24 C ANISOU 3063 C TYR D 127 7101 6330 3758 631 -151 122 C ATOM 3064 O TYR D 127 34.927 20.830 -26.820 1.00 44.05 O ANISOU 3064 O TYR D 127 6712 6347 3679 445 -100 126 O ATOM 3065 CB TYR D 127 35.822 18.902 -24.334 1.00 48.29 C ANISOU 3065 CB TYR D 127 7639 6693 4015 1010 -346 139 C ATOM 3066 CG TYR D 127 36.817 17.994 -23.659 1.00 51.54 C ANISOU 3066 CG TYR D 127 8204 7092 4288 1441 -521 74 C ATOM 3067 CD1 TYR D 127 38.016 18.505 -23.154 1.00 54.38 C ANISOU 3067 CD1 TYR D 127 8217 7800 4646 1663 -616 -52 C ATOM 3068 CD2 TYR D 127 36.582 16.622 -23.559 1.00 54.15 C ANISOU 3068 CD2 TYR D 127 9050 7054 4471 1639 -626 114 C ATOM 3069 CE1 TYR D 127 38.949 17.677 -22.540 1.00 60.26 C ANISOU 3069 CE1 TYR D 127 9078 8566 5251 2145 -840 -154 C ATOM 3070 CE2 TYR D 127 37.511 15.776 -22.942 1.00 60.21 C ANISOU 3070 CE2 TYR D 127 10042 7756 5078 2125 -857 43 C ATOM 3071 CZ TYR D 127 38.690 16.317 -22.434 1.00 62.86 C ANISOU 3071 CZ TYR D 127 9976 8485 5422 2413 -976 -101 C ATOM 3072 OH TYR D 127 39.620 15.510 -21.827 1.00 69.78 O ANISOU 3072 OH TYR D 127 11041 9340 6134 2969 -1261 -213 O ATOM 3073 N ILE D 128 33.872 18.829 -26.846 1.00 44.48 N ANISOU 3073 N ILE D 128 7301 5961 3640 536 -151 165 N ATOM 3074 CA ILE D 128 32.698 19.305 -27.598 1.00 42.66 C ANISOU 3074 CA ILE D 128 7049 5676 3483 250 -107 186 C ATOM 3075 C ILE D 128 31.377 18.733 -27.037 1.00 43.47 C ANISOU 3075 C ILE D 128 7354 5578 3587 33 -109 232 C ATOM 3076 O ILE D 128 31.336 17.610 -26.550 1.00 44.81 O ANISOU 3076 O ILE D 128 7837 5535 3654 64 -128 264 O ATOM 3077 CB ILE D 128 32.828 19.039 -29.128 1.00 42.70 C ANISOU 3077 CB ILE D 128 7102 5681 3441 279 -84 114 C ATOM 3078 CG1 ILE D 128 32.860 17.535 -29.450 1.00 44.20 C ANISOU 3078 CG1 ILE D 128 7633 5636 3526 435 -122 59 C ATOM 3079 CG2 ILE D 128 34.074 19.748 -29.712 1.00 41.17 C ANISOU 3079 CG2 ILE D 128 6661 5772 3209 380 -17 55 C ATOM 3080 CD1 ILE D 128 32.489 17.207 -30.897 1.00 43.51 C ANISOU 3080 CD1 ILE D 128 7663 5487 3384 383 -115 -19 C ATOM 3081 N PRO D 129 30.296 19.523 -27.073 1.00 43.13 N ANISOU 3081 N PRO D 129 7140 5612 3637 -194 -95 217 N ATOM 3082 CA PRO D 129 29.025 18.931 -26.676 1.00 44.51 C ANISOU 3082 CA PRO D 129 7416 5697 3798 -452 -60 201 C ATOM 3083 C PRO D 129 28.538 18.034 -27.812 1.00 46.31 C ANISOU 3083 C PRO D 129 7833 5769 3993 -550 -91 144 C ATOM 3084 O PRO D 129 28.371 18.503 -28.948 1.00 45.67 O ANISOU 3084 O PRO D 129 7635 5758 3960 -524 -150 79 O ATOM 3085 CB PRO D 129 28.112 20.142 -26.512 1.00 43.89 C ANISOU 3085 CB PRO D 129 7012 5830 3834 -566 -69 127 C ATOM 3086 CG PRO D 129 28.664 21.174 -27.510 1.00 42.33 C ANISOU 3086 CG PRO D 129 6689 5698 3696 -407 -158 116 C ATOM 3087 CD PRO D 129 30.158 20.906 -27.585 1.00 41.92 C ANISOU 3087 CD PRO D 129 6732 5620 3577 -221 -129 187 C ATOM 3088 N SER D 130 28.335 16.755 -27.511 1.00 48.61 N ANISOU 3088 N SER D 130 8480 5818 4171 -672 -70 171 N ATOM 3089 CA SER D 130 28.033 15.758 -28.537 1.00 50.23 C ANISOU 3089 CA SER D 130 8958 5809 4317 -754 -121 105 C ATOM 3090 C SER D 130 26.663 15.915 -29.194 1.00 50.98 C ANISOU 3090 C SER D 130 8868 6017 4484 -1083 -138 -19 C ATOM 3091 O SER D 130 26.449 15.410 -30.301 1.00 52.73 O ANISOU 3091 O SER D 130 9225 6133 4676 -1114 -217 -106 O ATOM 3092 CB SER D 130 28.170 14.347 -27.975 1.00 53.10 C ANISOU 3092 CB SER D 130 9862 5803 4511 -821 -127 169 C ATOM 3093 OG SER D 130 27.149 14.079 -27.033 1.00 56.00 O ANISOU 3093 OG SER D 130 10304 6147 4826 -1255 -26 209 O ATOM 3094 N ASN D 131 25.742 16.608 -28.533 1.00 50.27 N ANISOU 3094 N ASN D 131 8450 6175 4476 -1296 -82 -65 N ATOM 3095 CA ASN D 131 24.409 16.834 -29.091 1.00 51.04 C ANISOU 3095 CA ASN D 131 8267 6477 4648 -1552 -131 -246 C ATOM 3096 C ASN D 131 24.386 17.938 -30.158 1.00 49.49 C ANISOU 3096 C ASN D 131 7808 6448 4548 -1292 -296 -326 C ATOM 3097 O ASN D 131 23.333 18.197 -30.752 1.00 51.41 O ANISOU 3097 O ASN D 131 7818 6870 4845 -1401 -412 -502 O ATOM 3098 CB ASN D 131 23.406 17.149 -27.972 1.00 52.29 C ANISOU 3098 CB ASN D 131 8125 6910 4834 -1839 -5 -329 C ATOM 3099 CG ASN D 131 23.767 18.416 -27.198 1.00 49.37 C ANISOU 3099 CG ASN D 131 7479 6743 4537 -1572 12 -296 C ATOM 3100 OD1 ASN D 131 24.913 18.875 -27.229 1.00 47.74 O ANISOU 3100 OD1 ASN D 131 7380 6421 4338 -1252 -34 -163 O ATOM 3101 ND2 ASN D 131 22.793 18.987 -26.515 1.00 49.77 N ANISOU 3101 ND2 ASN D 131 7158 7120 4630 -1712 78 -452 N ATOM 3102 N TYR D 132 25.540 18.575 -30.393 1.00 46.92 N ANISOU 3102 N TYR D 132 7539 6072 4217 -970 -317 -208 N ATOM 3103 CA TYR D 132 25.709 19.630 -31.420 1.00 45.91 C ANISOU 3103 CA TYR D 132 7309 6027 4108 -764 -458 -230 C ATOM 3104 C TYR D 132 26.116 19.090 -32.798 1.00 46.70 C ANISOU 3104 C TYR D 132 7659 5992 4092 -696 -521 -241 C ATOM 3105 O TYR D 132 26.247 19.823 -33.774 1.00 46.36 O ANISOU 3105 O TYR D 132 7630 5989 3997 -575 -629 -244 O ATOM 3106 CB TYR D 132 26.761 20.652 -30.957 1.00 43.72 C ANISOU 3106 CB TYR D 132 6977 5788 3845 -561 -415 -106 C ATOM 3107 CG TYR D 132 26.174 21.771 -30.131 1.00 42.94 C ANISOU 3107 CG TYR D 132 6620 5848 3849 -541 -462 -152 C ATOM 3108 CD1 TYR D 132 25.421 21.492 -28.990 1.00 40.33 C ANISOU 3108 CD1 TYR D 132 6125 5632 3567 -688 -376 -224 C ATOM 3109 CD2 TYR D 132 26.369 23.114 -30.492 1.00 41.27 C ANISOU 3109 CD2 TYR D 132 6375 5657 3649 -385 -592 -137 C ATOM 3110 CE1 TYR D 132 24.870 22.509 -28.239 1.00 41.71 C ANISOU 3110 CE1 TYR D 132 6046 5988 3815 -623 -414 -318 C ATOM 3111 CE2 TYR D 132 25.810 24.144 -29.742 1.00 40.84 C ANISOU 3111 CE2 TYR D 132 6135 5706 3675 -306 -673 -217 C ATOM 3112 CZ TYR D 132 25.066 23.824 -28.615 1.00 40.95 C ANISOU 3112 CZ TYR D 132 5925 5881 3751 -398 -580 -326 C ATOM 3113 OH TYR D 132 24.499 24.802 -27.858 1.00 42.46 O ANISOU 3113 OH TYR D 132 5911 6216 4004 -281 -647 -454 O ATOM 3114 N VAL D 133 26.268 17.787 -32.871 1.00 48.31 N ANISOU 3114 N VAL D 133 8119 6012 4224 -783 -463 -254 N ATOM 3115 CA VAL D 133 27.107 17.175 -33.866 1.00 49.11 C ANISOU 3115 CA VAL D 133 8500 5972 4188 -624 -463 -259 C ATOM 3116 C VAL D 133 26.395 15.910 -34.322 1.00 51.67 C ANISOU 3116 C VAL D 133 9084 6099 4450 -824 -527 -377 C ATOM 3117 O VAL D 133 25.661 15.303 -33.543 1.00 53.12 O ANISOU 3117 O VAL D 133 9300 6206 4676 -1100 -499 -398 O ATOM 3118 CB VAL D 133 28.469 16.903 -33.165 1.00 48.71 C ANISOU 3118 CB VAL D 133 8544 5865 4098 -399 -331 -158 C ATOM 3119 CG1 VAL D 133 28.810 15.419 -33.072 1.00 51.27 C ANISOU 3119 CG1 VAL D 133 9256 5906 4319 -340 -323 -195 C ATOM 3120 CG2 VAL D 133 29.568 17.754 -33.729 1.00 46.96 C ANISOU 3120 CG2 VAL D 133 8204 5818 3819 -185 -278 -124 C ATOM 3121 N ALA D 134 26.559 15.537 -35.588 1.00 53.12 N ANISOU 3121 N ALA D 134 9468 6207 4506 -737 -606 -467 N ATOM 3122 CA ALA D 134 25.993 14.277 -36.087 1.00 55.88 C ANISOU 3122 CA ALA D 134 10137 6322 4774 -924 -687 -601 C ATOM 3123 C ALA D 134 27.067 13.468 -36.792 1.00 57.52 C ANISOU 3123 C ALA D 134 10724 6325 4805 -640 -663 -644 C ATOM 3124 O ALA D 134 27.958 14.043 -37.425 1.00 57.00 O ANISOU 3124 O ALA D 134 10586 6418 4652 -359 -608 -630 O ATOM 3125 CB ALA D 134 24.807 14.523 -37.010 1.00 56.69 C ANISOU 3125 CB ALA D 134 10104 6556 4879 -1124 -874 -758 C ATOM 3126 N ARG D 135 26.988 12.140 -36.677 1.00 60.31 N ANISOU 3126 N ARG D 135 11503 6332 5080 -723 -699 -714 N ATOM 3127 CA ARG D 135 27.957 11.269 -37.322 1.00 62.29 C ANISOU 3127 CA ARG D 135 12153 6364 5150 -382 -711 -814 C ATOM 3128 C ARG D 135 27.745 11.301 -38.821 1.00 62.98 C ANISOU 3128 C ARG D 135 12302 6529 5100 -353 -802 -978 C ATOM 3129 O ARG D 135 26.613 11.250 -39.292 1.00 63.83 O ANISOU 3129 O ARG D 135 12398 6629 5224 -682 -938 -1063 O ATOM 3130 CB ARG D 135 27.844 9.826 -36.820 1.00 65.93 C ANISOU 3130 CB ARG D 135 13180 6337 5534 -473 -784 -854 C ATOM 3131 CG ARG D 135 29.001 8.934 -37.279 1.00 69.64 C ANISOU 3131 CG ARG D 135 14080 6565 5816 28 -825 -984 C ATOM 3132 CD ARG D 135 28.641 7.475 -37.199 1.00 78.25 C ANISOU 3132 CD ARG D 135 15878 7075 6779 -105 -979 -1072 C ATOM 3133 NE ARG D 135 29.779 6.609 -37.511 1.00 83.97 N ANISOU 3133 NE ARG D 135 17047 7539 7319 482 -1059 -1228 N ATOM 3134 CZ ARG D 135 30.511 5.968 -36.601 1.00 87.48 C ANISOU 3134 CZ ARG D 135 17858 7681 7701 818 -1126 -1181 C ATOM 3135 NH1 ARG D 135 30.234 6.086 -35.308 1.00 87.34 N ANISOU 3135 NH1 ARG D 135 17854 7564 7767 571 -1098 -949 N ATOM 3136 NH2 ARG D 135 31.525 5.201 -36.981 1.00 91.35 N ANISOU 3136 NH2 ARG D 135 18716 7977 8014 1439 -1239 -1390 N ATOM 3137 N VAL D 136 28.855 11.366 -39.549 1.00 63.30 N ANISOU 3137 N VAL D 136 12390 6681 4979 40 -723 -1048 N ATOM 3138 CA VAL D 136 28.871 11.393 -41.001 1.00 64.95 C ANISOU 3138 CA VAL D 136 12710 6985 4981 119 -771 -1204 C ATOM 3139 C VAL D 136 29.052 9.990 -41.590 1.00 69.44 C ANISOU 3139 C VAL D 136 13811 7207 5367 275 -864 -1431 C ATOM 3140 O VAL D 136 29.892 9.220 -41.120 1.00 71.11 O ANISOU 3140 O VAL D 136 14260 7224 5536 592 -825 -1487 O ATOM 3141 CB VAL D 136 29.998 12.337 -41.498 1.00 63.76 C ANISOU 3141 CB VAL D 136 12299 7223 4706 395 -578 -1170 C ATOM 3142 CG1 VAL D 136 30.335 12.109 -42.979 1.00 66.46 C ANISOU 3142 CG1 VAL D 136 12860 7655 4737 548 -565 -1361 C ATOM 3143 CG2 VAL D 136 29.599 13.766 -41.291 1.00 60.21 C ANISOU 3143 CG2 VAL D 136 11472 7034 4371 186 -561 -976 C ATOM 3144 N ASP D 137 28.257 9.664 -42.609 1.00 72.01 N ANISOU 3144 N ASP D 137 14349 7442 5570 84 -1025 -1583 N ATOM 3145 CA ASP D 137 28.532 8.503 -43.462 1.00 76.99 C ANISOU 3145 CA ASP D 137 15498 7790 5964 282 -1116 -1841 C ATOM 3146 C ASP D 137 29.815 8.689 -44.265 1.00 78.08 C ANISOU 3146 C ASP D 137 15606 8201 5858 772 -942 -1968 C ATOM 3147 O ASP D 137 30.265 7.766 -44.942 1.00 82.00 O ANISOU 3147 O ASP D 137 16501 8524 6133 1061 -982 -2222 O ATOM 3148 CB ASP D 137 27.370 8.232 -44.428 1.00 79.31 C ANISOU 3148 CB ASP D 137 15981 7987 6165 -61 -1344 -1995 C ATOM 3149 CG ASP D 137 26.218 7.513 -43.757 1.00 81.79 C ANISOU 3149 CG ASP D 137 16471 7962 6643 -555 -1513 -2002 C ATOM 3150 OD1 ASP D 137 25.786 6.442 -44.281 1.00 84.20 O ANISOU 3150 OD1 ASP D 137 17267 7909 6818 -710 -1692 -2215 O ATOM 3151 OD2 ASP D 137 25.775 8.021 -42.694 1.00 78.71 O ANISOU 3151 OD2 ASP D 137 15740 7676 6490 -812 -1451 -1808 O TER 3152 ASP D 137 HETATM 3153 C1 EDO A 2 29.293 60.397 1.846 1.00 28.16 C HETATM 3154 O1 EDO A 2 29.497 61.485 0.945 1.00 28.96 O HETATM 3155 C2 EDO A 2 28.899 59.193 1.010 1.00 30.83 C HETATM 3156 O2 EDO A 2 27.979 59.596 -0.026 1.00 36.13 O HETATM 3157 C1 EDO C 1 25.964 45.573 -4.187 1.00 69.85 C HETATM 3158 O1 EDO C 1 25.379 46.220 -3.040 1.00 69.45 O HETATM 3159 C2 EDO C 1 25.199 44.295 -4.555 1.00 70.89 C HETATM 3160 O2 EDO C 1 25.154 44.135 -5.987 1.00 70.42 O HETATM 3161 O HOH A 3 22.903 54.283 7.576 1.00 22.00 O HETATM 3162 O HOH A 4 29.443 71.934 -8.062 1.00 9.86 O HETATM 3163 O HOH A 8 26.626 70.112 28.900 1.00 23.82 O HETATM 3164 O HOH A 9 31.397 50.101 -5.332 1.00 17.24 O HETATM 3165 O HOH A 10 31.634 65.780 26.170 1.00 11.38 O HETATM 3166 O HOH A 11 42.839 66.817 1.205 1.00 8.33 O HETATM 3167 O HOH A 12 38.040 46.296 4.386 1.00 20.83 O HETATM 3168 O HOH A 14 31.768 51.256 -7.736 1.00 18.51 O HETATM 3169 O HOH A 18 40.616 66.329 -0.303 1.00 10.29 O HETATM 3170 O HOH A 19 27.937 47.433 -13.433 1.00 32.15 O HETATM 3171 O HOH A 20 28.767 52.214 1.522 1.00 15.31 O HETATM 3172 O HOH A 21 29.453 69.287 -7.454 1.00 12.88 O HETATM 3173 O HOH A 22 39.654 72.756 4.714 1.00 11.06 O HETATM 3174 O HOH A 26 26.762 43.231 -16.234 1.00 27.96 O HETATM 3175 O HOH A 27 34.071 50.497 -8.845 1.00 17.45 O HETATM 3176 O HOH A 28 28.798 64.975 -1.429 1.00 12.89 O HETATM 3177 O HOH A 31 30.191 61.337 -1.584 1.00 15.76 O HETATM 3178 O HOH A 35 35.819 66.794 5.326 1.00 11.02 O HETATM 3179 O HOH A 36 29.530 63.729 2.484 1.00 11.22 O HETATM 3180 O HOH A 37 33.218 71.861 12.975 1.00 16.38 O HETATM 3181 O HOH A 38 43.827 51.370 11.116 1.00 19.10 O HETATM 3182 O HOH A 39 31.029 66.279 10.680 1.00 15.04 O HETATM 3183 O HOH A 40 39.261 75.179 16.814 1.00 17.08 O HETATM 3184 O HOH A 42 41.138 72.376 7.082 1.00 12.56 O HETATM 3185 O HOH A 211 42.871 58.746 -4.746 1.00 16.60 O HETATM 3186 O HOH A 212 34.102 62.777 -5.773 1.00 16.75 O HETATM 3187 O HOH A 213 23.856 54.914 4.635 1.00 22.65 O HETATM 3188 O HOH A 214 28.753 74.110 -6.203 1.00 16.55 O HETATM 3189 O HOH A 215 29.811 59.402 21.237 1.00 20.24 O HETATM 3190 O HOH A 216 42.226 66.303 3.685 1.00 14.70 O HETATM 3191 O HOH A 217 28.051 65.738 2.765 1.00 16.10 O HETATM 3192 O HOH A 218 44.855 68.409 17.563 1.00 16.59 O HETATM 3193 O HOH A 219 46.593 71.137 -2.100 1.00 18.60 O HETATM 3194 O HOH A 220 41.671 52.604 11.416 1.00 19.73 O HETATM 3195 O HOH A 221 41.502 73.443 17.643 1.00 20.89 O HETATM 3196 O HOH A 222 29.204 64.802 26.616 1.00 18.53 O HETATM 3197 O HOH A 223 45.227 74.073 12.025 1.00 18.15 O HETATM 3198 O HOH A 224 32.357 66.336 14.872 1.00 17.52 O HETATM 3199 O HOH A 225 42.566 68.632 18.596 1.00 21.23 O HETATM 3200 O HOH A 226 27.272 62.675 -1.461 1.00 21.22 O HETATM 3201 O HOH A 227 29.516 58.341 19.031 1.00 22.26 O HETATM 3202 O HOH A 228 40.302 50.185 -1.075 1.00 25.83 O HETATM 3203 O HOH A 229 39.528 53.439 17.255 1.00 35.66 O HETATM 3204 O HOH A 230 38.147 47.472 -0.661 1.00 24.46 O HETATM 3205 O HOH A 231 33.225 54.840 -9.810 1.00 28.71 O HETATM 3206 O HOH A 232 39.893 60.048 -7.988 1.00 24.32 O HETATM 3207 O HOH A 233 43.799 73.089 16.101 1.00 21.77 O HETATM 3208 O HOH A 234 27.170 53.933 -0.036 1.00 27.40 O HETATM 3209 O HOH A 235 40.481 74.750 3.259 1.00 28.81 O HETATM 3210 O HOH A 236 39.293 73.041 8.875 1.00 29.09 O HETATM 3211 O HOH A 237 43.703 70.516 21.268 1.00 29.09 O HETATM 3212 O HOH A 238 45.071 74.961 14.605 1.00 24.99 O HETATM 3213 O HOH A 239 25.078 65.273 21.388 1.00 29.32 O HETATM 3214 O HOH A 240 23.842 49.559 -2.338 1.00 34.25 O HETATM 3215 O HOH A 241 27.221 55.969 -3.453 1.00 24.31 O HETATM 3216 O HOH A 242 43.534 56.834 -6.410 1.00 30.66 O HETATM 3217 O HOH A 243 41.698 47.089 5.146 1.00 34.86 O HETATM 3218 O HOH A 244 43.432 74.550 0.737 1.00 28.68 O HETATM 3219 O HOH A 245 37.412 57.784 -8.755 1.00 29.15 O HETATM 3220 O HOH A 246 28.276 71.255 6.464 1.00 30.31 O HETATM 3221 O HOH A 247 28.968 62.465 4.887 1.00 28.05 O HETATM 3222 O HOH A 248 26.046 51.337 3.620 1.00 28.75 O HETATM 3223 O HOH A 249 41.534 74.621 20.342 1.00 21.80 O HETATM 3224 O HOH A 250 38.397 49.263 -2.469 1.00 28.95 O HETATM 3225 O HOH A 251 43.022 75.198 9.923 1.00 27.85 O HETATM 3226 O HOH A 252 40.819 76.944 -5.298 1.00 30.74 O HETATM 3227 O HOH A 253 23.029 59.750 3.725 1.00 30.72 O HETATM 3228 O HOH A 254 26.051 56.335 -5.746 1.00 34.41 O HETATM 3229 O HOH A 255 27.589 47.092 -6.716 1.00 35.14 O HETATM 3230 O HOH A 256 26.901 56.304 -1.100 1.00 30.30 O HETATM 3231 O HOH A 257 30.691 76.100 -0.676 1.00 36.98 O HETATM 3232 O HOH A 258 27.424 62.889 10.397 1.00 32.37 O HETATM 3233 O HOH A 259 50.267 67.593 14.426 1.00 32.27 O HETATM 3234 O HOH A 260 33.155 70.354 4.904 1.00 31.79 O HETATM 3235 O HOH A 261 38.817 76.498 11.435 1.00 36.67 O HETATM 3236 O HOH A 262 33.627 56.985 -11.317 1.00 34.90 O HETATM 3237 O HOH A 263 36.485 60.748 -8.057 1.00 41.24 O HETATM 3238 O HOH A 264 35.928 81.741 0.148 1.00 44.59 O HETATM 3239 O HOH A 265 33.914 64.829 -7.551 1.00 41.82 O HETATM 3240 O HOH A 266 32.086 45.783 9.861 1.00 17.77 O HETATM 3241 O HOH A 267 44.795 71.362 17.451 1.00 16.94 O HETATM 3242 O HOH A 268 48.078 69.197 19.786 1.00 35.76 O HETATM 3243 O HOH A 269 44.537 72.691 -4.513 1.00 36.44 O HETATM 3244 O HOH A 270 30.375 67.641 -9.925 1.00 27.37 O HETATM 3245 O HOH A 271 28.596 64.320 -11.022 1.00 40.56 O HETATM 3246 O HOH A 272 25.412 63.096 0.561 1.00 23.17 O HETATM 3247 O HOH A 273 44.946 61.589 -2.753 1.00 30.55 O HETATM 3248 O HOH A 274 44.689 76.142 8.093 1.00 37.01 O HETATM 3249 O HOH A 275 27.136 58.088 -6.973 1.00 39.85 O HETATM 3250 O HOH A 276 44.885 55.537 0.188 1.00 32.20 O HETATM 3251 O HOH A 277 44.643 53.019 3.212 1.00 19.55 O HETATM 3252 O HOH A 278 48.598 56.251 2.797 1.00 23.61 O HETATM 3253 O HOH A 279 33.735 74.208 2.179 1.00 37.28 O HETATM 3254 O HOH A 280 45.261 50.077 9.378 1.00 35.23 O HETATM 3255 O HOH A 281 24.945 68.220 17.647 1.00 61.57 O HETATM 3256 O HOH A 282 47.903 59.870 18.223 1.00 27.30 O HETATM 3257 O HOH A 283 27.124 61.689 -4.309 1.00 22.60 O HETATM 3258 O HOH A 284 47.264 73.886 6.228 1.00 20.93 O HETATM 3259 O HOH A 285 28.828 49.330 -5.836 1.00 37.33 O HETATM 3260 O HOH A 286 28.595 66.369 8.079 1.00 31.48 O HETATM 3261 O HOH A 287 48.183 74.416 8.293 1.00 32.38 O HETATM 3262 O HOH A 288 24.147 42.522 -9.769 1.00 13.36 O HETATM 3263 O HOH A 289 39.725 76.511 20.732 1.00 41.17 O HETATM 3264 O HOH A 290 52.159 57.634 6.114 1.00 35.95 O HETATM 3265 O HOH A 291 47.646 61.613 16.422 1.00 18.79 O HETATM 3266 O HOH A 292 26.338 61.706 4.311 1.00 32.27 O HETATM 3267 O HOH A 293 29.024 72.661 -10.835 1.00 29.45 O HETATM 3268 O HOH A 294 27.839 72.606 -13.180 1.00 23.90 O HETATM 3269 O HOH A 295 29.243 76.445 -7.734 1.00 16.55 O HETATM 3270 O HOH A 296 37.124 73.270 5.038 1.00 27.15 O HETATM 3271 O HOH A 297 36.432 71.990 7.327 1.00 38.39 O HETATM 3272 O HOH B 6 41.967 68.442 22.743 1.00 12.77 O HETATM 3273 O HOH B 13 32.817 62.619 43.641 1.00 14.56 O HETATM 3274 O HOH B 16 44.715 77.487 25.705 1.00 20.88 O HETATM 3275 O HOH B 17 49.385 79.834 35.787 1.00 18.08 O HETATM 3276 O HOH B 73 43.130 75.339 22.329 1.00 28.89 O HETATM 3277 O HOH B 75 46.214 71.056 48.708 1.00 23.99 O HETATM 3278 O HOH B 139 49.673 68.353 24.571 1.00 31.32 O HETATM 3279 O HOH B 140 32.859 62.693 37.478 1.00 27.55 O HETATM 3280 O HOH B 141 36.308 60.763 40.494 1.00 31.56 O HETATM 3281 O HOH B 142 37.512 62.890 25.827 1.00 21.18 O HETATM 3282 O HOH B 143 35.727 77.961 33.842 1.00 29.13 O HETATM 3283 O HOH B 174 46.688 60.082 20.967 1.00 23.26 O HETATM 3284 O HOH B 186 45.208 75.158 46.310 1.00 20.98 O HETATM 3285 O HOH B 189 44.636 80.701 41.335 1.00 22.25 O HETATM 3286 O HOH B 196 44.658 62.122 27.932 1.00 26.41 O HETATM 3287 O HOH C 2 29.403 46.304 6.929 1.00 13.14 O HETATM 3288 O HOH C 5 32.880 47.075 7.401 1.00 19.05 O HETATM 3289 O HOH C 7 38.873 24.133 -0.395 1.00 18.61 O HETATM 3290 O HOH C 15 37.020 25.110 1.326 1.00 22.93 O HETATM 3291 O HOH C 23 29.015 16.979 -8.140 1.00 27.31 O HETATM 3292 O HOH C 24 27.420 28.605 -29.310 1.00 27.81 O HETATM 3293 O HOH C 25 41.658 47.819 9.308 1.00 29.80 O HETATM 3294 O HOH C 29 26.352 25.419 -12.536 1.00 19.86 O HETATM 3295 O HOH C 32 35.012 18.461 -5.552 1.00 22.79 O HETATM 3296 O HOH C 33 36.653 44.652 -3.820 1.00 17.02 O HETATM 3297 O HOH C 34 27.699 41.018 0.311 1.00 31.31 O HETATM 3298 O HOH C 41 42.707 37.190 -4.020 1.00 24.92 O HETATM 3299 O HOH C 43 37.288 33.876 8.842 1.00 30.51 O HETATM 3300 O HOH C 44 23.989 25.735 -23.797 1.00 25.89 O HETATM 3301 O HOH C 211 31.165 44.119 6.288 1.00 15.15 O HETATM 3302 O HOH C 212 37.203 45.127 -1.160 1.00 22.08 O HETATM 3303 O HOH C 213 31.306 15.423 -14.842 1.00 23.61 O HETATM 3304 O HOH C 214 31.723 25.405 -3.291 1.00 25.69 O HETATM 3305 O HOH C 215 24.931 41.913 -1.645 1.00 24.75 O HETATM 3306 O HOH C 216 32.987 18.073 -7.029 1.00 25.01 O HETATM 3307 O HOH C 217 38.397 24.417 -2.876 1.00 28.28 O HETATM 3308 O HOH C 218 26.349 29.046 0.185 1.00 26.90 O HETATM 3309 O HOH C 219 42.682 34.330 6.103 1.00 28.60 O HETATM 3310 O HOH C 220 27.190 19.776 -10.458 1.00 25.49 O HETATM 3311 O HOH C 221 41.338 32.513 4.597 1.00 34.65 O HETATM 3312 O HOH C 222 38.770 31.782 8.643 1.00 31.79 O HETATM 3313 O HOH C 223 46.225 33.168 -3.850 1.00 34.84 O HETATM 3314 O HOH C 224 34.358 18.754 -3.047 1.00 30.74 O HETATM 3315 O HOH C 225 34.981 38.281 10.460 1.00 32.39 O HETATM 3316 O HOH C 226 32.485 29.815 7.461 1.00 36.44 O HETATM 3317 O HOH C 227 25.889 25.975 -7.770 1.00 27.74 O HETATM 3318 O HOH C 228 42.460 18.883 2.568 1.00 33.99 O HETATM 3319 O HOH C 229 36.244 16.715 -14.716 1.00 32.34 O HETATM 3320 O HOH C 230 26.145 31.763 -0.536 1.00 31.73 O HETATM 3321 O HOH C 231 31.962 38.276 9.895 1.00 44.90 O HETATM 3322 O HOH C 232 43.086 34.900 -0.438 1.00 32.47 O HETATM 3323 O HOH C 233 21.764 38.742 -1.657 1.00 32.97 O HETATM 3324 O HOH C 234 37.808 16.344 0.465 1.00 42.29 O HETATM 3325 O HOH C 235 25.747 19.650 -3.568 1.00 35.97 O HETATM 3326 O HOH C 236 34.663 31.368 8.777 1.00 52.69 O HETATM 3327 O HOH C 237 45.296 36.954 -17.203 1.00 45.54 O HETATM 3328 O HOH C 238 31.294 14.347 -9.498 1.00 41.91 O HETATM 3329 O HOH C 239 38.139 37.785 -11.352 1.00 39.05 O HETATM 3330 O HOH C 240 46.000 32.068 -10.983 1.00 44.63 O HETATM 3331 O HOH C 241 24.337 26.698 -5.505 1.00 54.63 O HETATM 3332 O HOH C 242 42.570 29.064 2.500 1.00 43.91 O HETATM 3333 O HOH C 243 32.431 31.016 11.235 1.00 47.73 O HETATM 3334 O HOH C 244 38.948 43.917 0.148 1.00 45.54 O HETATM 3335 O HOH C 245 42.176 36.541 2.293 1.00 55.23 O HETATM 3336 O HOH C 246 44.182 26.351 3.457 1.00 54.01 O HETATM 3337 O HOH C 247 36.291 30.298 10.577 1.00 55.36 O HETATM 3338 O HOH C 248 41.599 47.913 12.186 1.00 26.63 O HETATM 3339 O HOH C 249 38.848 41.590 1.024 0.50 22.30 O HETATM 3340 O HOH C 250 41.420 39.005 1.688 1.00 58.38 O HETATM 3341 O HOH C 251 18.566 26.802 -10.076 1.00 39.96 O HETATM 3342 O HOH C 252 22.568 28.611 -2.350 1.00 46.81 O HETATM 3343 O HOH C 253 35.515 19.476 -20.327 1.00 39.60 O HETATM 3344 O HOH C 254 37.342 21.481 -17.231 1.00 34.80 O HETATM 3345 O HOH C 255 34.941 21.413 -17.487 1.00 29.07 O HETATM 3346 O HOH C 256 46.188 25.170 -8.823 1.00 35.27 O HETATM 3347 O HOH C 257 27.551 31.734 3.905 1.00 25.15 O HETATM 3348 O HOH C 258 26.972 33.213 1.714 1.00 38.87 O HETATM 3349 O HOH C 259 18.563 25.224 -13.491 1.00 38.83 O HETATM 3350 O HOH C 260 42.678 29.685 9.905 1.00 56.12 O HETATM 3351 O HOH C 261 20.278 26.039 -8.344 1.00 40.47 O HETATM 3352 O HOH C 262 24.660 30.769 -26.527 1.00 34.01 O HETATM 3353 O HOH C 263 45.941 27.302 -7.666 1.00 53.19 O HETATM 3354 O HOH C 264 35.462 37.339 -15.806 1.00 40.77 O HETATM 3355 O HOH C 265 31.424 42.816 8.556 1.00 37.45 O HETATM 3356 O HOH D 30 34.059 21.500 -21.419 1.00 26.11 O HETATM 3357 O HOH D 51 38.691 26.673 -30.166 1.00 27.77 O HETATM 3358 O HOH D 69 41.423 19.770 -24.199 1.00 26.39 O HETATM 3359 O HOH D 139 33.647 13.973 -20.864 1.00 28.38 O HETATM 3360 O HOH D 140 25.067 30.435 -36.664 1.00 35.46 O HETATM 3361 O HOH D 141 46.762 24.802 -32.787 1.00 27.14 O HETATM 3362 O HOH D 142 42.569 21.928 -26.093 1.00 41.33 O HETATM 3363 O HOH D 143 36.705 24.043 -35.424 1.00 39.65 O HETATM 3364 O HOH D 190 31.894 7.919 -42.444 1.00 39.25 O HETATM 3365 O HOH D 199 35.462 21.399 -41.184 1.00 30.71 O HETATM 3366 O HOH D 200 29.230 7.752 -31.129 1.00 33.71 O HETATM 3367 O HOH D 201 22.710 14.805 -33.242 1.00 34.51 O HETATM 3368 O HOH D 208 27.670 6.440 -40.094 1.00 35.96 O CONECT 3153 3154 3155 CONECT 3154 3153 CONECT 3155 3153 3156 CONECT 3156 3155 CONECT 3157 3158 3159 CONECT 3158 3157 CONECT 3159 3157 3160 CONECT 3160 3159 MASTER 442 0 2 12 14 0 3 6 3336 4 8 36 END
Display Options:
Goto PDB code:
3D presentation of molecule is powered by
3Dmol
, which supports all modern browsers and mobile devices via WebGL.
Hold mouse button:
left to rotate,middle to shift,right to zoom
Related entries of code: 3rbb
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%
3rea
RCSB PDB
PDBbind
61aa, >3REA_2|Chains... at 100%
3reb
RCSB PDB
PDBbind
90aa, >3REB_2|Chains... *
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
3rbb
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
HIV-1 Nef protein (delta 1-44 N-terminal)
Ligand Name
engineered HCK SH3 domain
EC.Number
E.C.-.-.-.-
Resolution
2.35(Å)
Affinity (Kd/Ki/IC50)
Kd=12.3nM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2011) Traffic Vol. 12: pp. 867-877
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
This site has been visited
times since Nov 2007.
Copyright ©2007-2024 涓婃捣鐩堣禌鎬濅俊鎭鎶鏈夐檺鍏徃 缃戠珯澶囨鍙凤細
娌狪CP澶2021015625鍙-3
娌叕缃戝畨澶囷細
姝ｅ湪鐢宠涓
Technical Support锛堟妧鏈敮鎸侊級:
yingsaisi@foxmail.com
times since Nov 2007. 
娌叕缃戝畨澶囷細姝ｅ湪鐢宠涓