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*** test_NM_2xu4 ***elNémo ID: 2402141053552747942Job options:ID = 2402141053552747942 JOBID = test_NM_2xu4 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 test_NM_2xu4 HEADER HYDROLASE 14-OCT-10 2XU4 TITLE CATHEPSIN L WITH A NITRILE INHIBITOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: CATHEPSIN L1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 114-333; COMPND 5 SYNONYM: MAJOR EXCRETED PROTEIN, MEP; COMPND 6 EC: 3.4.22.15; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HYDROLASE, DRUG DESIGN, THIOL PROTEASE EXPDTA X-RAY DIFFRACTION AUTHOR D.W.BANNER,J.M.BENZ,W.HAAP REVDAT 1 12-JAN-11 2XU4 0 JRNL AUTH L.A.HARDEGGER,B.KUHN,B.SPINNLER,L.ANSELM,R.ECABERT,M.STIHLE, JRNL AUTH 2 B.GSELL,R.THOMA,J.DIEZ,J.BENZ,J.M.PLANCHER,G.HARTMANN, JRNL AUTH 3 D.W.BANNER,W.HAAP,F.DIEDERICH JRNL TITL SYSTEMATIC INVESTIGATION OF HALOGEN BONDING IN JRNL TITL 2 PROTEIN-LIGAND INTERACTIONS. JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 50 314 2011 JRNL REFN ISSN 1433-7851 JRNL PMID 21184410 JRNL DOI 10.1002/ANIE.201006781 REMARK 2 REMARK 2 RESOLUTION. 1.12 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0081 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.12 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.68 REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE REMARK 3 COMPLETENESS FOR RANGE (%) : 95.80 REMARK 3 NUMBER OF REFLECTIONS : 72914 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.14171 REMARK 3 R VALUE (WORKING SET) : 0.14036 REMARK 3 FREE R VALUE : 0.16725 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 3814 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.120 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.149 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5037 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.46 REMARK 3 BIN R VALUE (WORKING SET) : 0.317 REMARK 3 BIN FREE R VALUE SET COUNT : 245 REMARK 3 BIN FREE R VALUE : 0.317 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1745 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 47 REMARK 3 SOLVENT ATOMS : 252 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 15.5 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.523 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.30 REMARK 3 B22 (A**2) : -1.30 REMARK 3 B33 (A**2) : 1.95 REMARK 3 B12 (A**2) : -0.65 REMARK 3 B13 (A**2) : 0.00 REMARK 3 B23 (A**2) : 0.00 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.031 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.032 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.031 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.591 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.983 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.976 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1848 ; 0.012 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 1247 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2515 ; 1.452 ; 1.971 REMARK 3 BOND ANGLES OTHERS (DEGREES): 3036 ; 0.875 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 233 ; 5.580 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 86 ;36.446 ;25.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 292 ;11.534 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;15.926 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 249 ; 0.086 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2131 ; 0.007 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 383 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 10561 ; 4.677 ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): 252 ;11.255 ; 5.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3039 ; 6.923 ; 5.000 REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS. ZERO OCCUPANCY HYDROGENS DELETED. REMARK 4 REMARK 4 2XU4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-OCT-10. REMARK 100 THE PDBE ID CODE IS EBI-45777. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-AUG-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 3.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.75 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SADABS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84484 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.10 REMARK 200 RESOLUTION RANGE LOW (A) : 50.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 10.14 REMARK 200 R MERGE (I) : 0.07 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.10 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.19 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 10.15 REMARK 200 R MERGE FOR SHELL (I) : 0.77 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.04 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: IN HOUSE STRUCTURE REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 42.4 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRIC ACID PH 3.5, 25 % REMARK 280 PEG 3350 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.47467 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 16.73733 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.10600 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 8.36867 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 41.84333 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 GLU A 176 REMARK 465 SER A 177 REMARK 465 ASP A 178 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 ASP A 162 15.36 -142.48 REMARK 500 SER A 174 -129.24 59.05 REMARK 500 ARG A 205 55.82 -118.21 REMARK 500 ALA A 214 63.95 -153.63 REMARK 500 REMARK 500 REMARK: NULL REMARK 600 REMARK 600 HETEROGEN REMARK 600 REMARK 600 DJT: ORIGINAL CRYSTALLISED COMPOUND WAS (2S,4R)-4-(2-CHLORO- REMARK 600 BENZENESULFONYL)-1-[1-(4-FLUORO-PHENYL)-CYCLOPROPANECARBONYL]- REMARK 600 PYRROLIDINE-2-CARBOXYLIC ACID (1-CYANO-CYCLOPROPYL)-AMIDE. REMARK 600 THIS REACTS WITH CYS TO FORM THE COMPOUND PRESENT VIA REDUCTION REMARK 600 OF THE TRIPLE BOND REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DJT A1221 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1223 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1MHW RELATED DB: PDB REMARK 900 DESIGN OF NON-COVALENT INHIBITORS OF HUMAN REMARK 900 CATHEPSIN L.FROM THE 96-RESIDUE PROREGION REMARK 900 TO OPTIMIZED TRIPEPTIDES REMARK 900 RELATED ID: 1CJL RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A CYSTEINE PROTEASE PROFORM REMARK 900 RELATED ID: 1CS8 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF PROCATHEPSIN L REMARK 900 RELATED ID: 2VHS RELATED DB: PDB REMARK 900 CATHSILICATEIN, A CHIMERA REMARK 900 RELATED ID: 1ICF RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED REMARK 900 P41 II FRAGMENT IN COMPLEX WITH CATHEPSIN L REMARK 900 RELATED ID: 2XU5 RELATED DB: PDB REMARK 900 CATHEPSIN L WITH A NITRILE INHIBITOR REMARK 900 RELATED ID: 2XU1 RELATED DB: PDB REMARK 900 CATHEPSIN L WITH A NITRILE INHIBITOR REMARK 900 RELATED ID: 2XU3 RELATED DB: PDB REMARK 900 CATHEPSIN L WITH A NITRILE INHIBITOR DBREF 2XU4 A 1 220 UNP P07711 CATL1_HUMAN 114 333 SEQRES 1 A 220 ALA PRO ARG SER VAL ASP TRP ARG GLU LYS GLY TYR VAL SEQRES 2 A 220 THR PRO VAL LYS ASN GLN GLY GLN CYS GLY SER CYS TRP SEQRES 3 A 220 ALA PHE SER ALA THR GLY ALA LEU GLU GLY GLN MET PHE SEQRES 4 A 220 ARG LYS THR GLY ARG LEU ILE SER LEU SER GLU GLN ASN SEQRES 5 A 220 LEU VAL ASP CYS SER GLY PRO GLN GLY ASN GLU GLY CYS SEQRES 6 A 220 ASN GLY GLY LEU MET ASP TYR ALA PHE GLN TYR VAL GLN SEQRES 7 A 220 ASP ASN GLY GLY LEU ASP SER GLU GLU SER TYR PRO TYR SEQRES 8 A 220 GLU ALA THR GLU GLU SER CYS LYS TYR ASN PRO LYS TYR SEQRES 9 A 220 SER VAL ALA ASN ASP THR GLY PHE VAL ASP ILE PRO LYS SEQRES 10 A 220 GLN GLU LYS ALA LEU MET LYS ALA VAL ALA THR VAL GLY SEQRES 11 A 220 PRO ILE SER VAL ALA ILE ASP ALA GLY HIS GLU SER PHE SEQRES 12 A 220 LEU PHE TYR LYS GLU GLY ILE TYR PHE GLU PRO ASP CYS SEQRES 13 A 220 SER SER GLU ASP MET ASP HIS GLY VAL LEU VAL VAL GLY SEQRES 14 A 220 TYR GLY PHE GLU SER THR GLU SER ASP ASN ASN LYS TYR SEQRES 15 A 220 TRP LEU VAL LYS ASN SER TRP GLY GLU GLU TRP GLY MET SEQRES 16 A 220 GLY GLY TYR VAL LYS MET ALA LYS ASP ARG ARG ASN HIS SEQRES 17 A 220 CYS GLY ILE ALA SER ALA ALA SER TYR PRO THR VAL HET DJT A1221 58 HET GOL A1222 12 HET GOL A1223 12 HETNAM DJT (2S,4R)-4-(2-CHLOROPHENYL)SULFONYL-1-[1-(4- HETNAM 2 DJT FLUOROPHENYL)CYCLOPROPYL]CARBONYL-N-[1- HETNAM 3 DJT (IMINOMETHYL)CYCLOPROPYL]PYRROLIDINE-2-CARBOXAMIDE HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN FORMUL 2 DJT C25 H25 CL F N3 O4 S FORMUL 3 GOL 2(C3 H8 O3) FORMUL 4 HOH *252(H2 O) HELIX 1 1 ARG A 8 GLY A 11 5 4 HELIX 2 2 SER A 24 GLY A 43 1 20 HELIX 3 3 SER A 49 SER A 57 1 9 HELIX 4 4 GLU A 63 GLY A 67 5 5 HELIX 5 5 LEU A 69 GLY A 81 1 13 HELIX 6 6 ASN A 101 LYS A 103 5 3 HELIX 7 7 GLN A 118 GLY A 130 1 13 HELIX 8 8 HIS A 140 PHE A 145 1 6 HELIX 9 9 ASN A 207 ILE A 211 5 5 SHEET 1 AA 2 VAL A 5 ASP A 6 0 SHEET 2 AA 2 HIS A 163 PHE A 172 1 O TYR A 170 N VAL A 5 SHEET 1 AB 2 ILE A 132 ILE A 136 0 SHEET 2 AB 2 HIS A 163 PHE A 172 -1 O HIS A 163 N ILE A 136 SHEET 1 AC 5 ILE A 150 TYR A 151 0 SHEET 2 AC 5 TYR A 198 ALA A 202 1 O LYS A 200 N TYR A 151 SHEET 3 AC 5 LYS A 181 LYS A 186 -1 O TRP A 183 N MET A 201 SHEET 4 AC 5 HIS A 163 PHE A 172 -1 O LEU A 166 N LYS A 186 SHEET 5 AC 5 ILE A 132 ILE A 136 -1 O ILE A 132 N VAL A 167 SHEET 1 AD 5 ILE A 150 TYR A 151 0 SHEET 2 AD 5 TYR A 198 ALA A 202 1 O LYS A 200 N TYR A 151 SHEET 3 AD 5 LYS A 181 LYS A 186 -1 O TRP A 183 N MET A 201 SHEET 4 AD 5 HIS A 163 PHE A 172 -1 O LEU A 166 N LYS A 186 SHEET 5 AD 5 VAL A 5 ASP A 6 1 O VAL A 5 N TYR A 170 SHEET 1 AE 2 LEU A 83 ASP A 84 0 SHEET 2 AE 2 SER A 105 ALA A 107 -1 N VAL A 106 O LEU A 83 SHEET 1 AF 2 GLY A 111 ASP A 114 0 SHEET 2 AF 2 SER A 216 THR A 219 -1 O TYR A 217 N VAL A 113 SSBOND 1 CYS A 22 CYS A 65 1555 1555 2.05 SSBOND 2 CYS A 56 CYS A 98 1555 1555 2.04 SSBOND 3 CYS A 156 CYS A 209 1555 1555 2.05 LINK SG CYS A 25 C5 DJT A1221 1555 1555 1.80 SITE 1 AC1 22 ARG A 8 GLU A 9 GLY A 11 GLN A 19 SITE 2 AC1 22 GLY A 23 SER A 24 CYS A 25 TRP A 26 SITE 3 AC1 22 GLU A 63 GLY A 67 GLY A 68 LEU A 69 SITE 4 AC1 22 MET A 70 ALA A 135 MET A 161 ASP A 162 SITE 5 AC1 22 HIS A 163 GLY A 164 ALA A 214 GOL A1222 SITE 6 AC1 22 HOH A2096 HOH A2250 SITE 1 AC2 9 ASP A 162 HIS A 163 GLU A 191 GLY A 196 SITE 2 AC2 9 DJT A1221 HOH A2218 HOH A2223 HOH A2251 SITE 3 AC2 9 HOH A2252 SITE 1 AC3 1 ASN A 18 CRYST1 85.362 85.362 50.212 90.00 90.00 120.00 P 65 6 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 0.011715 0.006764 0.000000 0.00000 SCALE2 0.000000 0.013527 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019916 0.00000 ATOM 1 N ALA A 1 25.572 37.376 7.952 1.00 28.04 N ANISOU 1 N ALA A 1 2842 3265 4545 -504 -450 -805 N ATOM 2 CA ALA A 1 24.703 36.828 6.865 1.00 21.94 C ANISOU 2 CA ALA A 1 2641 2451 3243 -209 217 -416 C ATOM 3 C ALA A 1 23.245 37.214 7.113 1.00 18.66 C ANISOU 3 C ALA A 1 2616 1815 2657 -437 -39 -681 C ATOM 4 O ALA A 1 22.902 37.610 8.225 1.00 19.03 O ANISOU 4 O ALA A 1 2553 2107 2568 -296 -183 -699 O ATOM 5 CB ALA A 1 24.854 35.303 6.817 1.00 23.12 C ANISOU 5 CB ALA A 1 2341 2390 4051 -246 265 -276 C ATOM 6 HA ALA A 1 24.991 37.201 6.006 1.00 23.82 H ANISOU 6 HA ALA A 1 2821 2640 3588 -83 418 -72 H ATOM 7 N PRO A 2 22.377 37.093 6.086 1.00 18.06 N ANISOU 7 N PRO A 2 2737 1759 2364 -428 139 -425 N ATOM 8 CA PRO A 2 20.957 37.282 6.345 1.00 18.09 C ANISOU 8 CA PRO A 2 2601 1873 2397 -49 -202 -138 C ATOM 9 C PRO A 2 20.434 36.266 7.369 1.00 16.64 C ANISOU 9 C PRO A 2 2154 2087 2078 -131 -366 -290 C ATOM 10 O PRO A 2 21.084 35.258 7.619 1.00 18.33 O ANISOU 10 O PRO A 2 2606 1832 2527 -80 -469 -349 O ATOM 11 CB PRO A 2 20.318 37.067 4.960 1.00 19.30 C ANISOU 11 CB PRO A 2 3263 2113 1956 -49 31 103 C ATOM 12 CG PRO A 2 21.403 37.265 3.998 1.00 22.08 C ANISOU 12 CG PRO A 2 3029 2592 2766 -434 160 -179 C ATOM 13 CD PRO A 2 22.627 36.771 4.669 1.00 20.84 C ANISOU 13 CD PRO A 2 3230 2472 2213 -350 185 -115 C ATOM 14 HA PRO A 2 20.777 38.190 6.658 1.00 19.49 H ANISOU 14 HA PRO A 2 2912 1995 2496 32 -81 -236 H ATOM 15 HB2 PRO A 2 19.964 36.167 4.894 1.00 18.66 H ANISOU 15 HB2 PRO A 2 2531 2340 2218 -123 -147 -161 H ATOM 16 HB3 PRO A 2 19.616 37.722 4.822 1.00 19.60 H ANISOU 16 HB3 PRO A 2 2820 2345 2280 -177 -222 -2 H ATOM 17 HG2 PRO A 2 21.223 36.752 3.195 1.00 20.33 H ANISOU 17 HG2 PRO A 2 2701 2564 2460 -29 292 -64 H ATOM 18 HG3 PRO A 2 21.485 38.209 3.789 1.00 20.95 H ANISOU 18 HG3 PRO A 2 2817 2639 2504 -271 265 -62 H ATOM 19 HD2 PRO A 2 22.713 35.813 4.553 1.00 19.96 H ANISOU 19 HD2 PRO A 2 3127 2552 1903 -275 217 -411 H ATOM 20 HD3 PRO A 2 23.406 37.245 4.340 1.00 20.72 H ANISOU 20 HD3 PRO A 2 2920 2496 2454 -90 252 -122 H ATOM 21 N ARG A 3 19.284 36.551 7.951 1.00 16.60 N ANISOU 21 N ARG A 3 2318 1961 2029 -114 -223 -370 N ATOM 22 CA ARG A 3 18.648 35.646 8.909 1.00 16.36 C ANISOU 22 CA ARG A 3 2121 1955 2139 -122 -350 -316 C ATOM 23 C ARG A 3 17.875 34.527 8.221 1.00 14.35 C ANISOU 23 C ARG A 3 2056 2110 1283 -196 -316 4 C ATOM 24 O ARG A 3 17.574 33.512 8.827 1.00 15.21 O ANISOU 24 O ARG A 3 2542 2002 1234 -126 -509 11 O ATOM 25 CB ARG A 3 17.689 36.410 9.808 1.00 16.37 C ANISOU 25 CB ARG A 3 2481 2059 1678 -106 -208 -107 C ATOM 26 CG ARG A 3 18.235 37.627 10.550 1.00 20.38 C ANISOU 26 CG ARG A 3 2950 2504 2288 -150 -161 -686 C ATOM 27 CD ARG A 3 19.570 37.334 11.109 1.00 19.83 C ANISOU 27 CD ARG A 3 3147 2470 1917 97 -284 -895 C ATOM 28 NE ARG A 3 20.110 38.467 11.863 1.00 19.03 N ANISOU 28 NE ARG A 3 3045 2339 1847 169 -582 -686 N ATOM 29 CZ ARG A 3 21.367 38.529 12.292 1.00 20.39 C ANISOU 29 CZ ARG A 3 2894 2475 2376 -37 -419 -697 C ATOM 30 NH1 ARG A 3 22.216 37.526 12.064 1.00 23.12 N ANISOU 30 NH1 ARG A 3 2805 2648 3330 91 -822 -693 N ATOM 31 NH2 ARG A 3 21.784 39.602 12.941 1.00 21.61 N ANISOU 31 NH2 ARG A 3 3205 2440 2564 -83 -591 -725 N ATOM 32 H ARG A 3 18.839 37.272 7.803 1.00 17.36 H ANISOU 32 H ARG A 3 2275 2113 2206 -56 -164 -164 H ATOM 33 HA ARG A 3 19.330 35.226 9.473 1.00 16.15 H ANISOU 33 HA ARG A 3 2020 2230 1886 -293 -352 -300 H ATOM 34 HB2 ARG A 3 16.948 36.720 9.264 1.00 16.37 H ANISOU 34 HB2 ARG A 3 2188 2059 1970 -57 -56 -1 H ATOM 35 HB3 ARG A 3 17.354 35.795 10.480 1.00 18.52 H ANISOU 35 HB3 ARG A 3 2683 2291 2060 -18 -71 178 H ATOM 36 HG2 ARG A 3 18.318 38.372 9.935 1.00 18.43 H ANISOU 36 HG2 ARG A 3 2049 2307 2645 -238 7 -597 H ATOM 37 HG3 ARG A 3 17.635 37.847 11.277 1.00 19.63 H ANISOU 37 HG3 ARG A 3 2983 2194 2280 -107 -112 -456 H ATOM 38 HD2 ARG A 3 19.512 36.569 11.703 1.00 19.84 H ANISOU 38 HD2 ARG A 3 2361 2569 2606 -164 102 -545 H ATOM 39 HD3 ARG A 3 20.184 37.152 10.383 1.00 18.16 H ANISOU 39 HD3 ARG A 3 2907 1853 2138 -69 -172 -603 H ATOM 40 HE ARG A 3 19.619 39.301 11.811 1.00 18.80 H ANISOU 40 HE ARG A 3 2828 2139 2174 -49 -115 -458 H ATOM 41 HH11 ARG A 3 21.967 36.823 11.638 1.00 18.62 H ANISOU 41 HH11 ARG A 3 2464 2331 2279 -38 -80 -267 H ATOM 42 HH12 ARG A 3 23.025 37.578 12.350 1.00 20.49 H ANISOU 42 HH12 ARG A 3 2522 2752 2510 -202 -226 -243 H ATOM 43 HH21 ARG A 3 21.242 40.252 13.097 1.00 19.46 H ANISOU 43 HH21 ARG A 3 2927 2408 2056 -212 -333 -525 H ATOM 44 HH22 ARG A 3 22.592 39.642 13.230 1.00 19.36 H ANISOU 44 HH22 ARG A 3 2791 2268 2294 -333 -14 -455 H ATOM 45 N SER A 4 17.548 34.734 6.953 1.00 14.62 N ANISOU 45 N SER A 4 2634 1585 1334 -215 -507 -83 N ATOM 46 CA SER A 4 16.933 33.696 6.121 1.00 15.66 C ANISOU 46 CA SER A 4 2478 1908 1564 -252 -484 -340 C ATOM 47 C SER A 4 17.334 33.851 4.684 1.00 15.02 C ANISOU 47 C SER A 4 2355 1905 1445 0 -602 -228 C ATOM 48 O SER A 4 17.546 34.975 4.206 1.00 18.38 O ANISOU 48 O SER A 4 3029 1796 2158 -333 -241 -278 O ATOM 49 CB SER A 4 15.428 33.680 6.269 1.00 19.33 C ANISOU 49 CB SER A 4 2487 2581 2275 -271 -273 -320 C ATOM 50 OG SER A 4 14.856 34.847 5.792 1.00 24.30 O ANISOU 50 OG SER A 4 2841 3116 3275 129 -818 -80 O ATOM 51 H SER A 4 17.660 35.479 6.539 1.00 14.11 H ANISOU 51 H SER A 4 2190 1671 1497 -139 -339 37 H ATOM 52 HA SER A 4 17.263 32.826 6.424 1.00 15.13 H ANISOU 52 HA SER A 4 2462 1730 1555 -437 -213 -250 H ATOM 53 HB2 SER A 4 15.074 32.930 5.768 1.00 19.42 H ANISOU 53 HB2 SER A 4 2329 2794 2254 -479 -200 -286 H ATOM 54 HB3 SER A 4 15.207 33.583 7.208 1.00 20.39 H ANISOU 54 HB3 SER A 4 2624 2779 2341 -194 -78 -407 H ATOM 55 N VAL A 5 17.477 32.713 4.012 1.00 14.33 N ANISOU 55 N VAL A 5 2034 1743 1667 -136 -405 -150 N ATOM 56 CA VAL A 5 17.855 32.621 2.617 1.00 14.42 C ANISOU 56 CA VAL A 5 2175 1630 1674 -65 -405 -59 C ATOM 57 C VAL A 5 17.031 31.488 2.012 1.00 13.92 C ANISOU 57 C VAL A 5 2284 1638 1366 -125 -474 40 C ATOM 58 O VAL A 5 16.863 30.425 2.590 1.00 13.98 O ANISOU 58 O VAL A 5 2347 1596 1368 -45 -622 54 O ATOM 59 CB VAL A 5 19.358 32.328 2.466 1.00 14.44 C ANISOU 59 CB VAL A 5 2172 1638 1677 -110 -294 -39 C ATOM 60 CG1 VAL A 5 19.745 31.986 1.038 1.00 16.32 C ANISOU 60 CG1 VAL A 5 2449 2169 1581 -296 -358 -107 C ATOM 61 CG2 VAL A 5 20.192 33.501 3.034 1.00 16.15 C ANISOU 61 CG2 VAL A 5 2335 1943 1858 -343 -389 -131 C ATOM 62 H VAL A 5 17.355 31.941 4.371 1.00 15.24 H ANISOU 62 H VAL A 5 2190 1824 1774 -73 -203 -38 H ATOM 63 HA VAL A 5 17.639 33.455 2.148 1.00 14.77 H ANISOU 63 HA VAL A 5 2201 1615 1794 -89 -301 -9 H ATOM 64 HB VAL A 5 19.566 31.541 3.012 1.00 14.52 H ANISOU 64 HB VAL A 5 2057 1755 1703 -35 -139 54 H ATOM 65 N ASP A 6 16.537 31.701 0.808 1.00 13.17 N ANISOU 65 N ASP A 6 2076 1634 1293 -44 -328 56 N ATOM 66 CA ASP A 6 15.817 30.638 0.075 1.00 13.24 C ANISOU 66 CA ASP A 6 1916 1661 1451 51 -463 16 C ATOM 67 C ASP A 6 16.051 30.795 -1.417 1.00 13.21 C ANISOU 67 C ASP A 6 1960 1589 1467 92 -478 -27 C ATOM 68 O ASP A 6 15.371 31.566 -2.070 1.00 13.99 O ANISOU 68 O ASP A 6 2072 1739 1502 132 -536 145 O ATOM 69 CB ASP A 6 14.340 30.630 0.444 1.00 14.98 C ANISOU 69 CB ASP A 6 1987 1737 1965 -20 -291 -26 C ATOM 70 CG ASP A 6 13.595 29.420 -0.108 1.00 13.71 C ANISOU 70 CG ASP A 6 1975 2008 1223 -82 -404 -36 C ATOM 71 OD1 ASP A 6 14.103 28.751 -1.017 1.00 14.67 O ANISOU 71 OD1 ASP A 6 2107 1899 1565 -111 -195 10 O ATOM 72 OD2 ASP A 6 12.468 29.186 0.360 1.00 17.03 O ANISOU 72 OD2 ASP A 6 2026 2159 2284 -229 -118 -114 O ATOM 73 H ASP A 6 16.594 32.446 0.382 1.00 13.15 H ANISOU 73 H ASP A 6 1993 1591 1413 57 -297 69 H ATOM 74 HA ASP A 6 16.184 29.766 0.333 1.00 13.50 H ANISOU 74 HA ASP A 6 2000 1591 1538 -5 -326 65 H ATOM 75 HB2 ASP A 6 14.259 30.612 1.410 1.00 13.04 H ANISOU 75 HB2 ASP A 6 1760 1260 1934 -168 -337 -146 H ATOM 76 HB3 ASP A 6 13.917 31.429 0.094 1.00 14.83 H ANISOU 76 HB3 ASP A 6 1892 1884 1857 85 -187 0 H ATOM 77 N TRP A 7 17.044 30.094 -1.955 1.00 12.79 N ANISOU 77 N TRP A 7 1682 1810 1365 47 -459 65 N ATOM 78 CA TRP A 7 17.402 30.174 -3.364 1.00 12.76 C ANISOU 78 CA TRP A 7 1822 1574 1452 -79 -368 131 C ATOM 79 C TRP A 7 16.293 29.692 -4.295 1.00 12.95 C ANISOU 79 C TRP A 7 1689 1888 1342 0 -211 -99 C ATOM 80 O TRP A 7 16.323 29.997 -5.479 1.00 13.67 O ANISOU 80 O TRP A 7 1835 1907 1449 -50 -401 140 O ATOM 81 CB TRP A 7 18.725 29.439 -3.659 1.00 13.24 C ANISOU 81 CB TRP A 7 1800 1810 1417 -62 -390 2 C ATOM 82 CG TRP A 7 19.922 30.119 -2.991 1.00 13.34 C ANISOU 82 CG TRP A 7 1909 1781 1376 -117 -426 -43 C ATOM 83 CD1 TRP A 7 20.653 29.677 -1.924 1.00 13.64 C ANISOU 83 CD1 TRP A 7 1758 1838 1584 -13 -380 119 C ATOM 84 CD2 TRP A 7 20.449 31.406 -3.323 1.00 14.01 C ANISOU 84 CD2 TRP A 7 1952 1910 1459 -150 -425 140 C ATOM 85 NE1 TRP A 7 21.612 30.583 -1.616 1.00 15.87 N ANISOU 85 NE1 TRP A 7 1866 1990 2171 -85 -747 299 N ATOM 86 CE2 TRP A 7 21.515 31.653 -2.457 1.00 14.60 C ANISOU 86 CE2 TRP A 7 1887 1979 1679 -307 -455 145 C ATOM 87 CE3 TRP A 7 20.129 32.363 -4.289 1.00 15.47 C ANISOU 87 CE3 TRP A 7 2209 2002 1663 -131 -533 259 C ATOM 88 CZ2 TRP A 7 22.262 32.822 -2.503 1.00 16.87 C ANISOU 88 CZ2 TRP A 7 2121 2065 2222 -436 -493 321 C ATOM 89 CZ3 TRP A 7 20.877 33.519 -4.362 1.00 17.87 C ANISOU 89 CZ3 TRP A 7 2491 2120 2178 -310 -580 282 C ATOM 90 CH2 TRP A 7 21.928 33.744 -3.465 1.00 16.98 C ANISOU 90 CH2 TRP A 7 2538 1974 1938 -382 -474 191 C ATOM 91 H TRP A 7 17.535 29.548 -1.507 1.00 12.36 H ANISOU 91 H TRP A 7 1738 1543 1414 -1 -354 72 H ATOM 92 HA TRP A 7 17.554 31.119 -3.577 1.00 13.83 H ANISOU 92 HA TRP A 7 1982 1586 1687 -129 -249 124 H ATOM 93 HB2 TRP A 7 18.668 28.529 -3.326 1.00 12.86 H ANISOU 93 HB2 TRP A 7 1625 1753 1507 -37 -205 -42 H ATOM 94 HB3 TRP A 7 18.883 29.436 -4.614 1.00 13.00 H ANISOU 94 HB3 TRP A 7 1730 1750 1457 -254 -335 -69 H ATOM 95 HD1 TRP A 7 20.535 28.861 -1.496 1.00 13.81 H ANISOU 95 HD1 TRP A 7 1900 1753 1592 84 -291 59 H ATOM 96 HE1 TRP A 7 22.192 30.498 -0.987 1.00 13.46 H ANISOU 96 HE1 TRP A 7 1517 2078 1519 81 -246 -11 H ATOM 97 HE3 TRP A 7 19.429 32.216 -4.884 1.00 13.79 H ANISOU 97 HE3 TRP A 7 1761 1963 1515 65 -233 226 H ATOM 98 HZ2 TRP A 7 22.996 32.949 -1.946 1.00 13.95 H ANISOU 98 HZ2 TRP A 7 1800 1645 1853 -216 -126 34 H ATOM 99 HZ3 TRP A 7 20.669 34.164 -4.999 1.00 15.24 H ANISOU 99 HZ3 TRP A 7 2004 1907 1879 -121 -180 65 H ATOM 100 HH2 TRP A 7 22.419 34.531 -3.529 1.00 15.89 H ANISOU 100 HH2 TRP A 7 2032 1904 2102 -144 -197 176 H ATOM 101 N ARG A 8 15.377 28.864 -3.781 1.00 13.54 N ANISOU 101 N ARG A 8 1762 1769 1614 -6 -430 191 N ATOM 102 CA ARG A 8 14.249 28.445 -4.613 1.00 14.10 C ANISOU 102 CA ARG A 8 1751 2062 1545 -25 -363 56 C ATOM 103 C ARG A 8 13.449 29.649 -5.103 1.00 14.04 C ANISOU 103 C ARG A 8 1777 2065 1491 -50 -449 -38 C ATOM 104 O ARG A 8 12.992 29.670 -6.224 1.00 14.26 O ANISOU 104 O ARG A 8 1742 2178 1497 87 -458 -109 O ATOM 105 CB ARG A 8 13.312 27.514 -3.850 1.00 13.74 C ANISOU 105 CB ARG A 8 1720 1998 1501 42 -357 -28 C ATOM 106 CG ARG A 8 13.982 26.260 -3.312 1.00 13.72 C ANISOU 106 CG ARG A 8 1802 1935 1475 148 -219 -97 C ATOM 107 CD ARG A 8 13.054 25.471 -2.397 1.00 16.28 C ANISOU 107 CD ARG A 8 2022 2057 2104 -18 75 -32 C ATOM 108 NE ARG A 8 12.675 26.205 -1.193 1.00 15.07 N ANISOU 108 NE ARG A 8 2082 1926 1715 -70 -266 87 N ATOM 109 CZ ARG A 8 11.959 25.718 -0.180 1.00 17.79 C ANISOU 109 CZ ARG A 8 2417 2075 2266 -106 192 172 C ATOM 110 NH1 ARG A 8 11.501 24.469 -0.205 1.00 19.12 N ANISOU 110 NH1 ARG A 8 2804 2127 2334 -295 -5 190 N ATOM 111 NH2 ARG A 8 11.679 26.488 0.869 1.00 19.78 N ANISOU 111 NH2 ARG A 8 2960 2201 2354 5 29 39 N ATOM 112 H ARG A 8 15.385 28.548 -2.983 1.00 13.04 H ANISOU 112 H ARG A 8 1634 1834 1485 72 -276 52 H ATOM 113 HA ARG A 8 14.589 27.962 -5.395 1.00 14.30 H ANISOU 113 HA ARG A 8 1843 1915 1673 -143 -262 0 H ATOM 114 HB2 ARG A 8 12.930 28.001 -3.106 1.00 13.90 H ANISOU 114 HB2 ARG A 8 1840 1733 1706 -3 -208 -44 H ATOM 115 HB3 ARG A 8 12.603 27.234 -4.448 1.00 14.03 H ANISOU 115 HB3 ARG A 8 1571 2189 1568 4 -279 -25 H ATOM 116 HG2 ARG A 8 14.228 25.688 -4.056 1.00 15.05 H ANISOU 116 HG2 ARG A 8 2207 1844 1666 -1 -104 -200 H ATOM 117 HG3 ARG A 8 14.769 26.496 -2.800 1.00 13.50 H ANISOU 117 HG3 ARG A 8 1739 1863 1528 154 -211 -17 H ATOM 118 HD2 ARG A 8 12.251 25.238 -2.884 1.00 15.18 H ANISOU 118 HD2 ARG A 8 2040 1986 1740 72 121 -115 H ATOM 119 HD3 ARG A 8 13.516 24.672 -2.112 1.00 15.80 H ANISOU 119 HD3 ARG A 8 2056 2027 1919 -115 -47 9 H ATOM 120 HE ARG A 8 13.193 27.001 -1.008 1.00 15.47 H ANISOU 120 HE ARG A 8 1950 1925 2001 -48 -162 75 H ATOM 121 HH11 ARG A 8 11.668 23.954 -0.872 1.00 18.05 H ANISOU 121 HH11 ARG A 8 2335 2173 2348 -253 -40 157 H ATOM 122 HH12 ARG A 8 11.038 24.169 0.454 1.00 17.52 H ANISOU 122 HH12 ARG A 8 2327 2006 2322 -144 -87 142 H ATOM 123 HH21 ARG A 8 11.964 27.298 0.900 1.00 18.08 H ANISOU 123 HH21 ARG A 8 2344 2292 2231 10 -155 -3 H ATOM 124 HH22 ARG A 8 11.213 26.177 1.522 1.00 18.40 H ANISOU 124 HH22 ARG A 8 2520 2149 2320 46 6 -141 H ATOM 125 N GLU A 9 13.301 30.648 -4.252 1.00 14.63 N ANISOU 125 N GLU A 9 1955 2178 1423 169 -533 -119 N ATOM 126 CA GLU A 9 12.528 31.852 -4.574 1.00 16.02 C ANISOU 126 CA GLU A 9 1933 2251 1900 163 -509 114 C ATOM 127 C GLU A 9 13.165 32.728 -5.649 1.00 15.88 C ANISOU 127 C GLU A 9 2062 1970 2000 113 -473 69 C ATOM 128 O GLU A 9 12.492 33.594 -6.227 1.00 19.98 O ANISOU 128 O GLU A 9 2389 2410 2792 409 -643 400 O ATOM 129 CB GLU A 9 12.247 32.632 -3.289 1.00 19.40 C ANISOU 129 CB GLU A 9 2301 2505 2563 673 -291 -387 C ATOM 130 CG GLU A 9 11.399 31.802 -2.295 1.00 23.81 C ANISOU 130 CG GLU A 9 2727 3762 2557 439 -353 174 C ATOM 131 CD GLU A 9 11.112 32.471 -0.963 0.50 25.26 C ANISOU 131 CD GLU A 9 2990 3443 3165 386 54 -256 C ATOM 132 OE1 GLU A 9 11.816 33.432 -0.596 0.50 29.09 O ANISOU 132 OE1 GLU A 9 3841 3412 3797 391 -645 -478 O ATOM 133 OE2 GLU A 9 10.178 32.006 -0.274 0.50 28.04 O ANISOU 133 OE2 GLU A 9 3874 3838 2938 451 269 307 O ATOM 134 H GLU A 9 13.651 30.661 -3.467 1.00 13.80 H ANISOU 134 H GLU A 9 1596 2204 1443 13 -450 -59 H ATOM 135 HA GLU A 9 11.658 31.566 -4.923 1.00 16.69 H ANISOU 135 HA GLU A 9 1765 2371 2204 168 -377 159 H ATOM 136 HB2 GLU A 9 13.088 32.855 -2.862 1.00 19.61 H ANISOU 136 HB2 GLU A 9 2617 2831 2001 486 -401 -325 H ATOM 137 HB3 GLU A 9 11.756 33.440 -3.507 1.00 21.31 H ANISOU 137 HB3 GLU A 9 2335 2323 3438 481 -374 -285 H ATOM 138 HG2 GLU A 9 10.549 31.592 -2.711 1.00 24.40 H ANISOU 138 HG2 GLU A 9 2724 3455 3092 107 -232 63 H ATOM 139 HG3 GLU A 9 11.868 30.977 -2.098 1.00 22.05 H ANISOU 139 HG3 GLU A 9 2670 3035 2670 -20 -209 -156 H ATOM 140 N LYS A 10 14.449 32.502 -5.912 1.00 15.87 N ANISOU 140 N LYS A 10 2013 2186 1831 132 -522 -40 N ATOM 141 CA LYS A 10 15.211 33.218 -6.920 1.00 16.77 C ANISOU 141 CA LYS A 10 2041 1955 2373 221 -299 104 C ATOM 142 C LYS A 10 15.405 32.426 -8.202 1.00 15.77 C ANISOU 142 C LYS A 10 2013 1976 2000 113 -468 276 C ATOM 143 O LYS A 10 16.108 32.881 -9.084 1.00 17.26 O ANISOU 143 O LYS A 10 2274 1998 2285 56 -234 300 O ATOM 144 CB LYS A 10 16.586 33.637 -6.367 1.00 17.94 C ANISOU 144 CB LYS A 10 2276 2394 2145 -139 -427 248 C ATOM 145 CG LYS A 10 16.535 34.424 -5.061 1.00 23.88 C ANISOU 145 CG LYS A 10 3123 3368 2580 -446 29 -407 C ATOM 146 CD LYS A 10 15.623 35.646 -5.100 1.00 30.32 C ANISOU 146 CD LYS A 10 3899 3706 3916 38 -58 -349 C ATOM 147 CE LYS A 10 15.569 36.358 -3.729 1.00 33.23 C ANISOU 147 CE LYS A 10 4531 4212 3882 208 152 -376 C ATOM 148 NZ LYS A 10 14.193 36.823 -3.361 0.50 35.96 N ANISOU 148 NZ LYS A 10 4414 4931 4314 281 153 -723 N ATOM 149 H LYS A 10 14.928 31.924 -5.496 1.00 15.56 H ANISOU 149 H LYS A 10 2013 1949 1947 126 -402 -81 H ATOM 150 HA LYS A 10 14.734 34.037 -7.167 1.00 17.86 H ANISOU 150 HA LYS A 10 2162 1942 2682 222 -256 165 H ATOM 151 HB2 LYS A 10 17.113 32.838 -6.209 1.00 18.31 H ANISOU 151 HB2 LYS A 10 1981 2522 2454 -109 -357 292 H ATOM 152 HB3 LYS A 10 17.030 34.196 -7.024 1.00 18.60 H ANISOU 152 HB3 LYS A 10 2298 2294 2473 -98 -73 141 H ATOM 153 HG2 LYS A 10 16.216 33.838 -4.357 1.00 23.50 H ANISOU 153 HG2 LYS A 10 2838 3595 2493 -254 186 -387 H ATOM 154 HG3 LYS A 10 17.430 34.732 -4.849 1.00 22.93 H ANISOU 154 HG3 LYS A 10 3280 3154 2277 -523 -80 -362 H ATOM 155 HD2 LYS A 10 15.958 36.276 -5.757 1.00 28.48 H ANISOU 155 HD2 LYS A 10 3331 3648 3840 147 -102 -337 H ATOM 156 HD3 LYS A 10 14.720 35.374 -5.326 1.00 28.79 H ANISOU 156 HD3 LYS A 10 3665 3573 3698 173 153 72 H ATOM 157 HE2 LYS A 10 15.877 35.750 -3.040 1.00 32.37 H ANISOU 157 HE2 LYS A 10 4218 4220 3861 -180 107 -226 H ATOM 158 HE3 LYS A 10 16.146 37.137 -3.760 1.00 30.76 H ANISOU 158 HE3 LYS A 10 4361 4091 3233 285 -106 -289 H ATOM 159 N GLY A 11 14.817 31.229 -8.298 1.00 14.57 N ANISOU 159 N GLY A 11 1902 1887 1744 180 -270 267 N ATOM 160 CA GLY A 11 14.894 30.449 -9.523 1.00 15.22 C ANISOU 160 CA GLY A 11 1906 1879 1998 59 -267 132 C ATOM 161 C GLY A 11 16.113 29.557 -9.676 1.00 11.64 C ANISOU 161 C GLY A 11 1819 1554 1050 -102 -55 359 C ATOM 162 O GLY A 11 16.395 29.128 -10.803 1.00 13.43 O ANISOU 162 O GLY A 11 1935 1990 1178 80 -180 230 O ATOM 163 H GLY A 11 14.370 30.846 -7.672 1.00 15.70 H ANISOU 163 H GLY A 11 1894 2153 1919 82 -177 280 H ATOM 164 HA2 GLY A 11 14.870 31.050 -10.282 1.00 13.53 H ANISOU 164 HA2 GLY A 11 1611 1723 1803 123 -157 -33 H ATOM 165 HA3 GLY A 11 14.110 29.881 -9.574 1.00 14.80 H ANISOU 165 HA3 GLY A 11 1838 1894 1891 87 -114 156 H ATOM 166 N TYR A 12 16.805 29.265 -8.567 1.00 12.98 N ANISOU 166 N TYR A 12 1848 1674 1407 -150 -313 406 N ATOM 167 CA TYR A 12 18.066 28.506 -8.624 1.00 12.62 C ANISOU 167 CA TYR A 12 1826 1688 1278 -109 -295 560 C ATOM 168 C TYR A 12 17.906 26.990 -8.617 1.00 12.95 C ANISOU 168 C TYR A 12 1663 1709 1546 -59 -364 322 C ATOM 169 O TYR A 12 18.883 26.282 -8.829 1.00 13.64 O ANISOU 169 O TYR A 12 1711 1701 1769 -53 -171 302 O ATOM 170 CB TYR A 12 18.959 28.858 -7.447 1.00 13.32 C ANISOU 170 CB TYR A 12 2042 1628 1389 -2 -408 335 C ATOM 171 CG TYR A 12 19.804 30.109 -7.576 1.00 14.45 C ANISOU 171 CG TYR A 12 1946 1715 1829 -80 -500 288 C ATOM 172 CD1 TYR A 12 19.221 31.375 -7.724 1.00 15.39 C ANISOU 172 CD1 TYR A 12 1918 1734 2193 -99 -440 390 C ATOM 173 CD2 TYR A 12 21.180 30.031 -7.487 1.00 13.84 C ANISOU 173 CD2 TYR A 12 1936 1930 1390 -70 -43 496 C ATOM 174 CE1 TYR A 12 20.011 32.515 -7.812 1.00 17.08 C ANISOU 174 CE1 TYR A 12 2247 1789 2451 -225 -498 604 C ATOM 175 CE2 TYR A 12 21.970 31.170 -7.562 1.00 16.36 C ANISOU 175 CE2 TYR A 12 1969 2129 2115 -248 -73 338 C ATOM 176 CZ TYR A 12 21.389 32.394 -7.745 1.00 15.43 C ANISOU 176 CZ TYR A 12 2198 1949 1715 -386 -249 341 C ATOM 177 OH TYR A 12 22.196 33.505 -7.803 1.00 21.15 O ANISOU 177 OH TYR A 12 2939 2213 2883 -835 -137 342 O ATOM 178 H TYR A 12 16.563 29.487 -7.773 1.00 12.65 H ANISOU 178 H TYR A 12 1725 1741 1340 -91 -558 246 H ATOM 179 HA TYR A 12 18.550 28.750 -9.441 1.00 13.37 H ANISOU 179 HA TYR A 12 1954 1840 1285 -179 -149 306 H ATOM 180 HB2 TYR A 12 18.397 28.973 -6.668 1.00 13.10 H ANISOU 180 HB2 TYR A 12 1824 1555 1598 12 -381 -8 H ATOM 181 HB3 TYR A 12 19.569 28.122 -7.284 1.00 12.29 H ANISOU 181 HB3 TYR A 12 1614 1706 1349 -60 -269 206 H ATOM 182 HD1 TYR A 12 18.296 31.452 -7.780 1.00 15.37 H ANISOU 182 HD1 TYR A 12 1901 1870 2067 19 -224 260 H ATOM 183 HD2 TYR A 12 21.587 29.203 -7.371 1.00 14.36 H ANISOU 183 HD2 TYR A 12 1882 1949 1623 26 -130 144 H ATOM 184 HE1 TYR A 12 19.618 33.351 -7.924 1.00 16.75 H ANISOU 184 HE1 TYR A 12 2482 1722 2159 -126 -188 324 H ATOM 185 HE2 TYR A 12 22.894 31.096 -7.513 1.00 16.44 H ANISOU 185 HE2 TYR A 12 1952 2370 1923 -236 10 170 H ATOM 186 N VAL A 13 16.690 26.499 -8.363 1.00 12.88 N ANISOU 186 N VAL A 13 1655 1597 1639 28 -269 449 N ATOM 187 CA VAL A 13 16.504 25.117 -7.966 1.00 11.97 C ANISOU 187 CA VAL A 13 1762 1540 1244 48 -389 269 C ATOM 188 C VAL A 13 15.470 24.402 -8.823 1.00 12.44 C ANISOU 188 C VAL A 13 1642 1699 1385 10 -311 167 C ATOM 189 O VAL A 13 14.357 24.876 -8.970 1.00 13.32 O ANISOU 189 O VAL A 13 1688 1694 1675 109 -277 121 O ATOM 190 CB VAL A 13 16.107 25.041 -6.494 1.00 12.14 C ANISOU 190 CB VAL A 13 1651 1669 1293 50 -344 244 C ATOM 191 CG1 VAL A 13 16.097 23.578 -5.991 1.00 13.57 C ANISOU 191 CG1 VAL A 13 1883 1645 1629 31 -238 313 C ATOM 192 CG2 VAL A 13 17.077 25.871 -5.579 1.00 13.97 C ANISOU 192 CG2 VAL A 13 1886 1816 1603 -10 -406 11 C ATOM 193 H VAL A 13 15.958 26.946 -8.415 1.00 11.92 H ANISOU 193 H VAL A 13 1662 1442 1424 6 -215 191 H ATOM 194 HA VAL A 13 17.352 24.636 -8.067 1.00 11.88 H ANISOU 194 HA VAL A 13 1604 1457 1450 -118 -234 240 H ATOM 195 HB VAL A 13 15.203 25.405 -6.388 1.00 12.84 H ANISOU 195 HB VAL A 13 1635 1565 1677 -32 -164 180 H ATOM 196 N THR A 14 15.852 23.269 -9.397 1.00 12.41 N ANISOU 196 N THR A 14 1468 1801 1442 14 -203 87 N ATOM 197 CA THR A 14 14.923 22.446 -10.159 1.00 11.81 C ANISOU 197 CA THR A 14 1683 1833 971 0 -284 234 C ATOM 198 C THR A 14 13.936 21.749 -9.209 1.00 12.14 C ANISOU 198 C THR A 14 1497 1750 1363 168 -40 298 C ATOM 199 O THR A 14 14.174 21.633 -8.019 1.00 12.87 O ANISOU 199 O THR A 14 1839 1693 1357 -7 -127 322 O ATOM 200 CB THR A 14 15.642 21.391 -10.976 1.00 12.35 C ANISOU 200 CB THR A 14 1728 1759 1202 -33 -175 233 C ATOM 201 OG1 THR A 14 16.395 20.535 -10.124 1.00 12.96 O ANISOU 201 OG1 THR A 14 1828 1547 1548 -35 -231 302 O ATOM 202 CG2 THR A 14 16.550 22.028 -12.031 1.00 13.60 C ANISOU 202 CG2 THR A 14 1929 2141 1094 29 -28 292 C ATOM 203 H THR A 14 16.649 22.948 -9.346 1.00 12.21 H ANISOU 203 H THR A 14 1462 1779 1396 -11 -156 234 H ATOM 204 HA THR A 14 14.422 23.022 -10.772 1.00 12.07 H ANISOU 204 HA THR A 14 1634 1725 1224 39 -240 270 H ATOM 205 HB THR A 14 14.982 20.856 -11.444 1.00 13.10 H ANISOU 205 HB THR A 14 1682 1792 1501 57 -191 37 H ATOM 206 N PRO A 15 12.805 21.263 -9.720 1.00 13.12 N ANISOU 206 N PRO A 15 1830 1659 1493 -59 -206 348 N ATOM 207 CA PRO A 15 11.902 20.501 -8.863 1.00 12.90 C ANISOU 207 CA PRO A 15 1673 1738 1490 0 -173 318 C ATOM 208 C PRO A 15 12.563 19.246 -8.255 1.00 12.50 C ANISOU 208 C PRO A 15 1717 1435 1597 -48 -38 135 C ATOM 209 O PRO A 15 13.585 18.750 -8.744 1.00 13.34 O ANISOU 209 O PRO A 15 1771 1790 1506 -12 48 276 O ATOM 210 CB PRO A 15 10.753 20.141 -9.818 1.00 13.51 C ANISOU 210 CB PRO A 15 1759 1834 1540 -17 -228 250 C ATOM 211 CG PRO A 15 10.772 21.236 -10.859 1.00 14.50 C ANISOU 211 CG PRO A 15 1855 2070 1583 -112 -269 363 C ATOM 212 CD PRO A 15 12.222 21.548 -11.033 1.00 13.50 C ANISOU 212 CD PRO A 15 1855 1822 1451 -135 -230 284 C ATOM 213 HA PRO A 15 11.557 21.068 -8.143 1.00 12.63 H ANISOU 213 HA PRO A 15 1567 1530 1702 -24 -179 223 H ATOM 214 HB2 PRO A 15 10.918 19.277 -10.226 1.00 14.08 H ANISOU 214 HB2 PRO A 15 1714 1866 1767 -128 -97 120 H ATOM 215 HB3 PRO A 15 9.912 20.140 -9.335 1.00 13.26 H ANISOU 215 HB3 PRO A 15 1728 1622 1687 -113 -193 172 H ATOM 216 HG2 PRO A 15 10.386 20.910 -11.687 1.00 13.47 H ANISOU 216 HG2 PRO A 15 1689 1851 1575 15 -182 293 H ATOM 217 HG3 PRO A 15 10.288 22.010 -10.532 1.00 13.25 H ANISOU 217 HG3 PRO A 15 1745 1792 1497 -328 -287 341 H ATOM 218 HD2 PRO A 15 12.614 20.976 -11.711 1.00 13.35 H ANISOU 218 HD2 PRO A 15 1848 1625 1598 -237 -290 132 H ATOM 219 HD3 PRO A 15 12.331 22.486 -11.248 1.00 12.47 H ANISOU 219 HD3 PRO A 15 1746 1722 1269 59 -240 171 H ATOM 220 N VAL A 16 11.952 18.746 -7.197 1.00 12.59 N ANISOU 220 N VAL A 16 1523 1656 1604 24 -60 215 N ATOM 221 CA VAL A 16 12.430 17.552 -6.528 1.00 12.16 C ANISOU 221 CA VAL A 16 1522 1665 1432 65 -92 128 C ATOM 222 C VAL A 16 12.380 16.362 -7.488 1.00 12.09 C ANISOU 222 C VAL A 16 1665 1764 1161 -21 -149 146 C ATOM 223 O VAL A 16 11.398 16.130 -8.219 1.00 13.03 O ANISOU 223 O VAL A 16 1740 1868 1340 91 -298 49 O ATOM 224 CB VAL A 16 11.604 17.300 -5.263 1.00 12.54 C ANISOU 224 CB VAL A 16 1635 1612 1518 155 32 57 C ATOM 225 CG1 VAL A 16 11.901 15.904 -4.671 1.00 14.50 C ANISOU 225 CG1 VAL A 16 2278 1819 1412 182 -182 286 C ATOM 226 CG2 VAL A 16 11.865 18.394 -4.221 1.00 14.53 C ANISOU 226 CG2 VAL A 16 2154 1845 1521 52 131 -86 C ATOM 227 H VAL A 16 11.239 19.088 -6.857 1.00 12.55 H ANISOU 227 H VAL A 16 1578 1538 1651 21 -57 108 H ATOM 228 HA VAL A 16 13.362 17.694 -6.263 1.00 12.05 H ANISOU 228 HA VAL A 16 1536 1589 1452 44 -91 52 H ATOM 229 HB VAL A 16 10.652 17.327 -5.494 1.00 13.14 H ANISOU 229 HB VAL A 16 1595 1680 1715 120 79 126 H ATOM 230 N LYS A 17 13.475 15.615 -7.485 1.00 12.11 N ANISOU 230 N LYS A 17 1566 1599 1433 -79 -151 94 N ATOM 231 CA LYS A 17 13.663 14.444 -8.328 1.00 11.96 C ANISOU 231 CA LYS A 17 1616 1700 1227 -16 -213 144 C ATOM 232 C LYS A 17 13.622 13.206 -7.424 1.00 11.13 C ANISOU 232 C LYS A 17 1400 1700 1127 28 -134 148 C ATOM 233 O LYS A 17 13.552 13.314 -6.195 1.00 12.11 O ANISOU 233 O LYS A 17 1764 1645 1191 -65 77 162 O ATOM 234 CB LYS A 17 15.006 14.535 -9.057 1.00 12.84 C ANISOU 234 CB LYS A 17 1692 1781 1404 -46 -94 265 C ATOM 235 CG LYS A 17 15.140 15.768 -9.970 1.00 11.80 C ANISOU 235 CG LYS A 17 1825 1698 959 -6 -25 18 C ATOM 236 CD LYS A 17 16.473 15.821 -10.702 1.00 13.06 C ANISOU 236 CD LYS A 17 1754 1811 1396 -138 -8 256 C ATOM 237 CE LYS A 17 16.720 17.116 -11.453 1.00 12.70 C ANISOU 237 CE LYS A 17 1632 1797 1396 152 -36 324 C ATOM 238 NZ LYS A 17 18.022 17.169 -12.203 1.00 12.93 N ANISOU 238 NZ LYS A 17 1621 1707 1582 -33 12 258 N ATOM 239 H LYS A 17 14.154 15.769 -6.980 1.00 12.01 H ANISOU 239 H LYS A 17 1499 1664 1397 -128 -70 65 H ATOM 240 HA LYS A 17 12.948 14.375 -8.994 1.00 11.90 H ANISOU 240 HA LYS A 17 1619 1658 1241 102 -227 138 H ATOM 241 HB2 LYS A 17 15.718 14.573 -8.400 1.00 12.03 H ANISOU 241 HB2 LYS A 17 1580 1568 1422 123 -45 192 H ATOM 242 HB3 LYS A 17 15.111 13.748 -9.612 1.00 12.61 H ANISOU 242 HB3 LYS A 17 1498 1741 1549 -99 -70 204 H ATOM 243 HG2 LYS A 17 14.434 15.747 -10.634 1.00 11.84 H ANISOU 243 HG2 LYS A 17 1699 1499 1301 19 -124 51 H ATOM 244 HG3 LYS A 17 15.064 16.571 -9.431 1.00 12.94 H ANISOU 244 HG3 LYS A 17 1866 1588 1460 -62 -143 -76 H ATOM 245 HD2 LYS A 17 17.188 15.715 -10.055 1.00 12.32 H ANISOU 245 HD2 LYS A 17 1779 1444 1457 117 -6 200 H ATOM 246 HD3 LYS A 17 16.504 15.096 -11.346 1.00 12.19 H ANISOU 246 HD3 LYS A 17 1291 1798 1540 33 52 180 H ATOM 247 HE2 LYS A 17 16.005 17.241 -12.097 1.00 12.71 H ANISOU 247 HE2 LYS A 17 1603 1734 1492 152 -83 138 H ATOM 248 HE3 LYS A 17 16.717 17.848 -10.817 1.00 12.62 H ANISOU 248 HE3 LYS A 17 1402 1776 1616 -27 -98 214 H ATOM 249 N ASN A 18 13.671 12.029 -8.053 1.00 12.62 N ANISOU 249 N ASN A 18 1899 1689 1206 78 64 134 N ATOM 250 CA ASN A 18 13.567 10.754 -7.353 1.00 12.17 C ANISOU 250 CA ASN A 18 1780 1681 1160 5 -151 117 C ATOM 251 C ASN A 18 14.604 9.770 -7.868 1.00 12.06 C ANISOU 251 C ASN A 18 1801 1559 1220 -20 -19 222 C ATOM 252 O ASN A 18 14.537 9.309 -9.014 1.00 13.31 O ANISOU 252 O ASN A 18 1961 1780 1316 9 -144 67 O ATOM 253 CB ASN A 18 12.157 10.170 -7.506 1.00 14.19 C ANISOU 253 CB ASN A 18 1766 1784 1840 33 -226 -53 C ATOM 254 CG ASN A 18 11.887 9.038 -6.530 1.00 14.98 C ANISOU 254 CG ASN A 18 2085 1714 1892 -198 32 -203 C ATOM 255 OD1 ASN A 18 12.809 8.415 -5.973 1.00 16.61 O ANISOU 255 OD1 ASN A 18 2151 1915 2242 -70 334 316 O ATOM 256 ND2 ASN A 18 10.606 8.785 -6.294 1.00 18.25 N ANISOU 256 ND2 ASN A 18 2160 2315 2456 -452 207 -128 N ATOM 257 H ASN A 18 13.761 11.945 -8.905 1.00 11.87 H ANISOU 257 H ASN A 18 1635 1635 1239 -9 86 109 H ATOM 258 HA ASN A 18 13.725 10.892 -6.396 1.00 12.42 H ANISOU 258 HA ASN A 18 1895 1642 1180 -11 -130 90 H ATOM 259 HB2 ASN A 18 11.508 10.872 -7.337 1.00 14.77 H ANISOU 259 HB2 ASN A 18 1746 1857 2007 -5 -27 -105 H ATOM 260 HB3 ASN A 18 12.044 9.829 -8.407 1.00 14.30 H ANISOU 260 HB3 ASN A 18 1699 1869 1862 -89 -135 -115 H ATOM 261 N GLN A 19 15.567 9.444 -7.010 1.00 12.30 N ANISOU 261 N GLN A 19 1788 1583 1302 -35 -59 136 N ATOM 262 CA GLN A 19 16.627 8.511 -7.375 1.00 12.89 C ANISOU 262 CA GLN A 19 1769 1573 1554 -33 -127 140 C ATOM 263 C GLN A 19 16.134 7.069 -7.514 1.00 12.61 C ANISOU 263 C GLN A 19 1880 1594 1317 -75 25 237 C ATOM 264 O GLN A 19 16.830 6.234 -8.126 1.00 12.54 O ANISOU 264 O GLN A 19 2002 1778 983 -61 -139 -13 O ATOM 265 CB GLN A 19 17.748 8.573 -6.354 1.00 12.09 C ANISOU 265 CB GLN A 19 1804 1631 1157 13 55 -1 C ATOM 266 CG GLN A 19 17.387 8.043 -4.993 1.00 12.11 C ANISOU 266 CG GLN A 19 1687 1620 1291 -156 17 85 C ATOM 267 CD GLN A 19 18.486 8.260 -3.969 1.00 12.75 C ANISOU 267 CD GLN A 19 1895 1696 1252 -81 -123 270 C ATOM 268 OE1 GLN A 19 18.634 9.345 -3.432 1.00 13.58 O ANISOU 268 OE1 GLN A 19 1874 1764 1522 46 -332 78 O ATOM 269 NE2 GLN A 19 19.303 7.255 -3.775 1.00 15.06 N ANISOU 269 NE2 GLN A 19 1969 1786 1967 42 -191 301 N ATOM 270 H GLN A 19 15.628 9.758 -6.213 1.00 12.64 H ANISOU 270 H GLN A 19 1749 1655 1399 -140 -147 35 H ATOM 271 HA GLN A 19 17.002 8.781 -8.239 1.00 11.48 H ANISOU 271 HA GLN A 19 1532 1366 1463 -2 -223 77 H ATOM 272 HB2 GLN A 19 18.493 8.048 -6.683 1.00 11.99 H ANISOU 272 HB2 GLN A 19 1616 1558 1379 -68 55 88 H ATOM 273 HB3 GLN A 19 18.020 9.498 -6.249 1.00 11.86 H ANISOU 273 HB3 GLN A 19 1648 1574 1283 41 -14 164 H ATOM 274 HG2 GLN A 19 16.589 8.486 -4.670 1.00 11.88 H ANISOU 274 HG2 GLN A 19 1711 1541 1260 -151 64 148 H ATOM 275 HG3 GLN A 19 17.230 7.089 -5.053 1.00 12.92 H ANISOU 275 HG3 GLN A 19 1817 1561 1530 -39 -57 148 H ATOM 276 N GLY A 20 14.969 6.750 -6.948 1.00 13.52 N ANISOU 276 N GLY A 20 1692 1683 1760 -22 -1 271 N ATOM 277 CA GLY A 20 14.475 5.375 -7.089 1.00 15.00 C ANISOU 277 CA GLY A 20 1884 1798 2015 -224 -98 146 C ATOM 278 C GLY A 20 15.420 4.400 -6.410 1.00 15.50 C ANISOU 278 C GLY A 20 1954 1872 2062 -183 -150 121 C ATOM 279 O GLY A 20 16.060 4.732 -5.416 1.00 15.21 O ANISOU 279 O GLY A 20 2196 1707 1874 -175 -141 311 O ATOM 280 H GLY A 20 14.463 7.273 -6.491 1.00 13.73 H ANISOU 280 H GLY A 20 1720 1817 1677 -74 0 155 H ATOM 281 HA2 GLY A 20 14.414 5.149 -8.028 1.00 15.57 H ANISOU 281 HA2 GLY A 20 2102 1824 1989 -65 -59 112 H ATOM 282 HA3 GLY A 20 13.595 5.296 -6.687 1.00 15.20 H ANISOU 282 HA3 GLY A 20 1903 1793 2079 -213 -40 86 H ATOM 283 N GLN A 21 15.484 3.198 -6.970 1.00 16.92 N ANISOU 283 N GLN A 21 2123 1741 2562 -96 45 156 N ATOM 284 CA GLN A 21 16.229 2.092 -6.371 1.00 18.74 C ANISOU 284 CA GLN A 21 2232 1866 3021 -117 -152 402 C ATOM 285 C GLN A 21 17.611 2.019 -7.008 1.00 20.02 C ANISOU 285 C GLN A 21 2348 1784 3475 -6 50 232 C ATOM 286 O GLN A 21 17.992 1.054 -7.687 1.00 23.63 O ANISOU 286 O GLN A 21 2980 2152 3847 -130 248 -233 O ATOM 287 CB GLN A 21 15.483 0.784 -6.559 1.00 20.73 C ANISOU 287 CB GLN A 21 2520 1954 3400 -172 22 -61 C ATOM 288 CG GLN A 21 14.137 0.714 -5.834 1.00 24.26 C ANISOU 288 CG GLN A 21 2757 2573 3887 -247 422 160 C ATOM 289 CD GLN A 21 14.242 0.973 -4.324 0.50 25.86 C ANISOU 289 CD GLN A 21 3137 2887 3799 229 372 58 C ATOM 290 OE1 GLN A 21 13.605 1.890 -3.797 0.50 33.39 O ANISOU 290 OE1 GLN A 21 4399 3513 4775 708 810 -259 O ATOM 291 NE2 GLN A 21 15.066 0.185 -3.634 0.50 28.21 N ANISOU 291 NE2 GLN A 21 4157 2453 4106 -93 138 667 N ATOM 292 H GLN A 21 15.099 2.991 -7.711 1.00 16.34 H ANISOU 292 H GLN A 21 2281 1561 2367 73 161 41 H ATOM 293 HA GLN A 21 16.350 2.245 -5.412 1.00 18.79 H ANISOU 293 HA GLN A 21 2390 1778 2970 -51 -174 303 H ATOM 294 HB2 GLN A 21 15.316 0.653 -7.505 1.00 21.04 H ANISOU 294 HB2 GLN A 21 2730 1989 3275 -146 14 49 H ATOM 295 HB3 GLN A 21 16.034 0.060 -6.222 1.00 20.65 H ANISOU 295 HB3 GLN A 21 2771 1874 3200 -204 86 74 H ATOM 296 HG2 GLN A 21 13.543 1.382 -6.210 1.00 24.03 H ANISOU 296 HG2 GLN A 21 2706 2733 3691 -20 390 -130 H ATOM 297 HG3 GLN A 21 13.759 -0.171 -5.959 1.00 24.01 H ANISOU 297 HG3 GLN A 21 2505 2724 3893 -274 164 155 H ATOM 298 N CYS A 22 18.331 3.103 -6.838 1.00 16.66 N ANISOU 298 N CYS A 22 1991 1711 2627 172 102 72 N ATOM 299 CA CYS A 22 19.701 3.231 -7.282 1.00 14.65 C ANISOU 299 CA CYS A 22 1990 1915 1660 146 -49 -87 C ATOM 300 C CYS A 22 20.347 4.144 -6.249 1.00 13.60 C ANISOU 300 C CYS A 22 1973 1828 1366 195 89 -15 C ATOM 301 O CYS A 22 19.766 5.168 -5.872 1.00 14.21 O ANISOU 301 O CYS A 22 1825 1741 1832 34 111 -140 O ATOM 302 CB CYS A 22 19.754 3.816 -8.705 1.00 14.81 C ANISOU 302 CB CYS A 22 1976 1920 1728 106 -216 72 C ATOM 303 SG CYS A 22 21.369 4.438 -9.269 1.00 15.20 S ANISOU 303 SG CYS A 22 2101 1794 1877 22 -213 331 S ATOM 304 H CYS A 22 18.037 3.811 -6.449 1.00 15.91 H ANISOU 304 H CYS A 22 1992 1982 2068 179 62 -15 H ATOM 305 HA CYS A 22 20.150 2.362 -7.277 1.00 13.98 H ANISOU 305 HA CYS A 22 1869 1748 1695 -26 22 40 H ATOM 306 HB2 CYS A 22 19.484 3.120 -9.322 1.00 14.63 H ANISOU 306 HB2 CYS A 22 2029 1853 1677 72 -59 71 H ATOM 307 HB3 CYS A 22 19.124 4.550 -8.754 1.00 15.33 H ANISOU 307 HB3 CYS A 22 2058 1816 1950 78 -192 15 H ATOM 308 N GLY A 23 21.538 3.773 -5.794 1.00 13.16 N ANISOU 308 N GLY A 23 1938 1595 1464 74 142 42 N ATOM 309 CA GLY A 23 22.276 4.542 -4.797 1.00 13.63 C ANISOU 309 CA GLY A 23 2139 1508 1532 3 -9 132 C ATOM 310 C GLY A 23 23.038 5.723 -5.374 1.00 12.79 C ANISOU 310 C GLY A 23 1892 1744 1223 39 -92 301 C ATOM 311 O GLY A 23 24.261 5.832 -5.257 1.00 14.36 O ANISOU 311 O GLY A 23 1942 1751 1763 -36 -306 416 O ATOM 312 H GLY A 23 21.953 3.064 -6.052 1.00 13.35 H ANISOU 312 H GLY A 23 1834 1584 1653 32 117 0 H ATOM 313 HA2 GLY A 23 22.908 3.964 -4.344 1.00 13.09 H ANISOU 313 HA2 GLY A 23 1851 1511 1608 -90 95 182 H ATOM 314 HA3 GLY A 23 21.658 4.885 -4.134 1.00 12.65 H ANISOU 314 HA3 GLY A 23 1740 1510 1555 -164 -96 75 H ATOM 315 N SER A 24 22.273 6.648 -5.970 1.00 13.53 N ANISOU 315 N SER A 24 1825 1553 1763 4 -8 413 N ATOM 316 CA SER A 24 22.789 7.770 -6.757 1.00 13.02 C ANISOU 316 CA SER A 24 1658 1635 1651 12 0 428 C ATOM 317 C SER A 24 22.569 9.100 -6.070 1.00 12.24 C ANISOU 317 C SER A 24 1554 1615 1481 -146 23 408 C ATOM 318 O SER A 24 22.667 10.138 -6.706 1.00 12.35 O ANISOU 318 O SER A 24 1703 1632 1358 -60 -49 372 O ATOM 319 CB SER A 24 22.152 7.777 -8.129 1.00 13.51 C ANISOU 319 CB SER A 24 1832 1638 1663 -10 -53 236 C ATOM 320 OG SER A 24 20.752 7.784 -7.966 1.00 13.23 O ANISOU 320 OG SER A 24 1777 1756 1491 57 -135 61 O ATOM 321 H SER A 24 21.415 6.651 -5.922 1.00 12.30 H ANISOU 321 H SER A 24 1795 1408 1469 -53 -15 228 H ATOM 322 HA SER A 24 23.754 7.662 -6.885 1.00 13.65 H ANISOU 322 HA SER A 24 1642 1756 1786 -54 -3 232 H ATOM 323 HB2 SER A 24 22.427 8.567 -8.620 1.00 12.88 H ANISOU 323 HB2 SER A 24 1858 1575 1460 15 -126 150 H ATOM 324 HB3 SER A 24 22.421 6.979 -8.608 1.00 13.54 H ANISOU 324 HB3 SER A 24 1703 1593 1846 -68 0 200 H ATOM 325 N CYS A 25 22.331 9.093 -4.766 1.00 12.68 N ANISOU 325 N CYS A 25 1789 1553 1474 6 -23 357 N ATOM 326 CA CYS A 25 22.084 10.335 -4.032 1.00 12.56 C ANISOU 326 CA CYS A 25 1672 1787 1310 -29 -51 182 C ATOM 327 C CYS A 25 23.146 11.413 -4.322 1.00 12.01 C ANISOU 327 C CYS A 25 1657 1720 1184 -15 -241 172 C ATOM 328 O CYS A 25 22.820 12.587 -4.493 1.00 13.14 O ANISOU 328 O CYS A 25 1766 1717 1507 -15 -204 305 O ATOM 329 CB CYS A 25 21.964 10.091 -2.527 1.00 12.31 C ANISOU 329 CB CYS A 25 1669 1669 1336 -42 -54 110 C ATOM 330 SG CYS A 25 23.439 9.306 -1.779 1.00 13.47 S ANISOU 330 SG CYS A 25 1915 1791 1411 -25 -195 353 S ATOM 331 H CYS A 25 22.309 8.388 -4.275 1.00 12.25 H ANISOU 331 H CYS A 25 1721 1591 1339 -248 -156 305 H ATOM 332 HA CYS A 25 21.224 10.695 -4.332 1.00 12.28 H ANISOU 332 HA CYS A 25 1638 1715 1310 -22 -5 128 H ATOM 333 HB2 CYS A 25 21.825 10.943 -2.083 1.00 12.55 H ANISOU 333 HB2 CYS A 25 1737 1643 1385 -98 -33 90 H ATOM 334 HB3 CYS A 25 21.205 9.509 -2.365 1.00 12.22 H ANISOU 334 HB3 CYS A 25 1724 1549 1366 -4 72 75 H ATOM 335 N TRP A 26 24.412 10.993 -4.331 1.00 12.79 N ANISOU 335 N TRP A 26 1666 1665 1526 -32 -131 294 N ATOM 336 CA TRP A 26 25.553 11.872 -4.589 1.00 12.31 C ANISOU 336 CA TRP A 26 1665 1757 1253 -47 -230 236 C ATOM 337 C TRP A 26 25.402 12.568 -5.970 1.00 11.44 C ANISOU 337 C TRP A 26 1646 1553 1147 119 -137 82 C ATOM 338 O TRP A 26 25.854 13.719 -6.140 1.00 12.81 O ANISOU 338 O TRP A 26 1753 1602 1512 15 -275 326 O ATOM 339 CB TRP A 26 26.848 11.038 -4.560 1.00 12.51 C ANISOU 339 CB TRP A 26 1616 1850 1287 -23 -152 586 C ATOM 340 CG TRP A 26 26.845 9.880 -5.508 1.00 12.98 C ANISOU 340 CG TRP A 26 1811 1664 1453 -26 -316 610 C ATOM 341 CD1 TRP A 26 26.335 8.604 -5.285 1.00 13.76 C ANISOU 341 CD1 TRP A 26 1843 1556 1827 19 -61 452 C ATOM 342 CD2 TRP A 26 27.297 9.881 -6.854 1.00 13.24 C ANISOU 342 CD2 TRP A 26 1995 1794 1238 61 -447 663 C ATOM 343 NE1 TRP A 26 26.448 7.846 -6.419 1.00 14.01 N ANISOU 343 NE1 TRP A 26 1929 1611 1783 91 -166 427 N ATOM 344 CE2 TRP A 26 27.046 8.597 -7.395 1.00 13.47 C ANISOU 344 CE2 TRP A 26 1492 1611 2013 179 -71 480 C ATOM 345 CE3 TRP A 26 27.868 10.859 -7.707 1.00 12.28 C ANISOU 345 CE3 TRP A 26 1631 1752 1281 134 -112 429 C ATOM 346 CZ2 TRP A 26 27.369 8.270 -8.708 1.00 14.95 C ANISOU 346 CZ2 TRP A 26 1596 1863 2220 55 31 289 C ATOM 347 CZ3 TRP A 26 28.198 10.519 -8.993 1.00 13.01 C ANISOU 347 CZ3 TRP A 26 1688 1952 1302 57 0 410 C ATOM 348 CH2 TRP A 26 27.945 9.237 -9.477 1.00 14.96 C ANISOU 348 CH2 TRP A 26 2016 1852 1814 139 6 292 C ATOM 349 H TRP A 26 24.630 10.183 -4.159 1.00 12.70 H ANISOU 349 H TRP A 26 1724 1606 1493 7 -126 122 H ATOM 350 HA TRP A 26 25.605 12.560 -3.892 1.00 12.63 H ANISOU 350 HA TRP A 26 1785 1808 1206 -73 -318 231 H ATOM 351 HB2 TRP A 26 27.594 11.611 -4.796 1.00 12.40 H ANISOU 351 HB2 TRP A 26 1644 1727 1340 -33 -147 455 H ATOM 352 HB3 TRP A 26 26.974 10.687 -3.666 1.00 13.30 H ANISOU 352 HB3 TRP A 26 1985 1761 1305 42 -149 564 H ATOM 353 HD1 TRP A 26 25.966 8.309 -4.484 1.00 12.68 H ANISOU 353 HD1 TRP A 26 1644 1470 1703 -124 -264 383 H ATOM 354 HE1 TRP A 26 26.225 7.019 -6.492 1.00 13.60 H ANISOU 354 HE1 TRP A 26 1689 1665 1812 14 -110 370 H ATOM 355 HE3 TRP A 26 28.045 11.714 -7.387 1.00 13.04 H ANISOU 355 HE3 TRP A 26 1640 1745 1568 91 61 327 H ATOM 356 HZ2 TRP A 26 27.223 7.415 -9.042 1.00 15.46 H ANISOU 356 HZ2 TRP A 26 1831 1881 2162 79 -9 247 H ATOM 357 HZ3 TRP A 26 28.591 11.152 -9.549 1.00 12.39 H ANISOU 357 HZ3 TRP A 26 1448 1893 1363 48 -17 331 H ATOM 358 HH2 TRP A 26 28.178 9.034 -10.354 1.00 14.76 H ANISOU 358 HH2 TRP A 26 1805 1976 1827 123 -105 144 H ATOM 359 N ALA A 27 24.831 11.875 -6.962 1.00 11.94 N ANISOU 359 N ALA A 27 1768 1641 1124 -19 -198 235 N ATOM 360 CA ALA A 27 24.686 12.426 -8.300 1.00 11.42 C ANISOU 360 CA ALA A 27 1596 1593 1149 -48 -13 343 C ATOM 361 C ALA A 27 23.610 13.527 -8.296 1.00 12.08 C ANISOU 361 C ALA A 27 1614 1533 1440 -37 -74 281 C ATOM 362 O ALA A 27 23.779 14.562 -8.944 1.00 12.37 O ANISOU 362 O ALA A 27 1678 1634 1388 -57 9 360 O ATOM 363 CB ALA A 27 24.386 11.348 -9.307 1.00 13.53 C ANISOU 363 CB ALA A 27 1765 1714 1660 37 -90 -67 C ATOM 364 H ALA A 27 24.524 11.076 -6.875 1.00 10.89 H ANISOU 364 H ALA A 27 1704 1504 929 127 -165 210 H ATOM 365 HA ALA A 27 25.533 12.842 -8.566 1.00 12.02 H ANISOU 365 HA ALA A 27 1538 1682 1347 -70 -55 274 H ATOM 366 N PHE A 28 22.545 13.322 -7.531 1.00 11.68 N ANISOU 366 N PHE A 28 1593 1510 1335 -53 -126 268 N ATOM 367 CA PHE A 28 21.485 14.323 -7.418 1.00 11.61 C ANISOU 367 CA PHE A 28 1649 1532 1227 -7 -211 158 C ATOM 368 C PHE A 28 21.985 15.541 -6.635 1.00 11.05 C ANISOU 368 C PHE A 28 1758 1575 865 91 -155 91 C ATOM 369 O PHE A 28 21.652 16.674 -6.984 1.00 12.66 O ANISOU 369 O PHE A 28 1607 1522 1682 14 -261 292 O ATOM 370 CB PHE A 28 20.225 13.707 -6.759 1.00 12.89 C ANISOU 370 CB PHE A 28 1488 1681 1728 12 -214 204 C ATOM 371 CG PHE A 28 19.487 12.797 -7.690 1.00 11.24 C ANISOU 371 CG PHE A 28 1514 1583 1173 -80 81 356 C ATOM 372 CD1 PHE A 28 19.834 11.475 -7.819 1.00 12.01 C ANISOU 372 CD1 PHE A 28 1508 1647 1407 22 -106 328 C ATOM 373 CD2 PHE A 28 18.485 13.289 -8.534 1.00 11.60 C ANISOU 373 CD2 PHE A 28 1624 1620 1161 20 -17 297 C ATOM 374 CE1 PHE A 28 19.213 10.671 -8.740 1.00 12.72 C ANISOU 374 CE1 PHE A 28 1775 1667 1391 -68 -138 288 C ATOM 375 CE2 PHE A 28 17.851 12.480 -9.467 1.00 13.36 C ANISOU 375 CE2 PHE A 28 1554 1754 1765 -41 -213 124 C ATOM 376 CZ PHE A 28 18.228 11.179 -9.591 1.00 12.55 C ANISOU 376 CZ PHE A 28 1920 1683 1165 -128 -203 241 C ATOM 377 H PHE A 28 22.409 12.610 -7.070 1.00 11.36 H ANISOU 377 H PHE A 28 1639 1380 1295 -96 -100 132 H ATOM 378 HA PHE A 28 21.233 14.626 -8.315 1.00 11.55 H ANISOU 378 HA PHE A 28 1652 1522 1214 23 -337 -9 H ATOM 379 HB2 PHE A 28 20.487 13.195 -5.977 1.00 11.68 H ANISOU 379 HB2 PHE A 28 1503 1501 1431 -36 -21 37 H ATOM 380 HB3 PHE A 28 19.623 14.422 -6.499 1.00 12.71 H ANISOU 380 HB3 PHE A 28 1642 1599 1587 -23 -112 177 H ATOM 381 HD1 PHE A 28 20.514 11.129 -7.292 1.00 11.78 H ANISOU 381 HD1 PHE A 28 1374 1731 1368 43 -9 290 H ATOM 382 HD2 PHE A 28 18.254 14.189 -8.485 1.00 12.04 H ANISOU 382 HD2 PHE A 28 1510 1619 1446 12 -3 242 H ATOM 383 HE1 PHE A 28 19.455 9.777 -8.807 1.00 12.97 H ANISOU 383 HE1 PHE A 28 1684 1682 1559 -54 -25 231 H ATOM 384 HE2 PHE A 28 17.184 12.829 -10.011 1.00 12.61 H ANISOU 384 HE2 PHE A 28 1523 1816 1452 -25 -68 104 H ATOM 385 HZ PHE A 28 17.780 10.615 -10.179 1.00 12.86 H ANISOU 385 HZ PHE A 28 1606 1797 1483 -178 -101 81 H ATOM 386 N SER A 29 22.728 15.328 -5.552 1.00 12.02 N ANISOU 386 N SER A 29 1786 1570 1209 -91 -353 339 N ATOM 387 CA SER A 29 23.330 16.434 -4.803 1.00 11.72 C ANISOU 387 CA SER A 29 1700 1633 1120 -35 -103 180 C ATOM 388 C SER A 29 24.239 17.268 -5.740 1.00 11.02 C ANISOU 388 C SER A 29 1934 1650 603 -50 -233 169 C ATOM 389 O SER A 29 24.157 18.510 -5.761 1.00 12.95 O ANISOU 389 O SER A 29 1541 1565 1815 -34 -272 354 O ATOM 390 CB SER A 29 24.111 15.907 -3.603 1.00 11.92 C ANISOU 390 CB SER A 29 1779 1473 1274 -87 -191 359 C ATOM 391 OG SER A 29 24.778 16.978 -2.987 1.00 12.42 O ANISOU 391 OG SER A 29 1707 1635 1377 -140 -359 296 O ATOM 392 H SER A 29 22.898 14.550 -5.227 1.00 10.98 H ANISOU 392 H SER A 29 1511 1513 1146 165 -116 167 H ATOM 393 HA SER A 29 22.619 17.019 -4.469 1.00 12.16 H ANISOU 393 HA SER A 29 1536 1637 1445 -37 -151 223 H ATOM 394 HB2 SER A 29 23.493 15.507 -2.973 1.00 11.32 H ANISOU 394 HB2 SER A 29 1584 1447 1269 23 -155 259 H ATOM 395 HB3 SER A 29 24.760 15.252 -3.903 1.00 12.00 H ANISOU 395 HB3 SER A 29 1568 1680 1308 -127 -114 274 H ATOM 396 N ALA A 30 25.025 16.588 -6.570 1.00 12.34 N ANISOU 396 N ALA A 30 1525 1538 1625 -38 -52 191 N ATOM 397 CA ALA A 30 25.980 17.269 -7.438 1.00 11.87 C ANISOU 397 CA ALA A 30 1659 1603 1245 -81 -233 231 C ATOM 398 C ALA A 30 25.268 18.003 -8.571 1.00 12.14 C ANISOU 398 C ALA A 30 1525 1675 1412 -30 -227 283 C ATOM 399 O ALA A 30 25.599 19.165 -8.876 1.00 13.42 O ANISOU 399 O ALA A 30 1628 1640 1829 14 -132 479 O ATOM 400 CB ALA A 30 26.967 16.287 -7.980 1.00 12.56 C ANISOU 400 CB ALA A 30 1635 1911 1226 78 -273 209 C ATOM 401 H ALA A 30 25.020 15.731 -6.646 1.00 11.80 H ANISOU 401 H ALA A 30 1632 1542 1308 -52 -137 156 H ATOM 402 HA ALA A 30 26.475 17.932 -6.914 1.00 12.04 H ANISOU 402 HA ALA A 30 1479 1666 1428 -112 -233 223 H ATOM 403 N THR A 31 24.258 17.394 -9.188 1.00 12.59 N ANISOU 403 N THR A 31 1536 1702 1543 -17 -315 416 N ATOM 404 CA THR A 31 23.514 18.110 -10.227 1.00 11.85 C ANISOU 404 CA THR A 31 1853 1738 910 -34 -212 257 C ATOM 405 C THR A 31 22.780 19.305 -9.631 1.00 11.32 C ANISOU 405 C THR A 31 1610 1563 1126 -231 -176 228 C ATOM 406 O THR A 31 22.724 20.357 -10.253 1.00 12.33 O ANISOU 406 O THR A 31 1713 1671 1300 -121 -161 353 O ATOM 407 CB THR A 31 22.528 17.238 -11.028 1.00 11.40 C ANISOU 407 CB THR A 31 1606 1584 1139 58 -124 164 C ATOM 408 OG1 THR A 31 21.604 16.647 -10.125 1.00 12.06 O ANISOU 408 OG1 THR A 31 1593 1761 1226 90 -43 330 O ATOM 409 CG2 THR A 31 23.217 16.189 -11.920 1.00 13.00 C ANISOU 409 CG2 THR A 31 1848 1568 1521 65 151 76 C ATOM 410 H THR A 31 23.987 16.594 -9.028 1.00 11.19 H ANISOU 410 H THR A 31 1528 1510 1212 121 -198 147 H ATOM 411 HA THR A 31 24.160 18.469 -10.872 1.00 12.31 H ANISOU 411 HA THR A 31 1668 1651 1356 -33 -100 273 H ATOM 412 HB THR A 31 22.029 17.821 -11.620 1.00 10.81 H ANISOU 412 HB THR A 31 1443 1485 1178 -47 -101 172 H ATOM 413 N GLY A 32 22.270 19.176 -8.412 1.00 11.52 N ANISOU 413 N GLY A 32 1589 1623 1163 11 -191 341 N ATOM 414 CA GLY A 32 21.598 20.294 -7.768 1.00 12.92 C ANISOU 414 CA GLY A 32 1700 1656 1549 -107 -117 109 C ATOM 415 C GLY A 32 22.541 21.478 -7.625 1.00 11.47 C ANISOU 415 C GLY A 32 1684 1569 1104 -12 -278 183 C ATOM 416 O GLY A 32 22.175 22.629 -7.871 1.00 12.24 O ANISOU 416 O GLY A 32 1697 1631 1322 64 -163 377 O ATOM 417 H GLY A 32 22.292 18.458 -7.939 1.00 11.39 H ANISOU 417 H GLY A 32 1669 1454 1203 -287 -136 236 H ATOM 418 HA2 GLY A 32 21.292 20.029 -6.887 1.00 12.66 H ANISOU 418 HA2 GLY A 32 1659 1597 1553 -53 -69 63 H ATOM 419 HA3 GLY A 32 20.832 20.567 -8.297 1.00 12.03 H ANISOU 419 HA3 GLY A 32 1536 1552 1480 -83 18 30 H ATOM 420 N ALA A 33 23.743 21.212 -7.120 1.00 13.04 N ANISOU 420 N ALA A 33 1664 1658 1632 -71 -321 613 N ATOM 421 CA ALA A 33 24.682 22.298 -6.846 1.00 12.38 C ANISOU 421 CA ALA A 33 1717 1764 1220 -79 -375 337 C ATOM 422 C ALA A 33 25.101 22.917 -8.194 1.00 11.52 C ANISOU 422 C ALA A 33 1564 1600 1212 47 -292 281 C ATOM 423 O ALA A 33 25.231 24.149 -8.298 1.00 13.57 O ANISOU 423 O ALA A 33 2060 1632 1461 -141 -258 360 O ATOM 424 CB ALA A 33 25.889 21.796 -6.074 1.00 13.91 C ANISOU 424 CB ALA A 33 1633 1954 1697 -55 -428 538 C ATOM 425 H ALA A 33 24.031 20.423 -6.931 1.00 12.24 H ANISOU 425 H ALA A 33 1609 1594 1446 114 -75 236 H ATOM 426 HA ALA A 33 24.241 22.989 -6.309 1.00 12.59 H ANISOU 426 HA ALA A 33 1505 1864 1413 -97 -89 395 H ATOM 427 N LEU A 34 25.352 22.099 -9.206 1.00 12.89 N ANISOU 427 N LEU A 34 1690 1678 1527 -140 110 221 N ATOM 428 CA LEU A 34 25.790 22.595 -10.490 1.00 13.26 C ANISOU 428 CA LEU A 34 1701 1877 1460 -192 -32 276 C ATOM 429 C LEU A 34 24.655 23.343 -11.212 1.00 13.20 C ANISOU 429 C LEU A 34 1868 1673 1472 -260 -87 374 C ATOM 430 O LEU A 34 24.896 24.353 -11.867 1.00 13.71 O ANISOU 430 O LEU A 34 1942 1778 1488 -126 -84 532 O ATOM 431 CB LEU A 34 26.403 21.478 -11.356 1.00 14.34 C ANISOU 431 CB LEU A 34 1974 1982 1489 -63 -42 205 C ATOM 432 CG LEU A 34 27.074 21.924 -12.648 1.00 15.19 C ANISOU 432 CG LEU A 34 2035 2197 1537 -47 -48 355 C ATOM 433 CD1 LEU A 34 28.090 23.090 -12.466 1.00 17.42 C ANISOU 433 CD1 LEU A 34 2073 2535 2011 -291 -383 655 C ATOM 434 CD2 LEU A 34 27.756 20.744 -13.341 1.00 17.97 C ANISOU 434 CD2 LEU A 34 2219 2482 2124 262 184 269 C ATOM 435 H LEU A 34 25.276 21.243 -9.170 1.00 12.37 H ANISOU 435 H LEU A 34 1652 1645 1403 -62 -55 177 H ATOM 436 HA LEU A 34 26.498 23.251 -10.322 1.00 13.29 H ANISOU 436 HA LEU A 34 1660 1738 1650 -145 59 335 H ATOM 437 HB2 LEU A 34 27.070 21.018 -10.820 1.00 13.97 H ANISOU 437 HB2 LEU A 34 1827 1967 1512 -93 51 258 H ATOM 438 HB3 LEU A 34 25.696 20.857 -11.591 1.00 14.20 H ANISOU 438 HB3 LEU A 34 1817 1917 1659 42 0 151 H ATOM 439 HG LEU A 34 26.385 22.244 -13.250 1.00 14.51 H ANISOU 439 HG LEU A 34 1929 2036 1548 -83 -24 278 H ATOM 440 N GLU A 35 23.410 22.886 -11.066 1.00 12.96 N ANISOU 440 N GLU A 35 1738 1488 1696 -101 -131 334 N ATOM 441 CA GLU A 35 22.242 23.617 -11.564 1.00 12.84 C ANISOU 441 CA GLU A 35 1817 1760 1299 8 -82 385 C ATOM 442 C GLU A 35 22.211 25.032 -10.993 1.00 13.26 C ANISOU 442 C GLU A 35 1799 1643 1596 -141 -150 471 C ATOM 443 O GLU A 35 21.999 26.008 -11.738 1.00 14.26 O ANISOU 443 O GLU A 35 2063 1731 1622 -92 -354 508 O ATOM 444 CB GLU A 35 20.927 22.851 -11.253 1.00 13.47 C ANISOU 444 CB GLU A 35 1766 1678 1674 -17 -355 419 C ATOM 445 CG GLU A 35 20.699 21.616 -12.146 1.00 13.65 C ANISOU 445 CG GLU A 35 1766 1658 1760 -21 -235 334 C ATOM 446 CD GLU A 35 19.728 20.563 -11.591 1.00 11.92 C ANISOU 446 CD GLU A 35 1783 1712 1032 -21 -316 198 C ATOM 447 OE1 GLU A 35 19.233 20.728 -10.450 1.00 12.62 O ANISOU 447 OE1 GLU A 35 1693 1708 1394 55 -176 172 O ATOM 448 OE2 GLU A 35 19.541 19.572 -12.341 1.00 12.45 O ANISOU 448 OE2 GLU A 35 1747 1639 1344 -49 -212 167 O ATOM 449 H GLU A 35 23.215 22.142 -10.683 1.00 11.72 H ANISOU 449 H GLU A 35 1613 1416 1421 -56 -32 173 H ATOM 450 HA GLU A 35 22.316 23.694 -12.538 1.00 14.87 H ANISOU 450 HA GLU A 35 2064 2274 1311 104 -59 328 H ATOM 451 HB2 GLU A 35 20.953 22.557 -10.330 1.00 13.17 H ANISOU 451 HB2 GLU A 35 1657 1751 1595 25 24 335 H ATOM 452 HB3 GLU A 35 20.176 23.451 -11.385 1.00 13.72 H ANISOU 452 HB3 GLU A 35 1736 1784 1691 74 -146 247 H ATOM 453 HG2 GLU A 35 20.338 21.920 -12.992 1.00 12.76 H ANISOU 453 HG2 GLU A 35 1684 1618 1546 22 18 277 H ATOM 454 HG3 GLU A 35 21.550 21.181 -12.299 1.00 13.99 H ANISOU 454 HG3 GLU A 35 1700 1957 1658 -31 -228 214 H ATOM 455 N GLY A 36 22.432 25.156 -9.694 1.00 13.50 N ANISOU 455 N GLY A 36 1974 1569 1583 -187 -69 343 N ATOM 456 CA GLY A 36 22.487 26.447 -9.028 1.00 12.59 C ANISOU 456 CA GLY A 36 1720 1642 1420 41 -195 328 C ATOM 457 C GLY A 36 23.591 27.353 -9.547 1.00 14.23 C ANISOU 457 C GLY A 36 1927 1675 1802 -139 -129 283 C ATOM 458 O GLY A 36 23.353 28.542 -9.811 1.00 14.39 O ANISOU 458 O GLY A 36 2049 1681 1737 -172 -157 403 O ATOM 459 H GLY A 36 22.554 24.492 -9.160 1.00 12.51 H ANISOU 459 H GLY A 36 1748 1601 1401 59 7 222 H ATOM 460 HA2 GLY A 36 22.620 26.312 -8.078 1.00 13.69 H ANISOU 460 HA2 GLY A 36 1796 2011 1392 83 -146 258 H ATOM 461 HA3 GLY A 36 21.640 26.903 -9.151 1.00 13.70 H ANISOU 461 HA3 GLY A 36 1709 1891 1604 104 -220 206 H ATOM 462 N GLN A 37 24.791 26.808 -9.690 1.00 13.56 N ANISOU 462 N GLN A 37 1898 1627 1626 -231 -195 404 N ATOM 463 CA GLN A 37 25.933 27.633 -10.075 1.00 13.94 C ANISOU 463 CA GLN A 37 1907 1838 1551 -226 -201 502 C ATOM 464 C GLN A 37 25.851 27.996 -11.547 1.00 13.37 C ANISOU 464 C GLN A 37 2091 1468 1520 -79 -291 349 C ATOM 465 O GLN A 37 26.252 29.111 -11.941 1.00 16.70 O ANISOU 465 O GLN A 37 2421 1828 2097 -402 -12 671 O ATOM 466 CB GLN A 37 27.260 26.970 -9.691 1.00 13.82 C ANISOU 466 CB GLN A 37 1835 1682 1733 -252 -87 412 C ATOM 467 CG GLN A 37 27.507 26.910 -8.210 1.00 14.00 C ANISOU 467 CG GLN A 37 1728 1992 1597 -225 -80 209 C ATOM 468 CD GLN A 37 27.324 28.264 -7.586 1.00 15.50 C ANISOU 468 CD GLN A 37 2013 1986 1891 -389 -298 -1 C ATOM 469 OE1 GLN A 37 28.164 29.150 -7.767 1.00 18.50 O ANISOU 469 OE1 GLN A 37 2191 2177 2661 -525 -378 541 O ATOM 470 NE2 GLN A 37 26.222 28.461 -6.862 1.00 15.49 N ANISOU 470 NE2 GLN A 37 2133 1899 1853 -171 -150 261 N ATOM 471 H GLN A 37 24.971 25.975 -9.572 1.00 13.62 H ANISOU 471 H GLN A 37 1938 1602 1633 -148 -87 227 H ATOM 472 HA GLN A 37 25.879 28.480 -9.588 1.00 13.09 H ANISOU 472 HA GLN A 37 1590 1868 1515 -283 -170 416 H ATOM 473 HB2 GLN A 37 27.268 26.061 -10.031 1.00 13.83 H ANISOU 473 HB2 GLN A 37 1787 1817 1651 -260 -88 215 H ATOM 474 HB3 GLN A 37 27.986 27.474 -10.090 1.00 13.95 H ANISOU 474 HB3 GLN A 37 1845 1741 1712 -206 74 275 H ATOM 475 HG2 GLN A 37 26.878 26.293 -7.804 1.00 13.37 H ANISOU 475 HG2 GLN A 37 1713 1789 1576 -82 -49 219 H ATOM 476 HG3 GLN A 37 28.416 26.619 -8.047 1.00 14.99 H ANISOU 476 HG3 GLN A 37 1727 2247 1719 -198 -93 239 H ATOM 477 N MET A 38 25.320 27.108 -12.391 1.00 14.81 N ANISOU 477 N MET A 38 2316 1943 1365 -402 -177 299 N ATOM 478 CA MET A 38 25.095 27.436 -13.787 1.00 13.58 C ANISOU 478 CA MET A 38 2015 1834 1311 -138 7 246 C ATOM 479 C MET A 38 24.047 28.549 -13.916 1.00 15.95 C ANISOU 479 C MET A 38 2282 1769 2007 -63 83 591 C ATOM 480 O MET A 38 24.210 29.447 -14.755 1.00 15.43 O ANISOU 480 O MET A 38 2460 1853 1549 -11 178 435 O ATOM 481 CB MET A 38 24.661 26.221 -14.625 1.00 13.98 C ANISOU 481 CB MET A 38 2027 2102 1182 -97 -186 113 C ATOM 482 CG MET A 38 25.770 25.210 -14.939 1.00 14.85 C ANISOU 482 CG MET A 38 2121 1812 1709 -38 -192 421 C ATOM 483 SD MET A 38 27.254 25.863 -15.792 1.00 16.93 S ANISOU 483 SD MET A 38 2358 2088 1985 -52 41 481 S ATOM 484 CE MET A 38 26.553 26.569 -17.295 1.00 16.77 C ANISOU 484 CE MET A 38 2522 2076 1771 76 224 373 C ATOM 485 H MET A 38 25.090 26.308 -12.175 1.00 12.97 H ANISOU 485 H MET A 38 1988 1674 1265 -73 -215 144 H ATOM 486 HA MET A 38 25.935 27.769 -14.164 1.00 14.60 H ANISOU 486 HA MET A 38 2021 2001 1522 -220 -47 402 H ATOM 487 HB2 MET A 38 23.968 25.747 -14.139 1.00 14.39 H ANISOU 487 HB2 MET A 38 2051 1800 1614 -102 -233 270 H ATOM 488 HB3 MET A 38 24.297 26.536 -15.467 1.00 14.27 H ANISOU 488 HB3 MET A 38 2008 1976 1436 25 -270 232 H ATOM 489 HG2 MET A 38 26.070 24.815 -14.106 1.00 15.35 H ANISOU 489 HG2 MET A 38 2282 1992 1556 -31 -141 340 H ATOM 490 HG3 MET A 38 25.392 24.519 -15.504 1.00 15.30 H ANISOU 490 HG3 MET A 38 2066 2038 1708 80 -180 188 H ATOM 491 N PHE A 39 22.995 28.487 -13.097 1.00 15.30 N ANISOU 491 N PHE A 39 2144 1674 1993 -88 -41 559 N ATOM 492 CA PHE A 39 21.986 29.554 -13.042 1.00 15.53 C ANISOU 492 CA PHE A 39 2293 1774 1833 -16 83 556 C ATOM 493 C PHE A 39 22.597 30.892 -12.622 1.00 15.35 C ANISOU 493 C PHE A 39 2334 1681 1815 10 90 494 C ATOM 494 O PHE A 39 22.323 31.923 -13.245 1.00 16.76 O ANISOU 494 O PHE A 39 2678 1918 1769 -32 278 741 O ATOM 495 CB PHE A 39 20.815 29.200 -12.124 1.00 15.50 C ANISOU 495 CB PHE A 39 2186 1924 1776 -93 -54 530 C ATOM 496 CG PHE A 39 19.727 30.231 -12.136 1.00 15.11 C ANISOU 496 CG PHE A 39 2203 1847 1689 -138 75 444 C ATOM 497 CD1 PHE A 39 18.853 30.336 -13.206 1.00 15.47 C ANISOU 497 CD1 PHE A 39 2489 1720 1668 -114 -42 204 C ATOM 498 CD2 PHE A 39 19.603 31.112 -11.107 1.00 14.38 C ANISOU 498 CD2 PHE A 39 2079 1780 1602 -1 -100 495 C ATOM 499 CE1 PHE A 39 17.858 31.298 -13.212 1.00 15.94 C ANISOU 499 CE1 PHE A 39 2098 2098 1860 -222 -29 290 C ATOM 500 CE2 PHE A 39 18.617 32.049 -11.073 1.00 15.10 C ANISOU 500 CE2 PHE A 39 2019 1924 1794 -25 -113 409 C ATOM 501 CZ PHE A 39 17.750 32.157 -12.143 1.00 14.56 C ANISOU 501 CZ PHE A 39 1852 1859 1820 42 -113 379 C ATOM 502 H PHE A 39 22.837 27.832 -12.562 1.00 13.90 H ANISOU 502 H PHE A 39 2153 1586 1543 -165 -127 305 H ATOM 503 HA PHE A 39 21.620 29.674 -13.944 1.00 15.12 H ANISOU 503 HA PHE A 39 2022 1891 1830 102 97 382 H ATOM 504 HB2 PHE A 39 20.431 28.359 -12.419 1.00 14.77 H ANISOU 504 HB2 PHE A 39 1827 2054 1729 27 -21 271 H ATOM 505 HB3 PHE A 39 21.142 29.111 -11.216 1.00 15.05 H ANISOU 505 HB3 PHE A 39 2011 2000 1705 -93 28 266 H ATOM 506 HD1 PHE A 39 18.933 29.752 -13.923 1.00 17.10 H ANISOU 506 HD1 PHE A 39 2652 1998 1846 -238 23 1 H ATOM 507 HD2 PHE A 39 20.181 31.043 -10.382 1.00 14.90 H ANISOU 507 HD2 PHE A 39 1783 2120 1758 -86 -86 368 H ATOM 508 HE1 PHE A 39 17.268 31.360 -13.927 1.00 16.38 H ANISOU 508 HE1 PHE A 39 2016 2318 1889 -204 -21 184 H ATOM 509 HE2 PHE A 39 18.552 32.636 -10.355 1.00 15.30 H ANISOU 509 HE2 PHE A 39 1813 2049 1951 -28 -127 232 H ATOM 510 HZ PHE A 39 17.082 32.804 -12.135 1.00 15.51 H ANISOU 510 HZ PHE A 39 1727 1951 2212 12 -21 444 H ATOM 511 N AARG A 40 23.395 30.884 -11.564 0.70 17.23 N ANISOU 511 N AARG A 40 2660 1678 2209 -202 -218 485 N ATOM 512 CA AARG A 40 24.108 32.080 -11.124 0.70 16.59 C ANISOU 512 CA AARG A 40 2350 2002 1948 -321 352 113 C ATOM 513 C AARG A 40 24.843 32.696 -12.311 0.70 16.83 C ANISOU 513 C AARG A 40 3009 1794 1592 -348 177 112 C ATOM 514 O AARG A 40 24.654 33.886 -12.632 0.70 18.18 O ANISOU 514 O AARG A 40 2515 1979 2412 -38 237 478 O ATOM 515 CB AARG A 40 25.108 31.696 -10.043 0.70 18.12 C ANISOU 515 CB AARG A 40 2448 2443 1991 -320 216 183 C ATOM 516 CG AARG A 40 25.739 32.852 -9.313 0.70 21.67 C ANISOU 516 CG AARG A 40 3323 2604 2305 -411 57 -64 C ATOM 517 CD AARG A 40 26.718 32.284 -8.316 0.70 25.28 C ANISOU 517 CD AARG A 40 3353 3528 2722 -420 -291 12 C ATOM 518 NE AARG A 40 27.481 33.298 -7.594 0.70 28.63 N ANISOU 518 NE AARG A 40 3571 3206 4101 -414 -707 -95 N ATOM 519 CZ AARG A 40 28.557 33.032 -6.862 0.70 30.82 C ANISOU 519 CZ AARG A 40 3268 3384 5056 -148 -824 -384 C ATOM 520 NH1AARG A 40 29.016 31.787 -6.754 0.70 24.92 N ANISOU 520 NH1AARG A 40 3782 3030 2657 -554 -279 566 N ATOM 521 NH2AARG A 40 29.184 34.019 -6.241 0.70 30.44 N ANISOU 521 NH2AARG A 40 4595 3668 3303 -262 -946 -397 N ATOM 522 H AARG A 40 23.538 30.188 -11.079 0.70 15.05 H ANISOU 522 H AARG A 40 2248 1753 1718 80 78 317 H ATOM 523 HA AARG A 40 23.477 32.736 -10.761 0.70 17.67 H ANISOU 523 HA AARG A 40 2483 2137 2093 -191 224 -44 H ATOM 524 HB2AARG A 40 24.652 31.156 -9.378 0.70 18.62 H ANISOU 524 HB2AARG A 40 2521 2471 2083 -159 236 317 H ATOM 525 HB3AARG A 40 25.821 31.179 -10.445 0.70 18.37 H ANISOU 525 HB3AARG A 40 2457 2441 2079 -237 168 168 H ATOM 526 HG2AARG A 40 26.219 33.421 -9.934 0.70 21.25 H ANISOU 526 HG2AARG A 40 2763 2433 2877 -387 104 -65 H ATOM 527 HG3AARG A 40 25.059 33.354 -8.836 0.70 22.04 H ANISOU 527 HG3AARG A 40 3227 2707 2438 -461 109 -137 H ATOM 528 HD2AARG A 40 26.234 31.752 -7.668 0.70 23.39 H ANISOU 528 HD2AARG A 40 3112 2838 2936 0 -310 134 H ATOM 529 HD3AARG A 40 27.348 31.726 -8.799 0.70 25.48 H ANISOU 529 HD3AARG A 40 3280 3302 3096 -324 -165 186 H ATOM 530 HE AARG A 40 27.092 34.184 -7.527 0.70 26.62 H ANISOU 530 HE AARG A 40 3312 3479 3323 -156 -267 -103 H ATOM 531 HH11AARG A 40 28.624 31.133 -7.148 0.70 25.32 H ANISOU 531 HH11AARG A 40 3212 3327 3081 -230 -83 -58 H ATOM 532 HH12AARG A 40 29.715 31.631 -6.277 0.70 25.69 H ANISOU 532 HH12AARG A 40 3272 3386 3101 -208 -116 -87 H ATOM 533 HH21AARG A 40 28.895 34.826 -6.308 0.70 27.60 H ANISOU 533 HH21AARG A 40 3589 3654 3243 -326 -345 -414 H ATOM 534 HH22AARG A 40 29.883 33.856 -5.767 0.70 27.29 H ANISOU 534 HH22AARG A 40 3547 3524 3294 -296 -167 -358 H ATOM 535 N BARG A 40 23.432 30.879 -11.584 0.30 16.42 N ANISOU 535 N BARG A 40 2383 1780 2075 -143 -62 416 N ATOM 536 CA BARG A 40 24.112 32.091 -11.105 0.30 16.23 C ANISOU 536 CA BARG A 40 2293 1904 1967 -178 184 213 C ATOM 537 C BARG A 40 25.002 32.718 -12.181 0.30 16.40 C ANISOU 537 C BARG A 40 2471 1873 1887 -228 59 330 C ATOM 538 O BARG A 40 25.123 33.948 -12.259 0.30 14.37 O ANISOU 538 O BARG A 40 2431 1892 1136 -404 -558 359 O ATOM 539 CB BARG A 40 24.955 31.768 -9.866 0.30 17.37 C ANISOU 539 CB BARG A 40 2422 2126 2051 -194 46 285 C ATOM 540 CG BARG A 40 26.017 32.811 -9.533 0.30 19.32 C ANISOU 540 CG BARG A 40 2543 2293 2501 -268 -23 82 C ATOM 541 CD BARG A 40 26.865 32.395 -8.333 0.30 20.49 C ANISOU 541 CD BARG A 40 2659 2623 2504 -232 -169 -139 C ATOM 542 NE BARG A 40 26.336 32.874 -7.055 0.30 22.40 N ANISOU 542 NE BARG A 40 2702 3155 2651 157 104 9 N ATOM 543 CZ BARG A 40 25.199 33.548 -6.915 0.30 19.88 C ANISOU 543 CZ BARG A 40 2526 2589 2437 -121 261 416 C ATOM 544 NH1BARG A 40 24.465 33.822 -7.976 0.30 21.36 N ANISOU 544 NH1BARG A 40 2662 2933 2520 -127 -117 -295 N ATOM 545 NH2BARG A 40 24.797 33.944 -5.713 0.30 19.39 N ANISOU 545 NH2BARG A 40 2625 2245 2495 66 -288 -112 N ATOM 546 H BARG A 40 23.625 30.175 -11.130 0.30 14.75 H ANISOU 546 H BARG A 40 2055 1788 1760 66 50 231 H ATOM 547 HA BARG A 40 23.437 32.754 -10.847 0.30 17.12 H ANISOU 547 HA BARG A 40 2266 2062 2174 -108 49 39 H ATOM 548 HB2BARG A 40 24.365 31.697 -9.101 0.30 17.18 H ANISOU 548 HB2BARG A 40 2266 2253 2009 -10 -9 160 H ATOM 549 HB3BARG A 40 25.407 30.921 -10.010 0.30 17.10 H ANISOU 549 HB3BARG A 40 2227 2287 1983 -123 -7 80 H ATOM 550 HG2BARG A 40 26.606 32.921 -10.296 0.30 18.55 H ANISOU 550 HG2BARG A 40 2276 2186 2583 -221 -45 13 H ATOM 551 HG3BARG A 40 25.583 33.652 -9.321 0.30 19.46 H ANISOU 551 HG3BARG A 40 2557 2384 2451 -262 21 -111 H ATOM 552 HD2BARG A 40 26.899 31.427 -8.295 0.30 20.47 H ANISOU 552 HD2BARG A 40 2512 2639 2626 -78 -107 123 H ATOM 553 HD3BARG A 40 27.759 32.754 -8.439 0.30 19.98 H ANISOU 553 HD3BARG A 40 2534 2528 2528 -10 -32 -16 H ATOM 554 HE BARG A 40 26.836 32.660 -6.251 0.30 20.21 H ANISOU 554 HE BARG A 40 2523 2616 2540 23 172 -98 H ATOM 555 HH11BARG A 40 24.723 33.567 -8.756 0.30 20.82 H ANISOU 555 HH11BARG A 40 2713 2686 2510 -89 33 -44 H ATOM 556 HH12BARG A 40 23.728 34.258 -7.888 0.30 20.45 H ANISOU 556 HH12BARG A 40 2690 2771 2305 -107 -43 -21 H ATOM 557 HH21BARG A 40 25.274 33.765 -5.019 0.30 19.34 H ANISOU 557 HH21BARG A 40 2432 2431 2484 -3 -115 152 H ATOM 558 HH22BARG A 40 24.060 34.379 -5.627 0.30 19.21 H ANISOU 558 HH22BARG A 40 2476 2421 2402 -1 -144 70 H ATOM 559 N LYS A 41 25.642 31.870 -12.980 1.00 16.94 N ANISOU 559 N LYS A 41 2795 1936 1706 -167 272 584 N ATOM 560 CA LYS A 41 26.516 32.312 -14.043 1.00 16.68 C ANISOU 560 CA LYS A 41 2671 2356 1308 -192 22 565 C ATOM 561 C LYS A 41 25.762 32.812 -15.276 1.00 15.12 C ANISOU 561 C LYS A 41 2592 2053 1100 -32 279 441 C ATOM 562 O LYS A 41 26.150 33.830 -15.877 1.00 19.67 O ANISOU 562 O LYS A 41 3271 2252 1950 -124 383 870 O ATOM 563 CB LYS A 41 27.427 31.152 -14.491 1.00 19.25 C ANISOU 563 CB LYS A 41 2585 2382 2345 -21 24 567 C ATOM 564 CG LYS A 41 28.505 31.508 -15.545 1.00 22.32 C ANISOU 564 CG LYS A 41 3436 2719 2323 -139 465 406 C ATOM 565 CD LYS A 41 29.230 30.238 -16.010 1.00 28.67 C ANISOU 565 CD LYS A 41 3494 3618 3782 738 387 145 C ATOM 566 CE LYS A 41 30.509 30.518 -16.813 1.00 33.34 C ANISOU 566 CE LYS A 41 3849 5155 3664 461 623 -70 C ATOM 567 NZ LYS A 41 30.267 31.340 -18.037 1.00 42.94 N ANISOU 567 NZ LYS A 41 6009 5153 5153 -146 682 1051 N ATOM 568 H LYS A 41 25.643 31.017 -12.877 1.00 15.78 H ANISOU 568 H LYS A 41 2314 1872 1808 -234 93 341 H ATOM 569 HA LYS A 41 27.088 33.038 -13.717 1.00 16.75 H ANISOU 569 HA LYS A 41 2092 2412 1857 -96 38 552 H ATOM 570 HB2 LYS A 41 27.888 30.807 -13.710 1.00 18.86 H ANISOU 570 HB2 LYS A 41 2517 2497 2153 -67 40 372 H ATOM 571 HB3 LYS A 41 26.870 30.454 -14.870 1.00 19.61 H ANISOU 571 HB3 LYS A 41 2616 2593 2242 116 -47 211 H ATOM 572 HG2 LYS A 41 28.092 31.920 -16.319 1.00 21.40 H ANISOU 572 HG2 LYS A 41 2933 2745 2451 -186 401 377 H ATOM 573 HG3 LYS A 41 29.158 32.107 -15.150 1.00 23.09 H ANISOU 573 HG3 LYS A 41 2540 3346 2886 -71 312 515 H ATOM 574 HD2 LYS A 41 29.477 29.714 -15.231 1.00 27.79 H ANISOU 574 HD2 LYS A 41 3690 3043 3825 305 150 21 H ATOM 575 HD3 LYS A 41 28.632 29.725 -16.575 1.00 27.58 H ANISOU 575 HD3 LYS A 41 4041 3004 3431 689 440 37 H ATOM 576 HE2 LYS A 41 31.136 30.999 -16.249 1.00 35.97 H ANISOU 576 HE2 LYS A 41 4075 4354 5235 -66 491 -154 H ATOM 577 HE3 LYS A 41 30.896 29.674 -17.092 1.00 31.06 H ANISOU 577 HE3 LYS A 41 3160 4741 3901 -13 506 -64 H ATOM 578 N THR A 42 24.719 32.097 -15.703 1.00 19.01 N ANISOU 578 N THR A 42 2738 2551 1932 -147 -209 686 N ATOM 579 CA THR A 42 24.080 32.298 -17.020 1.00 16.97 C ANISOU 579 CA THR A 42 2568 2207 1673 25 30 385 C ATOM 580 C THR A 42 22.648 32.865 -16.999 1.00 17.37 C ANISOU 580 C THR A 42 2838 2129 1631 197 270 1120 C ATOM 581 O THR A 42 22.162 33.328 -18.050 1.00 18.16 O ANISOU 581 O THR A 42 3045 2353 1501 287 307 1027 O ATOM 582 CB THR A 42 23.957 30.978 -17.840 1.00 18.35 C ANISOU 582 CB THR A 42 3003 2346 1622 64 328 348 C ATOM 583 OG1 THR A 42 22.955 30.150 -17.242 1.00 18.49 O ANISOU 583 OG1 THR A 42 2959 2414 1650 79 -95 849 O ATOM 584 CG2 THR A 42 25.289 30.259 -17.973 1.00 19.64 C ANISOU 584 CG2 THR A 42 3090 2582 1791 292 205 590 C ATOM 585 H THR A 42 24.354 31.468 -15.244 1.00 16.12 H ANISOU 585 H THR A 42 2386 2078 1661 33 -116 275 H ATOM 586 HA THR A 42 24.624 32.916 -17.551 1.00 17.68 H ANISOU 586 HA THR A 42 2581 2371 1763 -41 -20 477 H ATOM 587 HB THR A 42 23.666 31.204 -18.738 1.00 16.64 H ANISOU 587 HB THR A 42 2578 1936 1806 -237 142 402 H ATOM 588 N GLY A 43 21.986 32.781 -15.845 1.00 17.68 N ANISOU 588 N GLY A 43 3000 2050 1666 -58 373 986 N ATOM 589 CA GLY A 43 20.570 33.113 -15.759 1.00 18.70 C ANISOU 589 CA GLY A 43 2819 2307 1976 -106 271 872 C ATOM 590 C GLY A 43 19.610 32.069 -16.334 1.00 18.10 C ANISOU 590 C GLY A 43 2786 2345 1744 0 311 560 C ATOM 591 O GLY A 43 18.394 32.314 -16.389 1.00 21.23 O ANISOU 591 O GLY A 43 3024 2464 2576 401 62 1049 O ATOM 592 H GLY A 43 22.329 32.537 -15.096 1.00 16.64 H ANISOU 592 H GLY A 43 2680 2032 1609 -166 347 771 H ATOM 593 HA2 GLY A 43 20.411 33.949 -16.222 1.00 19.43 H ANISOU 593 HA2 GLY A 43 3272 1978 2134 232 189 483 H ATOM 594 HA3 GLY A 43 20.339 33.243 -14.826 1.00 18.62 H ANISOU 594 HA3 GLY A 43 2748 2277 2048 16 143 452 H ATOM 595 N ARG A 44 20.119 30.897 -16.727 1.00 18.55 N ANISOU 595 N ARG A 44 2810 2087 2151 167 178 1027 N ATOM 596 CA ARG A 44 19.274 29.833 -17.307 1.00 19.34 C ANISOU 596 CA ARG A 44 2712 2230 2405 285 -10 797 C ATOM 597 C ARG A 44 19.339 28.612 -16.389 1.00 16.34 C ANISOU 597 C ARG A 44 2374 2092 1741 41 -578 468 C ATOM 598 O ARG A 44 20.442 28.129 -16.072 1.00 17.12 O ANISOU 598 O ARG A 44 2312 2250 1942 189 -111 597 O ATOM 599 CB ARG A 44 19.748 29.392 -18.711 1.00 22.65 C ANISOU 599 CB ARG A 44 3478 2668 2459 -202 515 814 C ATOM 600 CG ARG A 44 19.353 30.258 -19.904 1.00 24.54 C ANISOU 600 CG ARG A 44 3909 2683 2729 153 606 903 C ATOM 601 CD ARG A 44 19.679 29.527 -21.222 1.00 31.01 C ANISOU 601 CD ARG A 44 4526 4212 3045 317 99 -175 C ATOM 602 NE ARG A 44 19.461 30.357 -22.413 0.50 34.32 N ANISOU 602 NE ARG A 44 4848 4856 3334 284 -203 105 N ATOM 603 CZ ARG A 44 20.171 30.292 -23.543 0.50 34.40 C ANISOU 603 CZ ARG A 44 4975 4256 3840 171 294 289 C ATOM 604 NH1 ARG A 44 21.187 29.444 -23.680 0.50 35.74 N ANISOU 604 NH1 ARG A 44 5079 4679 3819 326 -216 229 N ATOM 605 NH2 ARG A 44 19.869 31.100 -24.553 0.50 35.99 N ANISOU 605 NH2 ARG A 44 4556 4893 4225 280 -22 193 N ATOM 606 H ARG A 44 20.947 30.677 -16.667 1.00 19.36 H ANISOU 606 H ARG A 44 2706 2493 2156 79 223 516 H ATOM 607 HA ARG A 44 18.343 30.129 -17.378 1.00 19.10 H ANISOU 607 HA ARG A 44 2767 1950 2540 306 -104 768 H ATOM 608 HB2 ARG A 44 20.718 29.354 -18.699 1.00 22.48 H ANISOU 608 HB2 ARG A 44 3394 2629 2516 -104 319 166 H ATOM 609 HB3 ARG A 44 19.399 28.504 -18.884 1.00 21.07 H ANISOU 609 HB3 ARG A 44 3057 2561 2386 160 70 626 H ATOM 610 HG2 ARG A 44 18.399 30.433 -19.877 1.00 24.71 H ANISOU 610 HG2 ARG A 44 3668 2942 2778 -131 -84 326 H ATOM 611 HG3 ARG A 44 19.852 31.090 -19.882 1.00 22.58 H ANISOU 611 HG3 ARG A 44 3434 2870 2276 129 172 896 H ATOM 612 HD2 ARG A 44 20.610 29.261 -21.188 1.00 28.65 H ANISOU 612 HD2 ARG A 44 4281 3612 2993 29 371 -131 H ATOM 613 HD3 ARG A 44 19.113 28.743 -21.295 1.00 31.22 H ANISOU 613 HD3 ARG A 44 4041 4284 3537 370 29 -229 H ATOM 614 HE ARG A 44 18.717 30.979 -22.391 0.50 32.17 H ANISOU 614 HE ARG A 44 4478 4224 3521 -133 -60 172 H ATOM 615 HH11 ARG A 44 21.409 28.907 -23.049 0.50 34.04 H ANISOU 615 HH11 ARG A 44 4419 4292 4221 0 36 38 H ATOM 616 HH12 ARG A 44 21.625 29.428 -24.420 0.50 34.19 H ANISOU 616 HH12 ARG A 44 4387 4314 4287 33 -7 121 H ATOM 617 HH21 ARG A 44 19.217 31.656 -24.479 0.50 34.27 H ANISOU 617 HH21 ARG A 44 4604 4392 4022 -58 -117 217 H ATOM 618 HH22 ARG A 44 20.325 31.066 -25.282 0.50 33.45 H ANISOU 618 HH22 ARG A 44 4618 3987 4104 -38 -68 442 H ATOM 619 N LEU A 45 18.168 28.145 -15.946 1.00 16.00 N ANISOU 619 N LEU A 45 2211 1965 1900 353 -492 556 N ATOM 620 CA LEU A 45 18.064 26.908 -15.179 1.00 14.98 C ANISOU 620 CA LEU A 45 2143 1699 1848 379 -456 271 C ATOM 621 C LEU A 45 17.798 25.736 -16.099 1.00 15.93 C ANISOU 621 C LEU A 45 2212 1921 1918 103 -593 208 C ATOM 622 O LEU A 45 16.741 25.665 -16.723 1.00 17.19 O ANISOU 622 O LEU A 45 2611 2227 1693 129 -882 277 O ATOM 623 CB LEU A 45 16.964 27.037 -14.139 1.00 14.52 C ANISOU 623 CB LEU A 45 2179 1661 1676 43 -435 279 C ATOM 624 CG LEU A 45 16.887 25.876 -13.146 1.00 15.34 C ANISOU 624 CG LEU A 45 2291 1651 1886 66 -432 377 C ATOM 625 CD1 LEU A 45 18.197 25.693 -12.409 1.00 16.93 C ANISOU 625 CD1 LEU A 45 2244 2289 1898 -131 -469 860 C ATOM 626 CD2 LEU A 45 15.744 26.103 -12.160 1.00 15.50 C ANISOU 626 CD2 LEU A 45 2433 1970 1485 -71 -471 167 C ATOM 627 H LEU A 45 17.411 28.532 -16.081 1.00 14.88 H ANISOU 627 H LEU A 45 2208 1564 1879 291 -497 216 H ATOM 628 HA LEU A 45 18.907 26.756 -14.712 1.00 13.76 H ANISOU 628 HA LEU A 45 2110 1559 1558 183 -382 312 H ATOM 629 HB2 LEU A 45 17.113 27.855 -13.639 1.00 14.52 H ANISOU 629 HB2 LEU A 45 2022 1639 1853 -74 -244 238 H ATOM 630 HB3 LEU A 45 16.112 27.092 -14.600 1.00 14.16 H ANISOU 630 HB3 LEU A 45 2086 1667 1627 95 -324 238 H ATOM 631 HG LEU A 45 16.699 25.055 -13.627 1.00 15.32 H ANISOU 631 HG LEU A 45 2108 1695 2015 -45 -161 276 H ATOM 632 N ILE A 46 18.762 24.824 -16.180 1.00 15.45 N ANISOU 632 N ILE A 46 2488 1942 1437 215 -431 230 N ATOM 633 CA ILE A 46 18.627 23.623 -16.995 1.00 14.59 C ANISOU 633 CA ILE A 46 2241 1827 1476 -47 -373 347 C ATOM 634 C ILE A 46 18.904 22.390 -16.132 1.00 13.95 C ANISOU 634 C ILE A 46 2121 1708 1472 82 -257 205 C ATOM 635 O ILE A 46 19.971 22.237 -15.538 1.00 15.06 O ANISOU 635 O ILE A 46 2118 1840 1761 -132 -380 525 O ATOM 636 CB ILE A 46 19.581 23.618 -18.224 1.00 15.68 C ANISOU 636 CB ILE A 46 2552 1992 1411 3 -382 334 C ATOM 637 CG1 ILE A 46 19.425 24.916 -19.035 1.00 16.27 C ANISOU 637 CG1 ILE A 46 2811 2145 1224 45 -127 377 C ATOM 638 CG2 ILE A 46 19.362 22.352 -19.097 1.00 17.23 C ANISOU 638 CG2 ILE A 46 2945 2189 1413 36 -86 83 C ATOM 639 CD1 ILE A 46 20.456 25.087 -20.142 1.00 20.17 C ANISOU 639 CD1 ILE A 46 3135 2698 1827 135 324 718 C ATOM 640 H ILE A 46 19.515 24.877 -15.769 1.00 14.34 H ANISOU 640 H ILE A 46 2013 1673 1761 67 -75 66 H ATOM 641 HA ILE A 46 17.709 23.558 -17.333 1.00 15.55 H ANISOU 641 HA ILE A 46 2196 1844 1868 196 -435 208 H ATOM 642 HB ILE A 46 20.490 23.586 -17.885 1.00 16.03 H ANISOU 642 HB ILE A 46 2294 1899 1895 125 -143 235 H ATOM 643 HG12 ILE A 46 18.545 24.932 -19.443 1.00 15.94 H ANISOU 643 HG12 ILE A 46 2649 1582 1822 255 -132 287 H ATOM 644 HG13 ILE A 46 19.521 25.675 -18.439 1.00 17.03 H ANISOU 644 HG13 ILE A 46 2442 1936 2090 122 -70 143 H ATOM 645 N SER A 47 17.921 21.503 -16.077 1.00 13.33 N ANISOU 645 N SER A 47 1913 1858 1291 95 -116 298 N ATOM 646 CA SER A 47 18.062 20.266 -15.329 1.00 13.02 C ANISOU 646 CA SER A 47 1887 1687 1373 127 -63 192 C ATOM 647 C SER A 47 19.177 19.414 -15.961 1.00 11.24 C ANISOU 647 C SER A 47 1683 1591 996 -56 -254 92 C ATOM 648 O SER A 47 19.206 19.219 -17.190 1.00 13.07 O ANISOU 648 O SER A 47 2005 1885 1072 72 -197 127 O ATOM 649 CB SER A 47 16.731 19.536 -15.352 1.00 13.81 C ANISOU 649 CB SER A 47 1749 2062 1434 138 -276 460 C ATOM 650 OG SER A 47 16.777 18.379 -14.531 1.00 13.29 O ANISOU 650 OG SER A 47 1899 1993 1158 175 -104 331 O ATOM 651 H SER A 47 17.160 21.595 -16.468 1.00 13.41 H ANISOU 651 H SER A 47 1806 1770 1516 255 -42 193 H ATOM 652 HA SER A 47 18.292 20.471 -14.400 1.00 12.05 H ANISOU 652 HA SER A 47 1795 1405 1375 210 -52 209 H ATOM 653 HB2 SER A 47 16.038 20.128 -15.020 1.00 13.46 H ANISOU 653 HB2 SER A 47 1886 1672 1557 -96 -168 188 H ATOM 654 HB3 SER A 47 16.532 19.270 -16.263 1.00 12.40 H ANISOU 654 HB3 SER A 47 1836 1416 1459 174 -184 440 H ATOM 655 N LEU A 48 20.043 18.892 -15.089 1.00 12.44 N ANISOU 655 N LEU A 48 1743 1733 1251 -2 -277 251 N ATOM 656 CA LEU A 48 21.226 18.150 -15.501 1.00 13.31 C ANISOU 656 CA LEU A 48 1650 1818 1586 0 -58 475 C ATOM 657 C LEU A 48 21.102 16.641 -15.267 1.00 13.11 C ANISOU 657 C LEU A 48 1822 1674 1482 -40 47 85 C ATOM 658 O LEU A 48 20.314 16.181 -14.431 1.00 13.54 O ANISOU 658 O LEU A 48 1718 1832 1592 22 -78 338 O ATOM 659 CB LEU A 48 22.443 18.709 -14.775 1.00 12.74 C ANISOU 659 CB LEU A 48 1605 1792 1442 24 64 345 C ATOM 660 CG LEU A 48 22.743 20.195 -15.014 1.00 12.33 C ANISOU 660 CG LEU A 48 1785 1795 1102 85 -277 349 C ATOM 661 CD1 LEU A 48 23.896 20.626 -14.101 1.00 13.08 C ANISOU 661 CD1 LEU A 48 2006 2099 863 -137 -130 31 C ATOM 662 CD2 LEU A 48 23.035 20.479 -16.432 1.00 14.10 C ANISOU 662 CD2 LEU A 48 2332 1988 1037 -237 -524 446 C ATOM 663 H LEU A 48 19.962 18.954 -14.235 1.00 11.93 H ANISOU 663 H LEU A 48 1655 1639 1237 20 -337 313 H ATOM 664 HA LEU A 48 21.367 18.272 -16.462 1.00 13.72 H ANISOU 664 HA LEU A 48 1946 1750 1516 -31 -39 177 H ATOM 665 HB2 LEU A 48 22.299 18.588 -13.824 1.00 12.61 H ANISOU 665 HB2 LEU A 48 1757 1597 1436 4 113 209 H ATOM 666 HB3 LEU A 48 23.221 18.197 -15.049 1.00 12.55 H ANISOU 666 HB3 LEU A 48 1613 1742 1411 -39 45 172 H ATOM 667 HG LEU A 48 21.965 20.715 -14.763 1.00 14.33 H ANISOU 667 HG LEU A 48 1806 1741 1896 -19 -64 196 H ATOM 668 N SER A 49 21.915 15.886 -15.997 1.00 12.45 N ANISOU 668 N SER A 49 1771 1773 1186 17 -130 165 N ATOM 669 CA SER A 49 21.809 14.424 -16.050 1.00 12.27 C ANISOU 669 CA SER A 49 1766 1764 1133 -84 -123 232 C ATOM 670 C SER A 49 22.552 13.698 -14.932 1.00 12.24 C ANISOU 670 C SER A 49 1783 1697 1168 107 -36 174 C ATOM 671 O SER A 49 23.780 13.573 -14.962 1.00 13.08 O ANISOU 671 O SER A 49 1735 1796 1437 -21 59 414 O ATOM 672 CB SER A 49 22.316 13.919 -17.389 1.00 13.13 C ANISOU 672 CB SER A 49 1990 1859 1139 -162 114 322 C ATOM 673 OG SER A 49 22.317 12.485 -17.431 1.00 13.81 O ANISOU 673 OG SER A 49 1933 1795 1516 -9 -20 343 O ATOM 674 H SER A 49 22.554 16.203 -16.478 1.00 12.56 H ANISOU 674 H SER A 49 1655 1603 1512 35 -62 98 H ATOM 675 HA SER A 49 20.863 14.175 -15.990 1.00 12.48 H ANISOU 675 HA SER A 49 1657 1694 1389 116 -16 141 H ATOM 676 HB2 SER A 49 21.737 14.253 -18.090 1.00 11.72 H ANISOU 676 HB2 SER A 49 1708 1546 1197 -68 71 -15 H ATOM 677 HB3 SER A 49 23.222 14.237 -17.528 1.00 12.86 H ANISOU 677 HB3 SER A 49 1729 1706 1450 111 -10 131 H ATOM 678 N GLU A 50 21.816 13.198 -13.942 1.00 12.89 N ANISOU 678 N GLU A 50 1590 2018 1286 63 -60 293 N ATOM 679 CA GLU A 50 22.400 12.284 -12.956 1.00 12.59 C ANISOU 679 CA GLU A 50 1552 1743 1486 -8 -110 278 C ATOM 680 C GLU A 50 22.895 10.997 -13.616 1.00 12.52 C ANISOU 680 C GLU A 50 1732 1794 1228 -71 -63 218 C ATOM 681 O GLU A 50 23.919 10.442 -13.194 1.00 13.72 O ANISOU 681 O GLU A 50 1585 1959 1669 80 3 298 O ATOM 682 CB GLU A 50 21.364 11.968 -11.877 1.00 12.51 C ANISOU 682 CB GLU A 50 1577 1755 1421 27 -93 204 C ATOM 683 CG GLU A 50 20.958 13.156 -11.054 1.00 12.60 C ANISOU 683 CG GLU A 50 1651 1693 1442 5 63 307 C ATOM 684 CD GLU A 50 19.880 13.998 -11.692 1.00 12.83 C ANISOU 684 CD GLU A 50 1718 1654 1500 -49 -80 271 C ATOM 685 OE1 GLU A 50 19.158 13.508 -12.598 1.00 13.40 O ANISOU 685 OE1 GLU A 50 1753 1790 1547 -8 -62 109 O ATOM 686 OE2 GLU A 50 19.766 15.161 -11.291 1.00 12.27 O ANISOU 686 OE2 GLU A 50 1637 1765 1258 -15 -195 171 O ATOM 687 H GLU A 50 20.980 13.359 -13.839 1.00 12.36 H ANISOU 687 H GLU A 50 1572 1680 1443 40 -102 166 H ATOM 688 HA GLU A 50 23.165 12.719 -12.524 1.00 12.20 H ANISOU 688 HA GLU A 50 1524 1707 1403 79 -94 195 H ATOM 689 HB2 GLU A 50 20.575 11.590 -12.295 1.00 12.72 H ANISOU 689 HB2 GLU A 50 1489 1790 1551 43 -65 203 H ATOM 690 HB3 GLU A 50 21.747 11.316 -11.269 1.00 12.18 H ANISOU 690 HB3 GLU A 50 1581 1652 1391 -19 -75 160 H ATOM 691 HG2 GLU A 50 20.626 12.840 -10.203 1.00 12.31 H ANISOU 691 HG2 GLU A 50 1629 1676 1370 -61 -14 237 H ATOM 692 HG3 GLU A 50 21.733 13.720 -10.913 1.00 12.35 H ANISOU 692 HG3 GLU A 50 1585 1667 1439 50 103 220 H ATOM 693 N GLN A 51 22.182 10.493 -14.610 1.00 12.26 N ANISOU 693 N GLN A 51 1740 1681 1235 51 -119 269 N ATOM 694 CA GLN A 51 22.586 9.246 -15.273 1.00 13.59 C ANISOU 694 CA GLN A 51 1811 1537 1815 -46 -12 216 C ATOM 695 C GLN A 51 23.975 9.377 -15.905 1.00 14.00 C ANISOU 695 C GLN A 51 1936 1762 1619 87 102 276 C ATOM 696 O GLN A 51 24.779 8.459 -15.853 1.00 13.83 O ANISOU 696 O GLN A 51 1959 1762 1533 166 119 52 O ATOM 697 CB GLN A 51 21.571 8.826 -16.339 1.00 13.77 C ANISOU 697 CB GLN A 51 1939 1907 1385 -69 189 131 C ATOM 698 CG GLN A 51 21.732 7.358 -16.753 1.00 14.34 C ANISOU 698 CG GLN A 51 1931 1885 1631 12 8 55 C ATOM 699 CD GLN A 51 21.368 6.387 -15.643 1.00 15.51 C ANISOU 699 CD GLN A 51 2035 1887 1970 -78 -102 269 C ATOM 700 OE1 GLN A 51 20.301 6.483 -15.031 1.00 16.40 O ANISOU 700 OE1 GLN A 51 2154 1943 2131 62 19 317 O ATOM 701 NE2 GLN A 51 22.270 5.439 -15.369 1.00 17.16 N ANISOU 701 NE2 GLN A 51 2211 1999 2307 121 -20 373 N ATOM 702 H GLN A 51 21.462 10.844 -14.922 1.00 12.40 H ANISOU 702 H GLN A 51 1521 1746 1443 -14 -49 167 H ATOM 703 HA GLN A 51 22.633 8.539 -14.597 1.00 13.31 H ANISOU 703 HA GLN A 51 1860 1598 1597 -46 37 134 H ATOM 704 HB2 GLN A 51 20.676 8.938 -15.986 1.00 13.59 H ANISOU 704 HB2 GLN A 51 1782 1792 1587 -59 45 159 H ATOM 705 HB3 GLN A 51 21.688 9.377 -17.128 1.00 14.52 H ANISOU 705 HB3 GLN A 51 2092 1874 1550 -148 126 214 H ATOM 706 HG2 GLN A 51 21.147 7.180 -17.506 1.00 14.32 H ANISOU 706 HG2 GLN A 51 1811 1870 1759 -11 -11 48 H ATOM 707 HG3 GLN A 51 22.653 7.198 -17.008 1.00 14.77 H ANISOU 707 HG3 GLN A 51 1844 1869 1897 6 -67 91 H ATOM 708 N ASN A 52 24.259 10.527 -16.504 1.00 13.96 N ANISOU 708 N ASN A 52 1933 1760 1611 143 96 340 N ATOM 709 CA ASN A 52 25.595 10.830 -17.044 1.00 13.95 C ANISOU 709 CA ASN A 52 1795 1729 1775 221 80 291 C ATOM 710 C ASN A 52 26.653 10.681 -15.943 1.00 14.56 C ANISOU 710 C ASN A 52 1941 2069 1520 105 173 496 C ATOM 711 O ASN A 52 27.703 10.074 -16.165 1.00 14.19 O ANISOU 711 O ASN A 52 1939 1953 1500 147 5 419 O ATOM 712 CB ASN A 52 25.522 12.256 -17.598 1.00 13.54 C ANISOU 712 CB ASN A 52 1790 1685 1668 66 -41 265 C ATOM 713 CG ASN A 52 26.716 12.712 -18.434 1.00 14.95 C ANISOU 713 CG ASN A 52 2033 1953 1695 94 134 453 C ATOM 714 OD1 ASN A 52 26.599 13.740 -19.133 1.00 15.17 O ANISOU 714 OD1 ASN A 52 1962 2101 1701 55 111 575 O ATOM 715 ND2 ASN A 52 27.855 12.043 -18.327 1.00 15.11 N ANISOU 715 ND2 ASN A 52 2015 2210 1513 177 40 399 N ATOM 716 H ASN A 52 23.686 11.158 -16.614 1.00 13.06 H ANISOU 716 H ASN A 52 1705 1650 1607 7 9 141 H ATOM 717 HA ASN A 52 25.811 10.214 -17.773 1.00 13.93 H ANISOU 717 HA ASN A 52 1756 1693 1844 32 75 199 H ATOM 718 HB2 ASN A 52 24.743 12.325 -18.171 1.00 13.76 H ANISOU 718 HB2 ASN A 52 1875 1686 1666 203 -89 153 H ATOM 719 HB3 ASN A 52 25.436 12.873 -16.855 1.00 13.48 H ANISOU 719 HB3 ASN A 52 1611 1725 1782 1 -35 150 H ATOM 720 N LEU A 53 26.373 11.198 -14.751 1.00 13.18 N ANISOU 720 N LEU A 53 1600 1778 1627 58 59 412 N ATOM 721 CA LEU A 53 27.320 11.038 -13.646 1.00 14.23 C ANISOU 721 CA LEU A 53 1571 1975 1860 -23 -75 362 C ATOM 722 C LEU A 53 27.439 9.575 -13.206 1.00 14.82 C ANISOU 722 C LEU A 53 1611 1937 2082 101 94 395 C ATOM 723 O LEU A 53 28.531 9.055 -12.979 1.00 15.48 O ANISOU 723 O LEU A 53 1617 2082 2181 123 -1 377 O ATOM 724 CB LEU A 53 26.918 11.911 -12.459 1.00 14.18 C ANISOU 724 CB LEU A 53 1746 1883 1755 21 -91 441 C ATOM 725 CG LEU A 53 26.990 13.425 -12.673 1.00 14.19 C ANISOU 725 CG LEU A 53 1729 1883 1778 -78 -181 343 C ATOM 726 CD1 LEU A 53 26.469 14.137 -11.447 1.00 14.34 C ANISOU 726 CD1 LEU A 53 1983 1669 1795 0 -106 412 C ATOM 727 CD2 LEU A 53 28.432 13.865 -12.992 1.00 16.71 C ANISOU 727 CD2 LEU A 53 1788 2058 2501 -67 82 498 C ATOM 728 H LEU A 53 25.660 11.639 -14.558 1.00 13.50 H ANISOU 728 H LEU A 53 1566 1762 1800 32 -26 258 H ATOM 729 HA LEU A 53 28.209 11.319 -13.947 1.00 14.52 H ANISOU 729 HA LEU A 53 1610 1903 2003 -66 -25 243 H ATOM 730 HB2 LEU A 53 26.003 11.691 -12.224 1.00 13.75 H ANISOU 730 HB2 LEU A 53 1686 1728 1808 20 -154 222 H ATOM 731 HB3 LEU A 53 27.498 11.689 -11.713 1.00 14.03 H ANISOU 731 HB3 LEU A 53 1608 1929 1791 112 -56 338 H ATOM 732 HG LEU A 53 26.427 13.667 -13.424 1.00 14.28 H ANISOU 732 HG LEU A 53 1818 1832 1772 227 -109 309 H ATOM 733 N VAL A 54 26.307 8.901 -13.076 1.00 13.63 N ANISOU 733 N VAL A 54 1574 1958 1645 151 195 377 N ATOM 734 CA VAL A 54 26.289 7.515 -12.628 1.00 14.92 C ANISOU 734 CA VAL A 54 1930 1870 1867 96 38 278 C ATOM 735 C VAL A 54 27.116 6.638 -13.578 1.00 15.54 C ANISOU 735 C VAL A 54 1920 2031 1954 138 103 276 C ATOM 736 O VAL A 54 27.916 5.811 -13.134 1.00 17.79 O ANISOU 736 O VAL A 54 2116 2184 2458 435 299 589 O ATOM 737 CB VAL A 54 24.825 7.010 -12.500 1.00 13.73 C ANISOU 737 CB VAL A 54 2036 1930 1250 -77 -120 584 C ATOM 738 CG1 VAL A 54 24.769 5.477 -12.435 1.00 18.18 C ANISOU 738 CG1 VAL A 54 2244 1848 2815 125 43 728 C ATOM 739 CG2 VAL A 54 24.154 7.638 -11.271 1.00 15.64 C ANISOU 739 CG2 VAL A 54 2041 2336 1563 -109 98 325 C ATOM 740 H VAL A 54 25.532 9.231 -13.249 1.00 13.57 H ANISOU 740 H VAL A 54 1602 1880 1674 95 -1 183 H ATOM 741 HA VAL A 54 26.711 7.464 -11.744 1.00 14.17 H ANISOU 741 HA VAL A 54 1811 1683 1887 42 45 332 H ATOM 742 HB VAL A 54 24.321 7.290 -13.292 1.00 14.28 H ANISOU 742 HB VAL A 54 1960 1955 1508 459 -224 316 H ATOM 743 N ASP A 55 26.909 6.802 -14.876 1.00 15.92 N ANISOU 743 N ASP A 55 2041 2111 1894 194 152 223 N ATOM 744 CA ASP A 55 27.514 5.946 -15.904 1.00 16.06 C ANISOU 744 CA ASP A 55 2177 2000 1923 56 113 110 C ATOM 745 C ASP A 55 28.984 6.254 -16.176 1.00 16.65 C ANISOU 745 C ASP A 55 2237 2044 2043 105 369 255 C ATOM 746 O ASP A 55 29.720 5.375 -16.622 1.00 18.70 O ANISOU 746 O ASP A 55 2322 2056 2725 239 470 316 O ATOM 747 CB ASP A 55 26.773 6.077 -17.243 1.00 16.02 C ANISOU 747 CB ASP A 55 2216 2113 1757 168 335 128 C ATOM 748 CG ASP A 55 25.315 5.605 -17.196 1.00 16.56 C ANISOU 748 CG ASP A 55 2191 2335 1764 106 -24 247 C ATOM 749 OD1 ASP A 55 24.913 4.895 -16.241 1.00 18.51 O ANISOU 749 OD1 ASP A 55 2361 2242 2427 103 351 411 O ATOM 750 OD2 ASP A 55 24.594 5.957 -18.170 1.00 16.99 O ANISOU 750 OD2 ASP A 55 2304 2059 2089 286 -61 241 O ATOM 751 H ASP A 55 26.407 7.419 -15.202 1.00 15.17 H ANISOU 751 H ASP A 55 1958 1947 1858 25 51 172 H ATOM 752 HA ASP A 55 27.455 5.011 -15.616 1.00 16.03 H ANISOU 752 HA ASP A 55 2093 2012 1983 37 76 142 H ATOM 753 HB2 ASP A 55 26.778 7.007 -17.516 1.00 16.18 H ANISOU 753 HB2 ASP A 55 2201 2011 1933 203 46 6 H ATOM 754 HB3 ASP A 55 27.230 5.535 -17.904 1.00 16.46 H ANISOU 754 HB3 ASP A 55 2285 2041 1927 205 166 -58 H ATOM 755 N CYS A 56 29.397 7.504 -15.978 1.00 15.75 N ANISOU 755 N CYS A 56 1953 1911 2120 253 286 347 N ATOM 756 CA CYS A 56 30.637 7.989 -16.578 1.00 16.35 C ANISOU 756 CA CYS A 56 2097 2015 2098 219 409 247 C ATOM 757 C CYS A 56 31.709 8.439 -15.599 1.00 16.58 C ANISOU 757 C CYS A 56 2063 1979 2254 222 334 247 C ATOM 758 O CYS A 56 32.851 8.612 -16.013 1.00 18.86 O ANISOU 758 O CYS A 56 2022 2682 2460 277 341 653 O ATOM 759 CB CYS A 56 30.329 9.157 -17.533 1.00 16.92 C ANISOU 759 CB CYS A 56 2692 2251 1486 205 592 244 C ATOM 760 SG CYS A 56 29.134 8.799 -18.816 1.00 18.03 S ANISOU 760 SG CYS A 56 2568 2263 2017 246 135 478 S ATOM 761 H CYS A 56 28.981 8.092 -15.509 1.00 15.52 H ANISOU 761 H CYS A 56 1851 2111 1932 127 169 142 H ATOM 762 HA CYS A 56 31.035 7.279 -17.123 1.00 17.07 H ANISOU 762 HA CYS A 56 2064 2182 2239 181 390 72 H ATOM 763 HB2 CYS A 56 30.001 9.906 -17.015 1.00 16.92 H ANISOU 763 HB2 CYS A 56 2212 1975 2239 244 332 175 H ATOM 764 HB3 CYS A 56 31.154 9.411 -17.975 1.00 16.76 H ANISOU 764 HB3 CYS A 56 2315 2057 1996 199 351 239 H ATOM 765 N SER A 57 31.387 8.630 -14.317 1.00 16.08 N ANISOU 765 N SER A 57 1923 1943 2243 233 202 148 N ATOM 766 CA SER A 57 32.359 9.197 -13.380 1.00 15.94 C ANISOU 766 CA SER A 57 2051 2158 1848 38 164 498 C ATOM 767 C SER A 57 33.087 8.172 -12.505 1.00 16.76 C ANISOU 767 C SER A 57 1819 2246 2302 261 203 418 C ATOM 768 O SER A 57 33.659 8.513 -11.485 1.00 16.40 O ANISOU 768 O SER A 57 1839 2307 2083 353 224 589 O ATOM 769 CB SER A 57 31.765 10.331 -12.528 1.00 15.73 C ANISOU 769 CB SER A 57 1784 2107 2083 -25 59 349 C ATOM 770 OG SER A 57 30.712 9.899 -11.675 1.00 15.90 O ANISOU 770 OG SER A 57 1765 2174 2100 290 117 638 O ATOM 771 H SER A 57 30.627 8.444 -13.962 1.00 15.97 H ANISOU 771 H SER A 57 1965 2123 1980 167 114 228 H ATOM 772 HA SER A 57 33.058 9.628 -13.912 1.00 16.63 H ANISOU 772 HA SER A 57 2026 2255 2034 -73 228 315 H ATOM 773 HB2 SER A 57 32.467 10.718 -11.983 1.00 16.41 H ANISOU 773 HB2 SER A 57 1870 2304 2061 26 -32 297 H ATOM 774 HB3 SER A 57 31.413 11.009 -13.126 1.00 14.93 H ANISOU 774 HB3 SER A 57 1941 2011 1719 -134 57 205 H ATOM 775 N GLY A 58 33.119 6.928 -12.958 1.00 16.93 N ANISOU 775 N GLY A 58 2028 2188 2216 250 319 536 N ATOM 776 CA GLY A 58 33.955 5.911 -12.340 1.00 18.18 C ANISOU 776 CA GLY A 58 2200 2116 2590 431 332 467 C ATOM 777 C GLY A 58 35.427 6.299 -12.264 1.00 18.95 C ANISOU 777 C GLY A 58 2224 2453 2520 545 246 566 C ATOM 778 O GLY A 58 36.047 6.104 -11.216 1.00 19.28 O ANISOU 778 O GLY A 58 2109 2412 2804 294 48 655 O ATOM 779 H GLY A 58 32.665 6.635 -13.626 1.00 18.39 H ANISOU 779 H GLY A 58 2252 2294 2440 277 177 289 H ATOM 780 HA2 GLY A 58 33.883 5.086 -12.846 1.00 18.76 H ANISOU 780 HA2 GLY A 58 2471 2301 2357 481 286 334 H ATOM 781 HA3 GLY A 58 33.639 5.744 -11.441 1.00 16.74 H ANISOU 781 HA3 GLY A 58 2122 1974 2261 224 -101 298 H ATOM 782 N PRO A 59 36.002 6.833 -13.375 1.00 18.11 N ANISOU 782 N PRO A 59 1910 2427 2542 262 252 292 N ATOM 783 CA PRO A 59 37.430 7.138 -13.332 1.00 19.79 C ANISOU 783 CA PRO A 59 1944 2556 3018 397 132 262 C ATOM 784 C PRO A 59 37.807 8.083 -12.192 1.00 18.44 C ANISOU 784 C PRO A 59 1790 2588 2628 263 192 330 C ATOM 785 O PRO A 59 38.912 7.997 -11.625 1.00 21.87 O ANISOU 785 O PRO A 59 2160 2963 3186 291 -217 643 O ATOM 786 CB PRO A 59 37.658 7.771 -14.695 1.00 20.10 C ANISOU 786 CB PRO A 59 2368 2601 2665 237 449 -52 C ATOM 787 CG PRO A 59 36.746 6.983 -15.596 1.00 21.04 C ANISOU 787 CG PRO A 59 2244 3056 2692 308 571 -197 C ATOM 788 CD PRO A 59 35.491 6.893 -14.757 1.00 19.23 C ANISOU 788 CD PRO A 59 2136 2763 2405 461 418 213 C ATOM 789 HA PRO A 59 37.955 6.313 -13.262 1.00 20.14 H ANISOU 789 HA PRO A 59 1913 2387 3352 245 99 151 H ATOM 790 HB2 PRO A 59 37.397 8.705 -14.675 1.00 20.38 H ANISOU 790 HB2 PRO A 59 2315 2589 2838 234 296 216 H ATOM 791 HB3 PRO A 59 38.582 7.677 -14.955 1.00 21.07 H ANISOU 791 HB3 PRO A 59 2315 2853 2835 290 311 -58 H ATOM 792 HG2 PRO A 59 36.586 7.468 -16.420 1.00 19.00 H ANISOU 792 HG2 PRO A 59 1973 2514 2730 -37 572 -176 H ATOM 793 HG3 PRO A 59 37.120 6.105 -15.768 1.00 18.82 H ANISOU 793 HG3 PRO A 59 1938 2761 2449 15 477 -11 H ATOM 794 HD2 PRO A 59 34.948 7.686 -14.877 1.00 17.66 H ANISOU 794 HD2 PRO A 59 1936 2495 2276 174 251 161 H ATOM 795 HD3 PRO A 59 34.997 6.086 -14.974 1.00 18.66 H ANISOU 795 HD3 PRO A 59 2312 2556 2222 471 283 304 H ATOM 796 N GLN A 60 36.881 8.985 -11.843 1.00 18.37 N ANISOU 796 N GLN A 60 1992 2257 2730 136 152 203 N ATOM 797 CA GLN A 60 37.098 9.948 -10.776 1.00 16.42 C ANISOU 797 CA GLN A 60 1652 2439 2146 238 -123 388 C ATOM 798 C GLN A 60 36.915 9.386 -9.368 1.00 18.12 C ANISOU 798 C GLN A 60 1878 2721 2285 34 -225 423 C ATOM 799 O GLN A 60 37.255 10.028 -8.366 1.00 18.94 O ANISOU 799 O GLN A 60 2392 2485 2319 105 -480 473 O ATOM 800 CB GLN A 60 36.172 11.155 -10.945 1.00 16.97 C ANISOU 800 CB GLN A 60 1969 2311 2166 200 -208 423 C ATOM 801 CG GLN A 60 36.540 12.028 -12.139 1.00 17.21 C ANISOU 801 CG GLN A 60 1855 2156 2527 216 42 536 C ATOM 802 CD GLN A 60 36.217 11.429 -13.488 1.00 18.26 C ANISOU 802 CD GLN A 60 2019 2279 2639 325 97 249 C ATOM 803 OE1 GLN A 60 35.341 10.579 -13.608 1.00 19.19 O ANISOU 803 OE1 GLN A 60 2207 2296 2789 172 -109 318 O ATOM 804 NE2 GLN A 60 36.922 11.882 -14.515 1.00 20.55 N ANISOU 804 NE2 GLN A 60 2021 3058 2726 223 121 502 N ATOM 805 H GLN A 60 36.109 9.051 -12.214 1.00 16.36 H ANISOU 805 H GLN A 60 2068 1876 2269 263 155 30 H ATOM 806 HA GLN A 60 38.017 10.282 -10.838 1.00 18.15 H ANISOU 806 HA GLN A 60 1778 2540 2575 76 23 299 H ATOM 807 HB2 GLN A 60 35.259 10.847 -11.058 1.00 15.15 H ANISOU 807 HB2 GLN A 60 1888 1793 2074 325 -23 312 H ATOM 808 HB3 GLN A 60 36.231 11.711 -10.152 1.00 17.57 H ANISOU 808 HB3 GLN A 60 2050 2251 2372 93 -175 271 H ATOM 809 HG2 GLN A 60 36.057 12.865 -12.068 1.00 17.27 H ANISOU 809 HG2 GLN A 60 2026 2019 2515 114 2 348 H ATOM 810 HG3 GLN A 60 37.494 12.200 -12.114 1.00 18.77 H ANISOU 810 HG3 GLN A 60 1914 2425 2792 76 105 262 H ATOM 811 N GLY A 61 36.372 8.176 -9.278 1.00 16.95 N ANISOU 811 N GLY A 61 1830 2334 2276 141 -277 375 N ATOM 812 CA GLY A 61 36.171 7.502 -7.995 1.00 18.43 C ANISOU 812 CA GLY A 61 1966 2864 2170 185 -151 380 C ATOM 813 C GLY A 61 34.730 7.169 -7.640 1.00 16.36 C ANISOU 813 C GLY A 61 2080 2386 1749 -12 -196 237 C ATOM 814 O GLY A 61 34.471 6.609 -6.566 1.00 19.34 O ANISOU 814 O GLY A 61 2154 2715 2480 301 -63 1006 O ATOM 815 H GLY A 61 36.099 7.712 -9.946 1.00 17.69 H ANISOU 815 H GLY A 61 2045 2553 2124 255 -39 180 H ATOM 816 HA2 GLY A 61 36.531 8.042 -7.275 1.00 16.89 H ANISOU 816 HA2 GLY A 61 1833 2351 2233 142 40 385 H ATOM 817 HA3 GLY A 61 36.666 6.667 -8.009 1.00 16.65 H ANISOU 817 HA3 GLY A 61 2060 2392 1873 -155 -50 344 H ATOM 818 N ASN A 62 33.768 7.547 -8.465 1.00 16.37 N ANISOU 818 N ASN A 62 1867 1885 2465 158 15 762 N ATOM 819 CA ASN A 62 32.384 7.223 -8.116 1.00 15.12 C ANISOU 819 CA ASN A 62 1890 1924 1928 69 -46 686 C ATOM 820 C ASN A 62 32.064 5.775 -8.449 1.00 15.64 C ANISOU 820 C ASN A 62 2252 1932 1755 -20 276 569 C ATOM 821 O ASN A 62 32.764 5.118 -9.234 1.00 17.40 O ANISOU 821 O ASN A 62 2234 2029 2348 86 384 603 O ATOM 822 CB ASN A 62 31.414 8.210 -8.749 1.00 14.36 C ANISOU 822 CB ASN A 62 1776 1999 1681 160 32 534 C ATOM 823 CG ASN A 62 31.527 9.568 -8.125 1.00 15.58 C ANISOU 823 CG ASN A 62 1873 1980 2064 -11 -56 473 C ATOM 824 OD1 ASN A 62 31.754 9.705 -6.944 1.00 15.93 O ANISOU 824 OD1 ASN A 62 1934 1983 2135 -6 -107 462 O ATOM 825 ND2 ASN A 62 31.412 10.607 -8.956 1.00 15.38 N ANISOU 825 ND2 ASN A 62 1736 2045 2063 -76 -67 601 N ATOM 826 H ASN A 62 33.872 7.974 -9.204 1.00 14.16 H ANISOU 826 H ASN A 62 1661 1904 1812 54 -25 196 H ATOM 827 HA ASN A 62 32.273 7.308 -7.146 1.00 15.08 H ANISOU 827 HA ASN A 62 1846 1970 1912 215 -175 488 H ATOM 828 HB2 ASN A 62 31.608 8.287 -9.696 1.00 14.90 H ANISOU 828 HB2 ASN A 62 1781 2217 1663 141 -32 536 H ATOM 829 HB3 ASN A 62 30.506 7.893 -8.618 1.00 14.39 H ANISOU 829 HB3 ASN A 62 1791 1982 1693 89 27 299 H ATOM 830 N GLU A 63 30.984 5.288 -7.837 1.00 16.01 N ANISOU 830 N GLU A 63 1801 1816 2465 148 165 730 N ATOM 831 CA GLU A 63 30.654 3.855 -7.884 1.00 14.80 C ANISOU 831 CA GLU A 63 2024 1965 1632 -54 360 575 C ATOM 832 C GLU A 63 29.227 3.621 -8.379 1.00 15.03 C ANISOU 832 C GLU A 63 2024 1862 1825 107 275 583 C ATOM 833 O GLU A 63 28.532 2.697 -7.935 1.00 14.76 O ANISOU 833 O GLU A 63 2061 1764 1783 17 210 512 O ATOM 834 CB GLU A 63 30.896 3.199 -6.523 1.00 14.18 C ANISOU 834 CB GLU A 63 2056 1860 1472 132 191 278 C ATOM 835 CG GLU A 63 32.285 3.396 -6.010 1.00 16.59 C ANISOU 835 CG GLU A 63 2255 2048 1999 226 -102 315 C ATOM 836 CD GLU A 63 32.462 2.662 -4.704 1.00 20.37 C ANISOU 836 CD GLU A 63 3148 2994 1597 189 -756 92 C ATOM 837 OE1 GLU A 63 31.770 2.973 -3.703 1.00 24.66 O ANISOU 837 OE1 GLU A 63 3641 3420 2309 -46 75 373 O ATOM 838 OE2 GLU A 63 33.253 1.740 -4.690 1.00 24.35 O ANISOU 838 OE2 GLU A 63 4165 2633 2453 442 -824 399 O ATOM 839 H GLU A 63 30.424 5.762 -7.388 1.00 15.56 H ANISOU 839 H GLU A 63 1906 2004 2002 -92 87 368 H ATOM 840 HA GLU A 63 31.247 3.407 -8.522 1.00 14.68 H ANISOU 840 HA GLU A 63 1968 2047 1560 -99 260 451 H ATOM 841 HB2 GLU A 63 30.280 3.573 -5.875 1.00 14.84 H ANISOU 841 HB2 GLU A 63 2227 1939 1472 90 239 190 H ATOM 842 HB3 GLU A 63 30.746 2.244 -6.605 1.00 14.56 H ANISOU 842 HB3 GLU A 63 2293 1808 1431 205 107 351 H ATOM 843 HG2 GLU A 63 32.921 3.046 -6.654 1.00 16.41 H ANISOU 843 HG2 GLU A 63 2020 2103 2113 -32 -70 153 H ATOM 844 HG3 GLU A 63 32.445 4.339 -5.852 1.00 18.45 H ANISOU 844 HG3 GLU A 63 2257 2239 2512 9 -34 -89 H ATOM 845 N GLY A 64 28.773 4.480 -9.276 1.00 15.34 N ANISOU 845 N GLY A 64 2110 1820 1896 -52 45 588 N ATOM 846 CA GLY A 64 27.490 4.253 -9.938 1.00 15.17 C ANISOU 846 CA GLY A 64 2102 1768 1893 47 83 439 C ATOM 847 C GLY A 64 26.316 4.274 -8.970 1.00 15.13 C ANISOU 847 C GLY A 64 2051 2040 1658 154 -8 251 C ATOM 848 O GLY A 64 26.191 5.178 -8.123 1.00 14.93 O ANISOU 848 O GLY A 64 2015 1827 1830 -65 168 390 O ATOM 849 H GLY A 64 29.177 5.196 -9.528 1.00 14.10 H ANISOU 849 H GLY A 64 2147 1616 1592 26 157 322 H ATOM 850 HA2 GLY A 64 27.512 3.394 -10.388 1.00 15.08 H ANISOU 850 HA2 GLY A 64 1976 1834 1917 158 118 338 H ATOM 851 HA3 GLY A 64 27.347 4.943 -10.604 1.00 14.95 H ANISOU 851 HA3 GLY A 64 2291 1778 1610 133 18 260 H ATOM 852 N CYS A 65 25.455 3.252 -9.083 1.00 13.60 N ANISOU 852 N CYS A 65 2264 2231 671 55 69 254 N ATOM 853 CA CYS A 65 24.340 3.079 -8.154 1.00 13.93 C ANISOU 853 CA CYS A 65 2177 1776 1337 205 288 338 C ATOM 854 C CYS A 65 24.757 2.552 -6.780 1.00 14.10 C ANISOU 854 C CYS A 65 1948 1876 1532 -23 103 492 C ATOM 855 O CYS A 65 23.908 2.282 -5.951 1.00 13.96 O ANISOU 855 O CYS A 65 1975 1942 1387 116 12 527 O ATOM 856 CB CYS A 65 23.299 2.133 -8.770 1.00 15.76 C ANISOU 856 CB CYS A 65 2201 1971 1813 168 17 382 C ATOM 857 SG CYS A 65 22.359 2.859 -10.134 1.00 15.51 S ANISOU 857 SG CYS A 65 2252 2024 1615 -15 -80 244 S ATOM 858 H CYS A 65 25.502 2.648 -9.694 1.00 14.31 H ANISOU 858 H CYS A 65 2026 1889 1518 329 202 42 H ATOM 859 HA CYS A 65 23.909 3.947 -8.013 1.00 14.55 H ANISOU 859 HA CYS A 65 1956 1812 1760 231 127 399 H ATOM 860 HB2 CYS A 65 23.748 1.341 -9.106 1.00 15.32 H ANISOU 860 HB2 CYS A 65 1992 1978 1849 6 55 232 H ATOM 861 HB3 CYS A 65 22.657 1.877 -8.089 1.00 14.95 H ANISOU 861 HB3 CYS A 65 2026 1988 1667 173 -84 253 H ATOM 862 N ASN A 66 26.061 2.417 -6.552 1.00 13.50 N ANISOU 862 N ASN A 66 1916 1631 1582 30 19 378 N ATOM 863 CA ASN A 66 26.526 1.961 -5.253 1.00 13.91 C ANISOU 863 CA ASN A 66 1837 1820 1628 90 -11 448 C ATOM 864 C ASN A 66 26.999 3.054 -4.305 1.00 14.04 C ANISOU 864 C ASN A 66 1909 1860 1564 29 -222 498 C ATOM 865 O ASN A 66 27.278 2.784 -3.162 1.00 19.13 O ANISOU 865 O ASN A 66 3152 2359 1755 -335 -678 677 O ATOM 866 CB ASN A 66 27.646 0.934 -5.408 1.00 15.72 C ANISOU 866 CB ASN A 66 1992 2000 1981 246 134 516 C ATOM 867 CG ASN A 66 27.237 -0.223 -6.248 1.00 16.12 C ANISOU 867 CG ASN A 66 2263 1869 1989 390 306 447 C ATOM 868 OD1 ASN A 66 27.806 -0.501 -7.333 1.00 20.48 O ANISOU 868 OD1 ASN A 66 3116 2678 1986 650 479 357 O ATOM 869 ND2 ASN A 66 26.211 -0.890 -5.798 1.00 15.99 N ANISOU 869 ND2 ASN A 66 2628 1610 1837 7 116 519 N ATOM 870 H ASN A 66 26.691 2.567 -7.113 1.00 13.75 H ANISOU 870 H ASN A 66 1875 1823 1523 36 0 279 H ATOM 871 HA ASN A 66 25.788 1.505 -4.804 1.00 13.60 H ANISOU 871 HA ASN A 66 1852 1837 1479 44 -29 350 H ATOM 872 HB2 ASN A 66 28.420 1.353 -5.814 1.00 16.09 H ANISOU 872 HB2 ASN A 66 1901 2410 1801 170 117 344 H ATOM 873 HB3 ASN A 66 27.875 0.592 -4.531 1.00 15.68 H ANISOU 873 HB3 ASN A 66 1992 1956 2009 323 97 484 H ATOM 874 N GLY A 67 27.122 4.276 -4.809 1.00 14.53 N ANISOU 874 N GLY A 67 1886 1824 1810 103 -56 544 N ATOM 875 CA GLY A 67 27.563 5.402 -4.005 1.00 14.35 C ANISOU 875 CA GLY A 67 1827 1832 1790 162 129 439 C ATOM 876 C GLY A 67 28.644 6.219 -4.700 1.00 13.32 C ANISOU 876 C GLY A 67 1762 1618 1679 218 24 399 C ATOM 877 O GLY A 67 29.111 5.892 -5.794 1.00 14.82 O ANISOU 877 O GLY A 67 1928 1991 1709 118 131 459 O ATOM 878 H GLY A 67 26.955 4.486 -5.625 1.00 13.72 H ANISOU 878 H GLY A 67 1916 1596 1698 242 154 415 H ATOM 879 HA2 GLY A 67 27.917 5.099 -3.155 1.00 14.16 H ANISOU 879 HA2 GLY A 67 1863 1809 1708 122 148 370 H ATOM 880 HA3 GLY A 67 26.807 5.985 -3.830 1.00 15.09 H ANISOU 880 HA3 GLY A 67 1644 1933 2155 87 21 308 H ATOM 881 N GLY A 68 28.994 7.329 -4.059 1.00 14.03 N ANISOU 881 N GLY A 68 1824 1933 1574 38 -285 400 N ATOM 882 CA GLY A 68 29.911 8.258 -4.675 1.00 14.53 C ANISOU 882 CA GLY A 68 1732 1898 1888 93 -173 354 C ATOM 883 C GLY A 68 30.024 9.524 -3.876 1.00 14.83 C ANISOU 883 C GLY A 68 1703 1981 1951 -2 -239 271 C ATOM 884 O GLY A 68 29.402 9.674 -2.825 1.00 14.57 O ANISOU 884 O GLY A 68 1904 1851 1781 89 -286 561 O ATOM 885 H GLY A 68 28.714 7.556 -3.278 1.00 14.52 H ANISOU 885 H GLY A 68 1772 1905 1839 37 -104 180 H ATOM 886 HA2 GLY A 68 29.602 8.485 -5.567 1.00 14.05 H ANISOU 886 HA2 GLY A 68 1720 1905 1713 92 37 312 H ATOM 887 HA3 GLY A 68 30.790 7.854 -4.744 1.00 15.42 H ANISOU 887 HA3 GLY A 68 1717 2085 2055 98 -173 208 H ATOM 888 N ALEU A 69 30.861 10.427 -4.371 0.70 15.07 N ANISOU 888 N ALEU A 69 1834 1889 2001 217 -15 508 N ATOM 889 CA ALEU A 69 31.146 11.692 -3.722 0.70 15.46 C ANISOU 889 CA ALEU A 69 2093 1994 1785 142 -313 434 C ATOM 890 C ALEU A 69 30.846 12.863 -4.669 0.70 13.80 C ANISOU 890 C ALEU A 69 1800 1813 1628 -12 -69 353 C ATOM 891 O ALEU A 69 31.185 12.845 -5.850 0.70 14.66 O ANISOU 891 O ALEU A 69 1889 1925 1756 -31 -23 521 O ATOM 892 CB ALEU A 69 32.618 11.789 -3.306 0.70 17.69 C ANISOU 892 CB ALEU A 69 1942 2302 2476 17 -74 524 C ATOM 893 CG ALEU A 69 33.241 10.737 -2.378 0.70 17.25 C ANISOU 893 CG ALEU A 69 2415 2592 1547 240 -300 68 C ATOM 894 CD1ALEU A 69 34.673 11.148 -2.029 0.70 23.15 C ANISOU 894 CD1ALEU A 69 2201 3474 3120 297 -411 194 C ATOM 895 CD2ALEU A 69 32.468 10.554 -1.073 0.70 16.99 C ANISOU 895 CD2ALEU A 69 2251 3006 1197 99 -584 76 C ATOM 896 H ALEU A 69 31.291 10.323 -5.109 0.70 15.76 H ANISOU 896 H ALEU A 69 1892 2146 1948 40 -72 261 H ATOM 897 HA ALEU A 69 30.589 11.796 -2.923 0.70 14.61 H ANISOU 897 HA ALEU A 69 1919 1778 1854 -81 -239 519 H ATOM 898 HB2ALEU A 69 33.143 11.780 -4.122 0.70 16.53 H ANISOU 898 HB2ALEU A 69 2119 2009 2151 42 -238 354 H ATOM 899 HB3ALEU A 69 32.733 12.651 -2.874 0.70 17.21 H ANISOU 899 HB3ALEU A 69 1817 2564 2155 51 -103 266 H ATOM 900 HG ALEU A 69 33.272 9.883 -2.836 0.70 17.94 H ANISOU 900 HG ALEU A 69 2417 2325 2073 397 234 200 H ATOM 901 N BLEU A 69 30.848 10.432 -4.384 0.30 14.50 N ANISOU 901 N BLEU A 69 1783 1845 1881 162 -38 275 N ATOM 902 CA BLEU A 69 31.146 11.688 -3.726 0.30 14.35 C ANISOU 902 CA BLEU A 69 1845 1888 1718 146 -146 260 C ATOM 903 C BLEU A 69 30.836 12.848 -4.666 0.30 14.05 C ANISOU 903 C BLEU A 69 1824 1835 1679 -28 -125 277 C ATOM 904 O BLEU A 69 31.154 12.801 -5.853 0.30 15.42 O ANISOU 904 O BLEU A 69 1981 2098 1779 -67 9 436 O ATOM 905 CB BLEU A 69 32.621 11.743 -3.333 0.30 14.58 C ANISOU 905 CB BLEU A 69 1748 1916 1875 56 63 329 C ATOM 906 CG BLEU A 69 33.046 10.869 -2.151 0.30 15.90 C ANISOU 906 CG BLEU A 69 2040 2070 1929 336 -218 209 C ATOM 907 CD1BLEU A 69 32.311 11.280 -0.885 0.30 13.47 C ANISOU 907 CD1BLEU A 69 1931 1491 1694 441 -320 629 C ATOM 908 CD2BLEU A 69 32.850 9.387 -2.427 0.30 17.46 C ANISOU 908 CD2BLEU A 69 2478 1964 2191 412 -304 364 C ATOM 909 H BLEU A 69 31.259 10.337 -5.134 0.30 15.00 H ANISOU 909 H BLEU A 69 1859 1998 1842 65 -70 127 H ATOM 910 HA BLEU A 69 30.607 11.788 -2.913 0.30 13.78 H ANISOU 910 HA BLEU A 69 1695 1755 1786 -18 -100 314 H ATOM 911 HB2BLEU A 69 33.149 11.468 -4.099 0.30 14.97 H ANISOU 911 HB2BLEU A 69 1859 1969 1860 40 -39 52 H ATOM 912 HB3BLEU A 69 32.840 12.660 -3.106 0.30 14.58 H ANISOU 912 HB3BLEU A 69 1760 1955 1823 146 10 130 H ATOM 913 HG BLEU A 69 33.993 11.010 -1.994 0.30 16.68 H ANISOU 913 HG BLEU A 69 2000 2311 2026 270 -100 273 H ATOM 914 N MET A 70 30.207 13.887 -4.130 1.00 14.91 N ANISOU 914 N MET A 70 1892 1769 2002 -16 -205 294 N ATOM 915 CA MET A 70 29.887 15.057 -4.932 1.00 14.06 C ANISOU 915 CA MET A 70 1784 1776 1783 -15 -229 244 C ATOM 916 C MET A 70 31.125 15.723 -5.539 1.00 15.31 C ANISOU 916 C MET A 70 1802 2241 1772 -96 -96 39 C ATOM 917 O MET A 70 31.109 16.080 -6.720 1.00 15.13 O ANISOU 917 O MET A 70 1739 1971 2036 -39 -165 381 O ATOM 918 CB MET A 70 29.087 16.054 -4.107 1.00 13.13 C ANISOU 918 CB MET A 70 1897 1826 1263 -142 -175 292 C ATOM 919 CG MET A 70 27.663 15.586 -3.705 1.00 13.53 C ANISOU 919 CG MET A 70 1800 1780 1559 -100 -234 210 C ATOM 920 SD MET A 70 27.559 14.406 -2.347 1.00 14.08 S ANISOU 920 SD MET A 70 1827 1823 1698 -54 -285 410 S ATOM 921 CE MET A 70 27.505 15.490 -0.969 1.00 15.06 C ANISOU 921 CE MET A 70 1934 2091 1696 120 -66 556 C ATOM 922 H MET A 70 29.955 13.934 -3.309 1.00 13.90 H ANISOU 922 H MET A 70 1883 1489 1910 43 -261 198 H ATOM 923 HA MET A 70 29.307 14.769 -5.668 1.00 13.90 H ANISOU 923 HA MET A 70 1773 1852 1653 16 -85 89 H ATOM 924 HB2 MET A 70 29.575 16.244 -3.290 1.00 14.30 H ANISOU 924 HB2 MET A 70 1733 2184 1513 -91 -290 171 H ATOM 925 HB3 MET A 70 28.989 16.871 -4.621 1.00 13.49 H ANISOU 925 HB3 MET A 70 2008 1630 1485 -87 -150 188 H ATOM 926 HG2 MET A 70 27.149 16.368 -3.460 1.00 12.92 H ANISOU 926 HG2 MET A 70 1850 1656 1403 -166 -226 220 H ATOM 927 HG3 MET A 70 27.257 15.167 -4.478 1.00 13.17 H ANISOU 927 HG3 MET A 70 1773 1720 1507 24 -180 155 H ATOM 928 N ASP A 71 32.221 15.776 -4.784 1.00 16.16 N ANISOU 928 N ASP A 71 1892 1949 2297 -112 -361 727 N ATOM 929 CA ASP A 71 33.457 16.367 -5.319 1.00 15.71 C ANISOU 929 CA ASP A 71 1892 2013 2062 -22 -335 753 C ATOM 930 C ASP A 71 33.992 15.572 -6.512 1.00 17.04 C ANISOU 930 C ASP A 71 1889 2173 2411 127 -180 642 C ATOM 931 O ASP A 71 34.522 16.158 -7.455 1.00 17.39 O ANISOU 931 O ASP A 71 1853 2142 2609 12 46 591 O ATOM 932 CB ASP A 71 34.536 16.494 -4.239 1.00 17.14 C ANISOU 932 CB ASP A 71 1868 2555 2088 -51 -327 669 C ATOM 933 CG ASP A 71 34.285 17.644 -3.275 1.00 16.42 C ANISOU 933 CG ASP A 71 1750 2538 1951 -161 -101 656 C ATOM 934 OD1 ASP A 71 33.376 18.477 -3.517 1.00 19.03 O ANISOU 934 OD1 ASP A 71 2040 2403 2786 -161 -361 473 O ATOM 935 OD2 ASP A 71 35.055 17.714 -2.254 1.00 19.47 O ANISOU 935 OD2 ASP A 71 2185 2595 2616 -419 -651 669 O ATOM 936 H ASP A 71 32.277 15.488 -3.976 1.00 14.84 H ANISOU 936 H ASP A 71 1759 2043 1834 -49 -90 153 H ATOM 937 HA ASP A 71 33.255 17.267 -5.648 1.00 15.38 H ANISOU 937 HA ASP A 71 1934 1880 2031 -76 -264 598 H ATOM 938 HB2 ASP A 71 34.569 15.673 -3.724 1.00 15.60 H ANISOU 938 HB2 ASP A 71 1839 2432 1656 -83 -317 417 H ATOM 939 HB3 ASP A 71 35.393 16.650 -4.665 1.00 16.30 H ANISOU 939 HB3 ASP A 71 1916 2144 2131 -180 -259 369 H ATOM 940 N TYR A 72 33.856 14.237 -6.483 1.00 16.10 N ANISOU 940 N TYR A 72 1778 2116 2223 51 -219 590 N ATOM 941 CA TYR A 72 34.281 13.430 -7.630 1.00 16.24 C ANISOU 941 CA TYR A 72 1867 2170 2132 -146 -38 648 C ATOM 942 C TYR A 72 33.423 13.741 -8.854 1.00 14.83 C ANISOU 942 C TYR A 72 1957 1793 1885 318 41 293 C ATOM 943 O TYR A 72 33.895 13.700 -10.000 1.00 16.38 O ANISOU 943 O TYR A 72 1910 2131 2180 60 183 353 O ATOM 944 CB TYR A 72 34.222 11.925 -7.333 1.00 16.13 C ANISOU 944 CB TYR A 72 1938 2070 2121 153 45 487 C ATOM 945 CG TYR A 72 35.216 11.393 -6.343 1.00 18.92 C ANISOU 945 CG TYR A 72 2068 2375 2744 441 -251 446 C ATOM 946 CD1 TYR A 72 36.337 12.133 -5.961 1.00 21.32 C ANISOU 946 CD1 TYR A 72 2477 2597 3024 181 -427 276 C ATOM 947 CD2 TYR A 72 35.044 10.120 -5.794 1.00 19.61 C ANISOU 947 CD2 TYR A 72 2704 2197 2548 345 -592 251 C ATOM 948 CE1 TYR A 72 37.258 11.615 -5.065 1.00 26.73 C ANISOU 948 CE1 TYR A 72 2369 3852 3932 692 -703 341 C ATOM 949 CE2 TYR A 72 35.961 9.596 -4.887 1.00 23.52 C ANISOU 949 CE2 TYR A 72 3051 2753 3129 1089 -749 268 C ATOM 950 CZ TYR A 72 37.059 10.356 -4.520 1.00 31.26 C ANISOU 950 CZ TYR A 72 3565 4902 3408 -53 -1712 1458 C ATOM 951 OH TYR A 72 37.975 9.862 -3.623 1.00 35.59 O ANISOU 951 OH TYR A 72 3678 5896 3949 1534 -1496 947 O ATOM 952 H TYR A 72 33.533 13.787 -5.826 1.00 15.80 H ANISOU 952 H TYR A 72 1871 2076 2055 -112 -197 342 H ATOM 953 HA TYR A 72 35.202 13.661 -7.866 1.00 17.28 H ANISOU 953 HA TYR A 72 1801 2258 2506 -131 -47 336 H ATOM 954 HB2 TYR A 72 33.340 11.721 -6.989 1.00 15.01 H ANISOU 954 HB2 TYR A 72 1920 1814 1966 -23 -85 346 H ATOM 955 HB3 TYR A 72 34.361 11.443 -8.164 1.00 17.84 H ANISOU 955 HB3 TYR A 72 2099 2373 2305 39 159 236 H ATOM 956 HD1 TYR A 72 36.485 12.978 -6.313 1.00 21.69 H ANISOU 956 HD1 TYR A 72 2713 2659 2867 -24 -18 145 H ATOM 957 HD2 TYR A 72 34.304 9.613 -6.040 1.00 19.53 H ANISOU 957 HD2 TYR A 72 2554 2536 2330 124 -154 286 H ATOM 958 HE1 TYR A 72 37.996 12.121 -4.810 1.00 25.72 H ANISOU 958 HE1 TYR A 72 2843 4254 2673 366 -543 -31 H ATOM 959 HE2 TYR A 72 35.831 8.750 -4.522 1.00 23.15 H ANISOU 959 HE2 TYR A 72 3644 3051 2100 970 -478 326 H ATOM 960 N ALA A 73 32.117 13.959 -8.627 1.00 15.37 N ANISOU 960 N ALA A 73 1861 2062 1914 -9 97 616 N ATOM 961 CA ALA A 73 31.227 14.404 -9.715 1.00 14.11 C ANISOU 961 CA ALA A 73 1862 1791 1707 -82 102 274 C ATOM 962 C ALA A 73 31.669 15.759 -10.318 1.00 14.08 C ANISOU 962 C ALA A 73 1608 1879 1861 -56 -35 391 C ATOM 963 O ALA A 73 31.735 15.914 -11.531 1.00 14.92 O ANISOU 963 O ALA A 73 1774 1879 2013 -25 13 527 O ATOM 964 CB ALA A 73 29.762 14.478 -9.200 1.00 15.55 C ANISOU 964 CB ALA A 73 1726 1843 2339 -85 179 475 C ATOM 965 H ALA A 73 31.731 13.852 -7.865 1.00 14.66 H ANISOU 965 H ALA A 73 1891 1958 1718 -55 -1 245 H ATOM 966 HA ALA A 73 31.254 13.738 -10.434 1.00 15.79 H ANISOU 966 HA ALA A 73 2149 1872 1977 -29 77 87 H ATOM 967 N PHE A 74 31.987 16.714 -9.441 1.00 14.76 N ANISOU 967 N PHE A 74 1719 1839 2047 -19 -163 448 N ATOM 968 CA PHE A 74 32.465 18.008 -9.910 1.00 14.94 C ANISOU 968 CA PHE A 74 1905 1843 1928 -129 -10 402 C ATOM 969 C PHE A 74 33.791 17.852 -10.671 1.00 15.67 C ANISOU 969 C PHE A 74 1789 1992 2170 -65 -39 511 C ATOM 970 O PHE A 74 34.008 18.502 -11.686 1.00 16.07 O ANISOU 970 O PHE A 74 1894 1993 2218 -87 -77 602 O ATOM 971 CB PHE A 74 32.624 19.012 -8.773 1.00 14.83 C ANISOU 971 CB PHE A 74 1980 1980 1674 -168 -107 529 C ATOM 972 CG PHE A 74 31.370 19.230 -7.923 1.00 13.87 C ANISOU 972 CG PHE A 74 1905 1668 1693 -7 -157 510 C ATOM 973 CD1 PHE A 74 30.103 19.298 -8.505 1.00 14.52 C ANISOU 973 CD1 PHE A 74 1904 1830 1781 -87 -234 419 C ATOM 974 CD2 PHE A 74 31.469 19.435 -6.566 1.00 14.38 C ANISOU 974 CD2 PHE A 74 1760 1878 1825 -166 -230 117 C ATOM 975 CE1 PHE A 74 28.952 19.495 -7.706 1.00 14.36 C ANISOU 975 CE1 PHE A 74 1901 1646 1907 -45 -209 475 C ATOM 976 CE2 PHE A 74 30.333 19.640 -5.762 1.00 14.68 C ANISOU 976 CE2 PHE A 74 1774 1760 2041 -36 -142 477 C ATOM 977 CZ PHE A 74 29.061 19.643 -6.348 1.00 14.40 C ANISOU 977 CZ PHE A 74 1751 1803 1914 -60 -124 324 C ATOM 978 H PHE A 74 31.940 16.631 -8.586 1.00 14.12 H ANISOU 978 H PHE A 74 1774 1588 2001 -98 -38 299 H ATOM 979 HA PHE A 74 31.813 18.375 -10.542 1.00 13.80 H ANISOU 979 HA PHE A 74 1843 1613 1785 -57 57 216 H ATOM 980 HB2 PHE A 74 33.329 18.700 -8.184 1.00 14.71 H ANISOU 980 HB2 PHE A 74 1901 1830 1857 68 -52 334 H ATOM 981 HB3 PHE A 74 32.873 19.870 -9.151 1.00 14.56 H ANISOU 981 HB3 PHE A 74 1928 1758 1843 -34 -8 352 H ATOM 982 HD1 PHE A 74 30.003 19.167 -9.419 1.00 14.57 H ANISOU 982 HD1 PHE A 74 1966 1766 1801 -126 -233 362 H ATOM 983 HD2 PHE A 74 32.306 19.401 -6.163 1.00 13.99 H ANISOU 983 HD2 PHE A 74 1739 1823 1751 -87 -153 350 H ATOM 984 HE1 PHE A 74 28.113 19.512 -8.106 1.00 14.45 H ANISOU 984 HE1 PHE A 74 1854 1740 1897 -162 -153 403 H ATOM 985 HE2 PHE A 74 30.425 19.747 -4.843 1.00 14.20 H ANISOU 985 HE2 PHE A 74 1593 1824 1978 -56 -72 486 H ATOM 986 HZ PHE A 74 28.306 19.803 -5.831 1.00 14.77 H ANISOU 986 HZ PHE A 74 1760 1814 2036 -88 -69 295 H ATOM 987 N GLN A 75 34.669 16.977 -10.200 1.00 15.97 N ANISOU 987 N GLN A 75 1940 2125 2001 6 -21 603 N ATOM 988 CA GLN A 75 35.894 16.675 -10.913 1.00 15.63 C ANISOU 988 CA GLN A 75 1844 2031 2062 -208 67 536 C ATOM 989 C GLN A 75 35.641 16.066 -12.291 1.00 16.42 C ANISOU 989 C GLN A 75 1895 2152 2192 5 -36 398 C ATOM 990 O GLN A 75 36.321 16.405 -13.262 1.00 17.10 O ANISOU 990 O GLN A 75 1863 2344 2289 -17 24 420 O ATOM 991 CB GLN A 75 36.799 15.741 -10.100 1.00 16.11 C ANISOU 991 CB GLN A 75 2064 2093 1962 13 48 387 C ATOM 992 CG GLN A 75 38.233 15.665 -10.592 1.00 20.06 C ANISOU 992 CG GLN A 75 2069 2783 2768 119 143 618 C ATOM 993 CD GLN A 75 38.939 16.994 -10.529 1.00 22.50 C ANISOU 993 CD GLN A 75 2198 3145 3206 -237 188 330 C ATOM 994 OE1 GLN A 75 39.009 17.629 -9.480 1.00 23.79 O ANISOU 994 OE1 GLN A 75 2178 3764 3094 -425 -178 282 O ATOM 995 NE2 GLN A 75 39.453 17.429 -11.654 1.00 24.33 N ANISOU 995 NE2 GLN A 75 2854 3459 2930 -883 54 302 N ATOM 996 H GLN A 75 34.574 16.546 -9.462 1.00 14.22 H ANISOU 996 H GLN A 75 1979 1721 1703 -65 -10 209 H ATOM 997 HA GLN A 75 36.378 17.515 -11.051 1.00 16.54 H ANISOU 997 HA GLN A 75 1925 1837 2521 -107 76 367 H ATOM 998 HB2 GLN A 75 36.824 16.054 -9.182 1.00 16.95 H ANISOU 998 HB2 GLN A 75 2189 2168 2083 -25 -207 194 H ATOM 999 HB3 GLN A 75 36.430 14.845 -10.129 1.00 16.02 H ANISOU 999 HB3 GLN A 75 2074 1980 2029 149 -27 208 H ATOM 1000 HG2 GLN A 75 38.722 15.043 -10.031 1.00 19.84 H ANISOU 1000 HG2 GLN A 75 2186 2796 2556 369 -71 123 H ATOM 1001 HG3 GLN A 75 38.241 15.354 -11.511 1.00 18.65 H ANISOU 1001 HG3 GLN A 75 1690 2725 2668 125 222 635 H ATOM 1002 N TYR A 76 34.689 15.121 -12.380 1.00 14.74 N ANISOU 1002 N TYR A 76 1845 2071 1682 35 101 423 N ATOM 1003 CA TYR A 76 34.330 14.532 -13.673 1.00 15.68 C ANISOU 1003 CA TYR A 76 1995 2156 1803 69 11 287 C ATOM 1004 C TYR A 76 33.938 15.615 -14.657 1.00 15.08 C ANISOU 1004 C TYR A 76 1880 2067 1781 14 -79 200 C ATOM 1005 O TYR A 76 34.378 15.610 -15.794 1.00 16.62 O ANISOU 1005 O TYR A 76 1924 2292 2098 -146 263 403 O ATOM 1006 CB TYR A 76 33.166 13.521 -13.550 1.00 14.61 C ANISOU 1006 CB TYR A 76 2144 1929 1477 72 329 101 C ATOM 1007 CG TYR A 76 32.543 13.165 -14.858 1.00 14.74 C ANISOU 1007 CG TYR A 76 2120 2054 1424 -67 345 348 C ATOM 1008 CD1 TYR A 76 33.119 12.240 -15.685 1.00 16.14 C ANISOU 1008 CD1 TYR A 76 1958 1918 2256 -28 108 -80 C ATOM 1009 CD2 TYR A 76 31.362 13.774 -15.274 1.00 16.69 C ANISOU 1009 CD2 TYR A 76 1892 1859 2590 -42 161 30 C ATOM 1010 CE1 TYR A 76 32.564 11.913 -16.875 1.00 15.35 C ANISOU 1010 CE1 TYR A 76 2127 1915 1788 61 245 267 C ATOM 1011 CE2 TYR A 76 30.792 13.464 -16.500 1.00 17.08 C ANISOU 1011 CE2 TYR A 76 1963 2016 2508 -52 122 203 C ATOM 1012 CZ TYR A 76 31.387 12.540 -17.308 1.00 15.76 C ANISOU 1012 CZ TYR A 76 2027 1867 2091 -80 218 491 C ATOM 1013 OH TYR A 76 30.816 12.222 -18.523 1.00 17.19 O ANISOU 1013 OH TYR A 76 2015 2260 2255 -54 47 484 O ATOM 1014 H TYR A 76 34.247 14.810 -11.711 1.00 15.19 H ANISOU 1014 H TYR A 76 1853 2173 1745 72 187 356 H ATOM 1015 HA TYR A 76 35.108 14.059 -14.036 1.00 15.42 H ANISOU 1015 HA TYR A 76 1954 1932 1971 -5 -49 166 H ATOM 1016 HB2 TYR A 76 33.505 12.703 -13.153 1.00 14.46 H ANISOU 1016 HB2 TYR A 76 1822 1902 1768 117 -9 -78 H ATOM 1017 HB3 TYR A 76 32.477 13.899 -12.984 1.00 14.68 H ANISOU 1017 HB3 TYR A 76 1903 1935 1740 170 128 -40 H ATOM 1018 HD1 TYR A 76 33.905 11.821 -15.421 1.00 16.12 H ANISOU 1018 HD1 TYR A 76 1973 2044 2108 -62 117 133 H ATOM 1019 HD2 TYR A 76 30.962 14.415 -14.732 1.00 16.98 H ANISOU 1019 HD2 TYR A 76 2170 1965 2317 -42 456 227 H ATOM 1020 HE1 TYR A 76 32.981 11.286 -17.421 1.00 15.86 H ANISOU 1020 HE1 TYR A 76 2089 1945 1991 -22 245 115 H ATOM 1021 HE2 TYR A 76 30.005 13.882 -16.767 1.00 16.96 H ANISOU 1021 HE2 TYR A 76 1980 2033 2430 -40 201 320 H ATOM 1022 N VAL A 77 33.083 16.537 -14.231 1.00 16.38 N ANISOU 1022 N VAL A 77 1895 2161 2168 98 299 506 N ATOM 1023 CA VAL A 77 32.567 17.536 -15.165 1.00 15.00 C ANISOU 1023 CA VAL A 77 1858 2114 1725 -54 -91 191 C ATOM 1024 C VAL A 77 33.732 18.376 -15.735 1.00 17.08 C ANISOU 1024 C VAL A 77 1788 2484 2217 49 29 553 C ATOM 1025 O VAL A 77 33.792 18.641 -16.940 1.00 17.38 O ANISOU 1025 O VAL A 77 2127 2189 2284 30 281 550 O ATOM 1026 CB VAL A 77 31.480 18.435 -14.522 1.00 15.28 C ANISOU 1026 CB VAL A 77 1822 1898 2086 -48 20 348 C ATOM 1027 CG1 VAL A 77 31.032 19.521 -15.493 1.00 16.37 C ANISOU 1027 CG1 VAL A 77 2204 2095 1919 -25 -120 392 C ATOM 1028 CG2 VAL A 77 30.261 17.613 -14.067 1.00 15.46 C ANISOU 1028 CG2 VAL A 77 1747 2178 1947 -80 -124 487 C ATOM 1029 H VAL A 77 32.801 16.609 -13.422 1.00 14.85 H ANISOU 1029 H VAL A 77 1893 1812 1936 49 -52 280 H ATOM 1030 HA VAL A 77 32.154 17.065 -15.920 1.00 17.41 H ANISOU 1030 HA VAL A 77 2303 2337 1973 -152 -123 -59 H ATOM 1031 HB VAL A 77 31.859 18.874 -13.733 1.00 14.59 H ANISOU 1031 HB VAL A 77 1723 1864 1956 72 43 363 H ATOM 1032 N GLN A 78 34.666 18.736 -14.865 1.00 16.86 N ANISOU 1032 N GLN A 78 1936 2221 2249 -134 99 606 N ATOM 1033 CA GLN A 78 35.857 19.466 -15.272 1.00 17.47 C ANISOU 1033 CA GLN A 78 2085 2064 2486 -135 425 376 C ATOM 1034 C GLN A 78 36.717 18.636 -16.207 1.00 17.74 C ANISOU 1034 C GLN A 78 2006 2378 2355 -34 375 401 C ATOM 1035 O GLN A 78 37.055 19.095 -17.290 1.00 19.46 O ANISOU 1035 O GLN A 78 2287 2700 2405 -115 474 491 O ATOM 1036 CB GLN A 78 36.666 19.877 -14.049 1.00 18.90 C ANISOU 1036 CB GLN A 78 2181 2222 2775 -117 168 342 C ATOM 1037 CG GLN A 78 37.882 20.720 -14.389 1.00 21.42 C ANISOU 1037 CG GLN A 78 2284 2655 3197 -371 110 302 C ATOM 1038 CD GLN A 78 38.648 21.231 -13.184 1.00 22.71 C ANISOU 1038 CD GLN A 78 2516 2905 3204 -468 107 78 C ATOM 1039 OE1 GLN A 78 38.560 20.694 -12.082 1.00 26.52 O ANISOU 1039 OE1 GLN A 78 3079 3407 3589 -415 -656 589 O ATOM 1040 NE2 GLN A 78 39.442 22.284 -13.412 1.00 28.23 N ANISOU 1040 NE2 GLN A 78 2736 3366 4621 -842 -177 473 N ATOM 1041 H GLN A 78 34.630 18.572 -14.021 1.00 15.62 H ANISOU 1041 H GLN A 78 1832 1990 2110 -137 184 221 H ATOM 1042 HA GLN A 78 35.588 20.279 -15.747 1.00 17.51 H ANISOU 1042 HA GLN A 78 2256 2001 2395 -209 356 313 H ATOM 1043 HB2 GLN A 78 36.101 20.397 -13.458 1.00 18.91 H ANISOU 1043 HB2 GLN A 78 2258 2289 2638 -27 36 256 H ATOM 1044 HB3 GLN A 78 36.975 19.079 -13.593 1.00 19.31 H ANISOU 1044 HB3 GLN A 78 2550 2209 2575 14 146 211 H ATOM 1045 HG2 GLN A 78 38.500 20.189 -14.916 1.00 20.22 H ANISOU 1045 HG2 GLN A 78 2203 2657 2822 -352 71 446 H ATOM 1046 HG3 GLN A 78 37.592 21.489 -14.904 1.00 20.58 H ANISOU 1046 HG3 GLN A 78 2510 2407 2900 -412 365 178 H ATOM 1047 N ASP A 79 37.055 17.411 -15.800 1.00 16.13 N ANISOU 1047 N ASP A 79 1841 2413 1875 -43 245 288 N ATOM 1048 CA ASP A 79 37.889 16.515 -16.599 1.00 17.36 C ANISOU 1048 CA ASP A 79 2170 2412 2012 -90 482 213 C ATOM 1049 C ASP A 79 37.297 16.260 -17.992 1.00 17.49 C ANISOU 1049 C ASP A 79 2028 2444 2171 314 231 245 C ATOM 1050 O ASP A 79 38.003 16.153 -19.002 1.00 19.36 O ANISOU 1050 O ASP A 79 2263 3004 2088 -13 264 134 O ATOM 1051 CB ASP A 79 38.034 15.135 -15.936 1.00 18.36 C ANISOU 1051 CB ASP A 79 2209 2438 2329 186 274 270 C ATOM 1052 CG ASP A 79 38.834 15.144 -14.632 1.00 20.05 C ANISOU 1052 CG ASP A 79 2358 2655 2603 9 52 492 C ATOM 1053 OD1 ASP A 79 39.477 16.160 -14.293 1.00 22.27 O ANISOU 1053 OD1 ASP A 79 2079 2999 3382 -139 11 288 O ATOM 1054 OD2 ASP A 79 38.779 14.099 -13.926 1.00 20.76 O ANISOU 1054 OD2 ASP A 79 2805 3071 2013 -170 -136 616 O ATOM 1055 H ASP A 79 36.804 17.075 -15.049 1.00 15.84 H ANISOU 1055 H ASP A 79 1923 2255 1840 -155 257 156 H ATOM 1056 HA ASP A 79 38.780 16.907 -16.710 1.00 17.70 H ANISOU 1056 HA ASP A 79 1984 2356 2385 75 360 26 H ATOM 1057 HB2 ASP A 79 37.150 14.791 -15.737 1.00 17.64 H ANISOU 1057 HB2 ASP A 79 2347 2083 2270 26 245 162 H ATOM 1058 HB3 ASP A 79 38.487 14.537 -16.551 1.00 19.74 H ANISOU 1058 HB3 ASP A 79 2326 2484 2688 155 320 69 H ATOM 1059 N ASN A 80 35.973 16.088 -17.997 1.00 18.51 N ANISOU 1059 N ASN A 80 2073 2615 2345 -144 234 680 N ATOM 1060 CA ASN A 80 35.216 15.677 -19.170 1.00 17.77 C ANISOU 1060 CA ASN A 80 1905 2233 2613 35 168 437 C ATOM 1061 C ASN A 80 34.921 16.827 -20.115 1.00 16.53 C ANISOU 1061 C ASN A 80 1868 2464 1948 -63 423 345 C ATOM 1062 O ASN A 80 34.586 16.608 -21.270 1.00 20.51 O ANISOU 1062 O ASN A 80 2659 3171 1962 -264 202 670 O ATOM 1063 CB ASN A 80 33.893 15.083 -18.688 1.00 17.06 C ANISOU 1063 CB ASN A 80 1914 2323 2244 123 160 779 C ATOM 1064 CG ASN A 80 33.123 14.383 -19.774 1.00 17.30 C ANISOU 1064 CG ASN A 80 1934 2727 1909 -45 460 534 C ATOM 1065 OD1 ASN A 80 33.654 13.519 -20.467 1.00 19.13 O ANISOU 1065 OD1 ASN A 80 2383 2844 2038 160 255 362 O ATOM 1066 ND2 ASN A 80 31.846 14.750 -19.935 1.00 17.65 N ANISOU 1066 ND2 ASN A 80 2060 2819 1826 72 134 831 N ATOM 1067 H ASN A 80 35.477 16.209 -17.306 1.00 18.11 H ANISOU 1067 H ASN A 80 1985 2392 2503 35 206 424 H ATOM 1068 HA ASN A 80 35.711 14.989 -19.661 1.00 19.05 H ANISOU 1068 HA ASN A 80 2004 2479 2752 38 347 302 H ATOM 1069 HB2 ASN A 80 34.080 14.424 -18.002 1.00 17.27 H ANISOU 1069 HB2 ASN A 80 2681 1932 1946 87 143 435 H ATOM 1070 HB3 ASN A 80 33.338 15.792 -18.325 1.00 16.96 H ANISOU 1070 HB3 ASN A 80 1921 2173 2347 -7 115 595 H ATOM 1071 N GLY A 81 35.040 18.046 -19.612 1.00 17.49 N ANISOU 1071 N GLY A 81 2065 2342 2237 -68 36 600 N ATOM 1072 CA GLY A 81 34.715 19.226 -20.386 1.00 17.59 C ANISOU 1072 CA GLY A 81 2083 2408 2192 39 265 593 C ATOM 1073 C GLY A 81 33.233 19.438 -20.614 1.00 17.51 C ANISOU 1073 C GLY A 81 2125 2558 1970 37 229 689 C ATOM 1074 O GLY A 81 32.865 20.167 -21.528 1.00 20.21 O ANISOU 1074 O GLY A 81 2059 3104 2514 -143 -29 1168 O ATOM 1075 H GLY A 81 35.306 18.226 -18.815 1.00 16.87 H ANISOU 1075 H GLY A 81 2031 2121 2256 141 103 388 H ATOM 1076 HA2 GLY A 81 35.150 19.173 -21.251 1.00 16.90 H ANISOU 1076 HA2 GLY A 81 2070 2269 2080 -32 142 438 H ATOM 1077 HA3 GLY A 81 35.060 20.007 -19.926 1.00 17.40 H ANISOU 1077 HA3 GLY A 81 2071 2292 2249 379 155 378 H ATOM 1078 N GLY A 82 32.375 18.853 -19.778 1.00 17.14 N ANISOU 1078 N GLY A 82 2053 2397 2061 -158 162 499 N ATOM 1079 CA GLY A 82 30.941 19.005 -19.968 1.00 14.66 C ANISOU 1079 CA GLY A 82 2087 2096 1386 -224 191 185 C ATOM 1080 C GLY A 82 30.110 17.989 -19.211 1.00 15.00 C ANISOU 1080 C GLY A 82 2028 1886 1784 -169 96 265 C ATOM 1081 O GLY A 82 30.613 17.031 -18.613 1.00 16.27 O ANISOU 1081 O GLY A 82 1961 2182 2037 78 363 407 O ATOM 1082 H GLY A 82 32.595 18.374 -19.099 1.00 14.95 H ANISOU 1082 H GLY A 82 1948 1858 1874 -200 246 219 H ATOM 1083 HA2 GLY A 82 30.727 18.918 -20.910 1.00 16.20 H ANISOU 1083 HA2 GLY A 82 2462 2194 1496 -182 -16 209 H ATOM 1084 HA3 GLY A 82 30.680 19.890 -19.679 1.00 15.01 H ANISOU 1084 HA3 GLY A 82 2042 1936 1722 -322 9 185 H ATOM 1085 N LEU A 83 28.806 18.246 -19.233 1.00 15.05 N ANISOU 1085 N LEU A 83 2005 1924 1788 -63 183 467 N ATOM 1086 CA LEU A 83 27.805 17.373 -18.665 1.00 13.81 C ANISOU 1086 CA LEU A 83 1963 1977 1306 -44 68 439 C ATOM 1087 C LEU A 83 26.522 17.547 -19.441 1.00 14.02 C ANISOU 1087 C LEU A 83 2002 1917 1406 -23 16 277 C ATOM 1088 O LEU A 83 26.085 18.676 -19.670 1.00 15.27 O ANISOU 1088 O LEU A 83 1982 2029 1791 38 38 545 O ATOM 1089 CB LEU A 83 27.572 17.700 -17.191 1.00 13.45 C ANISOU 1089 CB LEU A 83 1774 1889 1447 -21 129 228 C ATOM 1090 CG LEU A 83 26.640 16.777 -16.374 1.00 14.01 C ANISOU 1090 CG LEU A 83 1792 2153 1377 -76 -7 442 C ATOM 1091 CD1 LEU A 83 27.291 15.399 -16.234 1.00 17.50 C ANISOU 1091 CD1 LEU A 83 2361 1933 2352 -50 197 456 C ATOM 1092 CD2 LEU A 83 26.229 17.311 -14.993 1.00 15.53 C ANISOU 1092 CD2 LEU A 83 1911 2593 1396 62 177 344 C ATOM 1093 H LEU A 83 28.475 18.958 -19.587 1.00 13.99 H ANISOU 1093 H LEU A 83 2112 1658 1546 -113 124 178 H ATOM 1094 HA LEU A 83 28.099 16.443 -18.748 1.00 13.37 H ANISOU 1094 HA LEU A 83 1734 1912 1431 -166 91 193 H ATOM 1095 HB2 LEU A 83 28.435 17.708 -16.747 1.00 13.42 H ANISOU 1095 HB2 LEU A 83 1805 1805 1488 -57 71 55 H ATOM 1096 HB3 LEU A 83 27.193 18.593 -17.149 1.00 14.23 H ANISOU 1096 HB3 LEU A 83 1829 1823 1753 -80 -3 154 H ATOM 1097 HG LEU A 83 25.821 16.651 -16.877 1.00 15.25 H ANISOU 1097 HG LEU A 83 1763 2231 1799 -212 -10 23 H ATOM 1098 N ASP A 84 25.901 16.439 -19.806 1.00 14.01 N ANISOU 1098 N ASP A 84 1971 1874 1478 59 148 305 N ATOM 1099 CA ASP A 84 24.665 16.479 -20.565 1.00 14.29 C ANISOU 1099 CA ASP A 84 2027 2012 1387 41 96 359 C ATOM 1100 C ASP A 84 23.446 16.926 -19.743 1.00 13.14 C ANISOU 1100 C ASP A 84 1969 1707 1314 -34 -21 338 C ATOM 1101 O ASP A 84 23.376 16.763 -18.536 1.00 13.62 O ANISOU 1101 O ASP A 84 2002 1858 1314 29 35 281 O ATOM 1102 CB ASP A 84 24.412 15.121 -21.227 1.00 15.39 C ANISOU 1102 CB ASP A 84 2036 1895 1916 61 -37 372 C ATOM 1103 CG ASP A 84 25.404 14.814 -22.363 1.00 15.02 C ANISOU 1103 CG ASP A 84 1946 1995 1763 -82 -188 93 C ATOM 1104 OD1 ASP A 84 25.987 15.788 -22.931 1.00 16.64 O ANISOU 1104 OD1 ASP A 84 2356 2096 1869 93 207 477 O ATOM 1105 OD2 ASP A 84 25.571 13.633 -22.745 1.00 16.03 O ANISOU 1105 OD2 ASP A 84 2435 2018 1638 2 -19 280 O ATOM 1106 H ASP A 84 26.177 15.645 -19.621 1.00 14.11 H ANISOU 1106 H ASP A 84 1910 1847 1603 74 100 205 H ATOM 1107 HA ASP A 84 24.772 17.135 -21.283 1.00 14.01 H ANISOU 1107 HA ASP A 84 2009 1853 1458 14 101 300 H ATOM 1108 HB2 ASP A 84 24.487 14.420 -20.561 1.00 15.60 H ANISOU 1108 HB2 ASP A 84 2258 1904 1765 178 -67 263 H ATOM 1109 HB3 ASP A 84 23.521 15.118 -21.604 1.00 15.31 H ANISOU 1109 HB3 ASP A 84 2042 1945 1829 92 -43 271 H ATOM 1110 N SER A 85 22.446 17.442 -20.460 1.00 15.06 N ANISOU 1110 N SER A 85 2000 2097 1624 123 -170 395 N ATOM 1111 CA SER A 85 21.157 17.779 -19.862 1.00 14.47 C ANISOU 1111 CA SER A 85 2142 1938 1417 114 -29 335 C ATOM 1112 C SER A 85 20.358 16.537 -19.460 1.00 13.48 C ANISOU 1112 C SER A 85 1885 1997 1239 148 -150 317 C ATOM 1113 O SER A 85 20.526 15.455 -20.028 1.00 14.71 O ANISOU 1113 O SER A 85 2023 1957 1609 149 -78 340 O ATOM 1114 CB SER A 85 20.304 18.609 -20.825 1.00 15.33 C ANISOU 1114 CB SER A 85 2090 1903 1828 126 -41 443 C ATOM 1115 OG SER A 85 19.866 17.804 -21.899 1.00 17.20 O ANISOU 1115 OG SER A 85 2372 2192 1971 -10 -393 432 O ATOM 1116 H SER A 85 22.491 17.604 -21.303 1.00 13.50 H ANISOU 1116 H SER A 85 1742 1752 1633 166 -99 346 H ATOM 1117 HA SER A 85 21.311 18.318 -19.058 1.00 15.84 H ANISOU 1117 HA SER A 85 2250 2015 1752 49 -141 114 H ATOM 1118 HB2 SER A 85 19.535 18.958 -20.352 1.00 16.41 H ANISOU 1118 HB2 SER A 85 1845 2156 2234 32 -27 367 H ATOM 1119 HB3 SER A 85 20.839 19.339 -21.175 1.00 14.78 H ANISOU 1119 HB3 SER A 85 2025 1914 1677 163 -21 408 H ATOM 1120 N GLU A 86 19.515 16.717 -18.449 1.00 13.32 N ANISOU 1120 N GLU A 86 2188 1897 975 98 -192 261 N ATOM 1121 CA GLU A 86 18.568 15.672 -18.056 1.00 14.53 C ANISOU 1121 CA GLU A 86 2018 1872 1627 74 -81 252 C ATOM 1122 C GLU A 86 17.743 15.199 -19.267 1.00 15.11 C ANISOU 1122 C GLU A 86 2045 2074 1620 15 42 218 C ATOM 1123 O GLU A 86 17.551 14.018 -19.488 1.00 15.70 O ANISOU 1123 O GLU A 86 2276 2181 1508 -17 -358 166 O ATOM 1124 CB GLU A 86 17.650 16.227 -16.963 1.00 14.55 C ANISOU 1124 CB GLU A 86 1998 1816 1714 39 -132 133 C ATOM 1125 CG GLU A 86 16.731 15.240 -16.263 1.00 15.55 C ANISOU 1125 CG GLU A 86 1864 2092 1953 -139 -251 266 C ATOM 1126 CD GLU A 86 17.486 14.458 -15.235 1.00 14.24 C ANISOU 1126 CD GLU A 86 2150 1816 1444 -29 -77 45 C ATOM 1127 OE1 GLU A 86 18.041 13.421 -15.630 1.00 17.91 O ANISOU 1127 OE1 GLU A 86 3032 2174 1597 407 -60 -114 O ATOM 1128 OE2 GLU A 86 17.544 14.874 -14.037 1.00 13.75 O ANISOU 1128 OE2 GLU A 86 1868 1909 1448 -12 -43 6 O ATOM 1129 H GLU A 86 19.472 17.434 -17.978 1.00 14.30 H ANISOU 1129 H GLU A 86 1974 1846 1611 101 -57 95 H ATOM 1130 HA GLU A 86 19.057 14.905 -17.693 1.00 14.59 H ANISOU 1130 HA GLU A 86 1997 1711 1833 27 -77 162 H ATOM 1131 HB2 GLU A 86 18.204 16.637 -16.280 1.00 14.38 H ANISOU 1131 HB2 GLU A 86 1817 1848 1799 9 -85 96 H ATOM 1132 HB3 GLU A 86 17.085 16.907 -17.363 1.00 14.70 H ANISOU 1132 HB3 GLU A 86 1904 1840 1839 39 -151 95 H ATOM 1133 HG2 GLU A 86 16.021 15.726 -15.816 1.00 15.45 H ANISOU 1133 HG2 GLU A 86 1998 1944 1925 -152 -177 195 H ATOM 1134 HG3 GLU A 86 16.359 14.620 -16.910 1.00 14.76 H ANISOU 1134 HG3 GLU A 86 1790 2009 1808 12 -173 257 H ATOM 1135 N GLU A 87 17.259 16.146 -20.064 1.00 14.37 N ANISOU 1135 N GLU A 87 2145 2000 1314 -97 -115 22 N ATOM 1136 CA GLU A 87 16.411 15.805 -21.201 1.00 16.08 C ANISOU 1136 CA GLU A 87 2253 2334 1520 -134 -281 -50 C ATOM 1137 C GLU A 87 17.152 14.926 -22.226 1.00 15.15 C ANISOU 1137 C GLU A 87 2209 2288 1256 -72 -319 122 C ATOM 1138 O GLU A 87 16.583 13.981 -22.775 1.00 17.83 O ANISOU 1138 O GLU A 87 2336 2444 1993 -110 -360 -144 O ATOM 1139 CB GLU A 87 15.855 17.081 -21.823 1.00 19.38 C ANISOU 1139 CB GLU A 87 2686 2574 2103 268 -354 105 C ATOM 1140 CG GLU A 87 14.784 16.853 -22.871 1.00 25.12 C ANISOU 1140 CG GLU A 87 3019 3980 2544 153 -722 265 C ATOM 1141 CD GLU A 87 13.864 18.065 -23.105 1.00 32.15 C ANISOU 1141 CD GLU A 87 3942 4560 3713 878 -1240 282 C ATOM 1142 OE1 GLU A 87 13.925 19.081 -22.367 1.00 38.57 O ANISOU 1142 OE1 GLU A 87 5578 4532 4543 651 -1392 -30 O ATOM 1143 OE2 GLU A 87 13.055 17.982 -24.053 1.00 35.35 O ANISOU 1143 OE2 GLU A 87 4417 5646 3367 611 -1242 669 O ATOM 1144 H GLU A 87 17.407 16.988 -19.967 1.00 14.49 H ANISOU 1144 H GLU A 87 2008 1944 1553 0 -154 13 H ATOM 1145 HA GLU A 87 15.647 15.286 -20.871 1.00 16.76 H ANISOU 1145 HA GLU A 87 2001 2403 1965 -40 -192 -161 H ATOM 1146 HB2 GLU A 87 15.471 17.620 -21.114 1.00 20.85 H ANISOU 1146 HB2 GLU A 87 2809 2513 2598 172 -49 -49 H ATOM 1147 HB3 GLU A 87 16.582 17.565 -22.245 1.00 19.65 H ANISOU 1147 HB3 GLU A 87 2867 2280 2317 304 -171 163 H ATOM 1148 HG2 GLU A 87 15.214 16.642 -23.715 1.00 24.71 H ANISOU 1148 HG2 GLU A 87 3247 3595 2546 -409 -712 -145 H ATOM 1149 HG3 GLU A 87 14.228 16.110 -22.592 1.00 24.95 H ANISOU 1149 HG3 GLU A 87 2775 3863 2841 9 -409 -362 H ATOM 1150 N SER A 88 18.439 15.217 -22.446 1.00 14.87 N ANISOU 1150 N SER A 88 2197 2160 1291 -96 -370 225 N ATOM 1151 CA SER A 88 19.230 14.511 -23.462 1.00 16.59 C ANISOU 1151 CA SER A 88 2269 2132 1902 -30 -167 68 C ATOM 1152 C SER A 88 19.698 13.140 -22.960 1.00 15.31 C ANISOU 1152 C SER A 88 2066 2295 1453 -4 -77 213 C ATOM 1153 O SER A 88 20.001 12.256 -23.775 1.00 17.08 O ANISOU 1153 O SER A 88 2810 2378 1300 265 0 393 O ATOM 1154 CB SER A 88 20.474 15.321 -23.857 1.00 16.16 C ANISOU 1154 CB SER A 88 2367 2338 1433 28 -64 197 C ATOM 1155 OG SER A 88 21.466 15.311 -22.850 1.00 17.42 O ANISOU 1155 OG SER A 88 2259 2348 2011 -115 -264 153 O ATOM 1156 H SER A 88 18.879 15.822 -22.022 1.00 15.81 H ANISOU 1156 H SER A 88 2220 1942 1844 -55 -298 107 H ATOM 1157 HA SER A 88 18.687 14.376 -24.267 1.00 15.28 H ANISOU 1157 HA SER A 88 2198 1917 1688 256 -15 25 H ATOM 1158 HB2 SER A 88 20.850 14.936 -24.665 1.00 16.91 H ANISOU 1158 HB2 SER A 88 2355 2191 1876 104 5 -103 H ATOM 1159 HB3 SER A 88 20.208 16.238 -24.026 1.00 15.51 H ANISOU 1159 HB3 SER A 88 2032 2156 1704 -56 -91 -128 H ATOM 1160 N TYR A 89 19.792 12.952 -21.646 1.00 15.27 N ANISOU 1160 N TYR A 89 2299 2016 1486 -3 34 257 N ATOM 1161 CA TYR A 89 20.423 11.746 -21.088 1.00 14.96 C ANISOU 1161 CA TYR A 89 2202 1959 1520 49 131 175 C ATOM 1162 C TYR A 89 19.616 11.413 -19.842 1.00 14.38 C ANISOU 1162 C TYR A 89 2124 2118 1219 134 -149 319 C ATOM 1163 O TYR A 89 20.010 11.667 -18.684 1.00 14.46 O ANISOU 1163 O TYR A 89 2151 2053 1289 -26 -141 264 O ATOM 1164 CB TYR A 89 21.909 12.036 -20.826 1.00 14.78 C ANISOU 1164 CB TYR A 89 2179 2059 1378 42 68 85 C ATOM 1165 CG TYR A 89 22.841 10.871 -20.539 1.00 14.48 C ANISOU 1165 CG TYR A 89 2183 2124 1194 17 270 363 C ATOM 1166 CD1 TYR A 89 22.390 9.650 -20.089 1.00 15.45 C ANISOU 1166 CD1 TYR A 89 2012 2065 1793 -123 -12 316 C ATOM 1167 CD2 TYR A 89 24.218 11.019 -20.717 1.00 16.40 C ANISOU 1167 CD2 TYR A 89 2094 2006 2128 -126 -4 381 C ATOM 1168 CE1 TYR A 89 23.283 8.604 -19.797 1.00 16.41 C ANISOU 1168 CE1 TYR A 89 2230 2117 1887 32 229 446 C ATOM 1169 CE2 TYR A 89 25.089 9.998 -20.469 1.00 16.05 C ANISOU 1169 CE2 TYR A 89 2144 2171 1781 -44 145 368 C ATOM 1170 CZ TYR A 89 24.627 8.794 -20.005 1.00 17.82 C ANISOU 1170 CZ TYR A 89 2172 2065 2531 23 194 415 C ATOM 1171 OH TYR A 89 25.545 7.806 -19.763 1.00 18.51 O ANISOU 1171 OH TYR A 89 2155 2439 2438 175 269 608 O ATOM 1172 H TYR A 89 19.507 13.505 -21.052 1.00 14.72 H ANISOU 1172 H TYR A 89 2094 1962 1534 -8 -73 187 H ATOM 1173 HA TYR A 89 20.368 10.996 -21.714 1.00 15.06 H ANISOU 1173 HA TYR A 89 2044 2076 1600 38 143 62 H ATOM 1174 HB2 TYR A 89 22.261 12.483 -21.612 1.00 14.64 H ANISOU 1174 HB2 TYR A 89 2195 1740 1628 0 83 169 H ATOM 1175 HB3 TYR A 89 21.970 12.641 -20.071 1.00 16.23 H ANISOU 1175 HB3 TYR A 89 2469 2029 1667 -103 92 -64 H ATOM 1176 HD1 TYR A 89 21.484 9.516 -19.938 1.00 15.21 H ANISOU 1176 HD1 TYR A 89 2035 2093 1650 -135 43 161 H ATOM 1177 HD2 TYR A 89 24.549 11.830 -21.028 1.00 15.52 H ANISOU 1177 HD2 TYR A 89 2187 1940 1767 -169 67 148 H ATOM 1178 HE1 TYR A 89 22.965 7.783 -19.499 1.00 16.09 H ANISOU 1178 HE1 TYR A 89 2183 1919 2011 -54 84 142 H ATOM 1179 HE2 TYR A 89 26.001 10.126 -20.596 1.00 16.36 H ANISOU 1179 HE2 TYR A 89 2091 2121 2003 -69 20 213 H ATOM 1180 N PRO A 90 18.422 10.848 -20.068 1.00 15.82 N ANISOU 1180 N PRO A 90 2364 2393 1253 -274 -60 387 N ATOM 1181 CA PRO A 90 17.478 10.716 -18.967 1.00 15.83 C ANISOU 1181 CA PRO A 90 2285 2362 1366 -211 -72 483 C ATOM 1182 C PRO A 90 17.821 9.690 -17.896 1.00 14.86 C ANISOU 1182 C PRO A 90 2056 2126 1462 -234 104 483 C ATOM 1183 O PRO A 90 18.614 8.761 -18.114 1.00 16.73 O ANISOU 1183 O PRO A 90 2483 2190 1684 -50 -109 180 O ATOM 1184 CB PRO A 90 16.171 10.308 -19.655 1.00 19.39 C ANISOU 1184 CB PRO A 90 2161 3070 2136 -228 -257 464 C ATOM 1185 CG PRO A 90 16.525 9.897 -21.007 1.00 22.15 C ANISOU 1185 CG PRO A 90 2877 3349 2188 -735 -370 15 C ATOM 1186 CD PRO A 90 17.826 10.512 -21.368 1.00 17.11 C ANISOU 1186 CD PRO A 90 2523 2614 1361 47 -252 283 C ATOM 1187 HA PRO A 90 17.345 11.585 -18.536 1.00 16.03 H ANISOU 1187 HA PRO A 90 2065 2277 1748 26 80 513 H ATOM 1188 HB2 PRO A 90 15.758 9.571 -19.176 1.00 18.69 H ANISOU 1188 HB2 PRO A 90 2223 2417 2460 -155 -107 44 H ATOM 1189 HB3 PRO A 90 15.571 11.065 -19.686 1.00 19.76 H ANISOU 1189 HB3 PRO A 90 2312 2674 2520 -381 -391 421 H ATOM 1190 HG2 PRO A 90 16.596 8.930 -21.034 1.00 21.08 H ANISOU 1190 HG2 PRO A 90 2310 3294 2403 -300 -107 216 H ATOM 1191 HG3 PRO A 90 15.835 10.197 -21.619 1.00 19.89 H ANISOU 1191 HG3 PRO A 90 2532 2858 2167 -255 12 -177 H ATOM 1192 HD2 PRO A 90 18.377 9.869 -21.840 1.00 17.95 H ANISOU 1192 HD2 PRO A 90 2816 2101 1902 -83 -436 -78 H ATOM 1193 HD3 PRO A 90 17.682 11.314 -21.894 1.00 16.65 H ANISOU 1193 HD3 PRO A 90 2400 2361 1565 118 -495 81 H ATOM 1194 N TYR A 91 17.197 9.859 -16.746 1.00 15.19 N ANISOU 1194 N TYR A 91 2119 2293 1360 -272 35 453 N ATOM 1195 CA TYR A 91 17.496 9.038 -15.575 1.00 14.43 C ANISOU 1195 CA TYR A 91 2135 2197 1151 -259 9 260 C ATOM 1196 C TYR A 91 16.819 7.665 -15.634 1.00 15.88 C ANISOU 1196 C TYR A 91 2152 2230 1651 -289 -300 341 C ATOM 1197 O TYR A 91 15.599 7.574 -15.756 1.00 19.36 O ANISOU 1197 O TYR A 91 2130 2533 2690 -417 -415 623 O ATOM 1198 CB TYR A 91 17.123 9.763 -14.287 1.00 13.66 C ANISOU 1198 CB TYR A 91 1856 2127 1204 -315 -8 237 C ATOM 1199 CG TYR A 91 17.559 9.016 -13.053 1.00 13.59 C ANISOU 1199 CG TYR A 91 1914 2037 1211 -287 -179 157 C ATOM 1200 CD1 TYR A 91 18.906 8.764 -12.803 1.00 14.28 C ANISOU 1200 CD1 TYR A 91 1948 2113 1362 -156 -119 241 C ATOM 1201 CD2 TYR A 91 16.637 8.522 -12.145 1.00 13.02 C ANISOU 1201 CD2 TYR A 91 1806 1799 1340 -96 -42 60 C ATOM 1202 CE1 TYR A 91 19.303 8.077 -11.675 1.00 13.27 C ANISOU 1202 CE1 TYR A 91 1691 1960 1390 -119 -86 221 C ATOM 1203 CE2 TYR A 91 17.032 7.814 -11.027 1.00 13.39 C ANISOU 1203 CE2 TYR A 91 1797 2124 1165 -310 -132 83 C ATOM 1204 CZ TYR A 91 18.363 7.591 -10.788 1.00 13.04 C ANISOU 1204 CZ TYR A 91 1783 1770 1399 -35 107 108 C ATOM 1205 OH TYR A 91 18.774 6.904 -9.670 1.00 13.66 O ANISOU 1205 OH TYR A 91 1998 1748 1444 38 -80 55 O ATOM 1206 H TYR A 91 16.585 10.448 -16.610 1.00 15.31 H ANISOU 1206 H TYR A 91 2262 2201 1353 -217 14 325 H ATOM 1207 HA TYR A 91 18.463 8.891 -15.545 1.00 14.37 H ANISOU 1207 HA TYR A 91 2129 1913 1417 -147 17 176 H ATOM 1208 HB2 TYR A 91 17.555 10.631 -14.279 1.00 14.06 H ANISOU 1208 HB2 TYR A 91 1785 1797 1760 20 -22 215 H ATOM 1209 HB3 TYR A 91 16.160 9.872 -14.254 1.00 14.04 H ANISOU 1209 HB3 TYR A 91 1874 1902 1555 -98 -135 154 H ATOM 1210 HD1 TYR A 91 19.549 9.086 -13.393 1.00 13.25 H ANISOU 1210 HD1 TYR A 91 1872 1682 1477 -91 -126 220 H ATOM 1211 HD2 TYR A 91 15.730 8.661 -12.296 1.00 13.70 H ANISOU 1211 HD2 TYR A 91 1811 1864 1530 -45 -78 87 H ATOM 1212 HE1 TYR A 91 20.207 7.924 -11.520 1.00 13.19 H ANISOU 1212 HE1 TYR A 91 1674 1843 1493 -39 -1 103 H ATOM 1213 HE2 TYR A 91 16.394 7.501 -10.429 1.00 12.95 H ANISOU 1213 HE2 TYR A 91 1727 1720 1473 -144 -15 126 H ATOM 1214 N GLU A 92 17.620 6.607 -15.508 1.00 14.39 N ANISOU 1214 N GLU A 92 2342 2389 734 -155 -27 166 N ATOM 1215 CA GLU A 92 17.135 5.231 -15.581 1.00 17.43 C ANISOU 1215 CA GLU A 92 2487 2316 1820 -325 121 253 C ATOM 1216 C GLU A 92 17.265 4.430 -14.289 1.00 16.40 C ANISOU 1216 C GLU A 92 2298 2094 1837 -285 -35 136 C ATOM 1217 O GLU A 92 16.768 3.312 -14.217 1.00 18.09 O ANISOU 1217 O GLU A 92 2841 2228 1804 -516 -88 29 O ATOM 1218 CB GLU A 92 17.881 4.483 -16.686 1.00 18.96 C ANISOU 1218 CB GLU A 92 2960 2513 1730 -620 -91 -244 C ATOM 1219 CG GLU A 92 17.873 5.148 -18.063 1.00 22.73 C ANISOU 1219 CG GLU A 92 3906 3130 1598 -588 105 -208 C ATOM 1220 CD GLU A 92 16.476 5.399 -18.617 1.00 27.91 C ANISOU 1220 CD GLU A 92 4121 3501 2982 -153 -378 675 C ATOM 1221 OE1 GLU A 92 15.503 4.718 -18.207 1.00 30.61 O ANISOU 1221 OE1 GLU A 92 4002 4817 2811 -550 -257 200 O ATOM 1222 OE2 GLU A 92 16.355 6.278 -19.501 1.00 36.14 O ANISOU 1222 OE2 GLU A 92 6895 4530 2305 -487 -949 797 O ATOM 1223 H GLU A 92 18.469 6.661 -15.385 1.00 15.62 H ANISOU 1223 H GLU A 92 2244 2118 1570 -88 125 111 H ATOM 1224 HA GLU A 92 16.184 5.232 -15.812 1.00 18.70 H ANISOU 1224 HA GLU A 92 2604 2428 2073 -322 -221 336 H ATOM 1225 HB2 GLU A 92 18.809 4.387 -16.418 1.00 18.83 H ANISOU 1225 HB2 GLU A 92 2716 2122 2315 -324 247 -74 H ATOM 1226 HB3 GLU A 92 17.484 3.604 -16.786 1.00 20.28 H ANISOU 1226 HB3 GLU A 92 2741 2236 2727 -275 -87 -114 H ATOM 1227 HG2 GLU A 92 18.329 6.002 -18.005 1.00 22.86 H ANISOU 1227 HG2 GLU A 92 3712 2657 2313 -127 325 183 H ATOM 1228 HG3 GLU A 92 18.338 4.571 -18.689 1.00 22.93 H ANISOU 1228 HG3 GLU A 92 3896 2867 1946 -396 330 62 H ATOM 1229 N ALA A 93 17.960 4.970 -13.290 1.00 16.42 N ANISOU 1229 N ALA A 93 2525 1866 1846 -354 -37 49 N ATOM 1230 CA ALA A 93 18.119 4.290 -11.981 1.00 15.74 C ANISOU 1230 CA ALA A 93 2249 1917 1813 -59 -30 -17 C ATOM 1231 C ALA A 93 18.775 2.895 -12.107 1.00 16.73 C ANISOU 1231 C ALA A 93 2638 1800 1918 -214 58 -237 C ATOM 1232 O ALA A 93 18.428 1.966 -11.380 1.00 19.10 O ANISOU 1232 O ALA A 93 3115 1877 2263 -64 -5 110 O ATOM 1233 CB ALA A 93 16.786 4.198 -11.246 1.00 15.61 C ANISOU 1233 CB ALA A 93 2346 1788 1796 -101 80 191 C ATOM 1234 H ALA A 93 18.357 5.731 -13.325 1.00 15.65 H ANISOU 1234 H ALA A 93 2031 1834 2082 -168 123 36 H ATOM 1235 HA ALA A 93 18.716 4.834 -11.427 1.00 15.27 H ANISOU 1235 HA ALA A 93 2189 1743 1871 56 3 -94 H ATOM 1236 N THR A 94 19.711 2.767 -13.032 1.00 18.22 N ANISOU 1236 N THR A 94 2408 2055 2459 9 191 158 N ATOM 1237 CA THR A 94 20.508 1.550 -13.130 1.00 19.24 C ANISOU 1237 CA THR A 94 2789 2259 2262 235 -31 -51 C ATOM 1238 C THR A 94 21.844 1.889 -13.796 1.00 18.50 C ANISOU 1238 C THR A 94 3115 2716 1198 325 34 167 C ATOM 1239 O THR A 94 21.961 2.923 -14.407 1.00 26.09 O ANISOU 1239 O THR A 94 3505 2201 4205 149 1054 436 O ATOM 1240 CB THR A 94 19.728 0.450 -13.881 1.00 22.18 C ANISOU 1240 CB THR A 94 3205 2840 2382 158 213 -774 C ATOM 1241 OG1 THR A 94 20.384 -0.815 -13.709 1.00 32.42 O ANISOU 1241 OG1 THR A 94 4221 2978 5118 644 6 -922 O ATOM 1242 CG2 THR A 94 19.595 0.781 -15.369 1.00 26.55 C ANISOU 1242 CG2 THR A 94 3130 4666 2291 143 -350 -922 C ATOM 1243 H THR A 94 19.908 3.367 -13.616 1.00 17.57 H ANISOU 1243 H THR A 94 2401 2185 2087 -42 32 75 H ATOM 1244 HA THR A 94 20.707 1.216 -12.230 1.00 17.26 H ANISOU 1244 HA THR A 94 2134 2110 2315 -79 172 148 H ATOM 1245 HB THR A 94 18.833 0.388 -13.511 1.00 23.24 H ANISOU 1245 HB THR A 94 2961 2850 3016 -105 -26 -154 H ATOM 1246 N GLU A 95 22.858 1.037 -13.659 1.00 24.84 N ANISOU 1246 N GLU A 95 3206 3910 2321 734 159 1254 N ATOM 1247 CA GLU A 95 24.139 1.335 -14.291 1.00 28.84 C ANISOU 1247 CA GLU A 95 3207 4370 3378 81 368 233 C ATOM 1248 C GLU A 95 24.147 0.789 -15.708 1.00 28.38 C ANISOU 1248 C GLU A 95 3541 3955 3284 -1 496 375 C ATOM 1249 O GLU A 95 23.563 -0.250 -16.018 1.00 27.92 O ANISOU 1249 O GLU A 95 4055 3358 3194 177 952 627 O ATOM 1250 CB GLU A 95 25.340 0.824 -13.483 1.00 33.77 C ANISOU 1250 CB GLU A 95 3503 4757 4570 340 -118 254 C ATOM 1251 CG GLU A 95 26.694 1.245 -14.099 0.50 33.02 C ANISOU 1251 CG GLU A 95 3609 4687 4247 227 41 -76 C ATOM 1252 CD GLU A 95 27.728 1.725 -13.095 0.50 32.53 C ANISOU 1252 CD GLU A 95 4180 3773 4404 -68 -223 170 C ATOM 1253 OE1 GLU A 95 27.885 1.101 -12.028 0.50 30.16 O ANISOU 1253 OE1 GLU A 95 3604 4622 3230 -66 996 -219 O ATOM 1254 OE2 GLU A 95 28.410 2.730 -13.397 0.50 30.36 O ANISOU 1254 OE2 GLU A 95 3600 3742 4191 471 -432 821 O ATOM 1255 H GLU A 95 22.831 0.298 -13.220 1.00 22.95 H ANISOU 1255 H GLU A 95 3360 2693 2666 339 -213 316 H ATOM 1256 HA GLU A 95 24.244 2.308 -14.347 1.00 28.59 H ANISOU 1256 HA GLU A 95 3210 4287 3364 -54 225 136 H ATOM 1257 HB2 GLU A 95 25.283 1.192 -12.589 1.00 30.60 H ANISOU 1257 HB2 GLU A 95 3207 4083 4334 47 -184 460 H ATOM 1258 HB3 GLU A 95 25.311 -0.145 -13.448 1.00 32.28 H ANISOU 1258 HB3 GLU A 95 3636 4646 3981 262 -128 123 H ATOM 1259 HG2 GLU A 95 27.071 0.487 -14.573 0.50 32.08 H ANISOU 1259 HG2 GLU A 95 3850 4253 4084 -48 45 43 H ATOM 1260 HG3 GLU A 95 26.552 1.978 -14.715 0.50 32.51 H ANISOU 1260 HG3 GLU A 95 3854 4293 4203 54 -28 -253 H ATOM 1261 N GLU A 96 24.794 1.536 -16.579 1.00 26.71 N ANISOU 1261 N GLU A 96 3586 3548 3011 -557 558 -489 N ATOM 1262 CA GLU A 96 24.872 1.189 -17.982 1.00 24.42 C ANISOU 1262 CA GLU A 96 3246 3096 2936 -46 370 -525 C ATOM 1263 C GLU A 96 26.142 1.841 -18.498 1.00 24.15 C ANISOU 1263 C GLU A 96 3524 2609 3040 -15 419 -196 C ATOM 1264 O GLU A 96 26.819 2.571 -17.754 1.00 23.64 O ANISOU 1264 O GLU A 96 3184 2507 3288 186 502 -319 O ATOM 1265 CB GLU A 96 23.647 1.731 -18.695 1.00 25.90 C ANISOU 1265 CB GLU A 96 3462 3278 3101 167 549 78 C ATOM 1266 CG GLU A 96 23.417 3.156 -18.317 1.00 28.62 C ANISOU 1266 CG GLU A 96 4069 3144 3661 -3 -36 154 C ATOM 1267 CD GLU A 96 22.244 3.816 -18.975 1.00 29.17 C ANISOU 1267 CD GLU A 96 4089 3137 3855 -64 -227 578 C ATOM 1268 OE1 GLU A 96 21.226 3.135 -19.223 1.00 38.38 O ANISOU 1268 OE1 GLU A 96 4650 3666 6264 -487 -749 224 O ATOM 1269 OE2 GLU A 96 22.345 5.048 -19.200 1.00 25.78 O ANISOU 1269 OE2 GLU A 96 3505 2742 3547 -108 486 -334 O ATOM 1270 H GLU A 96 25.201 2.267 -16.380 1.00 24.65 H ANISOU 1270 H GLU A 96 3333 3192 2841 -63 -18 -325 H ATOM 1271 HA GLU A 96 24.930 0.219 -18.109 1.00 23.90 H ANISOU 1271 HA GLU A 96 3196 2991 2894 -138 247 -148 H ATOM 1272 HB2 GLU A 96 23.778 1.684 -19.654 1.00 28.24 H ANISOU 1272 HB2 GLU A 96 3860 3821 3049 -96 200 25 H ATOM 1273 HB3 GLU A 96 22.870 1.213 -18.433 1.00 25.89 H ANISOU 1273 HB3 GLU A 96 3349 3241 3247 -16 98 -1 H ATOM 1274 HG2 GLU A 96 23.272 3.216 -17.361 1.00 25.16 H ANISOU 1274 HG2 GLU A 96 3129 2771 3660 24 -31 -30 H ATOM 1275 HG3 GLU A 96 24.203 3.656 -18.570 1.00 27.22 H ANISOU 1275 HG3 GLU A 96 3889 3267 3186 117 52 -30 H ATOM 1276 N SER A 97 26.475 1.553 -19.754 1.00 25.26 N ANISOU 1276 N SER A 97 3754 2590 3251 -269 729 -412 N ATOM 1277 CA SER A 97 27.645 2.135 -20.395 1.00 25.34 C ANISOU 1277 CA SER A 97 3595 2615 3418 -204 590 -123 C ATOM 1278 C SER A 97 27.535 3.661 -20.463 1.00 25.89 C ANISOU 1278 C SER A 97 3112 2666 4056 -46 861 -55 C ATOM 1279 O SER A 97 26.436 4.209 -20.595 1.00 25.67 O ANISOU 1279 O SER A 97 3308 2921 3524 33 580 167 O ATOM 1280 CB SER A 97 27.808 1.581 -21.816 1.00 27.86 C ANISOU 1280 CB SER A 97 4042 3226 3317 -365 714 -269 C ATOM 1281 OG SER A 97 26.785 2.077 -22.661 1.00 35.69 O ANISOU 1281 OG SER A 97 4505 4705 4347 33 3 -522 O ATOM 1282 H SER A 97 26.028 1.017 -20.258 1.00 24.24 H ANISOU 1282 H SER A 97 3179 3047 2983 -69 282 -155 H ATOM 1283 HA SER A 97 28.445 1.902 -19.879 1.00 25.94 H ANISOU 1283 HA SER A 97 3675 2687 3492 -119 458 -71 H ATOM 1284 HB2 SER A 97 28.669 1.858 -22.167 1.00 28.23 H ANISOU 1284 HB2 SER A 97 3973 3456 3294 -297 604 -96 H ATOM 1285 HB3 SER A 97 27.757 0.613 -21.790 1.00 29.58 H ANISOU 1285 HB3 SER A 97 4362 3291 3585 -579 482 -577 H ATOM 1286 N CYS A 98 28.681 4.330 -20.373 1.00 24.70 N ANISOU 1286 N CYS A 98 2983 2411 3990 188 729 204 N ATOM 1287 CA CYS A 98 28.733 5.777 -20.516 1.00 21.03 C ANISOU 1287 CA CYS A 98 2809 2458 2721 207 532 286 C ATOM 1288 C CYS A 98 28.326 6.183 -21.921 1.00 21.74 C ANISOU 1288 C CYS A 98 3047 2513 2698 -12 324 64 C ATOM 1289 O CYS A 98 28.904 5.725 -22.902 1.00 25.20 O ANISOU 1289 O CYS A 98 3787 2906 2878 276 569 118 O ATOM 1290 CB CYS A 98 30.141 6.299 -20.222 1.00 20.67 C ANISOU 1290 CB CYS A 98 2932 2756 2166 96 566 522 C ATOM 1291 SG CYS A 98 30.307 8.094 -20.331 1.00 22.30 S ANISOU 1291 SG CYS A 98 3019 2679 2773 331 534 475 S ATOM 1292 H CYS A 98 29.445 3.963 -20.229 1.00 22.77 H ANISOU 1292 H CYS A 98 3151 2370 3129 151 251 133 H ATOM 1293 HA CYS A 98 28.115 6.186 -19.877 1.00 20.87 H ANISOU 1293 HA CYS A 98 2728 2552 2648 228 254 24 H ATOM 1294 HB2 CYS A 98 30.389 6.034 -19.322 1.00 21.98 H ANISOU 1294 HB2 CYS A 98 3301 2678 2372 288 172 411 H ATOM 1295 HB3 CYS A 98 30.758 5.907 -20.860 1.00 20.94 H ANISOU 1295 HB3 CYS A 98 2692 2767 2495 213 264 110 H ATOM 1296 N LYS A 99 27.331 7.057 -21.998 1.00 21.93 N ANISOU 1296 N LYS A 99 2965 2702 2664 30 257 245 N ATOM 1297 CA LYS A 99 26.776 7.514 -23.261 1.00 22.21 C ANISOU 1297 CA LYS A 99 3369 2474 2594 54 57 45 C ATOM 1298 C LYS A 99 26.905 9.029 -23.384 1.00 19.64 C ANISOU 1298 C LYS A 99 2626 2452 2383 300 20 -215 C ATOM 1299 O LYS A 99 26.170 9.653 -24.134 1.00 21.27 O ANISOU 1299 O LYS A 99 2976 2632 2472 149 -25 252 O ATOM 1300 CB LYS A 99 25.299 7.116 -23.371 1.00 27.18 C ANISOU 1300 CB LYS A 99 3296 3414 3616 -23 -215 275 C ATOM 1301 CG LYS A 99 25.063 5.617 -23.508 1.00 31.21 C ANISOU 1301 CG LYS A 99 4046 3663 4146 -636 -436 139 C ATOM 1302 CD LYS A 99 23.627 5.239 -23.118 1.00 34.55 C ANISOU 1302 CD LYS A 99 4041 4095 4991 -863 -413 -66 C ATOM 1303 CE LYS A 99 23.443 3.734 -23.027 0.50 33.08 C ANISOU 1303 CE LYS A 99 3980 3982 4606 -440 -108 38 C ATOM 1304 NZ LYS A 99 24.390 3.121 -22.075 0.50 31.39 N ANISOU 1304 NZ LYS A 99 4236 4061 3627 -1029 50 445 N ATOM 1305 H LYS A 99 26.949 7.412 -21.314 1.00 21.07 H ANISOU 1305 H LYS A 99 2755 2618 2631 18 43 107 H ATOM 1306 HA LYS A 99 27.255 7.108 -24.013 1.00 22.03 H ANISOU 1306 HA LYS A 99 3402 2282 2683 128 -89 -119 H ATOM 1307 HB2 LYS A 99 24.836 7.422 -22.576 1.00 27.08 H ANISOU 1307 HB2 LYS A 99 3183 3687 3417 -246 -161 381 H ATOM 1308 HB3 LYS A 99 24.913 7.535 -24.156 1.00 27.26 H ANISOU 1308 HB3 LYS A 99 3329 3720 3307 114 -118 39 H ATOM 1309 HG2 LYS A 99 25.205 5.356 -24.431 1.00 31.86 H ANISOU 1309 HG2 LYS A 99 4396 3513 4196 -103 -386 64 H ATOM 1310 HG3 LYS A 99 25.680 5.146 -22.929 1.00 29.11 H ANISOU 1310 HG3 LYS A 99 3983 3220 3857 -155 155 29 H ATOM 1311 HD2 LYS A 99 23.418 5.619 -22.251 1.00 32.96 H ANISOU 1311 HD2 LYS A 99 3997 3812 4714 -263 -267 337 H ATOM 1312 HD3 LYS A 99 23.014 5.579 -23.789 1.00 32.34 H ANISOU 1312 HD3 LYS A 99 3878 3949 4457 -262 216 -90 H ATOM 1313 HE2 LYS A 99 22.542 3.541 -22.725 0.50 32.38 H ANISOU 1313 HE2 LYS A 99 4202 3713 4388 -389 147 72 H ATOM 1314 HE3 LYS A 99 23.595 3.341 -23.901 0.50 30.81 H ANISOU 1314 HE3 LYS A 99 3534 3921 4249 -138 -257 321 H ATOM 1315 N TYR A 100 27.853 9.624 -22.667 1.00 17.54 N ANISOU 1315 N TYR A 100 2572 2403 1686 25 300 251 N ATOM 1316 CA TYR A 100 28.081 11.078 -22.773 1.00 16.79 C ANISOU 1316 CA TYR A 100 2565 2382 1430 175 215 72 C ATOM 1317 C TYR A 100 28.282 11.481 -24.221 1.00 17.40 C ANISOU 1317 C TYR A 100 2781 2236 1593 199 469 181 C ATOM 1318 O TYR A 100 29.055 10.853 -24.960 1.00 19.71 O ANISOU 1318 O TYR A 100 3324 2576 1590 418 677 191 O ATOM 1319 CB TYR A 100 29.313 11.498 -21.970 1.00 17.56 C ANISOU 1319 CB TYR A 100 2416 2324 1930 93 179 279 C ATOM 1320 CG TYR A 100 29.662 12.954 -22.154 1.00 17.95 C ANISOU 1320 CG TYR A 100 2342 2273 2204 161 245 334 C ATOM 1321 CD1 TYR A 100 28.872 13.951 -21.597 1.00 16.42 C ANISOU 1321 CD1 TYR A 100 2055 2315 1868 26 42 263 C ATOM 1322 CD2 TYR A 100 30.757 13.338 -22.936 1.00 17.48 C ANISOU 1322 CD2 TYR A 100 2484 2451 1706 -19 261 -125 C ATOM 1323 CE1 TYR A 100 29.167 15.295 -21.786 1.00 17.34 C ANISOU 1323 CE1 TYR A 100 2214 2283 2091 70 113 174 C ATOM 1324 CE2 TYR A 100 31.066 14.679 -23.120 1.00 18.42 C ANISOU 1324 CE2 TYR A 100 2387 2453 2157 66 241 265 C ATOM 1325 CZ TYR A 100 30.270 15.659 -22.539 1.00 17.06 C ANISOU 1325 CZ TYR A 100 2332 2221 1926 -43 102 262 C ATOM 1326 OH TYR A 100 30.559 17.001 -22.700 1.00 18.31 O ANISOU 1326 OH TYR A 100 2738 2270 1946 -10 256 342 O ATOM 1327 H TYR A 100 28.380 9.226 -22.117 1.00 18.41 H ANISOU 1327 H TYR A 100 2454 2315 2226 139 121 149 H ATOM 1328 HA TYR A 100 27.303 11.553 -22.414 1.00 16.53 H ANISOU 1328 HA TYR A 100 2313 2370 1596 -38 333 200 H ATOM 1329 HB2 TYR A 100 29.139 11.350 -21.027 1.00 16.31 H ANISOU 1329 HB2 TYR A 100 2136 2190 1871 -20 16 144 H ATOM 1330 HB3 TYR A 100 30.072 10.966 -22.254 1.00 17.62 H ANISOU 1330 HB3 TYR A 100 2435 2214 2045 -4 211 94 H ATOM 1331 HD1 TYR A 100 28.132 13.712 -21.089 1.00 16.75 H ANISOU 1331 HD1 TYR A 100 2038 2429 1894 -38 32 161 H ATOM 1332 HD2 TYR A 100 31.297 12.687 -23.323 1.00 17.78 H ANISOU 1332 HD2 TYR A 100 2211 2467 2075 109 82 -36 H ATOM 1333 HE1 TYR A 100 28.637 15.948 -21.389 1.00 17.20 H ANISOU 1333 HE1 TYR A 100 2165 2307 2063 22 0 51 H ATOM 1334 HE2 TYR A 100 31.807 14.921 -23.628 1.00 18.02 H ANISOU 1334 HE2 TYR A 100 2169 2582 2095 -41 59 103 H ATOM 1335 N ASN A 101 27.590 12.539 -24.623 1.00 18.11 N ANISOU 1335 N ASN A 101 2818 2252 1811 138 305 240 N ATOM 1336 CA ASN A 101 27.757 13.127 -25.957 1.00 17.87 C ANISOU 1336 CA ASN A 101 2511 2486 1790 182 254 290 C ATOM 1337 C ASN A 101 28.040 14.608 -25.773 1.00 18.54 C ANISOU 1337 C ASN A 101 2509 2480 2055 59 225 307 C ATOM 1338 O ASN A 101 27.181 15.315 -25.232 1.00 17.17 O ANISOU 1338 O ASN A 101 2674 2461 1385 118 172 367 O ATOM 1339 CB ASN A 101 26.485 12.930 -26.793 1.00 18.55 C ANISOU 1339 CB ASN A 101 2688 2568 1791 -35 221 340 C ATOM 1340 CG ASN A 101 26.673 13.337 -28.255 1.00 19.23 C ANISOU 1340 CG ASN A 101 2895 2703 1708 13 -160 467 C ATOM 1341 OD1 ASN A 101 27.487 14.218 -28.561 1.00 21.84 O ANISOU 1341 OD1 ASN A 101 3385 2965 1946 -178 285 523 O ATOM 1342 ND2 ASN A 101 25.923 12.713 -29.149 1.00 25.01 N ANISOU 1342 ND2 ASN A 101 3552 3381 2567 -245 -506 -60 N ATOM 1343 H ASN A 101 27.004 12.945 -24.141 1.00 16.71 H ANISOU 1343 H ASN A 101 2296 2221 1831 -13 193 314 H ATOM 1344 HA ASN A 101 28.501 12.702 -26.428 1.00 18.54 H ANISOU 1344 HA ASN A 101 2556 2563 1925 77 362 179 H ATOM 1345 HB2 ASN A 101 26.240 11.992 -26.772 1.00 18.59 H ANISOU 1345 HB2 ASN A 101 2761 2477 1824 79 103 330 H ATOM 1346 HB3 ASN A 101 25.768 13.467 -26.421 1.00 18.41 H ANISOU 1346 HB3 ASN A 101 2487 2430 2075 -93 68 232 H ATOM 1347 N PRO A 102 29.229 15.095 -26.194 1.00 17.33 N ANISOU 1347 N PRO A 102 2639 2546 1398 100 158 260 N ATOM 1348 CA PRO A 102 29.521 16.516 -25.992 1.00 18.78 C ANISOU 1348 CA PRO A 102 2379 2630 2125 -145 223 389 C ATOM 1349 C PRO A 102 28.554 17.470 -26.697 1.00 17.98 C ANISOU 1349 C PRO A 102 2525 2384 1921 -194 312 353 C ATOM 1350 O PRO A 102 28.400 18.603 -26.253 1.00 20.04 O ANISOU 1350 O PRO A 102 2820 2441 2352 110 376 363 O ATOM 1351 CB PRO A 102 30.945 16.672 -26.546 1.00 19.03 C ANISOU 1351 CB PRO A 102 2443 2847 1940 -253 280 456 C ATOM 1352 CG PRO A 102 31.131 15.524 -27.444 1.00 21.23 C ANISOU 1352 CG PRO A 102 2659 3003 2404 -100 248 115 C ATOM 1353 CD PRO A 102 30.326 14.406 -26.899 1.00 19.17 C ANISOU 1353 CD PRO A 102 2317 2838 2128 136 81 124 C ATOM 1354 HA PRO A 102 29.525 16.725 -25.037 1.00 17.32 H ANISOU 1354 HA PRO A 102 2022 2326 2231 18 180 154 H ATOM 1355 HB2 PRO A 102 31.025 17.507 -27.035 1.00 19.16 H ANISOU 1355 HB2 PRO A 102 2371 2684 2225 -283 141 381 H ATOM 1356 HB3 PRO A 102 31.583 16.641 -25.816 1.00 19.51 H ANISOU 1356 HB3 PRO A 102 2371 2635 2404 42 47 262 H ATOM 1357 HG2 PRO A 102 30.822 15.759 -28.333 1.00 19.62 H ANISOU 1357 HG2 PRO A 102 2482 2489 2482 -99 137 45 H ATOM 1358 HG3 PRO A 102 32.070 15.283 -27.466 1.00 20.47 H ANISOU 1358 HG3 PRO A 102 2604 2734 2437 -197 12 125 H ATOM 1359 HD2 PRO A 102 29.982 13.862 -27.625 1.00 18.47 H ANISOU 1359 HD2 PRO A 102 2345 2540 2132 340 152 53 H ATOM 1360 HD3 PRO A 102 30.853 13.880 -26.277 1.00 19.86 H ANISOU 1360 HD3 PRO A 102 2499 2684 2362 123 -108 49 H ATOM 1361 N ALYS A 103 27.905 16.998 -27.765 0.60 19.67 N ANISOU 1361 N ALYS A 103 2662 2632 2177 106 40 208 N ATOM 1362 CA ALYS A 103 26.908 17.803 -28.501 0.60 20.10 C ANISOU 1362 CA ALYS A 103 2678 2737 2221 66 104 467 C ATOM 1363 C ALYS A 103 25.758 18.244 -27.584 0.60 19.03 C ANISOU 1363 C ALYS A 103 2591 2498 2139 81 22 575 C ATOM 1364 O ALYS A 103 25.109 19.265 -27.841 0.60 20.09 O ANISOU 1364 O ALYS A 103 2809 2552 2269 189 36 611 O ATOM 1365 CB ALYS A 103 26.318 17.015 -29.688 0.60 23.81 C ANISOU 1365 CB ALYS A 103 3249 3094 2703 73 -282 81 C ATOM 1366 CG ALYS A 103 27.324 16.414 -30.701 0.60 27.08 C ANISOU 1366 CG ALYS A 103 3477 3740 3072 -14 81 -68 C ATOM 1367 CD ALYS A 103 27.606 17.327 -31.867 0.60 28.35 C ANISOU 1367 CD ALYS A 103 3714 3757 3298 -130 -140 209 C ATOM 1368 H ALYS A 103 28.020 16.211 -28.085 0.60 19.64 H ANISOU 1368 H ALYS A 103 2552 2595 2314 -9 -36 138 H ATOM 1369 HA ALYS A 103 27.343 18.608 -28.854 0.60 20.10 H ANISOU 1369 HA ALYS A 103 2580 2630 2426 120 198 342 H ATOM 1370 HB2ALYS A 103 25.799 16.277 -29.331 0.60 23.51 H ANISOU 1370 HB2ALYS A 103 3181 2942 2809 136 -195 6 H ATOM 1371 HB3ALYS A 103 25.729 17.608 -30.181 0.60 23.57 H ANISOU 1371 HB3ALYS A 103 3181 3105 2669 -94 -325 132 H ATOM 1372 HG2ALYS A 103 28.167 16.234 -30.260 0.60 25.62 H ANISOU 1372 HG2ALYS A 103 3363 3238 3133 -53 170 23 H ATOM 1373 HG3ALYS A 103 26.955 15.589 -31.054 0.60 25.54 H ANISOU 1373 HG3ALYS A 103 3220 3475 3007 239 65 0 H ATOM 1374 HD2ALYS A 103 26.784 17.467 -32.362 0.60 27.05 H ANISOU 1374 HD2ALYS A 103 3438 3483 3356 12 74 47 H ATOM 1375 HD3ALYS A 103 27.940 18.173 -31.532 0.60 27.44 H ANISOU 1375 HD3ALYS A 103 3372 3633 3419 131 -32 65 H ATOM 1376 N BLYS A 103 27.914 17.026 -27.776 0.40 19.71 N ANISOU 1376 N BLYS A 103 2596 2623 2267 95 32 176 N ATOM 1377 CA BLYS A 103 26.936 17.867 -28.475 0.40 19.74 C ANISOU 1377 CA BLYS A 103 2617 2602 2278 15 89 402 C ATOM 1378 C BLYS A 103 25.757 18.258 -27.575 0.40 18.69 C ANISOU 1378 C BLYS A 103 2557 2409 2133 26 13 514 C ATOM 1379 O BLYS A 103 25.093 19.267 -27.828 0.40 19.75 O ANISOU 1379 O BLYS A 103 2778 2502 2224 167 88 566 O ATOM 1380 CB BLYS A 103 26.413 17.158 -29.727 0.40 22.24 C ANISOU 1380 CB BLYS A 103 3153 2743 2555 95 -149 111 C ATOM 1381 CG BLYS A 103 27.496 16.713 -30.705 0.40 24.71 C ANISOU 1381 CG BLYS A 103 3178 3379 2828 44 72 107 C ATOM 1382 CD BLYS A 103 28.183 17.883 -31.354 0.40 24.28 C ANISOU 1382 CD BLYS A 103 2968 3156 3100 156 64 12 C ATOM 1383 CE BLYS A 103 29.057 17.435 -32.505 0.40 23.80 C ANISOU 1383 CE BLYS A 103 2793 3489 2758 197 -12 368 C ATOM 1384 NZ BLYS A 103 28.291 16.590 -33.439 0.40 25.54 N ANISOU 1384 NZ BLYS A 103 3059 3350 3292 -131 357 -26 N ATOM 1385 H BLYS A 103 28.026 16.252 -28.133 0.40 19.23 H ANISOU 1385 H BLYS A 103 2429 2570 2305 -27 -21 152 H ATOM 1386 HA BLYS A 103 27.379 18.692 -28.762 0.40 19.82 H ANISOU 1386 HA BLYS A 103 2491 2537 2500 44 185 257 H ATOM 1387 HB2BLYS A 103 25.923 16.367 -29.452 0.40 22.25 H ANISOU 1387 HB2BLYS A 103 2980 2769 2703 82 -101 50 H ATOM 1388 HB3BLYS A 103 25.820 17.762 -30.200 0.40 22.15 H ANISOU 1388 HB3BLYS A 103 2998 2836 2578 -38 -244 111 H ATOM 1389 HG2BLYS A 103 28.165 16.197 -30.229 0.40 24.26 H ANISOU 1389 HG2BLYS A 103 3047 3128 3042 1 56 -14 H ATOM 1390 HG3BLYS A 103 27.093 16.173 -31.403 0.40 23.73 H ANISOU 1390 HG3BLYS A 103 3010 3098 2906 191 156 19 H ATOM 1391 HD2BLYS A 103 27.505 18.472 -31.710 0.40 24.22 H ANISOU 1391 HD2BLYS A 103 2979 3102 3120 92 -2 -19 H ATOM 1392 HD3BLYS A 103 28.734 18.344 -30.703 0.40 24.96 H ANISOU 1392 HD3BLYS A 103 3082 3306 3092 105 -30 57 H ATOM 1393 HE2BLYS A 103 29.379 18.213 -32.988 0.40 23.91 H ANISOU 1393 HE2BLYS A 103 3056 3058 2970 148 -33 114 H ATOM 1394 HE3BLYS A 103 29.802 16.917 -32.163 0.40 24.92 H ANISOU 1394 HE3BLYS A 103 2940 2994 3535 306 68 225 H ATOM 1395 N TYR A 104 25.499 17.476 -26.527 1.00 17.33 N ANISOU 1395 N TYR A 104 2633 2324 1624 18 -136 200 N ATOM 1396 CA TYR A 104 24.369 17.760 -25.624 1.00 17.39 C ANISOU 1396 CA TYR A 104 2480 2258 1867 98 -93 120 C ATOM 1397 C TYR A 104 24.810 18.322 -24.285 1.00 15.85 C ANISOU 1397 C TYR A 104 2200 2002 1821 -171 245 162 C ATOM 1398 O TYR A 104 24.024 18.398 -23.354 1.00 16.28 O ANISOU 1398 O TYR A 104 2298 2279 1607 51 179 287 O ATOM 1399 CB TYR A 104 23.468 16.514 -25.467 1.00 18.69 C ANISOU 1399 CB TYR A 104 2464 2188 2447 104 -1 -33 C ATOM 1400 CG TYR A 104 23.050 15.930 -26.820 1.00 18.77 C ANISOU 1400 CG TYR A 104 2891 2316 1924 -306 30 420 C ATOM 1401 CD1 TYR A 104 22.703 16.771 -27.884 1.00 20.70 C ANISOU 1401 CD1 TYR A 104 3435 2167 2261 5 -407 331 C ATOM 1402 CD2 TYR A 104 23.057 14.567 -27.065 1.00 18.95 C ANISOU 1402 CD2 TYR A 104 3022 2406 1769 170 -88 308 C ATOM 1403 CE1 TYR A 104 22.352 16.265 -29.152 1.00 22.16 C ANISOU 1403 CE1 TYR A 104 3148 2517 2751 -136 -895 125 C ATOM 1404 CE2 TYR A 104 22.702 14.053 -28.324 1.00 19.96 C ANISOU 1404 CE2 TYR A 104 3035 2490 2057 138 -243 54 C ATOM 1405 CZ TYR A 104 22.359 14.915 -29.372 1.00 20.00 C ANISOU 1405 CZ TYR A 104 2988 2592 2019 74 -461 -15 C ATOM 1406 OH TYR A 104 22.014 14.435 -30.620 1.00 25.64 O ANISOU 1406 OH TYR A 104 3820 3461 2458 -201 -897 -378 O ATOM 1407 H TYR A 104 25.943 16.776 -26.307 1.00 16.91 H ANISOU 1407 H TYR A 104 2472 2178 1773 -53 112 237 H ATOM 1408 HA TYR A 104 23.797 18.453 -26.011 1.00 18.62 H ANISOU 1408 HA TYR A 104 2565 2315 2194 88 -163 242 H ATOM 1409 HB2 TYR A 104 23.953 15.830 -24.979 1.00 17.51 H ANISOU 1409 HB2 TYR A 104 2324 2241 2086 -63 -20 -13 H ATOM 1410 HB3 TYR A 104 22.664 16.760 -24.985 1.00 18.83 H ANISOU 1410 HB3 TYR A 104 2374 2470 2310 51 -40 26 H ATOM 1411 HD1 TYR A 104 22.702 17.691 -27.760 1.00 19.43 H ANISOU 1411 HD1 TYR A 104 2837 2210 2335 107 -164 226 H ATOM 1412 HD2 TYR A 104 23.293 13.981 -26.382 1.00 18.23 H ANISOU 1412 HD2 TYR A 104 2556 2333 2038 345 -141 276 H ATOM 1413 HE1 TYR A 104 22.121 16.848 -29.838 1.00 20.48 H ANISOU 1413 HE1 TYR A 104 2929 2572 2277 44 -379 0 H ATOM 1414 HE2 TYR A 104 22.710 13.134 -28.467 1.00 20.76 H ANISOU 1414 HE2 TYR A 104 2989 2467 2432 34 -205 17 H ATOM 1415 N SER A 105 26.065 18.731 -24.176 1.00 15.56 N ANISOU 1415 N SER A 105 2185 2010 1717 -31 133 37 N ATOM 1416 CA SER A 105 26.536 19.318 -22.944 1.00 16.02 C ANISOU 1416 CA SER A 105 2360 1942 1782 -236 188 19 C ATOM 1417 C SER A 105 25.911 20.697 -22.735 1.00 15.78 C ANISOU 1417 C SER A 105 2193 2008 1793 -135 172 299 C ATOM 1418 O SER A 105 25.894 21.512 -23.665 1.00 16.88 O ANISOU 1418 O SER A 105 2688 2330 1393 -38 75 231 O ATOM 1419 CB SER A 105 28.053 19.445 -22.932 1.00 17.99 C ANISOU 1419 CB SER A 105 2302 2386 2144 8 -84 186 C ATOM 1420 OG SER A 105 28.455 20.059 -21.726 1.00 16.84 O ANISOU 1420 OG SER A 105 2292 2206 1900 -32 42 346 O ATOM 1421 H SER A 105 26.658 18.685 -24.796 1.00 15.49 H ANISOU 1421 H SER A 105 2002 2073 1809 2 77 -25 H ATOM 1422 HA SER A 105 26.281 18.739 -22.197 1.00 16.18 H ANISOU 1422 HA SER A 105 2404 1981 1760 -27 -62 186 H ATOM 1423 HB2 SER A 105 28.448 18.561 -22.991 1.00 18.14 H ANISOU 1423 HB2 SER A 105 2354 2265 2271 -130 25 139 H ATOM 1424 HB3 SER A 105 28.336 19.991 -23.682 1.00 16.12 H ANISOU 1424 HB3 SER A 105 1964 2182 1976 -18 -19 -55 H ATOM 1425 N VAL A 106 25.461 20.956 -21.508 1.00 14.82 N ANISOU 1425 N VAL A 106 2231 1861 1538 -17 -73 493 N ATOM 1426 CA VAL A 106 24.859 22.234 -21.142 1.00 14.50 C ANISOU 1426 CA VAL A 106 2392 2171 944 141 38 377 C ATOM 1427 C VAL A 106 25.506 22.853 -19.894 1.00 14.87 C ANISOU 1427 C VAL A 106 2360 2001 1285 95 -68 357 C ATOM 1428 O VAL A 106 25.087 23.907 -19.454 1.00 15.89 O ANISOU 1428 O VAL A 106 2399 1919 1719 121 -266 228 O ATOM 1429 CB VAL A 106 23.313 22.117 -20.944 1.00 16.01 C ANISOU 1429 CB VAL A 106 2301 2113 1667 74 -245 493 C ATOM 1430 CG1 VAL A 106 22.603 21.699 -22.235 1.00 17.71 C ANISOU 1430 CG1 VAL A 106 2509 2561 1659 107 -329 506 C ATOM 1431 CG2 VAL A 106 22.982 21.136 -19.811 1.00 17.70 C ANISOU 1431 CG2 VAL A 106 2453 2558 1712 -160 149 574 C ATOM 1432 H VAL A 106 25.490 20.387 -20.865 1.00 15.42 H ANISOU 1432 H VAL A 106 2481 1764 1613 -318 -218 461 H ATOM 1433 HA VAL A 106 25.006 22.875 -21.869 1.00 14.87 H ANISOU 1433 HA VAL A 106 2538 1730 1383 -156 -255 422 H ATOM 1434 HB VAL A 106 22.961 22.994 -20.688 1.00 17.13 H ANISOU 1434 HB VAL A 106 2162 2159 2187 -35 -46 282 H ATOM 1435 N ALA A 107 26.519 22.211 -19.314 1.00 15.24 N ANISOU 1435 N ALA A 107 2292 1796 1702 65 -192 292 N ATOM 1436 CA ALA A 107 27.142 22.700 -18.100 1.00 15.11 C ANISOU 1436 CA ALA A 107 2152 1896 1692 -120 -57 211 C ATOM 1437 C ALA A 107 28.617 22.367 -18.110 1.00 15.75 C ANISOU 1437 C ALA A 107 2116 2208 1659 -168 53 229 C ATOM 1438 O ALA A 107 29.055 21.470 -18.802 1.00 17.66 O ANISOU 1438 O ALA A 107 2054 2230 2425 89 -65 74 O ATOM 1439 CB ALA A 107 26.463 22.097 -16.865 1.00 15.85 C ANISOU 1439 CB ALA A 107 2012 2213 1797 -168 -80 397 C ATOM 1440 H ALA A 107 26.870 21.484 -19.607 1.00 15.27 H ANISOU 1440 H ALA A 107 2072 1920 1808 -29 -71 117 H ATOM 1441 HA ALA A 107 27.058 23.674 -18.050 1.00 15.83 H ANISOU 1441 HA ALA A 107 2311 1892 1810 -148 -59 220 H ATOM 1442 N ASN A 108 29.370 23.118 -17.327 1.00 16.13 N ANISOU 1442 N ASN A 108 2184 1916 2026 7 -288 367 N ATOM 1443 CA ASN A 108 30.801 22.941 -17.198 1.00 16.01 C ANISOU 1443 CA ASN A 108 2112 1970 1999 12 -38 135 C ATOM 1444 C ASN A 108 31.169 23.365 -15.785 1.00 16.03 C ANISOU 1444 C ASN A 108 2100 1994 1995 -146 -27 177 C ATOM 1445 O ASN A 108 30.421 24.087 -15.103 1.00 16.12 O ANISOU 1445 O ASN A 108 2378 2585 1160 -7 -174 280 O ATOM 1446 CB ASN A 108 31.563 23.822 -18.194 1.00 18.28 C ANISOU 1446 CB ASN A 108 2345 2437 2164 -1 7 443 C ATOM 1447 CG ASN A 108 31.354 23.409 -19.641 0.50 17.92 C ANISOU 1447 CG ASN A 108 2235 2437 2135 -244 175 431 C ATOM 1448 OD1 ASN A 108 30.538 23.997 -20.354 0.50 19.64 O ANISOU 1448 OD1 ASN A 108 2619 2552 2291 -261 -135 487 O ATOM 1449 ND2 ASN A 108 32.083 22.398 -20.073 0.50 17.59 N ANISOU 1449 ND2 ASN A 108 2142 2239 2300 -500 90 254 N ATOM 1450 H ASN A 108 29.061 23.763 -16.848 1.00 16.17 H ANISOU 1450 H ASN A 108 1899 2162 2079 -139 -153 157 H ATOM 1451 HA ASN A 108 31.051 22.003 -17.329 1.00 16.66 H ANISOU 1451 HA ASN A 108 2148 2010 2171 26 -38 47 H ATOM 1452 HB2 ASN A 108 31.251 24.735 -18.102 1.00 18.06 H ANISOU 1452 HB2 ASN A 108 2269 2276 2313 -226 14 370 H ATOM 1453 HB3 ASN A 108 32.512 23.781 -18.001 1.00 18.19 H ANISOU 1453 HB3 ASN A 108 2262 2368 2281 -150 124 155 H ATOM 1454 N ASP A 109 32.339 22.943 -15.327 1.00 15.37 N ANISOU 1454 N ASP A 109 2212 2198 1430 -29 106 214 N ATOM 1455 CA ASP A 109 32.863 23.501 -14.079 1.00 16.20 C ANISOU 1455 CA ASP A 109 2413 2129 1612 -56 -89 252 C ATOM 1456 C ASP A 109 34.390 23.448 -14.091 1.00 17.77 C ANISOU 1456 C ASP A 109 2309 2396 2045 35 38 615 C ATOM 1457 O ASP A 109 34.995 22.755 -14.928 1.00 20.09 O ANISOU 1457 O ASP A 109 2351 2800 2481 -124 9 71 O ATOM 1458 CB ASP A 109 32.204 22.958 -12.777 1.00 17.75 C ANISOU 1458 CB ASP A 109 2499 2459 1785 -142 2 456 C ATOM 1459 CG ASP A 109 32.614 21.559 -12.393 1.00 20.13 C ANISOU 1459 CG ASP A 109 2939 2215 2493 -5 214 266 C ATOM 1460 OD1 ASP A 109 33.810 21.227 -12.469 1.00 26.00 O ANISOU 1460 OD1 ASP A 109 2960 3407 3511 481 -404 540 O ATOM 1461 OD2 ASP A 109 31.719 20.841 -11.892 1.00 21.73 O ANISOU 1461 OD2 ASP A 109 3352 2507 2397 -108 223 556 O ATOM 1462 H ASP A 109 32.835 22.350 -15.705 1.00 16.05 H ANISOU 1462 H ASP A 109 2122 2074 1900 -70 1 68 H ATOM 1463 HA ASP A 109 32.653 24.458 -14.086 1.00 15.91 H ANISOU 1463 HA ASP A 109 2191 2087 1765 -152 -14 197 H ATOM 1464 HB2 ASP A 109 32.443 23.532 -12.038 1.00 16.60 H ANISOU 1464 HB2 ASP A 109 2136 2316 1852 145 291 233 H ATOM 1465 HB3 ASP A 109 31.241 22.962 -12.890 1.00 18.52 H ANISOU 1465 HB3 ASP A 109 2430 2483 2121 -97 148 145 H ATOM 1466 N THR A 110 34.967 24.278 -13.229 1.00 20.07 N ANISOU 1466 N THR A 110 2359 2641 2625 -286 27 358 N ATOM 1467 CA THR A 110 36.406 24.538 -13.191 1.00 21.56 C ANISOU 1467 CA THR A 110 2317 3128 2744 -262 137 391 C ATOM 1468 C THR A 110 37.054 23.995 -11.920 1.00 23.36 C ANISOU 1468 C THR A 110 2449 3466 2960 -598 -335 354 C ATOM 1469 O THR A 110 38.174 24.361 -11.580 1.00 28.86 O ANISOU 1469 O THR A 110 2235 4650 4078 -643 -445 435 O ATOM 1470 CB THR A 110 36.678 26.065 -13.260 1.00 24.33 C ANISOU 1470 CB THR A 110 2548 3149 3545 -475 259 508 C ATOM 1471 OG1 THR A 110 35.988 26.731 -12.187 1.00 23.40 O ANISOU 1471 OG1 THR A 110 2839 3073 2978 -760 -35 494 O ATOM 1472 CG2 THR A 110 36.199 26.628 -14.598 1.00 23.61 C ANISOU 1472 CG2 THR A 110 2546 2983 3441 -654 -105 281 C ATOM 1473 H THR A 110 34.532 24.720 -12.633 1.00 19.85 H ANISOU 1473 H THR A 110 2234 2656 2649 -269 -96 212 H ATOM 1474 HA THR A 110 36.847 24.112 -13.956 1.00 22.63 H ANISOU 1474 HA THR A 110 2443 3313 2840 -167 143 287 H ATOM 1475 HB THR A 110 37.630 26.234 -13.187 1.00 24.62 H ANISOU 1475 HB THR A 110 2621 3129 3601 -387 -203 184 H ATOM 1476 N GLY A 111 36.346 23.116 -11.231 1.00 21.07 N ANISOU 1476 N GLY A 111 1945 3474 2586 -34 -110 442 N ATOM 1477 CA GLY A 111 36.786 22.587 -9.951 1.00 21.41 C ANISOU 1477 CA GLY A 111 2226 3492 2415 51 -110 152 C ATOM 1478 C GLY A 111 35.683 22.745 -8.936 1.00 18.32 C ANISOU 1478 C GLY A 111 2059 2672 2229 80 -224 511 C ATOM 1479 O GLY A 111 34.501 22.823 -9.266 1.00 18.56 O ANISOU 1479 O GLY A 111 1973 2602 2474 -247 -303 479 O ATOM 1480 H GLY A 111 35.593 22.791 -11.489 1.00 19.37 H ANISOU 1480 H GLY A 111 2372 2583 2404 -151 -170 158 H ATOM 1481 HA2 GLY A 111 37.574 23.055 -9.634 1.00 19.65 H ANISOU 1481 HA2 GLY A 111 2265 2989 2211 29 27 283 H ATOM 1482 HA3 GLY A 111 36.996 21.644 -10.040 1.00 19.63 H ANISOU 1482 HA3 GLY A 111 2148 3254 2056 -218 39 256 H ATOM 1483 N PHE A 112 36.084 22.789 -7.682 1.00 18.84 N ANISOU 1483 N PHE A 112 1832 3121 2203 -377 -61 289 N ATOM 1484 CA PHE A 112 35.176 22.867 -6.555 1.00 16.03 C ANISOU 1484 CA PHE A 112 2052 2311 1725 -155 -228 443 C ATOM 1485 C PHE A 112 35.844 23.455 -5.309 1.00 17.08 C ANISOU 1485 C PHE A 112 1835 2524 2128 -350 -244 202 C ATOM 1486 O PHE A 112 37.072 23.527 -5.231 1.00 18.13 O ANISOU 1486 O PHE A 112 1800 2882 2203 -558 -273 489 O ATOM 1487 CB PHE A 112 34.594 21.466 -6.240 1.00 18.33 C ANISOU 1487 CB PHE A 112 2029 2198 2736 -202 -335 333 C ATOM 1488 CG PHE A 112 35.650 20.425 -5.929 1.00 17.59 C ANISOU 1488 CG PHE A 112 1941 2173 2569 -213 -190 299 C ATOM 1489 CD1 PHE A 112 36.090 20.236 -4.618 1.00 18.48 C ANISOU 1489 CD1 PHE A 112 2022 2423 2574 -292 -214 377 C ATOM 1490 CD2 PHE A 112 36.201 19.654 -6.938 1.00 19.55 C ANISOU 1490 CD2 PHE A 112 2016 2601 2808 -143 -217 117 C ATOM 1491 CE1 PHE A 112 37.092 19.293 -4.318 1.00 19.32 C ANISOU 1491 CE1 PHE A 112 2445 2479 2414 -93 -158 570 C ATOM 1492 CE2 PHE A 112 37.187 18.724 -6.654 1.00 19.71 C ANISOU 1492 CE2 PHE A 112 2318 2416 2752 16 6 41 C ATOM 1493 CZ PHE A 112 37.633 18.546 -5.342 1.00 20.57 C ANISOU 1493 CZ PHE A 112 2215 2820 2779 -133 28 329 C ATOM 1494 H PHE A 112 36.912 22.770 -7.448 1.00 18.08 H ANISOU 1494 H PHE A 112 1935 2676 2255 -75 -191 155 H ATOM 1495 HA PHE A 112 34.431 23.457 -6.791 1.00 16.31 H ANISOU 1495 HA PHE A 112 2066 2191 1938 -115 -243 205 H ATOM 1496 HB2 PHE A 112 34.010 21.536 -5.469 1.00 16.09 H ANISOU 1496 HB2 PHE A 112 2221 1480 2411 -197 -396 333 H ATOM 1497 HB3 PHE A 112 34.090 21.157 -7.009 1.00 17.36 H ANISOU 1497 HB3 PHE A 112 2056 2140 2398 -23 -96 251 H ATOM 1498 HD1 PHE A 112 35.730 20.755 -3.935 1.00 19.53 H ANISOU 1498 HD1 PHE A 112 2280 2596 2543 -198 -163 320 H ATOM 1499 HD2 PHE A 112 35.921 19.776 -7.817 1.00 19.49 H ANISOU 1499 HD2 PHE A 112 2268 2561 2573 -118 145 276 H ATOM 1500 HE1 PHE A 112 37.381 19.172 -3.442 1.00 19.81 H ANISOU 1500 HE1 PHE A 112 2264 2842 2420 -119 -108 591 H ATOM 1501 HE2 PHE A 112 37.551 18.212 -7.339 1.00 20.40 H ANISOU 1501 HE2 PHE A 112 2449 2546 2754 -56 193 90 H ATOM 1502 HZ PHE A 112 38.282 17.907 -5.156 1.00 21.03 H ANISOU 1502 HZ PHE A 112 2525 2652 2811 -75 -30 304 H ATOM 1503 N VAL A 113 35.014 23.883 -4.361 1.00 16.18 N ANISOU 1503 N VAL A 113 1754 2523 1870 -342 -346 418 N ATOM 1504 CA VAL A 113 35.431 24.431 -3.100 1.00 16.50 C ANISOU 1504 CA VAL A 113 1893 2498 1878 -310 -254 399 C ATOM 1505 C VAL A 113 34.840 23.575 -1.988 1.00 15.80 C ANISOU 1505 C VAL A 113 1784 2335 1883 -313 -378 436 C ATOM 1506 O VAL A 113 33.635 23.322 -1.979 1.00 17.25 O ANISOU 1506 O VAL A 113 1782 2451 2320 -378 -484 698 O ATOM 1507 CB VAL A 113 34.977 25.900 -2.980 1.00 17.52 C ANISOU 1507 CB VAL A 113 2466 2415 1774 -381 -750 448 C ATOM 1508 CG1 VAL A 113 35.226 26.460 -1.586 1.00 19.15 C ANISOU 1508 CG1 VAL A 113 2910 2542 1822 -367 -530 315 C ATOM 1509 CG2 VAL A 113 35.644 26.778 -4.064 1.00 19.19 C ANISOU 1509 CG2 VAL A 113 2642 2182 2467 -463 -103 279 C ATOM 1510 H VAL A 113 34.158 23.860 -4.446 1.00 16.42 H ANISOU 1510 H VAL A 113 1754 2353 2130 -253 -291 292 H ATOM 1511 HA VAL A 113 36.408 24.403 -3.026 1.00 16.72 H ANISOU 1511 HA VAL A 113 1906 2645 1802 -472 -286 269 H ATOM 1512 HB VAL A 113 34.010 25.932 -3.136 1.00 17.02 H ANISOU 1512 HB VAL A 113 2274 2310 1882 -224 -221 56 H ATOM 1513 N ASP A 114 35.692 23.152 -1.049 1.00 18.32 N ANISOU 1513 N ASP A 114 1947 2648 2363 -491 -732 610 N ATOM 1514 CA ASP A 114 35.287 22.450 0.166 1.00 17.88 C ANISOU 1514 CA ASP A 114 1998 2652 2142 -161 -569 470 C ATOM 1515 C ASP A 114 35.192 23.478 1.277 1.00 19.28 C ANISOU 1515 C ASP A 114 2301 2501 2522 -467 -254 307 C ATOM 1516 O ASP A 114 36.157 24.215 1.539 1.00 22.70 O ANISOU 1516 O ASP A 114 2381 3287 2955 -752 -549 149 O ATOM 1517 CB ASP A 114 36.299 21.364 0.549 1.00 18.90 C ANISOU 1517 CB ASP A 114 2125 2806 2248 -97 -524 572 C ATOM 1518 CG ASP A 114 36.272 20.182 -0.389 1.00 20.46 C ANISOU 1518 CG ASP A 114 2071 2632 3069 -98 -729 308 C ATOM 1519 OD1 ASP A 114 35.186 19.834 -0.867 1.00 22.06 O ANISOU 1519 OD1 ASP A 114 1963 3199 3217 -116 -636 -179 O ATOM 1520 OD2 ASP A 114 37.328 19.583 -0.663 1.00 29.56 O ANISOU 1520 OD2 ASP A 114 2230 4208 4791 432 -864 -616 O ATOM 1521 H ASP A 114 36.543 23.269 -1.097 1.00 16.89 H ANISOU 1521 H ASP A 114 1846 2483 2086 -5 -413 207 H ATOM 1522 HA ASP A 114 34.409 22.034 0.043 1.00 17.39 H ANISOU 1522 HA ASP A 114 1974 2371 2263 -130 -277 324 H ATOM 1523 HB2 ASP A 114 37.193 21.740 0.533 1.00 17.49 H ANISOU 1523 HB2 ASP A 114 2067 2334 2245 87 -223 292 H ATOM 1524 HB3 ASP A 114 36.092 21.040 1.440 1.00 19.34 H ANISOU 1524 HB3 ASP A 114 2278 2552 2516 -33 -277 716 H ATOM 1525 N ILE A 115 34.046 23.535 1.941 1.00 17.10 N ANISOU 1525 N ILE A 115 2329 2462 1706 -155 -534 510 N ATOM 1526 CA ILE A 115 33.758 24.554 2.942 1.00 17.88 C ANISOU 1526 CA ILE A 115 2166 2536 2089 -458 -526 201 C ATOM 1527 C ILE A 115 34.314 24.122 4.308 1.00 19.47 C ANISOU 1527 C ILE A 115 2391 3011 1994 -379 -465 180 C ATOM 1528 O ILE A 115 34.227 22.938 4.637 1.00 20.33 O ANISOU 1528 O ILE A 115 2044 3201 2479 -371 -890 757 O ATOM 1529 CB ILE A 115 32.234 24.744 3.009 1.00 18.44 C ANISOU 1529 CB ILE A 115 2191 2841 1975 -383 -562 68 C ATOM 1530 CG1 ILE A 115 31.725 25.301 1.681 1.00 18.42 C ANISOU 1530 CG1 ILE A 115 2312 2771 1912 -174 -588 -60 C ATOM 1531 CG2 ILE A 115 31.822 25.667 4.118 1.00 18.02 C ANISOU 1531 CG2 ILE A 115 2232 2941 1672 -331 -399 339 C ATOM 1532 CD1 ILE A 115 30.265 25.124 1.481 1.00 20.04 C ANISOU 1532 CD1 ILE A 115 2289 2677 2646 -414 -612 363 C ATOM 1533 H ILE A 115 33.405 22.973 1.829 1.00 17.24 H ANISOU 1533 H ILE A 115 2149 2345 2054 -23 -166 145 H ATOM 1534 HA ILE A 115 34.165 25.404 2.675 1.00 18.87 H ANISOU 1534 HA ILE A 115 2252 2424 2493 -217 -201 297 H ATOM 1535 HB ILE A 115 31.825 23.879 3.168 1.00 18.91 H ANISOU 1535 HB ILE A 115 1965 2671 2546 -56 -220 249 H ATOM 1536 HG12 ILE A 115 31.920 26.250 1.631 1.00 17.24 H ANISOU 1536 HG12 ILE A 115 1828 2681 2041 -46 -313 -28 H ATOM 1537 HG13 ILE A 115 32.170 24.842 0.952 1.00 18.50 H ANISOU 1537 HG13 ILE A 115 2553 2476 1998 -238 -322 92 H ATOM 1538 N PRO A 116 34.886 25.063 5.120 1.00 20.53 N ANISOU 1538 N PRO A 116 2619 3074 2105 -464 -850 432 N ATOM 1539 CA PRO A 116 35.266 24.683 6.486 1.00 20.92 C ANISOU 1539 CA PRO A 116 2423 3399 2126 -406 -726 430 C ATOM 1540 C PRO A 116 34.142 24.007 7.262 1.00 20.30 C ANISOU 1540 C PRO A 116 2283 3468 1960 -32 -530 345 C ATOM 1541 O PRO A 116 32.966 24.341 7.078 1.00 21.70 O ANISOU 1541 O PRO A 116 2155 3447 2643 -368 -868 668 O ATOM 1542 CB PRO A 116 35.644 26.020 7.128 1.00 21.71 C ANISOU 1542 CB PRO A 116 2233 3536 2476 -309 -593 1 C ATOM 1543 CG PRO A 116 36.117 26.852 5.996 1.00 22.98 C ANISOU 1543 CG PRO A 116 2665 3018 3047 -449 -672 186 C ATOM 1544 CD PRO A 116 35.216 26.470 4.840 1.00 22.47 C ANISOU 1544 CD PRO A 116 2626 3193 2717 -644 -483 456 C ATOM 1545 HA PRO A 116 36.052 24.098 6.469 1.00 19.58 H ANISOU 1545 HA PRO A 116 2593 3224 1622 -288 -337 527 H ATOM 1546 HB2 PRO A 116 34.868 26.421 7.549 1.00 24.12 H ANISOU 1546 HB2 PRO A 116 2464 3435 3263 75 -415 222 H ATOM 1547 HB3 PRO A 116 36.354 25.884 7.775 1.00 21.61 H ANISOU 1547 HB3 PRO A 116 2303 3507 2399 -70 -538 -185 H ATOM 1548 HG2 PRO A 116 36.022 27.790 6.217 1.00 24.11 H ANISOU 1548 HG2 PRO A 116 2956 3165 3039 -178 -338 -74 H ATOM 1549 HG3 PRO A 116 37.042 26.637 5.797 1.00 21.08 H ANISOU 1549 HG3 PRO A 116 2784 2859 2365 -336 -508 125 H ATOM 1550 HD2 PRO A 116 34.416 27.017 4.843 1.00 20.41 H ANISOU 1550 HD2 PRO A 116 2872 2948 1932 -470 -395 123 H ATOM 1551 HD3 PRO A 116 35.697 26.546 4.001 1.00 21.63 H ANISOU 1551 HD3 PRO A 116 2846 2542 2827 -232 -236 215 H ATOM 1552 N LYS A 117 34.526 23.072 8.136 1.00 21.62 N ANISOU 1552 N LYS A 117 2200 3143 2871 -254 -877 579 N ATOM 1553 CA LYS A 117 33.579 22.161 8.807 1.00 20.81 C ANISOU 1553 CA LYS A 117 2348 2988 2570 -97 -600 352 C ATOM 1554 C LYS A 117 32.905 22.797 10.039 1.00 18.74 C ANISOU 1554 C LYS A 117 2269 2461 2391 -222 -872 175 C ATOM 1555 O LYS A 117 32.999 22.315 11.183 1.00 24.17 O ANISOU 1555 O LYS A 117 2974 3323 2887 197 -646 941 O ATOM 1556 CB LYS A 117 34.282 20.836 9.111 1.00 21.62 C ANISOU 1556 CB LYS A 117 2214 2926 3075 -161 -796 264 C ATOM 1557 CG LYS A 117 34.912 20.183 7.870 1.00 23.65 C ANISOU 1557 CG LYS A 117 2639 3269 3076 1 -622 196 C ATOM 1558 CD LYS A 117 35.678 18.909 8.181 1.00 25.97 C ANISOU 1558 CD LYS A 117 3436 3429 2999 269 -428 363 C ATOM 1559 CE LYS A 117 36.359 18.335 6.947 1.00 31.22 C ANISOU 1559 CE LYS A 117 3816 4046 3999 382 -47 -513 C ATOM 1560 NZ LYS A 117 37.062 17.069 7.262 1.00 42.47 N ANISOU 1560 NZ LYS A 117 5903 3606 6625 496 -141 -280 N ATOM 1561 H LYS A 117 35.344 22.948 8.372 1.00 19.54 H ANISOU 1561 H LYS A 117 2115 2894 2414 158 -461 82 H ATOM 1562 HA LYS A 117 32.867 21.958 8.171 1.00 18.83 H ANISOU 1562 HA LYS A 117 2218 2603 2332 -81 -353 176 H ATOM 1563 HB2 LYS A 117 34.990 20.997 9.755 1.00 21.52 H ANISOU 1563 HB2 LYS A 117 2161 3333 2681 -42 -606 391 H ATOM 1564 HB3 LYS A 117 33.636 20.214 9.480 1.00 22.61 H ANISOU 1564 HB3 LYS A 117 2543 2703 3342 -167 -426 89 H ATOM 1565 HG2 LYS A 117 34.207 19.960 7.241 1.00 23.94 H ANISOU 1565 HG2 LYS A 117 2626 3596 2873 -144 -448 173 H ATOM 1566 HG3 LYS A 117 35.534 20.803 7.460 1.00 23.91 H ANISOU 1566 HG3 LYS A 117 2765 3055 3264 -29 -423 -11 H ATOM 1567 HD2 LYS A 117 36.362 19.102 8.841 1.00 24.65 H ANISOU 1567 HD2 LYS A 117 2914 3157 3294 315 -294 407 H ATOM 1568 HD3 LYS A 117 35.061 18.243 8.523 1.00 26.77 H ANISOU 1568 HD3 LYS A 117 3414 3099 3658 129 -415 -7 H ATOM 1569 HE2 LYS A 117 35.691 18.153 6.266 1.00 33.28 H ANISOU 1569 HE2 LYS A 117 4308 4852 3485 -305 154 -506 H ATOM 1570 HE3 LYS A 117 37.012 18.971 6.616 1.00 29.47 H ANISOU 1570 HE3 LYS A 117 3875 4007 3313 421 -86 -308 H ATOM 1571 N GLN A 118 32.232 23.910 9.783 1.00 19.37 N ANISOU 1571 N GLN A 118 1944 2881 2535 -46 -852 355 N ATOM 1572 CA GLN A 118 31.502 24.636 10.790 1.00 19.85 C ANISOU 1572 CA GLN A 118 2289 2683 2569 104 -694 430 C ATOM 1573 C GLN A 118 30.221 25.162 10.164 1.00 17.93 C ANISOU 1573 C GLN A 118 2147 2676 1986 -217 -583 394 C ATOM 1574 O GLN A 118 30.201 25.569 8.993 1.00 17.50 O ANISOU 1574 O GLN A 118 2082 2472 2095 -360 -620 460 O ATOM 1575 CB GLN A 118 32.290 25.844 11.333 1.00 27.06 C ANISOU 1575 CB GLN A 118 3240 3682 3357 -285 -1167 -403 C ATOM 1576 CG GLN A 118 33.681 25.569 11.897 1.00 29.02 C ANISOU 1576 CG GLN A 118 3145 3673 4208 -608 -1266 -238 C ATOM 1577 CD GLN A 118 34.807 26.063 11.001 1.00 36.28 C ANISOU 1577 CD GLN A 118 3935 5381 4467 -40 -314 534 C ATOM 1578 OE1 GLN A 118 34.634 27.007 10.226 1.00 40.36 O ANISOU 1578 OE1 GLN A 118 5565 5316 4454 -446 -666 604 O ATOM 1579 NE2 GLN A 118 35.982 25.450 11.134 1.00 43.69 N ANISOU 1579 NE2 GLN A 118 4893 6937 4769 1307 383 255 N ATOM 1580 H GLN A 118 32.183 24.270 9.004 1.00 19.46 H ANISOU 1580 H GLN A 118 2459 2389 2544 -43 -547 248 H ATOM 1581 HA GLN A 118 31.269 24.049 11.539 1.00 21.76 H ANISOU 1581 HA GLN A 118 2951 2928 2387 463 -594 485 H ATOM 1582 HB2 GLN A 118 32.373 26.492 10.617 1.00 24.59 H ANISOU 1582 HB2 GLN A 118 2549 2970 3824 -299 -430 -447 H ATOM 1583 HB3 GLN A 118 31.771 26.236 12.052 1.00 26.69 H ANISOU 1583 HB3 GLN A 118 3550 2972 3617 -349 -617 -51 H ATOM 1584 HG2 GLN A 118 33.764 26.024 12.749 1.00 26.76 H ANISOU 1584 HG2 GLN A 118 2662 3740 3764 -159 -1064 47 H ATOM 1585 HG3 GLN A 118 33.793 24.615 12.025 1.00 29.91 H ANISOU 1585 HG3 GLN A 118 3545 3901 3919 315 -491 -139 H ATOM 1586 N GLU A 119 29.172 25.219 10.963 1.00 16.72 N ANISOU 1586 N GLU A 119 2185 2355 1811 -94 -776 421 N ATOM 1587 CA GLU A 119 27.904 25.723 10.466 1.00 16.58 C ANISOU 1587 CA GLU A 119 2073 2350 1874 -254 -912 114 C ATOM 1588 C GLU A 119 27.920 27.222 10.151 1.00 18.65 C ANISOU 1588 C GLU A 119 2391 2401 2293 -284 -983 357 C ATOM 1589 O GLU A 119 27.199 27.655 9.265 1.00 16.74 O ANISOU 1589 O GLU A 119 2301 2425 1633 -340 -592 424 O ATOM 1590 CB GLU A 119 26.789 25.403 11.447 1.00 16.62 C ANISOU 1590 CB GLU A 119 2366 2084 1865 -143 -654 -32 C ATOM 1591 CG GLU A 119 26.367 23.930 11.423 1.00 16.30 C ANISOU 1591 CG GLU A 119 2263 2101 1829 -107 -774 156 C ATOM 1592 CD GLU A 119 25.189 23.693 12.304 1.00 17.51 C ANISOU 1592 CD GLU A 119 2105 2379 2166 190 -572 368 C ATOM 1593 OE1 GLU A 119 25.374 23.586 13.538 1.00 19.70 O ANISOU 1593 OE1 GLU A 119 2926 2342 2216 -233 -855 285 O ATOM 1594 OE2 GLU A 119 24.070 23.638 11.751 1.00 16.24 O ANISOU 1594 OE2 GLU A 119 2215 2307 1647 -135 -495 112 O ATOM 1595 H GLU A 119 29.169 24.975 11.788 1.00 16.02 H ANISOU 1595 H GLU A 119 2242 2065 1779 180 -538 285 H ATOM 1596 HA GLU A 119 27.691 25.256 9.631 1.00 16.35 H ANISOU 1596 HA GLU A 119 1836 2501 1874 -224 -628 -11 H ATOM 1597 HB2 GLU A 119 27.081 25.618 12.346 1.00 17.57 H ANISOU 1597 HB2 GLU A 119 2498 2291 1885 -83 -592 -185 H ATOM 1598 HB3 GLU A 119 26.009 25.935 11.220 1.00 16.82 H ANISOU 1598 HB3 GLU A 119 2355 2070 1965 -65 -487 -20 H ATOM 1599 HG2 GLU A 119 26.130 23.678 10.517 1.00 16.81 H ANISOU 1599 HG2 GLU A 119 2400 2088 1898 -109 -580 -117 H ATOM 1600 HG3 GLU A 119 27.101 23.382 11.744 1.00 16.29 H ANISOU 1600 HG3 GLU A 119 2144 2113 1930 117 -418 -52 H ATOM 1601 N LYS A 120 28.730 28.013 10.844 1.00 19.66 N ANISOU 1601 N LYS A 120 2521 2586 2360 -382 -1100 367 N ATOM 1602 CA LYS A 120 28.886 29.433 10.467 1.00 21.18 C ANISOU 1602 CA LYS A 120 2931 2450 2665 -267 -1021 269 C ATOM 1603 C LYS A 120 29.424 29.577 9.053 1.00 20.43 C ANISOU 1603 C LYS A 120 2471 2235 3055 -420 -756 532 C ATOM 1604 O LYS A 120 28.931 30.399 8.281 1.00 19.73 O ANISOU 1604 O LYS A 120 2699 2149 2648 -467 -1151 247 O ATOM 1605 CB LYS A 120 29.810 30.188 11.433 1.00 24.66 C ANISOU 1605 CB LYS A 120 3332 3157 2877 -594 -1088 -12 C ATOM 1606 CG LYS A 120 29.082 30.918 12.544 1.00 35.60 C ANISOU 1606 CG LYS A 120 4349 5012 4165 -80 -322 -913 C ATOM 1607 CD LYS A 120 29.916 32.067 13.135 1.00 38.82 C ANISOU 1607 CD LYS A 120 5493 4371 4883 -143 -507 -976 C ATOM 1608 CE LYS A 120 29.303 32.588 14.437 1.00 43.27 C ANISOU 1608 CE LYS A 120 5870 5593 4978 -19 -90 -939 C ATOM 1609 NZ LYS A 120 30.236 33.463 15.218 1.00 45.75 N ANISOU 1609 NZ LYS A 120 6633 6247 4503 -454 -74 -1112 N ATOM 1610 H LYS A 120 29.190 27.766 11.527 1.00 16.12 H ANISOU 1610 H LYS A 120 1774 2488 1863 44 -469 49 H ATOM 1611 HA LYS A 120 28.005 29.862 10.492 1.00 21.65 H ANISOU 1611 HA LYS A 120 2861 2518 2846 -278 -698 168 H ATOM 1612 HB2 LYS A 120 30.424 29.560 11.844 1.00 24.26 H ANISOU 1612 HB2 LYS A 120 2969 3768 2478 -501 -891 94 H ATOM 1613 HB3 LYS A 120 30.313 30.851 10.934 1.00 25.86 H ANISOU 1613 HB3 LYS A 120 2994 2836 3993 -487 -756 -41 H ATOM 1614 HG2 LYS A 120 28.265 31.301 12.191 1.00 35.06 H ANISOU 1614 HG2 LYS A 120 4341 4465 4514 -52 100 -223 H ATOM 1615 HG3 LYS A 120 28.878 30.290 13.255 1.00 32.79 H ANISOU 1615 HG3 LYS A 120 3498 4793 4167 235 -88 -798 H ATOM 1616 HD2 LYS A 120 30.812 31.748 13.326 1.00 36.72 H ANISOU 1616 HD2 LYS A 120 4958 4466 4526 -706 -252 -389 H ATOM 1617 HD3 LYS A 120 29.947 32.799 12.499 1.00 39.59 H ANISOU 1617 HD3 LYS A 120 4792 4985 5262 -68 -72 -387 H ATOM 1618 HE2 LYS A 120 28.512 33.109 14.227 1.00 42.54 H ANISOU 1618 HE2 LYS A 120 5660 5479 5022 -112 344 -331 H ATOM 1619 HE3 LYS A 120 29.063 31.834 14.999 1.00 43.50 H ANISOU 1619 HE3 LYS A 120 5309 5827 5390 195 -105 -439 H ATOM 1620 N ALA A 121 30.440 28.788 8.711 1.00 19.37 N ANISOU 1620 N ALA A 121 2307 2569 2481 -428 -1110 120 N ATOM 1621 CA ALA A 121 31.008 28.815 7.370 1.00 20.51 C ANISOU 1621 CA ALA A 121 2239 2676 2878 -444 -757 422 C ATOM 1622 C ALA A 121 30.003 28.335 6.331 1.00 18.37 C ANISOU 1622 C ALA A 121 2338 2633 2008 -575 -320 462 C ATOM 1623 O ALA A 121 29.912 28.903 5.246 1.00 20.15 O ANISOU 1623 O ALA A 121 2236 2744 2674 -657 -796 1027 O ATOM 1624 CB ALA A 121 32.271 27.984 7.304 1.00 20.65 C ANISOU 1624 CB ALA A 121 2268 2473 3106 -403 -821 533 C ATOM 1625 H ALA A 121 30.815 28.229 9.247 1.00 19.83 H ANISOU 1625 H ALA A 121 2699 2272 2563 -92 -694 72 H ATOM 1626 HA ALA A 121 31.249 29.738 7.147 1.00 20.34 H ANISOU 1626 HA ALA A 121 2476 2388 2861 -259 -477 3 H ATOM 1627 N LEU A 122 29.262 27.276 6.659 1.00 16.81 N ANISOU 1627 N LEU A 122 2126 2410 1852 -358 -635 604 N ATOM 1628 CA LEU A 122 28.239 26.790 5.737 1.00 16.57 C ANISOU 1628 CA LEU A 122 2054 2216 2025 -260 -521 326 C ATOM 1629 C LEU A 122 27.187 27.861 5.504 1.00 16.05 C ANISOU 1629 C LEU A 122 2160 2029 1909 -350 -631 35 C ATOM 1630 O LEU A 122 26.772 28.072 4.385 1.00 16.05 O ANISOU 1630 O LEU A 122 2098 2131 1868 -352 -581 170 O ATOM 1631 CB LEU A 122 27.600 25.502 6.269 1.00 15.35 C ANISOU 1631 CB LEU A 122 1941 2056 1836 -111 -608 293 C ATOM 1632 CG LEU A 122 26.457 24.914 5.414 1.00 13.86 C ANISOU 1632 CG LEU A 122 1869 1952 1442 -26 -486 338 C ATOM 1633 CD1 LEU A 122 26.880 24.609 4.012 1.00 16.21 C ANISOU 1633 CD1 LEU A 122 2614 2138 1403 56 -503 194 C ATOM 1634 CD2 LEU A 122 25.877 23.663 6.096 1.00 15.89 C ANISOU 1634 CD2 LEU A 122 2136 1779 2121 -232 -431 286 C ATOM 1635 H LEU A 122 29.333 26.830 7.390 1.00 15.28 H ANISOU 1635 H LEU A 122 2178 1950 1676 77 -322 303 H ATOM 1636 HA LEU A 122 28.666 26.592 4.878 1.00 16.77 H ANISOU 1636 HA LEU A 122 2217 2101 2054 -293 -436 229 H ATOM 1637 HB2 LEU A 122 28.291 24.828 6.347 1.00 15.07 H ANISOU 1637 HB2 LEU A 122 1732 2101 1892 -137 -458 100 H ATOM 1638 HB3 LEU A 122 27.238 25.692 7.149 1.00 14.33 H ANISOU 1638 HB3 LEU A 122 1796 1656 1993 -241 -533 24 H ATOM 1639 HG LEU A 122 25.739 25.564 5.363 1.00 14.41 H ANISOU 1639 HG LEU A 122 1756 1801 1917 -132 -427 243 H ATOM 1640 N MET A 123 26.770 28.559 6.553 1.00 14.07 N ANISOU 1640 N MET A 123 1961 1802 1580 -416 -500 387 N ATOM 1641 CA MET A 123 25.792 29.626 6.370 1.00 16.52 C ANISOU 1641 CA MET A 123 2196 1916 2166 -248 -331 55 C ATOM 1642 C MET A 123 26.325 30.725 5.460 1.00 17.11 C ANISOU 1642 C MET A 123 2207 1871 2420 -283 -811 326 C ATOM 1643 O MET A 123 25.607 31.205 4.580 1.00 16.67 O ANISOU 1643 O MET A 123 2377 1921 2033 -291 -749 135 O ATOM 1644 CB MET A 123 25.365 30.220 7.706 1.00 16.31 C ANISOU 1644 CB MET A 123 2241 1920 2033 -305 -587 11 C ATOM 1645 CG MET A 123 24.450 31.416 7.522 1.00 17.69 C ANISOU 1645 CG MET A 123 2485 1986 2248 -155 -618 -26 C ATOM 1646 SD MET A 123 23.626 32.006 9.007 1.00 19.75 S ANISOU 1646 SD MET A 123 2860 2116 2525 -319 -245 11 S ATOM 1647 CE MET A 123 25.015 32.513 10.017 1.00 20.77 C ANISOU 1647 CE MET A 123 3432 2306 2153 -306 -505 -292 C ATOM 1648 H MET A 123 27.028 28.438 7.364 1.00 16.68 H ANISOU 1648 H MET A 123 2154 2624 1559 -403 -475 354 H ATOM 1649 HA MET A 123 24.990 29.244 5.955 1.00 14.74 H ANISOU 1649 HA MET A 123 1918 1863 1819 -10 -178 29 H ATOM 1650 HB2 MET A 123 24.887 29.548 8.217 1.00 16.30 H ANISOU 1650 HB2 MET A 123 1893 2012 2286 -108 -255 16 H ATOM 1651 HB3 MET A 123 26.156 30.507 8.187 1.00 16.96 H ANISOU 1651 HB3 MET A 123 1919 2443 2083 -315 -343 -15 H ATOM 1652 HG2 MET A 123 24.969 32.160 7.180 1.00 17.58 H ANISOU 1652 HG2 MET A 123 2159 2009 2510 -17 -456 12 H ATOM 1653 HG3 MET A 123 23.768 31.173 6.883 1.00 17.45 H ANISOU 1653 HG3 MET A 123 2005 2401 2225 -153 -391 114 H ATOM 1654 N ALYS A 124 27.583 31.133 5.681 0.50 18.87 N ANISOU 1654 N ALYS A 124 2372 2357 2439 -639 -750 467 N ATOM 1655 CA ALYS A 124 28.263 32.134 4.830 0.50 19.16 C ANISOU 1655 CA ALYS A 124 2402 2156 2720 -481 -681 569 C ATOM 1656 C ALYS A 124 28.143 31.743 3.407 0.50 19.36 C ANISOU 1656 C ALYS A 124 2310 2399 2647 -91 -695 695 C ATOM 1657 O ALYS A 124 27.737 32.527 2.543 0.50 16.68 O ANISOU 1657 O ALYS A 124 1290 2321 2727 -762 -835 899 O ATOM 1658 CB ALYS A 124 29.778 32.207 5.124 0.50 17.30 C ANISOU 1658 CB ALYS A 124 2201 2111 2258 -174 -228 149 C ATOM 1659 CG ALYS A 124 30.573 33.058 4.105 0.50 17.11 C ANISOU 1659 CG ALYS A 124 2414 2133 1953 -383 -340 -63 C ATOM 1660 CD ALYS A 124 32.028 33.263 4.512 0.50 19.86 C ANISOU 1660 CD ALYS A 124 2205 2779 2562 -366 -48 -63 C ATOM 1661 CE ALYS A 124 32.851 32.025 4.347 0.50 21.83 C ANISOU 1661 CE ALYS A 124 2601 2876 2815 -246 298 -119 C ATOM 1662 NZ ALYS A 124 34.229 32.251 4.812 0.50 26.99 N ANISOU 1662 NZ ALYS A 124 2490 3725 4040 2 83 12 N ATOM 1663 H ALYS A 124 28.074 30.846 6.326 0.50 15.14 H ANISOU 1663 H ALYS A 124 1769 1957 2026 -191 -241 50 H ATOM 1664 HA ALYS A 124 27.863 33.019 4.959 0.50 19.22 H ANISOU 1664 HA ALYS A 124 2134 2374 2791 -291 -347 589 H ATOM 1665 HB2ALYS A 124 29.905 32.603 6.000 0.50 16.82 H ANISOU 1665 HB2ALYS A 124 1925 2233 2231 -177 -149 108 H ATOM 1666 HB3ALYS A 124 30.150 31.314 5.113 0.50 18.34 H ANISOU 1666 HB3ALYS A 124 2478 2160 2328 -83 -135 138 H ATOM 1667 HG2ALYS A 124 30.565 32.607 3.246 0.50 18.39 H ANISOU 1667 HG2ALYS A 124 2563 2333 2089 -128 -76 -205 H ATOM 1668 HG3ALYS A 124 30.154 33.928 4.023 0.50 16.99 H ANISOU 1668 HG3ALYS A 124 2415 2267 1770 -184 76 15 H ATOM 1669 HD2ALYS A 124 32.416 33.958 3.958 0.50 20.17 H ANISOU 1669 HD2ALYS A 124 2243 2842 2577 -311 73 -53 H ATOM 1670 HD3ALYS A 124 32.061 33.523 5.445 0.50 17.99 H ANISOU 1670 HD3ALYS A 124 1792 2523 2517 -279 -295 39 H ATOM 1671 HE2ALYS A 124 32.465 31.320 4.888 0.50 22.86 H ANISOU 1671 HE2ALYS A 124 2959 2819 2906 -171 135 75 H ATOM 1672 HE3ALYS A 124 32.879 31.776 3.411 0.50 24.48 H ANISOU 1672 HE3ALYS A 124 3435 3083 2781 99 253 -65 H ATOM 1673 N BLYS A 124 27.546 31.162 5.694 0.50 18.14 N ANISOU 1673 N BLYS A 124 2376 2149 2365 -592 -766 410 N ATOM 1674 CA BLYS A 124 28.053 32.270 4.925 0.50 17.35 C ANISOU 1674 CA BLYS A 124 2036 2049 2504 -363 -882 541 C ATOM 1675 C BLYS A 124 28.315 31.809 3.441 0.50 18.16 C ANISOU 1675 C BLYS A 124 2236 2314 2350 -316 -996 662 C ATOM 1676 O BLYS A 124 28.245 32.641 2.537 0.50 17.76 O ANISOU 1676 O BLYS A 124 1750 2662 2334 -281 -716 913 O ATOM 1677 CB BLYS A 124 29.256 32.935 5.687 0.50 14.28 C ANISOU 1677 CB BLYS A 124 1645 1718 2063 -38 -306 -72 C ATOM 1678 CG BLYS A 124 28.940 33.639 7.081 0.50 15.18 C ANISOU 1678 CG BLYS A 124 1971 1715 2082 -142 -22 31 C ATOM 1679 CD BLYS A 124 30.215 34.069 7.902 0.50 14.66 C ANISOU 1679 CD BLYS A 124 1965 1837 1765 -135 138 -16 C ATOM 1680 CE BLYS A 124 29.801 34.803 9.167 0.50 16.82 C ANISOU 1680 CE BLYS A 124 2432 2333 1623 -78 -11 -105 C ATOM 1681 NZ BLYS A 124 30.981 35.105 10.052 0.50 16.80 N ANISOU 1681 NZ BLYS A 124 2225 2525 1631 -583 148 311 N ATOM 1682 H BLYS A 124 28.090 30.844 6.279 0.50 14.31 H ANISOU 1682 H BLYS A 124 1771 1752 1911 -248 -178 103 H ATOM 1683 HA BLYS A 124 27.356 32.958 4.881 0.50 18.18 H ANISOU 1683 HA BLYS A 124 1939 2219 2747 -299 -766 481 H ATOM 1684 HB2BLYS A 124 29.918 32.248 5.860 0.50 14.62 H ANISOU 1684 HB2BLYS A 124 1629 1914 2011 37 -331 -40 H ATOM 1685 HB3BLYS A 124 29.642 33.609 5.108 0.50 14.51 H ANISOU 1685 HB3BLYS A 124 1629 1875 2006 -47 -222 -38 H ATOM 1686 HG2BLYS A 124 28.415 34.438 6.913 0.50 15.26 H ANISOU 1686 HG2BLYS A 124 2005 1837 1953 -28 88 62 H ATOM 1687 HG3BLYS A 124 28.430 33.023 7.631 0.50 15.60 H ANISOU 1687 HG3BLYS A 124 1939 1849 2139 -120 -49 136 H ATOM 1688 HD2BLYS A 124 30.720 33.279 8.155 0.50 15.71 H ANISOU 1688 HD2BLYS A 124 2030 1962 1978 -102 -10 114 H ATOM 1689 HD3BLYS A 124 30.761 34.664 7.365 0.50 14.83 H ANISOU 1689 HD3BLYS A 124 1857 1890 1887 -130 107 35 H ATOM 1690 HE2BLYS A 124 29.381 35.643 8.925 0.50 16.40 H ANISOU 1690 HE2BLYS A 124 2221 2170 1839 -93 134 -293 H ATOM 1691 HE3BLYS A 124 29.181 34.251 9.667 0.50 15.34 H ANISOU 1691 HE3BLYS A 124 1894 2170 1764 76 13 -277 H ATOM 1692 N ALA A 125 28.523 30.509 3.158 1.00 18.54 N ANISOU 1692 N ALA A 125 1937 2392 2716 -230 -653 619 N ATOM 1693 CA ALA A 125 28.581 29.989 1.790 1.00 18.57 C ANISOU 1693 CA ALA A 125 1887 2452 2714 -232 -272 748 C ATOM 1694 C ALA A 125 27.193 29.961 1.170 1.00 17.33 C ANISOU 1694 C ALA A 125 1972 2576 2034 -183 -182 428 C ATOM 1695 O ALA A 125 27.016 30.384 0.010 1.00 17.89 O ANISOU 1695 O ALA A 125 1992 2525 2277 -11 -215 830 O ATOM 1696 CB ALA A 125 29.188 28.575 1.749 1.00 20.33 C ANISOU 1696 CB ALA A 125 2138 2632 2952 86 -525 617 C ATOM 1697 H ALA A 125 28.699 29.917 3.757 1.00 18.35 H ANISOU 1697 H ALA A 125 2200 2228 2543 -78 -344 451 H ATOM 1698 HA ALA A 125 29.147 30.574 1.245 1.00 19.49 H ANISOU 1698 HA ALA A 125 2082 2473 2850 -434 -142 519 H ATOM 1699 N VAL A 126 26.203 29.449 1.904 1.00 14.96 N ANISOU 1699 N VAL A 126 1901 2141 1638 -89 -394 333 N ATOM 1700 CA VAL A 126 24.839 29.418 1.356 1.00 14.18 C ANISOU 1700 CA VAL A 126 1962 1800 1623 -203 -451 -152 C ATOM 1701 C VAL A 126 24.377 30.838 1.028 1.00 13.93 C ANISOU 1701 C VAL A 126 2029 1887 1376 -213 -412 -12 C ATOM 1702 O VAL A 126 23.785 31.066 -0.028 1.00 14.96 O ANISOU 1702 O VAL A 126 2061 1803 1817 -128 -752 -11 O ATOM 1703 CB VAL A 126 23.857 28.747 2.343 1.00 14.65 C ANISOU 1703 CB VAL A 126 1855 1890 1821 -44 -343 97 C ATOM 1704 CG1 VAL A 126 22.410 28.882 1.835 1.00 15.42 C ANISOU 1704 CG1 VAL A 126 1958 2293 1606 104 -368 61 C ATOM 1705 CG2 VAL A 126 24.221 27.254 2.592 1.00 15.62 C ANISOU 1705 CG2 VAL A 126 2105 1915 1913 -58 -686 151 C ATOM 1706 H VAL A 126 26.292 29.134 2.699 1.00 14.54 H ANISOU 1706 H VAL A 126 1959 1929 1634 101 -318 258 H ATOM 1707 HA VAL A 126 24.841 28.901 0.523 1.00 15.22 H ANISOU 1707 HA VAL A 126 2181 1943 1657 -153 -294 -196 H ATOM 1708 HB VAL A 126 23.912 29.213 3.203 1.00 14.70 H ANISOU 1708 HB VAL A 126 1726 2013 1845 -87 -291 43 H ATOM 1709 N ALA A 127 24.674 31.792 1.910 1.00 14.35 N ANISOU 1709 N ALA A 127 1994 1871 1586 -44 -566 -101 N ATOM 1710 CA ALA A 127 24.200 33.155 1.736 1.00 14.82 C ANISOU 1710 CA ALA A 127 1950 1873 1805 -75 -488 -50 C ATOM 1711 C ALA A 127 24.792 33.837 0.493 1.00 15.66 C ANISOU 1711 C ALA A 127 2378 1767 1805 -119 -576 52 C ATOM 1712 O ALA A 127 24.128 34.677 -0.128 1.00 19.19 O ANISOU 1712 O ALA A 127 2712 1963 2615 -398 -1035 542 O ATOM 1713 CB ALA A 127 24.474 33.977 2.965 1.00 17.37 C ANISOU 1713 CB ALA A 127 2803 1627 2167 -101 -263 -296 C ATOM 1714 H ALA A 127 25.149 31.666 2.616 1.00 12.80 H ANISOU 1714 H ALA A 127 1518 1897 1446 -117 -307 -107 H ATOM 1715 HA ALA A 127 23.227 33.128 1.617 1.00 16.80 H ANISOU 1715 HA ALA A 127 1909 2165 2306 100 -373 -35 H ATOM 1716 N THR A 128 26.033 33.494 0.138 1.00 15.50 N ANISOU 1716 N THR A 128 2501 2032 1353 -155 -487 138 N ATOM 1717 CA THR A 128 26.747 34.137 -0.976 1.00 17.51 C ANISOU 1717 CA THR A 128 2956 2132 1564 -240 -338 316 C ATOM 1718 C THR A 128 26.777 33.403 -2.339 1.00 20.25 C ANISOU 1718 C THR A 128 4084 2022 1588 -330 -467 238 C ATOM 1719 O THR A 128 26.707 34.022 -3.381 1.00 25.64 O ANISOU 1719 O THR A 128 5683 2146 1913 79 -163 519 O ATOM 1720 CB THR A 128 28.196 34.461 -0.543 1.00 21.84 C ANISOU 1720 CB THR A 128 2915 2935 2447 -743 -78 -232 C ATOM 1721 OG1 THR A 128 28.938 33.256 -0.307 1.00 26.27 O ANISOU 1721 OG1 THR A 128 3568 3568 2846 -187 -202 -314 O ATOM 1722 CG2 THR A 128 28.192 35.284 0.735 1.00 23.78 C ANISOU 1722 CG2 THR A 128 3196 3159 2679 -889 -311 -568 C ATOM 1723 H THR A 128 26.490 32.876 0.525 1.00 15.24 H ANISOU 1723 H THR A 128 2331 1842 1615 -97 -145 174 H ATOM 1724 HA THR A 128 26.318 35.000 -1.152 1.00 19.18 H ANISOU 1724 HA THR A 128 3274 2028 1984 -186 10 306 H ATOM 1725 HB THR A 128 28.632 34.977 -1.239 1.00 24.19 H ANISOU 1725 HB THR A 128 2910 3519 2762 -456 318 -23 H ATOM 1726 N VAL A 129 26.861 32.074 -2.305 1.00 16.02 N ANISOU 1726 N VAL A 129 2357 1895 1833 -569 -254 323 N ATOM 1727 CA VAL A 129 27.140 31.257 -3.477 1.00 16.96 C ANISOU 1727 CA VAL A 129 2128 2126 2187 -397 -382 59 C ATOM 1728 C VAL A 129 25.858 30.773 -4.127 1.00 15.04 C ANISOU 1728 C VAL A 129 2202 1749 1763 -390 -297 64 C ATOM 1729 O VAL A 129 25.736 30.818 -5.333 1.00 16.02 O ANISOU 1729 O VAL A 129 2401 1824 1861 -403 -381 424 O ATOM 1730 CB VAL A 129 28.040 30.036 -3.064 1.00 18.01 C ANISOU 1730 CB VAL A 129 2067 2610 2165 -69 -450 73 C ATOM 1731 CG1 VAL A 129 28.243 29.051 -4.215 1.00 19.22 C ANISOU 1731 CG1 VAL A 129 2364 2311 2626 11 -427 -26 C ATOM 1732 CG2 VAL A 129 29.401 30.559 -2.504 1.00 20.69 C ANISOU 1732 CG2 VAL A 129 2230 2945 2683 -232 -669 52 C ATOM 1733 H VAL A 129 26.747 31.612 -1.588 1.00 16.86 H ANISOU 1733 H VAL A 129 2339 2145 1919 -325 -329 494 H ATOM 1734 HA VAL A 129 27.632 31.787 -4.139 1.00 16.65 H ANISOU 1734 HA VAL A 129 1912 2238 2175 -244 -145 -68 H ATOM 1735 HB VAL A 129 27.592 29.547 -2.344 1.00 18.65 H ANISOU 1735 HB VAL A 129 2270 2307 2507 -39 -329 178 H ATOM 1736 N GLY A 130 24.922 30.263 -3.326 1.00 16.45 N ANISOU 1736 N GLY A 130 1971 2298 1977 -391 -408 423 N ATOM 1737 CA GLY A 130 23.790 29.497 -3.858 1.00 12.82 C ANISOU 1737 CA GLY A 130 1934 1748 1188 -79 -239 344 C ATOM 1738 C GLY A 130 23.667 28.181 -3.098 1.00 12.52 C ANISOU 1738 C GLY A 130 2122 1737 897 -72 -166 288 C ATOM 1739 O GLY A 130 24.271 27.982 -2.051 1.00 14.12 O ANISOU 1739 O GLY A 130 2157 1856 1350 -211 -514 388 O ATOM 1740 H GLY A 130 24.916 30.345 -2.470 1.00 14.10 H ANISOU 1740 H GLY A 130 1613 1729 2012 -335 -283 155 H ATOM 1741 HA2 GLY A 130 23.932 29.298 -4.797 1.00 12.76 H ANISOU 1741 HA2 GLY A 130 2151 1370 1326 -156 147 383 H ATOM 1742 HA3 GLY A 130 22.968 29.997 -3.771 1.00 12.39 H ANISOU 1742 HA3 GLY A 130 1869 1567 1271 -178 -146 167 H ATOM 1743 N PRO A 131 22.892 27.251 -3.672 1.00 13.15 N ANISOU 1743 N PRO A 131 1807 1688 1501 -163 -312 446 N ATOM 1744 CA PRO A 131 22.748 25.930 -3.108 1.00 12.84 C ANISOU 1744 CA PRO A 131 1769 1535 1573 -70 -225 286 C ATOM 1745 C PRO A 131 24.093 25.181 -2.980 1.00 12.72 C ANISOU 1745 C PRO A 131 1822 1696 1313 31 6 379 C ATOM 1746 O PRO A 131 24.952 25.285 -3.864 1.00 12.66 O ANISOU 1746 O PRO A 131 1844 1962 1004 -125 -292 422 O ATOM 1747 CB PRO A 131 21.798 25.232 -4.089 1.00 13.07 C ANISOU 1747 CB PRO A 131 1757 1543 1663 -11 -204 130 C ATOM 1748 CG PRO A 131 20.990 26.356 -4.694 1.00 14.00 C ANISOU 1748 CG PRO A 131 1827 1515 1977 -6 -291 198 C ATOM 1749 CD PRO A 131 22.013 27.454 -4.839 1.00 12.56 C ANISOU 1749 CD PRO A 131 1728 1600 1443 43 -221 238 C ATOM 1750 HA PRO A 131 22.321 25.999 -2.232 1.00 11.98 H ANISOU 1750 HA PRO A 131 1606 1331 1614 -114 -187 289 H ATOM 1751 HB2 PRO A 131 22.307 24.768 -4.773 1.00 13.03 H ANISOU 1751 HB2 PRO A 131 1685 1555 1709 -56 -132 149 H ATOM 1752 HB3 PRO A 131 21.224 24.615 -3.608 1.00 12.56 H ANISOU 1752 HB3 PRO A 131 1646 1494 1632 54 -165 73 H ATOM 1753 HG2 PRO A 131 20.639 26.088 -5.558 1.00 12.89 H ANISOU 1753 HG2 PRO A 131 1589 1522 1786 24 -84 267 H ATOM 1754 HG3 PRO A 131 20.278 26.619 -4.091 1.00 12.84 H ANISOU 1754 HG3 PRO A 131 1799 1310 1769 -113 -324 162 H ATOM 1755 HD2 PRO A 131 22.506 27.352 -5.666 1.00 12.85 H ANISOU 1755 HD2 PRO A 131 1804 1632 1446 77 -230 52 H ATOM 1756 HD3 PRO A 131 21.574 28.318 -4.792 1.00 11.92 H ANISOU 1756 HD3 PRO A 131 1559 1564 1406 -33 -160 177 H ATOM 1757 N ILE A 132 24.219 24.447 -1.885 1.00 12.59 N ANISOU 1757 N ILE A 132 1629 1828 1325 -218 -275 402 N ATOM 1758 CA ILE A 132 25.477 23.802 -1.502 1.00 12.27 C ANISOU 1758 CA ILE A 132 1651 1746 1264 -119 -267 304 C ATOM 1759 C ILE A 132 25.274 22.289 -1.296 1.00 12.68 C ANISOU 1759 C ILE A 132 1682 1706 1427 -165 -327 159 C ATOM 1760 O ILE A 132 24.317 21.894 -0.629 1.00 12.91 O ANISOU 1760 O ILE A 132 1547 1725 1632 -80 -403 390 O ATOM 1761 CB ILE A 132 26.012 24.392 -0.193 1.00 12.43 C ANISOU 1761 CB ILE A 132 1896 1717 1108 109 -197 156 C ATOM 1762 CG1 ILE A 132 26.173 25.915 -0.267 1.00 14.63 C ANISOU 1762 CG1 ILE A 132 1910 1800 1847 -165 -436 330 C ATOM 1763 CG2 ILE A 132 27.321 23.675 0.248 1.00 14.26 C ANISOU 1763 CG2 ILE A 132 1800 1837 1778 17 -428 132 C ATOM 1764 CD1 ILE A 132 27.130 26.401 -1.346 1.00 15.00 C ANISOU 1764 CD1 ILE A 132 2246 1854 1600 -6 -180 170 C ATOM 1765 H ILE A 132 23.579 24.298 -1.330 1.00 11.67 H ANISOU 1765 H ILE A 132 1678 1419 1335 -107 -209 373 H ATOM 1766 HA ILE A 132 26.147 23.922 -2.206 1.00 12.07 H ANISOU 1766 HA ILE A 132 1798 1583 1202 -66 -164 24 H ATOM 1767 HB ILE A 132 25.349 24.213 0.491 1.00 13.08 H ANISOU 1767 HB ILE A 132 1845 1711 1414 -80 -74 34 H ATOM 1768 HG12 ILE A 132 25.306 26.312 -0.436 1.00 14.32 H ANISOU 1768 HG12 ILE A 132 1999 1603 1837 -6 -269 124 H ATOM 1769 HG13 ILE A 132 26.509 26.234 0.585 1.00 13.62 H ANISOU 1769 HG13 ILE A 132 1770 1685 1717 -4 -80 111 H ATOM 1770 N SER A 133 26.130 21.475 -1.913 1.00 12.47 N ANISOU 1770 N SER A 133 1612 1591 1533 -187 -337 354 N ATOM 1771 CA SER A 133 26.106 20.034 -1.664 1.00 12.26 C ANISOU 1771 CA SER A 133 1667 1551 1438 -200 -334 300 C ATOM 1772 C SER A 133 26.560 19.740 -0.251 1.00 12.56 C ANISOU 1772 C SER A 133 1784 1647 1339 -167 -304 181 C ATOM 1773 O SER A 133 27.588 20.257 0.192 1.00 13.46 O ANISOU 1773 O SER A 133 1666 1958 1491 -271 -367 479 O ATOM 1774 CB SER A 133 26.994 19.295 -2.652 1.00 12.70 C ANISOU 1774 CB SER A 133 1731 1673 1418 -274 -262 263 C ATOM 1775 OG SER A 133 26.497 19.353 -3.976 1.00 13.34 O ANISOU 1775 OG SER A 133 1740 1909 1418 23 -287 329 O ATOM 1776 H SER A 133 26.727 21.731 -2.476 1.00 12.54 H ANISOU 1776 H SER A 133 1711 1455 1598 -152 -201 233 H ATOM 1777 HA SER A 133 25.191 19.702 -1.775 1.00 12.30 H ANISOU 1777 HA SER A 133 1630 1528 1516 -145 -333 253 H ATOM 1778 HB2 SER A 133 27.880 19.687 -2.634 1.00 12.90 H ANISOU 1778 HB2 SER A 133 1609 1622 1670 -121 -293 274 H ATOM 1779 HB3 SER A 133 27.046 18.366 -2.382 1.00 12.20 H ANISOU 1779 HB3 SER A 133 1738 1636 1259 -189 -292 179 H ATOM 1780 N VAL A 134 25.820 18.888 0.458 1.00 13.13 N ANISOU 1780 N VAL A 134 1551 1823 1615 -230 -477 382 N ATOM 1781 CA VAL A 134 26.200 18.475 1.810 1.00 13.03 C ANISOU 1781 CA VAL A 134 1743 1753 1453 -203 -433 272 C ATOM 1782 C VAL A 134 25.992 16.974 1.992 1.00 13.56 C ANISOU 1782 C VAL A 134 1943 1680 1529 -97 -479 297 C ATOM 1783 O VAL A 134 25.117 16.344 1.379 1.00 13.29 O ANISOU 1783 O VAL A 134 1817 1751 1481 -73 -448 386 O ATOM 1784 CB VAL A 134 25.435 19.260 2.927 1.00 12.82 C ANISOU 1784 CB VAL A 134 1792 1617 1459 -124 -480 293 C ATOM 1785 CG1 VAL A 134 25.682 20.773 2.843 1.00 15.02 C ANISOU 1785 CG1 VAL A 134 1809 1597 2299 -157 -496 247 C ATOM 1786 CG2 VAL A 134 23.918 18.960 2.915 1.00 15.03 C ANISOU 1786 CG2 VAL A 134 1774 1814 2122 -170 -291 494 C ATOM 1787 H VAL A 134 25.091 18.530 0.175 1.00 12.02 H ANISOU 1787 H VAL A 134 1438 1717 1411 -61 -306 77 H ATOM 1788 HA VAL A 134 27.156 18.647 1.937 1.00 12.97 H ANISOU 1788 HA VAL A 134 1703 1798 1427 -113 -427 310 H ATOM 1789 HB VAL A 134 25.778 18.960 3.794 1.00 13.76 H ANISOU 1789 HB VAL A 134 1921 1896 1410 159 -334 318 H ATOM 1790 N ALA A 135 26.797 16.422 2.887 1.00 12.79 N ANISOU 1790 N ALA A 135 1652 1745 1461 -129 -305 372 N ATOM 1791 CA ALA A 135 26.667 15.069 3.416 1.00 12.69 C ANISOU 1791 CA ALA A 135 1784 1707 1330 -219 -487 345 C ATOM 1792 C ALA A 135 25.906 15.129 4.725 1.00 12.92 C ANISOU 1792 C ALA A 135 1734 1614 1558 64 -340 361 C ATOM 1793 O ALA A 135 26.161 15.977 5.586 1.00 13.80 O ANISOU 1793 O ALA A 135 1974 1769 1500 -116 -358 354 O ATOM 1794 CB ALA A 135 28.046 14.474 3.662 1.00 13.74 C ANISOU 1794 CB ALA A 135 1888 2014 1317 143 -100 336 C ATOM 1795 H ALA A 135 27.465 16.844 3.229 1.00 11.76 H ANISOU 1795 H ALA A 135 1521 1568 1378 -4 -159 238 H ATOM 1796 HA ALA A 135 26.187 14.498 2.781 1.00 14.15 H ANISOU 1796 HA ALA A 135 1947 1770 1658 -242 -332 10 H ATOM 1797 N ILE A 136 24.980 14.191 4.916 1.00 12.75 N ANISOU 1797 N ILE A 136 1889 1698 1255 -124 -343 280 N ATOM 1798 CA ILE A 136 24.278 14.060 6.203 1.00 13.20 C ANISOU 1798 CA ILE A 136 1933 1700 1380 76 -272 378 C ATOM 1799 C ILE A 136 24.179 12.588 6.653 1.00 11.71 C ANISOU 1799 C ILE A 136 1649 1734 1065 -31 -552 419 C ATOM 1800 O ILE A 136 24.259 11.677 5.806 1.00 13.96 O ANISOU 1800 O ILE A 136 2022 1767 1514 -126 -254 215 O ATOM 1801 CB ILE A 136 22.830 14.670 6.206 1.00 13.38 C ANISOU 1801 CB ILE A 136 1932 1560 1592 35 -323 89 C ATOM 1802 CG1 ILE A 136 21.952 13.975 5.161 1.00 12.69 C ANISOU 1802 CG1 ILE A 136 1957 1714 1149 -3 -305 380 C ATOM 1803 CG2 ILE A 136 22.873 16.187 5.978 1.00 13.48 C ANISOU 1803 CG2 ILE A 136 2060 1679 1383 -4 -310 461 C ATOM 1804 CD1 ILE A 136 20.448 14.306 5.255 1.00 14.31 C ANISOU 1804 CD1 ILE A 136 1911 2016 1511 23 -212 434 C ATOM 1805 H ILE A 136 24.736 13.617 4.324 1.00 13.28 H ANISOU 1805 H ILE A 136 1883 1632 1528 55 -264 68 H ATOM 1806 HA ILE A 136 24.793 14.527 6.892 1.00 12.72 H ANISOU 1806 HA ILE A 136 1783 1669 1378 79 -60 194 H ATOM 1807 HB ILE A 136 22.443 14.511 7.081 1.00 11.74 H ANISOU 1807 HB ILE A 136 1731 1242 1486 -72 -489 143 H ATOM 1808 HG12 ILE A 136 22.255 14.230 4.275 1.00 13.53 H ANISOU 1808 HG12 ILE A 136 2091 1728 1320 -178 -17 252 H ATOM 1809 HG13 ILE A 136 22.032 13.015 5.264 1.00 12.65 H ANISOU 1809 HG13 ILE A 136 1891 1630 1283 -139 -181 197 H ATOM 1810 N ASP A 137 23.994 12.387 7.944 1.00 12.65 N ANISOU 1810 N ASP A 137 1986 1718 1099 -1 -505 323 N ATOM 1811 CA ASP A 137 23.599 11.081 8.490 1.00 13.33 C ANISOU 1811 CA ASP A 137 1963 1717 1383 -10 -154 340 C ATOM 1812 C ASP A 137 22.066 10.962 8.378 1.00 14.44 C ANISOU 1812 C ASP A 137 1966 1775 1742 -42 -116 383 C ATOM 1813 O ASP A 137 21.337 11.512 9.207 1.00 15.99 O ANISOU 1813 O ASP A 137 1959 2169 1948 53 -205 105 O ATOM 1814 CB ASP A 137 24.055 10.944 9.933 1.00 14.36 C ANISOU 1814 CB ASP A 137 2129 1900 1426 -5 -303 366 C ATOM 1815 CG ASP A 137 23.575 9.672 10.571 1.00 15.02 C ANISOU 1815 CG ASP A 137 2211 1829 1667 255 -449 541 C ATOM 1816 OD1 ASP A 137 23.126 8.751 9.854 1.00 16.44 O ANISOU 1816 OD1 ASP A 137 2308 1988 1948 -113 -218 469 O ATOM 1817 OD2 ASP A 137 23.672 9.627 11.809 1.00 15.32 O ANISOU 1817 OD2 ASP A 137 2149 2036 1636 -67 -268 430 O ATOM 1818 H ASP A 137 24.089 12.999 8.541 1.00 12.79 H ANISOU 1818 H ASP A 137 1858 1717 1285 50 -112 134 H ATOM 1819 HA ASP A 137 24.014 10.362 7.970 1.00 13.70 H ANISOU 1819 HA ASP A 137 1909 1708 1588 -141 -198 140 H ATOM 1820 HB2 ASP A 137 25.023 10.951 9.962 1.00 15.69 H ANISOU 1820 HB2 ASP A 137 2088 2279 1593 93 -299 290 H ATOM 1821 HB3 ASP A 137 23.703 11.686 10.449 1.00 14.00 H ANISOU 1821 HB3 ASP A 137 1930 1880 1508 -226 -279 196 H ATOM 1822 N ALA A 138 21.616 10.257 7.334 1.00 14.03 N ANISOU 1822 N ALA A 138 1832 1636 1862 -61 -144 392 N ATOM 1823 CA ALA A 138 20.199 10.008 7.059 1.00 12.66 C ANISOU 1823 CA ALA A 138 1773 1705 1329 -59 119 342 C ATOM 1824 C ALA A 138 19.774 8.591 7.460 1.00 13.20 C ANISOU 1824 C ALA A 138 1868 1560 1588 -35 -83 229 C ATOM 1825 O ALA A 138 18.634 8.215 7.249 1.00 13.78 O ANISOU 1825 O ALA A 138 1895 1757 1580 -123 -68 433 O ATOM 1826 CB ALA A 138 19.934 10.191 5.608 1.00 14.03 C ANISOU 1826 CB ALA A 138 1942 1921 1468 -174 -9 456 C ATOM 1827 H ALA A 138 22.140 9.895 6.755 1.00 14.31 H ANISOU 1827 H ALA A 138 1667 1855 1915 -195 -152 221 H ATOM 1828 HA ALA A 138 19.642 10.648 7.547 1.00 13.58 H ANISOU 1828 HA ALA A 138 1888 1582 1688 -65 14 112 H ATOM 1829 N GLY A 139 20.682 7.844 8.072 1.00 14.19 N ANISOU 1829 N GLY A 139 1715 1711 1964 -14 20 466 N ATOM 1830 CA GLY A 139 20.430 6.437 8.412 1.00 13.35 C ANISOU 1830 CA GLY A 139 1956 1587 1529 82 106 202 C ATOM 1831 C GLY A 139 19.664 6.232 9.696 1.00 12.58 C ANISOU 1831 C GLY A 139 2064 1490 1224 111 -43 52 C ATOM 1832 O GLY A 139 20.161 5.658 10.668 1.00 15.20 O ANISOU 1832 O GLY A 139 2158 1788 1828 13 -105 654 O ATOM 1833 H GLY A 139 21.460 8.116 8.313 1.00 13.61 H ANISOU 1833 H GLY A 139 1733 1695 1741 48 36 214 H ATOM 1834 HA2 GLY A 139 21.281 5.979 8.498 1.00 13.63 H ANISOU 1834 HA2 GLY A 139 1805 1569 1803 -50 67 201 H ATOM 1835 HA3 GLY A 139 19.936 6.013 7.693 1.00 12.57 H ANISOU 1835 HA3 GLY A 139 1796 1659 1319 189 238 156 H ATOM 1836 N HIS A 140 18.415 6.674 9.681 1.00 13.46 N ANISOU 1836 N HIS A 140 1929 1816 1367 -75 -10 435 N ATOM 1837 CA HIS A 140 17.556 6.662 10.850 1.00 13.28 C ANISOU 1837 CA HIS A 140 2001 1782 1261 18 -17 225 C ATOM 1838 C HIS A 140 16.129 6.520 10.415 1.00 13.38 C ANISOU 1838 C HIS A 140 1999 1475 1610 -6 -109 79 C ATOM 1839 O HIS A 140 15.734 7.184 9.467 1.00 13.64 O ANISOU 1839 O HIS A 140 1967 1776 1438 -27 65 248 O ATOM 1840 CB HIS A 140 17.725 7.981 11.579 1.00 15.27 C ANISOU 1840 CB HIS A 140 2147 1939 1715 -40 -197 -19 C ATOM 1841 CG HIS A 140 19.057 8.097 12.231 1.00 15.45 C ANISOU 1841 CG HIS A 140 2069 1900 1900 -35 -163 -212 C ATOM 1842 ND1 HIS A 140 20.111 8.822 11.725 1.00 18.02 N ANISOU 1842 ND1 HIS A 140 2148 2273 2427 -150 -251 32 N ATOM 1843 CD2 HIS A 140 19.523 7.466 13.322 1.00 15.87 C ANISOU 1843 CD2 HIS A 140 2204 1984 1839 -142 -197 28 C ATOM 1844 CE1 HIS A 140 21.163 8.637 12.504 1.00 16.98 C ANISOU 1844 CE1 HIS A 140 2182 2219 2047 -365 -321 -31 C ATOM 1845 NE2 HIS A 140 20.826 7.832 13.492 1.00 20.36 N ANISOU 1845 NE2 HIS A 140 2146 3088 2500 -203 -26 279 N ATOM 1846 H HIS A 140 18.033 6.994 8.981 1.00 12.47 H ANISOU 1846 H HIS A 140 1879 1513 1346 -30 27 317 H ATOM 1847 HA HIS A 140 17.788 5.924 11.452 1.00 13.19 H ANISOU 1847 HA HIS A 140 1873 1827 1311 9 104 289 H ATOM 1848 HB2 HIS A 140 17.635 8.709 10.944 1.00 15.22 H ANISOU 1848 HB2 HIS A 140 2068 1793 1919 24 -43 -8 H ATOM 1849 HB3 HIS A 140 17.047 8.055 12.269 1.00 14.57 H ANISOU 1849 HB3 HIS A 140 2069 1593 1872 -14 -144 -41 H ATOM 1850 HD2 HIS A 140 19.044 6.902 13.856 1.00 16.67 H ANISOU 1850 HD2 HIS A 140 2254 2023 2055 -41 127 -31 H ATOM 1851 HE1 HIS A 140 21.982 9.042 12.412 1.00 17.61 H ANISOU 1851 HE1 HIS A 140 1993 2235 2463 -117 -97 -73 H ATOM 1852 N GLU A 141 15.338 5.704 11.102 1.00 13.70 N ANISOU 1852 N GLU A 141 2036 1506 1663 -57 -185 223 N ATOM 1853 CA GLU A 141 13.922 5.586 10.765 1.00 13.47 C ANISOU 1853 CA GLU A 141 2036 1974 1104 -39 -138 216 C ATOM 1854 C GLU A 141 13.207 6.926 10.879 1.00 13.33 C ANISOU 1854 C GLU A 141 1836 1797 1431 -274 -94 300 C ATOM 1855 O GLU A 141 12.298 7.213 10.091 1.00 13.36 O ANISOU 1855 O GLU A 141 1957 1780 1338 -129 -162 75 O ATOM 1856 CB GLU A 141 13.247 4.544 11.674 1.00 14.40 C ANISOU 1856 CB GLU A 141 1949 1854 1666 -37 -170 368 C ATOM 1857 CG GLU A 141 13.723 3.133 11.338 1.00 16.42 C ANISOU 1857 CG GLU A 141 2255 2036 1948 109 20 97 C ATOM 1858 CD GLU A 141 13.036 2.049 12.106 1.00 19.52 C ANISOU 1858 CD GLU A 141 2844 1951 2621 93 91 323 C ATOM 1859 OE1 GLU A 141 11.932 2.276 12.592 1.00 23.32 O ANISOU 1859 OE1 GLU A 141 2821 2507 3530 -161 495 624 O ATOM 1860 OE2 GLU A 141 13.629 0.950 12.211 1.00 23.29 O ANISOU 1860 OE2 GLU A 141 4461 2225 2161 831 304 381 O ATOM 1861 H GLU A 141 15.596 5.217 11.762 1.00 13.04 H ANISOU 1861 H GLU A 141 1859 1585 1507 111 -68 114 H ATOM 1862 HA GLU A 141 13.840 5.278 9.839 1.00 15.17 H ANISOU 1862 HA GLU A 141 2255 2176 1332 -283 -70 -106 H ATOM 1863 HB2 GLU A 141 13.466 4.730 12.601 1.00 13.37 H ANISOU 1863 HB2 GLU A 141 1870 1651 1556 -161 72 435 H ATOM 1864 HB3 GLU A 141 12.287 4.583 11.540 1.00 15.16 H ANISOU 1864 HB3 GLU A 141 1897 2004 1857 -58 -52 156 H ATOM 1865 HG2 GLU A 141 13.567 2.975 10.395 1.00 17.29 H ANISOU 1865 HG2 GLU A 141 2242 2279 2047 17 -96 -44 H ATOM 1866 HG3 GLU A 141 14.671 3.071 11.526 1.00 16.94 H ANISOU 1866 HG3 GLU A 141 2306 2139 1989 240 -113 15 H ATOM 1867 N SER A 142 13.649 7.778 11.799 1.00 13.69 N ANISOU 1867 N SER A 142 2030 1758 1412 -96 -93 211 N ATOM 1868 CA SER A 142 13.042 9.106 11.932 1.00 13.04 C ANISOU 1868 CA SER A 142 1878 1949 1126 38 -7 126 C ATOM 1869 C SER A 142 13.190 9.930 10.660 1.00 12.62 C ANISOU 1869 C SER A 142 1965 1703 1124 -25 -30 60 C ATOM 1870 O SER A 142 12.325 10.765 10.370 1.00 13.79 O ANISOU 1870 O SER A 142 2015 1834 1391 47 -132 156 O ATOM 1871 CB SER A 142 13.634 9.849 13.123 1.00 13.55 C ANISOU 1871 CB SER A 142 2198 1782 1166 137 -279 144 C ATOM 1872 OG SER A 142 15.033 9.979 12.983 1.00 14.14 O ANISOU 1872 OG SER A 142 2290 1827 1256 -116 -85 42 O ATOM 1873 H SER A 142 14.284 7.619 12.357 1.00 13.23 H ANISOU 1873 H SER A 142 1740 1739 1547 -84 -33 23 H ATOM 1874 HA SER A 142 12.083 8.994 12.101 1.00 13.73 H ANISOU 1874 HA SER A 142 1879 1935 1401 -99 -42 252 H ATOM 1875 HB2 SER A 142 13.238 10.733 13.171 1.00 14.81 H ANISOU 1875 HB2 SER A 142 2352 1599 1675 -30 -124 151 H ATOM 1876 HB3 SER A 142 13.441 9.353 13.934 1.00 13.23 H ANISOU 1876 HB3 SER A 142 2060 1702 1264 -76 -273 128 H ATOM 1877 N PHE A 143 14.288 9.738 9.927 1.00 13.31 N ANISOU 1877 N PHE A 143 1781 1943 1332 43 -94 284 N ATOM 1878 CA PHE A 143 14.514 10.420 8.658 1.00 12.41 C ANISOU 1878 CA PHE A 143 1892 1626 1194 54 -89 94 C ATOM 1879 C PHE A 143 13.742 9.766 7.526 1.00 13.31 C ANISOU 1879 C PHE A 143 2066 1752 1238 -122 -151 221 C ATOM 1880 O PHE A 143 13.108 10.433 6.722 1.00 13.83 O ANISOU 1880 O PHE A 143 2035 1801 1417 -145 -234 268 O ATOM 1881 CB PHE A 143 16.008 10.491 8.371 1.00 13.08 C ANISOU 1881 CB PHE A 143 1877 1736 1355 -45 -183 128 C ATOM 1882 CG PHE A 143 16.349 11.419 7.250 1.00 12.92 C ANISOU 1882 CG PHE A 143 1727 1775 1407 42 51 109 C ATOM 1883 CD1 PHE A 143 16.531 12.776 7.470 1.00 13.95 C ANISOU 1883 CD1 PHE A 143 1949 1809 1540 -104 -240 245 C ATOM 1884 CD2 PHE A 143 16.465 10.945 5.963 1.00 14.07 C ANISOU 1884 CD2 PHE A 143 2194 1800 1350 152 25 248 C ATOM 1885 CE1 PHE A 143 16.851 13.623 6.406 1.00 13.37 C ANISOU 1885 CE1 PHE A 143 1737 1713 1630 -176 -256 225 C ATOM 1886 CE2 PHE A 143 16.764 11.786 4.920 1.00 13.91 C ANISOU 1886 CE2 PHE A 143 2114 2081 1089 141 -70 198 C ATOM 1887 CZ PHE A 143 16.963 13.115 5.132 1.00 14.44 C ANISOU 1887 CZ PHE A 143 1940 2067 1478 111 -358 327 C ATOM 1888 H PHE A 143 14.928 9.210 10.151 1.00 12.47 H ANISOU 1888 H PHE A 143 1832 1589 1316 -43 -131 159 H ATOM 1889 HA PHE A 143 14.194 11.343 8.733 1.00 13.42 H ANISOU 1889 HA PHE A 143 1971 1577 1551 8 -83 132 H ATOM 1890 HB2 PHE A 143 16.464 10.807 9.164 1.00 13.47 H ANISOU 1890 HB2 PHE A 143 1927 1781 1408 -38 -185 51 H ATOM 1891 HB3 PHE A 143 16.328 9.605 8.138 1.00 12.86 H ANISOU 1891 HB3 PHE A 143 1711 1727 1446 -121 -83 73 H ATOM 1892 HD1 PHE A 143 16.461 13.120 8.331 1.00 13.61 H ANISOU 1892 HD1 PHE A 143 1834 1690 1646 -99 -103 136 H ATOM 1893 HD2 PHE A 143 16.336 10.039 5.796 1.00 13.84 H ANISOU 1893 HD2 PHE A 143 1956 1812 1488 242 1 58 H ATOM 1894 HE1 PHE A 143 16.978 14.531 6.557 1.00 14.47 H ANISOU 1894 HE1 PHE A 143 1896 1648 1952 -20 -237 249 H ATOM 1895 HE2 PHE A 143 16.845 11.441 4.061 1.00 14.82 H ANISOU 1895 HE2 PHE A 143 1972 2329 1329 274 380 3 H ATOM 1896 HZ PHE A 143 17.168 13.678 4.420 1.00 14.41 H ANISOU 1896 HZ PHE A 143 1901 2003 1570 110 -275 295 H ATOM 1897 N LEU A 144 13.790 8.442 7.456 1.00 12.71 N ANISOU 1897 N LEU A 144 2129 1732 967 -89 -128 256 N ATOM 1898 CA LEU A 144 13.078 7.741 6.388 1.00 14.30 C ANISOU 1898 CA LEU A 144 2177 1898 1357 -200 -326 187 C ATOM 1899 C LEU A 144 11.579 8.069 6.418 1.00 14.35 C ANISOU 1899 C LEU A 144 2175 1901 1376 -318 -366 154 C ATOM 1900 O LEU A 144 10.970 8.215 5.361 1.00 15.51 O ANISOU 1900 O LEU A 144 2167 2182 1543 -366 -503 317 O ATOM 1901 CB LEU A 144 13.342 6.220 6.491 1.00 15.66 C ANISOU 1901 CB LEU A 144 2631 1781 1537 -291 -215 101 C ATOM 1902 CG LEU A 144 14.630 5.636 5.867 1.00 20.63 C ANISOU 1902 CG LEU A 144 2764 2665 2409 81 85 276 C ATOM 1903 CD1 LEU A 144 14.520 5.688 4.349 1.00 21.72 C ANISOU 1903 CD1 LEU A 144 2823 3117 2311 372 214 211 C ATOM 1904 CD2 LEU A 144 15.977 6.236 6.315 1.00 21.86 C ANISOU 1904 CD2 LEU A 144 2990 2925 2390 -287 514 -391 C ATOM 1905 H LEU A 144 14.217 7.938 8.007 1.00 12.58 H ANISOU 1905 H LEU A 144 1646 1793 1339 93 -153 143 H ATOM 1906 HA LEU A 144 13.427 8.054 5.528 1.00 13.49 H ANISOU 1906 HA LEU A 144 2161 1752 1212 -236 -383 -7 H ATOM 1907 HB2 LEU A 144 13.360 5.984 7.432 1.00 16.39 H ANISOU 1907 HB2 LEU A 144 2588 1951 1686 -183 -286 358 H ATOM 1908 HB3 LEU A 144 12.593 5.761 6.077 1.00 16.44 H ANISOU 1908 HB3 LEU A 144 2528 1895 1820 -236 -293 106 H ATOM 1909 HG LEU A 144 14.662 4.697 6.105 1.00 19.64 H ANISOU 1909 HG LEU A 144 2679 2506 2278 89 27 -12 H ATOM 1910 N PHE A 145 11.033 8.210 7.634 1.00 14.45 N ANISOU 1910 N PHE A 145 2057 1839 1592 -243 -305 149 N ATOM 1911 CA PHE A 145 9.600 8.459 7.858 1.00 14.91 C ANISOU 1911 CA PHE A 145 2078 2082 1502 -98 -363 258 C ATOM 1912 C PHE A 145 9.283 9.927 8.214 1.00 14.55 C ANISOU 1912 C PHE A 145 2007 2105 1416 -41 -158 322 C ATOM 1913 O PHE A 145 8.176 10.253 8.629 1.00 15.74 O ANISOU 1913 O PHE A 145 2036 2225 1719 -19 -95 399 O ATOM 1914 CB PHE A 145 9.076 7.485 8.918 1.00 17.07 C ANISOU 1914 CB PHE A 145 1955 2242 2288 -312 -297 569 C ATOM 1915 CG PHE A 145 9.146 6.047 8.486 1.00 18.62 C ANISOU 1915 CG PHE A 145 2107 2319 2649 -448 -181 379 C ATOM 1916 CD1 PHE A 145 8.320 5.589 7.492 1.00 23.49 C ANISOU 1916 CD1 PHE A 145 3477 2580 2868 -289 -857 190 C ATOM 1917 CD2 PHE A 145 10.057 5.174 9.039 1.00 22.63 C ANISOU 1917 CD2 PHE A 145 3077 2128 3393 -240 -587 454 C ATOM 1918 CE1 PHE A 145 8.380 4.272 7.081 1.00 29.13 C ANISOU 1918 CE1 PHE A 145 4097 2832 4140 -56 -1090 -433 C ATOM 1919 CE2 PHE A 145 10.123 3.851 8.626 1.00 23.17 C ANISOU 1919 CE2 PHE A 145 2709 2516 3577 -154 41 -140 C ATOM 1920 CZ PHE A 145 9.289 3.413 7.649 1.00 25.93 C ANISOU 1920 CZ PHE A 145 3480 2828 3543 -14 -294 -255 C ATOM 1921 H PHE A 145 11.480 8.160 8.367 1.00 13.86 H ANISOU 1921 H PHE A 145 1916 1884 1464 -139 -143 128 H ATOM 1922 HA PHE A 145 9.114 8.262 7.031 1.00 16.27 H ANISOU 1922 HA PHE A 145 2034 2432 1716 -302 -366 -2 H ATOM 1923 HB2 PHE A 145 9.603 7.586 9.726 1.00 16.17 H ANISOU 1923 HB2 PHE A 145 2159 2160 1822 -18 -59 586 H ATOM 1924 HB3 PHE A 145 8.146 7.690 9.104 1.00 18.13 H ANISOU 1924 HB3 PHE A 145 2075 2645 2168 -230 -104 339 H ATOM 1925 HD1 PHE A 145 7.702 6.165 7.104 1.00 20.83 H ANISOU 1925 HD1 PHE A 145 2576 2949 2386 -133 -297 -109 H ATOM 1926 HD2 PHE A 145 10.628 5.468 9.710 1.00 19.04 H ANISOU 1926 HD2 PHE A 145 2443 2180 2608 232 -28 311 H ATOM 1927 HE1 PHE A 145 7.811 3.969 6.411 1.00 23.29 H ANISOU 1927 HE1 PHE A 145 3122 2732 2995 -285 3 -209 H ATOM 1928 HE2 PHE A 145 10.736 3.269 9.015 1.00 22.74 H ANISOU 1928 HE2 PHE A 145 3051 2363 3225 3 92 -239 H ATOM 1929 HZ PHE A 145 9.328 2.527 7.369 1.00 24.42 H ANISOU 1929 HZ PHE A 145 3350 2862 3066 -116 -9 -201 H ATOM 1930 N TYR A 146 10.248 10.825 8.009 1.00 15.02 N ANISOU 1930 N TYR A 146 1934 2035 1734 14 9 365 N ATOM 1931 CA TYR A 146 10.042 12.247 8.229 1.00 14.13 C ANISOU 1931 CA TYR A 146 1788 2087 1492 -75 -280 203 C ATOM 1932 C TYR A 146 8.921 12.809 7.339 1.00 14.04 C ANISOU 1932 C TYR A 146 1927 1986 1422 -109 -267 269 C ATOM 1933 O TYR A 146 8.823 12.508 6.155 1.00 14.31 O ANISOU 1933 O TYR A 146 1961 2015 1459 -78 -386 304 O ATOM 1934 CB TYR A 146 11.334 13.008 7.955 1.00 14.75 C ANISOU 1934 CB TYR A 146 1948 1913 1742 -106 -123 220 C ATOM 1935 CG TYR A 146 11.162 14.514 7.890 1.00 14.20 C ANISOU 1935 CG TYR A 146 1838 1931 1626 -148 -42 231 C ATOM 1936 CD1 TYR A 146 11.087 15.271 9.037 1.00 14.19 C ANISOU 1936 CD1 TYR A 146 1881 1992 1515 164 -142 278 C ATOM 1937 CD2 TYR A 146 11.039 15.160 6.662 1.00 13.04 C ANISOU 1937 CD2 TYR A 146 1812 1798 1343 -105 327 34 C ATOM 1938 CE1 TYR A 146 10.941 16.648 8.986 1.00 13.73 C ANISOU 1938 CE1 TYR A 146 1782 1942 1491 30 -261 134 C ATOM 1939 CE2 TYR A 146 10.851 16.522 6.604 1.00 13.08 C ANISOU 1939 CE2 TYR A 146 1795 1806 1366 -89 -62 145 C ATOM 1940 CZ TYR A 146 10.812 17.269 7.755 1.00 13.33 C ANISOU 1940 CZ TYR A 146 1804 1808 1452 222 -53 70 C ATOM 1941 OH TYR A 146 10.672 18.648 7.627 1.00 14.35 O ANISOU 1941 OH TYR A 146 1941 1806 1704 133 -201 247 O ATOM 1942 H TYR A 146 11.039 10.629 7.739 1.00 14.95 H ANISOU 1942 H TYR A 146 1903 2151 1625 -2 -110 158 H ATOM 1943 HA TYR A 146 9.799 12.389 9.168 1.00 14.31 H ANISOU 1943 HA TYR A 146 1707 2211 1519 88 -236 267 H ATOM 1944 HB2 TYR A 146 11.968 12.814 8.663 1.00 13.94 H ANISOU 1944 HB2 TYR A 146 1688 1852 1754 -45 -39 52 H ATOM 1945 HB3 TYR A 146 11.696 12.717 7.103 1.00 14.84 H ANISOU 1945 HB3 TYR A 146 1897 1962 1777 -128 -111 141 H ATOM 1946 HD1 TYR A 146 11.179 14.854 9.863 1.00 14.04 H ANISOU 1946 HD1 TYR A 146 1807 1966 1558 -6 -161 281 H ATOM 1947 HD2 TYR A 146 11.063 14.664 5.876 1.00 13.93 H ANISOU 1947 HD2 TYR A 146 1838 1916 1537 -201 46 -142 H ATOM 1948 HE1 TYR A 146 10.906 17.147 9.770 1.00 14.17 H ANISOU 1948 HE1 TYR A 146 1845 2050 1487 -14 -175 108 H ATOM 1949 HE2 TYR A 146 10.791 16.944 5.779 1.00 13.33 H ANISOU 1949 HE2 TYR A 146 1760 1902 1402 -98 -57 172 H ATOM 1950 N LYS A 147 8.105 13.658 7.961 1.00 14.96 N ANISOU 1950 N LYS A 147 1966 2173 1544 44 -217 348 N ATOM 1951 CA LYS A 147 6.986 14.318 7.288 1.00 15.01 C ANISOU 1951 CA LYS A 147 1900 2158 1643 17 -205 411 C ATOM 1952 C LYS A 147 7.015 15.848 7.420 1.00 14.72 C ANISOU 1952 C LYS A 147 1644 2125 1824 8 -181 339 C ATOM 1953 O LYS A 147 6.863 16.525 6.397 1.00 16.29 O ANISOU 1953 O LYS A 147 2047 2172 1968 -17 -436 422 O ATOM 1954 CB LYS A 147 5.625 13.808 7.801 1.00 17.53 C ANISOU 1954 CB LYS A 147 2014 2387 2257 -35 6 454 C ATOM 1955 CG LYS A 147 5.376 12.328 7.542 1.00 21.70 C ANISOU 1955 CG LYS A 147 2854 2396 2992 -160 -17 443 C ATOM 1956 CD LYS A 147 4.033 11.888 8.143 1.00 25.98 C ANISOU 1956 CD LYS A 147 3206 2984 3678 -748 226 28 C ATOM 1957 CE LYS A 147 2.889 12.075 7.172 0.50 29.57 C ANISOU 1957 CE LYS A 147 3255 3710 4268 -354 -111 -58 C ATOM 1958 NZ LYS A 147 1.558 11.884 7.822 0.50 36.19 N ANISOU 1958 NZ LYS A 147 3404 4977 5368 270 419 523 N ATOM 1959 H LYS A 147 8.176 13.870 8.791 1.00 14.44 H ANISOU 1959 H LYS A 147 1705 2105 1674 -10 -248 136 H ATOM 1960 HA LYS A 147 7.022 14.116 6.330 1.00 15.13 H ANISOU 1960 HA LYS A 147 1797 2251 1701 84 -304 246 H ATOM 1961 HB2 LYS A 147 5.583 13.954 8.759 1.00 18.15 H ANISOU 1961 HB2 LYS A 147 1926 2719 2251 -2 118 423 H ATOM 1962 HB3 LYS A 147 4.918 14.307 7.362 1.00 17.48 H ANISOU 1962 HB3 LYS A 147 1896 2477 2267 58 -11 174 H ATOM 1963 HG2 LYS A 147 5.355 12.166 6.586 1.00 21.69 H ANISOU 1963 HG2 LYS A 147 2743 2474 3024 -11 -239 161 H ATOM 1964 HG3 LYS A 147 6.081 11.806 7.957 1.00 21.26 H ANISOU 1964 HG3 LYS A 147 3113 2313 2651 47 -24 141 H ATOM 1965 HD2 LYS A 147 4.083 10.946 8.370 1.00 25.26 H ANISOU 1965 HD2 LYS A 147 3034 3025 3537 -572 470 89 H ATOM 1966 HD3 LYS A 147 3.845 12.411 8.938 1.00 25.20 H ANISOU 1966 HD3 LYS A 147 3004 3018 3551 -88 313 284 H ATOM 1967 HE2 LYS A 147 2.931 12.967 6.795 0.50 30.59 H ANISOU 1967 HE2 LYS A 147 3861 3678 4080 27 -51 -75 H ATOM 1968 HE3 LYS A 147 2.965 11.412 6.471 0.50 28.88 H ANISOU 1968 HE3 LYS A 147 3559 3584 3828 -164 -250 197 H ATOM 1969 N GLU A 148 7.185 16.384 8.636 1.00 16.07 N ANISOU 1969 N GLU A 148 2123 2111 1870 -4 -184 303 N ATOM 1970 CA GLU A 148 6.950 17.809 8.938 1.00 16.44 C ANISOU 1970 CA GLU A 148 2124 2156 1965 -34 -193 233 C ATOM 1971 C GLU A 148 7.856 18.359 10.017 1.00 17.38 C ANISOU 1971 C GLU A 148 2101 2396 2105 143 -105 -154 C ATOM 1972 O GLU A 148 8.174 17.663 10.973 1.00 19.35 O ANISOU 1972 O GLU A 148 2314 2673 2364 127 -111 207 O ATOM 1973 CB GLU A 148 5.514 18.024 9.476 1.00 18.00 C ANISOU 1973 CB GLU A 148 2198 2502 2137 183 -202 39 C ATOM 1974 CG GLU A 148 4.385 17.734 8.502 1.00 17.46 C ANISOU 1974 CG GLU A 148 2219 2534 1879 100 -59 -9 C ATOM 1975 CD GLU A 148 4.296 18.697 7.331 1.00 17.27 C ANISOU 1975 CD GLU A 148 2499 2536 1524 357 -165 -237 C ATOM 1976 OE1 GLU A 148 4.795 19.849 7.414 1.00 17.23 O ANISOU 1976 OE1 GLU A 148 2576 2652 1319 301 -350 19 O ATOM 1977 OE2 GLU A 148 3.745 18.324 6.272 1.00 18.23 O ANISOU 1977 OE2 GLU A 148 2532 2655 1740 181 -452 13 O ATOM 1978 H GLU A 148 7.438 15.933 9.323 1.00 15.24 H ANISOU 1978 H GLU A 148 1880 2154 1757 42 -100 211 H ATOM 1979 HA GLU A 148 7.065 18.345 8.127 1.00 17.19 H ANISOU 1979 HA GLU A 148 2452 2038 2038 16 -135 223 H ATOM 1980 HB2 GLU A 148 5.388 17.440 10.240 1.00 16.64 H ANISOU 1980 HB2 GLU A 148 1895 2293 2132 110 -151 -62 H ATOM 1981 HB3 GLU A 148 5.422 18.947 9.761 1.00 17.58 H ANISOU 1981 HB3 GLU A 148 2163 2409 2105 -17 -112 97 H ATOM 1982 HG2 GLU A 148 4.500 16.841 8.143 1.00 17.92 H ANISOU 1982 HG2 GLU A 148 2098 2433 2277 -7 18 -21 H ATOM 1983 HG3 GLU A 148 3.545 17.783 8.983 1.00 17.74 H ANISOU 1983 HG3 GLU A 148 2152 2393 2194 9 -14 -19 H ATOM 1984 N GLY A 149 8.163 19.646 9.894 1.00 17.88 N ANISOU 1984 N GLY A 149 2086 2524 2183 -117 -216 195 N ATOM 1985 CA GLY A 149 8.799 20.408 10.958 1.00 18.44 C ANISOU 1985 CA GLY A 149 2188 2481 2335 96 -146 -6 C ATOM 1986 C GLY A 149 10.296 20.285 10.935 1.00 15.38 C ANISOU 1986 C GLY A 149 2170 1993 1678 125 -341 -58 C ATOM 1987 O GLY A 149 10.889 19.859 9.946 1.00 15.81 O ANISOU 1987 O GLY A 149 2222 1991 1792 -117 -77 -5 O ATOM 1988 H GLY A 149 8.009 20.113 9.189 1.00 18.29 H ANISOU 1988 H GLY A 149 2299 2537 2111 227 -37 103 H ATOM 1989 HA2 GLY A 149 8.478 20.104 11.822 1.00 18.20 H ANISOU 1989 HA2 GLY A 149 2235 2392 2284 89 -128 -72 H ATOM 1990 HA3 GLY A 149 8.570 21.345 10.862 1.00 18.13 H ANISOU 1990 HA3 GLY A 149 1921 2461 2507 58 -62 43 H ATOM 1991 N ILE A 150 10.910 20.700 12.026 1.00 15.39 N ANISOU 1991 N ILE A 150 2332 2180 1332 77 -188 112 N ATOM 1992 CA ILE A 150 12.355 20.739 12.074 1.00 15.51 C ANISOU 1992 CA ILE A 150 2233 1979 1679 126 -139 -120 C ATOM 1993 C ILE A 150 12.816 19.366 12.570 1.00 15.42 C ANISOU 1993 C ILE A 150 2289 2006 1562 -23 -322 43 C ATOM 1994 O ILE A 150 12.410 18.923 13.659 1.00 19.59 O ANISOU 1994 O ILE A 150 3323 2287 1832 115 125 155 O ATOM 1995 CB ILE A 150 12.896 21.859 12.982 1.00 16.10 C ANISOU 1995 CB ILE A 150 2378 2129 1608 -20 -24 -132 C ATOM 1996 CG1 ILE A 150 12.479 23.244 12.433 1.00 18.28 C ANISOU 1996 CG1 ILE A 150 2820 2132 1992 162 148 -151 C ATOM 1997 CG2 ILE A 150 14.425 21.742 13.107 1.00 18.38 C ANISOU 1997 CG2 ILE A 150 2361 2510 2113 -135 -181 -410 C ATOM 1998 CD1 ILE A 150 12.818 24.415 13.398 1.00 21.83 C ANISOU 1998 CD1 ILE A 150 3919 2281 2095 -209 116 -200 C ATOM 1999 H ILE A 150 10.517 20.962 12.746 1.00 15.61 H ANISOU 1999 H ILE A 150 2230 1958 1742 46 -69 -190 H ATOM 2000 HA ILE A 150 12.709 20.895 11.175 1.00 14.93 H ANISOU 2000 HA ILE A 150 2250 1712 1710 17 -154 -59 H ATOM 2001 HB ILE A 150 12.509 21.746 13.864 1.00 17.08 H ANISOU 2001 HB ILE A 150 2600 2170 1718 -106 131 -229 H ATOM 2002 HG12 ILE A 150 12.935 23.406 11.592 1.00 17.09 H ANISOU 2002 HG12 ILE A 150 2476 1989 2027 41 23 -31 H ATOM 2003 HG13 ILE A 150 11.519 23.250 12.292 1.00 17.85 H ANISOU 2003 HG13 ILE A 150 2722 2098 1962 182 260 93 H ATOM 2004 N TYR A 151 13.641 18.724 11.742 1.00 14.86 N ANISOU 2004 N TYR A 151 2052 1789 1801 7 -219 329 N ATOM 2005 CA TYR A 151 14.173 17.410 11.990 1.00 13.79 C ANISOU 2005 CA TYR A 151 1972 1784 1481 -56 -270 313 C ATOM 2006 C TYR A 151 15.319 17.480 13.001 1.00 13.79 C ANISOU 2006 C TYR A 151 2239 1791 1206 -31 -299 354 C ATOM 2007 O TYR A 151 16.300 18.192 12.817 1.00 14.02 O ANISOU 2007 O TYR A 151 2243 1863 1218 -122 -223 156 O ATOM 2008 CB TYR A 151 14.677 16.775 10.711 1.00 14.60 C ANISOU 2008 CB TYR A 151 2122 1808 1615 -88 -276 195 C ATOM 2009 CG TYR A 151 15.218 15.376 10.946 1.00 13.72 C ANISOU 2009 CG TYR A 151 2092 1830 1289 -68 -97 182 C ATOM 2010 CD1 TYR A 151 14.366 14.310 11.155 1.00 13.65 C ANISOU 2010 CD1 TYR A 151 2006 1859 1320 -121 -383 107 C ATOM 2011 CD2 TYR A 151 16.571 15.130 10.945 1.00 15.27 C ANISOU 2011 CD2 TYR A 151 2035 1891 1876 -96 29 330 C ATOM 2012 CE1 TYR A 151 14.853 13.024 11.359 1.00 14.50 C ANISOU 2012 CE1 TYR A 151 2099 1794 1615 -165 -312 69 C ATOM 2013 CE2 TYR A 151 17.073 13.861 11.143 1.00 15.01 C ANISOU 2013 CE2 TYR A 151 2003 1933 1767 -47 -270 209 C ATOM 2014 CZ TYR A 151 16.204 12.811 11.368 1.00 13.56 C ANISOU 2014 CZ TYR A 151 2059 1934 1159 -59 -310 165 C ATOM 2015 OH TYR A 151 16.735 11.561 11.566 1.00 14.84 O ANISOU 2015 OH TYR A 151 2163 1844 1629 -53 -206 21 O ATOM 2016 H TYR A 151 13.916 19.059 10.999 1.00 14.30 H ANISOU 2016 H TYR A 151 2089 1578 1764 -5 -189 213 H ATOM 2017 HA TYR A 151 13.464 16.838 12.351 1.00 14.91 H ANISOU 2017 HA TYR A 151 1992 1751 1921 -31 -86 259 H ATOM 2018 HB2 TYR A 151 13.945 16.712 10.078 1.00 13.98 H ANISOU 2018 HB2 TYR A 151 1790 1891 1628 23 -78 32 H ATOM 2019 HB3 TYR A 151 15.390 17.321 10.343 1.00 13.85 H ANISOU 2019 HB3 TYR A 151 1842 1696 1723 75 -187 53 H ATOM 2020 HD1 TYR A 151 13.448 14.455 11.157 1.00 14.31 H ANISOU 2020 HD1 TYR A 151 1994 2003 1439 -87 -226 55 H ATOM 2021 HD2 TYR A 151 17.160 15.834 10.804 1.00 14.82 H ANISOU 2021 HD2 TYR A 151 2051 1864 1716 -133 -86 118 H ATOM 2022 HE1 TYR A 151 14.266 12.320 11.508 1.00 13.81 H ANISOU 2022 HE1 TYR A 151 2046 1799 1402 -92 -142 38 H ATOM 2023 HE2 TYR A 151 17.992 13.718 11.148 1.00 14.95 H ANISOU 2023 HE2 TYR A 151 1984 2067 1629 -29 -187 101 H ATOM 2024 N PHE A 152 15.189 16.719 14.084 1.00 13.80 N ANISOU 2024 N PHE A 152 2117 2192 931 -69 -85 280 N ATOM 2025 CA PHE A 152 16.209 16.553 15.112 1.00 14.68 C ANISOU 2025 CA PHE A 152 2344 2042 1192 87 -353 295 C ATOM 2026 C PHE A 152 16.162 15.085 15.543 1.00 15.33 C ANISOU 2026 C PHE A 152 2190 1892 1740 -93 -218 73 C ATOM 2027 O PHE A 152 15.130 14.589 15.946 1.00 17.25 O ANISOU 2027 O PHE A 152 2259 2472 1823 18 -21 551 O ATOM 2028 CB PHE A 152 15.960 17.455 16.328 1.00 16.12 C ANISOU 2028 CB PHE A 152 2498 2155 1473 54 -156 78 C ATOM 2029 CG PHE A 152 17.066 17.406 17.359 1.00 16.75 C ANISOU 2029 CG PHE A 152 2523 2427 1412 208 -160 -68 C ATOM 2030 CD1 PHE A 152 18.212 18.175 17.204 1.00 19.89 C ANISOU 2030 CD1 PHE A 152 2714 2986 1856 -109 -173 155 C ATOM 2031 CD2 PHE A 152 16.966 16.578 18.471 1.00 20.04 C ANISOU 2031 CD2 PHE A 152 2639 2884 2088 60 -536 573 C ATOM 2032 CE1 PHE A 152 19.224 18.133 18.135 1.00 24.46 C ANISOU 2032 CE1 PHE A 152 2841 3802 2648 -246 -602 288 C ATOM 2033 CE2 PHE A 152 17.987 16.517 19.418 1.00 20.16 C ANISOU 2033 CE2 PHE A 152 3111 2721 1825 162 -733 68 C ATOM 2034 CZ PHE A 152 19.106 17.296 19.247 1.00 23.83 C ANISOU 2034 CZ PHE A 152 2791 3941 2321 8 -513 194 C ATOM 2035 H PHE A 152 14.475 16.269 14.255 1.00 13.65 H ANISOU 2035 H PHE A 152 2022 1812 1352 79 -74 276 H ATOM 2036 HA PHE A 152 17.093 16.756 14.746 1.00 14.45 H ANISOU 2036 HA PHE A 152 2191 1668 1628 139 -299 72 H ATOM 2037 HB2 PHE A 152 15.879 18.373 16.024 1.00 16.41 H ANISOU 2037 HB2 PHE A 152 2207 2094 1934 109 -171 54 H ATOM 2038 HB3 PHE A 152 15.136 17.180 16.760 1.00 16.70 H ANISOU 2038 HB3 PHE A 152 2391 2073 1880 165 -30 24 H ATOM 2039 HD1 PHE A 152 18.292 18.733 16.466 1.00 19.98 H ANISOU 2039 HD1 PHE A 152 2919 2383 2288 9 -124 202 H ATOM 2040 HD2 PHE A 152 16.207 16.052 18.583 1.00 18.64 H ANISOU 2040 HD2 PHE A 152 2619 2590 1870 169 -269 279 H ATOM 2041 HE1 PHE A 152 19.985 18.655 18.022 1.00 22.63 H ANISOU 2041 HE1 PHE A 152 2648 3216 2734 80 -363 -63 H ATOM 2042 HE2 PHE A 152 17.907 15.964 20.161 1.00 19.89 H ANISOU 2042 HE2 PHE A 152 2871 2597 2091 589 -600 200 H ATOM 2043 HZ PHE A 152 19.790 17.265 19.876 1.00 22.35 H ANISOU 2043 HZ PHE A 152 2498 3676 2317 343 -316 -77 H ATOM 2044 N GLU A 153 17.301 14.424 15.464 1.00 14.59 N ANISOU 2044 N GLU A 153 2240 1812 1492 -3 -269 118 N ATOM 2045 CA GLU A 153 17.441 13.023 15.811 1.00 13.65 C ANISOU 2045 CA GLU A 153 2074 1876 1234 -9 -112 194 C ATOM 2046 C GLU A 153 18.541 12.913 16.866 1.00 15.14 C ANISOU 2046 C GLU A 153 2532 1889 1331 -42 -372 220 C ATOM 2047 O GLU A 153 19.707 13.128 16.560 1.00 15.83 O ANISOU 2047 O GLU A 153 2462 2230 1322 -50 -431 8 O ATOM 2048 CB GLU A 153 17.745 12.229 14.540 1.00 14.57 C ANISOU 2048 CB GLU A 153 2097 1937 1499 -31 -254 -20 C ATOM 2049 CG GLU A 153 18.201 10.763 14.777 1.00 15.55 C ANISOU 2049 CG GLU A 153 2231 1886 1790 -4 -353 42 C ATOM 2050 CD GLU A 153 17.290 9.995 15.718 1.00 15.95 C ANISOU 2050 CD GLU A 153 2066 2103 1890 187 -369 343 C ATOM 2051 OE1 GLU A 153 16.119 9.771 15.361 1.00 16.28 O ANISOU 2051 OE1 GLU A 153 2314 2045 1827 -162 -451 312 O ATOM 2052 OE2 GLU A 153 17.748 9.625 16.830 1.00 17.37 O ANISOU 2052 OE2 GLU A 153 2645 2253 1700 97 -484 197 O ATOM 2053 H GLU A 153 18.030 14.768 15.188 1.00 15.11 H ANISOU 2053 H GLU A 153 2205 1746 1788 16 -247 168 H ATOM 2054 HA GLU A 153 16.602 12.681 16.178 1.00 15.45 H ANISOU 2054 HA GLU A 153 2087 1924 1858 -4 62 162 H ATOM 2055 HB2 GLU A 153 16.936 12.197 14.010 1.00 14.20 H ANISOU 2055 HB2 GLU A 153 1952 1889 1552 41 -154 -103 H ATOM 2056 HB3 GLU A 153 18.445 12.683 14.046 1.00 13.86 H ANISOU 2056 HB3 GLU A 153 1908 1758 1600 184 -54 -182 H ATOM 2057 HG2 GLU A 153 18.204 10.298 13.926 1.00 15.97 H ANISOU 2057 HG2 GLU A 153 2190 1942 1935 4 -149 -87 H ATOM 2058 HG3 GLU A 153 19.096 10.762 15.153 1.00 16.02 H ANISOU 2058 HG3 GLU A 153 2062 2138 1884 135 -173 -8 H ATOM 2059 N PRO A 154 18.188 12.564 18.130 1.00 15.63 N ANISOU 2059 N PRO A 154 2476 2142 1319 97 -415 208 N ATOM 2060 CA PRO A 154 19.200 12.512 19.195 1.00 17.20 C ANISOU 2060 CA PRO A 154 2646 2518 1370 -63 -534 -185 C ATOM 2061 C PRO A 154 20.373 11.581 18.886 1.00 16.93 C ANISOU 2061 C PRO A 154 2432 2228 1771 -81 -604 165 C ATOM 2062 O PRO A 154 21.485 11.836 19.352 1.00 18.59 O ANISOU 2062 O PRO A 154 2697 2420 1943 -123 -958 85 O ATOM 2063 CB PRO A 154 18.414 12.016 20.402 1.00 18.90 C ANISOU 2063 CB PRO A 154 3137 2581 1463 400 -140 27 C ATOM 2064 CG PRO A 154 17.011 12.372 20.132 1.00 20.46 C ANISOU 2064 CG PRO A 154 3029 2942 1801 64 -116 43 C ATOM 2065 CD PRO A 154 16.827 12.342 18.651 1.00 18.41 C ANISOU 2065 CD PRO A 154 2504 2620 1868 42 -359 305 C ATOM 2066 HA PRO A 154 19.541 13.411 19.381 1.00 18.26 H ANISOU 2066 HA PRO A 154 2474 2432 2031 14 -500 -149 H ATOM 2067 HB2 PRO A 154 18.510 11.055 20.488 1.00 19.34 H ANISOU 2067 HB2 PRO A 154 2871 2409 2065 -164 -77 -163 H ATOM 2068 HB3 PRO A 154 18.731 12.465 21.201 1.00 17.99 H ANISOU 2068 HB3 PRO A 154 2613 2423 1799 -71 217 -200 H ATOM 2069 HG2 PRO A 154 16.429 11.723 20.557 1.00 19.86 H ANISOU 2069 HG2 PRO A 154 3107 2607 1832 229 -127 116 H ATOM 2070 HG3 PRO A 154 16.833 13.261 20.477 1.00 18.89 H ANISOU 2070 HG3 PRO A 154 2368 2783 2025 -14 -132 142 H ATOM 2071 HD2 PRO A 154 16.492 11.477 18.368 1.00 17.25 H ANISOU 2071 HD2 PRO A 154 2280 2443 1829 225 -151 232 H ATOM 2072 HD3 PRO A 154 16.235 13.061 18.379 1.00 18.07 H ANISOU 2072 HD3 PRO A 154 2432 2346 2086 22 -150 117 H ATOM 2073 N ASP A 155 20.141 10.513 18.116 1.00 15.97 N ANISOU 2073 N ASP A 155 2247 2168 1653 -241 -388 285 N ATOM 2074 CA ASP A 155 21.210 9.564 17.800 1.00 17.03 C ANISOU 2074 CA ASP A 155 2359 2250 1860 -113 -509 152 C ATOM 2075 C ASP A 155 21.916 9.879 16.461 1.00 17.50 C ANISOU 2075 C ASP A 155 2504 2125 2021 180 -347 338 C ATOM 2076 O ASP A 155 22.575 9.021 15.931 1.00 17.62 O ANISOU 2076 O ASP A 155 2726 2438 1527 330 -425 411 O ATOM 2077 CB ASP A 155 20.628 8.131 17.789 1.00 17.49 C ANISOU 2077 CB ASP A 155 2477 2243 1925 -195 -405 130 C ATOM 2078 CG ASP A 155 21.696 7.032 17.913 1.00 22.20 C ANISOU 2078 CG ASP A 155 2723 2611 3100 163 -444 -203 C ATOM 2079 OD1 ASP A 155 22.703 7.245 18.602 1.00 21.66 O ANISOU 2079 OD1 ASP A 155 3067 2526 2635 -103 -611 580 O ATOM 2080 OD2 ASP A 155 21.532 5.929 17.322 1.00 21.62 O ANISOU 2080 OD2 ASP A 155 3412 2728 2076 105 -445 -55 O ATOM 2081 H ASP A 155 19.380 10.312 17.770 1.00 16.11 H ANISOU 2081 H ASP A 155 2158 2216 1745 -259 -254 152 H ATOM 2082 HA ASP A 155 21.889 9.599 18.505 1.00 17.10 H ANISOU 2082 HA ASP A 155 2064 2537 1894 -177 -354 39 H ATOM 2083 HB2 ASP A 155 20.016 8.037 18.535 1.00 18.43 H ANISOU 2083 HB2 ASP A 155 2637 2276 2087 -154 -195 70 H ATOM 2084 HB3 ASP A 155 20.153 7.996 16.955 1.00 18.45 H ANISOU 2084 HB3 ASP A 155 2351 2625 2031 -292 -338 -161 H ATOM 2085 N CYS A 156 21.807 11.114 15.942 1.00 15.58 N ANISOU 2085 N CYS A 156 2382 2105 1432 29 -120 135 N ATOM 2086 CA CYS A 156 22.484 11.472 14.710 1.00 15.60 C ANISOU 2086 CA CYS A 156 2287 2079 1558 89 -80 193 C ATOM 2087 C CYS A 156 23.981 11.614 14.956 1.00 17.94 C ANISOU 2087 C CYS A 156 2267 2243 2307 54 -141 203 C ATOM 2088 O CYS A 156 24.404 11.976 16.040 1.00 23.42 O ANISOU 2088 O CYS A 156 2340 3702 2855 -24 -314 -557 O ATOM 2089 CB CYS A 156 21.925 12.779 14.106 1.00 15.93 C ANISOU 2089 CB CYS A 156 2366 1893 1793 0 85 159 C ATOM 2090 SG CYS A 156 21.443 12.521 12.424 1.00 16.74 S ANISOU 2090 SG CYS A 156 2334 1997 2029 -87 -388 352 S ATOM 2091 H CYS A 156 21.353 11.752 16.294 1.00 15.55 H ANISOU 2091 H CYS A 156 2170 1982 1754 -60 18 210 H ATOM 2092 HA CYS A 156 22.349 10.755 14.056 1.00 15.32 H ANISOU 2092 HA CYS A 156 2134 2002 1685 175 139 103 H ATOM 2093 HB2 CYS A 156 21.142 13.069 14.595 1.00 16.63 H ANISOU 2093 HB2 CYS A 156 2058 2076 2181 11 -43 133 H ATOM 2094 HB3 CYS A 156 22.605 13.470 14.124 1.00 15.53 H ANISOU 2094 HB3 CYS A 156 2065 1996 1837 90 -37 96 H ATOM 2095 N SER A 157 24.755 11.296 13.932 1.00 16.24 N ANISOU 2095 N SER A 157 2048 2004 2119 6 -387 277 N ATOM 2096 CA SER A 157 26.201 11.395 13.948 1.00 15.79 C ANISOU 2096 CA SER A 157 2102 2172 1725 -39 -436 463 C ATOM 2097 C SER A 157 26.652 12.573 13.103 1.00 17.13 C ANISOU 2097 C SER A 157 2247 2267 1991 -196 -424 568 C ATOM 2098 O SER A 157 26.097 12.831 12.014 1.00 17.26 O ANISOU 2098 O SER A 157 2421 2062 2075 21 -523 562 O ATOM 2099 CB SER A 157 26.818 10.138 13.335 1.00 17.94 C ANISOU 2099 CB SER A 157 2210 2217 2386 229 -307 588 C ATOM 2100 OG SER A 157 28.236 10.251 13.288 1.00 17.35 O ANISOU 2100 OG SER A 157 2150 2588 1853 248 -239 714 O ATOM 2101 H SER A 157 24.450 11.011 13.179 1.00 16.31 H ANISOU 2101 H SER A 157 1973 2099 2122 -63 -314 246 H ATOM 2102 HA SER A 157 26.534 11.495 14.864 1.00 17.36 H ANISOU 2102 HA SER A 157 2178 2674 1742 -105 -449 507 H ATOM 2103 HB2 SER A 157 26.580 9.370 13.879 1.00 17.71 H ANISOU 2103 HB2 SER A 157 2469 2101 2158 -96 -131 224 H ATOM 2104 HB3 SER A 157 26.480 10.024 12.433 1.00 16.66 H ANISOU 2104 HB3 SER A 157 1965 2110 2253 47 -16 310 H ATOM 2105 N ASER A 158 27.661 13.288 13.598 0.70 17.88 N ANISOU 2105 N ASER A 158 2305 2346 2142 -115 -725 741 N ATOM 2106 CA ASER A 158 28.323 14.327 12.820 0.70 17.53 C ANISOU 2106 CA ASER A 158 2290 2215 2156 -70 -616 646 C ATOM 2107 C ASER A 158 29.578 13.834 12.078 0.70 17.42 C ANISOU 2107 C ASER A 158 2201 2430 1986 -425 -578 227 C ATOM 2108 O ASER A 158 30.249 14.629 11.421 0.70 20.83 O ANISOU 2108 O ASER A 158 2496 3102 2313 -558 -724 943 O ATOM 2109 CB ASER A 158 28.694 15.512 13.720 0.70 21.09 C ANISOU 2109 CB ASER A 158 3390 2334 2288 -45 -444 317 C ATOM 2110 OG ASER A 158 27.566 16.030 14.423 0.70 21.14 O ANISOU 2110 OG ASER A 158 2487 2459 3085 -179 -708 563 O ATOM 2111 H ASER A 158 27.985 13.188 14.389 0.70 16.21 H ANISOU 2111 H ASER A 158 2131 2218 1809 100 -343 357 H ATOM 2112 HA ASER A 158 27.703 14.665 12.146 0.70 17.72 H ANISOU 2112 HA ASER A 158 2533 2384 1815 202 -395 604 H ATOM 2113 HB2ASER A 158 29.356 15.218 14.365 0.70 18.44 H ANISOU 2113 HB2ASER A 158 2555 2243 2207 -160 -146 7 H ATOM 2114 HB3ASER A 158 29.064 16.219 13.169 0.70 20.98 H ANISOU 2114 HB3ASER A 158 3148 2235 2589 -157 -379 191 H ATOM 2115 N BSER A 158 27.682 13.273 13.567 0.30 17.78 N ANISOU 2115 N BSER A 158 2208 2350 2195 -145 -444 431 N ATOM 2116 CA BSER A 158 28.314 14.314 12.766 0.30 17.85 C ANISOU 2116 CA BSER A 158 2352 2265 2163 -188 -345 311 C ATOM 2117 C BSER A 158 29.591 13.836 12.074 0.30 17.83 C ANISOU 2117 C BSER A 158 2348 2445 1981 -322 -288 196 C ATOM 2118 O BSER A 158 30.297 14.639 11.462 0.30 19.72 O ANISOU 2118 O BSER A 158 2424 2924 2144 -411 -509 733 O ATOM 2119 CB BSER A 158 28.627 15.524 13.635 0.30 17.95 C ANISOU 2119 CB BSER A 158 2530 2212 2076 36 -294 271 C ATOM 2120 OG BSER A 158 29.401 15.141 14.753 0.30 19.28 O ANISOU 2120 OG BSER A 158 2388 2633 2304 -52 -532 175 O ATOM 2121 H BSER A 158 28.036 13.166 14.343 0.30 16.42 H ANISOU 2121 H BSER A 158 2020 2229 1989 -8 -221 174 H ATOM 2122 HA BSER A 158 27.697 14.610 12.069 0.30 17.80 H ANISOU 2122 HA BSER A 158 2494 2284 1985 -57 -235 293 H ATOM 2123 HB2BSER A 158 29.125 16.171 13.111 0.30 17.93 H ANISOU 2123 HB2BSER A 158 2388 2179 2244 -46 -154 76 H ATOM 2124 HB3BSER A 158 27.795 15.915 13.945 0.30 18.06 H ANISOU 2124 HB3BSER A 158 2328 2423 2108 -81 -299 264 H ATOM 2125 N GLU A 159 29.886 12.541 12.172 1.00 19.41 N ANISOU 2125 N GLU A 159 2607 2686 2080 -32 -304 640 N ATOM 2126 CA GLU A 159 31.058 11.954 11.531 1.00 22.01 C ANISOU 2126 CA GLU A 159 2329 2646 3387 61 -236 654 C ATOM 2127 C GLU A 159 30.709 10.903 10.490 1.00 20.72 C ANISOU 2127 C GLU A 159 2864 2491 2515 305 -14 908 C ATOM 2128 O GLU A 159 31.416 10.766 9.492 1.00 25.52 O ANISOU 2128 O GLU A 159 2846 3829 3018 859 265 992 O ATOM 2129 CB GLU A 159 31.952 11.277 12.578 1.00 25.63 C ANISOU 2129 CB GLU A 159 3143 3559 3036 586 -325 638 C ATOM 2130 CG GLU A 159 32.297 12.111 13.805 1.00 31.41 C ANISOU 2130 CG GLU A 159 3512 4113 4306 145 -950 -72 C ATOM 2131 CD GLU A 159 33.105 11.328 14.850 0.50 30.74 C ANISOU 2131 CD GLU A 159 4061 4222 3393 -114 -741 -65 C ATOM 2132 OE1 GLU A 159 32.779 10.153 15.131 0.50 28.88 O ANISOU 2132 OE1 GLU A 159 4331 3996 2643 337 -524 -214 O ATOM 2133 OE2 GLU A 159 34.068 11.893 15.402 0.50 36.47 O ANISOU 2133 OE2 GLU A 159 3708 5548 4599 -293 -919 -176 O ATOM 2134 H GLU A 159 29.428 11.969 12.616 1.00 19.27 H ANISOU 2134 H GLU A 159 2620 2430 2270 -221 -305 329 H ATOM 2135 HA GLU A 159 31.599 12.639 11.086 1.00 22.02 H ANISOU 2135 HA GLU A 159 2681 2967 2718 -52 17 454 H ATOM 2136 HB2 GLU A 159 31.500 10.477 12.890 1.00 23.74 H ANISOU 2136 HB2 GLU A 159 3182 3350 2487 599 -303 407 H ATOM 2137 HB3 GLU A 159 32.787 11.029 12.152 1.00 26.34 H ANISOU 2137 HB3 GLU A 159 2717 3263 4026 468 -433 618 H ATOM 2138 HG2 GLU A 159 32.828 12.874 13.528 1.00 30.38 H ANISOU 2138 HG2 GLU A 159 3751 4104 3685 334 -202 -49 H ATOM 2139 HG3 GLU A 159 31.479 12.412 14.230 1.00 29.29 H ANISOU 2139 HG3 GLU A 159 3985 3650 3493 -193 -400 7 H ATOM 2140 N ASP A 160 29.643 10.143 10.744 1.00 18.53 N ANISOU 2140 N ASP A 160 2831 2466 1742 283 -275 739 N ATOM 2141 C ASP A 160 28.084 9.483 9.053 1.00 19.65 C ANISOU 2141 C ASP A 160 2398 2661 2405 -34 -295 887 C ATOM 2142 O ASP A 160 26.964 9.309 9.398 1.00 28.13 O ANISOU 2142 O ASP A 160 2608 4054 4025 229 71 2342 O ATOM 2143 H ASP A 160 29.118 10.261 11.413 1.00 19.97 H ANISOU 2143 H ASP A 160 2581 2587 2419 173 -55 203 H ATOM 2144 CA AASP A 160 29.247 9.017 9.902 0.50 19.15 C ANISOU 2144 CA AASP A 160 2612 2631 2031 422 -210 447 C ATOM 2145 CB AASP A 160 28.796 7.810 10.746 0.50 18.87 C ANISOU 2145 CB AASP A 160 2518 2533 2116 222 -270 343 C ATOM 2146 CG AASP A 160 29.950 7.042 11.387 0.50 21.11 C ANISOU 2146 CG AASP A 160 2839 2365 2817 420 -424 372 C ATOM 2147 OD1AASP A 160 31.134 7.298 11.078 0.50 17.93 O ANISOU 2147 OD1AASP A 160 2609 2145 2057 556 -868 56 O ATOM 2148 OD2AASP A 160 29.648 6.153 12.216 0.50 25.62 O ANISOU 2148 OD2AASP A 160 3590 2922 3221 9 -724 829 O ATOM 2149 HA AASP A 160 29.982 8.737 9.317 0.50 19.96 H ANISOU 2149 HA AASP A 160 2391 2674 2519 102 -50 262 H ATOM 2150 HB2AASP A 160 28.214 8.120 11.457 0.50 19.13 H ANISOU 2150 HB2AASP A 160 2378 2421 2467 20 -73 218 H ATOM 2151 HB3AASP A 160 28.315 7.188 10.176 0.50 20.46 H ANISOU 2151 HB3AASP A 160 2532 2768 2472 118 -157 67 H ATOM 2152 CA BASP A 160 29.263 9.027 9.896 0.50 19.05 C ANISOU 2152 CA BASP A 160 2640 2534 2064 477 -195 473 C ATOM 2153 CB BASP A 160 28.904 7.795 10.744 0.50 19.60 C ANISOU 2153 CB BASP A 160 2929 2342 2175 471 -244 460 C ATOM 2154 CG BASP A 160 29.922 7.513 11.849 0.50 19.80 C ANISOU 2154 CG BASP A 160 3074 2066 2384 331 -446 333 C ATOM 2155 OD1BASP A 160 31.085 7.953 11.735 0.50 25.83 O ANISOU 2155 OD1BASP A 160 2730 3184 3900 522 -454 382 O ATOM 2156 OD2BASP A 160 29.556 6.846 12.840 0.50 22.52 O ANISOU 2156 OD2BASP A 160 3564 2920 2072 761 -395 544 O ATOM 2157 HA BASP A 160 29.998 8.780 9.297 0.50 20.22 H ANISOU 2157 HA BASP A 160 2425 2700 2556 159 -55 224 H ATOM 2158 HB2BASP A 160 28.045 7.936 11.171 0.50 20.32 H ANISOU 2158 HB2BASP A 160 2714 2453 2553 9 -180 268 H ATOM 2159 HB3BASP A 160 28.864 7.016 10.168 0.50 20.43 H ANISOU 2159 HB3BASP A 160 2596 2636 2528 -19 -218 147 H ATOM 2160 N MET A 161 28.377 10.128 7.943 1.00 16.26 N ANISOU 2160 N MET A 161 2077 2246 1854 -70 -482 397 N ATOM 2161 CA MET A 161 27.345 10.553 6.972 1.00 15.02 C ANISOU 2161 CA MET A 161 1818 1998 1888 6 -358 342 C ATOM 2162 C MET A 161 27.199 9.482 5.890 1.00 15.30 C ANISOU 2162 C MET A 161 1939 1985 1888 65 -377 395 C ATOM 2163 O MET A 161 28.152 8.774 5.551 1.00 17.24 O ANISOU 2163 O MET A 161 2101 2561 1886 358 -262 385 O ATOM 2164 CB MET A 161 27.696 11.908 6.330 1.00 14.56 C ANISOU 2164 CB MET A 161 1785 2100 1648 83 -64 314 C ATOM 2165 CG MET A 161 27.722 13.096 7.318 1.00 14.62 C ANISOU 2165 CG MET A 161 2156 2216 1182 113 -228 481 C ATOM 2166 SD MET A 161 29.224 13.261 8.319 1.00 17.18 S ANISOU 2166 SD MET A 161 2372 2284 1870 142 -629 358 S ATOM 2167 CE MET A 161 30.408 13.623 7.003 1.00 20.94 C ANISOU 2167 CE MET A 161 2278 2859 2818 -176 -32 -25 C ATOM 2168 H MET A 161 29.176 10.343 7.708 1.00 15.56 H ANISOU 2168 H MET A 161 1931 2193 1789 229 -390 302 H ATOM 2169 HA MET A 161 26.485 10.662 7.430 1.00 15.44 H ANISOU 2169 HA MET A 161 1918 1925 2023 -83 -186 370 H ATOM 2170 HB2 MET A 161 28.567 11.834 5.911 1.00 15.59 H ANISOU 2170 HB2 MET A 161 1727 2199 1997 20 -35 165 H ATOM 2171 HB3 MET A 161 27.029 12.109 5.654 1.00 13.68 H ANISOU 2171 HB3 MET A 161 1776 1776 1646 109 -74 142 H ATOM 2172 HG2 MET A 161 27.619 13.917 6.812 1.00 14.29 H ANISOU 2172 HG2 MET A 161 1893 1944 1591 171 -201 359 H ATOM 2173 HG3 MET A 161 26.976 13.000 7.931 1.00 15.26 H ANISOU 2173 HG3 MET A 161 2133 1918 1744 13 3 243 H ATOM 2174 N ASP A 162 25.993 9.355 5.347 1.00 13.86 N ANISOU 2174 N ASP A 162 1826 1754 1685 33 -255 427 N ATOM 2175 CA ASP A 162 25.683 8.283 4.412 1.00 13.60 C ANISOU 2175 CA ASP A 162 1817 1865 1481 78 -28 391 C ATOM 2176 C ASP A 162 24.746 8.725 3.272 1.00 12.96 C ANISOU 2176 C ASP A 162 1911 1594 1417 199 -22 171 C ATOM 2177 O ASP A 162 24.219 7.896 2.554 1.00 14.21 O ANISOU 2177 O ASP A 162 2060 1600 1739 24 -75 192 O ATOM 2178 CB ASP A 162 25.053 7.103 5.173 1.00 14.71 C ANISOU 2178 CB ASP A 162 2062 1573 1953 75 -19 348 C ATOM 2179 CG ASP A 162 23.678 7.433 5.761 1.00 14.67 C ANISOU 2179 CG ASP A 162 2116 1631 1825 -2 118 389 C ATOM 2180 OD1 ASP A 162 23.209 8.574 5.622 1.00 14.10 O ANISOU 2180 OD1 ASP A 162 1982 1648 1725 84 -10 228 O ATOM 2181 OD2 ASP A 162 23.071 6.539 6.407 1.00 17.15 O ANISOU 2181 OD2 ASP A 162 2351 1715 2450 -82 521 409 O ATOM 2182 H ASP A 162 25.330 9.873 5.523 1.00 14.29 H ANISOU 2182 H ASP A 162 1789 1868 1769 -35 -124 217 H ATOM 2183 HA ASP A 162 26.508 7.959 3.994 1.00 14.90 H ANISOU 2183 HA ASP A 162 1667 2050 1945 57 -83 209 H ATOM 2184 HB2 ASP A 162 24.957 6.350 4.573 1.00 15.11 H ANISOU 2184 HB2 ASP A 162 2007 1878 1856 0 -37 182 H ATOM 2185 HB3 ASP A 162 25.637 6.861 5.908 1.00 13.70 H ANISOU 2185 HB3 ASP A 162 2058 1461 1686 -64 88 291 H ATOM 2186 N HIS A 163 24.573 10.035 3.061 1.00 13.20 N ANISOU 2186 N HIS A 163 1781 1609 1623 -86 -299 368 N ATOM 2187 CA HIS A 163 23.604 10.526 2.090 1.00 12.69 C ANISOU 2187 CA HIS A 163 1862 1705 1252 -50 -226 277 C ATOM 2188 C HIS A 163 23.985 11.943 1.679 1.00 12.55 C ANISOU 2188 C HIS A 163 1773 1686 1309 3 -192 228 C ATOM 2189 O HIS A 163 24.238 12.785 2.520 1.00 14.76 O ANISOU 2189 O HIS A 163 2406 1884 1317 -163 -344 226 O ATOM 2190 CB HIS A 163 22.235 10.513 2.777 1.00 13.87 C ANISOU 2190 CB HIS A 163 1907 1591 1770 34 -78 410 C ATOM 2191 CG HIS A 163 21.075 10.735 1.852 1.00 14.08 C ANISOU 2191 CG HIS A 163 1827 2001 1520 -73 -19 260 C ATOM 2192 ND1 HIS A 163 20.950 10.065 0.657 1.00 19.17 N ANISOU 2192 ND1 HIS A 163 2007 3175 2101 280 -252 -471 N ATOM 2193 CD2 HIS A 163 19.979 11.533 1.964 1.00 14.17 C ANISOU 2193 CD2 HIS A 163 2135 1839 1406 -8 -108 375 C ATOM 2194 CE1 HIS A 163 19.831 10.448 0.070 1.00 18.21 C ANISOU 2194 CE1 HIS A 163 2094 3128 1693 148 -300 -325 C ATOM 2195 NE2 HIS A 163 19.237 11.354 0.827 1.00 13.94 N ANISOU 2195 NE2 HIS A 163 1860 1803 1632 -181 -148 345 N ATOM 2196 H HIS A 163 25.011 10.657 3.461 1.00 12.25 H ANISOU 2196 H HIS A 163 1570 1631 1452 64 -172 224 H ATOM 2197 HA HIS A 163 23.581 9.949 1.299 1.00 13.77 H ANISOU 2197 HA HIS A 163 1933 1736 1560 -10 -257 56 H ATOM 2198 HB2 HIS A 163 22.106 9.658 3.212 1.00 14.05 H ANISOU 2198 HB2 HIS A 163 2108 1606 1623 -79 19 321 H ATOM 2199 HB3 HIS A 163 22.216 11.219 3.442 1.00 13.27 H ANISOU 2199 HB3 HIS A 163 1549 1661 1832 -116 -88 294 H ATOM 2200 HD2 HIS A 163 19.788 12.115 2.664 1.00 14.62 H ANISOU 2200 HD2 HIS A 163 1862 1904 1786 -85 -130 103 H ATOM 2201 HE1 HIS A 163 19.524 10.150 -0.756 1.00 16.46 H ANISOU 2201 HE1 HIS A 163 2083 2399 1771 -522 -191 -106 H ATOM 2202 N GLY A 164 24.031 12.157 0.373 1.00 12.26 N ANISOU 2202 N GLY A 164 1866 1489 1304 21 -404 232 N ATOM 2203 CA GLY A 164 24.324 13.469 -0.214 1.00 11.79 C ANISOU 2203 CA GLY A 164 1951 1584 945 104 -323 260 C ATOM 2204 C GLY A 164 23.026 14.149 -0.581 1.00 12.52 C ANISOU 2204 C GLY A 164 1661 1510 1585 -90 -291 283 C ATOM 2205 O GLY A 164 22.197 13.546 -1.261 1.00 13.23 O ANISOU 2205 O GLY A 164 1850 1661 1512 -47 -503 348 O ATOM 2206 H GLY A 164 23.893 11.549 -0.219 1.00 12.67 H ANISOU 2206 H GLY A 164 1834 1592 1387 76 -192 73 H ATOM 2207 HA2 GLY A 164 24.854 13.356 -1.019 1.00 12.73 H ANISOU 2207 HA2 GLY A 164 1743 1673 1419 -113 -52 39 H ATOM 2208 HA3 GLY A 164 24.822 14.018 0.410 1.00 11.85 H ANISOU 2208 HA3 GLY A 164 1565 1544 1391 4 -156 98 H ATOM 2209 N VAL A 165 22.877 15.397 -0.139 1.00 12.98 N ANISOU 2209 N VAL A 165 1677 1621 1631 21 -341 240 N ATOM 2210 CA VAL A 165 21.685 16.219 -0.400 1.00 12.27 C ANISOU 2210 CA VAL A 165 1619 1635 1407 -47 -308 357 C ATOM 2211 C VAL A 165 22.118 17.659 -0.703 1.00 11.61 C ANISOU 2211 C VAL A 165 1622 1647 1141 -26 -107 262 C ATOM 2212 O VAL A 165 23.292 17.927 -0.876 1.00 12.22 O ANISOU 2212 O VAL A 165 1546 1583 1513 -23 -261 261 O ATOM 2213 CB VAL A 165 20.684 16.138 0.791 1.00 12.95 C ANISOU 2213 CB VAL A 165 1779 1689 1451 6 -235 325 C ATOM 2214 CG1 VAL A 165 20.099 14.719 0.937 1.00 15.22 C ANISOU 2214 CG1 VAL A 165 1956 1691 2135 -89 -200 435 C ATOM 2215 CG2 VAL A 165 21.322 16.564 2.104 1.00 13.93 C ANISOU 2215 CG2 VAL A 165 2033 1940 1320 166 -210 280 C ATOM 2216 H VAL A 165 23.476 15.809 0.322 1.00 11.80 H ANISOU 2216 H VAL A 165 1489 1555 1436 69 -123 168 H ATOM 2217 HA VAL A 165 21.228 15.884 -1.201 1.00 12.33 H ANISOU 2217 HA VAL A 165 1525 1677 1483 -8 -220 174 H ATOM 2218 HB VAL A 165 19.931 16.738 0.623 1.00 12.81 H ANISOU 2218 HB VAL A 165 1687 1639 1540 -32 -198 203 H ATOM 2219 N LEU A 166 21.158 18.570 -0.783 1.00 11.99 N ANISOU 2219 N LEU A 166 1438 1635 1481 -145 -142 275 N ATOM 2220 CA LEU A 166 21.457 19.933 -1.230 1.00 11.88 C ANISOU 2220 CA LEU A 166 1576 1695 1243 -351 -131 188 C ATOM 2221 C LEU A 166 20.836 20.926 -0.264 1.00 11.50 C ANISOU 2221 C LEU A 166 1631 1791 946 -110 -292 319 C ATOM 2222 O LEU A 166 19.633 20.906 -0.052 1.00 12.89 O ANISOU 2222 O LEU A 166 1634 1791 1473 -107 -195 225 O ATOM 2223 CB LEU A 166 20.877 20.118 -2.620 1.00 11.62 C ANISOU 2223 CB LEU A 166 1712 1445 1255 -43 -187 45 C ATOM 2224 CG LEU A 166 21.198 21.454 -3.281 1.00 12.48 C ANISOU 2224 CG LEU A 166 1770 1568 1402 45 -75 257 C ATOM 2225 CD1 LEU A 166 22.645 21.428 -3.757 1.00 13.63 C ANISOU 2225 CD1 LEU A 166 1650 1828 1699 -106 -184 357 C ATOM 2226 CD2 LEU A 166 20.246 21.685 -4.457 1.00 12.77 C ANISOU 2226 CD2 LEU A 166 1730 1553 1565 -121 -183 387 C ATOM 2227 H LEU A 166 20.330 18.437 -0.600 1.00 11.33 H ANISOU 2227 H LEU A 166 1481 1509 1315 -175 -94 204 H ATOM 2228 HA LEU A 166 22.423 20.085 -1.259 1.00 12.12 H ANISOU 2228 HA LEU A 166 1508 1591 1505 -159 -189 271 H ATOM 2229 HB2 LEU A 166 21.211 19.406 -3.189 1.00 11.72 H ANISOU 2229 HB2 LEU A 166 1593 1524 1336 -71 -127 1 H ATOM 2230 HB3 LEU A 166 19.913 20.043 -2.552 1.00 11.59 H ANISOU 2230 HB3 LEU A 166 1674 1504 1223 38 -148 116 H ATOM 2231 HG LEU A 166 21.091 22.182 -2.649 1.00 13.07 H ANISOU 2231 HG LEU A 166 1859 1473 1632 -158 -148 161 H ATOM 2232 N VAL A 167 21.638 21.822 0.315 1.00 12.49 N ANISOU 2232 N VAL A 167 1670 1615 1459 -71 -319 225 N ATOM 2233 CA VAL A 167 21.118 22.928 1.104 1.00 12.16 C ANISOU 2233 CA VAL A 167 1574 1668 1378 -154 -323 211 C ATOM 2234 C VAL A 167 20.774 24.084 0.161 1.00 11.64 C ANISOU 2234 C VAL A 167 1621 1808 994 38 -196 155 C ATOM 2235 O VAL A 167 21.632 24.598 -0.561 1.00 13.58 O ANISOU 2235 O VAL A 167 1552 1771 1836 -87 -140 362 O ATOM 2236 CB VAL A 167 22.120 23.388 2.225 1.00 11.85 C ANISOU 2236 CB VAL A 167 1675 1696 1129 -90 -231 141 C ATOM 2237 CG1 VAL A 167 21.643 24.673 2.893 1.00 14.14 C ANISOU 2237 CG1 VAL A 167 2131 2019 1221 -12 -171 -176 C ATOM 2238 CG2 VAL A 167 22.316 22.304 3.284 1.00 13.56 C ANISOU 2238 CG2 VAL A 167 2084 2037 1031 -135 -224 352 C ATOM 2239 H VAL A 167 22.496 21.808 0.259 1.00 12.42 H ANISOU 2239 H VAL A 167 1661 1684 1372 -140 -244 202 H ATOM 2240 HA VAL A 167 20.294 22.643 1.551 1.00 12.43 H ANISOU 2240 HA VAL A 167 1623 1623 1476 -118 -243 246 H ATOM 2241 HB VAL A 167 22.992 23.568 1.815 1.00 11.32 H ANISOU 2241 HB VAL A 167 1591 1398 1312 -135 -295 203 H ATOM 2242 N VAL A 168 19.495 24.480 0.156 1.00 12.09 N ANISOU 2242 N VAL A 168 1591 1472 1529 -83 -179 224 N ATOM 2243 CA VAL A 168 19.028 25.561 -0.709 1.00 12.66 C ANISOU 2243 CA VAL A 168 1833 1579 1396 -144 -266 270 C ATOM 2244 C VAL A 168 18.745 26.866 0.049 1.00 12.79 C ANISOU 2244 C VAL A 168 1648 1720 1490 -42 -374 141 C ATOM 2245 O VAL A 168 18.366 27.859 -0.570 1.00 14.02 O ANISOU 2245 O VAL A 168 2046 1684 1593 -88 -397 252 O ATOM 2246 CB VAL A 168 17.775 25.145 -1.526 1.00 13.66 C ANISOU 2246 CB VAL A 168 1773 1910 1506 107 -406 12 C ATOM 2247 CG1 VAL A 168 18.062 23.898 -2.345 1.00 14.19 C ANISOU 2247 CG1 VAL A 168 1933 1651 1807 -60 -468 14 C ATOM 2248 CG2 VAL A 168 16.572 24.980 -0.621 1.00 13.71 C ANISOU 2248 CG2 VAL A 168 2012 1845 1350 6 -400 313 C ATOM 2249 H VAL A 168 18.885 24.137 0.655 1.00 11.58 H ANISOU 2249 H VAL A 168 1592 1426 1381 -22 -178 181 H ATOM 2250 HA VAL A 168 19.728 25.771 -1.362 1.00 12.88 H ANISOU 2250 HA VAL A 168 1804 1567 1520 -19 -185 269 H ATOM 2251 HB VAL A 168 17.566 25.864 -2.158 1.00 12.43 H ANISOU 2251 HB VAL A 168 1518 1707 1498 -23 -192 -12 H ATOM 2252 N GLY A 169 18.929 26.878 1.358 1.00 13.13 N ANISOU 2252 N GLY A 169 1945 1497 1544 -98 -358 92 N ATOM 2253 CA GLY A 169 18.672 28.025 2.193 1.00 13.30 C ANISOU 2253 CA GLY A 169 1829 1607 1617 25 -119 157 C ATOM 2254 C GLY A 169 18.633 27.659 3.648 1.00 13.54 C ANISOU 2254 C GLY A 169 1792 1718 1632 -134 -159 187 C ATOM 2255 O GLY A 169 19.067 26.567 4.029 1.00 13.48 O ANISOU 2255 O GLY A 169 2055 1665 1402 -69 -347 122 O ATOM 2256 H GLY A 169 19.217 26.201 1.803 1.00 12.29 H ANISOU 2256 H GLY A 169 1714 1603 1351 -12 -148 98 H ATOM 2257 HA2 GLY A 169 17.813 28.399 1.950 1.00 13.27 H ANISOU 2257 HA2 GLY A 169 1704 1797 1540 -63 -135 71 H ATOM 2258 HA3 GLY A 169 19.357 28.697 2.054 1.00 11.92 H ANISOU 2258 HA3 GLY A 169 1673 1528 1325 87 -178 -26 H ATOM 2259 N TYR A 170 18.121 28.580 4.454 1.00 13.56 N ANISOU 2259 N TYR A 170 1870 1683 1597 -61 -610 75 N ATOM 2260 CA TYR A 170 18.010 28.415 5.884 1.00 13.87 C ANISOU 2260 CA TYR A 170 2061 1610 1596 -167 -436 -72 C ATOM 2261 C TYR A 170 17.036 29.453 6.412 1.00 14.32 C ANISOU 2261 C TYR A 170 2225 1485 1730 -166 -419 -121 C ATOM 2262 O TYR A 170 16.706 30.419 5.733 1.00 15.50 O ANISOU 2262 O TYR A 170 2327 1519 2041 -44 -474 5 O ATOM 2263 CB TYR A 170 19.397 28.523 6.564 1.00 13.09 C ANISOU 2263 CB TYR A 170 2013 1664 1293 4 -361 -40 C ATOM 2264 CG TYR A 170 20.107 29.851 6.387 1.00 13.38 C ANISOU 2264 CG TYR A 170 1913 1676 1493 37 -554 77 C ATOM 2265 CD1 TYR A 170 19.814 30.926 7.211 1.00 15.32 C ANISOU 2265 CD1 TYR A 170 2226 1910 1683 -185 -379 -190 C ATOM 2266 CD2 TYR A 170 21.065 30.014 5.406 1.00 15.16 C ANISOU 2266 CD2 TYR A 170 2184 1687 1887 -84 -232 -57 C ATOM 2267 CE1 TYR A 170 20.492 32.168 7.058 1.00 15.19 C ANISOU 2267 CE1 TYR A 170 2074 1829 1869 -39 -291 -80 C ATOM 2268 CE2 TYR A 170 21.716 31.224 5.215 1.00 15.08 C ANISOU 2268 CE2 TYR A 170 2233 1749 1745 -146 -338 -133 C ATOM 2269 CZ TYR A 170 21.438 32.287 6.051 1.00 14.05 C ANISOU 2269 CZ TYR A 170 2172 1771 1394 -62 -493 -14 C ATOM 2270 OH TYR A 170 22.140 33.460 5.826 1.00 15.72 O ANISOU 2270 OH TYR A 170 2242 1805 1924 -260 -433 -5 O ATOM 2271 H TYR A 170 17.824 29.338 4.173 1.00 14.14 H ANISOU 2271 H TYR A 170 1957 1640 1774 -50 -332 129 H ATOM 2272 HA TYR A 170 17.643 27.527 6.075 1.00 13.81 H ANISOU 2272 HA TYR A 170 1886 1597 1763 -18 -186 13 H ATOM 2273 HB2 TYR A 170 19.283 28.387 7.517 1.00 13.51 H ANISOU 2273 HB2 TYR A 170 1780 1962 1390 61 -182 52 H ATOM 2274 HB3 TYR A 170 19.975 27.831 6.207 1.00 13.67 H ANISOU 2274 HB3 TYR A 170 1958 1707 1526 -99 -86 -53 H ATOM 2275 HD1 TYR A 170 19.183 30.828 7.886 1.00 15.38 H ANISOU 2275 HD1 TYR A 170 2147 1711 1985 -6 -228 -99 H ATOM 2276 HD2 TYR A 170 21.259 29.302 4.840 1.00 14.82 H ANISOU 2276 HD2 TYR A 170 2084 1704 1841 -113 -246 -58 H ATOM 2277 HE1 TYR A 170 20.292 32.884 7.615 1.00 15.27 H ANISOU 2277 HE1 TYR A 170 2114 1792 1896 -81 -205 -69 H ATOM 2278 HE2 TYR A 170 22.362 31.307 4.552 1.00 15.07 H ANISOU 2278 HE2 TYR A 170 2144 1568 2013 -19 -210 -86 H ATOM 2279 N GLY A 171 16.585 29.275 7.643 1.00 14.81 N ANISOU 2279 N GLY A 171 2194 1747 1685 65 -504 -41 N ATOM 2280 CA GLY A 171 15.638 30.196 8.232 1.00 15.69 C ANISOU 2280 CA GLY A 171 2117 1924 1918 -37 -235 9 C ATOM 2281 C GLY A 171 15.376 29.820 9.661 1.00 16.12 C ANISOU 2281 C GLY A 171 2201 2090 1831 -14 -412 -45 C ATOM 2282 O GLY A 171 16.195 29.168 10.314 1.00 15.43 O ANISOU 2282 O GLY A 171 2160 1775 1926 -17 -371 -121 O ATOM 2283 H GLY A 171 16.817 28.623 8.154 1.00 15.16 H ANISOU 2283 H GLY A 171 2249 1720 1791 -70 -426 56 H ATOM 2284 HA2 GLY A 171 14.805 30.167 7.738 1.00 15.41 H ANISOU 2284 HA2 GLY A 171 1996 2133 1725 -40 -79 117 H ATOM 2285 HA3 GLY A 171 15.991 31.099 8.205 1.00 15.80 H ANISOU 2285 HA3 GLY A 171 2126 1827 2051 86 -182 -87 H ATOM 2286 N PHE A 172 14.232 30.253 10.156 1.00 17.19 N ANISOU 2286 N PHE A 172 2447 2189 1896 277 -208 102 N ATOM 2287 CA PHE A 172 13.859 30.018 11.537 1.00 18.50 C ANISOU 2287 CA PHE A 172 2587 2422 2018 318 95 -39 C ATOM 2288 C PHE A 172 12.350 29.896 11.668 1.00 20.82 C ANISOU 2288 C PHE A 172 2525 2787 2595 521 87 96 C ATOM 2289 O PHE A 172 11.607 30.471 10.865 1.00 23.16 O ANISOU 2289 O PHE A 172 2646 2936 3217 592 -112 402 O ATOM 2290 CB PHE A 172 14.386 31.131 12.438 1.00 20.33 C ANISOU 2290 CB PHE A 172 2832 2863 2029 142 -141 -108 C ATOM 2291 CG PHE A 172 13.909 32.505 12.062 1.00 20.91 C ANISOU 2291 CG PHE A 172 3252 2676 2015 173 -5 -362 C ATOM 2292 CD1 PHE A 172 14.614 33.274 11.133 1.00 21.23 C ANISOU 2292 CD1 PHE A 172 3072 2588 2405 -103 -248 -348 C ATOM 2293 CD2 PHE A 172 12.764 33.036 12.643 1.00 24.93 C ANISOU 2293 CD2 PHE A 172 3292 2696 3481 172 455 -49 C ATOM 2294 CE1 PHE A 172 14.187 34.541 10.789 1.00 21.67 C ANISOU 2294 CE1 PHE A 172 3151 3067 2012 260 -317 -112 C ATOM 2295 CE2 PHE A 172 12.323 34.306 12.299 1.00 24.14 C ANISOU 2295 CE2 PHE A 172 3003 3201 2967 477 15 168 C ATOM 2296 CZ PHE A 172 13.038 35.060 11.366 1.00 24.44 C ANISOU 2296 CZ PHE A 172 3545 2826 2915 347 304 -134 C ATOM 2297 H PHE A 172 13.647 30.696 9.706 1.00 17.00 H ANISOU 2297 H PHE A 172 2225 2052 2180 81 -314 55 H ATOM 2298 HA PHE A 172 14.249 29.173 11.840 1.00 18.10 H ANISOU 2298 HA PHE A 172 2291 2569 2016 94 -62 300 H ATOM 2299 HB2 PHE A 172 14.099 30.957 13.349 1.00 20.09 H ANISOU 2299 HB2 PHE A 172 2763 2668 2201 11 101 -224 H ATOM 2300 HB3 PHE A 172 15.355 31.133 12.395 1.00 20.58 H ANISOU 2300 HB3 PHE A 172 2831 2759 2230 -18 110 -71 H ATOM 2301 HD1 PHE A 172 15.384 32.929 10.742 1.00 21.48 H ANISOU 2301 HD1 PHE A 172 2906 2664 2588 -107 -157 21 H ATOM 2302 HD2 PHE A 172 12.286 32.534 13.262 1.00 23.01 H ANISOU 2302 HD2 PHE A 172 2858 2925 2957 158 78 -89 H ATOM 2303 HE1 PHE A 172 14.663 35.041 10.165 1.00 22.58 H ANISOU 2303 HE1 PHE A 172 2972 2790 2814 160 -116 -44 H ATOM 2304 HE2 PHE A 172 11.554 34.654 12.689 1.00 23.34 H ANISOU 2304 HE2 PHE A 172 2862 2863 3143 143 -3 -149 H ATOM 2305 HZ PHE A 172 12.746 35.912 11.135 1.00 23.54 H ANISOU 2305 HZ PHE A 172 3031 2837 3075 107 -158 -88 H ATOM 2306 N GLU A 173 11.895 29.152 12.675 1.00 26.36 N ANISOU 2306 N GLU A 173 3014 3768 3233 544 185 937 N ATOM 2307 CA GLU A 173 10.470 29.019 12.951 1.00 28.89 C ANISOU 2307 CA GLU A 173 3308 4233 3434 137 472 792 C ATOM 2308 C GLU A 173 10.133 29.920 14.129 1.00 30.52 C ANISOU 2308 C GLU A 173 3697 4170 3728 540 388 533 C ATOM 2309 O GLU A 173 11.008 30.273 14.921 1.00 34.31 O ANISOU 2309 O GLU A 173 3938 4195 4902 356 3 61 O ATOM 2310 CB GLU A 173 10.091 27.567 13.265 1.00 34.46 C ANISOU 2310 CB GLU A 173 4010 4048 5035 -35 389 562 C ATOM 2311 CG GLU A 173 9.889 26.686 12.032 1.00 42.20 C ANISOU 2311 CG GLU A 173 5322 5005 5706 221 91 -276 C ATOM 2312 CD GLU A 173 9.298 25.326 12.377 1.00 48.72 C ANISOU 2312 CD GLU A 173 6842 5315 6353 -525 95 -225 C ATOM 2313 OE1 GLU A 173 9.455 24.875 13.537 1.00 54.51 O ANISOU 2313 OE1 GLU A 173 6653 7259 6799 -472 226 664 O ATOM 2314 OE2 GLU A 173 8.674 24.704 11.490 1.00 52.78 O ANISOU 2314 OE2 GLU A 173 6028 6849 7174 -241 -582 -551 O ATOM 2315 H GLU A 173 12.398 28.714 13.218 1.00 23.67 H ANISOU 2315 H GLU A 173 3462 2769 2761 300 -176 224 H ATOM 2316 HA GLU A 173 9.941 29.309 12.180 1.00 29.09 H ANISOU 2316 HA GLU A 173 3044 4033 3975 230 -76 177 H ATOM 2317 HB2 GLU A 173 10.794 27.169 13.801 1.00 34.88 H ANISOU 2317 HB2 GLU A 173 4408 3708 5133 197 300 493 H ATOM 2318 HB3 GLU A 173 9.259 27.563 13.764 1.00 34.05 H ANISOU 2318 HB3 GLU A 173 4017 4039 4881 -461 294 589 H ATOM 2319 HG2 GLU A 173 9.283 27.131 11.420 1.00 41.84 H ANISOU 2319 HG2 GLU A 173 4995 5560 5339 -49 120 -188 H ATOM 2320 HG3 GLU A 173 10.747 26.540 11.603 1.00 41.67 H ANISOU 2320 HG3 GLU A 173 5292 5505 5036 250 -94 -211 H ATOM 2321 N SER A 174 8.858 30.282 14.237 1.00 33.62 N ANISOU 2321 N SER A 174 3841 4850 4080 913 -7 380 N ATOM 2322 CA SER A 174 8.385 31.166 15.286 1.00 35.21 C ANISOU 2322 CA SER A 174 4646 4789 3941 907 363 489 C ATOM 2323 C SER A 174 9.136 32.514 15.191 1.00 45.39 C ANISOU 2323 C SER A 174 5899 5286 6060 18 -407 951 C ATOM 2324 O SER A 174 9.202 33.104 14.098 1.00 45.82 O ANISOU 2324 O SER A 174 6610 5000 5798 606 1521 557 O ATOM 2325 CB SER A 174 8.518 30.464 16.651 1.00 31.75 C ANISOU 2325 CB SER A 174 4143 4237 3681 426 -372 -68 C ATOM 2326 OG SER A 174 7.773 31.128 17.645 1.00 30.45 O ANISOU 2326 OG SER A 174 3694 4400 3473 75 -55 359 O ATOM 2327 H SER A 174 8.237 30.021 13.701 1.00 34.25 H ANISOU 2327 H SER A 174 3843 4543 4625 281 105 200 H ATOM 2328 HA SER A 174 7.433 31.347 15.138 1.00 33.27 H ANISOU 2328 HA SER A 174 4737 4507 3397 888 46 88 H ATOM 2329 HB2 SER A 174 8.179 29.559 16.565 1.00 33.21 H ANISOU 2329 HB2 SER A 174 4202 4390 4025 85 -27 128 H ATOM 2330 HB3 SER A 174 9.449 30.437 16.919 1.00 32.78 H ANISOU 2330 HB3 SER A 174 3910 4475 4068 257 3 32 H ATOM 2331 N THR A 175 9.702 32.994 16.300 1.00 55.53 N ANISOU 2331 N THR A 175 8297 6499 6303 -352 82 -774 N ATOM 2332 CA THR A 175 10.554 34.189 16.277 1.00 56.56 C ANISOU 2332 CA THR A 175 7649 6886 6952 -379 -129 -741 C ATOM 2333 C THR A 175 11.704 34.084 17.281 1.00 67.08 C ANISOU 2333 C THR A 175 7746 9648 8090 -76 -587 -261 C ATOM 2334 O THR A 175 12.742 33.483 16.994 1.00 70.35 O ANISOU 2334 O THR A 175 8270 9823 8634 382 -467 -157 O ATOM 2335 CB THR A 175 9.735 35.477 16.534 1.00 60.57 C ANISOU 2335 CB THR A 175 8852 6610 7551 11 -190 -197 C ATOM 2336 OG1 THR A 175 10.599 36.617 16.448 1.00 65.35 O ANISOU 2336 OG1 THR A 175 7876 7476 9477 -202 236 -616 O ATOM 2337 CG2 THR A 175 9.040 35.446 17.909 1.00 59.39 C ANISOU 2337 CG2 THR A 175 10096 5050 7420 463 149 -567 C ATOM 2338 H THR A 175 9.609 32.655 17.084 1.00 51.89 H ANISOU 2338 H THR A 175 6494 6866 6355 152 -287 -377 H ATOM 2339 HA THR A 175 10.962 34.275 15.390 1.00 59.06 H ANISOU 2339 HA THR A 175 7581 7431 7428 -124 142 85 H ATOM 2340 HB THR A 175 9.047 35.552 15.854 1.00 59.92 H ANISOU 2340 HB THR A 175 7912 7305 7550 -100 197 -67 H ATOM 2341 N ASN A 179 16.853 26.980 19.623 1.00 46.73 N ANISOU 2341 N ASN A 179 6540 5871 5343 -63 -473 43 N ATOM 2342 CA ASN A 179 16.703 25.708 18.914 1.00 44.66 C ANISOU 2342 CA ASN A 179 6140 5666 5160 726 -226 378 C ATOM 2343 C ASN A 179 15.612 25.759 17.829 1.00 44.31 C ANISOU 2343 C ASN A 179 5809 5366 5660 29 -365 362 C ATOM 2344 O ASN A 179 14.972 24.738 17.534 1.00 41.39 O ANISOU 2344 O ASN A 179 6494 4651 4580 377 1096 -140 O ATOM 2345 CB ASN A 179 16.410 24.574 19.913 1.00 45.95 C ANISOU 2345 CB ASN A 179 6071 5853 5534 -182 -334 356 C ATOM 2346 CG ASN A 179 17.583 24.281 20.840 0.50 45.80 C ANISOU 2346 CG ASN A 179 6036 5598 5768 137 -257 500 C ATOM 2347 OD1 ASN A 179 18.740 24.539 20.508 0.50 47.57 O ANISOU 2347 OD1 ASN A 179 5991 6622 5459 332 51 -13 O ATOM 2348 ND2 ASN A 179 17.282 23.727 22.011 0.50 45.91 N ANISOU 2348 ND2 ASN A 179 6622 5221 5598 -143 -351 241 N ATOM 2349 H ASN A 179 16.113 27.309 19.913 1.00 47.04 H ANISOU 2349 H ASN A 179 6627 5492 5751 -125 -148 -53 H ATOM 2350 HA ASN A 179 17.549 25.496 18.472 1.00 45.04 H ANISOU 2350 HA ASN A 179 5624 5807 5681 -68 -206 136 H ATOM 2351 HB2 ASN A 179 15.649 24.826 20.460 1.00 45.66 H ANISOU 2351 HB2 ASN A 179 5994 5522 5832 -105 -269 205 H ATOM 2352 HB3 ASN A 179 16.214 23.758 19.427 1.00 46.60 H ANISOU 2352 HB3 ASN A 179 5936 5885 5882 -29 -61 103 H ATOM 2353 N ASN A 180 15.413 26.939 17.226 1.00 32.96 N ANISOU 2353 N ASN A 180 4060 5570 2891 -740 421 81 N ATOM 2354 CA ASN A 180 14.383 27.113 16.194 1.00 29.59 C ANISOU 2354 CA ASN A 180 3539 4595 3109 -299 552 -38 C ATOM 2355 C ASN A 180 14.863 27.434 14.798 1.00 24.64 C ANISOU 2355 C ASN A 180 2725 3593 3043 7 -47 282 C ATOM 2356 O ASN A 180 14.051 27.694 13.910 1.00 24.84 O ANISOU 2356 O ASN A 180 2657 3210 3569 -189 -234 707 O ATOM 2357 CB ASN A 180 13.360 28.146 16.622 1.00 33.06 C ANISOU 2357 CB ASN A 180 4907 4288 3366 104 458 -516 C ATOM 2358 CG ASN A 180 12.230 27.539 17.392 1.00 34.17 C ANISOU 2358 CG ASN A 180 4578 4037 4365 81 526 -277 C ATOM 2359 OD1 ASN A 180 11.815 26.392 17.148 1.00 35.27 O ANISOU 2359 OD1 ASN A 180 5553 3950 3895 -148 -28 69 O ATOM 2360 ND2 ASN A 180 11.709 28.304 18.338 1.00 35.69 N ANISOU 2360 ND2 ASN A 180 4490 5233 3836 284 224 -595 N ATOM 2361 H ASN A 180 15.862 27.653 17.390 1.00 34.09 H ANISOU 2361 H ASN A 180 3992 5036 3925 -72 -106 -243 H ATOM 2362 HA ASN A 180 13.907 26.263 16.099 1.00 27.80 H ANISOU 2362 HA ASN A 180 3711 3987 2865 71 336 303 H ATOM 2363 HB2 ASN A 180 13.795 28.801 17.191 1.00 33.47 H ANISOU 2363 HB2 ASN A 180 4433 4246 4036 -49 -9 -187 H ATOM 2364 HB3 ASN A 180 12.979 28.588 15.848 1.00 33.15 H ANISOU 2364 HB3 ASN A 180 4094 4336 4163 -173 42 -171 H ATOM 2365 N LYS A 181 16.166 27.377 14.596 1.00 18.05 N ANISOU 2365 N LYS A 181 2719 2344 1795 -334 -337 -242 N ATOM 2366 CA LYS A 181 16.716 27.564 13.275 1.00 17.49 C ANISOU 2366 CA LYS A 181 2572 2344 1729 -105 -461 -272 C ATOM 2367 C LYS A 181 16.789 26.252 12.496 1.00 16.13 C ANISOU 2367 C LYS A 181 2423 2142 1562 -329 -60 -88 C ATOM 2368 O LYS A 181 16.894 25.161 13.059 1.00 17.05 O ANISOU 2368 O LYS A 181 2268 2160 2049 -236 -405 140 O ATOM 2369 CB LYS A 181 18.094 28.214 13.360 1.00 16.41 C ANISOU 2369 CB LYS A 181 2482 2183 1567 -48 -299 -184 C ATOM 2370 CG LYS A 181 18.013 29.608 13.947 1.00 19.37 C ANISOU 2370 CG LYS A 181 2650 2354 2354 -77 -347 -564 C ATOM 2371 CD LYS A 181 19.359 30.262 14.093 1.00 21.67 C ANISOU 2371 CD LYS A 181 2693 2806 2733 -166 -385 -620 C ATOM 2372 CE LYS A 181 20.039 29.865 15.358 1.00 22.59 C ANISOU 2372 CE LYS A 181 2619 3149 2813 -104 -331 -272 C ATOM 2373 NZ LYS A 181 21.352 30.573 15.496 1.00 27.29 N ANISOU 2373 NZ LYS A 181 2914 3941 3510 -519 -840 -246 N ATOM 2374 H LYS A 181 16.755 27.229 15.204 1.00 19.20 H ANISOU 2374 H LYS A 181 2746 2660 1888 -31 -204 137 H ATOM 2375 HA LYS A 181 16.144 28.179 12.771 1.00 17.33 H ANISOU 2375 HA LYS A 181 2271 2264 2048 -86 -55 7 H ATOM 2376 HB2 LYS A 181 18.669 27.676 13.928 1.00 17.66 H ANISOU 2376 HB2 LYS A 181 2290 2432 1986 58 -157 79 H ATOM 2377 HB3 LYS A 181 18.472 28.281 12.469 1.00 18.18 H ANISOU 2377 HB3 LYS A 181 2740 2311 1854 210 58 -42 H ATOM 2378 HG2 LYS A 181 17.476 30.163 13.361 1.00 18.80 H ANISOU 2378 HG2 LYS A 181 2466 2182 2492 -94 -39 -297 H ATOM 2379 HG3 LYS A 181 17.602 29.563 14.825 1.00 19.04 H ANISOU 2379 HG3 LYS A 181 2772 2041 2420 165 -215 -455 H ATOM 2380 HD2 LYS A 181 19.925 29.999 13.350 1.00 21.58 H ANISOU 2380 HD2 LYS A 181 2724 2685 2791 -57 -163 -143 H ATOM 2381 HD3 LYS A 181 19.245 31.225 14.101 1.00 20.79 H ANISOU 2381 HD3 LYS A 181 2379 2759 2762 -285 -79 -255 H ATOM 2382 HE2 LYS A 181 19.482 30.108 16.114 1.00 23.62 H ANISOU 2382 HE2 LYS A 181 3208 2994 2770 40 -145 -138 H ATOM 2383 HE3 LYS A 181 20.201 28.909 15.351 1.00 23.58 H ANISOU 2383 HE3 LYS A 181 2957 3121 2880 -32 -63 -200 H ATOM 2384 N TYR A 182 16.756 26.367 11.175 1.00 15.14 N ANISOU 2384 N TYR A 182 2253 1941 1557 88 -382 -102 N ATOM 2385 CA TYR A 182 16.832 25.222 10.277 1.00 14.33 C ANISOU 2385 CA TYR A 182 1982 1971 1490 -14 -287 -94 C ATOM 2386 C TYR A 182 17.560 25.516 8.988 1.00 13.64 C ANISOU 2386 C TYR A 182 1897 1751 1534 -151 -312 -53 C ATOM 2387 O TYR A 182 17.605 26.667 8.523 1.00 15.10 O ANISOU 2387 O TYR A 182 2271 1646 1819 -212 -370 -24 O ATOM 2388 CB TYR A 182 15.438 24.631 9.966 1.00 14.37 C ANISOU 2388 CB TYR A 182 2091 1875 1492 -152 -106 -80 C ATOM 2389 CG TYR A 182 14.486 25.610 9.297 1.00 15.61 C ANISOU 2389 CG TYR A 182 1841 2005 2082 -213 -140 184 C ATOM 2390 CD1 TYR A 182 14.533 25.827 7.925 1.00 16.95 C ANISOU 2390 CD1 TYR A 182 2188 2250 2002 130 -430 -36 C ATOM 2391 CD2 TYR A 182 13.577 26.333 10.035 1.00 16.93 C ANISOU 2391 CD2 TYR A 182 2172 2456 1804 30 -469 -134 C ATOM 2392 CE1 TYR A 182 13.682 26.728 7.309 1.00 18.62 C ANISOU 2392 CE1 TYR A 182 2221 2756 2098 128 -657 124 C ATOM 2393 CE2 TYR A 182 12.714 27.231 9.440 1.00 18.96 C ANISOU 2393 CE2 TYR A 182 2655 2285 2264 432 -512 -342 C ATOM 2394 CZ TYR A 182 12.769 27.416 8.082 1.00 18.82 C ANISOU 2394 CZ TYR A 182 2363 2427 2361 231 -625 -33 C ATOM 2395 OH TYR A 182 11.886 28.330 7.529 1.00 23.44 O ANISOU 2395 OH TYR A 182 2857 3221 2828 593 -546 714 O ATOM 2396 H TYR A 182 16.688 27.119 10.763 1.00 15.15 H ANISOU 2396 H TYR A 182 2137 1905 1713 -79 -159 -33 H ATOM 2397 HA TYR A 182 17.343 24.527 10.736 1.00 14.57 H ANISOU 2397 HA TYR A 182 2033 1834 1667 -39 -88 51 H ATOM 2398 HB2 TYR A 182 15.546 23.872 9.372 1.00 14.76 H ANISOU 2398 HB2 TYR A 182 2085 1860 1661 -188 -43 -128 H ATOM 2399 HB3 TYR A 182 15.030 24.341 10.797 1.00 15.44 H ANISOU 2399 HB3 TYR A 182 2126 2053 1685 7 90 15 H ATOM 2400 HD1 TYR A 182 15.147 25.356 7.409 1.00 17.03 H ANISOU 2400 HD1 TYR A 182 2194 2193 2081 -100 -162 0 H ATOM 2401 HD2 TYR A 182 13.532 26.202 10.954 1.00 17.83 H ANISOU 2401 HD2 TYR A 182 2537 2322 1914 -161 -106 48 H ATOM 2402 HE1 TYR A 182 13.712 26.861 6.392 1.00 18.42 H ANISOU 2402 HE1 TYR A 182 2449 2389 2160 -35 -469 227 H ATOM 2403 HE2 TYR A 182 12.097 27.700 9.953 1.00 19.19 H ANISOU 2403 HE2 TYR A 182 2266 2333 2691 73 -162 -240 H ATOM 2404 N TRP A 183 18.108 24.454 8.422 1.00 13.37 N ANISOU 2404 N TRP A 183 2074 1567 1438 -106 -436 128 N ATOM 2405 CA TRP A 183 18.577 24.420 7.070 1.00 13.44 C ANISOU 2405 CA TRP A 183 2037 1630 1437 -263 -391 141 C ATOM 2406 C TRP A 183 17.444 23.902 6.164 1.00 14.26 C ANISOU 2406 C TRP A 183 2060 1763 1594 -250 -486 193 C ATOM 2407 O TRP A 183 16.753 22.953 6.508 1.00 14.27 O ANISOU 2407 O TRP A 183 2040 1719 1661 -275 -496 220 O ATOM 2408 CB TRP A 183 19.750 23.450 6.966 1.00 13.83 C ANISOU 2408 CB TRP A 183 2160 1644 1450 -198 -411 -21 C ATOM 2409 CG TRP A 183 20.944 23.793 7.752 1.00 14.33 C ANISOU 2409 CG TRP A 183 1983 1775 1687 -55 -426 -68 C ATOM 2410 CD1 TRP A 183 21.362 23.189 8.895 1.00 14.74 C ANISOU 2410 CD1 TRP A 183 2006 1784 1810 -196 -467 59 C ATOM 2411 CD2 TRP A 183 21.901 24.814 7.461 1.00 13.68 C ANISOU 2411 CD2 TRP A 183 2183 1804 1209 -77 -306 21 C ATOM 2412 NE1 TRP A 183 22.519 23.763 9.335 1.00 13.68 N ANISOU 2412 NE1 TRP A 183 1943 1802 1450 -140 -368 24 N ATOM 2413 CE2 TRP A 183 22.871 24.776 8.486 1.00 14.63 C ANISOU 2413 CE2 TRP A 183 2101 1682 1774 -131 -582 180 C ATOM 2414 CE3 TRP A 183 22.030 25.767 6.443 1.00 13.41 C ANISOU 2414 CE3 TRP A 183 2014 1951 1129 -105 -247 38 C ATOM 2415 CZ2 TRP A 183 23.956 25.649 8.533 1.00 15.86 C ANISOU 2415 CZ2 TRP A 183 1960 1967 2099 -159 -347 210 C ATOM 2416 CZ3 TRP A 183 23.112 26.653 6.496 1.00 14.68 C ANISOU 2416 CZ3 TRP A 183 2175 1816 1586 -206 -222 127 C ATOM 2417 CH2 TRP A 183 24.064 26.571 7.535 1.00 14.88 C ANISOU 2417 CH2 TRP A 183 2053 1897 1703 -219 -272 -47 C ATOM 2418 H TRP A 183 18.217 23.705 8.833 1.00 13.60 H ANISOU 2418 H TRP A 183 2035 1628 1503 -154 -301 213 H ATOM 2419 HA TRP A 183 18.863 25.308 6.770 1.00 13.91 H ANISOU 2419 HA TRP A 183 1942 1624 1718 -235 -184 118 H ATOM 2420 HB2 TRP A 183 19.453 22.573 7.254 1.00 13.75 H ANISOU 2420 HB2 TRP A 183 1909 1735 1579 -132 -206 100 H ATOM 2421 HB3 TRP A 183 20.024 23.405 6.036 1.00 14.08 H ANISOU 2421 HB3 TRP A 183 1970 1852 1527 -294 -279 90 H ATOM 2422 HD1 TRP A 183 20.932 22.475 9.307 1.00 14.02 H ANISOU 2422 HD1 TRP A 183 1770 1772 1785 -31 -245 2 H ATOM 2423 HE1 TRP A 183 22.947 23.538 10.046 1.00 12.77 H ANISOU 2423 HE1 TRP A 183 1614 1740 1495 134 -191 47 H ATOM 2424 HE3 TRP A 183 21.399 25.826 5.763 1.00 13.04 H ANISOU 2424 HE3 TRP A 183 1667 1913 1375 249 -170 125 H ATOM 2425 HZ2 TRP A 183 24.597 25.587 9.204 1.00 13.81 H ANISOU 2425 HZ2 TRP A 183 1717 1747 1783 -118 -78 16 H ATOM 2426 HZ3 TRP A 183 23.217 27.289 5.826 1.00 14.62 H ANISOU 2426 HZ3 TRP A 183 2217 1692 1646 26 -10 92 H ATOM 2427 HH2 TRP A 183 24.781 27.161 7.541 1.00 14.73 H ANISOU 2427 HH2 TRP A 183 1812 1840 1943 -48 -96 5 H ATOM 2428 N LEU A 184 17.251 24.523 5.015 1.00 13.45 N ANISOU 2428 N LEU A 184 1922 1662 1524 -177 -372 111 N ATOM 2429 CA LEU A 184 16.318 24.015 4.002 1.00 13.20 C ANISOU 2429 CA LEU A 184 1741 1831 1440 -133 -260 161 C ATOM 2430 C LEU A 184 17.045 23.051 3.076 1.00 12.62 C ANISOU 2430 C LEU A 184 1709 1778 1307 -114 -352 203 C ATOM 2431 O LEU A 184 17.946 23.455 2.344 1.00 13.72 O ANISOU 2431 O LEU A 184 1807 1765 1639 -271 -209 -3 O ATOM 2432 CB LEU A 184 15.792 25.180 3.150 1.00 14.59 C ANISOU 2432 CB LEU A 184 1934 1827 1781 -246 -613 253 C ATOM 2433 CG LEU A 184 14.777 26.145 3.756 1.00 17.10 C ANISOU 2433 CG LEU A 184 2314 2292 1889 -69 -179 221 C ATOM 2434 CD1 LEU A 184 14.583 27.432 2.915 1.00 19.14 C ANISOU 2434 CD1 LEU A 184 2584 2193 2495 0 -228 320 C ATOM 2435 CD2 LEU A 184 13.402 25.456 3.945 1.00 18.23 C ANISOU 2435 CD2 LEU A 184 2106 2639 2179 -23 -320 264 C ATOM 2436 H LEU A 184 17.653 25.248 4.791 1.00 13.19 H ANISOU 2436 H LEU A 184 1777 1623 1610 -72 -238 116 H ATOM 2437 HA LEU A 184 15.562 23.556 4.423 1.00 13.47 H ANISOU 2437 HA LEU A 184 1676 1735 1706 -103 -211 129 H ATOM 2438 HB2 LEU A 184 16.558 25.709 2.878 1.00 14.65 H ANISOU 2438 HB2 LEU A 184 2008 1692 1866 -172 -404 211 H ATOM 2439 HB3 LEU A 184 15.382 24.802 2.355 1.00 14.62 H ANISOU 2439 HB3 LEU A 184 1804 2158 1593 -178 -446 224 H ATOM 2440 HG LEU A 184 15.097 26.413 4.631 1.00 17.72 H ANISOU 2440 HG LEU A 184 2258 2438 2036 -104 -204 52 H ATOM 2441 N VAL A 185 16.660 21.767 3.133 1.00 12.31 N ANISOU 2441 N VAL A 185 1645 1769 1261 -183 -238 -24 N ATOM 2442 CA VAL A 185 17.393 20.705 2.447 1.00 12.16 C ANISOU 2442 CA VAL A 185 1777 1839 1004 -95 -373 -51 C ATOM 2443 C VAL A 185 16.512 19.995 1.404 1.00 10.63 C ANISOU 2443 C VAL A 185 1596 1637 804 31 -442 206 C ATOM 2444 O VAL A 185 15.433 19.455 1.762 1.00 12.31 O ANISOU 2444 O VAL A 185 1610 1806 1261 -107 -165 88 O ATOM 2445 CB VAL A 185 17.969 19.715 3.485 1.00 11.98 C ANISOU 2445 CB VAL A 185 1719 2010 822 -67 -312 16 C ATOM 2446 CG1 VAL A 185 18.625 18.525 2.825 1.00 14.06 C ANISOU 2446 CG1 VAL A 185 2250 2085 1004 121 6 78 C ATOM 2447 CG2 VAL A 185 18.929 20.429 4.420 1.00 14.91 C ANISOU 2447 CG2 VAL A 185 2270 1925 1470 -376 -752 237 C ATOM 2448 H VAL A 185 15.973 21.486 3.566 1.00 12.99 H ANISOU 2448 H VAL A 185 1642 1754 1539 -68 -154 137 H ATOM 2449 HA VAL A 185 18.151 21.099 1.970 1.00 11.83 H ANISOU 2449 HA VAL A 185 1669 1526 1299 9 -350 51 H ATOM 2450 HB VAL A 185 17.231 19.379 4.031 1.00 12.56 H ANISOU 2450 HB VAL A 185 1677 1668 1425 -7 -148 95 H ATOM 2451 N LYS A 186 16.937 20.015 0.149 1.00 11.64 N ANISOU 2451 N LYS A 186 2061 1655 703 -137 -505 280 N ATOM 2452 CA LYS A 186 16.312 19.307 -0.948 1.00 10.85 C ANISOU 2452 CA LYS A 186 1628 1934 559 95 -304 121 C ATOM 2453 C LYS A 186 16.835 17.858 -0.960 1.00 11.01 C ANISOU 2453 C LYS A 186 1651 1739 793 -106 -36 47 C ATOM 2454 O LYS A 186 18.044 17.621 -1.021 1.00 11.44 O ANISOU 2454 O LYS A 186 1619 1714 1011 -117 -158 140 O ATOM 2455 CB LYS A 186 16.680 19.937 -2.253 1.00 10.53 C ANISOU 2455 CB LYS A 186 1716 1727 555 74 -236 7 C ATOM 2456 CG LYS A 186 15.937 19.475 -3.439 1.00 10.31 C ANISOU 2456 CG LYS A 186 1727 1694 496 219 -324 118 C ATOM 2457 CD LYS A 186 16.525 19.967 -4.745 1.00 10.84 C ANISOU 2457 CD LYS A 186 2003 1558 556 -14 -254 33 C ATOM 2458 CE LYS A 186 15.641 19.741 -5.921 1.00 10.35 C ANISOU 2458 CE LYS A 186 1963 1551 417 100 -131 -43 C ATOM 2459 NZ LYS A 186 16.335 19.885 -7.201 1.00 11.81 N ANISOU 2459 NZ LYS A 186 1858 2134 493 92 -262 261 N ATOM 2460 H LYS A 186 17.629 20.460 -0.100 1.00 11.57 H ANISOU 2460 H LYS A 186 1681 1711 1003 103 -209 -6 H ATOM 2461 HA LYS A 186 15.337 19.310 -0.852 1.00 11.42 H ANISOU 2461 HA LYS A 186 1606 1671 1060 -132 -196 144 H ATOM 2462 HB2 LYS A 186 16.531 20.892 -2.179 1.00 11.29 H ANISOU 2462 HB2 LYS A 186 1592 1606 1091 -153 -249 71 H ATOM 2463 HB3 LYS A 186 17.621 19.777 -2.422 1.00 10.85 H ANISOU 2463 HB3 LYS A 186 1567 1573 981 -176 -222 145 H ATOM 2464 HG2 LYS A 186 15.940 18.505 -3.464 1.00 10.34 H ANISOU 2464 HG2 LYS A 186 1458 1630 839 -85 -202 86 H ATOM 2465 HG3 LYS A 186 15.024 19.798 -3.384 1.00 11.13 H ANISOU 2465 HG3 LYS A 186 1481 1569 1177 -113 -256 106 H ATOM 2466 HD2 LYS A 186 16.690 20.919 -4.673 1.00 11.19 H ANISOU 2466 HD2 LYS A 186 1636 1562 1050 -94 -297 71 H ATOM 2467 HD3 LYS A 186 17.359 19.500 -4.907 1.00 10.80 H ANISOU 2467 HD3 LYS A 186 1700 1438 962 -261 -120 135 H ATOM 2468 HE2 LYS A 186 15.291 18.839 -5.876 1.00 10.40 H ANISOU 2468 HE2 LYS A 186 1460 1610 882 64 -134 -15 H ATOM 2469 HE3 LYS A 186 14.914 20.381 -5.894 1.00 11.00 H ANISOU 2469 HE3 LYS A 186 1569 1522 1085 -113 -157 82 H ATOM 2470 N ASN A 187 15.919 16.898 -0.854 1.00 11.98 N ANISOU 2470 N ASN A 187 1578 1575 1397 -35 -296 17 N ATOM 2471 CA ASN A 187 16.258 15.484 -0.975 1.00 11.34 C ANISOU 2471 CA ASN A 187 1644 1562 1102 52 -236 175 C ATOM 2472 C ASN A 187 15.969 14.995 -2.387 1.00 11.24 C ANISOU 2472 C ASN A 187 1618 1597 1055 -119 -143 245 C ATOM 2473 O ASN A 187 15.512 15.768 -3.240 1.00 11.70 O ANISOU 2473 O ASN A 187 1956 1722 766 -30 -62 176 O ATOM 2474 CB ASN A 187 15.519 14.712 0.141 1.00 11.51 C ANISOU 2474 CB ASN A 187 1726 1664 983 -53 -143 -51 C ATOM 2475 CG ASN A 187 16.096 13.354 0.466 1.00 11.57 C ANISOU 2475 CG ASN A 187 2242 1653 498 40 128 -56 C ATOM 2476 OD1 ASN A 187 17.076 12.895 -0.109 1.00 12.21 O ANISOU 2476 OD1 ASN A 187 1818 1751 1070 102 -76 112 O ATOM 2477 ND2 ASN A 187 15.508 12.733 1.480 1.00 14.73 N ANISOU 2477 ND2 ASN A 187 2423 2179 993 78 256 445 N ATOM 2478 H ASN A 187 15.082 17.042 -0.712 1.00 11.01 H ANISOU 2478 H ASN A 187 1591 1493 1098 -46 -227 53 H ATOM 2479 HA ASN A 187 17.218 15.367 -0.818 1.00 11.52 H ANISOU 2479 HA ASN A 187 1581 1613 1182 -8 -160 0 H ATOM 2480 HB2 ASN A 187 15.550 15.242 0.953 1.00 11.99 H ANISOU 2480 HB2 ASN A 187 1802 1550 1202 -123 23 -170 H ATOM 2481 HB3 ASN A 187 14.597 14.585 -0.125 1.00 12.74 H ANISOU 2481 HB3 ASN A 187 1622 1915 1301 -98 2 -217 H ATOM 2482 N SER A 188 16.266 13.716 -2.652 1.00 11.57 N ANISOU 2482 N SER A 188 1681 1643 1072 -1 -259 198 N ATOM 2483 CA SER A 188 16.102 13.104 -3.976 1.00 11.40 C ANISOU 2483 CA SER A 188 1621 1652 1059 -22 -249 223 C ATOM 2484 C SER A 188 15.278 11.841 -3.845 1.00 12.22 C ANISOU 2484 C SER A 188 1570 1540 1532 47 -189 45 C ATOM 2485 O SER A 188 15.544 10.851 -4.492 1.00 12.08 O ANISOU 2485 O SER A 188 1774 1623 1192 -18 -37 94 O ATOM 2486 CB SER A 188 17.455 12.797 -4.640 1.00 12.02 C ANISOU 2486 CB SER A 188 1648 1767 1149 -86 -258 57 C ATOM 2487 OG SER A 188 18.322 12.077 -3.802 1.00 12.69 O ANISOU 2487 OG SER A 188 1713 1750 1357 -78 -315 108 O ATOM 2488 H SER A 188 16.585 13.170 -2.072 1.00 10.87 H ANISOU 2488 H SER A 188 1499 1569 1062 11 -232 113 H ATOM 2489 HA SER A 188 15.615 13.715 -4.566 1.00 11.57 H ANISOU 2489 HA SER A 188 1761 1525 1108 67 -331 64 H ATOM 2490 HB2 SER A 188 17.307 12.288 -5.452 1.00 11.77 H ANISOU 2490 HB2 SER A 188 1628 1554 1290 -24 -242 1 H ATOM 2491 HB3 SER A 188 17.880 13.640 -4.863 1.00 11.45 H ANISOU 2491 HB3 SER A 188 1525 1554 1272 74 -161 -91 H ATOM 2492 N TRP A 189 14.252 11.906 -3.016 1.00 12.58 N ANISOU 2492 N TRP A 189 1795 1483 1500 -98 -43 -57 N ATOM 2493 CA TRP A 189 13.376 10.766 -2.740 1.00 11.60 C ANISOU 2493 CA TRP A 189 1798 1517 1092 -37 26 5 C ATOM 2494 C TRP A 189 11.959 11.031 -3.202 1.00 13.53 C ANISOU 2494 C TRP A 189 1741 1659 1739 -111 43 184 C ATOM 2495 O TRP A 189 11.029 10.395 -2.744 1.00 14.11 O ANISOU 2495 O TRP A 189 1827 1936 1595 -233 10 262 O ATOM 2496 CB TRP A 189 13.403 10.411 -1.269 1.00 11.83 C ANISOU 2496 CB TRP A 189 1772 1564 1158 -207 45 19 C ATOM 2497 CG TRP A 189 14.710 9.811 -0.781 1.00 12.90 C ANISOU 2497 CG TRP A 189 1967 1735 1199 2 -49 45 C ATOM 2498 CD1 TRP A 189 15.789 9.404 -1.528 1.00 14.01 C ANISOU 2498 CD1 TRP A 189 1914 1935 1471 129 -136 46 C ATOM 2499 CD2 TRP A 189 15.029 9.504 0.583 1.00 12.92 C ANISOU 2499 CD2 TRP A 189 1908 1816 1183 -123 -110 -55 C ATOM 2500 NE1 TRP A 189 16.770 8.903 -0.702 1.00 14.40 N ANISOU 2500 NE1 TRP A 189 1905 2392 1173 164 63 253 N ATOM 2501 CE2 TRP A 189 16.328 8.941 0.597 1.00 13.87 C ANISOU 2501 CE2 TRP A 189 1991 2101 1176 61 111 337 C ATOM 2502 CE3 TRP A 189 14.370 9.698 1.818 1.00 13.83 C ANISOU 2502 CE3 TRP A 189 2122 1818 1313 39 88 48 C ATOM 2503 CZ2 TRP A 189 16.966 8.553 1.807 1.00 15.48 C ANISOU 2503 CZ2 TRP A 189 2171 2392 1318 236 55 532 C ATOM 2504 CZ3 TRP A 189 15.006 9.294 3.007 1.00 15.80 C ANISOU 2504 CZ3 TRP A 189 2232 2413 1358 -42 75 332 C ATOM 2505 CH2 TRP A 189 16.286 8.731 2.984 1.00 15.70 C ANISOU 2505 CH2 TRP A 189 2411 2330 1221 62 85 623 C ATOM 2506 H TRP A 189 14.022 12.616 -2.588 1.00 12.40 H ANISOU 2506 H TRP A 189 1774 1494 1443 -1 -128 -18 H ATOM 2507 HA TRP A 189 13.690 9.981 -3.235 1.00 11.84 H ANISOU 2507 HA TRP A 189 1791 1482 1225 -105 48 -45 H ATOM 2508 HB2 TRP A 189 13.240 11.217 -0.754 1.00 11.82 H ANISOU 2508 HB2 TRP A 189 1774 1595 1120 -161 49 6 H ATOM 2509 HB3 TRP A 189 12.709 9.760 -1.084 1.00 12.44 H ANISOU 2509 HB3 TRP A 189 1831 1466 1426 -128 195 119 H ATOM 2510 HD1 TRP A 189 15.858 9.462 -2.451 1.00 11.98 H ANISOU 2510 HD1 TRP A 189 1422 1611 1518 180 -32 195 H ATOM 2511 HE1 TRP A 189 17.527 8.586 -0.961 1.00 13.63 H ANISOU 2511 HE1 TRP A 189 1767 2123 1286 21 61 286 H ATOM 2512 HE3 TRP A 189 13.514 10.059 1.841 1.00 14.22 H ANISOU 2512 HE3 TRP A 189 1912 2011 1480 -144 88 73 H ATOM 2513 HZ2 TRP A 189 17.822 8.188 1.800 1.00 15.46 H ANISOU 2513 HZ2 TRP A 189 1944 2279 1649 -17 -129 279 H ATOM 2514 HZ3 TRP A 189 14.567 9.400 3.820 1.00 15.42 H ANISOU 2514 HZ3 TRP A 189 2168 2264 1427 -243 153 468 H ATOM 2515 HH2 TRP A 189 16.686 8.478 3.785 1.00 15.44 H ANISOU 2515 HH2 TRP A 189 2277 2241 1345 -111 33 690 H ATOM 2516 N GLY A 190 11.817 11.950 -4.154 1.00 11.94 N ANISOU 2516 N GLY A 190 1502 1696 1336 -182 7 0 N ATOM 2517 CA GLY A 190 10.535 12.337 -4.692 1.00 11.81 C ANISOU 2517 CA GLY A 190 1820 1646 1019 -192 -211 -35 C ATOM 2518 C GLY A 190 9.767 13.270 -3.768 1.00 11.89 C ANISOU 2518 C GLY A 190 1549 1888 1080 -235 68 35 C ATOM 2519 O GLY A 190 10.132 13.537 -2.615 1.00 13.13 O ANISOU 2519 O GLY A 190 1873 1901 1214 -172 -52 -117 O ATOM 2520 H GLY A 190 12.470 12.371 -4.521 1.00 12.26 H ANISOU 2520 H GLY A 190 1676 1527 1454 -155 188 -75 H ATOM 2521 HA2 GLY A 190 9.994 11.548 -4.853 1.00 12.01 H ANISOU 2521 HA2 GLY A 190 1488 1551 1523 -110 -70 142 H ATOM 2522 HA3 GLY A 190 10.669 12.792 -5.538 1.00 11.64 H ANISOU 2522 HA3 GLY A 190 1604 1564 1252 -37 166 59 H ATOM 2523 N AGLU A 191 8.648 13.764 -4.287 0.70 15.46 N ANISOU 2523 N AGLU A 191 1751 2475 1648 24 -196 -37 N ATOM 2524 CA AGLU A 191 7.900 14.793 -3.582 0.70 18.29 C ANISOU 2524 CA AGLU A 191 1978 2244 2727 65 -41 -243 C ATOM 2525 C AGLU A 191 6.933 14.226 -2.539 0.70 15.79 C ANISOU 2525 C AGLU A 191 1988 2474 1534 186 -431 -494 C ATOM 2526 O AGLU A 191 6.340 14.991 -1.787 0.70 19.44 O ANISOU 2526 O AGLU A 191 2204 2783 2399 167 55 -818 O ATOM 2527 CB AGLU A 191 7.197 15.735 -4.577 0.70 19.57 C ANISOU 2527 CB AGLU A 191 2479 2404 2553 364 -74 -382 C ATOM 2528 CG AGLU A 191 6.020 15.132 -5.293 0.70 21.49 C ANISOU 2528 CG AGLU A 191 2459 2765 2940 263 -264 -158 C ATOM 2529 CD AGLU A 191 5.398 16.085 -6.291 0.70 26.51 C ANISOU 2529 CD AGLU A 191 4165 3143 2762 439 -655 -92 C ATOM 2530 OE1AGLU A 191 5.339 17.309 -6.013 0.70 25.86 O ANISOU 2530 OE1AGLU A 191 2894 2997 3932 686 -412 138 O ATOM 2531 OE2AGLU A 191 4.962 15.601 -7.353 0.70 30.46 O ANISOU 2531 OE2AGLU A 191 4364 4400 2806 3 -929 0 O ATOM 2532 H AGLU A 191 8.309 13.519 -5.037 0.70 15.25 H ANISOU 2532 H AGLU A 191 1680 2378 1733 -149 -275 85 H ATOM 2533 HA AGLU A 191 8.536 15.354 -3.091 0.70 18.74 H ANISOU 2533 HA AGLU A 191 2445 2318 2355 -19 -88 -238 H ATOM 2534 HB2AGLU A 191 6.880 16.511 -4.089 0.70 20.06 H ANISOU 2534 HB2AGLU A 191 2787 2202 2633 349 124 -160 H ATOM 2535 HB3AGLU A 191 7.839 16.011 -5.249 0.70 19.78 H ANISOU 2535 HB3AGLU A 191 2505 2467 2541 289 -96 -293 H ATOM 2536 HG2AGLU A 191 6.301 14.338 -5.769 0.70 21.22 H ANISOU 2536 HG2AGLU A 191 2746 2747 2567 -82 -186 -223 H ATOM 2537 HG3AGLU A 191 5.336 14.902 -4.646 0.70 21.61 H ANISOU 2537 HG3AGLU A 191 2670 2650 2890 124 -173 -226 H ATOM 2538 N BGLU A 191 8.649 13.772 -4.284 0.30 14.90 N ANISOU 2538 N BGLU A 191 1707 2287 1666 -13 -181 -85 N ATOM 2539 CA BGLU A 191 7.851 14.765 -3.566 0.30 16.58 C ANISOU 2539 CA BGLU A 191 1856 2250 2192 97 -141 -190 C ATOM 2540 C BGLU A 191 7.054 14.197 -2.418 0.30 15.75 C ANISOU 2540 C BGLU A 191 1754 2361 1867 213 -233 -305 C ATOM 2541 O BGLU A 191 6.712 14.916 -1.482 0.30 15.67 O ANISOU 2541 O BGLU A 191 1391 2779 1782 107 -630 -633 O ATOM 2542 CB BGLU A 191 6.897 15.452 -4.523 0.30 16.36 C ANISOU 2542 CB BGLU A 191 1930 2153 2131 114 -127 -213 C ATOM 2543 CG BGLU A 191 7.625 16.294 -5.500 0.30 17.39 C ANISOU 2543 CG BGLU A 191 2143 2402 2062 31 -89 -123 C ATOM 2544 CD BGLU A 191 6.718 17.224 -6.235 0.30 22.07 C ANISOU 2544 CD BGLU A 191 2855 2453 3075 234 -250 297 C ATOM 2545 OE1BGLU A 191 6.042 16.786 -7.186 0.30 25.00 O ANISOU 2545 OE1BGLU A 191 3605 3289 2604 200 -664 876 O ATOM 2546 OE2BGLU A 191 6.701 18.407 -5.863 0.30 31.82 O ANISOU 2546 OE2BGLU A 191 4864 2344 4882 227 -460 226 O ATOM 2547 H BGLU A 191 8.328 13.555 -5.052 0.30 14.15 H ANISOU 2547 H BGLU A 191 1588 2127 1661 -146 -194 71 H ATOM 2548 HA BGLU A 191 8.448 15.452 -3.204 0.30 16.62 H ANISOU 2548 HA BGLU A 191 2125 2150 2038 81 -213 -123 H ATOM 2549 HB2BGLU A 191 6.395 14.782 -5.013 0.30 16.43 H ANISOU 2549 HB2BGLU A 191 2139 2154 1947 96 -160 -166 H ATOM 2550 HB3BGLU A 191 6.294 16.022 -4.020 0.30 16.15 H ANISOU 2550 HB3BGLU A 191 2025 1979 2131 106 -80 -122 H ATOM 2551 HG2BGLU A 191 8.287 16.825 -5.031 0.30 18.31 H ANISOU 2551 HG2BGLU A 191 2330 2246 2381 -132 49 -230 H ATOM 2552 HG3BGLU A 191 8.058 15.716 -6.146 0.30 17.85 H ANISOU 2552 HG3BGLU A 191 2343 2275 2160 -36 5 -136 H ATOM 2553 N GLU A 192 6.773 12.906 -2.470 1.00 16.45 N ANISOU 2553 N GLU A 192 1806 2538 1904 -131 -231 -457 N ATOM 2554 CA GLU A 192 5.899 12.284 -1.460 1.00 18.56 C ANISOU 2554 CA GLU A 192 1988 2783 2278 -115 204 -561 C ATOM 2555 C GLU A 192 6.579 12.048 -0.113 1.00 19.03 C ANISOU 2555 C GLU A 192 2286 2791 2154 -369 207 -111 C ATOM 2556 O GLU A 192 5.918 11.716 0.872 1.00 23.10 O ANISOU 2556 O GLU A 192 2603 3444 2726 -425 704 -214 O ATOM 2557 CB GLU A 192 5.292 10.990 -1.986 1.00 22.94 C ANISOU 2557 CB GLU A 192 2717 2782 3215 -545 300 -536 C ATOM 2558 CG GLU A 192 4.257 11.243 -3.093 1.00 28.42 C ANISOU 2558 CG GLU A 192 2917 3815 4064 -781 -358 -252 C ATOM 2559 CD GLU A 192 3.708 9.976 -3.732 1.00 36.73 C ANISOU 2559 CD GLU A 192 4616 4412 4925 -1093 -1032 -731 C ATOM 2560 OE1 GLU A 192 3.972 8.864 -3.215 1.00 41.11 O ANISOU 2560 OE1 GLU A 192 5262 4140 6216 -721 -279 -656 O ATOM 2561 OE2 GLU A 192 3.003 10.106 -4.756 1.00 48.30 O ANISOU 2561 OE2 GLU A 192 6272 7170 4907 -944 -1675 -977 O ATOM 2562 H GLU A 192 7.106 12.347 -3.029 1.00 16.08 H ANISOU 2562 H GLU A 192 1911 2216 1982 12 -31 -138 H ATOM 2563 HA GLU A 192 5.141 12.881 -1.289 1.00 19.47 H ANISOU 2563 HA GLU A 192 2178 2724 2493 26 233 -269 H ATOM 2564 HB2 GLU A 192 5.989 10.425 -2.348 1.00 22.84 H ANISOU 2564 HB2 GLU A 192 3256 2513 2910 -245 198 -404 H ATOM 2565 HB3 GLU A 192 4.840 10.532 -1.260 1.00 24.73 H ANISOU 2565 HB3 GLU A 192 2995 2869 3531 -433 406 -256 H ATOM 2566 HG2 GLU A 192 3.509 11.730 -2.714 1.00 29.20 H ANISOU 2566 HG2 GLU A 192 3419 4050 3622 -227 -196 219 H ATOM 2567 HG3 GLU A 192 4.671 11.771 -3.793 1.00 28.44 H ANISOU 2567 HG3 GLU A 192 3449 3671 3684 -19 -97 -159 H ATOM 2568 N TRP A 193 7.897 12.255 -0.065 1.00 17.04 N ANISOU 2568 N TRP A 193 2231 2216 2023 -391 70 -100 N ATOM 2569 CA TRP A 193 8.681 12.181 1.171 1.00 16.31 C ANISOU 2569 CA TRP A 193 2296 1943 1956 -347 144 18 C ATOM 2570 C TRP A 193 8.827 13.589 1.771 1.00 14.73 C ANISOU 2570 C TRP A 193 1973 1969 1653 -126 43 77 C ATOM 2571 O TRP A 193 9.004 14.560 1.037 1.00 14.20 O ANISOU 2571 O TRP A 193 1949 2016 1427 -51 -354 75 O ATOM 2572 CB TRP A 193 10.068 11.591 0.882 1.00 15.38 C ANISOU 2572 CB TRP A 193 2286 1939 1616 -270 38 138 C ATOM 2573 CG TRP A 193 10.944 11.549 2.096 1.00 15.69 C ANISOU 2573 CG TRP A 193 2386 1950 1625 -174 -40 109 C ATOM 2574 CD1 TRP A 193 11.034 10.525 3.004 1.00 14.57 C ANISOU 2574 CD1 TRP A 193 2232 1757 1545 -12 125 12 C ATOM 2575 CD2 TRP A 193 11.841 12.566 2.558 1.00 13.53 C ANISOU 2575 CD2 TRP A 193 2093 1716 1331 57 100 28 C ATOM 2576 NE1 TRP A 193 11.915 10.851 4.009 1.00 15.39 N ANISOU 2576 NE1 TRP A 193 2572 1733 1539 -113 -36 201 N ATOM 2577 CE2 TRP A 193 12.422 12.096 3.769 1.00 13.82 C ANISOU 2577 CE2 TRP A 193 2109 1708 1433 20 54 85 C ATOM 2578 CE3 TRP A 193 12.196 13.842 2.093 1.00 13.24 C ANISOU 2578 CE3 TRP A 193 1998 1821 1211 17 -75 78 C ATOM 2579 CZ2 TRP A 193 13.355 12.823 4.477 1.00 13.97 C ANISOU 2579 CZ2 TRP A 193 2135 1780 1391 121 -49 118 C ATOM 2580 CZ3 TRP A 193 13.117 14.577 2.831 1.00 13.12 C ANISOU 2580 CZ3 TRP A 193 1840 1660 1485 54 -139 143 C ATOM 2581 CH2 TRP A 193 13.688 14.059 4.013 1.00 13.60 C ANISOU 2581 CH2 TRP A 193 1878 1706 1581 204 -194 152 C ATOM 2582 H TRP A 193 8.381 12.435 -0.752 1.00 16.53 H ANISOU 2582 H TRP A 193 2073 2230 1975 -109 25 -71 H ATOM 2583 HA TRP A 193 8.233 11.605 1.825 1.00 16.75 H ANISOU 2583 HA TRP A 193 2241 2008 2113 -305 168 99 H ATOM 2584 HB2 TRP A 193 9.963 10.683 0.556 1.00 15.45 H ANISOU 2584 HB2 TRP A 193 2163 1883 1821 -260 -105 170 H ATOM 2585 HB3 TRP A 193 10.511 12.135 0.212 1.00 14.95 H ANISOU 2585 HB3 TRP A 193 2156 1839 1682 -184 -22 189 H ATOM 2586 HD1 TRP A 193 10.553 9.730 2.957 1.00 15.20 H ANISOU 2586 HD1 TRP A 193 2112 1786 1877 -2 99 43 H ATOM 2587 HE1 TRP A 193 12.126 10.346 4.672 1.00 14.63 H ANISOU 2587 HE1 TRP A 193 2262 1664 1630 156 69 158 H ATOM 2588 HE3 TRP A 193 11.822 14.189 1.315 1.00 12.78 H ANISOU 2588 HE3 TRP A 193 1688 1711 1455 252 -101 83 H ATOM 2589 HZ2 TRP A 193 13.839 12.430 5.167 1.00 13.39 H ANISOU 2589 HZ2 TRP A 193 1853 1649 1582 201 23 144 H ATOM 2590 HZ3 TRP A 193 13.373 15.419 2.532 1.00 13.22 H ANISOU 2590 HZ3 TRP A 193 1939 1618 1466 116 -23 110 H ATOM 2591 HH2 TRP A 193 14.309 14.562 4.483 1.00 13.45 H ANISOU 2591 HH2 TRP A 193 1780 1854 1476 137 -100 165 H ATOM 2592 N GLY A 194 8.737 13.714 3.090 1.00 15.73 N ANISOU 2592 N GLY A 194 2430 1826 1718 -256 355 149 N ATOM 2593 CA GLY A 194 8.986 14.998 3.730 1.00 14.89 C ANISOU 2593 CA GLY A 194 2136 1896 1625 -101 171 59 C ATOM 2594 C GLY A 194 7.981 16.045 3.322 1.00 13.16 C ANISOU 2594 C GLY A 194 1807 2153 1039 -154 171 -76 C ATOM 2595 O GLY A 194 6.803 15.745 3.124 1.00 15.97 O ANISOU 2595 O GLY A 194 1802 2775 1490 -330 107 -336 O ATOM 2596 H GLY A 194 8.536 13.078 3.632 1.00 14.86 H ANISOU 2596 H GLY A 194 2088 1822 1736 -116 92 242 H ATOM 2597 HA2 GLY A 194 9.877 15.300 3.496 1.00 14.29 H ANISOU 2597 HA2 GLY A 194 1959 1926 1543 -9 -3 16 H ATOM 2598 HA3 GLY A 194 8.941 14.891 4.693 1.00 15.03 H ANISOU 2598 HA3 GLY A 194 2026 2038 1645 -40 48 131 H ATOM 2599 N AMET A 195 8.465 17.285 3.225 0.50 13.41 N ANISOU 2599 N AMET A 195 1748 1901 1444 57 -189 -179 N ATOM 2600 CA AMET A 195 7.657 18.466 2.956 0.50 13.10 C ANISOU 2600 CA AMET A 195 1554 2083 1338 144 -117 -317 C ATOM 2601 C AMET A 195 7.773 18.734 1.455 0.50 13.12 C ANISOU 2601 C AMET A 195 1707 1893 1384 84 -262 -170 C ATOM 2602 O AMET A 195 8.602 19.523 1.016 0.50 14.47 O ANISOU 2602 O AMET A 195 1716 2075 1707 -37 -251 -37 O ATOM 2603 CB AMET A 195 8.158 19.668 3.780 0.50 11.87 C ANISOU 2603 CB AMET A 195 1466 1860 1183 108 -152 -8 C ATOM 2604 CG AMET A 195 8.113 19.452 5.286 0.50 11.49 C ANISOU 2604 CG AMET A 195 1451 1794 1118 46 -29 -118 C ATOM 2605 SD AMET A 195 8.679 20.873 6.238 0.50 12.18 S ANISOU 2605 SD AMET A 195 1589 1902 1136 24 -170 -78 S ATOM 2606 CE AMET A 195 7.350 22.029 5.853 0.50 13.68 C ANISOU 2606 CE AMET A 195 1990 2005 1201 255 -547 -98 C ATOM 2607 H AMET A 195 9.299 17.474 3.317 0.50 12.89 H ANISOU 2607 H AMET A 195 1681 1774 1440 107 -33 -16 H ATOM 2608 HA AMET A 195 6.721 18.297 3.192 0.50 13.73 H ANISOU 2608 HA AMET A 195 1634 1916 1665 -27 -79 -138 H ATOM 2609 HB2AMET A 195 9.079 19.851 3.535 0.50 11.92 H ANISOU 2609 HB2AMET A 195 1554 1737 1236 100 18 67 H ATOM 2610 HB3AMET A 195 7.605 20.438 3.575 0.50 12.25 H ANISOU 2610 HB3AMET A 195 1485 1729 1438 15 -27 150 H ATOM 2611 HG2AMET A 195 7.198 19.264 5.548 0.50 12.13 H ANISOU 2611 HG2AMET A 195 1467 1762 1377 0 -25 33 H ATOM 2612 HG3AMET A 195 8.681 18.699 5.511 0.50 11.56 H ANISOU 2612 HG3AMET A 195 1430 1734 1226 -66 -17 104 H ATOM 2613 N BMET A 195 8.439 17.288 3.235 0.50 14.49 N ANISOU 2613 N BMET A 195 1824 1990 1690 -15 -255 50 N ATOM 2614 CA BMET A 195 7.577 18.418 2.955 0.50 14.65 C ANISOU 2614 CA BMET A 195 1779 2272 1513 170 -222 -103 C ATOM 2615 C BMET A 195 7.752 18.729 1.474 0.50 13.78 C ANISOU 2615 C BMET A 195 1734 1992 1509 57 -428 -75 C ATOM 2616 O BMET A 195 8.592 19.526 1.073 0.50 15.03 O ANISOU 2616 O BMET A 195 1816 2128 1765 -72 -356 -9 O ATOM 2617 CB BMET A 195 7.922 19.599 3.867 0.50 14.75 C ANISOU 2617 CB BMET A 195 1792 2225 1586 161 -174 -47 C ATOM 2618 CG BMET A 195 7.588 19.322 5.322 0.50 14.91 C ANISOU 2618 CG BMET A 195 1750 2319 1595 248 -4 -108 C ATOM 2619 SD BMET A 195 7.905 20.690 6.430 0.50 18.57 S ANISOU 2619 SD BMET A 195 2735 2350 1968 -80 201 -134 S ATOM 2620 CE BMET A 195 9.516 21.155 5.835 0.50 19.09 C ANISOU 2620 CE BMET A 195 2497 2179 2576 -141 36 -182 C ATOM 2621 H BMET A 195 9.265 17.506 3.338 0.50 13.48 H ANISOU 2621 H BMET A 195 1752 1832 1536 50 -56 30 H ATOM 2622 HA BMET A 195 6.642 18.181 3.126 0.50 15.42 H ANISOU 2622 HA BMET A 195 1857 2155 1844 81 -112 -44 H ATOM 2623 HB2BMET A 195 8.874 19.775 3.807 0.50 14.52 H ANISOU 2623 HB2BMET A 195 1852 1965 1700 58 -24 8 H ATOM 2624 HB3BMET A 195 7.423 20.381 3.585 0.50 15.27 H ANISOU 2624 HB3BMET A 195 1828 2031 1940 29 -34 101 H ATOM 2625 HG2BMET A 195 6.648 19.093 5.391 0.50 16.50 H ANISOU 2625 HG2BMET A 195 1856 2389 2022 64 34 104 H ATOM 2626 HG3BMET A 195 8.132 18.578 5.622 0.50 15.35 H ANISOU 2626 HG3BMET A 195 1897 2122 1813 16 -66 159 H ATOM 2627 N GLY A 196 6.978 18.038 0.645 1.00 13.23 N ANISOU 2627 N GLY A 196 1533 2204 1289 -33 -79 -207 N ATOM 2628 CA GLY A 196 7.156 18.127 -0.788 1.00 12.82 C ANISOU 2628 CA GLY A 196 1686 1914 1271 56 -323 -15 C ATOM 2629 C GLY A 196 8.543 17.724 -1.295 1.00 12.94 C ANISOU 2629 C GLY A 196 1533 1898 1486 -115 -292 136 C ATOM 2630 O GLY A 196 9.019 18.241 -2.291 1.00 14.51 O ANISOU 2630 O GLY A 196 1865 1913 1731 90 -78 292 O ATOM 2631 H GLY A 196 6.344 17.516 0.897 1.00 13.12 H ANISOU 2631 H GLY A 196 1686 1835 1462 22 -118 -79 H ATOM 2632 HA2 GLY A 196 6.991 19.041 -1.069 1.00 13.59 H ANISOU 2632 HA2 GLY A 196 1782 1769 1613 -65 -138 -66 H ATOM 2633 HA3 GLY A 196 6.500 17.561 -1.223 1.00 11.95 H ANISOU 2633 HA3 GLY A 196 1536 1731 1272 58 -57 -101 H ATOM 2634 N GLY A 197 9.205 16.841 -0.555 1.00 13.01 N ANISOU 2634 N GLY A 197 1714 1852 1375 -41 -166 141 N ATOM 2635 CA GLY A 197 10.540 16.393 -0.918 1.00 13.50 C ANISOU 2635 CA GLY A 197 1664 1749 1715 -46 -177 -75 C ATOM 2636 C GLY A 197 11.682 17.098 -0.237 1.00 11.84 C ANISOU 2636 C GLY A 197 1742 1730 1025 -49 -57 23 C ATOM 2637 O GLY A 197 12.830 16.720 -0.449 1.00 12.48 O ANISOU 2637 O GLY A 197 1676 1657 1406 7 -204 79 O ATOM 2638 H GLY A 197 8.903 16.470 0.158 1.00 13.07 H ANISOU 2638 H GLY A 197 1797 1695 1473 -117 -108 110 H ATOM 2639 HA2 GLY A 197 10.667 16.487 -1.875 1.00 12.13 H ANISOU 2639 HA2 GLY A 197 1380 1573 1656 -112 -291 -125 H ATOM 2640 HA3 GLY A 197 10.619 15.450 -0.710 1.00 13.55 H ANISOU 2640 HA3 GLY A 197 1780 1745 1621 -74 -103 -68 H ATOM 2641 N TYR A 198 11.348 18.079 0.613 1.00 11.00 N ANISOU 2641 N TYR A 198 1487 1796 895 65 -168 85 N ATOM 2642 CA TYR A 198 12.273 18.879 1.413 1.00 11.54 C ANISOU 2642 CA TYR A 198 1474 1599 1310 -80 -175 33 C ATOM 2643 C TYR A 198 12.212 18.477 2.893 1.00 11.83 C ANISOU 2643 C TYR A 198 1635 1559 1299 0 -231 -45 C ATOM 2644 O TYR A 198 11.229 17.906 3.391 1.00 12.47 O ANISOU 2644 O TYR A 198 1633 1797 1306 -20 -192 123 O ATOM 2645 CB TYR A 198 11.931 20.384 1.289 1.00 11.66 C ANISOU 2645 CB TYR A 198 1615 1713 1100 34 -228 48 C ATOM 2646 CG TYR A 198 12.413 20.984 0.001 1.00 12.00 C ANISOU 2646 CG TYR A 198 1706 1689 1162 74 -157 139 C ATOM 2647 CD1 TYR A 198 11.662 20.905 -1.180 1.00 12.62 C ANISOU 2647 CD1 TYR A 198 1835 1762 1195 19 -189 93 C ATOM 2648 CD2 TYR A 198 13.660 21.594 -0.068 1.00 12.57 C ANISOU 2648 CD2 TYR A 198 1668 1715 1392 97 -266 398 C ATOM 2649 CE1 TYR A 198 12.153 21.389 -2.398 1.00 12.83 C ANISOU 2649 CE1 TYR A 198 1975 1763 1135 92 -320 204 C ATOM 2650 CE2 TYR A 198 14.139 22.094 -1.234 1.00 12.82 C ANISOU 2650 CE2 TYR A 198 1897 1575 1399 -32 -339 432 C ATOM 2651 CZ TYR A 198 13.414 21.999 -2.397 1.00 13.04 C ANISOU 2651 CZ TYR A 198 1849 1836 1266 129 -200 317 C ATOM 2652 OH TYR A 198 13.944 22.488 -3.565 1.00 14.10 O ANISOU 2652 OH TYR A 198 2313 1788 1254 9 26 74 O ATOM 2653 H TYR A 198 10.534 18.312 0.753 1.00 11.73 H ANISOU 2653 H TYR A 198 1423 1706 1328 -45 -153 7 H ATOM 2654 HA TYR A 198 13.185 18.741 1.088 1.00 12.24 H ANISOU 2654 HA TYR A 198 1496 1686 1465 -25 -126 64 H ATOM 2655 HB2 TYR A 198 10.972 20.506 1.335 1.00 11.79 H ANISOU 2655 HB2 TYR A 198 1564 1564 1350 -83 -182 51 H ATOM 2656 HB3 TYR A 198 12.357 20.865 2.016 1.00 11.28 H ANISOU 2656 HB3 TYR A 198 1539 1577 1170 -61 -140 50 H ATOM 2657 HD1 TYR A 198 10.838 20.474 -1.164 1.00 12.97 H ANISOU 2657 HD1 TYR A 198 1637 1930 1361 146 -214 94 H ATOM 2658 HD2 TYR A 198 14.182 21.651 0.700 1.00 12.03 H ANISOU 2658 HD2 TYR A 198 1568 1705 1297 132 -143 247 H ATOM 2659 HE1 TYR A 198 11.649 21.330 -3.177 1.00 12.87 H ANISOU 2659 HE1 TYR A 198 1675 1995 1219 377 -286 190 H ATOM 2660 HE2 TYR A 198 14.981 22.486 -1.252 1.00 12.91 H ANISOU 2660 HE2 TYR A 198 1674 1821 1408 134 -131 298 H ATOM 2661 N VAL A 199 13.305 18.740 3.591 1.00 12.39 N ANISOU 2661 N VAL A 199 1691 1718 1298 -25 -291 57 N ATOM 2662 CA VAL A 199 13.353 18.632 5.026 1.00 12.20 C ANISOU 2662 CA VAL A 199 1708 1667 1257 -17 -254 55 C ATOM 2663 C VAL A 199 14.007 19.876 5.618 1.00 12.41 C ANISOU 2663 C VAL A 199 1720 1576 1418 52 -176 77 C ATOM 2664 O VAL A 199 14.962 20.395 5.064 1.00 13.51 O ANISOU 2664 O VAL A 199 1773 1712 1646 -101 -212 191 O ATOM 2665 CB VAL A 199 14.097 17.303 5.472 1.00 12.56 C ANISOU 2665 CB VAL A 199 1796 1487 1489 -17 -113 64 C ATOM 2666 CG1 VAL A 199 15.464 17.142 4.770 1.00 11.97 C ANISOU 2666 CG1 VAL A 199 1870 1955 720 -114 -259 46 C ATOM 2667 CG2 VAL A 199 14.241 17.171 7.006 1.00 13.31 C ANISOU 2667 CG2 VAL A 199 1781 1866 1410 -99 -130 244 C ATOM 2668 H VAL A 199 14.043 19.003 3.237 1.00 12.09 H ANISOU 2668 H VAL A 199 1607 1709 1274 75 -255 39 H ATOM 2669 HA VAL A 199 12.440 18.588 5.378 1.00 12.74 H ANISOU 2669 HA VAL A 199 1722 1679 1437 8 -162 90 H ATOM 2670 HB VAL A 199 13.539 16.554 5.183 1.00 13.21 H ANISOU 2670 HB VAL A 199 1803 1612 1602 -41 -176 -5 H ATOM 2671 N LYS A 200 13.469 20.312 6.754 1.00 12.15 N ANISOU 2671 N LYS A 200 1714 1610 1290 -90 -173 127 N ATOM 2672 CA LYS A 200 14.081 21.364 7.558 1.00 13.26 C ANISOU 2672 CA LYS A 200 1873 1664 1501 -108 -414 119 C ATOM 2673 C LYS A 200 14.946 20.675 8.597 1.00 12.42 C ANISOU 2673 C LYS A 200 1903 1723 1092 46 -184 28 C ATOM 2674 O LYS A 200 14.427 20.055 9.515 1.00 16.89 O ANISOU 2674 O LYS A 200 2182 2618 1615 180 58 615 O ATOM 2675 CB LYS A 200 13.005 22.210 8.238 1.00 14.60 C ANISOU 2675 CB LYS A 200 2058 1481 2006 -110 -285 134 C ATOM 2676 CG LYS A 200 12.192 23.021 7.256 1.00 15.29 C ANISOU 2676 CG LYS A 200 2021 2039 1747 -33 -238 236 C ATOM 2677 CD LYS A 200 11.126 23.831 7.951 1.00 16.54 C ANISOU 2677 CD LYS A 200 2262 2068 1954 7 -139 54 C ATOM 2678 CE LYS A 200 10.342 24.701 6.985 1.00 18.30 C ANISOU 2678 CE LYS A 200 2625 2244 2084 280 -172 130 C ATOM 2679 NZ LYS A 200 9.241 25.450 7.669 1.00 20.42 N ANISOU 2679 NZ LYS A 200 2587 2599 2572 396 -600 -728 N ATOM 2680 H LYS A 200 12.738 20.007 7.088 1.00 12.51 H ANISOU 2680 H LYS A 200 1598 1571 1581 -6 -127 61 H ATOM 2681 HA LYS A 200 14.625 21.953 7.000 1.00 13.22 H ANISOU 2681 HA LYS A 200 1975 1469 1578 -50 -432 180 H ATOM 2682 HB2 LYS A 200 12.398 21.629 8.721 1.00 14.37 H ANISOU 2682 HB2 LYS A 200 1947 1696 1816 -46 -220 122 H ATOM 2683 HB3 LYS A 200 13.432 22.827 8.853 1.00 13.95 H ANISOU 2683 HB3 LYS A 200 1827 1781 1692 -51 -162 81 H ATOM 2684 HG2 LYS A 200 12.781 23.637 6.792 1.00 15.08 H ANISOU 2684 HG2 LYS A 200 2112 1763 1851 -8 -241 184 H ATOM 2685 HG3 LYS A 200 11.770 22.428 6.621 1.00 15.06 H ANISOU 2685 HG3 LYS A 200 1898 1943 1880 -36 -132 160 H ATOM 2686 HD2 LYS A 200 10.504 23.228 8.388 1.00 16.42 H ANISOU 2686 HD2 LYS A 200 2091 2049 2096 61 -120 46 H ATOM 2687 HD3 LYS A 200 11.545 24.410 8.607 1.00 16.93 H ANISOU 2687 HD3 LYS A 200 2233 2132 2065 -57 -118 14 H ATOM 2688 HE2 LYS A 200 10.941 25.349 6.582 1.00 18.99 H ANISOU 2688 HE2 LYS A 200 2774 2165 2275 105 -402 196 H ATOM 2689 HE3 LYS A 200 9.946 24.143 6.298 1.00 16.48 H ANISOU 2689 HE3 LYS A 200 2015 2203 2041 329 -6 128 H ATOM 2690 N AMET A 201 16.263 20.728 8.397 0.50 12.94 N ANISOU 2690 N AMET A 201 1860 1911 1142 -256 -518 87 N ATOM 2691 CA AMET A 201 17.229 20.116 9.313 0.50 13.33 C ANISOU 2691 CA AMET A 201 1933 1751 1377 -112 -556 65 C ATOM 2692 C AMET A 201 17.576 21.107 10.441 0.50 12.24 C ANISOU 2692 C AMET A 201 1863 1653 1134 -120 -618 218 C ATOM 2693 O AMET A 201 17.697 22.300 10.190 0.50 12.06 O ANISOU 2693 O AMET A 201 1498 1564 1519 188 -232 306 O ATOM 2694 CB AMET A 201 18.500 19.696 8.554 0.50 13.22 C ANISOU 2694 CB AMET A 201 1958 1712 1351 -197 -461 231 C ATOM 2695 CG AMET A 201 18.292 18.628 7.480 0.50 13.86 C ANISOU 2695 CG AMET A 201 1798 1851 1615 -330 -124 0 C ATOM 2696 SD AMET A 201 17.928 16.973 8.123 0.50 14.32 S ANISOU 2696 SD AMET A 201 2122 1892 1425 -10 -331 230 S ATOM 2697 CE AMET A 201 19.451 16.556 8.988 0.50 15.32 C ANISOU 2697 CE AMET A 201 1681 2025 2115 34 -98 380 C ATOM 2698 H AMET A 201 16.632 21.118 7.726 0.50 12.58 H ANISOU 2698 H AMET A 201 1775 1529 1475 65 -236 159 H ATOM 2699 HA AMET A 201 16.840 19.307 9.707 0.50 12.91 H ANISOU 2699 HA AMET A 201 1877 1575 1450 62 -336 -18 H ATOM 2700 HB2AMET A 201 18.877 20.478 8.123 0.50 13.88 H ANISOU 2700 HB2AMET A 201 2115 1538 1619 -78 -320 207 H ATOM 2701 HB3AMET A 201 19.131 19.339 9.193 0.50 13.35 H ANISOU 2701 HB3AMET A 201 1896 1756 1421 34 -314 207 H ATOM 2702 HG2AMET A 201 17.548 18.895 6.917 0.50 11.82 H ANISOU 2702 HG2AMET A 201 1765 1310 1415 -277 -15 -118 H ATOM 2703 HG3AMET A 201 19.099 18.565 6.946 0.50 14.66 H ANISOU 2703 HG3AMET A 201 1804 1956 1809 -105 -77 49 H ATOM 2704 N BMET A 201 16.258 20.797 8.469 0.50 13.44 N ANISOU 2704 N BMET A 201 1900 1889 1318 -152 -478 186 N ATOM 2705 CA BMET A 201 17.157 20.112 9.383 0.50 13.41 C ANISOU 2705 CA BMET A 201 1958 1665 1468 -99 -554 94 C ATOM 2706 C BMET A 201 17.753 21.046 10.420 0.50 12.96 C ANISOU 2706 C BMET A 201 2118 1733 1072 -8 -511 153 C ATOM 2707 O BMET A 201 18.277 22.097 10.088 0.50 10.97 O ANISOU 2707 O BMET A 201 1752 1726 690 3 -421 -39 O ATOM 2708 CB BMET A 201 18.262 19.420 8.608 0.50 13.66 C ANISOU 2708 CB BMET A 201 2155 1738 1296 -43 -416 168 C ATOM 2709 CG BMET A 201 17.736 18.327 7.730 0.50 14.70 C ANISOU 2709 CG BMET A 201 1942 1625 2017 -174 -203 -32 C ATOM 2710 SD BMET A 201 19.048 17.352 6.987 0.50 13.71 S ANISOU 2710 SD BMET A 201 2092 2021 1093 63 -203 211 S ATOM 2711 CE BMET A 201 19.779 16.495 8.395 0.50 12.89 C ANISOU 2711 CE BMET A 201 2292 1817 788 84 314 415 C ATOM 2712 H BMET A 201 16.654 21.266 7.866 0.50 12.79 H ANISOU 2712 H BMET A 201 1779 1568 1512 83 -256 130 H ATOM 2713 HA BMET A 201 16.665 19.405 9.851 0.50 13.57 H ANISOU 2713 HA BMET A 201 2026 1586 1540 53 -364 120 H ATOM 2714 HB2BMET A 201 18.716 20.069 8.048 0.50 13.66 H ANISOU 2714 HB2BMET A 201 2033 1483 1672 -61 -398 140 H ATOM 2715 HB3BMET A 201 18.885 19.022 9.234 0.50 14.08 H ANISOU 2715 HB3BMET A 201 1897 1961 1490 69 -249 267 H ATOM 2716 HG2BMET A 201 17.183 17.733 8.260 0.50 14.46 H ANISOU 2716 HG2BMET A 201 1891 1769 1835 -24 -110 7 H ATOM 2717 HG3BMET A 201 17.211 18.720 7.015 0.50 13.14 H ANISOU 2717 HG3BMET A 201 1753 1664 1574 -311 -80 -216 H ATOM 2718 N ALA A 202 17.720 20.642 11.679 1.00 13.83 N ANISOU 2718 N ALA A 202 2334 1761 1156 -147 -645 276 N ATOM 2719 CA ALA A 202 18.122 21.511 12.802 1.00 14.09 C ANISOU 2719 CA ALA A 202 2073 2210 1068 -18 -473 64 C ATOM 2720 C ALA A 202 19.448 22.226 12.451 1.00 13.87 C ANISOU 2720 C ALA A 202 2304 2003 962 -97 -452 243 C ATOM 2721 O ALA A 202 20.436 21.586 12.083 1.00 15.30 O ANISOU 2721 O ALA A 202 2045 2006 1762 -212 -644 13 O ATOM 2722 CB ALA A 202 18.254 20.719 14.108 1.00 16.42 C ANISOU 2722 CB ALA A 202 2701 2291 1244 -467 -818 229 C ATOM 2723 H ALA A 202 17.528 19.837 11.915 1.00 13.63 H ANISOU 2723 H ALA A 202 2151 1657 1371 132 -392 321 H ATOM 2724 HA ALA A 202 17.432 22.193 12.935 1.00 15.28 H ANISOU 2724 HA ALA A 202 2235 1912 1656 -85 -407 38 H ATOM 2725 N LYS A 203 19.455 23.544 12.636 1.00 15.63 N ANISOU 2725 N LYS A 203 2159 1929 1847 -117 -538 263 N ATOM 2726 CA LYS A 203 20.614 24.383 12.353 1.00 15.72 C ANISOU 2726 CA LYS A 203 2223 1814 1933 -164 -436 21 C ATOM 2727 C LYS A 203 21.134 25.006 13.644 1.00 16.03 C ANISOU 2727 C LYS A 203 2315 1996 1779 -289 -218 45 C ATOM 2728 O LYS A 203 20.366 25.384 14.541 1.00 15.85 O ANISOU 2728 O LYS A 203 2327 2204 1490 -56 -468 145 O ATOM 2729 CB LYS A 203 20.225 25.482 11.356 1.00 15.98 C ANISOU 2729 CB LYS A 203 2167 1824 2079 -144 -592 70 C ATOM 2730 CG LYS A 203 21.272 26.555 11.114 1.00 15.33 C ANISOU 2730 CG LYS A 203 2176 2000 1648 -172 -448 43 C ATOM 2731 CD LYS A 203 20.928 27.389 9.857 1.00 14.51 C ANISOU 2731 CD LYS A 203 1897 1945 1669 -62 -273 32 C ATOM 2732 CE LYS A 203 21.904 28.570 9.632 1.00 14.64 C ANISOU 2732 CE LYS A 203 2060 2020 1482 -155 -175 -9 C ATOM 2733 NZ LYS A 203 21.680 29.627 10.671 1.00 15.45 N ANISOU 2733 NZ LYS A 203 2439 2167 1262 -34 -431 14 N ATOM 2734 H LYS A 203 18.783 23.990 12.933 1.00 15.77 H ANISOU 2734 H LYS A 203 2253 1976 1761 -180 -394 105 H ATOM 2735 HA LYS A 203 21.331 23.850 11.951 1.00 15.36 H ANISOU 2735 HA LYS A 203 2206 1839 1791 -123 -442 76 H ATOM 2736 HB2 LYS A 203 20.027 25.067 10.502 1.00 15.09 H ANISOU 2736 HB2 LYS A 203 1975 1861 1895 -122 -260 91 H ATOM 2737 HB3 LYS A 203 19.432 25.927 11.689 1.00 15.40 H ANISOU 2737 HB3 LYS A 203 2262 1833 1757 -192 -381 59 H ATOM 2738 HG2 LYS A 203 21.297 27.157 11.873 1.00 14.90 H ANISOU 2738 HG2 LYS A 203 2073 1871 1715 -151 -388 43 H ATOM 2739 HG3 LYS A 203 22.138 26.140 10.981 1.00 15.03 H ANISOU 2739 HG3 LYS A 203 2215 1892 1604 -123 -400 54 H ATOM 2740 HD2 LYS A 203 20.958 26.820 9.076 1.00 14.19 H ANISOU 2740 HD2 LYS A 203 1896 1862 1634 -11 -225 75 H ATOM 2741 HD3 LYS A 203 20.037 27.758 9.962 1.00 14.65 H ANISOU 2741 HD3 LYS A 203 1944 1920 1702 -22 -192 1 H ATOM 2742 HE2 LYS A 203 22.818 28.255 9.705 1.00 15.24 H ANISOU 2742 HE2 LYS A 203 1999 2127 1665 -190 -192 101 H ATOM 2743 HE3 LYS A 203 21.747 28.959 8.757 1.00 14.15 H ANISOU 2743 HE3 LYS A 203 2128 1800 1449 -8 -121 -120 H ATOM 2744 N ASP A 204 22.457 25.130 13.726 1.00 15.22 N ANISOU 2744 N ASP A 204 2254 2117 1410 -30 -359 -42 N ATOM 2745 CA ASP A 204 23.120 25.707 14.896 1.00 16.69 C ANISOU 2745 CA ASP A 204 2490 2198 1654 52 -686 -4 C ATOM 2746 C ASP A 204 22.822 24.925 16.185 1.00 17.74 C ANISOU 2746 C ASP A 204 2964 2346 1430 -500 -1083 -172 C ATOM 2747 O ASP A 204 22.716 25.478 17.276 1.00 19.52 O ANISOU 2747 O ASP A 204 3618 2468 1330 -471 -789 -65 O ATOM 2748 CB ASP A 204 22.852 27.219 15.012 1.00 17.81 C ANISOU 2748 CB ASP A 204 2491 2136 2140 -277 -646 31 C ATOM 2749 CG ASP A 204 23.311 27.986 13.758 1.00 16.82 C ANISOU 2749 CG ASP A 204 2779 2283 1328 -67 -770 -266 C ATOM 2750 OD1 ASP A 204 24.351 27.591 13.180 1.00 20.71 O ANISOU 2750 OD1 ASP A 204 2560 2483 2824 -92 -385 237 O ATOM 2751 OD2 ASP A 204 22.622 28.959 13.346 1.00 18.91 O ANISOU 2751 OD2 ASP A 204 2675 2462 2045 -12 -834 -85 O ATOM 2752 H ASP A 204 23.000 24.893 13.107 1.00 15.83 H ANISOU 2752 H ASP A 204 2302 1922 1789 -42 -182 -132 H ATOM 2753 HA ASP A 204 24.084 25.613 14.753 1.00 18.53 H ANISOU 2753 HA ASP A 204 2387 2348 2302 -183 -668 -60 H ATOM 2754 HB2 ASP A 204 21.903 27.373 15.132 1.00 17.83 H ANISOU 2754 HB2 ASP A 204 2525 2067 2182 -78 -539 -58 H ATOM 2755 HB3 ASP A 204 23.343 27.571 15.771 1.00 15.72 H ANISOU 2755 HB3 ASP A 204 2377 2042 1554 -190 -270 180 H ATOM 2756 N ARG A 205 22.728 23.604 16.012 1.00 17.39 N ANISOU 2756 N ARG A 205 2503 2126 1977 -107 -649 44 N ATOM 2757 CA ARG A 205 22.691 22.651 17.100 1.00 18.85 C ANISOU 2757 CA ARG A 205 2687 2393 2082 -153 -529 258 C ATOM 2758 C ARG A 205 23.907 21.721 16.992 1.00 16.92 C ANISOU 2758 C ARG A 205 2544 2541 1344 -225 -348 249 C ATOM 2759 O ARG A 205 23.784 20.496 16.927 1.00 19.46 O ANISOU 2759 O ARG A 205 2733 2481 2180 -208 -369 332 O ATOM 2760 CB ARG A 205 21.363 21.885 17.092 1.00 20.27 C ANISOU 2760 CB ARG A 205 2628 2389 2683 -156 -598 235 C ATOM 2761 CG ARG A 205 20.144 22.802 17.258 1.00 23.43 C ANISOU 2761 CG ARG A 205 2781 3042 3077 113 -474 -116 C ATOM 2762 CD ARG A 205 18.915 22.071 17.724 1.00 26.71 C ANISOU 2762 CD ARG A 205 3293 3875 2978 -46 0 77 C ATOM 2763 NE ARG A 205 19.062 21.577 19.093 1.00 32.93 N ANISOU 2763 NE ARG A 205 4273 4528 3711 -341 -621 1100 N ATOM 2764 CZ ARG A 205 18.094 20.976 19.778 1.00 33.41 C ANISOU 2764 CZ ARG A 205 3903 5226 3562 361 217 795 C ATOM 2765 NH1 ARG A 205 16.890 20.780 19.226 1.00 37.43 N ANISOU 2765 NH1 ARG A 205 4297 5317 4606 -205 -157 904 N ATOM 2766 NH2 ARG A 205 18.327 20.566 21.019 1.00 38.83 N ANISOU 2766 NH2 ARG A 205 4933 6402 3419 -266 166 984 N ATOM 2767 H ARG A 205 22.688 23.222 15.243 1.00 16.44 H ANISOU 2767 H ARG A 205 2399 1829 2018 -105 -306 33 H ATOM 2768 HA ARG A 205 22.755 23.120 17.958 1.00 18.40 H ANISOU 2768 HA ARG A 205 2536 2386 2067 -142 -327 230 H ATOM 2769 HB2 ARG A 205 21.274 21.420 16.246 1.00 20.14 H ANISOU 2769 HB2 ARG A 205 2416 2639 2594 -258 -343 178 H ATOM 2770 HB3 ARG A 205 21.364 21.247 17.822 1.00 21.08 H ANISOU 2770 HB3 ARG A 205 2905 2549 2554 -196 -109 217 H ATOM 2771 HG2 ARG A 205 20.351 23.487 17.913 1.00 24.85 H ANISOU 2771 HG2 ARG A 205 3592 3023 2825 187 -139 -123 H ATOM 2772 HG3 ARG A 205 19.940 23.212 16.403 1.00 21.64 H ANISOU 2772 HG3 ARG A 205 2499 2692 3031 279 -282 -174 H ATOM 2773 HD2 ARG A 205 18.160 22.679 17.700 1.00 25.14 H ANISOU 2773 HD2 ARG A 205 3118 3606 2826 -211 0 195 H ATOM 2774 HD3 ARG A 205 18.755 21.311 17.143 1.00 26.99 H ANISOU 2774 HD3 ARG A 205 3088 3370 3795 -237 -98 167 H ATOM 2775 HE ARG A 205 19.863 21.833 19.576 1.00 29.41 H ANISOU 2775 HE ARG A 205 4077 3934 3161 202 -238 177 H ATOM 2776 HH11 ARG A 205 16.725 21.039 18.424 1.00 32.23 H ANISOU 2776 HH11 ARG A 205 3762 4219 4262 -49 -81 169 H ATOM 2777 HH12 ARG A 205 16.272 20.389 19.678 1.00 34.06 H ANISOU 2777 HH12 ARG A 205 4315 4393 4232 -96 19 164 H ATOM 2778 HH21 ARG A 205 19.099 20.689 21.378 1.00 33.37 H ANISOU 2778 HH21 ARG A 205 4779 4463 3436 178 120 623 H ATOM 2779 HH22 ARG A 205 17.706 20.175 21.468 1.00 33.39 H ANISOU 2779 HH22 ARG A 205 4796 4357 3532 25 118 480 H ATOM 2780 N ARG A 206 25.084 22.331 16.964 1.00 16.81 N ANISOU 2780 N ARG A 206 2577 2483 1324 -208 -323 237 N ATOM 2781 CA ARG A 206 26.360 21.619 17.037 1.00 18.10 C ANISOU 2781 CA ARG A 206 2613 2344 1918 -117 -386 346 C ATOM 2782 C ARG A 206 26.512 20.609 15.892 1.00 17.51 C ANISOU 2782 C ARG A 206 2584 2301 1767 -260 -537 445 C ATOM 2783 O ARG A 206 26.863 19.461 16.070 1.00 19.75 O ANISOU 2783 O ARG A 206 2732 2325 2445 -162 -660 642 O ATOM 2784 CB ARG A 206 26.583 21.026 18.450 1.00 20.54 C ANISOU 2784 CB ARG A 206 2859 2840 2102 114 -626 482 C ATOM 2785 CG ARG A 206 26.769 22.126 19.506 1.00 22.17 C ANISOU 2785 CG ARG A 206 3146 3194 2083 104 -498 363 C ATOM 2786 CD ARG A 206 26.944 21.621 20.922 1.00 23.01 C ANISOU 2786 CD ARG A 206 3496 2986 2258 -131 -827 446 C ATOM 2787 NE ARG A 206 27.053 22.728 21.881 1.00 30.67 N ANISOU 2787 NE ARG A 206 5420 3329 2902 -495 -145 -107 N ATOM 2788 CZ ARG A 206 26.851 22.613 23.193 1.00 33.33 C ANISOU 2788 CZ ARG A 206 5786 3804 3071 -877 320 -307 C ATOM 2789 NH1 ARG A 206 26.523 21.444 23.741 1.00 31.71 N ANISOU 2789 NH1 ARG A 206 5503 3657 2888 28 -512 323 N ATOM 2790 NH2 ARG A 206 26.977 23.680 23.971 1.00 41.69 N ANISOU 2790 NH2 ARG A 206 7957 4188 3694 -551 -613 -868 N ATOM 2791 H ARG A 206 25.179 23.183 16.904 1.00 17.78 H ANISOU 2791 H ARG A 206 2421 2407 1925 -83 -216 60 H ATOM 2792 HA ARG A 206 27.068 22.284 16.907 1.00 18.68 H ANISOU 2792 HA ARG A 206 2558 2301 2239 -82 -214 106 H ATOM 2793 HB2 ARG A 206 25.829 20.473 18.704 1.00 19.38 H ANISOU 2793 HB2 ARG A 206 2767 2845 1751 325 -213 432 H ATOM 2794 HB3 ARG A 206 27.399 20.507 18.440 1.00 20.10 H ANISOU 2794 HB3 ARG A 206 2675 2869 2093 -10 -441 521 H ATOM 2795 HG2 ARG A 206 27.558 22.643 19.279 1.00 21.26 H ANISOU 2795 HG2 ARG A 206 3036 2838 2204 233 -337 104 H ATOM 2796 HG3 ARG A 206 25.988 22.702 19.495 1.00 20.62 H ANISOU 2796 HG3 ARG A 206 2981 2916 1938 -82 -386 382 H ATOM 2797 HD2 ARG A 206 26.161 21.102 21.143 1.00 23.18 H ANISOU 2797 HD2 ARG A 206 3389 3093 2322 107 -134 279 H ATOM 2798 HD3 ARG A 206 27.745 21.077 20.980 1.00 22.94 H ANISOU 2798 HD3 ARG A 206 3293 3332 2088 -91 -488 538 H ATOM 2799 HE ARG A 206 27.387 23.576 21.546 1.00 27.62 H ANISOU 2799 HE ARG A 206 4168 3194 3129 -149 -102 -142 H ATOM 2800 HH11 ARG A 206 26.440 20.746 23.258 1.00 29.78 H ANISOU 2800 HH11 ARG A 206 4242 3672 3399 -209 31 104 H ATOM 2801 HH12 ARG A 206 26.398 21.387 24.590 1.00 31.28 H ANISOU 2801 HH12 ARG A 206 4511 4126 3245 -31 386 137 H ATOM 2802 HH21 ARG A 206 27.187 24.442 23.631 1.00 34.28 H ANISOU 2802 HH21 ARG A 206 5201 3990 3834 -58 -161 -924 H ATOM 2803 HH22 ARG A 206 26.848 23.614 24.819 1.00 34.33 H ANISOU 2803 HH22 ARG A 206 5353 3763 3926 37 -23 -878 H ATOM 2804 N ASN A 207 26.253 21.096 14.677 1.00 15.54 N ANISOU 2804 N ASN A 207 2329 1968 1605 -169 -457 256 N ATOM 2805 CA ASN A 207 26.480 20.337 13.454 1.00 15.98 C ANISOU 2805 CA ASN A 207 2087 2207 1778 -178 -530 -29 C ATOM 2806 C ASN A 207 25.682 19.036 13.441 1.00 15.93 C ANISOU 2806 C ASN A 207 2168 2143 1742 -121 -573 59 C ATOM 2807 O ASN A 207 26.208 17.951 13.188 1.00 15.48 O ANISOU 2807 O ASN A 207 2239 2153 1487 -112 -748 126 O ATOM 2808 CB ASN A 207 27.979 20.093 13.253 1.00 15.32 C ANISOU 2808 CB ASN A 207 2084 2030 1706 -109 -761 50 C ATOM 2809 CG ASN A 207 28.299 19.533 11.890 1.00 16.53 C ANISOU 2809 CG ASN A 207 2237 2321 1720 -517 -594 12 C ATOM 2810 OD1 ASN A 207 27.524 19.683 10.950 1.00 16.53 O ANISOU 2810 OD1 ASN A 207 2353 2626 1301 -463 -377 169 O ATOM 2811 ND2 ASN A 207 29.457 18.879 11.772 1.00 16.76 N ANISOU 2811 ND2 ASN A 207 2539 2530 1299 -234 -110 -48 N ATOM 2812 H ASN A 207 25.939 21.883 14.532 1.00 15.65 H ANISOU 2812 H ASN A 207 2279 2010 1654 -66 -291 223 H ATOM 2813 HA ASN A 207 26.164 20.881 12.702 1.00 14.54 H ANISOU 2813 HA ASN A 207 1843 2002 1679 -8 -279 -132 H ATOM 2814 HB2 ASN A 207 28.451 20.935 13.348 1.00 15.23 H ANISOU 2814 HB2 ASN A 207 2063 1887 1836 -40 -308 87 H ATOM 2815 HB3 ASN A 207 28.295 19.460 13.916 1.00 15.59 H ANISOU 2815 HB3 ASN A 207 2292 1892 1737 42 -368 130 H ATOM 2816 N HIS A 208 24.384 19.195 13.664 1.00 15.62 N ANISOU 2816 N HIS A 208 2247 1977 1709 -133 -486 228 N ATOM 2817 CA HIS A 208 23.471 18.071 13.749 1.00 15.35 C ANISOU 2817 CA HIS A 208 2264 1844 1723 -32 -243 368 C ATOM 2818 C HIS A 208 23.449 17.256 12.455 1.00 14.99 C ANISOU 2818 C HIS A 208 2069 1912 1714 -128 -201 383 C ATOM 2819 O HIS A 208 23.297 17.806 11.396 1.00 15.25 O ANISOU 2819 O HIS A 208 2238 1780 1776 -80 -495 395 O ATOM 2820 CB HIS A 208 22.094 18.588 14.123 1.00 17.93 C ANISOU 2820 CB HIS A 208 2514 1952 2345 262 -92 257 C ATOM 2821 CG HIS A 208 21.182 17.520 14.596 1.00 21.53 C ANISOU 2821 CG HIS A 208 2832 2480 2869 159 -17 523 C ATOM 2822 ND1 HIS A 208 21.397 16.832 15.777 1.00 23.68 N ANISOU 2822 ND1 HIS A 208 3084 2666 3244 -51 -137 883 N ATOM 2823 CD2 HIS A 208 20.073 16.998 14.039 1.00 23.83 C ANISOU 2823 CD2 HIS A 208 2946 2605 3501 114 53 275 C ATOM 2824 CE1 HIS A 208 20.436 15.939 15.926 1.00 23.48 C ANISOU 2824 CE1 HIS A 208 3268 2888 2764 -427 -374 297 C ATOM 2825 NE2 HIS A 208 19.625 16.018 14.878 1.00 21.07 N ANISOU 2825 NE2 HIS A 208 3298 2161 2544 423 -275 141 N ATOM 2826 H HIS A 208 24.008 19.962 13.763 1.00 15.85 H ANISOU 2826 H HIS A 208 2223 1953 1846 -190 -263 159 H ATOM 2827 HA HIS A 208 23.773 17.485 14.474 1.00 15.70 H ANISOU 2827 HA HIS A 208 2397 1867 1700 112 -256 280 H ATOM 2828 HB2 HIS A 208 22.180 19.237 14.839 1.00 19.01 H ANISOU 2828 HB2 HIS A 208 2517 2583 2123 224 -96 91 H ATOM 2829 HB3 HIS A 208 21.690 19.004 13.345 1.00 17.44 H ANISOU 2829 HB3 HIS A 208 2219 2225 2182 151 -141 102 H ATOM 2830 HD2 HIS A 208 19.686 17.256 13.233 1.00 19.26 H ANISOU 2830 HD2 HIS A 208 2562 1726 3028 -428 341 146 H ATOM 2831 HE1 HIS A 208 20.350 15.358 16.644 1.00 18.95 H ANISOU 2831 HE1 HIS A 208 2117 2512 2569 -161 -326 73 H ATOM 2832 N CYS A 209 23.639 15.950 12.584 1.00 14.43 N ANISOU 2832 N CYS A 209 1922 1878 1682 -55 -358 395 N ATOM 2833 CA CYS A 209 23.687 14.994 11.485 1.00 14.94 C ANISOU 2833 CA CYS A 209 2045 1883 1748 -44 -257 313 C ATOM 2834 C CYS A 209 24.818 15.233 10.499 1.00 13.64 C ANISOU 2834 C CYS A 209 1959 1731 1492 -83 -436 484 C ATOM 2835 O CYS A 209 24.817 14.702 9.387 1.00 14.77 O ANISOU 2835 O CYS A 209 2271 1994 1345 -280 -348 550 O ATOM 2836 CB CYS A 209 22.335 14.923 10.756 1.00 16.25 C ANISOU 2836 CB CYS A 209 2115 1966 2092 -207 -425 205 C ATOM 2837 SG CYS A 209 20.930 14.399 11.791 1.00 17.08 S ANISOU 2837 SG CYS A 209 2102 1960 2428 -94 -359 350 S ATOM 2838 H CYS A 209 23.750 15.568 13.347 1.00 14.76 H ANISOU 2838 H CYS A 209 2048 1929 1630 -7 -174 377 H ATOM 2839 HA CYS A 209 23.842 14.109 11.873 1.00 14.81 H ANISOU 2839 HA CYS A 209 1985 1860 1781 -119 -65 353 H ATOM 2840 HB2 CYS A 209 22.123 15.795 10.389 1.00 15.21 H ANISOU 2840 HB2 CYS A 209 1857 1993 1927 37 -251 86 H ATOM 2841 HB3 CYS A 209 22.407 14.280 10.034 1.00 16.29 H ANISOU 2841 HB3 CYS A 209 2126 1868 2195 -110 -425 182 H ATOM 2842 N GLY A 210 25.806 16.041 10.914 1.00 14.92 N ANISOU 2842 N GLY A 210 2190 1986 1493 -239 -453 359 N ATOM 2843 CA GLY A 210 26.999 16.258 10.083 1.00 14.68 C ANISOU 2843 CA GLY A 210 2326 1817 1433 -227 -362 387 C ATOM 2844 C GLY A 210 26.838 17.156 8.874 1.00 12.89 C ANISOU 2844 C GLY A 210 2016 1873 1008 -73 -278 117 C ATOM 2845 O GLY A 210 27.642 17.089 7.950 1.00 13.92 O ANISOU 2845 O GLY A 210 1836 1969 1484 -95 -127 296 O ATOM 2846 H GLY A 210 25.828 16.462 11.661 1.00 14.97 H ANISOU 2846 H GLY A 210 2068 1819 1799 -95 -259 121 H ATOM 2847 HA2 GLY A 210 27.323 15.399 9.770 1.00 15.25 H ANISOU 2847 HA2 GLY A 210 2261 1819 1714 -212 -350 313 H ATOM 2848 HA3 GLY A 210 27.692 16.645 10.640 1.00 13.29 H ANISOU 2848 HA3 GLY A 210 1956 1809 1284 174 -325 321 H ATOM 2849 N ILE A 211 25.788 17.987 8.894 1.00 13.66 N ANISOU 2849 N ILE A 211 2024 1967 1198 -108 -241 285 N ATOM 2850 CA ILE A 211 25.451 18.789 7.740 1.00 13.32 C ANISOU 2850 CA ILE A 211 1960 2154 947 -220 -230 187 C ATOM 2851 C ILE A 211 26.575 19.750 7.253 1.00 14.23 C ANISOU 2851 C ILE A 211 1733 2092 1579 -120 -412 397 C ATOM 2852 O ILE A 211 26.657 20.044 6.055 1.00 14.33 O ANISOU 2852 O ILE A 211 2012 1827 1602 -148 -377 397 O ATOM 2853 CB ILE A 211 24.113 19.500 7.956 1.00 15.26 C ANISOU 2853 CB ILE A 211 1932 2229 1636 -120 -390 282 C ATOM 2854 CG1 ILE A 211 23.570 20.005 6.600 1.00 15.38 C ANISOU 2854 CG1 ILE A 211 2116 2260 1467 -167 -268 277 C ATOM 2855 CG2 ILE A 211 24.206 20.573 9.024 1.00 16.79 C ANISOU 2855 CG2 ILE A 211 2398 2306 1672 241 -445 184 C ATOM 2856 CD1 ILE A 211 22.079 20.266 6.604 1.00 14.40 C ANISOU 2856 CD1 ILE A 211 2173 2624 673 -26 -498 -12 C ATOM 2857 H ILE A 211 25.268 18.090 9.570 1.00 13.12 H ANISOU 2857 H ILE A 211 1950 1704 1330 -85 -121 534 H ATOM 2858 HA ILE A 211 25.308 18.160 7.002 1.00 14.36 H ANISOU 2858 HA ILE A 211 2171 1952 1331 -153 -562 124 H ATOM 2859 HB ILE A 211 23.491 18.831 8.283 1.00 15.14 H ANISOU 2859 HB ILE A 211 1960 2167 1625 71 -144 362 H ATOM 2860 HG12 ILE A 211 24.016 20.833 6.362 1.00 15.10 H ANISOU 2860 HG12 ILE A 211 2186 1931 1619 55 -264 158 H ATOM 2861 HG13 ILE A 211 23.743 19.335 5.922 1.00 14.84 H ANISOU 2861 HG13 ILE A 211 1942 2039 1656 -225 -385 222 H ATOM 2862 N ALA A 212 27.466 20.129 8.180 1.00 14.52 N ANISOU 2862 N ALA A 212 2000 2092 1423 -170 -531 621 N ATOM 2863 CA ALA A 212 28.613 20.957 7.803 1.00 14.39 C ANISOU 2863 CA ALA A 212 1921 1919 1625 -145 -326 354 C ATOM 2864 C ALA A 212 29.923 20.195 7.709 1.00 14.42 C ANISOU 2864 C ALA A 212 1949 2027 1501 -139 -446 407 C ATOM 2865 O ALA A 212 30.975 20.803 7.508 1.00 16.52 O ANISOU 2865 O ALA A 212 1952 2234 2091 -333 -428 305 O ATOM 2866 CB ALA A 212 28.760 22.131 8.774 1.00 16.66 C ANISOU 2866 CB ALA A 212 2312 2017 2001 -83 -332 114 C ATOM 2867 H ALA A 212 27.428 19.926 9.015 1.00 13.99 H ANISOU 2867 H ALA A 212 2016 1921 1379 6 -300 416 H ATOM 2868 HA ALA A 212 28.452 21.349 6.920 1.00 14.14 H ANISOU 2868 HA ALA A 212 1902 1826 1642 19 -121 389 H ATOM 2869 N SER A 213 29.882 18.868 7.833 1.00 14.71 N ANISOU 2869 N SER A 213 1722 2066 1800 -120 -393 399 N ATOM 2870 CA SER A 213 31.108 18.073 7.817 1.00 13.99 C ANISOU 2870 CA SER A 213 1945 2083 1287 45 -650 453 C ATOM 2871 C SER A 213 31.741 17.814 6.452 1.00 14.94 C ANISOU 2871 C SER A 213 2027 2229 1419 -325 -403 398 C ATOM 2872 O SER A 213 32.938 17.548 6.411 1.00 17.14 O ANISOU 2872 O SER A 213 1922 2622 1966 -55 -492 567 O ATOM 2873 CB SER A 213 30.864 16.747 8.536 1.00 15.73 C ANISOU 2873 CB SER A 213 1888 2239 1848 11 -445 715 C ATOM 2874 OG SER A 213 30.534 16.942 9.904 1.00 17.20 O ANISOU 2874 OG SER A 213 2172 2520 1842 -30 -387 745 O ATOM 2875 H SER A 213 29.164 18.406 7.919 1.00 14.29 H ANISOU 2875 H SER A 213 1841 1983 1605 -146 -266 265 H ATOM 2876 HA SER A 213 31.782 18.547 8.348 1.00 14.57 H ANISOU 2876 HA SER A 213 1696 2159 1678 -27 -346 95 H ATOM 2877 HB2 SER A 213 30.128 16.290 8.103 1.00 16.07 H ANISOU 2877 HB2 SER A 213 1881 2114 2110 9 -198 287 H ATOM 2878 HB3 SER A 213 31.667 16.205 8.482 1.00 16.02 H ANISOU 2878 HB3 SER A 213 1983 1811 2291 -69 -420 405 H ATOM 2879 N ALA A 214 30.986 17.878 5.355 1.00 14.45 N ANISOU 2879 N ALA A 214 1819 2136 1533 -80 -411 421 N ATOM 2880 CA ALA A 214 31.515 17.640 4.017 1.00 14.58 C ANISOU 2880 CA ALA A 214 1773 2183 1584 -158 -394 360 C ATOM 2881 C ALA A 214 30.667 18.386 3.002 1.00 14.90 C ANISOU 2881 C ALA A 214 2063 2028 1570 -153 -366 481 C ATOM 2882 O ALA A 214 30.025 17.795 2.138 1.00 16.13 O ANISOU 2882 O ALA A 214 2144 2283 1698 -215 -468 426 O ATOM 2883 CB ALA A 214 31.593 16.152 3.728 1.00 15.85 C ANISOU 2883 CB ALA A 214 2296 2139 1588 14 -214 400 C ATOM 2884 H ALA A 214 30.145 18.056 5.365 1.00 14.93 H ANISOU 2884 H ALA A 214 1806 2098 1768 -94 -315 265 H ATOM 2885 HA ALA A 214 32.424 18.003 3.959 1.00 15.90 H ANISOU 2885 HA ALA A 214 1708 2306 2026 -61 -196 293 H ATOM 2886 N ALA A 215 30.703 19.710 3.135 1.00 14.36 N ANISOU 2886 N ALA A 215 1896 2119 1438 -241 -544 499 N ATOM 2887 CA ALA A 215 29.927 20.599 2.285 1.00 13.55 C ANISOU 2887 CA ALA A 215 1909 2028 1210 -165 -462 338 C ATOM 2888 C ALA A 215 30.812 21.168 1.198 1.00 14.26 C ANISOU 2888 C ALA A 215 1845 2023 1549 -294 -373 467 C ATOM 2889 O ALA A 215 31.997 21.482 1.439 1.00 15.48 O ANISOU 2889 O ALA A 215 1819 2439 1622 -332 -544 583 O ATOM 2890 CB ALA A 215 29.375 21.714 3.127 1.00 14.34 C ANISOU 2890 CB ALA A 215 2028 2313 1104 -197 -386 92 C ATOM 2891 H ALA A 215 31.189 20.117 3.718 1.00 12.93 H ANISOU 2891 H ALA A 215 1431 2100 1380 33 -305 273 H ATOM 2892 HA ALA A 215 29.181 20.114 1.880 1.00 12.47 H ANISOU 2892 HA ALA A 215 1550 1822 1363 5 -266 280 H ATOM 2893 N SER A 216 30.279 21.315 -0.005 1.00 14.15 N ANISOU 2893 N SER A 216 1713 2016 1647 -104 -424 678 N ATOM 2894 CA SER A 216 31.081 21.767 -1.120 1.00 13.95 C ANISOU 2894 CA SER A 216 1877 1942 1480 -135 -464 574 C ATOM 2895 C SER A 216 30.210 22.254 -2.259 1.00 13.35 C ANISOU 2895 C SER A 216 1700 2279 1091 -202 -216 513 C ATOM 2896 O SER A 216 28.985 22.041 -2.279 1.00 13.83 O ANISOU 2896 O SER A 216 1652 2057 1546 -218 -355 370 O ATOM 2897 CB SER A 216 31.991 20.639 -1.596 1.00 14.77 C ANISOU 2897 CB SER A 216 1773 2209 1630 -190 -259 493 C ATOM 2898 OG SER A 216 31.235 19.615 -2.193 1.00 15.57 O ANISOU 2898 OG SER A 216 1989 2019 1908 -145 -401 435 O ATOM 2899 H SER A 216 29.455 21.158 -0.196 1.00 14.07 H ANISOU 2899 H SER A 216 1682 2050 1614 -28 -324 232 H ATOM 2900 HA SER A 216 31.639 22.517 -0.831 1.00 13.98 H ANISOU 2900 HA SER A 216 1600 2131 1578 -162 -398 500 H ATOM 2901 HB2 SER A 216 32.609 20.989 -2.256 1.00 15.53 H ANISOU 2901 HB2 SER A 216 1971 2186 1741 -229 -145 481 H ATOM 2902 HB3 SER A 216 32.483 20.274 -0.845 1.00 14.24 H ANISOU 2902 HB3 SER A 216 1779 2058 1574 29 -185 317 H ATOM 2903 N TYR A 217 30.831 22.926 -3.212 1.00 13.67 N ANISOU 2903 N TYR A 217 1711 2207 1274 -194 -215 616 N ATOM 2904 CA TYR A 217 30.150 23.422 -4.411 1.00 12.65 C ANISOU 2904 CA TYR A 217 1840 1953 1012 -232 -105 479 C ATOM 2905 C TYR A 217 31.101 23.516 -5.593 1.00 13.42 C ANISOU 2905 C TYR A 217 1853 2069 1176 -461 -17 568 C ATOM 2906 O TYR A 217 32.307 23.675 -5.397 1.00 14.69 O ANISOU 2906 O TYR A 217 1691 2063 1827 -350 -237 427 O ATOM 2907 CB TYR A 217 29.468 24.767 -4.126 1.00 14.39 C ANISOU 2907 CB TYR A 217 1813 2035 1617 -75 -258 403 C ATOM 2908 CG TYR A 217 30.400 25.910 -3.771 1.00 15.99 C ANISOU 2908 CG TYR A 217 2008 2108 1958 -168 -418 441 C ATOM 2909 CD1 TYR A 217 30.722 26.158 -2.456 1.00 17.39 C ANISOU 2909 CD1 TYR A 217 2045 2505 2056 -299 -221 64 C ATOM 2910 CD2 TYR A 217 30.915 26.758 -4.743 1.00 17.40 C ANISOU 2910 CD2 TYR A 217 2452 1971 2187 -206 -286 466 C ATOM 2911 CE1 TYR A 217 31.540 27.207 -2.098 1.00 19.78 C ANISOU 2911 CE1 TYR A 217 2577 2573 2365 -356 -292 -350 C ATOM 2912 CE2 TYR A 217 31.751 27.826 -4.388 1.00 19.32 C ANISOU 2912 CE2 TYR A 217 2307 2169 2863 -322 0 195 C ATOM 2913 CZ TYR A 217 32.058 28.042 -3.053 1.00 20.83 C ANISOU 2913 CZ TYR A 217 2536 2282 3096 -447 -198 -85 C ATOM 2914 OH TYR A 217 32.891 29.082 -2.672 1.00 24.59 O ANISOU 2914 OH TYR A 217 2827 2589 3925 -620 -213 -550 O ATOM 2915 H TYR A 217 31.670 23.117 -3.190 1.00 13.01 H ANISOU 2915 H TYR A 217 1628 1956 1358 -58 -90 385 H ATOM 2916 HA TYR A 217 29.447 22.783 -4.648 1.00 12.41 H ANISOU 2916 HA TYR A 217 1427 2014 1274 -83 -65 468 H ATOM 2917 HB2 TYR A 217 28.968 25.035 -4.911 1.00 14.52 H ANISOU 2917 HB2 TYR A 217 1716 2215 1586 67 -214 249 H ATOM 2918 HB3 TYR A 217 28.857 24.648 -3.381 1.00 14.88 H ANISOU 2918 HB3 TYR A 217 1952 2038 1663 -44 -133 289 H ATOM 2919 HD1 TYR A 217 30.375 25.607 -1.792 1.00 16.79 H ANISOU 2919 HD1 TYR A 217 2174 2340 1863 78 -233 108 H ATOM 2920 HD2 TYR A 217 30.703 26.616 -5.635 1.00 16.88 H ANISOU 2920 HD2 TYR A 217 2235 2106 2071 -62 -32 437 H ATOM 2921 HE1 TYR A 217 31.748 27.345 -1.203 1.00 20.20 H ANISOU 2921 HE1 TYR A 217 2452 2786 2435 -52 -308 -550 H ATOM 2922 HE2 TYR A 217 32.100 28.385 -5.044 1.00 19.12 H ANISOU 2922 HE2 TYR A 217 2166 2066 3031 -210 180 132 H ATOM 2923 N PRO A 218 30.602 23.470 -6.836 1.00 13.62 N ANISOU 2923 N PRO A 218 1810 2060 1303 -15 -164 323 N ATOM 2924 CA PRO A 218 31.436 23.572 -8.025 1.00 14.09 C ANISOU 2924 CA PRO A 218 2039 1993 1320 -237 -143 409 C ATOM 2925 C PRO A 218 31.720 25.025 -8.324 1.00 15.12 C ANISOU 2925 C PRO A 218 1981 2077 1686 -164 -352 677 C ATOM 2926 O PRO A 218 30.871 25.895 -8.052 1.00 15.67 O ANISOU 2926 O PRO A 218 2019 1965 1968 -345 -166 371 O ATOM 2927 CB PRO A 218 30.574 22.940 -9.109 1.00 14.12 C ANISOU 2927 CB PRO A 218 2033 1991 1339 -68 -285 363 C ATOM 2928 CG PRO A 218 29.147 23.234 -8.663 1.00 14.49 C ANISOU 2928 CG PRO A 218 1949 1885 1669 -173 -370 584 C ATOM 2929 CD PRO A 218 29.177 23.236 -7.192 1.00 14.44 C ANISOU 2929 CD PRO A 218 1855 2004 1626 -176 -325 262 C ATOM 2930 HA PRO A 218 32.269 23.067 -7.920 1.00 13.24 H ANISOU 2930 HA PRO A 218 1857 1825 1347 -339 -81 228 H ATOM 2931 HB2 PRO A 218 30.760 23.351 -9.968 1.00 14.44 H ANISOU 2931 HB2 PRO A 218 2213 1853 1419 -253 -244 334 H ATOM 2932 HB3 PRO A 218 30.736 21.984 -9.142 1.00 14.49 H ANISOU 2932 HB3 PRO A 218 2100 1907 1498 -203 -176 376 H ATOM 2933 HG2 PRO A 218 28.874 24.102 -8.999 1.00 14.61 H ANISOU 2933 HG2 PRO A 218 2240 1662 1647 -3 -189 235 H ATOM 2934 HG3 PRO A 218 28.555 22.540 -8.991 1.00 13.71 H ANISOU 2934 HG3 PRO A 218 1992 1667 1549 55 -194 220 H ATOM 2935 HD2 PRO A 218 28.622 23.954 -6.854 1.00 14.44 H ANISOU 2935 HD2 PRO A 218 1735 1848 1903 -221 -264 354 H ATOM 2936 HD3 PRO A 218 28.883 22.377 -6.855 1.00 13.39 H ANISOU 2936 HD3 PRO A 218 1824 1902 1359 11 -164 204 H ATOM 2937 N THR A 219 32.917 25.281 -8.827 1.00 17.46 N ANISOU 2937 N THR A 219 2008 1978 2645 -332 -143 424 N ATOM 2938 CA THR A 219 33.260 26.596 -9.325 1.00 17.80 C ANISOU 2938 CA THR A 219 2423 2143 2195 -403 89 466 C ATOM 2939 C THR A 219 32.975 26.559 -10.822 1.00 17.79 C ANISOU 2939 C THR A 219 2260 2177 2323 -322 -211 283 C ATOM 2940 O THR A 219 33.136 25.526 -11.485 1.00 19.06 O ANISOU 2940 O THR A 219 2285 2432 2524 -90 -95 183 O ATOM 2941 CB THR A 219 34.726 26.963 -9.002 1.00 19.29 C ANISOU 2941 CB THR A 219 2468 2732 2128 -888 423 502 C ATOM 2942 OG1 THR A 219 35.605 25.983 -9.564 1.00 22.38 O ANISOU 2942 OG1 THR A 219 2367 2849 3284 -631 -45 85 O ATOM 2943 CG2 THR A 219 34.942 27.060 -7.496 1.00 21.46 C ANISOU 2943 CG2 THR A 219 2816 3000 2336 -997 57 106 C ATOM 2944 H THR A 219 33.551 24.704 -8.895 1.00 16.46 H ANISOU 2944 H THR A 219 2137 2127 1988 -217 -77 249 H ATOM 2945 HA THR A 219 32.682 27.275 -8.920 1.00 18.34 H ANISOU 2945 HA THR A 219 2606 1993 2368 -319 -112 323 H ATOM 2946 HB THR A 219 34.928 27.828 -9.391 1.00 20.72 H ANISOU 2946 HB THR A 219 2728 2460 2684 -741 79 469 H ATOM 2947 N VAL A 220 32.524 27.687 -11.355 1.00 21.78 N ANISOU 2947 N VAL A 220 3373 2321 2580 91 -158 368 N ATOM 2948 CA VAL A 220 32.107 27.766 -12.759 1.00 20.91 C ANISOU 2948 CA VAL A 220 2936 2381 2624 16 -121 592 C ATOM 2949 C VAL A 220 32.717 28.978 -13.454 1.00 25.07 C ANISOU 2949 C VAL A 220 3233 2913 3378 -260 319 879 C ATOM 2950 O VAL A 220 32.747 29.039 -14.676 1.00 32.54 O ANISOU 2950 O VAL A 220 5262 3702 3398 -378 -64 1398 O ATOM 2951 CB VAL A 220 30.558 27.774 -12.911 1.00 22.76 C ANISOU 2951 CB VAL A 220 2876 3048 2720 30 232 561 C ATOM 2952 CG1 VAL A 220 29.974 26.425 -12.478 1.00 22.08 C ANISOU 2952 CG1 VAL A 220 2890 2791 2707 106 -56 465 C ATOM 2953 CG2 VAL A 220 29.909 28.939 -12.133 1.00 24.99 C ANISOU 2953 CG2 VAL A 220 3173 2883 3436 292 117 545 C ATOM 2954 OXT VAL A 220 33.198 29.897 -12.792 1.00 28.46 O ANISOU 2954 OXT VAL A 220 4376 2989 3447 -534 480 805 O ATOM 2955 H VAL A 220 32.461 28.430 -10.927 1.00 20.84 H ANISOU 2955 H VAL A 220 2744 2352 2819 20 -3 259 H ATOM 2956 HA VAL A 220 32.442 26.981 -13.241 1.00 21.63 H ANISOU 2956 HA VAL A 220 2771 2764 2682 -132 -35 185 H ATOM 2957 HB VAL A 220 30.341 27.897 -13.858 1.00 22.76 H ANISOU 2957 HB VAL A 220 2799 2925 2921 -161 -137 568 H TER 2958 VAL A 220 HETATM 2959 C1 DJT A1221 26.920 8.773 0.217 1.00 12.95 C ANISOU 2959 C1 DJT A1221 1848 1748 1323 185 -170 196 C HETATM 2960 C2 DJT A1221 26.200 7.860 -0.752 1.00 12.53 C ANISOU 2960 C2 DJT A1221 1706 1797 1257 248 -258 257 C HETATM 2961 CL2 DJT A1221 30.219 13.683 0.129 1.00 20.30 CL ANISOU 2961 CL2 DJT A1221 2611 2423 2678 6 -258 577 CL HETATM 2962 N3 DJT A1221 24.990 7.456 -0.267 1.00 14.63 N ANISOU 2962 N3 DJT A1221 1912 1842 1806 82 -31 244 N HETATM 2963 C4 DJT A1221 24.051 6.690 -1.066 1.00 13.90 C ANISOU 2963 C4 DJT A1221 1761 2033 1486 -52 132 414 C HETATM 2964 C5 DJT A1221 23.078 7.547 -1.806 1.00 14.18 C ANISOU 2964 C5 DJT A1221 2168 1748 1472 -67 -186 194 C HETATM 2965 O6 DJT A1221 26.607 7.589 -1.894 1.00 14.81 O ANISOU 2965 O6 DJT A1221 2184 2044 1398 -228 -42 197 O HETATM 2966 C7 DJT A1221 24.507 5.375 -1.655 1.00 15.67 C ANISOU 2966 C7 DJT A1221 1913 1955 2084 -37 -146 183 C HETATM 2967 C8 DJT A1221 23.558 5.388 -0.467 1.00 15.28 C ANISOU 2967 C8 DJT A1221 2080 1838 1886 -40 -132 523 C HETATM 2968 N9 DJT A1221 22.063 7.096 -2.430 1.00 14.23 N ANISOU 2968 N9 DJT A1221 1967 2021 1416 -59 -160 383 N HETATM 2969 N10 DJT A1221 28.243 8.298 0.626 1.00 13.84 N ANISOU 2969 N10 DJT A1221 1733 1797 1727 25 -253 496 N HETATM 2970 C11 DJT A1221 29.316 9.227 0.216 1.00 13.40 C ANISOU 2970 C11 DJT A1221 1742 1891 1456 147 -43 477 C HETATM 2971 C12 DJT A1221 28.555 10.571 0.027 1.00 14.06 C ANISOU 2971 C12 DJT A1221 2083 1777 1479 75 -351 446 C HETATM 2972 C13 DJT A1221 27.178 10.106 -0.494 1.00 13.71 C ANISOU 2972 C13 DJT A1221 1869 1857 1481 162 -62 386 C HETATM 2973 S14 DJT A1221 28.255 11.491 1.557 1.00 14.67 S ANISOU 2973 S14 DJT A1221 1930 1881 1763 93 -282 324 S HETATM 2974 C15 DJT A1221 29.872 11.920 2.177 1.00 15.24 C ANISOU 2974 C15 DJT A1221 2057 2097 1634 -31 -365 94 C HETATM 2975 C16 DJT A1221 30.683 12.844 1.541 1.00 17.12 C ANISOU 2975 C16 DJT A1221 2193 2290 2019 -25 -129 244 C HETATM 2976 C17 DJT A1221 31.937 13.148 2.029 1.00 19.49 C ANISOU 2976 C17 DJT A1221 2245 2593 2567 -242 -266 303 C HETATM 2977 C18 DJT A1221 32.374 12.533 3.165 1.00 19.05 C ANISOU 2977 C18 DJT A1221 1919 3099 2218 138 -201 -6 C HETATM 2978 C19 DJT A1221 31.585 11.625 3.821 1.00 19.05 C ANISOU 2978 C19 DJT A1221 2081 2612 2544 193 -665 311 C HETATM 2979 C20 DJT A1221 30.342 11.308 3.331 1.00 16.60 C ANISOU 2979 C20 DJT A1221 2170 2401 1733 62 -474 159 C HETATM 2980 O22 DJT A1221 27.539 12.703 1.160 1.00 15.39 O ANISOU 2980 O22 DJT A1221 2089 1973 1785 168 -469 225 O HETATM 2981 O23 DJT A1221 27.684 10.638 2.552 1.00 15.82 O ANISOU 2981 O23 DJT A1221 2145 2358 1508 25 -311 415 O HETATM 2982 C24 DJT A1221 28.360 7.223 1.411 1.00 14.41 C ANISOU 2982 C24 DJT A1221 2028 1849 1597 163 -32 522 C HETATM 2983 O25 DJT A1221 27.335 6.626 1.758 1.00 15.79 O ANISOU 2983 O25 DJT A1221 1986 1993 2020 63 -206 581 O HETATM 2984 C26 DJT A1221 30.266 7.498 3.130 1.00 16.42 C ANISOU 2984 C26 DJT A1221 2115 2101 2023 84 -244 385 C HETATM 2985 C27 DJT A1221 29.741 6.845 1.849 1.00 15.30 C ANISOU 2985 C27 DJT A1221 2101 1924 1785 217 -109 532 C HETATM 2986 C28 DJT A1221 29.865 6.022 3.121 1.00 15.90 C ANISOU 2986 C28 DJT A1221 2239 2055 1746 202 -180 516 C HETATM 2987 C29 DJT A1221 31.165 5.428 -1.399 1.00 20.81 C ANISOU 2987 C29 DJT A1221 3052 2604 2249 887 102 424 C HETATM 2988 C30 DJT A1221 32.432 5.951 -1.356 1.00 23.31 C ANISOU 2988 C30 DJT A1221 3079 2836 2942 744 531 430 C HETATM 2989 C31 DJT A1221 32.829 6.743 -0.301 1.00 25.41 C ANISOU 2989 C31 DJT A1221 3001 3298 3355 -114 806 330 C HETATM 2990 C32 DJT A1221 31.956 7.033 0.714 1.00 20.58 C ANISOU 2990 C32 DJT A1221 2517 2555 2745 63 222 313 C HETATM 2991 C33 DJT A1221 30.673 6.525 0.695 1.00 16.58 C ANISOU 2991 C33 DJT A1221 2306 1916 2076 524 5 481 C HETATM 2992 C34 DJT A1221 30.285 5.705 -0.350 1.00 19.95 C ANISOU 2992 C34 DJT A1221 2705 2641 2232 841 -165 30 C HETATM 2993 F35 DJT A1221 33.319 5.674 -2.347 1.00 31.69 F ANISOU 2993 F35 DJT A1221 4024 4459 3555 963 1346 500 F HETATM 2994 H1 DJT A1221 26.314 8.951 1.101 1.00 12.99 H ANISOU 2994 H1 DJT A1221 1834 1606 1496 -73 -25 130 H HETATM 2995 HN3 DJT A1221 24.700 7.762 0.597 1.00 14.27 H ANISOU 2995 HN3 DJT A1221 1776 1817 1826 37 7 246 H HETATM 2996 H7 DJT A1221 24.096 5.087 -2.623 1.00 14.94 H ANISOU 2996 H7 DJT A1221 1837 1863 1973 0 -62 248 H HETATM 2997 H7A DJT A1221 25.537 5.068 -1.472 1.00 15.34 H ANISOU 2997 H7A DJT A1221 1944 1840 2043 -29 -168 219 H HETATM 2998 H8 DJT A1221 22.519 5.114 -0.646 1.00 14.12 H ANISOU 2998 H8 DJT A1221 2036 1577 1751 13 -73 339 H HETATM 2999 H8A DJT A1221 23.968 5.085 0.494 1.00 14.09 H ANISOU 2999 H8A DJT A1221 2109 1363 1882 144 -191 258 H HETATM 3000 H11 DJT A1221 29.785 8.892 -0.706 1.00 14.85 H ANISOU 3000 H11 DJT A1221 1963 2083 1594 -11 -17 144 H HETATM 3001 H11A DJT A1221 30.059 9.320 1.007 1.00 12.85 H ANISOU 3001 H11A DJT A1221 1646 1655 1580 135 -44 252 H HETATM 3002 H12 DJT A1221 29.056 11.202 -0.707 1.00 14.17 H ANISOU 3002 H12 DJT A1221 2019 1629 1736 11 -174 308 H HETATM 3003 H13 DJT A1221 26.410 10.830 -0.221 1.00 13.26 H ANISOU 3003 H13 DJT A1221 1912 1583 1541 -45 -1 167 H HETATM 3004 H13A DJT A1221 27.204 9.972 -1.574 1.00 12.70 H ANISOU 3004 H13A DJT A1221 1731 1570 1524 18 -74 212 H HETATM 3005 H17 DJT A1221 32.555 13.881 1.531 1.00 18.56 H ANISOU 3005 H17 DJT A1221 2185 2276 2590 -55 139 -98 H HETATM 3006 H18 DJT A1221 33.349 12.775 3.560 1.00 19.44 H ANISOU 3006 H18 DJT A1221 2047 3015 2322 29 -194 -316 H HETATM 3007 H19 DJT A1221 31.957 11.139 4.709 1.00 17.05 H ANISOU 3007 H19 DJT A1221 1803 2647 2025 447 -368 -96 H HETATM 3008 H20 DJT A1221 29.731 10.578 3.841 1.00 16.32 H ANISOU 3008 H20 DJT A1221 2223 2196 1780 184 -462 223 H HETATM 3009 H26 DJT A1221 31.329 7.715 3.218 1.00 17.29 H ANISOU 3009 H26 DJT A1221 2077 2333 2156 97 -116 258 H HETATM 3010 H26A DJT A1221 29.604 8.201 3.632 1.00 16.25 H ANISOU 3010 H26A DJT A1221 1988 2103 2082 -103 -158 241 H HETATM 3011 H28 DJT A1221 28.944 5.750 3.637 1.00 14.72 H ANISOU 3011 H28 DJT A1221 2129 1874 1589 237 -248 408 H HETATM 3012 H28A DJT A1221 30.667 5.292 3.178 1.00 14.44 H ANISOU 3012 H28A DJT A1221 2006 2032 1448 66 -262 412 H HETATM 3013 H29 DJT A1221 30.863 4.801 -2.220 1.00 23.46 H ANISOU 3013 H29 DJT A1221 3522 2972 2417 682 396 46 H HETATM 3014 H31 DJT A1221 33.828 7.152 -0.283 1.00 25.09 H ANISOU 3014 H31 DJT A1221 2658 3499 3376 268 513 567 H HETATM 3015 H32 DJT A1221 32.281 7.658 1.527 1.00 21.39 H ANISOU 3015 H32 DJT A1221 2571 2671 2885 90 -163 356 H HETATM 3016 H34 DJT A1221 29.281 5.308 -0.374 1.00 19.23 H ANISOU 3016 H34 DJT A1221 2909 2430 1967 525 -134 38 H HETATM 3017 C1 GOL A1222 19.766 6.036 4.415 1.00 28.63 C ANISOU 3017 C1 GOL A1222 4056 3665 3155 -109 243 290 C HETATM 3018 O1 GOL A1222 19.136 4.794 4.743 1.00 30.11 O ANISOU 3018 O1 GOL A1222 4961 3332 3147 81 -238 556 O HETATM 3019 C2 GOL A1222 20.193 5.989 2.952 1.00 25.99 C ANISOU 3019 C2 GOL A1222 3699 2932 3243 205 123 425 C HETATM 3020 O2 GOL A1222 21.095 4.894 2.768 1.00 31.36 O ANISOU 3020 O2 GOL A1222 4111 3291 4511 454 44 -187 O HETATM 3021 C3 GOL A1222 20.897 7.271 2.573 1.00 23.40 C ANISOU 3021 C3 GOL A1222 3316 3186 2386 96 105 229 C HETATM 3022 O3 GOL A1222 21.169 7.248 1.180 1.00 22.32 O ANISOU 3022 O3 GOL A1222 3377 2689 2414 90 128 32 O HETATM 3023 H11 GOL A1222 20.638 6.193 5.054 1.00 29.22 H ANISOU 3023 H11 GOL A1222 3905 3920 3276 277 199 131 H HETATM 3024 H12 GOL A1222 19.070 6.862 4.574 1.00 25.99 H ANISOU 3024 H12 GOL A1222 3688 3352 2834 -341 -6 235 H HETATM 3025 HO1 GOL A1222 19.778 4.075 4.662 1.00 29.82 H ANISOU 3025 HO1 GOL A1222 4111 3653 3564 -162 -21 112 H HETATM 3026 H2 GOL A1222 19.307 5.885 2.314 1.00 26.62 H ANISOU 3026 H2 GOL A1222 3628 3197 3287 -67 192 58 H HETATM 3027 H31 GOL A1222 21.825 7.357 3.140 1.00 22.98 H ANISOU 3027 H31 GOL A1222 3264 3009 2456 305 88 135 H HETATM 3028 H32 GOL A1222 20.265 8.127 2.817 1.00 20.97 H ANISOU 3028 H32 GOL A1222 2850 2969 2147 -192 31 158 H HETATM 3029 C1 GOL A1223 13.397 6.359 -11.314 1.00 43.16 C ANISOU 3029 C1 GOL A1223 5226 5589 5584 -45 -353 375 C HETATM 3030 O1 GOL A1223 13.192 6.083 -12.707 1.00 41.97 O ANISOU 3030 O1 GOL A1223 4278 5699 5967 155 -1163 51 O HETATM 3031 C2 GOL A1223 12.058 6.411 -10.575 1.00 43.86 C ANISOU 3031 C2 GOL A1223 5155 5188 6319 180 -389 -56 C HETATM 3032 O2 GOL A1223 11.998 7.568 -9.741 1.00 44.66 O ANISOU 3032 O2 GOL A1223 6865 6174 3929 -194 -149 36 O HETATM 3033 C3 GOL A1223 11.848 5.180 -9.702 1.00 43.53 C ANISOU 3033 C3 GOL A1223 5082 5980 5475 -464 -202 -1 C HETATM 3034 O3 GOL A1223 11.005 5.493 -8.584 1.00 47.15 O ANISOU 3034 O3 GOL A1223 5928 6458 5526 142 -269 -1147 O HETATM 3035 H11 GOL A1223 13.906 7.320 -11.210 1.00 41.58 H ANISOU 3035 H11 GOL A1223 5498 5257 5041 196 -102 44 H HETATM 3036 H12 GOL A1223 14.043 5.592 -10.885 1.00 38.61 H ANISOU 3036 H12 GOL A1223 4966 5104 4599 -156 -25 -58 H HETATM 3037 HO1 GOL A1223 12.727 5.241 -12.803 1.00 43.61 H ANISOU 3037 HO1 GOL A1223 5351 5474 5745 -38 -21 42 H HETATM 3038 H2 GOL A1223 11.248 6.452 -11.317 1.00 41.77 H ANISOU 3038 H2 GOL A1223 5282 5226 5363 -149 -69 -326 H HETATM 3039 H31 GOL A1223 12.803 4.806 -9.339 1.00 38.65 H ANISOU 3039 H31 GOL A1223 5406 4728 4549 -360 -76 -195 H HETATM 3040 H32 GOL A1223 11.384 4.390 -10.296 1.00 39.73 H ANISOU 3040 H32 GOL A1223 4894 5439 4760 99 25 8 H HETATM 3041 O HOH A2001 28.172 37.519 7.306 1.00 30.80 O ANISOU 3041 O HOH A2001 2603 4255 4843 -529 379 -412 O HETATM 3042 O HOH A2002 25.018 36.055 10.429 1.00 29.78 O ANISOU 3042 O HOH A2002 3115 3507 4692 -230 -517 -895 O HETATM 3043 O HOH A2003 22.274 35.163 10.262 1.00 21.91 O ANISOU 3043 O HOH A2003 3022 2235 3064 185 -555 -635 O HETATM 3044 O HOH A2004 17.252 33.904 13.681 1.00 32.41 O ANISOU 3044 O HOH A2004 4240 4729 3344 -193 -594 -649 O HETATM 3045 O HOH A2005 17.419 38.465 6.881 1.00 22.63 O ANISOU 3045 O HOH A2005 3060 2415 3123 286 9 -212 O HETATM 3046 O HOH A2006 24.798 38.362 12.475 1.00 30.95 O ANISOU 3046 O HOH A2006 3710 2907 5143 -432 -102 -558 O HETATM 3047 O HOH A2007 18.524 32.827 11.236 1.00 19.63 O ANISOU 3047 O HOH A2007 2998 2244 2215 27 -939 -279 O HETATM 3048 O HOH A2008 19.258 34.719 -1.640 1.00 29.73 O ANISOU 3048 O HOH A2008 4732 3356 3206 -213 -532 393 O HETATM 3049 O HOH A2009 8.908 36.022 -6.388 0.50 26.75 O ANISOU 3049 O HOH A2009 3811 3764 2586 287 -78 169 O HETATM 3050 O HOH A2010 17.762 36.444 1.951 1.00 28.40 O ANISOU 3050 O HOH A2010 4085 3215 3487 170 -101 423 O HETATM 3051 O HOH A2011 14.438 36.684 -9.636 1.00 46.58 O ANISOU 3051 O HOH A2011 5214 5979 6503 203 -65 46 O HETATM 3052 O HOH A2012 10.170 23.029 -7.002 1.00 22.90 O ANISOU 3052 O HOH A2012 2817 3120 2762 313 -405 166 O HETATM 3053 O HOH A2013 16.964 34.351 -0.317 1.00 23.81 O ANISOU 3053 O HOH A2013 3673 2051 3320 -167 -515 308 O HETATM 3054 O HOH A2014 11.994 30.060 2.908 1.00 28.40 O ANISOU 3054 O HOH A2014 3714 3692 3384 609 -280 351 O HETATM 3055 O HOH A2015 37.854 15.227 -3.480 1.00 37.51 O ANISOU 3055 O HOH A2015 5030 4122 5100 76 -658 700 O HETATM 3056 O HOH A2016 9.718 25.887 2.936 1.00 27.85 O ANISOU 3056 O HOH A2016 2909 4101 3570 253 46 472 O HETATM 3057 O HOH A2017 13.997 27.687 -7.959 1.00 14.77 O ANISOU 3057 O HOH A2017 1931 1958 1722 114 -435 187 O HETATM 3058 O HOH A2018 10.519 23.452 2.289 1.00 28.21 O ANISOU 3058 O HOH A2018 3691 3014 4013 -28 15 39 O HETATM 3059 O HOH A2019 9.831 25.052 -2.933 1.00 26.03 O ANISOU 3059 O HOH A2019 1960 4508 3420 89 -398 907 O HETATM 3060 O HOH A2020 8.103 25.574 0.397 1.00 31.16 O ANISOU 3060 O HOH A2020 4494 4248 3095 781 -190 183 O HETATM 3061 O HOH A2021 14.435 34.540 -1.299 1.00 43.02 O ANISOU 3061 O HOH A2021 5860 5546 4938 -1 -179 -198 O HETATM 3062 O HOH A2022 8.947 33.490 -3.084 1.00 32.76 O ANISOU 3062 O HOH A2022 4061 4458 3928 -445 -478 307 O HETATM 3063 O HOH A2023 9.595 33.937 -5.697 0.50 25.38 O ANISOU 3063 O HOH A2023 3332 2467 3841 -52 -211 63 O HETATM 3064 O HOH A2024 16.996 35.340 -9.766 1.00 32.95 O ANISOU 3064 O HOH A2024 4517 2717 5283 -482 17 485 O HETATM 3065 O HOH A2025 21.025 35.874 -8.105 1.00 33.21 O ANISOU 3065 O HOH A2025 4768 2597 5252 -46 -220 420 O HETATM 3066 O HOH A2026 12.324 25.433 -6.323 1.00 28.97 O ANISOU 3066 O HOH A2026 3221 3540 4246 232 -533 49 O HETATM 3067 O HOH A2027 22.911 28.051 -20.415 1.00 27.56 O ANISOU 3067 O HOH A2027 4233 3194 3043 290 337 576 O HETATM 3068 O HOH A2028 13.253 18.286 -11.496 1.00 17.49 O ANISOU 3068 O HOH A2028 2165 2560 1918 437 -278 217 O HETATM 3069 O HOH A2029 11.346 16.411 -11.019 1.00 22.33 O ANISOU 3069 O HOH A2029 3045 3607 1829 -774 -302 461 O HETATM 3070 O HOH A2030 8.728 16.910 -8.296 1.00 27.86 O ANISOU 3070 O HOH A2030 2537 3261 4785 445 -397 -327 O HETATM 3071 O HOH A2031 10.391 13.483 -8.122 1.00 20.22 O ANISOU 3071 O HOH A2031 2217 2503 2963 -157 -257 76 O HETATM 3072 O HOH A2032 9.596 20.343 -6.318 1.00 17.27 O ANISOU 3072 O HOH A2032 2319 2305 1937 350 221 398 O HETATM 3073 O HOH A2033 13.235 15.672 -15.296 1.00 26.66 O ANISOU 3073 O HOH A2033 3148 3283 3698 0 388 16 O HETATM 3074 O HOH A2034 12.653 12.417 -10.769 0.50 25.63 O ANISOU 3074 O HOH A2034 4471 2710 2557 -111 -544 -284 O HETATM 3075 O HOH A2035 13.193 6.052 -3.220 1.00 42.66 O ANISOU 3075 O HOH A2035 6347 5699 4161 211 266 -453 O HETATM 3076 O HOH A2036 9.870 6.319 -4.605 1.00 36.97 O ANISOU 3076 O HOH A2036 5315 3192 5537 -705 535 593 O HETATM 3077 O HOH A2037 14.450 11.198 -11.119 1.00 25.89 O ANISOU 3077 O HOH A2037 3575 3298 2962 42 152 454 O HETATM 3078 O HOH A2038 8.311 10.236 -7.351 1.00 32.37 O ANISOU 3078 O HOH A2038 3100 4078 5121 25 -683 78 O HETATM 3079 O HOH A2039 33.795 2.805 -15.046 0.50 32.46 O ANISOU 3079 O HOH A2039 4020 4105 4207 138 245 -26 O HETATM 3080 O HOH A2040 17.673 4.026 -3.170 1.00 27.71 O ANISOU 3080 O HOH A2040 3778 3998 2749 -6 -338 587 O HETATM 3081 O HOH A2041 39.691 3.856 -13.333 1.00 32.53 O ANISOU 3081 O HOH A2041 3776 3741 4842 -446 -320 -559 O HETATM 3082 O HOH A2042 38.036 14.955 -6.960 1.00 35.31 O ANISOU 3082 O HOH A2042 4749 3601 5066 -3 -548 178 O HETATM 3083 O HOH A2043 18.241 -1.477 -5.942 1.00 48.81 O ANISOU 3083 O HOH A2043 6104 5508 6932 294 -316 172 O HETATM 3084 O HOH A2044 16.809 1.423 -1.798 0.50 28.53 O ANISOU 3084 O HOH A2044 3425 3508 3904 -297 -310 9 O HETATM 3085 O HOH A2045 11.972 3.751 -5.213 1.00 38.59 O ANISOU 3085 O HOH A2045 4562 5105 4996 -424 625 -22 O HETATM 3086 O HOH A2046 20.007 -0.046 -9.534 0.50 30.69 O ANISOU 3086 O HOH A2046 3697 3190 4773 -50 180 210 O HETATM 3087 O HOH A2047 14.019 2.551 -9.307 1.00 24.61 O ANISOU 3087 O HOH A2047 3382 3238 2728 -549 -90 -711 O HETATM 3088 O HOH A2048 24.201 -1.502 -9.242 1.00 27.99 O ANISOU 3088 O HOH A2048 4130 2929 3575 559 -35 104 O HETATM 3089 O HOH A2049 20.059 1.320 -3.628 1.00 30.38 O ANISOU 3089 O HOH A2049 3760 5141 2642 125 -205 1474 O HETATM 3090 O HOH A2050 41.177 18.379 -5.147 1.00 39.96 O ANISOU 3090 O HOH A2050 3810 5723 5651 -289 -346 -188 O HETATM 3091 O HOH A2051 19.879 18.118 -5.375 1.00 13.05 O ANISOU 3091 O HOH A2051 1749 1781 1427 48 -274 240 O HETATM 3092 O HOH A2052 40.909 17.076 -22.011 1.00 41.60 O ANISOU 3092 O HOH A2052 4427 6303 5073 -52 33 57 O HETATM 3093 O HOH A2053 41.141 18.949 -18.340 1.00 51.50 O ANISOU 3093 O HOH A2053 5771 6445 7350 -50 102 -74 O HETATM 3094 O HOH A2054 21.453 20.913 -25.682 1.00 35.85 O ANISOU 3094 O HOH A2054 4725 4460 4434 -73 -202 261 O HETATM 3095 O HOH A2055 19.228 18.045 -9.513 1.00 12.67 O ANISOU 3095 O HOH A2055 1788 1807 1219 -102 -187 218 O HETATM 3096 O HOH A2056 13.825 15.862 -18.124 1.00 34.66 O ANISOU 3096 O HOH A2056 3582 4943 4643 287 -294 219 O HETATM 3097 O HOH A2057 19.025 14.985 -27.411 1.00 34.05 O ANISOU 3097 O HOH A2057 5848 4375 2712 40 -939 17 O HETATM 3098 O HOH A2058 19.878 24.116 -7.324 1.00 13.40 O ANISOU 3098 O HOH A2058 1741 1769 1579 -55 -271 312 O HETATM 3099 O HOH A2059 18.249 22.007 -8.176 1.00 12.28 O ANISOU 3099 O HOH A2059 1680 1766 1218 108 -125 315 O HETATM 3100 O HOH A2060 21.154 25.883 -14.398 1.00 15.11 O ANISOU 3100 O HOH A2060 2266 1951 1523 76 -340 371 O HETATM 3101 O HOH A2061 30.690 28.714 -8.094 1.00 25.14 O ANISOU 3101 O HOH A2061 2547 2326 4678 -254 -2 547 O HETATM 3102 O HOH A2062 22.760 22.535 -29.483 1.00 35.36 O ANISOU 3102 O HOH A2062 5233 5344 2856 334 -111 646 O HETATM 3103 O HOH A2063 27.169 36.518 -12.262 1.00 45.67 O ANISOU 3103 O HOH A2063 5583 6171 5597 -265 42 -345 O HETATM 3104 O HOH A2064 26.510 33.995 -6.227 0.30 21.07 O ANISOU 3104 O HOH A2064 2670 1891 3443 -8 -176 -259 O HETATM 3105 O HOH A2065 24.435 33.641 -6.096 0.70 29.75 O ANISOU 3105 O HOH A2065 3348 3331 4625 149 -388 509 O HETATM 3106 O HOH A2066 34.866 25.766 -18.087 1.00 41.95 O ANISOU 3106 O HOH A2066 4794 6464 4678 -167 183 -73 O HETATM 3107 O HOH A2067 40.302 24.428 -8.241 1.00 39.58 O ANISOU 3107 O HOH A2067 4335 5373 5328 -200 -17 -84 O HETATM 3108 O HOH A2068 39.308 26.294 -2.559 1.00 43.49 O ANISOU 3108 O HOH A2068 5115 5144 6263 -78 71 313 O HETATM 3109 O HOH A2069 28.143 35.664 -14.947 1.00 26.33 O ANISOU 3109 O HOH A2069 3630 2988 3383 -130 -534 839 O HETATM 3110 O HOH A2070 22.621 33.101 -20.747 1.00 30.94 O ANISOU 3110 O HOH A2070 5799 3694 2261 295 87 495 O HETATM 3111 O HOH A2071 22.679 27.451 -17.636 1.00 22.25 O ANISOU 3111 O HOH A2071 3257 2227 2967 69 149 394 O HETATM 3112 O HOH A2072 17.843 33.924 -18.794 1.00 34.56 O ANISOU 3112 O HOH A2072 5338 3732 4062 -287 -461 427 O HETATM 3113 O HOH A2073 17.268 34.436 -15.065 1.00 27.94 O ANISOU 3113 O HOH A2073 3699 3115 3801 140 319 656 O HETATM 3114 O HOH A2074 23.399 30.582 -21.560 1.00 35.60 O ANISOU 3114 O HOH A2074 5670 3576 4279 212 -19 322 O HETATM 3115 O HOH A2075 15.663 29.316 -16.923 1.00 24.72 O ANISOU 3115 O HOH A2075 2856 3174 3359 769 -258 567 O HETATM 3116 O HOH A2076 22.402 23.623 -15.399 1.00 16.18 O ANISOU 3116 O HOH A2076 2517 1964 1664 -144 -548 468 O HETATM 3117 O HOH A2077 17.221 18.990 -19.240 1.00 15.72 O ANISOU 3117 O HOH A2077 2136 1996 1841 229 -180 284 O HETATM 3118 O HOH A2078 15.537 21.917 -17.789 1.00 18.86 O ANISOU 3118 O HOH A2078 2020 2906 2240 452 -434 306 O HETATM 3119 O HOH A2079 14.178 17.883 -14.011 1.00 18.05 O ANISOU 3119 O HOH A2079 1822 2874 2160 107 -87 181 O HETATM 3120 O HOH A2080 10.149 14.689 12.575 1.00 41.25 O ANISOU 3120 O HOH A2080 6146 5784 3741 46 -84 7 O HETATM 3121 O HOH A2081 16.348 12.444 -12.415 1.00 21.58 O ANISOU 3121 O HOH A2081 2974 2946 2278 -64 -263 352 O HETATM 3122 O HOH A2082 7.776 5.292 3.425 0.50 38.90 O ANISOU 3122 O HOH A2082 5381 4990 4406 -79 -69 27 O HETATM 3123 O HOH A2083 10.552 6.217 2.280 1.00 49.31 O ANISOU 3123 O HOH A2083 7200 5450 6084 272 -216 -184 O HETATM 3124 O HOH A2084 26.265 9.166 19.187 0.50 32.04 O ANISOU 3124 O HOH A2084 4287 4196 3689 59 -270 112 O HETATM 3125 O HOH A2085 26.907 8.437 16.965 1.00 32.98 O ANISOU 3125 O HOH A2085 5402 4360 2769 87 -209 94 O HETATM 3126 O HOH A2086 34.173 8.689 -18.311 1.00 34.15 O ANISOU 3126 O HOH A2086 4339 4987 3648 -148 611 344 O HETATM 3127 O HOH A2087 32.205 5.244 -15.094 1.00 22.45 O ANISOU 3127 O HOH A2087 2529 2369 3629 491 -185 152 O HETATM 3128 O HOH A2088 36.379 3.582 -13.879 0.50 27.69 O ANISOU 3128 O HOH A2088 4501 2940 3077 209 -7 -60 O HETATM 3129 O HOH A2089 40.821 6.255 -12.908 1.00 25.95 O ANISOU 3129 O HOH A2089 2107 3746 4007 285 -119 -359 O HETATM 3130 O HOH A2090 38.302 12.667 -8.692 1.00 26.85 O ANISOU 3130 O HOH A2090 3405 3168 3627 -202 -666 400 O HETATM 3131 O HOH A2091 36.432 10.672 -17.199 1.00 32.15 O ANISOU 3131 O HOH A2091 4600 4274 3342 568 -516 107 O HETATM 3132 O HOH A2092 36.269 3.907 -6.355 1.00 39.07 O ANISOU 3132 O HOH A2092 4666 4020 6156 85 -220 430 O HETATM 3133 O HOH A2093 35.916 5.454 -4.290 1.00 34.54 O ANISOU 3133 O HOH A2093 3305 6148 3669 566 92 -13 O HETATM 3134 O HOH A2094 34.973 3.647 -8.878 1.00 34.67 O ANISOU 3134 O HOH A2094 3820 4821 4532 868 343 -187 O HETATM 3135 O HOH A2095 34.396 3.074 -4.302 0.50 18.45 O ANISOU 3135 O HOH A2095 3169 2355 1486 -140 -42 382 O HETATM 3136 O HOH A2096 29.749 2.736 -1.905 1.00 26.94 O ANISOU 3136 O HOH A2096 3428 3893 2915 -183 -444 433 O HETATM 3137 O HOH A2097 29.980 6.391 -11.130 1.00 18.34 O ANISOU 3137 O HOH A2097 2478 2387 2102 -212 -29 954 O HETATM 3138 O HOH A2098 21.424 0.512 -6.077 1.00 21.72 O ANISOU 3138 O HOH A2098 2560 2010 3680 -11 261 738 O HETATM 3139 O HOH A2099 12.833 6.763 0.679 0.50 31.77 O ANISOU 3139 O HOH A2099 4705 3331 4033 -282 -330 -193 O HETATM 3140 O HOH A2100 26.769 2.016 -0.603 1.00 24.77 O ANISOU 3140 O HOH A2100 3172 2823 3415 96 390 446 O HETATM 3141 O HOH A2101 23.802 -1.027 -6.718 1.00 22.77 O ANISOU 3141 O HOH A2101 3029 2175 3446 127 -236 502 O HETATM 3142 O HOH A2102 34.390 14.780 -0.420 1.00 27.81 O ANISOU 3142 O HOH A2102 2836 3792 3938 53 -870 751 O HETATM 3143 O HOH A2103 33.522 17.382 0.550 1.00 33.16 O ANISOU 3143 O HOH A2103 3447 4788 4361 -181 -322 244 O HETATM 3144 O HOH A2104 32.027 15.318 -1.869 1.00 18.38 O ANISOU 3144 O HOH A2104 2237 2457 2289 39 -279 647 O HETATM 3145 O HOH A2105 41.813 19.321 -13.018 1.00 39.46 O ANISOU 3145 O HOH A2105 3669 5777 5544 -228 -170 11 O HETATM 3146 O HOH A2106 39.961 16.624 -7.202 1.00 31.56 O ANISOU 3146 O HOH A2106 2978 3879 5133 33 -148 195 O HETATM 3147 O HOH A2107 39.712 20.323 -9.460 1.00 29.69 O ANISOU 3147 O HOH A2107 3556 4246 3479 -12 -413 460 O HETATM 3148 O HOH A2108 32.381 10.932 -20.211 1.00 21.37 O ANISOU 3148 O HOH A2108 2495 3114 2510 190 308 116 O HETATM 3149 O HOH A2109 39.091 23.775 -16.208 0.50 33.96 O ANISOU 3149 O HOH A2109 4137 4115 4648 -301 23 277 O HETATM 3150 O HOH A2110 36.324 21.627 -18.199 1.00 36.46 O ANISOU 3150 O HOH A2110 3836 4648 5370 4 -74 381 O HETATM 3151 O HOH A2111 40.801 16.411 -18.913 1.00 31.03 O ANISOU 3151 O HOH A2111 2761 5110 3918 -271 323 -69 O HETATM 3152 O HOH A2112 36.066 12.411 -19.285 1.00 36.32 O ANISOU 3152 O HOH A2112 3829 4294 5677 83 263 -66 O HETATM 3153 O HOH A2113 34.780 13.536 -23.061 1.00 31.28 O ANISOU 3153 O HOH A2113 4118 5103 2661 515 147 -146 O HETATM 3154 O HOH A2114 33.123 19.645 -25.060 1.00 38.00 O ANISOU 3154 O HOH A2114 5133 4513 4789 -220 -334 452 O HETATM 3155 O HOH A2115 21.292 18.802 -23.980 1.00 29.09 O ANISOU 3155 O HOH A2115 3934 3673 3443 -228 98 -9 O HETATM 3156 O HOH A2116 14.747 13.232 -18.974 1.00 27.21 O ANISOU 3156 O HOH A2116 4174 3877 2285 -297 -449 229 O HETATM 3157 O HOH A2117 19.773 11.416 -15.794 1.00 14.50 O ANISOU 3157 O HOH A2117 1848 2098 1562 -88 -188 111 O HETATM 3158 O HOH A2118 14.513 13.320 -14.355 1.00 23.98 O ANISOU 3158 O HOH A2118 2756 3462 2893 -93 -270 334 O HETATM 3159 O HOH A2119 16.501 20.824 -21.170 1.00 31.89 O ANISOU 3159 O HOH A2119 5751 3498 2865 148 -1125 555 O HETATM 3160 O HOH A2120 14.081 12.953 -21.956 1.00 35.15 O ANISOU 3160 O HOH A2120 3622 4569 5161 -406 -383 48 O HETATM 3161 O HOH A2121 19.600 12.327 -26.485 1.00 29.73 O ANISOU 3161 O HOH A2121 5720 4401 1172 98 -470 708 O HETATM 3162 O HOH A2122 21.808 9.913 -24.066 1.00 37.56 O ANISOU 3162 O HOH A2122 6012 4634 3625 68 -191 -89 O HETATM 3163 O HOH A2123 19.532 7.402 -20.287 1.00 27.57 O ANISOU 3163 O HOH A2123 4377 3660 2437 -459 302 -66 O HETATM 3164 O HOH A2124 14.964 11.806 -16.587 1.00 21.92 O ANISOU 3164 O HOH A2124 2681 2589 3057 154 -301 343 O HETATM 3165 O HOH A2125 13.581 9.427 -16.373 1.00 29.77 O ANISOU 3165 O HOH A2125 3097 3329 4884 -249 -154 491 O HETATM 3166 O HOH A2126 15.936 0.743 -10.670 1.00 34.39 O ANISOU 3166 O HOH A2126 5099 4199 3769 -352 437 416 O HETATM 3167 O HOH A2127 26.270 0.770 -10.364 1.00 28.40 O ANISOU 3167 O HOH A2127 4253 2256 4280 409 -252 283 O HETATM 3168 O HOH A2128 31.047 4.063 -12.652 1.00 31.85 O ANISOU 3168 O HOH A2128 3838 3778 4484 -55 733 -293 O HETATM 3169 O HOH A2129 29.213 2.698 -16.603 1.00 29.94 O ANISOU 3169 O HOH A2129 4015 2788 4571 130 -313 187 O HETATM 3170 O HOH A2130 24.743 0.056 -21.570 0.50 27.49 O ANISOU 3170 O HOH A2130 4210 3878 2355 -240 92 -552 O HETATM 3171 O HOH A2131 31.138 2.965 -20.013 1.00 33.40 O ANISOU 3171 O HOH A2131 3819 3436 5433 580 212 170 O HETATM 3172 O HOH A2132 23.746 11.636 -24.615 0.50 26.50 O ANISOU 3172 O HOH A2132 4629 4220 1219 227 151 215 O HETATM 3173 O HOH A2133 23.806 9.582 -25.509 1.00 41.02 O ANISOU 3173 O HOH A2133 5559 5839 4186 -71 -388 0 O HETATM 3174 O HOH A2134 33.132 17.364 -23.460 1.00 22.29 O ANISOU 3174 O HOH A2134 2573 3273 2623 -286 175 541 O HETATM 3175 O HOH A2135 24.017 10.754 -28.233 1.00 37.69 O ANISOU 3175 O HOH A2135 4902 4132 5285 -489 -23 -77 O HETATM 3176 O HOH A2136 30.363 20.487 -26.012 1.00 36.66 O ANISOU 3176 O HOH A2136 4292 3851 5785 -262 564 194 O HETATM 3177 O HOH A2137 23.017 19.683 -29.741 1.00 32.13 O ANISOU 3177 O HOH A2137 4030 4204 3974 173 -411 367 O HETATM 3178 O HOH A2138 29.333 18.348 -33.401 0.40 18.50 O ANISOU 3178 O HOH A2138 2686 3381 961 339 -581 483 O HETATM 3179 O HOH A2139 23.973 15.556 -32.476 1.00 32.14 O ANISOU 3179 O HOH A2139 4739 3477 3994 -620 -154 -291 O HETATM 3180 O HOH A2140 30.604 21.623 -22.435 1.00 32.28 O ANISOU 3180 O HOH A2140 3602 3941 4722 -336 -163 514 O HETATM 3181 O HOH A2141 28.531 22.745 -22.105 1.00 34.30 O ANISOU 3181 O HOH A2141 5066 4185 3779 -215 -477 430 O HETATM 3182 O HOH A2142 23.179 24.849 -17.750 1.00 19.26 O ANISOU 3182 O HOH A2142 3032 2179 2106 355 575 555 O HETATM 3183 O HOH A2143 24.398 25.905 -21.381 1.00 31.38 O ANISOU 3183 O HOH A2143 5225 3057 3638 277 239 441 O HETATM 3184 O HOH A2144 30.384 26.780 -16.550 1.00 30.06 O ANISOU 3184 O HOH A2144 4398 2962 4060 -53 80 763 O HETATM 3185 O HOH A2145 33.547 21.492 -17.737 1.00 19.24 O ANISOU 3185 O HOH A2145 2352 2648 2310 -189 100 284 O HETATM 3186 O HOH A2146 36.364 23.862 -17.064 1.00 38.29 O ANISOU 3186 O HOH A2146 4976 4525 5046 -127 505 188 O HETATM 3187 O HOH A2147 39.064 22.114 -7.530 1.00 26.48 O ANISOU 3187 O HOH A2147 2088 3522 4450 -53 -194 16 O HETATM 3188 O HOH A2148 39.954 21.594 -4.729 1.00 40.28 O ANISOU 3188 O HOH A2148 4474 5128 5700 -461 -319 191 O HETATM 3189 O HOH A2149 38.516 23.871 -1.193 1.00 26.18 O ANISOU 3189 O HOH A2149 1999 4443 3505 -772 -641 438 O HETATM 3190 O HOH A2150 35.526 20.403 4.246 0.50 25.99 O ANISOU 3190 O HOH A2150 3047 4257 2568 545 -729 119 O HETATM 3191 O HOH A2151 37.534 21.441 4.291 0.50 31.31 O ANISOU 3191 O HOH A2151 4772 4279 2842 -18 -588 -285 O HETATM 3192 O HOH A2152 30.331 23.464 6.211 1.00 32.12 O ANISOU 3192 O HOH A2152 3546 4308 4351 24 -542 547 O HETATM 3193 O HOH A2153 31.526 21.782 13.655 1.00 41.96 O ANISOU 3193 O HOH A2153 5349 5729 4864 84 -217 344 O HETATM 3194 O HOH A2154 37.459 22.744 8.754 1.00 27.00 O ANISOU 3194 O HOH A2154 2323 4702 3232 -185 -841 419 O HETATM 3195 O HOH A2155 33.859 19.701 12.623 1.00 44.92 O ANISOU 3195 O HOH A2155 6033 5714 5320 33 33 124 O HETATM 3196 O HOH A2156 27.296 24.548 15.081 1.00 30.45 O ANISOU 3196 O HOH A2156 4103 3663 3801 -595 -973 -141 O HETATM 3197 O HOH A2157 29.235 23.678 13.580 1.00 24.11 O ANISOU 3197 O HOH A2157 3394 2767 2999 -169 -793 769 O HETATM 3198 O HOH A2158 29.497 27.051 13.569 1.00 27.36 O ANISOU 3198 O HOH A2158 4250 3578 2566 219 -1033 127 O HETATM 3199 O HOH A2159 32.175 29.412 3.663 1.00 42.85 O ANISOU 3199 O HOH A2159 4812 5517 5950 -192 -282 330 O HETATM 3200 O HOH A2160 34.648 29.896 5.679 1.00 43.91 O ANISOU 3200 O HOH A2160 5449 5232 6002 -363 104 423 O HETATM 3201 O HOH A2161 32.303 32.720 10.508 1.00 36.74 O ANISOU 3201 O HOH A2161 4724 4507 4727 -234 -181 63 O HETATM 3202 O HOH A2162 29.438 36.551 11.846 1.00 34.59 O ANISOU 3202 O HOH A2162 4340 4015 4787 -241 250 -206 O HETATM 3203 O HOH A2163 33.331 32.236 7.617 1.00 31.43 O ANISOU 3203 O HOH A2163 2864 5014 4064 -19 80 -1 O HETATM 3204 O HOH A2164 21.467 35.548 0.124 1.00 35.49 O ANISOU 3204 O HOH A2164 4821 4153 4511 534 318 287 O HETATM 3205 O HOH A2165 24.138 36.493 -2.432 1.00 36.87 O ANISOU 3205 O HOH A2165 4676 4569 4761 -381 -22 556 O HETATM 3206 O HOH A2166 32.081 32.522 0.961 1.00 55.15 O ANISOU 3206 O HOH A2166 6819 6748 7387 -133 -84 -121 O HETATM 3207 O HOH A2167 24.553 26.107 -6.403 1.00 13.28 O ANISOU 3207 O HOH A2167 1891 1903 1252 -41 -219 381 O HETATM 3208 O HOH A2168 18.932 10.867 10.010 1.00 28.95 O ANISOU 3208 O HOH A2168 3181 3564 4253 -13 163 -227 O HETATM 3209 O HOH A2169 24.540 7.289 12.924 1.00 25.48 O ANISOU 3209 O HOH A2169 2924 2871 3882 -13 -197 863 O HETATM 3210 O HOH A2170 22.934 6.095 10.784 1.00 20.61 O ANISOU 3210 O HOH A2170 2843 2365 2622 133 -517 465 O HETATM 3211 O HOH A2171 12.619 -1.140 13.557 0.50 19.04 O ANISOU 3211 O HOH A2171 2233 1783 3215 -35 -191 469 O HETATM 3212 O HOH A2172 10.273 11.448 11.966 1.00 29.17 O ANISOU 3212 O HOH A2172 3225 4656 3200 1050 506 135 O HETATM 3213 O HOH A2173 8.444 8.055 4.120 1.00 29.02 O ANISOU 3213 O HOH A2173 3035 3710 4277 -241 7 306 O HETATM 3214 O HOH A2174 8.613 10.190 5.027 0.50 18.42 O ANISOU 3214 O HOH A2174 2624 2892 1481 63 78 -20 O HETATM 3215 O HOH A2175 7.808 14.256 10.755 1.00 22.71 O ANISOU 3215 O HOH A2175 3449 3344 1834 207 53 -59 O HETATM 3216 O HOH A2176 1.216 14.581 7.547 1.00 37.52 O ANISOU 3216 O HOH A2176 5254 4388 4613 177 85 428 O HETATM 3217 O HOH A2177 4.557 16.262 4.838 1.00 17.73 O ANISOU 3217 O HOH A2177 1817 3057 1862 157 -436 53 O HETATM 3218 O HOH A2178 1.490 16.749 6.030 1.00 16.88 O ANISOU 3218 O HOH A2178 2266 2650 1497 138 -177 113 O HETATM 3219 O HOH A2179 9.281 21.881 14.209 1.00 31.82 O ANISOU 3219 O HOH A2179 3704 4755 3631 177 196 -812 O HETATM 3220 O HOH A2180 12.305 15.619 14.456 1.00 29.20 O ANISOU 3220 O HOH A2180 3160 4446 3485 -366 -149 724 O HETATM 3221 O HOH A2181 13.317 12.572 15.089 1.00 32.32 O ANISOU 3221 O HOH A2181 4537 3805 3936 -733 96 -349 O HETATM 3222 O HOH A2182 13.233 15.258 17.880 1.00 39.01 O ANISOU 3222 O HOH A2182 4580 5178 5065 -421 461 -517 O HETATM 3223 O HOH A2183 13.970 10.259 16.973 1.00 30.71 O ANISOU 3223 O HOH A2183 4016 4254 3395 -190 -484 -487 O HETATM 3224 O HOH A2184 16.372 8.191 18.751 1.00 30.58 O ANISOU 3224 O HOH A2184 4418 3784 3415 -93 489 194 O HETATM 3225 O HOH A2185 24.127 11.492 18.806 1.00 38.81 O ANISOU 3225 O HOH A2185 4588 6017 4140 -228 -454 -429 O HETATM 3226 O HOH A2186 24.801 7.366 15.617 1.00 26.38 O ANISOU 3226 O HOH A2186 3502 3561 2958 340 -81 468 O HETATM 3227 O HOH A2187 26.170 13.128 18.104 1.00 32.04 O ANISOU 3227 O HOH A2187 4492 4592 3087 -337 -281 210 O HETATM 3228 O HOH A2188 29.134 9.302 15.541 1.00 31.32 O ANISOU 3228 O HOH A2188 4637 4407 2856 537 -1079 977 O HETATM 3229 O HOH A2189 28.946 12.651 16.179 1.00 27.77 O ANISOU 3229 O HOH A2189 3450 3951 3149 -262 -902 1082 O HETATM 3230 O HOH A2190 32.021 15.989 14.440 1.00 41.14 O ANISOU 3230 O HOH A2190 4214 6183 5233 157 -463 61 O HETATM 3231 O HOH A2191 25.211 7.915 8.522 1.00 25.95 O ANISOU 3231 O HOH A2191 3405 3659 2793 34 -168 636 O HETATM 3232 O HOH A2192 26.988 6.207 13.614 1.00 27.48 O ANISOU 3232 O HOH A2192 3692 3624 3123 609 160 1079 O HETATM 3233 O HOH A2193 32.514 7.303 13.906 1.00 33.54 O ANISOU 3233 O HOH A2193 4631 4946 3166 363 -470 -584 O HETATM 3234 O HOH A2194 28.263 5.950 6.536 1.00 27.94 O ANISOU 3234 O HOH A2194 4069 3069 3475 804 -103 693 O HETATM 3235 O HOH A2195 31.011 9.672 6.584 1.00 28.47 O ANISOU 3235 O HOH A2195 3055 4664 3096 300 205 881 O HETATM 3236 O HOH A2196 23.981 4.119 6.393 1.00 19.60 O ANISOU 3236 O HOH A2196 2880 1870 2697 14 258 640 O HETATM 3237 O HOH A2197 13.980 30.964 4.493 1.00 28.85 O ANISOU 3237 O HOH A2197 2791 3599 4571 160 -635 -751 O HETATM 3238 O HOH A2198 12.767 31.849 8.052 1.00 28.92 O ANISOU 3238 O HOH A2198 3301 3930 3754 782 235 1165 O HETATM 3239 O HOH A2199 10.133 29.883 8.779 1.00 30.89 O ANISOU 3239 O HOH A2199 4092 4038 3604 370 -722 -397 O HETATM 3240 O HOH A2200 7.961 23.449 9.304 1.00 34.02 O ANISOU 3240 O HOH A2200 3488 4362 5074 398 -106 432 O HETATM 3241 O HOH A2201 10.188 31.970 19.331 1.00 43.17 O ANISOU 3241 O HOH A2201 5826 5731 4845 -44 193 325 O HETATM 3242 O HOH A2202 15.371 32.769 15.963 1.00 53.95 O ANISOU 3242 O HOH A2202 8004 5619 6875 -331 -206 -180 O HETATM 3243 O HOH A2203 12.861 31.375 19.130 1.00 47.61 O ANISOU 3243 O HOH A2203 5834 5773 6482 202 -79 41 O HETATM 3244 O HOH A2204 14.022 35.288 15.297 0.50 31.31 O ANISOU 3244 O HOH A2204 4620 4629 2645 67 -217 -537 O HETATM 3245 O HOH A2205 15.098 30.110 20.307 1.00 45.98 O ANISOU 3245 O HOH A2205 5916 5965 5589 292 209 -55 O HETATM 3246 O HOH A2206 16.761 23.865 15.449 1.00 31.40 O ANISOU 3246 O HOH A2206 5933 3524 2472 -621 -561 -121 O HETATM 3247 O HOH A2207 21.969 29.464 17.917 1.00 42.47 O ANISOU 3247 O HOH A2207 5660 6101 4374 -157 -258 -4 O HETATM 3248 O HOH A2208 11.768 28.338 4.997 1.00 31.41 O ANISOU 3248 O HOH A2208 3750 4374 3810 275 -211 792 O HETATM 3249 O HOH A2209 17.931 17.619 -7.162 1.00 12.84 O ANISOU 3249 O HOH A2209 1736 1647 1495 -27 9 309 O HETATM 3250 O HOH A2210 19.516 16.633 -3.162 1.00 14.25 O ANISOU 3250 O HOH A2210 2190 2007 1215 -16 -8 328 O HETATM 3251 O HOH A2211 15.833 16.121 -5.976 1.00 12.61 O ANISOU 3251 O HOH A2211 1893 1996 900 -194 -160 201 O HETATM 3252 O HOH A2212 19.946 14.001 -2.814 1.00 15.86 O ANISOU 3252 O HOH A2212 1899 1838 2288 77 -633 162 O HETATM 3253 O HOH A2213 10.847 7.445 -2.002 1.00 39.84 O ANISOU 3253 O HOH A2213 5406 4667 5063 -250 -265 293 O HETATM 3254 O HOH A2214 8.323 10.309 -3.066 1.00 26.58 O ANISOU 3254 O HOH A2214 2696 3151 4251 -366 328 -165 O HETATM 3255 O HOH A2215 12.784 14.005 -1.693 1.00 12.15 O ANISOU 3255 O HOH A2215 1691 1784 1140 -29 -176 173 O HETATM 3256 O HOH A2216 7.947 13.073 -7.076 1.00 25.44 O ANISOU 3256 O HOH A2216 2624 4563 2478 395 -31 -635 O HETATM 3257 O HOH A2217 5.153 15.794 0.601 1.00 19.47 O ANISOU 3257 O HOH A2217 2505 2427 2463 -355 514 -400 O HETATM 3258 O HOH A2218 7.564 19.369 -7.881 1.00 24.51 O ANISOU 3258 O HOH A2218 2565 3316 3430 190 143 192 O HETATM 3259 O HOH A2219 4.066 17.537 -9.041 1.00 38.95 O ANISOU 3259 O HOH A2219 4355 5689 4754 338 -445 54 O HETATM 3260 O HOH A2220 2.518 15.189 -9.239 1.00 42.15 O ANISOU 3260 O HOH A2220 4746 5603 5665 -387 227 119 O HETATM 3261 O HOH A2221 7.061 11.157 -4.995 1.00 35.23 O ANISOU 3261 O HOH A2221 3801 5566 4015 -271 -149 -394 O HETATM 3262 O HOH A2222 8.528 22.256 0.861 1.00 20.21 O ANISOU 3262 O HOH A2222 2467 2415 2794 362 -318 513 O HETATM 3263 O HOH A2223 8.490 20.509 -3.672 1.00 19.46 O ANISOU 3263 O HOH A2223 2665 2764 1963 496 78 361 O HETATM 3264 O HOH A2224 12.624 22.400 -5.871 1.00 17.70 O ANISOU 3264 O HOH A2224 2279 2707 1740 59 -259 39 O HETATM 3265 O HOH A2225 22.848 21.805 13.612 1.00 15.60 O ANISOU 3265 O HOH A2225 2508 1972 1446 -221 -501 183 O HETATM 3266 O HOH A2226 18.409 26.181 16.297 1.00 23.84 O ANISOU 3266 O HOH A2226 3189 3077 2792 220 -147 -197 O HETATM 3267 O HOH A2227 18.919 30.190 10.584 1.00 16.08 O ANISOU 3267 O HOH A2227 2405 2176 1528 -64 -201 -3 O HETATM 3268 O HOH A2228 21.439 32.654 11.528 1.00 22.43 O ANISOU 3268 O HOH A2228 3551 2948 2022 -339 -18 -136 O HETATM 3269 O HOH A2229 25.077 29.001 11.053 1.00 21.35 O ANISOU 3269 O HOH A2229 3353 2710 2047 0 -342 243 O HETATM 3270 O HOH A2230 26.612 27.212 14.756 1.00 27.66 O ANISOU 3270 O HOH A2230 3480 4110 2919 6 -420 131 O HETATM 3271 O HOH A2231 25.860 30.890 12.995 1.00 40.92 O ANISOU 3271 O HOH A2231 5906 4252 5388 -623 -249 -144 O HETATM 3272 O HOH A2232 20.241 27.263 18.184 1.00 38.99 O ANISOU 3272 O HOH A2232 5132 4675 5005 -40 -450 -156 O HETATM 3273 O HOH A2233 15.673 21.490 16.626 1.00 30.74 O ANISOU 3273 O HOH A2233 4470 3966 3245 -497 -39 341 O HETATM 3274 O HOH A2234 23.400 18.197 18.103 1.00 28.28 O ANISOU 3274 O HOH A2234 4511 3051 3182 -285 -583 558 O HETATM 3275 O HOH A2235 25.909 25.203 17.287 1.00 28.46 O ANISOU 3275 O HOH A2235 3333 3170 4308 -244 -737 45 O HETATM 3276 O HOH A2236 27.041 24.491 26.768 1.00 38.18 O ANISOU 3276 O HOH A2236 5638 4595 4272 -304 -142 251 O HETATM 3277 O HOH A2237 29.664 21.802 16.307 1.00 41.59 O ANISOU 3277 O HOH A2237 4999 5344 5457 -168 -205 33 O HETATM 3278 O HOH A2238 30.920 18.616 14.443 1.00 27.93 O ANISOU 3278 O HOH A2238 3245 4845 2522 56 -873 506 O HETATM 3279 O HOH A2239 20.920 19.164 10.682 1.00 17.14 O ANISOU 3279 O HOH A2239 2233 2425 1852 131 -718 -40 O HETATM 3280 O HOH A2240 24.774 14.941 15.111 1.00 19.55 O ANISOU 3280 O HOH A2240 3001 2044 2381 -73 -813 347 O HETATM 3281 O HOH A2241 28.151 17.930 5.076 1.00 14.31 O ANISOU 3281 O HOH A2241 1831 2004 1602 -154 -415 503 O HETATM 3282 O HOH A2242 32.405 20.871 5.139 1.00 18.15 O ANISOU 3282 O HOH A2242 2506 2671 1718 -476 -613 310 O HETATM 3283 O HOH A2243 33.896 19.532 2.097 1.00 23.83 O ANISOU 3283 O HOH A2243 2260 3022 3770 93 -259 1094 O HETATM 3284 O HOH A2244 30.579 17.507 -0.562 1.00 20.06 O ANISOU 3284 O HOH A2244 3381 2188 2052 -377 106 506 O HETATM 3285 O HOH A2245 33.019 29.751 0.191 1.00 41.14 O ANISOU 3285 O HOH A2245 5391 4860 5377 -261 -652 -368 O HETATM 3286 O HOH A2246 38.243 26.137 -8.600 1.00 33.52 O ANISOU 3286 O HOH A2246 3324 4280 5131 -581 -328 -69 O HETATM 3287 O HOH A2247 32.819 26.631 -16.074 1.00 32.33 O ANISOU 3287 O HOH A2247 4391 3626 4264 -345 406 1073 O HETATM 3288 O HOH A2248 32.601 30.019 -9.422 1.00 32.87 O ANISOU 3288 O HOH A2248 4491 3152 4844 -431 94 257 O HETATM 3289 O HOH A2249 20.387 4.341 -2.012 1.00 20.63 O ANISOU 3289 O HOH A2249 2655 3163 2018 -268 240 304 O HETATM 3290 O HOH A2250 26.918 4.238 2.727 1.00 27.59 O ANISOU 3290 O HOH A2250 4721 2509 3251 -161 -457 444 O HETATM 3291 O HOH A2251 19.119 6.968 -0.599 1.00 24.90 O ANISOU 3291 O HOH A2251 3216 3458 2785 408 316 512 O HETATM 3292 O HOH A2252 23.694 5.048 2.922 1.00 33.02 O ANISOU 3292 O HOH A2252 5231 4062 3251 -350 -65 414 O CONECT 303 857 CONECT 330 2964 CONECT 760 1291 CONECT 857 303 CONECT 1291 760 CONECT 2090 2837 CONECT 2837 2090 CONECT 2959 2960 2969 2972 2994 CONECT 2960 2959 2962 2965 CONECT 2961 2975 CONECT 2962 2960 2963 2995 CONECT 2963 2962 2964 2966 2967 CONECT 2964 330 2963 2968 CONECT 2965 2960 CONECT 2966 2963 2967 2996 2997 CONECT 2967 2963 2966 2998 2999 CONECT 2968 2964 CONECT 2969 2959 2970 2982 CONECT 2970 2969 2971 3000 3001 CONECT 2971 2970 2972 2973 3002 CONECT 2972 2959 2971 3003 3004 CONECT 2973 2971 2974 2980 2981 CONECT 2974 2973 2975 2979 CONECT 2975 2961 2974 2976 CONECT 2976 2975 2977 3005 CONECT 2977 2976 2978 3006 CONECT 2978 2977 2979 3007 CONECT 2979 2974 2978 3008 CONECT 2980 2973 CONECT 2981 2973 CONECT 2982 2969 2983 2985 CONECT 2983 2982 CONECT 2984 2985 2986 3009 3010 CONECT 2985 2982 2984 2986 2991 CONECT 2986 2984 2985 3011 3012 CONECT 2987 2988 2992 3013 CONECT 2988 2987 2989 2993 CONECT 2989 2988 2990 3014 CONECT 2990 2989 2991 3015 CONECT 2991 2985 2990 2992 CONECT 2992 2987 2991 3016 CONECT 2993 2988 CONECT 2994 2959 CONECT 2995 2962 CONECT 2996 2966 CONECT 2997 2966 CONECT 2998 2967 CONECT 2999 2967 CONECT 3000 2970 CONECT 3001 2970 CONECT 3002 2971 CONECT 3003 2972 CONECT 3004 2972 CONECT 3005 2976 CONECT 3006 2977 CONECT 3007 2978 CONECT 3008 2979 CONECT 3009 2984 CONECT 3010 2984 CONECT 3011 2986 CONECT 3012 2986 CONECT 3013 2987 CONECT 3014 2989 CONECT 3015 2990 CONECT 3016 2992 CONECT 3017 3018 3019 3023 3024 CONECT 3018 3017 3025 CONECT 3019 3017 3020 3021 3026 CONECT 3020 3019 CONECT 3021 3019 3022 3027 3028 CONECT 3022 3021 CONECT 3023 3017 CONECT 3024 3017 CONECT 3025 3018 CONECT 3026 3019 CONECT 3027 3021 CONECT 3028 3021 CONECT 3029 3030 3031 3035 3036 CONECT 3030 3029 3037 CONECT 3031 3029 3032 3033 3038 CONECT 3032 3031 CONECT 3033 3031 3034 3039 3040 CONECT 3034 3033 CONECT 3035 3029 CONECT 3036 3029 CONECT 3037 3030 CONECT 3038 3031 CONECT 3039 3033 CONECT 3040 3033 MASTER 311 0 3 9 18 0 10 6 3291 1 89 17 END If you find results from this site helpful for your research, please cite one of our papers:
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