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*** 1exr ***elNémo ID: 240124131923244126Job options:ID = 240124131923244126 JOBID = 1exr USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER 1exr HEADER METAL TRANSPORT 03-MAY-00 1EXR TITLE THE 1.0 ANGSTROM CRYSTAL STRUCTURE OF CA+2 BOUND CALMODULIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALMODULIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PARAMECIUM TETRAURELIA; SOURCE 3 ORGANISM_TAXID: 5888; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM109; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PKK233-3 KEYWDS CALMODULIN, HIGH RESOLUTION, DISORDER, METAL TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR M.A.WILSON,A.T.BRUNGER REVDAT 4 24-JUL-19 1EXR 1 REMARK REVDAT 3 24-FEB-09 1EXR 1 VERSN REVDAT 2 09-SEP-03 1EXR 1 JRNL REMARK DBREF MASTER REVDAT 1 20-SEP-00 1EXR 0 JRNL AUTH M.A.WILSON,A.T.BRUNGER JRNL TITL THE 1.0 A CRYSTAL STRUCTURE OF CA(2+)-BOUND CALMODULIN: AN JRNL TITL 2 ANALYSIS OF DISORDER AND IMPLICATIONS FOR FUNCTIONALLY JRNL TITL 3 RELEVANT PLASTICITY JRNL REF J.MOL.BIOL. V. 301 1237 2000 JRNL REFN ISSN 0022-2836 JRNL PMID 10966818 JRNL DOI 10.1006/JMBI.2000.4029 REMARK 2 REMARK 2 RESOLUTION. 1.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 500.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 3 CROSS-VALIDATION METHOD : FREE R REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.136 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.134 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.163 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 7782 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 77150 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.124 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.122 REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.151 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 6361 REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 63169 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1150 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 5 REMARK 3 SOLVENT ATOMS : 178 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1327.0 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1089.0 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 36 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 14894 REMARK 3 NUMBER OF RESTRAINTS : 22732 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 ANGLE DISTANCES (A) : 0.030 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.023 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.070 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.080 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.080 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.050 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.100 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91 (1973)201-228 REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE R REMARK 3 (NO CUTOFF) BY 9% REMARK 4 REMARK 4 1EXR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-00. REMARK 100 THE DEPOSITION ID IS D_1000011001. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-JUL-99 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.0 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL9-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.886 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78247 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : 0.07300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.04 REMARK 200 COMPLETENESS FOR SHELL (%) : 83.9 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : 0.50600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: UNPUBLISHED 1.1 A PARAMECIUM TETRAURELIA REMARK 200 CALMODULIN REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 40.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, CALCIUM CHLORIDE, SODIUM REMARK 280 CACODYLATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 278K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 ALA A 1 REMARK 465 LYS A 148 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLU A 54 OE1 - CD - OE2 ANGL. DEV. = 12.9 DEGREES REMARK 500 LEU A 69 CA - CB - CG ANGL. DEV. = 14.1 DEGREES REMARK 500 ARG A 74 CD - NE - CZ ANGL. DEV. = 16.7 DEGREES REMARK 500 ARG A 74 NE - CZ - NH1 ANGL. DEV. = 8.4 DEGREES REMARK 500 ARG A 74 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 GLU A 78 OE1 - CD - OE2 ANGL. DEV. = -7.4 DEGREES REMARK 500 ASP A 119 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 ASP A 122 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES REMARK 500 ARG A 126 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES REMARK 500 ARG A 143 CG - CD - NE ANGL. DEV. = 29.0 DEGREES REMARK 500 ARG A 143 CD - NE - CZ ANGL. DEV. = 17.1 DEGREES REMARK 500 ARG A 143 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 ARG A 143 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES REMARK 500 SER A 147 CA - C - O ANGL. DEV. = 15.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLN A 3 -70.65 -175.69 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1000 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A2122 O REMARK 620 2 GLU A 31 OE1 83.1 REMARK 620 3 THR A 26 O 105.7 75.8 REMARK 620 4 ASP A 22 OD1 86.7 126.8 156.1 REMARK 620 5 GLU A 31 OE2 90.1 53.0 124.2 75.0 REMARK 620 6 ASP A 20 OD1 164.1 112.7 80.2 82.9 98.7 REMARK 620 7 ASP A 24 OD1 81.8 146.3 79.6 82.2 156.2 84.9 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1001 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 56 OD1 REMARK 620 2 ASN A 60 OD1 85.9 REMARK 620 3 THR A 62 O 79.3 79.5 REMARK 620 4 HOH A2011 O 143.3 73.0 67.7 REMARK 620 5 GLU A 67 OE1 103.1 157.1 81.6 88.0 REMARK 620 6 ASP A 58 OD1 77.6 76.5 147.6 123.8 125.8 REMARK 620 7 HOH A2127 O 152.8 92.7 127.2 60.1 88.5 75.7 REMARK 620 8 GLU A 67 OE2 87.4 151.1 126.7 124.9 51.5 74.6 80.7 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 140 OE1 REMARK 620 2 ASP A 133 OD1 147.3 REMARK 620 3 ASP A 129 OD1 108.7 93.5 REMARK 620 4 GLU A 140 OE2 52.3 158.4 81.8 REMARK 620 5 HOH A2129 O 83.0 79.2 166.2 100.6 REMARK 620 6 HIS A 135 O 79.6 76.9 89.4 123.9 100.2 REMARK 620 7 ASP A 131 OD1 126.8 78.1 83.6 80.4 83.4 153.5 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1003 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A2123 O REMARK 620 2 GLU A 47 OE1 85.4 REMARK 620 3 GLU A 47 OE2 133.3 52.8 REMARK 620 4 HOH A2125 O 81.6 86.9 76.7 REMARK 620 5 HOH A2126 O 148.9 110.5 74.4 124.3 REMARK 620 6 HOH A2124 O 76.2 91.1 118.9 157.8 77.0 REMARK 620 7 ASP A 58 OD2 88.5 169.7 128.9 84.0 78.8 95.5 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1004 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 93 OD1 REMARK 620 2 ASP A 95 OD1 86.8 REMARK 620 3 LEU A 99 O 86.9 155.4 REMARK 620 4 GLU A 104 OE1 98.6 126.8 77.7 REMARK 620 5 GLU A 104 OE2 100.3 74.6 130.0 52.3 REMARK 620 6 HOH A2128 O 174.2 88.4 96.2 86.9 81.5 REMARK 620 7 ASN A 97 OD1 87.5 77.4 78.7 155.2 150.3 88.3 REMARK 620 N 1 2 3 4 5 6 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1000 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1004 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CLM RELATED DB: PDB REMARK 900 1.8 ANGSTROM STRUCTURE OF WILD TYPE PARAMECIUM TETRAURELIA REMARK 900 CALMODULIN REMARK 900 RELATED ID: 1OSA RELATED DB: PDB REMARK 900 1.68 ANGSTROM STRUCTURE OF RECOMBINANT PARAMECIUM TETRAURELIA REMARK 900 CALMODULIN DBREF 1EXR A 1 148 UNP P07463 CALM_PARTE 2 149 SEQRES 1 A 148 ALA GLU GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS SEQRES 2 A 148 GLU ALA PHE ALA LEU PHE ASP LYS ASP GLY ASP GLY THR SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE SEQRES 6 A 148 PRO GLU PHE LEU SER LEU MET ALA ARG LYS MET LYS GLU SEQRES 7 A 148 GLN ASP SER GLU GLU GLU LEU ILE GLU ALA PHE LYS VAL SEQRES 8 A 148 PHE ASP ARG ASP GLY ASN GLY LEU ILE SER ALA ALA GLU SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR SEQRES 10 A 148 ASP ASP GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE SEQRES 11 A 148 ASP GLY ASP GLY HIS ILE ASN TYR GLU GLU PHE VAL ARG SEQRES 12 A 148 MET MET VAL SER LYS HET CA A1000 1 HET CA A1001 1 HET CA A1002 1 HET CA A1003 1 HET CA A1004 1 HETNAM CA CALCIUM ION FORMUL 2 CA 5(CA 2+) FORMUL 7 HOH *178(H2 O) HELIX 1 1 THR A 5 ASP A 20 1 16 HELIX 2 2 THR A 28 LEU A 39 1 12 HELIX 3 3 THR A 44 GLU A 54 1 11 HELIX 4 4 PHE A 65 ASP A 93 1 29 HELIX 5 5 SER A 101 LEU A 112 1 12 HELIX 6 6 THR A 117 ASP A 129 1 13 HELIX 7 7 ASN A 137 SER A 147 1 11 SHEET 1 A 2 THR A 26 ILE A 27 0 SHEET 2 A 2 ILE A 63 ASP A 64 -1 N ILE A 63 O ILE A 27 LINK CA CA A1000 O HOH A2122 1555 1555 2.35 LINK CA CA A1000 OE1 GLU A 31 1555 1555 2.47 LINK CA CA A1000 O THR A 26 1555 1555 2.36 LINK CA CA A1000 OD1 ASP A 22 1555 1555 2.44 LINK CA CA A1000 OE2 GLU A 31 1555 1555 2.48 LINK CA CA A1000 OD1 ASP A 20 1555 1555 2.31 LINK CA CA A1000 OD1 ASP A 24 1555 1555 2.35 LINK CA CA A1001 OD1 ASP A 56 1555 1555 2.34 LINK CA CA A1001 OD1 ASN A 60 1555 1555 2.40 LINK CA CA A1001 O THR A 62 1555 1555 2.41 LINK CA CA A1001 O HOH A2011 1555 1555 2.90 LINK CA CA A1001 OE1 GLU A 67 1555 1555 2.47 LINK CA CA A1001 OD1 ASP A 58 1555 1555 2.44 LINK CA CA A1001 O HOH A2127 1555 1555 2.42 LINK CA CA A1001 OE2 GLU A 67 1555 1555 2.60 LINK CA CA A1002 OE1 GLU A 140 1555 1555 2.44 LINK CA CA A1002 OD1 ASP A 133 1555 1555 2.39 LINK CA CA A1002 OD1 ASP A 129 1555 1555 2.30 LINK CA CA A1002 OE2 GLU A 140 1555 1555 2.55 LINK CA CA A1002 O HOH A2129 1555 1555 2.42 LINK CA CA A1002 O HIS A 135 1555 1555 2.35 LINK CA CA A1002 OD1 ASP A 131 1555 1555 2.35 LINK CA CA A1003 O HOH A2123 1555 1555 2.41 LINK CA CA A1003 OE1 GLU A 47 1555 1555 2.50 LINK CA CA A1003 OE2 GLU A 47 1555 1555 2.45 LINK CA CA A1003 O HOH A2125 1555 1555 2.40 LINK CA CA A1003 O HOH A2126 1555 1555 2.36 LINK CA CA A1003 O HOH A2124 1555 1555 2.41 LINK CA CA A1004 OD1 ASP A 93 1555 1555 2.30 LINK CA CA A1004 OD1 ASP A 95 1555 1555 2.33 LINK CA CA A1004 O LEU A 99 1555 1555 2.28 LINK CA CA A1004 OE1 GLU A 104 1555 1555 2.46 LINK CA CA A1004 OE2 GLU A 104 1555 1555 2.54 LINK CA CA A1004 O HOH A2128 1555 1555 2.37 LINK CA CA A1004 OD1 ASN A 97 1555 1555 2.42 LINK CA CA A1003 OD2 ASP A 58 1555 1545 2.38 SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26 SITE 2 AC1 6 GLU A 31 HOH A2122 SITE 1 AC2 7 ASP A 56 ASP A 58 ASN A 60 THR A 62 SITE 2 AC2 7 GLU A 67 HOH A2011 HOH A2127 SITE 1 AC3 6 ASP A 129 ASP A 131 ASP A 133 HIS A 135 SITE 2 AC3 6 GLU A 140 HOH A2129 SITE 1 AC4 6 GLU A 47 ASP A 58 HOH A2123 HOH A2124 SITE 2 AC4 6 HOH A2125 HOH A2126 SITE 1 AC5 6 ASP A 93 ASP A 95 ASN A 97 LEU A 99 SITE 2 AC5 6 GLU A 104 HOH A2128 CRYST1 25.015 29.415 52.761 89.54 86.10 82.39 P 1 1 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 0.039976 -0.005341 -0.002731 0.00000 SCALE2 0.000000 0.034298 0.000034 0.00000 SCALE3 0.000000 0.000000 0.018997 0.00000 ATOM 1 N GLU A 2 43.445 22.193 16.450 1.00 73.63 N ANISOU 1 N GLU A 2 10821 6903 10252 2913 678 -3029 N ATOM 2 CA GLU A 2 44.063 20.888 16.709 1.00 54.51 C ANISOU 2 CA GLU A 2 5247 7113 8351 1480 1726 -1999 C ATOM 3 C GLU A 2 43.253 19.758 16.065 1.00 43.35 C ANISOU 3 C GLU A 2 4470 6363 5639 1361 1887 -217 C ATOM 4 O GLU A 2 42.032 19.888 16.012 1.00 56.10 O ANISOU 4 O GLU A 2 4505 7071 9741 1301 1176 1385 O ATOM 5 CB GLU A 2 44.191 20.638 18.194 1.00 47.59 C ANISOU 5 CB GLU A 2 2385 7778 7918 372 2340 -2864 C ATOM 6 CG GLU A 2 44.656 19.300 18.619 1.00 45.96 C ANISOU 6 CG GLU A 2 2506 7992 6964 -232 650 -2519 C ATOM 7 CD GLU A 2 43.705 18.165 18.854 1.00 48.36 C ANISOU 7 CD GLU A 2 1406 7640 9329 295 131 -2609 C ATOM 8 OE1 GLU A 2 43.991 17.337 19.725 1.00 57.68 O ANISOU 8 OE1 GLU A 2 2541 6219 13156 58 -1026 -1530 O ATOM 9 OE2 GLU A 2 42.673 18.032 18.165 1.00 67.34 O ANISOU 9 OE2 GLU A 2 3276 13352 8958 -2242 -843 -1859 O ATOM 10 N GLN A 3 44.017 18.747 15.676 1.00 43.35 N ANISOU 10 N GLN A 3 6161 5708 4604 2258 621 350 N ATOM 11 CA GLN A 3 43.537 17.695 14.807 1.00 43.98 C ANISOU 11 CA GLN A 3 4857 8152 3702 3008 429 -946 C ATOM 12 C GLN A 3 44.577 16.589 14.589 1.00 32.96 C ANISOU 12 C GLN A 3 3143 7390 1991 1992 -1068 -1051 C ATOM 13 O GLN A 3 44.279 15.499 15.107 1.00 32.39 O ANISOU 13 O GLN A 3 2268 7297 2741 1297 -686 -1546 O ATOM 14 CB GLN A 3 43.084 18.249 13.460 1.00 55.09 C ANISOU 14 CB GLN A 3 6475 9073 5384 4718 -881 -183 C ATOM 15 CG GLN A 3 42.109 17.382 12.679 1.00 54.76 C ANISOU 15 CG GLN A 3 5513 10285 5010 4907 -1304 161 C ATOM 16 CD GLN A 3 40.860 17.060 13.478 1.00 56.67 C ANISOU 16 CD GLN A 3 8340 8986 4205 3073 -552 1570 C ATOM 17 OE1 GLN A 3 40.994 16.649 14.628 1.00 69.10 O ANISOU 17 OE1 GLN A 3 14801 7863 3590 7630 584 440 O ATOM 18 NE2 GLN A 3 39.641 17.205 12.979 1.00 57.86 N ANISOU 18 NE2 GLN A 3 6432 9081 6471 3758 1612 2237 N ATOM 19 N LEU A 4 45.660 16.805 13.868 1.00 30.29 N ANISOU 19 N LEU A 4 3783 6249 1475 2510 -776 -357 N ATOM 20 CA LEU A 4 46.704 15.831 13.550 1.00 29.51 C ANISOU 20 CA LEU A 4 3353 6103 1759 2153 -1296 -1419 C ATOM 21 C LEU A 4 48.129 16.353 13.615 1.00 28.22 C ANISOU 21 C LEU A 4 3559 5792 1371 1859 -1123 -968 C ATOM 22 O LEU A 4 48.508 17.449 13.168 1.00 32.63 O ANISOU 22 O LEU A 4 4314 5139 2943 2114 -1446 -1021 O ATOM 23 CB LEU A 4 46.537 15.239 12.129 1.00 32.41 C ANISOU 23 CB LEU A 4 3079 7462 1772 1995 -1335 -1555 C ATOM 24 CG LEU A 4 45.227 14.533 11.821 1.00 34.37 C ANISOU 24 CG LEU A 4 3344 7442 2273 1731 -1308 -1842 C ATOM 25 CD1 LEU A 4 45.072 14.269 10.326 1.00 36.23 C ANISOU 25 CD1 LEU A 4 3852 7473 2440 1899 -1753 -1959 C ATOM 26 CD2 LEU A 4 45.137 13.224 12.585 1.00 35.72 C ANISOU 26 CD2 LEU A 4 3306 7584 2683 1818 -1207 -1601 C ATOM 27 N THR A 5 49.020 15.460 14.115 1.00 24.13 N ANISOU 27 N THR A 5 2946 4924 1296 1323 -918 -1167 N ATOM 28 CA THR A 5 50.447 15.810 14.079 1.00 23.38 C ANISOU 28 CA THR A 5 3172 4470 1241 1093 -939 -721 C ATOM 29 C THR A 5 51.039 15.570 12.684 1.00 22.54 C ANISOU 29 C THR A 5 3035 4509 1022 385 -1020 -657 C ATOM 30 O THR A 5 50.461 14.847 11.858 1.00 19.96 O ANISOU 30 O THR A 5 2985 3520 1081 321 -634 -520 O ATOM 31 CB THR A 5 51.236 14.959 15.073 1.00 19.48 C ANISOU 31 CB THR A 5 2373 3971 1058 623 -462 -572 C ATOM 32 OG1 THR A 5 51.155 13.611 14.632 1.00 18.67 O ANISOU 32 OG1 THR A 5 1970 4091 1032 318 -398 -575 O ATOM 33 CG2 THR A 5 50.648 15.068 16.495 1.00 22.08 C ANISOU 33 CG2 THR A 5 2805 4618 969 -141 -445 -769 C ATOM 34 N GLU A 6 52.224 16.134 12.437 1.00 24.24 N ANISOU 34 N GLU A 6 3620 4190 1401 -117 -852 -921 N ATOM 35 CA GLU A 6 52.947 15.908 11.180 1.00 23.41 C ANISOU 35 CA GLU A 6 3530 4065 1300 -244 -729 -405 C ATOM 36 C GLU A 6 53.233 14.406 11.037 1.00 21.17 C ANISOU 36 C GLU A 6 2756 4230 1057 62 -372 -271 C ATOM 37 O GLU A 6 53.136 13.822 9.913 1.00 20.41 O ANISOU 37 O GLU A 6 2690 3943 1121 -555 -481 -220 O ATOM 38 CB GLU A 6 54.201 16.766 11.171 1.00 29.54 C ANISOU 38 CB GLU A 6 3963 4952 2309 -875 -662 -992 C ATOM 39 CG GLU A 6 54.891 16.943 9.799 1.00 34.48 C ANISOU 39 CG GLU A 6 4984 4430 3686 -355 511 739 C ATOM 40 CD GLU A 6 55.262 18.434 9.823 1.00 41.97 C ANISOU 40 CD GLU A 6 7150 3939 4858 424 836 195 C ATOM 41 OE1 GLU A 6 54.687 18.992 10.803 1.00 58.16 O ANISOU 41 OE1 GLU A 6 11624 6703 3771 3540 -904 -1012 O ATOM 42 OE2 GLU A 6 56.009 18.919 9.000 1.00 59.80 O ANISOU 42 OE2 GLU A 6 6138 5293 11288 -2129 2556 305 O ATOM 43 N GLU A 7 53.533 13.702 12.116 1.00 20.13 N ANISOU 43 N GLU A 7 2165 4220 1262 -334 -373 -135 N ATOM 44 CA GLU A 7 53.762 12.263 12.038 1.00 18.74 C ANISOU 44 CA GLU A 7 1656 4340 1124 108 -470 -177 C ATOM 45 C GLU A 7 52.498 11.484 11.693 1.00 16.59 C ANISOU 45 C GLU A 7 1625 3792 888 310 -347 -274 C ATOM 46 O GLU A 7 52.569 10.583 10.885 1.00 17.01 O ANISOU 46 O GLU A 7 1644 3692 1128 494 -374 -322 O ATOM 47 CB GLU A 7 54.372 11.761 13.341 1.00 20.40 C ANISOU 47 CB GLU A 7 1515 5030 1205 -318 -461 297 C ATOM 48 CG GLU A 7 54.593 10.273 13.376 1.00 25.03 C ANISOU 48 CG GLU A 7 3005 5273 1233 604 -981 253 C ATOM 49 CD GLU A 7 55.520 9.719 12.310 1.00 28.18 C ANISOU 49 CD GLU A 7 3212 5821 1675 1431 -829 620 C ATOM 50 OE1 GLU A 7 56.482 10.353 11.807 1.00 41.67 O ANISOU 50 OE1 GLU A 7 2978 7764 5090 1280 591 426 O ATOM 51 OE2 GLU A 7 55.305 8.552 11.930 1.00 33.78 O ANISOU 51 OE2 GLU A 7 3733 6252 2849 1979 -1138 -518 O ATOM 52 N GLN A 8 51.345 11.827 12.274 1.00 16.10 N ANISOU 52 N GLN A 8 1606 3693 820 377 -360 -202 N ATOM 53 CA GLN A 8 50.125 11.194 11.846 1.00 15.79 C ANISOU 53 CA GLN A 8 1603 3596 802 340 -439 -149 C ATOM 54 C GLN A 8 49.860 11.431 10.346 1.00 14.53 C ANISOU 54 C GLN A 8 1676 3012 834 335 -299 -187 C ATOM 55 O GLN A 8 49.477 10.500 9.631 1.00 14.74 O ANISOU 55 O GLN A 8 1746 2968 887 282 -398 -150 O ATOM 56 CB GLN A 8 48.901 11.729 12.636 1.00 17.49 C ANISOU 56 CB GLN A 8 1570 4211 865 362 -308 -146 C ATOM 57 CG GLN A 8 48.898 11.267 14.104 1.00 19.61 C ANISOU 57 CG GLN A 8 1712 4811 929 -61 -237 -66 C ATOM 58 CD GLN A 8 47.721 11.984 14.800 1.00 22.58 C ANISOU 58 CD GLN A 8 1907 5782 890 194 -286 -480 C ATOM 59 OE1 GLN A 8 47.751 13.197 14.980 1.00 23.84 O ANISOU 59 OE1 GLN A 8 1583 5869 1605 416 -332 -822 O ATOM 60 NE2 GLN A 8 46.715 11.193 15.121 1.00 25.44 N ANISOU 60 NE2 GLN A 8 1702 6546 1416 -258 -188 -1222 N ATOM 61 N AILE A 9 50.042 12.619 9.863 0.60 15.47 N ANISOU 61 N AILE A 9 1965 2991 922 202 -781 -308 N ATOM 62 N BILE A 9 50.064 12.669 9.955 0.40 15.79 N ANISOU 62 N BILE A 9 2130 2878 993 465 -167 -275 N ATOM 63 CA AILE A 9 49.760 12.880 8.443 0.60 16.16 C ANISOU 63 CA AILE A 9 2382 3000 756 385 -545 -300 C ATOM 64 CA BILE A 9 49.894 13.068 8.557 0.40 14.97 C ANISOU 64 CA BILE A 9 2288 2477 923 -33 -270 -374 C ATOM 65 C AILE A 9 50.740 12.096 7.568 0.60 16.68 C ANISOU 65 C AILE A 9 2239 3039 1059 311 -573 -379 C ATOM 66 C BILE A 9 50.739 12.182 7.629 0.40 15.01 C ANISOU 66 C BILE A 9 2285 2689 729 302 -548 -222 C ATOM 67 O AILE A 9 50.344 11.527 6.549 0.60 13.30 O ANISOU 67 O AILE A 9 2127 2080 845 387 -510 -91 O ATOM 68 O BILE A 9 50.215 11.661 6.634 0.40 13.83 O ANISOU 68 O BILE A 9 1927 2592 737 -175 -109 -359 O ATOM 69 CB AILE A 9 49.712 14.388 8.233 0.60 17.94 C ANISOU 69 CB AILE A 9 2984 3034 796 414 -406 -347 C ATOM 70 CB BILE A 9 50.201 14.546 8.306 0.40 15.90 C ANISOU 70 CB BILE A 9 2289 2546 1204 -86 -466 -365 C ATOM 71 CG1AILE A 9 48.529 15.065 8.881 0.60 19.71 C ANISOU 71 CG1AILE A 9 2456 3151 1883 413 -672 -810 C ATOM 72 CG1BILE A 9 49.111 15.466 8.868 0.40 14.83 C ANISOU 72 CG1BILE A 9 2099 2377 1158 -108 -545 -224 C ATOM 73 CG2AILE A 9 49.644 14.632 6.712 0.60 18.98 C ANISOU 73 CG2AILE A 9 2856 3403 954 399 -1131 -62 C ATOM 74 CG2BILE A 9 50.339 14.857 6.814 0.40 13.92 C ANISOU 74 CG2BILE A 9 1554 2455 1279 -617 -478 -279 C ATOM 75 CD1AILE A 9 48.524 16.563 9.024 0.60 23.19 C ANISOU 75 CD1AILE A 9 3229 3191 2390 507 -920 -988 C ATOM 76 CD1BILE A 9 49.568 16.907 8.941 0.40 21.29 C ANISOU 76 CD1BILE A 9 3756 2333 1999 -249 -881 -495 C ATOM 77 N ALA A 10 52.006 12.040 7.976 1.00 16.22 N ANISOU 77 N ALA A 10 2140 2976 1047 96 -428 -316 N ATOM 78 CA ALA A 10 52.970 11.271 7.207 1.00 15.86 C ANISOU 78 CA ALA A 10 2032 3012 983 -114 -280 -258 C ATOM 79 C ALA A 10 52.525 9.824 7.134 1.00 14.08 C ANISOU 79 C ALA A 10 1514 2837 999 143 -389 -98 C ATOM 80 O ALA A 10 52.586 9.200 6.066 1.00 14.53 O ANISOU 80 O ALA A 10 1636 2715 1170 140 -266 -110 O ATOM 81 CB ALA A 10 54.346 11.404 7.820 1.00 18.40 C ANISOU 81 CB ALA A 10 1848 3480 1663 -359 -211 -704 C ATOM 82 N AGLU A 11 52.061 9.296 8.275 0.44 15.90 N ANISOU 82 N AGLU A 11 1831 3026 1186 246 -330 151 N ATOM 83 N BGLU A 11 52.057 9.197 8.209 0.56 15.09 N ANISOU 83 N BGLU A 11 1665 2902 1165 433 -482 269 N ATOM 84 CA AGLU A 11 51.546 7.936 8.363 0.44 14.66 C ANISOU 84 CA AGLU A 11 1882 2833 856 460 -290 113 C ATOM 85 CA BGLU A 11 51.682 7.783 8.120 0.56 15.80 C ANISOU 85 CA BGLU A 11 2067 2757 1179 592 -547 425 C ATOM 86 C AGLU A 11 50.383 7.727 7.397 0.44 13.66 C ANISOU 86 C AGLU A 11 1864 2650 678 294 -196 291 C ATOM 87 C BGLU A 11 50.422 7.562 7.298 0.56 14.26 C ANISOU 87 C BGLU A 11 1683 2643 1091 413 -107 64 C ATOM 88 O AGLU A 11 50.391 6.775 6.606 0.44 12.45 O ANISOU 88 O AGLU A 11 1812 1781 1137 -214 -195 611 O ATOM 89 O BGLU A 11 50.190 6.519 6.668 0.56 17.23 O ANISOU 89 O BGLU A 11 2665 2656 1227 718 -516 -85 O ATOM 90 CB AGLU A 11 51.112 7.561 9.802 0.44 17.94 C ANISOU 90 CB AGLU A 11 2935 3147 734 350 -485 358 C ATOM 91 CB BGLU A 11 51.550 7.251 9.567 0.56 16.15 C ANISOU 91 CB BGLU A 11 1706 3260 1169 -32 -211 333 C ATOM 92 CG AGLU A 11 52.323 7.209 10.666 0.44 21.16 C ANISOU 92 CG AGLU A 11 3062 3861 1116 374 -698 432 C ATOM 93 CG BGLU A 11 52.838 7.443 10.375 0.56 20.25 C ANISOU 93 CG BGLU A 11 2411 3868 1415 -199 -868 717 C ATOM 94 CD AGLU A 11 52.011 7.191 12.138 0.44 25.14 C ANISOU 94 CD AGLU A 11 4149 4432 971 744 -895 485 C ATOM 95 CD BGLU A 11 52.867 6.691 11.676 0.56 22.28 C ANISOU 95 CD BGLU A 11 3111 3902 1452 180 -621 808 C ATOM 96 OE1AGLU A 11 50.841 7.137 12.571 0.44 31.42 O ANISOU 96 OE1AGLU A 11 4924 5490 1523 835 277 930 O ATOM 97 OE1BGLU A 11 51.880 5.993 12.030 0.56 32.07 O ANISOU 97 OE1BGLU A 11 2816 6477 2893 154 -342 2594 O ATOM 98 OE2AGLU A 11 52.985 7.223 12.925 0.44 28.65 O ANISOU 98 OE2AGLU A 11 5697 3481 1709 1159 -2106 -124 O ATOM 99 OE2BGLU A 11 53.923 6.803 12.349 0.56 26.18 O ANISOU 99 OE2BGLU A 11 3245 4686 2018 462 -993 1298 O ATOM 100 N APHE A 12 49.411 8.638 7.472 0.74 12.88 N ANISOU 100 N APHE A 12 1674 2288 930 18 -214 370 N ATOM 101 N BPHE A 12 49.598 8.607 7.312 0.26 13.92 N ANISOU 101 N BPHE A 12 1671 2721 895 440 -304 -236 N ATOM 102 CA APHE A 12 48.304 8.548 6.541 0.74 12.86 C ANISOU 102 CA APHE A 12 1631 2357 897 -88 -231 288 C ATOM 103 CA BPHE A 12 48.330 8.560 6.599 0.26 13.28 C ANISOU 103 CA BPHE A 12 1701 2406 939 104 -350 315 C ATOM 104 C APHE A 12 48.737 8.638 5.082 0.74 10.52 C ANISOU 104 C APHE A 12 1469 1587 943 148 -223 93 C ATOM 105 C BPHE A 12 48.559 8.720 5.105 0.26 12.24 C ANISOU 105 C BPHE A 12 1437 2278 937 230 -249 171 C ATOM 106 O APHE A 12 48.228 7.899 4.227 0.74 10.86 O ANISOU 106 O APHE A 12 1282 1715 1128 259 -266 -12 O ATOM 107 O BPHE A 12 47.882 8.163 4.245 0.26 8.55 O ANISOU 107 O BPHE A 12 728 1626 893 533 -113 372 O ATOM 108 CB APHE A 12 47.233 9.654 6.827 0.74 13.43 C ANISOU 108 CB APHE A 12 1516 2905 682 74 -261 -133 C ATOM 109 CB BPHE A 12 47.404 9.653 7.146 0.26 14.93 C ANISOU 109 CB BPHE A 12 1644 3229 801 470 -210 245 C ATOM 110 CG APHE A 12 46.406 9.387 8.081 0.74 15.90 C ANISOU 110 CG APHE A 12 1522 3568 950 -439 -177 -191 C ATOM 111 CG BPHE A 12 46.779 9.369 8.508 0.26 18.63 C ANISOU 111 CG BPHE A 12 1868 4193 1019 -816 47 -219 C ATOM 112 CD1APHE A 12 45.729 8.177 8.186 0.74 22.70 C ANISOU 112 CD1APHE A 12 2592 4631 1403 -1692 511 -951 C ATOM 113 CD1BPHE A 12 46.363 8.099 8.866 0.26 22.51 C ANISOU 113 CD1BPHE A 12 2286 4506 1761 -1195 860 -239 C ATOM 114 CD2APHE A 12 46.355 10.237 9.122 0.74 15.13 C ANISOU 114 CD2APHE A 12 1375 3374 998 -167 -71 -164 C ATOM 115 CD2BPHE A 12 46.611 10.372 9.442 0.26 18.09 C ANISOU 115 CD2BPHE A 12 2022 4183 668 171 -363 53 C ATOM 116 CE1APHE A 12 45.018 7.857 9.320 0.74 24.63 C ANISOU 116 CE1APHE A 12 3016 4877 1464 -1686 412 -313 C ATOM 117 CE1BPHE A 12 45.792 7.812 10.087 0.26 20.64 C ANISOU 117 CE1BPHE A 12 1481 4958 1404 -1364 272 -211 C ATOM 118 CE2APHE A 12 45.581 9.970 10.240 0.74 18.86 C ANISOU 118 CE2APHE A 12 1439 4836 893 -801 -213 -347 C ATOM 119 CE2BPHE A 12 46.019 10.110 10.665 0.26 19.05 C ANISOU 119 CE2BPHE A 12 2004 4757 478 -375 -640 -44 C ATOM 120 CZ APHE A 12 44.940 8.767 10.347 0.74 21.27 C ANISOU 120 CZ APHE A 12 1691 5343 1047 -1284 249 -355 C ATOM 121 CZ BPHE A 12 45.596 8.836 10.984 0.26 21.51 C ANISOU 121 CZ BPHE A 12 2052 5044 1079 -690 -67 -54 C ATOM 122 N ALYS A 13 49.695 9.522 4.764 0.60 11.31 N ANISOU 122 N ALYS A 13 1421 1923 954 41 -184 233 N ATOM 123 N BLYS A 13 49.588 9.511 4.789 0.40 11.20 N ANISOU 123 N BLYS A 13 1573 2039 644 144 -252 -222 N ATOM 124 CA ALYS A 13 50.180 9.678 3.402 0.60 10.51 C ANISOU 124 CA ALYS A 13 1492 1590 911 -22 -297 75 C ATOM 125 CA BLYS A 13 50.030 9.641 3.407 0.40 10.54 C ANISOU 125 CA BLYS A 13 1569 1678 760 126 -194 -203 C ATOM 126 C ALYS A 13 50.851 8.423 2.882 0.60 9.38 C ANISOU 126 C ALYS A 13 1187 1366 1011 -270 -166 211 C ATOM 127 C BLYS A 13 50.691 8.339 2.963 0.40 9.21 C ANISOU 127 C BLYS A 13 1178 1618 705 -5 39 90 C ATOM 128 O ALYS A 13 50.784 8.019 1.699 0.60 8.81 O ANISOU 128 O ALYS A 13 977 1342 1027 -368 -7 216 O ATOM 129 O BLYS A 13 50.352 7.902 1.842 0.40 8.43 O ANISOU 129 O BLYS A 13 1023 1402 779 -64 202 -20 O ATOM 130 CB ALYS A 13 51.173 10.843 3.303 0.60 12.72 C ANISOU 130 CB ALYS A 13 2131 1434 1270 -202 64 89 C ATOM 131 CB BLYS A 13 50.949 10.841 3.242 0.40 10.09 C ANISOU 131 CB BLYS A 13 1382 1764 687 17 -498 -316 C ATOM 132 CG ALYS A 13 50.554 12.228 3.335 0.60 12.59 C ANISOU 132 CG ALYS A 13 2189 1533 1063 -98 -388 -110 C ATOM 133 CG BLYS A 13 51.423 11.239 1.864 0.40 14.79 C ANISOU 133 CG BLYS A 13 2183 2402 1035 -89 -189 290 C ATOM 134 CD ALYS A 13 51.479 13.381 3.018 0.60 18.14 C ANISOU 134 CD ALYS A 13 3360 1456 2075 -551 -179 -272 C ATOM 135 CD BLYS A 13 51.239 12.694 1.508 0.40 29.52 C ANISOU 135 CD BLYS A 13 4350 3420 3444 1755 1073 1838 C ATOM 136 CE ALYS A 13 50.713 14.710 2.957 0.60 22.58 C ANISOU 136 CE ALYS A 13 5076 1494 2011 -8 385 -136 C ATOM 137 CE BLYS A 13 50.819 13.045 0.081 0.40 37.43 C ANISOU 137 CE BLYS A 13 6485 4456 3280 3071 1589 2220 C ATOM 138 NZ ALYS A 13 51.606 15.877 2.828 0.60 29.13 N ANISOU 138 NZ ALYS A 13 5726 1526 3816 -110 1640 147 N ATOM 139 NZ BLYS A 13 51.381 14.371 -0.347 0.40 30.33 N ANISOU 139 NZ BLYS A 13 5235 4254 2036 3109 1281 1490 N ATOM 140 N GLU A 14 51.571 7.722 3.759 1.00 10.98 N ANISOU 140 N GLU A 14 1347 1675 1150 -18 -197 236 N ATOM 141 CA GLU A 14 52.197 6.459 3.379 1.00 11.86 C ANISOU 141 CA GLU A 14 1455 1747 1304 96 -123 168 C ATOM 142 C GLU A 14 51.131 5.406 3.064 1.00 11.82 C ANISOU 142 C GLU A 14 1486 1587 1420 119 -166 385 C ATOM 143 O GLU A 14 51.230 4.617 2.102 1.00 12.70 O ANISOU 143 O GLU A 14 1497 1554 1776 263 -221 95 O ATOM 144 CB GLU A 14 53.140 5.974 4.522 1.00 15.01 C ANISOU 144 CB GLU A 14 1469 2064 2168 163 -446 433 C ATOM 145 CG GLU A 14 54.369 6.835 4.703 1.00 18.80 C ANISOU 145 CG GLU A 14 1574 2933 2637 -120 -456 273 C ATOM 146 CD GLU A 14 55.151 6.551 5.982 1.00 27.48 C ANISOU 146 CD GLU A 14 1914 5971 2555 28 -802 -358 C ATOM 147 OE1 GLU A 14 54.567 6.274 7.043 1.00 27.17 O ANISOU 147 OE1 GLU A 14 2854 4832 2638 423 -835 271 O ATOM 148 OE2 GLU A 14 56.400 6.660 5.994 1.00 34.88 O ANISOU 148 OE2 GLU A 14 1873 6901 4478 622 -1047 156 O ATOM 149 N ALA A 15 50.061 5.384 3.877 1.00 11.67 N ANISOU 149 N ALA A 15 1490 1646 1297 8 -226 494 N ATOM 150 CA ALA A 15 48.960 4.448 3.626 1.00 11.89 C ANISOU 150 CA ALA A 15 1565 1354 1598 76 -200 661 C ATOM 151 C ALA A 15 48.280 4.775 2.282 1.00 10.70 C ANISOU 151 C ALA A 15 1467 1100 1499 -50 -192 496 C ATOM 152 O ALA A 15 47.969 3.888 1.488 1.00 13.00 O ANISOU 152 O ALA A 15 1874 1094 1973 -183 -442 509 O ATOM 153 CB ALA A 15 47.971 4.470 4.762 1.00 14.35 C ANISOU 153 CB ALA A 15 1697 2067 1687 2 -9 935 C ATOM 154 N PHE A 16 48.001 6.075 2.071 1.00 9.34 N ANISOU 154 N PHE A 16 1288 1201 1057 61 -145 364 N ATOM 155 CA PHE A 16 47.395 6.480 0.792 1.00 8.45 C ANISOU 155 CA PHE A 16 1162 1007 1040 -80 -188 204 C ATOM 156 C PHE A 16 48.233 6.057 -0.379 1.00 8.21 C ANISOU 156 C PHE A 16 1226 835 1058 -35 -109 135 C ATOM 157 O PHE A 16 47.686 5.591 -1.412 1.00 8.95 O ANISOU 157 O PHE A 16 1329 813 1259 103 -228 97 O ATOM 158 CB PHE A 16 47.218 8.009 0.814 1.00 8.36 C ANISOU 158 CB PHE A 16 1231 994 950 -15 -154 90 C ATOM 159 CG PHE A 16 46.484 8.571 -0.372 1.00 7.37 C ANISOU 159 CG PHE A 16 1157 766 877 -138 -109 86 C ATOM 160 CD1 PHE A 16 45.107 8.614 -0.414 1.00 8.53 C ANISOU 160 CD1 PHE A 16 1117 941 1181 -145 -109 236 C ATOM 161 CD2 PHE A 16 47.190 9.084 -1.436 1.00 8.44 C ANISOU 161 CD2 PHE A 16 1212 929 1067 -64 -40 165 C ATOM 162 CE1 PHE A 16 44.442 9.156 -1.508 1.00 8.92 C ANISOU 162 CE1 PHE A 16 1217 812 1361 -159 -316 149 C ATOM 163 CE2 PHE A 16 46.553 9.620 -2.534 1.00 9.01 C ANISOU 163 CE2 PHE A 16 1548 841 1036 -92 -50 235 C ATOM 164 CZ PHE A 16 45.163 9.663 -2.573 1.00 9.14 C ANISOU 164 CZ PHE A 16 1594 600 1279 -121 -381 221 C ATOM 165 N ALA A 17 49.537 6.223 -0.276 1.00 8.73 N ANISOU 165 N ALA A 17 1193 969 1155 -62 -74 109 N ATOM 166 CA ALA A 17 50.459 5.882 -1.385 1.00 9.18 C ANISOU 166 CA ALA A 17 1273 1083 1133 86 -69 79 C ATOM 167 C ALA A 17 50.368 4.440 -1.777 1.00 10.51 C ANISOU 167 C ALA A 17 1424 1056 1515 224 -125 -7 C ATOM 168 O ALA A 17 50.576 4.108 -2.971 1.00 12.06 O ANISOU 168 O ALA A 17 1739 1241 1601 201 -30 -157 O ATOM 169 CB ALA A 17 51.864 6.313 -0.985 1.00 10.81 C ANISOU 169 CB ALA A 17 1244 1553 1312 -171 76 120 C ATOM 170 N LEU A 18 50.110 3.524 -0.834 1.00 10.59 N ANISOU 170 N LEU A 18 1372 1091 1559 261 -321 88 N ATOM 171 CA LEU A 18 49.972 2.115 -1.220 1.00 11.42 C ANISOU 171 CA LEU A 18 1441 981 1915 347 -265 10 C ATOM 172 C LEU A 18 48.882 1.885 -2.202 1.00 10.28 C ANISOU 172 C LEU A 18 1376 761 1769 215 -112 119 C ATOM 173 O LEU A 18 48.956 1.002 -3.054 1.00 12.65 O ANISOU 173 O LEU A 18 1439 973 2395 306 -314 -268 O ATOM 174 CB LEU A 18 49.698 1.259 0.036 1.00 19.09 C ANISOU 174 CB LEU A 18 3617 1256 2380 405 -900 725 C ATOM 175 CG LEU A 18 49.301 -0.206 -0.323 1.00 21.34 C ANISOU 175 CG LEU A 18 3608 1227 3273 265 -544 576 C ATOM 176 CD1 LEU A 18 50.511 -0.957 -0.886 1.00 30.08 C ANISOU 176 CD1 LEU A 18 4137 1663 5631 528 41 30 C ATOM 177 CD2 LEU A 18 48.688 -0.926 0.841 1.00 29.88 C ANISOU 177 CD2 LEU A 18 5620 1848 3883 -109 49 1039 C ATOM 178 N PHE A 19 47.807 2.685 -2.112 1.00 9.03 N ANISOU 178 N PHE A 19 1285 745 1402 118 -92 225 N ATOM 179 CA PHE A 19 46.708 2.595 -3.048 1.00 8.68 C ANISOU 179 CA PHE A 19 1162 598 1537 -56 -80 243 C ATOM 180 C PHE A 19 46.953 3.396 -4.326 1.00 8.07 C ANISOU 180 C PHE A 19 1072 547 1447 -69 -175 106 C ATOM 181 O PHE A 19 46.590 2.958 -5.419 1.00 8.74 O ANISOU 181 O PHE A 19 1114 653 1555 -208 -225 62 O ATOM 182 CB PHE A 19 45.399 3.110 -2.401 1.00 9.31 C ANISOU 182 CB PHE A 19 1210 694 1635 -52 -24 194 C ATOM 183 CG PHE A 19 44.885 2.254 -1.272 1.00 9.51 C ANISOU 183 CG PHE A 19 1174 773 1667 -34 -58 326 C ATOM 184 CD1 PHE A 19 43.982 1.216 -1.516 1.00 11.46 C ANISOU 184 CD1 PHE A 19 1342 1170 1843 -324 -51 370 C ATOM 185 CD2 PHE A 19 45.312 2.478 0.019 1.00 11.34 C ANISOU 185 CD2 PHE A 19 1629 1086 1591 -301 129 153 C ATOM 186 CE1 PHE A 19 43.539 0.401 -0.518 1.00 12.98 C ANISOU 186 CE1 PHE A 19 1603 1352 1976 -434 23 553 C ATOM 187 CE2 PHE A 19 44.855 1.623 1.036 1.00 14.14 C ANISOU 187 CE2 PHE A 19 2076 1616 1682 -455 -198 542 C ATOM 188 CZ PHE A 19 43.939 0.627 0.753 1.00 12.90 C ANISOU 188 CZ PHE A 19 1771 1275 1854 -296 166 561 C ATOM 189 N ASP A 20 47.543 4.587 -4.198 1.00 8.52 N ANISOU 189 N ASP A 20 1329 631 1278 -281 -234 216 N ATOM 190 CA ASP A 20 47.768 5.491 -5.306 1.00 7.43 C ANISOU 190 CA ASP A 20 1118 538 1166 -112 -222 87 C ATOM 191 C ASP A 20 49.013 5.082 -6.062 1.00 8.75 C ANISOU 191 C ASP A 20 1186 618 1521 -47 -131 228 C ATOM 192 O ASP A 20 50.085 5.715 -6.020 1.00 10.32 O ANISOU 192 O ASP A 20 1035 920 1963 -191 -249 310 O ATOM 193 CB ASP A 20 47.839 6.934 -4.815 1.00 8.19 C ANISOU 193 CB ASP A 20 1316 574 1221 -222 -297 158 C ATOM 194 CG ASP A 20 48.078 7.909 -5.950 1.00 7.50 C ANISOU 194 CG ASP A 20 1044 538 1269 -136 -315 150 C ATOM 195 OD1 ASP A 20 47.863 7.544 -7.118 1.00 7.79 O ANISOU 195 OD1 ASP A 20 1037 703 1219 -187 -205 170 O ATOM 196 OD2 ASP A 20 48.484 9.062 -5.656 1.00 8.56 O ANISOU 196 OD2 ASP A 20 1247 559 1447 -266 -292 156 O ATOM 197 N LYS A 21 48.898 3.976 -6.798 1.00 9.97 N ANISOU 197 N LYS A 21 1254 666 1867 26 144 27 N ATOM 198 CA LYS A 21 49.964 3.285 -7.532 1.00 12.02 C ANISOU 198 CA LYS A 21 1460 721 2385 149 349 156 C ATOM 199 C LYS A 21 50.726 4.183 -8.470 1.00 10.89 C ANISOU 199 C LYS A 21 1324 904 1909 173 113 32 C ATOM 200 O LYS A 21 51.946 4.020 -8.611 1.00 12.86 O ANISOU 200 O LYS A 21 1314 1409 2164 341 273 360 O ATOM 201 CB LYS A 21 49.421 2.068 -8.298 1.00 15.07 C ANISOU 201 CB LYS A 21 2263 807 2655 24 547 -209 C ATOM 202 CG LYS A 21 48.752 1.002 -7.488 1.00 13.01 C ANISOU 202 CG LYS A 21 1328 1196 2420 -159 -29 -204 C ATOM 203 CD LYS A 21 49.673 0.566 -6.366 1.00 15.84 C ANISOU 203 CD LYS A 21 919 2255 2843 -248 -120 611 C ATOM 204 CE LYS A 21 49.214 -0.839 -5.808 1.00 15.69 C ANISOU 204 CE LYS A 21 1483 1393 3087 -179 -414 -53 C ATOM 205 NZ LYS A 21 49.951 -1.144 -4.547 1.00 12.29 N ANISOU 205 NZ LYS A 21 1341 695 2634 -102 227 79 N ATOM 206 N ASP A 22 50.005 5.067 -9.128 1.00 10.00 N ANISOU 206 N ASP A 22 1098 867 1834 26 121 27 N ATOM 207 CA ASP A 22 50.622 5.935 -10.122 1.00 9.95 C ANISOU 207 CA ASP A 22 1048 1059 1674 -68 130 -7 C ATOM 208 C ASP A 22 50.954 7.307 -9.605 1.00 9.63 C ANISOU 208 C ASP A 22 1056 932 1670 19 -118 108 C ATOM 209 O ASP A 22 51.445 8.143 -10.357 1.00 10.89 O ANISOU 209 O ASP A 22 1373 1191 1576 -294 30 229 O ATOM 210 CB ASP A 22 49.844 6.029 -11.426 1.00 11.01 C ANISOU 210 CB ASP A 22 1241 1202 1742 14 -1 -121 C ATOM 211 CG ASP A 22 48.534 6.778 -11.338 1.00 10.36 C ANISOU 211 CG ASP A 22 1309 985 1641 42 -210 -241 C ATOM 212 OD1 ASP A 22 48.113 7.194 -10.234 1.00 9.48 O ANISOU 212 OD1 ASP A 22 1050 883 1668 -135 -56 -87 O ATOM 213 OD2 ASP A 22 47.940 6.899 -12.427 1.00 13.80 O ANISOU 213 OD2 ASP A 22 1744 1709 1789 513 -345 -355 O ATOM 214 N GLY A 23 50.758 7.567 -8.294 1.00 9.13 N ANISOU 214 N GLY A 23 996 807 1667 -141 -73 200 N ATOM 215 CA GLY A 23 51.165 8.826 -7.701 1.00 9.50 C ANISOU 215 CA GLY A 23 1154 924 1532 -197 -186 155 C ATOM 216 C GLY A 23 50.452 10.034 -8.231 1.00 8.83 C ANISOU 216 C GLY A 23 1053 875 1426 -386 -289 217 C ATOM 217 O GLY A 23 51.048 11.142 -8.196 1.00 12.42 O ANISOU 217 O GLY A 23 1492 945 2284 -480 -759 394 O ATOM 218 N ASP A 24 49.237 9.932 -8.723 1.00 8.29 N ANISOU 218 N ASP A 24 995 722 1434 -230 -185 134 N ATOM 219 CA ASP A 24 48.518 11.082 -9.243 1.00 8.33 C ANISOU 219 CA ASP A 24 1049 825 1292 -261 -201 152 C ATOM 220 C ASP A 24 47.675 11.791 -8.228 1.00 7.68 C ANISOU 220 C ASP A 24 1086 614 1216 -233 -300 166 C ATOM 221 O ASP A 24 46.955 12.739 -8.570 1.00 8.88 O ANISOU 221 O ASP A 24 1318 708 1350 -133 -272 120 O ATOM 222 CB ASP A 24 47.656 10.734 -10.479 1.00 8.32 C ANISOU 222 CB ASP A 24 1191 842 1127 -177 -99 131 C ATOM 223 CG ASP A 24 46.299 10.171 -10.065 1.00 7.96 C ANISOU 223 CG ASP A 24 1212 739 1071 -320 -238 129 C ATOM 224 OD1 ASP A 24 46.270 9.452 -9.049 1.00 7.74 O ANISOU 224 OD1 ASP A 24 1264 599 1078 -223 -182 58 O ATOM 225 OD2 ASP A 24 45.304 10.417 -10.768 1.00 9.50 O ANISOU 225 OD2 ASP A 24 1197 1021 1393 -358 -214 424 O ATOM 226 N GLY A 25 47.744 11.412 -6.951 1.00 7.54 N ANISOU 226 N GLY A 25 987 589 1289 -185 -319 62 N ATOM 227 CA GLY A 25 46.928 12.066 -5.933 1.00 7.50 C ANISOU 227 CA GLY A 25 1106 563 1182 -257 -301 104 C ATOM 228 C GLY A 25 45.518 11.603 -5.832 1.00 6.87 C ANISOU 228 C GLY A 25 1082 485 1043 -140 -251 179 C ATOM 229 O GLY A 25 44.725 12.228 -5.118 1.00 7.44 O ANISOU 229 O GLY A 25 1158 469 1201 -118 -271 63 O ATOM 230 N THR A 26 45.172 10.515 -6.498 1.00 7.15 N ANISOU 230 N THR A 26 1003 455 1259 -171 -181 87 N ATOM 231 CA THR A 26 43.815 9.967 -6.428 1.00 7.23 C ANISOU 231 CA THR A 26 1085 492 1170 -225 -165 148 C ATOM 232 C THR A 26 43.920 8.447 -6.389 1.00 7.12 C ANISOU 232 C THR A 26 972 403 1328 -150 -179 44 C ATOM 233 O THR A 26 44.880 7.857 -6.907 1.00 7.79 O ANISOU 233 O THR A 26 1093 506 1362 -228 -119 37 O ATOM 234 CB THR A 26 42.906 10.362 -7.595 1.00 7.78 C ANISOU 234 CB THR A 26 1038 549 1367 -141 -215 57 C ATOM 235 OG1 THR A 26 43.195 9.637 -8.799 1.00 9.17 O ANISOU 235 OG1 THR A 26 1298 864 1321 -82 -388 -143 O ATOM 236 CG2 THR A 26 42.944 11.850 -7.864 1.00 8.63 C ANISOU 236 CG2 THR A 26 1350 652 1275 -136 -423 134 C ATOM 237 N ILE A 27 42.899 7.839 -5.799 1.00 7.30 N ANISOU 237 N ILE A 27 1001 404 1366 -135 -64 77 N ATOM 238 CA ILE A 27 42.705 6.385 -5.817 1.00 7.78 C ANISOU 238 CA ILE A 27 1015 439 1502 -202 -116 146 C ATOM 239 C ILE A 27 41.475 6.112 -6.709 1.00 8.23 C ANISOU 239 C ILE A 27 1091 442 1594 -241 -195 231 C ATOM 240 O ILE A 27 40.357 6.587 -6.399 1.00 8.36 O ANISOU 240 O ILE A 27 1019 613 1544 -134 -166 214 O ATOM 241 CB ILE A 27 42.504 5.789 -4.439 1.00 8.29 C ANISOU 241 CB ILE A 27 1036 561 1555 -91 -142 194 C ATOM 242 CG1 ILE A 27 43.641 6.122 -3.466 1.00 8.26 C ANISOU 242 CG1 ILE A 27 1220 538 1381 -80 -152 92 C ATOM 243 CG2 ILE A 27 42.276 4.267 -4.544 1.00 9.78 C ANISOU 243 CG2 ILE A 27 1296 574 1845 -324 -408 338 C ATOM 244 CD1 ILE A 27 43.331 5.832 -2.049 1.00 10.08 C ANISOU 244 CD1 ILE A 27 1552 850 1429 16 -1 173 C ATOM 245 N THR A 28 41.688 5.355 -7.772 1.00 8.54 N ANISOU 245 N THR A 28 977 500 1768 -204 -298 85 N ATOM 246 CA THR A 28 40.654 4.920 -8.685 1.00 9.03 C ANISOU 246 CA THR A 28 941 734 1757 -225 -347 136 C ATOM 247 C THR A 28 40.079 3.575 -8.289 1.00 9.38 C ANISOU 247 C THR A 28 974 613 1977 -206 -344 113 C ATOM 248 O THR A 28 40.661 2.835 -7.470 1.00 8.88 O ANISOU 248 O THR A 28 1106 615 1652 -257 -329 93 O ATOM 249 CB THR A 28 41.171 4.831 -10.130 1.00 10.13 C ANISOU 249 CB THR A 28 1330 813 1707 -151 -299 135 C ATOM 250 OG1 THR A 28 42.194 3.834 -10.095 1.00 10.90 O ANISOU 250 OG1 THR A 28 1397 923 1822 -38 -209 121 O ATOM 251 CG2 THR A 28 41.709 6.140 -10.668 1.00 11.16 C ANISOU 251 CG2 THR A 28 1398 977 1866 -177 -191 231 C ATOM 252 N THR A 29 38.943 3.197 -8.898 1.00 10.72 N ANISOU 252 N THR A 29 1343 902 1830 -400 -623 311 N ATOM 253 CA THR A 29 38.451 1.837 -8.728 1.00 11.81 C ANISOU 253 CA THR A 29 1648 958 1881 -681 -720 238 C ATOM 254 C THR A 29 39.528 0.822 -9.148 1.00 11.45 C ANISOU 254 C THR A 29 1800 807 1742 -700 -730 112 C ATOM 255 O THR A 29 39.679 -0.193 -8.483 1.00 13.27 O ANISOU 255 O THR A 29 1761 986 2295 -762 -805 460 O ATOM 256 CB THR A 29 37.166 1.580 -9.528 1.00 12.84 C ANISOU 256 CB THR A 29 1545 1361 1973 -794 -585 310 C ATOM 257 OG1 THR A 29 37.435 1.928 -10.894 1.00 15.81 O ANISOU 257 OG1 THR A 29 1876 2131 1999 -839 -856 706 O ATOM 258 CG2 THR A 29 35.962 2.315 -8.967 1.00 16.17 C ANISOU 258 CG2 THR A 29 1689 1960 2497 -318 -841 154 C ATOM 259 N LYS A 30 40.242 1.124 -10.249 1.00 12.26 N ANISOU 259 N LYS A 30 2011 1031 1614 -526 -681 86 N ATOM 260 CA LYS A 30 41.260 0.174 -10.730 1.00 14.05 C ANISOU 260 CA LYS A 30 2459 1239 1640 -307 -669 -186 C ATOM 261 C LYS A 30 42.340 -0.019 -9.668 1.00 11.59 C ANISOU 261 C LYS A 30 1877 892 1633 -326 -360 -236 C ATOM 262 O LYS A 30 42.767 -1.169 -9.415 1.00 13.55 O ANISOU 262 O LYS A 30 2331 771 2046 -353 -556 -238 O ATOM 263 CB LYS A 30 41.855 0.637 -12.053 1.00 20.00 C ANISOU 263 CB LYS A 30 2974 3010 1616 177 -430 84 C ATOM 264 CG LYS A 30 42.490 -0.532 -12.785 1.00 40.41 C ANISOU 264 CG LYS A 30 5830 5266 4259 2717 2134 403 C ATOM 265 CD LYS A 30 43.951 -0.705 -12.427 1.00 55.99 C ANISOU 265 CD LYS A 30 6299 6762 8212 3700 1173 334 C ATOM 266 CE LYS A 30 44.265 -2.129 -12.010 1.00 59.77 C ANISOU 266 CE LYS A 30 6650 6592 9467 4128 1356 3 C ATOM 267 NZ LYS A 30 44.100 -3.070 -13.168 1.00 68.75 N ANISOU 267 NZ LYS A 30 6620 7709 11793 1119 3740 -1940 N ATOM 268 N GLU A 31 42.822 1.066 -9.058 1.00 10.25 N ANISOU 268 N GLU A 31 1596 658 1642 -217 -330 -99 N ATOM 269 CA GLU A 31 43.863 0.972 -8.061 1.00 9.87 C ANISOU 269 CA GLU A 31 1586 474 1690 -281 -284 -81 C ATOM 270 C GLU A 31 43.429 0.286 -6.801 1.00 9.32 C ANISOU 270 C GLU A 31 1358 473 1710 -193 -317 -85 C ATOM 271 O GLU A 31 44.145 -0.502 -6.208 1.00 10.13 O ANISOU 271 O GLU A 31 1376 525 1949 -172 -304 98 O ATOM 272 CB GLU A 31 44.377 2.411 -7.762 1.00 9.48 C ANISOU 272 CB GLU A 31 1402 516 1685 -254 -278 -8 C ATOM 273 CG GLU A 31 45.245 2.934 -8.865 1.00 9.96 C ANISOU 273 CG GLU A 31 1136 589 2060 -204 -131 -134 C ATOM 274 CD GLU A 31 45.654 4.366 -8.696 1.00 9.16 C ANISOU 274 CD GLU A 31 1171 471 1837 -116 -302 3 C ATOM 275 OE1 GLU A 31 44.840 5.164 -8.141 1.00 8.71 O ANISOU 275 OE1 GLU A 31 1226 475 1607 -188 -72 58 O ATOM 276 OE2 GLU A 31 46.750 4.748 -9.169 1.00 10.82 O ANISOU 276 OE2 GLU A 31 1012 639 2459 -178 -120 -190 O ATOM 277 N LEU A 32 42.208 0.600 -6.351 1.00 9.70 N ANISOU 277 N LEU A 32 1393 387 1903 -154 -320 135 N ATOM 278 CA LEU A 32 41.670 -0.112 -5.196 1.00 9.76 C ANISOU 278 CA LEU A 32 1358 478 1873 -156 -233 82 C ATOM 279 C LEU A 32 41.609 -1.636 -5.512 1.00 9.26 C ANISOU 279 C LEU A 32 1435 439 1643 -41 -105 26 C ATOM 280 O LEU A 32 41.970 -2.483 -4.725 1.00 9.89 O ANISOU 280 O LEU A 32 1465 493 1799 -87 -48 113 O ATOM 281 CB LEU A 32 40.278 0.415 -4.858 1.00 9.73 C ANISOU 281 CB LEU A 32 1522 493 1683 -24 -313 22 C ATOM 282 CG LEU A 32 39.548 -0.343 -3.748 1.00 10.00 C ANISOU 282 CG LEU A 32 1483 720 1595 -92 -131 -141 C ATOM 283 CD1 LEU A 32 40.339 -0.384 -2.470 1.00 12.02 C ANISOU 283 CD1 LEU A 32 1835 1222 1512 -18 -99 -88 C ATOM 284 CD2 LEU A 32 38.167 0.281 -3.587 1.00 12.66 C ANISOU 284 CD2 LEU A 32 1682 1187 1940 250 3 -33 C ATOM 285 N GLY A 33 41.190 -1.946 -6.746 1.00 9.51 N ANISOU 285 N GLY A 33 1291 536 1785 -138 -168 -5 N ATOM 286 CA GLY A 33 41.182 -3.354 -7.159 1.00 9.58 C ANISOU 286 CA GLY A 33 1354 505 1780 -122 -298 -42 C ATOM 287 C GLY A 33 42.573 -3.992 -7.139 1.00 8.73 C ANISOU 287 C GLY A 33 1392 485 1443 -139 -197 9 C ATOM 288 O GLY A 33 42.692 -5.121 -6.661 1.00 9.51 O ANISOU 288 O GLY A 33 1407 470 1737 -123 -105 7 O ATOM 289 N THR A 34 43.589 -3.286 -7.595 1.00 9.22 N ANISOU 289 N THR A 34 1438 437 1629 -101 -84 35 N ATOM 290 CA THR A 34 44.935 -3.839 -7.535 1.00 9.32 C ANISOU 290 CA THR A 34 1410 613 1518 -37 -10 -35 C ATOM 291 C THR A 34 45.311 -4.230 -6.117 1.00 9.04 C ANISOU 291 C THR A 34 1391 519 1526 -157 -118 -66 C ATOM 292 O THR A 34 45.851 -5.320 -5.878 1.00 9.49 O ANISOU 292 O THR A 34 1501 575 1530 -21 -194 -126 O ATOM 293 CB THR A 34 45.921 -2.846 -8.112 1.00 10.72 C ANISOU 293 CB THR A 34 1671 624 1780 23 92 105 C ATOM 294 OG1 THR A 34 45.516 -2.497 -9.484 1.00 12.35 O ANISOU 294 OG1 THR A 34 1730 1030 1934 -84 147 415 O ATOM 295 CG2 THR A 34 47.326 -3.412 -8.094 1.00 11.87 C ANISOU 295 CG2 THR A 34 1536 893 2081 -111 101 64 C ATOM 296 N VAL A 35 45.037 -3.348 -5.163 1.00 9.46 N ANISOU 296 N VAL A 35 1435 594 1564 -189 -137 -127 N ATOM 297 CA VAL A 35 45.359 -3.620 -3.778 1.00 9.59 C ANISOU 297 CA VAL A 35 1474 671 1499 -327 -82 -115 C ATOM 298 C VAL A 35 44.587 -4.801 -3.223 1.00 9.99 C ANISOU 298 C VAL A 35 1546 676 1576 -336 -260 -34 C ATOM 299 O VAL A 35 45.106 -5.718 -2.595 1.00 10.98 O ANISOU 299 O VAL A 35 1812 710 1650 -294 -435 -30 O ATOM 300 CB VAL A 35 45.177 -2.379 -2.892 1.00 10.18 C ANISOU 300 CB VAL A 35 1513 687 1667 -284 -38 -200 C ATOM 301 CG1 VAL A 35 45.423 -2.743 -1.456 1.00 13.35 C ANISOU 301 CG1 VAL A 35 2470 1072 1529 -584 91 -234 C ATOM 302 CG2 VAL A 35 46.150 -1.296 -3.347 1.00 10.52 C ANISOU 302 CG2 VAL A 35 1407 726 1865 -293 -72 -79 C ATOM 303 N AMET A 36 43.265 -4.829 -3.463 0.61 9.55 N ANISOU 303 N AMET A 36 1529 622 1479 -402 -194 -8 N ATOM 304 N BMET A 36 43.279 -4.765 -3.543 0.40 9.62 N ANISOU 304 N BMET A 36 1391 511 1754 -199 -13 -352 N ATOM 305 CA AMET A 36 42.563 -5.997 -2.912 0.61 9.67 C ANISOU 305 CA AMET A 36 1511 689 1473 -182 191 94 C ATOM 306 CA BMET A 36 42.392 -5.820 -3.083 0.40 8.43 C ANISOU 306 CA BMET A 36 1514 502 1189 -208 -419 -22 C ATOM 307 C AMET A 36 43.010 -7.283 -3.537 0.61 8.91 C ANISOU 307 C AMET A 36 1441 619 1326 -153 -338 16 C ATOM 308 C BMET A 36 42.842 -7.187 -3.590 0.40 8.25 C ANISOU 308 C BMET A 36 1276 505 1352 -74 -344 54 C ATOM 309 O AMET A 36 43.154 -8.328 -2.887 0.61 8.86 O ANISOU 309 O AMET A 36 1335 654 1378 -135 -400 90 O ATOM 310 O BMET A 36 42.792 -8.167 -2.830 0.40 9.28 O ANISOU 310 O BMET A 36 1774 481 1271 -262 -306 -3 O ATOM 311 CB AMET A 36 41.068 -5.722 -3.160 0.61 8.82 C ANISOU 311 CB AMET A 36 1549 394 1408 -253 55 138 C ATOM 312 CB BMET A 36 40.950 -5.559 -3.541 0.40 9.24 C ANISOU 312 CB BMET A 36 1304 641 1565 -27 92 306 C ATOM 313 CG AMET A 36 40.593 -4.532 -2.319 0.61 9.04 C ANISOU 313 CG AMET A 36 1407 807 1221 -200 24 -63 C ATOM 314 CG BMET A 36 40.216 -4.404 -2.910 0.40 10.79 C ANISOU 314 CG BMET A 36 1358 1227 1516 -126 348 -135 C ATOM 315 SD AMET A 36 38.887 -4.074 -2.591 0.61 10.33 S ANISOU 315 SD AMET A 36 1564 699 1663 -82 -152 51 S ATOM 316 SD BMET A 36 40.166 -4.292 -1.131 0.40 17.38 S ANISOU 316 SD BMET A 36 3104 2006 1492 869 -7 72 S ATOM 317 CE AMET A 36 38.075 -5.513 -1.865 0.61 15.46 C ANISOU 317 CE AMET A 36 1525 943 3408 -101 561 252 C ATOM 318 CE BMET A 36 39.991 -6.002 -0.672 0.40 37.98 C ANISOU 318 CE BMET A 36 8122 3349 2960 -2581 -1598 1724 C ATOM 319 N ARG A 37 43.263 -7.249 -4.852 1.00 8.85 N ANISOU 319 N ARG A 37 1412 560 1389 -182 -315 40 N ATOM 320 CA ARG A 37 43.728 -8.469 -5.523 1.00 8.72 C ANISOU 320 CA ARG A 37 1352 557 1404 -107 -256 13 C ATOM 321 C ARG A 37 45.013 -8.946 -4.884 1.00 9.08 C ANISOU 321 C ARG A 37 1343 593 1515 -166 -301 117 C ATOM 322 O ARG A 37 45.238 -10.171 -4.765 1.00 10.13 O ANISOU 322 O ARG A 37 1591 643 1616 13 -496 82 O ATOM 323 CB ARG A 37 43.895 -8.238 -7.027 1.00 9.06 C ANISOU 323 CB ARG A 37 1395 657 1391 -96 -199 57 C ATOM 324 CG ARG A 37 42.607 -8.086 -7.778 1.00 9.04 C ANISOU 324 CG ARG A 37 1422 605 1408 -79 -164 38 C ATOM 325 CD ARG A 37 42.750 -8.045 -9.295 1.00 11.49 C ANISOU 325 CD ARG A 37 1843 1063 1459 118 -292 244 C ATOM 326 NE ARG A 37 43.191 -6.785 -9.813 1.00 13.02 N ANISOU 326 NE ARG A 37 1810 1358 1780 -111 -181 461 N ATOM 327 CZ ARG A 37 42.399 -5.726 -10.064 1.00 12.41 C ANISOU 327 CZ ARG A 37 1966 1080 1670 -208 -247 506 C ATOM 328 NH1 ARG A 37 41.136 -5.769 -9.835 1.00 13.99 N ANISOU 328 NH1 ARG A 37 1830 1004 2481 -185 -586 412 N ATOM 329 NH2 ARG A 37 42.920 -4.644 -10.524 1.00 14.76 N ANISOU 329 NH2 ARG A 37 1914 1485 2209 -313 -259 794 N ATOM 330 N SER A 38 45.882 -8.040 -4.481 1.00 9.97 N ANISOU 330 N SER A 38 1335 761 1692 -185 -354 70 N ATOM 331 CA SER A 38 47.143 -8.421 -3.841 1.00 12.32 C ANISOU 331 CA SER A 38 1660 1042 1980 -105 -731 33 C ATOM 332 C SER A 38 46.908 -9.115 -2.537 1.00 14.32 C ANISOU 332 C SER A 38 2050 1410 1981 -129 -876 220 C ATOM 333 O SER A 38 47.789 -9.873 -2.066 1.00 18.89 O ANISOU 333 O SER A 38 2368 1925 2885 96 -1047 691 O ATOM 334 CB SER A 38 48.060 -7.234 -3.628 1.00 13.93 C ANISOU 334 CB SER A 38 1422 1319 2553 -234 -680 -68 C ATOM 335 OG SER A 38 47.684 -6.460 -2.462 1.00 18.65 O ANISOU 335 OG SER A 38 1942 1843 3300 -257 -776 -959 O ATOM 336 N ALEU A 39 45.783 -8.876 -1.911 0.53 13.54 N ANISOU 336 N ALEU A 39 2156 1271 1717 -357 -815 170 N ATOM 337 N BLEU A 39 45.772 -8.924 -1.907 0.47 14.47 N ANISOU 337 N BLEU A 39 2205 1573 1722 -248 -783 222 N ATOM 338 CA ALEU A 39 45.351 -9.363 -0.626 0.53 15.72 C ANISOU 338 CA ALEU A 39 2721 1819 1433 -310 -949 144 C ATOM 339 CA BLEU A 39 45.500 -9.545 -0.623 0.47 16.08 C ANISOU 339 CA BLEU A 39 2850 1576 1684 -405 -792 177 C ATOM 340 C ALEU A 39 44.531 -10.645 -0.765 0.53 14.17 C ANISOU 340 C ALEU A 39 2606 1395 1382 -162 -563 373 C ATOM 341 C BLEU A 39 44.423 -10.610 -0.748 0.47 15.17 C ANISOU 341 C BLEU A 39 2436 1750 1579 -361 -652 196 C ATOM 342 O ALEU A 39 44.232 -11.250 0.251 0.53 19.14 O ANISOU 342 O ALEU A 39 3005 2694 1573 -119 -476 984 O ATOM 343 O BLEU A 39 43.821 -11.011 0.230 0.47 17.74 O ANISOU 343 O BLEU A 39 2545 2639 1556 -458 -366 -65 O ATOM 344 CB ALEU A 39 44.552 -8.289 0.135 0.53 18.16 C ANISOU 344 CB ALEU A 39 3988 1719 1192 -271 -827 -83 C ATOM 345 CB BLEU A 39 45.124 -8.453 0.385 0.47 19.21 C ANISOU 345 CB BLEU A 39 3474 2142 1683 -415 -916 -231 C ATOM 346 CG ALEU A 39 45.299 -7.041 0.601 0.53 19.15 C ANISOU 346 CG ALEU A 39 3191 2473 1614 -809 -26 -487 C ATOM 347 CG BLEU A 39 46.082 -7.269 0.493 0.47 20.27 C ANISOU 347 CG BLEU A 39 3413 2490 1798 -597 -743 -691 C ATOM 348 CD1ALEU A 39 44.377 -5.968 1.169 0.53 20.90 C ANISOU 348 CD1ALEU A 39 4673 1809 1458 -481 -16 -270 C ATOM 349 CD1BLEU A 39 45.413 -6.124 1.241 0.47 20.56 C ANISOU 349 CD1BLEU A 39 3664 1992 2155 -574 -227 -145 C ATOM 350 CD2ALEU A 39 46.317 -7.478 1.651 0.53 26.65 C ANISOU 350 CD2ALEU A 39 4239 3530 2357 -157 -1145 -1407 C ATOM 351 CD2BLEU A 39 47.382 -7.707 1.158 0.47 22.49 C ANISOU 351 CD2BLEU A 39 3575 2210 2760 -512 -1033 -605 C ATOM 352 N GLY A 40 44.204 -11.115 -1.967 1.00 12.04 N ANISOU 352 N GLY A 40 2007 1065 1502 -138 -459 344 N ATOM 353 CA GLY A 40 43.453 -12.323 -2.149 1.00 12.21 C ANISOU 353 CA GLY A 40 2014 922 1705 95 -357 285 C ATOM 354 C GLY A 40 41.968 -12.180 -2.412 1.00 10.59 C ANISOU 354 C GLY A 40 1914 668 1440 -171 -176 268 C ATOM 355 O GLY A 40 41.243 -13.157 -2.329 1.00 12.30 O ANISOU 355 O GLY A 40 2145 764 1765 -242 141 239 O ATOM 356 N GLN A 41 41.539 -10.952 -2.757 1.00 10.43 N ANISOU 356 N GLN A 41 1753 817 1394 -254 -560 264 N ATOM 357 CA GLN A 41 40.122 -10.769 -3.117 1.00 10.24 C ANISOU 357 CA GLN A 41 1600 988 1304 -353 -431 237 C ATOM 358 C GLN A 41 40.076 -10.156 -4.496 1.00 8.24 C ANISOU 358 C GLN A 41 1336 693 1102 -191 -191 105 C ATOM 359 O GLN A 41 40.897 -9.260 -4.812 1.00 9.91 O ANISOU 359 O GLN A 41 1558 897 1312 -302 -294 219 O ATOM 360 CB GLN A 41 39.422 -9.912 -2.096 1.00 14.59 C ANISOU 360 CB GLN A 41 2000 2517 1027 -260 39 103 C ATOM 361 CG GLN A 41 37.914 -10.024 -2.204 1.00 14.86 C ANISOU 361 CG GLN A 41 2037 1430 2181 80 -126 74 C ATOM 362 CD GLN A 41 37.240 -9.317 -1.010 1.00 18.34 C ANISOU 362 CD GLN A 41 2499 1301 3168 -351 849 -118 C ATOM 363 OE1 GLN A 41 37.747 -8.424 -0.429 1.00 19.79 O ANISOU 363 OE1 GLN A 41 2892 1926 2702 -149 478 -556 O ATOM 364 NE2 GLN A 41 36.123 -9.895 -0.602 1.00 25.29 N ANISOU 364 NE2 GLN A 41 2621 1981 5006 -230 1543 -351 N ATOM 365 N ASN A 42 39.138 -10.564 -5.336 1.00 8.08 N ANISOU 365 N ASN A 42 1374 655 1040 -114 -191 98 N ATOM 366 CA ASN A 42 39.061 -10.138 -6.732 1.00 7.42 C ANISOU 366 CA ASN A 42 1215 623 981 -114 -99 111 C ATOM 367 C ASN A 42 37.691 -9.551 -6.984 1.00 7.86 C ANISOU 367 C ASN A 42 1247 558 1183 -85 -219 69 C ATOM 368 O ASN A 42 36.837 -10.148 -7.654 1.00 8.94 O ANISOU 368 O ASN A 42 1307 747 1341 -129 -363 21 O ATOM 369 CB ASN A 42 39.394 -11.271 -7.686 1.00 7.97 C ANISOU 369 CB ASN A 42 1292 580 1156 -61 -214 31 C ATOM 370 CG ASN A 42 40.852 -11.647 -7.563 1.00 8.06 C ANISOU 370 CG ASN A 42 1274 544 1245 -154 -192 105 C ATOM 371 OD1 ASN A 42 41.264 -12.217 -6.537 1.00 8.84 O ANISOU 371 OD1 ASN A 42 1382 801 1176 10 -263 165 O ATOM 372 ND2 ASN A 42 41.650 -11.287 -8.557 1.00 8.06 N ANISOU 372 ND2 ASN A 42 1246 589 1226 -167 -127 56 N ATOM 373 N APRO A 43 37.463 -8.342 -6.471 0.63 7.64 N ANISOU 373 N APRO A 43 1224 498 1180 -117 -90 102 N ATOM 374 N BPRO A 43 37.357 -8.412 -6.373 0.37 9.96 N ANISOU 374 N BPRO A 43 1518 718 1547 100 -501 -181 N ATOM 375 CA APRO A 43 36.142 -7.719 -6.570 0.63 8.37 C ANISOU 375 CA APRO A 43 1256 508 1415 -92 -150 195 C ATOM 376 CA BPRO A 43 36.008 -7.850 -6.523 0.37 9.77 C ANISOU 376 CA BPRO A 43 1557 858 1298 210 -410 -203 C ATOM 377 C APRO A 43 35.873 -7.352 -8.028 0.63 9.14 C ANISOU 377 C APRO A 43 1362 840 1270 154 -190 -20 C ATOM 378 C BPRO A 43 35.843 -7.388 -7.971 0.37 8.75 C ANISOU 378 C BPRO A 43 1368 605 1351 -229 -313 38 C ATOM 379 O APRO A 43 36.755 -7.035 -8.834 0.63 9.24 O ANISOU 379 O APRO A 43 1521 762 1228 203 -253 248 O ATOM 380 O BPRO A 43 36.823 -7.091 -8.663 0.37 13.07 O ANISOU 380 O BPRO A 43 1732 1327 1907 97 362 -122 O ATOM 381 CB APRO A 43 36.273 -6.491 -5.676 0.63 8.22 C ANISOU 381 CB APRO A 43 1188 725 1212 -62 -181 65 C ATOM 382 CB BPRO A 43 35.980 -6.659 -5.571 0.37 10.65 C ANISOU 382 CB BPRO A 43 1445 1036 1567 -113 -319 -468 C ATOM 383 CG APRO A 43 37.736 -6.145 -5.756 0.63 9.18 C ANISOU 383 CG APRO A 43 1263 558 1668 -123 -232 3 C ATOM 384 CG BPRO A 43 37.206 -6.747 -4.726 0.37 10.55 C ANISOU 384 CG BPRO A 43 1564 848 1597 -243 -370 -275 C ATOM 385 CD APRO A 43 38.432 -7.484 -5.799 0.63 8.27 C ANISOU 385 CD APRO A 43 1235 624 1284 -136 -26 -141 C ATOM 386 CD BPRO A 43 38.192 -7.576 -5.510 0.37 9.88 C ANISOU 386 CD BPRO A 43 1441 778 1533 -230 -332 -102 C ATOM 387 N THR A 44 34.572 -7.297 -8.349 1.00 9.89 N ANISOU 387 N THR A 44 1541 618 1599 -61 -458 6 N ATOM 388 CA THR A 44 34.194 -6.809 -9.657 1.00 9.95 C ANISOU 388 CA THR A 44 1598 728 1452 -45 -434 12 C ATOM 389 C THR A 44 34.203 -5.287 -9.677 1.00 10.18 C ANISOU 389 C THR A 44 1686 714 1468 21 -466 -20 C ATOM 390 O THR A 44 34.267 -4.600 -8.661 1.00 9.39 O ANISOU 390 O THR A 44 1413 690 1465 -18 -361 -12 O ATOM 391 CB THR A 44 32.780 -7.293 -10.004 1.00 11.86 C ANISOU 391 CB THR A 44 1652 837 2016 24 -632 -24 C ATOM 392 OG1 THR A 44 31.885 -6.664 -9.073 1.00 11.69 O ANISOU 392 OG1 THR A 44 1472 876 2093 -88 -529 269 O ATOM 393 CG2 THR A 44 32.700 -8.800 -9.937 1.00 12.33 C ANISOU 393 CG2 THR A 44 2241 756 1688 -234 -549 85 C ATOM 394 N GLU A 45 34.106 -4.735 -10.884 1.00 11.19 N ANISOU 394 N GLU A 45 2050 808 1393 117 -487 5 N ATOM 395 CA GLU A 45 34.024 -3.296 -11.046 1.00 10.91 C ANISOU 395 CA GLU A 45 1825 722 1598 102 -378 50 C ATOM 396 C GLU A 45 32.859 -2.710 -10.254 1.00 10.24 C ANISOU 396 C GLU A 45 1509 693 1690 47 -516 138 C ATOM 397 O GLU A 45 32.985 -1.663 -9.641 1.00 10.21 O ANISOU 397 O GLU A 45 1540 692 1647 7 -309 70 O ATOM 398 CB GLU A 45 33.982 -2.896 -12.524 1.00 13.87 C ANISOU 398 CB GLU A 45 2390 1214 1664 -25 -269 340 C ATOM 399 CG GLU A 45 34.012 -1.377 -12.677 1.00 15.02 C ANISOU 399 CG GLU A 45 2616 1217 1875 -145 -112 397 C ATOM 400 CD GLU A 45 35.293 -0.664 -12.345 1.00 18.42 C ANISOU 400 CD GLU A 45 2525 1378 3094 -142 -531 782 C ATOM 401 OE1 GLU A 45 36.325 -1.270 -12.129 1.00 22.57 O ANISOU 401 OE1 GLU A 45 2353 2203 4019 300 228 956 O ATOM 402 OE2 GLU A 45 35.291 0.598 -12.275 1.00 19.02 O ANISOU 402 OE2 GLU A 45 3064 1469 2693 -277 -375 274 O ATOM 403 N ALA A 46 31.689 -3.401 -10.257 1.00 11.49 N ANISOU 403 N ALA A 46 1573 834 1958 -33 -736 111 N ATOM 404 CA ALA A 46 30.532 -2.900 -9.503 1.00 11.63 C ANISOU 404 CA ALA A 46 1305 950 2165 -35 -671 323 C ATOM 405 C ALA A 46 30.806 -2.833 -8.006 1.00 10.38 C ANISOU 405 C ALA A 46 1125 640 2177 44 -484 216 C ATOM 406 O ALA A 46 30.468 -1.860 -7.337 1.00 11.14 O ANISOU 406 O ALA A 46 1090 656 2485 114 -404 173 O ATOM 407 CB ALA A 46 29.299 -3.751 -9.824 1.00 13.84 C ANISOU 407 CB ALA A 46 1641 1094 2522 -181 -813 63 C ATOM 408 N GLU A 47 31.461 -3.847 -7.473 1.00 9.97 N ANISOU 408 N GLU A 47 1158 573 2056 -127 -544 202 N ATOM 409 CA GLU A 47 31.804 -3.861 -6.070 1.00 9.34 C ANISOU 409 CA GLU A 47 1287 562 1699 -96 -321 209 C ATOM 410 C GLU A 47 32.816 -2.752 -5.754 1.00 9.06 C ANISOU 410 C GLU A 47 1253 689 1500 -71 -261 169 C ATOM 411 O GLU A 47 32.706 -2.078 -4.725 1.00 9.24 O ANISOU 411 O GLU A 47 1184 723 1601 -50 -162 61 O ATOM 412 CB GLU A 47 32.423 -5.228 -5.694 1.00 9.14 C ANISOU 412 CB GLU A 47 992 670 1809 -74 -196 198 C ATOM 413 CG GLU A 47 31.378 -6.339 -5.686 1.00 10.97 C ANISOU 413 CG GLU A 47 1166 666 2334 -162 -372 343 C ATOM 414 CD GLU A 47 31.918 -7.724 -5.482 1.00 10.63 C ANISOU 414 CD GLU A 47 1193 623 2222 -156 -184 33 C ATOM 415 OE1 GLU A 47 32.996 -8.036 -6.051 1.00 10.34 O ANISOU 415 OE1 GLU A 47 1286 671 1972 -47 -295 180 O ATOM 416 OE2 GLU A 47 31.201 -8.553 -4.889 1.00 15.87 O ANISOU 416 OE2 GLU A 47 1700 871 3460 104 532 656 O ATOM 417 N LEU A 48 33.809 -2.554 -6.615 1.00 8.44 N ANISOU 417 N LEU A 48 1076 597 1536 -39 -328 -53 N ATOM 418 CA LEU A 48 34.792 -1.522 -6.399 1.00 8.88 C ANISOU 418 CA LEU A 48 1167 514 1693 -121 -281 37 C ATOM 419 C LEU A 48 34.136 -0.133 -6.430 1.00 8.80 C ANISOU 419 C LEU A 48 1105 581 1656 -92 -289 60 C ATOM 420 O LEU A 48 34.505 0.753 -5.658 1.00 9.21 O ANISOU 420 O LEU A 48 1152 571 1776 -88 -271 -44 O ATOM 421 CB LEU A 48 35.877 -1.639 -7.439 1.00 9.43 C ANISOU 421 CB LEU A 48 1207 602 1774 -106 -293 -68 C ATOM 422 CG LEU A 48 36.815 -2.845 -7.295 1.00 9.53 C ANISOU 422 CG LEU A 48 1271 615 1734 -82 -242 -72 C ATOM 423 CD1 LEU A 48 37.596 -3.125 -8.547 1.00 10.64 C ANISOU 423 CD1 LEU A 48 1225 868 1949 -112 -222 -232 C ATOM 424 CD2 LEU A 48 37.710 -2.653 -6.085 1.00 12.06 C ANISOU 424 CD2 LEU A 48 1555 1195 1834 90 -404 -44 C ATOM 425 N GLN A 49 33.192 0.058 -7.343 1.00 9.18 N ANISOU 425 N GLN A 49 1163 480 1847 -5 -382 -64 N ATOM 426 CA GLN A 49 32.508 1.341 -7.432 1.00 9.62 C ANISOU 426 CA GLN A 49 1182 616 1858 90 -184 68 C ATOM 427 C GLN A 49 31.743 1.654 -6.195 1.00 9.16 C ANISOU 427 C GLN A 49 1049 629 1804 -23 -230 131 C ATOM 428 O GLN A 49 31.718 2.819 -5.734 1.00 9.49 O ANISOU 428 O GLN A 49 1287 577 1741 14 -240 38 O ATOM 429 CB GLN A 49 31.633 1.364 -8.706 1.00 10.38 C ANISOU 429 CB GLN A 49 1322 860 1762 209 -181 155 C ATOM 430 CG GLN A 49 31.076 2.760 -8.971 1.00 11.87 C ANISOU 430 CG GLN A 49 1843 1041 1627 489 32 301 C ATOM 431 CD GLN A 49 32.182 3.712 -9.319 1.00 16.01 C ANISOU 431 CD GLN A 49 2386 1098 2600 564 842 678 C ATOM 432 OE1 GLN A 49 32.403 4.758 -8.681 1.00 17.54 O ANISOU 432 OE1 GLN A 49 2057 1291 3316 77 66 666 O ATOM 433 NE2 GLN A 49 32.885 3.455 -10.382 1.00 22.80 N ANISOU 433 NE2 GLN A 49 3615 1701 3345 1165 1951 1347 N ATOM 434 N ASP A 50 31.080 0.663 -5.615 1.00 9.52 N ANISOU 434 N ASP A 50 1192 634 1790 -101 -287 74 N ATOM 435 CA ASP A 50 30.364 0.892 -4.370 1.00 10.37 C ANISOU 435 CA ASP A 50 1196 824 1921 -71 -128 136 C ATOM 436 C ASP A 50 31.347 1.297 -3.290 1.00 10.69 C ANISOU 436 C ASP A 50 1438 959 1666 -76 -87 197 C ATOM 437 O ASP A 50 31.034 2.182 -2.484 1.00 11.16 O ANISOU 437 O ASP A 50 1425 1192 1624 -88 9 208 O ATOM 438 CB ASP A 50 29.587 -0.327 -3.948 1.00 11.57 C ANISOU 438 CB ASP A 50 1181 1028 2186 -91 5 156 C ATOM 439 CG ASP A 50 28.287 -0.528 -4.671 1.00 13.93 C ANISOU 439 CG ASP A 50 1306 1177 2810 -284 -116 96 C ATOM 440 OD1 ASP A 50 27.784 0.387 -5.322 1.00 14.25 O ANISOU 440 OD1 ASP A 50 1282 1420 2711 305 -173 -86 O ATOM 441 OD2 ASP A 50 27.759 -1.666 -4.571 1.00 16.94 O ANISOU 441 OD2 ASP A 50 1518 1568 3352 -512 -223 208 O ATOM 442 N MET A 51 32.512 0.661 -3.226 1.00 10.31 N ANISOU 442 N MET A 51 1330 963 1623 -141 -261 308 N ATOM 443 CA MET A 51 33.489 1.018 -2.206 1.00 10.93 C ANISOU 443 CA MET A 51 1596 962 1595 -44 -317 248 C ATOM 444 C MET A 51 33.957 2.444 -2.385 1.00 10.67 C ANISOU 444 C MET A 51 1601 905 1547 -1 -419 167 C ATOM 445 O MET A 51 34.062 3.206 -1.390 1.00 12.53 O ANISOU 445 O MET A 51 1961 1096 1704 0 -326 -85 O ATOM 446 CB MET A 51 34.687 0.051 -2.252 1.00 10.90 C ANISOU 446 CB MET A 51 1544 927 1670 -29 -320 292 C ATOM 447 CG MET A 51 34.349 -1.383 -1.879 1.00 12.65 C ANISOU 447 CG MET A 51 1880 954 1973 -62 -551 268 C ATOM 448 SD MET A 51 35.692 -2.528 -2.020 1.00 15.60 S ANISOU 448 SD MET A 51 2216 983 2727 181 -621 366 S ATOM 449 CE MET A 51 36.658 -2.067 -0.588 1.00 20.70 C ANISOU 449 CE MET A 51 2317 2188 3359 -133 -1206 538 C ATOM 450 N AILE A 52 34.269 2.924 -3.574 0.52 9.30 N ANISOU 450 N AILE A 52 1012 873 1648 -350 -524 136 N ATOM 451 N BILE A 52 34.273 2.797 -3.619 0.48 9.90 N ANISOU 451 N BILE A 52 1606 453 1701 88 -187 54 N ATOM 452 CA AILE A 52 34.702 4.316 -3.822 0.52 9.63 C ANISOU 452 CA AILE A 52 1268 742 1650 -307 -359 -8 C ATOM 453 CA BILE A 52 34.667 4.198 -3.912 0.48 9.34 C ANISOU 453 CA BILE A 52 1416 411 1722 5 -529 -28 C ATOM 454 C AILE A 52 33.544 5.238 -3.514 0.52 9.56 C ANISOU 454 C AILE A 52 1363 743 1528 -323 -88 214 C ATOM 455 C BILE A 52 33.573 5.185 -3.569 0.48 9.48 C ANISOU 455 C BILE A 52 1471 382 1747 -78 -342 79 C ATOM 456 O AILE A 52 33.655 6.281 -2.865 0.52 12.36 O ANISOU 456 O AILE A 52 1636 1417 1642 82 -420 -444 O ATOM 457 O BILE A 52 33.871 6.232 -2.950 0.48 9.57 O ANISOU 457 O BILE A 52 1809 321 1508 -109 -86 104 O ATOM 458 CB AILE A 52 35.245 4.446 -5.254 0.52 9.07 C ANISOU 458 CB AILE A 52 1311 447 1688 -133 -245 -144 C ATOM 459 CB BILE A 52 35.118 4.297 -5.382 0.48 10.26 C ANISOU 459 CB BILE A 52 1199 725 1976 -186 -204 95 C ATOM 460 CG1AILE A 52 36.490 3.596 -5.578 0.52 11.72 C ANISOU 460 CG1AILE A 52 1136 602 2714 -141 45 72 C ATOM 461 CG1BILE A 52 36.406 3.460 -5.519 0.48 15.19 C ANISOU 461 CG1BILE A 52 1515 1345 2910 179 209 180 C ATOM 462 CG2AILE A 52 35.464 5.933 -5.570 0.52 9.32 C ANISOU 462 CG2AILE A 52 1346 545 1650 -25 1 -106 C ATOM 463 CG2BILE A 52 35.225 5.730 -5.880 0.48 11.38 C ANISOU 463 CG2BILE A 52 1990 680 1654 -321 -246 -113 C ATOM 464 CD1AILE A 52 37.727 3.880 -4.815 0.52 14.61 C ANISOU 464 CD1AILE A 52 1519 458 3572 -168 -614 262 C ATOM 465 CD1BILE A 52 37.675 4.193 -5.373 0.48 17.44 C ANISOU 465 CD1BILE A 52 1301 1399 3927 211 531 451 C ATOM 466 N ASN A 53 32.326 4.884 -3.952 1.00 9.60 N ANISOU 466 N ASN A 53 1298 669 1680 -89 52 -96 N ATOM 467 CA ASN A 53 31.204 5.787 -3.722 1.00 10.19 C ANISOU 467 CA ASN A 53 1490 731 1652 37 106 -36 C ATOM 468 C ASN A 53 30.979 6.063 -2.257 1.00 11.56 C ANISOU 468 C ASN A 53 1506 1173 1713 68 147 -161 C ATOM 469 O ASN A 53 30.532 7.158 -1.907 1.00 12.03 O ANISOU 469 O ASN A 53 1626 1203 1741 201 169 -133 O ATOM 470 CB ASN A 53 29.925 5.245 -4.345 1.00 11.24 C ANISOU 470 CB ASN A 53 1345 1042 1882 36 192 -46 C ATOM 471 CG ASN A 53 29.854 5.298 -5.847 1.00 10.22 C ANISOU 471 CG ASN A 53 1291 773 1819 150 69 -46 C ATOM 472 OD1 ASN A 53 28.868 4.704 -6.405 1.00 14.13 O ANISOU 472 OD1 ASN A 53 1461 1562 2347 135 -113 -285 O ATOM 473 ND2 ASN A 53 30.780 5.883 -6.500 1.00 9.88 N ANISOU 473 ND2 ASN A 53 1708 706 1341 65 -94 -13 N ATOM 474 N GLU A 54 31.267 5.106 -1.386 1.00 14.78 N ANISOU 474 N GLU A 54 2779 1056 1780 3 556 103 N ATOM 475 CA GLU A 54 31.153 5.347 0.058 1.00 17.10 C ANISOU 475 CA GLU A 54 3281 1452 1763 -157 739 238 C ATOM 476 C GLU A 54 32.100 6.390 0.620 1.00 17.45 C ANISOU 476 C GLU A 54 3701 1436 1493 -77 158 223 C ATOM 477 O GLU A 54 31.804 6.920 1.721 1.00 23.28 O ANISOU 477 O GLU A 54 5280 1852 1715 -300 705 -91 O ATOM 478 CB GLU A 54 31.378 4.019 0.816 1.00 22.44 C ANISOU 478 CB GLU A 54 4971 1459 2098 -153 1313 510 C ATOM 479 CG GLU A 54 30.444 2.959 0.470 1.00 23.76 C ANISOU 479 CG GLU A 54 3779 1821 3427 -122 1533 838 C ATOM 480 CD GLU A 54 29.067 3.203 -0.048 1.00 34.26 C ANISOU 480 CD GLU A 54 4297 5043 3677 499 840 157 C ATOM 481 OE1 GLU A 54 28.328 3.516 0.907 1.00 33.61 O ANISOU 481 OE1 GLU A 54 4235 5245 3290 2106 751 1802 O ATOM 482 OE2 GLU A 54 28.926 3.037 -1.303 1.00 46.97 O ANISOU 482 OE2 GLU A 54 5939 8299 3607 2642 593 188 O ATOM 483 N AVAL A 55 33.214 6.624 -0.055 0.44 14.25 N ANISOU 483 N AVAL A 55 2568 901 1945 548 -386 109 N ATOM 484 N BVAL A 55 33.142 6.754 -0.095 0.56 14.38 N ANISOU 484 N BVAL A 55 2852 1324 1289 4 -509 0 N ATOM 485 CA AVAL A 55 34.359 7.427 0.344 0.44 15.60 C ANISOU 485 CA AVAL A 55 2728 1437 1762 590 -870 -74 C ATOM 486 CA BVAL A 55 34.178 7.613 0.500 0.56 15.76 C ANISOU 486 CA BVAL A 55 3372 830 1787 169 -863 -219 C ATOM 487 C AVAL A 55 34.396 8.791 -0.350 0.44 15.69 C ANISOU 487 C AVAL A 55 2786 1582 1595 -211 -676 -61 C ATOM 488 C BVAL A 55 34.516 8.800 -0.382 0.56 12.87 C ANISOU 488 C BVAL A 55 2350 710 1832 492 -873 -183 C ATOM 489 O AVAL A 55 34.767 9.793 0.294 0.44 9.59 O ANISOU 489 O AVAL A 55 1103 1534 1005 466 105 -361 O ATOM 490 O BVAL A 55 35.243 9.747 -0.036 0.56 10.18 O ANISOU 490 O BVAL A 55 1250 1239 1380 336 -20 -432 O ATOM 491 CB AVAL A 55 35.722 6.680 0.143 0.44 14.02 C ANISOU 491 CB AVAL A 55 2318 2465 545 248 576 702 C ATOM 492 CB BVAL A 55 35.375 6.670 0.806 0.56 18.78 C ANISOU 492 CB BVAL A 55 3918 1110 2106 204 -2125 205 C ATOM 493 CG1AVAL A 55 36.858 7.533 0.712 0.44 13.81 C ANISOU 493 CG1AVAL A 55 2095 1172 1980 489 962 609 C ATOM 494 CG1BVAL A 55 36.670 7.419 1.113 0.56 19.46 C ANISOU 494 CG1BVAL A 55 3031 3614 748 -437 -229 304 C ATOM 495 CG2AVAL A 55 35.670 5.366 0.860 0.44 12.15 C ANISOU 495 CG2AVAL A 55 1973 1107 1537 297 -243 -341 C ATOM 496 CG2BVAL A 55 35.012 5.715 1.953 0.56 21.35 C ANISOU 496 CG2BVAL A 55 3856 1044 3214 -586 -1879 404 C ATOM 497 N ASP A 56 34.005 8.834 -1.615 1.00 17.25 N ANISOU 497 N ASP A 56 3858 900 1794 -149 -1161 -70 N ATOM 498 CA ASP A 56 34.204 9.907 -2.558 1.00 15.46 C ANISOU 498 CA ASP A 56 3448 507 1920 147 -1108 -55 C ATOM 499 C ASP A 56 33.243 11.039 -2.338 1.00 12.45 C ANISOU 499 C ASP A 56 1987 907 1836 -411 -561 189 C ATOM 500 O ASP A 56 32.173 11.151 -2.957 1.00 15.88 O ANISOU 500 O ASP A 56 2173 1558 2303 -605 -874 225 O ATOM 501 CB ASP A 56 34.072 9.349 -3.985 1.00 16.84 C ANISOU 501 CB ASP A 56 3815 726 1859 -50 -1180 32 C ATOM 502 CG ASP A 56 34.135 10.417 -5.068 1.00 12.12 C ANISOU 502 CG ASP A 56 1958 696 1952 7 -689 106 C ATOM 503 OD1 ASP A 56 34.725 11.455 -4.805 1.00 11.25 O ANISOU 503 OD1 ASP A 56 1409 777 2088 114 -504 -259 O ATOM 504 OD2 ASP A 56 33.553 10.124 -6.139 1.00 13.16 O ANISOU 504 OD2 ASP A 56 2268 887 1844 -136 -893 117 O ATOM 505 N ALA A 57 33.590 11.959 -1.458 1.00 12.46 N ANISOU 505 N ALA A 57 1615 873 2247 -115 -397 -137 N ATOM 506 CA ALA A 57 32.721 13.009 -1.023 1.00 13.59 C ANISOU 506 CA ALA A 57 1703 1140 2322 -90 -194 25 C ATOM 507 C ALA A 57 32.321 13.972 -2.148 1.00 12.49 C ANISOU 507 C ALA A 57 1309 893 2544 -60 -126 138 C ATOM 508 O ALA A 57 31.155 14.491 -2.043 1.00 16.56 O ANISOU 508 O ALA A 57 1468 1865 2961 272 17 128 O ATOM 509 CB ALA A 57 33.315 13.755 0.183 1.00 14.84 C ANISOU 509 CB ALA A 57 1924 1411 2304 113 -28 -345 C ATOM 510 N ASP A 58 33.167 14.296 -3.085 1.00 12.82 N ANISOU 510 N ASP A 58 1339 968 2565 -105 -149 114 N ATOM 511 CA ASP A 58 32.787 15.300 -4.096 1.00 12.17 C ANISOU 511 CA ASP A 58 1060 1061 2505 229 -135 178 C ATOM 512 C ASP A 58 32.242 14.620 -5.352 1.00 14.17 C ANISOU 512 C ASP A 58 1150 1158 3077 -4 -616 242 C ATOM 513 O ASP A 58 31.861 15.310 -6.284 1.00 15.93 O ANISOU 513 O ASP A 58 1843 1338 2869 380 -846 137 O ATOM 514 CB ASP A 58 33.922 16.255 -4.425 1.00 12.14 C ANISOU 514 CB ASP A 58 1338 691 2583 41 -249 12 C ATOM 515 CG ASP A 58 35.182 15.636 -4.962 1.00 10.58 C ANISOU 515 CG ASP A 58 1145 569 2305 32 -381 383 C ATOM 516 OD1 ASP A 58 35.152 14.395 -5.178 1.00 10.30 O ANISOU 516 OD1 ASP A 58 1539 589 1784 66 -592 8 O ATOM 517 OD2 ASP A 58 36.145 16.393 -5.209 1.00 10.39 O ANISOU 517 OD2 ASP A 58 1344 613 1990 -42 -331 119 O ATOM 518 N GLY A 59 32.173 13.282 -5.408 1.00 14.69 N ANISOU 518 N GLY A 59 1650 1093 2840 -146 -542 196 N ATOM 519 CA GLY A 59 31.512 12.626 -6.522 1.00 16.07 C ANISOU 519 CA GLY A 59 1370 1507 3227 9 -1054 69 C ATOM 520 C GLY A 59 32.329 12.708 -7.800 1.00 14.80 C ANISOU 520 C GLY A 59 1671 967 2986 -86 -1048 -69 C ATOM 521 O GLY A 59 31.713 12.494 -8.863 1.00 17.34 O ANISOU 521 O GLY A 59 1704 1767 3117 -24 -1257 -28 O ATOM 522 N ASN A 60 33.616 12.979 -7.798 1.00 13.93 N ANISOU 522 N ASN A 60 1659 834 2802 -267 -1189 490 N ATOM 523 CA ASN A 60 34.395 13.043 -9.011 1.00 15.63 C ANISOU 523 CA ASN A 60 2002 1308 2628 -657 -1259 934 C ATOM 524 C ASN A 60 34.849 11.676 -9.428 1.00 14.22 C ANISOU 524 C ASN A 60 1600 1593 2211 -584 -943 621 C ATOM 525 O ASN A 60 35.497 11.598 -10.498 1.00 17.75 O ANISOU 525 O ASN A 60 1912 2630 2204 -807 -790 827 O ATOM 526 CB ASN A 60 35.533 14.043 -8.916 1.00 15.69 C ANISOU 526 CB ASN A 60 1963 1471 2526 -642 -1392 841 C ATOM 527 CG ASN A 60 36.616 13.666 -7.960 1.00 9.01 C ANISOU 527 CG ASN A 60 1299 785 1338 -38 -428 148 C ATOM 528 OD1 ASN A 60 36.522 12.667 -7.198 1.00 9.98 O ANISOU 528 OD1 ASN A 60 1413 728 1652 -110 -553 258 O ATOM 529 ND2 ASN A 60 37.638 14.489 -7.969 1.00 10.09 N ANISOU 529 ND2 ASN A 60 1264 938 1632 -207 -479 415 N ATOM 530 N GLY A 61 34.535 10.599 -8.680 1.00 11.70 N ANISOU 530 N GLY A 61 1400 1140 1905 -301 -754 301 N ATOM 531 CA GLY A 61 34.841 9.258 -9.131 1.00 11.82 C ANISOU 531 CA GLY A 61 1274 1379 1839 -265 -569 116 C ATOM 532 C GLY A 61 36.078 8.633 -8.527 1.00 9.90 C ANISOU 532 C GLY A 61 1174 1228 1359 -266 -315 7 C ATOM 533 O GLY A 61 36.330 7.471 -8.747 1.00 11.11 O ANISOU 533 O GLY A 61 1345 1142 1735 -325 -397 -87 O ATOM 534 N THR A 62 36.865 9.455 -7.805 1.00 9.11 N ANISOU 534 N THR A 62 1140 960 1361 -201 -414 131 N ATOM 535 CA THR A 62 38.110 8.977 -7.198 1.00 8.43 C ANISOU 535 CA THR A 62 1154 862 1188 -151 -296 161 C ATOM 536 C THR A 62 38.230 9.489 -5.779 1.00 7.85 C ANISOU 536 C THR A 62 1140 612 1229 -38 -299 175 C ATOM 537 O THR A 62 37.498 10.387 -5.389 1.00 8.59 O ANISOU 537 O THR A 62 1234 817 1214 71 -299 163 O ATOM 538 CB THR A 62 39.328 9.369 -8.034 1.00 8.31 C ANISOU 538 CB THR A 62 1223 845 1091 -281 -324 111 C ATOM 539 OG1 THR A 62 39.438 10.810 -7.955 1.00 8.31 O ANISOU 539 OG1 THR A 62 1202 768 1186 -149 -199 25 O ATOM 540 CG2 THR A 62 39.275 8.884 -9.459 1.00 9.30 C ANISOU 540 CG2 THR A 62 1414 951 1167 -172 -163 -9 C ATOM 541 N ILE A 63 39.124 8.894 -5.001 1.00 7.76 N ANISOU 541 N ILE A 63 1180 709 1058 -68 -229 101 N ATOM 542 CA ILE A 63 39.366 9.286 -3.619 1.00 7.21 C ANISOU 542 CA ILE A 63 1053 569 1116 -22 -219 95 C ATOM 543 C ILE A 63 40.680 10.068 -3.542 1.00 7.24 C ANISOU 543 C ILE A 63 1109 570 1073 -42 -166 204 C ATOM 544 O ILE A 63 41.724 9.562 -3.960 1.00 8.41 O ANISOU 544 O ILE A 63 1096 742 1357 -141 -173 102 O ATOM 545 CB ILE A 63 39.455 8.058 -2.709 1.00 8.03 C ANISOU 545 CB ILE A 63 1213 680 1158 -106 -156 247 C ATOM 546 CG1 ILE A 63 38.219 7.169 -2.781 1.00 9.46 C ANISOU 546 CG1 ILE A 63 1362 848 1384 -263 -97 173 C ATOM 547 CG2 ILE A 63 39.756 8.477 -1.283 1.00 9.19 C ANISOU 547 CG2 ILE A 63 1535 822 1135 -174 -224 228 C ATOM 548 CD1 ILE A 63 38.439 5.778 -2.148 1.00 15.25 C ANISOU 548 CD1 ILE A 63 2459 926 2408 -392 -106 367 C ATOM 549 N ASP A 64 40.625 11.283 -3.005 1.00 7.71 N ANISOU 549 N ASP A 64 1154 673 1100 -132 -236 224 N ATOM 550 CA ASP A 64 41.840 12.071 -2.809 1.00 7.73 C ANISOU 550 CA ASP A 64 1284 704 949 -165 -197 182 C ATOM 551 C ASP A 64 42.294 11.964 -1.356 1.00 7.85 C ANISOU 551 C ASP A 64 1308 698 978 -200 -260 246 C ATOM 552 O ASP A 64 41.684 11.287 -0.519 1.00 7.94 O ANISOU 552 O ASP A 64 1241 776 999 -212 -173 280 O ATOM 553 CB ASP A 64 41.623 13.526 -3.250 1.00 8.77 C ANISOU 553 CB ASP A 64 1625 676 1030 -301 -287 255 C ATOM 554 CG ASP A 64 40.617 14.269 -2.468 1.00 9.08 C ANISOU 554 CG ASP A 64 1705 582 1163 -153 -440 250 C ATOM 555 OD1 ASP A 64 40.310 13.864 -1.340 1.00 10.12 O ANISOU 555 OD1 ASP A 64 1917 739 1189 -57 -275 212 O ATOM 556 OD2 ASP A 64 40.151 15.308 -2.978 1.00 11.34 O ANISOU 556 OD2 ASP A 64 2141 676 1493 -73 -330 293 O ATOM 557 N PHE A 65 43.455 12.584 -1.079 1.00 8.91 N ANISOU 557 N PHE A 65 1418 962 1004 -464 -323 398 N ATOM 558 CA PHE A 65 44.018 12.419 0.278 1.00 9.05 C ANISOU 558 CA PHE A 65 1306 1089 1043 -409 -343 312 C ATOM 559 C PHE A 65 43.115 12.983 1.337 1.00 9.19 C ANISOU 559 C PHE A 65 1456 905 1131 -394 -304 344 C ATOM 560 O PHE A 65 42.893 12.306 2.353 1.00 9.70 O ANISOU 560 O PHE A 65 1469 1098 1119 -315 -244 350 O ATOM 561 CB PHE A 65 45.458 12.975 0.279 1.00 11.01 C ANISOU 561 CB PHE A 65 1466 1632 1085 -661 -259 473 C ATOM 562 CG PHE A 65 46.075 12.788 1.656 1.00 10.76 C ANISOU 562 CG PHE A 65 1300 1810 979 -660 -212 287 C ATOM 563 CD1 PHE A 65 46.267 11.529 2.155 1.00 10.29 C ANISOU 563 CD1 PHE A 65 1245 1747 918 -43 -76 120 C ATOM 564 CD2 PHE A 65 46.438 13.875 2.420 1.00 14.84 C ANISOU 564 CD2 PHE A 65 2515 1827 1297 -1014 -548 292 C ATOM 565 CE1 PHE A 65 46.864 11.320 3.415 1.00 12.17 C ANISOU 565 CE1 PHE A 65 1512 2070 1042 83 -245 39 C ATOM 566 CE2 PHE A 65 47.066 13.693 3.644 1.00 16.76 C ANISOU 566 CE2 PHE A 65 2924 2217 1228 -949 -580 97 C ATOM 567 CZ PHE A 65 47.305 12.426 4.103 1.00 15.22 C ANISOU 567 CZ PHE A 65 2335 2472 977 -250 -476 -16 C ATOM 568 N PRO A 66 42.545 14.197 1.220 1.00 10.73 N ANISOU 568 N PRO A 66 1925 880 1271 -400 -336 177 N ATOM 569 CA PRO A 66 41.582 14.635 2.221 1.00 11.62 C ANISOU 569 CA PRO A 66 1896 916 1605 -74 -453 -33 C ATOM 570 C PRO A 66 40.412 13.679 2.475 1.00 9.86 C ANISOU 570 C PRO A 66 1698 946 1103 97 -358 38 C ATOM 571 O PRO A 66 39.979 13.435 3.617 1.00 10.97 O ANISOU 571 O PRO A 66 1864 1110 1195 41 -292 -45 O ATOM 572 CB PRO A 66 41.105 16.015 1.748 1.00 16.58 C ANISOU 572 CB PRO A 66 2826 807 2667 -60 -587 88 C ATOM 573 CG PRO A 66 42.156 16.448 0.851 1.00 18.23 C ANISOU 573 CG PRO A 66 3831 1200 1895 114 -452 466 C ATOM 574 CD PRO A 66 42.806 15.258 0.250 1.00 12.69 C ANISOU 574 CD PRO A 66 2474 733 1616 -569 -716 467 C ATOM 575 N GLU A 67 39.864 13.126 1.396 1.00 8.85 N ANISOU 575 N GLU A 67 1500 743 1119 21 -234 72 N ATOM 576 CA GLU A 67 38.763 12.166 1.543 1.00 9.06 C ANISOU 576 CA GLU A 67 1453 915 1075 79 -205 36 C ATOM 577 C GLU A 67 39.218 10.906 2.271 1.00 8.08 C ANISOU 577 C GLU A 67 1244 882 943 -20 -64 84 C ATOM 578 O GLU A 67 38.492 10.324 3.091 1.00 9.22 O ANISOU 578 O GLU A 67 1224 1202 1078 -49 -58 204 O ATOM 579 CB GLU A 67 38.209 11.798 0.132 1.00 8.30 C ANISOU 579 CB GLU A 67 1262 772 1120 10 -224 8 C ATOM 580 CG GLU A 67 37.403 12.941 -0.474 1.00 9.37 C ANISOU 580 CG GLU A 67 1484 822 1253 214 -281 -49 C ATOM 581 CD GLU A 67 37.087 12.757 -1.954 1.00 9.06 C ANISOU 581 CD GLU A 67 1426 656 1361 156 -393 -52 C ATOM 582 OE1 GLU A 67 37.765 11.985 -2.645 1.00 8.97 O ANISOU 582 OE1 GLU A 67 1560 667 1179 101 -422 2 O ATOM 583 OE2 GLU A 67 36.151 13.473 -2.442 1.00 10.71 O ANISOU 583 OE2 GLU A 67 1615 901 1554 244 -567 -76 O ATOM 584 N APHE A 68 40.413 10.448 1.957 0.59 8.66 N ANISOU 584 N APHE A 68 1280 874 1138 32 -11 376 N ATOM 585 N BPHE A 68 40.412 10.448 1.958 0.41 9.08 N ANISOU 585 N BPHE A 68 1313 839 1299 -3 76 351 N ATOM 586 CA APHE A 68 41.006 9.276 2.617 0.59 9.62 C ANISOU 586 CA APHE A 68 1251 1076 1327 70 111 625 C ATOM 587 CA BPHE A 68 41.019 9.332 2.669 0.41 10.27 C ANISOU 587 CA BPHE A 68 1431 995 1477 153 200 474 C ATOM 588 C APHE A 68 41.330 9.563 4.070 0.59 10.14 C ANISOU 588 C APHE A 68 1296 1281 1275 24 117 698 C ATOM 589 C BPHE A 68 41.172 9.601 4.155 0.41 10.40 C ANISOU 589 C BPHE A 68 1256 1266 1429 59 98 525 C ATOM 590 O APHE A 68 41.069 8.680 4.927 0.59 10.76 O ANISOU 590 O APHE A 68 1287 1391 1412 107 281 816 O ATOM 591 O BPHE A 68 40.736 8.815 5.013 0.41 11.37 O ANISOU 591 O BPHE A 68 1488 1270 1560 -39 -50 695 O ATOM 592 CB APHE A 68 42.212 8.847 1.772 0.59 9.69 C ANISOU 592 CB APHE A 68 1227 982 1472 45 140 557 C ATOM 593 CB BPHE A 68 42.413 9.091 2.083 0.41 9.19 C ANISOU 593 CB BPHE A 68 1138 1084 1268 -120 -66 479 C ATOM 594 CG APHE A 68 42.954 7.627 2.250 0.59 8.66 C ANISOU 594 CG APHE A 68 1229 923 1139 -58 87 479 C ATOM 595 CG BPHE A 68 43.147 7.930 2.721 0.41 7.66 C ANISOU 595 CG BPHE A 68 1145 935 831 -138 -63 268 C ATOM 596 CD1APHE A 68 42.627 6.369 1.821 0.59 9.26 C ANISOU 596 CD1APHE A 68 1298 963 1256 37 48 309 C ATOM 597 CD1BPHE A 68 44.239 8.152 3.524 0.41 9.27 C ANISOU 597 CD1BPHE A 68 1260 1305 958 -96 -216 78 C ATOM 598 CD2APHE A 68 44.000 7.759 3.133 0.59 8.74 C ANISOU 598 CD2APHE A 68 1315 950 1055 -70 66 389 C ATOM 599 CD2BPHE A 68 42.705 6.648 2.465 0.41 11.08 C ANISOU 599 CD2BPHE A 68 1669 969 1573 12 -629 -79 C ATOM 600 CE1APHE A 68 43.365 5.270 2.273 0.59 11.54 C ANISOU 600 CE1APHE A 68 1726 938 1721 68 -181 334 C ATOM 601 CE1BPHE A 68 44.928 7.061 4.084 0.41 10.54 C ANISOU 601 CE1BPHE A 68 1113 1677 1214 -10 -241 289 C ATOM 602 CE2APHE A 68 44.764 6.657 3.589 0.59 10.09 C ANISOU 602 CE2APHE A 68 1437 1247 1150 162 -19 351 C ATOM 603 CE2BPHE A 68 43.395 5.558 3.000 0.41 12.11 C ANISOU 603 CE2BPHE A 68 1615 953 2033 -3 -286 192 C ATOM 604 CZ APHE A 68 44.414 5.407 3.139 0.59 10.16 C ANISOU 604 CZ APHE A 68 1247 1066 1547 261 175 454 C ATOM 605 CZ BPHE A 68 44.501 5.784 3.787 0.41 11.46 C ANISOU 605 CZ BPHE A 68 1438 1394 1523 394 -114 164 C ATOM 606 N LEU A 69 41.790 10.744 4.426 1.00 11.01 N ANISOU 606 N LEU A 69 1335 1445 1403 -161 -124 735 N ATOM 607 CA LEU A 69 42.046 11.111 5.832 1.00 13.94 C ANISOU 607 CA LEU A 69 1891 1945 1460 -574 -568 853 C ATOM 608 C LEU A 69 40.736 11.117 6.588 1.00 13.06 C ANISOU 608 C LEU A 69 2229 1672 1060 -173 -470 215 C ATOM 609 O LEU A 69 40.652 10.629 7.739 1.00 15.68 O ANISOU 609 O LEU A 69 2183 2655 1118 -465 -403 539 O ATOM 610 CB LEU A 69 42.695 12.449 5.856 1.00 19.23 C ANISOU 610 CB LEU A 69 2993 2064 2250 -1048 -1315 944 C ATOM 611 CG LEU A 69 44.091 12.789 5.760 1.00 18.98 C ANISOU 611 CG LEU A 69 3003 1918 2291 -988 -821 368 C ATOM 612 CD1 LEU A 69 44.321 14.323 5.947 1.00 23.21 C ANISOU 612 CD1 LEU A 69 2971 2017 3828 -879 -1184 -278 C ATOM 613 CD2 LEU A 69 44.899 12.115 6.810 1.00 20.92 C ANISOU 613 CD2 LEU A 69 2966 2714 2267 -484 -1066 74 C ATOM 614 N ASER A 70 39.690 11.654 6.026 0.78 12.65 N ANISOU 614 N ASER A 70 2100 1806 899 -197 -256 117 N ATOM 615 N BSER A 70 39.683 11.625 5.973 0.22 13.63 N ANISOU 615 N BSER A 70 2138 2054 985 -73 -431 -4 N ATOM 616 CA ASER A 70 38.429 11.737 6.721 0.78 14.51 C ANISOU 616 CA ASER A 70 2410 2216 887 251 -89 -241 C ATOM 617 CA BSER A 70 38.345 11.614 6.524 0.22 15.88 C ANISOU 617 CA BSER A 70 2343 2511 1181 307 -142 -100 C ATOM 618 C ASER A 70 37.887 10.352 7.027 0.78 14.26 C ANISOU 618 C ASER A 70 1871 2580 967 103 238 178 C ATOM 619 C BSER A 70 37.880 10.200 6.847 0.22 15.09 C ANISOU 619 C BSER A 70 1711 2858 1166 163 -239 363 C ATOM 620 O ASER A 70 37.539 10.065 8.163 0.78 20.07 O ANISOU 620 O ASER A 70 2621 3893 1111 369 381 665 O ATOM 621 O BSER A 70 37.331 9.930 7.906 0.22 15.31 O ANISOU 621 O BSER A 70 1921 3061 835 579 -425 359 O ATOM 622 CB ASER A 70 37.512 12.582 5.842 0.78 15.13 C ANISOU 622 CB ASER A 70 2508 2030 1210 465 -90 -423 C ATOM 623 CB BSER A 70 37.369 12.244 5.522 0.22 14.49 C ANISOU 623 CB BSER A 70 2289 1636 1579 343 -355 -504 C ATOM 624 OG ASER A 70 36.227 12.646 6.408 0.78 20.57 O ANISOU 624 OG ASER A 70 2523 3235 2057 671 151 -329 O ATOM 625 OG BSER A 70 37.358 13.640 5.727 0.22 16.30 O ANISOU 625 OG BSER A 70 2280 1397 2517 -646 226 98 O ATOM 626 N ALEU A 71 37.804 9.453 6.054 0.53 12.15 N ANISOU 626 N ALEU A 71 1369 2036 1213 53 54 410 N ATOM 627 N BLEU A 71 38.108 9.306 5.896 0.47 12.71 N ANISOU 627 N BLEU A 71 1338 2276 1214 -248 204 610 N ATOM 628 CA ALEU A 71 37.275 8.094 6.213 0.53 12.64 C ANISOU 628 CA ALEU A 71 1254 2422 1126 -394 -53 787 C ATOM 629 CA BLEU A 71 37.825 7.871 6.048 0.47 16.16 C ANISOU 629 CA BLEU A 71 1722 2355 2063 -458 -25 1068 C ATOM 630 C ALEU A 71 38.131 7.209 7.110 0.53 12.91 C ANISOU 630 C ALEU A 71 1342 2264 1299 -500 -162 837 C ATOM 631 C BLEU A 71 38.581 7.412 7.293 0.47 16.18 C ANISOU 631 C BLEU A 71 1741 2682 1725 -180 353 1141 C ATOM 632 O ALEU A 71 37.686 6.366 7.897 0.53 15.63 O ANISOU 632 O ALEU A 71 1532 2323 2084 -949 -378 1223 O ATOM 633 O BLEU A 71 37.994 6.927 8.278 0.47 17.81 O ANISOU 633 O BLEU A 71 2380 2603 1783 -929 442 956 O ATOM 634 CB ALEU A 71 37.175 7.388 4.842 0.53 13.80 C ANISOU 634 CB ALEU A 71 1640 2302 1300 -925 -295 838 C ATOM 635 CB BLEU A 71 38.215 7.114 4.769 0.47 16.24 C ANISOU 635 CB BLEU A 71 2409 1677 2083 -698 -529 940 C ATOM 636 CG ALEU A 71 37.583 5.899 4.967 0.53 24.20 C ANISOU 636 CG ALEU A 71 3262 2610 3323 50 848 200 C ATOM 637 CG BLEU A 71 38.549 5.603 4.814 0.47 21.46 C ANISOU 637 CG BLEU A 71 3692 2100 2362 281 -846 1227 C ATOM 638 CD1ALEU A 71 36.466 4.935 4.686 0.53 32.24 C ANISOU 638 CD1ALEU A 71 4563 2006 5681 -673 1340 271 C ATOM 639 CD1BLEU A 71 37.592 4.912 3.867 0.47 28.35 C ANISOU 639 CD1BLEU A 71 4177 2533 4062 -693 70 -738 C ATOM 640 CD2ALEU A 71 38.776 5.772 4.033 0.53 23.71 C ANISOU 640 CD2ALEU A 71 2953 4770 1287 264 -107 -118 C ATOM 641 CD2BLEU A 71 39.971 5.407 4.357 0.47 29.31 C ANISOU 641 CD2BLEU A 71 3668 2934 4536 801 -743 1436 C ATOM 642 N AMET A 72 39.474 7.386 7.028 0.67 13.09 N ANISOU 642 N AMET A 72 1306 2273 1395 -435 -83 908 N ATOM 643 N BMET A 72 39.904 7.599 7.290 0.33 14.06 N ANISOU 643 N BMET A 72 1671 2305 1366 111 346 994 N ATOM 644 CA AMET A 72 40.367 6.603 7.893 0.67 14.57 C ANISOU 644 CA AMET A 72 1462 2245 1828 -497 -234 1080 C ATOM 645 CA BMET A 72 40.795 7.164 8.365 0.33 13.83 C ANISOU 645 CA BMET A 72 2047 1562 1647 -28 19 1049 C ATOM 646 C AMET A 72 40.298 7.013 9.318 0.67 16.84 C ANISOU 646 C AMET A 72 2045 2702 1652 -661 -504 1178 C ATOM 647 C BMET A 72 40.263 7.478 9.746 0.33 17.29 C ANISOU 647 C BMET A 72 2416 2644 1508 147 -15 1135 C ATOM 648 O AMET A 72 40.174 6.200 10.235 0.67 19.71 O ANISOU 648 O AMET A 72 2867 2841 1782 -571 -603 1413 O ATOM 649 O BMET A 72 40.369 6.722 10.710 0.33 16.98 O ANISOU 649 O BMET A 72 1703 3067 1680 -266 -180 1454 O ATOM 650 CB AMET A 72 41.848 6.809 7.512 0.67 16.21 C ANISOU 650 CB AMET A 72 1477 2081 2599 -274 -161 1526 C ATOM 651 CB BMET A 72 42.179 7.842 8.295 0.33 18.67 C ANISOU 651 CB BMET A 72 1862 2592 2640 -172 -54 1358 C ATOM 652 CG AMET A 72 42.166 6.091 6.243 0.67 18.79 C ANISOU 652 CG AMET A 72 2128 2274 2740 345 392 1694 C ATOM 653 CG BMET A 72 43.055 7.287 7.190 0.33 19.97 C ANISOU 653 CG BMET A 72 2096 2458 3036 -260 304 1309 C ATOM 654 SD AMET A 72 42.076 4.339 6.456 0.67 23.78 S ANISOU 654 SD AMET A 72 3707 2244 3085 563 677 1424 S ATOM 655 SD BMET A 72 43.119 5.490 7.272 0.33 24.09 S ANISOU 655 SD BMET A 72 3883 2338 2933 -589 -635 624 S ATOM 656 CE AMET A 72 43.386 4.004 7.615 0.67 35.74 C ANISOU 656 CE AMET A 72 5244 4514 3820 2553 217 2557 C ATOM 657 CE BMET A 72 44.857 5.209 7.039 0.33 30.16 C ANISOU 657 CE BMET A 72 5255 4085 2120 1939 1666 1337 C ATOM 658 N AALA A 73 40.418 8.307 9.560 0.54 14.98 N ANISOU 658 N AALA A 73 1465 2636 1591 -136 -171 1050 N ATOM 659 N BALA A 73 39.668 8.655 9.843 0.46 16.19 N ANISOU 659 N BALA A 73 1948 2989 1215 337 144 886 N ATOM 660 CA AALA A 73 40.338 8.769 10.932 0.54 17.68 C ANISOU 660 CA AALA A 73 1627 3417 1673 -272 -245 736 C ATOM 661 CA BALA A 73 39.261 9.082 11.177 0.46 16.55 C ANISOU 661 CA BALA A 73 1863 3428 998 -103 -132 806 C ATOM 662 C AALA A 73 39.041 8.301 11.600 0.54 17.58 C ANISOU 662 C AALA A 73 1767 3639 1273 -336 -312 947 C ATOM 663 C BALA A 73 38.035 8.292 11.586 0.46 16.51 C ANISOU 663 C BALA A 73 1786 3487 1000 -30 -29 706 C ATOM 664 O AALA A 73 39.056 7.927 12.777 0.54 21.10 O ANISOU 664 O AALA A 73 2003 4506 1507 -79 -371 1410 O ATOM 665 O BALA A 73 37.963 7.813 12.716 0.46 16.36 O ANISOU 665 O BALA A 73 2032 3099 1083 -430 -306 738 O ATOM 666 CB AALA A 73 40.422 10.273 10.996 0.54 18.04 C ANISOU 666 CB AALA A 73 1402 3456 1997 -414 -449 379 C ATOM 667 CB BALA A 73 38.976 10.557 11.188 0.46 21.88 C ANISOU 667 CB BALA A 73 3603 3309 1403 -252 643 270 C ATOM 668 N AARG A 74 37.942 8.291 10.862 0.51 16.68 N ANISOU 668 N AARG A 74 1508 3502 1326 13 -140 997 N ATOM 669 N BARG A 74 37.075 8.163 10.692 0.49 15.34 N ANISOU 669 N BARG A 74 1629 2979 1221 227 -147 830 N ATOM 670 CA AARG A 74 36.694 7.773 11.398 0.51 16.59 C ANISOU 670 CA AARG A 74 1473 3394 1438 167 -52 919 C ATOM 671 CA BARG A 74 35.920 7.332 11.012 0.49 17.15 C ANISOU 671 CA BARG A 74 1521 3387 1606 191 79 948 C ATOM 672 C AARG A 74 36.752 6.254 11.532 0.51 18.92 C ANISOU 672 C AARG A 74 2091 3422 1674 372 512 1397 C ATOM 673 C BARG A 74 36.319 5.950 11.439 0.49 18.66 C ANISOU 673 C BARG A 74 1852 3451 1786 195 352 1347 C ATOM 674 O AARG A 74 36.329 5.765 12.595 0.51 23.26 O ANISOU 674 O AARG A 74 2527 4192 2120 703 1023 1785 O ATOM 675 O BARG A 74 35.891 5.365 12.424 0.49 24.55 O ANISOU 675 O BARG A 74 2278 4621 2430 570 825 2123 O ATOM 676 CB AARG A 74 35.525 8.256 10.548 0.51 17.54 C ANISOU 676 CB AARG A 74 1448 3633 1582 309 98 1142 C ATOM 677 CB BARG A 74 34.994 7.272 9.776 0.49 18.13 C ANISOU 677 CB BARG A 74 1557 3283 2049 108 -226 911 C ATOM 678 CG AARG A 74 35.327 9.766 10.636 0.51 21.74 C ANISOU 678 CG AARG A 74 2076 3579 2606 198 -336 1517 C ATOM 679 CG BARG A 74 34.195 8.596 9.900 0.49 20.42 C ANISOU 679 CG BARG A 74 2036 3578 2146 417 -1001 -202 C ATOM 680 CD AARG A 74 34.302 10.310 9.659 0.51 21.88 C ANISOU 680 CD AARG A 74 1585 3699 3028 340 -445 1142 C ATOM 681 CD BARG A 74 32.913 8.183 10.666 0.49 26.32 C ANISOU 681 CD BARG A 74 2669 3903 3427 1148 189 347 C ATOM 682 NE AARG A 74 33.072 9.557 9.606 0.51 20.82 N ANISOU 682 NE AARG A 74 1526 3449 2935 389 151 1308 N ATOM 683 NE BARG A 74 31.808 8.339 9.758 0.49 26.77 N ANISOU 683 NE BARG A 74 1859 4084 4230 464 436 1755 N ATOM 684 CZ AARG A 74 32.563 8.803 8.641 0.51 24.04 C ANISOU 684 CZ AARG A 74 1428 4225 3482 217 -784 1361 C ATOM 685 CZ BARG A 74 30.881 7.635 9.182 0.49 35.02 C ANISOU 685 CZ BARG A 74 3281 5328 4696 576 -639 568 C ATOM 686 NH1AARG A 74 33.220 8.641 7.485 0.51 32.15 N ANISOU 686 NH1AARG A 74 3992 6029 2196 -3214 -682 1214 N ATOM 687 NH1BARG A 74 30.644 6.333 9.284 0.49 37.71 N ANISOU 687 NH1BARG A 74 6834 5729 1766 -1107 -1467 -29 N ATOM 688 NH2AARG A 74 31.393 8.172 8.776 0.51 26.55 N ANISOU 688 NH2AARG A 74 1755 4204 4129 -70 -758 2097 N ATOM 689 NH2BARG A 74 30.040 8.299 8.380 0.49 48.87 N ANISOU 689 NH2BARG A 74 6373 7275 4920 817 -2713 640 N ATOM 690 N LYS A 75 37.229 5.418 10.614 1.00 19.83 N ANISOU 690 N LYS A 75 2555 3263 1716 484 484 1422 N ATOM 691 CA LYS A 75 37.442 3.966 10.753 1.00 22.03 C ANISOU 691 CA LYS A 75 2984 3276 2111 415 554 1413 C ATOM 692 C LYS A 75 38.219 3.702 12.012 1.00 20.78 C ANISOU 692 C LYS A 75 2285 3139 2471 634 694 1735 C ATOM 693 O LYS A 75 37.989 2.747 12.748 1.00 22.48 O ANISOU 693 O LYS A 75 2628 3243 2672 563 831 1939 O ATOM 694 CB LYS A 75 38.121 3.398 9.485 1.00 23.99 C ANISOU 694 CB LYS A 75 3419 2961 2737 -611 1080 689 C ATOM 695 CG LYS A 75 37.109 3.135 8.363 1.00 34.70 C ANISOU 695 CG LYS A 75 6082 4501 2601 104 -264 865 C ATOM 696 CD LYS A 75 37.787 2.423 7.204 1.00 42.14 C ANISOU 696 CD LYS A 75 8026 4719 3266 1413 -927 -19 C ATOM 697 CE LYS A 75 36.930 1.452 6.424 1.00 51.60 C ANISOU 697 CE LYS A 75 8855 6371 4382 1291 -1848 -913 C ATOM 698 NZ LYS A 75 37.336 1.351 4.982 1.00 60.20 N ANISOU 698 NZ LYS A 75 10628 6522 5724 -1121 260 -3055 N ATOM 699 N AMET A 76 39.168 4.546 12.387 0.60 22.19 N ANISOU 699 N AMET A 76 2672 3398 2360 357 450 1897 N ATOM 700 N BMET A 76 39.189 4.574 12.275 0.40 21.46 N ANISOU 700 N BMET A 76 2600 3333 2221 426 529 1875 N ATOM 701 CA AMET A 76 39.962 4.230 13.588 0.60 22.35 C ANISOU 701 CA AMET A 76 2896 3127 2470 93 401 2084 C ATOM 702 CA BMET A 76 40.015 4.503 13.474 0.40 22.95 C ANISOU 702 CA BMET A 76 3278 3211 2233 206 312 1986 C ATOM 703 C AMET A 76 39.234 4.607 14.852 0.60 23.16 C ANISOU 703 C AMET A 76 3711 2780 2310 138 486 2001 C ATOM 704 C BMET A 76 39.116 4.451 14.710 0.40 23.38 C ANISOU 704 C BMET A 76 3880 2848 2156 352 502 1606 C ATOM 705 O AMET A 76 39.565 4.174 15.974 0.60 27.59 O ANISOU 705 O AMET A 76 4752 3568 2162 557 -282 1446 O ATOM 706 O BMET A 76 39.251 3.575 15.594 0.40 15.46 O ANISOU 706 O BMET A 76 2480 1927 1467 -490 -3 846 O ATOM 707 CB AMET A 76 41.265 4.995 13.470 0.60 21.85 C ANISOU 707 CB AMET A 76 3072 2568 2663 11 150 1854 C ATOM 708 CB BMET A 76 40.958 5.707 13.556 0.40 23.54 C ANISOU 708 CB BMET A 76 3507 3016 2422 276 52 1861 C ATOM 709 CG AMET A 76 41.977 4.702 12.151 0.60 25.41 C ANISOU 709 CG AMET A 76 2557 4113 2985 -495 319 1563 C ATOM 710 CG BMET A 76 42.320 5.501 12.962 0.40 26.37 C ANISOU 710 CG BMET A 76 3580 4020 2420 -215 399 2216 C ATOM 711 SD AMET A 76 43.286 5.863 11.871 0.60 27.17 S ANISOU 711 SD AMET A 76 3068 4389 2867 -1066 143 1267 S ATOM 712 SD BMET A 76 43.679 6.613 13.327 0.40 37.03 S ANISOU 712 SD BMET A 76 4551 4482 5035 -1171 1578 1153 S ATOM 713 CE AMET A 76 43.081 7.156 13.087 0.60 36.85 C ANISOU 713 CE AMET A 76 6020 2272 5709 473 544 1340 C ATOM 714 CE BMET A 76 42.869 8.209 13.366 0.40 26.95 C ANISOU 714 CE BMET A 76 2949 4416 2875 -1471 -19 2751 C ATOM 715 N LYS A 77 38.194 5.414 14.734 1.00 22.41 N ANISOU 715 N LYS A 77 3846 2473 2196 104 401 1469 N ATOM 716 CA LYS A 77 37.319 5.569 15.927 1.00 25.50 C ANISOU 716 CA LYS A 77 4985 2177 2525 264 906 943 C ATOM 717 C LYS A 77 36.402 4.392 16.057 1.00 21.01 C ANISOU 717 C LYS A 77 3571 2311 2100 716 762 1137 C ATOM 718 O LYS A 77 36.095 3.838 17.136 1.00 22.36 O ANISOU 718 O LYS A 77 4364 2240 1890 506 1002 758 O ATOM 719 CB LYS A 77 36.528 6.892 15.811 1.00 32.34 C ANISOU 719 CB LYS A 77 7437 2200 2652 1034 1437 957 C ATOM 720 CG LYS A 77 37.274 8.189 16.076 1.00 44.16 C ANISOU 720 CG LYS A 77 9962 2251 4568 65 2761 445 C ATOM 721 CD LYS A 77 36.396 9.416 15.855 1.00 50.35 C ANISOU 721 CD LYS A 77 9575 2120 7434 -287 1121 -160 C ATOM 722 CE LYS A 77 37.056 10.566 15.129 1.00 52.43 C ANISOU 722 CE LYS A 77 10166 2339 7415 109 363 926 C ATOM 723 NZ LYS A 77 36.129 11.175 14.121 1.00 59.77 N ANISOU 723 NZ LYS A 77 10508 3418 8782 1563 -6 646 N ATOM 724 N AGLU A 78 35.918 3.940 14.899 0.58 20.26 N ANISOU 724 N AGLU A 78 2793 2897 2006 654 972 1196 N ATOM 725 N BGLU A 78 35.904 3.837 14.950 0.42 18.75 N ANISOU 725 N BGLU A 78 2409 2730 1985 975 724 1303 N ATOM 726 CA AGLU A 78 35.115 2.729 14.852 0.58 19.93 C ANISOU 726 CA AGLU A 78 2482 3068 2022 598 914 1137 C ATOM 727 CA BGLU A 78 35.032 2.669 15.101 0.42 20.38 C ANISOU 727 CA BGLU A 78 2380 3418 1947 497 239 1522 C ATOM 728 C AGLU A 78 35.859 1.580 15.510 0.58 19.18 C ANISOU 728 C AGLU A 78 2415 2918 1955 270 735 1189 C ATOM 729 C BGLU A 78 35.830 1.436 15.462 0.42 16.78 C ANISOU 729 C BGLU A 78 1963 2715 1697 -119 7 1077 C ATOM 730 O AGLU A 78 35.327 0.857 16.378 0.58 17.77 O ANISOU 730 O AGLU A 78 2470 2702 1579 -377 343 835 O ATOM 731 O BGLU A 78 35.319 0.495 16.092 0.42 23.24 O ANISOU 731 O BGLU A 78 2534 3854 2442 100 489 2275 O ATOM 732 CB AGLU A 78 34.779 2.385 13.397 0.58 24.34 C ANISOU 732 CB AGLU A 78 3661 3504 2082 291 392 1337 C ATOM 733 CB BGLU A 78 34.247 2.457 13.810 0.42 22.00 C ANISOU 733 CB BGLU A 78 3138 3395 1828 899 43 1294 C ATOM 734 CG AGLU A 78 33.350 2.523 12.935 0.58 29.15 C ANISOU 734 CG AGLU A 78 3639 4537 2900 -73 56 618 C ATOM 735 CG BGLU A 78 33.771 1.056 13.468 0.42 27.10 C ANISOU 735 CG BGLU A 78 3620 4034 2643 259 431 528 C ATOM 736 CD AGLU A 78 33.016 3.192 11.631 0.58 31.19 C ANISOU 736 CD AGLU A 78 3636 5163 3053 -2 -661 565 C ATOM 737 CD BGLU A 78 33.422 0.981 11.990 0.42 34.22 C ANISOU 737 CD BGLU A 78 5215 4426 3360 1250 -1321 271 C ATOM 738 OE1AGLU A 78 33.609 2.876 10.573 0.58 39.96 O ANISOU 738 OE1AGLU A 78 7659 4987 2535 -1179 -261 -440 O ATOM 739 OE1BGLU A 78 33.184 2.063 11.403 0.42 38.35 O ANISOU 739 OE1BGLU A 78 6041 5046 3487 785 -53 1406 O ATOM 740 OE2AGLU A 78 32.122 4.072 11.518 0.58 42.80 O ANISOU 740 OE2AGLU A 78 2622 7129 6511 255 -1541 1769 O ATOM 741 OE2BGLU A 78 33.388 -0.119 11.389 0.42 52.25 O ANISOU 741 OE2BGLU A 78 9877 5596 4380 3217 -2996 -1093 O ATOM 742 N GLN A 79 37.108 1.399 15.084 1.00 18.48 N ANISOU 742 N GLN A 79 2179 2918 1926 177 429 1344 N ATOM 743 CA GLN A 79 37.882 0.234 15.502 1.00 18.67 C ANISOU 743 CA GLN A 79 2189 2773 2131 117 417 1145 C ATOM 744 C GLN A 79 38.166 0.301 16.983 1.00 18.14 C ANISOU 744 C GLN A 79 2317 2466 2108 195 441 1205 C ATOM 745 O GLN A 79 38.151 -0.727 17.681 1.00 18.74 O ANISOU 745 O GLN A 79 2288 2549 2285 -31 523 1358 O ATOM 746 CB GLN A 79 39.108 0.177 14.577 1.00 25.77 C ANISOU 746 CB GLN A 79 3485 3532 2773 1068 1516 1487 C ATOM 747 CG GLN A 79 38.747 -0.351 13.185 1.00 39.28 C ANISOU 747 CG GLN A 79 6660 5905 2358 111 1832 1396 C ATOM 748 CD GLN A 79 39.916 -0.689 12.287 1.00 46.38 C ANISOU 748 CD GLN A 79 6828 7354 3441 484 1643 -823 C ATOM 749 OE1 GLN A 79 39.881 -1.559 11.409 1.00 61.45 O ANISOU 749 OE1 GLN A 79 8974 8925 5448 5108 -1684 -2698 O ATOM 750 NE2 GLN A 79 41.046 0.006 12.488 1.00 66.58 N ANISOU 750 NE2 GLN A 79 6736 11273 7289 -1052 2585 -746 N ATOM 751 N AASP A 80 38.453 1.475 17.540 0.31 18.38 N ANISOU 751 N AASP A 80 2376 2448 2160 165 241 1266 N ATOM 752 N BASP A 80 38.399 1.490 17.507 0.69 18.43 N ANISOU 752 N BASP A 80 2349 2475 2177 -50 362 1227 N ATOM 753 CA AASP A 80 38.646 1.539 18.987 0.31 19.26 C ANISOU 753 CA AASP A 80 2569 2548 2203 -402 124 1352 C ATOM 754 CA BASP A 80 38.672 1.642 18.929 0.69 19.64 C ANISOU 754 CA BASP A 80 2504 2592 2366 -281 -20 1229 C ATOM 755 C AASP A 80 37.393 1.016 19.689 0.31 18.83 C ANISOU 755 C AASP A 80 2655 2354 2146 -366 207 1234 C ATOM 756 C BASP A 80 37.432 1.324 19.748 0.69 18.51 C ANISOU 756 C BASP A 80 2902 2339 1793 -516 108 725 C ATOM 757 O AASP A 80 37.450 0.073 20.479 0.31 19.57 O ANISOU 757 O AASP A 80 2600 3097 1741 -497 -29 1496 O ATOM 758 O BASP A 80 37.485 0.721 20.823 0.69 20.94 O ANISOU 758 O BASP A 80 3604 2598 1755 -1160 -230 758 O ATOM 759 CB AASP A 80 38.946 2.962 19.427 0.31 22.62 C ANISOU 759 CB AASP A 80 2687 2971 2937 -866 -13 894 C ATOM 760 CB BASP A 80 39.201 3.048 19.135 0.69 24.01 C ANISOU 760 CB BASP A 80 3294 3027 2803 -940 397 863 C ATOM 761 CG AASP A 80 40.066 3.580 18.625 0.31 27.10 C ANISOU 761 CG AASP A 80 3328 3370 3599 -1293 275 1170 C ATOM 762 CG BASP A 80 40.668 3.143 18.763 0.69 27.04 C ANISOU 762 CG BASP A 80 3183 3305 3788 -1013 168 1006 C ATOM 763 OD1AASP A 80 40.996 2.825 18.247 0.31 33.96 O ANISOU 763 OD1AASP A 80 4381 4338 4186 -1007 1858 1178 O ATOM 764 OD1BASP A 80 41.381 2.111 18.795 0.69 31.66 O ANISOU 764 OD1BASP A 80 3910 4307 3814 15 648 1077 O ATOM 765 OD2AASP A 80 39.998 4.801 18.366 0.31 32.20 O ANISOU 765 OD2AASP A 80 3240 3660 5336 -1658 -953 2055 O ATOM 766 OD2BASP A 80 41.056 4.293 18.426 0.69 36.98 O ANISOU 766 OD2BASP A 80 3670 4041 6339 -1775 -124 1974 O ATOM 767 N ASER A 81 36.268 1.625 19.339 0.46 19.08 N ANISOU 767 N ASER A 81 2725 2279 2245 -101 445 1158 N ATOM 768 N BSER A 81 36.239 1.651 19.236 0.54 18.78 N ANISOU 768 N BSER A 81 2732 2323 2078 -89 436 573 N ATOM 769 CA ASER A 81 34.956 1.250 19.875 0.46 21.04 C ANISOU 769 CA ASER A 81 2894 3098 2001 137 915 945 C ATOM 770 CA BSER A 81 35.029 1.241 19.972 0.54 20.47 C ANISOU 770 CA BSER A 81 3003 2823 1952 394 856 847 C ATOM 771 C ASER A 81 34.755 -0.249 19.855 0.46 18.93 C ANISOU 771 C ASER A 81 2163 3212 1816 -423 468 1138 C ATOM 772 C BSER A 81 34.736 -0.241 19.838 0.54 18.30 C ANISOU 772 C BSER A 81 2237 3147 1570 -336 137 890 C ATOM 773 O ASER A 81 34.410 -0.916 20.839 0.46 18.83 O ANISOU 773 O ASER A 81 1380 3584 2193 328 707 1612 O ATOM 774 O BSER A 81 34.143 -0.857 20.735 0.54 26.66 O ANISOU 774 O BSER A 81 4883 3829 1418 -1190 449 965 O ATOM 775 CB ASER A 81 33.860 1.963 19.077 0.46 22.72 C ANISOU 775 CB ASER A 81 2757 3569 2306 681 1201 870 C ATOM 776 CB BSER A 81 33.784 2.008 19.520 0.54 22.60 C ANISOU 776 CB BSER A 81 3020 3704 1861 641 548 603 C ATOM 777 OG ASER A 81 33.758 3.337 19.417 0.46 29.00 O ANISOU 777 OG ASER A 81 4470 3031 3519 328 1186 1786 O ATOM 778 OG BSER A 81 32.575 1.286 19.725 0.54 30.44 O ANISOU 778 OG BSER A 81 2898 5070 3599 778 1463 1521 O ATOM 779 N AGLU A 82 34.983 -0.836 18.675 0.56 17.40 N ANISOU 779 N AGLU A 82 1885 2823 1902 -242 365 1267 N ATOM 780 N BGLU A 82 35.125 -0.804 18.695 0.44 17.09 N ANISOU 780 N BGLU A 82 2093 2630 1770 -220 222 1011 N ATOM 781 CA AGLU A 82 34.787 -2.278 18.567 0.56 18.44 C ANISOU 781 CA AGLU A 82 2052 2867 2089 -343 34 1278 C ATOM 782 CA BGLU A 82 34.895 -2.233 18.479 0.44 16.89 C ANISOU 782 CA BGLU A 82 1780 2639 1999 -344 310 1131 C ATOM 783 C AGLU A 82 35.764 -3.020 19.467 0.56 15.59 C ANISOU 783 C AGLU A 82 2061 2449 1413 -495 -1 846 C ATOM 784 C BGLU A 82 35.763 -3.019 19.454 0.44 16.39 C ANISOU 784 C BGLU A 82 1985 2456 1787 -451 73 915 C ATOM 785 O AGLU A 82 35.429 -4.041 20.074 0.56 18.16 O ANISOU 785 O AGLU A 82 2198 3267 1436 -985 -286 1416 O ATOM 786 O BGLU A 82 35.332 -3.995 20.067 0.44 19.09 O ANISOU 786 O BGLU A 82 1952 2006 3295 -353 -148 1234 O ATOM 787 CB AGLU A 82 34.877 -2.755 17.120 0.56 20.09 C ANISOU 787 CB AGLU A 82 2656 3036 1942 -436 -702 1261 C ATOM 788 CB BGLU A 82 35.152 -2.645 17.037 0.44 19.94 C ANISOU 788 CB BGLU A 82 2811 2938 1829 -1225 -319 788 C ATOM 789 CG AGLU A 82 34.857 -4.242 17.014 0.56 27.92 C ANISOU 789 CG AGLU A 82 4915 3075 2618 -327 -745 927 C ATOM 790 CG BGLU A 82 34.127 -2.000 16.103 0.44 24.37 C ANISOU 790 CG BGLU A 82 3022 4170 2066 -259 -2 978 C ATOM 791 CD AGLU A 82 34.173 -5.034 15.954 0.56 29.69 C ANISOU 791 CD AGLU A 82 5849 3410 2021 -1405 -78 1054 C ATOM 792 CD BGLU A 82 34.581 -2.030 14.657 0.44 33.41 C ANISOU 792 CD BGLU A 82 4661 5951 2084 337 372 2087 C ATOM 793 OE1AGLU A 82 34.719 -5.035 14.827 0.56 44.98 O ANISOU 793 OE1AGLU A 82 9073 6186 1831 -2168 551 1354 O ATOM 794 OE1BGLU A 82 35.806 -2.087 14.408 0.44 39.09 O ANISOU 794 OE1BGLU A 82 4966 7677 2211 939 1029 1390 O ATOM 795 OE2AGLU A 82 33.139 -5.712 16.208 0.56 40.68 O ANISOU 795 OE2AGLU A 82 8092 4241 3123 -3386 -601 2146 O ATOM 796 OE2BGLU A 82 33.690 -1.994 13.781 0.44 43.13 O ANISOU 796 OE2BGLU A 82 5706 8682 2000 2046 -37 2183 O ATOM 797 N GLU A 83 37.002 -2.565 19.581 1.00 16.72 N ANISOU 797 N GLU A 83 2112 2400 1841 -526 -30 1127 N ATOM 798 CA GLU A 83 37.978 -3.254 20.443 1.00 17.69 C ANISOU 798 CA GLU A 83 2066 2699 1956 -517 -116 1172 C ATOM 799 C GLU A 83 37.511 -3.262 21.861 1.00 18.01 C ANISOU 799 C GLU A 83 2066 2850 1925 -858 -320 1224 C ATOM 800 O GLU A 83 37.679 -4.245 22.593 1.00 19.20 O ANISOU 800 O GLU A 83 1989 3138 2168 -987 -582 1566 O ATOM 801 CB GLU A 83 39.366 -2.565 20.362 1.00 22.30 C ANISOU 801 CB GLU A 83 2007 3831 2636 -666 -40 1685 C ATOM 802 CG GLU A 83 40.368 -3.334 21.200 1.00 21.57 C ANISOU 802 CG GLU A 83 2105 3417 2673 -515 -159 1263 C ATOM 803 CD GLU A 83 40.507 -4.806 20.825 1.00 23.03 C ANISOU 803 CD GLU A 83 2742 3612 2397 -433 -16 993 C ATOM 804 OE1 GLU A 83 40.422 -5.129 19.605 1.00 33.67 O ANISOU 804 OE1 GLU A 83 5469 4831 2492 487 -367 572 O ATOM 805 OE2 GLU A 83 40.727 -5.625 21.693 1.00 24.78 O ANISOU 805 OE2 GLU A 83 3591 3279 2544 -119 70 949 O ATOM 806 N GLU A 84 36.922 -2.184 22.331 1.00 17.67 N ANISOU 806 N GLU A 84 1895 2983 1834 -976 -201 913 N ATOM 807 CA GLU A 84 36.393 -2.147 23.682 1.00 21.94 C ANISOU 807 CA GLU A 84 3203 3444 1691 -1892 -134 449 C ATOM 808 C GLU A 84 35.289 -3.205 23.887 1.00 18.82 C ANISOU 808 C GLU A 84 2382 3203 1564 -1330 -219 705 C ATOM 809 O GLU A 84 35.201 -3.849 24.937 1.00 18.42 O ANISOU 809 O GLU A 84 2147 3311 1540 -1069 -190 732 O ATOM 810 CB GLU A 84 35.763 -0.788 24.032 1.00 27.85 C ANISOU 810 CB GLU A 84 4409 3579 2595 -2230 704 -530 C ATOM 811 CG GLU A 84 35.160 -0.722 25.422 1.00 43.83 C ANISOU 811 CG GLU A 84 7790 5464 3398 -1628 2311 -577 C ATOM 812 CD GLU A 84 34.911 0.686 25.941 1.00 60.49 C ANISOU 812 CD GLU A 84 10902 6743 5339 -891 3107 -2320 C ATOM 813 OE1 GLU A 84 34.438 1.590 25.209 1.00 72.38 O ANISOU 813 OE1 GLU A 84 15567 4550 7384 -1257 1738 -2549 O ATOM 814 OE2 GLU A 84 35.198 0.893 27.146 1.00 76.69 O ANISOU 814 OE2 GLU A 84 13858 9456 5824 -349 2500 -3710 O ATOM 815 N ALEU A 85 34.395 -3.404 22.900 0.51 16.08 N ANISOU 815 N ALEU A 85 2007 2507 1597 -717 -174 704 N ATOM 816 N BLEU A 85 34.432 -3.311 22.863 0.49 15.63 N ANISOU 816 N BLEU A 85 1889 2687 1362 -804 86 723 N ATOM 817 CA ALEU A 85 33.347 -4.417 23.071 0.51 14.30 C ANISOU 817 CA ALEU A 85 1708 2286 1439 -460 -223 461 C ATOM 818 CA BLEU A 85 33.362 -4.293 22.873 0.49 13.88 C ANISOU 818 CA BLEU A 85 1426 2519 1328 -466 -16 692 C ATOM 819 C ALEU A 85 33.902 -5.819 22.942 0.51 14.71 C ANISOU 819 C ALEU A 85 1384 2399 1806 -360 116 818 C ATOM 820 C BLEU A 85 33.936 -5.703 22.946 0.49 13.14 C ANISOU 820 C BLEU A 85 1122 2577 1295 -484 -179 692 C ATOM 821 O ALEU A 85 33.453 -6.788 23.593 0.51 13.37 O ANISOU 821 O ALEU A 85 1301 2534 1245 -383 -173 1048 O ATOM 822 O BLEU A 85 33.436 -6.503 23.790 0.49 12.75 O ANISOU 822 O BLEU A 85 1273 2333 1238 -754 -73 524 O ATOM 823 CB ALEU A 85 32.236 -4.134 22.072 0.51 14.03 C ANISOU 823 CB ALEU A 85 1535 2375 1420 -97 8 353 C ATOM 824 CB BLEU A 85 32.461 -4.102 21.657 0.49 13.53 C ANISOU 824 CB BLEU A 85 1539 2303 1298 -295 54 789 C ATOM 825 CG ALEU A 85 31.422 -2.855 22.324 0.51 15.95 C ANISOU 825 CG ALEU A 85 1423 2152 2487 -319 408 598 C ATOM 826 CG BLEU A 85 31.526 -2.880 21.772 0.49 16.24 C ANISOU 826 CG BLEU A 85 1888 2305 1978 -161 22 822 C ATOM 827 CD1ALEU A 85 30.501 -2.558 21.165 0.51 22.53 C ANISOU 827 CD1ALEU A 85 2172 2727 3660 -17 -184 1745 C ATOM 828 CD1BLEU A 85 30.995 -2.555 20.374 0.49 17.18 C ANISOU 828 CD1BLEU A 85 2277 1897 2354 -411 -200 1296 C ATOM 829 CD2ALEU A 85 30.624 -2.973 23.620 0.51 23.91 C ANISOU 829 CD2ALEU A 85 2119 3857 3107 607 1207 594 C ATOM 830 CD2BLEU A 85 30.379 -3.063 22.747 0.49 20.35 C ANISOU 830 CD2BLEU A 85 1765 4043 1925 238 104 202 C ATOM 831 N ILE A 86 34.903 -5.986 22.100 1.00 13.12 N ANISOU 831 N ILE A 86 1312 2435 1239 -417 -93 906 N ATOM 832 CA ILE A 86 35.545 -7.291 22.044 1.00 13.46 C ANISOU 832 CA ILE A 86 1233 2546 1336 -289 -150 880 C ATOM 833 C ILE A 86 36.190 -7.633 23.379 1.00 13.88 C ANISOU 833 C ILE A 86 1094 2773 1409 -515 -208 1041 C ATOM 834 O ILE A 86 36.045 -8.745 23.865 1.00 15.02 O ANISOU 834 O ILE A 86 1140 2906 1662 -595 -240 1300 O ATOM 835 CB ILE A 86 36.566 -7.272 20.878 1.00 15.15 C ANISOU 835 CB ILE A 86 1357 2987 1413 -232 -131 703 C ATOM 836 CG1 ILE A 86 35.848 -7.171 19.557 1.00 16.08 C ANISOU 836 CG1 ILE A 86 1825 2949 1336 -198 -128 849 C ATOM 837 CG2 ILE A 86 37.499 -8.447 20.991 1.00 20.40 C ANISOU 837 CG2 ILE A 86 1837 3950 1964 609 195 1157 C ATOM 838 CD1 ILE A 86 36.735 -6.895 18.340 1.00 21.08 C ANISOU 838 CD1 ILE A 86 2271 4141 1596 219 280 1196 C ATOM 839 N AGLU A 87 36.954 -6.682 23.950 0.58 15.36 N ANISOU 839 N AGLU A 87 1496 2904 1434 -645 -261 1059 N ATOM 840 N BGLU A 87 36.901 -6.664 23.966 0.42 15.08 N ANISOU 840 N BGLU A 87 1240 3063 1425 -794 -241 1171 N ATOM 841 CA AGLU A 87 37.572 -7.046 25.234 0.58 16.18 C ANISOU 841 CA AGLU A 87 1191 3410 1545 -954 -377 1121 C ATOM 842 CA BGLU A 87 37.573 -6.752 25.256 0.42 16.41 C ANISOU 842 CA BGLU A 87 1295 3503 1436 -1072 -285 1162 C ATOM 843 C AGLU A 87 36.497 -7.342 26.257 0.58 15.63 C ANISOU 843 C AGLU A 87 1305 3228 1406 -1153 -386 912 C ATOM 844 C BGLU A 87 36.635 -7.115 26.393 0.42 16.66 C ANISOU 844 C BGLU A 87 1329 3600 1402 -1065 -334 1158 C ATOM 845 O AGLU A 87 36.682 -8.390 26.920 0.58 16.03 O ANISOU 845 O AGLU A 87 1356 3575 1160 -1162 -556 1091 O ATOM 846 O BGLU A 87 36.851 -7.899 27.331 0.42 17.33 O ANISOU 846 O BGLU A 87 1195 4357 1033 -1221 -538 1223 O ATOM 847 CB AGLU A 87 38.543 -5.950 25.674 0.58 15.05 C ANISOU 847 CB AGLU A 87 1304 2626 1790 -719 -284 1136 C ATOM 848 CB BGLU A 87 38.255 -5.414 25.567 0.42 15.91 C ANISOU 848 CB BGLU A 87 1403 3238 1406 -861 -424 1275 C ATOM 849 CG AGLU A 87 39.697 -5.821 24.693 0.58 14.59 C ANISOU 849 CG AGLU A 87 1134 2448 1962 -581 -215 692 C ATOM 850 CG BGLU A 87 39.510 -5.150 24.746 0.42 15.55 C ANISOU 850 CG BGLU A 87 1595 2673 1639 -972 -132 856 C ATOM 851 CD AGLU A 87 40.474 -4.530 24.875 0.58 17.38 C ANISOU 851 CD AGLU A 87 1425 2506 2673 -745 122 595 C ATOM 852 CD BGLU A 87 40.561 -6.203 25.066 0.42 19.53 C ANISOU 852 CD BGLU A 87 1502 3174 2744 -790 -277 885 C ATOM 853 OE1AGLU A 87 41.462 -4.360 24.170 0.58 20.46 O ANISOU 853 OE1AGLU A 87 1387 2698 3689 -643 460 697 O ATOM 854 OE1BGLU A 87 40.459 -7.347 24.568 0.42 19.23 O ANISOU 854 OE1BGLU A 87 1428 3529 2347 -56 -375 438 O ATOM 855 OE2AGLU A 87 40.031 -3.721 25.713 0.58 30.39 O ANISOU 855 OE2AGLU A 87 3318 4215 4014 -2508 1535 -1385 O ATOM 856 OE2BGLU A 87 41.465 -5.816 25.849 0.42 27.40 O ANISOU 856 OE2BGLU A 87 2109 3510 4790 -656 -1450 524 O ATOM 857 N ALA A 88 35.471 -6.502 26.341 1.00 16.65 N ANISOU 857 N ALA A 88 1331 3482 1513 -1077 -273 959 N ATOM 858 CA ALA A 88 34.431 -6.809 27.355 1.00 16.77 C ANISOU 858 CA ALA A 88 1570 3570 1232 -1122 -176 644 C ATOM 859 C ALA A 88 33.833 -8.185 27.133 1.00 15.56 C ANISOU 859 C ALA A 88 1246 3455 1209 -1011 -228 859 C ATOM 860 O ALA A 88 33.648 -8.970 28.086 1.00 17.40 O ANISOU 860 O ALA A 88 1458 3811 1341 -992 -224 1094 O ATOM 861 CB ALA A 88 33.381 -5.723 27.338 1.00 17.83 C ANISOU 861 CB ALA A 88 1839 3552 1383 -984 -174 418 C ATOM 862 N PHE A 89 33.517 -8.535 25.882 1.00 14.06 N ANISOU 862 N PHE A 89 1298 2740 1303 -799 -293 941 N ATOM 863 CA PHE A 89 32.947 -9.835 25.610 1.00 12.77 C ANISOU 863 CA PHE A 89 1085 2553 1215 -389 -259 838 C ATOM 864 C PHE A 89 33.857 -10.945 26.139 1.00 14.13 C ANISOU 864 C PHE A 89 960 2828 1582 -407 -287 1115 C ATOM 865 O PHE A 89 33.395 -11.907 26.729 1.00 14.94 O ANISOU 865 O PHE A 89 1097 2949 1629 -405 -242 1404 O ATOM 866 CB PHE A 89 32.695 -9.983 24.094 1.00 11.93 C ANISOU 866 CB PHE A 89 1010 2295 1228 -225 -98 816 C ATOM 867 CG PHE A 89 32.048 -11.290 23.781 1.00 11.55 C ANISOU 867 CG PHE A 89 963 2256 1168 -220 -88 707 C ATOM 868 CD1 PHE A 89 30.666 -11.411 23.837 1.00 11.62 C ANISOU 868 CD1 PHE A 89 1016 2234 1165 -185 -135 504 C ATOM 869 CD2 PHE A 89 32.771 -12.422 23.466 1.00 14.33 C ANISOU 869 CD2 PHE A 89 1125 2341 1978 -39 -276 772 C ATOM 870 CE1 PHE A 89 30.027 -12.604 23.616 1.00 12.36 C ANISOU 870 CE1 PHE A 89 1075 2471 1148 -297 15 187 C ATOM 871 CE2 PHE A 89 32.156 -13.650 23.215 1.00 14.55 C ANISOU 871 CE2 PHE A 89 1368 2292 1866 95 -172 474 C ATOM 872 CZ PHE A 89 30.780 -13.710 23.299 1.00 13.44 C ANISOU 872 CZ PHE A 89 1427 2357 1324 -202 -67 323 C ATOM 873 N ALYS A 90 35.160 -10.937 25.756 0.51 14.25 N ANISOU 873 N ALYS A 90 1000 2629 1783 -387 -294 1324 N ATOM 874 N BLYS A 90 35.152 -10.616 26.002 0.49 16.06 N ANISOU 874 N BLYS A 90 992 3095 2015 -523 -406 1443 N ATOM 875 CA ALYS A 90 36.035 -12.103 25.959 0.51 11.05 C ANISOU 875 CA ALYS A 90 833 2218 1145 -635 -471 570 C ATOM 876 CA BLYS A 90 36.158 -11.518 26.548 0.49 12.55 C ANISOU 876 CA BLYS A 90 973 2491 1304 -483 -609 325 C ATOM 877 C ALYS A 90 36.248 -12.375 27.440 0.51 10.13 C ANISOU 877 C ALYS A 90 957 1731 1161 -427 -257 543 C ATOM 878 C BLYS A 90 36.204 -11.508 28.066 0.49 12.04 C ANISOU 878 C BLYS A 90 1140 2147 1287 -368 -404 358 C ATOM 879 O ALYS A 90 36.521 -13.495 27.856 0.51 11.17 O ANISOU 879 O ALYS A 90 1197 1754 1291 -191 -199 575 O ATOM 880 O BLYS A 90 36.588 -12.574 28.590 0.49 13.23 O ANISOU 880 O BLYS A 90 1462 2211 1356 -80 -350 333 O ATOM 881 CB ALYS A 90 37.404 -11.881 25.285 0.51 11.72 C ANISOU 881 CB ALYS A 90 1134 1961 1358 -569 -129 621 C ATOM 882 CB BLYS A 90 37.483 -11.168 25.839 0.49 12.67 C ANISOU 882 CB BLYS A 90 1100 2245 1469 -352 -337 557 C ATOM 883 CG ALYS A 90 37.407 -12.124 23.785 0.51 12.34 C ANISOU 883 CG ALYS A 90 1478 1716 1495 -129 54 329 C ATOM 884 CG BLYS A 90 37.399 -11.451 24.324 0.49 13.60 C ANISOU 884 CG BLYS A 90 1416 2275 1478 -94 -399 438 C ATOM 885 CD ALYS A 90 38.709 -12.002 23.064 0.51 13.23 C ANISOU 885 CD ALYS A 90 1302 2276 1450 77 -61 627 C ATOM 886 CD BLYS A 90 38.717 -11.466 23.627 0.49 16.28 C ANISOU 886 CD BLYS A 90 1485 2944 1756 610 -315 -365 C ATOM 887 CE ALYS A 90 39.474 -10.740 23.409 0.51 13.05 C ANISOU 887 CE ALYS A 90 1364 2280 1313 -57 187 647 C ATOM 888 CE BLYS A 90 38.927 -11.329 22.150 0.49 18.73 C ANISOU 888 CE BLYS A 90 1043 3839 2235 269 -50 1178 C ATOM 889 NZ ALYS A 90 40.837 -10.800 22.749 0.51 16.79 N ANISOU 889 NZ ALYS A 90 1285 2972 2125 -130 173 -124 N ATOM 890 NZ BLYS A 90 40.351 -10.847 21.932 0.49 25.86 N ANISOU 890 NZ BLYS A 90 1530 3153 5143 -308 121 2315 N ATOM 891 N AVAL A 91 36.145 -11.311 28.232 0.54 10.86 N ANISOU 891 N AVAL A 91 1108 1839 1180 -44 -174 494 N ATOM 892 N BVAL A 91 35.822 -10.469 28.795 0.46 10.85 N ANISOU 892 N BVAL A 91 1010 1999 1113 -381 -227 661 N ATOM 893 CA AVAL A 91 36.129 -11.496 29.681 0.54 12.30 C ANISOU 893 CA AVAL A 91 1184 2329 1159 -472 -224 374 C ATOM 894 CA BVAL A 91 35.761 -10.569 30.264 0.46 12.13 C ANISOU 894 CA BVAL A 91 1311 2224 1073 -757 -417 497 C ATOM 895 C AVAL A 91 34.863 -12.223 30.115 0.54 10.49 C ANISOU 895 C AVAL A 91 1192 1776 1019 -295 -273 379 C ATOM 896 C BVAL A 91 34.662 -11.546 30.671 0.46 10.23 C ANISOU 896 C BVAL A 91 1029 2007 850 -490 -155 281 C ATOM 897 O AVAL A 91 34.974 -13.144 30.907 0.54 12.54 O ANISOU 897 O AVAL A 91 1328 2130 1308 -59 -94 639 O ATOM 898 O BVAL A 91 34.861 -12.339 31.582 0.46 11.23 O ANISOU 898 O BVAL A 91 1027 2066 1173 -279 -132 524 O ATOM 899 CB AVAL A 91 36.205 -10.131 30.406 0.54 15.43 C ANISOU 899 CB AVAL A 91 2152 2441 1270 -1063 -298 299 C ATOM 900 CB BVAL A 91 35.560 -9.202 30.952 0.46 14.00 C ANISOU 900 CB BVAL A 91 1867 2278 1175 -1031 -421 313 C ATOM 901 CG1AVAL A 91 36.067 -10.255 31.897 0.54 16.63 C ANISOU 901 CG1AVAL A 91 2523 2603 1193 -887 -655 214 C ATOM 902 CG1BVAL A 91 35.295 -9.281 32.447 0.46 13.53 C ANISOU 902 CG1BVAL A 91 1448 2280 1411 -381 84 489 C ATOM 903 CG2AVAL A 91 37.528 -9.488 30.145 0.54 19.00 C ANISOU 903 CG2AVAL A 91 2257 3032 1930 -1408 -1037 1129 C ATOM 904 CG2BVAL A 91 36.776 -8.320 30.715 0.46 12.49 C ANISOU 904 CG2BVAL A 91 1587 1900 1256 -544 -31 281 C ATOM 905 N APHE A 92 33.682 -11.744 29.707 0.61 12.36 N ANISOU 905 N APHE A 92 1106 2092 1499 -261 -130 721 N ATOM 906 N BPHE A 92 33.513 -11.548 29.994 0.39 10.92 N ANISOU 906 N BPHE A 92 1024 2032 1092 -440 -217 428 N ATOM 907 CA APHE A 92 32.450 -12.437 30.120 0.61 11.45 C ANISOU 907 CA APHE A 92 1136 1949 1265 -269 -54 605 C ATOM 908 CA BPHE A 92 32.393 -12.450 30.271 0.39 10.60 C ANISOU 908 CA BPHE A 92 930 1907 1191 -375 -265 535 C ATOM 909 C APHE A 92 32.549 -13.906 29.746 0.61 11.15 C ANISOU 909 C APHE A 92 971 1961 1304 -54 -131 612 C ATOM 910 C BPHE A 92 32.477 -13.848 29.679 0.39 12.57 C ANISOU 910 C BPHE A 92 1403 1699 1674 -300 498 697 C ATOM 911 O APHE A 92 32.163 -14.813 30.485 0.61 11.44 O ANISOU 911 O APHE A 92 1447 1872 1029 -135 -22 342 O ATOM 912 O BPHE A 92 31.933 -14.773 30.312 0.39 11.82 O ANISOU 912 O BPHE A 92 724 1752 2017 76 276 1099 O ATOM 913 CB APHE A 92 31.204 -11.809 29.509 0.61 10.42 C ANISOU 913 CB APHE A 92 1122 1604 1234 -334 -60 552 C ATOM 914 CB BPHE A 92 31.053 -11.829 29.827 0.39 11.10 C ANISOU 914 CB BPHE A 92 982 2239 996 -87 -154 317 C ATOM 915 CG APHE A 92 30.753 -10.562 30.253 0.61 9.76 C ANISOU 915 CG APHE A 92 975 1702 1033 -420 -114 565 C ATOM 916 CG BPHE A 92 30.664 -10.627 30.690 0.39 13.48 C ANISOU 916 CG BPHE A 92 1590 2043 1487 -180 534 388 C ATOM 917 CD1APHE A 92 30.155 -10.652 31.512 0.61 15.09 C ANISOU 917 CD1APHE A 92 1930 2347 1455 -189 508 562 C ATOM 918 CD1BPHE A 92 29.916 -10.760 31.865 0.39 12.69 C ANISOU 918 CD1BPHE A 92 1584 2366 871 -489 77 313 C ATOM 919 CD2APHE A 92 30.897 -9.305 29.742 0.61 13.83 C ANISOU 919 CD2APHE A 92 2252 1610 1393 -266 374 413 C ATOM 920 CD2BPHE A 92 31.075 -9.370 30.280 0.39 15.00 C ANISOU 920 CD2BPHE A 92 2325 2124 1251 -121 528 620 C ATOM 921 CE1APHE A 92 29.732 -9.504 32.177 0.61 16.83 C ANISOU 921 CE1APHE A 92 2282 2459 1654 -781 662 28 C ATOM 922 CE1BPHE A 92 29.591 -9.608 32.569 0.39 14.82 C ANISOU 922 CE1BPHE A 92 1914 2619 1099 -646 408 69 C ATOM 923 CE2APHE A 92 30.502 -8.167 30.380 0.61 15.51 C ANISOU 923 CE2APHE A 92 2475 1802 1615 -186 354 192 C ATOM 924 CE2BPHE A 92 30.746 -8.238 30.995 0.39 13.96 C ANISOU 924 CE2BPHE A 92 2096 2011 1197 -439 -26 441 C ATOM 925 CZ APHE A 92 29.879 -8.270 31.609 0.61 16.56 C ANISOU 925 CZ APHE A 92 2536 2307 1449 -425 296 -40 C ATOM 926 CZ BPHE A 92 29.986 -8.372 32.141 0.39 14.31 C ANISOU 926 CZ BPHE A 92 1788 2416 1235 -543 -9 -42 C ATOM 927 N ASP A 93 33.054 -14.137 28.512 1.00 12.14 N ANISOU 927 N ASP A 93 1167 2049 1395 -71 175 666 N ATOM 928 CA ASP A 93 33.108 -15.474 27.968 1.00 12.43 C ANISOU 928 CA ASP A 93 1247 2123 1354 -39 122 665 C ATOM 929 C ASP A 93 34.299 -16.248 28.524 1.00 13.83 C ANISOU 929 C ASP A 93 1291 2353 1610 184 228 687 C ATOM 930 O ASP A 93 35.365 -16.416 27.925 1.00 16.02 O ANISOU 930 O ASP A 93 1507 2697 1880 439 454 867 O ATOM 931 CB ASP A 93 33.220 -15.399 26.440 1.00 13.55 C ANISOU 931 CB ASP A 93 1486 2293 1369 160 302 572 C ATOM 932 CG ASP A 93 33.299 -16.766 25.770 1.00 14.63 C ANISOU 932 CG ASP A 93 1496 2353 1710 412 469 508 C ATOM 933 OD1 ASP A 93 32.902 -17.725 26.409 1.00 16.02 O ANISOU 933 OD1 ASP A 93 2107 2261 1719 272 536 437 O ATOM 934 OD2 ASP A 93 33.756 -16.820 24.604 1.00 15.56 O ANISOU 934 OD2 ASP A 93 1473 2860 1579 352 461 286 O ATOM 935 N ARG A 94 34.136 -16.706 29.792 1.00 13.44 N ANISOU 935 N ARG A 94 1242 2283 1583 56 92 728 N ATOM 936 CA ARG A 94 35.261 -17.201 30.584 1.00 15.05 C ANISOU 936 CA ARG A 94 1367 2183 2169 144 27 1015 C ATOM 937 C ARG A 94 35.967 -18.368 29.930 1.00 15.88 C ANISOU 937 C ARG A 94 1238 2324 2471 144 223 1088 C ATOM 938 O ARG A 94 37.204 -18.484 30.059 1.00 19.56 O ANISOU 938 O ARG A 94 1205 2765 3460 191 153 957 O ATOM 939 CB ARG A 94 34.779 -17.552 31.990 1.00 16.59 C ANISOU 939 CB ARG A 94 1446 2919 1939 400 -235 1074 C ATOM 940 CG ARG A 94 34.216 -16.398 32.818 1.00 19.74 C ANISOU 940 CG ARG A 94 1877 3312 2311 603 195 934 C ATOM 941 CD ARG A 94 33.862 -16.888 34.231 1.00 21.05 C ANISOU 941 CD ARG A 94 2643 3292 2062 527 -112 822 C ATOM 942 NE ARG A 94 35.044 -17.164 35.019 1.00 23.55 N ANISOU 942 NE ARG A 94 2107 4210 2632 719 246 1468 N ATOM 943 CZ ARG A 94 35.279 -18.159 35.849 1.00 24.35 C ANISOU 943 CZ ARG A 94 3906 3048 2298 436 -1420 379 C ATOM 944 NH1 ARG A 94 34.386 -19.122 36.089 1.00 39.46 N ANISOU 944 NH1 ARG A 94 3733 3266 7995 1083 -176 2508 N ATOM 945 NH2 ARG A 94 36.442 -18.178 36.481 1.00 31.24 N ANISOU 945 NH2 ARG A 94 3266 5241 3362 2173 -980 9 N ATOM 946 N ASP A 95 35.262 -19.269 29.271 1.00 15.98 N ANISOU 946 N ASP A 95 1283 2485 2302 450 233 680 N ATOM 947 CA ASP A 95 35.906 -20.421 28.638 1.00 17.81 C ANISOU 947 CA ASP A 95 1461 2757 2550 912 129 644 C ATOM 948 C ASP A 95 36.289 -20.205 27.175 1.00 19.22 C ANISOU 948 C ASP A 95 1983 2782 2538 1077 188 514 C ATOM 949 O ASP A 95 36.813 -21.108 26.504 1.00 22.32 O ANISOU 949 O ASP A 95 2320 3119 3044 1393 784 545 O ATOM 950 CB ASP A 95 35.086 -21.702 28.719 1.00 19.56 C ANISOU 950 CB ASP A 95 2047 2558 2827 884 212 405 C ATOM 951 CG ASP A 95 33.776 -21.739 27.956 1.00 17.85 C ANISOU 951 CG ASP A 95 2150 2134 2497 635 191 321 C ATOM 952 OD1 ASP A 95 33.492 -20.727 27.267 1.00 17.47 O ANISOU 952 OD1 ASP A 95 2080 2218 2340 853 327 307 O ATOM 953 OD2 ASP A 95 33.072 -22.760 28.118 1.00 24.93 O ANISOU 953 OD2 ASP A 95 2982 2409 4081 130 -255 664 O ATOM 954 N GLY A 96 36.076 -19.040 26.617 1.00 17.90 N ANISOU 954 N GLY A 96 1609 2576 2618 546 722 612 N ATOM 955 CA GLY A 96 36.487 -18.732 25.243 1.00 21.74 C ANISOU 955 CA GLY A 96 1999 3674 2586 977 827 774 C ATOM 956 C GLY A 96 35.733 -19.402 24.130 1.00 22.16 C ANISOU 956 C GLY A 96 2284 3588 2547 1484 690 559 C ATOM 957 O GLY A 96 36.215 -19.335 22.988 1.00 26.10 O ANISOU 957 O GLY A 96 2654 4511 2753 1341 1031 90 O ATOM 958 N ASN A 97 34.568 -19.960 24.372 1.00 21.35 N ANISOU 958 N ASN A 97 2106 3656 2348 1487 388 276 N ATOM 959 CA ASN A 97 33.880 -20.725 23.317 1.00 21.86 C ANISOU 959 CA ASN A 97 2887 3208 2209 1524 710 -48 C ATOM 960 C ASN A 97 32.966 -19.853 22.462 1.00 20.99 C ANISOU 960 C ASN A 97 2711 3422 1840 1264 534 -73 C ATOM 961 O ASN A 97 32.316 -20.429 21.591 1.00 26.22 O ANISOU 961 O ASN A 97 4514 3535 1914 1470 15 -392 O ATOM 962 CB ASN A 97 33.174 -21.935 23.939 1.00 24.85 C ANISOU 962 CB ASN A 97 3483 2905 3055 1533 1042 -50 C ATOM 963 CG ASN A 97 31.832 -21.554 24.547 1.00 20.57 C ANISOU 963 CG ASN A 97 2913 2445 2459 1001 494 -314 C ATOM 964 OD1 ASN A 97 31.638 -20.375 24.975 1.00 17.88 O ANISOU 964 OD1 ASN A 97 2599 2306 1888 1058 216 -214 O ATOM 965 ND2 ASN A 97 30.900 -22.512 24.621 1.00 23.12 N ANISOU 965 ND2 ASN A 97 3070 2551 3164 738 -261 -719 N ATOM 966 N GLY A 98 32.971 -18.537 22.683 1.00 19.31 N ANISOU 966 N GLY A 98 2185 3205 1947 1124 608 195 N ATOM 967 CA GLY A 98 32.236 -17.597 21.873 1.00 18.47 C ANISOU 967 CA GLY A 98 2067 3271 1678 708 206 58 C ATOM 968 C GLY A 98 30.782 -17.413 22.320 1.00 15.47 C ANISOU 968 C GLY A 98 2012 2378 1488 601 229 -45 C ATOM 969 O GLY A 98 30.038 -16.711 21.667 1.00 16.46 O ANISOU 969 O GLY A 98 2143 2670 1443 448 51 145 O ATOM 970 N LEU A 99 30.420 -18.008 23.444 1.00 15.63 N ANISOU 970 N LEU A 99 1826 2666 1446 643 67 67 N ATOM 971 CA LEU A 99 29.066 -17.939 23.994 1.00 13.28 C ANISOU 971 CA LEU A 99 1757 2016 1274 540 32 45 C ATOM 972 C LEU A 99 29.151 -17.604 25.460 1.00 13.78 C ANISOU 972 C LEU A 99 1666 2286 1282 783 -31 -31 C ATOM 973 O LEU A 99 29.819 -18.349 26.199 1.00 17.25 O ANISOU 973 O LEU A 99 2758 2515 1282 1394 215 249 O ATOM 974 CB LEU A 99 28.310 -19.248 23.788 1.00 14.88 C ANISOU 974 CB LEU A 99 2160 1745 1748 583 229 -85 C ATOM 975 CG LEU A 99 28.083 -19.739 22.366 1.00 16.59 C ANISOU 975 CG LEU A 99 1884 2513 1906 440 28 -321 C ATOM 976 CD1 LEU A 99 27.464 -21.132 22.354 1.00 23.60 C ANISOU 976 CD1 LEU A 99 3195 2305 3465 451 -502 -893 C ATOM 977 CD2 LEU A 99 27.172 -18.819 21.607 1.00 18.10 C ANISOU 977 CD2 LEU A 99 1923 3040 1915 424 26 8 C ATOM 978 N AILE A 100 28.538 -16.516 25.902 0.90 10.61 N ANISOU 978 N AILE A 100 1296 1742 994 255 -37 125 N ATOM 979 N BILE A 100 28.470 -16.544 25.873 0.09 10.69 N ANISOU 979 N BILE A 100 1055 1795 1211 262 -14 105 N ATOM 980 CA AILE A 100 28.485 -16.246 27.333 0.90 9.81 C ANISOU 980 CA AILE A 100 1142 1653 933 154 -36 88 C ATOM 981 CA BILE A 100 28.350 -16.259 27.295 0.09 9.32 C ANISOU 981 CA BILE A 100 801 1536 1204 167 -33 110 C ATOM 982 C AILE A 100 27.322 -17.050 27.872 0.90 9.50 C ANISOU 982 C AILE A 100 1237 1444 928 -70 -177 -20 C ATOM 983 C BILE A 100 27.232 -17.098 27.891 0.09 8.80 C ANISOU 983 C BILE A 100 906 1362 1075 -63 -252 3 C ATOM 984 O AILE A 100 26.158 -16.850 27.474 0.90 10.13 O ANISOU 984 O AILE A 100 1305 1502 1043 -3 -210 115 O ATOM 985 O BILE A 100 26.055 -16.970 27.549 0.09 9.08 O ANISOU 985 O BILE A 100 866 1423 1163 -25 -237 -247 O ATOM 986 CB AILE A 100 28.273 -14.768 27.612 0.90 9.13 C ANISOU 986 CB AILE A 100 932 1553 985 -18 -59 172 C ATOM 987 CB BILE A 100 28.064 -14.777 27.575 0.09 9.74 C ANISOU 987 CB BILE A 100 953 1393 1354 -98 -238 127 C ATOM 988 CG1AILE A 100 29.339 -13.864 27.005 0.90 10.36 C ANISOU 988 CG1AILE A 100 930 1873 1134 -5 -91 364 C ATOM 989 CG1BILE A 100 29.238 -13.874 27.184 0.09 10.04 C ANISOU 989 CG1BILE A 100 1082 1825 907 -244 -205 309 C ATOM 990 CG2AILE A 100 28.137 -14.537 29.108 0.90 9.18 C ANISOU 990 CG2AILE A 100 880 1538 1070 -211 -26 76 C ATOM 991 CG2BILE A 100 27.660 -14.567 29.020 0.09 6.20 C ANISOU 991 CG2BILE A 100 -109 1021 1444 -145 -327 65 C ATOM 992 CD1AILE A 100 28.949 -12.423 26.938 0.90 10.75 C ANISOU 992 CD1AILE A 100 1241 1735 1109 -136 -196 430 C ATOM 993 CD1BILE A 100 30.524 -14.681 27.121 0.09 17.34 C ANISOU 993 CD1BILE A 100 1137 3066 2385 194 324 1969 C ATOM 994 N SER A 101 27.617 -17.988 28.811 1.00 9.89 N ANISOU 994 N SER A 101 1199 1393 1166 70 -184 49 N ATOM 995 CA SER A 101 26.572 -18.758 29.475 1.00 10.27 C ANISOU 995 CA SER A 101 1393 1349 1158 -150 -287 71 C ATOM 996 C SER A 101 26.039 -18.034 30.674 1.00 9.74 C ANISOU 996 C SER A 101 1246 1387 1068 -240 -230 132 C ATOM 997 O SER A 101 26.607 -17.067 31.197 1.00 9.49 O ANISOU 997 O SER A 101 1092 1401 1114 -300 -188 68 O ATOM 998 CB SER A 101 27.165 -20.108 29.887 1.00 12.14 C ANISOU 998 CB SER A 101 1618 1398 1598 -171 -292 48 C ATOM 999 OG SER A 101 28.049 -19.890 30.983 1.00 11.29 O ANISOU 999 OG SER A 101 1516 1356 1417 -119 -310 269 O ATOM 1000 N ALA A 102 24.902 -18.528 31.178 1.00 10.81 N ANISOU 1000 N ALA A 102 1387 1535 1185 -576 -204 82 N ATOM 1001 CA ALA A 102 24.374 -18.005 32.427 1.00 10.69 C ANISOU 1001 CA ALA A 102 1240 1619 1200 -452 -181 167 C ATOM 1002 C ALA A 102 25.383 -18.132 33.574 1.00 10.27 C ANISOU 1002 C ALA A 102 1139 1620 1142 -513 -111 231 C ATOM 1003 O ALA A 102 25.510 -17.211 34.399 1.00 11.11 O ANISOU 1003 O ALA A 102 1330 1795 1097 -464 -91 94 O ATOM 1004 CB ALA A 102 23.071 -18.711 32.730 1.00 13.52 C ANISOU 1004 CB ALA A 102 1044 2527 1565 -573 -190 10 C ATOM 1005 N ALA A 103 26.078 -19.251 33.669 1.00 11.12 N ANISOU 1005 N ALA A 103 1428 1503 1295 -491 -242 334 N ATOM 1006 CA ALA A 103 27.044 -19.412 34.744 1.00 11.64 C ANISOU 1006 CA ALA A 103 1386 1750 1286 -517 -186 434 C ATOM 1007 C ALA A 103 28.186 -18.414 34.623 1.00 9.77 C ANISOU 1007 C ALA A 103 1248 1340 1124 -223 -212 511 C ATOM 1008 O ALA A 103 28.620 -17.809 35.617 1.00 10.63 O ANISOU 1008 O ALA A 103 1336 1610 1093 -417 -268 425 O ATOM 1009 CB ALA A 103 27.572 -20.847 34.756 1.00 14.26 C ANISOU 1009 CB ALA A 103 1862 1563 1992 -653 -574 729 C ATOM 1010 N GLU A 104 28.647 -18.214 33.408 1.00 9.68 N ANISOU 1010 N GLU A 104 1191 1358 1129 -361 -143 303 N ATOM 1011 CA GLU A 104 29.733 -17.224 33.187 1.00 9.38 C ANISOU 1011 CA GLU A 104 985 1418 1161 -202 -98 364 C ATOM 1012 C GLU A 104 29.282 -15.833 33.521 1.00 9.15 C ANISOU 1012 C GLU A 104 1026 1359 1091 -259 -114 273 C ATOM 1013 O GLU A 104 29.995 -15.072 34.194 1.00 10.22 O ANISOU 1013 O GLU A 104 1244 1476 1164 -422 -297 300 O ATOM 1014 CB GLU A 104 30.184 -17.298 31.725 1.00 9.64 C ANISOU 1014 CB GLU A 104 1132 1332 1199 -152 -15 327 C ATOM 1015 CG GLU A 104 30.993 -18.518 31.406 1.00 11.21 C ANISOU 1015 CG GLU A 104 1193 1549 1518 122 94 486 C ATOM 1016 CD GLU A 104 31.281 -18.734 29.941 1.00 12.08 C ANISOU 1016 CD GLU A 104 1384 1670 1535 381 235 479 C ATOM 1017 OE1 GLU A 104 30.537 -18.227 29.084 1.00 11.43 O ANISOU 1017 OE1 GLU A 104 1428 1557 1356 204 -25 245 O ATOM 1018 OE2 GLU A 104 32.279 -19.456 29.640 1.00 14.06 O ANISOU 1018 OE2 GLU A 104 1542 2084 1717 649 202 510 O ATOM 1019 N LEU A 105 28.110 -15.456 33.036 1.00 9.14 N ANISOU 1019 N LEU A 105 1126 1273 1075 -221 -248 201 N ATOM 1020 CA LEU A 105 27.597 -14.119 33.312 1.00 9.41 C ANISOU 1020 CA LEU A 105 1242 1290 1042 -239 -204 222 C ATOM 1021 C LEU A 105 27.441 -13.890 34.810 1.00 9.46 C ANISOU 1021 C LEU A 105 1179 1309 1105 -260 -245 177 C ATOM 1022 O LEU A 105 27.818 -12.847 35.342 1.00 10.16 O ANISOU 1022 O LEU A 105 1523 1273 1064 -319 -332 243 O ATOM 1023 CB LEU A 105 26.258 -13.914 32.583 1.00 9.91 C ANISOU 1023 CB LEU A 105 1334 1433 999 -132 -220 189 C ATOM 1024 CG LEU A 105 25.613 -12.573 32.772 1.00 10.76 C ANISOU 1024 CG LEU A 105 1403 1625 1058 54 -141 231 C ATOM 1025 CD1 LEU A 105 26.540 -11.423 32.394 1.00 11.78 C ANISOU 1025 CD1 LEU A 105 1617 1493 1365 -77 -113 312 C ATOM 1026 CD2 LEU A 105 24.310 -12.489 31.952 1.00 12.76 C ANISOU 1026 CD2 LEU A 105 1580 1713 1555 -10 -506 216 C ATOM 1027 N ARG A 106 26.895 -14.883 35.508 1.00 9.22 N ANISOU 1027 N ARG A 106 1224 1234 1043 -231 -173 136 N ATOM 1028 CA ARG A 106 26.719 -14.722 36.953 1.00 9.65 C ANISOU 1028 CA ARG A 106 1425 1214 1027 -229 -228 160 C ATOM 1029 C ARG A 106 28.056 -14.566 37.655 1.00 9.45 C ANISOU 1029 C ARG A 106 1550 1164 878 -290 -212 202 C ATOM 1030 O ARG A 106 28.210 -13.758 38.572 1.00 10.64 O ANISOU 1030 O ARG A 106 1605 1354 1083 -341 -257 38 O ATOM 1031 CB ARG A 106 25.870 -15.881 37.488 1.00 9.92 C ANISOU 1031 CB ARG A 106 1580 1118 1071 -245 -105 45 C ATOM 1032 CG ARG A 106 25.440 -15.634 38.915 1.00 11.16 C ANISOU 1032 CG ARG A 106 1712 1444 1085 -441 -125 16 C ATOM 1033 CD ARG A 106 24.342 -16.590 39.346 1.00 11.19 C ANISOU 1033 CD ARG A 106 1669 1292 1290 -276 83 91 C ATOM 1034 NE ARG A 106 24.571 -17.943 39.133 1.00 12.34 N ANISOU 1034 NE ARG A 106 1841 1334 1514 -297 -164 218 N ATOM 1035 CZ ARG A 106 25.209 -18.729 39.967 1.00 12.70 C ANISOU 1035 CZ ARG A 106 1914 1616 1296 1 -77 248 C ATOM 1036 NH1 ARG A 106 25.783 -18.243 41.075 1.00 13.78 N ANISOU 1036 NH1 ARG A 106 1710 2065 1461 -61 -148 267 N ATOM 1037 NH2 ARG A 106 25.363 -20.040 39.717 1.00 18.51 N ANISOU 1037 NH2 ARG A 106 3315 1395 2324 -102 -613 491 N ATOM 1038 N AHIS A 107 29.019 -15.368 37.207 0.34 8.71 N ANISOU 1038 N AHIS A 107 1338 1275 698 -394 -167 278 N ATOM 1039 N BHIS A 107 29.054 -15.396 37.312 0.66 10.87 N ANISOU 1039 N BHIS A 107 1564 1243 1322 -137 -313 89 N ATOM 1040 CA AHIS A 107 30.341 -15.358 37.814 0.34 10.82 C ANISOU 1040 CA AHIS A 107 1341 1812 957 -526 -254 99 C ATOM 1041 CA BHIS A 107 30.352 -15.252 37.989 0.66 10.92 C ANISOU 1041 CA BHIS A 107 1699 1429 1020 -78 -407 103 C ATOM 1042 C AHIS A 107 31.077 -14.031 37.693 0.34 12.08 C ANISOU 1042 C AHIS A 107 1434 1933 1225 -608 -250 220 C ATOM 1043 C BHIS A 107 30.956 -13.870 37.775 0.66 11.22 C ANISOU 1043 C BHIS A 107 1529 1508 1228 -114 -458 152 C ATOM 1044 O AHIS A 107 31.706 -13.553 38.647 0.34 10.34 O ANISOU 1044 O AHIS A 107 1185 1313 1430 -333 -574 536 O ATOM 1045 O BHIS A 107 31.380 -13.167 38.696 0.66 11.35 O ANISOU 1045 O BHIS A 107 1425 1552 1338 32 -565 -22 O ATOM 1046 CB AHIS A 107 31.184 -16.457 37.142 0.34 11.82 C ANISOU 1046 CB AHIS A 107 1495 1992 1002 -49 -738 143 C ATOM 1047 CB BHIS A 107 31.290 -16.355 37.492 0.66 11.21 C ANISOU 1047 CB BHIS A 107 1582 1529 1148 -119 -360 0 C ATOM 1048 CG AHIS A 107 32.441 -16.649 37.944 0.34 14.84 C ANISOU 1048 CG AHIS A 107 1867 1761 2012 -231 -1208 429 C ATOM 1049 CG BHIS A 107 32.739 -16.176 37.885 0.66 13.34 C ANISOU 1049 CG BHIS A 107 1600 1881 1588 -106 -497 320 C ATOM 1050 ND1AHIS A 107 33.504 -15.796 37.976 0.34 15.41 N ANISOU 1050 ND1AHIS A 107 1653 2031 2172 -184 -1192 460 N ATOM 1051 ND1BHIS A 107 33.159 -16.647 39.130 0.66 16.57 N ANISOU 1051 ND1BHIS A 107 1780 2900 1615 246 -608 392 N ATOM 1052 CD2AHIS A 107 32.745 -17.648 38.805 0.34 17.00 C ANISOU 1052 CD2AHIS A 107 2150 1900 2408 -208 -1576 617 C ATOM 1053 CD2BHIS A 107 33.826 -15.605 37.308 0.66 17.50 C ANISOU 1053 CD2BHIS A 107 1734 2369 2546 -538 -846 932 C ATOM 1054 CE1AHIS A 107 34.432 -16.266 38.805 0.34 16.26 C ANISOU 1054 CE1AHIS A 107 1611 2672 1897 -226 -997 917 C ATOM 1055 CE1BHIS A 107 34.453 -16.356 39.258 0.66 16.43 C ANISOU 1055 CE1BHIS A 107 1833 2463 1946 236 -754 -2 C ATOM 1056 NE2AHIS A 107 33.988 -17.399 39.330 0.34 16.81 N ANISOU 1056 NE2AHIS A 107 1992 2032 2363 -207 -1290 511 N ATOM 1057 NE2BHIS A 107 34.900 -15.723 38.175 0.66 16.67 N ANISOU 1057 NE2BHIS A 107 1648 2367 2319 -8 -711 140 N ATOM 1058 N VAL A 108 30.977 -13.409 36.516 1.00 11.16 N ANISOU 1058 N VAL A 108 1430 1596 1215 -411 -345 99 N ATOM 1059 CA VAL A 108 31.596 -12.123 36.256 1.00 11.53 C ANISOU 1059 CA VAL A 108 1309 1750 1322 -500 -195 150 C ATOM 1060 C VAL A 108 30.769 -11.023 36.930 1.00 11.56 C ANISOU 1060 C VAL A 108 1444 1521 1426 -458 -223 204 C ATOM 1061 O VAL A 108 31.342 -10.062 37.513 1.00 12.76 O ANISOU 1061 O VAL A 108 1533 1794 1522 -642 -118 14 O ATOM 1062 CB VAL A 108 31.797 -11.899 34.755 1.00 13.24 C ANISOU 1062 CB VAL A 108 1521 2127 1382 -551 -220 254 C ATOM 1063 CG1 VAL A 108 32.393 -10.525 34.485 1.00 16.48 C ANISOU 1063 CG1 VAL A 108 2430 2328 1502 -907 -419 539 C ATOM 1064 CG2 VAL A 108 32.707 -13.012 34.228 1.00 15.11 C ANISOU 1064 CG2 VAL A 108 1690 2541 1509 -577 -41 -57 C ATOM 1065 N MET A 109 29.428 -11.088 36.943 1.00 10.64 N ANISOU 1065 N MET A 109 1487 1281 1275 -457 -182 227 N ATOM 1066 CA MET A 109 28.666 -10.046 37.624 1.00 10.52 C ANISOU 1066 CA MET A 109 1643 1102 1250 -457 -138 182 C ATOM 1067 C MET A 109 28.987 -10.007 39.125 1.00 11.37 C ANISOU 1067 C MET A 109 1689 1371 1259 -723 -241 127 C ATOM 1068 O MET A 109 29.093 -8.902 39.674 1.00 11.98 O ANISOU 1068 O MET A 109 1696 1448 1409 -648 -246 136 O ATOM 1069 CB MET A 109 27.164 -10.222 37.416 1.00 11.30 C ANISOU 1069 CB MET A 109 1620 1337 1336 -334 -275 175 C ATOM 1070 CG MET A 109 26.722 -9.953 35.979 1.00 12.45 C ANISOU 1070 CG MET A 109 1683 1642 1404 -247 -365 382 C ATOM 1071 SD MET A 109 27.062 -8.306 35.343 1.00 16.69 S ANISOU 1071 SD MET A 109 2467 1701 2175 -164 -516 573 S ATOM 1072 CE MET A 109 25.967 -7.417 36.328 1.00 21.47 C ANISOU 1072 CE MET A 109 4936 1711 1510 -375 532 174 C ATOM 1073 N THR A 110 29.187 -11.175 39.754 1.00 11.08 N ANISOU 1073 N THR A 110 1682 1393 1136 -691 -235 228 N ATOM 1074 CA THR A 110 29.596 -11.157 41.171 1.00 11.80 C ANISOU 1074 CA THR A 110 1691 1629 1161 -519 -261 55 C ATOM 1075 C THR A 110 30.881 -10.390 41.314 1.00 11.50 C ANISOU 1075 C THR A 110 1652 1411 1308 -441 -369 165 C ATOM 1076 O THR A 110 31.060 -9.583 42.258 1.00 12.59 O ANISOU 1076 O THR A 110 1734 1601 1450 -441 -469 143 O ATOM 1077 CB THR A 110 29.715 -12.619 41.665 1.00 14.17 C ANISOU 1077 CB THR A 110 2201 1864 1320 -894 -481 515 C ATOM 1078 OG1 THR A 110 28.415 -13.216 41.608 1.00 18.55 O ANISOU 1078 OG1 THR A 110 2584 2643 1822 -1402 -510 633 O ATOM 1079 CG2 THR A 110 30.144 -12.649 43.113 1.00 21.50 C ANISOU 1079 CG2 THR A 110 3647 2947 1576 -1607 -1122 922 C ATOM 1080 N AASN A 111 31.845 -10.634 40.457 0.72 11.72 N ANISOU 1080 N AASN A 111 1473 1537 1443 -487 -484 125 N ATOM 1081 N BASN A 111 31.778 -10.642 40.375 0.28 11.41 N ANISOU 1081 N BASN A 111 1573 1090 1671 -117 -238 416 N ATOM 1082 CA AASN A 111 33.111 -9.834 40.563 0.72 10.91 C ANISOU 1082 CA AASN A 111 1423 1157 1564 -216 -409 -124 C ATOM 1083 CA BASN A 111 33.114 -10.070 40.212 0.28 11.93 C ANISOU 1083 CA BASN A 111 1564 1283 1687 -165 -293 -49 C ATOM 1084 C AASN A 111 32.887 -8.368 40.312 0.72 10.52 C ANISOU 1084 C AASN A 111 1163 1266 1567 -204 -281 187 C ATOM 1085 C BASN A 111 33.055 -8.580 39.879 0.28 11.88 C ANISOU 1085 C BASN A 111 1444 1471 1600 -322 -262 550 C ATOM 1086 O AASN A 111 33.646 -7.556 40.907 0.72 12.14 O ANISOU 1086 O AASN A 111 1534 1135 1946 -241 -566 -71 O ATOM 1087 O BASN A 111 34.093 -7.890 39.997 0.28 15.67 O ANISOU 1087 O BASN A 111 1583 1638 2733 -484 -401 -54 O ATOM 1088 CB AASN A 111 34.138 -10.489 39.672 0.72 12.73 C ANISOU 1088 CB AASN A 111 1267 1689 1880 -169 -507 -402 C ATOM 1089 CB BASN A 111 33.896 -10.846 39.145 0.28 15.73 C ANISOU 1089 CB BASN A 111 1653 2340 1984 128 -155 -302 C ATOM 1090 CG AASN A 111 34.671 -11.785 40.267 0.72 15.99 C ANISOU 1090 CG AASN A 111 1335 1742 2997 198 -650 -333 C ATOM 1091 CG BASN A 111 35.370 -10.896 39.477 0.28 19.65 C ANISOU 1091 CG BASN A 111 1390 2986 3089 -487 243 -218 C ATOM 1092 OD1AASN A 111 35.190 -12.663 39.560 0.72 19.42 O ANISOU 1092 OD1AASN A 111 1830 2230 3317 324 -760 -719 O ATOM 1093 OD1BASN A 111 35.791 -10.030 40.232 0.28 36.84 O ANISOU 1093 OD1BASN A 111 3093 5201 5705 -2046 -725 -1532 O ATOM 1094 ND2AASN A 111 34.605 -12.004 41.573 0.72 15.05 N ANISOU 1094 ND2AASN A 111 1571 1204 2942 413 -1201 -353 N ATOM 1095 ND2BASN A 111 36.139 -11.837 38.963 0.28 29.48 N ANISOU 1095 ND2BASN A 111 2146 5504 3552 1186 1321 360 N ATOM 1096 N LEU A 112 31.937 -8.018 39.487 1.00 12.23 N ANISOU 1096 N LEU A 112 1596 1354 1696 -309 -546 194 N ATOM 1097 CA LEU A 112 31.610 -6.611 39.254 1.00 12.32 C ANISOU 1097 CA LEU A 112 1326 1393 1964 -377 -453 531 C ATOM 1098 C LEU A 112 30.797 -6.029 40.410 1.00 12.84 C ANISOU 1098 C LEU A 112 1651 1205 2023 -262 -513 352 C ATOM 1099 O LEU A 112 30.411 -4.857 40.312 1.00 15.85 O ANISOU 1099 O LEU A 112 2048 1466 2510 -87 -700 268 O ATOM 1100 CB LEU A 112 30.911 -6.438 37.907 1.00 13.96 C ANISOU 1100 CB LEU A 112 1828 1567 1908 -731 -522 582 C ATOM 1101 CG LEU A 112 31.781 -6.800 36.683 1.00 16.37 C ANISOU 1101 CG LEU A 112 2403 1921 1895 -839 -328 600 C ATOM 1102 CD1 LEU A 112 30.943 -6.765 35.414 1.00 17.70 C ANISOU 1102 CD1 LEU A 112 2493 2376 1855 -242 -263 522 C ATOM 1103 CD2 LEU A 112 33.015 -5.878 36.584 1.00 23.78 C ANISOU 1103 CD2 LEU A 112 2959 3862 2215 -1852 241 270 C ATOM 1104 N GLY A 113 30.573 -6.805 41.478 1.00 12.63 N ANISOU 1104 N GLY A 113 1447 1319 2031 -538 -90 113 N ATOM 1105 CA GLY A 113 29.920 -6.340 42.661 1.00 11.96 C ANISOU 1105 CA GLY A 113 1384 1136 2024 -368 -373 -98 C ATOM 1106 C GLY A 113 28.448 -6.612 42.751 1.00 10.77 C ANISOU 1106 C GLY A 113 1437 846 1808 -400 -153 -89 C ATOM 1107 O GLY A 113 27.837 -6.080 43.670 1.00 12.21 O ANISOU 1107 O GLY A 113 1610 1251 1779 -263 -344 -325 O ATOM 1108 N GLU A 114 27.901 -7.412 41.862 1.00 10.83 N ANISOU 1108 N GLU A 114 1457 999 1659 -404 -156 -117 N ATOM 1109 CA GLU A 114 26.501 -7.716 41.763 1.00 10.90 C ANISOU 1109 CA GLU A 114 1500 1094 1547 -485 -201 -33 C ATOM 1110 C GLU A 114 26.278 -9.211 41.970 1.00 10.53 C ANISOU 1110 C GLU A 114 1542 1085 1373 -444 -186 -50 C ATOM 1111 O GLU A 114 26.577 -9.996 41.073 1.00 12.62 O ANISOU 1111 O GLU A 114 1878 1342 1576 -612 201 -378 O ATOM 1112 CB GLU A 114 25.964 -7.282 40.420 1.00 12.25 C ANISOU 1112 CB GLU A 114 1808 1359 1488 -336 -258 -4 C ATOM 1113 CG GLU A 114 26.014 -5.799 40.224 1.00 13.47 C ANISOU 1113 CG GLU A 114 2053 1422 1642 -224 -460 65 C ATOM 1114 CD GLU A 114 25.043 -5.069 41.132 1.00 13.60 C ANISOU 1114 CD GLU A 114 2043 1242 1883 -347 -355 89 C ATOM 1115 OE1 GLU A 114 25.117 -3.832 41.051 1.00 20.40 O ANISOU 1115 OE1 GLU A 114 3909 1235 2607 -2 399 186 O ATOM 1116 OE2 GLU A 114 24.254 -5.684 41.843 1.00 15.09 O ANISOU 1116 OE2 GLU A 114 1562 1634 2536 -212 -206 97 O ATOM 1117 N ALYS A 115 25.682 -9.508 43.109 0.67 10.04 N ANISOU 1117 N ALYS A 115 1489 997 1330 -278 -79 -66 N ATOM 1118 N BLYS A 115 25.797 -9.656 43.134 0.33 8.64 N ANISOU 1118 N BLYS A 115 1343 805 1135 -204 -413 -159 N ATOM 1119 CA ALYS A 115 25.405 -10.896 43.486 0.67 10.41 C ANISOU 1119 CA ALYS A 115 1692 959 1306 -327 -183 -21 C ATOM 1120 CA BLYS A 115 25.539 -11.059 43.429 0.33 8.47 C ANISOU 1120 CA BLYS A 115 1218 692 1309 133 -208 15 C ATOM 1121 C ALYS A 115 23.973 -11.208 43.054 0.67 10.09 C ANISOU 1121 C ALYS A 115 1661 1001 1172 -373 64 -337 C ATOM 1122 C BLYS A 115 24.137 -11.435 42.948 0.33 6.77 C ANISOU 1122 C BLYS A 115 1295 372 906 25 -77 180 C ATOM 1123 O ALYS A 115 23.013 -10.824 43.730 0.67 12.99 O ANISOU 1123 O ALYS A 115 1756 1448 1732 -231 197 -559 O ATOM 1124 O BLYS A 115 23.202 -11.044 43.648 0.33 5.93 O ANISOU 1124 O BLYS A 115 1110 307 835 -172 -284 37 O ATOM 1125 CB ALYS A 115 25.733 -11.038 44.979 0.67 11.16 C ANISOU 1125 CB ALYS A 115 1927 1002 1311 9 -143 -66 C ATOM 1126 CB BLYS A 115 25.545 -11.421 44.920 0.33 10.13 C ANISOU 1126 CB BLYS A 115 1638 944 1269 -217 -392 -59 C ATOM 1127 CG ALYS A 115 25.739 -12.481 45.437 0.67 11.67 C ANISOU 1127 CG ALYS A 115 1761 1024 1650 -301 -353 128 C ATOM 1128 CG BLYS A 115 26.870 -11.226 45.599 0.33 9.76 C ANISOU 1128 CG BLYS A 115 1449 1046 1215 -422 -207 174 C ATOM 1129 CD ALYS A 115 26.931 -13.306 45.018 0.67 13.90 C ANISOU 1129 CD ALYS A 115 2532 1009 1739 63 30 259 C ATOM 1130 CD BLYS A 115 26.906 -11.726 47.045 0.33 9.94 C ANISOU 1130 CD BLYS A 115 1464 1081 1233 19 -168 211 C ATOM 1131 CE ALYS A 115 26.858 -14.688 45.624 0.67 14.31 C ANISOU 1131 CE ALYS A 115 3151 841 1447 -53 -26 46 C ATOM 1132 CE BLYS A 115 28.299 -11.434 47.614 0.33 19.02 C ANISOU 1132 CE BLYS A 115 1911 3209 2106 -738 -816 1103 C ATOM 1133 NZ ALYS A 115 25.554 -15.404 45.345 0.67 17.14 N ANISOU 1133 NZ ALYS A 115 3780 702 2029 -360 -726 -209 N ATOM 1134 NZ BLYS A 115 28.347 -11.456 49.093 0.33 20.50 N ANISOU 1134 NZ BLYS A 115 1611 4085 2091 -675 -790 795 N ATOM 1135 N ALEU A 116 23.812 -11.835 41.890 0.58 8.48 N ANISOU 1135 N ALEU A 116 1437 726 1059 -335 69 -41 N ATOM 1136 N BLEU A 116 23.988 -12.078 41.810 0.41 8.29 N ANISOU 1136 N BLEU A 116 1441 783 927 50 -95 -25 N ATOM 1137 CA ALEU A 116 22.532 -12.052 41.240 0.58 8.35 C ANISOU 1137 CA ALEU A 116 1499 673 1002 -261 47 -18 C ATOM 1138 CA BLEU A 116 22.736 -12.250 41.087 0.41 8.35 C ANISOU 1138 CA BLEU A 116 1168 989 1017 -116 153 -69 C ATOM 1139 C ALEU A 116 22.152 -13.522 41.314 0.58 7.76 C ANISOU 1139 C ALEU A 116 1429 699 821 -276 -183 -41 C ATOM 1140 C BLEU A 116 22.175 -13.641 41.227 0.41 9.99 C ANISOU 1140 C BLEU A 116 1465 1053 1278 -307 293 44 C ATOM 1141 O ALEU A 116 23.021 -14.432 41.331 0.58 10.11 O ANISOU 1141 O ALEU A 116 1507 660 1672 -227 -115 7 O ATOM 1142 O BLEU A 116 22.897 -14.663 41.261 0.41 9.40 O ANISOU 1142 O BLEU A 116 1342 1057 1171 -307 -61 102 O ATOM 1143 CB ALEU A 116 22.543 -11.623 39.777 0.58 8.33 C ANISOU 1143 CB ALEU A 116 1322 824 1020 -259 171 -1 C ATOM 1144 CB BLEU A 116 22.961 -11.902 39.614 0.41 7.50 C ANISOU 1144 CB BLEU A 116 1088 782 979 -21 -15 -60 C ATOM 1145 CG ALEU A 116 22.967 -10.178 39.508 0.58 10.10 C ANISOU 1145 CG ALEU A 116 1634 887 1318 -207 207 208 C ATOM 1146 CG BLEU A 116 23.448 -10.473 39.341 0.41 10.45 C ANISOU 1146 CG BLEU A 116 2058 802 1112 -42 207 -20 C ATOM 1147 CD1ALEU A 116 23.186 -9.995 38.021 0.58 12.13 C ANISOU 1147 CD1ALEU A 116 1982 1199 1428 -88 259 483 C ATOM 1148 CD1BLEU A 116 23.731 -10.307 37.853 0.41 11.53 C ANISOU 1148 CD1BLEU A 116 1581 1712 1089 -145 -239 496 C ATOM 1149 CD2ALEU A 116 21.892 -9.242 40.010 0.58 12.56 C ANISOU 1149 CD2ALEU A 116 2014 801 1958 -52 487 282 C ATOM 1150 CD2BLEU A 116 22.427 -9.452 39.821 0.41 12.10 C ANISOU 1150 CD2BLEU A 116 1872 637 2088 -8 367 391 C ATOM 1151 N THR A 117 20.835 -13.742 41.308 1.00 8.50 N ANISOU 1151 N THR A 117 1503 777 949 -253 -177 97 N ATOM 1152 CA THR A 117 20.290 -15.094 41.300 1.00 8.53 C ANISOU 1152 CA THR A 117 1681 727 832 -396 -219 129 C ATOM 1153 C THR A 117 20.243 -15.648 39.897 1.00 8.10 C ANISOU 1153 C THR A 117 1394 824 860 -165 -208 28 C ATOM 1154 O THR A 117 20.332 -14.919 38.892 1.00 8.77 O ANISOU 1154 O THR A 117 1602 868 861 -305 -203 126 O ATOM 1155 CB THR A 117 18.875 -15.127 41.899 1.00 8.96 C ANISOU 1155 CB THR A 117 1758 796 851 -301 -145 143 C ATOM 1156 OG1 THR A 117 17.973 -14.530 40.989 1.00 9.85 O ANISOU 1156 OG1 THR A 117 1572 940 1231 -183 -98 54 O ATOM 1157 CG2 THR A 117 18.784 -14.480 43.253 1.00 10.72 C ANISOU 1157 CG2 THR A 117 2395 642 1034 -377 148 -15 C ATOM 1158 N ASP A 118 20.031 -16.969 39.790 1.00 8.45 N ANISOU 1158 N ASP A 118 1547 805 859 -324 -265 43 N ATOM 1159 CA ASP A 118 19.826 -17.590 38.493 1.00 8.68 C ANISOU 1159 CA ASP A 118 1519 977 802 -298 -152 20 C ATOM 1160 C ASP A 118 18.645 -16.980 37.745 1.00 9.14 C ANISOU 1160 C ASP A 118 1518 1012 943 -307 -288 -20 C ATOM 1161 O ASP A 118 18.727 -16.776 36.534 1.00 10.44 O ANISOU 1161 O ASP A 118 1811 1385 771 -196 -224 -3 O ATOM 1162 CB ASP A 118 19.624 -19.082 38.653 1.00 9.07 C ANISOU 1162 CB ASP A 118 1432 860 1153 -218 -213 -171 C ATOM 1163 CG ASP A 118 20.854 -19.832 39.074 1.00 9.39 C ANISOU 1163 CG ASP A 118 1383 959 1228 -147 -159 -199 C ATOM 1164 OD1 ASP A 118 21.989 -19.372 38.903 1.00 11.58 O ANISOU 1164 OD1 ASP A 118 1410 1469 1521 -351 -111 -154 O ATOM 1165 OD2 ASP A 118 20.610 -20.969 39.618 1.00 11.36 O ANISOU 1165 OD2 ASP A 118 1506 1003 1807 -53 -131 30 O ATOM 1166 N AASP A 119 17.580 -16.656 38.457 0.34 8.94 N ANISOU 1166 N AASP A 119 1346 1263 787 -291 -375 83 N ATOM 1167 N BASP A 119 17.556 -16.687 38.419 0.66 8.99 N ANISOU 1167 N BASP A 119 1574 994 849 -301 -255 51 N ATOM 1168 CA AASP A 119 16.379 -16.069 37.854 0.34 8.53 C ANISOU 1168 CA AASP A 119 1329 1254 658 -368 -324 173 C ATOM 1169 CA BASP A 119 16.428 -16.100 37.662 0.66 10.11 C ANISOU 1169 CA BASP A 119 1673 1024 1146 -150 -222 173 C ATOM 1170 C AASP A 119 16.650 -14.679 37.279 0.34 8.66 C ANISOU 1170 C AASP A 119 1060 1284 948 -181 -91 179 C ATOM 1171 C BASP A 119 16.837 -14.731 37.126 0.66 8.54 C ANISOU 1171 C BASP A 119 1176 1058 1012 -65 -257 26 C ATOM 1172 O AASP A 119 16.090 -14.294 36.242 0.34 6.57 O ANISOU 1172 O AASP A 119 537 1190 769 102 288 236 O ATOM 1173 O BASP A 119 16.543 -14.410 35.961 0.66 8.09 O ANISOU 1173 O BASP A 119 974 1327 772 53 102 151 O ATOM 1174 CB AASP A 119 15.227 -15.989 38.848 0.34 8.93 C ANISOU 1174 CB AASP A 119 1304 1075 1013 -79 -215 454 C ATOM 1175 CB BASP A 119 15.180 -16.037 38.509 0.66 11.81 C ANISOU 1175 CB BASP A 119 1420 1699 1366 -480 -278 215 C ATOM 1176 CG AASP A 119 14.437 -17.290 38.953 0.34 9.03 C ANISOU 1176 CG AASP A 119 1129 1488 815 -353 -139 -82 C ATOM 1177 CG BASP A 119 13.933 -15.929 37.672 0.66 18.19 C ANISOU 1177 CG BASP A 119 1685 3622 1605 -1125 -541 288 C ATOM 1178 OD1AASP A 119 14.661 -18.205 38.150 0.34 10.97 O ANISOU 1178 OD1AASP A 119 1409 1445 1314 -450 184 -151 O ATOM 1179 OD1BASP A 119 13.105 -15.097 37.998 0.66 32.94 O ANISOU 1179 OD1BASP A 119 3448 3365 5703 883 -3170 142 O ATOM 1180 OD2AASP A 119 13.596 -17.271 39.874 0.34 10.12 O ANISOU 1180 OD2AASP A 119 1037 1778 1030 -393 -47 13 O ATOM 1181 OD2BASP A 119 13.752 -16.725 36.715 0.66 27.56 O ANISOU 1181 OD2BASP A 119 3507 5035 1930 -2534 -831 -228 O ATOM 1182 N GLU A 120 17.489 -13.909 37.951 1.00 9.37 N ANISOU 1182 N GLU A 120 1717 909 933 -207 -145 129 N ATOM 1183 CA GLU A 120 17.926 -12.592 37.475 1.00 9.37 C ANISOU 1183 CA GLU A 120 1689 905 965 -75 -29 130 C ATOM 1184 C GLU A 120 18.822 -12.696 36.260 1.00 8.87 C ANISOU 1184 C GLU A 120 1414 1029 925 -137 -106 100 C ATOM 1185 O GLU A 120 18.641 -11.972 35.268 1.00 9.62 O ANISOU 1185 O GLU A 120 1455 1107 1094 -41 -10 270 O ATOM 1186 CB GLU A 120 18.610 -11.837 38.627 1.00 9.10 C ANISOU 1186 CB GLU A 120 1555 891 1011 -140 -9 87 C ATOM 1187 CG GLU A 120 17.670 -11.346 39.719 1.00 10.18 C ANISOU 1187 CG GLU A 120 1835 935 1097 21 -29 37 C ATOM 1188 CD GLU A 120 18.350 -10.772 40.944 1.00 9.58 C ANISOU 1188 CD GLU A 120 1841 695 1105 -53 133 6 C ATOM 1189 OE1 GLU A 120 19.423 -11.212 41.330 1.00 10.95 O ANISOU 1189 OE1 GLU A 120 2148 886 1127 -54 -282 58 O ATOM 1190 OE2 GLU A 120 17.738 -9.834 41.506 1.00 13.57 O ANISOU 1190 OE2 GLU A 120 2406 1224 1526 232 -124 -317 O ATOM 1191 N VAL A 121 19.812 -13.583 36.330 1.00 8.69 N ANISOU 1191 N VAL A 121 1449 1009 846 -127 -224 128 N ATOM 1192 CA VAL A 121 20.704 -13.740 35.193 1.00 9.39 C ANISOU 1192 CA VAL A 121 1531 1073 962 -144 -172 18 C ATOM 1193 C VAL A 121 19.965 -14.294 33.983 1.00 9.26 C ANISOU 1193 C VAL A 121 1366 1211 941 -130 -271 147 C ATOM 1194 O VAL A 121 20.222 -13.877 32.835 1.00 9.56 O ANISOU 1194 O VAL A 121 1315 1401 918 -186 -204 140 O ATOM 1195 CB VAL A 121 21.917 -14.604 35.620 1.00 11.33 C ANISOU 1195 CB VAL A 121 1448 1815 1042 31 -359 -75 C ATOM 1196 CG1 VAL A 121 22.753 -14.972 34.456 1.00 13.67 C ANISOU 1196 CG1 VAL A 121 1449 2579 1165 22 -45 10 C ATOM 1197 CG2 VAL A 121 22.759 -13.878 36.666 1.00 13.14 C ANISOU 1197 CG2 VAL A 121 1701 1894 1399 -61 -396 -289 C ATOM 1198 N ASP A 122 19.062 -15.232 34.195 1.00 9.34 N ANISOU 1198 N ASP A 122 1407 1264 877 -183 -199 55 N ATOM 1199 CA ASP A 122 18.298 -15.786 33.106 1.00 9.65 C ANISOU 1199 CA ASP A 122 1417 1402 850 -176 -260 9 C ATOM 1200 C ASP A 122 17.495 -14.706 32.394 1.00 9.66 C ANISOU 1200 C ASP A 122 1210 1510 949 -217 -212 96 C ATOM 1201 O ASP A 122 17.394 -14.682 31.167 1.00 10.63 O ANISOU 1201 O ASP A 122 1567 1644 826 -199 -304 75 O ATOM 1202 CB ASP A 122 17.414 -16.926 33.603 1.00 11.21 C ANISOU 1202 CB ASP A 122 1696 1602 960 -469 -417 54 C ATOM 1203 CG ASP A 122 18.238 -18.161 33.995 1.00 14.82 C ANISOU 1203 CG ASP A 122 2127 1765 1740 -284 -336 419 C ATOM 1204 OD1 ASP A 122 19.452 -18.301 33.757 1.00 17.52 O ANISOU 1204 OD1 ASP A 122 2130 2204 2323 -101 -198 150 O ATOM 1205 OD2 ASP A 122 17.598 -19.076 34.573 1.00 18.06 O ANISOU 1205 OD2 ASP A 122 2635 1845 2381 -200 -82 500 O ATOM 1206 N GLU A 123 16.897 -13.795 33.152 1.00 10.14 N ANISOU 1206 N GLU A 123 1560 1452 843 -87 -185 191 N ATOM 1207 CA GLU A 123 16.165 -12.682 32.536 1.00 10.75 C ANISOU 1207 CA GLU A 123 1437 1616 1030 -25 -212 309 C ATOM 1208 C GLU A 123 17.113 -11.798 31.722 1.00 10.38 C ANISOU 1208 C GLU A 123 1516 1440 987 -13 -134 212 C ATOM 1209 O GLU A 123 16.767 -11.369 30.613 1.00 11.66 O ANISOU 1209 O GLU A 123 1768 1752 910 33 -252 329 O ATOM 1210 CB GLU A 123 15.441 -11.887 33.623 1.00 11.79 C ANISOU 1210 CB GLU A 123 1454 1922 1105 93 -128 207 C ATOM 1211 CG GLU A 123 14.717 -10.684 33.072 1.00 16.77 C ANISOU 1211 CG GLU A 123 2039 2478 1855 708 -291 366 C ATOM 1212 CD GLU A 123 13.848 -9.963 34.069 1.00 20.94 C ANISOU 1212 CD GLU A 123 2158 2554 3245 571 453 202 C ATOM 1213 OE1 GLU A 123 13.739 -8.701 33.917 1.00 23.44 O ANISOU 1213 OE1 GLU A 123 3861 2549 2496 891 24 -38 O ATOM 1214 OE2 GLU A 123 13.260 -10.690 34.905 1.00 21.23 O ANISOU 1214 OE2 GLU A 123 2265 2986 2817 244 552 -57 O ATOM 1215 N MET A 124 18.320 -11.480 32.251 1.00 10.27 N ANISOU 1215 N MET A 124 1523 1445 933 -132 -139 129 N ATOM 1216 CA MET A 124 19.295 -10.710 31.464 1.00 10.60 C ANISOU 1216 CA MET A 124 1477 1583 966 -88 -92 234 C ATOM 1217 C MET A 124 19.601 -11.382 30.173 1.00 10.70 C ANISOU 1217 C MET A 124 1387 1733 947 -222 -243 208 C ATOM 1218 O MET A 124 19.688 -10.779 29.097 1.00 12.78 O ANISOU 1218 O MET A 124 1782 2089 985 -433 -155 420 O ATOM 1219 CB MET A 124 20.545 -10.506 32.328 1.00 11.74 C ANISOU 1219 CB MET A 124 1752 1634 1076 -378 -225 71 C ATOM 1220 CG MET A 124 20.388 -9.623 33.508 1.00 14.03 C ANISOU 1220 CG MET A 124 2692 1603 1038 -353 -222 103 C ATOM 1221 SD MET A 124 21.899 -9.653 34.558 1.00 18.86 S ANISOU 1221 SD MET A 124 3500 1891 1775 -332 -1137 -50 S ATOM 1222 CE MET A 124 23.026 -8.794 33.470 1.00 23.40 C ANISOU 1222 CE MET A 124 2240 3864 2787 91 -345 44 C ATOM 1223 N AILE A 125 19.834 -12.693 30.203 0.61 10.10 N ANISOU 1223 N AILE A 125 1368 1735 733 -272 -281 54 N ATOM 1224 N BILE A 125 19.827 -12.699 30.209 0.39 10.71 N ANISOU 1224 N BILE A 125 1526 1804 741 -119 -89 118 N ATOM 1225 CA AILE A 125 20.125 -13.328 28.930 0.61 11.16 C ANISOU 1225 CA AILE A 125 1442 1970 829 3 -306 -9 C ATOM 1226 CA BILE A 125 20.127 -13.570 29.096 0.39 11.33 C ANISOU 1226 CA BILE A 125 1314 2091 901 -193 -64 -98 C ATOM 1227 C AILE A 125 18.904 -13.332 28.029 0.61 9.53 C ANISOU 1227 C AILE A 125 1206 1720 697 34 -185 189 C ATOM 1228 C BILE A 125 18.965 -13.605 28.090 0.39 11.16 C ANISOU 1228 C BILE A 125 1332 1916 992 -208 -224 166 C ATOM 1229 O AILE A 125 19.047 -13.021 26.836 0.61 9.15 O ANISOU 1229 O AILE A 125 1372 1413 692 128 -136 52 O ATOM 1230 O BILE A 125 19.182 -13.580 26.873 0.39 12.04 O ANISOU 1230 O BILE A 125 1571 1983 1022 -64 -144 -55 O ATOM 1231 CB AILE A 125 20.625 -14.745 29.177 0.61 11.25 C ANISOU 1231 CB AILE A 125 1419 2110 745 276 -297 53 C ATOM 1232 CB BILE A 125 20.420 -15.020 29.517 0.39 11.22 C ANISOU 1232 CB BILE A 125 1344 2185 732 190 -243 -259 C ATOM 1233 CG1AILE A 125 22.000 -14.610 29.850 0.61 12.96 C ANISOU 1233 CG1AILE A 125 1332 2767 823 483 -157 -303 C ATOM 1234 CG1BILE A 125 21.666 -15.223 30.391 0.39 14.53 C ANISOU 1234 CG1BILE A 125 1409 3104 1008 57 -409 34 C ATOM 1235 CG2AILE A 125 20.648 -15.581 27.925 0.61 13.92 C ANISOU 1235 CG2AILE A 125 2168 2214 908 539 -560 -147 C ATOM 1236 CG2BILE A 125 20.445 -15.900 28.265 0.39 14.25 C ANISOU 1236 CG2BILE A 125 1996 2525 895 449 -308 -490 C ATOM 1237 CD1AILE A 125 22.517 -15.974 30.335 0.61 20.00 C ANISOU 1237 CD1AILE A 125 2484 3304 1811 1591 -1069 -659 C ATOM 1238 CD1BILE A 125 22.964 -15.183 29.569 0.39 21.27 C ANISOU 1238 CD1BILE A 125 1242 5294 1545 -537 -377 -559 C ATOM 1239 N ARG A 126 17.716 -13.660 28.551 1.00 11.02 N ANISOU 1239 N ARG A 126 1442 1914 828 -353 -236 126 N ATOM 1240 CA ARG A 126 16.539 -13.658 27.653 1.00 11.30 C ANISOU 1240 CA ARG A 126 1292 2008 994 -175 -281 11 C ATOM 1241 C ARG A 126 16.372 -12.342 26.918 1.00 11.97 C ANISOU 1241 C ARG A 126 1423 2166 958 16 -154 142 C ATOM 1242 O ARG A 126 16.005 -12.337 25.748 1.00 12.83 O ANISOU 1242 O ARG A 126 1459 2474 944 10 -321 94 O ATOM 1243 CB ARG A 126 15.257 -13.974 28.392 1.00 14.12 C ANISOU 1243 CB ARG A 126 1548 2625 1191 -376 -120 419 C ATOM 1244 CG ARG A 126 15.102 -15.397 28.805 1.00 15.95 C ANISOU 1244 CG ARG A 126 1929 2532 1598 -523 -383 482 C ATOM 1245 CD ARG A 126 13.690 -15.825 29.053 1.00 18.87 C ANISOU 1245 CD ARG A 126 1796 2688 2685 -593 -445 833 C ATOM 1246 NE ARG A 126 12.984 -14.957 29.956 1.00 18.33 N ANISOU 1246 NE ARG A 126 1769 2964 2230 -240 -676 1045 N ATOM 1247 CZ ARG A 126 13.124 -14.986 31.285 1.00 20.06 C ANISOU 1247 CZ ARG A 126 1906 3475 2241 -387 -963 984 C ATOM 1248 NH1 ARG A 126 13.908 -15.819 31.897 1.00 29.89 N ANISOU 1248 NH1 ARG A 126 2194 5535 3628 -210 -1305 2480 N ATOM 1249 NH2 ARG A 126 12.387 -14.116 31.958 1.00 31.46 N ANISOU 1249 NH2 ARG A 126 2952 5615 3386 68 -1055 -1068 N ATOM 1250 N GLU A 127 16.633 -11.202 27.589 1.00 11.44 N ANISOU 1250 N GLU A 127 1428 2074 844 42 -59 183 N ATOM 1251 CA GLU A 127 16.505 -9.895 26.987 1.00 13.24 C ANISOU 1251 CA GLU A 127 1628 2141 1260 273 0 337 C ATOM 1252 C GLU A 127 17.405 -9.749 25.780 1.00 13.55 C ANISOU 1252 C GLU A 127 1966 1986 1197 9 106 308 C ATOM 1253 O GLU A 127 17.067 -9.057 24.784 1.00 17.27 O ANISOU 1253 O GLU A 127 2493 2761 1309 174 -148 583 O ATOM 1254 CB GLU A 127 16.871 -8.811 28.021 1.00 15.78 C ANISOU 1254 CB GLU A 127 2572 1971 1454 532 187 92 C ATOM 1255 CG GLU A 127 15.854 -8.616 29.107 1.00 15.70 C ANISOU 1255 CG GLU A 127 2113 2334 1519 -144 163 205 C ATOM 1256 CD GLU A 127 14.651 -7.870 28.655 1.00 18.96 C ANISOU 1256 CD GLU A 127 1720 3046 2438 -190 -58 217 C ATOM 1257 OE1 GLU A 127 13.882 -8.665 27.984 1.00 26.39 O ANISOU 1257 OE1 GLU A 127 2645 4687 2693 -1486 -621 633 O ATOM 1258 OE2 GLU A 127 14.388 -6.681 28.943 1.00 30.29 O ANISOU 1258 OE2 GLU A 127 2614 2599 6295 179 139 869 O ATOM 1259 N ALA A 128 18.597 -10.326 25.833 1.00 12.83 N ANISOU 1259 N ALA A 128 1803 1987 1087 -80 135 202 N ATOM 1260 CA ALA A 128 19.595 -10.149 24.779 1.00 13.38 C ANISOU 1260 CA ALA A 128 1954 1918 1213 -348 221 175 C ATOM 1261 C ALA A 128 19.624 -11.312 23.775 1.00 11.41 C ANISOU 1261 C ALA A 128 1402 2003 930 -93 -99 243 C ATOM 1262 O ALA A 128 20.235 -11.144 22.712 1.00 12.07 O ANISOU 1262 O ALA A 128 1515 2101 969 -236 -59 218 O ATOM 1263 CB ALA A 128 20.994 -9.986 25.432 1.00 16.33 C ANISOU 1263 CB ALA A 128 2132 2718 1355 -1054 220 -220 C ATOM 1264 N ASP A 129 19.001 -12.427 24.107 1.00 11.64 N ANISOU 1264 N ASP A 129 1533 2046 842 -188 53 18 N ATOM 1265 CA ASP A 129 19.113 -13.634 23.321 1.00 11.01 C ANISOU 1265 CA ASP A 129 1259 2126 798 -304 -58 -67 C ATOM 1266 C ASP A 129 18.226 -13.501 22.097 1.00 12.37 C ANISOU 1266 C ASP A 129 1298 2513 887 -61 -36 108 C ATOM 1267 O ASP A 129 17.025 -13.191 22.230 1.00 15.64 O ANISOU 1267 O ASP A 129 1276 3231 1436 74 -62 118 O ATOM 1268 CB ASP A 129 18.673 -14.832 24.154 1.00 11.77 C ANISOU 1268 CB ASP A 129 1522 2064 886 -136 45 58 C ATOM 1269 CG ASP A 129 19.058 -16.181 23.593 1.00 11.96 C ANISOU 1269 CG ASP A 129 1394 2097 1052 -386 -62 -65 C ATOM 1270 OD1 ASP A 129 19.882 -16.270 22.638 1.00 11.78 O ANISOU 1270 OD1 ASP A 129 1426 2034 1017 -252 -67 -129 O ATOM 1271 OD2 ASP A 129 18.564 -17.201 24.118 1.00 12.90 O ANISOU 1271 OD2 ASP A 129 1434 1937 1531 -176 208 69 O ATOM 1272 N ILE A 130 18.800 -13.687 20.919 1.00 11.70 N ANISOU 1272 N ILE A 130 1034 2500 911 -201 -137 77 N ATOM 1273 CA ILE A 130 18.120 -13.580 19.661 1.00 12.45 C ANISOU 1273 CA ILE A 130 1185 2604 941 -48 -242 39 C ATOM 1274 C ILE A 130 17.918 -14.959 19.049 1.00 12.82 C ANISOU 1274 C ILE A 130 1288 2694 888 -118 -271 -39 C ATOM 1275 O ILE A 130 16.827 -15.278 18.579 1.00 15.29 O ANISOU 1275 O ILE A 130 1283 3077 1449 -150 -387 -238 O ATOM 1276 CB ILE A 130 18.873 -12.655 18.666 1.00 12.83 C ANISOU 1276 CB ILE A 130 1397 2580 897 36 -255 95 C ATOM 1277 CG1 ILE A 130 18.906 -11.247 19.213 1.00 14.12 C ANISOU 1277 CG1 ILE A 130 1640 2532 1194 19 -330 197 C ATOM 1278 CG2 ILE A 130 18.216 -12.756 17.261 1.00 15.31 C ANISOU 1278 CG2 ILE A 130 1875 2911 1029 55 -444 228 C ATOM 1279 CD1 ILE A 130 19.792 -10.306 18.470 1.00 15.40 C ANISOU 1279 CD1 ILE A 130 1998 2427 1427 97 -120 363 C ATOM 1280 N ASP A 131 18.923 -15.781 19.040 1.00 12.60 N ANISOU 1280 N ASP A 131 1225 2656 908 -117 -110 -105 N ATOM 1281 CA ASP A 131 18.873 -17.126 18.450 1.00 14.06 C ANISOU 1281 CA ASP A 131 1516 2822 1004 -95 -239 -261 C ATOM 1282 C ASP A 131 18.258 -18.155 19.387 1.00 14.22 C ANISOU 1282 C ASP A 131 1526 2593 1284 -263 -272 -391 C ATOM 1283 O ASP A 131 17.993 -19.266 18.966 1.00 18.56 O ANISOU 1283 O ASP A 131 2315 3034 1703 -697 -253 -546 O ATOM 1284 CB ASP A 131 20.223 -17.553 17.893 1.00 13.91 C ANISOU 1284 CB ASP A 131 1674 2547 1065 -47 -176 -345 C ATOM 1285 CG ASP A 131 21.295 -17.707 18.949 1.00 13.35 C ANISOU 1285 CG ASP A 131 1515 2446 1111 -196 -183 -314 C ATOM 1286 OD1 ASP A 131 20.947 -17.777 20.151 1.00 12.41 O ANISOU 1286 OD1 ASP A 131 1513 2163 1041 -285 -93 -181 O ATOM 1287 OD2 ASP A 131 22.477 -17.704 18.551 1.00 16.01 O ANISOU 1287 OD2 ASP A 131 1640 3397 1046 126 -31 -196 O ATOM 1288 N GLY A 132 17.952 -17.786 20.631 1.00 13.64 N ANISOU 1288 N GLY A 132 1442 2501 1238 -283 -81 -73 N ATOM 1289 CA GLY A 132 17.216 -18.664 21.533 1.00 14.95 C ANISOU 1289 CA GLY A 132 1386 2522 1772 -303 35 -70 C ATOM 1290 C GLY A 132 18.030 -19.773 22.180 1.00 15.58 C ANISOU 1290 C GLY A 132 1580 2743 1598 -572 -304 287 C ATOM 1291 O GLY A 132 17.408 -20.621 22.799 1.00 17.82 O ANISOU 1291 O GLY A 132 1995 2706 2071 -818 -123 177 O ATOM 1292 N ASP A 133 19.346 -19.753 22.096 1.00 14.03 N ANISOU 1292 N ASP A 133 1465 2282 1584 -422 -267 -10 N ATOM 1293 CA ASP A 133 20.161 -20.822 22.653 1.00 14.21 C ANISOU 1293 CA ASP A 133 1764 2009 1628 -264 -203 -406 C ATOM 1294 C ASP A 133 20.470 -20.622 24.149 1.00 13.90 C ANISOU 1294 C ASP A 133 1878 1823 1582 -339 -287 -102 C ATOM 1295 O ASP A 133 21.230 -21.404 24.724 1.00 15.49 O ANISOU 1295 O ASP A 133 2127 1760 1997 -351 -487 63 O ATOM 1296 CB ASP A 133 21.453 -20.983 21.843 1.00 14.67 C ANISOU 1296 CB ASP A 133 1976 1748 1851 -186 17 -409 C ATOM 1297 CG ASP A 133 22.472 -19.875 22.040 1.00 12.97 C ANISOU 1297 CG ASP A 133 1730 1848 1351 -119 -90 -178 C ATOM 1298 OD1 ASP A 133 22.101 -18.863 22.674 1.00 12.15 O ANISOU 1298 OD1 ASP A 133 1616 1733 1266 -196 -125 -51 O ATOM 1299 OD2 ASP A 133 23.634 -20.050 21.609 1.00 15.35 O ANISOU 1299 OD2 ASP A 133 1785 2108 1939 -8 -21 -300 O ATOM 1300 N GLY A 134 19.882 -19.609 24.801 1.00 12.75 N ANISOU 1300 N GLY A 134 1598 1935 1310 -472 -40 -82 N ATOM 1301 CA GLY A 134 20.151 -19.402 26.217 1.00 12.69 C ANISOU 1301 CA GLY A 134 1583 1917 1322 -497 -100 128 C ATOM 1302 C GLY A 134 21.520 -18.950 26.582 1.00 11.23 C ANISOU 1302 C GLY A 134 1419 1624 1223 -145 -105 45 C ATOM 1303 O GLY A 134 21.878 -18.934 27.740 1.00 12.48 O ANISOU 1303 O GLY A 134 1684 1857 1201 -167 -159 256 O ATOM 1304 N HIS A 135 22.262 -18.487 25.583 1.00 10.65 N ANISOU 1304 N HIS A 135 1339 1587 1120 -232 -222 17 N ATOM 1305 CA HIS A 135 23.592 -17.964 25.708 1.00 10.74 C ANISOU 1305 CA HIS A 135 1312 1593 1177 -131 -69 -17 C ATOM 1306 C HIS A 135 23.663 -16.625 24.943 1.00 9.80 C ANISOU 1306 C HIS A 135 1166 1600 956 -73 -177 56 C ATOM 1307 O HIS A 135 22.819 -16.377 24.083 1.00 10.62 O ANISOU 1307 O HIS A 135 1254 1724 1055 -233 -223 -16 O ATOM 1308 CB HIS A 135 24.632 -18.908 25.112 1.00 11.75 C ANISOU 1308 CB HIS A 135 1440 1728 1298 33 -46 21 C ATOM 1309 CG HIS A 135 24.770 -20.221 25.825 1.00 12.54 C ANISOU 1309 CG HIS A 135 1920 1560 1283 72 -292 -228 C ATOM 1310 ND1 HIS A 135 23.791 -21.162 25.867 1.00 14.75 N ANISOU 1310 ND1 HIS A 135 2202 1657 1744 -111 -290 -104 N ATOM 1311 CD2 HIS A 135 25.839 -20.693 26.494 1.00 14.36 C ANISOU 1311 CD2 HIS A 135 2071 1883 1501 227 -289 73 C ATOM 1312 CE1 HIS A 135 24.204 -22.213 26.567 1.00 17.51 C ANISOU 1312 CE1 HIS A 135 3048 1433 2174 -103 -672 -170 C ATOM 1313 NE2 HIS A 135 25.443 -21.954 26.963 1.00 16.16 N ANISOU 1313 NE2 HIS A 135 2601 1590 1950 346 -233 -63 N ATOM 1314 N AILE A 136 24.678 -15.819 25.205 0.71 9.88 N ANISOU 1314 N AILE A 136 1105 1630 1019 -59 -133 82 N ATOM 1315 N BILE A 136 24.655 -15.791 25.209 0.29 10.01 N ANISOU 1315 N BILE A 136 1221 1621 961 -106 -226 92 N ATOM 1316 CA AILE A 136 24.876 -14.565 24.480 0.71 9.61 C ANISOU 1316 CA AILE A 136 1006 1685 961 -33 -239 141 C ATOM 1317 CA BILE A 136 24.838 -14.521 24.513 0.29 9.64 C ANISOU 1317 CA BILE A 136 1100 1555 1009 42 -96 67 C ATOM 1318 C AILE A 136 26.127 -14.728 23.623 0.71 9.93 C ANISOU 1318 C AILE A 136 1114 1643 1017 -236 -190 95 C ATOM 1319 C BILE A 136 26.084 -14.587 23.633 0.29 8.42 C ANISOU 1319 C BILE A 136 995 1191 1014 170 -199 93 C ATOM 1320 O AILE A 136 27.245 -14.925 24.143 0.71 10.63 O ANISOU 1320 O AILE A 136 1054 2032 952 21 -45 63 O ATOM 1321 O BILE A 136 27.214 -14.600 24.154 0.29 8.58 O ANISOU 1321 O BILE A 136 1025 951 1286 -39 -319 186 O ATOM 1322 CB AILE A 136 24.931 -13.381 25.453 0.71 10.39 C ANISOU 1322 CB AILE A 136 1190 1580 1176 80 -317 101 C ATOM 1323 CB BILE A 136 24.957 -13.349 25.507 0.29 9.21 C ANISOU 1323 CB BILE A 136 990 1630 880 -147 21 76 C ATOM 1324 CG1AILE A 136 23.610 -13.285 26.242 0.71 10.88 C ANISOU 1324 CG1AILE A 136 1501 1555 1078 -43 -146 18 C ATOM 1325 CG1BILE A 136 23.850 -13.334 26.562 0.29 9.71 C ANISOU 1325 CG1BILE A 136 948 1877 865 -174 -10 78 C ATOM 1326 CG2AILE A 136 25.280 -12.101 24.690 0.71 10.63 C ANISOU 1326 CG2AILE A 136 1412 1689 937 -129 -388 39 C ATOM 1327 CG2BILE A 136 25.042 -12.036 24.732 0.29 12.86 C ANISOU 1327 CG2BILE A 136 1418 1427 2041 483 1140 241 C ATOM 1328 CD1AILE A 136 22.353 -13.198 25.337 0.71 14.80 C ANISOU 1328 CD1AILE A 136 1205 2553 1867 357 -89 -2 C ATOM 1329 CD1BILE A 136 23.945 -12.201 27.562 0.29 10.99 C ANISOU 1329 CD1BILE A 136 1234 1987 956 155 -65 -53 C ATOM 1330 N ASN A 137 25.925 -14.621 22.319 1.00 10.13 N ANISOU 1330 N ASN A 137 1033 1800 1017 33 -131 -13 N ATOM 1331 CA ASN A 137 27.063 -14.577 21.388 1.00 10.65 C ANISOU 1331 CA ASN A 137 1165 1804 1077 90 -61 -16 C ATOM 1332 C ASN A 137 27.506 -13.130 21.175 1.00 10.20 C ANISOU 1332 C ASN A 137 1041 1890 945 61 -112 49 C ATOM 1333 O ASN A 137 26.960 -12.179 21.722 1.00 10.48 O ANISOU 1333 O ASN A 137 1125 1860 998 19 -110 78 O ATOM 1334 CB ASN A 137 26.753 -15.363 20.120 1.00 12.30 C ANISOU 1334 CB ASN A 137 1358 2076 1241 -43 -19 -224 C ATOM 1335 CG ASN A 137 25.835 -14.630 19.160 1.00 12.91 C ANISOU 1335 CG ASN A 137 1689 2125 1090 -141 -184 -114 C ATOM 1336 OD1 ASN A 137 25.464 -13.484 19.300 1.00 13.08 O ANISOU 1336 OD1 ASN A 137 1566 2251 1151 54 -260 -75 O ATOM 1337 ND2 ASN A 137 25.456 -15.404 18.142 1.00 17.67 N ANISOU 1337 ND2 ASN A 137 2309 2860 1545 139 -534 -693 N ATOM 1338 N ATYR A 138 28.601 -12.898 20.410 0.62 11.24 N ANISOU 1338 N ATYR A 138 1183 2035 1052 -43 -54 77 N ATOM 1339 N BTYR A 138 28.549 -13.012 20.355 0.38 12.52 N ANISOU 1339 N BTYR A 138 1456 2144 1155 66 213 250 N ATOM 1340 CA ATYR A 138 29.139 -11.533 20.318 0.62 11.57 C ANISOU 1340 CA ATYR A 138 1049 2051 1298 -16 56 169 C ATOM 1341 CA BTYR A 138 29.168 -11.698 20.210 0.38 11.47 C ANISOU 1341 CA BTYR A 138 1330 2176 852 8 104 123 C ATOM 1342 C ATYR A 138 28.145 -10.598 19.645 0.62 11.03 C ANISOU 1342 C ATYR A 138 1147 2133 909 -4 89 124 C ATOM 1343 C BTYR A 138 28.202 -10.683 19.631 0.38 11.23 C ANISOU 1343 C BTYR A 138 1280 2147 838 -75 90 173 C ATOM 1344 O ATYR A 138 27.965 -9.464 20.090 0.62 11.46 O ANISOU 1344 O ATYR A 138 1273 1935 1146 -76 -160 239 O ATOM 1345 O BTYR A 138 28.052 -9.563 20.129 0.38 11.67 O ANISOU 1345 O BTYR A 138 1071 2203 1160 -9 3 43 O ATOM 1346 CB ATYR A 138 30.504 -11.526 19.611 0.62 11.58 C ANISOU 1346 CB ATYR A 138 1295 1989 1118 123 343 162 C ATOM 1347 CB BTYR A 138 30.454 -11.923 19.397 0.38 12.51 C ANISOU 1347 CB BTYR A 138 1468 2117 1167 20 337 25 C ATOM 1348 CG ATYR A 138 31.102 -10.134 19.453 0.62 11.63 C ANISOU 1348 CG ATYR A 138 1105 2074 1241 -57 80 272 C ATOM 1349 CG BTYR A 138 31.088 -10.573 19.136 0.38 11.75 C ANISOU 1349 CG BTYR A 138 1328 2116 1019 90 206 75 C ATOM 1350 CD1ATYR A 138 31.630 -9.407 20.494 0.62 13.43 C ANISOU 1350 CD1ATYR A 138 1225 2595 1283 -407 -73 377 C ATOM 1351 CD1BTYR A 138 31.582 -9.811 20.168 0.38 12.75 C ANISOU 1351 CD1BTYR A 138 1159 2630 1056 -423 -121 347 C ATOM 1352 CD2ATYR A 138 31.129 -9.501 18.213 0.62 12.62 C ANISOU 1352 CD2ATYR A 138 1609 2125 1060 59 432 110 C ATOM 1353 CD2BTYR A 138 31.143 -10.115 17.828 0.38 13.80 C ANISOU 1353 CD2BTYR A 138 1558 2671 1015 -328 208 183 C ATOM 1354 CE1ATYR A 138 32.169 -8.146 20.363 0.62 13.62 C ANISOU 1354 CE1ATYR A 138 1243 2548 1383 -428 -14 45 C ATOM 1355 CE1BTYR A 138 32.164 -8.570 19.956 0.38 12.13 C ANISOU 1355 CE1BTYR A 138 793 2461 1354 -192 -49 297 C ATOM 1356 CE2ATYR A 138 31.657 -8.235 18.055 0.62 13.84 C ANISOU 1356 CE2ATYR A 138 1526 2416 1316 -111 27 610 C ATOM 1357 CE2BTYR A 138 31.714 -8.882 17.616 0.38 13.76 C ANISOU 1357 CE2BTYR A 138 1422 2657 1149 -199 455 225 C ATOM 1358 CZ ATYR A 138 32.174 -7.567 19.119 0.62 14.20 C ANISOU 1358 CZ ATYR A 138 1715 1940 1739 22 292 208 C ATOM 1359 CZ BTYR A 138 32.200 -8.134 18.649 0.38 12.44 C ANISOU 1359 CZ BTYR A 138 965 2358 1402 -72 179 326 C ATOM 1360 OH ATYR A 138 32.691 -6.313 18.944 0.62 18.58 O ANISOU 1360 OH ATYR A 138 1676 2304 3079 -366 -188 640 O ATOM 1361 OH BTYR A 138 32.771 -6.914 18.382 0.38 17.62 O ANISOU 1361 OH BTYR A 138 2008 2544 2142 -469 -58 678 O ATOM 1362 N GLU A 139 27.507 -11.037 18.565 1.00 12.23 N ANISOU 1362 N GLU A 139 1441 2190 1016 9 -49 113 N ATOM 1363 CA GLU A 139 26.509 -10.119 17.954 1.00 12.62 C ANISOU 1363 CA GLU A 139 1501 2276 1019 -68 -134 169 C ATOM 1364 C GLU A 139 25.437 -9.725 18.941 1.00 11.70 C ANISOU 1364 C GLU A 139 1247 2167 1033 -55 -235 244 C ATOM 1365 O GLU A 139 25.050 -8.564 18.981 1.00 12.48 O ANISOU 1365 O GLU A 139 1528 2072 1142 -17 -242 282 O ATOM 1366 CB GLU A 139 25.898 -10.791 16.718 1.00 14.60 C ANISOU 1366 CB GLU A 139 1886 2691 970 -303 -216 170 C ATOM 1367 CG GLU A 139 24.786 -9.935 16.138 1.00 16.29 C ANISOU 1367 CG GLU A 139 2256 2801 1134 -226 -563 239 C ATOM 1368 CD GLU A 139 24.171 -10.532 14.873 1.00 18.94 C ANISOU 1368 CD GLU A 139 2547 3223 1427 -485 -787 161 C ATOM 1369 OE1 GLU A 139 24.709 -11.550 14.351 1.00 25.46 O ANISOU 1369 OE1 GLU A 139 4119 3939 1616 227 -1436 -615 O ATOM 1370 OE2 GLU A 139 23.200 -9.930 14.412 1.00 22.86 O ANISOU 1370 OE2 GLU A 139 2687 4150 1850 -266 -1126 68 O ATOM 1371 N GLU A 140 24.904 -10.690 19.703 1.00 10.87 N ANISOU 1371 N GLU A 140 1266 1935 929 -70 -254 50 N ATOM 1372 CA GLU A 140 23.851 -10.374 20.685 1.00 10.88 C ANISOU 1372 CA GLU A 140 1143 1999 991 -129 -189 121 C ATOM 1373 C GLU A 140 24.372 -9.404 21.732 1.00 10.19 C ANISOU 1373 C GLU A 140 1018 1801 1051 -87 -102 180 C ATOM 1374 O GLU A 140 23.643 -8.506 22.185 1.00 11.84 O ANISOU 1374 O GLU A 140 1197 1900 1402 41 -231 64 O ATOM 1375 CB GLU A 140 23.353 -11.674 21.314 1.00 10.64 C ANISOU 1375 CB GLU A 140 1226 1806 1008 -31 -197 44 C ATOM 1376 CG GLU A 140 22.596 -12.575 20.327 1.00 11.64 C ANISOU 1376 CG GLU A 140 1200 2147 1077 -245 -441 245 C ATOM 1377 CD GLU A 140 22.381 -13.972 20.819 1.00 10.30 C ANISOU 1377 CD GLU A 140 1115 1978 820 -160 -83 49 C ATOM 1378 OE1 GLU A 140 23.155 -14.459 21.708 1.00 11.28 O ANISOU 1378 OE1 GLU A 140 1139 2077 1070 -129 -256 149 O ATOM 1379 OE2 GLU A 140 21.417 -14.652 20.364 1.00 11.33 O ANISOU 1379 OE2 GLU A 140 1211 2125 969 -223 -256 38 O ATOM 1380 N APHE A 141 25.615 -9.612 22.151 0.53 10.23 N ANISOU 1380 N APHE A 141 1117 1732 1039 -51 -206 109 N ATOM 1381 N BPHE A 141 25.607 -9.618 22.156 0.47 10.37 N ANISOU 1381 N BPHE A 141 1119 1825 997 -23 -185 41 N ATOM 1382 CA APHE A 141 26.249 -8.753 23.133 0.53 10.57 C ANISOU 1382 CA APHE A 141 1089 1908 1020 -110 -118 72 C ATOM 1383 CA BPHE A 141 26.241 -8.740 23.123 0.47 10.57 C ANISOU 1383 CA BPHE A 141 1108 1858 1051 -148 -89 37 C ATOM 1384 C APHE A 141 26.373 -7.309 22.641 0.53 11.42 C ANISOU 1384 C APHE A 141 1172 1918 1249 -217 -155 59 C ATOM 1385 C BPHE A 141 26.305 -7.302 22.613 0.47 12.26 C ANISOU 1385 C BPHE A 141 1368 1904 1386 -173 7 111 C ATOM 1386 O APHE A 141 26.015 -6.358 23.321 0.53 13.10 O ANISOU 1386 O APHE A 141 1620 1880 1478 -219 -69 -26 O ATOM 1387 O BPHE A 141 25.855 -6.355 23.241 0.47 12.32 O ANISOU 1387 O BPHE A 141 1492 1845 1344 -43 -153 153 O ATOM 1388 CB APHE A 141 27.604 -9.328 23.501 0.53 10.77 C ANISOU 1388 CB APHE A 141 1028 2187 879 -99 -67 115 C ATOM 1389 CB BPHE A 141 27.620 -9.284 23.420 0.47 11.51 C ANISOU 1389 CB BPHE A 141 1086 2057 1231 -139 -153 -58 C ATOM 1390 CG APHE A 141 28.401 -8.512 24.494 0.53 11.51 C ANISOU 1390 CG APHE A 141 1101 2261 1009 -302 -54 116 C ATOM 1391 CG BPHE A 141 28.434 -8.569 24.470 0.47 11.83 C ANISOU 1391 CG BPHE A 141 1129 2219 1148 -415 -69 78 C ATOM 1392 CD1APHE A 141 28.037 -8.501 25.850 0.53 11.44 C ANISOU 1392 CD1APHE A 141 1019 2253 1076 -438 112 -239 C ATOM 1393 CD1BPHE A 141 28.329 -8.946 25.817 0.47 11.36 C ANISOU 1393 CD1BPHE A 141 1417 1772 1127 32 -96 86 C ATOM 1394 CD2APHE A 141 29.506 -7.770 24.084 0.53 10.93 C ANISOU 1394 CD2APHE A 141 1115 1976 1063 -133 120 63 C ATOM 1395 CD2BPHE A 141 29.306 -7.547 24.112 0.47 12.44 C ANISOU 1395 CD2BPHE A 141 1308 1987 1432 -355 -135 160 C ATOM 1396 CE1APHE A 141 28.782 -7.762 26.760 0.53 14.05 C ANISOU 1396 CE1APHE A 141 1349 2760 1231 -476 -239 -206 C ATOM 1397 CE1BPHE A 141 29.101 -8.312 26.769 0.47 13.87 C ANISOU 1397 CE1BPHE A 141 1919 2161 1190 -269 -244 165 C ATOM 1398 CE2APHE A 141 30.239 -7.050 25.021 0.53 13.97 C ANISOU 1398 CE2APHE A 141 1058 2719 1532 -386 -187 13 C ATOM 1399 CE2BPHE A 141 30.067 -6.916 25.091 0.47 14.08 C ANISOU 1399 CE2BPHE A 141 1140 2693 1515 -680 -60 104 C ATOM 1400 CZ APHE A 141 29.871 -7.038 26.339 0.53 15.57 C ANISOU 1400 CZ APHE A 141 1401 3062 1452 -757 -332 -460 C ATOM 1401 CZ BPHE A 141 29.951 -7.303 26.403 0.47 15.41 C ANISOU 1401 CZ BPHE A 141 1560 2893 1402 -575 -71 -61 C ATOM 1402 N VAL A 142 26.880 -7.163 21.407 1.00 11.84 N ANISOU 1402 N VAL A 142 1214 1994 1292 -161 -130 230 N ATOM 1403 CA VAL A 142 27.032 -5.837 20.820 1.00 13.02 C ANISOU 1403 CA VAL A 142 1547 1907 1491 -198 -146 235 C ATOM 1404 C VAL A 142 25.696 -5.170 20.666 1.00 14.52 C ANISOU 1404 C VAL A 142 1521 1940 2056 -115 55 430 C ATOM 1405 O VAL A 142 25.537 -3.995 21.022 1.00 16.40 O ANISOU 1405 O VAL A 142 1876 1849 2504 -101 161 420 O ATOM 1406 CB VAL A 142 27.748 -5.896 19.448 1.00 15.32 C ANISOU 1406 CB VAL A 142 1637 2324 1859 19 145 644 C ATOM 1407 CG1 VAL A 142 27.741 -4.547 18.742 1.00 17.14 C ANISOU 1407 CG1 VAL A 142 2203 2429 1882 -71 -49 689 C ATOM 1408 CG2 VAL A 142 29.195 -6.327 19.651 1.00 16.14 C ANISOU 1408 CG2 VAL A 142 1503 2631 1997 -88 72 572 C ATOM 1409 N AARG A 143 24.658 -5.867 20.143 0.48 13.09 N ANISOU 1409 N AARG A 143 1358 1833 1784 -52 69 765 N ATOM 1410 N BARG A 143 24.738 -5.948 20.138 0.52 15.49 N ANISOU 1410 N BARG A 143 1481 2355 2048 181 -170 -60 N ATOM 1411 CA AARG A 143 23.375 -5.186 19.950 0.48 16.92 C ANISOU 1411 CA AARG A 143 1505 2485 2441 280 -5 957 C ATOM 1412 CA BARG A 143 23.436 -5.352 19.888 0.52 15.37 C ANISOU 1412 CA BARG A 143 1572 2156 2114 121 -157 816 C ATOM 1413 C AARG A 143 22.788 -4.782 21.272 0.48 17.47 C ANISOU 1413 C AARG A 143 1655 2196 2787 342 415 943 C ATOM 1414 C BARG A 143 22.848 -4.751 21.136 0.52 16.52 C ANISOU 1414 C BARG A 143 1452 2419 2406 424 196 920 C ATOM 1415 O AARG A 143 22.081 -3.787 21.510 0.48 25.79 O ANISOU 1415 O AARG A 143 3288 2491 4021 1078 1691 1635 O ATOM 1416 O BARG A 143 22.340 -3.621 21.110 0.52 17.37 O ANISOU 1416 O BARG A 143 2067 2399 2134 458 153 987 O ATOM 1417 CB AARG A 143 22.413 -6.070 19.148 0.48 15.79 C ANISOU 1417 CB AARG A 143 1377 2146 2477 290 -149 1395 C ATOM 1418 CB BARG A 143 22.551 -6.424 19.247 0.52 16.33 C ANISOU 1418 CB BARG A 143 1451 2180 2573 -9 -270 1073 C ATOM 1419 CG AARG A 143 23.006 -6.543 17.831 0.48 17.08 C ANISOU 1419 CG AARG A 143 1430 2865 2195 358 -523 1152 C ATOM 1420 CG BARG A 143 22.545 -6.266 17.721 0.52 18.56 C ANISOU 1420 CG BARG A 143 2157 2396 2499 -89 -639 676 C ATOM 1421 CD AARG A 143 22.082 -7.373 17.042 0.48 19.77 C ANISOU 1421 CD AARG A 143 2045 3037 2431 -190 -810 1431 C ATOM 1422 CD BARG A 143 21.104 -6.426 17.194 0.52 25.74 C ANISOU 1422 CD BARG A 143 2566 3669 3544 10 -1325 269 C ATOM 1423 NE AARG A 143 21.784 -8.715 16.782 0.48 27.69 N ANISOU 1423 NE AARG A 143 3402 3249 3869 43 -1205 540 N ATOM 1424 NE BARG A 143 21.003 -7.587 16.371 0.52 21.60 N ANISOU 1424 NE BARG A 143 2484 2993 2731 -172 -1569 1143 N ATOM 1425 CZ AARG A 143 20.983 -9.086 15.763 0.48 28.04 C ANISOU 1425 CZ AARG A 143 3542 3460 3651 179 -897 -26 C ATOM 1426 CZ BARG A 143 20.125 -8.267 15.690 0.52 18.59 C ANISOU 1426 CZ BARG A 143 1966 3023 2075 -62 -1120 1164 C ATOM 1427 NH1AARG A 143 20.414 -8.251 14.923 0.48 30.24 N ANISOU 1427 NH1AARG A 143 3583 4129 3780 -901 -1453 681 N ATOM 1428 NH1BARG A 143 18.846 -7.940 15.634 0.52 20.93 N ANISOU 1428 NH1BARG A 143 1878 3056 3017 -223 -770 956 N ATOM 1429 NH2AARG A 143 20.781 -10.389 15.646 0.48 39.02 N ANISOU 1429 NH2AARG A 143 5905 3331 5589 1231 -1969 -1283 N ATOM 1430 NH2BARG A 143 20.552 -9.343 15.034 0.52 21.02 N ANISOU 1430 NH2BARG A 143 2307 2987 2693 9 -879 998 N ATOM 1431 N AMET A 144 23.047 -5.567 22.330 0.73 15.87 N ANISOU 1431 N AMET A 144 1645 1991 2394 73 272 551 N ATOM 1432 N BMET A 144 22.894 -5.446 22.256 0.27 14.60 N ANISOU 1432 N BMET A 144 1432 1910 2205 634 112 523 N ATOM 1433 CA AMET A 144 22.470 -5.063 23.570 0.73 17.91 C ANISOU 1433 CA AMET A 144 2090 2116 2599 198 378 406 C ATOM 1434 CA BMET A 144 22.379 -5.018 23.543 0.27 16.96 C ANISOU 1434 CA BMET A 144 1956 2195 2292 402 293 408 C ATOM 1435 C AMET A 144 23.234 -3.844 24.042 0.73 19.05 C ANISOU 1435 C AMET A 144 2359 2174 2706 -5 954 203 C ATOM 1436 C BMET A 144 23.252 -3.970 24.212 0.27 19.69 C ANISOU 1436 C BMET A 144 2205 2446 2829 335 537 -187 C ATOM 1437 O AMET A 144 22.658 -2.849 24.455 0.73 23.19 O ANISOU 1437 O AMET A 144 2891 1788 4134 9 1377 449 O ATOM 1438 O BMET A 144 22.733 -3.159 24.986 0.27 24.03 O ANISOU 1438 O BMET A 144 3385 2199 3547 -176 1766 -239 O ATOM 1439 CB AMET A 144 22.452 -6.204 24.592 0.73 16.63 C ANISOU 1439 CB AMET A 144 1898 2145 2275 233 389 340 C ATOM 1440 CB BMET A 144 22.208 -6.258 24.442 0.27 18.71 C ANISOU 1440 CB BMET A 144 3168 2225 1715 469 -203 348 C ATOM 1441 CG AMET A 144 21.903 -5.792 25.947 0.73 19.80 C ANISOU 1441 CG AMET A 144 2383 3172 1968 274 -209 -117 C ATOM 1442 CG BMET A 144 21.330 -6.070 25.665 0.27 21.28 C ANISOU 1442 CG BMET A 144 2656 2986 2442 -205 308 553 C ATOM 1443 SD AMET A 144 20.260 -5.027 25.910 0.73 20.95 S ANISOU 1443 SD AMET A 144 2403 2217 3339 249 1055 84 S ATOM 1444 SD BMET A 144 19.574 -6.430 25.425 0.27 25.43 S ANISOU 1444 SD BMET A 144 2752 2230 4681 -18 -443 836 S ATOM 1445 CE AMET A 144 19.693 -5.647 27.489 0.73 43.25 C ANISOU 1445 CE AMET A 144 5606 5619 5208 1101 3236 1791 C ATOM 1446 CE BMET A 144 18.960 -4.748 25.277 0.27 36.14 C ANISOU 1446 CE BMET A 144 4698 2898 6137 1941 -19 -1330 C ATOM 1447 N MET A 145 24.565 -3.924 23.977 1.00 19.22 N ANISOU 1447 N MET A 145 2357 2495 2452 -199 717 26 N ATOM 1448 CA MET A 145 25.390 -2.897 24.568 1.00 23.30 C ANISOU 1448 CA MET A 145 2722 2579 3553 -333 752 -289 C ATOM 1449 C MET A 145 25.225 -1.570 23.860 1.00 26.92 C ANISOU 1449 C MET A 145 4104 2359 3765 -145 1938 -286 C ATOM 1450 O MET A 145 25.295 -0.510 24.471 1.00 37.49 O ANISOU 1450 O MET A 145 7055 2591 4600 -271 2411 -838 O ATOM 1451 CB MET A 145 26.892 -3.256 24.504 1.00 24.29 C ANISOU 1451 CB MET A 145 2596 3612 3022 -468 417 -1345 C ATOM 1452 CG MET A 145 27.267 -4.404 25.410 1.00 26.10 C ANISOU 1452 CG MET A 145 3175 3867 2875 268 -763 -1897 C ATOM 1453 SD MET A 145 27.021 -4.174 27.148 1.00 35.69 S ANISOU 1453 SD MET A 145 5435 5324 2800 206 225 -1330 S ATOM 1454 CE MET A 145 25.397 -4.813 27.441 1.00 87.86 C ANISOU 1454 CE MET A 145 10721 12955 9706 -6473 6217 -6376 C ATOM 1455 N VAL A 146 24.997 -1.636 22.552 1.00 26.75 N ANISOU 1455 N VAL A 146 4101 2230 3835 -301 1589 167 N ATOM 1456 CA VAL A 146 24.857 -0.329 21.867 1.00 30.36 C ANISOU 1456 CA VAL A 146 4249 2394 4893 -83 2020 623 C ATOM 1457 C VAL A 146 23.396 0.103 21.704 1.00 34.19 C ANISOU 1457 C VAL A 146 4430 2695 5865 128 2079 1238 C ATOM 1458 O VAL A 146 23.211 1.192 21.177 1.00 38.65 O ANISOU 1458 O VAL A 146 5842 2925 5920 719 1689 1174 O ATOM 1459 CB VAL A 146 25.536 -0.395 20.500 1.00 31.65 C ANISOU 1459 CB VAL A 146 4308 3201 4515 113 1588 1163 C ATOM 1460 CG1 VAL A 146 26.973 -0.899 20.708 1.00 34.55 C ANISOU 1460 CG1 VAL A 146 3889 2998 6241 -123 2159 678 C ATOM 1461 CG2 VAL A 146 24.761 -1.253 19.521 1.00 31.34 C ANISOU 1461 CG2 VAL A 146 4886 2586 4437 331 1471 1182 C ATOM 1462 N SER A 147 22.457 -0.728 22.138 1.00 42.05 N ANISOU 1462 N SER A 147 4338 3855 7786 12 3105 1274 N ATOM 1463 CA SER A 147 21.035 -0.555 21.893 1.00 49.83 C ANISOU 1463 CA SER A 147 4726 5049 9159 -885 1231 2093 C ATOM 1464 C SER A 147 20.156 -1.376 22.809 1.00 44.39 C ANISOU 1464 C SER A 147 3643 3666 9559 -970 1280 1031 C ATOM 1465 O SER A 147 20.339 -2.042 23.820 1.00 43.47 O ANISOU 1465 O SER A 147 4227 3007 9284 158 2931 904 O ATOM 1466 CB SER A 147 20.729 -0.885 20.424 1.00 55.45 C ANISOU 1466 CB SER A 147 6665 5178 9226 1015 1128 1380 C ATOM 1467 OG SER A 147 21.172 -2.131 19.875 1.00 50.29 O ANISOU 1467 OG SER A 147 5747 4965 8395 2358 906 2864 O TER 1468 SER A 147 HETATM 1469 CA CA A1000 46.224 7.128 -8.698 1.00 7.59 CA ANISOU 1469 CA CA A1000 1024 529 1331 -178 -193 33 CA HETATM 1470 CA CA A1001 36.763 12.606 -4.815 1.00 10.83 CA ANISOU 1470 CA CA A1001 2049 526 1538 133 -782 -18 CA HETATM 1471 CA CA A1002 22.026 -16.616 21.879 1.00 10.84 CA ANISOU 1471 CA CA A1002 1227 1912 981 -198 -186 -32 CA HETATM 1472 CA CA A1003 32.674 -10.435 -5.410 1.00 10.87 CA ANISOU 1472 CA CA A1003 1374 673 2082 -102 -294 225 CA HETATM 1473 CA CA A1004 31.568 -19.422 27.202 1.00 14.02 CA ANISOU 1473 CA CA A1004 1781 1881 1666 585 235 275 CA HETATM 1474 O HOH A2000 40.789 16.842 -5.083 1.00 9.89 O ANISOU 1474 O HOH A2000 1318 765 1674 -196 -139 256 O HETATM 1475 O HOH A2001 42.295 10.880 -11.518 1.00 10.57 O ANISOU 1475 O HOH A2001 1520 1232 1265 -167 -306 -12 O HETATM 1476 O HOH A2002 41.705 -15.715 -2.868 1.00 10.01 O ANISOU 1476 O HOH A2002 1710 890 1203 -384 -226 257 O HETATM 1477 O HOH A2003 14.809 -17.116 42.346 1.00 10.54 O ANISOU 1477 O HOH A2003 1581 1114 1308 13 -139 85 O HETATM 1478 O HOH A2004 17.979 -8.051 43.547 1.00 10.03 O ANISOU 1478 O HOH A2004 1550 932 1329 -18 -109 188 O HETATM 1479 O HOH A2005 20.902 -8.716 21.717 1.00 13.83 O ANISOU 1479 O HOH A2005 1326 2395 1533 -52 -167 488 O HETATM 1480 O HOH A2006 39.631 -14.352 -5.796 1.00 10.60 O ANISOU 1480 O HOH A2006 1647 863 1517 -23 -105 286 O HETATM 1481 O HOH A2007 25.821 -7.292 45.147 1.00 11.30 O ANISOU 1481 O HOH A2007 1685 1004 1605 26 -208 -273 O HETATM 1482 O HOH A2008 36.202 16.090 -1.527 1.00 13.74 O ANISOU 1482 O HOH A2008 2183 821 2215 98 -378 104 O HETATM 1483 O HOH A2009 43.816 -12.458 -5.592 1.00 11.57 O ANISOU 1483 O HOH A2009 1594 766 2035 -195 -444 249 O HETATM 1484 O HOH A2010 52.000 7.240 -4.484 1.00 12.61 O ANISOU 1484 O HOH A2010 1508 1433 1848 -32 -285 22 O HETATM 1485 O HOH A2011 39.438 12.591 -5.939 1.00 14.76 O ANISOU 1485 O HOH A2011 2127 1702 1778 645 -1049 -645 O HETATM 1486 O HOH A2012 23.594 -20.291 29.426 1.00 14.53 O ANISOU 1486 O HOH A2012 1887 1811 1825 -451 -435 -82 O HETATM 1487 O HOH A2013 36.982 -12.298 42.999 1.00 11.44 O ANISOU 1487 O HOH A2013 1751 890 1707 -140 -330 239 O HETATM 1488 O HOH A2014 26.036 -12.451 39.997 1.00 14.73 O ANISOU 1488 O HOH A2014 2215 1561 1821 -861 463 -286 O HETATM 1489 O HOH A2015 35.716 10.477 2.709 1.00 14.74 O ANISOU 1489 O HOH A2015 1380 2379 1840 75 -89 -758 O HETATM 1490 O HOH A2016 27.219 2.992 -4.838 1.00 15.82 O ANISOU 1490 O HOH A2016 1744 1582 2685 166 540 130 O HETATM 1491 O HOH A2017 37.759 5.553 -10.145 1.00 17.36 O ANISOU 1491 O HOH A2017 1629 1413 3555 -124 -878 334 O HETATM 1492 O HOH A2018 29.677 -8.242 -8.575 1.00 15.18 O ANISOU 1492 O HOH A2018 1771 1812 2183 -416 -281 231 O HETATM 1493 O HOH A2019 15.594 -14.445 42.575 1.00 15.21 O ANISOU 1493 O HOH A2019 2105 1375 2298 -263 303 -108 O HETATM 1494 O HOH A2020 34.849 -5.298 40.077 1.00 15.75 O ANISOU 1494 O HOH A2020 2204 1532 2246 -387 -1002 151 O HETATM 1495 O HOH A2021 52.321 11.732 16.151 1.00 20.53 O ANISOU 1495 O HOH A2021 2114 4519 1168 446 -133 -99 O HETATM 1496 O HOH A2022 30.227 -15.187 19.454 1.00 16.24 O ANISOU 1496 O HOH A2022 1832 2640 1697 495 479 186 O HETATM 1497 O HOH A2023 25.425 -15.277 42.324 1.00 20.37 O ANISOU 1497 O HOH A2023 2678 2671 2390 228 -986 -139 O HETATM 1498 O HOH A2024 37.556 -5.765 -11.157 1.00 18.63 O ANISOU 1498 O HOH A2024 3099 1655 2325 743 579 560 O HETATM 1499 O HOH A2025 15.998 -20.312 39.410 1.00 15.31 O ANISOU 1499 O HOH A2025 2310 1700 1807 -124 -743 -349 O HETATM 1500 O HOH A2026 38.753 17.085 -1.700 1.00 17.50 O ANISOU 1500 O HOH A2026 2335 1342 2974 74 -435 -612 O HETATM 1501 O HOH A2027 15.168 -10.056 42.106 1.00 17.48 O ANISOU 1501 O HOH A2027 2573 2104 1966 0 -671 -248 O HETATM 1502 O HOH A2028 31.388 -3.465 -2.591 1.00 17.30 O ANISOU 1502 O HOH A2028 2121 2158 2294 -437 65 222 O HETATM 1503 O HOH A2029 14.857 -14.876 24.857 1.00 18.72 O ANISOU 1503 O HOH A2029 1591 3297 2223 150 -447 -159 O HETATM 1504 O HOH A2030 30.080 9.422 -3.288 1.00 25.13 O ANISOU 1504 O HOH A2030 4448 1999 3100 -1048 -1775 523 O HETATM 1505 O HOH A2031 28.414 -19.030 38.108 1.00 21.58 O ANISOU 1505 O HOH A2031 3345 3068 1786 -663 -346 1031 O HETATM 1506 O HOH A2032 37.256 -15.167 25.836 1.00 19.46 O ANISOU 1506 O HOH A2032 1600 3695 2098 -188 -101 1177 O HETATM 1507 O HOH A2033 35.576 -14.982 23.690 1.00 20.02 O ANISOU 1507 O HOH A2033 1659 3898 2049 -161 210 677 O HETATM 1508 O HOH A2034 49.137 -3.694 -3.983 1.00 25.91 O ANISOU 1508 O HOH A2034 1797 1104 6943 -91 215 892 O HETATM 1509 O HOH A2035 48.451 15.002 -7.827 1.00 20.97 O ANISOU 1509 O HOH A2035 3576 1511 2880 -1106 554 -697 O HETATM 1510 O HOH A2036 23.660 -18.477 36.405 1.00 18.12 O ANISOU 1510 O HOH A2036 2422 2817 1646 -894 -73 -175 O HETATM 1511 O HOH A2037 28.956 -4.454 45.659 1.00 29.98 O ANISOU 1511 O HOH A2037 2068 3536 5787 428 -1277 -3095 O HETATM 1512 O HOH A2038 34.472 6.204 -10.276 1.00 20.50 O ANISOU 1512 O HOH A2038 2733 2217 2839 -1216 -1045 355 O HETATM 1513 O HOH A2039 33.741 16.608 -8.484 1.00 20.72 O ANISOU 1513 O HOH A2039 2883 2058 2931 -145 -631 134 O HETATM 1514 O HOH A2040 24.111 -14.449 48.050 1.00 18.73 O ANISOU 1514 O HOH A2040 2142 1555 3420 143 -1 949 O HETATM 1515 O AHOH A2041 44.207 4.663 -11.870 0.33 8.04 O ANISOU 1515 O AHOH A2041 1265 769 1023 -355 32 -43 O HETATM 1516 O BHOH A2042 44.917 5.551 -12.815 0.33 11.39 O ANISOU 1516 O BHOH A2042 1655 1283 1388 -186 63 -542 O HETATM 1517 O CHOH A2043 43.481 3.315 -12.617 0.33 10.33 O ANISOU 1517 O CHOH A2043 1649 1064 1211 -330 -108 -338 O HETATM 1518 O AHOH A2044 50.218 9.127 -3.434 0.33 9.19 O ANISOU 1518 O AHOH A2044 1117 1001 1374 199 -334 -183 O HETATM 1519 O BHOH A2045 49.736 10.701 -4.027 0.33 7.48 O ANISOU 1519 O BHOH A2045 1018 726 1097 -123 -512 -122 O HETATM 1520 O CHOH A2046 51.287 9.050 -2.513 0.33 11.21 O ANISOU 1520 O CHOH A2046 1748 1097 1416 374 -333 62 O HETATM 1521 O HOH A2047 47.397 3.482 -11.670 1.00 20.63 O ANISOU 1521 O HOH A2047 2579 2275 2984 -186 468 -864 O HETATM 1522 O HOH A2048 16.293 -17.085 25.525 1.00 30.98 O ANISOU 1522 O HOH A2048 3938 2807 5026 -269 3132 72 O HETATM 1523 O HOH A2049 25.164 -21.850 32.473 1.00 21.55 O ANISOU 1523 O HOH A2049 3106 1886 3196 -1009 -1134 515 O HETATM 1524 O HOH A2050 25.731 -13.988 14.636 1.00 24.46 O ANISOU 1524 O HOH A2050 2866 4590 1837 -183 -798 -469 O HETATM 1525 O HOH A2051 31.745 8.394 -7.046 1.00 25.10 O ANISOU 1525 O HOH A2051 5320 1669 2547 -1788 -1586 668 O HETATM 1526 O HOH A2052 26.999 -17.592 47.052 1.00 34.68 O ANISOU 1526 O HOH A2052 6884 1673 4618 -820 -3553 570 O HETATM 1527 O HOH A2053 15.486 -21.459 23.871 1.00 25.28 O ANISOU 1527 O HOH A2053 2687 2558 4359 -1118 1656 -863 O HETATM 1528 O HOH A2054 31.784 -19.349 35.227 1.00 24.96 O ANISOU 1528 O HOH A2054 2962 3319 3204 563 -524 1205 O HETATM 1529 O HOH A2055 20.516 -8.178 28.667 1.00 21.77 O ANISOU 1529 O HOH A2055 3056 2487 2728 -597 -258 -64 O HETATM 1530 O HOH A2056 33.690 -6.382 -13.311 1.00 26.11 O ANISOU 1530 O HOH A2056 4594 2986 2340 414 -715 -1124 O HETATM 1531 O HOH A2057 18.395 -21.278 35.724 1.00 29.60 O ANISOU 1531 O HOH A2057 5373 2809 3064 -589 829 441 O HETATM 1532 O HOH A2058 28.258 -13.517 16.993 1.00 26.77 O ANISOU 1532 O HOH A2058 4393 3632 2145 304 890 -717 O HETATM 1533 O HOH A2059 33.145 -21.122 31.767 1.00 27.90 O ANISOU 1533 O HOH A2059 3806 3703 3092 1795 326 1349 O HETATM 1534 O HOH A2060 46.453 -0.102 -10.432 1.00 24.45 O ANISOU 1534 O HOH A2060 4282 1463 3544 225 1548 596 O HETATM 1535 O HOH A2061 15.569 -18.233 30.784 1.00 30.01 O ANISOU 1535 O HOH A2061 3443 3683 4275 986 -632 358 O HETATM 1536 O HOH A2062 50.446 9.900 -0.399 1.00 24.97 O ANISOU 1536 O HOH A2062 3612 3117 2758 384 -878 -91 O HETATM 1537 O HOH A2063 40.283 -3.190 -10.892 1.00 29.39 O ANISOU 1537 O HOH A2063 5875 2085 3208 1422 1155 1090 O HETATM 1538 O HOH A2064 39.387 3.086 -12.642 1.00 26.45 O ANISOU 1538 O HOH A2064 4416 3057 2576 511 -861 -537 O HETATM 1539 O HOH A2065 36.943 -15.021 40.078 1.00 30.53 O ANISOU 1539 O HOH A2065 2017 3403 6179 658 448 1391 O HETATM 1540 O AHOH A2066 28.229 -0.346 -7.875 0.50 16.14 O ANISOU 1540 O AHOH A2066 889 1620 3621 546 -354 332 O HETATM 1541 O BHOH A2067 28.242 1.640 -7.765 0.50 18.24 O ANISOU 1541 O BHOH A2067 1546 1273 4111 432 292 940 O HETATM 1542 O HOH A2068 18.045 -17.159 29.531 1.00 22.90 O ANISOU 1542 O HOH A2068 2382 3397 2922 -36 -656 -386 O HETATM 1543 O HOH A2069 31.525 -17.270 41.211 1.00 31.52 O ANISOU 1543 O HOH A2069 2671 6699 2606 -1672 -1059 1043 O HETATM 1544 O HOH A2070 32.863 1.752 -12.347 1.00 31.70 O ANISOU 1544 O HOH A2070 5844 3564 2639 2412 -268 309 O HETATM 1545 O HOH A2071 20.972 -18.610 35.394 1.00 28.01 O ANISOU 1545 O HOH A2071 3017 4667 2958 -975 1383 -583 O HETATM 1546 O HOH A2072 28.748 -3.705 -3.267 1.00 34.68 O ANISOU 1546 O HOH A2072 2096 2647 8433 -79 321 2826 O HETATM 1547 O HOH A2073 15.587 -16.467 16.379 1.00 32.32 O ANISOU 1547 O HOH A2073 1796 7329 3156 236 -441 -2028 O HETATM 1548 O HOH A2074 29.658 -22.002 31.223 1.00 29.80 O ANISOU 1548 O HOH A2074 3148 2023 6152 777 -1103 -157 O HETATM 1549 O HOH A2075 11.848 -19.490 39.935 1.00 31.49 O ANISOU 1549 O HOH A2075 2628 3687 5652 -588 -420 1449 O HETATM 1550 O HOH A2076 15.520 -15.402 22.225 1.00 31.54 O ANISOU 1550 O HOH A2076 4672 4970 2341 -1503 119 -235 O HETATM 1551 O HOH A2077 39.228 -19.578 28.304 1.00 30.97 O ANISOU 1551 O HOH A2077 2360 4808 4598 426 319 327 O HETATM 1552 O HOH A2078 11.322 -9.487 36.308 1.00 32.13 O ANISOU 1552 O HOH A2078 3370 5299 3537 943 695 -263 O HETATM 1553 O HOH A2079 41.463 -8.024 20.962 1.00 29.34 O ANISOU 1553 O HOH A2079 2080 4803 4265 -814 -869 -134 O HETATM 1554 O HOH A2080 46.531 0.288 -6.478 1.00 30.19 O ANISOU 1554 O HOH A2080 2682 2419 6372 -92 891 -817 O HETATM 1555 O HOH A2081 28.505 -22.554 26.178 1.00 35.77 O ANISOU 1555 O HOH A2081 2961 2821 7810 653 -2212 -717 O HETATM 1556 O HOH A2082 26.111 -18.062 17.264 1.00 35.20 O ANISOU 1556 O HOH A2082 4451 3739 5184 1023 -285 -2081 O HETATM 1557 O HOH A2083 28.956 -8.336 -3.895 1.00 40.58 O ANISOU 1557 O HOH A2083 3825 4834 6758 771 1988 2585 O HETATM 1558 O HOH A2084 28.838 11.990 -8.810 1.00 30.27 O ANISOU 1558 O HOH A2084 1832 5945 3724 -567 -461 1226 O HETATM 1559 O HOH A2085 14.146 -15.462 34.876 1.00 28.44 O ANISOU 1559 O HOH A2085 1966 4936 3905 -341 -835 761 O HETATM 1560 O HOH A2086 41.018 14.774 -6.961 1.00 13.41 O ANISOU 1560 O HOH A2086 2018 1042 2036 332 -391 -85 O HETATM 1561 O HOH A2087 23.068 -16.227 49.942 1.00 16.27 O ANISOU 1561 O HOH A2087 2237 1668 2279 -388 -883 609 O HETATM 1562 O HOH A2088 28.790 9.197 -5.602 1.00 18.68 O ANISOU 1562 O HOH A2088 2085 2560 2451 -624 -714 483 O HETATM 1563 O HOH A2089 13.505 -21.891 40.162 1.00 21.85 O ANISOU 1563 O HOH A2089 2307 3116 2880 -509 -489 -601 O HETATM 1564 O HOH A2090 17.746 -22.206 38.316 1.00 22.80 O ANISOU 1564 O HOH A2090 3076 2731 2857 -557 -124 -658 O HETATM 1565 O HOH A2091 49.941 2.266 -12.115 1.00 30.06 O ANISOU 1565 O HOH A2091 3859 2894 4668 780 1954 -351 O HETATM 1566 O HOH A2092 29.078 -17.394 40.211 1.00 24.67 O ANISOU 1566 O HOH A2092 2279 5146 1948 -617 -412 668 O HETATM 1567 O HOH A2093 14.282 -12.479 41.334 1.00 18.84 O ANISOU 1567 O HOH A2093 2765 2104 2290 -433 -215 286 O HETATM 1568 O HOH A2094 45.616 1.495 -12.291 1.00 22.63 O ANISOU 1568 O HOH A2094 3109 2305 3185 132 -180 -263 O HETATM 1569 O HOH A2095 43.962 -6.979 20.675 1.00 23.43 O ANISOU 1569 O HOH A2095 2145 3534 3224 436 -620 -122 O HETATM 1570 O HOH A2096 34.096 -2.838 38.969 1.00 27.61 O ANISOU 1570 O HOH A2096 4038 3072 3380 399 -1060 901 O HETATM 1571 O HOH A2097 37.858 -3.308 -12.223 1.00 30.27 O ANISOU 1571 O HOH A2097 4549 2581 4373 1177 1488 1705 O HETATM 1572 O HOH A2098 27.988 13.514 -10.750 1.00 30.50 O ANISOU 1572 O HOH A2098 4411 4001 3175 -151 -1748 705 O HETATM 1573 O HOH A2099 31.491 -2.699 39.010 1.00 34.83 O ANISOU 1573 O HOH A2099 4619 3171 5443 -629 606 1848 O HETATM 1574 O HOH A2100 30.500 -0.552 -12.203 1.00 34.35 O ANISOU 1574 O HOH A2100 5618 3391 4042 925 -1358 1000 O HETATM 1575 O HOH A2101 23.055 -22.517 30.895 1.00 41.33 O ANISOU 1575 O HOH A2101 6061 4378 5266 -3240 -2015 2137 O HETATM 1576 O HOH A2102 32.697 -14.477 41.218 1.00 30.96 O ANISOU 1576 O HOH A2102 3725 4325 3712 41 -760 1758 O HETATM 1577 O HOH A2103 26.549 -23.790 28.538 1.00 37.33 O ANISOU 1577 O HOH A2103 6377 3851 3956 2119 -1668 716 O HETATM 1578 O HOH A2104 11.478 -14.774 35.326 1.00 31.02 O ANISOU 1578 O HOH A2104 1989 5453 4343 -244 -743 1086 O HETATM 1579 O HOH A2105 28.056 -6.616 -6.850 1.00 38.06 O ANISOU 1579 O HOH A2105 2896 7786 3780 294 -670 -1041 O HETATM 1580 O HOH A2106 36.197 -2.990 27.461 1.00 29.68 O ANISOU 1580 O HOH A2106 4127 4742 2408 -1148 261 -88 O HETATM 1581 O HOH A2107 16.712 -7.855 39.856 1.00 30.20 O ANISOU 1581 O HOH A2107 6475 2478 2523 1899 -1087 -330 O HETATM 1582 O HOH A2108 12.346 -4.992 29.012 1.00 45.21 O ANISOU 1582 O HOH A2108 3953 5986 7238 85 132 2059 O HETATM 1583 O HOH A2109 10.155 -12.003 36.709 1.00 30.46 O ANISOU 1583 O HOH A2109 3040 5391 3144 499 -143 -659 O HETATM 1584 O HOH A2110 40.058 15.687 5.385 1.00 31.23 O ANISOU 1584 O HOH A2110 4408 4397 3061 -502 -159 -743 O HETATM 1585 O HOH A2111 34.298 10.749 6.300 1.00 36.71 O ANISOU 1585 O HOH A2111 3130 6610 4206 -1274 -1161 1748 O HETATM 1586 O HOH A2112 49.250 -0.811 -10.669 1.00 34.23 O ANISOU 1586 O HOH A2112 3312 5350 4343 326 811 -1704 O HETATM 1587 O HOH A2113 54.037 8.829 0.426 1.00 32.37 O ANISOU 1587 O HOH A2113 2490 4792 5020 -1216 564 -798 O HETATM 1588 O HOH A2114 27.204 -23.904 33.047 1.00 39.38 O ANISOU 1588 O HOH A2114 7651 3085 4228 -1065 450 568 O HETATM 1589 O HOH A2115 31.012 -20.152 38.014 1.00 34.73 O ANISOU 1589 O HOH A2115 3086 5025 5083 1158 50 933 O HETATM 1590 O HOH A2116 46.425 19.891 13.066 1.00 38.24 O ANISOU 1590 O HOH A2116 4236 4889 5405 402 -419 1227 O HETATM 1591 O HOH A2117 13.323 -22.008 24.319 1.00 34.66 O ANISOU 1591 O HOH A2117 5075 4313 3780 770 1437 -455 O HETATM 1592 O HOH A2118 34.988 13.024 3.462 1.00 37.72 O ANISOU 1592 O HOH A2118 5139 4743 4448 1985 -1852 -2073 O HETATM 1593 O HOH A2119 43.378 15.388 18.789 1.00 37.05 O ANISOU 1593 O HOH A2119 1755 5343 6978 846 -665 -818 O HETATM 1594 O HOH A2120 11.628 -7.194 35.152 1.00 34.74 O ANISOU 1594 O HOH A2120 5382 4614 3205 562 110 -319 O HETATM 1595 O HOH A2121 35.496 1.898 0.764 1.00 38.61 O ANISOU 1595 O HOH A2121 8466 2921 3283 923 -2247 -207 O HETATM 1596 O HOH A2122 44.846 7.205 -10.602 1.00 10.47 O ANISOU 1596 O HOH A2122 1196 1221 1563 -288 -311 -76 O HETATM 1597 O HOH A2123 34.133 -10.927 -7.266 1.00 11.31 O ANISOU 1597 O HOH A2123 1535 882 1882 -223 -523 177 O HETATM 1598 O HOH A2124 34.869 -10.511 -4.411 1.00 12.42 O ANISOU 1598 O HOH A2124 1507 1129 2082 68 -393 -93 O HETATM 1599 O HOH A2125 31.016 -10.538 -7.141 1.00 14.55 O ANISOU 1599 O HOH A2125 1686 1230 2611 -322 -567 507 O HETATM 1600 O HOH A2126 32.204 -10.618 -3.104 1.00 13.84 O ANISOU 1600 O HOH A2126 2118 977 2165 -32 -280 119 O HETATM 1601 O HOH A2127 38.095 14.626 -4.782 1.00 10.00 O ANISOU 1601 O HOH A2127 1390 940 1472 101 -287 15 O HETATM 1602 O HOH A2128 30.336 -21.323 27.900 1.00 20.07 O ANISOU 1602 O HOH A2128 2637 2157 2833 -361 720 -496 O HETATM 1603 O HOH A2129 24.034 -17.418 20.784 1.00 13.22 O ANISOU 1603 O HOH A2129 1336 2307 1380 13 -104 -166 O HETATM 1604 O HOH A2130 54.504 10.989 0.679 1.00 31.62 O ANISOU 1604 O HOH A2130 2390 5962 3662 -1983 1059 -1732 O HETATM 1605 O HOH A2131 14.288 -12.648 38.691 1.00 26.44 O ANISOU 1605 O HOH A2131 2821 3485 3738 -145 -281 -805 O HETATM 1606 O HOH A2132 51.344 8.866 15.549 1.00 34.98 O ANISOU 1606 O HOH A2132 5324 3380 4587 -417 -41 -444 O HETATM 1607 O HOH A2133 35.549 16.220 0.968 1.00 29.81 O ANISOU 1607 O HOH A2133 4368 4442 2515 -1362 -180 -594 O HETATM 1608 O HOH A2134 50.710 18.958 12.127 1.00 38.85 O ANISOU 1608 O HOH A2134 6513 5317 2930 321 -2981 69 O HETATM 1609 O HOH A2135 26.874 -2.390 39.940 1.00 31.54 O ANISOU 1609 O HOH A2135 5196 3069 3718 -523 260 -225 O HETATM 1610 O HOH A2136 24.232 -22.923 34.520 1.00 36.16 O ANISOU 1610 O HOH A2136 5527 3831 4382 -1972 631 -202 O HETATM 1611 O HOH A2137 37.758 2.743 1.818 1.00 34.10 O ANISOU 1611 O HOH A2137 3859 5122 3975 155 608 42 O HETATM 1612 O HOH A2138 32.486 -23.743 19.584 1.00 36.99 O ANISOU 1612 O HOH A2138 7124 2770 4161 -809 1801 -500 O HETATM 1613 O HOH A2139 28.537 10.101 -10.082 1.00 38.26 O ANISOU 1613 O HOH A2139 4266 5226 5047 -2026 -1457 2017 O HETATM 1614 O HOH A2140 48.262 7.843 12.020 1.00 33.39 O ANISOU 1614 O HOH A2140 3796 4932 3959 146 158 279 O HETATM 1615 O HOH A2141 20.126 -18.971 29.987 1.00 38.03 O ANISOU 1615 O HOH A2141 3862 7056 3533 -658 559 2159 O HETATM 1616 O HOH A2142 31.325 -21.709 33.349 1.00 41.34 O ANISOU 1616 O HOH A2142 4909 6175 4624 42 -482 3036 O HETATM 1617 O HOH A2143 17.558 -9.167 35.767 1.00 31.17 O ANISOU 1617 O HOH A2143 4455 3474 3913 17 -30 341 O HETATM 1618 O HOH A2144 14.755 -10.646 37.436 1.00 39.09 O ANISOU 1618 O HOH A2144 5216 6296 3342 508 -1175 1263 O HETATM 1619 O HOH A2145 28.210 0.410 -10.786 1.00 39.91 O ANISOU 1619 O HOH A2145 4518 4790 5856 1062 -460 -947 O HETATM 1620 O HOH A2146 31.958 -8.877 -0.889 1.00 41.14 O ANISOU 1620 O HOH A2146 6785 4193 4654 1804 -1029 -2411 O HETATM 1621 O HOH A2147 52.336 2.719 -11.133 1.00 39.73 O ANISOU 1621 O HOH A2147 4678 3833 6584 -447 1558 -2356 O HETATM 1622 O HOH A2148 15.782 -25.622 38.405 1.00 49.95 O ANISOU 1622 O HOH A2148 4982 8385 5612 -2872 -2171 -44 O HETATM 1623 O HOH A2149 25.784 -13.682 49.774 1.00 41.68 O ANISOU 1623 O HOH A2149 4563 6245 5028 -1688 75 975 O HETATM 1624 O HOH A2150 24.095 -21.106 35.938 1.00 43.78 O ANISOU 1624 O HOH A2150 5573 3715 7344 60 2629 1675 O HETATM 1625 O HOH A2151 55.502 10.834 3.254 1.00 44.34 O ANISOU 1625 O HOH A2151 2987 6732 7129 73 776 569 O HETATM 1626 O HOH A2152 39.636 15.429 7.957 1.00 40.60 O ANISOU 1626 O HOH A2152 5747 4545 5135 -149 -465 -2376 O HETATM 1627 O HOH A2153 15.626 -18.799 36.163 1.00 40.93 O ANISOU 1627 O HOH A2153 6110 4452 4989 312 463 -1955 O HETATM 1628 O HOH A2154 30.627 -22.589 20.476 1.00 41.87 O ANISOU 1628 O HOH A2154 6985 4112 4811 -1786 2608 -714 O HETATM 1629 O HOH A2155 28.295 -8.221 46.335 1.00 27.60 O ANISOU 1629 O HOH A2155 3930 2901 3655 -1036 -1376 1248 O HETATM 1630 O HOH A2156 35.232 4.130 -11.736 1.00 33.35 O ANISOU 1630 O HOH A2156 5015 4039 3616 -1341 -837 -553 O HETATM 1631 O HOH A2157 29.782 -9.676 44.753 1.00 25.48 O ANISOU 1631 O HOH A2157 3546 3281 2855 -26 269 363 O HETATM 1632 O HOH A2158 27.322 -21.607 37.930 1.00 38.67 O ANISOU 1632 O HOH A2158 5444 4155 5092 -1964 -405 400 O HETATM 1633 O HOH A2159 39.004 -22.581 27.995 1.00 37.05 O ANISOU 1633 O HOH A2159 3922 6049 4106 -15 421 26 O HETATM 1634 O HOH A2160 31.707 8.248 -10.026 1.00 38.85 O ANISOU 1634 O HOH A2160 2787 6406 5566 -1599 -1048 2082 O HETATM 1635 O HOH A2161 12.461 -17.449 40.907 0.60 18.47 O ANISOU 1635 O HOH A2161 1998 3164 1856 -146 -892 777 O HETATM 1636 O HOH A2162 20.148 -20.536 31.989 1.00 38.29 O ANISOU 1636 O HOH A2162 4009 7624 2917 -2727 -1119 1574 O HETATM 1637 O HOH A2163 13.610 -8.988 39.913 1.00 35.06 O ANISOU 1637 O HOH A2163 6338 3072 3913 824 719 166 O HETATM 1638 O HOH A2164 31.426 -2.634 -0.089 1.00 42.14 O ANISOU 1638 O HOH A2164 5008 5203 5799 -1938 215 -1721 O HETATM 1639 O HOH A2165 46.501 8.766 14.370 1.00 47.02 O ANISOU 1639 O HOH A2165 5001 5698 7167 -1765 1128 -1584 O HETATM 1640 O HOH A2166 38.771 17.316 18.874 1.00 49.37 O ANISOU 1640 O HOH A2166 4083 6573 8102 1386 -247 -2279 O HETATM 1641 O HOH A2167 29.639 -1.703 43.748 1.00 44.48 O ANISOU 1641 O HOH A2167 2803 7178 6919 1904 -659 -1772 O HETATM 1642 O HOH A2168 50.504 -5.523 -4.771 1.00 34.24 O ANISOU 1642 O HOH A2168 3314 4699 4997 -911 -357 -738 O HETATM 1643 O HOH A2169 23.084 -7.778 29.256 1.00 42.05 O ANISOU 1643 O HOH A2169 3828 6752 5396 -1253 735 -932 O HETATM 1644 O HOH A2170 27.942 -16.414 49.674 1.00 42.67 O ANISOU 1644 O HOH A2170 5750 4861 5603 -2378 430 -1587 O HETATM 1645 O HOH A2171 42.750 -2.232 25.172 1.00 40.65 O ANISOU 1645 O HOH A2171 4187 3405 7851 -599 1874 -493 O HETATM 1646 O HOH A2172 25.329 -7.136 30.407 1.00 36.12 O ANISOU 1646 O HOH A2172 3941 5373 4411 -1079 -1045 969 O HETATM 1647 O HOH A2173 11.730 -12.749 34.283 1.00 40.97 O ANISOU 1647 O HOH A2173 4388 4054 7124 125 1621 762 O HETATM 1648 O HOH A2174 40.613 17.745 17.101 1.00 40.87 O ANISOU 1648 O HOH A2174 4378 5789 5360 634 -1192 640 O HETATM 1649 O HOH A2175 47.441 1.538 3.068 1.00 39.60 O ANISOU 1649 O HOH A2175 5682 4324 5039 -1542 436 284 O HETATM 1650 O HOH A2176 33.898 -7.037 -2.077 1.00 45.34 O ANISOU 1650 O HOH A2176 7010 3666 6552 518 -1305 1918 O HETATM 1651 O HOH A2177 43.807 -4.841 21.930 1.00 47.83 O ANISOU 1651 O HOH A2177 4646 7132 6395 -435 -914 592 O CONECT 195 1469 CONECT 212 1469 CONECT 224 1469 CONECT 233 1469 CONECT 275 1469 CONECT 276 1469 CONECT 415 1472 CONECT 416 1472 CONECT 503 1470 CONECT 516 1470 CONECT 528 1470 CONECT 537 1470 CONECT 582 1470 CONECT 583 1470 CONECT 933 1473 CONECT 952 1473 CONECT 964 1473 CONECT 973 1473 CONECT 1017 1473 CONECT 1018 1473 CONECT 1270 1471 CONECT 1286 1471 CONECT 1298 1471 CONECT 1307 1471 CONECT 1378 1471 CONECT 1379 1471 CONECT 1469 195 212 224 233 CONECT 1469 275 276 1596 CONECT 1470 503 516 528 537 CONECT 1470 582 583 1485 1601 CONECT 1471 1270 1286 1298 1307 CONECT 1471 1378 1379 1603 CONECT 1472 415 416 1597 1598 CONECT 1472 1599 1600 CONECT 1473 933 952 964 973 CONECT 1473 1017 1018 1602 CONECT 1485 1470 CONECT 1596 1469 CONECT 1597 1472 CONECT 1598 1472 CONECT 1599 1472 CONECT 1600 1472 CONECT 1601 1470 CONECT 1602 1473 CONECT 1603 1471 MASTER 321 0 5 7 2 0 10 6 1333 1 45 12 END If you find results from this site helpful for 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